Particularly, but not exclusively, the present invention relates to the production and use of type II glycoproteins displaying glycolipid and phospholipid antigens.

Background of the Invention The CD1 gene cluster on human chromosome lq22-23 encodes a family of five type II glycoproteins which are expressed on the cell surface in association with beta-2- microglobulin (ß2m). According to their amino acid sequence homology the five CD1 isoforms segregate into group 1, containing CDla, Wb, c, and CDle, and group 2, containing CDld. While CD1 group 1 molecules are not present in mice and rat, CDld is conserved in all mammalian species studied to date.

In contrast to the highly polymorphic HLA class I and class II molecules, with which they share a common genetic ancestor, CD1 molecules are non-polymorphic. It was probably for this reason, that their role as antigen presenting molecules remained unrecognised for more than a decade after their initial description. The lack of polymorphism indicates that, as opposed to HLA class I and class II genes, the CD1 genes are subjected to very weak evolutionary pressure. Two features of CD1 molecules offer an explanation for this phenomenon. Firstly, CD1 molecules do not present peptides as HLA class I and HLA class II molecules do, but they present glycolipids and phospholipids to T lymphocytes. Immune escape of microbes

from HLA class I or class II-mediated responses can simply be achieved with functionally irrelevant changes in protein sequences abrogating binding and/or presentation of immunogenic peptides.

In contrast, lipid antigens cannot be easily mutated because lipids are end products of highly complex biosynthetic pathways, and because their physicochemical properties, which are essential to the organism, rely on their correct structure.

A second characteristic of CD1 molecules, which could also lower the ligand-induced evolutionary pressure on CD1, is their apparent high degree of ligand binding adaptability. In particular, human CDlb can present the carbohydrate epitope of either a mycobacterial derived eighty carbon containing (C80) glucomonomycolate (GMM) or a shorter thirty-two carbon (C32) synthetic GMM to the same T cell receptor, suggesting either adaptive conformational changes within the CD1 antigen binding groove or simply protrusion of the longer alkyl chain of the ligand at one end of the groove. The crystal structure of mouse CDld, which was determined in the absence of ligand, revealed two electrostatically neutral voluminous pockets A'and F', suited to bind the alkyl chains of CD1 lipid ligands.

However, it is still completely unknown how different lipid classes bind to the CD1 groove, and how the same CD1 binding pocket can accommodate alkyl chains of different lengths. Furthermore, while a common motif for CDlb and CDld-binding ligands has been proposed, consisting of a single proximal branched acyl chain or

two acyl chains, another CD1-molecule with high predicted structural similarity to CDlb, namely CDlc, presents single alkyl chain containing polyprenols to T cells.

Moreover, recent evidence indicates, that single alkyl chain lipids can also be bound and presented by CDld.

WO 01/94949 relates to compositions and methods for identifying CD1-antigens and CD1-restricted T cells. The compositions include soluble CD1 molecules. A method for identifying a CD1-restricted T cell comprising contacting a CD1-presented antigen complex with a putatative CD1- restricted T cell is disclosed.

WO 96/12190 relates to the presentation of hydrophobic antigens to T-cells by CD1 molecules and discloses the identification of human CDla, CDlb, CDlc, CDld and CDle.

WO 95/00163 relates to a method for isolating CD1- presented antigens from a sample.

In"Presentation of the same glycolipid by different CD1 molecules"A. Shamshiev et al J. Exp. Med (April 15,2002), 195 (8), pp. 1013-1021, the authors conclude that group I CD1 molecules present an overlapping set of self- glycolipids.

Summary of the Invention To elucidate the mechanisms and potential of lipid binding to CD1 the inventors attempted to crystallise human CDlb with bound ligand. They found that in order to ensure binding of only their chosen ligands to CD1, they had to develop a novel detergent-assisted protocol to

refold CDlb in vitro from completely denatured and reduced E. coli derived protein.

The inventors subsequently obtained two crystal structures of human CDlb, one with phosphatidylinositol (PI) at 2. 26A and another with ganglioside GM2 at 2.8 A.

The mode of ligand binding was almost identical for both structures. Interestingly, the C16 alkyl chain detergent used in the inventor's refolding protocol acted as an additional ligand in both structures by binding to those areas of the CDlb-binding groove that were not occupied by the glycolipid or phospholipid ligands.

Furthermore the inventors generated fluorescent tetramers of human CDld molecules loaded with the synthetic glycolipid alpha-galactosylceramide (aGC). These tetramers were shown by the inventors to specifically stain a human immunoregulatory T-lymphocyte population, i. e. invariant NKT cells.

Thus, at its most general, the invention provides a method for producing a CD1/ligand complex ; methods of diagnosing or treating patients using said CD1/ligand complex; and screening methods for determining new therapeutic targets on the CD1 complex, following determination of its crystal structure.

Accordingly, in a first aspect, there is provided a method of producing correctly folded recombinant CD1 molecules around various lipid ligands, such as gangliosides, phospholipids and glycosylceramides. The resulting CD1/ligand complex is biologically active, i. e. the ligand is displayed correctly by the CD1 molecule so

that it can be presented to immune components, e. g. T lymphocytes.

In the past, CDla and CDlb have been successfully refolded using immobilised enzymes. However, there was no evidence of ligand being present in the refolded molecules. As mentioned above, the inventors have devised a novel approach using single chain detergents. This approach is inexpensive and can easily be scaled up for industrial purposes. The inventors have further provided direct evidence that the lipid ligand is bound to the hydrophobic groove of CD1 molecules.

Thus, in accordance with the first aspect of the invention, there is provided a method of producing a CD1/ligand complex said method comprising the steps of: a) obtaining a denatured CD1 protein; b) contacting said denatured CD1 protein with ligand in an environment comprising detergent; and c) isolating said CD1/ligand complex.

Preferably, the CD1 protein is fully denatured and reduced to ensure that the protein is unfolded when initially contacted with ligand. Although it is preferable to also reduce the protein, the presence of native disulfide bridges would not prevent the protein from refolding with ligand. However, when expressed as inclusion bodies in E. coli, correct or native formation of disulfide bridges cannot be presumed. Proteins with incorrect disulfide bridges will not fold correctly and could potentially reduce the efficacy of in vitro refolding of other protein by increasing the tendency of protein-protein aggregation.

The ligand may be any lipid, but most preferably, it is a glycolipid (e. g. ganglioside GM2 or alpha- galactosylceramide) or phospholipid (e. g. phosphatidylinositol). The inventors have determined that the CD1 molecule is capable of displaying lipids of various sizes. Thus, for a single chain ligand the molecule is preferably anything up to 60 carbons in length, e. g. between 5,10 or 15 and 30,40 or 50 carbons in length. For a double chain ligand, the molecule may contain anything between 18 carbons to 100 carbons, e. g. between 10,20, 30 or 40 and 70,80, or 90 carbons in length.

Preferably, the detergent is a single chain detergent, such as acyclic single alkyl chain detergents with chain length C2-C60; sphingosines; ceramides with truncated alkyl chains; diacylglycerol-type lipids with truncated alkyl chains; and triacylglycerol-type lipids with truncated alkyl chains. The inventors favoured the use of cetyltrimethylammonium bromide (CTAB).

The method preferably further comprises the step of removing excess detergent from the environment prior to isolation of the CD1/ligand complex. The excess detergent which has not stably incorporated into the protein structure, may be removed by adding methylated or unmethylated beta-cyclodextrin in molar excess over detergent. The inventors prefer to use at least 12 molar excess of methyl-beta-cyclodextrin. However, other methods will be known to the person skilled in the art.

For example, other cyclodextrins (alpha and gamma) which vary in the size of their hydrophobic cavity. The

inventors preferred methyl-beta-cyclodextrin but other cyclodextrins will work in accordance with the invention.

Other methods for stripping off the excess detergent include the use of resins or dialysis.

It is preferred to use a step that allows rapid stripping of the detergent as slow removal by resins or dialysis may decrease the yield of the CD1/ligand complex.

The method according to the first aspect of the invention may be carried out using any CD1 molecules. However, preferably, the method is carried out on CDld, CDlc and most preferably on CDlb.

The environment comprising the detergent will also comprise various buffers to aid in the refolding event.

Preferably, an aqueous buffer is provided comprising Urea, L-Arginine, a buffer (e. g. Tris), and a redox- system (e. g. oxidized and reduced glutathione). The buffer constituents can be varied: L-Arginine can be used in various concentrations from 100mM, preferably at a concentration between 100mM to 1M, but may not even be essential to get a certain yield of refolded CD1. The same applies for Urea, which can certainly be used in concentrations ranging from OM to 4M. At the higher concentrations a dialysis step may be necessary. Instead of glutathione another redox system such as cysteamine- cystin, could be used and the molarities of glutathione can be varied.

The CD1 protein may be engineered to contain one or more biotinylation sites providing a means for complexing CD1 proteins using avidin to obtainmultimeric, e. g. dimer,

trimer, tetramer, forms of CD1 which may be useful in amplifying output signals in methods and assays for identifying ligand specific T-cells or antibodies.

In preferred arrangements, the CD1 protein may be complexed with the Fc portion of a selected immunoglobulin. The complex may be formed by using binding partners (biotin-avidin) or by chemical means (covalent, di-sulfide, H-bonds).

Preferably, the method of the first aspect may further comprise the step of labelling the CD1 protein with a chemical marker, more preferably a fluorescent compound, e. g. RPE or FITC. The labelled CD1 protein useful in identification of specific T-cell populations and for diagnosis of specific disease states. In particular, mulitmers, e. g dimers, trimers or tetramers, of labelled CD1/ligand complex may be used.

The method may further comprise the step of incorporating said CD1/ligand complex into a pharmaceutical composition. The pharmaceutical composition may comprise, in addition to one of the above substances, a pharmaceutically acceptable excipient, carrier, buffer, stabiliser or other materials well known to those skilled in the art. Such materials should be non-toxic and should not interfere with the efficacy of the active ingredient. The precise nature of the carrier or other material may depend on the rate of administration, e. g. oral, intravenous, cutaneous or subcutaneous, nasal, intramuscular, intraperitoneal routes.

In an embodiment of the present invention, the pharmaceutical composition may be used as a vaccine to

boost the immune response in an individual. Thus, it is preferable that the composition further comprises a suitable adjuvant. The pharmaceutical composition according to the present invention may be used to elicit cellular immune responses including lipid-specific CD4+CD8-, CD4-CD8+, and CD4 CD8 T cell responses.

Alternatively, antibody responses to the pharmaceutical composition would also be of therapeutic value.

The present invention provides a pharmaceutical composition comprising a CD1/ligand complex for treating diseases such as infectious diseases caused by parasites, mycobacteria, fungi, and bacteria; tumours and autoimmune diseases such as multiple sclerosis.

Depending on the disease to be treated, the ligand will be a lipid that is capable of inducing an immune response, against substances (e. g. tumour cells, bacteria, myobacteria etc. ) associated with the disease.

For example, ligands may be a) Mycobacterial cell wall lipids: Glycosyl-esters of mycolic acid (glucomonomycolate, mannose-monomycolate, etc. ) Phosphatidylinositomannosides (PIM2 to PIM6), as well as synthetic lipids modelled after mycobacterial cell wall lipids (synthetic glucomonomycolate, etc.) b) ganglioside lipids such as GM1 or GM2 or GM3, etc.; Also diacylglycerol-type bacterial cell wall lipids; c) sulfatide ; d) trypanosomal phospholipids; malarial cell wall lipids.

For the treatment of tumours, ligand may be lipids expressed on the surface of tumour cells.

Thus, embodiments of the present invention provide a CD1/ligand complex for use in the preparation of a medicament for treating infectious diseases caused by parasites, mycobacteria, fungi, and bacteria ; solid tumours; and autoimmune diseases. In preferred embodiments use of a CD1/ligand complex produced in accordance with the first aspect of the invention and a method of medical treatment comprising administering the CD1/ligand complex in therapeutically effective amounts are provided.

In accordance with a second aspect of the present invention, there is provided a method of inducing or boosting an immune response in an individual to a lipid antigen, said method comprising administering a CD1/ligand complex to said individual wherein the ligand in the CD1/ligand complex is said lipid antigen.

The CD1/ligand complex may be produced according to the first aspect of the invention.

The method may further comprise identifying the lipid antigen associated with a disease of the individual, i. e. cancer, infectious disease or autoimmune disease.

For example, the method may comprise identifying a lipid antigen over-expressed on the surface of tumour cells present in the individual. The identified lipid antigen may then be folded into a CD1 molecule in accordance with the first aspect of the invention thereby producing a

CD1/ligand complex which may be administered as a vaccine to said individual to raise an immune response against said tumour.

With regard to autoimmune diseases, the CD1 ligand complex may further comprise a toxin which is capable of disrupting an immune response raised against the lipid antigen. For example, the provision of a toxin- conjugated CD1/ligand complex may be used to eliminate specific T lymphocytes which interacted with the complex.

Autoimmune T lymphocytes represent a therapeutic target for such toxin-conjugated CDl/ligand complexes.

In a third aspect of the present invention, the CD1/ligand complex according to the present invention may also be used to diagnose a disease in an individual, by identifying the presence or absence of an immune response, i. e. CD/1 lipid-specific T-lymphocytes or antibodies, to a particular lipid antigen. Thus, a sample may be obtained from an individual, and contacted with a CD1/ligand complex of the invention. If the CD1/ligand complex was being used to identify the presence of an autoimmune disease, the complex would display a lipid antigen associated with this disease. If the sample comprised T-lymphocytes or antibodies already primed to the lipid antigen, these will be detected by the CD1/ligand complex contacted with the sample.

Standard labelling techniques may be used to identify any binding between the CD1/ligand complex and the immune components in the sample.

In accordance with any of the aspects described above, the CD1/ligand complex may be provided as a monomer,

dimer, trimer, tetramer etc. Complexes may be joined by standard means known in the art, e. g. using binding partners (biotin-avidin) or chemical means (co-valent, di-sulfide, hydrogen bonds), so that the ligand is displayed and could be recognised by the T cell receptor.

According to a fourth aspect of the present invention, the inventors have prepared a crystal of CD1/ligand complex and determined the crystal structure of CD1 and CD1/ligand complex. This provides for the first time methods of identifying or obtaining substances (e. g. agonists or antagonists) for modulating the activity of CD1 or CD1/ligand complex. Crystal structure information presented herein is useful in designing potential inhibitors and modelling them or their potential interaction with a CD1 or CD1/ligand complex binding cavity.

Potential modulating substances may be brought into contact with CD1 or CD1/ligand complex to test for ability to interact with the CD1 binding cavity. Actual substances may be identified from among potential substances synthesized following design and model work performed in silico. A substance identified using the present invention may be formulated into a composition, for instance a composition comprising a pharmaceutically acceptable excipient, and may be used in the manufacture of a medicament for use in a method of treatment.

Thus, in the fourth aspect of the invention, there is provided a crystal of CD1 and CD1/ligand complex.

Preferably, the ligand is a lipid, more preferably a glycolipid or a phospholipid. The crystal may have unit

cell dimensions of a = 87. 5 A 5%, b = 177 A 5% c = 75 A 5%.

Preferably a = 87. 5 A 0. 2%, b = 177 A 0.2 % c = 75 A 0. 2%.

In a preferred embodiment, the crystal structure of CD1 and CD1/ligand complex has the three dimensional atomic co-ordinates of Table 1.

In a preferred embodiment the ligand is phosphatidylinositol (PI) or ganglioside GM2 and the CD1 molecule is CDlb, CDlc or CDld, preferably CDlb.

A method for growing the crystal of the fourth aspect by sitting drop crystallisation using a precipitant comprising 0.2M Lithium nitrate and 20% w/v Polyethylene Glycol is also provided.

The coordinates of Table 1 provide a measure of atomic location in Angstroms (A), to a third decimal place. The coordinates are a relative set of positions that define a shape in three dimensions, but the skilled person would understand that an entirely different set of coordinates having a different origin and/or axes could define a similar or identical shape. Furthermore, the skilled person would understand that varying the relative atomic positions of the atoms of the structure so that the root mean square deviation of the residue backbone atoms (i. e. the nitrogen-carbon-carbon backbone atoms of the protein amino acid residues) is less than 1.5 A (preferably less than 1.0 A and more preferably less than 0.5 A) when superimposed on the coordinates provided in Table 1 for

the residue backbone atoms, will generally result in a structure which is substantially the same as the structure of Table 1 in terms of both its structural characteristics and potency for structure-based design of CD1 inhibitors. Likewise the skilled person would understand that changing the number and/or positions of the water molecules and/or substrate molecules of Table 1 will not generally affect the potency of the structure for structure-based design of CD1 inhibitors. Thus for the purposes described herein as being aspects of the present invention, it is within the scope of the invention if: the Table 1 coordinates are transposed to a different origin and/or axes ; the relative atomic positions of the atoms of the structure are varied so that the root mean square deviation of residue backbone atoms is less than 1.5 A (preferably less than 1.0 A and more preferably less than 0.5 A) when superimposed on the coordinates provided in Table 1 for the residue backbone atoms; and/or the number and/or positions of water molecules and/or substrate molecules is varied.

Reference herein to the coordinate data of Table 1 thus includes the coordinate data in which one or more individual values of the Table are varied in this way.

By"root mean square deviation"we mean the square root of the arithmetic mean of the squares of the deviations from the mean.

Thus, for example, varying the atomic positions of the atoms of the structure by up to about 0.2 A in any direction will result in a structure which is substantially the same as the structure of Table 1 in terms of both its structural characteristics and utility e. g. for structure-based drug design.

The provision of the high resolution structure of Table 1 provides those of skill in the art with a detailed insight into the mechanisms of action of CD1 or CD1/ligand complex. This insight provides a means to design new substances which have the potential to modulate, e. g. inhibit or enhance the process by which CD1 presents ligand to the immune system.

The provision of the crystal structure of CD1 and CD1/ligand complex allows a novel approach for drug discovery for modulators of this enzyme. Accordingly, in a fifth aspect of the invention a computer-based method of rational drug design is provided comprising the steps of: providing the structure of the CD1 or CD1/ligand complex as defined by the coordinates of Table 1 ; providing the structure of a candidate modulator molecule; and fitting the structure of the candidate modulator molecule to the structure of the CD1 or CD1/ligand complex of Table 1.

In an alternative aspect, the method of the invention may utilise the coordinates of atoms of interest of the CD1 which are in the vicinity of a putative ligand pocket in order to model the pocket in which the ligand fits.

These coordinates may be used to define a space which is then screened"in silico"against a candidate modulator molecule. Thus, in a sixth aspect, the invention provides a computer-based method of rational drug design which comprises: providing the coordinates of at least two atoms of

the CD1 of Table 1 ("selected coordinates") ; providing the structure of a candidate modulator molecule; and fitting the structure of the candidate modulator molecule to the selected coordinates of the CD1.

In practice, it will be desirable to model a sufficient number of atoms of the CD1 as defined by the coordinates of Table 1 which represent a binding pocket e. g. A'C'F' or T'.

Thus preferably there will be provided the coordinates of at least 5 or 10, more preferably at least 50 and even more preferably at least 100 selected atoms of the CD1 structure.

Preferably, the invention also relates to fragment linking or fragment growing approaches to rational drug design. Thus the step of providing the structure of a candidate modulator molecule may be performed by providing the structures of a plurality of molecular fragments and linking the molecular fragments to form a candidate modulator molecule. Furthermore the step of fitting the structure of the candidate modulator molecule may be performed before the molecular fragments are linked together, by separately fitting the structure of each molecular fragment, or after the molecular fragments are linked together.

Thus, the computer-based method of rational drug design may comprise: providing the coordinates of at least two atoms of the CD1 or CD1/ligand complex of Table 1;

providing the structures of a plurality of molecular fragments ; fitting the structure of each of the molecular fragments to the selected coordinates of the CD1 or CD1/ligand complex; and assembling the molecular fragments into a single molecule to form a candidate modulator molecule.

In one embodiment, the computer-based method may further comprise the steps of: obtaining or synthesising the candidate modulator molecule; contacting the candidate modulator molecule with CD1 ; and determining the ability of the candidate modulator molecule to interact with CD1.

In another embodiment, the computer-based method may further comprise the steps of: obtaining or synthesising the candidate modulator molecule ; forming a complex of CD1 and said candidate modulator molecule ; and analysing said complex by X-ray crystallography to determine the ability of said candidate modulator molecule to interact with CD1.

A further aspect of the invention provides a compound having a chemical structure selected using the method of any one of the previous aspects, said compound being a modulator of the activity of CD1, e. g. an inhibitor or enhancer of CD1 ligand presentation.

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

In any event, the determination of the three-dimensional structure of CD1 and CD1/ligand complex provides a basis for the design of new and specific ligands for CD1 or modulators of CD1 activity. For example, knowing the three-dimensional structure of CD1/ligand complex, computer modelling programs may be used to design different molecules expected to interact with possible or confirmed active sites, such as binding sites or other structural or functional features of CD1.

More specifically, a potential modulator of CD1/ligand complex activity can be examined through the use of computer modelling using a docking program such as GRAM, DOCK, or AUTODOCK (see Walters et al., Drug Discovery Today, Vol. 3, No. 4, (1998), 160-178, and Dunbrack et al., Folding and Design, 2, (1997), 27-42).

Accordingly, in a seventh aspect, the present invention provides a machine readable data storage medium comprising a data storage material encoded with machine

readable data, wherein the data is defined by all or a portion of the structure coordinates of CD1/ligand complex according to Table 1. The invention further includes use of the machine readable data storage medium to design modulators of the CD1/ligand complex.

In an eighth aspect of the invention, there is provided a computer system intended to generate structures and/or perform rational drug design for CD1/ligand complex, or complexes of CD1/ligand with a potential modulator, the system containing machine readable data comprising : (1) atomic coordinate data of Table 1, said data defining the three dimensional structure of CD1/ligand complex, or at least one sub-domain of the three-dimensional structure of CD1/ligand complex, or the coordinates of at least two atoms of CD1/ligand complex; or (2) structure factor data for CD1/ligand complex, said structure factor data being derivable from the atomic coordinate data of Table 1.

Having designed or selected possible binding candidate modulators (e. g. by in silico analysis,"wet"chemical methods, X-ray analysis etc. ) by determining those which have favourable fitting properties (e. g. strong attraction between candidate and CD1), these can then be screened for activity. Consequently, the method preferably further comprises the steps of: obtaining or synthesising the candidate modulator ; and contacting the candidate modulator with CD1/ligand complex to determine the ability of the candidate modulator to interact with CD1/ligand complex.

More preferably, in the latter step the candidate modulator is contacted with CD1/ligand complex under conditions to determine its function.

Following identification of a modulator (e. g. an enhancer or inhibitor), it may be manufactured and/or used in the preparation, i. e. manufacture or formulation, of a composition such as a medicament, pharmaceutical composition or drug. These may be administered to individuals.

In a ninth aspect, the present invention provides a method for identifying a candidate modulator (e. g. potential enhancer) of CD1/ligand complex comprising the steps of: providing the three-dimensional structure of CD1/ligand complex, or at least one sub-domain thereof, to characterise at least one active site of CD1, the three-dimensional structure being defined by atomic coordinate data according to Table 1; and identifying a candidate modulator molecule for interaction with the active site. Preferably, the candidate modulator molecule is identified by designing or selecting the molecule to interact with the active site.

If more than one CD1 active site is characterised and a plurality of respective compounds are designed or selected, the modulator may be formed by linking the respective compounds into a larger compound which maintains the relative positions and orientations of the respective compounds at the active sites. The larger

compound may be formed as a real molecule or by computer modelling.

Preferably, high throughput screening of compounds to select compounds with binding activity may be undertaken, those compounds showing binding activity being selected as possible candidate modulators, and further crystallized with CD1 (e. g. by co-crystallization or by soaking) for X-ray analysis. The resulting X-ray structure may be compared with that of Table 1 for a variety of purposes. For example, where the contacts made by such compounds interact with a plurality of active sites, e. g. where the contacts overlap with those made by lipid antigen, novel molecules comprising residues contacting both lipid antigen and the bound compound may be obtained.

Identified modulators (e. g. an enhancers or inhibitors), may then be manufactured and/or used in the preparation, i. e. manufacture or formulation, of a composition such as a medicament, pharmaceutical composition or drug. These may be administered to individuals.

A tenth aspect of the present invention provides a method of assessing the ability of a candidate modulator molecule to interact with CD1 or CD1/ligand complex comprising the steps of: obtaining or synthesising said candidate modulator molecule ; forming a crystallised composite of CD1 or CD1/ligand complex and said candidate modulator; and

analysing the composite by X-ray crystallography to determine the ability of the candidate modulator to interact with CD1 or CD1/ligand complex.

Preferably, the composite diffracts X-rays for the determination of atomic coordinates of the composite to a resolution of better than 3A, more preferably better than 2A. The crystallised composite may be formed by crystal soaking or co-crystallisation.

By utilising the high resolutions obtainable with X-ray crystallography, it is possible to determine the ability of the candidate modulator molecule to interact with CD1 or CD1/ligand complex by comparing the intensities and/or positions of X-ray diffraction spots from the composite with diffraction spots of uncomplexed CD1 or a previously identified CD1/ligand complex. Thus, the step of analysing the composite may involve analysing the intensities and/or positions of X-ray diffraction spots from the composite to determine the ability of the candidate modulator molecule to interact with CD1 or CDl/ligand complex.

In another aspect, the invention relates to a method of determining three dimensional structures of CD1/ligand complex homologues or analogues of unknown structure by utilising the structural coordinates of Table 1.

For example, if X-ray crystallographic or NMR spectroscopic data is provided for a CD1 homologue or analogue of unknown structure, the structure of CD1 as defined by Table 1 may be used to interpret that data to provide a likely structure for the CD1 homologue or

analogue by techniques which are well known in the art, e. g. phase modelling in the case of X-ray crystallography.

Thus, in an eleventh aspect of the present invention a method of determining three dimensional structures of CD1 or CD1/ligand complex homologues of unknown structure is provided, comprising the steps of: aligning a representation of an amino acid sequence of a CD1 or CD1/ligand complex homologue or analogue of unknown structure with the amino acid sequence of CD1 or CD1/ligand complex to match homologous regions of amino acid sequences; modelling the structure of the matched homologous regions of the homologue or analogue of unknown structure on the structure as defined in Table 1 of the corresponding regions of CD1 or CD1/ligand complex; and determining a conformation for the homologue or analogue of unknown structure which substantially preserves the structure of said matched homologous regions.

Preferably, said homologues have an amino acid sequence having at least 50% homology with said CD1, more preferably at least 60%, 70%, 80% or 90% homology.

In a twelfth aspect of the present invention there is provided a method for determining the structure of a protein comprising the steps of: providing the coordinates of Table 1 ; and either (a) positioning said coordinates in the crystal unit cell of said protein so as to provide a

structure for said protein, or (b) assigning NMR spectra peaks of said coordinates.

In a thirteenth aspect of the present invention there is provided a method for determining the structure of a compound bound to CD1/ligand complex comprising the steps of: providing a crystal of CD1/ligand complex; and soaking the crystal with the compound to form a complex; and determining the structure of the complex by employing the data of Table 1.

Aspects and embodiments of the present invention will now be illustrated, by way of example, with reference to the accompanying figures. Further aspects and embodiments will be apparent to those skilled in the art. All documents mentioned in this text are incorporated herein by reference.

Brief Description of the Drawings Figure 1: Structure of the human CDlb complex and of its ligands. a, CDlb structure (al-a3 domains in light shading, 2m in dark shading with left to right hatching) with bound PI (alkyl chains in grey shading with right to left hatching (C') and dark shading (A'), inositol dot filled in light grey and adjacent phosphate dot filled in black) and detergent molecules (dark shading (F') and dot filled in black (T') ) shown as Van Der Waals spheres. The internal hydrophobic cavity of ala2 is drawn as a transparent surface, and ligand binding channels are indicated as A', C', F'and T'. b, Chemical structures of

lipid and detergent ligands used in the refolding of CDlb complexes.

Figure 2: Binding and presentation of alkyl chain ligands by CDlb. All panels depict the CDlb/PI complex excepting b and c which show CDlb/GM2. a, Overview of the ale2 domain of CDlb with bound ligands. Close up views of the framed regions of the groove are shown in panels b-g. b and c, Positioning of the first glucosyl-and the phosphoinositol head groups in the CDlb-GM2 and CDlb-PI structures, respectively. Carbon atoms of the lipid ligand are grey shaded with right to left hatching, oxygens are black spheres, phosphate is hashed, and nitrogen dot filled black. Hydrogen bonds are shown as black dotted line. d, The F'channel with bound monoalkyl detergent. e, A single detergent molecule bound to tunnel T'traverses a path, unobstructed by bulky side chains, between channels A'and F'. f, A portal in the C'channel, stabilised by a unique disulfide bond Cysl31-Cysl45 (square dot infill), allows egress of the lipid from the interior of the protein. g, The bottom of the A'channel contains a hydrophobic pole formed by Vall2 and Phe70, which could guide the lipid ligand from the A'channel into the T'tunnel. In all panels, the Fo-Fc omit map electron density (thin line mesh, contoured at 2. 5o) was calculated after a simulated annealing during which the glycolipid (plus any residues and detergent within a distance of 3. 5A) were omitted, in panels d-g, the 2 Fo-Fc electron density of the protein structure is shown as a white surface, contoured at la.

Figure 3: Differences between CDlb and other CD1 isoforms. a, b, Structural comparison of the antigen binding cavity for hCDlb and mCDld. The hydrophobic groove and key side chains of CDlb and CDld are shaded.

The ligands present in the CDlb structures were superimposed onto the mCDld structure for direct comparison. c, Sequence alignment of the ale2 domains of human CDla-e and mCDld. Secondary structure elements of CDlb are shown above the protein sequence. A shaded background indicates those residues which confer the lipid binding properties of CDlb and which are conserved at equivalent positions in other CD1 isoforms.

Hydrophobic residues guiding the lipid ligands in CDlb at the bottom of channel A' (see Fig. 2g) and between channels C'and F'are indicated by triangles, respectively. Cysteine residues are boxed.

Figure 4: Models for binding of mycolic acid and triacylglycerol to CDlb. a, Chemical structures of mycolic acid from M. tuberculosis and of the triacylglycerol trilaurin. b, Mycolic acid modeled into the CDlb structure. The C60 long meromycolate chain (hash infill) could be fully contained within channels A', T' and F', thus forming a superchannel of some 70A length.

The shorter C25 alkyl chain (dark shaded) is therefore more likely to lodge in the C'channel. c, Model of triacylglycerol (trilaurin) binding to CDlb, demonstrating that the three C11 alkyl chains (dot infill) could separately bind to surface-linked channels A', C'and F'. To demonstrate the full binding potential of the CDlb groove, alkyl chains present in the CDlb-PI and CDlb-GM2 structures but not accounted for by the models are overlayed in light grey. Conversely,

polycarbon chains, which the crystal structures provide no models, are indicated by dotted lines.

Figure 5: CDld/aGC complexes are specific for human invariant NKT cells. Use of fluorescent CDld/aGC tetramers as a diagnostic composition in identifying human invariant NKT cells by FACS analysis. a, FSC-H/SSC- H plot used for gating of lymphocyte population. b, Propidium iodide staining gates out dead cells. c, Staining of human invariant NKT cells with anti-T-cell receptor (anti-TCR) Valpha24 antibody. d, e, CDld/aGC tetramers stain human invariant NKT cells.

Detailed Description Compared to in vivo folding, in vitro folding of proteins is generally much less effective. Mammalian cells possess a range of specialised helper proteins, e. g. chaperonins, disulfidases, proline isomerases, etc. , which enhance the yield of correctly folded molecules. Standard in vitro refolding protocols, which were successful for HLA class I molecules were completely unsuccessful for refolding CD1 molecules. As CD1 molecules are significantly more hydrophobic than HLA class I molecules, the inventors thought that the difficulties with standard protocols were due to hydrophobic interactions between partially folded CD1 molecules, causing the proteins to aggregate and precipitate. When a fully denatured protein starts to fold, it goes through a transition state, hydrophobic residues are exposed to the surroundings, and if two proteins meet, they will bind to each other and precipitate. To overcome this possible problem, the inventors used single chain detergents as folding assistants. The idea was that detergent molecules and

folding CD1 molecules would form mixed detergent-protein micelles which would allow the proteins to proceed with the folding beyond the molten-globule state, while being physically separated from each other.

The second stage of the process is to strip off the detergent from these micelles so as to allow the molecules to completely fold. The detergent is stripped using, for example, soluble cyclodextrins.

The inventors have been able to crystallise CDlb molecules generated by this method and have obtained high resolution structure of CDlb with bound ligand. The crystal structure revealed that the large groove of Cdlb is not only occupied by ligand but also by the detergent molecule.

The ligand is loaded in a way that allows optimal presentation of the antigenic epitope to the T cell receptor, while two detergent molecules per CD1 molecule fill the rest of the large groove. Thus, in accordance with the present invention, the loaded CD1 molecule (CD1/ligand complex) is considered biologically active.

As an example of the present invention, the inventors have refolded the extracellular region of human CDlb (hCDlb heavy chain residues 1-283 plus beta-2- microglobulin, ß2m) in vitro from completely denatured and reduced E. coli-derived proteins. Single alkyl chain detergents of sixteen carbon length (C16) were used as refolding assistants to protect exposed hydrophobic surfaces during early refolding stages, thereby reducing hydrophobic protein aggregation and precipitation. This

protocol yielded stable soluble CDlb/p2m-complexes, which mass spectrometry confirmed to be loaded with the specified lipid ligands plus detergent (see methods).

Soluble CDlb/p2m-proteins loaded either with phosphatidylinositol (PI) or ganglioside GM2 (GM2) 8 were crystallised, their structures determined by molecular replacement and refined using data to 2. 26A and 2. 8A, respectively (see Fig. 1,2, methods and supplementary information).

The CDlb heavy chain and ß2m structures are identical in the two complexes and unless otherwise stated the following analyses are based on the higher resolution CDlb/PI structure. The structures reveal a defined network of hydrophobic channels at the core of the alu2 domain which are precisely tailored for acyl binding and are saturated by four hydrocarbon chains of 11 to 22 carbon atoms in length. This binding groove architecture is radically different to that of classical MHC class I and II molecules. The total volume (2200A3) of the network is essentially filled by the hydrocarbon chains. No buried water molecules are present in either structure.

In an extension of the analogy with MHC class I binding pocket nomenclature introduced for mCDld, the three CDlb binding channels which connect directly to the surface are denoted as A', C'and F', with the fourth, a unique tunnel, designated T' (Fig. 1,2). Channels A', C', and F'interconnect via T'. The sequential connection of A', T'and F'provides the potential to accommodate up to 60 carbon atoms of a single acyl chain which could enter and exit between the al and a2 helices (along A'and F').

Channel C'remains separate, leading from the T cell

receptor (TCR) recognition surface between the al and a2 helices to a portal in the side of the molecule beneath the a2 helix (Fig 1,2d). Thus this channel can shelter acyl chains of some 16 carbon atoms fully from solvent whilst allowing egress for longer chains. The PI and GM2 ligands occupy channels A'and C', whilst two detergent molecules fill channels F'and T' (Fig. 1, 2,3). There is sufficient electron density to position unequivocally the link between the acyl chains and hence partial head- group structures for the glycolipids in the CDlb/GM2 and CDlb/PI complexes (Fig. 1,2a, 2b). The inositol ring of PI is partially ordered in the CDlb/PI complex, whilst only the first of the four sugar rings which branch off the GM2 lipid head is visible in the CDlb/GM2 crystal structure. Comparison with a classical MHC class I/peptide complex shows the glycolipid head groups to be presented by CDlb in a position analogous to that of the P4 residue in a peptide presented by MHC class I. The surface presented by the CDlb/glycolipid complexes appears compatible with standard TCR recognition, a conclusion borne out by mutagenesis studies mapping TCR binding to CDlb9. In contrast, key features of the a3 domain required for MHC class I binding to CD8 are not conserved in CDlblo.

Comparison of the CDlb complexes with the structure of mCDld, which does not include a specific bound ligand7, indicates broad equivalences but also very significant differences in the architecture of the binding groove (Fig. 3). Channel A'runs deeper in CDlb because Val63 replaces a bulky tryptophan at the equivalent position in mCDld (additionally Ala47 is replaced by Ile). Channel T', which in CDlb serves to connect channels A'and F',

is blocked in mCDld by the side chains of Leu100 and Valll8, equivalent to residues Gly98 and Glyll6 respectively in CDlb. Similarly, the exit portal for channel C'beneath the CDlb a2 helix (Fig. 2f) is closed off in CDld by Phel28 and Trpl33, being residues with bulky side chains, replacing Vall26 and Cysl31 respectively in CDlb. In CD1 alleles other than CDlb, the absence of a disulphide bridge (Cys 131-Cysl45, Fig 2f) pulls the a2 helix main chain more closely to the CD1 backbone. However, in addition to the differences hardwired by changes at sequence level the comparison of the CDlb and mCDld structures also implies both molecules may share some conformational adaptability. While channel F'is partially occluded in mCDld by the side chain of Leu84 the side chain conformation selected by the equivalent residue (Phe84) in the current CDlb structure frees up sufficient space for F'to accommodate a detergent molecule (Fig. 2d, 3). However, in the absence of ligand Phe84 may be expected to adopt an alternate conformation (analogous to that of Leu84 in mCDld) to pack against Phel44, Phe88 and Met90. This suggests a mechanism whereby the hydrophobic binding capacity of the channels may be tailored to ligand requirements, a phenomenon previously observed for binding of non- nucleoside inhibitors to HIV Reverse Transcriptase The current CDlb structures allow definition of the residues which confer the lipid binding properties of the alu2 domain. Sequence alignment of the CD1 family highlights channel A'and the associated portion of tunnel T'as the most conserved regions of the groove (Fig. 3c). Conversely, the central portion of tunnel T' is blocked in all other CD1 isoforms by the presence of

bulky side chains of residues equivalent to Gly98 and Glyll6 in CDlb. Similarly, the C'portal is occluded by tryptophan and phenylalanine residues which substitute for CDlb residues Cysl31 and Vall26, respectively in all other CD1 family members. Residues contributing to channel F'are least conserved. Overall, based on ligand binding architecture, CDlb appears to be unique among CD1 molecules.

The arrangement of the combined detergent and lipid ligands in the CDlb/PI and CDlb/GM2 structures provide a general model for describing the interaction of the CDlb- binding groove with alkyl chain containing ligands.

Mycobacterial mycolates (Fig. 4a), which play a crucial role in the adaptation of mycobacteria to intracellular growth and survival, were the first fully characterised ligands of human CDlb2. It has long been speculated about how lipid ligands of such large size could bind to CDlb.

Modelling of mycolic acid into the current CDlb structures demonstrates how the long C50-C56 meromycolate chain could be fully contained within a super channel consisting of the interconnected A', T'and F'channels, with the shorter C22-C26 alkyl chain binding to C' (Fig.

4b). The super channel has a maximum length of some 70A providing binding capacity for a single fatty acid chain of up to 60 carbons. In the case of only partial saturation of the superchannel's alkyl binding capacity, the F'channel could be closed off by selection of an alternative side chain conformation for Phe84 (see previously and Fig. 2d). This mechanism for adaptation to alkyl chain length would explain how CDlb can present either the large C80 mycobacterial glucomonomycolate or the shorter C32 synthetic glucomonomycolate to the same T

cell line. The superchannel also allows for the option of stably accommodating long chain monoalkyl ligands, which can therefore serve as T cell antigens.

Short chain fatty acids of the endoplasmic reticulum, such as palmitate, could also act as ligands for CDlb in a similar manner to the C16 chain detergents used in the current refolding protocol (see methods). However, since the affinity of a given ligand to CDlb is related to the polycarbon chain length, endogenous short chain fatty acids could exert a chaperone-like function before binding of higher affinity ligands. Consistent with this hypothesis is the fact that, despite a 500 fold molar excess of detergent over lipid in the refolding buffer, detergent molecules were bound only to the T'tunnel and F'channel, while both the A'and C'channels were occupied by the two alkyl chains of the lipid ligand.

This also suggests that surface CDlb molecules may still retain endogenous chaperones to account for any excess binding capacity, in particular in tunnel T'.

The arrangement of channels A', C'and F'strongly suggests that lipids containing three alkyl chains, such as endogenous triacylglycerols or mycobacterial triacyl trehalose, may bind to human CDlb (Fig. 4c).

Triacylglycerols, which are synthesised on membranes of the endoplasmic reticulum, are independent risk factors for coronary heart disease 14, 15. Activated memory T lymphocytes accumulate in atherosclerotic plaques and oxidized lipoproteins, which contain triacylglycerols, can act as immunogens for T celll8tl9.

Interestingly, a recent study has found that CDlb is highly expressed on macrophages in atherosclerotic

lesions, but not on normal tissue macrophages. It is therefore intriguing to speculate on the role of CDlb- mediated presentation of triacylglycerols to T lymphocytes in atherosclerosis.

The topology of CDlb is MHC class I-like (Fig. la) with close structural similarity to murine CDld. Tubes of electron density (common to both the CDlb/GM2 and CDlb/PI structures) delineate binding channels, buried between the al and a2 helices, occupied by four acyl chains.

These hydrocarbon chains are up to 80 carbon atoms in length. In the refined structures two of the acyl chains (in A'and C') are assigned to the tails of the glycolipid ligand and the remaining two (in F'and T') are accounted for by detergent molecules. Electron density at the CDlb surface linking chains A'and C' provide partial information for the position of the glycolipid head-group structures, which are relatively mobile as judged from crystallographic temperature factors.

The detergents used in the refolding of the single lipid complexes (see Methods) have supplemented GM2 and PI to saturate the acyl binding capacity of CDlb.

The structure of murine CDld7 does not include a specific bound ligand but the ala2 domain contains cavities designated as binding pockets A'and F'. Comparison with the CDlb complexes indicates broad equivalence of pocket A'to channels A'and of pocket F'to channel F'. The CDld cavities have a reduction in volume relative to the total CDlb network.

The main chain topology of CDlb differs markedly from MHC class I in the peak height attained by the kink in the a2 helix (residues 150-157 and 149-152 in CDlb and MHC class I respectively). Direct substitution of CDlb into a MHC class I/TCR complex (by simple superposition onto the MHC class I structure) therefore results in significant steric clashes between the TCR and this portion of the CDlb a2 helix. The upward displacement of the TCR necessary to provide a sterically acceptable dock onto the CDlb structure may facilitate incorporation at the recognition interface of the increased size of the glycolipid head group compared to an amino acid side chain. Given this modification the surface presented by the CDlb/glycolipid complexes appears compatible with standard TCR recognition, a conclusion borne out by mutagenesis studies mapping TCR binding to CD1.

Superposition of CDlb into the HLA A2/CD8aa crystal structure again reveals substantial steric clashes.

Given the highly conserved nature of the MHC class I/CD8 interaction these changes imply relative abolition of any such interaction. This is again consistent with the functional recognition of CD1 by CD8 T cells5.

CDld-tetramers generated using detergent refolding specifically detected human invariant natural killer (NK) T cells which recognise glycolipid presented by CDld and show specificity for alpha-galactosylceramide (aGC), (Figure 5). Human NKT cells expressing an invariant TCR Valpha24 chain are highly specific for CDld/aGC complex. Biotinylated human CDld molecules loaded with the synthetic glycolipid aGC were generated from completely denatured and reduced CDld protein and

complexed with fluorecent streptavidin. Fluorescent CDld/aGC tetramers specifically stained human NKT cells and demonstrated the use of CDl/ligand complexes for in vivo and in vitro T-cell identification and disease state diagnosis (Figure 5d, e).

Discussion A unique network of channels allows CDlb to accommodate glycolipids with two very long acyl tails. In CDlb the absence of side chains at Gly98 and Glyll6 opens channel T' (Fig 3c sequence alignments). It also indicates that certain of the CD1 family may have the capability to bind three acyl chain lipids. Such ligands would be expected to show strong binding consistent with enhanced avidity.

In contrast single acyl chain lipids would be penalized by reduced avidity.

Methods Protein expression, refolding and crystallization For expression of human CDlb (hCDlb) in bacterial inclusion bodies the plasmid hCDlb-pET23d, which encodes a truncated form of the hCDlb cDNA containing the extracellular al-a3 domains, was generated. The hCDlb coding sequence was amplified by PCR from monocyte- derived dendritic cell cDNA. Oligonucleotides used for PCR amplification (5'-3'and 3'-5') introduced 5'Ncol and 3'BamHl restriction sites, which allowed cloning into the bacterial expression vector pET23d (Invitrogen). The correct sequence of the hCDlb coding sequence was confirmed using automated sequencing. Plasmid hb2m-pET23d encoding extracellular human beta2-microglobulin (ffi2m) has been described previously. Both proteins were

expressed separately in E. coli BL21 (Invitrogen) and purified from inclusion bodies as described below.

The extracellular al-a3 domains of human CDlb (SWISS- PROT: P29016) and (32m were synthesised using a prokaryotic expression system (pET23d; Novagen, Milwaukee, WI). Both proteins were purified from E. coli (strain BL21) inclusion bodies, which were subsequently solubilised using 6M guanidine buffer containing lOmM DTT. Refolding of the fully denatured and reduced proteins was carried out at room temperature by dilution into buffer 1 (1M Urea, 300mM L-Arginine, 50mM Tris pH 7.5, 2mM EDTA, 5mM reduced glutathione, 0.5mM oxidized glutathione) supplemented with 500 uM hexadecyltrimethyl- ammoniumbromide (SIGMA, Illinois, USA) and 1 uM of either synthetic GM28 ligand or soy bean purified PI ligand (AVANTILIPIDS, USA). To remove excess detergent molecules methyl-p-cyclodextrin (FLUKA, Dorset, UK) was added to the refolding mix after 3 days. The refolding mix was concentrated using Amicon stir cells (AMICON, USA) and PM10 membranes (MILLIPORE). The soluble protein fractions were separated from the concentrated refolding mix by size exclusion chromatography using fast liquid pressure chromatography (FPLC; AMERSHAM PHARMACIA, UK) using a Superdex75 16/26 prep grade column (AMERSHAM PHARMACIA) equilibrated with buffer 2 (Tris 20mM, pH 6.0, 30mM NaCl). Monomeric hCDlb/hp2m-ligand complexes were collected at 150ml elution volume and repurified once in the same buffer. The pure protein peak containing purified monomeric hCDlb/h « 2m-ligand complexes was concentrated at 5mg/ml and used for sitting drop crystallisation

Crystallisation The best crystals for both complexes hCDlb/h « 2m-GM2 (CDlb/GM2) and hCDlb/hß2m-PI (CDlb/PI) were grown at 20°C from 2, of hCDlb protein at 5mg/ml with lul of precipitant (0.2M Lithium Nitrate, 20% w/v Polyethylene Glycol 3350, pH 7.1).

Structure Determination Crystals were flash frozen at 100K in mother liquor containing 20% glycerol. Diffraction data from one CDlb/GM2 crystal were collected at beamline ID-14 EH2 (ESRF, Grenoble France) with 0. 933A radiation, recorded on an ADSC Q4 CCD detector. Diffraction data from two CDlb/PI crystals were collected at beam line ID-29 (ESRF, Grenoble, France) with 0. 977A radiation, recorded on an ADSC Q210 detector.

Processing, merging and reduction of the data were achieved using programs DENZO and SCALEPACK. Processing statistics are given in the Supplementary Information.

The crystals belong to space group C2221 (a=87. 53A b=176. 89A c=75. 25A for CDlb/GM2 and a=87. 88A b=177. ooA c=75. 28A for CDlb/PI). In each case, one CD1 molecule per asymmetric unit is present, plus 63% solvent.

The molecular replacement solutions for both the CDlb/GM2 and CDlb/PI crystals were identified with the program AmoRe23, using respectively, as models, the 2. 8A resolution structure of mCDld (PDB accession code 1CD1) and the protein component of a partially refined structure of CDlb/GM2. The CNS program suite was used for refinement24. Approximately 3% of reflections were set aside for the Rfree calculations (535 and 751 observations

respectively for the GM2-Cdlb and PI-CDlb structures).

The initial rigid body refinement, allowing the al, a2, a3 and ß2m domains to move independently, resulted in an RworkOf 43. 2% (Rfree of 42. 2%) for the CDlb/GM2 and RworkOf 27. 7% (Rfree of 25. 96%) for the CDlb/PI structure. The models were improved through subsequent rebuilding and refinement cycles, which included positional and restrained B factor refinement, geometric regularization, and for the CDlb/PI structure, simulated annealing. The models were rebuilt with the program 025 into weighted 2Fo-Fc and Fo-Fc ccaic OMIT maps. In the first cycle of the refinement of the GM2-CDlb structure, the murine CDld ß2m sequence was replaced with human CDlb ß2m from an HLA-B8 structure (PDB accession code 1AGE). Clear electron density allowed residues in the a3 domain of Cdld to be mutated to the corresponding residues of CDlb. Further rounds of refinement enabled the rest of the CDlb residues to be located.

Once electron density for segments of acyl chains and individual waters could be identified, for the CDlb/GM2 (Rwork of 25. 4% (free=30. 2%) and for the CDlb/PI (Rworkof 28. 1% (Rfree=30. 2%), these were modelled into the missing density. Atomic models and parameters for the non-glycan portions of the GM2 and PI ligands were obtained from the lipid structure library26 (http://www. biochem. missouri. edu/-lesa/LIPIDS/membrane li pid. html). Topology and parameter files for CNS were then produced with the program PRODGM 27 and subsequently edited. Detergent molecules were modelled as alkyl chains.

The final refined structures showed good stereochemistry as assessed with the program PROCHECK28. The final model

of CDlb/GM2 has an Rorkof 22. 4% (Rfree=27. 5%) and comprises the CDlb heavy chain (residues A4-A279), the ß2m (residues BO-B99), 40 waters and 100 lipid ligand atoms. The final model of CDlb/PI has an RWorkof 20.3% (Rfree=23. 3%) and comprises the CDlb heavy chain (residues A3-A279), the ß2m (residues BO-B99), 232 waters, 3 NO3 molecules and 90 lipid ligand atoms. VOLUMES (Esnouf, unpublished program) identified cavities as surfaces accessible to methyls (1. 7A radius), but not to large probes (6A radius). The figures have been prepared using Bobscript9 and Raster3D3°.

The completeness of the protein and the ligands in the two models increased over the course of the refinement.

Comparisons between the GM2-CDlb and PI-CDlb structures furthermore eased the rebuilding procedure of each model.

Special care was taken during the refinement to keep the gap between the RwOrkand Rfree as small as possible, and the Rfree lower after each refinement cycle.

Generation of fluorescent CDld tetramers and FACS analysis Biotinylated human CDld molecules loaded with the synthetic glycolipid alpha-galactosylceramide (aGC) were generated from completely denatured and reduced inclusion body protein (see Methods-Protein expression, refolding and crystallization). The refolded CDld molecules were used to generate CDld/aGC-tetramers by binding the biotinylated CDld/aGC-complexes to fluorescent streptavidin. The resulting fluorescent CDld/aGC- tetramers were tested for use as diagnostic compositions in the identification of human invariant NKT cells in

vitro by fluorescent cell sorter analysis (FACS). Human invariant NKT cells, known to be highly specific for CDld/aGC-complex, were stained with FITC-anti-TCR Valpha24 antibody (Figure 5c) and RPE-CDld/aGC-tetramers (Figure 5d, e). Staining with propidium iodide allowed dead cells to be gated out of the analysis (Figure 5b).

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Table 1 REMARK coordinates from minimization refinement REMARK refinement resolution: 100-2.8 A REMARK starting r= 0.2241 free_r= 0.2755 REMARK final r=0.2239 free_r=0. 2751 REMARK rmsd bonds= 0.012288 rmsd angles= 1.72965 REMARK= 4.14112 REMARK target= mif cycles= 1 steps= 200 REMARK sg= C222 (1) a= 87.527 b= 176.885 c= 75.250 alpha= 90 beta= 90 gamma= 90 REMARK parameter file 1 : CNSTOPPAR : protein. param REMARK parameter file 2 : CNSTOPPAR : water_rep. param REMARK parameter file 3 : gm2. param REMARK molecular structure file : water_delete_swt2. mff REMARK input coordinates: bindividual_swt2. pdb REMARK reflection file= smallspot ren_notrun. cv REMARK ncs= none REMARK B-correction resolution: 6.0-2. 8 REMARK initial B-factor correction applied to fobs : REMARK B11=-2. 215 B22= 6.610 B33=-4.395 REMARK B12= 0.000 B13= 0.000 B23= 0.000 REMARK B-factor correction applied to coordinate array B:-0. 780 REMARK bulk solvent: density level= 0.26028 e/A"3, B-factor= 10 AA2 REMARK reflections with iFobsl/sigma_F < 0.0 rejected REMARK reflections with ifobsl > 10000 * rms (Fobs) rejected REMARK theoretical total number of refl. in resol. range: 14775 (100.0 %) REMARK number of unobserved reflections (no entry or IFI=O) : 1857 (12. 6 %) REMARK number of reflections rejected: 0 (0. 0 %) REMARK total number of reflections used: 12918 (87.4 %) REMARK number of reflections in working set: 12383 (83.8 %) REMARK number of reflections in test set: 535 (3. 6 %) CRYST1 87.527 176.885 75.250 90.00 90.00 90.00 C 2 2 21 REMARK FILENAME="/raid1/nathan/cd1/october_ref/minimize2_swt2.pdb" REMARK DATE: 12-Jan-02 23: 17: 32 created by user: nathan REMARK VERSION : 1.0 ATOM 1 CB PHE A 4 51.929 43.822-6. 765 1. 00 73. 67 A ATOM 2 CG PHEA 4 52.914 42.984-5. 978 1. 0080. 90 A ATOM 3 CD1 PHE A 4 53.885 43.591-5. 144 1. 00 86.16 A ATOM 4 CD2 PHE A 4 52.853 41.579-6. 047 1. 00 83. 50 A ATOM 5 CE1 PHE A 4 54.787 42.807-4. 377 1. 00 89. 56 A ATOM 6 CE2 PHE A 4 53. 745 40. 772-5.291 1. 00 88. 27 A ATOM 7 CZ PHE A 4 54.717 41.390-4. 449 1. 00 92. 08 A ATOM 8 C PHE A 4 50.178 43.764-4. 926 1. 00 64. 77 A ATOM 9 O PHE A 4 50.671 43.410-3. 846 1. 00 63. 78 A ATOM 10 N PHE A 4 51.682 45.777-5. 216 1. 00 68. 53 A ATOM 11 CA PHE A 4 50.959 44.658-5. 898 1. 00 68. 61 A ATOM 12 N GLN A 5 48. 975 43. 380-5. 345 1. 0060. 65 A ATOM 13 CA GLNA 5 48.093 42.530-4. 549 1. 0055. 97 A ATOM 14 CB GLN A 5 46. 654 43. 022-4. 659 1. 00 55. 20 A ATOM 15 CG GLN A 5 46. 400 44. 373-4. 041 1. 0055. 30 A ATOM 16 CD GLN A 5 44.953 44.768-4. 163 1. 00 56. 97 A ATOM 17 OE1 GLN A 5 44.068 44.111-3. 605 1. 00 61. 94 A ATOM 18 NE2 GLN A 5 44.692 45.826-4. 922 1. 0055. 96 A ATOM 19 C GLN A 5 48.153 41.056-4. 948 1. 00 53. 28 A ATOM 20 O GLN A 5 48.845 40.678-5. 903 1. 00 51. 52 A ATOM 21 N GLYA 6 47.405 40.236-4. 211 1. 0049. 75 A ATOM 22 CA GLY A 6 47.361 38.809-4. 463 1. 00 44. 45 A ATOM 23 C GLY A 6 48.494 38.064-3. 770 1. 00 42. 34 A ATOM 24 O GLY A 6 49.167 38.640-2. 899 1. 00 41. 42 A ATOM 25 N PRO A 7 48.743 36.787-4. 143 1. 00 39.21 A ATOM 26 CD PRO A 7 47.900 36.004-5. 060 1. 00 38. 57 A ATOM 27 CA PRO A 7 49.786 35.917-3. 589 1. 00 35. 72 A ATOM 28 CB PRO A 7 49.525 34.590-4. 296 1. 00 35. 65 A ATOM 29 CG PRO A 7 48.087 34.621-4. 524 1. 00 35. 80 A ATOM 30 C PRO A 7 51.223 36.380-3. 804 1. 00 34. 41 A ATOM 31 O PRO A 7 51.585 36. 872-4. 875 1. 00 32. 37 A ATOM 32 N THR A 8 52.025 36.214-2. 757 1. 00 33. 90 A ATOM 33 CA THRA 8 53.426 36.605-2. 757 1. 00 33. 35 A ATOM 34 CB THRA 8 53.705 37.700-1. 671 1. 00 36. 97 A ATOM 35 OG1 THR A 8 53.603 37.126-0. 359 1. 00 36. 12 A ATOM 36 CG2 THR A 8 52.712 38.869-1. 784 1. 00 37. 48 A ATOM 37 C THR A 8 54. 327 35. 404-2. 464 1. 00 32. 93 A ATOM 38 O THR A 8 55.539 35.564-2. 318 1. 00 33. 88 A ATOM 39 N SER A 9 53.742 34.210-2. 374 1. 00 32. 37 A ATOM 40 CA SERA 9 54.520 33.009-2. 060 1. 00 33. 55 A ATOM 41 CB SER A 9 54.350 32.636-0. 578 1. 00 33. 48 A ATOM 42 OG SERA 9 53.090 32.041-0. 306 1. 00 42. 47 A ATOM 43 C SER A 9 54.237 31.766-2. 881 1. 00 32. 69 A ATOM 44 O SER A 9 53.136 31.576-3. 391 1. 00 32. 67 A ATOM 45 N PHE A 10 55.256 30.924-2. 995 1. 00 30. 68 A ATOM 46 CA PHE A 10 55.126 29.648-3. 677 1. 00 28. 99 A ATOM 47 CB PHE A 10 55.941 29.547-4. 992 1. 00 25. 85 A ATOM 48 CG PHE A 10 55.841 28.176-5. 661 1. 00 22. 15 A ATOM 49 CD1 PHEA 10 54.613 27.728-6. 196 1. 00 19. 07 A ATOM 50 CD2 PHE A 10 56.922 27.273-5. 620 1. 00 22. 38 A ATOM 51 CE1 PHE A 10 54.446 26.401-6. 663 1. 00 11. 47 A ATOM 52 CE2 PHE A 10 56.775 25.932-6. 090 1. 00 17. 57 A ATOM 53 CZ PHE A 10 55.528 25.499-6. 609 1. 00 21. 64 A ATOM 54 C PHE A 10 55. 628 28. 602-2. 708 1. 00 28. 48 A ATOM 55 O PHE A 10 56. 624 28. 823-2. 010 1.00 29. 08 A ATOM 56 N HIS A 11 54.926 27.471-2. 684 1. 00 24. 50 A ATOM 57 CA HIS A 11 55. 308 26. 337-1. 863 1.00 29. 93 A ATOM 58 CB HIS A 11 54.980 26.524-0. 360 1. 00 31. 51 A ATOM 59 CG HIS A 11 53.529 26.726-0. 044 1. 00 31. 89 A ATOM 60 CD2 HIS A 11 52. 530 25. 838 0. 177 1.00 28. 38 A ATOM 61 ND1 HIS A 11 52.984 27.976 0.165 1. 0035. 50 A ATOM 62 CE1 HIS A 11 51. 713 27. 848 0. 503 1.00 35. 19 A ATOM 63 NE2 HIS A 11 51.413 26.561 0.518 1. 00 33. 61 A ATOM 64 C HIS A 11 54.766 25.023-2. 362 1. 00 30. 47 A ATOM 65 O HIS A 11 53.693 24.977-2. 971 1. 00 35. 31 A ATOM 66 N VAL A 12 55.557 23.972-2. 175 1. 00 26. 19 A ATOM 67 CA VALA 12 55.124 22.629-2. 529 1. 0024. 00 A ATOM 68 CB VAL A 12 56.170 21.832-3. 351 1. 00 22. 49 A ATOM 69 CG1 VAL A 12 56.179 22.299-4. 789 1. 00 19. 44 A ATOM 70 CG2 VAL A 12 57.549 21.960-2. 759 1. 00 27. 30 A ATOM 71 C VAL A 12 54.862 21.951-1. 197 1. 00 23. 00 A ATOM 72 O VAL A 12 55.469 22.328-0. 191 1. 00 27. 31 A ATOM 73 N ILE A 13 53.860 21.081-1. 149 1. 00 20. 40 A ATOM 74 CA LEA 13 53.558 20.363 0.082 1. 00 19. 37 A ATOM 75 CB ILE A 13 52.163 20.686 0.673 1. 00 16. 80 A ATOM 76 CG2 ILE A 13 52.088 22.156 1.072 1. 00 20. 19 A ATOM 77 CG1 ILE A 13 51.037 20.278-0. 275 1. 0020. 41 A ATOM 78 CD1 ILE A 13 49.661 20.318 0.366 1. 00 10. 24 A ATOM 79 C ILE A 13 53.720 18.870-0. 116 1. 00 23. 25 A ATOM 80 O ! LEA 13 53.701 18.376-1. 243 1. 00 30. 02 A ATOM 81 N GLN A 14 53.881 18.150 0.983 1. 00 24. 63 A ATOM 82 CA GLN A 14 54.067 16.712 0.917 1. 00 23. 15 A ATOM 83 CB GLN A 14 55.554 16.387 0.950 1. 00 18. 82 A ATOM 84 CG GLN A 14 55.884 14.907 0.848 1. 00 27. 43 A ATOM 85 CD GLN A 14 57.294 14.574 1.301 1. 00 32. 61 A ATOM 86 OE1 GLN A 14 57.571 13.435 1.651 1. 00 38. 93 A ATOM 87 NE2 GLN A 14 58.190 15.559 1.295 1. 00 26. 84 A ATOM 88 C GLN A 14 53.396 16.036 2.089 1. 00 25. 54 A ATOM 89 O GLN A 14 53.544 16.469 3.230 1. 00 27. 20 A ATOM 90 N THR A 15 52.652 14.977 1.795 1. 00 26. 19 A ATOM 91 CA THRA 15 52.003 14.190 2.832 1. 0025. 06 A ATOM 92 CB THRA 15 50.508 14.404 2.887 1. 00 19. 72 A ATOM 93 OG1 THR A 15 50.241 15.790 3.097 1. 00 24. 28 A ATOM 94 CG2 THR A 15 49.916 13.602 4.036 1. 00 20. 03 A ATOM 95 C THR A 15 52.302 12.744 2.517 1. 00 24. 30 A ATOM 96 O THR A 15 51.807 12.202 1.521 1. 00 27. 68 A ATOM 97 N SERA 16 53.118 12.137 3.369 1. 00 18. 72 A ATOM 98 CA SERA 16 53.507 10.762 3.185 1. 0022. 71 A ATOM 99 CB SER A 16 55.025 10.651 3.087 1. 00 20. 77 A ATOM 100 OG SER A 16 55.504 11.334 1.944 1. 00 26. 37 A ATOM 101 C SER A 16 52.941 9.852 4.259 1. 00 25. 87 A ATOM 102 O SER A 16 53.372 9.874 5.412 1. 00 25. 30 A ATOM 103 N SER A 17 51.945 9.068 3.862 1. 00 28. 31 A ATOM 104 CA SERA 17 51.289 8.128 4.749 1. 00 32. 91 A ATOM 105 CB SER A 17 49.813 8.000 4.367 1. 00 31. 41 A ATOM 106 OG SER A 17 49.201 9.275 4.266 1. 00 39. 90 A ATOM 107 C SER A 17 51.985 6.765 4.677 1. 00 37. 46 A ATOM 108 O SER A 17 52.086 6.161 3.597 1. 00 39. 16 A ATOM 109 N PHE A 18 52.518 6.330 5.820 1. 00 36. 30 A ATOM 110 CA PHEA 18 53.200 5.041 5.944 1. 0035. 20 A ATOM 111 CB PHEA 18 54.518 5.197 6.706 1. 0034. 82 A ATOM 112 CG PHE A 18 55.566 5.943 5.949 1. 00 34. 59 A ATOM 113 CD1 PHE A 18 55.631 7.340 6. 007 1.00 34. 76 A ATOM 114 CD2 PHE A 18 56.482 5.256 5.144 1. 00 37. 46 A ATOM 115 CE1 PHE A 18 56.597 8.055 5.265 1. 0031. 54 A ATOM 116 CE2 PHE A 18 57.459 5.956 4.388 1. 00 38. 15 A ATOM 117 CZ PHE A 18 57.512 7.365 4.453 1. 00 33. 75 A ATOM 118 C PHE A 18 52.274 4.131 6.721 1. 00 34. 41 A ATOM 119 O PHE A 18 52.008 4.386 7.894 1. 00 36. 11 A ATOM 120 N THR A 19 51.768 3.090 6.063 1. 00 34. 93 A ATOM 121 CA THRA 19 50.842 2.156 6. 704 1. 00 36. 53 A ATOM 122 CB THR A 19 49.795 1.634 5. 713 1. 00 36. 14 A ATOM 123 OG1 THR A 19 49.468 2.672 4.780 1. 00 42. 02 A ATOM 124 CG2 THR A 19 48.524 1.229 6.439 1. 00 30. 45 A ATOM 125 C THRA 19 51.603 1.007 7.352 1. 0036. 28 A ATOM 126 O THR A 19 51.368 0.688 8.522 1. 00 39. 62 A ATOM 127 N ASN A 20 52.486 0.378 6.581 1. 0036. 11 A ATOM 128 CA ASN A 20 53.330-0. 710 7.081 1. 00 34. 84 A ATOM 129 CB ASN A 20 52.685-2. 111 6. 917 1. 00 28. 80 A ATOM 130 CG ASNA 20 52.525-2. 548 5.462 1. 0037. 54 A ATOM 131 OD1 ASN A 20 53.505-2. 692 4.718 1. 00 34. 12 A ATOM 132 ND2 ASN A 20 51.280-2. 783 5. 055 1. 00 37. 94 A ATOM 133 C ASN A 20 54.734-0. 625 6. 475 1. 00 34. 18 A ATOM 134 O ASN A 20 55.043 0.286 5. 696 1. 00 29. 48 A ATOM 135 N SERA 21 55. 570-1.585 6. 854 1. 00 36. 12 A ATOM 136 CA SERA 21 56.963-1. 698 6. 421 1. 0037. 11 A ATOM 137 CB SERA 21 57.554-2. 989 6.999 1. 0041. 05 A ATOM 138 OG SERA 21 56.779-4. 123 6.617 1. 0042. 43 A ATOM 139 C SERA 21 57.230-1. 634 4.909 1. 0036. 16 A ATOM 140 O SER A 21 58.320-1. 239 4. 489 1. 00 32. 71 A ATOM 141 N THRA 22 56.235-2. 004 4.100 1. 0036. 32 A ATOM 142 CA THRA 22 56.366-2. 004 2.636 1. 0035. 08 A ATOM 143 CB THRA 22 56.540-3. 445 2.087 1. 0035. 28 A ATOM 144 OG1 THR A 22 55.522-4. 300 2.631 1. 00 36. 30 A ATOM 145 CG2 THR A 22 57.914-3. 991 2.429 1. 00 33. 55 A ATOM 146 C THRA 22 55.198-1. 325 1. 903 1. 00 34. 93 A ATOM 147 O THR A 22 54.998-1. 540 0.705 1. 00 31. 22 A ATOM 148 N TRP A 23 54.431-0. 518 2.631 1. 0037. 09 A ATOM 149 CA TRP A 23 53.300 0.213 2. 066 1. 00 41. 06 A ATOM 150 CB TRPA 23 51.970-0. 374 2.573 1. 0041. 78 A ATOM 151 CG TRPA 23 50.665 0.216 2.033 1. 0045. 59 A ATOM 152 CD2 TRP A 23 49.344-0. 238 2. 343 1. 00 49. 47 A ATOM 153 CE2TRPA 23 48.436 0.599 1.637 1. 0052. 81 A ATOM 154 CE3 TRP A 23 48.830-1. 271 3. 154 1. 0050. 06 A ATOM 155 CD1 TRP A 23 50.506 1.277 1. 170 1. 00 46. 82 A ATOM 156 NE1 TRP A 23 49.179 1.508 0. 932 1. 00 51. 30 A ATOM 157 CZ2 TRP A 23 47.028 0.435 1. 717 1. 00 55. 37 A ATOM 158 CZ3 TRP A 23 47.422-1. 438 3. 237 1. 00 52. 91 A ATOM 159 CH2 TRP A 23 46.542-0. 581 2. 518 1. 00 53. 45 A ATOM 160 C TRPA 23 53.454 1.669 2.486 1. 0042. 53 A ATOM 161 O TRPA 23 53.349 1.996 3.671 1. 0046. 10 A ATOM 162 N ALA A 24 53.616 2.534 1.484 1. 00 42. 53 A ATOM 163 CA ALA A 24 53.784 3.973 1. 683 1. 00 42. 34 A ATOM 164 CB ALA A 24 55.256 4.300 1.874 1. 0037. 91 A ATOM 165 C ALA A 24 53.243 4.771 0.507 1. 0041. 77 A ATOM 166 O ALA A 24 53.624 4.510-0. 637 1. 0044. 84 A ATOM 167 N GLN A 25 52.334 5.710 0. 774 1. 00 39. 63 A ATOM 168 CA GLN A 25 51.794 6.561-0. 291 1. 00 39. 88 A ATOM 169 CB GLNA 25 50.272 6.363-0. 506 1. 0042. 62 A ATOM 170 CG GLNA 25 49.330 6.644 0.687 1. 0055. 15 A ATOM 171 CD GLN A 25 49.034 5.414 1.563 1. 00 58. 69 A ATOM 172 OE1 GLN A 25 47.926 4.861 1. 530 1.00 51. 04 A ATOM 173 NE2 GLN A 25 50.013 5.010 2. 375 1. 0056. 05 A ATOM 174 C GLN A 25 52.169 8.019-0. 024 1. 00 36. 89 A ATOM 175 O GLN A 25 52.297 8.427 1.131 1. 00 35. 60 A ATOM 176 N THRA 26 52.431 8.763-1. 096 1. 0034. 48 A ATOM 177 CA THRA 26 52.818 10.174-1. 014 1. 0031. 30 A ATOM 178 CB THRA 26 54.271 10.376-1. 503 1. 0031. 28 A ATOM 179 OG1 THR A 26 55.154 9.558-0. 729 1. 0042. 52 A ATOM 180 CG2 THR A 26 54.721 11.830-1. 373 1. 0029. 92 A ATOM 181 C THRA 26 51.881 11.046-1. 854 1. 0031. 08 A ATOM 182 O THR A 26 51. 505 10. 676-2.971 1. 00 30. 88 A ATOM 183 N GLNA 27 51.498 12.191-1. 291 1. 0027. 71 A ATOM 184 CA GLN A 27 50.621 13.146-1. 963 1. 00 29. 08 A ATOM 185 CB GLNA 27 49.259 13.236-1. 269 1. 0027. 62 A ATOM 186 CG GLN A 27 48.345 12.047-1. 489 1. 00 27. 61 A ATOM 187 CD GLN A 27 47.290 11.939-0. 411 1. 00 33. 82 A ATOM 188 OE1 GLN A 27 46.172 12.430-0. 569 1. 00 33. 82 A ATOM 189 NE2 GLN A 27 47. 648 11. 305 0. 707 1.00 39. 62 A ATOM 190 C GLNA 27 51.297 14.504-1. 948 1. 0029. 47 A ATOM 191 O GLN A 27 51.757 14.961-0. 896 1. 00 34. 18 A ATOM 192 N GLYA 28 51. 364 15.133-3. 120 1. 00 27. 21 A ATOM 193 CA GLYA 28 51.997 16.437-3. 243 1. 0024. 49 A ATOM 194 C GLYA 28 51.227 17.401-4. 119 1. 0021. 22 A ATOM 195 O GLYA 28 50.300 16.989-4. 827 1. 0019. 53 A ATOM 196 N SERA 29 51. 596 18.681-4. 044 1. 0020. 10 A ATOM 197 CA SERA 29 50.966 19.763-4. 823 1. 0023. 73 A ATOM 198 CB SERA 29 49.494 19.965-4. 419 1. 0021. 25 A ATOM 199 OG SERA 29 49.365 20.035-3. 014 1. 00 15. 47 A ATOM 200 C SERA 29 51. 707 21. 085-4. 656 1. 00 22. 87 A ATOM 201 O SERA 29 52.344 21.314-3. 626 1. 0023. 19 A ATOM 202 N GLY A 30 51.597 21.947-5. 667 1. 00 19. 65 A ATOM 203 CA GLYA 30 52.230 23.259-5. 636 1. 0020. 83 A ATOM 204 C GLYA 30 51.175 24.335-5. 439 1. 0021. 10 A ATOM 205 O GLY A 30 50. 117 24. 324-6. 080 1. 0021. 74 A ATOM 206 N TRPA 31 51.450 25.248-4. 516 1. 0018. 57 A ATOM 207 CA TRP A 31 50.514 26.309-4. 174 1. 00 19. 43 A ATOM 208 CB TRPA 31 50.027 26.148-2. 712 1. 0021. 34 A ATOM 209 CG TRPA 31 49.475 24.786-2. 379 1. 0026. 45 A ATOM 210 CD2TRPA 31 48.095 24.422-2. 276 1. 0031. 52 A ATOM 211 CE2 TRP A 31 48.043 23.004-2. 195 1. 0032. 06 A ATOM 212 CE3 TRP A 31 46.890 25.150-2. 252 1. 0032. 10 A ATOM 213 CD1 TRP A 31 50.181 23.614-2. 305 1. 00 25. 22 A ATOM 214 NE1 TRP A 31 49.332 22.546-2. 217 1. 00 28. 18 A ATOM 215 CZ2 TRP A 31 46.825 22.293-2. 104 1. 0034. 27 A ATOM 216 CZ3 TRP A 31 45. 663 24. 440-2. 154 1. 0037. 09 A ATOM 217 CH2TRPA 31 45.649 23.024-2. 086 1. 0035. 19 A ATOM 218 C TRPA 31 51.141 27.677-4. 308 1. 0019. 94 A ATOM 219 O TRPA 31 52.351 27.828-4. 247 1. 0021. 30 A ATOM 220 N LEU A 32 50.275 28.673-4. 441 1. 00 20. 78 A ATOM 221 CA LEU A 32 50.630 30.081-4. 529 1. 00 16. 90 A ATOM 222 CB LEU A 32 50. 275 30. 605-5. 915 1. 00 18. 29 A ATOM 223 CG LEU A 32 51. 259 31.474-6. 701 1. 00 23. 71 A ATOM 224 CD1 LEU A 32 52.682 30.932-6. 676 1. 00 21. 52 A ATOM 225 CD2 LEU A 32 50.765 31.531-8. 132 1. 0022. 17 A ATOM 226 C LEU A 32 49.648 30.552-3. 473 1. 00 19. 67 A ATOM 227 O LEU A 32 48.444 30.663-3. 747 1. 00 21. 65 A ATOM 228 N ASP A 33 50.151 30.690-2. 239 1. 0019. 38 A ATOM 229 CA ASP A 33 49. 357 31.014-1. 039 1. 0021. 87 A ATOM 230 CB ASP A 33 48.649 32. 384-1. 125 1. 0033. 13 A ATOM 231 CG ASP A 33 49.531 33.557-0. 668 1. 0043. 30 A ATOM 232 OD1 ASP A 33 50. 773 33. 499-0. 838 1. 00 41. 40 A ATOM 233 OD2 ASP A 33 48.959 34.574-0. 185 1. 0045. 82 A ATOM 234 C ASP A 33 48.355 29.847-0. 862 1. 00 21. 96 A ATOM 235 O ASP A 33 48.759 28.688-0. 941 1. 00 23. 78 A ATOM 236 N ASP A 34 47.059 30.135-0. 769 1. 0022. 58 A ATOM 237 CA ASP A 34 46.046 29.092-0. 596 1. 00 25. 32 A ATOM 238 CB ASP A 34 44.837 29.640 0.162 1. 00 30. 12 A ATOM 239 CG ASP A 34 45.183 30.204 1.525 1. 00 39. 55 A ATOM 240 OD1 ASP A 34 46.380 30.430 1.829 1. 00 45. 91 A ATOM 241 OD2 ASP A 34 44.229 30.435 2.297 1. 00 44. 80 A ATOM 242 C ASP A 34 45.549 28.527-1. 924 1. 00 27. 43 A ATOM 243 O ASP A 34 44.794 27.550-1. 944 1. 00 29. 35 A ATOM 244 N LEU A 35 45.971 29.142-3. 028 1. 00 28. 35 A ATOM 245 CA LEU A 35 45. 554 28. 740-4. 376 1. 00 24. 26 A ATOM 246 CB LEU A 35 45.525 29.970-5. 288 1. 00 26. 06 A ATOM 247 CG LEU A 35 44.494 31.110-5. 186 1. 0028. 65 A ATOM 248 CD1 LEU A 35 43.653 31.123-3. 914 1. 00 23. 81 A ATOM 249 CD2 LEU A 35 45.234 32.423-5. 364 1. 00 22. 54 A ATOM 250 C LEU A 35 46.473 27.693-4. 976 1. 00 23. 33 A ATOM 251 O LEU A 35 47. 688 27. 894-5. 052 1. 00 24. 55 A ATOM 252 N GLN A 36 45.881 26. 591-5. 424 1. 00 19. 62 A ATOM 253 CA GLN A 36 46.631 25.485-6. 019 1. 00 19. 24 A ATOM 254 CB GLN A 36 45.846 24.178-5. 860 1. 00 18. 97 A ATOM 255 CG GLN A 36 46.697 22.932-5. 920 1. 00 16. 44 A ATOM 256 CD GLN A 36 45.896 21.641-5. 926 1. 00 22. 38 A ATOM 257 OE1 GLN A 36 44.738 21.593-5. 485 1. 00 25. 72 A ATOM 258 NE2 GLN A 36 46.520 20.573-6. 424 1. 00 12. 75 A ATOM 259 C GLN A 36 46.908 25.722-7. 491 1. 00 17. 93 A ATOM 260 O GLNA 36 46.011 26.113-8. 234 1. 0022. 05 A ATOM 261 N ILEA 37 48.157 25.505-7. 895 1. 0019. 94 A ATOM 262 CA ILE A 37 48.571 25.657-9. 289 1. 00 21. 88 A ATOM 263 CB ILE A 37 49.543 26.834-9. 505 1. 00 21. 23 A ATOM 264 CG2 ILEA 37 48.791 28.148-9. 339 1. 0018. 65 A ATOM 265 CG1 ILE A 37 50.742 26.747-8. 555 1. 00 25. 37 A ATOM 266 CD1 ILE A 37 51.782 27.836-8. 766 1. 00 27. 96 A ATOM 267 C ILE A 37 49. 161 24. 360-9. 833 1. 0026. 85 A ATOM 268 LEA37 49. 161 24. 134-11. 048 1. 00 32. 79 A ATOM 269 N HIS A 38 49. 660 23.508-8. 937 1. 00 26. 00 A ATOM 270 CA HIS A 38 50.208 22.210-9. 335 1. 0026. 02 A ATOM 271 CB HIS A 38 51.713 22.102-9. 092 1. 0023. 62 A ATOM 272 CG HIS A 38 52.524 23.149-9. 772 1. 00 23. 24 A ATOM 273 CD2 HIS A 38 52. 845 23. 322-11. 074 1. 00 29. 44 A ATOM 274 ND1 HIS A 38 53.137 24.171-9. 084 1. 0026. 10 A ATOM 275 CE1 HIS A 38 53.805 24.928-9. 934 1. 00 27. 52 A ATOM 276 NE2 HIS A 38 53. 643 24. 436-11. 148 1. 00 34. 86 A ATOM 277 C HIS A 38 49.548 21. 061-8. 593 1. 00 25. 80 A ATOM 278 O HIS A 38 49.110 21.187-7. 451 1. 0027. 91 A ATOM 279 N GLYA 39 49.480 19.937-9. 280 1. 0025. 69 A ATOM 280 CA GLYA 39 48.930 18.728-8. 713 1. 0028. 39 A ATOM 281 C GLYA 39 50.019 17.718-8. 985 1. 0028. 37 A ATOM 282 O GLYA 39 50.924 17.980-9. 789 1. 0028. 39 A ATOM 283 N TRP A 40 49.970 16.583-8. 306 1. 0027. 04 A ATOM 284 CA TRPA 40 50.978 15.576-8. 525 1. 0028. 49 A ATOM 285 CB TRP A 40 51.951 15.527-7. 347 1. 0023. 71 A ATOM 286 CG TRPA 40 53.123 14.592-7. 537 1. 0029. 17 A ATOM 287 CD2TRPA 40 54.304 14.829-8. 319 1. 0025. 51 A ATOM 288 CE2 TRP A 40 55.125 13.679-8. 193 1. 0026. 58 A ATOM 289 CE3 TRP A 40 54. 756 15. 904-9.111 1. 0026. 61 A ATOM 290 CD1 TRP A 40 53.272 13.348-6. 990 1. 00 27. 10 A ATOM 291 NE1 TRP A 40 54. 465 12. 794-7. 382 1. 00 30. 70 A ATOM 292 CZ2 TRP A 40 56.382 13.569-8. 829 1. 0028. 89 A ATOM 293 CZ3 TRP A 40 56.014 15.798-9. 754 1. 00 30. 05 A ATOM 294 CH2 TRP A 40 56. 808 14. 634-9. 603 1. 00 29. 31 A ATOM 295 C TRP A 40 50.349 14. 230-8.769 1. 00 31. 95 A ATOM 296 O TRP A 40 49.533 13.764-7. 971 1. 00 33. 56 A ATOM 297 N ASP A 41 50.737 13.620-9. 888 1. 0036. 76 A ATOM 298 CA ASP A 41 50.253 12.299-10. 256 1. 0042. 55 A ATOM 299 CB ASP A 41 50.038 12.186-11. 765 1. 0045. 43 A ATOM 300 CG ASP A 41 49.187 10.989-12. 134 1. 0048. 05 A ATOM 301 OD1 ASP A 41 47.943 11.142-12. 173 1. 00 46. 59 A ATOM 302 OD2 ASP A 41 49.765 9.898-12. 347 1. 00 39. 63 A ATOM 303 C ASP A 41 51. 309 11. 315-9.791 1. 0045. 00 A ATOM 304 O ASPA 41 52. 296 11. 074-10. 489 1. 00 46. 53 A ATOM 305 N SERA 42 51.075 10.773-8. 595 1. 0049. 95 A ATOM 306 CA SERA 42 51.948 9.815-7. 900 1. 0052. 11 A ATOM 307 CB SERA 42 51.285 9.381-6. 587 1. 00 53. 95 A ATOM 308 OG SERA 42 49.912 9.073-6. 790 1. 0058. 24 A ATOM 309 C SERA 42 52.408 8.588-8. 682 1. 00 51. 65 A ATOM 3100 SERA 42 53.586 8.226-8. 614 1. 0049. 09 A ATOM 311 N ASP A 43 51.482 7.997-9. 444 1. 00 53. 00 A ATOM 312 CA ASP A 43 51.735 6.807-10. 261 1. 0054. 32 A ATOM 313 CB ASP A 43 50.417 6.220-10. 790 1. 00 58. 89 A ATOM 314 CG ASP A 43 49.625 5.468-9. 720 1. 00 63. 99 A ATOM 315 OD1 ASP A 43 48.414 5.752-9. 569 1.00 66. 57 A ATOM 316 OD2 ASP A 43 50.200 4.580-9. 047 1. 0062. 46 A ATOM 317 C ASP A 43 52.692 7.051-11. 426 1.00 53. 67 A ATOM 318 O ASP A 43 53.673 6.318-11. 584 1. 00 55. 80 A ATOM 319 N SERA 44 52.419 8.089-12. 221 1. 0051. 38 A ATOM 320 CA SERA 44 53.263 8.434-13. 374 1. 00 49. 75 A ATOM 321 CB SERA 44 52.475 9.256-14. 402 1. 0048. 96 A ATOM 322 OG SERA 44 52.025 10.486-13. 860 1. 0045. 82 A ATOM 323 C SERA 44 54.525 9.193-12. 960 1.00 48. 86 A ATOM 3240 SERA 44 55.532 9.183-13. 680 1.00 49. 87 A ATOM 325 N GLY A 45 54.448 9.838-11. 793 1. 00 46. 48 A ATOM 326 CA GLY A 45 55.552 10.616-11. 254 1. 0042. 62 A ATOM 327 C GLY A 45 55.706 11.958-11. 945 1. 0040. 45 A ATOM 328 O GLY A 45 56.814 12.495-12. 016 1. 0044. 25 A ATOM 329 N THR A 46 54. 596 12. 506-12. 436 1.00 36. 02 A ATOM 330 CA THR A 46 54.603 13.779-13. 153 1. 0036. 84 A ATOM 331 CB THR A 46 54.251 13.586-14. 656 1.00 37. 13 A ATOM 332 OG1 THR A 46 53.091 12.758-14. 779 1. 00 42. 41 A ATOM 333 CG2 THRA46 55. 408 12. 963-15. 4231. 0033. 20 A ATOM 334 C THR A 46 53.656 14.819-12. 561 1. 0036. 82 A ATOM 335 O THR A 46 52.687 14.476-11. 871 1. 0037. 22 A ATOM 336 N ALA A 47 53.948 16.088-12. 851 1. 0033. 38 A ATOM 337 CA ALA A 47 53.160 17.222-12. 373 1. 0032. 35 A ATOM 338 CB ALA A 47 54.029 18.459-12. 320 1. 0031. 49 A ATOM 339 C ALA A 47 51.921 17.485-13. 223 1.00 30. 63 A ATOM 340 O ALA A 47 51.934 17.236-14. 433 1. 0034. 77 A ATOM 341 N ILE A 48 50. 830 17. 889-12. 564 1.00 26. 35 A ATOM 342 CA ILE A 48 49. 566 18. 219-13. 237 1. 00 26. 08 A ATOM 343 CB ILE A 48 48.347 17.552-12. 569 1. 0022. 25 A ATOM 344 CG2 ILEA 48 47.061 17.909-13. 326 1.00 25. 64 A ATOM 345 CG1 ILE A 48 48. 522 16. 035-12. 552 1.00 23. 04 A ATOM 346 CD1 ILEA 48 47. 518 15. 307-11. 675 1. 00 39. 79 A ATOM 347 C ILE A 48 49. 450 19. 737-13. 146 1.00 26. 17 A ATOM 348 O ILE A 48 49. 288 20. 287-12. 058 1. 00 28. 72 A ATOM 349 N PHE A 49 49. 531 20. 398-14. 297 1. 00 22. 39 A ATOM 350 CA PHE A 49 49.506 21.854-14. 366 1. 00 22. 56 A ATOM 351 CB PHE A 49 50.401 22.300-15. 509 1. 0026. 44 A ATOM 352 CG PHEA 49 51.810 21.805-15. 393 1. 0027. 04 A ATOM 353 CD1 PHE A 49 52. 796 22.593-14.753 1.00 27. 59 A ATOM 354 CD2 PHE A 49 52. 170 20. 559-15. 935 1. 00 18. 96 A ATOM 355 CE1 PHE A 49 54. 130 22. 149-14. 657 1. 00 21. 93 A ATOM 356 CE2 PHE A 49 53. 498 20. 093-15. 851 1. 0023. 82 A ATOM 357 CZ PHEA 49 54.486 20.890-15. 212 1. 0025. 58 A ATOM 358 C PHE A 49 48. 118 22. 467-14. 473 1. 0024. 09 A ATOM 359 O PHE A 49 47. 607 22. 712-15. 572 1.00 25. 99 A ATOM 360 N LEU A 50 47.565 22.794-13. 306 1. 0022. 89 A ATOM 361 CA LEU A 50 46.218 23.338-13. 152 1. 00 22. 84 A ATOM 362 CB LEU A 50 45.876 23.385-11. 664 1. 0023. 67 A ATOM 363 CG LEU A 50 45.426 22.126-10. 903 1. 00 26. 02 A ATOM 364 CD1 LEU A 50 45.733 20.811-11. 584 1. 00 21. 22 A ATOM 365 CD2 LEU A 50 46.053 22.163-9. 550 1. 0024. 11 A ATOM 366 C LEU A 50 45.850 24.662-13. 828 1. 0024. 54 A ATOM 367 O LEU A 50 44. 664 24.971-13. 984 1. 0022. 09 A ATOM 368 N LYS A 51 46. 857 25. 454-14. 189 1.00 27. 00 A ATOM 369 CA LYS A 51 46.643 26.741-14. 866 1. 00 30. 20 A ATOM 370 CB LYS A 51 46.887 27.906-13. 888 1. 0032. 32 A ATOM 371 CG LYS A 51 45.692 28.259-12. 967 1. 00 36. 44 A ATOM 372 CD LYS A 51 44.456 28.883-13. 633 1. 00 48. 38 A ATOM 373 CE LYS A 51 43.385 29.546-12. 748 1. 00 50. 72 A ATOM 374 NZ LYS A 51 42.605 28.601-11. 889 1. 0050. 70 A ATOM 375 C LYS A 51 47.577 26.808-16. 094 1. 0030. 57 A ATOM 376 O LYS A 51 48.661 26.216-16. 070 1. 0032. 04 A ATOM 377 N PRO A 52 47.160 27.487-17. 198 1. 00 30. 66 A ATOM 378 CD PRO A 52 45.858 28.134-17. 464 1. 00 29. 01 A ATOM 379 CA PRO A 52 48.021 27.571-18. 395 1. 0028. 53 A ATOM 380 CB PRO A 52 47.116 28.265-19. 420 1. 0027. 45 A ATOM 381 CG PRO A 52 46.188 29.073-18. 582 1. 0027. 63 A ATOM 382 C PRO A 52 49.376 28.279-18. 228 1. 00 26. 79 A ATOM 383 O PRO A 52 50. 255 28. 159-19. 077 1. 00 29. 65 A ATOM 384 N TRP A 53 49. 541 28. 967-17. 103 1.00 26. 93 A ATOM 385 CA TRP A 53 50.768 29.685-16. 766 1. 00 26. 43 A ATOM 386 CB TRP A 53 50.453 31.152-16. 438 1. 00 23. 67 A ATOM 387 CG TRPA 53 49.229 31.380-15. 576 1. 0026. 65 A ATOM 388 CD2 TRP A 53 49.143 31. 283-14. 147 1. 00 26. 26 A ATOM 389 CE2 TRP A 53 47.799 31.590-13. 788 1. 0027. 65 A ATOM 390 CE3 TRP A 53 50.067 30.965-13. 128 1. 00 24. 31 A ATOM 391 CD1 TRP A 53 47.975 31.730-16. 010 1. 00 32. 50 A ATOM 392 NE1 TRP A 53 47.115 31.859-14. 943 1. 00 32. 77 A ATOM 393 CZ2 TRP A 53 47. 354 31. 586-12. 447 1. 0027. 82 A ATOM 394 CZ3 TRP A 53 49. 626 30. 959-11. 790 1.00 25. 87 A ATOM 395 CH2TRPA 53 48.275 31.270-11. 466 1. 0024. 59 A ATOM 396 C TRPA 53 51.529 29.042-15. 597 1. 0029. 07 A ATOM 397 O TRP A 53 52. 473 29. 641-15. 070 1.00 29. 14 A ATOM 398 N SERA 54 51.113 27.833-15. 196 1. 0030. 82 A ATOM 399 CA SERA 54 51. 719 27. 089-14. 080 1.00 30. 95 A ATOM 400 CB SERA 54 50.968 25.788-13. 827 1. 0030. 92 A ATOM 401 OG SERA 54 49.644 26.028-13. 404 1. 0034. 23 A ATOM 402 C SERA 54 53.206 26.775-14. 206 1. 0032. 42 A ATOM 403 O SER A 54 53. 857 26. 466-13.211 1. 0029. 96 A ATOM 404 N LYS A 55 53.734 26.850-15. 427 1. 0034. 63 A ATOM 405 CA LYS A 55 55.149 26.588-15. 685 1. 0034. 85 A ATOM 406 CB LYS A 55 55. 365 26. 147-17. 135 1. 0036. 60 A ATOM 407 CG LYS A 55 55.048 24.696-17. 388 1. 00 37. 85 A ATOM 408 CD LYS A 55 55.214 24.191-18. 798 1. 00 46. 57 A ATOM 409 CE LYS A 55 55.034 22.696-19. 009 1. 0055. 19 A ATOM 410 NZ LYS A 55 55.115 22.297-20. 446 1. 0060. 80 A ATOM 411 C LYS A 55 56.015 27.805-15. 390 1. 0033. 64 A ATOM 412 O LYS A 55 57. 233 27. 669-15. 217 1.00 32. 78 A ATOM 413 N GLY A 56 55.381 28.980-15. 311 1. 0031. 28 A ATOM 414 CA GLYA 56 56.101 30.224-15. 062 1. 00 32. 49 A ATOM 415 C GLY A 56 56.932 30.600-16. 275 1. 00 33. 62 A ATOM 416 O GLY A 56 56.446 30.483-17. 403 1. 00 37. 47 A ATOM 417 N ASN A 57 58.193 30.972-16. 053 1. 00 33. 65 A ATOM 418 CA ASNA 57 59.119 31.336-17. 137 1. 0035. 23 A ATOM 419 CB ASN A 57 59.982 32.552-16. 733 1. 00 35. 75 A ATOM 420 CG ASN A 57 60. 798 32.323-15. 446 1. 00 42. 66 A ATOM 421 OD1 ASN A 57 60.438 31.505-14. 588 1. 0047. 45 A ATOM 422 ND2 ASN A 57 61. 884 33. 075-15. 301 1.00 41. 36 A ATOM 423 C ASN A 57 60.016 30.151-17. 540 1. 00 36. 02 A ATOM 424 O ASN A 57 60.830 30. 254-18.471 1. 00 38. 00 A ATOM 425 N PHE A 58 59.817 29.022-16. 858 1. 00 35. 33 A ATOM 426 CA PHE A 58 60.591 27.796-17. 063 1. 00 33. 24 A ATOM 427 CB PHEA 58 60.387 26.845-15. 870 1. 00 30. 04 A ATOM 428 CG PHE A 58 61. 118 27. 257-14. 593 1.00 27. 22 A ATOM 429 CD1 PHEA 58 61.322 26.313-13. 572 1. 0024. 65 A ATOM 430 CD2 PHE A 58 61.612 28.567-14. 403 1. 00 31. 06 A ATOM 431 CE1 PHE A 58 62. 010 26. 659-12. 373 1.00 25. 87 A ATOM 432 CE2 PHE A 58 62. 302 28. 933-13. 215 1.00 32. 32 A ATOM 433 CZ PHEA 58 62.502 27.975-12. 198 1. 0028. 31 A ATOM 434 C PHEA 58 60.348 27.047-18. 374 1. 0033. 81 A ATOM 435 O PHE A 58 59.234 27.048-18. 917 1. 0030. 97 A ATOM 436 N SERA 59 61. 417 26. 430-18. 879 1.00 34. 53 A ATOM 437 CA SERA 59 61.373 25.652-20. 117 1. 0036. 87 A ATOM 438 CB SERA 59 62.756 25.627-20. 792 1. 00 34. 39 A ATOM 439 OG SERA 59 63.746 25.029-19. 970 1. 0033. 57 A ATOM 440 C SER A 59 60.894 24.229-19. 841 1. 00 37. 64 A ATOM 441 O SER A 59 60.966 23.755-18. 703 1. 00 37. 74 A ATOM 442 N ASP A 60 60. 444 23. 540-20.891 1. 00 41. 01 A ATOM 443 CA ASP A 60 59.961 22.165-20. 771 1. 0044. 11 A ATOM 444 CB ASP A 60 59.223 21.728-22. 041 1. 0044. 15 A ATOM 445 CG ASP A 60 57.860 22.403-22. 190 1. 0050. 14 A ATOM 446 OD1 ASP. A 60 56. 930 21. 775-22. 751 1. 00 46. 97 A ATOM 447 OD2 ASP A 60 57. 712 23. 565-21. 742 1.00 53. 21 A ATOM 448 C ASP A 60 61.061 21.172-20. 397 1. 00 47. 50 A ATOM 449 O ASP A 60 60.770 20.022-20. 065 1. 00 52. 56 A ATOM 450 N LYS A 61 62.310 21.650-20. 404 1. 0046. 55 A ATOM 451 CA LYS A 61 63.486 20.858-20. 045 1. 00 45. 99 A ATOM 452 CB LYS A 61 64.716 21.354-20. 817 1. 0047. 05 A ATOM 453 CG LYS A 61 65. 986 20.504-20. 638 1. 0050. 16 A ATOM 454 CD LYS A 61 67.333 21.112-21. 061 1. 00 52. 41 A ATOM 455 CE LYS A 61 68.022 22.122-20. 130 1. 0053. 07 A ATOM 456 NZ LYS A 61 67.246 23.378-19. 872 1. 00 52. 88 A ATOM 457 C LYS A 61 63. 700 21. 064-18. 550 1.00 47. 10 A ATOM 458 O LYS A 61 63.921 20.109-17. 800 1. 0047. 19 A ATOM 459 N GLU A 62 63. 605 22. 329-18. 139 1.00 48. 52 A ATOM 460 CA GLU A 62 63.765 22.765-16. 748 1. 00 50. 03 A ATOM 461 CB GLU A 62 63.712 24.299-16. 683 1. 00 51. 72 A ATOM 462 CG GLU A 62 65.019 24.982-16. 321 1. 00 54. 69 A ATOM 463 CD GLU A 62 65.141 25.273-14. 829 1. 00 56. 68 A ATOM 464 OE1 GLU A 62 65. 521 24. 361-14. 057 1. 00 54. 68 A ATOM 465 OE2 GLU A 62 64. 862 26. 427-14. 433 1. 00 55. 36 A ATOM 466 C GLU A 62 62. 676 22. 176-15. 845 1. 00 48. 31 A ATOM 467 O GLU A 62 62. 925 21. 883-14. 673 1. 00 45. 31 A ATOM 468 N VALA 63 61.486 21.983-16. 418 1. 0046. 44 A ATOM 469 CA VALA 63 60.353 21.426-15. 694 1. 0048. 65 A ATOM 470 CB VAL A 63 58. 988 21. 913-16. 298 1. 00 50. 18 A ATOM 471 CG1 VALA 63 58. 487 21. 020-17. 435 1. 00 56. 61 A ATOM 472 CG2 VAL A 63 57. 956 22. 008-15. 216 1. 00 55. 56 A ATOM 473 C VAL A 63 60.430 19.898-15. 601 1. 0048. 16 A ATOM 474 O VAL A 63 59. 912 19. 305-14. 653 1. 0052. 00 A ATOM 475 N ALA A 64 61.081 19.281-16. 589 1. 0046. 68 A ATOM 476 CA ALA A 64 61.246 17.828-16. 640 1. 0043. 64 A ATOM 477 CB ALA A 64 61.499 17.365-18. 069 1. 0042. 27 A ATOM 478 C ALA A 64 62.389 17.403-15. 725 1. 0042. 55 A ATOM 479 O ALA A 64 62.377 16.289-15. 200 1. 0042. 31 A ATOM 480 N GLU A 65 63.354 18.310-15. 532 1. 00 41. 14 A ATOM 481 CA GLU A 65 64.515 18.088-14. 663 1. 0043. 37 A ATOM 482 CB GLU A 65 65.518 19.231-14. 793 1. 00 51. 45 A ATOM 483 CG GLU A 65 66.480 19.148-15. 961 1. 00 59. 65 A ATOM 484 CD GLU A 65 67.345 20.397-16. 068 1. 00 66. 37 A ATOM 485 OE1 GLU A 65 68.025 20.755-15. 073 1. 00 65. 18 A ATOM 486 OE2 GLU A 65 67.329 21.031-17. 144 1. 00 68. 37 A ATOM 487 C GLU A 65 64.026 18.072-13. 229 1. 00 41. 80 A ATOM 488 O GLU A 65 64.432 17.230-12. 428 1. 00 41. 27 A ATOM 489 N LEU A 66 63. 122 19. 008-12. 946 1. 00 39. 24 A ATOM 490 CA LEU A 66 62.504 19.177-11. 639 1. 0036. 80 A ATOM 491 CB LEU A 66 61.773 20.517-11. 581 1. 00 36. 44 A ATOM 492 CG LEU A 66 62.364 21.735-10. 851 1. 00 35. 92 A ATOM 493 CD1 LEU A 66 63.892 21.816-10. 882 1. 00 37. 76 A ATOM 494 CD2 LEU A 66 61. 757 22. 975-11. 473 1. 00 34. 23 A ATOM 495 C LEU A 66 61.553 18.031-11. 324 1. 00 37. 43 A ATOM 496 O LEU A 66 61.521 17.556-10. 184 1. 00 37. 77 A ATOM 497 N GLU A 67 60.831 17.553-12. 342 1. 00 34. 32 A ATOM 498 CA GLU A 67 59.908 16.428-12. 179 1. 00 36. 56 A ATOM 499 CB GLU A 67 59.139 16.144-13. 468 1. 00 37. 42 A ATOM 500 CG GLU A 67 57.838 16.922-13. 608 1. 00 44. 50 A ATOM 501 CD GLU A 67 57.053 16.565-14. 867 1. 00 49. 51 A ATOM 502 OE1 GLU A 67 57.662 16.080-15. 846 1. 00 56. 45 A ATOM 503 OE2 GLU A 67 55.819 16.773-14. 880 1. 00 46. 41 A ATOM 504 C GLU A 67 60. 688 15.182-11.765 1.00 36. 65 A ATOM 505 O GLU A 67 60.279 14.471-10. 849 1. 0037. 62 A ATOM 506 N GLU A 68 61.871 15.021-12. 362 1. 00 37. 46 A ATOM 507 CA GLU A 68 62. 780 13. 903-12. 101 1. 00 35. 41 A ATOM 508 CB GLU A 68 63. 921 13. 909-13. 139 1.00 41. 53 A ATOM 509 CG GLU A 68 65.021 12.830-12. 986 1. 00 51. 51 A ATOM 510 CD GLU A 68 64.582 11.432-13. 415 1. 00 60. 07 A ATOM 511 OE1 GLU A 68 64. 934 10. 456-12. 716 1.00 60. 31 A ATOM 512 OE2GLUA 68 63. 907 11. 304-14. 461 1.00 64. 96 A ATOM 513 C GLU A 68 63.339 13.975-10. 676 1. 0032. 78 A ATOM 514 O GLU A 68 63.377 12.957-9. 982 1. 00 31. 01 A ATOM 515 N ILE A 69 63.726 15.179-10. 235 1. 0029. 36 A ATOM 516 CA LEA 69 64.275 15.379-8. 886 1. 0027. 87 A ATOM 517 CB ILE A 69 64.720 16.865-8. 637 1. 0025. 09 A ATOM 518 CG2 ILE A 69 64.959 17.149-7. 103 1.00 4.18 A ATOM 519 CG1 LEA 69 65.972 17.172-9. 471 1. 00 17. 65 A ATOM 520 CD1 ILE A 69 66.419 18.638-9. 426 1. 00 12. 90 A ATOM 521 C ILE A 69 63.272 14.951-7. 811 1. 0030. 63 A ATOM 522 O LEA 69 63.620 14.170-6. 926 1. 00 31. 56 A ATOM 523 N PHE A 70 62.033 15.431-7. 934 1. 0031. 07 A ATOM 524 CA PHEA 70 60.971 15.114-6. 984 1. 0030. 26 A ATOM 525 CB PHE A 70 59.733 15.984-7. 226 1. 00 24. 78 A ATOM 526 CG PHEA 70 59.929 17.443-6. 898 1. 0025. 92 A ATOM 527 CD1 PHE A 70 60.405 17.845-5. 635 1. 00 27. 00 A ATOM 528 CD2 PHE A 70 59. 619 18.434-7. 849 1. 0025. 49 A ATOM 529 CE1 PHEA 70 60.573 19.228-5. 319 1. 0020. 57 A ATOM 530 CE2 PHE A 70 59.781 19.818-7. 553 1. 00 16.36 A ATOM 531 CZ PHEA 70 60.258 20.212-6. 286 1. 0019. 13 A ATOM 532 C PHEA 70 60.592 13.637-7. 030 1. 0034. 35 A ATOM 533 O PHEA 70 60.393 13.020-5. 982 1. 0034. 59 A ATOM 534 N ARG A 71 60.587 13.063-8. 235 1. 00 34. 68 A ATOM 535 CA ARG A 71 60.244 11.653-8. 450 1. 0036. 19 A ATOM 536 CB ARG A 71 60.217 11. 345-9. 946 1.00 38. 80 A ATOM 537 CG ARG A 71 59.550 10.046-10. 368 1. 0038. 12 A ATOM 538 CD ARG A 71 59.881 9.571-11. 784 1. 00 50. 80 A ATOM 539 NE ARG A 71 59.743 10.646-12. 777 1. 00 58. 26 A ATOM 540 CZ ARG A 71 60. 570 10. 850-13. 8011. 0058. 51 A ATOM 541 NH1 ARG A 71 60. 352 11. 861-14. 635 1. 00 59. 34 A ATOM 542 NH2 ARG A 71 61.609 10.044-13. 999 1. 0061. 88 A ATOM 543 C ARG A 71 61.229 10.721-7. 743 1. 0035. 72 A ATOM 544 O ARG A 71 60.803 9.806-7. 039 1. 00 37. 91 A ATOM 545 N VALA 72 62.532 10.985-7. 887 1. 0035. 06 A ATOM 546 CA VALA 72 63.545 10.153-7. 230 1. 0037. 24 A ATOM 547 CB VALA 72 64.988 10.271-7. 856 1. 0036. 44 A ATOM 548 CG1 VAL A 72 64.945 9.956-9. 347 1. 00 33. 54 A ATOM 549 CG2VALA 72 65.629 11.631-7. 586 1. 0039. 46 A ATOM 550 C VALA 72 63.576 10.409-5. 731 1. 0036. 23 A ATOM 551 O VALA 72 63.908 9.507-4. 961 1. 00 43. 22 A ATOM 552 N TYRA 73 63.180 11.625-5. 335 1. 0035. 97 A ATOM 553 CA TYRA 73 63.112 12.039-3. 928 1. 0033. 09 A ATOM 554 CB TYRA 73 62.899 13.563-3. 805 1. 0025. 52 A ATOM 555 CG TYRA 73 62.367 14.060-2. 466 1. 0025. 43 A ATOM 556 CD1 TYR A 73 63.203 14.146-1. 336 1. 00 27. 77 A ATOM 557 CE1 TYRA 73 62. 692 14.553-0. 068 1. 00 30. 79 A ATOM 558 CD2 TYR A 73 61.004 14.399-2. 309 1. 0024. 42 A ATOM 559 CE2 TYR A 73 60.483 14.797-1. 050 1. 0028. 72 A ATOM 560 CZ TYRA 73 61.331 14.869 0. 063 1.00 33. 24 A ATOM 561 OH TYRA 73 60.821 15.219 1.292 1. 0032. 55 A ATOM 562 C TYRA 73 61.985 11.279-3. 240 1. 0032. 50 A ATOM 563 O TYRA 73 62.205 10.686-2. 201 1. 0033. 75 A ATOM 564 N LEA 74 60.795 11.297-3. 842 1. 0035. 01 A ATOM 565 CA ILEA 74 59.603 10.627-3. 309 1. 0034. 53 A ATOM 566 CB LEA 74 58.349 10.954-4. 187 1. 0033. 84 A ATOM 567 CG2 ILEA 74 57.216 9.939-4. 000 1.00 33. 36 A ATOM 568 CG1 LEA 74 57.869 12.372-3. 845 1. 0030. 81 A ATOM 569 CD1 ILEA 74 56.926 12.992-4. 852 1. 0035. 17 A ATOM 570 C ILE A 74 59.835 9.136-3. 114 1. 00 35. 24 A ATOM 571 O ILE A 74 59.363 8.561-2. 133 1. 0040. 08 A ATOM 572 N PHE A 75 60.634 8.548-4. 003 E1.00 36. 16 A ATOM 573 CA PHEA 75 60.976 7.133-3. 922 1. 0036. 37 A ATOM 574 CB PHEA 75 61.521 6.628-5. 263 1. 00 34. 03 A ATOM 575 CG PHE A 75 61.843 5.153-5. 281 1. 00 38. 00 A ATOM 576 CD1 PHEA 75 60. 812 4. 190-5. 235 1. 00 40. 60 A ATOM 577 CD2 PHE A 75 63. 182 4. 715-5. 346 1.00 39. 54 A ATOM 578 CE1 PHEA 75 61.103 2.799-5. 251 1. 0036. 67 A ATOM 579 CE2 PHEA 75 63.498 3.330-5. 362 1. 0043. 08 A ATOM 580 CZ PHEA 75 62.448 2.367-5. 314 1. 0043. 83 A ATOM 581 C PHE A 75 62.019 6.940-2. 818 1. 00 36. 87 A ATOM 582 O PHE A 75 61.793 6. 181-1. 877 1. 0038. 17 A ATOM 583 N GLYA 76 63.126 7.674-2. 925 1. 0035. 28 A ATOM 584 CA GLYA 76 64.214 7.580-1. 963 1. 0037. 47 A ATOM 585 C GLYA 76 63.885 7.944-0. 527 1. 0038. 49 A ATOM 586 O GLYA 76 64.480 7.392 0.390 1. 0035. 98 A ATOM 587 N PHEA 77 62.928 8. 860-0. 347 1. 0042. 00 A ATOM 588 CA PHEA 77 62.463 9.329 0.966 1. 0041. 35 A ATOM 589 CB PHEA 77 61. 528 10. 546 0. 793 1.00 42. 11 A ATOM 590 CG PHEA 77 60.925 11.061 2.074 1. 0044. 91 A ATOM 591 CD1 PHEA 77 59.570 10.808 2.383 1. 00 47. 44 A ATOM 592 CD2 PHE A 77 61. 700 11. 798 2.981 1. 0044. 57 A ATOM 593 CE1 PHEA 77 58. 997 11. 288 3. 590 1.00 46. 70 A ATOM 594 CE2 PHE A 77 61.146 12.283 4.188 1. 00 43. 47 A ATOM 595 CZ PHEA 77 59.794 12.029 4.492 1. 0043. 90 A ATOM 596 C PHEA 77 61.717 8.179 1.623 1. 0040. 59 A ATOM 597 O PHE A 77 62.019 7.799 2. 753 1.00 39. 33 A ATOM 598 N ALA A 78 60.765 7.622 0.879 1. 00 38. 87 A ATOM 599 CA ALA A 78 59.956 6.505 1. 340 1.00 41. 33 A ATOM 600 CB ALA A 78 58. 917 6.165 0.307 1. 0036. 32 A ATOM 601 C ALA A 78 60.813 5.281 1.654 1. 0042. 29 A ATOM 602 O ALA A 78 60.686 4.702 2.726 1. 0042. 44 A ATOM 603 N ARG A 79 61.784 5.011 0.781 1. 0043. 99 A ATOM 604 CA ARG A 79 62.698 3.877 0. 902 1. 00 46. 77 A ATOM 605 CB ARG A 79 63.634 3.829-0. 305 1. 00 48. 88 A ATOM 606 CG ARG A 79 63.999 2.431-0. 770 1. 00 57. 25 A ATOM 607 CD ARG A 79 65.422 2.220-1. 235 1. 00 64. 00 A ATOM 608 NE ARG A 79 66.343 2.166-0. 100 1.00 72. 40 A ATOM 609 CZ ARG A 79 67.590 1.700-0. 151 1. 0074. 97 A ATOM 610 NH1 ARG A 79 68.100 1.241-1. 291 1. 00 75. 29 A ATOM 611 NH2 ARG A 79 68.323 1.666 0. 957 1.00 75. 56 A ATOM 612 C ARG A 79 63.542 3.899 2.170 1. 0047. 66 A ATOM 613 O ARG A 79 63.628 2.895 2.881 1. 0051. 11 A ATOM 614 N GLU A 80 64.107 5.062 2.481 1. 0047. 81 A ATOM 615 CA GLU A 80 64.965 5.192 3.650 1. 00 48. 17 A ATOM 616 CB GLU A 80 66.007 6.288 3.448 1. 00 48. 98 A ATOM 617 CG GLU A 80 66.846 6.153 2.162 1. 00 55. 96 A ATOM 618 CD GLU A 80 67.781 4.940 2.087 1. 00 61. 23 A ATOM 619 OE1 GLU A 80 68.410 4.784 1. 018 1. 00 66. 99 A ATOM 620 OE2 GLU A 80 67.911 4.154 3. 058 1. 00 63. 91 A ATOM 621 C GLU A 80 64.259 5.336 4.982 1. 0046. 59 A ATOM 622 O GLU A 80 64.843 5.047 6.029 1. 00 50. 59 A ATOM 623 N VAL A 81 62. 995 5.748 4.943 1. 0045. 25 A ATOM 624 CA VALA 81 62.197 5.877 6.159 1. 0041. 69 A ATOM 625 CB VAL A 81 61.015 6.885 5. 979 1. 00 39. 93 A ATOM 626 CG1 VAL A 81 60.042 6.824 7.144 1. 0045. 48 A ATOM 627 CG2 VAL A 81 61.548 8.298 5. 902 1.00 36. 04 A ATOM 628 C VAL A 81 61.733 4.464 6.531 1. 00 39. 84 A ATOM 629 O VAL A 81 61.755 4.099 7.705 1. 00 39. 97 A ATOM 630 N GLN A 82 61.429 3.649 5. 516 1. 00 39. 28 A ATOM 631 CA GLN A 82 60.998 2.264 5.726 1. 00 39. 46 A ATOM 632 CB GLN A 82 60.393 1.653 4.448 1. 00 32. 99 A ATOM 633 CG GLN A 82 59.118 2.342 3.915 1. 00 30. 48 A ATOM 634 CD GLN A 82 57.799 1.859 4.522 1. 00 34. 06 A ATOM 635 OE1 GLN A 82 57.673 1.682 5. 733 1. 00 37. 17 A ATOM 636 NE2 GLN A 82 56.798 1.653 3. 6641. 0036. 72 A ATOM 637 C GLN A 82 62. 184 1.423 6.207 1. 00 42. 48 A ATOM 638 O GLN A 82 61.998 0.469 6.959 1. 00 45. 77 A ATOM 639 N ASP A 83 63.396 1.844 5.833 1. 00 46. 50 A ATOM 640 CA ASP A 83 64.648 1.174 6.215 1. 00 50. 17 A ATOM 641 CB ASP A 83 65.789 1.575 5.272 1. 00 50. 85 A ATOM 642 CG ASP A 83 66.010 0.587 4.140 1. 00 55. 35 A ATOM 643 OD1 ASP A 83 67.003 0.774 3. 402 1. 00 58. 87 A ATOM 644 OD2 ASP A 83 65.218-0. 370 3.983 1. 00 58. 34 A ATOM 645 C ASP A 83 65.096 1.496 7. 633 1. 00 53. 32 A ATOM 646 O ASP A 83 65.586 0.619 8.347 1. 00 53. 81 A ATOM 647 N PHE A 84 64.964 2.765 8. 017 1. 00 57. 70 A ATOM 648 CA PHE A 84 65.381 3.218 9.340 1. 00 62. 33 A ATOM 649 CB PHE A 84 66.344 4.417 9.203 1. 00 66. 63 A ATOM 650 CG PHEA 84 67.710 4.063 8.635 1. 0075. 65 A ATOM 651 CD1 PHE A 84 68.369 4.959 7.769 1. 00 75. 83 A ATOM 652 CD2 PHE A 84 68.360 2.845 8. 980 1. 00 81. 57 A ATOM 653 CE1 PHEA 84 69.663 4.663 7. 244 1. 00 78. 46 A ATOM 654 CE2 PHEA 84 69.657 2.524 8. 468 1. 00 82. 65 A ATOM 655 CZ PHE A 84 70.310 3.439 7.596 1. 00 83. 43 A ATOM 656 C PHE A 84 64.247 3.512 10.337 1. 00 62. 70 A ATOM 657 O PHE A 84 64.417 4. 293 11.275 1.00 63. 61 A ATOM 658 N ALA A 85 63.126 2. 807 10.187 1.00 63. 58 A ATOM 659 CA ALA A 85 61.965 2.985 11.061 1. 0063. 63 A ATOM 660 CB ALA A 85 60.723 2.418 10.401 1. 00 63. 01 A ATOM 661 C ALA A 85 62.155 2.382 12.455 1. 00 63. 97 A ATOM 662 O ALA A 85 61.819 3.019 13.459 1. 00 65. 00 A ATOM 663 N GLY A 86 62.715 1.170 12.503 1. 00 63. 10 A ATOM 664 CA GLYA 86 62.966 0.484 13.765 1. 0062. 95 A ATOM 665 C GLYA 86 64.105 1.130 14.534 1. 0062. 74 A ATOM 666 O GLY A 86 64.082 1.197 15.769 1. 00 63. 65 A ATOM 667 N ASP A 87 65.058 1.668 13.772 1. 00 60. 90 A ATOM 668 CA ASP A 87 66.247 2.361 14.268 1. 00 61. 29 A ATOM 669 CB ASP A 87 67.134 2.721 13.069 1. 0065. 58 A ATOM 670 CG ASP A 87 68.609 2.807 13.416 1. 0070. 27 A ATOM 671 OD1 ASP A 87 69.358 1. 880 13. 025 1. 00 69. 62 A ATOM 672 OD2 ASP A 87 69.022 3.810 14.045 1. 0074. 83 A ATOM 673 C ASP A 87 65.834 3.643 15.006 1. 0061. 43 A ATOM 674 O ASP A 87 66.458 4.030 15.999 1. 0061. 11 A ATOM 675 N PHE A 88 64. 757 4.265 14.520 1. 00 60. 87 A ATOM 676 CA PHEA 88 64.209 5.497 15.085 1. 0060. 98 A ATOM 677 CB PHEA 88 63.778 6.442 13.961 1. 0056. 87 A ATOM 678 CG PHEA 88 64.875 7.338 13.454 1. 0053. 23 A ATOM 679 CD1 PHEA 88 64.811 8. 726 13.678 1.00 52. 89 A ATOM 680 CD2 PHE A 88 65.959 6. 816 12. 719 1. 00 55. 15 A ATOM 681 CE1 PHEA 88 65.815 9.601 13.174 1. 00 51. 41 A ATOM 682 CE2 PHE A 88 66.975 7.672 12.204 1. 00 56. 78 A ATOM 683 CZ PHEA 88 66.899 9.073 12.433 1. 0052. 70 A ATOM 684 C PHEA 88 63.041 5. 276 16. 051 1. 0063. 50 A ATOM 685 O PHEA 88 62. 469 6.245 16.573 1. 0063. 54 A ATOM 686 N GLN A 89 62.718 3.999 16.302 1. 00 66. 32 A ATOM 687 CA GLN A 89 61.637 3.549 17.207 1. 00 68. 79 A ATOM 688 CB GLNA 89 61.926 3.959 18.673 1. 0069. 83 A ATOM 689 CG GLNA 89 63.246 3.454 19.273 1. 0071. 35 A ATOM 690 CD GLN A 89 63.767 4.375 20.374 1. 00 74. 27 A ATOM 691 OE1 GLN A 89 63.638 4. 078 21. 565 1. 00 73. 80 A ATOM 692 NE2 GLN A 89 64.346 5. 507 19. 974 1. 00 72. 15 A ATOM 693 C GLNA 89 60.230 4.017 16.779 1. 0069. 38 A ATOM 694 O GLN A 89 59.361 4. 289 17. 620 1. 00 70. 94 A ATOM 695 N MET A 90 60.013 4.074 15.464 1. 00 68. 81 A ATOM 696 CA MET A 90 58. 741'4. 507 14.883 1. 0067. 37 A ATOM 697 CB META 90 58.952 4.968 13.443 1. 0066. 84 A ATOM 698 CG META 90 58.591 6.419 13.211 1. 0074. 69 A ATOM 699 SD META 90 59.850 7.565 13.773 1. 0081. 00 A ATOM 700 CE META 90 60.521 8.098 12.202 1. 0082. 51 A ATOM 701 C META 90 57.641 3.444 14.923 1. 0065. 59 A ATOM 702 O META 90 57.868 2.289 14.550 1. 0066. 48 A ATOM 703 N LYS A 91 56.451 3.859 15.361 1. 0062. 53 A ATOM 704 CA LYS A 91 55.284 2.979 15.471 1. 0059. 12 A ATOM 705 CB LYS A 91 54.563 3.249 16.802 1. 0062. 98 A ATOM 706 CG LYS A 91 53.544 2.201 17.242 1. 0066. 84 A ATOM 707 CD LYS A 91 54.077 0.926 17.888 1. 0072. 59 A ATOM 708 CE LYS A 91 53.043-0. 096 18.360 1. 0074. 52 A ATOM 709 NZ LYS A 91 53.672-1. 287 19.004 1. 0072. 19 A ATOM 710 C LYS A 91 54.324 3.203 14.294 1. 0055. 82 A ATOM 711 O LYS A 91 53.876 4.330 14.046 1. 00 55. 18 A ATOM 712 N TYRA 92 54.030 2.122 13.572 1. 0052. 34 A ATOM 713 CA TYRA 92 53.123 2.149 12.419 1. 0048. 10 A ATOM 714 CB TYRA 92 53.412 0.964 11.486 1. 0046. 79 A ATOM 715 CG TYRA 92 54.704 1.060 10.712 1. 0047. 00 A ATOM 716 CD1 TYRA 92 55.862 0. 394 11. 160 1. 00 51. 17 A ATOM 717 CE1 TYRA 92 57.083 0. 445 10. 417 1. 00 51. 06 A ATOM 718 CD2 TYR A 92 54.777 1.788 9. 506 1.00 50. 68 A ATOM 719 CE2 TYR A 92 55.993 1.847 8.749 1. 0048. 91 A ATOM 720 CZ TYRA 92 57.133 1.172 9. 216 1.00 50. 33 A ATOM 721 OH TYRA 92 58.304 1.205 8.496 1. 0048. 50 A ATOM 722 C TYRA 92 51.651 2. 106 12. 875 1. 0045. 73 A ATOM 723 O TYRA 92 51.338 1.418 13.850 1. 0046. 61 A ATOM 724 N PRO A 93 50.740 2.874 12.221 1. 0043. 23 A ATOM 725 CD PRO A 93 49.304 2.600 12.448 1. 0043. 06 A ATOM 726 CA PRO A 93 50.904 3.799 11.091 1. 0040. 88 A ATOM 727 CB PRO A 93 49.546 3.722 10.402 1. 0039. 73 A ATOM 728 CG PRO A 93 48.603 3.585 11.541 1. 0039. 09 A ATOM 729 C PRO A 93 51.250 5. 230 11.505 1.00 39. 55 A ATOM 730 O PRO A 93 50.877 5.670 12.595 1. 0041. 43 A ATOM 731 N PHE A 94 52.026 5.906 10.661 1. 0037. 36 A ATOM 732 CA PHE A 94 52.423 7.291 10.895 1. 00 35. 81 A ATOM 733 CB PHE A 94 53.776 7.389 11.636 1. 00 34. 23 A ATOM 734 CG PHEA 94 54.954 6.824 10.882 1. 0035. 49 A ATOM 735 CD1 PHE A 94 55.308 5. 478 11. 026 1. 00 38. 42 A ATOM 736 CD2 PHE A 94 55.760 7.657 10.072 1. 00 36. 72 A ATOM 737 CE1 PHE A 94 56.465 4.960 10.373 1. 0041. 53 A ATOM 738 CE2 PHE A 94 56.916 7.159 9.412 1. 0030. 49 A ATOM 739 CZ PHEA 94 57.271 5.812 9.562 1. 0038. 18 A ATOM 740 C PHE A 94 52.433 8.104 9. 602 1.00 34. 52 A ATOM 741 O PHE A 94 52.487 7.540 8.501 1. 0032. 15 A ATOM 742 N GLU A 95 52.398 9.428 9. 756 1. 00 33. 60 A ATOM 743 CA GLU A 95 52.400 10.360 8.626 1. 0030. 78 A ATOM 744 CB GLU A 95 51.047 11.040 8.448 1. 0029. 21 A ATOM 745 CG GLU A 95 49.928 10.208 7.929 1. 00 26. 20 A ATOM 746 CD GLU A 95 48.789 11.080 7.490 1. 00 34. 03 A ATOM 747 OE1 GLU A 95 48.274 11.837 8.349 1. 00 26. 49 A ATOM 748 OE2 GLU A 95 48.444 11.036 6.284 1. 0029. 13 A ATOM 749 C GLU A 95 53.413 11.476 8.762 1. 0030. 16 A ATOM 750 O GLU A 95 53.485 12.162 9.793 1. 0028. 48 A ATOM 751 N ILE A 96 54.168 11.676 7.689 1. 0030. 01 A ATOM 752 CA ILEA 96 55.156 12.739 7.635 1. 0029. 53 A ATOM 753 CB ILEA 96 56.534 12.238 7.134 1. 0029. 31 A ATOM 754 CG2 ILE A 96 57.516 13.405 7.053 1. 00 27. 43 A ATOM 755 CG1 ILE A 96 57.073 11.157 8.087 1. 0028. 60 A ATOM 756 CD1 ILE A 96 58.436 10.585 7.732 1. 00 26. 61 A ATOM 757 C ILE A 96 54.588 13.810 6.710 1. 0029. 44 A ATOM 758 O ILEA 96 53.901 13.499 5.738 1. 0031. 67 A ATOM 759 N GLNA 97 54.786 15.067 7.093 1. 0029. 92 A ATOM 760 CA GLN A 97 54.317 16.210 6.323 1. 00 30. 07 A ATOM 761 CB GLN A 97 53.196 16.933 7.059 1. 00 24. 15 A ATOM 762 CG GLN A 97 51.866 16.215 7.027 1. 00 28. 17 A ATOM 763 CD GLN A 97 50.838 16.859 7.926 1. 00 25. 45 A ATOM 764 OE1 GLN A 97 50.774 16.577 9.124 1. 00 29. 25 A ATOM 765 NE2 GLN A 97 49. 996 17. 701 7. 347 1. 00 25. 16 A ATOM 766 C GLN A 97 55.463 17.170 6.053 1. 00 31. 31 A ATOM 767 O GLN A 97 56. 395 17. 270 6.851 1. 00 34. 20 A ATOM 768 N GLY A 98 55. 394 17. 871 4. 928 1.00 30. 04 A ATOM 769 CA GLYA 98 56.446 18.808 4.597 1. 0028. 82 A ATOM 770 C GLYA 98 56.045 19.899 3.637 1. 0028. 41 A ATOM 771 O GLY A 98 55.498 19.623 2.580 1. 0032. 63 A ATOM 772 N LEA 99 56.339 21.137 4.016 1. 0025. 60 A ATOM 773 CA ILE A 99 56.043 22.315 3.216 1. 0024. 72 A ATOM 774 CB ILE A 99 55.041 23.247 3.971 1. 0027. 96 A ATOM 775 CG2 ILEA 99 55.565 23.610 5.369 1. 0023. 29 A ATOM 776 CG1 ILE A 99 54.717 24.495 3.150 1. 0028. 31 A ATOM 777 CD1 ILEA 99 53.577 25.324 3.718 1. 00 30. 23 A ATOM 778 C ILE A 99 57.384 23.003 2.940 1. 0028. 54 A ATOM 779 O LEA 99 58.229 23.106 3.840 1. 0028. 65 A ATOM 780 N ALA A 100 57.596 23.418 1.690 1. 00 30. 10 A ATOM 781 CA ALAA100 58. 842 24. 088 1.284 1. 0028. 30 A ATOM 782 CB ALA A 100 59.881 23.087 0.899 1. 00 19. 21 A ATOM 783 C ALA A 100 58.638 25.040 0.138 1. 00 26. 94 A ATOM 784 O ALA A 100 57. 976 24. 702-0. 842 1. 00 26. 61 A ATOM 785 N GLY A 101 59.249 26.213 0.255 1. 00 26. 88 A ATOM 786 CA GLY A 101 59.137 27.220-0. 781 1. 0032. 01 A ATOM 787 C GLY A 101 59.791 28.536-0. 418 1. 00 34. 40 A ATOM 788 O GLY A 101 60.599 28.593 0.512 1. 00 38. 68 A ATOM 789 N CYS A 102 59.394 29.601-1. 112 1. 00 31. 93 A ATOM 790 CA CYSA102 59.948 30.933-0. 887 1. 0032. 45 A ATOM 791 C CYS A 102 58.894 32.021-0. 998 1. 00 32. 57 A ATOM 792 O CYS A 102 57.792 31.754-1. 485 1. 00 38. 40 A ATOM 793 CB CYS A 102 61.082 31.188-1. 877 1. 00 35. 88 A ATOM 794 SG CYS A 102 60.652 30.848-3. 611 1. 00 41. 94 A ATOM 795 N GLU A 103 59.206 33.223-0. 506 1. 00 30. 47 A ATOM 796 CA GLU A 103 58.277 34.352-0. 589 1. 00 35. 43 A ATOM 797 CB GLU A 103 57.302 34.397 0.591 1. 00 41. 19 A ATOM 798 CG GLU A 103 57. 889 34. 552 1. 972 1.00 54. 77 A ATOM 799 CD GLU A 103 56.827 34.822 3.028 1. 00 60. 58 A ATOM 800 OE1 GLU A 103 55. 819 35. 520 2. 727 1. 00 62. 41 A ATOM 801 OE2 GLU A 103 57.018 34.344 4.166 1. 00 59. 23 A ATOM 802 C GLU A 103 58.891 35.726-0. 797 1. 00 37. 75 A ATOM 803 O GLU A 103 59.983 36.010-0. 317 1. 00 37. 34 A ATOM 804 N LEU A 104 58. 147 36. 586-1. 490 1.00 41. 55 A ATOM 805 CA LEU A 104 58.577 37.951-1. 783 1. 00 43. 60 A ATOM 806 CB LEU A 104 58.004 38.432-3. 122 1. 00 42. 55 A ATOM 807 CG LEU A 104 58.893 38.972-4. 257 1. 00 44. 85 A ATOM 808 CD1 LEU A 104 57.994 39.545-5. 336 1. 00 41. 06 A ATOM 809 CD2 LEU A 104 59. 885 40. 040-3. 790 1.00 43. 34 A ATOM 810 C LEU A 104 58. 105 38. 905-0. 715 1. 00 46. 07 A ATOM 811 O LEU A 104 56.961 38.822-0. 258 1. 00 51. 65 A ATOM 812 N HIS A 105 58.997 39.805-0. 320 1. 00 48. 58 A ATOM 813 CA HIS A 105 58.679 40.835 0. 663 1. 0054. 48 A ATOM 814 CB HIS A 105 59.670 40.817 1.822 1. 0056. 41 A ATOM 815 CG HIS A 105 59.503 39.648 2.732 1. 0060. 07 A ATOM 816 CD2 HIS A 105 60. 414 38. 858 3. 342 1. 00 60. 17 A ATOM 817 ND1 HIS A 105 58. 265 39. 154 3. 084 1. 00 61. 52 A ATOM 818 CE1 HIS A 105 58. 422 38. 107 3.871 1. 0062. 59 A ATOM 819 NE2 HIS A 105 59.716 37.906 4.043 1. 00 63. 88 A ATOM 820 C HIS A 105 58.758 42.175-0. 034 1. 00 56. 45 A ATOM 821 O HIS A 105 59. 337 42. 277-1. 122 1.00 58. 96 A ATOM 822 N SER A 106 58. 153 43. 196 0. 572 1.00 57. 09 A ATOM 823 CA SERA 106 58. 198 44. 544 0. 015 1. 00 56. 68 A ATOM 824 CB SERA 106 57.167 45.463 0.695 1. 00 56. 74 A ATOM 825 OG SERA 106 57.282 45.445 2.107 1. 00 62. 72 A ATOM 826 C SERA106 59. 636 45. 038 0. 213 1. 00 55. 19 A ATOM 827 O SERA106 60.214 44.889 1.300 1. 00 53. 43 A ATOM 828 N GLY A 107 60.240 45.471-0. 889 1. 00 52. 61 A ATOM 829 CA GLY A 107 61.614 45.939-0. 863 1. 00 53. 14 A ATOM 830 C GLY A 107 62. 495 45. 105-1. 778 1. 00 51. 00 A ATOM 831 O GLY A 107 63. 619 45. 510-2. 093 1. 00 51. 03 A ATOM 832 N GLY A 108 62.000 43.920-2. 149 1. 00 46. 61 A ATOM 833 CA GLY A 108 62. 716 43. 038-3. 052 1. 00 39. 17 A ATOM 834 C GLY A 108 63.260 41.736-2. 507 1. 00 38. 36 A ATOM 835 O GLY A 108 63.538 40.826-3. 287 1. 00 36. 01 A ATOM 836 N ALA A 109 63.403 41.631-1. 186 1. 00 38. 11 A ATOM 837 CA ALA A 109 63.951 40.427-0. 549 1. 0039. 48 A ATOM 838 CB ALA A 109 64.340 40.733 0.881 1. 00 37. 77 A ATOM 839 C ALA A 109 63.071 39.167-0. 605 1. 00 40. 37 A ATOM 840 O ALA A 109 61.843 39.242-0. 484 1. 00 42. 68 A ATOM 841 N ILE A 110 63. 714 38. 024-0. 853 1. 00 39. 57 A ATOM 842 CA ILE A 110 63. 036 36. 729-0. 933 1.00 37. 15 A ATOM 843 CB ILE A 110 63.140 36.093-2. 369 1. 00 36. 13 A ATOM 844 CG2 ILE A 110 62.789 34.574-2. 363 1. 00 20. 04 A ATOM 845 CG1 ILEA 110 62.214 36.860-3. 313 1. 0039. 63 A ATOM 846 CD1 ILE A 110 62.156 36.359-4. 722 1. 0043. 41 A ATOM 847 C ILEA110 63.531 35.744 0.119 1. 0038. 19 A ATOM 848 O ILE A 110 64.646 35.226 0.016 1. 0041. 20 A ATOM 849 N VAL A 111 62.686 35.462 1.108 1. 00 36. 80 A ATOM 850 CA VALA111 63. 053 34. 504 2. 142 1.00 40. 08 A ATOM 851 CB VAL A 111 62.637 34.952 3.587 1. 00 41. 09 A ATOM 852 CG1 VAL A 111 63. 309 36. 261 3. 942 1.00 43. 70 A ATOM 853 CG2 VAL A 111 61.135 35.073 3.739 1. 0046. 35 A ATOM 854 C VAL A 111 62.512 33.112 1.811 1. 00 38. 90 A ATOM 855 O VAL A 111 61.375 32.965 1.362 1. 00 38. 23 A ATOM 856 N SER A 112 63.373 32.113 1.960 1. 00 38. 89 A ATOM 857 CA SER A 112 63.009 30.733 1.702 1. 0037. 96 A ATOM 858 CB SERA 112 64.049 30.064 0.818 1. 00 37. 40 A ATOM 859 OG SERA 112 64. 088 30. 704-0. 437 1. 00 34. 96 A ATOM 860 C SER A 112 62.824 29.969 3.000 1. 00 39. 77 A ATOM 861 O SER A 112 63.412 30.323 4.029 1. 0043. 08 A ATOM 862 N PHE A 113 61.995 28.928 2.942 1. 00 36. 88 A ATOM 863 CA PHE A 113 61.684 28.104 4.104 1. 00 31. 77 A ATOM 864 CB PHE A 113 60. 396 28.628 4.783 1.00 34. 40 A ATOM 865 CG PHE A 113 59.187 28.735 3.852 1. 00 36. 42 A ATOM 866 CD1 PHEA113 58.234 27.697 3.780 1. 0035. 27 A ATOM 867 CD2 PHE A 113 58.998 29.870 3.046 1. 00 34. 59 A ATOM 868 CE1 PHEA113 57. 115 27. 784 2. 917 1.00 33. 07 A ATOM 869 CE2 PHE A 113 57. 874 29. 970 2. 176 1. 0035. 18 A ATOM 870 CZ PHE A 113 56.936 28.923 2.114 1. 00 32. 48 A ATOM 871 C PHE A 113 61.531 26.628 3.748 1. 00 28. 91 A ATOM 872 O PHE A 113 61.412 26.276 2.577 1. 00 30. 79 A ATOM 873 N LEU A 114 61.551 25.788 4.778 1. 00 26. 33 A ATOM 874 CA LEU A 114 61.354 24.340 4.676 1. 00 28. 66 A ATOM 875 CB LEU A 114 62.568 23.591 4.089 1. 00 20. 30 A ATOM. 876 CG LEU A 114 62.393 22.106 3.685 1. 00 21. 77 A ATOM 877 CD1 LEU A 114 63. 358 21. 743 2. 589 1. 00 20. 28 A ATOM 878 CD2 LEU A 114 62. 540 21. 119 4. 830 1. 00 15. 65 A ATOM 879 C LEU A 114 61.078 23.873 6.094 1. 00 30. 80 A ATOM 880 O LEU A 114 61. 902 24. 054 6. 983 1. 00 35. 00 A ATOM 881 N ARG A 115 59.893 23.314 6.303 1. 00 30. 87 A ATOM 882 CA ARGA115 59. 495 22.812 7.605 1.00 32. 88 A ATOM 883 CB ARG A 115 58.361 23.653 8.195 1. 00 32. 77 A ATOM 884 CG ARG A 115 58.657 25.120 8.389 1. 00 33. 71 A ATOM 885 CD ARG A 115 57.609 25.942 9.126 1. 00 43. 32 A ATOM 886 NE ARG A 115 56.311 26.006 8.447 1. 00 43. 25 A ATOM 887 CZ ARGA115 55. 996 26. 871 7. 480 1.00 46. 73 A ATOM 888 NH1 ARGA115 56.882 27.763 7.042 1. 0040. 65 A ATOM 889 NH2 ARG A 115 54.771 26.862 6.968 1. 00 46. 80 A ATOM 890 C ARG A 115 59. 023 21. 379 7.411 1. 00 34. 40 A ATOM 891 O ARG A 115 58.375 21.077 6.411 1. 00 39. 15 A ATOM 892 N GLY A 116 59.348 20.511 8.369 1. 00 34. 70 A ATOM 893 CA GLYA116 58. 961 19. 111 8. 315 1. 0031. 03 A ATOM 894 C GLYA116 58.137 18.741 9.530 1. 0032. 35 A ATOM 895 O GLYA116 58.197 19.441 10.551 1. 0032. 21 A ATOM 896 N ALA A 117 57.386 17.639 9.432 1. 00 32. 66 A ATOM 897 CA ALAA117 56.522 17.178 10.523 1. 0032. 27 A ATOM 898 CB ALA A 117 55.171 17.814 10.415 1. 00 31. 04 A ATOM 899 C ALAA117 56.351 15.674 10.649 1.00 31. 89 A ATOM 900 O ALA A 117 56.522 14.939 9.684 1. 00 32. 81 A ATOM 901 N LEU A 118 56.007 15.238 11.861 1. 00 33. 69 A ATOM 902 CA LEU A 118 55.760 13.830 12.187 1. 00 34. 62 A ATOM 903 CB LEU A 118 57. 006 13. 148 12. 784 1. 00 36. 40 A ATOM 904 CG LEU A 118 57.347 11.672 12.468 1. 00 38. 80 A ATOM 905 CD1 LEU A 118 58. 376 11. 188 13. 485 1. 00 36. 06 A ATOM 906 CD2 LEU A 118 56.143 10.723 12.482 1. 00 32. 26 A ATOM 907 C LEU A 118 54.648 13.830 13.226 1. 00 31. 64 A ATOM 908 O LEU A 118 54.742 14.528 14.239 1. 00 31.01 A ATOM 909 N GLY A 119 53.593 13.068 12.940 1. 00 30. 37 A ATOM 910 CA GLY A 119 52. 444 12.960 13.822 1. 00 33. 48 A ATOM 911 C GLYA119 51.684 14.258 14. 020 1. 0035. 73 A ATOM 912 O GLYA119 51.033 14.432 15.043 1. 0041. 06 A ATOM 913 N GLY A 120 51.804 15.177 13.063 1. 00 38. 64 A ATOM 914 CA GLYA120 51.131 16.464 13.143 1. 0041. 51 A ATOM 915 C GLYA120 51.853 17.514 13.966 1. 0045. 51 A ATOM 916 O GLYA120 51.332 18.618 14.176 1. 0046. 49 A ATOM 917 N LEU A 121 53.044 17.156 14.444 1. 00 47. 22 A ATOM 918 CA LEU A 121 53.882 18.037 15.258 1. 00 49. 90 A ATOM 919 CB LEU A 121 54. 215 17. 364 16. 599 1. 00 52. 33 A ATOM 920 CG LEU A 121 53. 152 17. 344 17. 706 1. 00 52. 25 A ATOM 921 CD1 LEU A 121 53. 140 15. 978 18. 384 1. 00 50. 17 A ATOM 922 CD2 LEU A 121 53.414 18.467 18.718 1. 00 47. 66 A ATOM 923 C LEU A 121 55.172 18.350 14.517 1. 00 47. 86 A ATOM 924 O LEU A 121 55.667 17.507 13.765 1. 00 48. 27 A ATOM 925 N ASP A 122 55.721 19.545 14.763 1. 00 44. 30 A ATOM 926 CA ASP A 122 56.972 20.005 14.146 1. 0043. 54 A ATOM 927 CB ASP A 122 57.367 21.381 14.699 1. 0046. 16 A ATOM 928 CG ASP A 122 56.525 22.520 14.135 1. 0049. 57 A ATOM 929 OD1 ASP A 122 56. 507 22. 701 12. 897 1. 00 56. 93 A ATOM 930 OD2 ASP A 122 55.917 23.266 14.934 1. 00 47. 52 A ATOM 931 C ASP A 122 58.132 19.024 14.372 1. 00 41. 88 A ATOM 932 O ASP A 122 58.265 18.450 15.454 1. 00 41. 96 A ATOM 933 N PHE A 123 58.915 18.781 13.328 1. 00 38. 01 A ATOM 934 CA PHE A 123 60.049 17.868 13.430 1. 00 39. 30 A ATOM 935 CB PHE A 123 59.874 16.720 12.436 1. 00 37. 69 A ATOM 936 CG PHE A 123 60.818 15.563 12.634 1. 00 38. 16 A ATOM 937 CD1 PHEA123 61.930 15.399 11.789 1. 0036. 46 A ATOM 938 CD2 PHE A 123 60.547 14.572 13.593 1. 00 37. 15 A ATOM 939 CE1 PHE A 123 62. 762 14. 253 11. 883 1. 0038. 26 A ATOM 940 CE2 PHE A 123 61.371 13.416 13.702 1. 00 34. 71 A ATOM 941 CZ PHE A 123 62.479 13.256 12.840 1. 00 33. 20 A ATOM 942 C PHE A 123 61.338 18.640 13.153 1. 00 41. 18 A ATOM 943 O PHE A 123 62.208 18.746 14.027 1. 00 41. 76 A ATOM 944 N LEU A 124 61.452 19.165 11.933 1. 00 39. 47 A ATOM 945 CA LEU A 124 62. 623 19. 925 11. 531 1. 00 37. 86 A ATOM 946 CB LEU A 124 63.552 19.067 10.658 1. 00 37. 86 A ATOM 947 CG LEU A 124 63.128 18.577 9.272 1. 00 35. 92 A ATOM 948 CD1 LEU A 124 63.601 19.534 8.196 1. 00 42. 21 A ATOM 949 CD2 LEU A 124 63.756 17.245 9.029 1. 00 29. 54 A ATOM 950 C LEU A 124 62.257 21.219 10.830 1. 00 37. 59 A ATOM 951 O LEU A 124 61. 100 21. 453 10. 498 1. 00 38. 71 A ATOM 952 N SERA125 63. 284 22. 017 10. 561 1. 0039. 46 A ATOM 953 CA SERA 125 63. 170 23. 308 9. 902 1.00 40. 58 A ATOM 954 CB SERA 125 62.911 24.397 10.947 1. 00 38. 20 A ATOM 955 OG SERA 125 62.699 25.652 10.341 1. 00 41. 96 A ATOM 956 C SERA 125 64.506 23.556 9.214 1. 00 42. 84 A ATOM 957 O SERA 125 65.471 22.838 9.480 1. 00 45. 68 A ATOM 958 N VAL A 126 64.546 24.507 8.277 1. 00 45. 71 A ATOM 959 CA VALA126 65.786 24.863 7.565 1. 0046. 68 A ATOM 960 CB VAL A 126 65.822 24.337 6.095 1. 00 44. 82 A ATOM 961 CG1 VALA126 67. 114 24. 759 5.381 1. 0046. 13 A ATOM 962 CG2 VAL A 126 65.730 22.828 6.073 1. 00 44. 24 A ATOM 963 C VAL A 126 66.016 26.371 7.578 1. 00 49. 34 A ATOM 964 O VALA126 65.431 27.112 6.783 1. 0048. 31 A ATOM 965 N LYS A 127 66.859 26.806 8.511 1. 00 55. 37 A ATOM 966 CA LYS A 127 67.229 28.211 8.664 1. 00 61. 29 A ATOM 967 CB LYS A 127 67. 148 28. 635 10. 139 1. 00 65. 84 A ATOM 968 CG LYS A 127 65.722 28.865 10.643 1. 00 71. 18 A ATOM 969 CD LYS A 127 65.553 29.316 12.094 1. 00 79. 56 A ATOM 970 CE LYS A 127 64.257 30.046 12.466 1. 00 81. 93 A ATOM 971 NZ LYS A 127 63.020 29.252 12.203 1. 00 80. 68 A ATOM 972 C LYS A 127 68.643 28.379 8.090 1. 00 62. 83 A ATOM 973 O LYS A 127 69.634 27.931 8.687 1. 00 64. 45 A ATOM 974 N ASN A 128 68.704 29.034 6.925 1. 00 62. 59 A ATOM 975 CA ASNA128 69.920 29.287 6.127 1. 0062. 19 A ATOM 976 CB ASN A 128 70.574 30.679 6.389 1. 00 64. 94 A ATOM 977 CG ASN A 128 71. 157 30. 844 7. 793 1. 00 67. 56 A ATOM 978 OD1 ASN A 128 70. 427 30. 996 8.781 1. 00 65. 20 A ATOM 979 ND2 ASN A 128 72.486 30.869 7.872 1. 00 66. 47 A ATOM 980 C ASN A 128 70.923 28.135 5.970 1. 00 59. 65 A ATOM 981 O ASN A 128 71.892 28.009 6.725 1. 00 60. 50 A ATOM 982 N ALA A 129 70.575 27.241 5.038 1. 00 58. 47 A ATOM 983 CA ALA A 129 71.336 26.040 4.645 1. 0059. 27 A ATOM 984 CB ALA A 129 72.660 26.441 3.951 1. 00 60. 88 A ATOM 985 C ALA A 129 71.584 24.901 5.656 1. 00 58. 35 A ATOM 986 O ALA A 129 72.257 23.916 5.316 1. 00 57. 52 A ATOM 987 N SER A 130 71.028 25.009 6.865 1. 00 56. 81 A ATOM 988 CA SERA 130 71.214 23.972 7.890 1. 00 56. 31 A ATOM 989 CB SER A 130 72.271 24.402 8.922 1. 00 57. 81 A ATOM 990 OG SER A 130 72.007 25.695 9.435 1. 00 63. 87 A ATOM 991 C SERA 130 69.940 23.496 8.592 1. 00 53. 42 A ATOM 992 O SERA 130 69.006 24.276 8.809 1. 00 51. 34 A ATOM 993 N CYS A 131 69.945 22.207 8.954 1. 00 51. 05 A ATOM 994 CA CYSA131 68.849 21.503 9.638 1. 0048. 37 A ATOM 995 C CYS A 131 68.690 21.965 11.079 1. 00 46. 74 A ATOM 996 O CYS A 131 69.636 21.894 11.862 1. 00 49. 94 A ATOM 997 CB CYS A 131 69.134 19.997 9.639 1. 00 48. 02 A ATOM 998 SG CYS A 131 67. 726 18. 871 9. 955 1. 00 53. 18 A ATOM 999 N VAL A 132 67.507 22.473 11.415 1. 00 46. 98 A ATOM 1000 CA VALA132 67.226 22.940 12.775 1. 0049. 89 A ATOM 1001 CB VAL A 132 66.768 24.430 12.815 1. 00 49. 02 A ATOM 1002 CG1 VAL A 132 66.611 24.906 14.258 1. 0047. 95 A ATOM 1003 CG2 VAL A 132 67.764 25.320 12.084 1. 00 53. 43 A ATOM 1004 C VAL A 132 66.149 22.040 13.396 1. 00 51. 78 A ATOM 1005 O VAL A 132 64.959 22.173 13.081 1. 00 50. 21 A ATOM 1006 N PRO A 133 66.559 21.099 14.277 1. 00 54. 52 A ATOM 1007 CD PRO A 133 67.943 20.785 14.693 1. 00 55. 19 A ATOM 1008 CA PRO A 133 65.610 20.190 14.927 1. 00 56. 41 A ATOM 1009 CB PRO A 133 66.531 19.189 15.627 1. 00 55. 54 A ATOM 1010 CG PRO A 133 67.744 19.985 15.949 1. 00 56. 91 A ATOM 1011 C PRO A 133 64.683 20. 904 15.913 1. 00 58. 75 A ATOM 1012 O PRO A 133 65.118 21.778 16.670 1. 00 63. 35 A ATOM 1013 N SERA 134 63.398 20.570 15.853 1. 00 59. 70 A ATOM 1014 CA SER A 134 62.407 21.164 16.744 1. 0062. 37 A ATOM 1015 CB SERA 134 61.026 21.135 16.090 1. 00 61. 48 A ATOM 1016 OG SERA 134 61.058 21.703 14.794 1. 00 71. 27 A ATOM 1017 C SER A 134 62.362 20.364 18.045 1. 00 64. 47 A ATOM 1018 O SER A 134 62.610 19.153 18.028 1. 00 65. 93 A ATOM 1019 N PRO A 135 62.110 21.031 19.201 1. 00 67. 18 A ATOM 1020 CD PRO A 135 62.071 22.490 19.436 1. 00 65. 85 A ATOM 1021 CA PRO A 135 62.040 20.313 20.486 1. 00 66. 35 A ATOM 1022 CB PRO A 135 61.891 21.448 21.502 1. 00 67. 36 A ATOM 1023 CG PRO A 135 61.271 22.576 20.693 1. 00 65. 52 A ATOM 1024 C PRO A 135 60.849 19.343 20.549 1. 00 66. 96 A ATOM 1025 O PRO A 135 60.823 18.426 21.380 1. 00 69. 92 A ATOM 1026 N GLU A 136 59.908 19.533 19.617 1. 00 64. 64 A ATOM 1027 CA GLU A 136 58.693 18.724 19.487 1. 00 63. 79 A ATOM 1028 CB GLU A 136 57.674 19.420 18.573 1. 00 66. 16 A ATOM 1029 CG GLU A 136 57. 602 20.952 18.661 1. 00 71. 73 A ATOM 1030 CD GLU A 136 57.086 21.474 19.994 1. 00 77. 81 A ATOM 1031 OE1 GLU A 136 56.111 20. 902 20. 536 1. 00 77. 39 A ATOM 1032 OE2 GLU A 136 57. 655 22. 473 20. 491 1. 00 79. 11 A ATOM 1033 C GLU A 136 59.040 17.358 18.899 1. 00 63. 88 A ATOM 1034 O GLU A 136 58.297 16.386 19.078 1. 00 63. 43 A ATOM 1035 N GLY A 137 60.170 17.311 18.187 1. 00 63. 59 A ATOM 1036 CA GLY A 137 60.659 16.083 17.580 1. 00 64. 00 A ATOM 1037 C GLY A 137 61.495 15.294 18.570 1. 00 64. 80 A ATOM 1038 O GLY A 137 61.654 14.077 18.429 1. 00 66. 07 A ATOM 1039 N GLY A 138 62.037 16.010 19.559 1. 00 64. 83 A ATOM 1040 CA GLYA138 62.846 15.418 20.614 1. 0065. 29 A ATOM 1041 C GLY A 138 64.213 14.914 20.201 1. 00 64. 60 A ATOM 1042 O GLY A 138 64.932 15.577 19.450 1. 00 61. 06 A ATOM 1043 N SERA 139 64.549 13.722 20.696 1. 00 65. 78 A ATOM 1044 CA SERA 139 65.822 13.058 20.410 1. 00 66. 93 A ATOM 1045 CB SERA 139 66.032 11.878 21.371 1. 00 68. 93 A ATOM 1046 OG SERA 139 64.936 10.975 21.340 1. 00 73. 17 A ATOM 1047 C SERA 139 65.875 12.583 18.956 1. 00 65. 48 A ATOM 1048 O SERA 139 66.939 12.606 18.328 1. 00 65. 54 A ATOM 1049 N ARG A 140 64.702 12.216 18.428 1. 00 62. 74 A ATOM 1050 CA ARGA140 64.528 11.748 17.050 1. 0059. 99 A ATOM 1051 CB ARG A 140 63.064 11.420 16.769 1. 00 61. 05 A ATOM 1052 CG ARG A 140 62.589 10.064 17.212 1. 00 64. 96 A ATOM 1053 CD ARG A 140 61.160 9.762 16.825 1. 00 66. 06 A ATOM 1054 NE ARG A 140 60.693 8.482 17.344 1. 00 74. 75 A ATOM 1055 CZ ARGA140 59.439 8.230 17.712 1. 0078. 40 A ATOM 1056 NH1 ARG A 140 58.500 9.170 17.626 1. 00 76. 07 A ATOM 1057 NH2 ARG A 140 59.117 7.022 18.156 1. 00 82. 69 A ATOM 1058 C ARG A 140 64.968 12.779 16.021 1. 00 57. 59 A ATOM 1059 O ARGA140 65.677 12.439 15.072 1. 0059. 81 A ATOM 1060 N ALA A 141 64.554 14.033 16.227 1. 00 53. 04 A ATOM 1061 CA ALAA141 64.881 15.141 15.328 1. 0049. 28 A ATOM 1062 CB ALA A 141 64.088 16.372 15.693 1. 00 43. 12 A ATOM 1063 C ALA A 141 66.373 15.440 15.300 1. 00 51. 50 A ATOM 1064 O ALA A 141 66.941 15.629 14.222 1. 00 52. 98 A ATOM 1065 N GLN A 142 67.008 15.411 16.477 1. 00 53. 16 A ATOM 1066 CA GLN A 142 68.453 15.641 16.619 1. 00 54. 05 A ATOM 1067 CB GLN A 142 68.846 15.696 18.096 1. 00 56. 91 A ATOM 1068 CG GLN A 142 68. 715 17.072 18.722 1. 00 63. 24 A ATOM 1069 CD GLN A 142 67.894 17.053 19.990 1. 00 67. 12 A ATOM 1070 OE1 GLN A 142 66. 766 17. 549 20. 016 1. 00 72. 69 A ATOM 1071 NE2 GLN A 142 68.446 16.467 21.049 1. 00 65. 91 A ATOM 1072 C GLN A 142 69.238 14.529 15.934 1. 00 52. 83 A ATOM 1073 O GLN A 142 70.210 14.785 15.222 1. 00 49. 71 A ATOM 1074 N LYS A 143 68. 725 13.309 16.090 1. 00 52. 77 A ATOM 1075 CA LYS A 143 69.294 12.089 15.525 1. 00 55. 63 A ATOM 1076 CB LYS A 143 68.540 10.889 16.110 1. 00 59. 15 A ATOM 1077 CG LYS A 143 69.197 9.519 16.009 1. 00 62.54 A ATOM 1078 CD LYS A 143 68.453 8.409 16.742 1. 00 65. 23 A ATOM 1079 CE LYS A 143 69.024 7.006 16.711 1. 00 70. 72 A ATOM 1080 NZ LYS A 143 68.230 6.098 17.596 1. 00 76. 02 A ATOM 1081 C LYS A 143 69.180 12.100 13.998 1. 00 55. 29 A ATOM 1082 O LYSA143 69.990 11.478 13.313 1. 0057. 24 A ATOM 1083 N PHE A 144 68.196 12.842 13.484 1. 00 55. 80 A ATOM 1084 CA PHEA144 67.955 12.959 12.045 1. 0056. 29 A ATOM 1085 CB PHE A 144 66.475 13.250 11.768 1. 00 59. 50 A ATOM 1086 CG PHE A 144 66.097 13.196 10.301 1. 00 62. 89 A ATOM 1087 CD1 PHEA144 66. 023 14. 375 9. 529 1.00 62. 07 A ATOM 1088 CD2 PHE A 144 65.801 11.968 9.684 1. 00 65. 21 A ATOM 1089 CE1 PHEA144 65. 659 14. 334 8. 157 1.00 58. 69 A ATOM 1090 CE2 PHE A 144 65.430 11.912 8.306 1. 00 63. 46 A ATOM 1091 CZ PHE A 144 65.360 13.098 7.546 1. 00 62. 06 A ATOM 1092 C PHE A 144 68.821 14.037 11.408 1. 00 56. 85 A ATOM 1093 O PHE A 144 69.415 13.798 10.359 1. 00 54. 33 A ATOM 1094 N CYS A 145 68.825 15.234 12.001 1. 00 57. 80 A ATOM 1095 CA CYSA145 69.620 16.358 11.492 1. 0060. 87 A ATOM 1096 C CYS A 145 71.126 16.070 11.526 1. 00 65. 31 A ATOM 1097 O CYS A 145 71.868 16.516 10.642 1. 00 65. 71 A ATOM 1098 CB CYS A 145 69.328 17.650 12.267 1. 00 59. 38 A ATOM 1099 SG CYS A 145 67.733 18.487 11.948 1. 00 53. 93 A ATOM 1100 N ALA A 146 71.548 15. 283 12.523 1. 00 67. 56 A ATOM 1101 CA ALA A 146 72.947 14.886 12.706 1. 0068. 65 A ATOM 1102 CB ALA A 146 73.161 14.347 14.109 1. 00 70. 37 A ATOM 1103 C ALA A 146 73.365 13.839 11.673 1. 0069. 58 A ATOM 1104 O ALAA146 74.554 13.680 11.381 1. 0070. 91 A ATOM 1105 N LEU A 147 72.372 13.138 11.127 1. 00 68. 46 A ATOM 1106 CA LEU A 147 72.587 12.113 10.114 1. 0068. 40 A ATOM 1107 CB LEU A 147 71.561 10.981 10.286 1. 00 65. 19 A ATOM 1108 CG LEU A 147 71.453 9.819 9.282 1. 00 67. 05 A ATOM 1109 CD1 LEU A 147 72.736 8.987 9. 243 1. 00 68. 69 A ATOM 1110 CD2 LEU A 147 70.263 8.940 9.648 1. 00 66. 79 A ATOM 1111 C LEU A 147 72.491 12.709 8.706 1. 0070. 05 A ATOM 1112 O LEU A 147 73.323 12.408 7.842 1. 00 71. 84 A ATOM 1113 N LEA148 71.513 13.594 8.506 1. 0069. 76 A ATOM 1114 CA LEA148 71.256 14.220 7.207 1. 0069. 31 A ATOM 1115 CB ILE A 148 69.834 14.904 7.192 1. 00 68. 14 A ATOM 1116 CG2 ILE A 148 69.899 16.410 7.478 1. 0067. 78 A ATOM 1117 CG1 ILEA 148 69. 117 14. 616 5. 875 1. 00 66. 25 A ATOM 1118 CD1 ILEA 148 68. 733 13. 159 5. 686 1. 00 63. 88 A ATOM 1119 C LEA148 72.358 15.130 6.649 1. 0070. 99 A ATOM 1120 O ILE A 148 72.487 15.266 5.433 1. 0070. 63 A ATOM 1121 N ILE A 149 73.172 15.701 7.537 1. 00 73. 91 A ATOM 1122 CA ILE A 149 74.267 16.593 7.137 1. 00 78. 04 A ATOM 1123 CB ILE A 149 74.777 17.473 8.329 1. 00 80. 82 A ATOM 1124 CG2 ILE A 149 73. 725 18. 534 8. 688 1. 00 81. 83 A ATOM 1125 CG1 ILEA 149 75. 159 16. 603 9. 539 1. 00 82. 61 A ATOM 1126 CD1 ILEA 149 75.996 17.318 10.602 1. 00 86. 76 A ATOM 1127 C ILE A 149 75.446 15.857 6.484 1. 0078. 75 A ATOM 1128 O ILE A 149 76.182 16.438 5.681 1. 0078. 73 A ATOM 1129 N GLNA150 75.562 14.563 6.793 1. 0079. 71 A ATOM 1130 CA GLNA150 76. 622 13. 688 6. 280 1.00 80. 58 A ATOM 1131 CB GLN A 150 76.685 12.407 7.117 1. 00 82. 55 A ATOM 1132 CG GLN A 150 77.079 12.635 8.576 1. 00 81. 89 A ATOM 1133 CD GLN A 150 76.922 11.390 9.432 1. 00 85. 14 A ATOM 1134 OE1 GLN A 150 76.139 11.377 10.382 1. 00 86. 57 A ATOM 1135 NE2 GLN A 150 77.671 10.337 9.105 1. 00 86. 03 A ATOM 1136 C GLN A 150 76.484 13.345 4.790 1. 00 79. 71 A ATOM 1137 O GLN A 150 77.455 12.941 4.143 1. 00 78. 99 A ATOM 1138 N TYR A 151 75.274 13.521 4.261 1. 00 79. 93 A ATOM 1139 CA TYRA151 74. 976 13. 265 2. 852 1.00 80. 93 A ATOM 1140 CB TYRA 151 73.600 12.586 2. 713 1. 00 82. 25 A ATOM 1141 CG TYRA151 73. 507 11. 193 3. 318 1. 0086. 10 A ATOM 1142 CD1 TYR A 151 73. 788 10. 047 2. 540 1. 00 86. 84 A ATOM 1143 CE1 TYRA151 73.726 8.740 3. 103 1.00 88. 91 A ATOM 1144 CD2TYRA151 73.156 11.008 4.675 1. 0086. 60 A ATOM 1145 CE2 TYR A 151 73.091 9.705 5.251 1. 00 87. 31 A ATOM 1146 CZ TYR A 151 73.379 8.581 4. 455 1. 0089. 10 A ATOM 1147 OH TYR A 151 73.323 7.316 4.995 1. 00 91. 60 A ATOM 1148 C TYR A 151 75.014 14.608 2.106 1. 00 80. 28 A ATOM 1149 O TYR A 151 73.995 15.293 1.976 1. 00 80. 47 A ATOM 1150 N GLN A 152 76.210 14.986 1.648 1. 00 79. 63 A ATOM 1151 CA GLNA152 76.450 16.252 0.937 1. 0077. 09 A ATOM 1152 CB GLN A 152 77.950 16.454 0.696 1. 00 79. 30 A ATOM 1153 CG GLN A 152 78.755 16.801 1.931 1. 00 78. 72 A ATOM 1154 CD GLN A 152 80.243 16.842 1.645 1. 00 80. 06 A ATOM 1155 OE1 GLN A 152 80.748 17.788 1.038 1. 00 78. 28 A ATOM 1156 NE2 GLN A 152 80.953 15.806 2.076 1. 00 82. 01 A ATOM 1157 C GLN A 152 75.716 16.418-0. 390 1. 00 73. 74 A ATOM 1158 O GLN A 152 75.307 17.528-0. 737 1. 00 71. 09 A ATOM 1159 N GLY A 153 75.542 15.306-1. 106 1. 00 71. 65 A ATOM 1160 CA GLYA153 74.871 15.308-2. 398 1. 0070. 80 A ATOM 1161 C GLY A 153 73.414 15.737-2. 382 1. 00 69. 00 A ATOM 1162 O GLY A 153 72.943 16.354-3. 347 1. 00 69. 85 A ATOM 1163 N ILE A 154 72. 710 15. 423-1.291 1. 00 66. 27 A ATOM 1164 CA ILE A 154 71.302 15.789-1. 152 1. 00 62. 42 A ATOM 1165 CB ILE A 154 70.441 14.704-0. 420 1. 00 59. 44 A ATOM 1166 CG2 ILE A 154 70.741 13.316-0. 987 1. 0062. 29 A ATOM 1167 CG1 ILEA 154 70. 676 14. 712 1. 088 1. 00 61. 56 A ATOM 1168 CD1 ILE A 154 69. 637 13. 949 1. 870 1.00 66. 06 A ATOM 1169 C ILE A 154 71.147 17.151-0. 486 1. 00 61. 92 A ATOM 1170 O ILE A 154 70.178 17.857-0. 744 1. 00 63. 80 A ATOM 1171 N MET A 155 72.127 17.520 0.339 1. 00 60. 06 A ATOM 1172 CA META 155 72.132 18.802 1.042 1. 00 59. 56 A ATOM 1173 CB META 155 73.185 18.796 2.147 1. 00 61. 15 A ATOM 1174 CG MET A 155 72.763 18.038 3.393 1. 00 63. 84 A ATOM 1175 SD MET A 155 71.413 18.850 4.267 1. 00 60. 30 A ATOM 1176 CE MET A 155 72.319 20.221 5.058 1. 00 70. 78 A ATOM 1177 C MET A 155 72.388 19.964 0.092 1. 00 58. 61 A ATOM 1178 O MET A 155 71.861 21.063 0.284 1. 0056. 80 A ATOM 1179 N GLU A 156 73.177 19.687-0. 947 1. 00 58. 35 A ATOM 1180 CA GLU A 156 73. 523 20. 668-1. 967 1. 00 58. 69 A ATOM 1181 CB GLU A 156 74.792 20.225-2. 731 1. 00 61. 60 A ATOM 1182 CG GLU A 156 75.244 21.071-3. 957 1. 00 65. 50 A ATOM 1183 CD GLU A 156 75.446 22.572-3. 686 1. 00 70. 83 A ATOM 1184 OE1 GLUA156 75.800 22.971-2. 552 1. 0070. 53 A ATOM 1185 OE2 GLU A 156 75. 240 23. 365-4. 632 1. 00 70. 43 A ATOM 1186 C GLU A 156 72. 340 20. 897-2. 902 1. 00 57. 35 A ATOM 1187 O GLU A 156 72.029 22.045-3. 220 1. 00 56. 91 A ATOM 1188 N THR A 157 71.645 19.819-3. 275 1. 00 55. 25 A ATOM 1189 CA THRA157 70.486 19.928-4. 164 1. 0055. 44 A ATOM 1190 CB THRA157 70.111 18.586-4. 836 1. 0056. 95 A ATOM 1191 OG1 THR A 157 70.058 17.546-3. 857 1. 00 64. 94 A ATOM 1192 CG2 THR A 157 71.124 18.225-5. 919 1. 0062. 42 A ATOM 1193 C THRA157 69.261 20.570-3. 511 1. 0052. 56 A ATOM 1194 O THRA157 68.372 21.034-4. 214 1. 0052. 87 A ATOM 1195 N VALA158 69.241 20.619-2. 173 1. 0051. 61 A ATOM 1196 CA VALA158 68.156 21.256-1. 407 1. 0047. 46 A ATOM 1197 CB VAL A 158 68. 064 20. 721 0. 073 1. 00 44. 47 A ATOM 1198 CG1 VALA 158 67. 094 21. 557 0. 917 1. 00 36. 48 A ATOM 1199 CG2 VAL A 158 67.574 19.288 0.084 1. 00 39. 96 A ATOM 1200 C VAL A 158 68.463 22.754-1. 398 1. 00 48. 17 A ATOM 1201 O VAL A 158 67.567 23. 577-1.589 1. 00 48. 44 A ATOM 1202 N ARG A 159 69.751 23.072-1. 245 1. 00 49. 13 A ATOM 1203 CA ARGA159 70.261 24.443-1. 212 1. 0047. 29 A ATOM 1204 CB ARG A 159 71.748 24.438-0. 843 1. 00 51. 04 A ATOM 1205 CG ARG A 159 72.224 25.685-0. 109 1. 00 56. 74 A ATOM 1206 CD ARG A 159 73.572 26.281-0. 513 1. 00 61. 94 A ATOM 1207 NE ARGA159 73.497 27.050-1. 760 1. 0061. 17 A ATOM 1208 CZ ARG A 159 74.054 26.690-2. 916 1. 00 59. 53 A ATOM 1209 NH1 ARG A 159 74. 740 25. 558-3. 011 1. 00 55. 39 A ATOM 1210 NH2 ARG A 159 73.927 27.468-3. 982 1. 00 57. 15 A ATOM 1211 C ARGA159 70.054 25.150-2. 559 1. 0045. 64 A ATOM 1212 O ARG A 159 69.671 26.323-2. 588 1. 00 49. 41 A ATOM 1213 N ILE A 160 70.261 24.420-3. 660 1. 00 40. 09 A ATOM 1214 CA ILE A 160 70. 078 24. 956-5. 017 1. 00 37. 78 A ATOM 1215 CB ILE A 160 70.593 23.957-6. 122 1. 00 38. 87 A ATOM 1216 CG2 ILE A 160 70.258 24.465-7. 544 1. 00 34. 33 A ATOM 1217 CG1 ILE A 160 72.109 23.754-5. 992 1. 00 36. 58 A ATOM 1218 CD1 ILEA 160 72.666 22.606-6. 832 1. 0039. 59 A ATOM 1219 C ILE A 160 68. 588 25. 240-5. 229 1. 00 36. 81 A ATOM 1220 O ILE A 160 68.212 26.337-5. 645 1. 00 36. 53 A ATOM 1221 N LEU A 161 67. 756 24. 265-4. 868 1. 00 34. 19 A ATOM 1222 CA LEU A 161 66. 309 24. 373-5. 012 1.00 34. 58 A ATOM 1223 CB LEU A 161 65.631 23.061-4. 631 1. 00 30. 35 A ATOM 1224 CG LEU A 161 65.611 21.953-5. 681 1. 00 33. 35 A ATOM 1225 CD1 LEU A 161 65. 130 20. 685-5. 017 1. 00 36. 24 A ATOM 1226 CD2 LEU A 161 64.733 22.304-6. 870 1. 00 35. 32 A ATOM 1227 C LEU A 161 65.671 25.506-4. 222 1. 00 36. 25 A ATOM 1228 O LEU A 161 64. 927 26. 325-4. 7671. 0034. 15 A ATOM 1229 N LEU A 162 66.064 25.595-2. 960 1. 00 36. 40 A ATOM 1230 CA LEU A 162 65.525 26.570-2. 033 1. 00 35. 92 A ATOM 1231 CB LEU A 162 65.806 26.069-0. 613 1. 00 33. 45 A ATOM 1232 CG LEU A 162 64. 813 26. 162 0. 545 1. 00 37. 17 A ATOM 1233 CD1 LEU A 162 63. 460 25. 613 0. 164 1. 00 37. 61 A ATOM 1234 CD2 LEU A 162 65.379 25.392 1.734 1. 00 35. 63 A ATOM 1235 C LEU A 162 66.016 28.008-2. 198 1. 00 36. 53 A ATOM 1236 O LEU A 162 65. 215 28. 937-2. 162 1. 00 34. 27 A ATOM 1237 N TYR A 163 67.309 28.179-2. 465 1. 00 38. 10 A ATOM 1238 CA TYR A 163 67.897 29.514-2. 552 1. 0038. 58 A ATOM 1239 CB TYR A 163 69.128 29.582-1. 641 1. 0035. 94 A ATOM 1240 CG TYR A 163 68.826 29.226-0. 187 1. 00 37. 42 A ATOM 1241 CD1 TYR A 163 68.187 30.147 0.676 1. 00 39. 64 A ATOM 1242 CE1 TYR A 163 67. 875 29. 801 2.031 1. 00 36. 87 A ATOM 1243 CD2 TYR A 163 69.151 27.953 0.329 1. 00 31. 64 A ATOM 1244 CE2 TYR A 163 68.846 27.596 1.676 1. 00 29. 31 A ATOM 1245 CZ TYR A 163 68.208 28.523 2.512 1. 0034. 59 A ATOM 1246 OH TYRA 163 67.887 28.169 3.801 1. 00 34. 87 A ATOM 1247 C TYR A 163 68.191 30.109-3. 925 1. 00 40. 63 A ATOM 1248 O TYR A 163 68.460 31.313-4. 035 1. 00 40. 10 A ATOM 1249 N GLU A 164 68.116 29.282-4. 967 1. 0042. 05 A ATOM 1250 CA GLUA164 68.359 29.731-6. 338 1. 0040. 86 A ATOM 1251 CB GLU A 164 69.601 29.058-6. 921 1. 00 41. 93 A ATOM 1252 CG GLU A 164 70.915 29.574-6. 355 1. 00 51. 14 A ATOM 1253 CD GLU A 164 72.098 28.656-6. 633 1. 00 57. 70 A ATOM 1254 OE1 GLU A 164 71. 920 27. 586-7. 270 1. 00 53. 58 A ATOM 1255 OE2 GLU A 164 73.216 29.012-6. 192 1. 00 58. 25 A ATOM 1256 C GLU A 164 67.162 29.496-7. 255 1. 00 40. 66 A ATOM 1257 O GLU A 164 66.642 30.451-7. 840 1. 00 39. 05 A ATOM 1258 N THR A 165 66. 695 28. 245-7. 322 1. 00 39. 59 A ATOM 1259 CA THRA165 65.571 27.848-8. 180 1. 0040. 09 A ATOM 1260 CB THR A 165 65. 483 26. 310-8. 320 1. 00 38. 50 A ATOM 1261 OG1 THR A 165 66. 775 25. 797-8. 667 1. 00 47. 25 A ATOM 1262 CG2 THR A 165 64.478 25.890-9. 393 1. 00 33. 05 A ATOM 1263 C THR A 165 64.216 28.386-7. 741 1. 00 41. 54 A ATOM 1264 O THR A 165 63.438 28.841-8. 589 1. 00 44. 93 A ATOM 1265 N CYS A 166 63.942 28.355-6. 435 1. 00 39. 79 A ATOM 1266 CA CYSA166 62.663 28.844-5. 912 1. 0038. 66 A ATOM 1267 C CYS A 166 62.429 30.324-6. 236 1. 00 37. 89 A ATOM 1268 O CYS A 166 61.351 30.659-6. 734 1. 00 37. 64 A ATOM 1269 CB CYS A 166 62.493 28.544-4. 412 1. 00 39. 64 A ATOM 1270 SG CYS A 166 60. 818 28. 826-3. 769 1. 00 41. 31 A ATOM 1271 N PRO A 167 63. 404 31. 228-5. 946 1. 00 37. 29 A ATOM 1272 CD PRO A 167 64.592 31.199-5. 066 1. 00 35. 25 A ATOM 1273 CA PRO A 167 63.101 32.617-6. 305 1. 00 38. 07 A ATOM 1274 CB PRO A 167 64.248 33.400-5. 669 1. 00 37. 97 A ATOM 1275 CG PRO A 167 65.322 32.412-5. 484 1. 00 39. 04 A ATOM 1276 C PRO A 167 63. 023 32. 839-7. 815 1. 00 39. 02 A ATOM 1277 O PRO A 167 62.153 33.582-8. 277 1. 00 41. 06 A ATOM 1278 N ARG A 168 63.834 32.090-8. 575 1. 00 37. 23 A ATOM 1279 CA ARGA168 63.860 32.191-10. 046 1. 0039. 91 A ATOM 1280 CB ARG A 168 64.969 31.308-10. 649 1. 00 41. 16 A ATOM 1281 CG ARG A 168 65.219 31.505-12. 155 1. 00 40. 39 A ATOM 1282 CD ARG A 168 66.325 30.694-12. 829 1. 00 42. 32 A ATOM 1283 NE ARG A 168 66.058 29.252-12. 881 1. 00 42. 32 A ATOM 1284 CZ ARG A 168 66.714 28.334-12. 167 1. 00 46. 28 A ATOM 1285 NH1 ARG A 168 67. 684 28. 691-11. 324 1. 00 43. 53 A ATOM 1286 NH2 ARG A 168 66.410 27.049-12. 301 1. 00 42. 08 A ATOM 1287 C ARG A 168 62.492 31.780-10. 583 1. 00 39. 46 A ATOM 1288 O ARG A 168 62.035 32. 289-11. 612 1. 00 41. 98 A ATOM 1289 N TYR A 169 61.815 30.931-9. 809 1. 00 36. 29 A ATOM 1290 CA TYRA169 60.489 30.463-10. 155 1. 0029. 76 A ATOM 1291 CB TYR A 169 60.213 29.084-9. 538 1. 00 27. 80 A ATOM 1292 CG TYR A 169 58.888 28.509-9. 975 1. 00 25. 28 A ATOM 1293 CD1 TYR A 169 57.831 28.346-9. 052 1. 0022. 28 A ATOM 1294 CE1 TYR A 169 56.548 27. 954-9.483 1. 0024. 86 A ATOM 1295 CD2 TYR A 169 58. 635 28. 248-11. 340 1. 00 26. 87 A ATOM 1296 CE2 TYR A 169 57. 356 27. 856-11. 783 1. 00 27. 00 A ATOM 1297 CZ TYRA169 56.323 27.717-10. 852 1. 0026. 50 A ATOM 1298 OH TYRA169 55.076 27.382-11. 295 1. 0021. 85 A ATOM 1299 C TYR A 169 59.401 31.456-9. 763 1. 00 27. 58 A ATOM 1300 O TYR A 169 58. 603 31. 838-10. 612 1. 00 25. 33 A ATOM 1301 N LEU A 170 59. 370 31. 838-8. 484 1. 00 26. 90 A ATOM 1302 CA LEU A 170 58.377 32.764-7. 927 1. 0028. 79 A ATOM 1303 CB LEU A 170 58. 832 33. 320-6. 575 1. 00 24. 02 A ATOM 1304 CG LEU A 170 57.927 33.331-5. 333 1. 00 18. 56 A ATOM 1305 CD1 LEU A 170 58. 325 34. 502-4. 493 1. 00 18. 70 A ATOM 1306 CD2 LEU A 170 56. 456 33. 436-5. 629 1. 00 15. 04 A ATOM 1307 C LEU A 170 58.035 33.935-8. 838 1. 00 33. 55 A ATOM 1308 O LEU A 170 56.868 34.123-9. 176 1. 00 36. 23 A ATOM 1309 N LEU A 171 59.062 34.642-9. 314 1. 00 35. 21 A ATOM 1310 CA LEU A 171 58.870 35.797-10. 193 1. 0034. 56 A ATOM 1311 CB LEU A 171 60.181 36.561-10. 406 1. 00 36. 47 A ATOM 1312 CG LEU A 171 60.728 37.477-9. 307 1. 00 35. 71 A ATOM 1313 CD1 LEU A 171 59. 648 38. 416-8. 776 1. 0040. 31 A ATOM 1314 CD2 LEU A 171 61.294 36.669-8. 197 1. 00 35. 90 A ATOM 1315 C LEU A 171 58.270 35.427-11. 533 1. 00 32. 95 A ATOM 1316 O LEU A 171 57. 479 36. 184-12. 078 1. 00 34. 00 A ATOM 1317 N GLY A 172 58. 620 34. 239-12. 024 1.00 31. 81 A ATOM 1318 CA GLYA172 58.104 33.751-13. 289 1. 0031. 84 A ATOM 1319 C GLY A 172 56.598 33.550-13. 265 1. 00 34. 61 A ATOM 1320 O GLY A 172 55.918 34.023-14. 178 1. 00 36. 02 A ATOM 1321 N VAL A 173 56. 085 32. 900-12. 210 1. 00 31. 71 A ATOM 1322 CA VAL A 173 54. 647 32. 647-12. 056 1. 00 27. 68 A ATOM 1323 CB VAL A 173 54.273 31.540-11. 021 1. 00 30. 25 A ATOM 1324 CG1 VAL A 173 53. 846 30. 276-11. 722 1. 00 22. 96 A ATOM 1325 CG2 VAL A 173 55. 375 31. 299-10. 025 1. 00 29. 31 A ATOM 1326 C VAL A 173 53.866 33.863-11. 639 1. 00 28. 03 A ATOM 1327 O VAL A 173 52.726 34.016-12. 063 1. 00 32. 70 A ATOM 1328 N LEU A 174 54.456 34.712-10. 792 1. 00 27. 78 A ATOM 1329 CA LEU A 174 53.776 35.923-10. 318 1. 00 26. 44 A ATOM 1330 CB LEU A 174 54. 565 36. 628-9. 220 1. 00 22. 08 A ATOM 1331 CG LEU A 174 54.622 35.946-7. 849 1. 00 26. 57 A ATOM 1332 CD1 LEU A 174 55.348 36.851-6. 885 1. 00 22. 52 A ATOM 1333 CD2 LEU A 174 53. 245 35. 575-7.301 1. 00 29. 25 A ATOM 1334 C LEU A 174 53. 533 36. 875-11. 456 1. 00 29. 66 A ATOM 1335 O LEU A 174 52. 519 37. 588-11. 479 1. 00 35. 07 A ATOM 1336 N ASN A 175 54.432 36.793-12. 438 1. 00 28. 20 A ATOM 1337 CA ASNA175 54.382 37.606-13. 634 1. 0029. 76 A ATOM 1338 CB ASN A 175 55.794 37.819-14. 174 1. 00 28. 17 A ATOM 1339 CG ASN A 175 55.825 38.705-15. 396 1. 00 32. 03 A ATOM 1340 OD1 ASN A 175 56.231 38.266-16. 469 1. 00 32. 91 A ATOM 1341 ND2 ASN A 175 55.383 39.955-15. 246 1. 00 33. 85 A ATOM 1342 C ASN A 175 53.483 36.947-14. 678 1. 00 30. 70 A ATOM 1343 O ASN A 175 52.559 37.585-15. 194 1. 00 33. 34 A ATOM 1344 N ALA A 176 53.738 35.667-14. 954 1. 00 28. 38 A ATOM 1345 CA ALA A 176 52. 964 34. 891-15. 929 1.00 26. 54 A ATOM 1346 CB ALAA176 53.523 33.485-16. 028 1. 0023. 51 A ATOM 1347 C ALA A 176 51.468 34.833-15. 607 1. 00 25. 36 A ATOM 1348 O ALA A 176 50.623 34.838-16. 514 1. 00 22. 95 A ATOM 1349 N GLY A 177 51. 165 34. 832-14. 309 1. 00 25. 53 A ATOM 1350 CA GLYA177 49.795 34.771-13. 843 1. 0026. 70 A ATOM 1351 C GLY A 177 49. 196 36. 079-13. 388 1. 00 30. 72 A ATOM 1352 O GLY A 177 48.127 36.073-12. 784 1. 00 29. 86 A ATOM 1353 N LYS A 178 49.860 37.188-13. 713 1. 00 32. 48 A ATOM 1354 CA LYS A 178 49.427 38.544-13. 360 1. 00 35. 81 A ATOM 1355 CB LYS A 178 50. 227 39. 551-14. 197 1. 00 40. 27 A ATOM 1356 CG LYS A 178 50.486 40.898-13. 534 1. 00 48. 99 A ATOM 1357 CD LYS A 178 51.037 42.048-14. 393 1. 00 59. 25 A ATOM 1358 CE LYS A 178 52.361 41.855-15. 142 1. 00 65. 20 A ATOM 1359 NZ LYS A 178 52.230 40. 965-16. 336 1. 00 63. 80 A ATOM 1360 C LYS A 178 47.916 38.772-13. 580 1. 00 35. 54 A ATOM 1361 O LYS A 178 47.225 39.297-12. 700 1. 00 32. 94 A ATOM 1362 N ALA A 179 47.417 38.248-14. 706 1. 00 34. 86 A ATOM 1363 CA ALA A 179 46. 019 38. 357-15. 1281. 0033. 38 A ATOM 1364 CB ALA A 179 45.857 37.756-16. 508 1. 00 34. 40 A ATOM 1365 C ALA A 179 44. 995 37.750-14. 164 1. 0034. 57 A ATOM 1366 O ALA A 179 43.954 38.358-13. 906 1. 00 35. 90 A ATOM 1367 N ASP A 180 45.294 36.563-13. 638 1. 00 36. 37 A ATOM 1368 CA ASP A 180 44.413 35.881-12. 689 1. 0036. 38 A ATOM 1369 CB ASP A 180 44.516 34.355-12. 846 1. 00 41. 17 A ATOM 1370 CG ASP A 180 43.836 33.826-14. 111 1. 0049. 45 A ATOM 1371 OD1 ASP A 180 43. 269 34. 627-14. 894 1.00 48. 60 A ATOM 1372 OD2 ASP A 180 43. 871 32. 587-14. 315 1. 00 47. 77 A ATOM 1373 C ASP A 180 44. 729 36. 251-11. 237 1. 00 36. 26 A ATOM 1374 O ASP A 180 43. 821 36. 458-10. 432 1. 00 37. 36 A ATOM 1375 N LEU A 181 46.019 36.357-10. 923 1. 00 34. 56 A ATOM 1376 CA LEU A 181 46.495 36.656-9. 573 1. 00 34. 29 A ATOM 1377 CB LEU A 181 47.989 36.342-9. 473 1. 00 29. 14 A ATOM 1378 CG LEU A 181 48.398 34.875-9. 660 1. 00 21. 21 A ATOM 1379 CD1 LEU A 181 49.875 34.778-9. 985 1.00 1.64 A ATOM 1380 CD2 LEU A 181 48. 054 34. 063-8. 421 1. 00 24. 13 A ATOM 1381 C LEU A 181 46.221 38.054-9. 023 1. 00 37. 49 A ATOM 13820 LEU A 181 45. 951 38. 205-7. 830 1.00 36. 57 A ATOM 1383 N GLN A 182 46. 312 39. 070-9. 883 1. 00 40. 97 A ATOM 1384 CA GLN A 182 46.078 40.461-9. 479 1. 00 41. 45 A ATOM 1385 CB GLNA182 47.216 41.361-9. 969 1. 0041. 13 A ATOM 1386 CG GLN A 182 48.489 41.201-9. 158 1. 00 47. 95 A ATOM 1387 CD GLN A 182 49.672 41.942-9. 741 1. 0052. 12 A ATOM 1388 OE1 GLN A 182 50. 648 41. 323-10. 173 1. 00 53. 86 A ATOM 1389 NE2 GLN A 182 49. 608 43. 272-9. 734 1. 00 53. 10 A ATOM 1390 C GLN A 182 44. 712 40. 969-9. 938 1. 00 41. 79 A ATOM 1391 O GLN A 182 44. 475 42. 174-10. 060 1.00 45. 06 A ATOM 1392 N ARG A 183 43. 804 40. 013-10. 112 1. 00 41. 19 A ATOM 1393 CA ARG A 183 42. 420 40. 218-10. 531 1. 00 40. 36 A ATOM 1394 CB ARG A 183 41. 895 38. 861-10. 980 1. 0039. 29 A ATOM 1395 CG ARGA183 40.548 38.788-11. 625 1. 0045. 05 A ATOM 1396 CD ARG A 183 40.040 37.367-11. 786 1. 00 49. 47 A ATOM 1397 NE ARG A 183 39.860 36.733-10. 479 1. 00 46. 56 A ATOM 1398 CZ ARG A 183 40.178 35.478-10. 183 1. 00 50. 01 A ATOM 1399 NH1 ARG A 183 40. 712 34. 680-11. 103 1. 00 54. 64 A ATOM 1400 NH2 ARG A 183 39.935 35.014-8. 963 1. 00 46. 58 A ATOM 1401 C ARG A 183 41. 612 40. 736-9. 329 1. 00 41. 17 A ATOM 1402 O ARG A 183 41. 966 40. 480-8. 177 1. 00 42. 90 A ATOM 1403 N GLN A 184 40. 555 41. 496-9. 598 1. 00 41. 11 A ATOM 1404 CA GLNA184 39.714 42.051-8. 536 1. 0038. 54 A ATOM 1405 CB GLN A 184 39.898 43.578-8. 445 1. 00 37. 25 A ATOM 1406 CG GLNA184 41.277 44.089-7. 989 1. 0034. 78 A ATOM 1407 CD GLN A 184 41.525 43.969-6. 489 1. 00 35. 10 A ATOM 1408 OE1 GLN A 184 42. 642 43. 689-6. 065 1. 00 39. 94 A ATOM 1409 NE2 GLN A 184 40. 494 44. 191-5. 685 1. 0028. 58 A ATOM 1410 C GLN A 184 38.237 41.716-8. 778 1. 00 38. 64 A ATOM 1411 O GLN A 184 37. 552 42. 412-9. 532 1.00 39. 95 A ATOM 1412 N VAL A 185 37.758 40.637-8. 154 1. 00 37. 64 A ATOM 1413 CA VALA185 36.362 40.208-8. 283 1. 0032. 79 A ATOM 1414 CB VAL A 185 36. 228 38. 663-8. 285 1. 00 29. 14 A ATOM 1415 CG1 VAL A 185 34.800 38.234-8. 559 1. 00 26. 50 A ATOM 1416 CG2 VAL A 185 37.122 38.062-9. 328 1. 00 28. 22 A ATOM 1417 C VAL A 185 35. 569 40. 792-7. 116 1.00 34. 54 A ATOM 1418 O VAL A 185 35.941 40.606-5. 952 1. 00 33. 29 A ATOM 1419 N LYS A 186 34.470 41.472-7. 454 1. 00 36. 12 A ATOM 1420 CA LYSA186 33.576 42.129-6. 494 1. 0035. 71 A ATOM 1421 CB LYS A 186 32.707 43.190-7. 200 1. 00 42. 50 A ATOM 1422 CG LYS A 186 33.486 44.348-7. 825 1. 00 44. 32 A ATOM 1423 CD LYSA186 32.692 45.536-8. 362 1. 0046. 43 A ATOM 1424 CE LYS A 186 33.491 46.635-9. 060 1. 00 49. 14 A ATOM 1425 NZ LYSA186 32.663 47.810-9. 443 1. 0048. 49 A ATOM 1426 C LYSA186 32.686 41.181-5. 679 1. 0032. 74 A ATOM 1427 O LYS A 186 32. 079 40. 253-6. 232 1.00 30. 57 A ATOM 1428 N PRO A 187 32.627 41.383-4. 343 1. 0031. 90 A ATOM 1429 CD PRO A 187 33.499 42.254-3. 527 1. 00 30. 15 A ATOM 1430 CA PRO A 187 31.803 40.538-3. 467 1. 00 30. 79 A ATOM 1431 CB PRO A 187 32.280 40.925-2. 068 1. 0027. 32 A ATOM 1432 CG PRO A 187 32.755 42.324-2. 225 1. 00 29. 39 A ATOM 1433 C PRO A 187 30.312 40.776-3. 583 1. 00 30. 84 A ATOM 1434 O PRO A 187 29.885 41.812-4. 094 1. 00 33. 09 A ATOM 1435 N GLU A 188 29.539 39.780-3. 159 1. 00 30. 01 A ATOM 1436 CA GLU A 188 28.091 39.877-3. 138 1. 00 34. 91 A ATOM 1437 CB GLU A 188 27.426 38.929-4. 147 1. 00 35. 78 A ATOM 1438 CG GLU A 188 27.410 37.446-3. 810 1. 00 46. 17 A ATOM 1439 CD GLU A 188 26.525 36.651-4. 749 1. 00 51. 78 A ATOM 1440 OE1 GLU A 188 27. 078 35. 962-5. 634 1. 00 54. 95 A ATOM 1441 OE2 GLU A 188 25.281 36.718-4. 601 1. 00 52. 24 A ATOM 1442 C GLU A 188 27.683 39.585-1. 696 1. 00 37. 38 A ATOM 1443 O GLU A 188 28.277 38.721-1. 041 1. 00 38. 01 A ATOM 1444 N ALA A 189 26.716 40.343-1. 186 1. 00 37. 63 A ATOM 1445 CA ALAA189 26. 280 40. 170 0. 190 1.00 38. 59 A ATOM 1446 CB ALA A 189 26. 782 41. 332 1. 044 1. 00 36. 00 A ATOM 1447 C ALA A 189 24.785 39.964 0.390 1. 00 41. 14 A ATOM 1448 O ALA A 189 23. 966 40. 398-0. 430 1.00 45. 10 A ATOM 1449 N TRP A 190 24.449 39.259 1.473 1. 00 39. 75 A ATOM 1450 CA TRPA190 23.068 38.977 1.844 1. 0036. 95 A ATOM 1451 CB TRP A 190 22.502 37.788 1.048 1. 00 37. 85 A ATOM 1452 CG TRP A 190 23.048 36.393 1.329 1. 00 40. 81 A ATOM 1453 CD2 TRP A 190 24.230 35.794 0.772 1. 00 39. 87 A ATOM 1454 CE2 TRP A 190 24.232 34.423 1.168 1. 00 40. 02 A ATOM 1455 CE3 TRP A 190 25. 288 36. 273-0. 031 1. 00 39. 53 A ATOM 1456 CD1 TRPA190 22. 416 35. 396 2. 037 1. 0041. 50 A ATOM 1457 NE1 TRP A 190 23. 118 34. 216 1. 938 1. 00 41. 69 A ATOM 1458 CZ2 TRP A 190 25.256 33.520 0.782 1. 00 39. 34 A ATOM 1459 CZ3 TRP A 190 26. 316 35. 372-0. 418 1. 00 37. 11 A ATOM 1460 CH2 TRP A 190 26.284 34.009-0. 007 1. 00 32. 91 A ATOM 1461 C TRP A 190 22.937 38.760 3.342 1. 00 36. 51 A ATOM 1462 O TRP A 190 23.912 38.421 4.008 1. 00 37. 26 A ATOM 1463 N LEU A 191 21.734 38.989 3.865 1. 00 37. 19 A ATOM 1464 CA LEU A 191 21.452 38.833 5.292 1. 00 38. 47 A ATOM 1465 CB LEU A 191 20. 893 40. 141 5. 878 1. 00 33. 81 A ATOM 1466 CG LEU A 191 21.702 41.435 5.727 1. 0036. 20 A ATOM 1467 CD1 LEU A 191 20. 897 42. 599 6. 252 1.00 31. 81 A ATOM 1468 CD2 LEU A 191 23. 056 41. 336 6. 440 1.00 30. 83 A ATOM 1469 C LEU A 191 20.456 37.716 5. 552 1. 00 40. 96 A ATOM 1470 O LEU A 191 19.688 37.332 4.662 1. 00 42. 61 A ATOM 1471 N SERA 192 20.498 37.187 6.774 1. 00 43. 12 A ATOM 1472 CA SER A 192 19.586 36.135 7.228 1. 0046. 55 A ATOM 1473 CB SERA 192 19.927 34.766 6.610 1. 00 45. 08 A ATOM 1474 OG SERA 192 21.177 34.275 7.054 1. 00 52. 03 A ATOM 1475 C SERA 192 19.579 36.055 8.756 1. 0048. 13 A ATOM 1476 O SER A 192 20.426 36.654 9.427 1. 0044. 13 A ATOM 1477 N SERA 193 18.582 35.358 9.290 1. 00 51. 60 A ATOM 1478 CA SER A 193 18.435 35.182 10.722 1. 0057. 17 A ATOM 1479 CB SERA 193 17.003 35.515 11.155 1. 00 60. 68 A ATOM 1480 OG SERA 193 16.869 35.503 12.569 1. 00 70. 42 A ATOM 1481 C SERA 193 18.772 33.735 11.031 1. 00 59. 77 A ATOM 1482 O SERA 193 18.010 32.823 10.697 1. 00 61. 21 A ATOM 1483 N GLY A 194 19.920 33.532 11.672 1. 00 63. 14 A ATOM 1484 CA GLYA194 20.362 32.191 12.022 1. 0066. 93 A ATOM 1485 C GLYA194 19.611 31.571 13.189 1. 0068. 67 A ATOM 1486 O GLY A 194 18.517 32.038 13.530 1. 00 69. 96 A ATOM 1487 N PRO A 195 20.145 30.491 13.797 1. 00 70. 30 A ATOM 1488 CD PRO A 195 21.304 29.685 13.366 1. 00 71. 33 A ATOM 1489 CA PRO A 195 19. 474 29. 847 14. 932 1. 00 70. 79 A ATOM 1490 CB PRO A 195 20.333 28.601 15.168 1. 00 71. 83 A ATOM 1491 CG PRO A 195 20.904 28.312 13.812 1. 00 70. 48 A ATOM 1492 C PRO A 195 19.488 30.770 16.151 1. 00 71. 87 A ATOM 1493 O PRO A 195 20.539 31.319 16.503 1. 00 71. 06 A ATOM 1494 N SERA 196 18.311 30.975 16.746 1. 00 71. 86 A ATOM 1495 CA SER A 196 18.147 31.833 17.924 1. 0074. 01 A ATOM 1496 CB SERA 196 16.660 32.037 18.224 1. 00 75. 96 A ATOM 1497 OG SERA 196 15.996 32.592 17.103 1. 00 77. 77 A ATOM 1498 C SERA196 18. 874 31. 264 19. 155 1. 00 73. 75 A ATOM 1499 O SER A 196 18.533 30.175 19.630 1. 00 70. 20 A ATOM 1500 N PRO A 197 19.910 31.980 19.658 1. 00 75. 60 A ATOM 1501 CD PRO A 197 20.468 33.236 19.126 1. 00 74. 74 A ATOM 1502 CA PRO A 197 20.697 31.555 20.826 1. 0078. 85 A ATOM 1503 CB PRO A 197 21.852 32.563 20.842 1. 00 77. 63 A ATOM 1504 CG PRO A 197 21.916 33.057 19.425 1. 00 75. 67 A ATOM 1505 C PRO A 197 19.896 31.607 22.128 1. 00 81. 40 A ATOM 1506 O PRO A 197 19.820 30.616 22.864 1. 00 83. 69 A ATOM 1507 N GLY A 198 19.317 32.773 22.401 1. 00 81. 99 A ATOM 1508 CA GLYA198 18.500 32.950 23.586 1. 0083. 75 A ATOM 1509 C GLY A 198 17.037 32.881 23.178 1. 00 85. 16 A ATOM 1510 O GLY A 198 16.735 33.070 21.989 1. 00 84. 97 A ATOM 1511 N PRO A 199 16.103 32.596 24.117 1. 0085. 76 A ATOM 1512 CD PRO A 199 16.354 32.183 25.512 1. 00 86. 41 A ATOM 1513 CA PRO A 199 14. 664 32. 509 23. 817 1. 00 85. 47 A ATOM 1514 CB PRO A 199 14.065 32.081 25.159 1. 00 85. 75 A ATOM 1515 CG PRO A 199 15.172 31.292 25.789 1. 00 85. 18 A ATOM 1516 C PRO A 199 14.071 33.840 23.338 1. 00 84. 72 A ATOM 1517 O PRO A 199 13.096 33.856 22.579 1. 00 85. 72 A ATOM 1518 N GLY A 200 14.691 34.938 23.773 1. 00 83. 09 A ATOM 1519 CA GLYA200 14.254 36.271 23.392 1. 0080. 65 A ATOM 1520 C GLY A 200 15.298 37.014 22. 575 1. 00 79. 41 A ATOM 1521 O GLY A 200 15. 165 38. 221 22.344 1. 00 78. 63 A ATOM 1522 N ARG A 201 16.347 36.299 22.159 1. 00 76. 88 A ATOM 1523 CA ARGA201 17.424 36.882 21.359 1. 0073. 00 A ATOM 1524 CB ARG A 201 18.806 36.462 21.884 1. 00 70. 54 A ATOM 1525 CG ARG A 201 19. 127 36. 939 23. 292 1. 00 67. 61 A ATOM 1526 CD ARG A 201 20. 586 37. 140 23. 645 1. 00 62. 85 A ATOM 1527 NE ARG A 201 21. 058 38. 462 23. 240 1. 00 64. 72 A ATOM 1528 CZ ARGA201 22.295 38.918 23.428 1. 0069. 51 A ATOM 1529 NH1 ARG A 201 23.220 38.159 24.008 1. 00 72. 62 A ATOM 1530 NH2 ARG A 201 22.596 40.167 23.093 1. 00 68. 63 A ATOM 1531 C ARG A 201 17.299 36.538 19.877 1. 00 72. 47 A ATOM 1532 O ARG A 201 16.315 35.915 19.451 1. 00 73. 36 A ATOM 1533 N LEU A 202 18.305 36.950 19.102 1. 00 69. 47 A ATOM 1534 CA LEU A 202 18.342 36.718 17.662 1. 00 65. 33 A ATOM 1535 CB LEU A 202 17.547 37.820 16.953 1. 00 67. 50 A ATOM 1536 CG LEU A 202 16.840 37.534 15.627 1. 00 69. 80 A ATOM 1537 CD1 LEU A 202 15.906 36.324 15.737 1. 00 72. 02 A ATOM 1538 CD2 LEU A 202 16.057 38.777 15.242 1. 00 68. 40 A ATOM 1539 C LEUA202 19.778 36.711 17.154 1. 0061. 67 A ATOM 1540 O LEU A 202 20.617 37.474 17.644 1. 00 58. 93 A ATOM 1541 N GLN A 203 20. 054 35. 821 16.198 1. 00 58. 89 A ATOM 1542 CA GLNA203 21.382 35.704 15.587 1. 0054. 44 A ATOM 1543 CB GLN A 203 21.796 34.235 15.418 1. 00 60. 36 A ATOM 1544 CG GLN A 203 23.277 34.028 15.055 1. 00 69. 42 A ATOM 1545 CD GLN A 203 23.638 32.563 14.859 1. 00 79. 33 A ATOM 1546 OE1 GLN A 203 23. 962 32. 134 13. 748 1. 00 83. 93 A ATOM 1547 NE2 GLN A 203 23.582 31.785 15.941 1. 00 84. 58 A ATOM 1548 C GLN A 203 21.381 36.408 14.232 1. 00 48. 28 A ATOM 1549 O GLN A 203 20.759 35.949 13.265 1. 00 46. 07 A ATOM 1550 N LEU A 204 22.075 37.536 14.188 1. 00 38. 41 A ATOM 1551 CA LEU A 204 22.188 38.335 12.985 1. 00 34. 94 A ATOM 1552 CB LEU A 204 22.357 39.805 13.375 1. 00 33. 37 A ATOM 1553 CG LEU A 204 21-132 40.727 13.352 1. 0029. 33 A ATOM 1554 CD1 LEU A 204 19.949 40.159 14.120 1. 00 24. 78 A ATOM 1555 CD2 LEU A 204 21.531 42.075 13.889 1. 00 20. 56 A ATOM 1556 C LEU A 204 23.354 37.839 12.137 1. 00 33. 31 A ATOM 1557 O LEU A 204 24.503 37.886 12.564 1. 00 36. 53 A ATOM 1558 N VALA205 23.047 37.344 10. 943 1. 00 30. 92 A ATOM 1559 CA VALA205 24.071 36.804 10.047 1. 0031. 74 A ATOM 1560 CB VAL A 205 23.722 35.344 9.575 1. 00 29. 38 A ATOM 1561 CG1 VALA205 24.931 34.691 8.934 1. 0029. 77 A ATOM 1562 CG2 VAL A 205 23.220 34.484 10.728 1. 00 20. 60 A ATOM 1563 C VAL A 205 24.324 37.644 8.794 1. 00 32. 67 A ATOM 1564 O VAL A 205 23.396 37.939 8.028 1. 00 33. 43 A ATOM 1565 N CYS A 206 25.585 38.024 8.600 1. 00 32. 95 A ATOM 1566 CA CYS A 206 25.994 38.768 7.408 1. 00 33. 30 A ATOM 1567 C CYS A 206 26.860 37.827 6.566 1. 00 32. 19 A ATOM 1568 O CYS A 206 27.836 37.246 7.057 1. 00 29. 93 A ATOM 1569 CB CYS A 206 26.784 40.044 7.742 1. 00 31. 16 A ATOM 1570 SG CYS A 206 27.108 41.067 6.259 1. 00 35. 43 A ATOM 1571 N HIS A 207 26.468 37.653 5.311 1. 0029. 19 A ATOM 1572 CA HIS A 207 27.191 36.787 4.392 1. 00 31. 34 A ATOM 1573 CB HIS A 207 26.242 35.849 3.668 1. 00 32. 49 A ATOM 1574 CG HIS A 207 25.274 35.115 4.543 1. 00 31. 45 A ATOM 1575 CD2 HIS A 207 24. 147 35. 523 5. 170 1. 00 31. 83 A ATOM 1576 ND1 HIS A 207 25.370 33.760 4.772 1. 00 33. 39 A ATOM 1577 CE1 HIS A 207 24.341 33.366 5.499 1. 00 36. 21 A ATOM 1578 NE2 HIS A 207 23.584 34.416 5.755 1. 00 32. 19 A ATOM 1579 C HIS A 207 27.891 37.612 3.320 1. 00 32. 31 A ATOM 1580 O HIS A 207 27.331 38.587 2.824 1. 00 33. 50 A ATOM 1581 N VAL A 208 29.122 37.221 2.984 1. 00 32. 08 A ATOM 1582 CA VALA208 29. 942 37. 875 1. 953 1. 00 30. 44 A ATOM 1583 CB VAL A 208 31. 164 38. 631 2. 544 1. 00 29. 19 A ATOM 1584 CG1 VALA208 31. 747 39. 567 1. 515 1. 00 33. 26 A ATOM 1585 CG2 VAL A 208 30.794 39.407 3.775 1. 00 32. 30 A ATOM 1586 C VAL A 208 30.491 36.714 1.132 1. 00 32. 73 A ATOM 1587 O VAL A 208 30.978 35.737 1.710 1. 00 36. 95 A ATOM 1588 N SER A 209 30.423 36.812-0. 198 1. 00 31. 87 A ATOM 1589 CA SERA209 30.904 35.738-1. 074 1. 00 28. 79 A ATOM 1590 CB SERA209 29.879 34.604-1. 154 1. 00 27. 59 A ATOM 1591 OG SERA209 30.464 33.405-1. 636 1. 00 34. 15 A ATOM 1592 C SERA209 31.210 36.182-2. 485 1. 00 28. 03 A ATOM 1593 O SERA209 30.703 37.196-2. 950 1. 00 29. 73 A ATOM 1594 N GLY A 210 32.020 35.375-3. 167 1. 00 31. 41 A ATOM 1595 CA GLY A 210 32.385 35.637-4. 545 1. 00 30. 02 A ATOM 1596 C GLY A 210 33.534 36.591-4. 785 1. 00 30. 23 A ATOM 1597 O GLY A 210 33.789 36.918-5. 944 1. 00 32. 97 A ATOM 1598 N PHE A 211 34. 282 36.949-3. 738 1. 00 28. 47 A ATOM 1599 CA PHE A 211 35.404 37.895-3. 871 1. 00 32. 22 A ATOM 1600 CB PHE A 211 35.396 38.908-2. 721 1. 00 29. 71 A ATOM 1601 CG PHEA211 35.523 38.300-1. 359 1. 0023. 92 A ATOM 1602 CD1 PHEA211 34.410 37.738-0. 722 1. 0029. 47 A ATOM 1603 CD2 PHE A 211 36.756 38.311-0. 689 1. 00 31. 19 A ATOM 1604 CE1 PHE A 211 34. 516 37. 188 0. 585 1.00 30. 81 A ATOM 1605 CE2 PHE A 211 36. 884 37. 768 0. 610 1.00 28. 41 A ATOM 1606 CZ PHE A 211 35.757 37.205 1.252 1. 00 29. 92 A ATOM 1607 C PHE A 211 36.833 37.378-4. 028 1. 00 32. 49 A ATOM 1608 O PHE A 211 37. 181 36. 314-3. 5291. 0036. 32 A ATOM 1609 N TYR A 212 37.669 38.219-4. 627 1. 00 31. 10 A ATOM 1610 CA TYRA212 39. 086 37. 944-4.831 1. 0031. 98 A ATOM 1611 CB TYR A 212 39.343 37.128-6. 115 1. 00 30. 56 A ATOM 1612 CG TYR A 212 40.802 36.764-6. 302 1. 00 29. 92 A ATOM 1613 CD1 TYR A 212 41.660 37.580-7. 072 1. 00 32. 17 A ATOM 1614 CE1 TYR A 212 43. 047 37. 336-7. 138 1.00 28. 64 A ATOM 1615 CD2 TYR A 212 41.368 35.675-5. 613 1. 00 32. 82 A ATOM 1616 CE2 TYR A 212 42.764 35.415-5. 674 1. 00 31. 84 A ATOM 1617 CZ TYR A 212 43.586 36.254-6. 436 1. 0029. 91 A ATOM 1618 OH TYRA212 44.927 36.012-6. 495 1. 0037. 17 A ATOM 1619 C TYR A 212 39.729 39.328-4. 934 1. 00 33. 72 A ATOM 1620 O TYR A 212 39. 190 40. 183-5. 640 1.00 35. 71 A ATOM 1621 N PRO A 213 40. 883 39. 574-4.251 1. 00 34. 08 A ATOM 1622 CD PROA213 41.614 40.803-4. 604 1. 0029. 11 A ATOM 1623 CA PRO A 213 41.725 38.753-3. 362 1. 00 32. 64 A ATOM 1624 CB PRO A 213 43.042 39. 530-3.316 1. 00 34. 82 A ATOM 1625 CG PROA213 43.028 40.335-4. 574 1. 0031. 67 A ATOM 1626 C PRO A 213 41.175 38.492-1. 965 1. 00 33. 01 A ATOM 1627 O PRO A 213 40.089 38.955-1. 613 1. 00 33. 00 A ATOM 1628 N LYS A 214 41.954 37.744-1. 190 1. 00 35. 70 A ATOM 1629 CA LYS A 214 41. 614 37. 337 0. 170 1. 00 35. 29 A ATOM 1630 CB LYS A 214 42.640 36.302 0.671 1. 00 37. 47 A ATOM 1631 CG LYS A 214 42.132 35.267 1.681 1. 00 42. 59 A ATOM 1632 CD LYS A 214 43.165 34.205 2.098 1. 00 45. 50 A ATOM 1633 CE LYSA214 42.885 33.341 3.319 1. 0040. 44 A ATOM 1634 NZ LYS A 214 41.828 32.328 3.078 1. 00 39. 30 A ATOM 1635 C LYS A 214 41.351 38.443 1.210 1. 00 34. 55 A ATOM 1636 O LYS A 214 40.331 38.356 1.897 1. 00 36. 52 A ATOM 1637 N PRO A 215 42.200 39.517 1.300 1. 00 34. 02 A ATOM 1638 CD PRO A 215 43.450 39.852 0.580 1. 00 29. 25 A ATOM 1639 CA PRO A 215 41.927 40.565 2.307 1. 00 32. 93 A ATOM 1640 CB PRO A 215 43.058 41.565 2.076 1. 00 29. 89 A ATOM 1641 CG PRO A 215 44.168 40.707 1.566 1. 00 26. 69 A ATOM 1642 C PRO A 215 40. 553 41. 236 2. 176 1. 00 33. 04 A ATOM 1643 O PRO A 215 40. 172 41. 695 1. 096 1.00 35. 39 A ATOM 1644 N VAL A 216 39. 807 41. 222 3.281 1. 00 34. 12 A ATOM 1645 CA VALA216 38. 458 41. 781 3. 354 1. 00 34. 46 A ATOM 1646 CB VALA216 37.411 40.729 2.840 1. 00 37. 32 A ATOM 1647 CG1 VALA216 37. 375 39. 497 3. 737 1. 00 35. 22 A ATOM 1648 CG2 VAL A 216 36. 027 41. 337 2. 657 1. 00 38. 63 A ATOM 1649 C VAL A 216 38. 125 42. 235 4. 782 1.00 35. 07 A ATOM 1650 O VAL A 216 38. 594 41. 654 5. 759 1. 00 35. 08 A ATOM 1651 N TRP A 217 37. 283 43. 257 4.881 1. 00 38. 29 A ATOM 1652 CA TRPA217 36. 870 43. 811 6. 163 1.00 43. 22 A ATOM 1653 CB TRPA217 37.360 45.267 6.250 1. 0048. 72 A ATOM 1654 CG TRPA217 37.259 45.929 7.604 1. 0058. 80 A ATOM 1655 CD2 TRP A 217 36.131 46.642 8.144 1. 00 63. 17 A ATOM 1656 CE2 TRP A 217 36.527 47.147 9.411 1. 0062. 34 A ATOM 1657 CE3 TRP A 217 34.822 46.909 7.679 1. 0063. 29 A ATOM 1658 CD1 TRP A 217 38. 252 46. 024 8. 538 1. 00 63. 36 A ATOM 1659 NE1 TRP A 217 37. 822 46. 755 9.621 1. 00 64. 88 A ATOM 1660 CZ2 TRP A 217 35. 664 47. 911 10. 226 1. 0061. 82 A ATOM 1661 CZ3 TRP A 217 33.956 47.672 8.489 1. 00 61. 42 A ATOM 1662 CH2 TRP A 217 34. 389 48. 164 9.751 1. 0061. 36 A ATOM 1663 C TRPA217 35.344 43.740 6.261 1. 0041. 50 A ATOM 1664 O TRP A 217 34.640 44.280 5.409 1. 00 43. 12 A ATOM 1665 N VAL A 218 34.834 43.052 7.281 1. 00 39. 50 A ATOM 1666 CA VAL A 218 33. 385 42. 923 7. 486 1.00 41. 78 A ATOM 1667 CB VALA218 32.797 41.526 7.040 1. 0042. 51 A ATOM 1668 CG1 VALA218 31. 262 41. 569 7. 029 1. 00 36. 38 A ATOM 1669 CG2 VAL A 218 33.303 41.107 5.666 1. 0042. 39 A ATOM 1670 C VALA218 33.046 43.103 8.960 1. 0043. 89 A ATOM 1671 O VAL A 218 33.579 42.397 9.823 1. 00 46. 60 A ATOM 1672 N MET A 219 32.155 44.048 9.245 1. 0044. 32 A ATOM 1673 CA MET A 219 31.717 44.309 10.613 1. 00 46. 39 A ATOM 1674 CB MET A 219 32.508 45.463 11.250 1. 0049. 14 A ATOM 1675 CG MET A 219 33.801 45.091 11.952 1. 0049. 04 A ATOM 1676 SD MET A 219 33.499 44.222 13.469 1. 00 55. 41 A ATOM 1677 CE MET A 219 34.146 45.380 14.681 1. 0053. 59 A ATOM 1678 C MET A 219 30.252 44.681 10.667 1. 0045. 87 A ATOM 1679 META219 29. 680 45. 159 9. 680 1.00 42. 56 A ATOM 1680 N TRP A 220 29. 650 44.426 11.826 1.00 45. 39 A ATOM 1681 CA TRPA220 28.271 44.804 12.076 1. 0048. 89 A ATOM 1682 CB TRPA220 27.587 43.817 13.018 1. 0046. 86 A ATOM 1683 CG TRP A 220 26.913 42.664 12.324 1. 00 50. 76 A ATOM 1684 CD2 TRP A 220 25.642 42.680 11.655 1. 0053. 11 A ATOM 1685 CE2 TRP A 220 25. 414 41. 365 11.158 1. 0055. 12 A ATOM 1686 CE3 TRP A 220 24.666 43.674 11.423 1. 0052. 75 A ATOM 1687 CD1 TRP A 220 27. 386 41. 382 12. 210 1. 00 51. 67 A ATOM 1688 NE1 TRP A 220 26. 494 40. 600 11. 513 1. 0052. 17 A ATOM 1689 CZ2 TRP A 220 24.244 41.017 10.435 1. 0051. 97 A ATOM 1690 CZ3 TRP A 220 23. 494 43. 329 10.699 1. 0052. 24 A ATOM 1691 CH2 TRP A 220 23. 302 42. 005 10.217 1. 0050. 74 A ATOM 1692 C TRP A 220 28. 356 46. 206 12. 701 1. 0051. 32 A ATOM 1693 O TRP A 220 29. 152 46. 436 13. 621 1. 0052. 61 A ATOM 1694 N MET A 221 27. 607 47. 151 12. 129 1.00 51. 46 A ATOM 1695 CA MET A 221 27.599 48.550 12.574 1. 0052. 64 A ATOM 1696 CB META221 27.962 49.481 11.403 1. 0052. 95 A ATOM 1697 CG META221 29.189 49.122 10.591 1. 0053. 85 A ATOM 1698 SD MET A 221 30. 744 49. 489 11. 379 1. 0058. 51 A ATOM 1699 CE META221 30.886 51.271 11.101 1. 0055. 93 A ATOM 1700 C MET A 221 26. 249 49. 032 13.110 1. 0050. 75 A ATOM 1701 O MET A 221 25. 222 48. 378 12.938 1. 0049. 10 A ATOM 1702 N ARG A 222 26.295 50.206 13.740 1. 00 50. 11 A ATOM 1703 CA ARGA222 25.139 50.930 14.266 1. 0049. 82 A ATOM 1704 CB ARGA222 24.985 50.779 15.788 1. 0047. 60 A ATOM 1705 CG ARG A 222 23.733 51.471 16.334 1. 00 46. 04 A ATOM 1706 CD ARG A 222 23.341 51.263 17.801 1. 00 49. 22 A ATOM 1707 NE ARGA222 22.802 49.928 18.091 1. 0050. 45 A ATOM 1708 CZ ARG A 222 21.606 49.473 17.705 1. 00 47. 85 A ATOM 1709 NH1 ARG A 222 20. 782 50.236 16.992 1.00 47. 98 A ATOM 1710 NH2 ARG A 222 21.233 48.243 18.033 1. 00 41. 59 A ATOM 1711 C ARGA222 25.498 52.364 13.874 1. 0049. 70 A ATOM 1712 O ARGA222 26.112 53.113 14.644 1. 0048. 97 A ATOM 1713 N GLYA223 25.201 52.682 12.615 1. 0052. 43 A ATOM 1714 CA GLYA223 25.495 53.987 12.053 1. 00 57. 13 A ATOM 1715 C GLYA223 26.964 54.033 11.688 1. 00 61. 54 A ATOM 1716 O GLYA223 27.401 53.391 10.724 1. 00 65. 21 A ATOM 1717 N GLU A 224 27.727 54.779 12.483 1. 00 62. 87 A ATOM 1718 CA GLU A 224 29.164 54.920 12.288 1. 00 63. 08 A ATOM 1719 CB GLU A 224 29.547 56.400 12.080 1. 00 62. 79 A ATOM 1720 CG GLU A 224 28.865 57.129 10.887 1. 00 67. 86 A ATOM 1721 CD GLU A 224 29.169 56.519 9.507 1. 00 68. 52 A ATOM 1722 OE1 GLU A 224 30. 316 56. 659 9. 023 1. 00 65. 84 A ATOM 1723 OE2 GLU A 224 28.249 55.919 8.901 1. 00 65. 44 A ATOM 1724 C GLU A 224 29.912 54.317 13.485 1. 00 65. 29 A ATOM 1725 O GLU A 224 31.128 54.484 13.611 1. 00 68. 00 A ATOM 1726 N GLN A 225 29.178 53.608 14.350 1. 00 66. 16 A ATOM 1727 CA GLNA225 29.746 52.960 15.539 1. 0066. 37 A ATOM 1728 CB GLN A 225 28.978 53.368 16.808 1. 00 68. 54 A ATOM 1729 CG GLN A 225 29.544 52.795 18.126 1. 00 75. 23 A ATOM 1730 CD GLN A 225 28.477 52.134 19.014 1. 00 83. 60 A ATOM 1731 OE1 GLNA225 27.491 51.571 18.522 1. 0084. 90 A ATOM 1732 NE2 GLN A 225 28.687 52.190 20.328 1. 00 82. 20 A ATOM 1733 C GLN A 225 29.702 51.444 15.375 1. 00 65. 18 A ATOM 1734 O GLN A 225 28.624 50.855 15.314 1. 00 67. 45 A ATOM 1735 N GLU A 226 30.879 50.822 15.332 1. 00 64. 47 A ATOM 1736 CA GLUA226 30.994 49.372 15.179 1. 0062. 17 A ATOM 1737 CB GLU A 226 32.310 48.981 14.490 1. 00 61. 73 A ATOM 1738 CG GLUA226 33.563 49.746 14.892 1. 0062. 80 A ATOM 1739 CD GLU A 226 34.715 49.491 13.924 1. 00 65. 24 A ATOM 1740 OE1 GLU A 226 35.453 48.502 14.121 1. 00 64. 30 A ATOM 1741 OE2 GLU A 226 34.875 50.271 12.955 1. 00 63. 54 A ATOM 1742 C GLU A 226 30.793 48.565 16.455 1. 00 61. 92 A ATOM 1743 O GLU A 226 31. 155 49. 006 17. 548 1. 00 63. 35 A ATOM 1744 N GLNA227 30.190 47.388 16.294 1. 0060. 91 A ATOM 1745 CA GLNA227 29.908 46.477 17.401 1. 0060. 19 A ATOM 1746 CB GLNA227 28.679 45.616 17.080 1. 0056. 17 A ATOM 1747 CG GLNA227 27.460 46.385 16.552 1. 0048. 71 A ATOM 1748 CD GLN A 227 26.918 47. 412 17.526 1. 00 44. 18 A ATOM 1749 OE1 GLN A 227 27.058 48.616 17.314 1. 0040. 98 A ATOM 1750 NE2 GLN A 227 26.287 46.940 18.596 1. 00 39. 04 A ATOM 1751 C GLNA227 31. 105 45. 579 17.683 1. 0061. 92 A ATOM 1752 O GLN A 227 31.661 44.975 16.765 1. 00 62. 24 A ATOM 1753 N GLN A 228 31. 492 45. 498 18. 956 1. 00 63. 78 A ATOM 1754 CA GLNA228 32.629 44.681 19.389 1. 0065. 71 A ATOM 1755 CB GLNA228 33.170 45.188 20.732 1. 0069. 34 A ATOM 1756 CG GLNA228 33.822 46.571 20.672 1. 0072. 53 A ATOM 1757 CD GLNA228 35.115 46.585 19.865 1. 0074. 79 A ATOM 1758 OE1 GLN A 228 36. 182 46. 225 20. 373 1. 00 76. 66 A ATOM 1759 NE2 GLN A 228 35. 022 46. 994 18. 602 1. 0071. 74 A ATOM 1760 C GLN A 228 32.340 43.185 19.478 1. 00 65. 65 A ATOM 1761 O GLNA228 33. 254 42. 368 19.318 1. 0067. 14 A ATOM 1762 N GLYA229 31.065 42.842 19.689 1. 0064. 00 A ATOM 1763 CA GLY A 229 30. 640 41. 451 19. 798 1. 00 62. 06 A ATOM 1764 C GLY A 229 30. 430 40. 734 18. 471 1. 0061. 19 A ATOM 1765 O GLYA229 29.817 39.653 18.426 1. 00 60. 85 A ATOM 1766 N THRA230 30.946 41.339 17.397 1. 0057. 07 A ATOM 1767 CA THRA230 30.852 40.803 16.041 1. 0052. 96 A ATOM 1768 CB THRA230 31.157 41.900 14.995 1. 0049. 97 A ATOM 1769 OG1 THRA230 30.294 43.018 15.215 1. 0056. 66 A ATOM 1770 CG2 THR A 230 30.943 41.400 13.576 1. 00 48. 29 A ATOM 1771 C THRA230 31.821 39.635 15.862 1. 00 51. 73 A ATOM 1772 O THR A 230 33.039 39.834 15.751 1. 00 51. 98 A ATOM 1773 N GLN A 231 31.267 38.423 15.874 1. 00 50. 10 A ATOM 1774 CA GLNA231 32.051 37.205 15.701 1. 0048. 68 A ATOM 1775 CB GLN A 231 31.408 36.018 16.416 1. 00 49. 76 A ATOM 1776 CG GLN A 231 31.376 36.147 17.930 1. 00 54. 56 A ATOM 1777 CD GLN A 231 30.512 35.084 18.583 1. 00 58. 51 A ATOM 1778 OE1 GLNA231 30. 997 34. 271 19. 374 1. 0059. 16 A ATOM 1779 NE2 GLN A 231 29.218 35.088 18.257 1. 00 60. 24 A ATOM 1780 C GLNA231 32.213 36.912 14.221 1. 0048. 94 A ATOM 1781 O GLN A 231 31.240 36.708 13.481 1. 00 47. 48 A ATOM 1782 N LEU A 232 33.471 36.956 13.805 1. 00 48. 98 A ATOM 1783 CA LEU A 232 33.896 36.724 12.436 1. 00 46. 97 A ATOM 1784 CB LEU A 232 35.210 37.480 12.231 1. 00 48. 69 A ATOM 1785 CG LEU A 232 35.746 37.860 10.859 1. 00 56. 14 A ATOM 1786 CD1 LEU A 232 34. 765 38. 788 10. 151 1. 00 62. 36 A ATOM 1787 CD2 LEU A 232 37.089 38.558 11.047 1. 00 60. 14 A ATOM 1788 C LEU A 232 34.103 35.223 12.207 1. 00 44. 95 A ATOM 1789 O LEUA232 34.634 34.529 13.077 1. 0043. 80 A ATOM 1790 N GLYA233 33.647 34.727 11.056 1. 00 45. 13 A ATOM 1791 CA GLYA233 33.799 33.317 10.712 1. 0041. 24 A ATOM 1792 C GLY A 233 35.120 33.065 10.002 1. 00 41. 26 A ATOM 1793 O GLY A 233 35.951 33.975 9.894 1. 00 41. 66 A ATOM 1794 N ASP A 234 35.324 31.842 9.519 1. 00 39. 94 A ATOM 1795 CA ASP A 234 36. 552 31. 488 8. 800 1.00 41. 90 A ATOM 1796 CB ASP A 234 36.824 29.979 8.878 1. 00 45. 92 A ATOM 1797 CG ASP A 234 37.146 29.500 10.281 1. 0048. 37 A ATOM 1798 OD1 ASP A 234 37.911 30.184 11.009 1. 00 48. 97 A ATOM 1799 OD2 ASP A 234 36.640 28.413 10.638 1. 00 47. 45 A ATOM 1800 C ASP A 234 36.421 31.876 7.334 1. 00 40. 15 A ATOM 1801 O ASP A 234 35.306 31.916 6.812 1. 00 39. 38 A ATOM 1802 N ILE A 235 37.550 32.169 6.679 1. 00 39. 22 A ATOM 1803 CA ILE A 235 37.541 32.528 5.258 1. 00 39. 23 A ATOM 1804 CB ILE A 235 38.714 33.475 4.849 1. 00 42. 01 A ATOM 1805 CG2 ILE A 235 38.537 33.917 3.393 1. 00 41. 46 A ATOM 1806 CG1 ILEA 235 38. 718 34. 741 5. 723 1.00 44. 63 A ATOM 1807 CD1 ILE A 235 39. 886 35. 718 5. 462 1. 00 52. 65 A ATOM 1808 C ILE A 235 37.552 31.231 4.447 1. 00 36. 87 A ATOM 1809 O ILE A 235 38.606 30.701 4.079 1. 00 41. 61 A ATOM 1810 N LEU A 236 36.342 30.722 4.238 1. 00 33. 85 A ATOM 1811 CA LEU A 236 36. 044 29. 491 3.516 1. 00 30. 64 A ATOM 1812 CB LEU A 236 34. 623 29. 049 3. 870 1. 00 30. 03 A ATOM 1813 CG LEU A 236 34.261 28.981 5.357 1. 00 31. 93 A ATOM 1814 CD1 LEUA236 32. 799 28. 627 5. 545 1. 00 31. 93 A ATOM 1815 CD2 LEU A 236 35.147 27.988 6.072 1. 00 38. 34 A ATOM 1816 C LEU A 236 36.190 29.645 1.996 1. 00 32. 80 A ATOM 1817 O LEU A 236 35.827 30.682 1.440 1. 00 32. 96 A ATOM 1818 N PRO A 237 36.728 28.614 1.303 1. 00 36. 06 A ATOM 1819 CD PRO A 237 37.460 27.434 1.813 1. 00 35. 03 A ATOM 1820 CA PRO A 237 36.895 28.723-0. 149 1. 00 36. 01 A ATOM 1821 CB PRO A 237 38.140 27.883-0. 398 1. 00 33. 37 A ATOM 1822 CG PRO A 237 37.951 26.756 0.547 1. 00 35. 64 A ATOM 1823 C PRO A 237 35.755 28.275-1. 042 1. 00 37. 17 A ATOM 1824 O PRO A 237 34.800 27.638-0. 612 1. 00 37. 46 A ATOM 1825 N ASN A 238 35.896 28.660-2. 300 1. 00 41. 09 A ATOM 1826 CA ASNA238 34. 997 28. 322-3.391 1. 0044. 34 A ATOM 1827 CB ASN A 238 34.194 29.550-3. 835 1. 00 46. 14 A ATOM 1828 CG ASN A 238 32.961 29.814-2. 977 1. 00 47. 61 A ATOM 1829 OD1 ASN A 238 32. 115 28. 932-2. 798 1. 00 49. 02 A ATOM 1830 ND2 ASN A 238 32. 814 31. 058-2. 509 1. 00 36. 72 A ATOM 1831 C ASN A 238 36. 027 27. 919-4.461 1. 00 46. 92 A ATOM 1832 O ASN A 238 37.092 28.548-4. 580 1. 00 49. 25 A ATOM 1833 N ALA A 239 35.732 26.862-5. 213 1. 00 46. 42 A ATOM 1834 CA ALA A 239 36.646 26.350-6. 237 1. 0045. 01 A ATOM 1835 CB ALAA239 36.186 25.017-6. 682 1. 0045. 84 A ATOM 1836 C ALA A 239 36.912 27.237-7. 453 1. 00 46. 63 A ATOM 1837 O ALA A 239 37.773 26.912-8. 283 1. 00 48. 77 A ATOM 1838 N ASNA240 36.172 28.344-7. 558 1. 0044. 16 A ATOM 1839 CA ASNA240 36.330 29.299-8. 660 1. 0042. 18 A ATOM 1840 CB ASN A 240 34.971 29.893-9. 082 1. 00 39. 66 A ATOM 1841 CG ASN A 240 34.283 30.654-7. 961 1. 00 38. 77 A ATOM 1842 OD1 ASN A 240 33. 682 31. 699-8. 179 1. 00 40. 51 A ATOM 1843 ND2 ASN A 240 34.373 30.129-6. 758 1. 00 37. 70 A ATOM 1844 C ASN A 240 37.308 30.402-8. 258 1. 00 39. 94 A ATOM 1845 O ASN A 240 37.249 31.523-8. 778 1. 00 43. 89 A ATOM 1846 N TRP A 241 38.182 30.067-7. 304 1. 00 36. 03 A ATOM 1847 CA TRPA241 39.213 30.955-6. 763 1. 0029. 85 A ATOM 1848 CB TRPA241 40.258 31.294-7. 840 1. 00 31. 42 A ATOM 1849 CG TRP A 241 41.293 30.225-8. 082 1. 00 30. 24 A ATOM 1850 CD2 TRP A 241 42.625 30.433-8. 547 1. 00 25. 52 A ATOM 1851 CE2 TRP A 241 43.268 29.163-8. 562 1. 00 31. 37 A ATOM 1852 CE3 TRP A 241 43.352 31.574-8. 950 1. 0024. 58 A ATOM 1853 CD1 TRP A 241 41. 173 28. 874-7.851 1. 00 27. 11 A ATOM 1854 NE1 TRP A 241 42.355 28.235-8. 132 1. 0029. 30 A ATOM 1855 CZ2 TRP A 241 44. 621 28.998-8. 965 1. 00 34. 22 A ATOM 1856 CZ3 TRP A 241 44.704 31.417-9. 352 1. 00 29. 97 A ATOM 1857 CH2 TRP A 241 45.320 30.131-9. 353 1. 00 33. 91 A ATOM 1858 C TRPA241 38.644 32.211-6. 116 1. 0027. 39 A ATOM 1859 O TRP A 241 39.128 33.323-6. 327 1. 00 27. 52 A ATOM 1860 N THR A 242 37. 536 32.028-5. 411 1. 00 27. 71 A ATOM 1861 CA THRA242 36.876 33.119-4. 705 1. 0029. 76 A ATOM 1862 CB THR A 242 35. 525 33.509 -5. 331 1. 00 33. 99 A ATOM 1863 OG1 THRA242 34.653 32. 374-5.373 1. 00 39. 34 A ATOM 1864 CG2 THR A 242 35.708 34.106-6. 735 1. 00 35. 13 A ATOM 1865 C THR A 242 36.672 32.695-3. 267 1. 00 27. 92 A ATOM 1866 O THR A 242 36.913 31.535-2. 922 1. 00 28. 80 A ATOM 1867 N TRP A 243 36.219 33.620-2. 427 1. 00 28. 54 A ATOM 1868 CA TRPA243 36.053 33.318-1. 003 1. 0032. 83 A ATOM 1869 CB TRPA243 37.063 34.131-0. 189 1. 0033. 62 A ATOM 1870 CG TRP A 243 38.486 33.990-0. 675 1. 00 32. 25 A ATOM 1871 CD2 TRP A 243 39.370 32.907-0. 409 1. 00 33. 41 A ATOM 1872 CE2 TRP A 243 40.560 33.147-1. 149 1. 0034. 43 A ATOM 1873 CE3 TRP A 243 39.280 31.745 0.384 1. 00 36. 33 A ATOM 1874 CD1 TRPA243 39.152 34.829-1. 528 1. 0033. 04 A ATOM 1875 NE1 TRP A 243 40. 396 34. 326-1. 8231. 0034. 71 A ATOM 1876 CZ2 TRP A 243 41.651 32.272-1. 121 1. 00 37. 63 A ATOM 1877 CZ3 TRP A 243 40.371 30.863 0.415 1. 00 42. 27 A ATOM 1878 CH2 TRP A 243 41.543 31.137-0. 338 1. 00 44. 94 A ATOM 1879 C TRP A 243 34.645 33.445-0. 423 1. 00 32. 72 A ATOM 1880 O TRP A 243 33. 704 33. 794-1. 138 1. 00 38. 67 A ATOM 1881 N TYR A 244 34.508 33.076 0.852 1. 00 27. 52 A ATOM 1882 CA TRP A 244 33. 240 33. 109 1. 582 1.00 28. 26 A ATOM 1883 CB TYR A 244 32.551 31.739 1.494 1. 00 28. 20 A ATOM 1884 CG TYR A 244 31.147 31.644 2.081 1. 0031. 11 A ATOM 1885 CD1 TYR A 244 30. 020 31. 847 1. 278 1. 00 35. 33 A ATOM 1886 CE1 TYR A 244 28. 705 31. 725 1. 805 1.00 37. 89 A ATOM 1887 CD2 TYR A 244 30.938 31.314 3.437 1. 00 34. 85 A ATOM 1888 CE2 TYR A 244 29.629 31.193 3.979 1. 0037. 18 A ATOM 1889 CZ TYR A 244 28.522 31.401 3.152 1. 00 35. 06 A ATOM 1890 OH TYR A 244 27.249 31.285 3.658 1. 00 38. 59 A ATOM 1891 C TYR A 244 33.543 33.466 3.044 1. 00 31. 88 A ATOM 1892 O TYR A 244 34.431 32.880 3.668 1. 00 31. 22 A ATOM 1893 N LEU A 245 32. 783 34.416 3.583 1. 00 31. 96 A ATOM 1894 CA LEU A 245 32.952 34.859 4.958 1. 00 32. 54 A ATOM 1895 CB LEU A 245 33.858 36.105 5.029 1. 00 32. 68 A ATOM 1896 CG LEU A 245 34.238 36.711 6.399 1. 00 37. 30 A ATOM 1897 CD1 LEU A 245 34. 797 35. 671 7. 359 1. 00 36. 47 A ATOM 1898 CD2 LEU A 245 35. 248 37. 808 6. 215 1. 00 35. 48 A ATOM 1899 C LEU A 245 31.597 35.137 5.587 1. 00 32. 69 A ATOM 1900 O LEU A 245 30.676 35.624 4.928 1. 00 32. 92 A ATOM 1901 N ARG A 246 31.503 34.801 6.868 1. 00 33. 31 A ATOM 1902 CA ARGA246 30.301 34.975 7.670 1. 0035. 69 A ATOM 1903 CB ARG A 246 29.908 33.617 8.252 1. 00 39. 66 A ATOM 1904 CG ARG A 246 28.467 33.200 8.074 1. 00 44. 38 A ATOM 1905 CD ARG A 246 28.077 31.866 8.705 1. 00 48. 04 A ATOM 1906 NE ARG A 246 28.544 31.768 10.091 1. 0050. 31 A ATOM 1907 CZ ARGA246 27.786 31. 465 11.143 1. 0048. 69 A ATOM 1908 NH1 ARG A 246 26.488 31.211 11.004 1. 0051. 53 A ATOM 1909 NH2 ARG A 246 28. 331 31.459 12.353 1. 00 47. 77 A ATOM 1910 C ARG A 246 30.657 35.932 8.811 1. 00 35. 97 A ATOM 1911 O ARG A 246 31.777 35.879 9.330 1. 00 38. 57 A ATOM 1912 N ALA A 247 29.738 36.835 9.159 1. 00 34. 10 A ATOM 1913 CA ALA A 247 29. 948 37. 781 10. 264 1.00 31. 41 A ATOM 1914 CB ALA A 247 30. 257 39. 161 9.751 1. 00 23. 10 A ATOM 1915 C ALAA247 28.673 37.785 11.074 1. 00 31. 57 A ATOM 1916 O ALAA247 27.622 38.205 10.585 1. 00 37. 24 A ATOM 1917 N THRA248 28.754 37.260 12.294 1. 00 31. 68 A ATOM 1918 CA THR A 248 27. 588 37.163 13.164 1.00 32. 17 A ATOM 1919 CB THRA248 27.378 35.722 13.669 1. 0032. 01 A ATOM 1920 OG1 THR A 248 28. 646 35. 079 13. 858 1. 00 29. 63 A ATOM 1921 CG2 THR A 248 26. 538 34. 940 12.691 1. 00 30. 26 A ATOM 1922 C THRA248 27.542 38.090 14.360 1. 00 34. 26 A ATOM 1923 O THRA248 28.572 38.614 14.789 1. 00 35. 14 A ATOM 1924 N LEU A 249 26.323 38.296 14.868 1. 00 35. 48 A ATOM 1925 CA LEUA249 26.062 39.118 16.051 1. 0036. 84 A ATOM 1926 CB LEU A 249 25.761 40.572 15.687 1. 00 31. 47 A ATOM 1927 CG LEU A 249 26.460 41.742 16.399 1. 00 30. 56 A ATOM 1928 CD1 LEU A 249 25.606 42.967 16.169 1. 00 28. 95 A ATOM 1929 CD2 LEU A 249 26.651 41.550 17.896 1. 00 33. 57 A ATOM 1930 C LEU A 249 24.874 38.568 16.826 1. 00 40. 63 A ATOM 1931 O LEU A 249 23.787 38.373 16.266 1. 00 39. 68 A ATOM 1932 N ASP A 250 25.109 38.300 18.114 1. 0046. 25 A ATOM 1933 CA ASP A 250 24.080 37.811 19. 037 1. 0050. 06 A ATOM 1934 CB ASP A 250 24.714 36.957 20.149 1. 00 58. 97 A ATOM 1935 CG ASP A 250 23.692 36.097 20.906 1. 00 67. 05 A ATOM 1936 OD1 ASP A 250 22. 483 36. 439 20. 944 1. 00 70. 25 A ATOM 1937 OD2 ASP A 250 24.111 35.059 21.467 1. 0071. 83 A ATOM 1938 C ASP A 250 23.469 39.091 19.616 1. 00 48. 54 A ATOM 1939 O ASP A 250 24.156 39.873 20.291 1. 00 46. 12 A ATOM 1940 N VAL A 251 22.187 39.301 19.332 1. 00 47. 44 A ATOM 1941 CA VALA251 21. 505 40. 511 19.771 1. 0050. 54 A ATOM 1942 CB VAL A 251 21.541 41.573 18.604 1. 00 47. 99 A ATOM 1943 CG1 VALA251 20. 314 41. 486 17. 691 1. 00 40. 56 A ATOM 1944 CG2 VAL A 251 21.775 42.965 19.152 1. 00 52. 67 A ATOM 1945 C VAL A 251 20.080 40.260 20.280 1. 00 52. 50 A ATOM 1946 O VAL A 251 19.480 39.230 19.965 1. 00 55. 99 A ATOM 1947 N ALA A 252 19.557 41.211 21.059 1. 00 52. 52 A ATOM 1948 CA ALA A 252 18.194 41.145 21.597 1. 0055. 64 A ATOM 1949 CB ALA A 252 18. 074 42.024 22.835 1.00 52. 54 A ATOM 1950 C ALAA252 17.198 41.597 20.512 1. 00 57. 75 A ATOM 1951 O ALAA252 17. 557 42. 401 19.640 1. 00 58. 27 A ATOM 1952 N ASP A 253 15.963 41.087 20.579 1. 0057. 26 A ATOM 1953 CA ASP A 253 14.893 41.383 19.610 1. 0059. 25 A ATOM 1954 CB ASP A 253 13.562 40.813 20.106 1. 00 63. 27 A ATOM 1955 CG ASP A 253 13.427 39.323 19.850 1. 00 67. 20 A ATOM 1956 OD1 ASP A 253 14. 457 38. 609 19. 842 1. 00 69. 63 A ATOM 1957 OD2 ASP A 253 12.281 38.863 19.656 1. 00 69. 35 A ATOM 1958 C ASP A 253 14.689 42.830 19.142 1. 0060. 01 A ATOM 1959 O ASP A 253 14. 679 43.097 17.932 1.00 59. 76 A ATOM 1960 N GLY A 254 14. 563 43.753 20.098 1.00 58. 86 A ATOM 1961 CA GLYA254 14.365 45.158 19.778 1. 0059. 04 A ATOM 1962 C GLYA254 15.591 45.889 19.248 1. 00 60. 11 A ATOM 1963 O GLY A 254 15. 456 46.859 18.495 1.00 62. 17 A ATOM 1964 N GLU A 255 16.780 45.392 19.597 1. 00 59. 12 A ATOM 1965 CA GLU A 255 18.056 45.992 19.186 1. 00 56. 62 A ATOM 1966 CB GLU A 255 19.181 45.508 20.093 1. 00 55. 52 A ATOM 1967 CG GLU A 255 18.971 45.747 21.566 1. 00 67. 43 A ATOM 1968 CD GLU A 255 20.188 45.359 22.383 1. 00 76. 42 A ATOM 1969 OE1 GLU A 255 20.694 46.225 23.132 1. 00 78. 97 A ATOM 1970 OE2 GLU A 255 20.648 44.196 22.272 1. 0081. 40 A ATOM 1971 C GLU A 255 18.467 45.744 17.733 1. 00 53. 87 A ATOM 1972 O GLU A 255 19.305 46.472 17.197 1. 00 52. 19 A ATOM 1973 N ALA A 256 17.865 44.729 17.106 1. 00 51. 60 A ATOM 1974 CA ALA A 256 18.146 44.341 15.718 1. 0048. 53 A ATOM 1975 CB ALAA256 17.327 43.119 15.342 1. 00 48. 51 A ATOM 1976 C ALAA256 17.922 45.454 14.701 1. 0047. 66 A ATOM 1977 O ALA A 256 18.633 45.541 13.700 1. 00 48. 63 A ATOM 1978 N ALA A 257 16.958 46.325 14.992 1. 00 46. 41 A ATOM 1979 CA ALAA257 16.638 47.459 14.128 1. 0043. 97 A ATOM 1980 CB ALA A 257 15.263 47.999 14.463 1. 0048. 66 A ATOM 1981 C ALAA257 17.687 48.544 14.313 1. 00 39. 32 A ATOM 1982 O ALAA257 18.098 48.827 15.438 1. 00 37. 31 A ATOM 1983 N GLYA258 18.130 49.120 13.200 1. 00 37. 24 A ATOM 1984 CA GLY A 258 19.141 50.166 13.239 1. 00 37. 80 A ATOM 1985 C GLYA258 20.511 49.617 12.897 1. 00 37. 65 A ATOM 1986 O GLYA258 21.412 50.360 12.484 1. 00 36. 24 A ATOM 1987 N LEU A 259 20.656 48.301 13.054 1. 00 36. 27 A ATOM 1988 CA LEU A 259 21.906 47.616 12.765 1. 00 34. 32 A ATOM 1989 CB LEU A 259 22.006 46.316 13.564 1. 00 28. 71 A ATOM 1990 CG LEU A 259 22.247 46.496 15.065 1. 00 30. 41 A ATOM 1991 CD1 LEU A 259 22.090 45.182 15.782 1. 0032. 04 A ATOM 1992 CD2 LEU A 259 23.624 47.080 15.342 1. 0023. 96 A ATOM 1993 C LEUA259 22.125 47.351 11.283 1. 0034. 93 A ATOM 1994 O LEU A 259 21.181 47.013 10.549 1. 00 34. 95 A ATOM 1995 N SERA260 23.368 47.565 10.852 1. 00 32. 55 A ATOM 1996 CA SER A 260 23. 768 47. 350 9. 468 1.00 32. 55 A ATOM 1997 CB SERA260 23.948 48.678 8.747 1. 00 32. 20 A ATOM 1998 OG SERA260 25.001 49.437 9.312 1. 00 39.79 A ATOM 1999 C SERA260 25.071 46.585 9.387 1. 00 33. 59 A ATOM 2000 O SERA260 25.849 46.591 10.336 1. 00 33. 61 A ATOM 2001 N CYS A 261 25.290 45.913 8.258 1. 00 32. 32 A ATOM 2002 CA CYSA261 26. 523 45. 164 8.009 1. 0032. 30 A ATOM 2003 C CYS A 261 27.341 46.009 7.040 1. 00 30. 09 A ATOM 2004 O CYS A 261 26.778 46.598 6.126 1. 00 30. 45 A ATOM 2005 CB CYS A 261 26.219 43.798 7.377 1. 00 30. 55 A ATOM 2006 SG CYS A 261 27.733 42.866 6.975 1. 00 39. 74 A ATOM 2007 N ARG A 262 28.654 46.082 7.240 1. 00 32. 23 A ATOM 2008 CA ARGA262 29.518 46.866 6.345 1. 0034. 34 A ATOM 2009 CB ARG A 262 30.068 48.099 7.067 1. 00 34. 96 A ATOM 2010 CG ARG A 262 30.551 49.209 6.152 1. 00 37. 87 A ATOM 2011 CD ARG A 262 31.084 50.443 6.841 1. 00 43. 91 A ATOM 2012 NE ARG A 262 31.462 51.494 5.902 1. 00 45. 42 A ATOM 2013 CZ ARGA262 31.151 52.780 6.050 1. 0049. 53 A ATOM 2014 NH1 ARG A 262 30. 444 53. 192 7.101 1. 00 44. 71 A ATOM 2015 NH2 ARG A 262 31.577 53.667 5.157 1. 0055. 16 A ATOM 2016 C ARG A 262 30.661 46.016 5.792 1. 00 33. 30 A ATOM 2017 O ARG A 262 31.414 45.399 6.550 1. 00 37. 32 A ATOM 2018 N VAL A 263 30. 789 46.001 4.468 1. 00 31. 00 A ATOM 2019 CA VALA263 31. 818 45. 216 3. 792 1.00 31. 90 A ATOM 2020 CB VAL A 263 31.191 44.157 2.819 1. 00 33. 26 A ATOM 2021 CG1 VALA263 32.271 43.310 2.139 1. 00 32. 38 A ATOM 2022 CG2 VAL A 263 30. 216 43. 255 3. 555 1. 00 35. 28 A ATOM 2023 C VAL A 263 32.764 46.094 2.992 1. 00 31. 25 A ATOM 2024 O VAL A 263 32.338 46.769 2.056 1. 00 34. 55 A ATOM 2025 N LYS A 264 34.044 46.068 3.362 1. 00 32. 52 A ATOM 2026 CA LYS A 264 35.086 46.814 2.652 1. 00 32. 36 A ATOM 2027 CB LYS A 264 35.981 47.612 3.603 1. 00 34. 16 A ATOM 2028 CG LYS A 264 35.338 48.741 4.383 1. 00 36. 18 A ATOM 2029 CD LYSA264 36.262 49.517 5.323 1. 0033. 55 A ATOM 2030 CE LYS A 264 35.665 50.617 6.182 1. 00 35. 45 A ATOM 2031 NZ LYS A 264 35. 344 51.834 5.395 1. 00 42. 44 A ATOM 2032 C LYSA264 35.961 45.791 1.940 1. 0032. 16 A ATOM 2033 O LYS A 264 36.399 44.808 2.557 1. 00 27. 82 A ATOM 2034 N HIS A 265 36.169 46.008 0.640 1. 00 30. 87 A ATOM 2035 CA HIS A 265 37.010 45.144-0. 188 1. 00 32. 35 A ATOM 2036 CB HIS A 265 36.191 44.038-0. 867 1. 00 33. 96 A ATOM 2037 CG HIS A 265 37.032 43.007-1. 557 1. 0037. 88 A ATOM 2038 CD2 HIS A 265 37. 605 41. 869-1. 099 1. 00 39. 55 A ATOM 2039 ND1 HIS A 265 37.417 43.126-2. 874 1. 00 35. 97 A ATOM 2040 CE1 HIS A 265 38. 195 42. 109-3. 196 1. 0040. 43 A ATOM 2041 NE2 HIS A 265 38. 325 41. 330-2. 138 1. 00 42. 02 A ATOM 2042 C HIS A 265 37.714 46.004-1. 231 1. 00 33. 27 A ATOM 2043 O HIS A 265 37.154 46.993-1. 700 1. 00 33. 48 A ATOM 2044 N SER A 266 38.927 45.593-1. 602 1. 00 34. 64 A ATOM 2045 CA SERA266 39.774 46.292-2. 574 1. 00 37. 74 A ATOM 2046 CB SER A 266 41.129 45.594-2. 657 1. 00 37. 51 A ATOM 2047 OG SER A 266 40.969 44.192-2. 779 1. 00 44. 90 A ATOM 2048 C SER A 266 39.196 46.492-3. 983 1. 00 40. 26 A ATOM 2049 O SER A 266 39.651 47.370-4. 731 1. 00 40. 94 A ATOM 2050 N SER A 267 38.193 45.684-4. 329 1. 00 41. 59 A ATOM 2051 CA SER A 267 37.525 45.754-5. 634 1. 00 43. 98 A ATOM 2052 CB SER A 267 36.990 44.381-6. 028 1. 00 45.91 A ATOM 2053 OG SER A 267 36.049 43. 915-5.079 1. 00 49. 29 A ATOM 2054 C SER A 267 36.376 46.746-5. 642 1. 00 44. 01 A ATOM 2055 O SERA 267 35.847 47.087-6. 702 1. 00 44. 88 A ATOM 2056 N LEU A 268 35. 972 47. 162-4. 444 1. 00 44. 95 A ATOM 2057 CA LEU A 268 34.882 48.110-4. 254 1. 0045. 44 A ATOM 2058 CB LEU A 268 34.246 47.890-2. 880 1. 0038. 17 A ATOM 2059 CG LEU A 268 33.001 46.997-2. 759 1. 00 31. 97 A ATOM 2060 CD1 LEU A 268 32. 906 45. 951-3.836 1. 00 29. 01 A ATOM 2061 CD2 LEU A 268 32. 952 46. 377-1. 384 1. 00 21. 26 A ATOM 2062 C LEU A 268 35.284 49.570-4. 453 1. 0049. 67 A ATOM 2063 O LEU A 268 34.446 50.392-4. 829 1. 00 55. 61 A ATOM 2064 N GLU A 269 36.570 49.870-4. 234 1. 00 51. 59 A ATOM 2065 CA GLU A 269 37.159 51.213-4. 398 1. 00 52. 46 A ATOM 2066 CB GLU A 269 37.346 51.546-5. 890 1. 00 54. 50 A ATOM 2067 CG GLU A 269 38.351 50.675-6. 624 1. 00 62. 03 A ATOM 2068 CD GLU A 269 38.382 50.965-8. 118 1. 0067. 59 A ATOM 2069 OE1 GLUA269 37.621 50.316-8. 871 1. 0068. 87 A ATOM 2070 OE2 GLU A 269 39.163 51.846-8. 537 1. 00 69. 43 A ATOM 2071 C GLU A 269 36.422 52.355-3. 686 1. 00 50. 69 A ATOM 2072 O GLU A 269 35.866 53.256-4. 330 1. 00 51. 81 A ATOM 2073 N GLY A 270 36.366 52.259-2. 358 1. 00 48. 81 A ATOM 2074 CA GLYA270 35.712 53.268-1. 543 1. 0048. 67 A ATOM 2075 C GLY A 270 34.211 53.100-1. 417 1. 00 51. 01 A ATOM 2076 O GLYA270 33.632 53.479-0. 394 1. 0051. 40 A ATOM 2077 N GLN A 271 33.587 52.528-2. 453 1. 00 51. 41 A ATOM 2078 CA GLN A 271 32.137 52.296-2. 496 1. 00 49. 20 A ATOM 2079 CB GLN A 271 31.638 52.245-3. 955 1. 00 50. 83 A ATOM 2080 CG GLN A 271 32.080 53.408-4. 864 1. 00 61. 19 A ATOM 2081 CD GLN A 271 31.614 54.780-4. 378 1. 00 66. 33 A ATOM 2082 OE1 GLNA271 30.431 55.116-4. 470 1. 0066. 77 A ATOM 2083 NE2 GLN A 271 32.551 55.577-3. 860 1. 00 68. 10 A ATOM 2084 C GLN A 271 31.757 51.015-1. 742 1. 00 46. 36 A ATOM 2085 O GLN A 271 31. 465 49. 982-2. 347 1. 00 43. 32 A ATOM 2086 N ASP A 272 31.742 51.122-0. 412 1. 00 43. 62 A ATOM 2087 CA ASP A 272 31.423 50.023 0.503 1. 00 45. 65 A ATOM 2088 CB ASP A 272 31.637 50.463 1.954 1. 00 48. 57 A ATOM 2089 CG ASP A 272 33.075 50.831 2.265 1. 00 50. 79 A ATOM 2090 OD1 ASP A 272 33. 322 51. 176 3. 443 1. 00 48. 34 A ATOM 2091 OD2 ASP A 272 33.950 50.778 1.365 1. 00 51. 21 A ATOM 2092 C ASP A 272 30. 004 49. 483 0.397 1. 0045. 62 A ATOM 2093 O ASP A 272 29.084 50.208 0.015 1. 00 51. 81 A ATOM 2094 N ILE A 273 29.838 48.214 0.762 1. 00 41. 88 A ATOM 2095 CA ILE A 273 28.538 47.560 0.740 1. 0039. 05 A ATOM 2096 CB ILE A 273 28. 656 46. 080 0.262 1. 0033. 95 A ATOM 2097 CG2 ILE A 273 27. 332 45. 325 0. 439 1. 00 35. 02 A ATOM 2098 CG1 ILE A 273 29. 063 46. 043-1. 210 1. 00 36. 23 A ATOM 2099 CD1 ILE A 273 29.433 44.667-1. 733 1. 00 38. 45 A ATOM 2100 C ILEA273 27. 932 47. 641 2. 143 1. 00 40. 93 A ATOM 2101 O ILE A 273 28.441 47.030 3.083 1. 00 40. 94 A ATOM 2102 N ILE A 274 26.907 48.483 2.291 1. 0041. 06 A ATOM 2103 CA ILE A 274 26.213 48.620 3.568 1. 0039. 84 A ATOM 2104 CB ILE A 274 26.155 50.079 4.104 1. 00 40. 69 A ATOM 2105 CG2 ILE A 274 25.857 50.050 5.594 1. 00 45. 66 A ATOM 2106 CG1 ILE A 274 27. 510 50. 795 3. 985 1. 00 46. 65 A ATOM 2107 CD1 ILE A 274 27.691 51.628 2.722 1. 0054. 78 A ATOM 2108 C ILE A 274 24.800 48.066 3.374 1. 0040. 35 A ATOM 2109 O ILE A 274 24. 092 48. 468 2. 448 1. 00 45. 02 A ATOM 2110 N LEU A 275 24. 443 47. 085 4. 202 1. 00 38. 45 A ATOM 2111 CA LEU A 275 23. 145 46. 411 4. 160 1.00 36. 48 A ATOM 2112 CB LEU A 275 23. 345 44. 949 3.774 1. 0038. 10 A ATOM 2113 CG LEU A 275 22. 978 44. 441 2. 377 1. 00 42. 93 A ATOM 2114 CD1 LEU A 275 23. 547 45. 294 1. 247 1. 00 42. 98 A ATOM 2115 CD2 LEU A 275 23.471 43.011 2.274 1. 00 41. 70 A ATOM 2116 C LEU A 275 22. 483 46. 495 5. 526 1.00 37. 90 A ATOM 2117 O LEU A 275 23. 046 46. 034 6. 515 1.00 42. 73 A ATOM 2118 N TYRA276 21. 265 47. 033 5. 566 1.00 37. 01 A ATOM 2119 CA TYR A 276 20. 528 47. 242 6. 816 1. 00 36. 07 A ATOM 2120 CB TYR A 276 19. 879 48. 640 6. 806 1.00 37. 47 A ATOM 2121 CG TYR A 276 20.827 49.813 6.558 1. 00 36. 86 A ATOM 2122 CD1 TYR A 276 21. 399 50. 034 5. 280 1. 00 37. 88 A ATOM 2123 CE1 TYR A 276 22.278 51.120 5.038 1. 00 38. 70 A ATOM 2124 CD2 TYR A 276 21.155 50.711 7.597 1. 0034. 77 A ATOM 2125 CE2 TYR A 276 22.042 51.804 7.373 1. 00 37. 81 A ATOM 2126 CZ TYR A 276 22.597 51.995 6.089 1. 00 42. 47 A ATOM 2127 OH TYR A 276 23.479 53.029 5.860 1. 00 45. 60 A ATOM 2128 C TYR A 276 19.473 46.184 7.138 1. 00 37. 59 A ATOM 2129 O TYR A 276 18.943 45.535 6.239 1. 00 37. 18 A ATOM 2130 N TRP A 277 19.148 46.048 8.425 1. 00 39. 45 A ATOM 2131 CA TRPA277 18. 150 45. 089 8. 885 1.00 43.54 A ATOM 2132 CB TRPA277 18.412 44.730 10.347 1. 0043. 41 A ATOM 2133 CG TRPA277 17.714 43.483 10.822 1. 0048. 28 A ATOM 2134 CD2 TRP A 277 18.110 42.120 10.588 1. 00 50. 56 A ATOM 2135 CE2 TRP A 277 17.165 41.293 11.256 1. 0052. 90 A ATOM 2136 CE3 TRP A 277 19. 172 41. 510 9.881 1. 0053. 37 A ATOM 2137 CD1 TRP A 277 16. 586 43. 426 11.588 1. 0051. 70 A ATOM 2138 NE1TRPA277 16. 252 42. 121 11.853 1. 0055. 10 A ATOM 2139 CZ2 TRP A 277 17.246 39.873 11.243 1. 00 52. 79 A ATOM 2140 CZ3 TRP A 277 19.258 40.087 9.865 1. 00 54. 22 A ATOM 2141 CH2 TRP A 277 18.292 39.292 10.548 1. 00 51. 34 A ATOM 2142 C TRPA277 16. 724 45. 626 8.671 1. 0049. 68 A ATOM 2143 0 TRPA277 16.381 46.716 9.131 1. 0047. 67 A ATOM 2144 N ARG A 278 15.913 44.805 8.000 1. 00 58. 94 A ATOM 2145 CA ARG A 278 14. 520 45. 081 7. 598 1. 00 67. 78 A ATOM 2146 CB ARG A 278 14.017 43.974 6.639 1. 00 69. 40 A ATOM 2147 CG ARGA278 13.807 42.551 7.226 1. 0074. 33 A ATOM 2148 CD ARGA278 15.009 41.813 7.833 1. 0074. 95 A ATOM 2149 NE ARGA278 14.770 40.385 8.023 1. 0071. 69 A ATOM 2150 CZ ARGA278 15.387 39.425 7.337 1. 0070. 98 A ATOM 2151 NH1 ARG A 278 16. 287 39. 735 6. 408 1. 00 65. 93 A ATOM 2152 NH2 ARG A 278 15.110 38.149 7.586 1. 0066. 80 A ATOM 2153 C ARG A 278 13.407 45.434 8.597 1. 00 72. 06 A ATOM 2154 O ARG A 278 12.565 46.284 8.288 1. 00 73. 74 A ATOM 2155 N ASN A 279 13.406 44.792 9.771 1. 00 78. 01 A ATOM 2156 CA ASN A 279 12. 405 44.968 10.855 1.00 81. 98 A ATOM 2157 CB ASN A 279 12.864 46.002 11.916 1. 00 85. 12 A ATOM 2158 CG ASNA279 13.085 47.406 11.347 1. 0088. 76 A ATOM 2159 OD1 ASN A 279 12.132 48.162 11.122 1. 00 85. 61 A ATOM 2160 ND2 ASN A 279 14.348 47.752 11.109 1. 00 89. 83 A ATOM 2161 C ASN A 279 10.906 45.145 10.500 1. 00 82. 59 A ATOM 2162 O ASN A 279 10.498 46.246 10. 059 1. 00 82. 18 A ATOM 2163 OXT ASN A 279 10. 154 44. 156 10. 659 1. 0082. 60 A ATOM 2164 CB MET B 0 50.461 8.808 15.966 1. 00 72. 08 B ATOM 2165 CG MET B 0 49.619 8.606 14.695 1. 00 75. 07 B ATOM 2166 SD MET B 0 47.903 8.083 15.000 1. 00 78. 58 B ATOM 2167 CE MET B 0 48.099 6.290 15.077 1. 00 77. 43 B ATOM 2168 C MET B 0 49.191 10.659 17.181 1. 00 64. 97 B ATOM 2169 O MET B 0 48.575 9.884 17.928 1. 00 63. 32 B ATOM 2170 N MET B 0 51.635 10.378 17.503 1. 00 68. 88 B ATOM 2171 CA MET B 0 50.516 10.247 16.521 1. 00 68. 85 B ATOM 2172 N ILE B 1 48.792 11.905 16.912 1. 00 58. 77 B ATOM 2173 CA ILE B 1 47.562 12.492 17.441 1. 00 51. 80 B ATOM 2174 CB ILE B 1 47.710 14.028 17.684 1. 00 53. 80 B ATOM 2175 CG2 ILE B 1 48.844 14.291 18.648 1. 00 57. 30 B ATOM 2176 CG1 ILE B 1 47.941 14. 792 16. 372 1. 00 51. 83 B ATOM 2177 CD1 ILEB 1 47.831 16. 304 16.504 1.00 59. 34 B ATOM 2178 C ILE B 1 46.361 12.252 16.530 1. 00 48. 83 B ATOM 2179 O ILE B 1 46.518 11.848 15.370 1. 00 50. 28 B ATOM 2180 N GLN B 2 45.169 12.505 17.071 1. 00 44. 89 B ATOM 2181 CA GLNB 2 43.897 12.352 16.354 1. 0041. 39 B ATOM 2182 CB GLN B 2 43.156 11.092 16.821 1. 00 38. 74 B ATOM 2183 CG GLN B 2 43.777 9.761 16.402 1. 00 44. 87 B ATOM 2184 CD GLN B 2 43.087 8.549 17.019 1. 00 50. 26 B ATOM 2185 OE1 GLN B 2 42.317 8. 668 17. 981 1. 0047. 38 B ATOM 2186 NE2 GLN B 2 43.371 7. 36716. 4661. 0046. 17 B ATOM 2187 C GLN B 2 43.017 13.577 16.606 1. 00 38. 06 B ATOM 2188 O GLN B 2 42.645 13.838 17.749 1. 00 39. 02 B ATOM 2189 N ARG B 3 42.736 14.350 15.555 1. 00 34. 90 B ATOM 2190 CA ARG B 3 41.886 15.550 15.651 1. 00 36. 32 B ATOM 2191 CB ARG B 3 42.619 16.790 15.117 1. 00 40. 90 B ATOM 2192 CG ARG B 3 43.905 17.199 15.827 1. 00 53. 02 B ATOM 2193 CD ARG B 3 44.827 18.157 15.056 1. 00 59. 17 B ATOM 2194 NE ARG B 3 44.915 19.503 15.629 1. 00 68. 17 B ATOM 2195 CZ ARG B 3 44.150 20.541 15.283 1. 00 70. 31 B ATOM 2196 NH1 ARG B 3 43.206 20.418 14.358 1. 00 69. 04 B ATOM 2197 NH2 ARG B 3 44.352 21.725 15. 847 1. 00 74. 08 B ATOM 2198 C ARG B 3 40.629 15.352 14.805 1. 00 33. 81 B ATOM 2199 O ARG B 3 40.729 14.879 13.680 1. 00 37. 18 B ATOM 2200 N THR B 4 39.462 15.721 15.334 1. 00 33. 35 B ATOM 2201 CA THRB 4 38.179 15.604 14.615 1. 0034. 68 B ATOM 2202 CB THR B 4 36.957 15.633 15.611 1. 00 38. 39 B ATOM 2203 OG1 THR B 4 36.907 14.392 16.310 1. 00 48. 93 B ATOM 2204 CG2 THR B 4 35.586 15.826 14.901 1. 00 35. 70 B ATOM 2205 C THR B 4 38.006 16.728 13.592 1. 00 34. 78 B ATOM 2206 O THR B 4 38.385 17.878 13.859 1. 00 35. 32 B ATOM 2207 N PRO B 5 37.466 16.403 12.396 1. 00 33. 78 B ATOM 2208 CD PRO B 5 37.307 15.071 11.779 1. 00 33. 19 B ATOM 2209 CA PRO B 5 37.260 17.439 11.382 1. 00 35. 70 B ATOM 2210 CB PRO B 5 36.934 16.626 10.122 1. 00 34. 88 B ATOM 2211 CG PRO B 5 36.364 15.362 10.655 1. 00 33. 48 B ATOM 2212 C PRO B 5 36.131 18.416 11.712 1. 00 35. 45 B ATOM 2213 O PRO B 5 35.123 18.035 12.305 1. 00 36. 90 B ATOM 2214 N LYS B 6 36.361 19.686 11.384 1. 00 35. 90 B ATOM 2215 CA LYS B 6 35.385 20.755 11.568 1. 00 34. 66 B ATOM 2216 CB LYS B 6 36.105 22.094 11.741 1. 00 29. 82 B ATOM 2217 CG LYS B 6 35.201 23.253 12.110 1. 00 32. 98 B ATOM 2218 CD LYS B 6 35.865 24.596 12.318 1. 00 39. 98 B ATOM 2219 CE LYS B 6 34.973 25.767 12.677 1. 00 44. 26 B ATOM 2220 NZ LYS B 6 35.773 27.018 12.821 1. 00 52. 30 B ATOM 2221 C LYS B 6 34.640 20.713 10.238 1. 00 37. 33 B ATOM 2222 O LYS B 6 35.273 20.654 9.179 1. 00 41. 00 B ATOM 2223 N ILE B 7 33. 311 20.666 10.291 1. 00 35. 58 B ATOM 2224 CA ILE B 7 32.501 20.576 9.074 1. 00 35. 53 B ATOM 2225 CB ILE B 7 31.628 19.281 9.101 1. 00 33. 05 B ATOM 2226 CG2 ILE B 7 30.870 19.099 7.784 1. 00 32. 20 B ATOM 2227 CG1 ILE B 7 32.516 18.051 9.326 1. 00 36. 04 B ATOM 2228 CD1 ILE B 7 31.835 16.924 10.054 1. 0043. 57 B ATOM 2229 C ILE B 7 31.607 21.793 8.818 1. 00 36. 85 B ATOM 2230 O ILE B 7 30.665 22.048 9.570 1. 00 40. 18 B ATOM 2231 N GLN B 8 31.886 22.521 7.739 1. 00 36. 06 B ATOM 2232 CA GLN B 8 31.071 23.682 7.371 1. 00 36. 85 B ATOM 2233 CB GLN B 8 31.907 24. 967 7.301 1. 00 37. 17 B ATOM 2234 CG GLN B 8 32.150 25.649 8.637 1. 00 37. 93 B ATOM 2235 CD GLN B 8 33.625 25.790 8.944 1. 0040. 65 B ATOM 2236 OE1 GLN B 8 34.109 26.892 9.212 1. 00 35. 89 B ATOM 2237 NE2 GLN B 8 34. 355 24. 670 8.901 1. 0043. 55 B ATOM 2238 C GLN B 8 30.362 23.466 6.038 1. 00 35. 24 B ATOM 2239 O GLN B 8 31.012 23.205 5.026 1. 00 39. 48 B ATOM 2240 N VAL B 9 29.030 23.520 6.051 1. 00 31. 72 B ATOM 2241 CA VALB 9 28.251 23.365 4.825 1. 0027. 63 B ATOM 2242 CB VAL B 9 27.118 22.323 4.941 1. 00 24. 00 B ATOM 2243 CG1 VAL B 9 26.559 22.004 3.550 1. 00 19. 53 B ATOM 2244 CG2 VAL B 9 27.628 21. 058 5.573 1. 00 21. 81 B ATOM 2245 C VAL B 9 27.681 24.729 4.458 1. 00 29. 23 B ATOM 2246 O VAL B 9 27.085 25.420 5.294 1. 00 32. 08 B ATOM 2247 N TYR B 10 27.886 25.109 3.200 1. 00 26. 34 B ATOM 2248 CA TYR B 10 27.453 26.403 2.695 1. 0029. 29 B ATOM 2249 CB TYR B 10 28.475 27.485 3.112 1. 00 22. 81 B ATOM 2250 CG TYR B 10 29. 923 27. 211 2. 703 1. 00 25. 25 B ATOM 2251 CD1 TYR B 10 30.710 26.267 3.399 1. 00 28. 00 B ATOM 2252 CE1 TYR B 10 32.042 25.981 3.017 1. 00 23. 59 B ATOM 2253 CD2 TYR B 10 30.509 27.878 1.604 1. 00 29. 82 B ATOM 2254 CE2 TYR B 10 31.853 27.602 1.211 1. 00 31. 18 B ATOM 2255 CZ TYR B 10 32.602 26.649 1.930 1. 0026. 91 B ATOM 2256 OH TYR B 10 33.893 26.371 1.571 1. 00 28. 91 B ATOM 2257 C TYR B 10 27.292 26.425 1.176 1. 00 34. 58 B ATOM 2258 O TYR B 10 27.959 25.671 0.461 1. 00 39. 07 B ATOM 2259 N SER B 11 26.421 27.308 0.689 1. 00 35. 09 B ATOM 2260 CA SERB 11 26.214 27.471-0. 744 1. 0035. 68 B ATOM 2261 CB SER B 11 24.733 27.695-1. 077 1. 00 39. 23 B ATOM 2262 OG SER B 11 24.172 28.766-0. 336 1. 00 40. 55 B ATOM 2263 C SERB 11 27.054 28.664-1. 182 1. 00 36. 55 B ATOM 2264 O SER B 11 27.262 29.593-0. 396 1. 00 38. 35 B ATOM 2265 N ARG B 12 27.543 28.630-2. 420 1. 00 35. 87 B ATOM 2266 CA ARG B 12 28.376 29.704-2. 968 1. 00 38. 53 B ATOM 2267 CB ARG B 12 28.956 29.265-4. 325 1. 00 38. 35 B ATOM 2268 CG ARG B 12 29.835 30.285-5. 049 1. 00 35. 25 B ATOM 2269 CD ARG B 12 30.263 29.961-6. 467 1. 00 37. 06 B ATOM 2270 NE ARG B 12 31.071 28.746-6. 544 1. 00 37. 54 B ATOM 2271 CZ ARG B 12 31.566 28.242-7. 672 1. 00 37. 32 B ATOM 2272 NH1 ARG B 12 31.341 28.838-8. 840 1. 00 36. 15 B ATOM 2273 NH2 ARG B 12 32.296 27.135-7. 633 1. 00 41. 65 B ATOM 2274 C ARG B 12 27.577 31.003-3. 113 1. 00 39. 97 B ATOM 2275 O ARG B 12 28.078 32.087-2. 807 1. 00 40. 06 B ATOM 2276 N HIS B 13 26.326 30.860-3. 550 1. 00 44. 56 B ATOM 2277 CA HIS B 13 25.401 31.976-3. 780 1. 00 46. 85 B ATOM 2278 CB HIS B 13 24.977 31.985-5. 258 1. 00 45. 38 B ATOM 2279 CG HIS B 13 26.119 32.124-6. 209 1. 0046. 10 B ATOM 2280 CD2 HIS B 13 26. 618 31. 272-7. 132 1. 00 50. 20 B ATOM 2281 ND1 HIS B 13 26.930 33.236-6. 234 1. 0045. 90 B ATOM 2282 CE1 HIS B 13 27.883 33.062-7. 131 1. 00 51. 44 B ATOM 2283 NE2 HIS B 13 27. 717 31. 877-7. 690 1. 00 54. 18 B ATOM 2284 C HIS B 13 24.164 31.806-2. 891 1. 00 48. 78 B ATOM 2285 O HIS B 13 23.905 30.696-2. 415 1. 00 49. 06 B ATOM 2286 N PRO B 14 23. 407 32. 903-2. 615 1. 00 51. 73 B ATOM 2287 CD PRO B 14 23.684 34.327-2. 898 1. 00 52. 04 B ATOM 2288 CA PRO B 14 22.204 32.782-1. 772 1. 00 51. 62 B ATOM 2289 CB PRO B 14 21.727 34.229-1. 629 1. 00 52. 24 B ATOM 2290 CG PRO B 14 22.328 34.938-2. 816 1. 00 56. 49 B ATOM 2291 C PRO B 14 21.120 31.907-2. 384 1. 00 52. 01 B ATOM 2292 O PRO B 14 20.871 31.957-3. 596 1. 00 54. 68 B ATOM 2293 N ALA B 15 20.494 31.106-1. 529 1. 00 52. 66 B ATOM 2294 CA ALA B 15 19.442 30.185-1. 928 1. 0054. 66 B ATOM 2295 CB ALA B 15 19.111 29.253-0. 768 1. 00 55. 67 B ATOM 2296 C ALA B 15 18.168 30.845-2. 473 1. 00 57. 46 B ATOM 2297 O ALA B 15 17.452 31.553-1. 750 1. 00 56. 52 B ATOM 2298 N GLU B 16 17.966 30.666-3. 781 1. 00 59. 99 B ATOM 2299 CA GLU B 16 16.796 31.158-4. 507 1. 00 62. 49 B ATOM 2300 CB GLU B 16 17.189 32. 214-5.552 1. 00 63. 82 B ATOM 2301 CG GLU B 16 15.995 32.929-6. 204 1. 00 68. 85 B ATOM 2302 CD GLU B 16 16.385 33.773-7. 407 1. 00 71. 52 B ATOM 2303 OE1 GLU B 16 16.609 34.990-7. 241 1. 00 71. 43 B ATOM 2304 OE2 GLU B 16 16.458 33.219-8. 526 1. 00 76. 08 B ATOM 2305 C GLU B 16 16.255 29.903-5. 192 1. 00 63. 52 B ATOM 2306 O GLU B 16 16.888 29.375-6. 114 1. 00 65. 28 B ATOM 2307 N ASN B 17 15.104 29.424-4. 711 1. 00 64. 49 B ATOM 2308 CA ASN B 17 14.434 28.215-5. 212 1. 00 65. 95 B ATOM 2309 CB ASN B 17 13.074 28.044-4. 531 1. 00 66. 72 B ATOM 2310 CG ASN B 17 13. 176 28.033-3. 016 1. 00 70. 92 B ATOM 2311 OD1 ASN B 17 13.077 26.983-2. 379 1. 00 70. 39 B ATOM 2312 ND2 ASN B 17 13.378 29. 210-2.430 1. 00 71. 88 B ATOM 2313 C ASN B 17 14.267 28.139-6. 734 1. 00 68. 32 B ATOM 2314 O ASN B 17 13.711 29.054-7. 356 1. 00 68. 83 B ATOM 2315 N GLY B 18 14.827 27.077-7. 319 1. 00 68. 56 B ATOM 2316 CA GLY B 18 14.754 26.867-8. 757 1. 00 69. 41 B ATOM 2317 C GLY B 18 15.997 27.277-9. 530 1. 00 70. 05 B ATOM 2318 O GLY B 18 16.232 26.765-10. 628 1. 00 71. 16 B ATOM 2319 N LYS B 19 16.793 28.186-8. 963 1. 00 69. 27 B ATOM 2320 CA LYS B 19 18.021 28.668-9. 602 1. 00 69. 17 B ATOM 2321 CB LYS B 19 18.301 30.122-9. 193 1. 00 69. 06 B ATOM 2322 CG LYS B 19 19.407 30.802-10. 006 1. 00 74. 59 B ATOM 2323 CD LYS B 19 19.941 32.141-9. 531 1. 00 78. 49 B ATOM 2324 CE LYS B 19 21.151 32.691-10. 280 1. 00 79. 37 B ATOM 2325 NZ LYS B 19 21.651 33.975-9. 709 1. 00 79. 83 B ATOM 2326 C LYS B 19 19.236 27.785-9. 277 1. 00 68. 19 B ATOM 2327 O LYS B 19 19.347 27.262-8. 169 1. 00 66. 86 B ATOM 2328 N SER B 20 20.145 27.654-10. 249 1. 00 68. 73 B ATOM 2329 CA SER B 20 21.378 26.862-10. 122 1. 00 65. 77 B ATOM 2330 CB SER B 20 22.054 26.693-11. 492 1. 00 67. 03 B ATOM 2331 OG SER B 20 23.086 25.719-11. 446 1. 00 66. 71 B ATOM 2332 C SER B 20 22.335 27.533-9. 136 1. 00 63. 05 B ATOM 2333 O SER B 20 22.391 28.764-9. 055 1. 00 64. 92 B ATOM 2334 N ASN B 21 23.089 26.709-8. 413 1. 00 59. 23 B ATOM 2335 CA ASN B 21 24.023 27.162-7. 379 1. 00 55. 18 B ATOM 2336 CB ASN B 21 23.208 27.353-6. 085 1. 00 53. 71 B ATOM 2337 CG ASN B 21 23.784 28.392-5. 149 1. 00 53. 12 B ATOM 2338 OD1 ASN B 21 24.997 28.569-5. 042 1. 00 56. 97 B ATOM 2339 ND2 ASN B 21 22.901 29.078-4. 443 1. 00 53. 79 B ATOM 2340 C ASN B 21 25.095 26.072-7. 169 1. 00 53. 17 B ATOM 2341 O ASN B 21 25.067 25.037-7. 835 1. 0052. 34 B ATOM 2342 N PHE B 22 26.025 26.311-6. 240 1. 00 49. 96 B ATOM 2343 CA PHE B 22 27.098 25.365-5. 894 1. 00 46. 85 B ATOM 2344 CB PHE B 22 28.477 25.938-6. 255 1. 00 48. 09 B ATOM 2345 CG PHE B 22 28.840 25.809-7. 704 1. 00 48. 92 B ATOM 2346 CD1 PHE B 22 29.726 24.792-8. 123 1. 00 51. 26 B ATOM 2347 CD2 PHE B 22 28.332 26.715-8. 659 1. 00 46. 56 B ATOM 2348 CE1 PHE B 22 30.115 24.671-9. 490 1. 00 48. 83 B ATOM 2349 CE2 PHE B 22 28.703 26.614-10. 028 1. 00 49. 75 B ATOM 2350 CZ PHE B 22 29.601 25.585-10. 446 1. 00 49. 54 B ATOM 2351 C PHE B 22 27.065 25.070-4. 392 1. 00 42. 99 B ATOM 2352 O PHE B 22 27.097 26.001-3. 593 1. 00 41. 26 B ATOM 2353 N LEU B 23 26.961 23.790-4. 017 1. 00 41. 76 B ATOM 2354 CA LEU B 23 26.933 23.370-2. 600 1. 0041. 04 B ATOM 2355 CB LEU B 23 25.997 22.173-2. 383 1. 00 43. 77 B ATOM 2356 CG LEU B 23 25.841 21.603-0. 965 1. 0045. 20 B ATOM 2357 CD1 LEU B 23 25. 097 22. 586-0. 074 1. 00 46. 74 B ATOM 2358 CD2 LEU B 23 25. 108 20. 276-1. 026 1. 00 43. 33 B ATOM 2359 C LEU B 23 28.326 22.972-2. 176 1. 00 40. 16 B ATOM 2360 O LEU B 23 28. 973 22. 185-2. 856 1. 00 41. 82 B ATOM 2361 N ASN B 24 28.760 23.480-1. 028 1. 00 38. 02 B ATOM 2362 CA ASN B 24 30.097 23.197-0. 535 1. 00 37. 24 B ATOM 2363 CB ASN B 24 30.944 24.470-0. 522 1. 00 37. 41 B ATOM 2364 CG ASN B 24 31.157 25.056-1. 894 1. 00 40. 13 B ATOM 2365 OD1 ASN B 24 32.128 24.736-2. 577 1. 00 47. 35 B ATOM 2366 ND2 ASN B 24 30.251 25.931-2. 306 1. 00 45. 19 B ATOM 2367 C ASN B 24 30.140 22.613 0.857 1. 00 37. 41 B ATOM 2368 O ASN B 24 29.317 22.943 1.712 1. 00 36. 01 B ATOM 2369 N CYS B 25 31.123 21.742 1.066 1. 00 37. 06 B ATOM 2370 CA CYS B 25 31.371 21.135 2.365 1. 00 35. 95 B ATOM 2371 C CYS B 25 32.875 21.208 2.587 1. 00 36. 60 B ATOM 2372 O CYS B 25 33.655 20.590 1.852 1. 00 37. 14 B ATOM 2373 CB CYS B 25 30.900 19.699 2.426 1. 00 35. 16 B ATOM 2374 SG CYS B 25 31.080 19.006 4.090 1. 00 37. 89 B ATOM 2375 N TYR B 26 33.269 22.015 3.568 1. 00 34. 57 B ATOM 2376 CA TYR B 26 34.669 22.219 3.896 1. 0033. 81 B ATOM 2377 CB TYR B 26 34.963 23.719 3.970 1. 0030. 30 B ATOM 2378 CG TYR B 26 36.411 24.104 4.178 1. 00 35. 29 B ATOM 2379 CD1 TYR B 26 37.381 23.867 3.179 1. 00 38. 22 B ATOM 2380 CE1 TYR B 26 38.735 24.290 3.351 1. 00 37. 08 B ATOM 2381 CD2 TYR B 26 36.817 24.764 5.359 1. 00 35. 96 B ATOM 2382 CE2 TYR B 26 38.163 25.195 5.542 1. 00 33. 83 B ATOM 2383 CZ TYR B 26 39.109 24.954 4.535 1. 0035. 97 B ATOM 2384 OH TYR B 26 40.404 25.382 4.707 1. 00 34. 85 B ATOM 2385 C TYR B 26 35.033 21.523 5.198 1. 00 34. 27 B ATOM 2386 O TYR B 26 34.568 21.907 6.277 1. 00 37. 90 B ATOM 2387 N VAL B 27 35.853 20.483 5.072 1. 00 31. 15 B ATOM 2388 CA VAL B 27 36.321 19.717 6.214 1. 0027. 96 B ATOM 2389 CB VAL B 27 36.215 18.188 5.971 1. 00 26. 79 B ATOM 2390 CG1 VAL B 27 34.772 17.780 5.976 1. 00 30. 48 B ATOM 2391 CG2 VAL B 27 36.829 17.791 4.641 1. 00 31. 36 B ATOM 2392 C VAL B 27 37.741 20.153 6.556 1. 00 26. 22 B ATOM 2393 O VAL B 27 38.639 20.091 5.715 1. 00 25. 30 B ATOM 2394 N SER B 28 37.924 20.621 7.786 1. 00 25. 41 B ATOM 2395 CA SER B 28 39.224 21.112 8.243 1. 00 27. 14 B ATOM 2396 CB SER B 28 39.282 22.648 8.143 1. 00 27. 65 B ATOM 2397 OG SER B 28 38.125 23.259 8.709 1. 00 31. 43 B ATOM 2398 C SER B 28 39.589 20.704 9.652 1. 00 27. 93 B ATOM 2399 O SER B 28 38.766 20.159 10.391 1. 00 22. 63 B ATOM 2400 N GLY B 29 40.844 20.974 10.001 1. 00 29. 95 B ATOM 2401 CA GLY B 29 41.358 20.677 11.326 1. 00 33. 37 B ATOM 2402 C GLY B 29 41.491 19.219 11.720 1. 00 35. 23 B ATOM 2403 O GLY B 29 41.449 18.914 12.912 1. 00 40. 29 B ATOM 2404 N PHE B 30 41.643 18.319 10.750 1. 00 32. 87 B ATOM 2405 CA PHE B 30 41.771 16.908 11.081 1. 00 29. 78 B ATOM 2406 CB PHE B 30 40.762 16.025 10.335 1. 00 25. 32 B ATOM 2407 CG PHE B 30 40.826 16.107 8.831 1. 00 27. 00 B ATOM 2408 CD1 PHE B 30 40.188 17.155 8.139 1. 00 30. 39 B ATOM 2409 CD2 PHE B 30 41.457 15.089 8.086 1. 00 25. 38 B ATOM 2410 CE1 PHE B 30 40.169 17.190 6.718 1. 00 24. 62 B ATOM 2411 CE2 PHE B 30 41.449 15.107 6.672 1. 00 13. 54 B ATOM 2412 CZ PHE B 30 40.802 16.161 5.986 1. 00 23. 67 B ATOM 2413 C PHE B 30 43.150 16.350 10.935 1. 00 31. 26 B ATOM 2414 O PHE B 30 43.985 16.912 10.238 1. 00 33. 82 B ATOM 2415 N HIS B 31 43.361 15.233 11.620 1. 00 34. 77 B ATOM 2416 CA HIS B 31 44.612 14.489 11.617 1. 00 36. 70 B ATOM 2417 CB HIS B 31 45.662 15.158 12.514 1. 00 36. 17 B ATOM 2418 CG HIS B 31 47.053 14.987 12.007 1. 00 45. 92 B ATOM 2419 CD2 HIS B 31 47.867 15.836 11.339 1. 00 47. 61 B ATOM 2420 ND1 HIS B 31 47.719 13.780 12.060 1. 00 55. 96 B ATOM 2421 CE1 HIS B 31 48.878 13.890 11.436 1. 00 52. 18 B ATOM 2422 NE2 HIS B 31 48.992 15.128 10.988 1. 00 49. 25 B ATOM 2423 C HIS B 31 44.271 13.070 12.114 1. 00 37. 16 B ATOM 2424 O HIS B 31 43.574 12.933 13.124 1. 00 36. 47 B ATOM 2425 N PRO B 32 44.653 12.003 11.361 1. 00 37. 20 B ATOM 2426 CD PRO B 32 44.509 10.669 11.961 1. 00 35. 64 B ATOM 2427 CA PRO B 32 45.370 11.869 10.084 1. 00 35. 18 B ATOM 2428 CB PRO B 32 45.715 10.381 10.045 1. 00 36. 59 B ATOM 2429 CG PRO B 32 45.741 9.991 11.471 1. 00 38. 22 B ATOM 2430 C PRO B 32 44.535 12.249 8.871 1. 00 35. 30 B ATOM 2431 O PRO B 32 43.350 12. 567 9.006 1. 00 35. 78 B ATOM 2432 N SER B 33 45.159 12.191 7.697 1. 00 34. 25 B ATOM 2433 CA SER B 33 44.519 12.552 6.441 1. 00 34. 55 B ATOM 2434 CB SER B 33 45.562 12.667 5.339 1. 00 31. 04 B ATOM 2435 OG SER B 33 46.218 11.434 5.124 1. 00 41. 76 B ATOM 2436 C SER B 33 43.367 11.676 5.979 1. 00 37. 63 B ATOM 2437 O SER B 33 42.342 12.213 5.569 1. 00 37. 20 B ATOM 2438 N ASP B 34 43.521 10.349 6.091 1. 00 41. 78 B ATOM 2439 CA ASP B 34 42.510 9.348 5.667 1. 00 47. 23 B ATOM 2440 CB ASP B 34 42.837 7.957 6.241 1. 00 53. 47 B ATOM 2441 CG ASP B 34 44.279 7.534 5.985 1. 00 62. 66 B ATOM 2442 OD1 ASP B 34 44.499 6.653 5. 128 1. 00 67. 32 B ATOM 2443 OD2 ASP B 34 45.193 8.079 6.648 1. 00 66. 68 B ATOM 2444 C ASP B 34 41.085 9.746 6.061 1. 0046. 20 B ATOM 2445 O ASP B 34 40.743 9.791 7.246 1. 00 49. 34 B ATOM 2446 N ILE B 35 40.301 10.134 5.060 1. 0045. 34 B ATOM 2447 CA ILE B 35 38.932 10.582 5.278 1. 00 46. 86 B ATOM 2448 CB ILE B 35 38.918 12.115 5.610 1. 0048. 43 B ATOM 2449 CG2 ILE B 35 39.379 12.929 4.400 1. 00 50. 45 B ATOM 2450 CG1 ILE B 35 37. 557 12. 568 6. 158 1. 00 48. 27 B ATOM 2451 CD1 ILE B 35 37.565 13.955 6.788 1. 0046. 32 B ATOM 2452 C ILE B 35 38.015 10.267 4.090 1. 00 47. 42 B ATOM 2453 O ILE B 35 38.446 10.240 2.928 1. 00 50. 90 B ATOM 2454 N GLU B 36 36.749 10.038 4.411 1. 00 43. 89 B ATOM 2455 CA GLU B 36 35.726 9.735 3.435 1. 00 43. 07 B ATOM 2456 CB GLU B 36 35.248 8.279 3.645 1. 0045. 95 B ATOM 2457 CG GLU B 36 33.851 7.885 3.125 1. 00 53. 64 B ATOM 2458 CD GLU B 36 33.677 8.079 1.631 1. 00 62. 80 B ATOM 2459 OE1 GLU B 36 34.421 7.442 0.851 1. 00 72. 82 B ATOM 2460 OE2 GLU B 36 32.798 8.882 1.247 1. 00 58. 81 B ATOM 2461 C GLU B 36 34.619 10.765 3.650 1. 00 42. 31 B ATOM 2462 O GLU B 36 34.060 10.868 4.741 1. 00 43. 22 B ATOM 2463 N VAL B 37 34.367 11.579 2.627 1. 00 39. 35 B ATOM 2464 CA VAL B 37 33.319 12.596 2.691 1. 00 38. 93 B ATOM 2465 CB VAL B 37 33.897 14.053 2.679 1. 00 39. 17 B ATOM 2466 CG1 VAL B 37 32.783 15.108 2.643 1. 00 33. 29 B ATOM 2467 CG2 VAL B 37 34.777 14.302 3.896 1. 00 39. 65 B ATOM 2468 C VAL B 37 32.356 12.408 1.522 1. 00 40. 93 B ATOM 2469 O VAL B 37 32.771 12.094 0.400 1. 00 43. 64 B ATOM 2470 N ASP B 38 31.068 12.576 1.819 1. 00 40. 80 B ATOM 2471 CA ASP B 38 29.995 12.465 0.840 1. 0040. 50 B ATOM 2472 CB ASP B 38 29.211 11.164 1.031 1. 0045. 22 B ATOM 2473 CG ASP B 38 29.912 9.968 0.447 1. 00 50. 50 B ATOM 2474 OD1 ASP B 38 30.345 10.048-0. 723 1. 00 55. 61 B ATOM 2475 OD2 ASP B 38 30. 028 8.949 1.160 1. 00 53. 26 B ATOM 2476 C ASP B 38 29.027 13.622 0.998 1. 00 40. 83 B ATOM 2477 O ASP B 38 28.878 14.181 2.085 1. 00 36. 47 B ATOM 2478 N LEU B 39 28.411 14.001-0. 115 1. 0042. 61 B ATOM 2479 CA LEU B 39 27. 405 15.052-0. 136 1. 00 47. 52 B ATOM 2480 CB LEU B 39 27.692 16.079-1. 238 1. 0047. 50 B ATOM 2481 CG LEU B 39 28.872 17.031-0. 992 1. 00 51. 72 B ATOM 2482 CD1 LEU B 39 28.972 18.057-2. 099 1. 00 52. 77 B ATOM 2483 CD2 LEU B 39 28.702 17.737 0.334 1. 00 49. 59 B ATOM 2484 C LEU B 39 26.089 14.322-0. 375 1. 00 52. 08 B ATOM 2485 O LEU B 39 25.968 13.535-1. 318 1. 00 53. 19 B ATOM 2486 N LEU B 40 25.139 14.524 0.535 1. 00 54. 23 B ATOM 2487 CA LEU B 40 23.848 13.851 0.462 1. 00 56. 30 B ATOM 2488 CB LEU B 40 23.467 13.287 1.834 1. 00 56. 03 B ATOM 2489 CG LEU B 40 24.497 12.510 2.658 1. 00 57. 10 B ATOM 2490 CD1 LEU B 40 23.839 11.958 3.910 1. 00 57. 03 B ATOM 2491 CD2 LEU B 40 25.103 11.389 1.838 1. 00 53. 52 B ATOM 2492 C LEU B 40 22.701 14.697-0. 047 1. 00 59. 26 B ATOM 2493 O LEU B 40 22.702 15.917 0.103 1. 00 61. 45 B ATOM 2494 N LYS B 41 21.738 14.020-0. 672 1. 00 61. 42 B ATOM 2495 CA LYS B 41 20.522 14.631-1. 195 1. 00 59. 70 B ATOM 2496 CB LYS B 41 20.487 14.610-2. 727 1. 00 57. 93 B ATOM 2497 CG LYS B 41 19.264 15. 289-3. 348 1. 00 61. 71 B ATOM 2498 CD LYS B 41 19.149 15. 246-4.871 1. 00 67. 77 B ATOM 2499 CE LYS B 41 17.868 15.776-5. 508 1. 00 65. 67 B ATOM 2500 NZ LYS B 41 17.644 17.213-5. 209 1. 00 68. 94 B ATOM 2501 C LYS B 41 19.421 13. 755-0.627 1. 00 60. 34 B ATOM 2502 O LYS B 41 19.236 12.607-1. 056 1. 00 59. 40 B ATOM 2503 N ASN B 42 18.764 14.289 0.405 1. 00 61. 13 B ATOM 2504 CA ASN B 42 17. 656 13. 651 1.131 1. 0061. 27 B ATOM 2505 CB ASN B 42 16.399 13.552 0.240 1. 00 57. 66 B ATOM 2506 CG ASN B 42 15.987 14.904-0. 350 1. 00 59. 14 B ATOM 2507 OD1 ASN B 42 15.671 15.842 0.382 1. 00 57. 44 B ATOM 2508 ND2 ASN B 42 16.014 15.008-1. 678 1. 00 49. 56 B ATOM 2509 C ASN B 42 18.032 12.298 1.746 1. 00 61. 22 B ATOM 2510 O ASN B 42 17.186 11.409 1.888 1. 00 65. 37 B ATOM 2511 N GLY B 43 19.311 12.163 2.101 1. 00 58. 75 B ATOM 2512 CA GLY B 43 19.817 10.937 2.699 1. 00 57. 89 B ATOM 2513 C GLY B 43 20.647 10.050 1.784 1. 00 58. 41 B ATOM 2514 O GLY B 43 21.333 9.144 2.266 1. 0055. 93 B ATOM 2515 N GLU B 44 20.583 10.294 0.473 1. 00 60. 31 B ATOM 2516 CA GLU B 44 21.338 9.506-0. 508 1. 00 63. 27 B ATOM 2517 CB GLU B 44 20.394 8.879-1. 536 1.00 67. 99 B ATOM 2518 CG GLU B 44 19.792 7.558-1. 058 1. 00 77. 25 B ATOM 2519 CD GLU B 44 18.479 7.213-1. 732 1. 00 83. 61 B ATOM 2520 OE1 GLU B 44 17.521 6.864-1. 002 1. 00 84. 56 B ATOM 2521 OE2 GLU B 44 18.403 7.280-2. 982 1. 00 87. 15 B ATOM 2522 C GLU B 44 22.448 10.297-1. 192 1. 00 62. 89 B ATOM 2523 O GLU B 44 22.242 11.446-1. 595 1. 00 60. 61 B ATOM 2524 N ARG B 45 23.611 9.652-1. 337 1. 00 62. 88 B ATOM 2525 CA ARG B 45 24.802 10.257-1. 936 1. 00 62. 14 B ATOM 2526 CB ARG B 45 26.039 9.367-1. 743 1. 00 63. 61 B ATOM 2527 CG ARG B 45 25.951 7.948-2. 302 1.00 74. 24 B ATOM 2528 CD ARG B 45 27.278 7.218-2. 535 1. 00 79. 20 B ATOM 2529 NE ARGB 45 28.111 7.909-3. 525 1. 0081. 54 B ATOM 2530 CZ ARG B 45 29.408 8.178-3. 382 1. 00 80. 45 B ATOM 2531 NH1 ARG B 45 30.055 7.813-2. 282 1. 00 78. 77 B ATOM 2532 NH2 ARG B 45 30.053 8.850-4. 330 1. 00 80. 03 B ATOM 2533 C ARG B 45 24.693 10.703-3. 384 1. 00 61. 36 B ATOM 2534 O ARG B 45 24.057 10.042-4. 202 1. 00 62. 25 B ATOM 2535 N ILE B 46 25.282 11.869-3. 655 1. 0061. 33 B ATOM 2536 CA ILE B 46 25.313 12.491-4. 979 1. 00 60. 64 B ATOM 2537 CB ILE B 46 25.397 14.038-4. 845 1. 00 57. 96 B ATOM 2538 CG2 ILE B 46 25.365 14.723-6. 229 1. 00 58. 46 B ATOM 2539 CG1 ILE B 46 24.231 14.530-3. 979 1. 00 56. 30 B ATOM 2540 CD1 ILE B 46 24.303 15.980-3. 544 1. 00 53. 78 B ATOM 2541 C ILE B 46 26.509 11.916-5. 757 1. 00 63. 27 B ATOM 2542 O ILE B 46 27. 598 11. 737-5. 198 1. 00 60. 65 B ATOM 2543 N GLU B 47 26.291 11.643-7. 044 1. 00 65. 95 B ATOM 2544 CA GLU B 47 27.302 11.040-7. 907 1. 00 70. 55 B ATOM 2545 CB GLU B 47 26.632 10.412-9. 138 1. 00 72. 94 B ATOM 2546 CG GLU B 47 27.251 9.080-9. 585 1. 00 75. 80 B ATOM 2547 CD GLU B 47 27.129 7.978-8. 534 1. 00 76. 24 B ATOM 2548 OE1 GLU B 47 26.047 7.355-8. 456 1. 00 78. 44 B ATOM 2549 OE2 GLU B 47 28.109 7.739-7. 791 1. 00 74. 16 B ATOM 2550 C GLU B 47 28. 510 11. 889-8. 315 1. 00 72. 59 B ATOM 2551 O GLU B 47 29.648 11.544-7. 967 1. 00 74. 59 B ATOM 2552 N LYS B 48 28.271 12.969-9. 062 1. 00 72. 15 B ATOM 2553 CA LYSB 48 29.352 13.849-9. 515 1. 0070. 12 B ATOM 2554 CB LYS B 48 29.014 14.490-10. 872 1. 00 72. 79 B ATOM 2555 CG LYS B 48 29.311 13.632-12. 109 1. 00 78. 25 B ATOM 2556 CD LYS B 48 28.420 12.425-12. 398 1. 00 83. 12 B ATOM 2557 CE LYS B 48 28.547 11. 774-13.771 1. 00 84. 55 B ATOM 2558 NZ LYS B 48 29.916 11.243-14. 034 1. 00 85. 11 B ATOM 2559 C LYS B 48 29.697 14.924-8. 481 1. 00 66. 85 B ATOM 2560 O LYS B 48 29.023 15.958-8. 385 1. 00 66. 94 B ATOM 2561 N VAL B 49 30.706 14.624-7. 661 1. 00 60. 19 B ATOM 2562 CA VALB 49 31.192 15.530-6. 615 1. 0054. 61 B ATOM 2563 CB VAL B 49 30.930 14.965-5. 173 1. 00 56. 47 B ATOM 2564 CG1 VAL B 49 31.430 15.941-4. 114 1. 00 56. 12 B ATOM 2565 CG2 VAL B 49 29.455 14.666-4. 946 1. 00 54. 06 B ATOM 2566 C VALB 49 32.702 15.675-6. 784 1. 0050. 10 B ATOM 2567 O VAL B 49 33.431 14.687-6. 676 1. 00 52. 15 B ATOM 2568 N GLU B 50 33.173 16.891-7. 043 1. 00 44. 78 B ATOM 2569 CA GLU B 50 34.612 17.110-7. 184 1. 0043. 51 B ATOM 2570 CB GLU B 50 34.936 18.188-8. 218 1. 00 48. 25 B ATOM 2571 CG GLU B 50 34.594 17.859-9. 658 1.00 57.23 B ATOM 2572 CD GLU B 50 33.228 18.380-10. 063 1. 00 66. 14 B ATOM 2573 OE1 GLU B 50 32. 326 17. 544-10. 306 1. 00 72. 78 B ATOM 2574 OE2 GLU B 50 33. 058 19. 623-10. 134 1. 00 62. 71 B ATOM 2575 C GLU B 50 35.206 17.506-5. 841 1. 00 38. 99 B ATOM 2576 O GLU B 50 34.489 17.988-4. 955 1. 00 37. 62 B ATOM 2577 N HIS B 51 36.501 17.254-5. 677 1. 00 33. 63 B ATOM 2578 CA HIS B 51 37.196 17.605-4. 443 1. 00 30. 83 B ATOM 2579 CB HIS B 51 37.145 16.469-3. 405 1. 00 32. 98 B ATOM 2580 CG HIS B 51 37.798 15.188-3. 841 1. 00 41. 75 B ATOM 2581 CD2 HIS B 51 39.008 14.656-3. 541 1. 0045. 53 B ATOM 2582 ND1 HIS B 51 37.193 14.298-4. 702 1. 0047. 24 B ATOM 2583 CE1 HIS B 51 38.003 13.276-4. 918 1. 0048. 79 B ATOM 2584 NE2 HIS B 51 39.112 13.469-4. 225 1. 0047. 55 B ATOM 2585 C HIS B 51 38.625 18.036-4. 676 1. 00 28. 11 B ATOM 2586 O HIS B 51 39.323 17.470-5. 523 1. 00 32. 23 B ATOM 2587 N SER B 52 39.075 18.995-3. 872 1. 00 24. 01 B ATOM 2588 CA SER B 52 40.442 19.504-3. 956 1. 00 22. 58 B ATOM 2589 CB SER B 52 40.607 20. 691-3.011 1. 00 23. 84 B ATOM 2590 OG SER B 52 40.312 20.321-1. 673 1. 00 23. 68 B ATOM 2591 C SER B 52 41.459 18.431-3. 565 1. 00 22. 93 B ATOM 2592 O SER B 52 41.122 17.457-2. 865 1. 00 21. 70 B ATOM 2593 N ASP B 53 42.700 18.601-4. 023 1. 00 20. 78 B ATOM 2594 CA ASP B 53 43.767 17.663-3. 665 1. 00 19. 44 B ATOM 2595 CB ASP B 53 45.037 17.893-4. 490 1. 00 15. 16 B ATOM 2596 CG ASP B 53 44.881 17.492-5. 943 1. 00 13. 07 B ATOM 2597 OD1 ASP B 53 43.895 16.812-6. 305 1. 00 22. 42 B ATOM 2598 OD2 ASP B 53 45.763 17.860-6. 737 1. 00 17. 12 B ATOM 2599 C ASP B 53 44.053 17.943-2. 202 1. 00 20. 25 B ATOM 2600 O ASP B 53 43.672 19.006-1. 681 1. 00 16. 31 B ATOM 2601 N LEU B 54 44.697 16.990-1. 535 1. 00 23. 25 B ATOM 2602 CA LEU B 54 45.004 17.131-0. 119 1. 00 21. 92 B ATOM 2603 CB LEU B 54 45.663 15.867 0.438 1. 00 22. 71 B ATOM 2604 CG LEU B 54 45.911 15.831 1.954 1. 00 19. 17 B ATOM 2605 CD1 LEU B 54 44.607 15.764 2.745 1. 00 15. 53 B ATOM 2606 CD2 LEU B 54 46.765 14.651 2.260 1. 00 21. 11 B ATOM 2607 C LEU B 54 45.869 18.331 0.181 1. 00 23. 12 B ATOM 2608 O LEU B 54 46.822 18.631-0. 544 1. 00 24. 88 B ATOM 2609 N SER B 55 45.470 19.041 1.228 1. 00 22. 11 B ATOM 2610 CA SER B 55 46.189 20.203 1.682 1. 00 22. 03 B ATOM 2611 CB SER B 55 45.557 21.445 1.101 1. 00 24. 87 B ATOM 2612 OG SER B 55 46.416 22.570 1.226 1. 00 18. 26 B ATOM 2613 C SER B 55 46.160 20.280 3.190 1. 00 22. 62 B ATOM 2614 O SER B 55 45.372 19.589 3.848 1. 00 23. 89 B ATOM 2615 N PHE B 56 47.065 21.086 3.730 1. 00 20. 60 B ATOM 2616 CA PHE B 56 47.136 21.315 5.163 1. 00 23. 11 B ATOM 2617 CB PHE B 56 48.036 20.292 5.893 1. 00 15. 39 B ATOM 2618 CG PHE B 56 49.422 20.175 5.348 1. 00 12. 76 B ATOM 2619 CD1 PHEB 56 49.767 19.075 4.550 1.00 9.42 B ATOM 2620 CD2 PHE B 56 50.409 21.133 5.668 1.00 4.77 B ATOM 2621 CE1 PHE B 56 51.080 18.915 4.074 1. 00 10. 26 B ATOM 2622 CE2 PHE B 56 51. 720 20. 996 5.201 1. 00 12. 21 B ATOM 2623 CZ PHE B 56 52.066 19.880 4.401 1. 00 15. 61 B ATOM 2624 C PHE B 56 47.508 22.760 5.493 1. 00 25. 39 B ATOM 2625 O PHE B 56 48.205 23.440 4.715 1. 00 25. 47 B ATOM 2626 N SERB 57 47.005 23.224 6.633 1. 00 25. 41 B ATOM 2627 CA SERB 57 47.265 24.572 7.116 1. 00 27. 42 B ATOM 2628 CB SERB 57 46.086 25.036 7.977 1. 00 26. 25 B ATOM 2629 OG SERB 57 45.765 24.067 8.958 1. 00 27. 53 B ATOM 2630 C SERB 57 48.590 24.616 7.898 1. 00 28. 95 B ATOM 2631 O SERB 57 49.280 23.599 8.013 1. 00 27. 75 B ATOM 2632 N LYSB 58 48.929 25.792 8.426 1. 00 34. 97 B ATOM 2633 CA LYS B 58 50.162 26.029 9.191 1. 00 40. 62 B ATOM 2634 CB LYSB 58 50.181 27.466 9.722 1. 0046. 52 B ATOM 2635 CG LYSB 58 51.163 28.409 9.020 1. 00 56. 78 B ATOM 2636 CD LYSB 58 52.677 28.151 9.168 1. 00 64. 53 B ATOM 2637 CE LYSB 58 53.304 28.121 10.571 1. 00 65. 62 B ATOM 2638 NZ LYSB 58 53.145 29.402 11.320 1. 00 68. 67 B ATOM 2639 C LYSB 58 50.432 25.066 10.351 1. 0041. 74 B ATOM 2640 O LYSB 58 51.522 24.486 10.440 1. 00 41. 58 B ATOM 2641 N ASP B 59 49.410 24.849 11.182 1. 0041. 20 B ATOM 2642 CA ASP B 59 49.493 23.962 12.350 1. 00 39. 21 B ATOM 2643 CB ASP B 59 48.375 24.300 13.354 1. 00 44. 59 B ATOM 2644 CG ASP B 59 46.974 24.109 12.778 1. 0049. 63 B ATOM 2645 OD1 ASP B 59 46.618 24.815 11.806 1. 00 57. 41 B ATOM 2646 OD2 ASP B 59 46.235 23.252 13.305 1. 0049. 33 B ATOM 2647 C ASP B 59 49.483 22.469 12.002 1. 00 36. 58 B ATOM 2648 O ASP B 59 49.325 21.616 12.884 1. 00 38. 70 B ATOM 2649 N TRP 8 60 49.708 22.183 10.713 1. 00 32. 93 B ATOM 2650 CA TRP B 60 49.765 20. 839 10.100 1. 00 27. 57 B ATOM 2651 CB TRP B 60 50.847 19.951 10.734 1. 00 27. 06 B ATOM 2652 CG TRP B 60 52.198 20.578 10.843 1. 00 34. 72 B ATOM 2653 CD2TRPB 60 53.167 20.716 9.803 1. 00 31. 34 B ATOM 2654 CE2 TRP B 60 54.315 21.313 10.382 1. 00 32. 06 B ATOM 2655 CE3 TRP B 60 53.189 20.382 8.437 1. 00 35. 14 B ATOM 2656 CD1TRPB 60 52.771 21.091 11.975 1. 00 34. 54 B ATOM 2657 NE1 TRP B 60 54.041 21.530 11.706 1. 00 38. 12 B ATOM 2658 CZ2 TRP B 60 55.480 21.586 9.641 1. 0036. 70 B ATOM 2659 CZ3 TRP B 60 54.357 20.650 7.691 1. 00 39. 62 B ATOM 2660 CH2 TRP B 60 55. 483 21. 247 8. 3031. 0035. 76 B ATOM 2661 C TRP B 60 48.469 20.046 9.995 1. 00 24. 18 B ATOM 2662 O TRP B 60 48.483 18.904 9.546 1. 00 22. 06 B ATOM 2663 N SERB 61 47.346 20.642 10.386 1. 00 24. 38 B ATOM 2664 CA SERB 61 46.065 19.945 10.299 1. 0023. 79 B ATOM 2665 CB SER B 61 45. 038 20. 567 11. 244 1. 00 19. 91 B ATOM 2666 OG SER B 61 44.529 21.796 10.751 1. 00 25. 95 B ATOM 2667 C SER B 61 45.577 19.984 8.854 1. 00 22. 56 B ATOM 2668 O SER B 61 45.799 20.967 8.145 1. 00 22. 63 B ATOM 2669 N PHE B 62 44.914 18.917 8.429 1. 00 23. 59 B ATOM 2670 CA PHEB 62 44.419 18.804 7.059 1. 0023. 93 B ATOM 2671 CB PHE B 62 44.355 17.342 6.643 1. 00 18. 06 B ATOM 2672 CG PHE B 62 45.651 16.619 6.778 1. 00 19. 45 B ATOM 2673 CD1 PHE B 62 46.600 16.662 5.748 1. 00 23. 94 B ATOM 2674 CD2 PHE B 62 45.925 15.857 7.920 1. 00 21. 34 B ATOM 2675 CE1 PHE B 62 47. 813 15. 946 5. 845 1. 00 21. 53 B ATOM 2676 CE2 PHE B 62 47.137 15.132 8.035 1. 00 24. 47 B ATOM 2677 CZ PHE B 62 48.080 15.175 6.993 1. 00 19. 80 B ATOM 2678 C PHE B 62 43.079 19.458 6.767 1. 00 27. 06 B ATOM 2679 O PHE B 62 42.219 19.566 7.655 1. 00 28. 41 B ATOM 2680 N TYR B 63 42.920 19.896 5.515 1. 00 26. 79 B ATOM 2681 CA TYR B 63 41.683 20.520 5.050 1. 00 23. 29 B ATOM 2682 CB TRY B 63 41.720 22.054 5.209 1. 0013. 04 B ATOM 2683 CG TYR B 63 42.595 22.824 4.250 1. 00 15. 86 B ATOM 2684 CD1 TYR B 63 42.112 23.215 2.976 1. 00 13. 19 B ATOM 2685 CE1 TYR B 63 42.894 23.982 2.091 1. 00 15. 30 B ATOM 2686 CD2 TYR B 63 43.886 23.217 4.615 1. 00 16. 66 B ATOM 2687 CE2 TYR B 63 44.689 23.999 3.727 1. 00 21. 33 B ATOM 2688 CZ TYR B 63 44.176 24.372 2.472 1. 0019. 35 B ATOM 2689 OH TYR B 63 44.933 25.116 1.599 1. 0031. 88 B ATOM 2690 C TYR B 63 41.346 20.100 3.622 1. 00 23. 29 B ATOM 2691 O TYR B 63 42. 251 19.877 2.813 1. 00 25. 58 B ATOM 2692 N LEU B 64 40.051 20.007 3.315 1. 00 22. 03 B ATOM 2693 CA LEU B 64 39.563 19.618 1.978 1. 0021. 65 B ATOM 2694 CB LEU B 64 39.394 18.093 1.867 1. 00 14. 45 B ATOM 2695 CG LEU B 64 40.589 17.158 1.699 1. 00 18. 34 B ATOM 2696 CD1 LEU B 64 40.201 15.752 2.073 1. 00 18. 41 B ATOM 2697 CD2 LEU B 64 41. 124 17. 236 0. 284 1. 00 22. 35 B ATOM 2698 C LEU B 64 38.210 20.257 1.673 1. 00 22. 35 B ATOM 2699 O LEU B 64 37.387 20.456 2.577 1. 00 22. 45 B ATOM 2700 N LEU B 65 37.971 20.532 0.393 1. 00 18. 35 B ATOM 2701 CA LEU B 65 36.716 21.124-0. 052 1. 00 21. 33 B ATOM 2702 CB LEU B 65 36.964 22. 482-0. 732 1. 00 21. 01 B ATOM 2703 CG LEU B 65 35.784 23.240-1. 381 1. 00 24. 09 B ATOM 2704 CD1 LEU B 65 34.841 23.788-0. 329 1. 00 20. 98 B ATOM 2705 CD2 LEU B 65 36. 294 24. 369-2. 262 1. 00 27. 19 B ATOM 2706 C LEU B 65 36. 015 20. 178-1. 020 1. 00 23. 30 B ATOM 2707 O LEU B 65 36.616 19.714-1. 989 1. 00 28. 77 B ATOM 2708 N TYR B 66 34.752 19.882-0. 730 1. 00 24. 64 B ATOM 2709 CA TYR B 66 33.923 19.013-1. 567 1. 0028. 50 B ATOM 2710 CB TYR B 66 33.388 17.816-0. 757 1. 00 27. 32 B ATOM 2711 CG TYR B 66 34. 387. 16.678-0. 579 1. 00 29. 42 B ATOM 2712 CD1 TYR B 66 35.538 16.835 0.226 1. 00 32. 05 B ATOM 2713 CE1 TYR B 66 36.503 15.789 0.359 1. 00 36. 28 B ATOM 2714 CD2 TYR B 66 34.208 15.446-1. 245 1. 00 27. 32 B ATOM 2715 CE2 TYR B 66 35.163 14.388-1. 122 1. 00 33. 06 B ATOM 2716 CZ TYR B 66 36.307 14.577-0. 322 1. 0037. 59 B ATOM 2717 OH TYR B 66 37.264 13.593-0. 234 1. 00 42. 84 B ATOM 2718 C TYR B 66 32.780 19.881-2. 088 1. 00 30. 24 B ATOM 2179 O TYR B 66 32. 093 20. 542-1. 298 1. 00 30. 40 B ATOM 2720 N TYR B 67 32.607 19.899-3. 412 1. 00 28. 39 B ATOM 2721 CA TYR B 67 31.582 20.713-4. 057 1. 0032. 55 B ATOM 2722 CB TYR B 67 32.190 22.056-4. 530 1. 00 31. 23 B ATOM 2723 CG TYR B 67 33.308 21.958-5. 564 1. 00 30. 03 B ATOM 2724 CD1 TYR B 67 34. 618 21. 578-5. 190 1. 00 28. 84 B ATOM 2725 CE1 TYR B 67 35. 659 21. 449-6. 154 1. 00 35. 20 B ATOM 2726 CD2 TYR B 67 33.054 22.219-6. 926 1. 00 31. 93 B ATOM 2727 CE2 TYR B 67 34.087 22.097-7. 911 1. 00 39. 48 B ATOM 2728 CZ TYR B 67 35.385 21.712-7. 514 1. 0040. 91 B ATOM 2729 OH TYR B 67 36.386 21.600-8. 460 1. 00 41. 41 B ATOM 2730 C TYR B 67 30.844 20.037-5. 215 1. 00 38. 26 B ATOM 2731 O TYR B 67 31.322 19.036-5. 758 1. 00 43. 29 B ATOM 2732 N THR B 68 29.703 20.627-5. 599 1. 00 42. 22 B ATOM 2733 CA THRB 68 28.846 20.167-6. 708 1. 0044. 75 B ATOM 2734 CB THR B 68 28.070 18.838-6. 374 1. 00 46. 21 B ATOM 2735 OG1 THR B 68 27.339 18.408-7. 529 1. 0049. 56 B ATOM 2736 CG2 THR B 68 27.106 19.010-5. 201 1. 00 40. 47 B ATOM 2737 C THR B 68 27.840 21.245-7. 140 1. 00 46. 84 B ATOM 2738 O THR B 68 27.291 21.955-6. 285 1. 00 42. 69 B ATOM 2739 N GLU B 69 27. 587 21. 323-8. 456 1.00 48. 87 B ATOM 2740 CA GLU B 69 26.644 22.282-9. 062 1. 00 51. 22 B ATOM 2741 CB GLU B 69 26.985 22.520-10. 551 1. 00 50. 00 B ATOM 2742 CG GLU B 69 26.182 23.654-11. 226 1. 00 57. 19 B ATOM 2743 CD GLU B 69 26.479 23.816-12. 716 1. 00 63. 28 B ATOM 2744 OE1 GLU B 69 27.480 24.484-13. 057 1. 00 65. 49 B ATOM 2745 OE2 GLU B 69 25.698 23.296-13. 550 1. 00 65. 09 B ATOM 2746 C GLU B 69 25.198 21.781-8. 912 1. 00 52. 54 B ATOM 2747 O GLU B 69 24.726 20.981-9. 721 1. 00 52. 73 B ATOM 2748 N PHE B 70 24.495 22.287-7. 897 1. 00 55. 19 B ATOM 2749 CA PHE B 70 23.120 21.867-7. 621 1. 00 58. 77 B ATOM 2750 CB PHE B 70 23.023 21.303-6. 179 1. 00 60. 76 B ATOM 2751 CG PHE B 70 22.885 22.350-5. 075 1. 00 60. 87 B ATOM 2752 CD1 PHE B 70 23.673 23.516-5. 037 1. 00 61. 60 B ATOM 2753 CD2 PHE B 70 21.946 22.155-4. 055 1. 00 63. 40 B ATOM 2754 CE1 PHE B 70 23.516 24.475-3. 991 1. 00 61. 44 B ATOM 2755 CE2 PHE B 70 21.779 23.101-3. 002 1. 00 63. 67 B ATOM 2756 CZ PHE B 70 22. 569 24. 264-2. 974 1. 00 61. 27 B ATOM 2757 C PHE B 70 22.021 22.899-7. 903 1. 00 60. 56 B ATOM 2758 O PHE B 70 22.312 24.056-8. 199 1. 00 60. 13 B ATOM 2759 N THR B 71 20.768 22.465-7. 760 1. 00 62. 83 B ATOM 2760 CA THR B 71 19.592 23.309-7. 967 1. 00 65. 10 B ATOM 2761 CB THR B 71 18.885 22. 962-9.309 1. 00 63. 04 B ATOM 2762 OG1 THR B 71 19.829 23.084-10. 380 1. 00 63. 34 B ATOM 2763 CG2 THR B 71 17.712 23.909-9. 582 1. 00 62. 09 B ATOM 2764 C THR B 71 18.645 23.127-6. 761 1. 00 67. 09 B ATOM 2765 O THR B 71 17. 950 22. 110-6. 660 1. 00 68. 86 B ATOM 2766 N PRO B 72 18.645 24.091-5. 810 1. 00 69. 39 B ATOM 2767 CD PRO B 72 19.604 25.212-5. 717 1. 00 68. 17 B ATOM 2768 CA PRO B 72 17.794 24.047-4. 607 1. 00 72. 97 B ATOM 2769 CB PRO B 72 18.441 25.093-3. 700 1. 00 72. 01 B ATOM 2770 CG PRO B 72 18.980 26.106-4. 682 1. 00 66. 79 B ATOM 2771 C PRO B 72 16.295 24.332-4. 802 1. 00 76. 33 B ATOM 2772 O PRO B 72 15.906 25.212-5. 577 1. 00 78. 23 B ATOM 2773 N THR B 73 15.465 23.549-4. 116 1. 00 78. 03 B ATOM 2774 CA THR B 73 14.012 23.703-4. 165 1. 00 79. 80 B ATOM 2775 CB THR B 73 13.321 22.561-4. 957 1. 00 79. 79 B ATOM 2776 OG1 THR B 73 13.837 21.300-4. 526 1. 00 76. 35 B ATOM 2777 CG2 THR B 73 13.516 22.726-6. 465 1. 00 78. 21 B ATOM 2778 C THR B 73 13.476 23.736-2. 736 1. 00 81. 12 B ATOM 2779 O THR B 73 14.259 23.731-1. 778 1. 00 81. 66 B ATOM 2780 N GLU B 74 12.148 23.755-2. 608 1. 00 82. 48 B ATOM 2781 CA GLUB 74 11.444 23.807-1. 323 1. 0083. 30 B ATOM 2782 CB GLU B 74 9.924 23.800-1. 552 1. 00 86. 76 B ATOM 2783 CG GLU B 74 9.299 25.181-1. 759 1. 00 88. 22 B ATOM 2784 CD GLU B 74 9.268 26.014-0. 480 1. 00 88. 90 B ATOM 2785 OE1 GLU B 74 10.171 26.859-0. 297 1. 00 91. 28 B ATOM 2786 OE2 GLU B 74 8.344 25.820 0.342 1. 00 83. 59 B ATOM 2787 C GLU B 74 11.819 22.783-0. 247 1. 00 82. 77 B ATOM 2788 O GLU B 74 12.549 23.122 0.684 1. 00 82. 37 B ATOM 2789 N LYS B 75 11.369 21.538-0. 396 1. 00 82. 57 B ATOM 2790 CA LYS B 75 11.648 20.512 0.606 1. 00 82. 95 B ATOM 2791 CB LYS B 75 10.403 19.649 0.853 1. 00 86. 03 B ATOM 2792 CG LYS B 75 10.022 19.554 2.334 1. 00 92. 10 B ATOM 2793 CD LYS B 75 9.647 20.860 3.056 1. 00 95. 40 B ATOM 2794 CE LYS B 75 9.730 20.880 4.582 1. 00 95. 86 B ATOM 2795 NZ LYS B 75 11.138 20.730 5.068 1. 00 94. 83 B ATOM 2796 C LYS B 75 12.889 19.640 0.418 1. 00 81. 66 B ATOM 2797 O LYS B 75 13.170 18.782 1.265 1. 00 82. 98 B ATOM 2798 N ASP B 76 13.652 19.889-0. 651 1. 00 78. 79 B ATOM 2799 CA ASP B 76 14.881 19.134-0. 938 1. 00 75. 03 B ATOM 2800 CB ASP B 76 15.397 19.440-2. 355 1. 00 77. 45 B ATOM 2801 CG ASP B 76 14.915 18.435-3. 408 1. 00 78. 40 B ATOM 2802 OD1 ASP B 76 14.634 17.266-3. 065 1. 00 82. 83 B ATOM 2803 OD2 ASP B 76 14.852 18.809-4. 599 1. 00 73. 68 B ATOM 2804 C ASP B 76 15.981 19.420 0.093 1. 00 72. 47 B ATOM 2805 O ASP B 76 16.628 20.473 0.059 1. 00 71. 95 B ATOM 2806 N GLU B 77 16.138 18.491 1.037 1. 00 70. 92 B ATOM 2807 CA GLUB 77 17.135 18.594 2.108 1. 0069. 88 B ATOM 2808 CB GLU B 77 16.656 17.861 3.368 1. 00 71. 14 B ATOM 2809 CG GLU B 77 15.403 18.457 4. 010 1. 00 73. 93 B ATOM 2810 CD GLU B 77 15.061 17.813 5.346 1. 00 76. 41 B ATOM 2811 OE1 GLU B 77 15.306 18.453 6.394 1. 00 75. 73 B ATOM 2812 OE2 GLU B 77 14.547 16.671 5.348 1. 00 74. 15 B ATOM 2813 C GLU B 77 18.501 18.058 1.682 1. 00 66. 82 B ATOM 2814 O GLU B 77 18.593 17.012 1.039 1. 00 65. 52 B ATOM 2815 N TYR B 78 19.546 18.819 2.012 1. 00 64. 11 B ATOM 2816 CA TYR B 78 20.937 18.478 1.694 1. 00 59. 21 B ATOM 2817 CB TYR B 78 21.543 19.521 0.749 1. 00 56. 46 B ATOM 2818 CG TYR B 78 20.929 19.547-0. 631 1. 00 55. 54 B ATOM 2819 CD1TYRB 78 19.816 20.367-0. 914 1. 0059. 43 B ATOM 2820 CE1 TYR B 78 19.211 20.373-2. 205 1. 0061. 63 B ATOM 2821 CD2 TYR B 78 21.438 18.733-1. 661 1. 00 56. 03 B ATOM 2822 CE2 TYR B 78 20.847 18.730-2. 957 1. 00 60. 47 B ATOM 2823 CZ TYR B 78 19.736 19.550-3. 217 1. 00 61. 76 B ATOM 2824 OH TYR B 78 19.164 19.548-4. 470 1. 00 66. 36 B ATOM 2825 C TYR B 78 21.794 18.371 2.960 1. 00 57. 39 B ATOM 2826 O TYR B 78 21.484 18.996 3.981 1. 00 61. 03 B ATOM 2827 N ALA B 79 22.871 17.584 2.880 1. 00 52. 75 B ATOM 2828 CA ALA B 79 23.789 17.365 4.003 1. 0047. 56 B ATOM 2829 CB ALA B 79 23.198 16.325 4.973 1. 00 48. 06 B ATOM 2830 C ALA B 79 25.192 16.932 3.569 1. 00 44. 84 B ATOM 2831 O ALA B 79 25.458 16.744 2.377 1. 00 42. 46 B ATOM 2832 N CYS B 80 26.085 16.805 4.552 1. 00 39. 84 B ATOM 2833 CA CYS B 80 27.460 16.377 4.330 1. 00 38. 62 B ATOM 2834 C CYS B 80 27.789 15.246 5.318 1. 00 39. 11 B ATOM 2835 O CYS B 80 27.752 15.440 6.536 1. 00 40. 73 B ATOM 2836 CB CYS B 80 28.420 17.558 4.500 1. 00 36. 59 B ATOM 2837 SG CYS B 80 30.130 17.213 3.978 1. 00 45. 02 B ATOM 2838 N ARG B 81 28.052 14.054 4.782 1. 00 38. 37 B ATOM 2839 CA ARG B 81 28.366 12.871 5.585 1. 00 35. 95 B ATOM 2840 CB ARG B 81 27.696 11.638 4.974 1. 00 37. 64 B ATOM 2841 CG ARG B 81 27.763 10.378 5.811 1. 00 44. 66 B ATOM 2842 CD ARG B 81 26.911 9.210 5.355 1. 00 50. 98 B ATOM 2843 NE ARG B 81 27.251 8.797 3.996 1. 0056. 79 B ATOM 2844 CZ ARG B 81 26.380 8.326 3.107 1. 00 56. 77 B ATOM 2845 NH1 ARG B 81 25.098 8.195 3.424 1. 00 59. 08 B ATOM 2846 NH2 ARG B 81 26.784 8.041 1.876 1. 00 59. 61 B ATOM 2847 C ARG B 81 29.871 12.701 5.617 1. 00 36. 05 B ATOM 2848 O ARG B 81 30.514 12.697 4.568 1. 00 36. 53 B ATOM 2849 N VAL B 82 30.425 12.572 6.825 1. 00 36. 04 B ATOM 2850 CA VAL B 82 31.878 12.447 7.025 1. 00 36. 24 B ATOM 2851 CB VAL B 82 32.457 13.755 7.692 1. 00 38. 45 B ATOM 2852 CG1 VAL B 82 33.964 13.655 7.923 1. 00 36. 32 B ATOM 2853 CG2 VAL B 82 32.155 14.988 6.839 1. 00 39. 19 B ATOM 2854 C VAL B 82 32.299 11.239 7.871 1. 00 34. 02 B ATOM 2855 O VAL B 82 31.785 11.039 8.963 1. 00 36. 26 B ATOM 2856 N ASN B 83 33.288 10.496 7.375 1. 00 34. 47 B ATOM 2857 CA ASN B 83 33.850 9.325 8. 053 1. 0038. 09 B ATOM 2858 CB ASN B 83 33.729 8.073 7.177 1. 00 41. 95 B ATOM 2859 CG ASN B 83 32.518 7.231 7.511 1. 0048. 30 B ATOM 2860 OD1 ASN B 83 32.378 6.741 8.641 1. 00 53. 26 B ATOM 2861 ND2 ASN B 83 31.642 7.030 6.522 1. 00 45. 95 B ATOM 2862 C ASN B 83 35.329 9.577 8.356 1. 00 38. 34 B ATOM 2863 O ASN B 83 36.120 9.831 7.440 1. 00 37. 37 B ATOM 2864 N HIS B 84 35.693 9.499 9.638 1. 00 36. 13 B ATOM 2865 CA HIS B 84 37.073 9.715 10.086 1. 00 34. 47 B ATOM 2866 CB HIS B 84 37.269 11.183 10.502 1. 00 31. 83 B ATOM 2867 CG HIS B 84 38.703 11.586 10.679 1. 00 30. 87 B ATOM 2868 CD2 HIS B 84 39.691 11.794 9.775 1. 00 24. 52 B ATOM 2869 ND1 HIS B 84 39.267 11.803 11.921 1. 00 27. 57 B ATOM 2870 CE1 HIS B 84 40.540 12.126 11.774 1. 00 29. 15 B ATOM 2871 NE2 HIS B 84 40.824 12.126 10.481 1. 00 32. 78 B ATOM 2872 C HIS B 84 37.338 8.792 11.270 1. 00 35. 88 B ATOM 2873 O HIS B 84 36.393 8.356 11.926 1. 00 43. 07 B ATOM 2874 N VAL B 85 38.617 8.530 11.558 1. 00 34. 38 B ATOM 2875 CA VAL B 85 39.045 7.657 12.664 1. 0036. 97 B ATOM 2876 CB VAL B 85 40.614 7.448 12.647 1. 00 40. 04 B ATOM 2877 CG1 VAL B 85 41.340 8.758 12.767 1. 00 35. 59 B ATOM 2878 CG2 VAL B 85 41.083 6.477 13.747 1. 00 38. 03 B ATOM 2879 C VAL B 85 38.554 8.096 14.055 1. 00 37. 89 B ATOM 2880 O VAL B 85 38.384 7.268 14.947 1. 00 41. 24 B ATOM 2881 N THR B 86 38.286 9.387 14.212 1. 00 38. 47 B ATOM 2882 CA THR B 86 37.805 9.925 15.481 1. 0042. 75 B ATOM 2883 CB THR B 86 38.062 11.430 15.579 1. 00 42. 87 B ATOM 2884 OG1 THR B 86 37.713 12.069 14.343 1. 00 41. 91 B ATOM 2885 CG2 THR B 86 39.509 11.703 15.906 1. 00 46. 51 B ATOM 2886 C THR B 86 36.321 9.660 15.722 1. 00 44. 64 B ATOM 2887 O THR B 86 35.877 9.563 16.869 1. 00 45. 37 B ATOM 2888 N LEU B 87 35.577 9.523 14.627 1. 0047. 70 B ATOM 2889 CA LEU B 87 34.137 9.276 14.659 1. 00 52. 47 B ATOM 2890 CB LEU B 87 33.489 9.845 13.396 1. 0048. 43 B ATOM 2891 CG LEU B 87 33.787 11.305 13.053 1. 00 45. 92 B ATOM 2892 CD1 LEU B 87 33.309 11.608 11.651 1. 0045. 41 B ATOM 2893 CD2 LEU B 87 33.142 12.234 14.055 1. 00 44. 88 B ATOM 2894 C LEU B 87 33.794 7.790 14.782 1. 00 57. 43 B ATOM 2895 O LEU B 87 34.378 6.945 14.090 1. 00 61. 07 B ATOM 2896 N SER B 88 32.849 7.484 15.673 1. 00 59. 24 B ATOM 2897 CA SER B 88 32.389 6.112 15.909 1. 00 60. 42 B ATOM 2898 CB SER B 88 31.693 6.022 17.273 1. 00 61. 00 B ATOM 2899 OG SER B 88 30.702 7.030 17.414 1. 00 61. 07 B ATOM 2900 C SER B 88 31.433 5.703 14.782 1. 00 60. 39 B ATOM 2901 O SER B 88 31.489 4.585 14.262 1. 00 59. 98 B ATOM 2902 N GLN B 89 30.583 6.653 14.404 1. 00 59. 33 B ATOM 2903 CA GLN B 89 29.606 6.489 13.339 1. 00 59. 63 B ATOM 2904 CB GLN B 89 28.186 6.342 13.933 1. 00 59. 28 B ATOM 2905 CG GLN B 89 27.726 7.482 14.849 1. 00 61. 70 B ATOM 2906 CD GLN B 89 27.173 7.005 16.182 1. 00 66. 32 B ATOM 2907 OE1 GLN B 89 27.388 5.855 16.592 1. 00 63. 96 B ATOM 2908 NE2 GLN B 89 26. 468 7.898 16.879 1. 00 61. 80 B ATOM 2909 C GLN B 89 29.732 7.750 12.468 1. 00 59. 65 B ATOM 2910 O GLN B 89 30.164 8.799 12.971 1. 00 58. 38 B ATOM 2911 N PRO B 90 29.442 7.653 11.145 1. 00 58. 94 B ATOM 2912 CD PRO B 90 29.132 6.465 10.329 1. 00 58. 85 B ATOM 2913 CA PRO B 90 29.541 8.831 10.272 1. 00 58. 95 B ATOM 2914 CB PRO B 90 29.058 8.299 8.915 1. 0057. 07 B ATOM 2915 CG PRO B 90 28.276 7.059 9.256 1. 00 58. 30 B ATOM 2916 C PRO B 90 28.726 10.040 10.750 1. 00 59. 31 B ATOM 2917 O PRO B 90 27.582 9.894 11.203 1. 00 60. 50 B ATOM 2918 N LYS B 91 29.366 11.208 10.714 1. 00 57. 25 B ATOM 2919 CA LYSB 91 28.756 12.457 11.151 1. 0057. 44 B ATOM 2920 CB LYS B 91 29.832 13.362 11.756 1. 00 57. 50 B ATOM 2921 CG LYS B 91 29.345 14.365 12.792 1. 00 58. 86 B ATOM 2922 CD LYS B 91 30.434 15.126 13.529 1. 00 62. 32 B ATOM 2923 CE LYS B 91 30.016 16.025 14.675 1. 00 70. 29 B ATOM 2924 NZ LYS B 91 31.208 16.620 15.345 1. 00 74. 58 B ATOM 2925 C LYS B 91 28.045 13.173 10.007 1. 00 56. 95 B ATOM 2926 O LYS B 91 28.646 13.434 8.965 1. 00 58. 81 B ATOM 2927 N ILE B 92 26.756 13.449 10.203 1. 00 56. 09 B ATOM 2928 CA ILE B 92 25.934 14.152 9. 219 1. 00 56. 88 B ATOM 2929 CB ILE B 92 24.600 13.376 8.849 1. 00 57. 41 B ATOM 2930 CG2 ILE B 92 24.911 12.174 7.981 1. 00 53. 32 B ATOM 2931 CG1 ILE B 92 23.734 13.020 10.087 1. 00 67. 54 B ATOM 2932 CD1 ILE B 92 24.236 11.889 11.034 1. 00 68. 16 B ATOM 2933 C ILE B 92 25. 614 15. 582 9. 686 1. 00 57. 95 B ATOM 2934 O ILE B 92 25.072 15.785 10.780 1. 00 62. 08 B ATOM 2935 N VAL B 93 26.046 16.570 8.904 1. 00 55. 50 B ATOM 2936 CA VAL B 93 25.790 17.980 9.214 1. 00 54. 35 B ATOM 2937 CB VAL B 93 27.110 18.814 9.334 1. 00 54. 86 B ATOM 2938 CG1 VAL B 93 26.801 20.297 9.601 1. 00 48. 52 B ATOM 2939 CG2 VAL B 93 27.997 18.263 10.457 1. 00 54. 00 B ATOM 2940 C VAL B 93 24.919 18.527 8.088 1. 00 56. 22 B ATOM 2941 O VAL B 93 25.367 18.626 6.942 1. 00 56. 71 B ATOM 2942 N LYS B 94 23.678 18.879 8.429 1. 00 57. 86 B ATOM 2943 CA LYSB 94 22.703 19.407 7.468 1. 0057. 36 B ATOM 2944 CB LYS B 94 21.282 19.399 8.058 1. 00 60. 25 B ATOM 2945 CG LYS B 94 20.646 18.020 8.220 1. 00 67. 80 B ATOM 2946 CD LYS B 94 19.120 17.960 8.408 1. 00 71. 97 B ATOM 2947 CE LYS B 94 18.504 18.509 9.697 1. 00 72. 95 B ATOM 2948 NZ LYS B 94 18.775 17.649 10.888 1. 00 71. 19 B ATOM 2949 C LYS B 94 23.022 20.804 6.950 1. 00 55. 43 B ATOM 2950 O LYS B 94 23.748 21.570 7.591 1. 00 56. 02 B ATOM 2951 N TRP B 95 22.503 21.106 5.762 1. 00 54. 01 B ATOM 2952 CA TRP B 95 22. 678 22. 412 5.151 1. 00 53. 37 B ATOM 2953 CB TRP B 95 22.710 22.313 3.617 1. 00 49. 79 B ATOM 2954 CG TRP B 95 22.757 23.650 2.889 1. 0046. 09 B ATOM 2955 CD2 TRP B 95 21.858 24.098 1.869 1. 00 46. 45 B ATOM 2956 CE2 TRP B 95 22.251 25.421 1.514 1. 00 46. 77 B ATOM 2957 CE3 TRP B 95 20.752 23.514 1.211 1. 00 47. 92 B ATOM 2958 CD1 TRP B 95 23. 638 24. 681 3.101 1. 00 47. 75 B ATOM 2959 NE1 TRP B 95 23.336 25.745 2.283 1. 00 45. 99 B ATOM 2960 CZ2 TRP B 95 21.572 26.180 0.524 1. 00 48. 69 B ATOM 2961 CZ3 TRP B 95 20.069 24.268 0.216 1. 00 49. 51 B ATOM 2962 CH2TRPB 95 20.489 25.591-0. 112 1. 0049. 34 B ATOM 2963 C TRP B 95 21.515 23.274 5.607 1. 00 56. 85 B ATOM 2964 O TRP B 95 20.352 22.977 5.315 1. 00 58. 10 B ATOM 2965 N ASP B 96 21.853 24.308 6.370 1. 00 60. 23 B ATOM 2966 CA ASP B 96 20. 887 25.267 6.883 1. 00 62. 78 B ATOM 2967 CB ASP B 96 21.165 25.528 8.369 1. 00 65. 30 B ATOM 2968 CG ASP B 96 20.026 26.257 9.088 1. 00 69. 61 B ATOM 2969 OD1 ASP B 96 19.757 25.894 10.256 1. 00 72. 50 B ATOM 2970 OD2 ASP B 96 19. 430 27. 203 8.521 1. 00 68. 75 B ATOM 2971 C ASP B 96 21. 120 26. 511 6.021 1. 00 64. 13 B ATOM 2972 O ASP B 96 22.210 27.093 6.019 1. 00 65. 24 B ATOM 2973 N ARG B 97 20.094 26.857 5.249 1. 00 65. 95 B ATOM 2974 CA ARG B 97 20.093 27.996 4.324 1. 00 68. 99 B ATOM 2975 CB ARG B 97 18.786 27.986 3.523 1. 00 70. 90 B ATOM 2976 CG ARG B 97 18.441 26.633 2.907 1. 00 72. 55 B ATOM 2977 CD ARG B 97 17.055 26.460 2.314 1. 00 75. 80 B ATOM 2978 NE ARG B 97 16.700 27.546 1.400 1. 00 77. 59 B ATOM 2979 CZ ARG B 97 15.907 27.416 0.337 1. 00 79. 58 B ATOM 2980 NH1 ARG B 97 15.374 26.238 0.027 1. 00 82. 01 B ATOM 2981 NH2 ARG B 97 15.635 28.476-0. 412 1. 00 78. 78 B ATOM 2982 C ARG B 97 20.244 29.360 5.006 1. 00 69. 04 B ATOM 2983 O ARG B 97 20.957 30.242 4.511 1. 00 69. 57 B ATOM 2984 N ASP B 98 19.586 29.495 6.156 1. 00 69. 42 B ATOM 2985 CA ASP B 98 19.576 30.722 6.952 1. 00 69. 10 B ATOM 2986 CB ASP B 98 18.286 30.790 7.789 1. 00 68. 41 B ATOM 2987 CG ASP B 98 17.024 30.820 6.933 1. 00 65. 33 B ATOM 2988 OD1 ASP B 98 16.520 29.735 6.571 1. 00 63. 91 B ATOM 2989 OD2 ASP B 98 16.532 31.927 6.631 1. 00 63. 15 B ATOM 2990 C ASP B 98 20.797 30.915 7.859 1. 00 69. 23 B ATOM 2991 O ASP B 98 20.948 31.972 8.478 1. 00 69. 50 B ATOM 2992 N MET B 99 21.661 29.902 7.929 1. 00 69. 40 B ATOM 2993 CA MET B 99 22.871 29.951 8.760 1. 00 69. 93 B ATOM 2994 CB MET B 99 23.245 28.542 9.219 1. 00 68. 02 B ATOM 2995 CG MET B 99 24.264 28.465 10.344 1. 00 69. 07 B ATOM 2996 SD MET B 99 24.770 26.770 10.628 1. 00 67. 08 B ATOM 2997 CE MET B 99 23.334 26.134 11.562 1. 00 59. 91 B ATOM 2998 C MET B 99 24.049 30.575 8.006 1. 00 70. 32 B ATOM 2999 O MET B 99 24.883 31.227 8.667 1. 00 68. 57 B ATOM 3000 OXT MET B 99 24.131 30.389 6.770 1. 00 72. 21 B ATOM 3001 C1 TWT D 2 57.390 23.811-11. 669 1. 00 45. 44 D ATOM 3002 C2 TWTD 2 57.670 22.393-11. 230 1. 0051. 36 D ATOM 3003 C3 TWTD 2 56.465 21.509-10. 963 1. 0053. 52 D ATOM 3004 C4 TWT D 2 56.547 20.564-9. 772 1. 00 54. 41 D ATOM 3005 C5 TWT D 2 55.564 20.779-8. 633 1. 00 48. 69 D ATOM 3006 C6 TWTD 2 54.750 19.579-8. 191 1. 0045. 72 D ATOM 3007 C7 TWT D 2 54.691 19.272-6. 701 1. 00 43. 46 D ATOM 3008 C8 TWTD 2 55.807 18.414-6. 120 1. 0040. 49 D ATOM 3009 C9 TWT D 2 55.479 17.561-4. 900 1. 00 39. 79 D ATOM 3010 C10 TWT D 2 56.642 17.096-4. 030 1. 00 35. 75 D ATOM 3011 C11 TWT D 2 56.914 17.880-2. 758 1. 00 42. 69 D ATOM 3012 C12 TWT D 2 58.156 17.501-1. 955 1. 00 46. 22 D ATOM 3013 C13 TWT D 2 58.933 18.601-1. 215 1. 00 45. 52 D ATOM 3014 C14 TWT D 2 58.554 18.882 0.244 1. 00 46. 99 D ATOM 3015 C15 TWT D 2 59.612 19.472 1.166 1. 00 38. 14 D ATOM 3016 C16 TWT D 2 60.463 18.523 1.984 1. 00 40. 55 D ATOM 3017 C17 TWT D 2 59.819 17.890 3.208 1. 00 44. 19 D ATOM 3018 C18 TWT D 2 60.706 17.525 4.387 1. 00 43. 18 D ATOM 3019 C19 TWT D 2 60.503 16.146 5.008 1. 00 46. 31 D ATOM 3020 C20 TWT D 2 60.665 16.023 6.520 1. 00 46. 01 D ATOM 3021 C21 TWT D 2 61.324 14.767 7.053 1. 0043. 56 D ATOM 3022 C22 TWT D 2 60.922 14.312 8.437 1. 00 48. 53 D ATOM 3023 C1 SWT F 1 71.717 11.979-6. 552 1.00131. 90 F ATOM 3024 01 SWT F 1 71.910 11.096-5. 488 1.00128. 30 F ATOM 3025 C2 SWT F 1 72. 785 13. 092-6. 548 1. 00132.86 F ATOM 3026 02 SWT F 1 72.688 13.863-5. 356 1.00131. 40 F ATOM 3027 C3 SWT F 1 72.575 13.998-7. 767 1.00132. 84 F ATOM 3028 03 SWT F 1 73.599 14.982-7. 822 1.00132. 29 F ATOM 3029 C4 SWT F 1 72.581 13.162-9. 055 1.00133. 69 F ATOM 3030 04 SWT F 1 72.269 13.995-10. 166 1.00134. 40 F ATOM 3031 C5 SWT F 1 71.553 12.019-8. 953 1.00133. 10 F ATOM 3032 05 SWT F 1 71.800 11.220-7. 771 1.00133. 66 F ATOM 3033 C6 SWT F 1 71.581 11.074-10. 151 1.00132. 42 F ATOM 3034 06 SWT F 1 72.647 10.136-10. 064 1.00126. 30 F ATOM 3035 CL6 SWT F 1 65. 105 16. 994-1. 642 1. 00 75. 32 F ATOM 3036 CL5 SWT F 1 66.321 16.767-2. 550 1. 00 81. 46 F ATOM 3037 CL4 SWT F 1 65.985 15.837-3. 722 1. 00 89. 26 F ATOM 3038 CL3 SWT F 1 66.537 14.430-3. 489 1. 00 96. 57 F ATOM 3039 CL2 SWT F 1 67.222 13.895-4. 747 1.00104. 40 F ATOM 3040 CL1 SWT F 1 68. 714 13. 654-4. 495 1. 00109.16 F ATOM 3041 O SWT F 1 69.530 14.563-4. 659 1.00108. 27 F ATOM 3042 N SWT F 1 68.996 12.508-3. 861 1.00112. 40 F ATOM 3043 CB2 SWT F 1 69.682 11.376-4. 526 1.00115. 41 F ATOM 3044 CB1 SWT F 1 71.210 11.514-4. 339 1.00120. 42 F ATOM 3045 CR1 SWT F 1 69.160 10.028-3. 974 1.00110. 88 F ATOM 3046 OR SWT F 1 69.695 9.779-2. 669 1.00112. 29 F ATOM 3047 CR2 SWT F 1 67.618 9.964-3. 937 1. 00104.53 F ATOM 3048 CR3 SWT F 1 67.037 10.705-2. 721 1. 00 95. 83 F ATOM 3049 CR4 SWT F 1 66.848 9.757-1. 534 1.00 91. 36 F ATOM 3050 CR5 SWT F 1 67. 291 10.412-0. 225 1. 00 88. 01 F ATOM 3051 CR6 SWT F 1 66.088 10.776 0.650 1. 00 83. 08 F ATOM 3052 CR7 SWT F 1 66. 016 12. 289 0. 873 1.00 80. 52 F ATOM 3053 CR8 SWT F 1 65. 305 12. 619 2. 176 1. 00 75. 19 F ATOM 3054 CR9 SWT F 1 65. 863 13. 759 3. 016 1. 00 73. 28 F ATOM 3055 CR10 SWT F 1 65.378 15.174 2.727 1. 00 72. 01 F ATOM 3056 CR11 SWT F 1 64.936 16.009 3.921 1. 00 70. 49 F ATOM 3057 CR12 SWT F 1 65.284 17.488 3.910 1. 00 72. 63 F ATOM 3058 CR13 SWT F 1 66.045 18.043 5.111 1. 00 74. 72 F ATOM 3059 CR14 SWT F 1 67.468 18.532 4.865 1. 00 79. 65 F ATOM 3060 CR15 SWT F 1 67.996 19.642 5.765 1. 00 82. 49 F ATOM 3061 CR16 SWT F 1 68. 643 20. 840 5. 094 1.00 81. 68 F ATOM 3062 CL7 SWT F 1 64.085 17.934-2. 295 1. 00 72. 09 F ATOM 3063 CL8 SWT F 1 63.211 18.611-1. 251 1. 00 69. 84 F ATOM 3064 CL9 SWT F 1 63.284 20.134-1. 160 1. 00 65. 16 F ATOM 3065 CL10 SWT F 1 62. 371 20. 934-2. 079 1. 00 60. 18 F ATOM 3066 CL11 SWT F 1 62.511 22.448-2. 058 1. 00 53. 57 F ATOM 3067 CL12 SWT F 1 61.307 23.246-2. 532 1. 00 48. 80 F ATOM 3068 CL13 SWT F 1 61.542 24.651-3. 026 1. 00 40. 57 F ATOM 3069 CL14 SWT F 1 61.707 24.797-4. 508 1. 00 37. 53 F ATOM 3070 CL15 SWT F 1 60. 454 25. 077-5. 288 1.00 32. 76 F ATOM 3071 CL16 SWT F 1 60. 630 25. 439-6. 738 1. 00 30. 20 F ATOM 3072 CL17 SWT F 1 60.228 24.407-7. 754 1. 00 33. 69 F ATOM 3073 CL18 SWT F 1 59. 647 24. 927-9. 026 1. 00 34. 28 F ATOM 3074 OH2 WAT S 2 42. 437 20. 412 0. 022 1.00 35. 65 S ATOM 3075 OH2 WAT S 3 53.094 15.104 10.333 1. 00 27. 31 S ATOM 3076 OH2 WAT S 4 33.716 30.014 10.501 1. 00 15. 62 S ATOM 3077 OH2 WAT S 5 49.193 19.185-17. 084 1. 00 31. 00 S ATOM 3078 OH2 WAT S 6 42.373 19.959-6. 918 1. 00 30. 87 S ATOM 3079 OH2 WAT S 7 48.550 17.560-2. 066 1. 00 32. 78 S ATOM 3080 OH2 WAT S 8 59. 484 14. 016-16. 309 1. 00 18. 35 S ATOM 3081 OH2 WAT S 9 49.570 24.297 1.265 1. 00 23. 45 S ATOM 3082 OH2 WAT S 10 32.173 34.424-7. 680 1.00 4.37 S ATOM 3083 OH2 WAT S 11 44.840 17.521-9. 337 1. 00 20. 74 S ATOM 3084 OH2 WAT S 12 20.436 14.835 3.162 1. 00 28. 97 S ATOM 3085 OH2 WAT S 13 38.712 49.435 8.538 1. 00 27. 66 S ATOM 3086 OH2 WAT S 14 49.118 5.938 6.699 1. 00 39. 82 S ATOM 3087 OH2 WAT S 15 39.880 27.701-10. 681 1. 00 25. 86 S ATOM 3088 OH2 WAT S 16 47.416 15.671-3. 910 1. 00 19. 43 S ATOM 3089 OH2 WAT S 17 25.674 42.441-2. 943 1. 0029. 65 S ATOM 3090 OH2 WAT S 19 24.770 29.564 2.661 1. 00 30. 73 S ATOM 3091 OH2 WAT S 20 41.015 27.077 2.253 1. 00 40. 18 S ATOM 3092 OH2 WAT S 21 54.479 21.295 17.281 1. 00 28. 10 S ATOM 3093 OH2 WAT S 22 36.925 46.454-9. 092 1. 0021. 15 S ATOM 3094 OH2 WAT S 24 45.732 41.064-2. 081 1. 00 30. 90 S ATOM 3095 OH2 WAT S 25 51. 874 26. 461-17.841 1. 00 26. 20 S ATOM 3096 OH2 WAT S 26 40.106 31.619-11. 887 1. 00 32. 47 S ATOM 3097 OH2 WAT S 27 42.925 22.512 8.538 1. 00 34. 79 S ATOM 3098 OH2 WAT S 28 66.807 23.047-11. 935 1. 00 33. 57 S ATOM 3099 OH2 WAT S 30 35.735 10.720-0. 617 1. 00 16. 73 S ATOM 3100 OH2 WAT S 31 49.354 14.273-5. 122 1. 00 21. 36 S ATOM 3101 OH2 WAT S 36 37.461 4.328 14.610 1. 00 26. 91 S ATOM 3102 OH2WATS 37 31. 064 48. 776 20. 335 1. 00 26. 22 S ATOM 3103 OH2 WAT S 38 39.419 23.835 11.381 1. 0023. 73 S ATOM 3104 OH2 WAT S 42 50.501 34.662-19. 238 1. 00 20. 32 S ATOM 3105 OH2 WAT S 43 27.883 24.679 8.563 1. 00 31. 47 S ATOM 3106 OH2 WAT S 46 19. 071 35.135-5. 226 1. 00 26. 48 S ATOM 3107 OH2 WAT S 47 50.999 21.470 15.352 1. 00 34. 63 S ATOM 3108 OH2 WAT S 48 32.407 31.536 7.666 1. 00 20. 23 S ATOM 3109 OH2 WAT S 49 18.121 47.897 10. 834 1. 00 34. 61 S ATOM 3110 OH2 WAT S 50 56.307 7.289 16.176 1. 0026. 67 S ATOM 3111 OH2 WAT S 51 44.551 35.789-2. 442 1. 00 10. 71 S ATOM 3112 OH2 WAT S 52 47.918 16.451-6. 563 1.00 8.65 S ATOM 3113 OH2 WAT S 53 74.597 12.531-0. 845 1. 0042. 09 S ATOM 3114 N1 DTI D 7 71.254 6.982-6. 846 1.00104. 35 D ATOM 3115 CN4 DTI D 7 69.974 6.871-6. 117 1.00103. 31 D ATOM 3116 CN5 DTI D 7 71.040 7.778-8. 065 1. 00102.10 D ATOM 3117 CN3 DTI D 7 71.721 5.634-7. 232 1. 00102.63 D ATOM 3118 C2 DTI D 7 72.564 6.911-4. 677 1.00100. 45 D ATOM 3119 C1 DTI D 7 72.279 7.664-6. 000 1.00101. 42 D ATOM 3120 C3 DTI D 7 72.890 7.890-3. 542 1.00100. 53 D ATOM 3121 C4 DTI D 7 72.820 7.226-2. 166 1. 00 97. 68 D ATOM 3122 C5 DTI D 7 71.485 7.283-1. 424 1. 00 94. 46 D ATOM 3123 C6 DTI D 7 71.371 8.220-0. 2251. 0089. 40 D ATOM 3124 C7 DTI D 7 70.225 7.953 0.746 1. 00 86. 05 D ATOM 3125 C8 DTI D 7 69.996 8.956 1.870 1. 00 86. 12 D ATOM 3126 C9 DTI D 7 69.760 8.402 3.274 1. 00 85. 94 D ATOM 3127 C10 DTI D 7 68.882 9.219 4.213 1. 00 84. 41 D ATOM 3128 C11 DTI D 7 68.448 8.573 5.526 1. 00 84. 95 D ATOM 3129 C12 DTI D 7 67.089 8.990 6. 100 1.00 85. 47 D ATOM 3130 C13 DTI D 7 66.608 8.276 7. 366 1.00 85. 28 D ATOM 3131 C14 DTI D 7 65.111 8.265 7.674 1. 00 80. 47 D ATOM 3132 C15 DTI D 7 64.698 8.019 9. 1241. 0077. 01 D ATOM 3133 C16 DTI D 7 63.275 8.346 9. 5291. 0072. 98 D END Supplementary Information-Statistics for data collection and refinement Data Collection CDlb/GM2 CDlb/PI Resolution range (A) 100-2.8 25-2.2 Completeness (%) (outer) 88.8 (71.1) 92.3 (89.8) Total observations 89500 334867 Unique reflections 13203 27623 Average I/a (I) 13.7 (1.8) 39.1 (15.8) (outer) Rmerge (%) (outer) 10.3 (32.5) 5.1 (20.6) Model refinement CDlb/GM2 CDlb/PI Maximum resolution 2.80 2.26 Number of reflections 12383/535 24656/751 (working set/test set) Rwork/Rfree (%) 22.4/27. 5 20.3/23. 3 r. m. s deviations from standard stereochemistry Bonds (A) 0.012288 0.007716 Angles (°) 1. 72965 1.47377 Number of atoms Protein 3000 3005 Ligand (s) 85 90 Waters 40 232 NO3 0 12 Ramachandran plot Most favoured (%) 88. 5 89.4 Additional (%) 11.2 9.3 Generous (%) 0.3 1. 2 Disallowed (%) 0 0 Values in parentheses refer to the highest resolution shells (the outer shell is between 2. 91-2.80Å and between 2.28-2. 20Å for the CDlb/GM2 the CDlb/PI data respectively). , E. Ej')- ()) ! R where Ii (h) is the ith measurement of reflection h and (I (h)) is the weighted mean of all measurements of h. V F F R= Eh IFobs-Fcalc I Eh obs where Fobs and Fcaic are the observed and calculated structure factor amplitudes respectively. Rwork and Rcryst were calculated using the working and test set, respectively.