WO2007039761A2 - Crystal structure of cd44 and its use - Google Patents

Abstract

The invention provides the crystal structure of the CD44 protein molecule. The structure is set out in Tables 1 to 4. The structure may be used in to model the interaction of compounds such as pharmaceuticals with this protein, and to determine the structure of related molecules.

Description

CRYSTAL STRUCTURE OF CD44 AND ITS USE

Field of the Invention.

The present invention relates to the crystal structure of a co-complex of the protein CD44 and hyaluronan (HA), and uses thereof.

Background to the Invention.

The hyaluronan receptor CD44 mediates cell adhesion and migration through pericellular matrix during the processes of embryonic morphogenesis and leukocyte homing. It has become increasingly clear that such interactions are particularly important to the pathology of inflammation and cancer and consequently CD44 is an attractive target for therapeutic drug development. However, the precise molecular details of the CD44-ligand interaction are currently unknown. It has previously been shown that the HA-binding domain comprises an extended form of the C-type lectin like Link module in which C- and N-terminal extensions form an additional structural lobe that is obligatory for ligand-binding.

The making and breaking of multiple weak binding interactions between cells and components of the extracellular matrix permits migration within the tissues during such diverse processes as embryonic morphogenesis, wound healing and inflammatory tissue homing (1 , 2) One ubiquitous component of the matrix that is central to these processes is the glycosaminoglycan hyaluronan, a high molecular weight co-polymer of N-acetylglusoamine and glucuronic acid (GlcNAcβi -4GIcUA)_n whose hygroscopic properties maintain low resistance pathways for cell movement in mesenchymal and other tissues. Unlike other glycosaminoglycans, hyaluronan is not covalently attached to a polypeptide core but exists as an independent non-branched polysaccharide that associates non-covalently with large matrix proteoglycans of the Link protein superfamily such as aggrecan, versican and link protein in the extracellular matrix. The interaction of cells with these protein-bound HA complexes and their subsequent migration is mediated primarily by the CD44 molecule, the major transmembrane receptor of the Link protein superfamily.

In addition to playing a general role in adhesion/migration, the CD44 molecule functions as a tissue homing receptor on inflammatory leukocytes. Functionally silent on resting leukocytes, CD44 becomes competent to bind HA after prior activation by pro-inflammatory cytokines (3-5). Thus, discrete populations of cells in peripheral blood are directed to extravasate at inflammatory sites, where they are thought to "roll" on HA displayed on the luminal surface of activated endothelial cells prior to transmigration (see eg. (3)). Moreover, the critical role of CD44 in inflammation has been confirmed in numerous animal models of disease including collagen-induced arthritis (6), experimental autoimmune encephalomyelitis, autoimmune diabetes (7) and pulmonary eosinophilia (8), where the development of inflammation was shown to be delayed by administration of CD44 function-blocking antibodies. The mechanism by which CD44 is activated to bind HA is not yet known, although evidence suggests that it involves re-modelling of N-Linked sugar chains within the CD44 HA-binding domain by means of a membrane associated sialidase activity (9-13). More recently, CD44 was shown to be functionally associated in leukocytes with another homing receptor, the α4β1 integrin VLA-4 - a ligand for the adhesion molecule VCAM-1 that mediates firm adhesion of lymphocytes and monocytes in inflamed vessel endothelium (14). CD44-mediated rolling on HA may therefore precede stable adhesion to endothelium via VLA-4/VCAM-1 in much the same way as selectin- mediated rolling on mucins. In light of its critical role in inflammation α4 integrin is currently a major target for antibody-based drug therapy. Likewise, CD44 represents an attractive target for antibody therapy. However, given the relatively simple structure of its carbohydrate ligand hyaluronan, CD44 would seem particularly suited to structure-based anti-inflammatory drug design.

The polypeptide domain that mediates protein-HA interactions is the so-called Link module (15), a conserved unit of approximately 100 residues, comprising two antiparallel β-sheets made from a total of six individual β strands (β1- β6) and two short α-helices that form a beta- fold, stabilized by two highly conserved disulfide bridges. Present either as a single unit, or as a tandem repeat in different members of the Link superfamily, the link module is structurally related to the carbohydrate-binding fold in C-type lectins, although the two gene families share no significant amino acid sequence homology (16). In the inflammation-associated protein TSG-6, a single copy of the consensus link module is sufficient to confer HA-binding on the molecule (17, 18). In CD44 however, the single Link module represents an elaboration of the basic consensus unit to form an enlarged and extended structure. Solved recently by a combination of NMR spectroscopy and X-ray crystallography, the CD44 HA-binding domain has the six β strands of the consensus Link module (β1-β6) extended by four additional β strands (denoted 0, 7, 8 and 9), coming from the N- and C-terminal extensions, which form a distinct structural lobe (19). Although obligatory for correct folding and ligand binding, the contribution of the extension remains unclear, the most likely possibility being that it participates in the regulation of ligand-binding affinity (20). For example the Link extension carries two of the sites for covalent attachment of N-glycan chains whose terminal sialylation blocks HA-binding, perhaps as a result of steric hindrance.

The precise molecular details of how the large hyaluronan polymer is bound within the Link module are currently unclear. Earlier studies had predicted the involvement of at least nine residues (Lys38, Arg41 , Tyr42, Lys68, Arg78, Tyr79, AsniOO, Asn101 and Tyr105) in the interaction site, based on the finding that their individual mutation to alanine either reduced or abolished HA-binding (21 , 22). More recently, these residues were shown to form a contiguous, putative binding patch on the surface of the CD44 polypeptide, dominated by a pair of tyrosine and arginine residues (R41/Y42 and R78/Y79) when their positions were plotted onto the CD44 apoprotein crystal structure (19). In addition, a further group of basic residues Lys38, Arg150, Arg154, Lys158 and Arg162 from the N- and C-terminal link extensions predicted as important for HA-binding (21) were shown to be distributed at the periphery of the binding patch, in such an orientation as to provide two possible modes for ligand interaction (19). Such models of the ligand-binding site are largely hypothetical, and yield little if any reliable information on the nature of the molecular interactions involved in HA-binding. This information is vital for an understanding of protein-HA interactions in general and for structure-based design of small molecule inhibitors of CD44 action in particular. Such knowledge would require a structure for the CD44-HA complex, yet no crystal structures of protein-HA complexes have been solved for any members of the link superfamily,

Disclosure of the Invention.

The present invention provides the co-crystallization of the murine CD44 with its ligand HA and elucidation of the 3D structure of the CD44:HA complex. This has revealed for the first time the molecular basis for HA-binding to a cell surface receptor and provides the necessary information for the development of small molecule inhibitors for the treatment of inflammatory and neoplastic diseases. In particular, it has been found that some of the predicted contact residues (Lys38, Lys68, AsniOO, Arg154, Arg158 and Arg162) do not appear to be involved in HA binding, and that others not predicted to be involved by previous studies (Cys77, Ile88, Asn94, Ile96, Cys97, Ala98 and Ala99 ) are involved in HA binding.

Another surprising feature of the present invention is the finding that the residue Arg45

(equivalent to Arg41 in human CD44) undergoes a significant conformational change during HA binding. The structure of the invention reveals this unexpected shift which was not predicted from the previous apo structure of human CD44.

We have also found that the binding groove for HA is surprisingly shallow and that the interactions between CD44 and HA are predominantly hydrogen bonds rather than ionic. The unusual nature of the binding groove in CD44 may therefore have evolved to permit weak engagement with ligand, consistent with the role of the receptor in making reversible low affinity interactions with large HA polymers during cell migration.

Thus the present invention relates to the crystal structure of a co-complex of CD44 and HA, which has identified novel interactions between HA and the CD44 receptor.

More particularly, the present inventors have obtained a novel co-crystal of CD44 with HA which is useful for the provision of atomic co-ordinate models of this protein. The models may be used in modelling the interaction of ligands with CD44, e.g. in the development of novel CD44-binding molecules or in the development or modification of existing CD44-binding molecules.

In a further aspect, the invention provides a three dimensional structure of CD44 set out in Tables 1 2, 4 or 5, and uses of these as well as the CD44 structure of Table 3.

In another aspect, the novel findings may be used to model the interaction of HA, and other ligands or potential ligands, to other protein structures which contain a Link module domain.

These and other aspects and embodiments of the present invention are discussed below. Brief Description of the Tables

Table 1 provides the co-ordinate data of the form A co-crystal of mouse CD44, in complex with HA.

Table 2 provides the co-ordinate data of the form B co-crystal of mouse CD44, in complex with HA.

Table 3 provides an apo structure of human CD44.

Table 4 provides a model of form B co-crystal of human CD44, in complex with HA. Table 5 provides a homology model of Lyve-1 , derived from the structure of Table 1. Table 6 sets out the atoms of the contact residues involved in HA-binding.

Brief Description of the Drawings

Figure 1. Alignment of Mouse CD44 1-183 (SEQ ID NO:1) vs. Human CD44 1-178 (SEQ ID NO:2) vs. LYVE-1 29-142 (SEQ ID NO:3). Residues of these molecules in the present specification are referred to by the numbering shown in this Figure.

Detailed Description of the Invention

A. Protein Crystals.

The present invention provides a CD44-HA co-crystal having a P2i space group, and unit cell dimensions of: a=30.8A, 6=82.1 A, c=32.3A, α=90.0°, β=117.9°, γ=90.0° ; or a=30.8A, ό=82.1 A, c=32.4A, α=90.0°, β=118.0°, γ=90.0° In either case, unit cell variability of 5% may be observed in all dimensions.

Such a co-crystal may be obtained using the methods described in the accompanying examples.

The invention thus further provides a CD44-HA co-crystal having a resolution of at least 1.3 A.

B. Crystal Co-ordinates. In a further aspect, the invention also provides a co-crystal of CD44-HA having the three- dimensional atomic co-ordinates of Table 1 or 2.

An advantageous feature of the structures defined by the atomic co-ordinates of Table 1 and 2 is that they have a resolution of about 1.3A, allowing resolution of the contacts between HA and residues of the CD44 to be resolved and identified.

Tables 1 and 2 give atomic co-ordinate data for the A and B forms of the co-crystal of CD44- HA. In Tables 1 and 2 the third column denotes the atom, the fourth the residue type, the fifth the chain identification (in this case, chain A for CD44 and C for the HA), the sixth the residue number, the seventh, eighth and ninth columns are the X, Y, Z co-ordinates respectively of the atom in question, the tenth column the occupancy of the atom, the eleventh the temperature factor of the atom, the twelfth the atom type. Ligand and solvent molecules are also included in the Table, the former as "C" chain atoms.

Table 3 provides atomic co-ordinate data for human CD44. This is pdb file 1 UUH. This is in a similar format to Table 1 , though comprises two copies of the CD44 protein, designated A chain and B chain. Solvent molecules are given chain identifiers to indicate the protein chain to which they are most closely associated with, where A chain solvent molecules are designated Z and B chain solvent molecules are designated Y. Reference to Table 3, selected co-ordinates thereof, or to the use of Table 3 or selected co-ordinates thereof, will be understood to refer to the use of either or both of the A or B chain. Where selected coordinates are used, the selected coordinates preferably will be derived from the same chain.

Table 4 provides a model of the human CD44 generated (see below) from the structure of Table 2, and is in a similar format to that Table.

Table 5 provides a homology model containing the Link domain of LYVE-1 (residues 29-146).

Tables 1 to 5 are set out in internally consistent formats. For example, in Tables 1, 2 and 4 the co-ordinates of the atoms of each amino acid residue are listed such that the backbone nitrogen atom is first, followed by the C-alpha backbone carbon atom, designated CA, followed by side chain residues (designated according to one standard convention) and finally the carbon and oxygen of the protein backbone. In Tables 3 and 5 the carbonyl (C and O) atoms precede the side chain atoms. Thus any suitable standard file format (e.g. such as a format consistent with that of the EBI Macromolecular Structure Database (Hinxton, UK)) which may include a different ordering of these atoms, or a different designation of the side-chain residue atoms, may be used or preferred by others of skill in the art. However it will be apparent that the use of a different file format to present or manipulate the co-ordinates of the Table is within the scope of the present invention.

The co-ordinates of Tables 1 to 5 provide a measure of atomic location in Angstroms, to 3 decimal places. The co-ordinates 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 structures of Table 1 to 5 by a root mean square deviation of less than 1.5 A, preferably less than 1.0 A₁ more preferably less than 0.5 A, and most preferably less than 0.2 A, will generally result in a structure which is substantially the same as the structure of Tables 1 to 5 respectively in terms of both structural characteristics and usefulness for structure-based analysis of CD44-interacting molecular structures.

Likewise the skilled person would understand that changing the number and/or positions of the sugar or water molecules of Tables 1 to 5 will not generally affect the usefulness of the structure for structure-based analysis of CD44-interacting structures. 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 to 5 co-ordinates 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 from Table 1 to 5 is less than 1.5 A, preferably less than 1.0 A, more preferably less than 0.5 A, and most preferably less than 0.2 A; and/or the number and/or positions of sugar or water molecules is varied.

Reference herein to the co-ordinate data of Tables 1 to 5 and the like thus includes the coordinate data in which one or more individual values of the Table are varied in this way. In particular, reference to an rmsd of less than 1.5 A will be understood to include reference to the above, smaller, preferred values.

Protein structure similarity is routinely expressed and measured by the root mean square deviation (rmsd), i.e. the square root of the arithmetic mean of the squares of the deviations from the mean. This measures the difference in positioning in space between two sets of equivalent atoms after their optimal superposition. The rmsd can be calculated over all atoms, over residue backbone atoms (i.e. the nitrogen-carbon-carbon backbone atoms of the protein amino acid residues), main chain atoms only (i.e. the nitrogen-carbon-oxygen-carbon backbone atoms of the protein amino acid residues), side chain atoms only or more usually over C-alpha atoms only. For the purposes of this invention, the rmsd can be calculated over any of these, using any of the methods outlined below. Preferably, the calculation is performed over all the atoms.

Methods of comparing protein structures are discussed in Methods of Enzymology, vol 115, pg 397-420. The necessary least-squares algebra to calculate rmsd has been given by Rossman and Argos (J. Biol. Chem., vol 250, pp7525 (1975)) although faster methods have been described by Kabsch (Acta Crystallogr., Section A, A92, 922 (1976)); Acta Cryst. A34, 827-828 (1978)), Hendrickson (Acta Crystallogr., Section A, A35, 158 (1979)); McLachan (J. MoI. Biol., vol 128, pp49 (1979)) and Kearsley (Acta Crystallogr., Section A, A45, 208 (1989)). Some algorithms use an iterative procedure in which the one molecule is moved relative to the other, such as that described by Ferro and Hermans (Ferro and Hermans, Acta Crystallographic, A33, 345-347 (1977)). Other methods e.g. Kabsch's algorithm locate the best fit directly.

Programs for determining rmsd include MNYFIT (part of a collection of programs called COMPOSER, Sutcliffe, M.J., Haneef, L₁ Carney, D. and Blundell, T.L. (1987) Protein Engineering, 1 , 377-384), MAPS (Lu, G. An Approach for Multiple Alignment of Protein Structures (1998, in manuscript and on http://bioinfo1.mbfys.lu.se/TOP/maps.html)).

Rmsd can also be calculated using programs such as LSQKAB (Collaborative Computational Project 4. The CCP4 Suite: Programs for Protein Crystallography, Acta Crystallographies, D50, (1994), 760-763), QUANTA (Jones et al., Acta Crystallography A47 (1991), 110-119 and commercially available from Accelerys, San Diego, CA), Insight (commercially available from Accelerys, San Diego, CA), Sybyl® (commercially available from Tripos, Inc., St Louis), O (Jones et al., Acta Crystallographica, A47, (1991), 110-119), and other co-ordinate fitting programs.

In₁ for example the programs LSQKAB and O, the user can define the residues in the two proteins that are to be paired for the purpose of the calculation. The atomic co-ordinates can then be superimposed according to this alignment and an rmsd value calculated. The program Sequoia (CM. Bruns, I. Hubatsch, M. Ridderstrόm, B. Mannervik, and J.A. Tainer (1999) Human Glutathione Transferase A4-4 Crystal Structures and Mutagenesis Reveal the Basis of High Catalytic Efficiency with Toxic Lipid Peroxidation Products, Journal of Molecular Biology 288(3): 427-439) performs the alignment of homologous protein sequences, and the superposition of homologous protein atomic co-ordinates.

Those of skill in the art will appreciate that in many applications of the invention, it is not necessary to utilise all the co-ordinates of Tables 1 to 5, but merely a portion of them, provided said portion include at least one atom from an amino acid residue involved in HA binding. For example, as described below, in methods of modelling candidate compounds with ligands, selected co-ordinates of CD44 or LYVE-1 may be used, and in particular the selected coordinates may include one or more atoms from one or more of the amino acid residues newly identified herein as interacting with HA.

In general, "selected co-ordinates" means for example at least 5, preferably at least 10, more preferably at least 50 and even more preferably at least 100, for example at least 500 or at least 1000 atoms of the CD44 structure, or other structures referred to herein. Reference herein to selected co-ordinates in all the various applications of the invention described herein is to be understood as including these preferred numbers of such co-ordinates.

In the case of the structure of Table 1or 2, the selected co-ordinates preferably include at least one atom from the amino acids in the group consisting of Arg45, Tyr46, Cys81 , Arg82, Tyr83, Ile92, Asn98, Ile100, Cys101 , Ala102, Ala103, His105, Tyr109 and Arg155. In the A form, e.g. that having the Table 1 structure, the residues Arg45 and Arg155 do not appear to make direct ligand contact. However, in the B form (Table 2 structure) the position of Arg45 is significantly shifted and thus appears to have an important role in the ligand-binding process. Thus both residues, and particularly Arg45, may be included in the selected co-ordinates. However, it is generally preferred that where said at least one atom from the above-mentioned group is from Arg45 or Arg155, then at least a second atom of another amino acid is also selected. Reference to the above-mentioned group is to be construed accordingly throughout this disclosure.

Preferably, the selected co-ordinates include at least one atom from at least one of Cys81 , Ile92, Asn98, HeIOO, Cys101 , Ala102 and Ala103 such as at least one atom from Cys81 ,

HeIOO, Cys101 , Ala102 and Ala103. More preferably, the selected co-ordinates include at least one atom from at least one of Cys81 , Ile92, Asn98, HeIOO₁ Cys101 , Ala102 and Ala103, preferably from at least one of Cys81 , lle100, Cys101 , Ala102 and Ala103, together with at least one atom of a second residue selected from Arg45, Tyr46, Cys81 , Arg82, Tyr83, Ne92, Asn98, HeIOO, Cys101 , Ala102, Ala1 O3, His105, Tyr109 and Arg155, particularly Arg45.

In another preferred embodiment, when the selected co-ordinates include at least one atom from the group of residues Cys81 , Ile92, Asn98, IleiOO, Cys101 , Ala102 and Ala103, and more preferably from the group of residues Cys81 , IleiOO, Cys101 , Ala102 and Ala103, the selected co-ordinates include at least one atom from at least 2, such as at least 3, more preferably at least 4, even more preferably at least 5 and most preferably all amino acids of these preferred groups. More preferably, the selected co-ordinates comprise at least 10, more preferably 25, more preferably 50 atoms from these groups of residues wherein at least one atom is from each member of the group.

In one aspect, the coordinate data of Table 2 or selected coordinates thereof are preferred, particularly wherein said coordinates include one or more from the group of residues Cys81 , Ile92, Asn98, Ile100, Cys101 , AIaI 02 and AIaI 03 together with one or more Arg45 atoms.

In the case of the structure of Table 3 or 4, the selected co-ordinates preferably include at least one atom from the amino acids in the group consisting of Arg41 ,Tyr42, Cys77, Arg78, Tyr79, lleδδ, Asn94, Ile96, Cys97, Ala98, Ala99, Asn101 , TyM 05 and Arg150. As with the mouse structure, Arg41 may be included in the selected co-ordinates. However, it is generally preferred that where said at least one atom from the above-mentioned group is from Arg41 or Arg150, then at least a second atom of another amino acid is also selected. Reference to the above-mentioned group is to be construed accordingly throughout this disclosure.

More preferably, the selected co-ordinates include at least one atom from at least one of Cys77, Ile88, Asn94, Ne96, Cys97, Ala98 and Ala99 such as at least one atom from Cys77, Ne96, Cys97, Ala98 and Ala99. More preferably, the selected co-ordinates include at least one atom from at least one of Cys77, lleδδ, Asn94, Ile96, Cys97, Ala98 and Ala99 , preferably from at least one of Cys77, Ile96, Cys97, Ala98 and Ala99, together with at least one atom of a second residue selected from Arg41 ,Tyr42, Cys77, Arg78, Tyr79, lleδδ, Asn94, Ile96, Cys97, Ala9δ, Ala99, Asn101 , TyM 05 and Arg150.

In another preferred embodiment, when the selected co-ordinates include at least one atom from the group of residues Cys77, lleδδ, Asn94, Ile96, Cys97, Ala98 and Ala99 , and more preferably from the group of residues Cys77, Ile96, Cys97, Ala98 and Ala99, the selected coordinates include at least one atom from at least 2, such as at least 3, more preferably at least 4, even more preferably at least 5 and most preferably all amino acids of these preferred groups. More preferably, the selected co-ordinates comprise at least 10, more preferably 25, more preferably 50 atoms from these groups of residues wherein at least one atom is from each member of the group.

Thus reference herein to selected co-ordinates of Table 3 or 4 includes the above preferred combinations of selected co-ordinates, generally derived, in the case of Table 3, either from the A chain or from the B chain of the structure. The above-mentioned selected co-ordinates are preferred as co-ordinates to be fitted to a ligand structure.

In one aspect, the coordinate data of Table 4 or selected coordinates thereof are preferred, particularly wherein said coordinates include one or more from the group of residues Cys77, Ile88, Asn94, Ile96, Cys97, Ala98 and Ala99 together with one or more Arg41 atoms.

Our new HA-binding model also has provided a detailed analysis of the precise atoms of CD44 involved in HA binding. These atoms are set out in Table 6 below: Table 6

Accordingly, in another preferred aspect, when the selected co-ordinates include one or more coordinates of any one of the amino acids set out in Table 6, the co-ordinate is, or includes, the specific atom of column 3 Table 6. Thus reference herein to the use of co-ordinates of any one of the residues set out in Table 6, either singly or in combination with other co-ordinates, will be understood, in a preferred aspect, to include the use of the co-ordinates of the specific atom(s) of Table 6, for example of 2 or more, such as 4 or more, for example from 6 to 12 atoms of Table 6. Other co-ordinates of the same residue may also be used at the same time.

In the case of Table 5, our data of HA binding to CD44, in conjunction with our mutagenesis studies, has allowed identification of residues involved in HA biding in this protein. This will facilitate the use of the structure of Table 5 for the development of ligands for LYVE-1. Thus, for Table 5 the selected coordinates include at least one atom from Cysδδ, Tyr87, Arg99, Asn103, Lys105, Cys106, Gly107, LysiOδ and Trp116. More preferably the selected coordinates include at least one atom from at least one of Cysδδ, Lys105, Cys106, Gly107 and Lys108. More preferably, the selected co-ordinates include at least one atom from at least one of Cysδδ, LysiOδ, Cys106, Gly107 and Lys108, together with at least one atom of a second residue selected from Cysδδ, Tyrδ7, Arg99, Asn103, LysiOδ, Cys106, Gly107, LysiOδ and Trp116. In another preferred embodiment, when the selected co-ordinates include at least one atom from the group of residues Cys85, Lys105, Cys106, Gly107 and Lys108, the selected coordinates include at least one atom from at least one atom from at least 2, such as at least 3, more preferably at least 4 amino acids of this group. More preferably, the selected coordinates comprise at least 10, more preferably 25, more preferably 50 atoms from these groups of residues wherein at least one atom is from each member of the group.

Thus reference herein to selected co-ordinates of Table 5 includes the above preferred combinations of selected co-ordinates. The above-mentioned selected co-ordinates are preferred as co-ordinates to be fitted to a ligand structure.

Thus reference herein to selected co-ordinates of any of Tables 1 to 5 includes the above preferred combinations of selected co-ordinates. The above-mentioned selected co-ordinates are preferred as co-ordinates where at least one of which is to be fitted to a ligand structure.

C. Computer Systems.

In another aspect, the present invention provides systems, particularly a computer system, the systems containing the atomic co-ordinate data of the of any one of Tables 1 to 5, or selected co-ordinates thereof, in particular the combinations and groups referred to above.

For example the computer system may comprise: (i) a computer-readable data storage medium comprising data storage material encoded with the computer-readable data; (ii) a working memory for storing instructions for processing said computer-readable data; and (iii) a central- processing unit coupled to said working memory and to said computer-readable data storage medium for processing said computer-readable data and thereby generating structures and/or performing rational drug design. The computer system may further comprise a display coupled to said central-processing unit for displaying said structures.

Such data is useful for a number of purposes, including the generation of structures to analyse the mechanisms of action of CD44 or LYVE-1 and/or to perform rational drug design of compounds, which interact with CD44 or LYVE-1.

In a further aspect, the present invention provides computer system containing computer- readable data comprising atomic co-ordinate data of Tables 1 , 2, 4 or 5 optionally varied by a rmsd of less than 1.5A or selected co-ordinates thereof. Preferably said selected co-ordinates include at least one atom from the amino acids Arg45, Tyr46, Cys81 , Arg82, Tyr83, Ile92, Asn98, HeIOO₁ Cys101 , Ala102, Ala103, His105, TyM 09 and Arg 155 in the case of Table 1 or 2, at least one atom from the amino acids Arg41 ,Tyr42, Cys77, Arg78, Tyr79, Ile88, Asn94, Ile96, Cys97, Ala98, Ala99, Asn101 , TyM 05 and Arg 150 in the case of Table 4, or at least one atom from the amino acids Cys85, Tyr87, Arg99, Asn103, Lys105, Cys106, Gly107, Lys108 and Trp116 in the case of Table 5. More preferred selected co-ordinates are those particular combinations and groups referred to above. In another aspect, the invention provides a computer-readable storage medium, comprising a data storage material encoded with computer readable data, wherein the data are defined atomic co-ordinate data of Table 1 or 2 optionally varied by a rmsd of less than 1.5A or selected co-ordinates thereof. Preferably said selected co-ordinates include at least one atom from the amino acids Arg45, Tyr46, Cys81 , Arg82, Tyr83, Ile92, Asn98, MeIOO, Cys101 , Ala102, Ala103, His105, Tyr109 and Arg155. More preferred selected co-ordinates are those particular combinations and groups referred to above.

In another aspect, the invention provides a computer-readable storage medium, comprising a data storage material encoded with computer readable data, wherein the data are defined atomic co-ordinate data of Table 4 optionally varied by a rmsd of less than 1.5A or selected coordinates thereof. Preferably said selected co-ordinates include at least one atom from the amino acids Arg41 ,Tyr42, Cys77, Arg78, Tyr79, Ile88, Asn94, Ile96, Cys97, Ala98, Ala99, Asn101 , Tyr105 and Arg150. More preferred selected co-ordinates are those particular combinations and groups referred to above.

In another aspect, the invention provides a computer-readable storage medium, comprising a data storage material encoded with computer readable data, wherein the data are defined atomic co-ordinate data of Table 5 optionally varied by a rmsd of less than 1.5A or selected co- ordinates thereof. Preferably said selected co-ordinates include at least one atom from the amino acids Cys85, Tyr87, Arg99, Asn103, Lys105, Cys106, Gly107, Lys108 and Trp116. More preferred selected co-ordinates are those particular combinations and groups referred to above.

As used herein, "computer readable media" refers to any medium or media, which can be read and accessed directly by a computer. Such media include, but are not limited to: magnetic storage media such as floppy discs, hard disc storage medium and magnetic tape; optical storage media such as optical discs or CD-ROM; electrical storage media such as RAM and ROM; and hybrids of these categories such as magnetic/optical storage media.

By providing such computer readable media, the atomic co-ordinate data derived from the Tables mentioned above can be routinely accessed to model CD44 or selected co-ordinates thereof. For example, RASMOL (Sayle et al., TIBS, Vol. 20, (1995), 374) is a publicly available computer software package, which allows access and analysis of atomic co-ordinate data for structure determination and/or rational drug design.

As used herein, "a computer system" refers to the hardware means, software means and data storage means used to analyse the atomic co-ordinate data derived from any one of Tables 1 , 2, 4 or 5 or selected co-ordinates thereof. The minimum hardware means of the computer- based systems of the present invention comprises a central processing unit (CPU), input means, output means and data storage means. Desirably a monitor is provided to visualize structure data. The data storage means may be RAM or means for accessing computer readable media of the invention. Examples of such systems are microcomputer workstations available from Silicon Graphics Incorporated and Sun Microsystems running Unix based or Windows XP operating systems.

The invention also provides a computer-readable data storage medium comprising a data storage material encoded with a first set of computer-readable data comprising any one of

Tables 1 , 2, 4 or 5 or selected co-ordinates thereof; which, when combined with a second set of machine readable data comprising an X-ray diffraction pattern of a Link module domain protein of unknown structure, particularly in the form of a co-complex with HA, using a machine programmed with the instructions for using said first set of data and said second set of data, can determine at least a portion of the electron density corresponding to the second set of machine readable data.

A further aspect of the invention provides a method of providing data for generating structures and/or performing rational drug redesign with CD44, CD44 homologues or analogues, complexes of CD44 with a compound, or complexes of CD44 homologues or analogues with compounds, the method comprising:

(i) establishing communication with a remote device containing computer-readable data comprising the structure of any one of Tables 1 to 4 optionally varied by a rmsd of less thani .5A or selected co-ordinates thereof; and (ii) receiving said computer-readable data from said remote device.

In the case of Table 1 or 2 said selected co-ordinates preferably include at least one atom from the amino acids Arg45, Tyr46, Cys81 , Arg82, Tyr83, Ile92, Asn98, IleiOO, Cys101 , Ala102, Ala103, His105, Tyr109 and Arg155 and in the case of Table 3 or 4 said selected coordinates include at least one atom from the amino acids Arg41 ,Tyr42, Cys77, Arg78, Tyr79, Ne88,

Asn94, Ile96, Cys97, Ala98, Ala99, Asn101 , Tyr105 and Arg150. The particular combinations and groups of selected co-ordinates referred to above are preferred in each case.

The invention also provides a method of providing data for generating structures and/or performing rational drug redesign with LYVE-1 , LYVE-1 homologues or analogues, complexes of LYVE-1 with a compound, or complexes of LYVE-1 homologues or analogues with compounds, the method comprising:

(i) establishing communication with a remote device containing computer-readable data comprising the structure of Table 5 optionally varied by a rmsd of less thani .5A or selected co- ordinates thereof; and

(ii) receiving said computer-readable data from said remote device.

The selected co-ordinates preferably include at least one atom from the amino acids Cys85, Tyr87, Arg99, Asn103, Lys105, Cys106, Gly107, Lys108 and Trp116. The particular combinations and groups of selected co-ordinates referred to above are preferred.

Thus the remote device may comprise e.g. a computer system or computer readable media of one of the previous aspects of the invention. The device may be in a different country or jurisdiction from where the computer-readable data is received. The communication may be via the internet, intranet, e-mail etc, transmitted through wires or by wireless means such as by terrestrial radio or by satellite. Typically the communication will be electronic in nature, but some or all of the communication pathway may be optical, for example, over optical fibres.

The data received may then be used in a computer-based method for the analysis of the interaction of a ligand with CD44 or LYVE-1 , said method as being further defined herein.

D. Link module domain structures.

The data of the present invention allows the provision of further Link module domain-containing protein structures which may be used in the same manner as the murine CD44 structure described herein. In particular, the identification of novel HA-binding residues allows the existing structure of human CD44 (Table 3) to be analysed and used for the development of ligands as described herein. Further, the invention also allows the present data has provided a model of LYVE-1 in which the HA-binding pocket may be determined by reference to the data provided herein.

E. Uses of the Structures of the Invention. The crystal structure of the present invention as well as the structures of other Link module domain containing proteins, may be used in several ways for drug design, based on the novel interactions defined by the structures of Tables 1 to 5.

In the case where the interaction of a ligand with CD44 protein or another Link module domain containing protein structure is to be analysed, by either co-crystallization, soaking or computationally docking the binding orientation of the ligand in the binding pocket, interactions of the ligand with the protein can be determined. This will guide specific modifications to the chemical structure designed to mediate or control the interaction of the drug with the protein. Such modifications can be designed with an aim to improve the interaction of existing drugs with the protein, or for the development of new drugs.

Our finding that the protein-carbohydrate interactions that bind the HA octasaccharide in CD44 are dominated by H-bonds rather than hydrophobic or electrostatic interactions is unusual and had not been expected. In general, receptor-ligand complexes that are dominated by ionic interactions represent poor targets for therapeutic interaction: complementary charges in candidate drugs often make for poor bioavailability. Thus in those aspects of the invention which relate to the fitting of ligands to the structures of Tables 1 to 5, fitting ligands via hydrogen bonds and non polar interactions (such as hydrophobic interactions) may be performed. Alternatively, or subsequent to such H-bond-based fitting, optimizing the binding of a lead compound can be pursued by targeting polar and hydrophobic interactions instead.

The small structural core to the CD44-HA interaction increases the chances of obtaining a low molecular weight antagonist. In addition, the deviation of the bound HA oligosaccharide from its preferred conformation might be exploited in inhibitor design by selecting chemical entities that already have a conformational preference towards the constrained state seen in the HA-CD44 complex.

Thus the structure of the CD44-HA complex disclosed herein will allow the design of a pharmacophore for in silico screening of chemical libraries to obtain small molecule inhibitors with the potential for therapy, e.g. for anti-inflammatory or anti-neoplastic therapy.

(i) In silico analysis and design Current computational techniques provide a powerful alternative to the need to generate crystals and generate and analyse diffraction date. Accordingly, a particularly preferred aspect of the invention relates to "in silico" methods directed to the analysis and development of ligands which interact with CD44 and other Link module domain containing structures of the present invention. Such in silico methods are well known in the art as such. For example, Card et a/, Nature Biotechnology, 2005, 23; 201-207 provides an illustration of how new compounds may be designed, based on in silico modifications of the binding of a low affinity starting compound which is in a co-complex crystal. Such modelling methods may be applied in the context of the present invention.

As illustrated herein, determination of the three-dimensional structure of CD44 provides important information about the HA-binding site of CD44. This information may then be used for rational design and modification of CD44 substrates and inhibitors, e.g. by computational techniques which identify possible binding ligands for the binding sites, by enabling linked- fragment approaches to drug design, and by enabling the identification and location of bound ligands using X-ray crystallographic analysis. These techniques are discussed in more detail below.

Thus as a result of the determination of the CD44-HA co-complex three-dimensional structure, more purely computational techniques for rational drug design may also be used to design structures whose interaction with CD44 is better understood (for an overview of these techniques see e.g. Walters et al (Drug Discovery Today, Vol.3, No.4, (1998), 160-178; Abagyan, R.; Totrov, M. Curr. Opin. Chem. Biol. 2001 , 5, 375-382). For example, automated ligand-receptor docking programs (discussed e.g. by Jones et al. in Current Opinion in Biotechnology, Vol.6, (1995), 652-656 and Halperin, I.; Ma, B.; Wolfson, H.; Nussinov, R. Proteins 2002, 47, 409-443), which require accurate information on the atomic co-ordinates of target receptors may be used.

The aspects of the invention described herein which utilize the CD44 structure in silico may be equally applied to both the CD44 structure from the data of Table 1 or 2, or selected co- ordinates thereof and the models of target Link module domain-containing proteins obtained by other aspects of the invention. Thus having determined a conformation of a protein by the method described above, such a conformation may be used in a computer-based method of rational drug design as described herein. In addition the availability of the structure of the CD44 structure will allow the generation of highly predictive pharmacophore models for virtual library screening or compound design.

Accordingly, the invention provides a computer-based method for the analysis of the interaction of a ligand with CD44, which comprises: providing the CD44 structure of Table 1 or 2 optionally varied by a rmsd of less than 1 ,5A or selected co-ordinates thereof; providing a ligand structure to be fitted to said CD44 structure or selected co-ordinates thereof; and fitting the ligand structure to said CD44 structure, wherein said ligand structure is fitted to at least one atom from the amino acids Arg45, Tyr46, Cys81 , Arg82, Tyr83, Ile92, Asn98, IleiOO, Cys101 , Ala102, Ala103, His105, Tyr109 and Arg155. More preferred selected coordinates are those particular combinations and groups referred to above.

The invention also provides a computer-based method for the analysis of the interaction of a ligand with CD44, which comprises: providing the CD44 structure of Table 3 or 4 optionally varied by a rmsd of less than 1.5A or selected co-ordinates thereof; providing a ligand structure to be fitted to said CD44 structure or selected co-ordinates thereof; and fitting the ligand structure to said CD44 structure, wherein said ligand structure is fitted to at least one atom from the amino acids Arg41 ,Tyr42, Cys77, Arg78, Tyr79, Ile88, Asn94, Iie96, Cys97, Ala98, Ala99, Asn101, Tyr105 and Arg150. More preferred selected co-ordinates are those particular combinations and groups referred to above.

The invention further provides a computer-based method for the analysis of the interaction of a ligand with LYVE-1 , which comprises: providing the LYVE-1 structure of Table 5 optionally varied by a rmsd of less than 1.5A or selected co-ordinates thereof; providing a ligand structure to be fitted to said LYVE-1 structure or selected coordinates thereof; and fitting the ligand structure to said LYVE-1 structure, wherein said ligand structure is fitted to at least one atom from the amino acids Cys85, Tyr87, Arg99, Asn103, Lys105, Cys106, GIy 107, Lys108 and Trp116. More preferred selected co-ordinates are those particular combinations and groups referred to above.

In practice, it will be desirable to model a sufficient number of atoms of the CD44 or LYVE-1 structure which represent a HA-binding pocket, e.g. the atoms of the residues identified in the accompanying examples.

In order to provide a three-dimensional structure of ligands to be fitted to a CD44 or LYVE-1 structure of the invention, the ligand structure may be modelled in three dimensions using commercially available software for this purpose or, if its crystal structure is available, the co- ordinates of the structure may be used to provide a representation of the ligand for fitting to a CD44 structure of the invention.

The HA binding pocket of CD44 molecules are of a size which can accommodate more than one ligand. In any event, the findings of the present invention may be used to examine or predict the interaction of two or more separate molecular structures within the CD44 binding pocket of the invention.

Thus the invention provides a computer-based method for the analysis of the interaction of two ligand structures within a CD44 or LYVE-1 binding pocket structure, which comprises: providing the structure of any one of Tables 1 to 5 or selected co-ordinates thereof; providing a first ligand structure; fitting the first ligand structure to said CD44 or LYVE-1 structure; providing a second ligand structure; and fitting the second ligand structure to a different part said CD44 or LYVE-1 structure.

Optionally the method of analysis further comprises providing a third ligand structure and also fitting that structure to the CD44 or LYVE-1 structure. Indeed, further ligand structures may be provided and fitted in the same way.

Following the fitting of the ligand structures, a person of skill in the art may seek to use molecular modelling to determine to what extent the structures interact with each other (e.g. by hydrogen bonding, other non-covalent interactions, or by reaction to provide a covalent bond between parts of the structures) or the interaction of one structure with CD44 or LYVE-1 is altered by the presence of another structure.

The person of skill in the art may use in silico modelling methods to alter one or more of the structures in order to design new structures which interact in different ways with CD44 or LYVE-1.

Newly designed structures may be synthesised and their interaction with CD44 or LYVE-1 may be determined or predicted as to how the newly designed structure binds to CD44 or LYVE-1. This process may be iterated so as to further alter the interaction between it and the CD44 or LYVE-1.

By "fitting", it is meant determining by automatic, or semi-automatic means, interactions between at least one atom of a molecular structure and at least one atom of a CD44 or LYVE-1 structure of the invention, and calculating the extent to which such an interaction is stable. Interactions include attraction and repulsion, brought about by H-bonding, charge, steric considerations and the like. Various computer-based methods for fitting are described further herein. In all the herein described aspects of the invention, the CD44 or LYVE-1 co-ordinates to be fitted preferably include the selected co-ordinates which have been identified as interacting with HA. More specifically, the interaction of a ligand or ligands with CD44 or LYVE-1 can be examined through the use of computer modelling using a docking program such as GOLD (Jones et al., J. MoI. Biol., 245, 43-53 (1995), Jones et al., J. MoI. Biol., 267, 727-748 (1997)), GRAMM (Vakser, I.A., Proteins , Suppl., 1 :226-230 (1997)), DOCK (Kuntz et al, J.Mol.Biol. 1982 , 161, 269-288, Makino et al, J.Comput.Chem. 1997, 18, 1812-1825), AUTODOCK (Goodsell et al, Proteins 1990, 8, 195-202, Morris et al, J.Comput.Chem. 1998, 19, 1639-1662.), FlexX, (Rarey et al, J.Mol.Biol. 1996, 261, 470-489) or ICM (Abagyan et al, J.Comput.Chem. 1994, 15, 488- 506). This procedure can include computer fitting of ligands to CD44 to ascertain how well the shape and the chemical structure of the ligand will bind to the protein.

Also computer-assisted, manual examination of the active site structure of the protein may be performed. The use of programs such as GRID (Goodford, J. Med. Chem., 28, (1985), 849- 857) - a program that determines probable interaction sites between molecules with various functional groups and an enzyme surface - may also be used to analyse the active site to predict, for example, the types of modifications which will alter the rate of metabolism of a ligand.

Computer programs can be employed to estimate the attraction, repulsion, and steric hindrance of the two binding partners (i.e. a CD44 or LYVE-1 structure and a ligand).

If a plurality (e.g. two) of smaller ligands are designed or selected, a ligand may be formed by linking the respective small ligands into a larger ligand, which maintains the relative positions and orientations of the respective ligands at the active sites. The larger ligand may be formed as a real molecule or by computer modelling.

Detailed structural information can then be obtained about the binding of the ligand to CD44, and in the light of this information adjustments can be made to the structure or functionality of the ligand, e.g. to alter its interaction with the protein. The above steps may be repeated and re-repeated as necessary.

As indicated above, molecular structures, which may be fitted to the CD44 or LYVE-1 structure of the invention, include compounds under development as potential pharmaceutical agents. The agents may be useful as anti-inflammatory drugs or for other indications in which CD44 or LYVE-1 -binding to agonize or antagonize the protein activity may be beneficial.

Ligands, which may be used in the present invention, will usually be compounds under development for pharmaceutical use. Generally such compounds will be organic molecules, which are typically from about 100 to 2000 Da, more preferably from about 100 to 1000 Da in molecular weight. Such compounds include peptides and derivatives thereof, steroids, anti- inflammatory drugs, anti-cancer agents, anti-bacterial or antiviral agents, neurological agents and the like. In principle, any compound under development in the field of pharmacy can be used in the present invention in order to facilitate its development or to allow further rational drug design to improve its properties. A ligand which may be used is a pharmacophore structure comprising three positions arranged to correspond geometrically to the positions of atoms 1188, 1193 and 1196 of Table 1 or 2, or the corresponding positions in Tables 3 or 4. The atoms of the pharmacophore may also correspond chemically to the atoms at these positions, i.e. may be O, N and C respectively, though other atoms with similar chemical and/or physical properties may also be used. By "correspond geometrically" it is meant that the pharmacophore contains three atoms whose relationship in three-dimensional space (i.e. distance and angles between the atoms) is substantially the same as the distances and angles between the positions of the above- mentioned atoms.

(H) Analysis and modification ofligands

Where the ligand of CD44 or LYVE-1 of potential or actual pharmaceutical use is known, the structure of the ligand may be modelled in order to determine residues of CD44 or LYVE-1 which interact with the agent. In any event, the present invention provides a process for predicting potential pharmaceutical compounds with the potential to bind to CD44 or LYVE-1. This may be performed by designing ligands in accordance with the invention as described herein, then iterating the process, for example by: modifying the ligand structure to reduce or increase at least one interaction with the CD44 or LYVE-1 structure; and optionally further obtaining or synthesising a compound which has said ligand structure; forming a complex of a CD44 or LYVE-1 protein and said compound; and analysing said complex by X-ray crystallography to determine the ability of said compound to interact with the CD44 or LYVE-1 protein.

Modification will be those conventional in the art known to the skilled medicinal chemist, and will include, for example, substitutions or removal of groups containing residues which interact with the amino acid side chain groups of a CD44 or LYVE-1 structure of the invention. For example, the replacements may include the addition or removal of groups in order to decrease or increase the charge of a group in a test compound, the replacement of a charge group with a group of the opposite charge, or the replacement of a hydrophobic group with a hydrophilic group or vice versa. It will be understood that these are only examples of the type of substitutions considered by medicinal chemists in the development of new pharmaceutical compounds and other modifications may be made, depending upon the nature of the starting compound and its activity.

Where a potential modified compound has been developed by fitting a starting compound to the CD44 or LYVE-1 structure of the invention and predicting from this a modified compound with an altered rate of metabolism, the invention further includes the step of synthesizing the modified compound and testing it in a in vivo or in vitro biological system in order to determine its activity and/or the rate at which it is metabolised.

The above-described processes of the invention may be iterated in that the modified compound may itself be the basis for further compound design. (Hi) Fragment linking and growing.

As indicated above, where two ligands are fitted to the HA-binding region of CD44 or LYVE-1 , this will allow allow the development of compounds based on a fragment linking or fragment growing approach.

For example, the binding of one or more molecular fragments can be determined in the protein binding pocket by X-ray crystallography. Molecular fragments are typically compounds with a molecular weight between 100 and 200 Da (Carr et al, Drug Discov Today. 2002 May 1;7(9):522- 7). This can then provide a starting point for medicinal chemistry to optimise the interactions using a structure-based approach. The fragments can be combined onto a template or used as the starting point for 'growing out' an inhibitor into other pockets of the protein (Blundell et al, Nat Rev Drug Discov. 2002 Jan;1(1):45-54). The fragments can be positioned in the HA binding pocket of the CD44 or LYVE-1 and then 'grown' to fill the space available, exploring the electrostatic, van der Waals or hydrogen-bonding interactions that are involved in molecular recognition. The potency of the original weakly binding fragment thus can be rapidly improved using iterative structure-based chemical synthesis.

It is also possible that one ligand may be fitted to another domain of the CD44 or LYVE-1 protein, such that this approach is used to develop a ligand which binds both to the HA-domain and to a separate domain of the protein.

At one or more stages in the fragment growing approach, the compound may be synthesized and tested in a biological system for its activity. This can be used to guide the further growing out of the fragment.

Where two fragment-binding regions are identified, a linked fragment approach may be based upon attempting to link the two fragments directly, or growing one or both fragments in the manner described above in order to obtain a larger, linked structure, which may have the desired properties.

Where the binding site of two or more ligands are determined they may be connected to form a potential lead compound that can be further refined using e.g. the iterative technique of Greer et al. For a virtual linked-fragment approach see Verlinde et al., J. of Computer-Aided Molecular Design, 6, (1992), 131-147, and for NMR and X-ray approaches see Shuker et al., Science, 274, (1996), 1531-1534 and Stout et al., Structure, 6, (1998), 839-848.

(iv) Compounds of the invention.

Where a compound structure has been developed by fitting a starting ligand to the CD44 or LYVE-1 structure of the invention and predicting from this a modified compound with an altered biological activity, the invention further includes the step of synthesizing the compound and testing it in an in vivo or in vitro biological system in order to determine its activity, e.g. its ability to act as an agonist or antagonist of CD44 or LYVE-1. Compounds which modulate the activity of CD44 have potential use in the treatment of inflammatory diseases, such as arthritis, autoimmune diabetes and asthma/pulmonary eosinophilia.

Given the abundant expression of LYVE-1 in lymphatic endothelium and its largely restricted expression therein, it is not unlikely that the receptor fulfils an important role relating to either basic lymphatic function (e.g. fluid drainage) or immune function (e.g. dendritic cell and lymphocyte trafficking to lymph node for antigen presentation). LYVE-1 may therefore prove to be an attractive target for the development of small molecule HA-blocking drugs for potential therapy of inflammatory disease involving the lymphatic network.

In another aspect, the invention includes a compound, which is identified by the methods of the invention described above.

Following identification of such a compound, 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.

Thus, the present invention extends in various aspects not only to a compound as provided by the invention, but also a pharmaceutical composition, medicament, drug or other composition comprising such a compound. The compositions may be used, for treatment (which may include preventative treatment) of disease such as inflammation. Such a treatment may comprise administration of such a composition to a patient, e.g. for treatment of disease; the use of such an inhibitor in the manufacture of a composition for administration, e.g. for treatment of disease; and a method of making a pharmaceutical composition comprising admixing such an inhibitor with a pharmaceutically acceptable excipient, vehicle or carrier, and optionally other ingredients.

Thus a further aspect of the present invention provides a method for preparing a medicament, pharmaceutical composition or drug, the method comprising: (a) identifying or modifying a compound by a method of any one of the other aspects of the invention disclosed herein; (b) optimising the structure of the molecule; and (c) preparing a medicament, pharmaceutical composition or drug containing the optimised compound.

The above-described processes of the invention may be iterated in that the modified compound may itself be the basis for further compound design.

By "optimising the structure" we mean e.g. adding molecular scaffolding, adding or varying functional groups, or connecting the molecule with other molecules (e.g. using a fragment linking approach) such that the chemical structure of the modulator molecule is changed while its original modulating functionality is maintained or enhanced. Such optimisation is regularly undertaken during drug development programmes to e.g. enhance potency, promote pharmacological acceptability, increase chemical stability etc. of lead compounds. Modification will be those conventional in the art known to the skilled medicinal chemist, and will include, for example, substitutions or removal of groups containing residues which interact with the amino acid side chain groups of a CD44 or LYVE-1 structure of the invention. For example, the replacements may include the addition or removal of groups in order to decrease or increase the charge of a group in a test compound, the replacement of a charge group with a group of the opposite charge, or the replacement of a hydrophobic group with a hydrophilic group or vice versa. It will be understood that these are only examples of the type of substitutions considered by medicinal chemists in the development of new pharmaceutical compounds and other modifications may be made, depending upon the nature of the starting compound and its activity.

Compositions may be formulated for any suitable route and means of administration. Pharmaceutically acceptable carriers or diluents include those used in formulations suitable for oral, rectal, nasal, topical (including buccal and sublingual), vaginal or parenteral (including subcutaneous, intramuscular, intravenous, intradermal, intrathecal and epidural) administration. The formulations may conveniently be presented in unit dosage form and may be prepared by any of the methods well known in the art of pharmacy.

For solid compositions, conventional non-toxic solid carriers include, for example, pharmaceutical grades of mannitol, lactose, cellulose, cellulose derivatives, starch, magnesium stearate, sodium saccharin, talcum, glucose, sucrose, magnesium carbonate, and the like may be used. Liquid pharmaceutically administrable compositions can, for example, be prepared by dissolving, dispersing, etc, an active compound as defined above and optional pharmaceutical adjuvants in a carrier, such as, for example, water, saline aqueous dextrose, glycerol, ethanol, and the like, to thereby form a solution or suspension. If desired, the pharmaceutical composition to be administered may also contain minor amounts of non-toxic auxiliary substances such as wetting or emulsifying agents, pH buffering agents and the like, for example, sodium acetate, sorbitan monolaurate, triethanolamine sodium acetate, sorbitan monolaurate, triethanolamine oleate, etc. Actual methods of preparing such dosage forms are known, or will be apparent, to those skilled in this art; for example, see Remington's

Pharmaceutical Sciences, Mack Publishing Company, Easton, Pennsylvania, 15th Edition, 1975.

All publications and patents mentioned in the above specification are herein incorporated by reference. Various modifications and variations of the described invention will be apparent to those of skill in the art without departing from the scope and spirit of the invention. Although the invention has been described in connection with specific preferred embodiments, it should be understood that the invention as claimed should not be unduly limited to such specific embodiments.

The following examples illustrate the invention. Example

Experimental Procedures.

Reagents:

HA oligosaccharides of defined length (i.e., HA₆, HA₈, HA₁₀, HA₂₂ and HA₂₆) were produced as described in Mahoney et al. (23). Biotinylated-HA (b-HA) was prepared from Genzyme medical grade HA (-1.2 MDa) as described in Mahoney et al., (23). The monoclonal antibody IM7 was obtained from Pharmingen (Oxford, UK). Two further antibodies specific for murine CD44, IRAW B14 and KM81 were obtained from Dr. Helen Yarwood (Imperial College, London, UK) and Dr Jayne Lesley (SaIk Institute, San Diego, USA). A full-length cDNA clone for mouse CD44 (the haemopoetic or standard form) was obtained from Dr. Helen Yarwood and sub- cloned into the mammalian expression vector pRcCMV (Invitrogen, Paisley, UK).

Cloning and expression of the HABD from mouse, human and mutated human CD44:

A segment of mouse CD44 cDNA encoding the HABD was prepared by PCR amplification using the forward primer GGAATTCtcatgaATCAGATCGATTTGAATGTAACCTGCCGC (SEQ ID NO:4) containing a Bsp HI site (lowercase) and the reverse primer

GCggatccTCAATCGATGTCTTCTTGGTGTGTTCTATAC (SEQ ID NO:5) containing a Bam HI site for ligation into the expression vector pET19b (Novagen, Nottingham, UK). The polypeptide, CD44^25"174, was equivalent to the first 152 residues of the mature N-terminus of mouse CD44 with the first two residues H²³Q being replaced by MN. N-terminal sequencing indicated that the translation initiating methionine was retained in the E. coli expressed protein. The HABD was expressed and purified to homogeneity as described previously (24).

The HABD construct for human CD44 was prepared and expressed according to the method described in Banerji et al 1998 (24). ¹⁵N labelling of human CD44^20'178 was carried out as described in Teriete et al 2004 (19). Mutated human CD44 constructs were prepared as described below and were expressed and labelled in the same manner as for the wild-type.

Crystallization of mouse CD44 HABD₁ and HABD/HA complexes, data collection and analysis:

For the preparation of mouse CD44^25"174 apoprotein crystals, droplets comprising of 200nl CD44^25'174(at a concentration of 0.5mM) mixed with 20OnI well solution were dispensed as sitting drops and allowed to undergo vapor diffusion with a well solution of 30% PEG monomethylether 5000, and 200 mM (NH₄)₂S0₄ in 100 mM MES buffer pH 6.5. Crystals comprising composites of plate-like sheets grew over the period of one week. Co-crystals of the CD44^25"174 -HA8 complex were prepared after addition of HAδmer (2mM final concn.) to the protein solution. Two different sets of crystallization conditions were then used. In the first case, the protein/HA sample was mixed 1 :1 with a well solution containing 25% (w/v) PEG 3350 and 10OmM NaCI in HEPES buffer pH 7. In the second case, the protein/HA sample was mixed with 25% PEG 3350 and 10OmM NaCI in 10OmM Hepes buffer pH8. Co-crystals grew over a period of two to eight weeks at room temperature. NMR spectroscopy

Samples for NMR were prepared from lyophilized hCD44^20"178 (0.3 mM: wild-type, R41A, R150A, R154A; 0.15 mM: K158A and R162A) in 10% (v/v) D₂O (containing 0.02% [w/v] Na- azide) and adjusted to pH 6.5. ¹H₁ ¹⁵N-HSQC spectra were acquired at 500 MHz in the absence and presence of HA₆ or HAi₀ at oligosaccharide to protein stoichiometries of 0:1 , 1 :1 , 2:1 , 3:1 and 4:1 as described before for the wild-type HABD (19). In the case of the R41A mutant, this was only titrated with HA₆ at 0: 1 , 1 : 1 , 2: 1 , 4: 1 , 6: 1 , 10: 1 and 18: 1 ratios. Here the chemical shift of the H^N nuclei of residues 80, 94, 97 and 110, and the N^H nuclei of residues 97 and 110, were measured at each ligand concentration, normalized to a maximal value of 1 and the average determined. These data were fitted in Microlocal Origin using a sum of least squares iterative improvement as described in (25). ¹H₁ ¹⁵N-HSQC spectra were also collected for wild- type hCD44^20"178 together with HA₂₂ at protein:oligomer stoichiometries of 1 :0, 1 :1 , 2:1 , and 1 :2. Translational diffusion measurements were made using a double stimulate echo method (26) on 0.6 mM unlabelled hCD44^20"178 in the presence of 2.4 mM HA₆ or HA₂₂ in 6% (v/v) D₂O, pH 6.5

Expression and purification of wild-type and site-directed CD44 mutants.

1. Mouse CD44

Constructs (K42A, R45A, A103E, A103Y, R155A, R159A, K163A and R167A) carrying mutations in the HABD within the full-length cDNA for mouse CD44H were prepared using the QuickChange™ kit from Stratagene (Amsterdam, Netherlands) according to the manufacturer's instructions. One further (triple) mutation of full length mouse CD44H (DGT156-158AAA) was amplified by means of a three reaction procedure using the following primer sets: reaction 1 , forward primer CGCGaagcttGGCTCCGGACACCATGGACAAG (SEQ ID NO:6) containing a Hind III site and reverse primer

CCCTTCTTGCTGTAGCGAGCAGCAGCACGGTTGACAATAGTTATGGTAACCGG (SEQ ID NO:7) (the region giving rise to mutations is underlined) and reaction 2, forward primer CCGGTTACCATAACTATTGTCAACCGTGCTGCTGCTCGCTACAGCAAGAAGGG (SEQ ID NO:8) and reverse primer GCtctagaGTTAATGGCGTAGGCACTACACCCC (SEQ ID NO:9) containing an Xba I site. The products from reactions 1 and 2 were gel purified, combined and used as template in reaction 3. The forward primer from reaction 1 and the reverse primer from reaction 2 were used to amplify a mutated version of the cDNA which was ligated into pRcCMV. All constructs were sequenced confirming the absence of any other changes to the coding sequence.

2. Human CD44

The single site mutants K38A, R41A, R150A, R154A, K158A and R162A of human CD44^20"178 (h CD44^20'178) were made using the Transformer Site-Directed Mutagenesis Kit (Clontech) and expressed in E. coli as described previously for the wild-type protein (24). The triple mutant DGT151-153AAA was constructed for analysis of HA binding by surface plasmon resonance. Mutagenesis was carried out according to the QuickChange™ mutatgenesis procedure using the forward primer GGACCAATTACCATAACTATTGTTAACCGTGCTGCCGCCCGCTATGTCCAGAAAGG (SEQ ID NO: 10) and the reverse primer

CCTTTCTGGACATAGCGGGCGGCAGCACGGTTAACAATAGTTATGGTAATTGGTCC (SEQ ID NO:11) with CD44^20"178 as template. .Both mutant and wild-type CD44 HABD were produced as unlabelled and uniformly ¹⁵N-labelled proteins, then refolded and purified to homogeneity as before (19, 24). Electrospray ionization mass spectrometry showed that the recombinant proteins had molecular weights within 2 Da of their theoretical masses.

Measurement of FI-HA binding by flow cytometry,

Recombinant pRcCMV plasmids designed for cell surface expression of full-length wild-type mouse CD44 and the mutants described above were transiently transfected into the CD44 negative human 293T fibroblast cell line using calcium phosphate precipitation. Transfected cells were stained with FITC-HA and the mouse CD44 specific antibody IM7. Transfectants were stained with two additional antibodies KM81 and IRAWB14 (also specific for mouse CD44) to assess expression levels of the mutated CD44 compared to the wild-type. Levels of fluorescence associated with the cells were measured using a Becton-Dickinson (Oxford, UK) FACScalibur™ flow cytometer and data were analysed with Cell Quest™ software (Becton- Dickinson). To determine FI-HA binding at discrete levels of cell surface CD44, the range of expression was categorised by applying 9 gates. Mean fluorescence intensity of FlTC-HA bound was then determined for each level of CD44 expression.

Measurement of bHA-binding by microtitre plate ELISA.

The interactions of polymeric HA with human wild-type and mutant hCD44^20'178 were investigated using a microtitre plate binding assay similar to that described in Teriete et a/ (19). Briefly, 96-well microtitre plates (Nunc Maxisorp) were coated (50 μl/well for 8 h at 20 ^"C) with either wildtype CD44, R41A R150A, R154A, K158A or R162A at concentrations of 2.5-40 μg/ml in 15 mM Na-carbonate, 34 mM Na-bicarbonate, pH 9.3. After blocking with BSA, the plates were incubated with bHA (5 μg/ml) in assay buffer (PBS, 0.05% (w/v) Tween 20) for 4 h at room temperature, and bound ligand then detected with ExtrAvidin alkaline phosphates conjugate and development with the substrate p-nitrophenyl phosphate essentially as described in (23). The absorbance values at 405 nm were measured after 20 min and corrected against blank wells. Data were plotted as the mean ± S.E.M (n=4).

Surface plasmon resonance (SPR).

Experiments were performed on a BIACORE 2000 in HEPES-EP running buffer (10 mM HEPES pH 7.4, 150 mM NaCI, 3 mM EDTA, 0.005% (v/v) surfactant P20) at a constant flow rate of 20 μl/min; 70 μl b-HA (1.9 mg/ml) was coupled to commercially prepared SA streptavidin-coated sensor chips. Following immobilization of the HA, binding analyses were performed using various concentrations of wild-type (0-169 μM) or mutant human CD44^20'178 (0-197 μM R150A, 0-99 μM R154A, 0-59 μM K168A, 0-45 μM R162A), where 40 μl of the protein solution was flowed over the sensor chip surface. The analyte was simultaneously passed over a blank flow cell (i.e., no with b-HA coupled) and this reference sensogram was subtracted from the data derived from the experimental flow cell. From these adjusted data, the maximum equilibrium binding was determined 125 s following the beginning of the injection. After each experiment the chip surface was regenerated using with 40 μl of 1 M ethanolamine, pH 8.5 that removed all bound protein but did not dissociate the b-HA. The sensor chip was then equilibrated with 50 μl HEPES-EP prior to the next injection. Scatchard analysis was performed to determine the validity of the 1:1 Langmuir association/dissociation model and data were analyzed using non-linear curve fitting of the Langmuir isotherm; data analysis was done with Microlocal Origin using a sum of least squares iterative improvement method. All experiments were performed at least twice.

Isothermal titration calorimetry. The interactions between wild-type mCD4425-174and HA oligosaccharides of different lengths (i.e., HA₈, HA₁₀, HA₂₆), and the binding of hCD44^20'178 to HA₁₀, were investigated on a MicroCal VP-ITC instrument at 25 ⁰C in 10 mM MES, 25 mM NaCI, pH 6.5, essentially as described before for the TSG-6 Link module, Link_TSG6 (23, 27). Oligosaccharide solutions (ranging from 1.93 to 8.47 μM, where the concentrations were determined on the basis of a control experiment with Link_TSG6) were added in 28 x 5-μl injections to protein at 0.176-0.404 mM; protein concentrations were determined by amino acid analysis (23). There was a spacing of 300 s between injections and a reference power of 15 μcal/s was used for all of the titrations. Data were fitted to a one-site model by non-linear least squares regression with the Origin software package, after subtracting heats resulting from the addition of oligomer into buffer alone, as described previously (23, 27).

Human model of form B CD44-HA complex crystal structure.

The structure was modelled by mutating all of the sequence differences in the HA binding domain of mouse CD44 to their human equivalents, and choosing the side chain rotamer that gave the least possible clashes. The loop region spanning residues 108-112 (which contains the deletion) was adopted from the human apoprotein structure, and the structure was energy minimised to relieve any strain thus introduced.

Results. Crystallization of a murine CD44-hyaluronan complex.

We previously reported a crystal structure for the hyaluronan-binding domain of human CD44 refined to a resolution of 2.2A using an N-terminal ectodomain construct (CD44^20'178) expressed as a recombinant protein in E. coli. To obtain a detailed structure for the ligand-bound receptor we prepared a complex between the same human CD44 apoprotein and a highly purified HA octasaccharide - the minimal sugar unit that displays efficient competition of native high molecular weight hyaluronan in plate-binding assays (19). However, all attempts to obtain such a complex either by co-crystallization with HA₈ or by soaking ligand into pre-formed apoprotein crystals were unsuccessful, most likely due to the high packing density and low water content of these structures (19). Attempts were therefore made to prepare co-crystals using the equivalent murine CD44 construct CD44 ^25"174; this differs from the human construct CD44^20'178 by a single residue insertion (V112) within the β5 chain of the Link module and a total of fifteen substitutions, eight of which involve surface charge alterations (K58Q, A68D, E71K, K72L, H89N, N105H, Q118H, N169H, numbered according to the mouse sequence). Crystallization of the murine CD44^25'174- hyaluronan complex was successfully achieved at a molar ratio of CD44:HA of 0.25:1 with 25%polyethylene glycol monomethyl ether 3350 and 0.1 M NaCI in either 0.1 M HEPES buffer pH 7.0 or pH 8.0 yielding cuboid (type A) or sheet-like (type B) crystals respectively.

Main features of the CD44-HA crystal structure

Initial inspection of the mCD44^25'174-HA8 crystals (A and B) revealed similarly well ordered polypeptide structures in which the distinctive C-type lectin-like extended Link module is visible as a beta sandwich made up of ten short β strands (βO- β9) in two sheets (Sl, βO, 1 ,2,6,7, 8 and 9; SII, β3,4 and 5) that together form a long curving β sheet, and two orthogonally disposed α helices, similar to that of the free human CD44 apoprotein. Within this complex, the bound HA oligomer can be seen to occupy a discrete binding patch in a groove that extends from the side of the hook-like loop between β strands 4 and 5 to the channel that connects β3, β4 and β5 (previously referred to as the SII sheet) with the rest of the Link module.

Superposition of the structure of crystal A with that of the human CD44 apoprotein shows that the two are almost identical, with the exception of a small kink in the loop at the end of the β5 strand in the mouse protein caused by the valine (V112) insertion. Curiously however, superposition of crystal B with the human apoprotein structure indicated a significant difference in electron density of the polypeptide chain in the loop between β1 and the first alpha helix (α1). This local conformational change was clearly visible when the backbone structures of crystals A and B were superimposed and its particular significance in terms of hyaluronan-binding is discussed below.

Characteristics of the binding site for hyaluronan.

1. Conformation of the bound sugar

Our previous analyses of bacterially expressed CD44 had indicated that the minimal saccharide length required for blockade of high molecular weight HA-binding corresponded to an HA 6- 8mer (19). This is confirmed in both the CD44-HA crystal complexes which show well defined electron densities for seven of the eight sugar residues (GlcNAc2-GlcNAc8) of the HA octasaccharide: the non-reducing terminal sugar (GIcUAI) does not adopt a stable conformation. Within the bound region of the saccharide chain, GlcNAc2 makes no obvious contact with the polypeptide and GlcUA3 forms only a tentative contact with R155; the electron density for both the amino acid and the sugar are very weak indicating that the contact is of relatively low occupancy. The core of sugar binding is therefore centred on a relatively small region of the HA octamer, involving primarily residues GlcUA5 through GlcNAcδ. This is reflected in the large temperature factor measured for GlcNAc2 (42.3 A²) and the much lower values for GlcUA5 through GlcNAcδ (14.0 - 17.5 A²). The relatively short footprint is apparent also from considerations of the conformational flexibility of bound HA. Whereas free HA oligomers are known to adopt a highly regular conformation, characterised by repeating torsion angles in the constituent α4 and β3 linkages, HA bound to protein can be expected to experience conformational constraints, as a consequence of sugar-protein interactions and intramolecular hydrogen bonds between neighbouring sugar residues. It was also observed that residues GlcNac 2 through GIcNAc 4 can be superimposed precisely on the preferred conformation of the sodium salt of an HA 8-mer. However, superimposition of sugars GlcNac 4- GIcNAc 8 on the HA 8mer shows that this portion of the chain is distorted, confirming the conformational constraint on these residues imposed by interaction with the binding cleft on CD44.

2, Nature of the ligand-binding interactions,

In both crystal forms, the sugar residues towards the non-reducing end of HA8 (GlcNAc2- GlcNAc4) can be seen to make the fewest contacts with protein (GlcUA3 making a weak interaction with R155 as described above), whereas those making the closest contacts (GlcUAδ-GlcNAcδ) lie within a shallow groove that traces a gently curving path around the distinctive hook-like region of the molecule. Consequently, a large segment of the contact surface is made up of residues that form the surface of the "hook", namely those located within the loop between β4 and β5 and the short intervening 3₁₀ helical structure. The identity of these residues as I92, N98, 1100, A102, A103 demonstrates an unexpectedly large contribution from aliphatic side-chain residues to HA-binding. The remainder of the binding groove is lined by the previously assigned "key" aromatic and basic residues R45, Y46, R82, Y83 (equivalent to human R41 , Y42, R78 and Y79) brought together from the loops between β1- α1 and α2- β3 and TyM 09 from the β5 strand. A most intriguing feature of this region of the binding surface is the conformational flexibility in the β1/α1 loop revealed by the differences between the A and B crystal forms. A conformational flip of the main-chain around residue G44 results in a side- chain rearrangement that brings the key residue R45 into contact with HA in crystal B, thereby displacing R82 from interacting with HA and producing a subtle shift in E41. The effect of this conformational change, which may well be induced by ligand-binding, would be to increase the binding affinity for HA and crystal form B may thus be the conformation of the receptor that predominates in the active form of the receptor at the cell surface.

The main binding interaction between HA and CD44 is focussed on GlcNAcδ, the sugar residue that experiences the most intimate contacts with the polypeptide chain is (change of accessible surface area upon binding = -133 A²). A novel feature of this interaction is the insertion of the methyl group of the acetyl moiety into a "pocket" which is lined by a number of (polar) main chain carbonyls in addition to the hydrophobic sidechains of Y83, and I92, each of which engage in H bonds with the sugar ring. The predominance of H bonds in the binding groove is also apparent for the remaining sugar interactions. Specifically, GlcNAc4 is co-ordinated by H- bonds to N98 and C101 , GlcUA7 is H bonded to Y83, 1100, C101 , A102, and A103, and GlcNacδ H-bonded to A103 (Cβ-C4/ Cβ-04), H 105 (Nε2-O6) and Y109 (ring OH-C6/ring OH to O6/Cζ-O6/). In all, some thirteen residues (R45, Y46, C81 , R82, Y83, 192, N98, 1100, C101 , A102, A103, N105 and Y109) make significant contacts with the HA oligosaccharide, and all of these involve hydrogen bonds, rather than electrostatic or hydrophobic interactions. This mode of sugar binding is very unusual. The majority of protein carbohydrate interactions are dominated by sugar stacking interactions, involving particularly the more hydrophobic face of constituent sugar moieties (reviewed in (28). Furthermore, such interactions had been implicated from earlier site-directed mutagenesis studies that suggested key roles for aromatic residues of human CD44 (ie, Y42, Y79 according to the human numbering) in HA-binding. Although their murine equivalents Y46, Y83, and Y109 are shown here to contact the HA oligomer, none of these interactions can be described as a stacking interaction, which would be characterised by having the ring-system of the sugar moiety approximately parallel with the planar aromatic residue. Rather, the role of these tyrosines appears predominantly to be the formation of hydrogen bonds, perhaps reflecting the need for CD44 to maintain low affinity oligosaccharide binding, without loss of sugar specificity.

HA-bindinq activities of human CD44 HABD mutants

NMR analysis

Mutagenesis studies have also implicated R41 as having a critical role in mediating the interaction with HA (21 , 22). The HSQC spectra for the R41 A mutant that were collected at various protein :hexasaccharide ratios showed that the R41A/HA₆ complex, unlike the mutants described above, is in fast exchange on the NMR timescale, which is consistent with a significant reduction in binding affinity. The fact that this interaction is in fast exchange allows the straightforward identification of amides that are perturbed on HA binding, without the requirement for de novo assignment of the protein in its bound state; i.e., amide resonances could be tracked as they change position with increasing ligand concentration, where close to maximal shift changes were seen with a 18-fold excess of HA₆ over protein. Compared to the wild-type hCD44^20"178 (19) relatively few amides are affected by HA₆ binding and the magnitude of the perturbations are much smaller. We identified significant chemical shift changes on the basis of an arbitrary threshold of 0.05 ppm H^N and 0.25 ppm N^H (i.e., 4-times lower than the values used before (19)). When these 'significantly' perturbed amides in the hCD44^20'178 R41A are mapped onto the mCD44^23'174/HA₈ 'low-dose' co-structure it can be seen that they generally correspond to residues that are in close proximity to the bound HA or are found in regions of the structure that are likely to undergo conformational rearrangements on binding (i.e., β1-α1 loop and hook regions). Interestingly, R78 (i.e., one of the residues implicated previously as having an essential role in HA binding (22)) and shown here to make a hydrogen bound contact with the 3-hydroxyl of the ring 5 GIcA was found to be in slow exchange on HA binding indicating that it is likely to make a central contribution to the interaction with HA in the context of this mutant. Overall this 'shift map' analysis for R41 A indicates that the human and mouse CD44 are likely to have very similar HA-binding sites. Importantly, none of the basic residues in the C-terminal extension, including those that were hypothesised to constitute to the 'mode-2' interaction site (19), were found to be perturbed.

The HSQC titration data for R41A in the presence of HA₆ were used to determine the affinity for this interaction. The normalized chemical shift changes relative to the protein in the absence of oligosaccharide, averaged over 6 nuclei, were plotted against the HA₆ concentration. Analysis of these data by non-linear regression (as described in Experimental Procedures) allowed the dissociation constant to be estimated at ~1.2 mM. The mutation of R41 to alanine clearly causes a large reduction in its affinity for short HA oligosaccharides. Surface Plasmon Resonance

The binding of the hCD44^20'178 mutants to polymeric HA was also investigated by SPR, where b-HA was coupled to a streptavidin-coated sensor chip. Preliminary experiments were conducted where the wild-type and mutant proteins were flowed over the chip surface at 0-12 μM. This demonstrated that a reasonable binding signal could be detected in all cases apart for the R41A mutant, which at 10 μM only gave 17 response units (RU) compared to 438 for the wild-type protein (i.e., after subtraction of the reference sensogram). This is consistent with the low affinity of R41 A for HA seen by microtitre plate assay and NMR; no further SPR experiments were carried out for this mutant. These experiments also indicated that the /c_on and /f_off were too fast to allow a steady state analysis, therefore the maximum binding responses were determined at equilibrium (125 s after injection) and the K₀ estimated on the basis of the 1 :1 Langmuir model. The wild-type protein and the R150A, R154A, K158A and R162A mutants were then analyzed over a wide range of concentrations such that the highest protein concentration used was significantly larger than the estimated dissociation constant (i.e., between ~5-15-fold) and the data fitted by non-linear regression. Scatchard analysis showed that there is some^' deviation from linearity indicating that the interaction of the hCD44^{20" 178} proteins with HA does not conform precisely to the Langmuir binding model. This is probably due to the heterogeneity of the coupled ligand since the b-HA used is of polydisperse molecular weight and is biotinylated randomly along the HA chain. Nevertheless these data are likely to provide reasonable estimates of the affinity and allow the relative activities of the various proteins to be compared.

The wild-type hCD44^20"178 was determined to bind to HA with a K₀ = 20 μM, which is in good agreement with the SPR value of 27 μM reported by Takeda and colleagues (31) and the K₀ of 13 μM determined by ITC for the interaction of mCD4425-174with HA₂₆. The R15OA mutant was found to have an approximately 2-fold reduced affinity compared to wild-type (K₀ = 41 μM), whereas R154A, K158A and R162A all exhibited lower K₀ values (11 , 8 and 7 μM, respectively). These data clearly demonstrate that the basic amino acids in the C-terminal extension of the HABD do not contribute significantly to HA binding, which is consistent with the NMR titrations experiments described above.

Functional role of the Link extension in mouse and human CD44

The nature of the CD44 hyaluronan-binding site revealed by the present crystal structure indicates no obvious contribution from residues within the C and N-terminal Link extensions, formed from the four supplementary β strands 0, 7, 8 and 9 that are essential for correct folding and function of the HA-binding domain (19, 29). A group of basic amino acids (R150, R154, K158 or R162) located within and around β9 had previously shown to be important for HA- binding to human CD44 through alanine mutagenesis (21 ; 22). This and the observation that HA binding to hCD44^20"178 caused widespread chemical shift perturbations detected by NMR spectroscopy, led us to hypothesize recently that there are two mutually exclusive modes of sugar binding which are defined by interactions with particular combinations of these basic residues (19). However, since these conclusions were drawn mostly from studies carried out using site-directed mutants of glycosylated human CD44, and the present crystal structure derives from murine CD44, it was important to re-assess the role of residues within the Link extension in the context of the murine protein, as well as in non-glycosylated human CD44. Hence, we examined the effects of mutating the residues equivalent to human K38 (K42), R150 (R155), R154 (R159), K158 (K163) and R162 (R167) in full-length mouse CD44 as well as investigating their effects in bacterially expressed human CD44^22"178 by a combination of FACS analysis, NMR spectroscopy and a plate-binding ELISA.

In the case of murine CD44, cDNAs encoding full-length wild-type receptor and site-directed mutants were transfected into the 293T cell line and the capacity to bind FI-HA assessed as a function of surface expression and authentic folding using the murine-reactive mAb IM7 and two conformation selective mAbs IRAWB14 and KM81. Mutation of either K42, R159, K163 or R167 to alanine had little if any effect on the ability of the receptor to bind FI-HA, measured at either high or low CD44 surface densities. In contrast, mutation of R155 reduced HA binding significantly compared to wild-type CD44, although not to the same extent as mutation of either R45 or A103.

In the case of human CD44, re-folded wild-type and hCD44^20"178 site-directed mutants R150A, R154A and K158A were compared for HA-binding using NMR spectroscopy. In each case, the mutants gave ¹H₁ ¹⁵N-HSQC spectra that were essentially the same as the wild-type hCD44^20"178 on binding to either HA₆ or HA₁₀. As reported before for hCD44^20"178, a four fold molar excess of the HA oligosaccharide over mutant protein was found to give rise to a 'fully perturbed' (i.e., bound) spectra, and the HA/protein complexes were all in slow exchange on the NMR timescale (19). This was even the case for R162A, which had a significantly different spectrum from wild-type in the absence of HA (see above). This indicates that HA binding is unaffected in this mutant and that it can adopt an identical bound conformation compared to the wild-type protein. On the basis of our previous finding that the interaction of HA₆/HA₁₀ with hCD44^20'178 causes very large chemical shift perturbations throughout much of the protein (19), it is clear that mutation of any one of these residues to alanine does not affect this 'shift pattern' and therefore does not have a major effect on the binding of the HABD to short HA oligosaccharides. Finally, we explored the possibility that mutation of the same basic residues might affect the interaction of hCD44^20'178 with polymeric HA, assessed using biotinylated HA in a standard ELISA (see Experimental Procedures). R150A, R154A and R162A again exhibited binding properties similar to those of the wild-type protein. In contrast, the K158 mutant showed significantly reduced binding activity in the plate assay. However, on the basis of the surface plasmon resonance (SPR) binding experiments this is likely to be an artefact caused by immobilization of the K158A protein. Hence we conclude that R150A (R155A), R154A (R159A), K158A (K163A) and R162A (R167A) are not involved to any significant extent in mediating the direct binding of HA in either mouse or human CD44, regardless of glycosylation.

Potential protein-protein interactions and co-operativitv in HA-binding.

The CD44-HA complex packs in the crystal lattice in such a way that the bound oligosaccharide units of neighbouring CD44 molecules resemble parallel segments of a single co-linear high molecular weight HA polymer. This pattern brings the individual CD44 molecules in sufficiently close proximity to suggest a protein:protein interface between adjacent molecules involving the loops between β8 - β9 on one molecule and the β5-β6 loop of its nearest neighbour. Clearly, contacts in a crystal lattice may not necessarily reflect such contacts in solution. Nevertheless, it is tempting to speculate they might resemble interactions that occur transiently on the surface of a cell engaging in multivalent binding to an HA polymer, as they could provide an element of co-operativity to the binding of HA. Such co-operativity has been suggested by previous experiments with mouse CD44, in which there was an apparent increase in binding affinity for HA when this was measured with multivalent (>25mer) oligosaccharide as compared with monovalent (<18mer) oligosaccharide (30). To investigate the likelihood of protein:protein interactions between neighbouring CD44 molecules we mutated three residues DGT (156-158) at the tip of the β8 - β9 loop in mouse CD44 to alanines, prior to determining the effects on HA- binding. The HA binding characteristics of the compound mutant were not significantly different from those of the wild-type protein. Furthermore, analysis by surface plasmon resonance also indicated no disruption in HA binding affinity (Kd approximately 10μM for immobilised polymeric HA). Together these results indicate that the β8 - β9 loop does not influence HA binding in the context of transfected 293T fibroblasts.

To explore the phenomenon of co-operativity more quantitatively, we compared the binding affinity of mCD4425-174for HA 8mer, 10mer and 24-26mer oligosaccharides using isothermal titration calorimetry (ITC), while at the same time probing for incident protein-protein interactions by NMR. The stoichiometries for binding of mCD44^25"174 to HA₈/HA₁₀ were determined to be close to 1 :1 as would be expected on the basis of previous studies (19, 30) and the co-structure described here, while that for HA₂₆ was 2:1. Significantly, the binding affinity of mCD44^25"174 for the divalent HA₂₆ oligomer (K_D = 16μM) was some fourfold lower than that measured for the monovalent HA₁₀ oligomer (K₀ = 51 μM), while the HA₆ oligomer (which is shorter than the length required for optimal binding to CD44, (19)) yielded a K₀ value of = 125μM. A similar binding affinity for HA₁₀ was estimated with hCD44^20"178 (K₀ = 61 μM), indicating that the mouse and human CD44 have equivalent HA-binding activities. Clearly, the higher affinity seen for divalent binding of HA to CD44 could arise through co-operative interactions between adjacent protein molecules. To test this possibility ¹H₁ ¹⁵N-HSQC spectra of ¹⁵N-labelled hCD44^20"178 were acquired in the presence of various ratios of an HA₂₂ oligosaccharide, which was demonstrated by translational diffusion measurements (26) to bind two CD44 HABDs. However, analysis of the HSQC spectra revealed an essentially identical pattern of chemical shift perturbations as compared to those seen previously with HA₁₀ (19), indicating that protein-protein contacts do not occur in the context of this divalent interaction, in the solution phase at least. Hence we conclude that the apparent co-operativity of HA-binding to CD44 is more likely due to stabilization of HA dynamics by interaction with the receptor, than to any effects brought about by receptor self-association.

Impact of the crystal complex on the design of small molecule inhibitors of CD44- HA interactions.

Certain unusual features of the CD44-HA interaction revealed from the crystal structure of the complex, namely the short sugar footprint, and the preponderance of H-bonds to the CD44 binding groove, affect both the validation of CD44 as a rational drug design target, and the approach which would be taken to design inhibitors. Firstly, the small structural core to the CD44-HA interaction that is centred on the GIcNAd -GlcUA4 tetrasaccharide increases the chances of obtaining a small molecule antagonist. Secondly, the largely H-bonded nature of the CD44-HA interaction means that improvement of the binding of a lead compound can be pursued by targetting polar and hydrophobic interactions instead of charged interactions. Interactions that are dominated by ionic interactions represent poor targets for therapeutic interaction, as complementary charges in candidate drugs often make for poor bioavailability.

A potentially similar HA-bindinq surface in the lymphatic endothelial hyaluronan receptor LYVE-1. The HA receptor LYVE-1 is expressed almost exclusively in endothelial cells of the lymphatic vasculature, a network that interweaves with but is developmentally distinct from the blood vasculature (5, 16). We originally identified LYVE-1 cDNA from homology searches of a commercial database (Human Genome Sciences/TIGR) and expressed the protein as a soluble Fc fusion partner (5). Subsequent analysis of ligand-binding and tissue expression using specific polyclonal and monoclonal antibodies confirmed LYVE-1 as an authentic receptor for HA with an apparent binding affinity and specificity for HA that is broadly similar to that of CD44. Unlike CD44 however, which is widely expressed, LYVE-1 is confined to lymphatic endothelium, and is absent from blood vascular endothelium and virtually all other cell types with the exception of liver and spleen sinusoidal endothelia and some populations of tissue macrophages (5, 16, 19).

Binding of LYVE-1 to HA.

Using ELISA plate-binding assays that measure the interaction between soluble biotinylated HA and immobilized LYVE-1 Fc, or immobilized HA and soluble LYVE-1 Fc, the receptor has been shown to bind HA in a saturable manner that may be blocked specifically by excess free HA, or by the monoclonal antibody 3A that has been generated against rhLYVE-1 in mice ((20) and see below for details of epitope analysis).

Molecular modelling of the LYVE-1 HA-binding site using CD44 crystal co-ordinates and site-directed mutagenesis.

Using the co-ordinates obtained from the X-ray crystallographic analysis of human CD44 apoprotein structure, we have modelled the homologous LYVE-1 HA-binding domain using the program Swissmodel. As predicted from the primary sequence, the LYVE-1 structure model exhibits a core Link domain made up of two β-sheets (β 1 ,2, 6 and β 3,4,5) flanked by two short a helices (α1, 2). In common with CD44, this core structure is extended by additional β-strands (βO and β7) that are linked by a third disulphide bridge contributed from sequences N and C- terminal to the consensus Link module. Unlike CD44 however, the LYVE-1 HA-binding domain appears to lack the equivalent of β-strands 8 and 9 and is therefore likely to be a more compact structure. A potential HA-binding face has been identified on the surface of the LYVE-1 structure by plotting the positions of amino acids defined as essential (Tyr87, Ile97 and Arg99) or important for ligand-binding (including Asn103, Lys105, Lys108 and Trp116) through site- directed mutagenesis studies. In addition, Tyr87, Arg99 and Trp116 have been identified as part of the epitope for the HA-blocking mAb 3A. Overall these residues define a coherent patch that is similar in nature and location to the ligand binding face identified in the mCD44:HA crystal complex.

Pharmacophore screening. The structure of the complex between CD44 and HA8 has allowed us to carry out a virtual screen of a library of 60,000 small, drug-like compounds (supplied by ChemDiv Inc, San Diego, CA, USA) using the FlexX docking program. The input consisted of the binding site and a pharmacaphore (GCU2:O6A, NAG3:N2, NAG3:C8). Approximately 25% of the compounds gave a solution in the docking procedure and these were ranked. Compounds achieving fewer than 7 docks or those that had very low solubility were excluded and the 100 compounds with the best scores were selected. A control group of 15 compounds evenly distributed amongst the ~15,000 compounds that had a solution were also selected.

The 115 compounds are assayed initially for their ability to block binding of biotinylated high molecular weight HA to purified immobilized CD44 in an established 96 well plate ELISA

(discussed in accompanying document on assays for small molecule inhibitors). Compounds showing activity are selected for further analysis, including the production of co-crystals with CD44.

References.

1. Tammi, M. I., A.J. Day, and E.A. Turley. 2002. Hyaluronan and homeostasis: a balancing act. J. Biol. Chem. 277:4581-4584.

2. Toole, B.P., T.N. Wight, and M.I. Tammi. 2002. Hyaluronan-cell interactions in cancer and vascular disease. J Biol Chem 277:4593-4596. 3. Mohamadzadeh, M., H. DeGrendele, H. Arizpe, P. Estess, and M. Siegelman. 1998. Proinflammatory stimuli regulate endothelial hyaluronan expression and CD44/HA-dependent primary adhesion. J. CHn. Invest. 101 :97-108.

4. Gee, K., M. Kozlowski, and A. Kumar. 2003. TNFα induces functionally active hyaluronan-adhesive CD44 by activating silidase through p38 mitogen-activated protein kinase in lipopolysaccharide-stimulated human monocytic cells. J. Biol. Chem. 278:37275-37287.

5. Levesque, M. C, and B. F. Haynes. 1999. TNFα and IL-4 regulation of hyaluronan binding to monocyte CD44 involves posttranslational modification of CD44. Cell. Immunol. 193:209-218.

6. Mikecz, K., K. Dennis, M. Shi, and J. H. Kim. 1999. Modulation of hyaluronan receptor (CD44) function in vivo in a murine model of rheumatoid arthritis. Arthritis Rheum. 42:659-668.

7. Weiss, L., S. Slavin, S. Reich, P. Cohen, S. Shuster, R. Stern, E. Kaganovsky, E. Okon, A.M. Rubinstein, and D. Naor. 2000. Induction of resistance to diabetes in non-obese diabetic mice by targeting CD44 with a specific monoclonal antibody. Proc. Natl. Acad. Sci. USA 97:285-290. 8. Katoh, S., N. Matsumoto, K. Kawakita, A. Tominaga, P. Kincade, and M. Matsukura. 2003. A role for CD44 in an antigen-induced murine model of pulmonary eosinophilia. J. CHn. Invest. 111 :1563-1570. 9. Lesley, J., N. English, A. Perschl, J. Gregoroff, and R. Hyman. 1995. Variant cell lines selected for alterations in the function of the hyaluronan receptor CD44 show differences in glycosylation. J. Exp. Med. 182:431-437.

10. English, N. M., J. F. Lesley, and R. Hyman. 1998. Site-specific de-N-glycosylation of CD44 can activate hyaluronan binding, and CD44 activation states show distinct threshold densities for hyaluronan binding. Cancer Res 58:3736-3742.

11. Katoh, S., Z. Zheng, K. Oritani, T. Shimozato, and P. Kincade. 1996. Glycosylation of CD44 negatively regulates its recognition of hyaluronan. J. Exp. Med. 182:419-429.

12. Liao, H.-X., M. C. Levesque, K. Patton, B. Bergamo, D. Jones, MA Moody, M. Telen, and B. F. Haynes. 1993. Regulation of human CD44H and CD44E isoform binding to hyaluronan by phorbol myristate acetate and anti-CD44 monoclonal and polyclonal antibodies. J. Immunol. 151 :6490-6499.

13. Katoh, S., T. Miyagi, H. Taniguchi, Y. Matsubara, J. Kadota, A. Tominaga, P.W. Kincade, S. Matsukura, and S. Kohno. 1999. An inducible sialidase regulates the hyaluronic acid binding ability of CD44-bearing human monocytes. J. Immunol. 162:5058-5061.

14. Nandi, A., P. Estess, and M. Siegelman. 2004. Bimolecular complex between rolling and firm adhesion receptors required for cell arrest; CD44 association with VLA-4 in T cell extravasation. Immunity 20:455-465.

15. Day, A. J., and G. D. Prestwich. 2002. Hyaluronan-binding proteins: tying up the giant. J Biol Chem 277:4585-4588.

16. Day, A.J. 1999. The structure and regulation of HA-binding proteins. Biochem. Soc. Trans. 27:115-121.

17. Kahmann, J. D., R. O'Brien, J. M. Werner, D. Heinegard, J. E. Ladbury, I. D. Campbell, and A.J. Day. 2000. Localization and characterization of the hyaluronan-binding site on the Link module form human TSG-6. Structure 8:763-774.

18. Kohda, D., CJ. Morton, A.A. Parkar, H. Hatanaka, F.M. Inagaki, LD. Campbell, and A.J. Day. 1996. Solution structure of the link module : a hyaluronan binding domain involved in extracellular matrix stability and cell migration. Cell 86:767-775.

19. Teriete, P., S. Banerji, M. Noble, CD. Blundell, A.J. Wright, A.R. Pickford, E. Lowe, D.J. Mahoney, M.I. Tammi, J. D. Kahmann, I. D. Campbell, A.J. Day, and D. G. Jackson. 2004.

Structure of the regulatory hyaluronan binding domain in the inflammatory leukocyte homing receptor CD44. MoI Cell 13:483-496.

20. Jackson, D. G. 2004. The lymphatic endothelial hyaluronan receptor LYVE-1. Glycoforum. 21. Peach, R.J., D. Hollenbaugh, I. Stamenkovic, and A. Aruffo. 1993. Identification of hyaluronic acid binding sites in the extracellular domain of CD44. J. Cell Biol. 122:257-264. 22. Bajorath, J., B. Greenfield, S. B. Munro, A.J. Day, and A. Aruffo. 1998. Identification of CD44 residues important for hyaluronan binding and delineation of the binding site. J. Biol. Chem. 273:338-343. 23. Mahoney, D. J., RT. Aplin, A. Calabro, V.C Hascall, and A.J. Day. 2001. Novel methods for the preparation and characterization of hyaluronan oligosaccharides of defined length. Glycobiology 11 :1025-1033. 24. Banerji, S., A.J. Day, J. D. Kahmann, and D.G. Jackson. 1998. Characterization of a functional hyaluronan-binding domain from the human CD44 molecule expressed in Escherichia coli. Protein Expr Purif 14:371-381.

25. Schwarz-Linek, U., J. M. Werner, A.R. Pickford, S. Gurusiddappa, J. H. Kim, E.S. Pilka, J.A. Briggs, T.S. Gough, M. Hook, I. D. Campbell, and J. R. Potts. 2003. Pathogenic bacteria attach to human fibronectin through a tandem beta-zipper. Nature 423:177-181.

26. Jerschow, A., and N. Muller. 1998. Efficient simulation of coherence transfer pathway selection by phase cycling and pulsed field gradients in NMR. J. Magn. Reson. 134:17-29.

27. Blundell, CD., D.J. Mahoney, A. Almond, P.L DeAngelis, J. D. Kahmann, P. Teriete, A.R. Pickford, I. D. Campbell, and A.J. Day. 2003. The link module from ovulation- and inflammation-associated protein TSG-6 changes conformation on hyaluronan binding. J. Biol. Chem. 278:49261-49270.

28. Boraston, A.B., D.N. Bolam, H.J. Gilbert, and G.J. Davies. 2004. Carbohydrate-binding modules: fine-tuning polysaccharide recognition. Biochem. J. 382:769-781. 29. Banerji, S., J. Ni, S.X. Wang, S. Clasper, J. Su, R. Tammi, M. Jones, and D.G. Jackson.

1999. LYVE-1 , a new homologue of the CD44 glycoprotein, is a lymph-specific receptor for hyaluronan. J Cell Biol 144:789-801.

30. Lesley, J., V. Hascall, M. Tammi, and R. Hyman. 2000. Hyaluronan binding by cell surface CD44. J. Biol. Chem. 275:26867-26975. 31. Takeda, M., H. Terasawa, M. Sakakura, Y. Yamaguchi, M. Kajiwara, H. Kawashima, M.

Miyasaka, and I. Shimada. 2004. 1 H, 13C and 15N backbone resonance assignments of the hyaluronan-binding domain of CD44. J Biomol NMR 29:97-98.

Table 1

TABLE 1

CRYSTl 30 . 794 32 . 051 32 . 278 90 . 00 117 . 8 9 90 . 00

ORIGXl 1.000000 0 .000000 0.000000 0.00000

ORIGX2 0.000000 1 .000000 0.000000 0.00000

ORIGX3 0.000000 0 .000000 1.000000 0.00000

SCALEl 0.032474 -0 .000001 0.017185 0.00000

SCALE2 0.000000 0 .012188 -0.000001 0.00000

SCALE3 0.000000 0 .000000 0.035052 0.00000

ATOM 1 N GLN A 25 15.675 12.394 3.650 1.00 11.65

ATOM 2 CA GLN A 25 15.315 11.386 2.620 1.00 10.51

ATOM 3 CB GLN A 25 16.576 10.686 2.111 1.00 11.83

ATOM 4 CG GLN A 25 16.568 10.353 0.619 1.00 14.29

ATOM 5 CD GLN A 25 15.595 9.270 0.256 1.00 18.15

ATOM 6 OEl GLN A 25 15.527 8.245 0.940 1.00 23.59

ATOM 7 NE2 GLN R 25 14.834 9.467 -0.834 1.00 14.53

ATOM 8 C GLN R 25 14.389 10.362 3.245 1.00 10.05

ATOM 9 O GLN R 25 14.595 9.946 4.378 1.00 10.69

ATOM 10 N ILE A 26 13.344 9.987 2.510 1.00 8.50

ATOM 11 CA ILE A 26 12.461 8.876 2.854 1.00 7.55

ATOM 12 CB ILE A 26 11.038 9.359 3.226 1.00 7.24

ATOM 13 CGl ILE A 26 11.059 10.125 4.550 1.00 7.78

ATOM 14 CDl ILE A 26 9.803 10.899 4.870 1.00 8.61

ATOM 15 CG2 ILE A 26 10.068 8.171 3.359 1.00 8.17

ATOM 16 C ILE A 26 12.374 7.937 1.665 1.00 7.29

ATOM 17 O ILE A 26 12.062 8.353 0.553 1.00 7.63

ATOM 18 N ASP A 27 12.605 6.655 1.919 1.00 6.77

ATOM 19 CA ASP A 27 12.452 5.629 0.887 1.00 6.31

ATOM 20 CB ASP A 27 13.667 4.721 0.830 1.00 7.76

ATOM 21 CG ASP A 27 14.825 5.339 0.037 1.00 12.00

ATOM 22 ODl ASP A 27 14.864 6.565 -0.178 1.00 15.06

ATOM 23 OD2 ASP A 27 15.702 4.584 -0.392 1.00 17.37

ATOM 24 C ASP A 27 11.219 4.815 1.191 1.00 4.44

ATOM 25 O ASP A 27 11.003 4.412 2.330 1.00 6.19

ATOM 26 N LED A 28 10.406 4.619 0.163 1.00 3.81

ATOM 27 CA LEU A 28 9.147 3.884 0.238 1.00 4.40

ATOM 28 CB LEU A 28 8.004 4.806 -0.150 1.00 4.60

ATOM 29 CG LED A 28 7.846 6.044 0.746 1.00 5.37

ATOM 30 CDl LEO A 28 6.773 6.920 0.154 1.00 6.59

ATOM 31 CD2 LED A 28 7.553 5.724 2.182 1.00 6.24

ATOM 32 C LED A 28 9.219 2.709 -0.711 1.00 4.35

ATOM 33 O LED A 28 9.161 2.879 -1.927 1.00 4.60

ATOM 34 N ASN A 29 9.347 1.509 -0.155 1.00 3.53

ATOM 35 CA ASN A 29 9.333 0.315 -0.971 1.00 3.70

ATOM 36 CB ASN A 29 10.103 -0.841 -0.314 1.00 4.20

ATOM 37 CG ASN A 29 11.569 -0.791 -0.584 1.00 7.25

ATOM 38 ODl ASN A 29 12.287 -0.126 0.127 1.00 10.86

ATOM 39 ND2 ASN A 29 12.024 -1.484 -1.633, 1.00 8.31

ATOM 40 C ASN A 29 7.915 -0.138 -1.172 1.00 3.64

ATOM 41 O ASN A 29 7.192 -0.312 -0.191 1.00 4.74

ATOM 42 N VAL A 30 7.513 -0.345 -2.426 1.00 2.76

ATOM 43 CA VAL A 30 6.131 -0.680 -2.762 1.00 3.96

ATOM 44 CB VAL A 30 5.476 0.405 -3.617 1.00 4.98

ATOM 45 CGl VAL A 30 6.138 0.529 -4.958 1.00 6.24

ATOM 46 CG2 VAL A 30 5.533 1.747 -2.901 1.00 6.14

ATOM 47 C VAL A 30 6.050 -2.022 -3.484 1.00 3.96

ATOM 48 O VAL A 30 6.965 -2.396 -4.213 1.00 5.39

ATOM 49 N THR A 31 4.962 -2.761 -3.244 1.00 3.88

ATOM 50 CA THR A 31 4.700 -3.999 -3.937 1.00 3.80

ATOM 51 CB THR A 31 3.970 -4.999 -3.022 1.00 4.77

ATOM 52 OGl THR A 31 2.668 -4.498 -2.693 1.00 3.86

ATOM 53 CG2 THR A 31 4.764 -5.257 -1.739 1.00 5.25

ATOM 54 C THR A 31 3.826 -3.796 -5.169 1.00 4.51

ATOM 55 O THR A 31 3.240 -2.735 -5.399 1.00 5.34

ATOM 56 N CYS A 32 3.702 -4.868 -5.929 1.00 3.93 Table 1

ATOM 57 CA CYS A 32 2.613 -5.007 -6.868 00 4.54

ATOM 58 CB CYS A 32 2.544 -6.437 -7.399 00 4.46

ATOM 59 SG CYS A 32 4.079 -7.032 -8.198 00 09

ATOM 60 C CYS A 32 1.284 -4.739 -6..190 00 93

ATOM 61 O CYS A 32 1.115 -4.958 -4,.988 00 68

ATOM 62 N ARG A 33 0.327 -4.283 -6. 988 00 56

ATOM 63 CA ARG A 33 -1.063 -4.131 -6.554 00 60

ATOM 64 CB ARG A 33 -1.727 -2.903 -7.189 00 58

ATOM 65 CG ARG A 33 -1.394 -1.536 -6.561 00 77

ATOM 66 CD ARG A 33 0.061 -1.156 -6.719 00 86

ATOM 67 NE ARG A 33 0.346 -0.952 -8.126 00 50

ATOM 68 CZ ARG A 33 .504 -1.190 -8.718 00 4.00

ATOM 69 NHl ARG A 33 .623 -0.916 -10.018 00 5.72

ATOM 70 NH2 ARG A 33 .552 -1.626 -8.062 00 4.44

ATOM 71 C ARG A 33 .860 -5.356 -6.909 00 57

ATOM 72 O ARG A 33 .673 -5.951 -7.981 00 27

ATOM 73 N TYR A 34 -2.749 -5.744 -6.007 00 32

ATOM 74 CA TYR A 34 -3.640 -6.865 -6.205 00 36

ATOM 75 CB TYR A 34 -3.317 -7.993 -5.222 00 4.95

ATOM 76 CG TYR A 34 -2.016 -8.646 -5.535 00 7.06

ATOM 77 CDl TYR A 34 -0.828 -8.078 -5.055 00 8.09

ATOM 78 CEl TYR A 34 0.377 -8.602 -5.348 00 9.03

ATOM 79 CZ TYR A 34 0.460 -9.700 -6.126 00 8.38

ATOM 80 OH TYR A 34 1.754 -10.139 -6.400 00 13.53

ATOM 81 CE2 TYR A 34 -0.677 -10.331 -6.651 00 9.29

ATOM 82 CD2 TYR A 34 948 -9.768 -6.354 00 94

ATOM 83 C TYR A 34 024 -6.349 -5.920 00 78

ATOM 84 O TYR A 34 346 -5.975 -4.788 00 41

ATOM 85 N ALA A 35 851 -6.248 -6.952 00 13

ATOM 86 CA ALA A 35 150 -5.597 -6.815 00 24

ATOM 87 CB ALA A 35 128 -6.496 -6.104 00 56

ATOM 88 C ALA A 35 016 -4.250 -6.091 00 91

ATOM 89 O ALA A 35 811 -3.891 -5.227 00 3.37

ATOM 90 N GLY A 36 991 -3.504 -6.481 00 3.25

ATOM 91 CA GLY A 36 5.754 -2.182 -5.932 00 39

ATOM 92 C GLY A 36 4.972 -2.086 -4.637 00 92

ATOM 93 O GLY A 36 4.577 -0.985 -4.262 00 27

ATOM 94 N VAL A 37 4.777 -3.209 -3.932 00 29

ATOM 95 CA VAL A 37 -4 124 -3.208 -2.631 00 3.32

ATOM 96 CB VAL A 37 4.753 -4.261 -1.,709 00 .50

ATOM 97 CGl VAL A 37 ^■4.079 -4.284 -0.347 00 .68

ATOM 98 CG2 VAL A 37 ^■6.232 -4.027 -1.541 00 .47

ATOM 99 C VAL A 37 ^■2.634 -3.455 -2.812 00 .45

ATOM 100 O VAL A 37 ^■2.239 -4.340 -3.562 00 .64

ATOM 101 N PHE A 38 ^■1.843 -2.670 -2. .091 00 .15

ATOM 102 CA PHE A 38 ^■0.394 -2.831 -2..099 00 .05

ATOM 103 CB PHE A 38 0.279 -1.961 -3.176 00 .89

ATOM 104 CG PHE A 38 0.052 -0.472 -3.049 00 .51

ATOM 105 CDl PHE A 38 1.102 0.357 -2.701 00 .20

ATOM 106 CEl PHE A 38 0.961 1.723 -2. .672 00 ,69

ATOM 107 CZ PHE A 38 ^■0.218 2.280 -2..934 00 ,63

ATOM 108 CE2 PHE A 38 -1 283 1.495 -3.299 00 .24

ATOM 109 CD2 PHE A 38 1.149 0.115 -3.360 00 .20

ATOM 110 C PHE A 38 0.175 -2.553 -0.737 00 .29

ATOM 111 O PHE A 38 0.518 -2.009 0.148 00 .81

ATOM 112 N HIS A 39 417 -2.983 -0.548 00 .04

ATOM 113 CA HIS A 39 163 -2.812 0.702 00 .39

ATOM 114 CB HIS A 39 732 -4.172 1.116 00 .96

ATOM 115 CG HIS A 39 788 -4.125 2.158 00 4.30

ATOM 116 NDl HIS A 39 5.119 -4.197 .832 00 6.82

ATOM 117 CEl HIS A 39 .838 -4.179 .938 00 6.56

ATOM 118 NE2 HIS A 39 .018 -4.110 .964 00 5.13

ATOM 119 CD2 HIS A 39 .728 -4.074 .502 00 5.87

ATOM 120 C HIS A 39 .248 -1.760 0.522 00 3.52

ATOM 121 O HIS A 39 .886 -1.700 -0.522 00 3.77

ATOM 122 N VAL A 40 3.431 -0.939 1.553 00 3.77

ATOM 123 CA VAL A 40 4.451 0.078 1.592 00 4.39

ATOM 124 CB VAL R 40 3.871 1.484 1.542 1.00 5.49 Table 1

ATOM 125 CGl VAL A 40 5.011 2.532 1.395 00 6.77

ATOM 126 CG2 VAL A 40 2.879 1.653 0.405 00 5.98

ATOM 127 C VAL A 40 5.261 -0.081 .875 00 4.23

ATOM 128 O VAL A 40 4.709 -0.160 .968 00 4.31

ATOM 129 N GLU A 41 6.586 -0.138 .705 00 4.59

ATOM 130 CA GLU A 41 7.528 -0.193 .820 00 5.18

ATOM 131 CB GLU A 41 8.349 -1 475 .788 00 6.14

ATOM 132 CG GLU A 41 9.394 .614 .845 00 7.26

ATOM 133 CD GLU A 41 10.080 .947 4.790 00 9.45

ATOM 134 OEl GLU A 41 9.532 .888 .146 00 14.26

ATOM 135 OE2 GLU A 41 11.182 .024 .405 00 12.17

ATOM 136 C GLU A 41 8.401 .035 .722 00 5.32

ATOM 137 O GLU A 41 8.901 .369 .661 00 4.94

ATOM 138 N LYS A 42 8.560 1.725 .844 00 5.62

ATOM 139 CA LYS A 42 9.323 2.971 .928 00 6.62

ATOM 140 CB LYS A 42 8.591 3.995 .801 00 6.87

ATOM 141 CG LYS A 42 9.348 5.278 .981 00 8.29

ATOM 142 CD LYS A 42 8.614 6.214 6.910 00 9.30

ATOM 143 CE LYS A 42 9.365 7.488 7.185 00 10.24

ATOM 144 NZ LYS A 42 8.805 8.170 8.377 00 12.26

ATOM 145 C LYS A 42 10.699 2.696 5.517 00 6.68

ATOM 146 O LYS R 42 10.835 2.156 6.618 00 7.38

ATOM 147 N ASN A 43 11.741 .062 4.774 00 7.11

ATOM 148 CA ASN A 43 13.132 .026 5.244 00 8.35

ATOM 149 CB ASN A 43 13.366 .082 6.330 00 8.69

ATOM 150 CG ASN A 43 13.282 .484 5.798 00 8.34

ATOM 151 ODl ASN A 43 13.519 .728 4.608 00 10.49

ATOM 152 ND2 ASN A 43 12.958 6.431 6.681 00 10.73

ATOM 153 C ASN A 43 13.585 1.669 5.727 00 9.00

ATOM 154 O ASN A 43 14.431 1.571 6.619 00 10.68

ATOM 155 N GLY A 44 13.050 0.619 5.135 00 8.99

ATOM 156 CA GLY A 44 13.518 -0.729 5.401 00 9.85

ATOM 157 C GLY A 44 13.261 .280 6.795 00 9.72

ATOM 158 O GLY A 44 13.906 .251 7.197 00 12.50

ATOM 159 N ARG A 45 12.318 .688 7.523 00 9.67

ATOM 160 CA ARG A 45 12.084 .104 8.903 00 9.44

ATOM 161 CB ARG R 45 13.015 -0.338 9.844 00 12.41

ATOM 162 CG ARG R 45 14.096 162 10.523 00 16.74

ATOM 163 CD ARG R 45 13.673 499 11.942 1.00 19.28

ATOM 164 NE ARG A 45 14.553 476 12.572 00 17.94

ATOM 165 CZ ARG A 45 14.255 760 12.762 00 20.86

ATOM 166 NHl ARG A 45 13.084 238 12.367 00 24.27

ATOM 167 NH2 ARG A 45 15.127 578 13.343 00 19.75

ATOM 168 C ARG A 45 10.654 0.787 9.264 00 8.55

ATOM 169 O ARG A 45 10.086 0.123 8.674 00 8.98

ATOM 170 N TYR A 46 10.104 1.501 10.249 00 7.33

ATOM 171 CA TYR A 46 8.758 1.169 10.777 00 7.51

ATOM 172 CB TYR A 46 8.324 2.174 11.846 00 6.91

ATOM 173 CG TYR A 46 7.889 -3.537 11.357 00 6.22

ATOM 174 CDl TYR R 46 8.488 4.688 11.829 00 6.31

ATOM 175 CEl TYR R 46 8.082 ^■5.924 11.419 00 6.72

ATOM 176 CZ TYR R 46 7.033 6.030 10.522 00 6.27

ATOM 177 OH TYR R 46 6.588 7.262 10.105 00 7.27

ATOM 178 CE2 TYR R 46 6.424 4.896 10.046 00 38

ATOM 179 CD2 TYR R 46 6.844 -3 669 10.472 00 72

ATOM 180 C TYR R 46 8.843 0.221 11.380 00 19

ATOM 181 O TYR A 46 9.552 0.422 12.361 00 9.17

ATOM 182 N SER A 47 8.230 1.212 10.760 00 5.98

ATOM 183 CA SER A 47 3.509 2.598 11.148 00 6.24

ATOM 184 CB SER A 47 9.792 3.087 10.471 00 8.30

ATOM 185 OG SER A 47 9.617 3.174 9.087 00 10.73

ATOM 186 C SER A 47 7.378 3.571 10.909 00 6.20

ATOM 187 O SER A 47 7.573 4.778 11.020 00 6.92

ATOM 188 N ILE A 48 6.190 066 10.627 00 5.42

ATOM 189 CA ILE A 48 5.069 923 10.252 00 5.87

ATOM 190 CB ILE A 48 4.447 469 8.902 00 5.79

ATOM 191 CGl ILE A 48 5.514 396 7.792 00 6.22

ATOM 192 CDl ILE A 48 5.003 2.782 6.504 1.00 6.90 Table 1

ATOM 193 CG2 ILE A 48 3.294 4.390 8.522 .00 7.59

ATOM 194 C ILE A 48 4.039 3.871 11.378 .00 5.87

ATOM 195 O ILE A 48 .587 2.799 11.775 .00 5.84

ATOM 196 N SER A 49 .651 5.032 11.878 ,00 6.10

ATOM 197 CA SER A 49 .558 5.141 12.843 .00 6.66

ATOM 198 CB SER A 49 .666 6.458 13.569 .00 7.07

ATOM 199 OG SER A 49 2.364 7.511 12.669 .00 8.22

ATOM 200 C SER A 49 1.210 5.093 12.130 .00 5.92

ATOM 201 O SER A 49 1.136 5.246 10.909 .00 5.91

ATOM 202 N ARG A 50 0.120 4.939 12.867 .00 7.68

ATOM 203 CA ARG A 50 -1.191 4.862 12.247 .00 7.52

ATOM 204 CB ARG A 50 -2.240 4.488 13.297 .00 9.49

ATOM 205 CG ARG A 50 -3.653 4.371 12.832 .00 11.34

ATOM 206 CD ARG A 50 -3.848 3.536 11.612 .00 16.36

ATOM 207 NE ARG A 50 -5.239 3.467 11.139 .00 17.58

ATOM 208 CZ ARG A 50 -6.061 4.498 10.918 .00 20.18

ATOM 209 NHl ARG A 50 -5.712 5.762 11.148 .00 24.21

ATOM 210 NH2 ARG A 50 .286 4.255 10.479 .00 20.17

ATOM 211 C ARG A 50 .547 6.179 11.539 .00 85

ATOM 212 O ARG A 50 .128 6.157 10.449 .00 47

ATOM 213 N THR A 51 .158 7.307 12.121 .00 84

ATOM 214 CA THR A 51 .433 8.594 11.445 .00 91

ATOM 215 CB THR A 51 -1.265 9.791 12.381 .00 9.18

ATOM 216 OGl THR A 51 -0.006 9.712 13.036 .00 10.02

ATOM 217 CG2 THR A 51 -2.376 9.805 13.422 .00 10.68

ATOM 218 C THR A 51 -0.573 8.768 10.194 .00 7.28

ATOM 219 O THR A 51 .063 9.237 9.150 .00 7.32

ATOM 220 N GLU A 52 .688 8.373 10.264 .00 6.65

ATOM 221 CA GLU A 52 .541 8.455 9.091 .00 6.71

ATOM 222 CB GLU A 52 .004 8.178 9.408 .00 6.97

ATOM 223 CG GLU A 52 .926 8.323 8.206 .00 7.98

ATOM 224 CD GLU A 52 .395 8.514 8.538 .00 9.55

ATOM 225 OEl GLU A 52 .729 8.790 9.721 .00 12.59

ATOM 225 OE2 GLU A 52 6.220 8.445 7.593 .00 10.27

ATOM 227 C GLU A 52 1.043 7.540 7.989 .00 6.23

ATOM 228 O GLU A 52 1.121 7.875 6.808 .00 6.66

ATOM 229 N ALA A 53 0.518 6.381 8.373 .00 5.17

ATOM 230 CA ALA A 53 0.025 5.417 7.392 .00 .58

ATOM 231 CB ALA A 53 -0.457 4.159 8.094 .00 .63

ATOM 232 C ALA A 53 099 6.021 6.561 .00 .89

ATOM 233 O ALA A 53 112 5.937 5.332 .00 .29

ATOM 234 N AALA A 54 058 6.623 7.242 0.50 5.55

ATOM 234 N BALA A 54 846 8.543 1.484 0.50 4.35

ATOM 235 CA AALA A 54 149 7.282 6.560 0.50 6.34

ATOM 235 CA BALA A 54 407 9.748 0.880 0.50 4.38

ATOM 236 CB AALA A 54 4.127 7.828 7.542 0.50 7.27

ATOM 236 CB BALA A 54 3.718 10.779 1.995 0.50 87

ATOM 237 C AALA A 54 ,642 8.379 5.623 0.50 91

ATOM 237 C BALA A 54 ,484 10.332 -0.202 0.50 4.31

ATOM 238 O AALA A 54 ,108 8.519 4.496 0.50 96

ATOM 238 O BALA A 54 ,956 10.811 -1.239 0.50 20

ATOM 239 N ASP A 55 ,698 9.181 6.103 00 87

ATOM 240 CA ASP A 55 ,127 10.253 5.284 00 5.46

ATOM 241 CB ASP A 55 0.208 11.109 6.153 1.00 5.99

ATOM 242 CG ASP A 55 0.985 12.034 7.093 1.00 8.76

ATOM 243 ODl ASP A 55 -2 208 12.136 6.936 1.00 11.48

ATOM 244 OD2 ASP A 55 0.367 12.653 7.983 1.00 10.33

ATOM 245 C ASP A 55 0.385 9.716 4.068 1.00 4.79

ATOM 246 O ASP A 55 0.426 10.297 2.988 00 4.78

ATOM 247 N LEU A 56 0.325 8.616 4.256 00 4.81

ATOM 248 CA LEU A 56 054 8.004 3.177 00 5.77

ATOM 249 CB LEU A 56 865 6.886 3.752 00 6.81

ATOM 250 CG LEU A 56 863 6.252 .848 00 9.79

ATOM 251 CDl LEU A 56 664 7.284 .057 00 10.98

ATOM 252 CD2 LEU A 56 3.761 5.398 .693 00 10.19

ATOM 253 C LEU A 56 0.120 7.478 .094 00 4.95

ATOM 254 O LEU A 56 0.302 7.754 0.909 1 00 5.25

ATOM 255 N ACYS A 57 0.917 6.752 2.491 0.50 4.35 Table 1

ATOM 255 N BCYS A 57 -2.866 8.840 3.492 0.50 1.92

ATOM 256 CA ACYS A 57 -1.894 6.305 1.503 0.50 >.25

ATOM 256 CA BCYS A 57 -4.273 8.891 3.922 0.50 i.23

ATOM 257 CB ACYS A 57 -2, .983 5.448 2.104 0.50 i.62

ATOM 257 CB BCYS A 57 -4.424 9.324 - 5.403 0.50 .07

ATOM 258 SG CYS A 57 -2.343 .842 2.781 0.50 .72

ATOM 259 C ACYS A 57 -2.492 .491 0.755 0.50 .03

ATOM 259 C BCYS A 57 -4.951 .542 -3 627 0.50 .00

ATOM 260 O ACYS A 57 -2, .643 .444 -0.453 0.50 .61

ATOM 260 O BCYS A 57 -5, .611 6.942 -4.484 0.50 .76

ATOM 261 N GLN A 58 -2.850 8.550 1.464 0.50 4.75

ATOM 262 CA GLN A 58 -3.420 9.706 0.792 0.50 5.01

ATOM 263 CB GLN A 58 -3.798 10.787 1.803 0.50 5.50

ATOM 264 CG GLN A 58 -4.439 12.006 1.161 0.50 6.59

ATOM 265 CD GLN A 58 -5.076 12.936 2.159 0.50 8.29

ATOM 266 OEl GLN A 58 -5.212 12.610 3.333 0.50 13.87

ATOM 267 NE2 GLN A 58 -5.489 14.097 1.692 0.50 13.03

ATOM 268 C GLN A 58 -2.468 10.265 -0.267 0.50 4.54

ATOM 269 O GLN A 58 -2.900 10.655 -1.358 0.50 4.25

ATOM 270 N ALA A 59 -1 174 10.307 0.042 .00 4.43

ATOM 271 CA ALA A 59 -0.183 10.796 -0.911 .00 4.79

ATOM 272 CB ALA A 59 1.176 10.867 -0.264 .00 5.67

ATOM 273 C ALA A 59 -0.135 9.946 -2.198 .00 4.57

ATOM 274 O ALA A 59 0.183 10.434 -3.285 .00 4.83

ATOM 275 N PHE A 60 -0.497 8.667 -2.078 .00 4.63

ATOM 276 CA PHE A 60 -0.647 7.761 -3.207 .00 5.22

ATOM 277 CB PHE A 60 -0.365 6.313 -2.783 .00 6.22

ATOM 278 CG PHE A 60 1. 098 5.971 -2.650 .00 5.79

ATOM 279 CDl PHE A 60 1.659 5.676 -1 425 .00 7.76

ATOM 280 CEl PHE A 60 3.006 5.353 1.322 .00 8.00

ATOM 281 CZ PHE A 60 3.761 5.284 2.449 .00 8.38

ATOM 282 CE2 PHE A 60 3.225 5.616 3.665 .00 7.76

ATOM 283 CD2 PHE A 60 1.908 5.940 3.763 .00 7.20

ATOM 284 C PHE A 60 -2.077 7.814 -3 809 00 5.07

ATOM 285 O PHE A 60 -2.434 6.950 4.607 00 6.10

ATOM 286 N ASN A 61 -2.884 8.788 ^■3.401 0.50 4.99

ATOM 287 CA ASN A 61 -4.264 8.897 -3 875 0.50 5.46

ATOM 288 CB ASN A 61 -4.289 9.226 5.365 0.50 6.53

ATOM 289 CG ASN A 61 -5.521 9.996 5.773 0.50 7.92

ATOM 290 ODl ASN A 61 -6.228 10.565 4.944 0.50 9.76

ATOM 291 ND2 ASN A 61 -5.772 10.038 -7 072 0.50 12.78

ATOM 292 C ASN A 61 -5.071 7.635 3.549 0.50 5.18

ATOM 293 O ASN A 61 -5.973 7.217 - 4.281 0.50 5.29

ATOM 294 N SER R 62 -4.737 7.067 2.403 .00 4.58

ATOM 295 CA SER A 62 -5.211 5.781 ^■1.946 .00 5.22

ATOM 296 CB SER A 62 -4 044 4.796 ^■1.989 ,00 4.98

ATOM 297 OG SER A 62 -3 609 548 3.318 ,00 5.94

ATOM 298 C SER A 62 -5.754 918 0.519 ,00 4.78

ATOM 299 O SER A 62 -5.611 980 0.106 ,00 5.72

ATOM 300 N ATHR A 63 -6.333 840 0.002 0.50 4.12

ATOM 300 N BTHR A 63 -11.049 -4.442 5.428 0.50 6.56

ATOM 301 GR ATHR R 63 -6.881 4.815 1.333 0.50 4.70

ATOM 301 CA BTHR R 63 -10.892 -5. 868 5.560 0.50 7.37

ATOM 302 CB ATHR R 63 -8.413 4. 782 1.270 0.50 5.30

ATOM 302 CB BTHR R 63 -11.731 -6.327 6.756 0.50 8.46

ATOM 303 OGl THR A 63 -8.832 3.734 0.382 0.50 6.51

ATOM 304 CG2 THR A 63 -8.998 6.132 0.787 0.50 6.77

ATOM 305 C ATHR A 63 -6.383 3.578 .062 0.50 4.37

ATOM 305 C BTHR A 63 -11.322 -5.624 .287 0.50 6.77

ATOM 306 O ATHR A 63 -5.909 2 623 .428 0.50 5.36

ATOM 306 O BTHR A 63 -10.641 -7 536 .824 0.50 6.96

ATOM 307 N LEO R 64 -6.481 3.556 .378 .00 4.13

ATOM 308 CA LEU R 64 -6.205 2.314 .087 .00 4.56

ATOM 309 CB LEO R 64 -6.253 2.546 .588 .00 5.08

ATOM 310 CG LEO R 64 -5.090 3.359 6.151 ,00 5.90

ATOM 311 CDl LEO R 64 -5.420 3.833 7.559 .00 9.41

ATOM 312 CD2 LEO R 64 -3.840 2.530 6.143 00 7.48

ATOM 313 C LEO R 64 -7.252 1.288 3.668 1.00 4.49 Table 1

ATOM 314 O LED A 64 -8.439 1.612 3.665 1.00 4.99

ATOM 315 N PRO A 65 -6.842 0.066 3.287 1.00 4.43

ATOM 316 CA PRO A 65 -7.824 -0.875 2.824 1.00 3.93

ATOM 317 CB PRO A 65 -6.982 -2.113 2.442 1.00 4.56

ATOM 318 CG PRO A 65 -5.606 -1.561 2.181 1.00 4.40

ATOM 319 CD PRO A 65 -5.477 -0.447 3.159 1.00 4.42

ATOM 320 C PRO A 65 -8.821 -1.276 3.896 1.00 4.37

ATOM 321 O PRO ft 65 -8.488 -1.339 5.061 1.00 5.20

ATOM 322 N ATHR A 66 10.02Q -1.631 3.467 0.50 4.42

ATOM 322 N BTHR A 66 -8.901 -6.156 1.422 0.50 4.53

ATOM 323 CA ATHR A 66 10.920 -2.313 4.353 0.50 5.57

ATOM 323 CA BTHR A 66 -7.712 -6.966 1.640 0.50 4.70

ATOM 324 CB ATHR A 66 12.377 -2.220 3.873 0.50 6.49

ATOM 324 CB BTHR A 66 -7.171 -6.679 3.053 0.50 5.70

ATOM 325 OGl THR A 66 12.507 -2.923 2.629 0.50 5.79

ATOM 326 CG2 THR A 66 12.793 -0.793 3.682 0.50 8.26

ATOM 327 C ATHR A 66 10.530 -3.776 4.416 0.50 5.48

ATOM 327 C BTHR A 66 -7.991 -8.462 1.388 0.50 4.89

ATOM 328 O ATHR A 66 -9.809 -4.308 3.566 0.50 5.06

ATOM 328 O BTHR A 66 -7.140 -9.162 0.862 0.50 4.45

ATOM 329 N MET A 67 11.029 -4.480 5.425 0.50 6.81

ATOM 330 CA MET A 67 10.815 -5.920 5.500 0.50 7.02

ATOM 331 CB MET A 67 11.538 -6.509 6.720 0.50 7.98

ATOM 332 CG MET A 67 11.316 -7.984 6.909 0.50 9.04

ATOM 333 SD MET A 67 -9.612 -8.326 7.369 0.50 11.48

ATOM 334 CE MET A 67 -9.502 -7.661 9.053 0.50 9.78

ATOM 335 C MET A 67 11.303 -6.635 4.234 0.50 6.60

ATOM 336 O MET A 67 10.650 -7.544 3.724 0.50 6.64

ATOM 337 N ASP A 68 12.474 -6.256 3.739 1.00 6.41

ATOM 338 CA ASP A 68 12.997 -6.897 2.537 1.00 7.26

ATOM 339 CB ASP A 68 14.447 -6.472 2.255 1.00 8.60

ATOM 340 CG ASP A 68 15.441 -7.038 3.252 1.00 13.83

ATOM 341 ODl ASP A 68 15.161 -8.096 3.846 1.00 16.32

ATOM 342 OD2 ASP A 68 16.513 -6.415 3.418 1.00 19.16

ATOM 343 C ASP A 68 12.114 -6.642 1.309 1.00 5.98

ATOM 344 O ASP A 68 11.883 -7.537 0.501 1.00 5.29

ATOM 345 N GLN A 69 11.579 -5.426 1.190 1.00 4.75

ATOM 346 CA GLN A 69 10.653 -5.144 0.096 1.00 4.18

ATOM 347 CB GLN A 69 10.286 -3.668 0.045 1.00 3.49

ATOM 348 CG GLN A 69 11.432 -2.816 -0.449 1.00 4.09

ATOM 349 CD GLN A 69 11.282 -1.334 -0.154 1.00 3.Sl

ATOM 350 OEl GLN A 69 10.465 -0.913 0.685 1.00 4.98

ATOM 351 NE2 GLN A 59 12.080 -0.530 -0.827 1.00 5.18

ATOM 352 C GLN A 69 -9.410 -6.003 0.206 1.00 3.79

ATOM 353 O GLN A 69 -8.928 -6.543 -0.807 1.00 3.46

ATOM 354 N AMET A 70 -8.887 -6.163 1.423 0.50 4.35

ATOM 354 N BMET A 70 -5.957 -10.728 -1.344 0.50 4.09

ATOM 355 CA AMET A 70 -7.727 -7.034 1.637 0.50 4.38

ATOM 355 CA BMET A 70 -5.450 -12.054 -0.976 0.50 4.42

ATOM 356 CB AMET A 70 -7.290 -7.011 3.100 0.50 5.11

ATOM 356 CB BMET A 70 -6.037 -12.441 0.375 0.50 4.38

ATOM 357 CG AMET A 70 -6.050 -7.854 3.370 0.50 5.45

ATOM 357 CG BMET A 70 -5.652 -13.821 0.909 0.50 3.97

ATOM 358 SD MET A 70 -4.588 -7.438 2.425 0.50 5.59

ATOM 359 CE MET A 70 -4.526 -5.718 2.975 0.50 5.97

ATOM 360 C AMET A 70 -8.033 -8.468 1.286 0.50 4.62

ATOM 360 C BMET A 70 -5.823 -13.092 -2.030 0.50 4.72

ATOM 361 O AMET A 70 -7.240 -9.142 0.645 0.50 3.92

ATOM 361 O BMET A 70 -4.962 -13.816 -2.559 0.50 4.84

ATOM 362 N LYS A 71 -9.185 -8.945 1.725 1.00 5.04

ATOM 363 CA LYS A 71 -9.539 -10.333 1.419 1.00 5.25

ATOM 364 CB LYS A 71 10.850 -10.714 2.094 1.00 5.83

ATOM 365 CG LYS A 71 10.694 -10.924 3.605 1.00 6.97

ATOM 366 CD LYS A 71 12.005 -11.282 4.302 1.00 8.46

ATOM 367 CE LYS A 71 11.774 -11.561 5.757 1.00 10.85

ATOM 368 NZ LYS A 71 13.064 -11.755 6.487 1.00 13.70

ATOM 369 C LYS A 71 -9.601 -10.597 -0.077 1.00 4.89

ATOM 370 O LYS A 71 -9.134 -11.608 -0.557 1.00 4.70 Table 1

ATOM 371 N LED A 72 -10.153 -9.657 -0.841 1.00 4.09

ATOM 372 CA LED A 72 -10.168 -9.848 -2.288 1.00 4.79

ATOM 373 CB LED A 72 -11.048 -8.802 -2.957 1.00 5.23

ATOM 374 CG LED A 72 -11.271 -9.119 -4.443 1.00 5.95

ATOM 375 CDl LEU A 72 -12.104 -10.380 -4.696 1.00 9.00

ATOM 376 CD2 LED A 72 -11.883 -7.915 -5.131 1.00 7.04

ATOM 377 C LEO A 72 -8.748 -9.831 -2.852 1.00 4.45

ATOM 378 O LEU A 72 -8.388 -10.655 -3.704 1.00 4.44

ATOM 379 N ALft A 73 -7.909 -8.927 -2.353 1.00 3.90

ATOM 380 CA AIA A 73 -6.518 -8.896 -2.802 1.00 4.51

ATOM 381 CB ALA A 73 -5.777 -7.749 -2.144 1.00 4.94

ATOM 382 C ALA A 73 -5.792 -10.211 -2.557 1.00 4.20

ATOM 383 O ALA A 73 -5.097 -10.722 -3.431 1.00 4.12

ATOM 384 N LEU A 74 -5.972 -10.766 -1.372 0.50 4.60

ATOM 385 CA LEU A 74 -5.342 -12.042 -1.055 0.50 4.75

ATOM 386 CB LEU A 74 -5.598 -12.356 0.405 0.50 4.48

ATOM 387 CG LEU A 74 -4.848 -13.543 0.993 0.50 6.03

ATOM 388 CDl LEU A 74 -4.841 -13.402 2.482 0.50 5.26

ATOM 389 CD2 LEU A 74 -5.459 -14.853 0.575 0.50 7.88

ATOM 390 C LEU A 74 -5.828 -13.158 -1.994 0.50 4.86

ATOM 391 O LEU A 74 -5.039 -14.023 -2.410 0.50 4.88

ATOM 392 N SER A 75 -7.109 -13.124 -2.368 1.00 5.39

ATOM 393 CA SER A 75 -7.623 -14.110 -3.307 1.00 5.78

ATOM 394 CB SER A 75 -9.142 -14.046 -3.399 1.00 6.34

ATOM 395 OG SER A 75 -9.577 -13.011 -4.232 1.00 8.06

ATOM 396 C SER A 75 -7.007 -14.023 -4.693 1.00 6.75

ATOM 397 O SER A 75 -7.002 -15.031 -5.412 1.00 8.58

ATOM 398 N LYS A 76 -6.488 -12.850 -5.055 1.00 6.72

ATOM 399 CA LYS A 76 -5.815 -12.589 -6.339 1.00 7.44

ATOM 400 CB LYS A 76 -5.962 -11.116 -6.778 1.00 8.90

ATOM 401 CG LYS A 76 -7.342 -10.536 -6.823 1.00 11.79

ATOM 402 CD LYS A 76 -8.146 -11.204 -7.830 1.00 12.55

ATOM 403 CE LYS A 76 -9.489 -10.492 -8.021 1.00 12.15

ATOM 404 NZ LYS A 76 -10.302 -11.221 -9.002 1.00 11.48

ATOM 405 C LYS A 76 -4.302 -12.863 -6.284 1.00 7.72

ATOM 406 O LYS A 76 -3.615 -12.671 -7.283 1.00 8.84

ATOM 407 N GLY A 77 -3.761 -13.285 -5.143 1.00 6.67

ATOM 408 CA GLY A 77 -2.344 -13.629 -5.063 1.00 6.32

ATOM 409 C GLY A 77 -1.511 -12.788 -4.135 1.00 5.20

ATOM 410 O GLY A 77 -0.300 -12.986 -4.083 1.00 6.14

ATOM 411 N PHE A 78 -2.131 -11.898 -3.367 1.00 4.30

ATOM 412 CA PHE A 78 -1.367 -10.998 -2.503 1.00 4.24

ATOM 413 CB PHE A 78 -2.193 -9.768 -2.149 1.00 4.15

ATOM 414 CG PHE A 78 -1.444 -8.662 -1.466 1.00 3.14

ATOM 415 CDl PHE A 78 -0.159 -8.296 -1.841 1.00 4.38

ATOM 416 CEl PHE A 78 0.471 -7.206 -1.244 1.00 5.15

ATOM 417 CZ PHE A 78 -0.169 -6.500 -0.289 1.00 4.89

ATOM 418 CE2 PHE A 78 -1.449 -6.868 0.106 1.00 5.22

ATOM 419 CD2 PHE A 78 -2.065 -7.929 -0.490 1.00 3.76

ATOM 420 C PHE A 78 -0.972 -11.674 -1.200 1.00 4.08

ATOM 421 O PHE A 78 -1.833 -12.104 -0.434 1.00 4.10

ATOM 422 N GLU A 79 0.335 -11.728 -0.929 1.00 3.86

ATOM 423 CA GLU A 79 0.805 -12.090 0.392 1.00 4.66

ATOM 424 CB GLU A 79 0.952 -13.601 0.599 1.00 5.88

ATOM 425 CG GLU A 79 2.028 -14.226 -0.208 1.00 7.34

ATOM 426 CD GLU A 79 2.278 -15.701 0.150 1.00 7.53

ATOM 427 OEl GLU A 79 2.987 -16.339 -0.648 1.00 10.12

ATOM 428 OE2 GLU A 79 1.766 -16.259 1.162 1.00 6.87

ATOM 429 C GLU A 79 2.093 -11.335 0.681 1.00 4.17

ATOM 430 O GLU A 79 2.821 -10.939 -0.225 1.00 5.23

ATOM 431 N THR A 80 2.334 -11.092 1.958 1.00 3.76

ATOM 432 CA THR A 80 3.588 -10.478 2.410 1.00 4.21

ATOM 433 CB THR A 80 3.451 -8.980 2.785 1.00 4.57

ATOM 434 OGl THR A 80 2.805 -8.893 4.048 1.00 5.14

ATOM 435 CG2 THR A 80 2.700 -8.141 1.731 1.00 5.83

ATOM 436 C THR A 80 4.006 -11.194 3.678 1.00 4.27

ATOM 437 O THR A 80 3.265 -12.002 4.234 1.00 5.07

ATOM 438 N CYS A 81 5.197 -10.874 4.169 1.00 4.97 Table 1

ATOM 439 CA CYS A 81 5.621 -11.328 5.482 1.00 5.43

ATOM 440 CB CYS A 81 6.896 -12.155 5.368 1.00 6.65

ATOM 441 SG CYS A 81 7.318 -13.031 6.888 1.00 9.27

ATOM 442 C CYS A 81 5.850 -10.111 6.365 1.00 5.19

ATOM 443 O CYS A 81 6.841 -10.044 7.080 1.00 7.36

ATOM 444 N ARG A 82 4.903 -9.168 6.333 1.00 4.79

ATOM 445 CA ARG A 82 5.032 -7.922 7.085 1.00 5.53

ATOM 44S CB ARG A 82 5.477 -6.784 6.171 1.00 6.35

ATOM 447 CG ARG A 82 6.816 -6.990 5.506 1.00 8.22

ATOM 448 CD ARG A 82 7.988 -6.904 6.462 1.00 9.19

ATOM 449 NE ARG A 82 8.208 -5.525 6.900 1.00 7.89

ATOM 450 CZ ARG A 82 9.172 -5.139 7.731 1.00 8.09

ATOM 451 NHl ARG A 82 9.273 -3.867 8.088 1.00 7.04

ATOM 452 NH2 ARG A 82 10.058 -6.016 8.185 1.00 9.92

ATOM 453 C ARG A 82 3.743 -7.495 7.681 1.00 5.15

ATOM 454 O ARG A 82 2.736 -7.428 6.973 1.00 6.02

ATOM 455 N TYR A 83 3.782 -7.140 8.961 1.00 4.69

ATOM 456 CA TYR A 83 2.640 -6.480 9.595 1.00 4.44

ATOM 457 CB TYR A 83 2.872 -6.342 11.118 1.00 6.89

ATOM 458 CG TYR A 33 2.857 -7.678 11.805 1.00 7.40

ATOM 459 CDl TYR A 83 4.026 -8.284 12.225 1.00 10.84

ATOM 460 CEl TYR A 83 4.004 -9.560 12.795 1.00 11.76

ATOM 461 CZ TYR A 83 2.797 -10.226 12.922 1.00 9.79

ATOM 462 OH TYR A 83 2.766 -11.497 13.487 1.00 13.70

ATOM 463 CE2 TYR A 83 1.628 -9.634 12.515 1.00 10.83

ATOM 464 CD2 TYR A 83 1.664 -8.361 11.951 1.00 6.97

ATOM 465 C TYR A 83 2.424 -5.098 9.004 1.00 3.45

ATOM 466 O TYR A 83 3.351 -4.336 8.884 1.00 4.88

ATOM 467 N GLY A 84 1.170 -4.761 8.719 1.00 3.42

ATOM 468 CA GLY A 84 0.860 -3.433 8.227 1.00 3.14

ATOM 469 C GLY A 84 -0.537 -3.005 8.531 1.00 2.72

ATOM 470 O GLY A 84 -1.442 -3.814 8.629 1.00 3.57

ATOM 471 N PHE A 85 -0.718 -1.701 8.668 1.00 3.00

ATOM 472 CA PHE A 85 -2.037 -1.156 8.876 1.00 3.40

ATOM 473 CB PHE A 85 -1.991 0.353 9.133 1.00 4.74

ATOM 474 CG PHE A 85 -1.193 0.745 10.309 1.00 4.96

ATOM 475 CDl PHE A 85 0.076 1.250 10.130 1.00 6.89

ATOM 476 CEl PHE A 85 0.830 1.645 11.136 1.00 9.76

ATOM 477 CZ PHE A 85 0.404 1.529 12.364 1.00 7.87

ATOM 478 CE2 PHE A 85 -0.854 1.026 12.666 1.00 8.37

ATOM 479 CD2 PHE A 85 -1.681 0.620 11.582 1.00 7.04

ATOM 480 C PHE A 85 -2.974 -1.344 7.706 1.00 3.84

ATOM 481 O PHE A 85 -2.624 -1.176 6.532 1.00 3.54

ATOM 482 N ILE A 86 -4.203 -1.700 8.074 1.00 3.68

ATOM 483 CA ILE A 86 -5.377 -1.490 7.230 1.00 4.27

ATOM 484 CB ILE A 86 -6.050 -2.777 6.762 1.00 4.44

ATOM 485 CGl ILE A 86 -6.558 -3.620 7.925 1.00 5.43

ATOM 486 CDl ILE A 86 -7.532 -4.705 7.484 1.00 5.98

ATOM 487 CG2 ILE A 86 -5.081 -3.569 5.897 1.00 5.64

ATOM 488 C ILE A 86 -6.312 -0.597 8.029 1.00 4.15

ATOM 489 O ILE A 86 -5.944 -0.084 9.078 1.00 5.16

ATOM 490 N GLO A 87 -7.511 -0.331 7.532 1.00 5.33

ATOM 491 CA GLU A 87 -8.478 0.437 8.314 1.00 6.41

ATOM 492 CB GLU A 87 -9.692 0.795 1.All 1.00 6.87

ATOM 493 CG GLU A 87 -10.628 1.785 8.166 1.00 9.21

ATOM 494 CD GLU A 87 -9.976 3.121 8.445 1.00 13.29

ATOM 495 OEl GLU A 87 -9.361 3.707 7.530 1.00 15.56

ATOM 496 OE2 GLU A 87 -10.079 3.600 9.604 1.00 20.04

ATOM 497 C GLU A 87 -8.906 -0.458 9.473 1.00 7.63

ATOM 498 O GLU A 87 -9.508 -1.511 9.291 1.00 9.71

ATOM 499 N GLY A 88 -8.563 -0.035 10.653 1.00 7.32

ATOM 500 CA GLY A 88 -9.034 -0.654 11.887 1.00 5.95

ATOM 501 C GLY A 88 -8.122 -1.660 12.546 1.00 5.92

ATOM 502 O GLY A 88 -8.254 -1.893 13.727 1.00 6.05

ATOM 503 N ASN A 89 -7.202 -2.281 11.807 1.00 4.20

ATOM 504 CA ASN A 89 -6.385 -3.355 12.363 1.00 4.16

ATOM 505 CB ASN A 89 -7.065 -4.728 12.159 1.00 4.59

ATOM 506 CG ASN A 89 -8.188 -4.962 13.153 1.00 5.48 Table 1

ATOM 507 ODl ASN A 89 -7 923 -5.280 14.333 .00 48

ATOM 508 ND2 ASN A 89 ^•9. 405 -4 .781 12.721 .00 75

ATOM 509 C ASN A 89 . 011 -3.364 11.726 .00 64

ATOM 510 O ASN A 89 .774 -2. 634 10.757 .00 52

ATOM 511 N VAL A 90 . 127 -4 .204 12.253 .00 3.75

ATOM 512 CA VAL A 90 . 811 -4 . 464 11.701 .00 97

ATOM 513 CB VAL A 90 ■1 .731 -4 .203 12.772 .00 52

ATOM 514 CGl VAL A 90 ^■0 .381 -4 . 616 12.285 .00 4.89

ATOM 515 CG2 VAL A 90 .711 -2 . 748 13.156 .00 5.73

ATOM 516 C VAL A 90 . 844 -5. 929 11.277 .00 4.07

ATOM 517 O VAL A 90 -3 240 -6. 798 12.063 .00 4.68

ATOM 518 N VAL A 91 . 431 -6. 200 10.050 .00 3.98

ATOM 519 CA VAL A 91 . 633 -7 . 518 9.441 .00 4.29

ATOM 520 CB VAL A 91 -3 898 -7 . 566 8.552 .00 4.68

ATOM 521 CGl VAL A 91 . 136 -7 . 132 9.305 .00 5.28

ATOM 522 CG2 VAL A 91 .716 -6. 720 7.283 .00 5.79

ATOM 523 C VAL A 91 -1 438 -7 . 948 8.624 .00 4.43

ATOM 524 O VAL A 91 0. 576 -7 . 148 8.284 .00 .67

ATOM 525 N ILE A 92 . 430 -9. 244 8.289 .00 .66

ATOM 526 CA ILE A 92 -0. 526 -9. 810 7.277 .00 .16

ATOM 527 CB ILE A 92 0 . 627 -10.665 7.860 .00 .16

ATOM 528 CGl ILE A 92 1 . 426 -9.921 8.905 .00 .28

ATOM 529 CDl ILE A 92 2 . 655 -10.646 9.416 .00 9.30

ATOM 530 CG2 ILE A 92 1 .523 -11.106 6.768 .00 6.89

ATOM 531 C ILE A 92 358 -10.737 6.389 .00 4.60

ATOM 532 O ILE A 92 901 -11.686 6.912 .00 5.00

ATOM 533 N PRO A 93 425 -10.466 5.080 .00 4.02

ATOM 534 CA PRO A 93 067 -11.411 4.191 .00 3.46

ATOM 535 CB PRO A 93 -2.323 -10.566 2.936 .00 4.12

ATOM 53S CG PRO A 93 -1.215 -9.562 2.921 .00 4.56

ATOM 537 CD PRO A 93 -0.853 -9.310 4.347 .00 4.09

ATOM 538 C PRO A 93 -1.151 -12.582 907 .00 3.40

ATOM 539 O PRO A 93 -0.001 -12.379 508 .00 3.49

ATOM 540 N ARG A 94 -1.663 -13.792 094 .00 3.73

ATOM 541 CA ARG A 94 -0.874 -15.001 908 .00 4.20

ATOM 542 CB ARG A 94 -0.594 -15.673 5.257 .00 4.92

ATOM 543 CG ARG A 94 0.342 -14.908 6.198 .00 5.09

ATOM 544 CD ARG A 94 1.714 -14.619 5.618 .00 5.34

ATOM 545 NE ARG A 94 2..389 -15.814 5.104 .00 5.52

ATOM 546 CZ ARG A 94 3..395 -15.805 4.243 .00 6.57

ATOM 547 NHl ARG A 94 3..885 -14.675 3.758 .00 7.91

ATOM 548 NH2 ARG A 94 3..954 -16.949 3. .889 .00 8.71

ATOM 549 C ARG A 94 -1..578 -16.005 3..025 .00 3.26

ATOM 550 O ARG A 94 -2..728 -16.366 3..275 .00 4.11

ATOM 551 N ILE A 95 -0.891 -16.477 1..993 .00 4.16

ATOM 552 CA ILE A 95 -1.410 -17.547 1..145 .00 4.82

ATOM 553 CB ILE A 95 -1.151 -17.229 -0.342 .00 4.76

ATOM 554 CGl ILE A 95 985 -16.008 -0.765 .00 5.48

ATOM 555 CDl ILE A 95 621 -15.395 -2.064 .00 6.96

ATOM 556 CG2 ILE A 95 -1.514 -18.439 -1.216 .00 4.45

ATOM 557 C ILE A 95 -0 0.771 -18.854 1.573 .00 4.27

ATOM 558 O ILE A 95 1.473 -19.816 1 874 .00 4.57

ATOM 559 N HIS A 96 0.556 -18.881 1 656 ,00 4.72

ATOM 560 CA HIS A 96 1.277 -20.107 1 989 ,00 5.81

ATOM 561 CB HIS A 96 2.513 -20.227 1 115 ,00 6.80

ATOM 562 CG HIS A 96 2.224 -20.072 -0.338 ,00 8.04

ATOM 563 NDl HIS A 96 1.758 -21.090 -1.147 1.00 10.65

ATOM 564 CEl HIS A 96 1.564 -20.618 -2.371 1.00 8.50

ATOM 565 NE2 HIS A 96 1.886 -19.337 -2.381 1.00 12.57

ATOM 566 CD2 HIS A 96 2.297 -18.977 -1.123 00 7.91

ATOM 567 C HIS A 96 1.666 -20.076 3.455 00 6.20

ATOM 568 O HIS A 96 2.115 -19.051 3.949 00 8.18

ATOM 569 N PRO A 97 1.478 -21.181 4.177 00 5.74

ATOM 570 CA PRO A 97 1.925 -21.200 5.564 00 6.56

ATOM 571 CB PRO A 97 1.375 -22.528 6.092 00 7.23

ATOM 572 CG PRO A 97 1.132 -23.326 4.943 00 6.73

ATOM 573 CD PRO A 97 0.807 -22.433 3.804 00 5.58

ATOM 574 C PRO A 97 3.447 -21.127 5.685 1.00 6.86 Table 1

ATOM 575 O PRO A 97 4.168 -21.901 5.070 1.00 8.25

ATOM 576 N ASN A 98 3.930 -20.162 6.459 1.00 7.81

ATOM 577 CA ASN A 98 5.366 -20.030 6.752 1.00 8.50

ATOM 578 CB ASN A 98 5.962 -18.896 5.918 1.00 9.12

ATOM 579 CG ASN A 98 7.473 -18.775 6.053 1.00 10.62

ATOM 580 ODl ASN A 98 8.005 -18.671 7.163 1.00 15.41

ATOM 581 ND2 ASN A 98 8.168 -18.740 4.915 1.00 16.91

ATOM 582 C ASN A 98 5.520 -19.734 8.231 1.00 9.17

ATOM 583 O ASN A 98 4.847 -18.857 8.767 1.00 9.37

ATOM 584 N ALA A 99 6.401 -20.469 8.900 1.00 10.01

ATOM 585 CA ALA A 99 6.496 -20.391 10.341 1.00 10.45

ATOM 586 CB ALA A 99 7.421 -21.475 10.882 1.00 10.70

ATOM 587 C ALA A 99 6.927 -19.040 10.887 1.00 10.87

ATOM 588 O ALA A 99 6.628 -18.786 12.037 1.00 12.58

ATOM 589 N ILE A 100 7.609 -18.204 10.095 1.00 11.84

ATOM 590 CA ILE A 100 8.047 -16.877 10.587 1.00 12.32

ATOM 591 CB ILE A 100 9.556 -16.623 10.371 1.00 12.86

ATOM 592 CGl ILE A 100 9.915 -16.582 8.885 1.00 14.40

ATOM 593 CDl ILE A 100 11.351 -16.030 8.591 1.00 14.80

ATOM 594 CG2 ILE A 100 10.368 -17.677 11.119 1.00 13.59

ATOM 595 C ILE A 100 7.252 -15.741 9.973 1.00 11.83

ATOM 596 O ILE A 100 7.613 -14.565 10.106 1.00 12.51

ATOM 597 N CYS A 101 6.135 -16.080 9.341 1.00 10.59

ATOM 593 CA CYS A 101 5.234 -15.074 8.805 1.00 10.71

ATOM 599 CB CYS A 101 5.201 -15.144 7.283 1.00 9.75

ATOM 600 SG CYS A 101 6.771 -14.967 6.509 1.00 10.67

ATOM 601 C CYS A 101 3.852 -15.337 9.352 1.00 9.98

ATOM 602 O CYS A 101 3.131 -16.183 8.826 1.00 11.79

ATOM 603 N ALA A 102 3.456 -14.633 10.394 1.00 10.10

ATOM 604 CA ALA A 102 2.172 -14.905 11.041 1.00 10.36

ATOM 605 CB ALA A 102 1.006 -14.606 10.094 1.00 11.31

ATOM 606 C ALA A 102 2.068 -16.340 11.566 1.00 11.02

ATOM 607 O ALA A 102 1.003 -16.953 11.567 1.00 10.91

ATOM 608 N ALA A 103 3.195 -16.864 12.021 1.00 11.15

ATOM 609 CA ALA A 103 3.236 -18.142 12.729 1.00 11.15

ATOM 610 CB ALA A 103 2.712 -17.963 14.139 1.00 11.84

ATOM 611 C ALA A 103 2.452 -19.221 11.998 1.00 10.92

ATOM 612 O ALA A 103 1.615 -19.928 12.577 1.00 10.92

ATOM 613 N ASN A 104 2.722 -19.334 10.709 1.00 9.93

ATOM 614 CA ASN A 104 2.187 -20.399 9.892 1.00 9.79

ATOM 615 CB ASN A 104 2.458 -21.743 10.570 1.00 10.06

ATOM 616 CG ASN A 104 2.918 -22.769 9.619 1.00 9.84

ATOM 617 ODl ASN A 104 2.456 -23.914 9.661 1.00 16.23

ATOM 618 ND2 ASN A 104 3.855 -22.413 8.768 1.00 9.06

ATOM 619 C ASN A 104 0.707 -20.280 9.506 1.00 9.74

ATOM 620 O ASN A 104 0.163 -21.173 8.863 1.00 10.54

ATOM 621 N HIS A 105 0.077 -19.155 9.840 1.00 8.96

ATOM 622 CA HIS A 105 -1.333 -18.946 9.526 1.00 8.60

ATOM 623 CB HIS A 105 -1.895 -17.787 10.364 1.00 9.72

ATOM 624 CG HIS A 105 -2.177 -18.145 11.790 1.00 12.50

ATOM 625 NDl HIS A 105 -3.457 -18.356 12.245 1.00 15.96

ATOM 626 CEl HIS A 105 -3.422 -18.650 13.535 1.00 16.18

ATOM 627 NE2 HIS A 105 -2.165 -18.626 13.933 1.00 15.81

ATOM 628 CD2 HIS A 105 -1.367 -18.291 12.863 1.00 14.02

ATOM 629 C HIS A 105 -1.507 -13.588 8.051 1.00 7.65

ATOM 630 O HIS A 105 -0.572 -18.120 7.412 1.00 8.02

ATOM 631 N THR A 106 -2.699 -18.868 7.522 1.00 6.48

ATOM 632 CA THR A 106 -3.090 -18.421 6.178 1.00 6.38

ATOM 633 CB THR A 106 -3.367 -19.566 5.188 1.00 7.31

ATOM 634 OGl THR A 106 -4.533 -20.299 5.582 1.00 7.93

ATOM 635 CG2 THR A 106 -2.172 -20.512 5.059 1.00 7.80

ATOM 636 C THR A 106 -4.319 -17.545 6.294 1.00 5.91

ATOM 637 O THR A 106 -5.008 -17.549 7.299 1.00 6.64

ATOM 638 N GLY A 107 -4.593 -16.780 5.246 1.00 4.78

ATOM 639 CA GLY A 107 -5.710 -15.856 5.285 1.00 5.06

ATOM 640 C GLY A 107 -5.211 -14.475 5.664 1.00 4.25

ATOM 641 O GLY A 107 -4.005 -14.230 5.698 1.00 4.81

ATOM 642 N VAL A 108 -6.137 -13.560 5.893 1.00 4.88 Table 1

ATOM 643 CA VAL A 108 5.748 -12.261 .402 00 .59

ATOM 644 CB VAL A 108 6.783 -11.182 .054 00 .37

ATOM 645 CGl VAL A 108 6.336 -9.819 .614 00 .82

ATOM 646 CG2 VAL A 108 6.976 -11.085 .577 00 .05

ATOM 647 C VAL A 108 -5 543 -12.378 .895 00 .08

ATOM 648 O VAL A 108 6.529 -12.412 8.654 00 8.57

ATOM 649 N TYR A 109 4.282 -12.499 8.321 00 5.81

ATOM 650 CA TYR A 109 970 -12.721 9.735 00 6.25

ATOM 651 CB TYR A 109 594 -13.335 9.906 00 8.00

ATOM 652 CG TYR A 109 278 -13.521 11.362 00 9.04

ATOM 653 CDl TYR A 109 842 -14.571 12.086 00 10.15

ATOM 654 CEl TYR A 109 607 -14.721 13.442 00 11.46

ATOM 655 CZ TYR A 109 802 -13.813 14.081 00 12.32

ATOM 656 OH TYR A 109 588 -14.003 15.430 00 13.59

ATOM 657 CE2 TYR A 109 235 -12.754 13.395 00 11.78

ATOM 658 CD2 TYR A 109 485 -12.615 12.033 00 10.27

ATOM 659 C TYR A 109 033 -11.382 10.450 .00 .61

ATOM 660 O TYR A 109 398 -10.428 10.038 .00 .10

ATOM 661 N ILE A 110 4.787 -11.341 11.538 .00 .22

ATOM 662 CA ILE A 110 4 924 -10.123 12.323 .00 .34

ATOM 663 CB ILE A 110 6.395 -9.904 12.750 .00 .63

ATOM 664 CGl ILE A 110 -7.333322 -9.867 11.534 .00 6.39

ATOM 665 CDl ILE A 110 8.784 -10.032 11.911 .00 8.51

ATOM 666 CG2 ILE A 110 6.573 -8.615 13.550 .00 6.62

ATOM 667 C ILE A 110 4.013 --1100..118822 13.544 .00 5.22

ATOM 668 O ILE A 110 4.085 -11.107 14.363 .00 6.41

ATOM 669 N LEO A 111 3.176 -9.171 13.694 .00 4.92

ATOM 670 CA LEO A 111 ^■2 320 -9.066 14.862 .00 4.71

ATOM 671 CB LEO A 111 ^■1 . 371 -7, 879 14.690 .00 5.00

ATOM 672 CG LEO A 111 0 . 446 -7.563 15.859 .00 5.81

ATOM 673 CDl LEU A 111 0 . 438 -8 . 715 16.195 .00 6.28

ATOM 674 CD2 LEO A 111 0 . 371 -6. 335 15.517 .00 6.88

ATOM 675 C LEO A 111 191 -8 . 830 16.070 .00 4.83

ATOM 676 O LEO A 111 O i l -7 , 914 16.078 .00 5.31

ATOM 677 N VAL A 112 026 -9.655 17.089 .00 3.37

ATOM 678 CA VAL A 112 833 -9.554 18.287 .00 3.79

ATOM 679 CB VAL A 112 305 -10.933 18.766 .00 3.80

ATOM 680 CGl VAL A 112 108 -10.834 20.051 .00 4.23

ATOM 681 CG2 VAL A 112 123 -11.609 17.702 .00 49

ATOM 682 C VAL A 112 090 -8.796 19.388 .00 00

ATOM 683 O VAL A 112 603 -7.806 19.872 .00 24

ATOM 684 N THR A 113 911 -9.250 19.777 .00 25

ATOM 685 CA THR A 113 218 -8.714 20.934 .00 07

ATOM 686 CB THR A 113 034 -9.768 22.024 .00 95

ATOM 687 OGl THR A 113 312 -10.274 22.405 .00 07

ATOM 688 CG2 THR A 113 -0 . 326 -9.206 23.228 .00 24

ATOM 689 C THR A 113 0 . 133 -8.183 20.527 .00 90

ATOM 690 O THR A 113 0 . 992 -8.923 20..031 .00 88

ATOM 691 N SER A 114 0 . 342 -6.897 20..763 .00 07

ATOM 692 CA SER A 114 1 . 644 -6.270 20.566 .00 2.22

ATOM 693 CB SER A 114 1 . 775 -5.754 19.140 .00 2.61

ATOM 694 OG SER A 114 981 -5.030 18.996 .00 2.95

ATOM 695 C SER A 114 786 -5.127 21.541 .00 16

ATOM 696 O SER A 114 0.830 -4.417 21.852 .00 98

ATOM 697 N ASN A 115 004 -4.887 22.020 .00 19

ATOM 698 CA ASN A 115 267 -3.709 22.871 .00 00

ATOM 699 CB ASN A 115 640 -3.797 23.579 .00 00

ATOM 700 CG ASN A 115 706 -4.753 24.763 .00 00

ATOM 701 ODl ASN A 115 709 -5.137 25.373 .00 18

ATOM 702 ND2 ASN A 115 957 -5.055 25.160 .00 00

ATOM 703 C ASN A 115 304 -2.402 22.065 .00 05

ATOM 704 O ASN A 115 3. 151 -1.337 22.652 .00 23

ATOM 705 N THR A 116 3 . 666 -2.495 20.794 .00 20

ATOM 706 CA THR A 116 4 . 222 -1.361 20.037 1.00 2.21

ATOM 707 CB THR A 116 5 . 576 -1.779 19.442 1.00 2.69

ATOM 708 OGl THR A 116 5 . 369 -2.950 18.653 1.00 2.79

ATOM 709 CG2 THR A 116 6. 634 -2.082 20.522 1.00 2.68

ATOM 710 C THR A 116 3 . 301 -0.898 18.934 1.00 2.23 Table 1

ATOM 711 O THR A 116 2.325 -1.558 18.598 1.00 2.77

ATOM 712 N SER A 117 3.602 0.270 18.374 1.00 2.65

ATOM 713 CA SER A 117 2.647 1.016 17.563 1.00 2.75

ATOM 714 CB SER A 117 2.417 2.347 18.236 1.00 3.30

ATOM 715 OG SER A 117 3.580 3.158 18.180 1.00 4.74

ATOM 716 C SER A 117 3.049 1.287 16.126 1.00 3.28

ATOM 717 O SER R 117 2.273 1.913 15.408 1.00 4.15

ATOM 713 N HIS A 118 4.236 0.845 15.711 1.00 3.03

ATOM 719 CA HIS A 118 4.789 1.181 14.388 1.00 2.95

ATOM 720 CB HIS A 118 6.132 1.910 14.506 1.00 3.85

ATOM 721 CG HIS A 118 5.982 3.345 14.912 1.00 4.49

ATOM 722 NDl HIS A 118 6.815 4.344 14.471 1.00 10.19

ATOM 723 CEl HIS A 118 6.439 5.494 15.005 1.00 7.50

ATOM 724 NE2 HIS A 118 5.400 5.278 15.787 1.00 7.17

ATOM 725 CD2 HIS A 118 5.122 3.934 15.779 1.00 4.82

ATOM 726 C HIS A 118 4.918 -0.048 13.529 1.00 3.56

ATOM 727 O HIS A 118 5.555 -1.025 13.928 1.00 4.03

ATOM 728 N TYR A 119 4.336 0.037 12.334 1.00 2.99

ATOM 729 CA TYR A 119 4.301 -1.102 11.437 1.00 3.41

ATOM 730 CB TYR A 119 2.968 -1.841 11.552 1.00 3.42

ATOM 731 CG TYR A 119 2.691 -2.347 12.945 1.00 3.67

ATOM 732 CDl TYR A 119 1.883 -1.634 13.813 1.00 3.93

ATOM 733 CEl TYR A 119 1.646 -2.090 15.091 1.00 3.37

ATOM 734 CZ TYR A 119 2.217 -3.247 15.524 1.00 2.88

ATOM 735 OH TYR A 119 2.033 -3.738 16.800 1.00 4.09

ATOM 736 CE2 TYR A 119 3.025 -3.961 14.685 1.00 2.80

ATOM 737 CD2 TYR A 119 3.247 -3.513 13.398 1.00 2.76

ATOM 738 C TYR A 119 4.597 -0.635 10.031 1.00 3.41

ATOM 739 O TYR A 119 5.127 0.469 9.844 1.00 4.49

ATOM 740 N ASP A 120 4.381 -1.498 9.040 1.00 3.34

ATOM 741 CA ASP A 120 4.323 -1.010 7.661 1.00 3.35

ATOM 742 CB ASP A 120 4.738 -2.112 6.669 1.00 3.73

ATOM 743 CG ASP A 120 6.158 -2.594 6.829 1.00 3.83

ATOM 744 ODl ASP A 120 6.979 -1.959 7.510 1.00 4.03

ATOM 745 OD2 ASP A 120 6.419 -3.620 6.203 1.00 5.42

ATOM 746 C ASP A 120 2.876 -0.562 7.397 1.00 3.66

ATOM 747 O ASP A 120 2.075 -0.486 8.328 1.00 3.42

ATOM 748 N THR A 121 2.538 -0.226 6.159 1.00 3.93

ATOM 749 CA THR A 121 1.125 0.010 5.833 1.00 3.65

ATOM 750 CB THR A 121 0.762 1.524 5.776 1.00 4.38

ATOM 751 OGl THR A 121 0.639 1.674 5.839 1.00 5.03

ATOM 752 CG2 THR A 121 1.302 2.223 4.557 1.00 5.72

ATOM 753 C THR A 121 0.731 -0.694 4.554 1.00 3.54

ATOM 754 O THR A 121 1.569 -0.961 3.676 1.00 4.44

ATOM 755 N TYR A 122 0.565 -0.953 4.451 1.00 2.96

ATOM 755 CA TYR A 122 1.186 -1.284 3.196 1.00 3.15

ATOM 757 CB TYR A 122 2.115 -2.517 3.348 1.00 3.05

ATOM 758 CG TYR A 122 1.330 -3.722 3.788 1.00 3.58

ATOM 759 CDl TYR A 122 1.225 -4.089 5.116 1.00 3.96

ATOM 760 CEl TYR A 122 0.416 -5.139 5.503 1.00 3.80

ATOM 761 CZ TYR A 122 0.262 -5.861 4.577 1.00 4.10

ATOM 762 OH TYR A 122 1.100 -6.887 4.947 1.00 4.56

ATOM 763 CE2 TYR A 122 0.139 -5.551 3.252 1.00 3.26

ATOM 764 CD2 TYR A 122 0.644 -4.475 2.861 1.00 3.84

ATOM 765 C TYR A 122 1.965 -0.087 2.720 1.00 3.49

ATOM 766 O TYR A 122 2.369 0.753 3.511 1.00 3.72

ATOM 767 N CYS A 123 2.170 -0.018 1.406 1.00 3.90

ATOM 768 CA CYS A 123 2.911 1.075 0.774 1.00 3.85

ATOM 769 CB CYS A 123 1.995 2.119 0.152 1.00 4.43

ATOM 770 SG CYS A 123 0.952 3.030 1.353 1.00 7.79

ATOM 771 C CYS A 123 3.766 0.477 -0.326 1.00 3.54

ATOM 772 O CYS A 123 3.446 -0.564 -0.873 1.00 3.88

ATOM 773 N PHE A 124 4.840 1.185 -0.655 1.00 2.86

ATOM 774 CA PHE A 124 5.803 0.758 -1.649 1.00 3.11

ATOM lib CB PHE A 124 7.139 0.331 -1.014 1.00 3.67

ATOM 776 CG PHE A 124 8.224 0.149 -2.037 1.00 3.18

ATOM 111 CDl PHE A 124 8.131 -0.846 -3.001 1.00 4.26

ATOM 778 CEl PHE A 124 9.079 -0.985 -3.974 1.00 4.18 Table 1

ATOM 779 CZ PHE A 124 -10.119 -0.126 -4.029 1.00 3.55

ATOM 780 CE2 PHE A 124 -10.235 0.883 -3.095 1.00 3.39

ATOM 781 CD2 PHE A 124 -9.280 1.040 -2.124 1.00 3.47

ATOM 782 C PHE A 124 -6.040 1.881 -2.651 1.00 2.93

ATOM 783 O PHE A 124 -6.508 2.938 -2.278 1.00 3.31

ATOM 784 N ASN A 125 -5.741 1.596 -3.920 1.00 3.27

ATOM 785 CA ASN A 125 -5.973 2.510 -5.022 1.00 3.79

ATOM 786 CB ASN A 125 -4.688 2.583 -5.836 1.00 4.41

ATOM 787 CG ASN A 125 -4.833 3.416 -7.081 1.00 7.26

ATOM 788 ODl ASN A 125 -5.855 4.086 -7.285 1.00 6.26

ATOM 789 ND2 ASN A 125 -3.841 3.308 -7.969 1.00 10.18

ATOM 790 C ASN A 125 -7.091 1.961 -5.901 1.00 3.77

ATOM 791 O ASN A 125 -6.914 0.998 -6.648 1.00 3.57

ATOM 792 N ALA A 126 -8.241 2.611 -5.836 1.00 3.69

ATOM 793 CA ALA A 126 -9.428 2.166 -6.567 1.00 4.58

ATOM 794 CB ALA A 126 -10.658 2.961 -6.122 1.00 6.03

ATOM 795 C ALA A 126 -9.254 2.273 -8.069 1.00 5.13

ATOM 796 O ALA A 126 -9.991 1.605 -8.791 1.00 6.66

ATOM 797 N SER A 127 -8.291 3.045 -8.563 1.00 4.43

ATOM 798 CA SER A 127 -8.066 3.207 -10.001 1.00 4.95

ATOM 799 CB SER A 127 -7.598 4.636 -10.282 1.00 6.59

ATOM 800 OG SER A 127 -8.635 5.531 -9.923 1.00 9.32

ATOM 801 C SER A 127 -7.078 2.199 -10.578 1.00 4.89

ATOM 802 O SER A 127 -6.844 2.201 -11.782 1.00 6.25

ATOM 803 N ALA A 128 -6.503 1.339 -9.747 1.00 4.16

ATOM 804 CA ALA A 128 -5.619 0.290 -10.220 1.00 4.34

ATOM 805 CB ALA A 128 -4.964 -0.399 -9.016 1.00 5.08

ATOM 806 C ALA A 128 -6.388 -0.735 -11.050 1.00 4.17

ATOM 807 O ALA A 128 -7.595 -0.838 -10.963 1.00 4.27

ATOM 808 N PRO A 129 -5.666 -1.556 -11.816 1.00 4.47

ATOM 809 CA PRO A 129 -6.328 -2.681 -12.479 1.00 4.26

ATOM 810 CB PRO A 129 -5.172 -3.336 -13.253 1.00 4.71

ATOM 811 CG PRO A 129 -4.180 -2.227 -13.456 1.00 4.99

ATOM 812 CD PRO A 129 -4.244 -1.482 -12.155 1.00 4.88

ATOM 813 C PRO A 129 -6.948 -3.680 -11.490 1.00 5.27

ATOM 814 O PRO A 129 -6.621 -3.721 -10.294 1.00 4.71

ATOM 815 N PRO A 130 -7.879 -4.482 -11.979 1.00 4.31

ATOM 816 CA PRO A 130 -8.620 -5.357 -11.083 1.00 4.47

ATOM 817 CB PRO A 130 -9.813 -5.792 -11.942 1.00 5.11

ATOM 818 CG PRO A 130 -9.308 -5.720 -13.343 1.00 4.51

ATOM 819 CD PRO A 130 -8.415 -4.515 -13.350 1.00 4.65

ATOM 820 C PRO A 130 -7.873 -6.570 -10.535 1.00 4.82

ATOM 821 O PRO A 130 -8.241 -7.082 -9.472 1.00 5.18

ATOM 822 N GLD A 131 -6.837 -7.018 -11.233 1.00 4.71

ATOM 823 CA GLO A 131 -6.123 -8.211 -10.814 1.00 5.15

ATOM 824 CB GLU A 131 -6.118 -9.255 -11.938 1.00 6.89

ATOM 825 CG GLD A 131 -7.351 -9.267 -12.855 1.00 9.23

ATOM 826 CD GLO A 131 -8.632 -9.691 -12.204 1.00 11.10

ATOM 827 OEl GLD A 131 -9.709 -9.581 -12.878 1.00 13.49

ATOM 828 OE2 GLO A 131 -8.588 -10.174 -11.061 1.00 14.38

ATOM 829 C GLO A 131 -4.731 -7.858 -10.286 1.00 5.29

ATOM 830 O GLO A 131 -4.596 -6.926 -9.532 1.00 5.70

ATOM 831 N GLO A 132 -3.690 -8.589 -10.671 1.00 5.39

ATOM 832 CA GLO A 132 -2.328 -8.298 -10.266 1.00 5.66

ATOM 833 CB GLO A 132 -1.459 -9.563 -10.301 1.00 6.70

ATOM 834 CG GLO A 132 -0.005 -9.340 -9.935 1.00 8.54

ATOM 835 CD GLU A 132 0.844 -10.604 -10.088 1.00 11.32

ATOM 836 OEl GLU A 132 1.450 -11.047 -9.087 1.00 18.15

ATOM 837 OE2 GLD A 132 0.927 -11.115 -11.217 1.00 16.13

ATOM 838 C GLD A 132 -1.725 -7.283 -11.211 1.00 4.54

ATOM 839 O GLO A 132 -1.787 -7.462 -12.413 1.00 6.22

ATOM 840 N ASP A 133 -1.167 -6.212 -10.661 1.00 4.65

ATOM 841 CA ASP A 133 -0.469 -5.199 -11.441 1.00 4.14

ATOM 842 CB ASP A 133 -1.207 -3.860 -11.388 1.00 4.04

ATOM 843 CG ASP A 133 -0.501 -2.772 -12.175 1.00 5.18

ATOM 844 ODl ASP A 133 0.403 -3.106 -12.944 1.00 6.34

ATOM 845 OD2 ASP A 133 -0.886 -1.594 -12.071 1.00 6.34

ATOM 846 C ASP A 133 0.933 -5.051 -10.880 1.00 4.14 Table 1

ATOM 847 O ASP A 133 116 -4.483 -9.814 .00 4.28

ATOM 848 N CYS A 134 906 -5.582 11.600 .00 4.49

ATOM 849 CA CYS A 134 306 -5.520 ^■11.193 .00 5.13

ATOM 850 CB CYS A 134 992 -6.881 11.247 .00 6.53

ATOM 851 SG CYS A 134 424 -7.981 -9.922 .00 9.93

ATOM 852 C CYS A 134 091 -4.477 11.957 .00 4.90

ATOM 853 O CYS A 134 5.326 -4.491 11.898 .00 6.04

ATOM 854 N THR A 135 408 -3.554 12.615 .00 4.41

ATOM 855 CA THR A 135 104 -2.445 13.226 .00 4.76

ATOM 856 CB THR A 135 3.233 -1.681 14.202 .00 5.36

ATOM 857 OGl THR A 135 2.106 -1.129 13.507 .00 5.69

ATOM 858 CG2 THR A 135 2.757 -2.587 15.336 .00 5.99

ATOM 859 C THR A 135 4.620 -1.522 12.147 .00 4.79

ATOM 860 O THR A 135 4.130 -1.515 11.022 .00 6.62

ATOM 861 N SER A 136 5.664 -0.771 12.473 .00 4.75

ATOM 862 CA SER A 136 6.262 0.121 11.477 .00 6.30

ATOM 863 CB SER A 136 7.568 0.671 11.978 .00 7.91

ATOM 864 OG SER A 136 8.492 -0.365 12.074 .00 12.74

ATOM 865 C SER A 136 5.389 1.289 11.120 .00 6.25

ATOM 866 O SER A 136 4.688 1.867 11.958 .00 7.40

ATOM 867 N VAL A 137 5.471 1.667 -9.854 .00 6.38

ATOM 868 CA VAL A 137 4.856 2.891 -9.357 .00 7.87

ATOM 869 CB VAL A 137 528 2.746 -7.883 .00 6.65

ATOM 870 CGl VAL A 137 947 4.054 -7.335 .00 7.71

ATOM 871 CG2 VAL A 137 592 1.571 -7.691 .00 7.51

ATOM 872 C VAL A 137 848 4.000 -9.581 .00 8.61

ATOM 873 O VAL A 137 001 3.900 -9.186 .00 8.42

ATOM 874 N ATHR A 138 379 5.077 10.216 0.50 11.49

ATOM 874 N BTHR A 138 -0.215 12.876 -4.795 0.50 6.87

ATOM 875 CA ATHR A 138 6.238 6.131 10.709 0.50 13.59

ATOM 875 CA BTHR A 138 -0.865 13.778 -3.907 0.50 6.17

ATOM 876 CB ATHR A 138 6.094 6.271 12.243 0.50 15.41

ATOM 876 CB BTHR A 138 -2. .105 13.094 -3.374 0.50 6.52

ATOM 877 OGl THR A 138 4..800 6.801 12.524 0.50 20.01

ATOM 878 CG2 THR A 138 6.239 4.937 -12.944 0.50 17.28

ATOM 879 C ATHR A 138 5.887 7.499 -10.132 0.50 13.99

ATOM 879 C BTHR A 138 0.044 14.295 -2.799 0.50 5.76

ATOM 880 O ATHR A 138 6.470 8.495 -10.549 0.50 15.86

ATOM 880 O BTHR A 138 -0.409 14.979 -1.886 0.50 6.26

ATOM 881 N ASP A 139 4.924 7.543 -9.222 00 14.21

ATOM 882 CA ASP A 139 4..277 8.785 -8.815 00 15.43

ATOM 883 CB ASP A 139 3..098 9.077 -9.764 00 17.23

ATOM 884 CG ASP A 139 3.513 9.171 -11.230 00 21.10

ATOM 885 ODl ASP A 139 2.756 8.700 -12.118 00 26.92

ATOM 886 OD2 ASP A 139 4..598 9.719 -11.519 00 28.31

ATOM 887 C ASP A 139 3..759 8.701 -7.374 00 15.22

ATOM 888 O ASP A 139 3..273 7.663 -6.925 1.00 15.72

ATOM 889 N LED A 140 3..856 9.816 -6.664 00 14.38

ATOM 890 CA LED A 140 3.,210 10.026 -5.398 00 12.90

ATOM 891 CB LED A 140 .297 10.329 -4.368 00 13.43

ATOM 892 CG LEU A 140 3..932 10.262 -2.904 00 14.65

ATOM 893 CDl LEU A 140 3..538 8.862 -2.483 00 15.57

ATOM 894 CD2 LEU A 140 5.094 10.745 -2.029 00 14.30

ATOM 895 C LEU A 140 2.288 11.223 -5.662 00 11.43

ATOM 896 O LEU A 140 2.642 12.359 -5.331 00 10.69

ATOM 897 N PRO A 141 1.130 10.996 -6.322 00 9.94

ATOM 898 CA PRO A 141 0.440 12.112 -6.982 00 9.59

ATOM 899 CB PRO A 141 0.714 11.420 -7.737 00 10.45

ATOM 900 CG PRO A 141 0.814 10.090 -7.234 00 11.91

ATOM 901 CD PRO A 141 0.421 9.712 -6.531 00 9.94

ATOM 902 C PRO A 141 0.112 13.184 -6.070 00 8.00

ATOM 903 O PRO A 141 0.373 14.305 -6.532 00 8.24

ATOM 904 N ASN A 142 0.403 12.850 -4.802 0.50 7.15

ATOM 905 CA ASN A 142 0.931 13.836 -3.830 0.50 6.74

ATOM 906 CB ASN A 142 -2 221 13.397 -3.099 0.50 6.75

ATOM 907 CG ASN A 142 3.335 12.934 -4.007 0.50 7.79

ATOM 908 ODl ASN A 142 4.218 12.179 -3.562 0.50 8.70

ATOM 909 ND2 ASN A 142 3.332 13.375 -5.248 0.50 9.53 Table 1

ATOM 910 C ASN R 142 0.043 14.174 -2.709 0.50 5.88

ATOM 911 O ASN A 142 -0.390 14.512 -1.620 0.50 6.43

ATOM 912 N SER A 143 1.345 14.045 -2.928 1.00 5.37

ATOM 913 CA SER A 143 2.297 14.635 -1.997 1.00 4.79

ATOM 914 CB SER A 143 3.687 14.089 -2.212 1.00 4.77

ATOM 915 OG SER A 143 4.176 14.446 -3.470 1.00 6.70

ATOM 916 C SER A 143 2.263 16.147 -2.175 1.00 3.81

ATOM 917 O SER A 143 1.873 16.673 -3.228 1.00 3.33

ATOM 918 N PHE A 144 2.681 16.842 -1.134 1.00 2.92

ATOM 919 CA PHE A 144 2.599 18.286 -1.140 1.00 2.95

ATOM 920 CB PHE A 144 1.616 18.813 -0.069 1.00 4.00

ATOM 921 CG PHE A 144 1.799 18.254 1.304 1.00 4.71

ATOM 922 CDl PHE A 144 2.710 18.818 2.179 1.00 5.27

ATOM 923 CEl PHE A 144 2.858 18.315 3.469 1.00 5.82

ATOM 924 CZ PHE A 144 2.079 17.255 3.887 1.00 6.56

ATOM 925 CE2 PHE A 144 1.147 16.720 3.035 1.00 6.28

ATOM 926 CD2 PHE A 144 1.000 17.221 1.763 1.00 6.15

ATOM 927 C PHE A 144 3.985 18.898 -1.059 1.00 3.00

ATOM 928 O PHE A 144 4.993 18.196 -0.940 1.00 3.75

ATOM 929 N ASP A 145 4.052 20.218 -1.174 1.00 2.19

ATOM 930 CA ASP A 145 5.332 20.900 -1.154 1.00 2.64

ATOM 931 CB ASP A 145 5.098 22.395 -1.282 1.00 2.65

ATOM 932 CG ASP A 145 6.371 23.173 -1.316 1.00 2.50

ATOM 933 ODl ASP A 145 6.794 23.669 -0.241 1.00 3.50

ATOM 934 OD2 ASP A 145 6.934 23.353 -2.416 1.00 3.19

ATOM 935 C ASP A 145 6.059 20.605 0.149 1.00 2.75

ATOM 936 O ASP A 145 5.457 20.575 1.217 1.00 2.96

ATOM 937 N GLY A 146 7.372 20.429 0.056 1.00 3.05

ATOM 938 CA GLY A 146 8.150 20.168 1.250 1.00 3.28

ATOM 939 C GLY A 146 9.595 19.879 0.926 1.00 3.27

ATOM 940 O GLY A 146 9.975 19.850 -0.241 1.00 4.67

ATOM 941 N PRO A 147 10.410 19.660 1.977 1.00 4.50

ATOM 942 CA PRO A 147 11.858 19.595 1.846 1.00 4.84

ATOM 943 CB PRO A 147 12.313 20.173 3.190 1.00 5.26

ATOM 944 CG PRO A 147 11.290 19.708 4.152 1.00 5.04

ATOM 945 CD PRO A 147 9.993 19.655 3.395 1.00 4.80

ATOM 946 C PRO A 147 12.449 18.190 1.676 1.00 5.26

ATOM 947 O PRO A 147 13.661 18.077 1.468 1.00 5.72

ATOM 948 N AVAL A 148 11.622 17.157 1.741 0.50 4.90

ATOM 948 N BVAL A 148 10.338 6.416 -4.315 0.50 3.79

ATOM 949 CA AVAL A 148 12.123 15.780 1.799 0.50 4.93

ATOM 949 CA BVAL A 148 9.553 5.194 -4.441 0.50 3.79

ATOM 950 CB AVAL A 148 11.172 14.885 2.633 0.50 5.02

ATOM 950 CB BVAL A 148 8.298 5.367 -5.351 0.50 4.49

ATOM 951 CGlAVAL A 148 11.784 13.494 2.832 0.50 5.63

ATOM 951 CGlBVAL A 148 7.545 6.653 -4.989 0.50 6.46

ATOM 952 CG2AVAL A 148 10.878 15.547 3.991 0.50 7.03

ATOM 952 CG2BVAL A 148 7.404 4.112 -5.284 0.50 4.68

ATOM 953 C AVAL A 148 12.295 15.185 0.405 0.50 4.73

ATOM 953 C BVAL A 148 10.447 4.131 -5.065 0.50 3.35

ATOM 954 O AVAL A 148 11.407 15.303 -0.422 0.50 5.29

ATOM 954 O BVAL A 148 11.017 4.329 -6.141 0.50 3.54

ATOM 955 N THR R 149 13.421 14.513 0.152 1.00 5.32

ATOM 956 CA THR R 149 13.545 13.711 -1.053 1.00 5.36

ATOM 957 CB THR R 149 14.996 13.473 -1.455 1.00 6.50

ATOM 958 OGl THR R 149 15.605 14.742 -1.731 1.00 7.88

ATOM 959 CG2 THR A 149 15.064 12.607 -2.705 1.00 6.71

ATOM 960 C THR A 149 12.847 12.382 -0.773 1.00 5.17

ATOM 961 O THR A 149 13.290 11.605 0.071 1.00 5.94

ATOM 962 N ILE Ά 150 11.726 12.164 -1.436 1.00 4.32

ATOM 963 CA ILE R 150 10.949 10.947 -1.280 1.00 4.28

ATOM 964 CB ILE R 150 9.443 11.269 -1.179 1.00 4.47

ATOM 965 CGl ILE R 150 9.186 12.260 -0.049 1.00 4.94

ATOM 966 CDl ILE R 150 7.821 12.892 -0.110 1.00 6.15

ATOM 967 CG2 ILE R 150 8.655 10.030 -0.951 1.00 4.70

ATOM 968 C ILE R 150 11.212 10.076 -2.493 1.00 4.75

ATOM 969 O ILE R 150 10.973 10.484 -3.609 1.00 5.44

ATOM 970 N THR R 151 11.667 8.842 -2.253 1.00 4.21 Table 1

ATOM 971 CA THR A 151 11.967 7.923 -3.335 1.00 4.07

ATOM 972 CB THR A 151 13.439 7.508 -3.286 1.00 4.32

ATOM 973 OGl THR A 151 14.258 8.677 -3.368 1.00 5.48

ATOM 974 CG2 THR A 151 13.793 6.612 -4.448 1.00 4.75

ATOM 975 C THR A 151 11.074 6.696 -3.243 1.00 3.76

ATOM 976 O THR A 151 11.053 6.024 -2.208 1.00 4.87

ATOM 977 N ILE A 152 10.313 6.440 -4.299 0.50 3.61

ATOM 978 CA ILE A 152 9.556 5.211 -4.456 0.50 3.81

ATOM 979 CB ILE A 152 8.356 5.402 -5.429 0.50 4.21

ATOM 980 CGl ILE A 152 7.310 6.348 -4.819 0.50 5.61

ATOM 9Bl CDl ILE A 152 6.395 6.962 -5.858 0.50 5.45

ATOM 982 CG2 ILE A 152 7.742 4.058 -5.809 0.50 4.01

ATOM 983 C ILE A 152 10.511 4.162 -5.025 0.50 3.34

ATOM 984 O ILE A 152 11.209 4.413 -6.009 0.50 3.30

ATOM 985 N VAL A 153 10.572 3.007 -4.370 1.00 2.75

ATOM 986 CA VAL A 153 11.446 1.917 -4.791 1.00 2.61

ATOM 987 CB VAL A 153 12.465 1.559 -3.693 1.00 2.81

ATOM 988 CGl VAL A 153 13.424 0.514 -4.190 1.00 2.88

ATOM 989 CG2 VAL A 153 13.193 2.793 -3.220 1.00 3.52

ATOM 990 C VAL A 153 10.566 0.728 -5.094 1.00 2.32

ATOM 991 O VAL A 153 9.870 0.221 -4.230 1.00 3.21

ATOM 992 N AASN A 154 10.607 0.277 -6.338 0.50 2.21

ATOM 992 N BASN A 154 13.466 -0.282 -9.851 0.50 2.47

ATOM 993 CA AASN A 154 9.871 -0.907 -6.761 0.50 2.64

ATOM 993 CA BASN A 154 13.043 0.962 -10.518 0.50 2.68

ATOM 994 CB AASN A 154 9.457 -0.749 -8.224 0.50 2.92

ATOM 994 CB BASN A 154 11.800 0.741 -11.464 0.50 2.59

ATOM 995 CG ASN A 154 8.479 0.387 -8.400 0.50 3.44

ATOM 996 ODl ASN A 154 7.277 0.211 -8.191 0.50 3.97

ATOM 997 ND2 ASN A 154 8.987 1.572 -8.740 0.50 3.96

ATOM 998 C AASN A 154 10.728 -2.147 -6.545 0.50 2.22

ATOM 998 C BASN A 154 12.716 2.001 -9.441 0.50 2.81

ATOM 999 O AASN A 154 11.940 -2.036 -6.376 0.50 2.38

ATOM 999 O BASN A 154 12.003 1.700 -8.493 0.50 2.86

ATOM 1000 N ARG A 155 10.105 -3.333 -6.512 1.00 2.88

ATOM 1001 CA ARG A 155 10.869 -4.549 -6.218 1.00 3.28

ATOM 1002 CB ARG A 155 9.919 -5.744 -6.078 1.00 4.53

ATOM 1003 CG ARG A 155 10.517 -7.003 -5.459 1.00 6.60

ATOM 1004 CD ARG A 155 9.516 -8.137 -5.563 1.00 9.76

ATOM 1005 NE ARG A 155 10.050 -9.384 -5.044 1.00 14.04

ATOM 1006 CZ ARG A 155 9.353 -10.516 -4.951 1.00 16.59

ATOM 1007 NHl ARG A 155 8.081 -10.567 -5.341 1.00 17.18

ATOM 1008 NH2 ARG A 155 9.939 -11.611 -4.469 1.00 18.32

ATOM 1009 C ARG A 155 11.918 -4.859 -7.255 1.00 2.97

ATOM 1010 O ARG A 155 12.941 -5.421 -6.916 1.00 2.95

ATOM 1011 N AASP A 156 11.679 -4.447 -8.499 0.50 2.68

ATOM 1011 N BASF A 156 11.656 6.214 -8.468 0.50 5.75

ATOM 1012 CA AASP A 156 12.670 -4.592 -9.561 0.50 2.60

ATOM 1012 CA BASP A 156 11.138 7.524 -8.871 0.50 6.72

ATOM 1013 CB AASP A 156 11.991 -4.646 -10.951 0.50 2.49

ATOM 1013 CB BASP A 156 9.703 7.409 -9.387 0.50 9.17

ATOM 1014 CG AASP A 156 11.320 -3.353 -11.357 0.50 3.71

ATOM 1014 CG BASP A 156 9.556 6.807 -10.772 0.50 11.00

ATOM 1015 ODl ASP A 156 11.461 -2.333 -10.643 0.50 3.52

ATOM 1016 OD2 ASP A 156 10.642 -3.390 -12.427 0.50 5.17

ATOM 1017 C AASP A 156 13.754 -3.532 -9.547 0.50 2.28

ATOM 1017 C BASP A 156 11.188 8.425 -7.642 0.50 6.26

ATOM 1018 O AASP A 156 14.604 -3.506 -10.437 0.50 2.12

ATOM 1018 O BASP A 156 10.613 8.091 -6.609 0.50 6.39

ATOM 1019 N GLY A 157 13.728 -2.674 -8.527 1.00 2.05

ATOM 1020 CA GLY A 157 14.757 -1.674 -8.347 1.00 2.32

ATOM 1021 C GLY A 157 14.482 -0.337 -8.992 1.00 2.54

ATOM 1022 O GLY A 157 15.193 0.624 -8.732 1.00 3.01

ATOM 1023 N THR A 158 13.486 -0.257 -9.842 0.50 2.36

ATOM 1024 CA THR A 158 13.243 1.009 -10.497 0.50 2.51

ATOM 1025 CB THR A 158 12.294 0.876 -11.661 0.50 2.63

ATOM 1026 OGl THR A 158 11.054 0.343 -11.203 0.50 2.72

ATOM 1027 CG2 THR A 158 12.875 -0.051 -12.703 0.50 3.27 Table 1

ATOM 1028 C THR A 158 12.739 2.002 -9.466 0.50 2.80

ATOM 1029 O THR A 158 11.944 1.682 -8.592 0.50 2.80

ATOM 1030 N ARG A 159 13.273 3.209 -9.582 1.00 3.06

ATOM 1031 CA ARG A 159 13.034 4.255 -8.621 1.00 4.44

ATOM 1032 CB ARG A 159 14.343 4.653 -7.964 1.00 5.14

ATOM 1033 CG ARG A 159 14.778 3.680 -6.940 1.00 4.77

ATOM 1034 CD ARG A 159 16.152 4.072 -6.359 1.00 5.97

ATOM 1035 NE ARG A 159 16.545 3.079 -5.385 1.00 5.71

ATOM 1036 CZ ARG A 159 16.826 3.217 -4.111 1.00 9.81

ATOM 1037 NHl ARG A 159 16.869 4.400 -3.445 1.00 11.73

ATOM 1038 NH2 ARG A 159 17.109 2.068 -3.505 1.00 9.09

ATOM 1039 C ARG A 159 12.460 5.505 -9.253 1.00 5.04

ATOM 1040 O ARG A 159 12.765 5.841 -10.404 1.00 5.86

ATOM 1041 N TYR A 160 11.621 6.181 -8.469 0.50 5.53

ATOM 1042 CA TYR A 150 11.101 7.506 -8.813 0.50 5.99

ATOM 1043 CB TYR A 160 9.620 7.440 -9.193 0.50 6.81

ATOM 1044 CG TYR A 160 8.965 8.801 -9.194 0.50 6.71

ATOM 1045 CDl TYR A 160 9.186 9.698 -10.232 0.50 5.34

ATOM 1046 CEl TYR A 160 8.593 10.967 -10.235 0.50 7.20

ATOM 1047 CZ TYR A 160 7.787 11.339 -9.181 0.50 7.77

ATOM 1048 OH TYR A 160 7.190 12.586 -9.155 0.50 7.59

ATOM 1049 CE2 TYR A 160 7.568 10.474 -8.136 0.50 6.81

ATOM 1050 CD2 TYR A 160 8.162 9.209 -8.140 0.50 7.16

ATOM 1051 C TYR A 160 11.285 8.389 -7.586 0.50 5.79

ATOM 1052 O TYR A 160 10.924 8.007 -6.487 0.50 6.13

ATOM 1053 N SER A 161 11.863 9.565 -7.764 1.00 6.03

ATOM 1054 CA SER A 161 12.078 10.486 -6.650 1.00 6.34

ATOM 1055 CB SER A 161 13.565 10.733 -6.386 1.00 7.87

ATOM 1056 OG SER A 161 14.258 9.543 -6.049 1.00 11.17

ATOM 1057 C SER A 161 11.398 11.827 -6.924 1.00 6.46

ATOM 1058 O SER A 161 11.299 12.284 -8.070 1.00 6.83

ATOM 1059 N LYS A 162 10.948 12.445 -5.839 1.00 6.24

ATOM 1060 CA LYS A 162 10.497 13.845 -5.885 1.00 6.44

ATOM 1061 CB LYS A 162 9.007 13.919 -6.205 1.00 7.69

ATOM 1062 CG LYS A 162 8.124 13.362 -5.123 1.00 8.55

ATOM 1063 CD LYS A 162 6.671 13.174 -5.541 1.00 9.15

ATOM 1064 CE LYS A 162 5.983 14.419 -6.083 1.00 9.43

ATOM 1065 NZ LYS A 162 4.492 14.216 -6.330 1.00 11.20

ATOM 1066 C LYS A 162 10.765 14.506 -4.553 1.00 6.31

ATOM 1067 O LYS A 162 10.881 13.842 -3.536 1.00 7.10

ATOM 1068 N LYS A 163 10.817 15.831 -4.575 1.00 5.67

ATOM 1069 CA LYS A 163 10.959 16.615 -3.368 1.00 6.07

ATOM 1070 CB LYS A 163 11.757 17.877 -3.664 1.00 7.21

ATOM 1071 CG LYS A 163 12.195 18.570 -2.416 1.00 10.29

ATOM 1072 CD LYS A 163 13.133 19.717 -2.702 1.00 10.28

ATOM 1073 CE LYS A 163 13.460 20.453 -1.424 1.00 12.86

ATOM 1074 NZ LYS A 163 14.500 21.493 -1.565 1.00 15.10

ATOM 1075 C LYS A 163 9.565 16.981 -2.868 1.00 4.81

ATOM 1076 O LYS A 163 8.748 17.502 -3.637 1.00 6.65

ATOM 1077 N GLY A 164 9.281 16.701 -1.599 1.00 4.31

ATOM 1078 CA GLY A 164 7.981 17.022 -1.057 1.00 3.91

ATOM 1079 C GLY A 164 7.813 16.662 0.398 1.00 3.44

ATOM 1080 O GLY A 164 8.775 16.554 1.157 1.00 3.96

ATOM 1081 N GLU A 165 6.569 16.462 0.782 1.00 3.17

ATOM 1082 CA GLO A 165 6.218 15.987 2.098 1.00 3.64

ATOM 1083 CB GLU A 165 6.181 17.164 3.086 1.00 4.26

ATOM 1084 CG GLU A 165 5.806 16.812 4.534 1.00 4.82

ATOM 1085 CD GLU A 165 6.703 15.751 5.140 1.00 6.10

ATOM 1086 OEl GLU A 165 7.748 16.127 5.711 1.00 7.65

ATOM 1087 OE2 GLU A 165 6.360 14.549 5.073 1.00 6.32

ATOM 1088 C GLU A 165 4.866 15.302 1.983 1.00 3.91

ATOM 1089 O GLU A 165 4.094 15.580 1.076 1.00 3.92

ATOM 1090 N TYR A 166 4.584 14.376 2.887 1.00 4.95

ATOM 1091 CA TYR A 166 3.242 13.799 2.977 1.00 5.58

ATOM 1092 CB TYR A 166 3.196 12.391 2.345 1.00 5.94

ATOM 1093 CG TYR A 166 4.099 11.393 3.030 1.00 6.12

ATOM 1094 CDl TYR A 166 3.670 10.658 4.131 1.00 5.73

ATOM 1095 CEl TYR A 166 4.517 9.769 4.784 1.00 5.65 Table 1

ATOM 1096 CZ TYR A 166 5.803 9.628 4.359 00 6.87

ATOM 1097 OH TYR A 166 6.659 8.763 4.980 00 9.40

ATOM 1098 CE2 TYR A 166 6.264 10.349 3.295 00 8.55

ATOM 1099 CD2 TYR A 166 5.412 11.228 2.628 00 7.11

ATOM 1100 C TYR A 166 2.714 13.729 4.408 00 5.40

ATOM 1101 O TYR A 166 1.526 13.513 4.607 00 5.75

ATOM 1102 N ARG A 167 3.576 13.947 5.403 00 5.62

ATOM 1103 CA ARG A 167 3.182 13.804 6.811 00 6.64

ATOM 1104 CB ARG A 167 4.405 13.512 7.672 00 6.60

ATOM 1105 CG ARG A 167 5.047 12.191 7.317 00 7.22

ATOM 1106 CD ARG A 167 6.430 12.044 7.892 00 7.83

ATOM 1107 NE ARG A 167 7.319 13.042 ,302 00 8.42

ATOM 1108 CZ ARG A 167 8.580 13.226 666 00 9.99

ATOM 1109 NHl ARG A 167 9.131 12.442 .583 00 10.55

ATOM 1110 NH2 ARG A 167 9.295 14.180 101 00 10.10

ATOM 1111 C ARG A 167 2.533 15.093 .262 00 6.76

ATOM 1112 O ARG A 167 3.103 16.178 ,099 00 8.19

ATOM 1113 N THR A 168 1.327 14.982 7.795 00 7.31

ATOM 1114 CA THR A 168 0.542 16.136 8.210 00 8.75

ATOM 1115 CB THR A 168 -0.919 16.050 7.714 00 8.56

ATOM 1116 OGl THR A 168 -1.611 15.021 8.419 00 10.50

ATOM 1117 CG2 THR A 168 -0.981 15.769 6.225 00 9.10

ATOM 1118 C THR A 168 0.534 16.306 9.723 00 9.61

ATOM 1119 O THR A 168 0.085 17.339 10.215 00 10.46

ATOM 1120 N HIS A 169 1.061 15.332 10.459 00 9.90

ATOM 1121 CA HIS A 169 1.094 15.396 11.928 00 11.22

ATOM 1122 CB HIS A 169 0.592 14.078 12.519 00 11.96

ATOM 1123 CG HIS A 169 -0.847 13.799 12.221 00 12.55

ATOM 1124 NDl HIS A 169 -1.866 14.148 13.081 00 16.10

ATOM 1125 CEl HIS A 169 -3.023 13.778 12.562 00 15.71

ATOM 1126 NE2 HIS A 169 -2.793 13.197 11.399 00 14.50

ATOM 1127 CD2 HIS A 169 -1.441 13.209 11.156 00 12.69

ATOM 1128 C HIS A 169 2.514 15.662 12.385 00 12.23

ATOM 1129 O HIS A 169 3.418 14.892 12.092 00 11.72

ATOM 1130 N GLN A 170 2.716 16.759 13.109 00 13.44

ATOM 1131 CA GLN A 170 4.047 17.132 13.596 00 14.12

ATOM 1132 CB GLN A 170 3.926 18.381 14.476 00 14.90

ATOM 1133 CG GLN A 170 5.189 18.828 15.215 00 15.36

ATOM 1134 CD GLN A 170 6.130 19.652 14.365 1.00 19.65

ATOM 1135 OEl GLN A 170 6.238 20.871 14.549 1.00 22.29

ATOM 1136 NE2 GLN A 170 6.842 18.998 13.454 1.00 21.22

ATOM 1137 C GLN A 170 4.739 16.003 14.362 00 14.43

ATOM 1138 O GLN A 170 5.945 15.795 14.213 00 15.03

ATOM 1139 N GLO A 171 3.977 15.256 15.153 00 15.28

ATOM 1140 CA GLO A 171 4.553 14.177 15.961 00 16.03

ATOM 1141 CB GLO A 171 3.540 13.623 16.964 00 17.29

ATOM 1142 CG GLO A 171 2.303 12.979 16.368 00 19.82

ATOM 1143 CD GLO A 171 1.211 13.977 15.995 00 23.52

ATOM 1144 OEl GLO A 171 1.444 15.213 16.036 00 24.78

ATOM 1145 OE2 GLU A 171 0.107 13.505 15.639 00 28.05

ATOM 1146 C GLU A 171 5.154 13.040 15.128 00 16.12

ATOM 1147 O GLU A 171 6.000 12.299 15.613 00 17.25

ATOM 114B N ASP A 172 4.719 12.909 13.879 00 15.56

ATOM 1149 CA ASP A 172 5.314 11.955 12.949 00 15.80

ATOM 1150 CB ASP A 172 4.305 11.550 11.861 00 14.54

ATOM 1151 CG ASP A 172 3.148 10.731 12.398 00 13.77

ATOM 1152 ODl ASP A 172 3.364 9.906 13.315 00 12.19

ATOM 1153 OD2 ASP A 172 2.022 10.898 11.884 00 10.99

ATOM 1154 C ASP A 172 6.565 12.498 12.268 00 16.33

ATOM 1155 O ASP A 172 7.271 11.750 11.600 00 17.98

ATOM 1156 N ILE A 173 6.833 13.790 12.395 00 17.49

ATOM 1157 CA ILE A 173 8.002 14.378 11.751 00 17.87

ATOM 1158 CB ILE A 173 7.661 15.709 11.080 00 17.89

ATOM 1159 CGl ILE A 173 6.589 15.468 10.015 00 17.55

ATOM 1160 CDl ILE A 173 5.978 16.709 9.442 00 17.46

ATOM 1161 CG2 ILE A 173 8.912 16.332 10.467 00 17.84

ATOM 1162 C ILE A 173 9.081 14.589 12.792 00 19.15

ATOM 1163 O ILE A 173 10.182 14.069 12.654 1.00 20.77 Table 1

ATOM 1164 OXT ILE A 173 8.861 15.269 13.791 00 20.69

ATOM 1165 03 GOL A 1 8.555 -4.450 -9.170 00 7.56

ATOM 1166 C3 GOL A 1 7.248 -4.815 -8.699 00 10.56

ATOM 1167 C2 GOL A 1 6.507 -3.803 -7.827 00 9.58

ATOM 1168 02 GOL A 1 .300 -3.413 -6.741 00 7.36

ATOM 1169 Cl GOL A 1 .995 -2. 661 -8.695 00 7.28

ATOM 1170 Ol GOL A 1 .401 -1.690 -7.971 00 9.30

ATOM 1171 Cl NAG C 1 .673 -15.897 19.466 00 21.39

ATOM 1172 Ol NAG C 1 .495 -16.611 20.662 00 22.91

ATOM 1173 C2 NAG C 1 3.146 -15.967 19.082 1.00 21.33

ATOM 1174 N2 NAG C 1 3.961 -15.526 20.216 00 22.21

ATOM 1175 C7 NAG C 1 5.224 -15.899 20.455 00 23.45

ATOM 1176 07 NAG C 1 5.982 -15.216 21.153 00 26.20

ATOM 1177 C8 NAG C 1 5.727 -17.184 19.871 1.00 22.69

ATOM 1178 C3 NAG C 1 3.359 -15.135 17.825 00 19.64

ATOM 1179 03 NAG C 1 4.719 -15.296 17.472 00 19.39

ATOM 1180 C4 NAG C 1 2.421 -15.682 16.743 00 19.94

ATOM 1181 04 NAG C 1 2.494 -14.920 15.544 00 18.72

ATOM 1182 C5 NAG C 1 0.969 -15.776 17.224 00 20.48

ATOM 1183 C6 NAG C 1 0.096 -16.481 16.195 00 21.31

ATOM 1184 06 NAG C 1 -1.258 -16.257 16.507 00 21.64

ATOM 1185 05 NAG C 1 0.875 -16.475 18.449 1.00 20.90

ATOM 1186 Cl GCϋ C 2 5.328 -14.217 16.732 00 18.25

ATOM 1187 C2 GCϋ C 2 6.828 -14.242 17.027 00 18.24

ATOM 1188 02 GCϋ C 2 7.025 -13.861 18.376 00 20.16

ATOM 1189 C3 GCϋ C 2 7..636 -13.311 16.119 00 17.37

ATOM 1190 03 GCD C 2 9..016 -13.506 16.386 00 18.05

ATOM 1191 C4 GCD C 2 7..302 -13.532 14.637 00 15.88

ATOM 1192 04 GCD C 2 7.891 -12.552 13.793 00 13.96

ATOM 1193 C5 GCϋ C 2 5.779 -13.490 14.486 00 16.01

ATOM 1194 C6 GCD C 2 5.357 -13.907 13.093 00 15.27

ATOM 1195 O6A GCD C 2 5.587 -15.088 12.734 00 15.32

ATOM 1196 O6B GCD C 2 4.770 -13.049 12.389 00 15.61

ATOM 1197 05 GCD C 2 5.105 -14.394 15.350 00 17.23

ATOM 1198 Cl NAG C 3 8.981 -12.958 12.947 00 13.86

ATOM 1199 C2 NAG C 3 9.197 -11.894 11.872 00 12.61

ATOM 1200 N2 NAG C 3 7.953 -11.765 11.107 00 12.46

ATOM 1201 C7 NAG C 3 7.326 -10.609 10.864 00 10.60

ATOM 1202 07 NAG C 3 7.702 -9.481 11.273 00 11.45

ATOM 1203 C8 NAG C 3 6.059 -10.789 10.072 00 10.14

ATOM 1204 C3 NAG C 3 10.377 -12.248 10.975 00 14.95

ATOM 1205 03 NAG C 3 10.671 -11.119 10.187 00 15.51

ATOM 1206 C4 NAG C 3 11.608 -12.618 11.814 00 15.46

ATOM 1207 04 NAG C 3 12.625 -13.150 10.989 00 18.71

ATOM 1208 C5 NAG C 3 11.244 -13.632 12.893 00 15.22

ATOM 1209 C6 NAG C 3 12.424 -13.950 13.818 00 17.81

ATOM 1210 06 NAG C 3 12.816 -12.787 14.518 1.00 21.86

ATOM 1211 05 NAG C 3 10.174 -13.133 13.679 00 14.38

ATOM 1212 Cl GCD C 4 10.433 -11.340 8.788 00 16.61

ATOM 1213 C2 GCϋ C 4 10.583 -10.000 8.093 00 17.10

ATOM 1214 02 GCU C 4 9.697 -9.062 8.652 00 18.27

ATOM 1215 C3 GCU C 4 10.269 -10.164 6.625 00 15.85

ATOM 1216 03 GCU C 4 10.597 -8.963 5.964 00 16.08

ATOM 1217 C4 GCU C 4 11.110 -11.286 6.006 1.00 17.22

ATOM 1218 04 GCU C 4 10.527 -11.547 4.750 00 18.11

ATOM 1219 C5 GCU C 4 11.114 -12.553 6.859 00 17.84

ATOM 1220 C6 GCU C 4 12.195 -13.529 6.384 00 19.27

ATOM 1221 O6A GCϋ C 4 13.325 -13.462 6.932 00 19.67

ATOM 1222 O6B GCU C 4 11.905 -14.349 5.473 00 20.19

ATOM 1223 05 GCU C 4 11.355 -12.247 8.218 00 17.43

ATOM 1224 Cl NAG C 5 11.410 -11.652 3.627 00 20.94

ATOM 1225 C2 NAG C 5 10.650 -12.493 2.609 00 23.10

ATOM 1226 N2 NAG C 5 10.359 -13.801 3.167 00 23.88

ATOM 1227 C7 NAG C 5 9.134 -14.324 3.135 00 23.80

ATOM 1228 07 NAG C 5 8.203 -13.853 2.485 00 24.54

ATOM 1229 C8 NAG C 5 8.940 -15.569 3.939 00 24.08

ATOM 1230 C3 NAG C 5 11.395 -12.598 1.276 00 25.30

ATOM 1231 03 NAG C 10.538 -13.196 0.322 1.00 28.77 Table 1

ATOM 1232 C4 NAG C 5 11.801 11.212 0.792 ,00 24.51

ATOM 1233 04 NAG C 5 12.672 11.330 -0.321 ,00 24.58

ATOM 1234 C5 NAG C 5 12.501 10.458 1.920 ,00 23.51

ATOM 1235 C6 NAG C 5 12.839 -9.027 1.531 ,00 23.79

ATOM 1236 06 NAG C 5 11.650 -8.281 1.384 00 25.30

ATOM 1237 05 NAG C 5 11.667 10.396 3.061 00 21.24

ATOM 1238 Cl GCO C 5 11.088 14.404 -0.229 ,00 32.56

ATOM 1239 C2 GCU C 6 9.935 15.174 -0.870 ,00 34.01

ATOM 1240 02 GCϋ C 6 9.122 15.699 0.157 1.00 35.02

ATOM 1241 C3 GCϋ C 6 10.402 16.333 -1.747 00 35.26

ATOM 1242 03 GCD C 6 9.333 16.735 -2.580 00 35.49

ATOM 1243 C4 GCD C 6 11.585 15.930 -2.616 00 35.93

ATOM 1244 04 GCD C 6 12.134 17.095 -3 181 00 37.61

ATOM 1245 C5 GCD C 6 12.651 15:225 -1 788 00 35.36

ATOM 124G C6 GCD C 6 13.839 14.788 -2 635 00 35.73

ATOM 1247 O6A GCD C 6 14.920 15.390 -2.462 00 35.87

ATOM 1248 O6B GCD C 6 13.669 13.844 -3.444 00 36.66

ATOM 1249 05 GCD C 5 12.091 14.088 -1.168 00 33.75

ATOM 1250 Cl NAG C 7 11.971 17.140 -4.609 00 40.20

ATOM 1251 C2 NAG C 7 12.805 18.331 -5.079 00 40.98

ATOM 1252 N2 NAG C 7 14.213 18.090 -4.810 00 41.62

ATOM 1253 C7 NAG C 7 14.926 18.821 -3.946 00 42.37

ATOM 1254 07 NAG C 7 15.803 18.328 -3.239 00 42.42

ATOM 1255 C8 NAG C 7 14.638 20.294 -3.857 00 42.81

ATOM 1256 C3 NAG C 7 12.593 18.617 -6.558 00 41.69

ATOM 1257 03 NAG C 7 13.324 19.756 -6.966 00 41.63

ATOM 1258 C4 NAG C 7 11.100 18.808 -6.781 00 42.24

ATOM 1259 04 NAG C 7 10.864 19.146 -8.131 00 42.56

ATOM 1260 C5 NAG C 7 10.405 17.503 -6.375 00 42.34

ATOM 1261 C6 NAG C 7 8.908 -17 480 -6.690 00 42.77

ATOM 1262 06 NAG C 7 8.201 -18.276 -5.765 00 43.63

ATOM 1263 05 NAG C 7 10.611 -17.279 -4. 987 00 41.24

ATOM 1264 OWl HOH W 1 -7.390 5, 962 4.644 00 11.01

ATOM 1265 OWl HOH W 2 9.028 -7.081 -9.204 00 14.25

ATOM 1266 OWl HOH W 3 1.985 1.368 -12.438 00 14.45

ATOM 1267 OWl HOH W 4 -0.489 13.057 2.796 00 9.67

ATOM 1268 OWl HOH W 5 -0.842 -2.896 23.456 00 8.65

ATOM 1269 OWl HOH W 6 -1.158 -11.966 16.987 00 17.64

ATOM 1270 OWl HOH W 7 -4.364 -4.039 -8.885 1.00 3.53

ATOM 1271 OWl HOH W 8 -5.705 -6.516 -13.906 00 7.31

ATOM 1272 OWl HOH W 9 -6.291 -16.018 9.338 00 36.42

ATOM 1273 OWl HOH W 10 7.786 0.655 7.428 00 5.76

ATOM 1274 OWl HOH W 11 -14.455 -4.736 5.264 00 15.85

ATOM 1275 OWl HOH W 12 6.963 -3.155 0.009 00 6.36

ATOM 1276 OWl HOH W 13 -10.204 1.663 1.579 00 6.79

ATOM 1277 OWl HOH W 14 4.994 -6.438 20.196 1.00 6.66

ATOM 1278 OWl HOH W 15 1.742 12.478 9.581 1.00 11.50

ATOM 1279 OWl HOH W 16 10.126 -5.587 -13.835 00 5.67

ATOM 1280 OWl HOH W 17 -5.450 1. 424 -13.813 00 17.76

ATOM 1281 OWl HOH W 18 7.847 — 2 969 -11.402 00 11.06

ATOM 1282 OWl HOH W 19 5.841 — 1 582 16.452 00 5.50

ATOM 1283 OWl HOH W 20 -5.796 -13.175 14.781 00 12.65

ATOM 1284 OWl HOH W 21 2.457 5.160 -10.683 00 19.48

ATOM 1285 OWl HOH W 22 6.766 21.820 -4.564 00 11.38

ATOM 1286 OWl HOH W 23 8.293 20.174 -2.894 00 11.30

ATOM 1287 OWl HOH W 24 -13.671 -1.015 -3.217 00 7.42

ATOM 1288 OWl HOH W 25 -5.294 0.444 11.930 00 11.01

ATOM 1289 OWl HOH W 26 12.750 -5.857 14.308 00 16.87

ATOM 1290 OWl HOH W 27 10.061 -1.112 -14.216 00 8.29

ATOM 1291 OWl HOH W 28 10.045 -8.595 12.783 00 12.07

ATOM 1292 OWl HOH W 29 3.627 -8.875 19.134 00 10.27

ATOM 1293 OWl HOH W 31 -8.851 -14.242 5.434 00 13.84

ATOM 1294 OWl HOH W 32 5.501 16.797 -3.457 00 12.37

ATOM 1295 OWl HOH W 33 -1.906 17.097 -0.803 00 21.42

ATOM 1296 OWl HOH W 34 3.467 -15.463 -3.190 00 26.83

ATOM 1297 OWl HOH W 35 3.393 18.815 7.262 00 20.08

ATOM 1298 OWl HOH W 36 -1.156 -0.082 -14.282 00 15.65

ATOM 1299 OWl HOH W 37 5.809 6.991 11.636 1.00 14.66 Table 1

ATOM 130Q OWl HOH W 38 1.100 -14.993 -5.042 1.00 23.26

ATOM 1301 OWl HOH W 39 15.720 16.775 0.364 1.00 23.04

ATOM 1302 OWl HOH W 40 11.732 -10.559 -11.707 1.00 16.77

ATOM 1303 OWl HOH W 41 -1.347 -23.424 8.221 1.00 22.85

ATOM 1304 OWl HOH W 42 12.377 -5.390 5.398 1.00 23.37

ATOM 1305 OWl HOH W 43 9.614 -8.502 3.480 1.00 17.83

ATOM 1306 OWl HOH W 44 9.751 3.961 13.933 1.00 21.21

ATOM 1307 OWl HOH W 45 13.185 -7.816 5.935 1.00 31.23

ATOM 1308 OWl HOH W 46 16.950 0.905 -6.705 1.00 10.93

ATOM 1309 OWl HOH W 47 -6.703 8.829 1.822 1.00 14.89

ATOM 1310 OWl HOH W 48 17.835 6.787 -4.998 1.00 26.47

ATOM 1311 OWl HOH W 49 -5.481 6.615 -7.204 1.00 21.08

ATOM 1312 OWl HOH W 50 14.056 -11.978 9.151 1.00- 27.14

ATOM 1313 OWl HOH W 51 8.106 10.102 10.247 1.00 16.13

ATOM 1314 OWl HOH W 52 14.039 -4.319 8.764 1.00 24.31

ATOM 1315 OWl HOH W 54 14.171 -9.181 6.350 1.00 31.79

ATOM 1316 OWl HOH W 55 9.371 6.753 10.595 1.00 15.83

ATOM 1317 OWl HOH W 56 10.811 21.573 -2.443 1.00 24.96

ATOM 1318 OWl HOH W 57 15.350 14.220 2.341 1.00 16.47

ATOM 1319 OWl HOH W 58 -6.379 11.410 -2.250 1.00 42.17

ATOM 1320 OWl HOH W 59 5.020 2.002 -14.750 1.00 16.82

ATOM 1321 OWO HOH W 60 2.152 -18.017 7.131 1.00 8.84

ATOM 1322 OWO HOH W 61 -1.683 -0.163 -9.953 1.00 7.74

ATOM 1323 OWO HOH W 62 10.118 -4.194 10.200 1.00 11.20

ATOM 1324 OWO HOH W 63 5.747 -6.991 -5.221 1.00 9.86

ATOM 1325 OWO HOH W 64 10.036 -2.782 -3.267 1.00 9.79

ATOM 1326 OWO HOH W 65 14.763 -2.273 -2.558 1.00 8.41

ATOM 1327 OWO HOH W 66 13.809 -6.053 -4.232 1.00 14.33

ATOM 1328 OWO HOH W 67 7.048 -9.230 2.615 1.00 12.78

ATOM 1329 OWO HOH W 68 1.986 -11.403 -3.448 1.00 12.18

ATOM 1330 OWO HOH W 69 12.410 2.429 -0.706 1.00 14.08

ATOM 1331 OWO HOH W 70 2.614 16.432 -5.876 1.00 14.57

ATOM 1332 OWO HOH W 71 10.093 3.485 4.885 1.00 12.02

ATOM 1333 OWO HOH W 72 1.393 -6.853 -14.033 1.00 14.04

ATOM 1334 OWO HOH W 73 4.511 12.017 -8.195 1.00 17.85

ATOM 1335 OWO HOH W 74 -8.671 4.266 -3.393 1.00 11.07

ATOM 1336 OWO HOH W 75 11.283 -6.644 13.561 1.00 16.78

ATOM 1337 OWO HOH W 76 6.252 -7.114 0.961 1.00 14.62

ATOM 1338 OWO HOH W 77 0.118 3.622 15.670 1.00 13.72

ATOM 1339 OWO HOH W 78 -6.431 -13.726 12.225 1.00 14.68

ATOM 1340 OWO HOH W 79 14.849 -2.561 1.391 1.00 17.43

ATOM 1341 OWO HOH W 80 11.604 0.644 2.654 1.00 14.19

ATOM 1342 OWO HOH W 81 -6.904 -7.704 16.840 1.00 14.33

ATOM 1343 OWO HOH W 82 -1.152 2.118 -7.581 ^■ 1.00 17.44

ATOM 1344 OWO HOH W 83 -9.964 -14.007 0.540 1.00 15.61

ATOM 1345 OWO HOH W 84 -4.413 -20.330 9.519 1.00 17.18

ATOM 1346 OWO HOH W 85 10.760 4.298 -1.634 1.00 17.18

ATOM 1347 OWO HOH W 86 -9.200 -12.071 8.820 1.00 20.44

ATOM 1348 OWO HOH W 87 -5.118 -22.943 5.703 1.00 17.06

ATOM 1349 OWO HOH W 88 -8.680 -9.788 16.594 1.00 18.59

ATOM 1350 OWO HOH W 89 7.018 -8.674 -7.261 1.00 18.84

ATOM 1351 OWO HOH W 90 -5.299 -16.759 -2.139 1.00 17.76

ATOM 1352 OWO HOH W 91 -5.728 7.984 4.015 1.00 18.02

ATOM 1353 owo HOH W 92 11.785 -2.626 7.631 1.00 17.13

ATOM 1354 OWO HOH W 93 11.952 -4.878 10.254 1.00 19.90

ATOM 1355 OWO HOH W 94 1.634 -12.244 15.841 1.00 17.01

ATOM 1356 OWO HOH W 95 -0.282 7.548 15.092 1.00 18.38

ATOM 1357 OWO HOH W 96 7.547 -6.909 -3.174 1.00 16.41

ATOM 1358 OWO HOH W 97 7.730 -22.600 7.521 1.00 21.40

ATOM 1359 OWO HOH W 98 12.393 7.670 -12.310 1.00 18.74

ATOM 1360 OWO HOH W 99 3.729 -8.809 -2.037 1.00 20.30

ATOM 1361 OWO HOH W 100 4.148 5.263 19.733 1.00 18.55

ATOM 1362 OWO HOH W 101 2.316 -4.233 -18.642 1.00 17.74

ATOM 1363 OWO HOH W 102 -0.714 -12.074 19.377 1.00 19.48

ATOM 1364 OWO HOH W 103 -3.990 17.672 -2.807 1.00 23.92

ATOM 1365 OWO HOH W 104 10.839 17.017 -7.209 1.00 22.40

ATOM 1366 OWO HOH W 105 8.546 -4.498 -1.868 1.00 18.12

ATOM 1367 OWO HOH W 106 8.722 18.458 6.350 1.00 21.23 Table 1

ATOM 1368 OWO HOH W 107 2.720 11.907 -9.537 27.04

ATOM 1369 OWO HOH W 108 9.085 24.794 0.468 21.63

ATOM 1370 OWO HOH W 109 5.743 8.463 13.980 19.04

ATOM 1371 OWO HOH W 110 3.782 -8.746 -4.602 23.26

ATOM 1372 OWO HOH W 111 0.406 -4.181 27.499 25.31

ATOM 1373 OWO HOH W 112 15.660 5.818 -11.602 23.96

ATOM 1374 OWO HOH ^•w 113 -7.364 2.735 13.578 25.60

ATOM 1375 OWO HOH W 114 11.202 9.968 8.439 21.44

ATOM 1376 OWO HOH W 115 -8.128 -12.359 15.760 21.18

ATOM 1377 OWO HOH W 116 12.864 10.083 -10.499 25.39

ATOM 1378 OWO HOH W 117 5.924 -10.406 -8.998 26.38

ATOM 1379 OWO HOH W 118 -9.144 -13.413 11.453 29.79

ATOM 1380 OWO HOH W 120 -10.709 -9.160 14.679 22.91

ATOM 1381 OWO HOH W 121 15.296 0.176 0.204 22.60

ATOM 1382 OWO HOH W 122 0.356 2.306 -10.316 24.70

ATOM 1383 OWO HOH W 123 5.666 -13.972 1.486 26.57

ATOM 1384 OWO HOH W 124 -0.223 6.245 -7.010 26.94

ATOM 1385 OWO HOH W 125 1.068 -5.071 25.440 19.64

ATOM 1386 OWO HOH W 126 8.812 25.323 -2.880 23.73

ATOM 1387 OWO HOH W 127 6.396 16.843 17.857 39.91

ATOM 1388 OWO HOH W 128 6.245 -18.421 2.339 33.56

ATOM 1389 OWO HOH W 129 -3.297 10.769 9.401 27.69

ATOM 1390 OWO HOH W 130 11.992 5.282 9.272 25.11

ATOM 1391 OWO HOH W 131 15.692 2.282 2.864 25.39

ATOM 1392 OWO HOH W 132 15.130 20.626 0.982 37.70

ATOM 1393 OWO HOH W 133 -3.676 4.739 -10.518 1.00 24.67

ATOM 1394 OWO HOH W 134 5.663 20.988 3.970 00 21.28

ATOM 1395 OWO HOH W 135 -5.266 9.534 10.512 00 33.13

ATOM 1396 OWO HOH W 136 2.479 5.947 18.199 00 34.86

ATOM 1397 OWO HOH W 137 2.001 -11.471 20.013 00 26.39

ATOM 1398 OWO HOH W 138 10.504 -20.185 7.481 00 35.60

ATOM 1399 OWO HOH W 140 1.564 6.589 -8.611 00 36.85

ATOM 1400 OWO HOH W 142 6.785 -17.037 14.305 00 23.74

ATOM 1401 OWO HOH W 143 5.773 -18.127 16.502 00 42.24

ATOM 1402 OWO HOH W 144 -2.713 7.105 -8.439 00 24.63

ATOM 1403 OWO HOH W 145 -12.164 1.308 11.719 00 27.37

ATOM 1404 OWO HOH W 146 5.350 -20.958 13.459 00 43.98

ATOM 1405 OWO HOH W 147 13.522 9.149 6.837 00 23.16

ATOM 1406 OWO HOH W 148 -16.895 -3.530 2.870 00 30.26

ATOM 1407 OWO HOH W 149 8.187 16.031 16.151 00 42.51

ATOM 1408 OWO HOH W 150 17.955 5.871 -0.876 00 32.61

ATOM 1409 OWO HOH W 151 16.307 -20.297 -6.597 00 30.40

ATOM 1410 OWO HOH W 152 -13.783 -9.539 0.061 00 24.18

ATOM 1411 OWO HOH W 153 -2.674 -12.935 21.943 00 39.32

ATOM 1412 OWO HOH W 154 -1.120 4.288 -6.030 00 25.39

ATOM 1413 OWO HOH W 155 12.094 -11.335 16.404 00 27.07

ATOM 1414 OWO HOH W 156 4.557 -12.981 21.758 00 29.44

ATOM 1415 OWO HOH W 157 0.849 -9.328 -13.368 00 27.83

ATOM 1416 OWO HOH W 158 -8.132 5.594 -4.935 00 19.05

ATOM 1417 OWO HOH W 159 -9.166 6.260 —7.504 00 26.56

ATOM 1418 OWO HOH W 161 11.549 17.528 7. ,505 00 35.88

ATOM 1419 OWO HOH W 162 7.821 17.666 -6.206 00 25.03

ATOM 1420 OWO HOH W 163 4.090 7.439 16.861 00 33.63

ATOM 1421 OWO HOH W 164 -4.076 12.801 9.056 00 32.88

ATOM 1422 OWO HOH W 165 16.133 14.800 4.786 00 38.91

ATOM 1423 OWO HOH W 166 6.344 -8.580 -1.125 00 27.93

ATOM 1424 OWO HOH W 168 -12.973 2.733 5.142 00 29.56

ATOM 1425 OWO HOH W 169 -2.299 2.356 -11.067 00 28.51

ATOM 1426 OWO HOH W 170 12.146 14.697 7.823 00 26.35

ATOM 1427 OWO HOH W 171 -4.329 15.787 -6.451 00 44.94

ATOM 1428 OWO HOH W 172 -12.737 -12.260 -1.058 00 31.73

ATOM 1429 OWO HOH W 173 -7.815 -17.832 -4.328 00 26.48

ATOM 1430 OWO HOH W 174 9.062 -6.081 2.622 00 31.73

ATOM 1431 OWO HOH W 175 -2.802 13.672 4.151 00 29.69

ATOM 1432 OWO HOH W 176 -1.501 14.371 0.753 00 25.46

ATOM 1433 OWO HOH W 177 -14.921 -10.539 2.308 00 37.98

ATOM 1434 OWO HOH W 178 10.841 -12.126 18.514 00 27.56

ATOM 1435 OWO HOH W 179 -2.847 1.791 -13.894 1.00 33.54 Table 1

ATOM 1436 OWO HOH W 180 14.537 1.942 10.780 1.00 34.67

ATOM 1437 OWO HOH W 181 0.202 4.260 -8.280 1.00 37.61

ATOM 1438 OWO HOH W 182 17.098 -1.028 7.656 1.00 31.29

END

TABLE 2

CRYSTl 30. ,800 82 .100 32. 400 90.00 118.00 90.00 P 1 21 1

SCALEl 0.032468 0. 000000 0.017263 0.00000

SCALE2 0.000000 0. 012180 0.000000 0.00000

SCALE3 0.000000 0. 000000 0.034956 0.00000

ATOM 1 N ASN A 24 15.947 15.993 4.621 1.00 47.50 N

ATOM 2 CA ASN A 24 15.571 14.566 4.811 1.00 44.48 C

ATOM 4 CB ASN A 24 14.108 14.469 5.269 1.00 43.36 C

ATOM 7 CG ASN A 24 13.945 14.364 6.789 1.00 45.23 C

ATOM 8 ODl ASN A 24 12.896 13.908 7.271 1.00 45.28 O

ATOM 9 ND2 ASN A 24 14.970 14.782 7.549 1.00 49.20 N

ATOM 12 C ASN A 24 15.731 13.734 3.539 1.00 42.69 C

ATOM 13 O ASN A 24 15.858 14.265 2.427 1.00 43.10 O

ATOM 17 N GLN A 25 15.710 12.418 3.728 1.00 39.93 N

ATOM 18 CA GLN A 25 15.580 11.468 2.632 1.00 37.93 C

ATOM 20 CB GLN A 25 16.960 11.003 2.151 1.00 40.41 C

ATOM 23 CG GLN A 25 17.162 11.033 0.629 1.00 42.30 C

ATOM 26 CD GLN A 25 16.890 9.696 -0.070 1.00 43.53 C

ATOM 27 OEl GLN A 25 16.302 8.772 0.509 1.00 43.98 O

ATOM 28 NE2 GLN A 25 17.342 9.587 -1.325 1.00 44.06 N

ATOM 31 C GLN A 25 14.730 10.301 3.134 1.00 34.34 C

ATOM 32 O GLN A 25 14.970 9.795 4.234 1.00 33.86 O

ATOM 34 N ILE A 26 13.719 9.919 2.341 1.00 31.11 N

ATOM 35 CA ILE A 26 12.773 8.852 2.677 1.00 27.72 C

ATOM 37 CB ILE A 26 11.377 9.416 3.065 1.00 26.82 C

ATOM 39 CGl ILE A 26 11.454 10.184 4.388 1.00 27.45 C

ATOM 42 CDl ILE A 26 10.186 10.925 4.764 1.00 26.97 C

ATOM 46 CG2 ILE A 26 10.325 8.292 3.166 1.00 25.20 C

ATOM 50 C ILE A 26 12.605 7.914 1.481 1.00 25.67 C

ATOM 51 O ILE A 26 12.244 8.350 0.378 1.00 24.88 O

ATOM 53 N ASP A 27 12.869 6.630 1.704 1.00 23.75 N

ATOM 54 CA ASP A 27 12.659 5.611 0.678 1.00 22.46 C

ATOM 56 CB ASP A 27 13.869 4.691 0.557 1.00 23.84 C

ATOM 59 CG ASP A 27 15.004 5.333 -0.196 1.00 27.22 C

ATOM 60 ODl ASP A 27 15.095 6.581 -0.188 1.00 30.57 O

ATOM 61 OD2 ASP A 27 15.811 4.592 -0.787 1.00 29.72 O

ATOM 62 C ASP A 27 11.413 4.803 0.979 1.00 19.41 C

ATOM 63 O ASP A 27 11.209 4.359 2.104 1.00 18.62 O

ATOM 65 N LEU A 28 10.586 4.634 -0.049 1.00 17.70 N

ATOM 66 CA LEU A 28 9.305 3.961 0.060 1.00 15.41 C

ATOM 68 CB LEU A 28 8.159 4.933 -0.267 1.00 15.06 C

ATOM 71 CG LEU A 28 8.044 6.201 0.596 1.00 15.31 C

ATOM 73 CDl LEU A 28 6.941 7.133 0.080 1.00 14.54 C

ATOM 77 CD2 LEU A 28 7.799 5.843 2.057 1.00 15.51 C

ATOM 81 C LEU A 28 9.313 2.772 -0.897 1.00 14.24 C

ATOM 82 O LEU A 28 9.148 2.924 -2.102 1.00 13.61 O

ATOM 84 N ASN A 29 9.559 1.591 -0.343 1.00 13.70 N

ATOM 85 CA ASN A 29 9.527 0.349 -1.111 1.00 13.32 C

ATOM 87 CB ASN A 29 10.371 -0.738 -0.437 1.00 13.91 C

ATOM 90 CG ASN A 29 11.842 -0.597 -0.747 1.00 16.55 C

ATOM 91 ODl ASN A 29 12.512 0.272 -0.206 1.00 18.34 O

ATOM 92 ND2 ASN A 29 12.354 -1.455 -1.635 1.00 18.31 N

ATOM 95 C ASN A 29 8.100 -0.117 -1.253 1.00 11.51 C

ATOM 96 O ASN A 29 7.407 -0.324 -0.263 1.00 10.06 O

ATOM 98 N VAL A 30 7.658 -0.257 -2.498 1.00 11.54 N

ATOM 99 CA VAL A 30 6.285 -0.634 -2.798 1.00 10.39 C

ATOM 101 CB VAL A 30 5.569 0.440 -3.656 1.00 10.55 C

ATOM 103 CGl VAL A 30 6.195 0.550 -5.044 1.00 11.68 C

ATOM 107 CG2 VAL A 30 5.573 1.805 -2.939 1.00 10.26 C

ATOM 111 C VAL A 30 6.261 -1.986 -3.519 1.00 10.68 C

ATOM 112 O VAL A 30 7.196 -2.323 -4.246 1.00 12.08 O

ATOM 114 N THR A 31 5.196 -2.757 -3.292 1.00 9.74 N

ATOM 115 CA THR A 31 4.974 -4.033 -3.974 1.00 9.92 C

ATOM 117 CB THR A 31 4.273 -5.063 -3.080 1.00 9.42 C

ATOM 119 OGl THR A 31 2.924 -4.636 -2.805 1.00 8.68 O

ATOM 121 CG2 THR A 31 5.041 -5.296 -1.779 1.00 9.45 C Table 2

ATOM 125 C THR A 31 4.065 -3.836 -5.188 1.00 10.01 C

ATOM 126 O THR A 31 3.526 -2.745 -5.406 1.00 9.24 O

ATOM 128 N CYS A 32 3.888 -4.910 -5.959 1.00 10.66 N

ATOM 129 CA CYS A 32 2.811 -4.996 -6.947 1.00 11.05 C

ATOM 131 CB CYS A 32 2.769 -6.398 -7.573 1.00 12.15 C

ATOM 134 SG CYS A 32 4.316 -6.924 -8.311 1.00 14.98 S

ATOM 136 C CYS A 32 1.475 -4.725 -6.247 00 9.79 C

ATOM 137 O CYS A 32 1.359 -4.916 -5.027 00 8.96 O

ATOM 139 N ARG A 33 0.495 -4.256 -7.012 00 9.28 N

ATOM 140 CA ARG A 33 -0.889 -4, 132 -6.543 00 B.69 C

ATOM 142 CB ARG A 33 -1.620 —2 929 -7.175 00 8.23 C

ATOM 145 CG ARG A 33 -1.326 -1.574 -6.549 00 93 C

ATOM 148 CD ARG A 33 0.155 -1.193 -6.694 00 35 C

ATOM 151 NE ARG A 33 0.462 -0.915 -8.085 00 84 N

ATOM 153 CZ ARG A 33 1.632 -1.122 -8.680 1.00 10.10 C

ATOM 154 NHl ARG A 33 1.756 -0.830 -9.977 1.00 11.28 N

ATOM 157 NH2 ARG A 33 2.666 624 -8.014 1.00 10.01 N

ATOM 160 C ARG A 33 -1.647 -5, 398 -6.895 1.00 9.12 C

ATOM 161 O ARG A 33 -1.413 997 -7.946 1.00 10.48 O

ATOM 163 N TYR A 34 -2.543 -5.795 -5.998 1.00 8.96 N

ATOM 164 CA TYR A 34 -3.467 -6.907 -6.193 1.00 9.84 C

ATOM 166 CB TYR A 34 -3.107 -8.083 -5.261 1.00 10.65 C

ATOM 169 CG TYR A 34 -1 743 -8.602 -5.592 1.00 11.27 C

ATOM 170 CDl TYR A 34 ^■0.615 -7.896 -5.202 1.00 11.87 C

ATOM 172 CEl TYR A 34 0.652 -8.321 -5.539 1.00 11.44 C

ATOM 174 CZ TYR A 34 0.805 -9.450 -6.272 1.00 12.65 C

ATOM 175 OH TYR A 34 2.083 -9.828 -6.584 1.00 14.81 O

ATOM 177 CE2 TYR A 34 -0.299 -10.180 -6.698 1.00 13.03 C

ATOM 179 CD2 TYR A 34 -1.570 -9.748 -6.360 00 12.53 C

ATOM 181 C TYR A 34 -4..854 -6.368 -5.891 00 9.31 C

ATOM 182 O TYR A 34 -5. 153 -5.997 -4.751 00 8.81 O

ATOM 184 N ALA A 35 -5.680 -6.272 -6.929 .00 9.90 N

ATOM 185 CA ALA A 35 -6.973 -5.646 -6.821 1.00 10.15 C

ATOM 187 CB ALA A 35 -7.923 -6.540 -6.040 1.00 10.83 C

ATOM 191 C ALA A 35 -6.840 -4.278 -6.156 1.00 9.32 C

ATOM 192 O ALA A 35 -7.657 -3.917 -5.316 1.00 8.95 O

ATOM 194 N GLY A 36 -5.797 -3.540 -6.530 00 8.98 N

ATOM 195 CA GLY A 36 -5.559 -2..191 -6.027 00 8.68 C

ATOM 198 C GLY A 36 -4..830 -2..097 -4.690 00 8.04 C

ATOM 199 O GLY A 36 -4..427 -1. 009 -4.293 00 7.55 O

ATOM 201 N VAL A 37 -4..661 -3.223 -3.997 00 8.29 N

ATOM 202 CA VAL A 37 -3..992 -3.239 -2.,691 00 8.06 C

ATOM 204 CB VAL A 37 -4..591 -4.319 -1..749 00 8.33 C

ATOM 206 CGl VAL A 37 -3..874 -4.334 -0.398 00 8.03 C

ATOM 210 CG2 VAL A 37 -6.067 -4 086 -1..542 00 8.67 C

ATOM 214 C VAL A 37 -2.492 -3 475 -2..857 00 8.12 C

ATOM 215 O VAL A 37 -2.075 -4 428 -3.544 00 8.98 O

ATOM 217 N PHE A 38 -1.693 -2 618 -2.216 00 7.58 N

ATOM 218 CA PHE A 38 -0.240 -2.805 -2.148 00 7.95 C

ATOM 220 CB PHE A 38 0.487 -1.958 -3.204 00 8.22 C

ATOM 223 CG PHE A 38 0.291 -0.455 -3.074 00 7.94 C

ATOM 224 CDl PHE A 38 1.365 0.372 -2.755 00 9.49 C

ATOM 226 CEl PHE A 38 1.216 1.761 -2. .672 00 8.90 C

ATOM 228 CZ PHE A 38 0.005 2.345 -2..929 00 8.58 C

ATOM 230 CE2 PHE A 38 -1.079 1.531 -3.266 1.00 9.30 C

ATOM 232 CD2 PHE A 38 -0.923 0.135 -3.348 1.00 7.96 C

ATOM 234 C PHE A 38 0.345 -2.538 -0.762 00 7.88 C

ATOM 235 O PHE A 38 -0.287 -1.912 0.090 00 8.09 O

ATOM 237 N HIS A 39 555 -3.048 -0.561 00 8.68 N

ATOM 238 CA HIS A 39 301 -2.914 0.682 00 9.02 C

ATOM 240 CB HIS A 39 924 -4.267 033 00 9.57 C

ATOM 243 CG HIS A 39 980 -4.216 094 00 9.48 C

ATOM 244 NDl HIS A 39 325 -4.205 795 00 9.82 N

ATOM 246 CEl HIS A 39 6.025 -4.206 917 1.00 10.03 C

ATOM 248 NE2 HIS A 39 5.183 -4.213 3.932 1.00 9.68 N

ATOM 250 CD2 HIS A 39 3.897 -4.231 3.445 1.00 9.94 C

ATOM 252 C HIS A 39 3.368 -1.831 0.504 1.00 9.86

ATOM 253 O HIS A 39 4.032 -1.766 -0.548 1.00 10.22 Table 2

ATOM 255 N N VAL A 40 3.513 -0.984 527 1.00 10.36 N ATOM 256 C CAA VAL A 40 4.531 0.061 550 1.00 11.56 C ATOM 258 C CBB VAL A 40 3.910 1.468 540 1.00 11.66 C ATOM 260 CGl VAL A 40 5.019 2.552 416 1.00 13.04 C ATOM 264 CG2 VAL A 40 2.877 1.584 0.439 1.00 10.71 C ATOM 268 C C VAL A 40 5.384 -0.081 2.803 1.00 12.58 C ATOM 269 O O VAL A 40 4.862 -0.136 3.921 1.00 11.94 O ATOM 271 N N GLO A 41 6.697 -0.133 2.600 1.00 14.39 N ATOM 272 C CAA GLU A 41 7.662 -0.161 3.686 1.00 16.02 C ATOM 274 C CBB GLU A 41 8.569 -1.365 3.527 1.00 16.39 C ATOM 277 C CGG GLU A 41 9.736 -1.405 4.476 1.00 18.39 C ATOM 280 C CDD GLU A 41 10.489 -2.712 4.381 1.00 20.40 C ATOM 281 OEl GLU A 41 9.978 -3.653 3.722 1.00 24.76 O ATOM 282 OE2 GLU A 41 11.567 -2.815 4.990 1.00 23.37 O ATOM 283 C C GLO A 41 8.467 1.122 3.637 1.00 17.20 C ATOM 284 O O GLU A 41 9.112 1.408 2.631 1.00 17.84 O ATOM 286 N N LYS A 42 8.428 1.899 4.710 1.00 18.38 N ATOM 287 C CAA LYS A 42 9.126 3.189 4.718 1.00 20.04 C ATOM 289 C CBB LYS A 42 8.303 4.264 5.417 1.00 20.18 C ATOM 292 C CGG LYS A 42 9.083 5.540 5.659 1.00 21.50 C ATOM 295 C CDD LYS A 42 8.557 6.298 6.842 1.00 22.28 C ATOM 298 C CEE LYS A 42 9.515 7.395 7.243 1.00 23.99 C ATOM 301 N NZZ LYS A 42 9.021 8.126 8.445 1.00 25.60 N ATOM 305 C C LYS A 42 10.486 3.074 5.385 1.00 21.87 C ATOM 306 O O LYS A 42 10.573 2.753 6.573 1.00 22.37 O ATOM 308 N N ASN A 43 11.537 3.377 4.621 1.00 23.38 N ATOM 309 C CAA ASN A 43 12.910 3.225 5.089 1.00 25.07 C ATOM 311 C CBB ASN A 43 13.270 4.324 6.105 1.00 26.13 C ATOM 314 C CGG ASN A 43 13.403 5.469 1.00 26.46 C ATOM 315 ODl ASN A 43 13.705 5.829 4.276 1.00 25.90 O ATOM 316 ND2 ASN A 43 13.205 6.732 6.274 1.00 27.73 N ATOM 319 C C ASN A 43 13.108 1.821 5.664 1.00 25.71 C ATOM 320 O O ASN A 43 13.168 0.848 4.912 1 1..00 26.59 O ATOM 322 N N GLY A 44 13.166 1.695 6.985 1 1..00 26.30 N ATOM 323 C CAA GLY A 44 13.302 0.373 7.600 1.00 25.86 C ATOM 326 C C GLY A 44 11.986 -0.357 7.837 1.00 24.43 C ATOM 327 O O GLY A 44 10.903 0.234 7.865 1.00 24.09 O ATOM 329 N N ARG A 45 12.095 -1.663 8.020 1.00 24.06 N ATOM 330 C CAA ARG A 45 10.971 -2.500 8.415 1.00 22.74 C ATOM 332 C CBB ARG A 45 11.525 -3.888 8.714 1.00 23.68 C ATOM 335 C CGG ARG A 45 10.549 -4.919 9.215 1.00 24.00 C ATOM 338 C CDD ARG A 45 11.243 -6.267 9.156 1.00 26.37 C ATOM 341 N NEE ARG A 45 10.606 -7.283 9.983 1.00 28.38 N ATOM 343 C CZZ ARG A 45 11.059 -7.696 11.162 1.00 30.83 C ATOM 344 NHl ARG A 45 12.158 -7.181 11.693 1.00 32.08 N ATOM 347 NH2 ARG A 45 10.395 -8.643 11.823 1.00 32.29 N ATOM 350 C C ARG A 45 10.236 -1.931 9.644 1.00 21.42 C ATOM 351 O O ARG A 45 10.853 -1.639 10.635 1.00 22.30 O ATOM 353 N N TYR A 46 8.919 -1.778 9.563 1.00 19.53 N ATOM 354 C CAA TYR A 46 8.093 -1.375 10.712 1.00 18.68 C ATOM 356 C CBB TYR A 46 8.115 -2.459 11.806 1.00 18.66 C ATOM 359 C CGG TYR A 46 7.654 -3.839 11.379 1.00 18.02 C ATOM 360 C CDDll TYR A 46 8.188 -4.979 11.981 1.00 18.99 C ATOM 362 C CEEll TYR A 46 7.766 -6.244 11.623 1.00 18.61 C ATOM 364 C CZZ TYR A 46 6.794 -6.392 10.631 1.00 17.53 C ATOM 365 O OHH TYR A 46 6.372 -7.655 10.264 1.00 17.15 O ATOM 367 CE2 TYR A 46 6.247 -5.274 10.027 1.00 16.18 C ATOM 369 CD2 TYR A 46 6.673 -4.011 10.398 1.00 16.05 C ATOM 371 C C TYR A 46 8.455 -0.027 11.347 1.00 18.94 C ATOM 372 O O TYR A 46 8.691 0.045 12.552 1.00 19.83 O ATOM 374 N N SER A 47 8.450 1.041 10.553 1.00 18.23 N ATOM 375 C CAA SER A 47 8.777 2.367 11.061 1.00 19.07 C ATOM 377 C CBB SER A 47 10.078 2.850 10.414 1.00 19.99 C ATOM 380 O OGG SER A 47 9.914 2.973 9.019 1.00 20.61 O ATOM 382 C C SER A 47 7.673 3.399 10.851 1.00 18.37 C ATOM 383 O O SER A 47 7.916 4.593 10.979 1.00 19.78 O ATOM 385 I ISSll ILE A 48 6.454 2.940 10.569 1.00 16.97 N ATOM 386 C CAA ILE A 48 5.326 3.818 10.256 1.00 16.77 C Table 2

ATOM 388 CB ILE A 48 4.619 3.356 8.930 1.00 15.41 C

ATOM 390 CGl ILE A 48 5.619 3.268 7.775 1.00 15.30 C

ATOM 393 CDl ILE A 48 5.051 2.638 6.528 1.00 14.94 C

ATOM 397 CG2 ILE A 48 3.481 4.268 8.563 1.00 15.50 C

ATOM 401 C ILE A 48 4.297 3.783 11.389 1.00 16.77 C

ATOM 402 O ILE A 48 3..897 2.708 11.822 1.00 15.60 O

ATOM 404 N SER A 49 3..349 4.953 11.844 1.00 17.56 N

ATOM 405 CA SER A 49 2.726 5.038 12.788 1.00 18.59 C

ATOM 407 CB SER A 49 2.801 6.317 13.618 1.00 20.17 C

ATOM 410 OG SER A 49 2.549 7.445 12.303 1.00 20.91 O

ATOM 412 C SER A 49 1.400 5.002 12.034 1.00 17.90 C

ATOM 413 O SER A 49 1.374 5.104 10.311 1.00 16.47 O

ATOM 415 N ARG A 50 0.298 4.867 12.761 1.00 19.30 N

ATOM 416 CA ARG A 50 -1.018 4.778 12.118 1.00 19.06 C

ATOM 418 CB ARG A 50 -2.080 4.313 13.127 1.00 20.81 C

ATOM 421 CG ARG A 50 -3.559 4.483 12.733 1.00 22.27 C

ATOM 424 CD ARG A 50 -4.020 3.951 11.350 1.00 25.70 C

ATOM 427 NE ARG A 50 -4.209 2.495 11.231 1.00 26.54 N

ATOM 429 CZ ARG A 50 -5.007 1.737 11.993 1.00 28.18 C

ATOM 430 NHl ARG A 50 -5.734 2.255 12.988 1.00 30.99 N

ATOM 433 NH2 ARG A 50 -5.075 0.431 11.765 1.00 26.33 N

ATOM 436 C ARG A 50 -1.375 6.107 11.439 1.00 19.38 C

ATOM 437 O ARG A 50 -1.932 6.107 10.336 1.00 18.44 O

ATOM 439 N THR A 51 -1.005 7.225 12.067 1.00 20.61 N

ATOM 440 CA THR A 51 -1.233 8.544 11.478 1.00 21.41 C

ATOM 442 CB THR A 51 -1.008 9.728 12.459 1.00 23.75 C

ATOM 444 OGl THR A 51 0.274 9.624 13.109 1.00 24.78 O

ATOM 446 CG2 THR A 51 -2.118 9.768 13.482 1.00 25.61 C

ATOM 450 C THR A 51 -0.393 8.751 10.231 1.00 20.22 C

ATOM 451 O THR A 51 -0.905 9.252 9.241 1.00 20.53 O

ATOM 453 N GLU A 52 0.878 8.352 10.265 1.00 19.27 N

ATOM 454 CA GLU A 52 728 9.091 1.00 18.24 C

ATOM 456 CB GLU A 52 192 8.211 9.417 1.00 18.34 C

ATOM 459 CG GLU A 52 101 8.351 8.193 1.00 18.35 C

ATOM 462 CD GLU A 52 5.571 8.320 8.525 1.00 19.49 C

ATOM 463 OEl GLϋ A 52 5.904 8.207 9.712 1.00 22.84 O

ATOM 464 OE2 GLU A 52 6.395 8.417 7.598 1.00 20.78 O

ATOM 465 C GLU A 52 1.277 7.587 7.944 1.00 16.34 C

ATOM 466 O GLU A 52 1.444 7.953 6.777 1.00 15.85 O

ATOM 468 N ALA A 53 0.737 6.412 8.281 1.00 15.02 N

ATOM 469 CA ALA A 53 0.275 5.445 7.285 1.00 13.44 C

ATOM 471 CB ALA A 53 -0.129 4.128 7.965 1.00 12.93 C

ATOM 475 C ALA A 53 -0.893 6.003 6.465 1.00 13.39 C

ATOM 476 O ALA A 53 -0.917 5.854 5.242 1.00 12.46 O

ATOM 478 N ALA A 54 -1..851 6.640 7.144 1.00 14.11 N

ATOM 479 CA ALA A 54 -2..974 7.276 6.476 1.00 14.91 C

ATOM 481 CB ALΔ A 54 -3 984 7.786 7.488 1.00 16.38 C

ATOM 485 C ALA A 54 .489 8.415 5.575 1.00 15.41 C

ATOM 486 O ALA A 54 2..949 8.547 4.450 1.00 15.18 O

ATOM 488 N ASP A 55 -1 539 9.211 6.065 1.00 15.32 N

ATOM 489 CA ASP A 55 -0.949 10.288 5.264 1.00 16.72 C

ATOM 491 CB ASP A 55 0.001 11.150 6.107 1.00 18.31 C

ATOM 494 CG ASP A 55 -0.729 12.040 7.100 1.00 20.67 C

ATOM 495 ODl ASP A 55 -1.956 12.217 6.994 1.00 22.01 O

ATOM 496 OD2 ASP A 55 -0.056 12.577 7.995 1.00 23.61 O

ATOM 497 C ASP A 55 -0.192 9.748 4.050 1.00 14.90 C

ATOM 498 O ASP A 55 -0.254 10.326 2.972 1.00 14.28 O

ATOM 500 N LEO A 56 0.511 8.640 4.242 1.00 13.79 N

ATOM 501 CA LEU A 56 1.257 7.993 3.176 1.00 13.07 C

ATOM 503 CB LEU A 56 2.064 6.813 3.748 1.00 12.74 C

ATOM 506 CG LEU A 56 3.174 6.185 2.896 1.00 12.33 C

ATOM 508 CDl LEU A 56 4.054 .224 2.236 1.00 14.66 C

ATOM 512 CD2 LEU A 56 3.994 .257 3.765 1.00 12.61 C

ATOM 516 C LEU A 56 0.329 .495 2.065 1.00 12.13 C

ATOM 517 O LEU A 56 0.555 .770 0.888 1.00 12.71 O

ATOM 519 N CYS A 57 -0.711 6.752 2, 434 1.00 11.18 N

ATOM 520 CA CYS A 57 -1.669 6.267 1.445 1.00 10.84 C

ATOM 522 CB CYS A 57 -2.759 5.406 2.088 1.00 10.29 C Table 2

ATOM 525 SG CYS A 57 200 3.780 2.750 1.00 8.91 S

ATOM 527 C CYS A 57 302 7.434 0.690 1.00 11.58 C

ATOM 528 O CYS A 57 429 7.377 -0 525 1.00 11.01 O

ATOM 530 N AGLN A 58 684 8.477 1.421 0.50 13.03 N

ATOM 531 N BGLN A 58 696 8.482 1.411 0.50 12.69 N

ATOM 532 CA AGLN A 58 -3.285 9.679 0.831 0.50 14.43 C

ATOM 533 CA BGLN A 58 -3.300 9.674 0.788 0.50 14.06 C

ATOM 536 CB AGLN A 58 -3.599 10.687 1.939 0.50 16.02 C

ATOM 537 CB BGLN A 58 -3.679 10.709 1.855 0.50 15.51 C

ATOM 542 CG AGLN A 58 -4.395 11.905 1.500 0.50 17.92 C

ATOM 543 CG BGLN A 58 -4.111 12.090 1.325 0.50 16.94 C

ATOM 548 CD AGLN A 58 -4.966 12.678 2.675 0.50 19.74 C

ATOM 549 CD BGLN A 58 -5.329 12.044 0.403 0.50 16.26 C

ATOM 550 OElAGLN A 58 -5.588 12.103 3.574 0.50 21.68 O

ATOM 551 OElBGLN A 58 -6.104 11.084 0.409 0.50 15.28 O

ATOM 552 NE2AGLN A 58 -4.759 13.985 2.677 0.50 22.23 N

ATOM 553 NE2BGLN A 58 -5.507 13.095 0.378 0.50 16.26 N

ATOM 558 C AGLN A 58 -2.377 10.314 0.229 0.50 14.76 C

ATOM 559 C BGLN A 58 -2.371 10.301 0.255 0.50 14.52 C

ATOM 560 O AGLN A 58 854 10.774 -1 278 0.50 15.26 O

ATOM 561 O BGLN A 58 830 10.749 1.317 0.50 15.01 O

ATOM 564 N ALA A 59 075 10.327 0.053 .00 14.64 N

ATOM 565 CA ALA A 59 049 10.831 0.877 .00 15.16 C

ATOM 567 CB ALA A 59 295 10.858 0.191 .00 15.58 C

ATOM 571 C ALA A 59 0.041 10.001 2.167 .00 14.56 C

ATOM 572 O ALA A 59 0.409 10.516 -3 230 .00 14.86 O

ATOM 574 N PHE A 60 -0 299 8.718 -2.056 .00 13.01 N

ATOM 575 CA PHE A 60 ^■0.419 7.819 -3.200 .00 12.69 C

ATOM 577 CB PHE A 60 ^■0.135 6.363 -2.754 .00 11.69 C

ATOM 580 CG PHE A 60 1.323 .998 2.685 .00 11.12 C

ATOM 581 CDl PHE A 60 1.904 .639 484 .00 11.67 C

ATOM 583 CEl PHE A 60 3.255 .278 1.414 00 12.03 C

ATOM 585 CZ PHE A 60 4.023 .265 2.553 00 12.35 C

ATOM 587 CE2 PHE A 60 3.451 .619 3.772 00 12.58 C

ATOM 589 CD2 PHE A 60 105 .977 3.833 00 12.58 C

ATOM 591 C PHE A 60 821 .849 3.845 00 13.01 C

ATOM 592 O PHE A 60 148 6.957 4.624 00 12.74 O

ATOM 594 N AASN A 61 634 8.856 3.521 0.50 13.88 N

ATOM 595 N BASN A 61 622 8.872 3.530 0.50 13.96 N

ATOM 596 CA AASN A 61 ^•4.016 8.921 3.985 0.50 14.25 C

ATOM 597 CA BASN A 61 ^■4.025 8.931 3.938 0.50 14.41 C

ATOM 600 CB AASN A 61 ^•4.061 9.231 -5.491 0.50 15.05 C

ATOM 601 CB BASN A 61 ^■4.146 9.363 -5 406 0.50 15.54 C

ATOM 606 CG AASN A 61 ^■5.414 9.756 5.940 0.50 16.12 C

ATOM 607 CG BASN A 61 ^•4.116 10.869 5.572 0.50 17.90 C

ATOM 608 ODlAASN A 61 6.039 10.554 5.241 0.50 17.26 O

ATOM 609 ODlBASN A 61 ^■4.774 11.603 -4 828 0.50 20.33 O

ATOM 610 ND2AASN A 61 -5 866 9.321 7.116 0.50 16.49 N

ATOM 611 ND2BASN A 61 -3.372 11.337 6.556 0.50 19.06 N

ATOM 616 C AASN A 61 -4.759 .616 3.669 0.50 13.40 C

ATOM 617 C BASN A 61 -4.719 .596 3.683 0.50 13.48 C

ATOM 618 O AASN A 61 -5.545 .121 4.474 0.50 13.31 O

ATOM 619 O BASN A 61 -5.415 .056 4.543 0.50 13.29 O

ATOM 622 N SER A 62 -4.480 .068 2.483 .00 12.90 N

ATOM 623 CA SER A 62 010 .794 2.050 .00 11.66 C

ATOM 625 CB SER A 62 886 .760 2.061 .00 10.67 C

ATOM 628 OG SER A 62 -3.343 .666 3.372 .00 9.95 O

ATOM 630 C SER A 62 -5.590 .956 0.655 .00 12.18 C

ATOM 631 O SER A 62 -5.509 .034 0.057 .00 13.02 O

ATOM 633 N THR A 63 -6.188 .880 0.159 .00 11.55 N

ATOM 634 CA THR A 63 -6.751 .832 1.173 .00 11.74 C

ATOM 636 CB THR A 63 -8.308 4.779 1.127 .00 12.76 C

ATOM 638 OGl THR A 63 -8.745 3.651 0.363 .00 12.52 O

ATOM 640 CG2 THR A 63 -8.883 6.056 0.502 .00 13.62 C

ATOM 644 C THR A 63 -6.210 3.601 1.878 1.00 10.56 C

ATOM 645 O THR A 63 -5.686 2.698 1.232 1.00 10.06 O

ATOM 647 N LED A 64 -6.304 3.577 3.203 1.00 10.81 N

ATOM 648 CA LEU A 64 -5.993 2.368 3.951 1.00 10.32 C Table 2

ATOM 650 CB LEU A 64 -6.016 2.647 5.451 1.00 11.35 C

ATOM 653 CG LEU A 64 -4.892 3.487 6.052 1.00 11.78 C

ATOM 655 CDl LEU A 64 -5.284 3.908 7.451 1.00 13.26 C

ATOM 659 CD2 LEU A 64 -3.602 2.718 6.081 1.00 12.40 C

ATOM 663 C LEU A 64 -7.064 1.324 3.575 1.00 10.12 C

ATOM 664 O LEU A 64 -8.256 1.647 3.583 1.00 10.92 O

ATOM 666 N PRO A 65 -6.649 0.108 3.174 1.00 9.24 N

ATOM 667 CA PRO A 65 -7.657 -0.866 2.743 1.00 9.70 C

ATOM 669 CB PRO A 65 -6.829 -2.107 2.372 1.00 9.17 C

ATOM 672 CG PRO A 65 -5.455 -1.563 2.022 1.00 8.30 C

ATOM 675 CD PRO A 65 -5.275 -0.404 3.001 1.00 8.28 C

ATOM 678 C PRO A 65 -8.690 -1.229 3.805 1.00 10.61 C

ATOM 679 O PRO A 65 -8.398 -1.206 5.004 1.00 10.21 O

ATOM 680 N THR A 66 -9.894 -1.550 3.356 1.00 11.32 N

ATOM 681 CA THR A 66 -10.861 -2.209 4.209 1.00 13.17 C

ATOM 683 CB THR A 66 -12.326 -2.117 3.670 1.00 14.64 C

ATOM 685 OGl THR A 66 -12.432 -2.813 2.427 1.00 14.32 O

ATOM 687 CG2 THR A 66 -12.777 -0.657 3.475 1.00 15.77 C

ATOM 691 C THR A 66 -10.458 -3.677 4.271 1.00 13.11 C

ATOM 692 O THR A 66 -9.650 -4.144 3.467 1.00 11.97 O

ATOM 694 N AMET A 67 -11.024 -4.406 5.225 0.50 14.18 N

ATOM 695 N BMET A 67 -11.046 -4.389 5.222 0.50 14.83 N

ATOM 696 CA AMET A 67 -10.761 -5.837 5.358 0.50 14.57 C

ATOM 697 CA BMET A 67 -10.822 -5.817 5.398 0.50 15.18 C

ATOM 700 CB AMBT A 67 -11.413 -6.404 6.629 0.50 15.99 C

ATOM 701 CB BMET A 67 -11.588 -6.312 6.634 0.50 17.36 C

ATOM 706 CG AMET A 67 -11.357 -7.935 6.743 0.50 16.50 C

ATOM 707 CG BMET A 67 -11.244 -7.726 7.071 0.50 18.40 C

ATOM 712 SD AMET A 67 -9.685 -8.633 6.741 0.50 13.76 S

ATOM 713 SD BMET A 67 -9.570 -7.874 7.729 0.50 20.06 S

ATOM 714 CE AMET A 67 -9.151 -8.179 8.395 0.50 14.68 C

ATOM 715 CE BMET A 67 -9.565 -9.592 8.226 0.50 20.74 C

ATOM 722 C AMET A 67 -11.241 -6.599 4.121 0.50 14.89 C

ATOM 723 C BMET A 67 -11.253 -6.593 4.150 0.50 15.29 C

ATOM 724 O AMET A 67 -10.526 -7.455 3.607 0.50 14.25 O

ATOM 725 O BMET A 67 -10.516 -7.442 3.657 0.50 14.59 O

ATOM 728 N ASP A 68 -12.436 -6.275 3.638 1.00 16.22 N

ATOM 729 CA ASP A 68 -12.948 -6.872 2.397 1.00 16.78 C

ATOM 731 CB ASP A 68 -14.363 -6.364 2.112 1.00 18.48 C

ATOM 734 CG ASP A 68 -15.420 -7.055 2.969 1.00 22.00 C

ATOM 735 ODl ASP A 68 -15.052 -7.923 3.796 1.00 22.81 O

ATOM 736 OD2 ASP A 68 -16.624 -6.742 2.789 1.00 24.54 O

ATOM 737 C ASP A 68 -12.041 -6.621 1.175 1.00 15.27 C

ATOM 738 O ASP A 68 -11.830 -7.521 0.361 1.00 15.39 O

ATOM 740 N GLN A 69 -11.517 -5.405 1.044 1.00 14.08 N

ATOM 741 CA GLN A 69 -10.528 -5.096 -0.012 1.00 12.59 C

ATOM 743 CB GLN A 69 -10.157 -3.609 0.015 1.00 11.69 C

ATOM 746 CG GLN A 69 -11.090 -2.740 -0.813 1.00 12.02 C

ATOM 749 CD GLN A 69 -11.141 -1.292 -0.343 1.00 11.90 C

ATOM 750 OEl GLN A 69 -10.376 -0.873 0.530 1.00 9.71 O

ATOM 751 NE2 GLN A 69 -12.056 -0.516 -0.926 1.00 14.10 N

ATOM 754 C GLN A 69 -9.259 -5.956 0.104 1.00 11.85 C

ATOM 755 O GLN A 69 -8.731 -6.443 -0.903 1.00 11.31 O

ATOM 757 N AMET A 70 -8.785 -6.128 1.335 0.50 11.97 N

ATOM 758 N BMET A 70 -8.762 -6.126 1.327 0.50 11.77 N

ATOM 759 CA AMET A 70 -7.618 -6.957 1.619 0.50 11.65 C

ATOM 760 CA BMET A 70 -7.592 -6.971 1.560 0.50 11.48 C

ATOM 763 CB AMET A 70 -7.223 -6.805 3.092 0.50 11.79 C

ATOM 764 CB BMET A 70 -7.087 -6.824 2.998 0.50 11.38 C

ATOM 769 CG AMET A 70 -5.876 -7.413 3.457 0.50 12.19 C

ATOM 770 CG BMET A 70 -5.949 -7.780 3.354 0.50 11.81 C

ATOM 775 SD AMET A 70 -4.483 -6.812 2.479 0.50 13.75 S

ATOM 776 SD BMET A 70 -4.482 -7.625 2.310 0.50 11.68 S

ATOM 111 CE AMET A 70 -4.508 -5.087 2.903 0.50 11.88 C

ATOM 118 CE BMET A 70 -3.795 -6.101 2.988 0.50 10.54 C

ATOM 785 C AMET A 70 -7.887 -8.436 1.290 0.50 12.59 C

ATOM 786 C BMET A 70 -7.893 -8.446 1.252 0.50 12.48 C

ATOM 787 O AMET A 70 -7.020 -9.132 0.748 0.50 12.03 O Table 2

ATOM 788 O BMET A 70 -7.048 -9.156 0.694 0.50 11.92 O

ATOM 791 N LYS A 71 -9.088 -8.905 1.615 1.00 13.77 N

ATOM 792 CA LYS A 71 -9.468 -10.295 1.358 1.00 15.66 C

ATOM 794 CB LYS A 71 -10.822 -10.628 2.002 1.00 17.48 C

ATOM 797 CG LYS A 71 -10.730 -10.842 3.503 1.00 18.37 C

ATOM 800 CD LYS A 71 -12.095 -11.046 4.147 1.00 20.22 C

ATOM 803 CE LYS A 71 -11.940 -11.395 5.618 1.00 21.81 C

ATOM 806 NZ LYS A 71 -13.184 -11.953 6.228 1.00 25.03 N

ATOM 810 C LYS A 71 -9.498 -10.597 -0.141 1.00 15.94 C

ATOM 811 O LYS A 71 -9.014 -11.643 -0.586 1.00 16.85 O

ATOM 813 N LEU A 72 -10.059 -9.684 -0.918 1.00 15.38 N

ATOM 814 CA LEU A 72 -10.086 -9.862 -2.367 1.00 15.67 C

ATOM 816 CB LEU A 72 -10.957 -8.809 -3.053 1.00 15.83 C

ATOM 319 CG LEU A 72 -11.250 -9.150 -4.525 1.00 16.69 C

ATOM 821 CDl LEU A 72 -12.234 -10.278 -4.631 1.00 19.27 C

ATOM 825 CD2 LEU A 72 -11.751 -7.933 -5.272 1.00 16.96 C

ATOM 829 C LEU A 72 -8.669 -9.845 -2.955 1.00 14.03 C

ATOM 830 O LEU A 72 -8.357 -10.632 -3.835 1.00 14.24 O

ATOM 832 N ALA A 73 -7.832 -8.938 -2.470 1.00 12.46 N

ATOM 833 CA ALA A 73 -6.432 -8.861 -2.892 1.00 11.85 C

ATOM 835 CB ALA A 73 -5.737 -7.741 -2.165 1.00 10.35 C

ATOM 839 C ALA A 73 -5.712 -10.193 -2.646 1.00 12.61 C

ATOM 840 O ALA A 73 -5.002 -10.694 -3.521 1.00 12.57 O

ATOM 842 N ALEU A 74 -5.919 -10.761 -1.462 0.50 12.85 N

ATOM 843 N BLEU A 74 -5.903 -10.751 -1.450 0.50 13.12 N

ATOM 844 CA ALEU A 74 -5.332 -12.050 -1.111 0.50 14.08 C

ATOM 845 CA BLEU A 74 -5.355 -12.062 -1.096 0.50 14.40 C

ATOM 848 CB ALEU A 74 -5.685 -12.425 0.334 0.50 14.37 C

ATOM 849 CB BLEO A 74 -5.798 -12.478 0.314 0.50 14.96 C

ATOM 854 CG ALEO A 74 -4.830 -13.502 1.014 0.50 14.92 C

ATOM 855 CG BLEU A 74 -5.498 -13.922 0.750 0.50 16.58 C

ATOM 858 CDlALEU A 74 -4.911 -13.350 2.521 0.50 14.38 C

ATOM 859 CDlBLEU A 74 -4.078 -14.055 1.236 0.50 16.36 C

ATOM 866 CD2ALEU A 74 -5.232 -14.915 0.597 0.50 16.30 C

ATOM 867 CD2BLEU A 74 -6.453 -14.369 1.837 0.50 18.10 C

ATOM 874 C ALEU A 74 -5.786 -13.133 -2.098 0.50 15.79 C

ATOM 875 C BLEU A 74 -5.784 -13.117 -2.116 0.50 15.95 C

ATOM 876 O ALEU A 74 -4.966 -13.911 -2.579 0.50 16.35 O

ATOM 877 O BLEU A 74 -4.952 -13.863 -2.624 0.50 16.43 O

ATOM 880 N SER A 75 -7.080 -13.160 -2.422 1.00 16.79 N

ATOM 881 CA SER A 75 -7.607 -14.133 -3.400 1.00 18.93 C

ATOM 883 CB SER A 75 -9.141 -14.039 -3.537 1.00 19.66 C

ATOM 886 OG SER A 75 -9.545 -12.911 -4.289 1.00 19.07 O

ATOM 888 C SER A 75 -6.921 -14.029 -A. Ill 1.00 19.05 C

ATOM 889 O SER A 75 -6.810 -15.032 -5.466 1.00 21.21 O

ATOM 891 N LYS A 76 -6.431 -12.837 -5.130 1.00 17.71 N

ATOM 892 CA LYS A 76 -5.719 -12.619 -6.404 1.00 18.13 C

ATOM 894 CB LYS A 76 -5.843 -11.163 -6.869 1.00 17.33 C

ATOM 897 CG LYS A 76 -7.210 -10.547 -6.830 1.00 17.64 C

ATOM 900 CD LYS A 76 -8.131 -11.221 -1.111 1.00 19.96 C

ATOM 903 CE LYS A 76 -9.370 -10.380 -7.979 1.00 20.00 C

ATOM 906 NZ LYS A 76 -10.427 -11.171 -8.672 1.00 22.28 N

ATOM 910 C LYS A 76 -4.212 -12.933 -6.353 1.00 18.40 C

ATOM 911 O LYS A 76 -3.506 -12.753 -7.354 1.00 13.99 O

ATOM 913 N GLY A 77 -3.707 -13.366 -5.201 1.00 18.08 N

ATOM 914 CA GLY A 77 -2.294 -13.731 -5.080 1.00 18.00 C

ATOM 917 C GLY A 77 -1.457 -12.862 -4.163 1.00 16.27 C

ATOM 918 O GLY A 77 -0.252 -13.070 -4.068 1.00 16.21 O

ATOM 920 N PHE A 78 -2.081 -11.897 -3.478 1.00 15.01 N

ATOM 921 CA PHE A 78 -1.353 -11.006 -2.580 1.00 13.76 C

ATOM 923 CB PHE A 78 -2.183 -9.749 -2.264 1.00 12.27 C

ATOM 926 CG PHE A 78 -1.422 -8.657 -1.532 1.00 11.41 C

ATOM 927 CDl PHE A 78 -0.090 -8.354 -1.843 1.00 11.58 C

ATOM 929 CEl PHE A 78 0.587 -7.336 -1.185 1.00 10.17 C

ATOM 931 CZ PHE A 78 -0.057 -6.607 -0.215 1.00 9.84 C

ATOM 933 CE2 PHE A 78 -1.384 -6.899 0.109 1.00 10.11 C

ATOM 935 CD2 PHE A 78 -2.052 -7.909 -0.549 1.00 10.46 C

ATOM 937 C PHE A 78 -1.009 -11.713 -1.273 1.00 13.99 C Table 2

ATOM 938 O PHE A 78 -1.892 -12.209 -0.584 1.00 14.17 O

ATOM 940 N GLϋ A 79 0.279 -11.747 -0.946 1.00 13.97 N

ATOM 941 CA GLU A 79 0.724 -12.123 0.392 1.00 14.46 C

ATOM 943 CB GLϋ A 79 0.799 -13.664 0.554 1.00 16.27 C

ATOM 946 CG GLϋ A 79 2.124 -14.300 0.182 1.00 17.76 C

ATOM 949 CD GLϋ A 79 2.140 -15.816 0.341 1.00 20.12 C

ATOM 950 OEl GLϋ A 79 2.795 -16.461 -0.492 1.00 22.12 O

ATOM 951 OE2 GLU A 79 1.504 -16.375 1.269 1.00 21.82 O

ATOM 952 C GLϋ A 79 2.058 -11.422 0.687 1.00 13.84 C

ATOM 953 O GLϋ A 79 2.834 -11.121 -0.228 1.00 15.01 O

ATOM 955 N THR A 80 2.285 -11.115 1.961 1.00 13.46 N

ATOM 956 CA THR A 80 3.567 -10.592 2.458 1.00 13.30 C

ATOM 958 CB THR A 80 3.469 -9.103 2.869 1.00 11.86 C

ATOM 960 OGl THR A 80 2.744 -9.004 4.103 1.00 10.80 O

ATOM 962 CG2 THR A 80 2.784 -8.247 1.767 1.00 10.78 C

ATOM 966 C THR A 80 3.931 -11.352 3.720 1.00 14.08 C

ATOM 967 O THR A 80 3.116 -12.098 4.250 1.00 13.78 O

ATOM 969 N CYS A 81 5.139 -11.109 4.221 1.00 15.19 N

ATOM 970 CA CYS A 81 5.545 -11.552 5.551 1.00 15.87 C

ATOM 972 CB CYS A 81 6.804 -12.409 5.450 1.00 17.97 C

ATOM 975 SG CYS A 81 7.148 -13.295 6.946 1.00 19.83 S

ATOM 977 C CYS A 81 5.788 -10.346 6.469 1.00 15.40 C

ATOM 978 O CYS A 81 6.742 -10.342 7.261 1.00 15.46 O

ATOM 980 N ARG A 82 4.896 -9.348 6.367 1.00 14.02 N

ATOM 981 CA ARG A 82 4.995 -8.079 7.101 1.00 13.29 C

ATOM 983 CB ARG A 82 5.497 -6.976 6.181 1.00 12.95 C

ATOM 986 CG ARG A 82 6.885 -7.180 5.692 1.00 15.31 C

ATOM 989 CD ARG A 82 7.871 -7.171 6.836 1.00 19.54 C

ATOM 992 NE ARG A 82 9.232 -7.082 6.329 1.00 21.96 N

ATOM 994 CZ ARG A 82 9.807 -5.957 5.921 1.00 23.09 C

ATOM 995 NHl ARG A 82 11.067 -5.986 5.468 1.00 24.30 N

ATOM 998 NH2 ARG A 82 9.142 -4.808 5.988 1.00 22.21 N

ATOM 1001 C ARG A 82 3.659 -7.616 7.676 1.00 12.68 C

ATOM 1002 O ARG A 82 2.635 -7.612 6.981 1.00 11.50 O

ATOM 1004 N TYR A 83 3.684 -7.219 8.947 1.00 13.11 N

ATOM 1005 CA TYR A 83 2.532 -6.600 9.595 1.00 12.88 C

ATOM 1007 CB TYR A 83 2.695 -6.572 11.120 1.00 14.97 C

ATOM 1010 CG TYR A 83 2.562 -7.933 11.763 1.00 16.80 C

ATOM 1011 CDl TYR A 83 3.682 -8.624 12.222 1.00 18.44 C

ATOM 1013 CEl TYR A 83 3.562 -9.885 12.797 1.00 19.49 C

ATOM 1015 CZ TYR A 83 2.319 -10.451 12.928 1.00 19.93 C

ATOM 1016 OH TYR A 83 2.196 -11.698 13.484 1.00 23.18 O

ATOM 1018 CE2 TYR A 83 1.192 -9.789 12.475 1.00 19.29 C

ATOM 1020 CD2 TYR A 83 1.321 -8.532 11.906 1.00 17.75 C

ATOM 1022 C TYR A 83 2.366 -5.183 9.049 1.00 11.62 C

ATOM 1023 O TYR A 83 3.337 -4.457 8.890 1.00 11.82 O

ATOM 1025 N GLY A 84 1.130 -4.799 8.772 1.00 10.44 N

ATOM 1026 CA GLY A 84 0.847 -3.501 8.196 1.00 9.69 C

ATOM 1029 C GLY A 84 -0.558 -3.034 8.486 1.00 9.39 C

ATOM 1030 O GLY A 84 -1.472 -3.844 8.613 1.00 8.84 O

ATOM 1032 N PHE A 85 -0.710 -1.713 8.566 1.00 9.45 N

ATOM 1033 CA PHE A 85 -1.998 -1.069 8.782 1.00 10.15 C

ATOM 1035 CB PHE A 85 -1.828 0.444 8.988 1.00 10.93 C

ATOM 1038 CG PHE A 85 -0.975 0.802 10.160 1.00 11.41 C

ATOM 1039 CDl PHE A 85 0.311 1.257 9.977 1.00 12.08 , C

ATOM 1041 CEl PHE A 85 1.108 1.588 11.064 1.00 12.85 C

ATOM 1043 CZ PHE A 85 0.631 1.450 12.348 1.00 13.86 C

ATOM 1045 CE2 PHE A 85 -0.651 0.988 12.554 1.00 14.43 C

ATOM 1047 CD2 PHE A 85 -1.455 0.664 11.453 1.00 13.84 C

ATOM 1049 C PHE A 85 -2.966 -1.279 7.626 1.00 10.07 C

ATOM 1050 O PHE A 85 -2.587 -1.196 6.458 1.00 8.57 O

ATOM 1052 N ILE A 86 -4.210 -1.608 7.983 1.00 11.02 N

ATOM 1053 CA ILE A 86 -5.362 -1.335 7.140 1.00 11.38 C

ATOM 1055 CB ILE A 86 -6.097 -2.629 6.670 1.00 11.19 C

ATOM 1057 CGl ILE A 86 -6.653 -3.440 7.837 1.00 12.03 C

ATOM 1060 CDl ILE A 86 -7.553 -4.554 7.393 1.00 12.44 C

ATOM 1064 CG2 ILE A 86 -5. 173 -3. 494 5. 836 1 . 00 10 . 30

ATOM 1068 C ILE A 86 -6.272 -0. 422 7 . 961 1 . 00 13 . 00 Table 2

ATOM 1069 O ILE A 86 -5.852 0.090 9.014 1.00 12.99 O

ATOM 1071 N GLD A 87 -7.482 -0.173 7.459 1.00 14.22 N

ATOM 1072 CA GLU A 87 -8.509 0.518 8.236 1.00 16.02 C

ATOM 1074 CB GLD A 87 -9.757 0.780 7.379 1.00 16.82 C

RTOM 1077 CG GLD A 87 -10.800 1.673 8.048 1.00 19.99 C

ATOM 1080 CD GLD A 87 -10.254 3.047 8.396 1.00 24.03 C

ATOM 1081 OEl GLO A 87 -9.535 3.633 7.554 1.00 25.51 0

ATOM 1082 OE2 GLD A 87 -10.538 3.542 9.511 1.00 28.38 O

ATOM 1083 C GLD A 87 -8.880 -0.310 9.476 1.00 17.60 C

ATOM 1084 O GLD A 87 -9.390 -1.439 9.361 1.00 19.03 O

ATOM 1086 N GLY A 88 -8.533 0.222 10.659 1.00 18.14 N

ATOM 1087 CA GLY A 88 -9.059 -0.382 11.904 1.00 18.97 C

ATOM 1090 C GLY A 88 -8.153 -1.403 12.565 1.00 18.27 C

ATOM 1091 O GLY A 88 -8.235 -1.582 13.768 1.00 19.83 0

ATOM 1093 N ASN A 89 -7.290 -2.065 '11.793 1.00 16.22 N

ATOM 1094 CA ASN A 89 -6.445 -3.159 12.297 1.00 15.92 C

ATOM 1096 CB ASN A 89 -7.148 -4.516 12.114 1.00 16.24 C

ATOM 1099 CG ASN A 89 -8.217 -4.771 13.156 1.00 18.10 C

ATOM 1100 ODl ASN A 89 -7.925 -5.018 14.333 1.00 19.94 O

ATOM 1101 ND2 ASN A 89 -9.463 -4.711 12.730 1.00 17.60 N

ATOM 1104 C ASN A 89 -5.063 -3.216 11.626 1.00 14.16 C

ATOM 1105 O ASN A 89 -4.811 -2.533 10.633 1.00 13.53 O

ATOM 1107 N VAL A 90 -4.184 -4.026 12.206 1.00 14.12 N

ATOM 1108 CA VAL A 90 -2.867 -4.343 11.653 1.00 13.34 C

ATOM 1110 CB VAL A 90 -1.764 -4.169 12.730 1.00 13.57 C

ATOM 1112 CGl VAL A 90 -0.403 -4.643 12.207 1.00 12.19 C

ATOM 1116 CG2 VAL A 90 -1.699 -2.703 13.172 1.00 14.27 C

ATOM 1120 C VAL A 90 -2.922 -5.800 11.228 1.00 13.68 C

ATOM 1121 O VAL A 90 -3.289 -6.670 12.020 1.00 15.10 O

ATOM 1123 N VAL A 91 -2.584 -6.065 9.968 1.00 13.28 N

ATOM 1124 CA VAL A 91 -2.738 -7.405 9.395 1.00 13.36 C

ATOM 1126 CB VAL A 91 -3.987 -7.469 8.490 1.00 13.78 C

ATOM 1128 CGl VAL A 91 -5.249 -7.013 9.258 1.00 14.97 C

ATOM 1132 CG2 VAL A 91 -3.780 -6.641 7.195 1.00 12.41 C

ATOM 1136 C VAL A 91 -1.527 -7.885 8.583 1.00 12.68 C

ATOM 1137 O VAL A 91 -0.629 -7.111 8.256 1.00 11.83 O

ATOM 1139 N ILE A 92 -1.510 -9.186 8.298 1.00 13.38 N

ATOM 1140 CA ILE A 92 -0.634 -9.786 7.284 1.00 13.28 C

ATOM 1142 CB ILE A 92 0.486 -10.696 7.854 1.00 14.02 C

ATOM 1144 CGl ILE A 92 1.249 -10.018 8.970 1.00 15.35 C

ATOM 1147 CDl ILE A 92 2.475 -10.795 9.433 1.00 16.40 C

ATOM 1151 CG2 ILE A 92 1.450 -11.108 6.743 1.00 14.01 C

ATOM 1155 C ILE A 92 -1.492 -10.706 6.413 1.00 13.36 C

ATOM 1156 O ILE A 92 -2.121 -11.621 6.938 1.00 14.06 O

ATOM 1158 N PRO A 93 -1.523 -10.460 5.087 1.00 12.58 N

ATOM 1159 CA PRO A 93 -2.157 -11.414 4.194 1.00 13.47 C

ATOM 1161 CB PRO A 93 -2.352 -10.608 2.905 1.00 12.92 C

ATOM 1164 CG PRO A 93 -1.239 -9.595 2.927 1.00 11.83 C

ATOM 1167 CD PRO A 93 -0.958 -9.306 4.364 1.00 11.44 C

ATOM 1170 C PRO A 93 -1.249 -12.608 3.933 1.00 14.19 C

ATOM 1171 O PRO A 93 -0.112 -12.423 3.502 1.00 13.37 O

ATOM 1172 N ARG A 94 -1.762 -13.813 4.180 1.00 15.65 N

ATOM 1173 CA ARG A 94 -1.009 -15.039 3.978 1.00 17.16 C

ATOM 1175 CB ARG A 94 -0.754 -15.700 5.332 1.00 18.35 C

ATOM 1178 CG ARG A 94 0.176 -14.910 6.272 1.00 16.87 C

ATOM 1181 CD ARG A 94 1.542 -14.627 5.653 1.00 16.60 C

ATOM 1184 NE ARG A 94 2.191 -15.839 5.163 1.00 18.36 N

ATOM 1186 CZ ARG A 94 3.175 -15.881 4.272 1.00 19.11 C

ATOM 1187 NHl ARG A 94 3.653 -14.770 3.735 1.00 17.85 N

ATOM 1190 NH2 ARG A 94 3.679 -17.058 3.903 1.00 21.63 N

ATOM 1193 C ARG A 94 -1.751 -16.011 3.068 1.00 18.61 C

ATOM 1194 O ARG A 94 -2.910 -16.341 3.321 1.00 19.57 O

ATOM 1196 N ILE A 95 -1.087 -16.454 2.002 1.00 19.17 N

ATOM 1197 CA ILE A 95 -1.627 -17.509 1.141 1.00 21.10 C

ATOM 1199 CB ILE A 95 -1.360 -17.236 -0.366 1.00 20.68 C

ATOM 1201 CGl ILE A 95 -2.152 -16.005 -0.807 1.00 19.06 C

ATOM 1204 CDl ILE A 95 -1.770 -15.469 -2.144 1.00 18.75 C

ATOM 1208 CG2 ILE A 95 -1.751 -18.465 -1.226 1.00 22.91 C Table 2

ATOM 1212 C ILE A 95 -1.055 -18.858 1.560 1.00 23.21 C

ATOM 1213 O ILE A 95 -1.815 -19.764 1.883 1.00 24.95 O

ATOM 1215 N HIS A 96 0.276 -18.968 1.575 1.00 23.74 N

ATOM 1216 CA HIS A 96 0.978 -20.193 1.984 1.00 26.18 C

ATOM 1218 CB HIS A 96 2.237 -20.410 1.141 1.00 26.99 C

ATOM 1221 CG HIS A 96 2.015 -20.218 -0.322 1.00 27.05 C

ATOM 1222 NDl HIS A 96 1.590 -21.234 -1.150 1.00 30.32 N

ATOM 1224 CEl HIS A 96 1.459 -20.767 -2.379 1.00 29.56 C

ATOM 1226 NE2 HIS A 96 1.795 -19.490 -2.380 1.00 26.76 N

ATOM 1228 CD2 HIS A 96 2.148 -19.124 -1.105 1.00 25.15 C

ATOM 1230 C HIS A 96 1.381 -20.140 3.459 1.00 26.26 C

ATOM 1231 O HIS A 96 1.848 -19.104 3.933 1.00 24.84 O

ATOM 1233 N PRO A 97 1.208 -21.254 4.188 1.00 28.44 N

ATOM 1234 CA PRO A 97 1.595 -21.280 5.591 1.00 29.10 C

ATOM 1236 CB PRO A 97 1.015 -22.600 6.092 1.00 31.61 C

ATOM 1239 CG PRO A 97 0.925 -23.447 4.910 1.00 32.95 C

ATOM 1242 CD PRO A 97 0.642 -22.543 3.756 1.00 31.03 C

ATOM 1245 C PRO A 97 3.112 -21.248 5.750 1.00 29.57 C

ATOM 1246 O PRO A 97 3.826 -21.991 5.089 1.00 30.96 O

ATOM 1247 N ASN A 98 3.583 -20.341 6.592 1.00 29.01 N

ATOM 1248 CA ASN A 98 4.999 -20.205 6.901 1.00 29.59 C

ATOM 1250 CB ASN A 98 5.599 -19.039 6.114 1.00 27.72 C

ATOM 1253 CG ASN A 98 7.097 -18.901 6.306 1.00 28.22 C

ATOM 1254 ODl ASN A 98 7.598 -18.928 7.431 1.00 29.33 O

ATOM 1255 ND2 ASN A 98 7.817 -18.721 5.209 1.00 28.32 N

ATOM 1258 C ASN A 98 5.095 -19.968 8.403 1.00 30.00 C

ATOM 1259 O ASN A 98 4.314 -19.185 8.958 1.00 28.45 O

ATOM 1261 N ALA A 99 6.044 -20.649 9.045 1.00 31.89 N

ATOM 1262 CA ALA A 99 6.170 -20.631 10.505 1.00 33.13 C

ATOM 1264 CB ALA A 99 7.185 -21.682 10.969 1.00 35.57 C

ATOM 1268 C ALA A 99 6.529 -19.258 11.078 1.00 31.58 C

ATOM 1269 O ALA A 99 6.151 -18.944 12.207 1.00 31.71 O

ATOM 1271 N ILE A 100 7.224 -18.442 10.289 1.00 30.95 N

ATOM 1272 CA ILE A 100 7.685 -17.121 10.735 1.00 29.60 C

ATOM 1274 CB ILE A 100 9.192 -16.949 10.462 1.00 30.21 C

ATOM 1276 CGl ILE A 100 9.505 -17.150 8.973 1.00 31.01 C

ATOM 1279 CDl ILE A 100 10.810 -16.541 8.542 1.00 31.09 C

ATOM 1283 CG2 ILE A 100 9.977 -17.950 11.292 1.00 33.33 C

ATOM 1287 C ILE A 100 6.909 -15.971 10.104 1.00 27.54 C

ATOM 1288 O ILE A 100 7.349 -14.822 10.184 1.00 26.62 O

ATOM 1290 N CYS A 101 5.760 -16.278 9.490 1.00 27.27 N

ATOM 1291 CA CYS A 101 4.863 -15.274 8.904 1.00 25.29 C

ATOM 1293 CB CYS A 101 4.916 -15.319 7.372 1.00 24.51 C

ATOM 1296 SG CYS A 101 6.568 -15.199 6.614 1.00 24.10 S

ATOM 1298 C CYS A 101 3.420 -15.490 9.387 1.00 25.74 C

ATOM 1299 O CYS A 101 2.657 -16.253 8.790 1.00 26.71 O

ATOM 1301 N ALA A 102 3.055 -14.803 10.469 1.00 25.19 N

ATOM 1302 CA ALA A 102 1.791 -15.025 11.183 1.00 25.89 C

ATOM 1304 CB ALA A 102 0.597 -14.626 10.318 1.00 25.03 C

ATOM 1308 C ALA A 102 1.642 -16.462 11.696 1.00 28.19 C

ATOM 1309 O ALA A 102 0.543 -17.003 11.739 1.00 28.95 O

ATOM 1311 N ALA A 103 2.762 -17.073 12.074 1.00 29.35 N

ATOM 1312 CA ALA A 103 2.759 -18.362 12.757 1.00 31.55 C

ATOM 1314 CB ALA A 103 2.307 -18.181 14.203 1.00 32.47 C

ATOM 1318 C ALA A 103 1.898 -19.403 12.048 1.00 32.65 C

ATOM 1319 O ALA A 103 0.970 -19.968 12.640 1.00 34.27 O

ATOM 1321 N ASN A 104 2.213 -19.635 10.772 1.00 31.78 N

ATOM 1322 CA ASN A 104 1.581 -20.679 9.964 1.00 32.95 C

ATOM 1324 CB ASN A 104 1.732 -22.050 10.651 1.00 35.91 C

ATOM 1327 CG ASN A 104 2.806 -22.898 10.031 1.00 37.38 C

ATOM 1328 ODl ASN A 104 3.164 -23.936 10.581 1.00 43.36 O

ATOM 1329 ND2 ASN A 104 3.312 -22.493 8.883 1.00 34.31 N

ATOM 1332 C ASN A 104 0.114 -20.448 9.568 1.00 32.08 C

ATOM 1333 O ASN A 104 -0.515 -21.338 9.003 1.00 33.52 O

ATOM 1335 N HIS A 105 -0.423 -19.259 9.833 1.00 30.01 N

ATOM 1336 CA HIS A 105 -1.815 -18.962 9.473 1.00 29.12 C

ATOM 1338 CB HIS A 105 -2.389 -17.823 10.328 1.00 28.57 C

ATOM 1341 CG HIS A 105 -2.763 -18.242 11.713 1.00 31.37 C Table 2

ATOM 1342 NDl HIS A 105 -3 970 -18.844 12.005 1.00 35.50 N

ATOM 1344 CEl HIS A 105 4.021 -19.117 13.297 1.00 36.76 C

ATOM 1346 NE2 HIS A 105 2.891 -18.717 13.851 1.00 35.35 N

ATOM 1348 CD2 HIS A 105 2.088 -18.169 12.883 1.00 32.41 C

ATOM 1350 C HIS A 105 1.925 -18.606 995 1.00 27.29 C

ATOM 1351 O HIS A 105 0.960 -18.140 372 1.00 25.58 O

ATOM 1353 N THR A 106 3.110 -18.853 447 1.00 27.01 N

ATOM 1354 CA THR A 106 3.467 -18.447 6.099 1.00 25.58 C

ATOM 1356 CB THR A 106 3.798 -19.662 5.187 1.00 27.28 C

ATOM 1358 OGl THR A 106 5.035 -20.261 5.590 1.00 27.49 O

ATOM 1360 CG2 THR A 106 2.688 -20.697 5.245 1.00 28.68 C

ATOM 1364 C THR A 106 4.678 -17.530 6.215 1.00 24.43 C

ATOM 1365 O THR A 106 5.380 -17.549 7.226 1.00 25.12 O

ATOM 1367 N GLY A 107 4.919 -16.727 5.184 1.00 22.59 N

ATOM 1368 CA GLY A 107 6.013 -15.774 5.201 1.00 21.65 C

ATOM 1371 C GLY A 107 -5 449 -14.439 5.619 1.00 19.58 C

ATOM 1372 O GLY A 107 4.233 -14.272 5.677 1.00 17.71 O

ATOM 1374 N VAL A 108 6.328 -13.483 5.891 1.00 18.99 N

ATOM 1375 CA VAL A 108 -5 886 -12.183 6.372 1.00 18.22 C

ATOM 1377 CB VAL A 108 6.355 -11.050 6.005 1.00 17.35 C

ATOM 1379 CGl VAL A 108 6.320 -9.699 6.524 1.00 16.11 C

ATOM 1383 CG2 VAL A 108 -7 058 -11.001 4.494 1.00 17.41 C

ATOM 1387 C VAL A 108 5.775 -12.298 7.873 1.00 19.17 C

ATOM 1388 O VAL A 108 6.789 -12.298 8.570 1.00 20.66 O

ATOM 1390 N TYR A 109 4.545 -12.433 8.362 1.00 19.29 N

ATOM 1391 CA TYR A 109 4.320 -12.618 9.786 1.00 20.33 C

ATOM 1393 CB TYR A 109 3.012 -13.358 10.074 1.00 21.56 C

ATOM 1396 CG TYR A 109 2.763 -13.527 11.562 1.00 22.80 C

ATOM 1397 CDl TYR A 109 3.332 -14.585 12.275 1.00 25.93 C

ATOM 1399 CEl TYR A 109 3.113 -14.728 13.647 1.00 27.33 C

ATOM 1401 CZ TYR A 109 2.318 -13.803 14.312 1.00 26.74 C

ATOM 1402 OH TYR A 109 084 -13.921 15.668 1.00 28.61 O

ATOM 1404 CE2 TYR A 109 746 -12.758 13.623 1.00 24.37 C

ATOM 1406 CD2 TYR A 109 969 -12.623 12.258 1.00 22.52 C

ATOM 1408 C TYR A 109 300 -11.258 10.464 1.00 19.21 C

ATOM 1409 O TYR A 109 549 -10.372 10.066 1.00 17.37 O

ATOM 1411 N ILE A 110 -5.112 -11.129 11.508 1.00 20.22 N

ATOM 1412 CA ILE A 110 -5.181 -9.914 12.294 1.00 19.83 C

ATOM 1414 CB ILE A 110 -6.613 -9.634 12.745 1.00 20.89 C

ATOM 1416 CGl ILE A 110 -7.550 -9.671 11.531 1.00 20.11 C

ATOM 1419 CDl ILE A 110 -9.034 -9.634 11.858 1.00 22.07 C

ATOM 1423 CG2 ILE A 110 -6.680 -8.266 13.465 1.00 20.81 C

ATOM 1427 C ILE A 110 -4.270 -10.011 13.521 1.00 20.25 C

ATOM 1428 O ILE A 110 -4.372 -10.961 14.301 1.00 22.13 O

ATOM 1430 N LEO A 111 -3.397 -9.015 13.687 1.00 18.79 N

ATOM 1431 CA LED A 111 -2.494 -8.944 14.841 1.00 19.42 C

ATOM 1433 CB LED A 111 -1.437 -7.856 14.634 1.00 18.15 C

ATOM 1436 CG LEO A 111 -0.488 -7.591 15.813 1.00 18.71 C

ATOM 1438 CDl LEO A 111 0.414 -8.783 16.063 1.00 19.72 C

ATOM 1442 CD2 LEO A 111 0.321 -6.358 15.542 1.00 17.83 C

ATOM 1446 C LEU A 111 -3.319 -8.651 16.095 1.00 21.03 C

ATOM 1447 O LEO A 111 -4.081 -7.669 16.148 1.00 21.27 O

ATOM 1449 N VAL A 112 -3. .178 -9.516 17.090 1.00 22.53 N

ATOM 1450 CA VAL A 112 -3..988 -9.447 18.295 1.00 24.20 C

ATOM 1452 CB VAL A 112 -4.419 -10.865 18.755 1.00 26.39 C

ATOM 1454 CGl VAL A 112 -5.173 -10.810 20.079 1.00 28.37 C

ATOM 1458 CG2 VAL A 112 -5.284 -11.521 17.682 1.00 26.70 C

ATOM 1452 C VAL A 112 -3.266 -8.734 19.438 1.00 24.56 C

ATOM 1463 O VAL A 112 -3.826 -7.836 20.057 1.00 25.46 O

ATOM 1465 N THR A 113 -2.035 -9.150 19.717 1.00 24.06 N

ATOM 1466 CA THR A 113 -1.308 -8.702 20.906 1.00 24.53 C

ATOM 1468 CB THR A 113 -1.153 -9.838 21.958 1.00 27.14 C

ATOM 1470 OGl THR A 113 -2.439 -10.266 22.433 1.00 29.36 O

ATOM 1472 CG2 THR A 113 -0.333 -9.368 23.151 1.00 28.76 C

ATOM 1476 C THR A 113 0.073 -8.182 20.509 1.00 22.53 C

ATOM 1477 O THR A 113 0.875 -8.918 19.932 1.00 21.43 O

ATOM 1479 N SER A 114 0.325 -6.909 20.808 1.00 21.51 N

ATOM 1480 CA SER A 114 1.634 -6.296 20.615 1.00 20.28 C Table 2

ATOM 1482 CB SER A 114 1.812 -5.871 19.154 00 18.29 C

ATOM 1485 OG SER A 114 3.049 -5.224 18.918 00 17.36 O

ATOM 1487 C SER A 114 1.787 -5.099 21.561 00 20.73 C

ATOM 1488 O SER A 114 0.818 -4.395 21.854 00 21.12 O

ATOM 1490 N ASN A 115 3.004 -4.901 22.061 00 20.81 N

ATOM 1491 CA ASN A 115 3.324 -3.752 22.906 00 21.53 C

ATOM 1493 CB ASN A 115 4.721 -3.901 23.545 00 22.38 C

ATOM 1496 CG ASN A 115 4.739 -4.771 24.787 00 24.18 C

ATOM 1497 ODl ASN A 115 3.704 — 5 091 25.367 00 24.91 O

ATOM 1498 ND2 ASN A 115 5.950 5.132 25.226 00 24.89 N

ATOM 1501 C ASN A 115 3.348 2.458 22.097 00 20.04 C

ATOM 1502 O ASN A 115 3.109 -1.391 22.633 00 20.65 O

ATOM 1504 N THR A 116 3.646 2.577 20.806 00 18.11 N

ATOM 1505 CA THR A 116 4.199 484 20.026 00 17.42 C

ATOM 1507 CB THR A 116 5.598 872 19.483 00 16.60 C

ATOM 1509 OGl THR A 116 5.506 095 18.744 00 15.87 O

ATOM 1511 CG2 THR A 116 6.578 048 20.618 00 18.34 C

ATOM 1515 C THR A 116 3.304 054 18.876 00 16.08 C

ATOM 1516 O THR A 116 2.424 1.792 18.455 00 15.81 O

ATOM 1518 N SER A 117 3.607 0.125 18.340 1.00 15.90 N

ATOM 1519 CA SER A 117 2. .694 0.907 17.526 00 15.09 C

ATOM 1521 CB SER A 117 2. .461 2.262 18.214 00 16.31 C

ATOM 1524 OG SER A 117 3.571 3.144 18.111 00 15.92 O

ATOM 1526 C SER A 117 3.139 1.151 16.087 00 14.07 C

ATOM 1527 O SER A 117 2.370 1.726 15.312 00 13.56 O

ATOM 1529 N HIS A 118 4.360 0.731 15.724 00 14.10 N

ATOM 1530 CA HIS A 118 4.920 030 14.395 00 12.92 C

ATOM 1532 CB HIS A 118 6.264 739 14.537 00 14.01 C

ATOM 1535 CG HIS A 118 6.135 186 14.902 00 15.43 C

ATOM 1536 NDl HIS A 118 6.947 169 14.381 00 16.23 N

ATOM 1538 CEl HIS A 118 6.598 340 14.882 00 16.98 C

ATOM 1540 NE2 HIS A 118 5.583 156 15.705 00 17.57 N

ATOM 1542 CD2 HIS A 118 5.274 816 15.733 00 16.60 C

ATOM 1544 C HIS A 118 5.039 0.204 13.513 00 12.34 C

ATOM 1545 O HIS A 118 5.602 1.223 13.927 00 13.21 O

ATOM 1547 N TYR A 119 4.452 0.134 12.316 00 10.99 N

ATOM 1548 CA TYR A 119 4.414 287 11.409 00 10.37 C

ATOM 1550 CB TYR A 119 3.056 006 11.527 00 10.05 C

ATOM 1553 CG TYR A 119 2.759 488 12.942 00 11.07 C

ATOM 1554 CDl TYR A 119 1.944 752 13.802 1.00 12.01 C

ATOM 1556 CEl TYR A 119 1.693 189 15.110 00 13.04 C

ATOM 1558 CZ TYR A 119 2.269 - 372 15.561 00 12.59 C

ATOM 1559 OH TYR A 119 2.039 -3 825 16.835 00 13.65 O

ATOM 1561 CE2 TYR A 119 3.077 -4.107 14.719 00 12.03 C

ATOM 1563 CD2 TYR A 119 3.322 -3 662 13.427 00 11.51 C

ATOM 1565 C TYR A 119 4.694 0.795 10.004 00 9.30 C

ATOM 1566 O TYR A 119 5.128 0.337 9.834 00 8.91 O

ATOM 1568 N ASP A 120 4.482 1.640 8.997 00 9.20 N

ATOM 1569 CA ASP A 120 4.416 1.160 7.610 00 8.53 C

ATOM 1571 CB ASP A 120 4.798 2.275 6.633 00 8.35 C

ATOM 1574 CG ASP A 120 6.242 2.732 6.784 00 8.43 C

ATOM 1575 ODl ASP A 120 7.089 1.987 7.348 00 9.74 O

ATOM 1576 OD2 ASP A 120 6.536 3.851 6.323 00 7.86 O

ATOM 1577 C ASP A 120 2.988 0.668 7.370 00 8.55 C

ATOM 1578 O ASP A 120 2.199 0.567 8.308 00 8.58 O

ATOM 1580 N THR A 121 2.643 0.332 6.130 00 8.09 N

ATOM 1581 CA THR A 121 1.243 0.069 5.812 00 7.67 C

ATOM 1583 CB THR A 121 0.909 1.456 5.753 00 8.07 C

ATOM 1585 OGl THR A 121 -0.511 1.636 5.778 00 6.95 O

ATOM 1587 CG2 THR A 121 1.488 2.110 4.519 00 9.16 C

ATOM 1591 C THR A 121 0.816 0.734 4.513 00 7.09 C

ATOM 1592 O THR A 121 1.634 -0.971 3.626 00 7.01 O

ATOM 1594 N TYR A 122 -0.476 -1 035 4.426 00 6.85 N

ATOM 1595 CA TYR A 122 -1 101 1 344 3.156 00 6.65 C

ATOM 1597 CB TYR A 122 2.052 2.530 3.317 00 6.62 C

ATOM 1600 CG TYR A 122 1.273 3.741 3.751 00 6.74 C

ATOM 1601 CDl TYR A 122 1.244 4.148 5.078 00 6.56 C

ATOM 1603 CEl TYR A 122 0.476 5.254 5.475 1.00 7.47 C Table 2

ATOM 1605 CZ TYR A 122 0.280 -5.936 4.535 1.00 7.39 C

ATOM 1606 OH TYR A 122 1.061 -7.025 4.874 1.00 7.63 O

ATOM 1608 CE2 TYR A 122 0.268 -5.528 3.219 1.00 7.74 C

ATOM 1610 CD2 TYR A 122 -0.491 -4.432 2.836 1.00 7.07 C

ATOM 1612 C TYR A 122 -1.810 -0.107 2.669 1.00 6.80 C

ATOM 1613 O TYR A 122 -2.211 0.734 3.468 1.00 6.83 O

ATOM 1615 N CYS A 123 -1.921 0.019 1.350 1.00 7.26 N

ATOM 1616 CA CYS A 123 -2.719 1.081 0.725 1.00 7.65 C

ATOM 1618 CB CYS A 123 -1.819 2.189 0.161 1.00 7.54 C

ATOM 1621 SG CYS A 123 -0.859 3.071 1.380 1.00 7.42 S

ATOM 1623 C CYS A 123 -3.593 0.506 -0.380 1.00 7.71 C

ATOM 1624 O CYS A 123 -3.332 -0.579 -0.894 1.00 7.77 O

ATOM 1626 N PHE A 124 -4.647 1.236 -0.727 1.00 8.78 N

ATOM 1627 CA PHE A 124 -5.587 0.787 -1.748 1.00 9.22 C

ATOM 1629 CB PHE A 124 -6.910 0.338 -1.135 1.00 9.54 C

ATOM 1632 CG PHE A 124 -7.997 0.161 -2.153 1.00 10.36 C

ATOM 1633 CDl PHE A 124 -7.915 -0.862 -3.030 1.00 11.08 C

ATOM 1635 CEl PHE A 124 -8.896 -1.036 -4.025 1.00 10.87 C

ATOM 1637 CZ PHE A 124 -9.968 -0.166 -4.074 1.00 11.10 C

ATOM 1639 CE2 PHE A 124 -10.061 0.868 -3.167 1.00 11.66 C

ATOM 1641 CD2 PHE A 124 -9.076 1.032 -2.212 1.00 11.03 C

ATOM 1643 C PHE A 124 -5.887 1.861 -2.778 1.00 9.76 C

ATOM 1644 O PHE A 124 -6.417 2.921 -2.438 1.00 9.82 O

ATOM 1646 N ASN A 125 -5.567 1.553 -4.036 1.00 10.37 N

ATOM 1647 CA ASN A 125 -5.824 2.438 -5.166 1.00 11.19 C

ATOM 1649 CB ASN A 125 -4.536 2.632 -5.968 1.00 11.42 C

ATOM 1652 CG ASN A 125 -4.716 3.575 -7.130 1.00 12.60 C

ATOM 1653 ODl ASN A 125 -5.808 4.075 -7.386 1.00 14.70 O

ATOM 1654 ND2 ASN A 125 -3.643 3.806 -7.855 1.00 15.77 N

ATOM 1657 C ASN A 125 -6.949 1.890 -6.075 1.00 11.85 C

ATOM 1658 O ASN A 125 -6.744 0.960 -6.857 1.00 11.66 O

ATOM 1660 N ALA A 126 -8.125 2.501 -5.975 1.00 12.90 N

ATOM 1661 CA ALA A 126 -9.301 2.079 -6.749 1.00 14.10 C

ATOM 1663 CB ALA A 126 -10.500 2.939 -6.386 1.00 15.15 C

ATOM 1667 C ALA A 126 -9.074 2.091 -8.268 1.00 14.74 C

ATOM 1668 O ALA A 126 -9.745 1.362 -8.995 1.00 16.11 O

ATOM 1670 N SER A 127 -8.127 2.907 -8.732 1.00 14.87 N

ATOM 1671 CA SER A 127 -7.838 3.071 -10.160 1.00 15.60 C

ATOM 1673 CB SER A 127 -7.260 4.472 -10.421 1.00 16.15 C

ATOM 1676 OG SER A 127 -8.243 5.454 -10.135 1.00 18.42 O

ATOM 1678 C SER A 127 -6.912 2.023 -10.744 1.00 15.30 C

ATOM 1679 O SER A 127 -6.694 2.010 -11.952 1.00 16.97 O

ATOM 1681 N ALA A 128 -6.361 1.142 -9.920 1.00 14.10 N

ATOM 1682 CA ALA A 128 -5.477 0.085 -10.434 1.00 14.32 C

ATOM 1684 CB ALA A 128 -4.657 -0.528 -9.287 1.00 13.29 C

ATOM 1688 C ALA A 128 -6.247 -1.006 -11.200 1.00 14.88 C

ATOM 1689 O ALA A 128 -7.460 -1.085 -11.125 1.00 15.29 O

ATOM 1691 N PRO A 129 -5.535 -1.843 -11.964 1.00 15.93 N

ATOM 1692 CA PRO A 129 -6.190 -3.023 -12.556 1.00 16.88 C

ATOM 1694 CB PRO A 129 -5.038 -3.739 -13.279 1.00 17.40 C

ATOM 1697 CG PRO A 129 -4.043 -2.667 -13.564 1.00 17.97 C

ATOM 1700 CD PRO A 129 -4.122 -1.734 -12.378 1.00 15.94 C

ATOM 1703 C PRO A 129 -6.812 -3.947 -11.506 1.00 16.25 C

ATOM 1704 O PRO A 129 -6.413 -3.905 -10.351 1.00 15.02 O

ATOM 1705 N PRO A 130 -7.768 -4.799 -11.913 1.00 17.83 N

ATOM 1706 CA PRO A 130 -8.488 -5.649 -10.959 1.00 18.10 C

ATOM 1708 CB PRO A 130 -9.665 -6.189 -11.784 1.00 19.64 C

ATOM 1711 CG PRO A 130 -9.175 -6.177 -13.205 1.00 20.42 C

ATOM 1714 CD PRO A 130 -8.231 -5.008 -13.301 1.00 19.34 C

ATOM 1717 C PRO A 130 -7.670 -6.801 -10.382 1.00 18.13 C

ATOM 1718 O PRO A 130 -8.014 -7.295 -9.308 1.00 18.37 O

ATOM 1719 N GLU A 131 -6.616 -7.227 -11.080 1.00 18.61 N

ATOM 1720 CA GLO R 131 -5.807 -8.374 -10.652 1.00 19.14 C

ATOM 1722 CB GLU R 131 -5.763 -9.445 -11.765 1.00 21.86 C

ATOM 1725 CG GLO R 131 -7.014 -9.540 -12.683 1.00 26.23 C

ATOM 1728 CD GLU A 131 -8.297 -10.028 -12.013 1.00 30.42 C

ATOM 1729 OEl GLO A 131 -9.386 -9.814 -12.599 1.00 34.83 O

ATOM 1730 OE2 GLU A 131 -8.235 -10.655 -10.936 1.00 32.85 O Table 2

ATOM 1731 C GLU A 131 4.389 -7.910 -10.223 1.00 17.92 C

ATOM 1732 O GLU A 131 4.264 -6.896 -9.532 1.00 17.31 O

ATOM 1734 N GLU A 132 3.337 -8.645 -10.597 1.00 18.21 N

ATOM 1735 CA GLU A 132 1.956 -8.253 -10.306 1.00 17.46 C

ATOM 1737 CB GLU A 132 1.024 -9.450 -10.468 1.00 18.84 C

ATOM 1740 CG GLU A 132 0.425 -9.181 -10.076 1.00 18.86 C

ATOM 1743 CD GLU A 132 1.263 -10.433 -10.159 1.00 21.00 C

ATOM 1744 OEl GLU A 132 1.813 -10.873 -9.125 1.00 23.07 O

ATOM 1745 OE2 GLU A 132 1.363 -10.986 -11.264 1.00 23.71 O

ATOM 1746 C GLU A 132 1.452 -7.139 -11.219 1.00 17.08 C

ATOM 1747 O GLU A 132 1.585 -7.234 -12.443 1.00 18.61 O

ATOM 1749 N ASP A 133 0.868 -6.102 -10.623 1.00 15.02 N

ATOM 1750 CA ASP A 133 0.180 -5.047 -11.370 1.00 15.18 C

ATOM 1752 CB ASP A 133 0.978 -3.736 -11.338 1.00 14.20 C

ATOM 1755 CG ASP A 133 0.343 -2.631 -12.180 1.00 14.42 C

ATOM 1756 ODl ASP A 133 0.584 -2.891 -12.961 1.00 14.41 O

ATOM 1757 OD2 ASP A 133 0.778 -1.476 -12.050 1.00 15.63 O

ATOM 1758 C ASP A 133 1.227 -4.843 -10.794 1.00 14.49 C

ATOM 1759 O ASP A 133 1.399 -4.238 -9.741 1.00 12.40 O

ATOM 1761 N CYS A 134 2.218 -5.362 -11.517 1.00 16.28 N

ATOM 1762 CA CYS A 134 3.621 -5.272 -11.139 1.00 16.82 C

ATOM 1764 CB CYS A 134 4.296 -6.639 -11.295 1.00 18.06 C

ATOM 1767 SG CYS A 134 3.790 -7.831 -10.065 1.00 18.23 S

ATOM 1769 C CYS A 134 4.364 -4.233 -11.962 1.00 17.78 C

ATOM 1770 O CYS A 134 5.593 -4.243 -11.993 1.00 18.57 O

ATOM 1772 N THR A 135 3.639 -3.343 -12.640 1.00 18.18 N

ATOM 1773 CA THR A 135 4.302 -2.216 -13.287 1.00 19.32 C

ATOM 1775 CB THR A 135 3.413 -1.433 -14.270 1.00 19.56 C

ATOM 1777 OGl THR R 135 2.252 -0.929 -13.599 1.00 17.83 O

ATOM 1779 CG2 THR R 135 3.009 -2.321 -15.450 1.00 21.05 C

ATOM 1783 C THR R 135 4.842 -1.293 -12.198 1.00 18.87 C

ATOM 1784 O THR A 135 4.365 -1.305 -11.063 1.00 17.66 O

ATOM 1786 N SER A 136 5.861 -0.524 -12.540 1.00 20.34 N

ATOM 1787 CA SER A 136 6.487 0.350 -11.575 1.00 20.36 C

ATOM 1789 CB SER A 136 7.821 0.858 -12.099 1.00 22.48 C

ATOM 1792 OG SER A 136 8.747 -0.216 -12.124 1.00 24.92 O

ATOM 1794 C SER A 136 5.576 1.505 -11.203 1.00 19.86 C

ATOM 1795 O SER A 136 4.837 2.031 -12.040 1.00 20.17 O

ATOM 1797 N VAL A 137 5.624 1.851 -9.918 1.00 19.05 N

ATOM 1798 CA VAL A 137 5.027 3.067 -9.391 1.00 18.88 C

ATOM 1800 CB VAL A 137 4.736 2.930 -7.881 1.00 17.41 C

ATOM 1802 CGl VAL A 137 4.139 4.218 -7.306 1.00 16.60 C

ATOM 1806 CG2 VAL A 137 3.800 1.747 -7.636 1.00 16.41 C

ATOM 1810 C VAL A 137 6.019 4.202 -9.664 1.00 20.50 C

ATOM 1811 O VAL A 137 7.206 4.105 -9.329 1.00 20.40 O

ATOM 1813 N THR A 138 5.511 5.256 -10.301 1.00 21.90 N

ATOM 1814 CA THR A 138 6.320 6.338 -10.840 1.00 23.91 C

ATOM 1816 CB THR A 138 6.041 6.540 -12.359 1.00 25.75 C

ATOM 1818 OGl THR A 138 4.687 7.004 -12.546 1.00 26.21 O

ATOM 1820 CG2 THR A 138 6.257 5.250 -13.138 1.00 26.26 C

ATOM 1824 C THR A 138 6.063 7.689 -10.167 1.00 24.23 C

ATOM 1825 O THR A 138 6.642 8.689 -10.575 1.00 25.49 O

ATOM 1827 N ASP A 139 5.179 7.734 -9.174 1.00 23.29 N

ATOM 1828 CA ASP A 139 4.851 9.004 -8.528 1.00 23.77 C

ATOM 1830 CB ASP A 139 3.962 9.886 -9.437 1.00 24.95 C

ATOM 1833 CG ASP A 139 3.912 11.381 -8.992 1.00 26.43 C

ATOM 1834 ODl ASP A 139 4.765 11.848 -8.203 1.00 25.48 O

ATOM 1835 OD2 ASP A 139 2.992 12.095 -9.452 1.00 28.93 O

ATOM 1836 C ASP A 139 4.180 8.802 -7.187 1.00 22.36 C

ATOM 1837 O ASP A 139 3.681 7.717 -6.870 1.00 21.62 O

ATOM 1839 N LEU A 140 4.257 9.862 -6.391 1.00 22.84 N

ATOM 1840 CA LEU A 140 3.515 10.033 -5.167 1.00 21.63 C

ATOM 1842 CB LEU A 140 4.518 10.295 -4.037 1.00 22.12 C

ATOM 1845 CG LEU A 140 4.120 10.074 -2.583 1.00 21.98 C

ATOM 1847 CDl LEU A 140 3.830 8.622 -2.301 1.00 20.44 C

ATOM 1851 CD2 LEU A 140 5.222 10.566 -1.660 1.00 22.90 C

ATOM 1855 C LEU A 140 2.627 11.245 -5.498 1.00 22.33

ATOM 1856 O LEU A 140 2.980 12.383 -5.184 1.00 23.77 Table 2

ATOM 1B58 N PRO A 141 1.503 11.010 6.220 ,00 21.32 N

ATOM 1859 CA PRO A 141 0.728 12.086 6.855 .00 21.79 C

ATOM 1861 CB PRO A 141 -0.412 11.338 -7 559 .00 21.42 C

ATOM 1864 CG PRO A 141 -0.486 10.024 6.898 .00 19.84 C

ATOM 1867 CD PRO A 141 0.900 9.692 6.491 .00 19.95 C

ATOM 1870 C PRO A 141 0.153 13.180 5.951 .00 22.10 C

ATOM 1871 O PRO A 141 0.070 14.341 6.381 .00 23.28 O

ATOM 1872 N AASN A 142 -0.256 12.825 4.730 0.50 20.61 N

ATOM 1873 N BASN A 142 -0.218 12.820 4.725 0.50 20.77 N

ATOM 1874 CA AASN A 142 -0.826 13.799 3.793 0.50 21.38 C

ATOM 1875 CA BASN A 142 -0.817 13.771 805 0.50 21.59 C

ATOM 1878 CB AASN A 142 -2.035 13.211 058 0.50 20.33 C

ATOM 1879 CB BASN A 142 -2.063 13.153 162 0.50 20.81 C

ATOM 1884 CG AASN A 142 -3.211 12.933 972 0.50 20.03 C

ATOM 1885 CG BASN A 142 -3.092 14.187 -2.755 0.50 22.90 C

ATOM 1886 ODlAASN A 142 -4.114 12.181 -3.603 0.50 18.30 O

ATOM 1887 ODlBASN A 142 -3.807 14.008 -1.767 0.50 23.68 O

ATOM 1888 ND2AASN A 142 -3.215 13.540 -5.158 0.50 20.26 N

ATOM 1889 ND2BASN A 142 -3.184 15.275 -3.522 0.50 25.49 N

ATOM 1894 C AASN A 142 0.167 14.338 -2.759 0.50 21.73 C

ATOM 1895 C BASN A 142 0.159 14.272 -2.732 0.50 21.80 C

ATOM 1896 O AASN A 142 -0.246 14.953 -1.778 0.50 22.49 O

ATOM 1897 O BASN A 142 -0.269 14.735 -1.702 0.50 22.42 O

ATOM 1900 N SER A 143 1.465 14.131 -2.975 .00 21.38 N

ATOM 1901 CA SER A 143 2.471 14.677 -2.058 .00 21.96 C

ATOM 1903 CB SER A 143 3.855 14.078 -2.311 .00 21.57 C

ATOM 1906 OG SER A 143 4.440 14.572 -3.496 .00 23.05 O

ATOM 1908 C SER A 143 2.477 16.197 -2.224 .00 23.70 C

ATOM 1909 O SER A 143 2.168 16.708 -3.312 .00 24.21 O

ATOM 1911 N PHE A 144 2.790 16.911 -1.146 .00 24.62 N

ATOM 1912 CA PHE A 144 2.782 18.375 -1.162 .00 26.89 C

ATOM 1914 CB PHE A 144 1.832 18.963 -0.096 .00 28.36 C

ATOM 1917 CG PHE A 144 2.006 18.405 1.288 .00 27.45 C

ATOM 1918 CDl PHE A 144 2.892 18.988 2.184 00 29.74 C

ATOM 1920 CEl PHE A 144 3.026 18.485 3.472 .00 29.39 C

ATOM 1922 CZ PHE A 144 2.257 17.389 3.874 .00 27.09 C

ATOM 1924 CE2 PHE A 144 1.363 16.827 2.996 .00 25.47 C

ATOM 1926 CD2 PHE A 144 1.231 17.338 1.717 .00 25.63 C

ATOM 1928 C PHE A 144 4.183 18.961 -1 044 .00 28.01 C

ATOM 1929 O PHE A 144 5.168 18.239 ^■0.887 .00 26.82 O

ATOM 1931 N ASP A 145 4.269 20.281 ^■1.162 .00 30.10 N

ATOM 1932 CA ASP A 145 5.549 20.972 ^•1.114 .00 32.00 C

ATOM 1934 CB ASP A 145 5.338 22.483 ^•1.218 .00 34.88 C

ATOM 1937 CG ASP A 145 6.644 23.245 ^■1.334 .00 37.42 C

ATOM 1938 ODl ASP A 145 7.258 23.524 ^■0.288 .00 37.11 O

ATOM 1939 OD2 ASP A 145 7.044 23.578 ^■2.467 1.00 37.62 O

ATOM 1940 C ASP A 145 6.286 20.610 0.175 1.00 31.30 C

ATOM 1941 O ASP A 145 5. ,674 20.510 1.234 ,00 30.67 O

ATOM 1943 N GLY A 146 7..594 20.402 0.080 ,00 31.50 N

ATOM 1944 CA GLY A 146 8.373 19.997 1.241 ,00 31.75 C

ATOM 1947 C GLY A 146 9.846 19.811 0.935 ,00 32.56 C

ATOM 1948 O GLY A 146 10.240 19.852 ^•0.225 ,00 32.74 O

ATOM 1950 N PRO A 147 10.668 19.598 977 ,00 33.36 N

ATOM 1951 CA PRO A 147 12.125 19.560 839 ,00 35.02 C

ATOM 1953 CB PRO A 147 12.594 20.084 197 ,00 36.68 C

ATOM 1956 CG PRO A 147 11.565 19.545 164 ,00 34.66 C

ATOM 1959 CD PRO A 147 10.262 19.378 380 ,00 32.96 C

ATOM 1962 C PRO A 147 12.697 18.150 606 00 33.27 C

ATOM 1963 O PRO A 147 13.881 18.014 294 00 34.86 O

ATOM 1964 N VAL A 148 11.873 17.117 737 00 30.72 N

ATOM 1965 CA VAL A 148 12.375 15.738 730 00 28.79 C

ATOM 1967 CB VAL A 148 11.432 14.785 510 00 26.16 C

ATOM 1969 CGl VAL A 148 12.080 13.394 2.701 00 25.21 C

ATOM 1973 CG2 VAL A 148 11.015 15.404 3.850 00 27.27 C

ATOM 1977 C VAL A 148 12.524 15.215 0.299 00 28.31 C

ATOM 1978 O VAL A 148 11.631 15.407 -0.517 00 27.60 O

ATOM 1980 N THR A 149 13.654 14.561 0.010 00 28.59 N

ATOM 1981 CA THR A 149 13.784 13.738 -1.188 1.00 27.89 C Table 2

ATOM 1983 CB THR A 149 15.264 13.482 -1.593 1.00 29.78 C

ATOM 1985 OGl THR A 149 15.922 14.721 -1.856 1.00 32.84 O

ATOM 1987 CG2 THR A 149 15.351 12.607 -2.845 1.00 29.05 C

ATOM 1991 C THR A 149 13.095 12.409 -0.906 1.00 25.33 C

ATOM 1992 O THR A 149 13.563 11.622 -0.071 1.00 24.92 O

ATOM 1994 N ILE A 150 11.971 12.183 -1.584 1.00 23.65 N

ATOM 1995 CA ILE A 150 11.171 10.983 -1.411 1.00 21.21 C

ATOM 1997 CB ILE A 150 9.666 11.310 -1.276 1.00 20.14 C

ATOM 1999 CGl ILE A 150 9.414 12.192 -0.049 1.00 21.12 C

ATOM 2002 CDl ILE A 150 8.075 12.922 -0.084 1.00 21.00 C

ATOM 2006 CG2 ILE A 150 8.850 10.028 -1.177 1.00 18.45 C

ATOM 2010 C ILE A 150 11.377 10.087 -2.626 1.00 20.55 C

ATOM 2011 O ILE A 150 11.144 10.503 -3.743 1.00 21.19 O

ATOM 2013 N THR A 151 11.808 8.852 -2.398 1.00 19.42 N

ATOM 2014 CA THR A 151 12.137 7.957 -3.488 1.00 19.07 C

ATOM 2016 CB THR A 151 13.625 7.532 -3.449 1.00 20.73 C

ATOM 2018 OGl THR A 151 14.454 8.703 -3.406 1.00 23.32 O

ATOM 2020 CG2 THR A 151 13.984 6.698 -4.679 1.00 21.28 C

ATOM 2024 C THR A 151 11.254 6.734 -3.416 1.00 16.60 C

ATOM 2025 O THR A 151 11.238 6.039 -2.409 1.00 15.27 O

ATOM 2027 N AILE A 152 10.490 6.496 -4.476 0.50 15.94 N

ATOM 2028 N BILE A 152 10.530 6.480 -4.501 0.50 16.12 N

ATOM 2029 CA AILE A 152 9.718 5.274 -4.596 0.50 14.43 C

ATOM 2030 CA BILE A 152 9.707 5.294 -4.618 0.50 14.62 C

ATOM 2033 CB AILE A 152 8.485 5.441 -5.513 0.50 13.97 C

ATOM 2034 CB BILE A 152 8.476 5.495 -5.560 0.50 14.33 C

ATOM 2037 CGlAILE A 152 7.402 6.245 -4.792 0.50 13.37 C

ATOM 2038 CGlBILE A 152 7.776 6.851 -5.330 0.50 14.94 C

ATOM 2043 CDlAILE A 152 6.591 7.121 -5.710 0.50 13.44 C

ATOM 2044 CDlBILE A 152 7.134 7.013 -3.957 0.50 14.37 C

ATOM 2051 CG2AILE A 152 7.931 4.080 -5.939 0.50 13.08 C

ATOM 2052 CG2BILE A 152 7.492 4.349 -5.390 0.50 12.84 C

ATOM 2059 C AILE A 152 10.649 4.225 -5.168 0.50 14.76 C

ATOM 2060 C BILE A 152 10.609 4.208 -5.193 0.50 14.84 C

ATOM 2061 O AILE A 152 11.252 4.433 -6.223 0.50 15.96 O

ATOM 2062 O BILE A 152 11.160 4.375 -6.284 0.50 16.00 O

ATOM 2065 N VAL A 153 10.761 3.108 -4.461 1.00 13.69 N

ATOM 2066 CA VAL A 153 11.602 1.995 -4.881 1.00 14.63 C

ATOM 2068 CB VAL A 153 12.653 1.615 -3.787 1.00 14.90 C

ATOM 2070 CGl VAL A 153 13.624 0.577 -4.316 1.00 15.64 C

ATOM 2074 CG2 VAL A 153 13.402 2.872 -3.297 1.00 16.58 C

ATOM 2078 C VAL A 153 10.723 0.792 -5.187 1.00 13.09 C

ATOM 2079 O VAL A 153 10.028 0.289 -4.313 1.00 11.06 O

ATOM 2081 N ASN A 154 10.764 0.344 -6.436 1.00 13.89 N

ATOM 2082 CA ASN A 154 10.024 -0.837 -6.866 1.00 13.75 C

ATOM 2084 CB ASN A 154 9.605 -0.671 -8.330 1.00 13.84 C

ATOM 2087 CG ASN A 154 8.628 0.490 -8.532 1.00 13.77 C

ATOM 2088 ODl ASN A 154 7.416 0.362 -8.285 1.00 10.79 O

ATOM 2089 ND2 ASN A 154 9.153 1.635 -8.965 1.00 13.79 N

ATOM 2092 C ASN A 154 10.876 -2.099 -6.675 1.00 14.86 C

ATOM 2093 O ASN A 154 12.113 -2.030 -6.611 1.00 16.58 O

ATOM 2095 N ARG A 155 10.230 -3.253 -6.595 1.00 14.90 N

ATOM 2096 CA ARG A 155 10.952 -4.511 -6.340 1.00 16.50 C

ATOM 2098 CB ARG A 155 9.967 -5.681 -6.210 1.00 16.89 C

ATOM 2101 CG ARG A 155 10.516 -6.867 -5.430 1.00 18.06 C

ATOM 2104 CD ARG A 155 9.477 -7.975 -5.205 1.00 20.31 C

ATOM 2107 NE ARG A 155 10.136 -9.213 -4.762 1.00 25.72 N

ATOM 2109 CZ ARG A 155 9.585 -10.430 -4.759 1.00 28.81 C

ATOM 2110 NHl ARG A 155 8.335 -10.626 -5.186 1.00 29.87 N

ATOM 2113 NH2 ARG A 155 10.303 -11.469 -4.327 1.00 30.64 N

ATOM 2116 C ARG A 155 12.042 -4.825 -7.382 1.00 18.06 C

ATOM 2117 O ARG A 155 13.056 -5.453 -7.047 1.00 18.31 O

ATOM 2119 N ASP A 156 11.831 -4.384 -8.630 1.00 17.93 N

ATOM 2120 CA ASP A 156 12.797 -4.562 -9.728 1.00 20.34 C

ATOM 2122 CB ASP A 156 12.090 -4.548 -11.102 1.00 20.46 C

ATOM 2125 CG ASP A 156 11.485 -3.195 -11.459 1.00 19.76 C

ATOM 2126 ODl ASP A 156 11.652 -2.211 -10.707 1.00 18.33 O

ATOM 2127 OD2 ASP A 156 10.810 -3.122 -12.507 1.00 20.49 O Table 2

ATOM 2128 C ASP A 156 13.916 -3.520 -9.721 1.00 21.30 C

ATOM 2129 O ASP A 156 14.781 -3.526 -10.600 1.00 23.10 O

ATOM 2131 N GLY A 157 13.866 -2.619 -8.740 1.00 20.24 N

ATOM 2132 CA GLY A 157 14.907 -1.649 -8.505 1.00 21.48 C

ATOM 2135 C GLY A 157 14.659 -0.313 -9.163 1.00 21.67 C

ATOM 2136 O GLY A 157 15.400 0.627 -8.924 1.00 22.49 O

ATOM 2138 N ATHR A 158 13.631 -0.215 -10.001 0.50 21.19 N

ATOM 2139 N BTHR A 158 13.615 -0.227 -9.984 0.50 21.54 N

ATOM 2140 CA ATHR A 158 13.344 1.052 -10.654 0.50 21.79 C

ATOM 2141 CA BTHR A 158 13.251 1.025 -10.634 0.50 22.10 C

ATOM 2144 CB ATHR A 158 12.279 0.938 -11.755 0.50 21.20 C

ATOM 2145 CB BTHR A 158 12.046 0.846 -11.580 0.50 21.46 C

ATOM 2148 OGlATHR A 158 11.102 0.316 -11.235 0.50 17.69 O

ATOM 2149 OGlBTHR A 158 12.413 -0.033 -12.647 0.50 24.09 O

ATOM 2152 CG2ATHR A 158 12.815 0.131 -12.929 0.50 23.49 C

ATOM 2153 CG2BTHR A 158 11.618 2.181 -12.177 0.50 22.07 C

ATOM 2160 C ATHR A 158 12.917 2.066 -9.613 0.50 20.62 C

ATOM 2161 C BTHR A 158 12.922 2.062 -9.577 0.50 20.88 C

ATOM 2162 O ATHR A 158 12.104 1.770 -8.736 0.50 18.51 O

ATOM 2163 O BTHR A 158 12.171 1.776 -8.643 0.50 18.81 O

ATOM 2166 N ARG A 159 13.485 3.259 -9.731 1.00 22.33 N

ATOM 2167 CA ARG A 159 13.316 4.328 -8.761 1.00 22.41 C

ATOM 2169 CB ARG A 159 14.671 4.685 -8.144 1.00 23.94 C

ATOM 2172 CG ARG A 159 15.049 3.794 -7.015 1.00 23.84 C

ATOM 2175 CD ARG A 159 16.466 4.040 -6.600 1.00 25.98 C

ATOM 2178 NE ARG A 159 16.705 3.454 -5.296 1.00 25.79 N

ATOM 2180 CZ ARG A 159 17.021 2.185 -5.074 1.00 26.75 C

ATOM 2181 NHl ARG A 159 17.178 1.313 -6.085 1.00 28.30 N

ATOM 2184 NH2 ARG A 159 17.202 1.792 -3.819 1.00 25.55 N

ATOM 2187 C ARG A 159 12.730 5.589 -9.350 1.00 23.38 C

ATOM 2188 O ARG A 159 13.056 5.972 -10.475 1.00 25.03 O

ATOM 2190 N ATYR A 160 11.834 6.221 -3.593 0.50 22.40 N

ATOM 2191 N BTYR A 160 11.908 6.256 -8.546 0.50 22.50 N

ATOM 2192 CA ATYR A 160 11.330 7.559 -8.918 0.50 23.04 C

ATOM 2193 CA BTYR A 160 11.336 7.547 -8.898 0.50 23.16 C

ATOM 2196 CB ATYR A 160 9.868 7.517 -9.383 0.50 22.01 C

ATOM 2197 CB BTYR A 160 9.890 7.366 -9.347 0.50 22.27 C

ATOM 2202 CG ATYR A 160 9.216 8.892 -9.401 0.50 22.52 C

ATOM 2203 CG BTYR A 160 9.758 6.913 -10.774 0.50 23.25 C

ATOM 2204 CDlATYR A 160 9.332 9.725 -10.511 0.50 24.71 C

ATOM 2205 CDlBTYR A 160 9.705 5.564 -11.093 0.50 22.71 C

ATOM 2208 CElATYR A 160 8.748 10.987 -10.528 0.50 25.28 C

ATOM 2209 CElBTYR A 160 9.580 5.149 -12.396 0.50 23.86 C

ATOM 2212 CZ ATYR A 160 8.043 11.430 -9.426 0.50 24.06 C

ATOM 2213 CZ BTYR A 160 9.511 6.085 -13.404 0.50 25.66 C

ATOM 2214 OH ATYR A 160 7.467 12.674 -9.442 0.50 24.62 O

ATOM 2215 OH BTYR A 160 9.374 5.675 -14.705 0.50 26.91 O

ATOM 2218 CE2ATYR A 160 7.922 10.627 -8.305 0.50 22.02 C

ATOM 2219 CE2BTYR A 160 9.567 7.432 -13.119 0.50 26.07 C

ATOM 2222 CD2ATYR A 160 8.504 9.365 -8.298 0.50 21.52 C

ATOM 2223 CD2BTYR A 160 9.683 7.839 -11.811 0.50 24.99 C

ATOM 2226 C ATYR A 160 11.454 8.449 -7.686 0.50 22.98 C

ATOM 2227 C BTYR A 160 11.406 8.476 -7.693 0.50 23.05 C

ATOM 2228 O ATYR A 160 10.967 8.096 -6.613 0.50 21.24 O

ATOM 2229 O BTYR A 160 10.842 8.172 -6.642 0.50 21.34 O

ATOM 2232 N SER A 161 12.102 9.600 -7.857 1.00 24.98 N

ATOM 2233 CA SER A 161 12.326 10.560 -6.774 1.00 25.52 C

ATOM 2235 CB SER A 161 13.827 10.812 -6.615 1.00 27.79 C

ATOM 2238 OG SER A 161 14.487 9.627 -6.218 1.00 28.69 O

ATOM 2240 C SER A 161 11.642 11.911 -7.014 1.00 26.33 C

ATOM 2241 O SER A 161 11.497 12.370 -8.161 1.00 27.09 O

ATOM 2243 N LYS A 162 11.250 12.543 -5.911 1.00 25.56 N

ATOM 2244 CA LYS A 162 10.725 13.900 -5.918 1.00 26.73 C

ATOM 2246 CB LYS A 162 9.207 13.908 -6.183 1.00 25.21 C

ATOM 2249 CG LYS A 162 3.325 13.628 -4.983 1.00 23.34 C

ATOM 2252 CD LYS A 162 6.889 13.262 -5.386 1.00 22.75 C

ATOM 2255 CE LYS A 162 6.175 14.399 -6.117 1.00 24.12 C

ATOM 2258 NZ LYS A 162 4.703 14.148 -6.320 1.00 22.25 N Table 2

ATOM 2262 C LYS A 162 11.038 14.541 -4.578 1.00 27.07 C

ATOM 2263 O LYS A 162 11.198 13.839 -3.576 1.00 25.28 O

ATOM 2265 N LYS A 163 11.148 15.870 -4.581 1.00 29.49 N

ATOM 2266 CA LYS A 163 11.229 16.656 -3.358 1.00 30.57 C

ATOM 2268 CB LYS A 163 11.993 17.959 -3.589 1.00 33.95 C

ATOM 2271 CG LYS A 163 12.334 18.701 -2.295 1.00 35.43 C

ATOM 2274 CD LYS A 163 13.243 19.899 -2.522 1.00 39.63 C

ATOM 2277 CE LYS A 163 12.632 21.189 -1.977 1.00 42.45 C

ATOM 2280 NZ LYS A 163 11.368 21.540 -2.705 1.00 42.12 N

ATOM 2284 C LYS A 163 9.807 16.960 -2.894 1.00 29.68 C

ATOM 2285 O LYS A 163 8.956 17.376 -3.694 1.00 29.56 O

ATOM 2287 N GLY A 164 9.536 16.738 -1.611 1.00 28.58 N

ATOM 2288 CA GLY A 164 8.227 17.086 -1.067 1.00 28.02 C

ATOM 2291 C GLY A 164 8.016 16.676 0.372 1.00 26.99 C

ATOM 2292 O GLY A 164 8.973 16.550 1.141 1.00 27.36 O

ATOM 2294 N GLU A 165 6.747 16.487 0.721 1.00 25.67 N

ATOM 2295 CA GLD A 165 6.347 16.020 2.035 1.00 24.89 C

ATOM 2297 CB GLϋ A 165 6.323 17.193 3.027 1.00 26.99 C

ATOM 2300 CG GLO A 165 5.998 16.812 4.457 1.00 26.50 C

ATOM 2303 CD GLO A 165 6.929 15.746 4.986 1.00 25.71 C

ATOM 2304 OEl GLO A 165 8.019 16.104 5.453 1.00 29.11 O

ATOM 2305 OE2 GLO A 165 6.580 14.549 4.930 1.00 22.88 O

ATOM 2306 C GLO A 165 4.972 15.351 1.935 1.00 23.17 C

ATOM 2307 O GLU A 165 4.198 15.635 1.009 1.00 23.03 O

ATOM 2309 N TYR A 166 4.696 14.428 2.854 1.00 21.92 N

ATOM 2310 CA TYR A 166 3.371 13.805 2.967 1.00 20.89 C

ATOM 2312 CB TYR A 166 3.384 12.402 2.332 1.00 18.85 C

ATOM 2315 CG TYR A 166 4.312 11.413 3.032 1.00 18.24 C

ATOM 2316 CDl TYR A 166 3.852 10.619 4.075 1.00 16.68 C

ATOM 2318 CEl TYR A 166 4.690 9.735 4.725 1.00 16.33 C

ATOM 2320 CZ TYR A 166 6.017 9.626 4.334 1.00 16.86 C

ATOM 2321 OH TYR A 166 6.842 8.739 4.979 1.00 17.51 O

ATOM 2323 CE2 TYR A 166 6.509 10.400 3.306 1.00 18.12 C

ATOM 2325 CD2 TYR A 166 5.654 11.293 2.656 1.00 19.14 C

ATOM 2327 C TYR A 166 2.853 13.743 4.415 1.00 20.96 C

ATOM 2328 O TYR A 166 1.669 13.542 4.632 1.00 20.01 O

ATOM 2330 N ARG A 167 3.735 13.922 5.396 1.00 22.56 N

ATOM 2331 CA ARG A 167 3.354 13.867 6.815 1.00 23.68 C

ATOM 2333 CB ARG A 167 4.580 13.561 7.692 1.00 23.83 C

ATOM 2336 CG ARG A 167 5.148 12.159 7.489 1.00 22.23 C

ATOM 2339 CD ARG A 167 6.600 12.010 7.977 1.00 22.86 C

ATOM 2342 NE ARG A 167 7.502 12.951 7.311 1.00 24.90 N

ATOM 2344 CZ ARG A 167 8.801 13.108 7.591 1.00 26.45 C

ATOM 2345 NHl ARG A 167 9.400 12.363 8.511 1.00 25.72 N

ATOM 2348 NH2 ARG A 167 9.516 14.018 6.928 1.00 28.39 N

ATOM 2351 C ARG A 167 2.664 15.165 7.265 1.00 26.16 C

ATOM 2352 O ARG A 167 3.218 16.261 7.131 1.00 28.03 O

ATOM 2354 N THR A 168 1.444 15.026 7.777 1.00 26.98 N

ATOM 2355 CA THR A 168 0.667 16.154 8.275 1.00 30.06 C

ATOM 2357 CB THR A 168 -0.806 16.074 7.824 1.00 29.84 C

ATOM 2359 OGl THR A 168 -1.471 15.003 8.503 1.00 27.89 O

ATOM 2361 CG2 THR A 168 -0.903 15.872 6.313 1.00 29.06 C

ATOM 2365 C THR A 168 0.684 16.283 9.806 1.00 32.16 C

ATOM 2366 O THR A 168 0.193 17.285 10.341 1.00 34.81 O

ATOM 2368 N HIS A 169 1.221 15.289 10.511 1.00 31.47 N

ATOM 2369 CA HIS A 169 1.341 15.374 11.980 1.00 33.83 C

ATOM 2371 CB HIS A 169 0.759 14.124 12.650 1.00 32.43 C

ATOM 2374 CG HIS A 169 -0.640 13.814 12.212 1.00 32.12 C

ATOM 2375 NDl HIS A 169 -1.751 14.268 12.888 1.00 34.81 N

ATOM 2377 CEl HIS A 169 -2.842 13.854 12.267 1.00 33.51 C

ATOM 2379 NE2 HIS A 169 -2.478 13.165 11.202 1.00 30.41 N

ATOM 2381 CD2 HIS A 169 -1.106 13.133 11.140 1.00 30.37 C

ATOM 2383 C HIS A 169 2.792 15.585 12.404 1.00 35.19 C

ATOM 2384 O HIS A 169 3.666 14.783 12.079 1.00 33.71 O

ATOM 2386 N GLN A 170 3.028 16.677 13.127 1.00 39.04 N

ATOM 2387 CA GLN A 170 4.349 17.031 13.673 1.00 40.77 C

ATOM 2389 CB GLN A 170 4.198 18.190 14.671 1.00 44.21 C

ATOM 2392 CG GLN A 170 5.498 18.705 15.255 1.00 46.20 C Table 2

ATOM 2395 CD GLN A 170 6.407 19.296 14.207 1.00 47.39 C

ATOM 2396 OEl GLN A 170 6.352 20.491 13.934 1.00 51.95 O

ATOM 2397 NE2 GLN A 170 7.246 18.466 13.611 1.00 45.31 N

ATOM 2400 C GLN A 170 5.048 15.859 14.360 1.00 40.00 C

ATOM 2401 O GLN A 170 6.226 15.601 14.107 1.00 39.60 O

ATOM 2403 N GLU A 171 4.309 15.141 15.201 1.00 40.28 N

ATOM 2404 CA GLU A 171 4.838 13.968 15.922 1.00 39.84 C

ATOM 2406 CB GLD A 171 3.744 13.311 16.771 1.00 40.14 C

ATOM 2409 CG GLD A 171 3.101 14.250 17.800 1.00 44.40 C

ATOM 2412 CD GLU A 171 1.817 14.917 17.312 1.00 46.38 C

ATOM 2413 OEl GLU A 171 1.573 14.987 16.081 1.00 45.88 O

ATOM 2414 OE2 GLU A 171 1.050 15.383 18.182 1.00 49.89 O

ATOM 2415 C GLU A 171 5.457 12.905 15.013 1.00 37.72 C

ATOM 2416 O GLU A 171 6.365 12.190 15.431 1.00 37.88 O

ATOM 2418 N ASP A 172 4.959 12.786 13.785 1.00 36.26 N

ATOM 2419 CA ASP A 172 5.528 11.851 12.806 1.00 34.06 C

ATOM 2421 CB ASP A 172 4.492 11.502 11.717 1.00 32.39 C

ATOM 2424 CG ASP A 172 3.314 10.693 12.256 1.00 30.78 C

ATOM 2425 ODl ASP A 172 3.540 9.789 13.095 1.00 28.27 O

ATOM 2426 OD2 ASP A 172 2.160 10.964 11.833 1.00 29.74 O

ATOM 2427 C ASP A 172 6.803 12.391 12.156 1.00 34.80 C

ATOM 2428 O ASP A 172 7.560 11.634 11.554 1.00 33.87 O

ATOM 2430 N ILE A 173 7.036 13.694 12.272 1.00 37.09 N

ATOM 2431 CA ILE A 173 8.179 14.347 11.643 1.00 38.02 C

ATOM 2433 CB ILE A 173 7.777 15.719 11.043 1.00 39.71 C

ATOM 2435 CGl ILE A 173 6.583 15.550 10.092 1.00 38.00 C

ATOM 2438 CDl ILE A 173 6.007 16.838 9.558 1.00 39.70 C

ATOM 2442 CG2 ILE A 173 8.959 16.361 10.321 1.00 40.98 C

ATOM 2446 C ILE A 173 9.281 14.506 12.688 1.00 39.79 C

ATOM 2447 O ILE A 173 10.201 13.693 12.772 1.00 39.06 O

ATOM 2449 OXT ILE A 173 9.268 15.436 13.485 1.00 42.11 O

ATOM 2450 03 GOL A 1 8.641 -4.330 -9.376 1.00 17.77 O

ATOM 2452 C3 GOL A 1 7.391 -4.751 -8.831 1.00 17.19 C

ATOM 2455 C2 GOL A 1 6.706 -3.707 -7.945 1.00 15.00 C

ATOM 2457 02 GOL A 1 7.471 -3.432 -6.789 1.00 14.33 O

ATOM 2459 Cl GOL A 1 6.407 -2.454 -8.760 1.00 15.59 C

ATOM 2462 Ol GOL A 1 5.602 -1.537 -8.056 1.00 14.65 O

ATOM 2464 Cl NAG C 1 1.081 -15.286 19.558 1.00135.62 C C

ATOM 2466 Ol NAG C 1 0.791 -15.753 20.856 1.00154.45 C O

ATOM 2468 C2 NAG C 1 2.587 -15.339 19.312 1.00127.56 C C

ATOM 2470 N2 NAG C 1 3.313 -14.542 20.295 1.00132.35 C N

ATOM 2472 C7 NAG C 1 4.230 -15.065 21.113 1.00142.33 C C

ATOM 2473 07 NAG C 1 5.322 -15.492 20.734 1.00137.89 C O

ATOM 2474 C8 NAG C 1 3.866 -15.105 22.566 1.00161.53 C C

ATOM 2478 C3 NAG C 1 2.914 -14.884 17.886 1.00108.94 C C

ATOM 2480 03 NAG C 1 4.280 -15.182 17.655 1.00102.59 C O

ATOM 2481 C4 NAG C 1 2.027 -15.591 16.853 1.00106.12 C C

ATOM 2483 04 NAG C 1 2.101 -14.946 15.597 1.00 92.63 C O

ATOM 2485 C5 NAG C 1 0.558 -15.642 17.277 1.00116.05 C C

ATOM 2487 C6 NAG C 1 -0.231 -16.551 16.337 1.00115.26 C C

ATOM 2490 06 NAG C 1 -1.572 -16.631 16.762 1.00125.75 C O

ATOM 2492 05 NAG C 1 0.428 -16.107 18.609 1.00132.62 C O

ATOM 2493 Cl GCU C 2 4.932 -14.245 16.778 1.00 87.39 C C

ATOM 2495 C2 GCU C 2 6.413 -14.184 17.144 1.00 87.62 C C

ATOM 2497 02 GCU C 2 6.550 -13.438 18.332 1.00 94.52 C O

ATOM 2499 C3 GCU C 2 7.302 -13.533 16.084 1.00 75.68 C C

ATOM 2501 03 GCU C 2 8.615 -14.024 16.239 1.00 78.47 C O

ATOM 2503 C4 GCU C 2 6.846 -13.753 14.643 1.00 66.42 C C

ATOM 2505 04 GCU C 2 7.347 -12.713 13.821 1.00 57.87 C O

ATOM 2506 C5 GCU C 2 5.330 -13.753 14.525 1.00 66.09 C C

ATOM 2508 C6 GCU C 2 4.896 -14.139 13.117 1.00 58.29 C C

ATOM 2509 O6A GCU C 2 5.123 -15.311 12.743 1.00 58.95 C O

ATOM 2510 O6B GCU C 2 4.344 -13.256 12.422 1.00 50.34 C O

ATOM 2511 05 GCU C 2 4.777 -14.658 15.447 1.00 77.80 C O

ATOM 2512 Cl NAG C 3 8.439 -13.166 12.997 1.00 55.97 C C

ATOM 2514 C2 NAG C 3 8.732 -12.129 11.914 1.00 49.16 C C

ATOM 2516 N2 NAG C 3 7.604 -11.986 11.005 1.00 44.25 C N

ATOM 2518 C7 NAG C 3 6.873 -10.887 10.897 1.00 41.24 C C Table 2

ATOM 2519 07 NAG C 3 7.204 -9.794 11.339 1.00 40.73 C O

ATOM 2520 C8 NAG C 3 5.576 -11.042 10.162 1.00 39.62 C C

ATOM 2524 C3 NAG C 3 9.966 -12.539 11.110 1.00 50.33 C C

ATOM 2526 03 NAG C 3 10.350 -11.480 10.261 1.00 48.02 C O

ATOM 2527 C4 NAG C 3 11.136 -12.890 12.024 1.00 56.09 C C

ATOM 2529 04 NAG C 3 12.200 -13.367 11.230 1.00 57.93 C O

ATOM 2531 C5 NAG C 3 10.692 -13.925 13.051 1.00 61.92 C C

ATOM 2533 C6 NAG C 3 11.797 -14.253 14.051 1.00 71.11 C C

ATOM 2536 06 NAG C 3 11.828 -13.269 15.064 1.00 73.18 C O

ATOM 2538 05 NAG C 3 9.596 -13.409 13.771 1.00 61.53 C O

ATOM 2539 Cl GCU C 4 10.212 -11.802 8.863 1.00 47.28 C C

ATOM 2541 C2 GCO C 4 10.375 -10.495 8.098 1.00 46.51 C C

ATOM 2543 02 GCD C 4 9.416 -9.583 8.570 1.00 43.70 C O

ATOM 2545 C3 GCD C 4 10.183 -10.714 6.608 1.00 47.50 C C

ATOM 2547 03 GCO C 4 10.568 -9.574 5.881 1.00 49.87 C O

ATOM 2549 C4 GCO C 4 11.016 -11.879 6.104 1.00 52.08 C C

ATOM 2551 04 GCO C 4 10.470 -12.221 4.858 1.00 55.22 C O

ATOM 2552 C5 GCD C 4 10.951 -13.093 7.025 1.00 52.07 C C

ATOM 2554 C6 GCD C 4 12.011 -14.090 6.580 1.00 58.09 C C

ATOM 2555 O6A GCD C 4 13.187 -13.876 6.947 1.00 62.38 C O

ATOM 2556 O6B GCO C 4 11.645 -15.050 5.859 1.00 59.56 C O

ATOM 2557 05 GCO C 4 11.143 -12.753 8.391 1.00 51.56 C O

ATOM 2558 Cl NAG C 5 11.425 -12.321 3.784 1.00 63.78 C C

ATOM 2560 C2 NAG C 5 10.732 -13.152 2.718 1.00 66.39 C C

ATOM 2562 N2 NAG C 5 10.390 -14.459 3.250 1.00 65.18 C N

ATOM 2564 C7 NAG C 5 9.133 -14.897 3.243 1.00 62.45 C C

ATOM 2565 07 NAG C 5 8.250 -14.414 2.535 1.00 62.04 C O

ATOM 2566 C8 NAG C 5 8.817 -16.045 4.153 1.00 62.16 C C

ATOM 2570 C3 NAG C 5 11.544 -13.291 1.435 1.00 76.07 C C

ATOM 2572 03 NAG C 5 10.686 -13.815 0.443 1.00 79.41 C O

ATOM 2573 C4 NAG C 5 12.086 -11.941 0.981 1.00 79.94 C C

ATOM 2575 04 NAG C 5 13.019 -12.139 -0.058 1.00 90.01 C O

ATOM 2577 C5 NAG C 5 12.734 -11.215 2.161 1.00 76.79 C C

ATOM 2579 C6 NAG C 5 13.248 -9.832 1. .768 1.00 82.23 C C

ATOM 2582 06 NAG C 5 12.180 -9.025 1..319 1.00 80.32 C O

ATOM 2584 05 NAG C 5 11.800 -11.082 3..222 1.00 67.58 C O

ATOM 2585 Cl GCO C 6 11.233 -14.971 -0..209 1.00 87.32 C C

ATOM 2587 C2 GCD C 6 10.067 -15.710 -0.858 1.00 87.39 C C

ATOM 2589 02 GCD C 6 9.343 -16.347 0.173 1.00 80.53 C O

ATOM 2591 C3 GCO C 6 10.490 -16.757 -1..892 1.00 96.39 C C

ATOM 2593 03 GCO C 6 9.397 -17.025 -2.742 1.00 97.43 C O

ATOM 2595 C4 GCD C 6 11.686 -16.324 -2.738 1.00107.28 C C

ATOM 2597 04 GCD C 6 12.244 -17.472 -3.342 1.00116.45 C O

ATOM 2598 C5 GCU C 6 12.758 -15.658 -1. 873 1.00106.31 C C

ATOM 2600 C6 GCO C 6 13.954 -15.133 -2.667 1.00118.55 C C

ATOM 2601 06A GCO C 6 15.077 -15.184 -2.117 1.00121.69 C O

ATOM 2602 06B GCO C 6 13.760 -14.669 -3.812 1.00126.42 C O

ATOM 2603 05 GCD C 6 12.196 -14.580 -1.159 1.00 97.91 C O

ATOM 2604 Cl NAG C 7 11.829 -17.695 -4.701 1.00125.82 C C

ATOM 2606 C2 NAG C 7 12.922 -18.521 -5.371 1.00138.92 C C

ATOM 2608 N2 NAG C 7 14.209 -17.858 -5.241 1.00145.43 C N

ATOM 2610 C7 NAG C 7 15.244 -18.460 -4.663 1.00148.83 C C

ATOM 2611 07 NAG C 7 16.251 -18.786 -5.287 1.00162.74 C O

ATOM 2612 C8 NAG C 7 15.136 -18.739 -3.193 1.00137.24 C C

ATOM 2616 C3 NAG C 7 12.573 -18.794 -6.830 1.00150.37 C C

ATOM 2618 03 NAG C 7 13.549 -19.630 -7.420 1.00162.95 C O

ATOM 2620 C4 NAG C 7 11.198 -19.453 -6.895 1.00144.09 C C

ATOM 2622 04 NAG C 7 10.790 -19.571 -8.240 1.00154.93 C O

ATOM 2624 C5 NAG C 7 10.162 -18.649 -5.105 1.00131.29 C C

ATOM 2626 C6 NAG C 7 8.834 -19.403 -6.054 1.00126.61 C C

ATOM 2629 06 NAG C 7 7.914 -18.726 -5.224 1.00116.33 C O

ATOM 2631 05 NAG C 7 10.605 -18.392 -4.782 1.00121.61 C O

ATOM 2632 O HOH W 1 7.279 21.846 -4.492 1.00 32.92 W O

ATOM 2635 O HOH W 2 3.876 -9.003 -4.410 1.00 35.11 W O

ATOM 2638 O HOH W 4 -10.582 4.115 -2.089 1.00 28.61 W O

ATOM 2641 O HOH W 5 8.147 0.656 7.402 1.00 11.69 W O

ATOM 2644 O HOH W 6 8.038 -2.827 -11.523 1.00 17.70 W O

ATOM 2647 O HOH W 7 -5.256 -20.441 9.418 1.00 35.19 W O Table 2

ATOM 2650 O HOH W 8 7.206 -3.169 -0.020 1.00 12.89 W O

ATOM 2653 O HOH W 9 -8.526 4.101 -3.594 1.00 14.76 W O

ATOM 2656 O HOH W 10 -5.923 -17.187 -2.538 1.00 33.18 W O

ATOM 2659 O HOH W 11 1.568 -6.907 -14.238 1.00 26.00 W O

ATOM 2662 O HOH W 12 10.125 1.656 1.370 1.00 15.25 W O

ATOM 2665 O HOH W 13 -1.664 -11.845 16.874 1.00 39.73 W O

ATOM 2668 O HOH W 14 5.610 2.366 -14.712 1.00 33.26 W 0

ATOM 2671 O HOH W 15 -1.576 -0.232 -10.150 1.00 18.16 W O

ATOM 2674 O HOH W 16 -0.359 13.046 2.890 1.00 20.91 W O

ATOM 2677 O HOH W 18 -4.192 -4.030 -8.986 1.00 10.41 W O

ATOM 2680 O HOH W 19 11.692 15.161 8.939 1.00 70.60 W O

ATOM 2683 O HOH W 20 -8.988 -13.970 5.403 1.00 27.19 W O

ATOM 2686 O HOH W 21 -6.985 -13.361 12.393 1.00 24.52 W O

ATOM 2689 O HOH W 22 5.232 -6.218 20.289 1.00 19.04 W O

ATOM 2692 O HOH W 23 -7.305 5.930 4.528 1.00 15.08 W O

ATOM 2695 O HOH W 24 1.884 -1.145 25.167 1.00 29.45 W O

ATOM 2698 O HOH W 25 10.152 -2.723 -3.301 1.00 20.37 W O

ATOM 2701 O HOH W 26 -1.592 -19.394 16.726 1.00 49.49 W O

ATOM 2704 O HOH W 27 16.763 6.467 3.143 1.00 50.21 W O

ATOM 2707 O HOH W 28 4.159 5.012 19.653 1.00 30.57 W O

ATOM 2710 O HOH W 29 14.348 -2.639 7.587 1.00 28.14 W O

ATOM 2713 O HOH W 30 1.781 -18.206 7.306 1.00 21.50 W O

ATOM 2716 O HOH W 31 -9.757 -1.764 -12.149 1.00 12.80 W O

ATOM 2719 O HOH W 32 12.253 -2.858 7.317 1.00 26.25 W O

ATOM 2722 O HOH W 33 5.924 20.886 3.791 1.00 41.42 W O

ATOM 2725 O HOH W 34 6.670 -7.249 0.907 1.00 29.31 W O

ATOM 2728 O HOH W 35 -9.931 -13.895 0.972 1.00 33.22 W O

ATOM 2731 O HOH W 36 -1.228 -5.915 23.937 1.00 33.11 W O

ATOM 2734 O HOH W 37 -5.111 -5.464 14.724 1.00 19.19 W O

ATOM 2737 O HOH W 38 -0.931 -2.853 23.488 1.00 25.73 W O

ATOM 2740 O HOH- W 39 1.999 12.403 9.506 1.00 19.65 W O

ATOM 2743 O HOH W 40 2.103 -11.695 -3.485 1.00 19.65 W O

ATOM 2746 O HOH W 41 14.506 -2.408 1.417 1.00 33.64 W O

ATOM 2749 O HOH W 42 -9.504 -12.658 8.876 1.00 47.65 W O

ATOM 2752 O HOH W 43 -5.336 -6.784 -13.835 1.00 19.88 W O

ATOM 2755 O HOH W 44 14.486 -4.694 5.137 1.00 26.03 W O

ATOM 2758 O HOH W 45 -1.117 0.179 -14.328 1.00 26.61 W O

ATOM 2761 O HOH W 46 -4.663 -16.588 -7.324 1.00 33.75 W O

ATOM 2764 O HOH W 47 12.031 -11.454 9.230 1.00 39.14 W O

ATOM 2767 O HOH W 48 3.097 16.371 -5.925 1.00 30.01 W O

ATOM 2770 O HOH W 49 1.277 -15.394 -4.878 1.00 35.85 W O

ATOM 2773 O HOH W 50 5.777 6.925 11.694 1.00 27.65 W O

ATOM 2776 O HOH W 51 7.256 -8.594 -7.637 1.00 28.48 W O

ATOM 2779 O HOH W 53 1.776 -11.643 19.526 1.00 42.02 W O

ATOM 2782 O HOH W 55 -5.349 1.058 -14.023 1.00 31.31 W O

ATOM 2785 O HOH W 56 5.568 17.013 -3.573 1.00 35.96 W O

ATOM 2788 O HOH W 57 7.438 -22.977 7.282 1.00 46.55 W O

ATOM 2791 O HOH W 58 2.559 5.588 -10.500 1.00 32.79 W O

ATOM 2794 O HOH W 59 3.503 -9.019 19.176 1.00 29.60 W O

ATOM 2797 O HOH W 60 5.284 9.645 -13.436 1.00 49.56 W O

ATOM 2800 O HOH W 61 18.875 15.248 -1.736 1.00 57.95 W O

ATOM 2803 O HOH W 62 -4.130 17.750 -2.710 1.00 39.82 W O

ATOM 2806 O HOH W 63 3.179 6.322 -14.639 1.00 45.26 W O

ATOM 2809 O HOH W 64 5.953 -17.267 14.911 1.00 61.50 W O

ATOM 2812 O HOH W 65 11.919 0.633 2.401 1.00 34.99 W O

ATOM 2815 O HOH W 66 15.484 5.443 -11.584 1.00 37.55 W O

ATOM 2818 O HOH W 67 1.670 -23.969 0.884 1.00 40.79 W O

ATOM 2821 O HOH W 68 3.898 19.005 7.368 1.00 47.39 W O

ATOM 2824 O HOH W 69 12.304 -3.784 12.061 1.00 41.70 W O

ATOM 2827 O HOH W 70 10.133 -4.179 10.170 1.00 25.38 W O

ATOM 2830 O HOH W 71 9.387 -7.978 3.059 1.00 44.46 W O

ATOM 2833 O HOH W 72 0.277 2.271 -10.520 1.00 43.54 W O

ATOM 2836 O HOH W 73 12.749 7.574 -12.501 1.00 30.04 W O

ATOM 2839 O HOH W 74 10.035 3.479 4.742 1.00 22.89 W O

ATOM 2842 O HOH W 75 9.401 16.523 15.964 1.00 60.39 W O

ATOM 2845 O HOH W 76 -5.573 7.625 3.842 1.00 24.91 W O

ATOM 2848 O HOH W 77 11.844 2.203 11.777 1.00 37.20 W O

ATOM 2851 O HOH W 78 14.403 -9.047 6.251 1.00 31.77 W O Table 2

ATOM 2854 O HOH W 79 13.739 7.779 9.276 1.00 44.94 W O

ATOM 2857 O HOH W 80 16.069 -11.565 -2.168 1.00 62.58 W O

ATOM 2860 O HOH W 81 2.019 1.518 -12.495 1.00 22.89 W O

ATOM 2863 O HOH W 82 -4.662 16.128 -7.237 1.00 45.28 W O

ATOM 2866 O HOH W 83 12.805 -6.158 14.365 1.00 39.15 W O

ATOM 2869 O HOH W 84 11.656 -3.639 1.673 1.00 34.65 W O

ATOM 2872 O HOH W 85 15.733 8.093 -7.975 1.00 51.38 W O

ATOM 2875 O HOH W 86 11.901 9.667 8.391 1.00 30.24 W O

ATOM 2878 O HOH W 87 15.863 16.679 0.259 1.00 39.22 W O

ATOM 2881 O HOH W 88 0.182 3.323 15.734 1.00 30.94 W O

ATOM 2884 O HOH W 89 1.735 -23.836 -3.504 1.00121.37 W O

ATOM 2887 O HOH W 90 8.363 17.804 -6.640 1.00 50.06 W O

ATOM 2890 O HOH W 91 1.306 -12.007 16.386 1.00 49.44 W O

ATOM 2893 O HOH W 92 17.651 -5.787 0.667 1.00 46.57 W O

ATOM 2896 O HOH W 93 9.504 6.472 10.298 1.00 40.08 W O

ATOM 2899 O HOH W 94 -6.222 -7.191 19.259 1.00 59.01 W O

ATOM 2902 O HOH W 95 9.146 18.348 6.303 1.00 40.00 W O

ATOM 2905 O HOH W 96 -6.612 8.935 2.044 1.00 28.98 W O

ATOM 2908 O HOH W 97 19.367 8.952 1.269 1.00 52.17 W O

ATOM 2911 O HOH W 98 -5.340 -23.033 5.924 1.00 38.64 W O

ATOM 2914 O HOH W 99 0.293 18.404 13.719 1.00 44.79 W O

ATOM 2917 O HOH W 100 -3.029 11.111 9.326 1.00 46.82 W O

ATOM 2920 O HOH W 102 -2.514 -13.089 21.249 1.00 49.15 W O

ATOM 2923 O HOH W 103 14.281 14.199 -6.701 1.00 54.36 W O

ATOM 2926 O HOH W 104 -6.033 10.799 6.058 1.00 39.94 W O

ATOM 2929 O HOH W 105 8.770 20.388 -2.908 1.00 31.49 W O

ATOM 2932 O HOH W 106 12.367 2.714 -0.935 1.00 21.97 W O

ATOM 2935 O HOH W 107 5.533 -7.353 -5.422 1.00 23.07 W O

ATOM 2938 O HOH W 108 3.750 -5.884 -14.538 1.00 24.34 W O

ATOM 2941 O HOH W 109 -7.777 5.771 -5.254 1.00 22.43 W O

ATOM 2944 O HOH W 110 4.230 -9.035 -1.879 1.00 32.80 W O

ATOM 2947 O HOH W 111 2.748 5.935 17.782 1.00 35.25 W O

ATOM 2950 O HOH W 112 -0.778 -12.054 19.400 1.00 39.16 W O

ATOM 2953 O HOH W 113 -9.283 -13.417 11.762 1.00 38.82 W O

ATOM 2956 O HOH W 115 11.237 -7.794 12.917 1.00 47.49 W O

ATOM 2959 O HOH W 116 10.250 -0.977 -14.372 1.00 22.25 W O

ATOM 2962 O HOH W 117 9.149 25.044 -2.731 1.00 47.89 W O

ATOM 2965 O HOH W 118 -5.831 -13.383 15.125 1.00 36.22 W O

ATOM 2968 O HOH W 119 -6.782 -7.583 16.964 1.00 23.41 W O

ATOM 2971 O HOH W 120 0.618 -21.950 -5.173 1.00 58.14 W O

ATOM 2974 O HOH W 121 6.961 -9.570 2.811 1.00 28.57 W O

ATOM 2977 O HOH W 122 -7.119 3.776 10.571 1.00 59.74 W O

ATOM 2980 O HOH W 123 -6.187 -16.152 9.863 1.00 44.26 W O

ATOM 2983 O HOH W 124 8.172 10.073 10.101 1.00 28.29 W O

ATOM 2986 O HOH W 125 13.259 -8.302 5.910 1.00 36.72 W O

ATOM 2989 O HOH W 126 3.513 -15.725 -3.058 1.00 49.14 W O

ATOM 2992 O HOH W 127 -3.007 -10.759 -12.652 1.00 39.98 W O

ATOM 2995 O HOH W 128 12.463 -7.572 -2.891 1.00 82.59 W O

ATOM 2998 O HOH W 129 -1.562 -23.766 8.022 1.00 42.90 W O

ATOM 3001 O HOH W 130 18.276 15.421 1.587 1.00 54.81 W O

ATOM 3004 O HOH W 131 16.269 16.735 8.929 1.00 54.48 W O

ATOM 3007 O HOH W 132 13.811 0.615 10.911 1.00 47.76 W O

ATOM 3010 O HOH W 133 18.549 14.306 6.561 1.00113.67 W O

ATOM 3013 O HOH W 134 12.379 17.436 7.088 1.00 66.73 W O

ATOM 3016 O HOH W 135 10.182 -13.999 -6.350 1.00 80.38 W O

ATOM 3019 O HOH W 136 0.169 7.990 15.430 1.00 43.38 W O

ATOM 3022 O HOH W 137 7.991 -8.868 13.265 1.00 48.55 W O

ATOM 3025 O HOH W 138 3.720 -10.466 16.696 1.00 34.25 W O

ATOM 3028 O HOH W 139 -0.758 2.137 -7.366 1.00 18.42 W O

ATOM 3031 O HOH W 140 11.139 17.151 -7.376 1.00 45.78 W O

END Table 3

TABLE 3

CRYSTl 48 . 881 77 . 266 87 . 668 90 . 00 90. 00 90 . 00 P 21 21 21

ATOM 1 N ALA A 20 12.776 9.674 30.388 1.00 20.58 N

ATOM 2 CA ALA A 20 11.814 8.654 29.868 1.00 20.56 C

ATOM 3 C ALA A 20 11.860 8.593 28.345 1.00 20.31 C

ATOM 4 O ALA A 20 12.223 9.569 27.685 1.00 20.06 O

ATOM 5 CB ALA A 20 10.392 8.930 30.369 1.00 20.24 C

ATOM 6 N GLN A 21 11.487 7.439 27.798 1.00 20.31 N

ATOM 7 CA GLN A 21 11.695 7.159 26.378 1.00 20.45 C

ATOM 8 C GLN A 21 10.542 6.370 25.774 1.00 19.33 C

ATOM 9 O GLN A 21 10.082 5.390 26.351 1.00 19.52 O

ATOM 10 CB GLN A 21 13.010 6.394 26.223 1.00 21.08 C

ATOM 11 CG GLN A 21 13.288 5.818 24.864 1.00 24.44 C

ATOM 12 CD GLN A 21 14.334 4.713 24.922 1.00 30.51 C

ATOM 13 OEl GLN A 21 14.684 4.235 26.010 1.00 31.51 O

ATOM 14 NE2 GLN A 21 14.836 4.302 23.751 1.00 31.93 N

ATOM 15 N ILE A 22 10.078 6.809 24.608 1.00 18.47 N

ATOM 16 CA ILE A 22 9.038 6.086 23.867 1.00 17.36 C

ATOM 17 C ILE A 22 9.506 5.761 22.445 1.00 16.66 C

ATOM 18 O ILE A 22 9.888 6.656 21.704 1.00 15.93 O

ATOM 19 CB ILE A 22 7.707 6.895 23.847 1.00 17.50 C

ATOM 20 CGl ILE A 22 7.104 6.963 25.269 1.00 17.49 C

ATOM 21 CG2 ILE A 22 6.724 6.297 22.813 1.00 16.37 C

ATOM 22 CDl ILE A 22 5.841 7.820 25.409 1.00 16.84 C

ATOM 23 N ASP A 23 9.484 4.476 22.085 1.00 16.38 N

ATOM 24 CA ASP A 23 9.834 4.046 20.724 1.00 16.37 C

ATOM 25 C ASP A 23 8.591 3.624 19.940 1.00 16.16 C

ATOM 26 O ASP A 23 7.802 2.792 20.399 1.00 16.00 O

ATOM 27 CB ASP A 23 10.835 2.880 20.737 1.00 16.28 C

ATOM 28 CG ASP A 23 12.146 3.227 21.428 1.00 17.47 C

ATOM 29 ODl ASP A 23 12.665 4.345 21.229 1.00 16.84 O

ATOM 30 OD2 ASP A 23 12.735 2.430 22.196 1.00 19.43 O

ATOM 31 N LEU A 24 8.440 4.177 18.742 1.00 15.94 N

ATOM 32 CA LEU A 24 7.292 3.865 17.907 1.00 15.90 C

ATOM 33 C LED A 24 7.741 3.224 16.601 1.00 16.18 C

ATOM 34 O LEU A 24 8.503 3.818 15.832 1.00 16.60 O

ATOM 35 CB LEU A 24 6.432 5.112 17.652 1.00 15.07 C

ATOM 36 CG LEU A 24 5.906 5.859 18.895 1.00 14.71 C

ATOM 37 CDl LEU A 24 5.364 7.259 18.564 1.00 12.04 C

ATOM 38 CD2 LEU A 24 4.860 5.046 19.673 1.00 13.02 C

ATOM 39 N ASN A 25 7.286 1.999 16.369 1.00 16.03 N

ATOM 40 CA ASN A 25 7.507 1.356 15.091 1.00 15.96 C

ATOM 41 C ASN A 25 6.263 1.522 14.253 1.00 15.78 C

ATOM 42 O ASN A 25 5.159 1.125 14.658 1.00 15.80 O

ATOM 43 CB ASN A 25 7.890 -0.107 15.256 1.00 15.90 C

ATOM 44 CG ASN A 25 9.305 -0.274 15.760 1.00 17.95 C

ATOM 45 ODl ASN A 25 9.580 -0.092 16.951 1.00 21.12 O

ATOM 46 ND2 ASN A 25 10.219 -0.619 14.859 1.00 18.38 N

ATOM 47 N ILE A 26 6.438 2.163 13.101 1.00 15.75 N

ATOM 48 CA ILE A 26 5.323 2.400 12.202 1.00 15.43 C

ATOM 49 C ILE A 26 5.465 1.678 10.858 1.00 15.22 C

ATOM 50 O ILE A 26 6.562 1.366 10.373 1.00 15.12 O

ATOM 51 CB ILE A 26 5.000 3.907 12.023 1.00 15.66 C

ATOM 52 CGl ILE A 26 6.040 4.594 11.146 1.00 16.24 C

ATOM 53 CG2 ILE A 26 4.853 4.607 13.382 1.00 16.06 C

ATOM 54 CDl ILE A 26 5.500 5.814 10.497 1.00 18.50 C

ATOM 55 N THR A 27 4.299 1.431 10.293 1.00 14.56 N

ATOM 56 CA THR A 27 4.090 0.714 9.071 1.00 14.28 C

ATOM 57 C THR A 27 3.949 1.744 7.926 1.00 13.99 C

ATOM 58 O THR A 27 3.653 2.919 8.168 1.00 13.56 O

ATOM 59 CB THR A 27 2.797 -0.087 9.353 1.00 14.52 C

ATOM 60 OGl THR A 27 3.098 -1.488 9.480 1.00 16.54 O

ATOM 61 CG2 THR A 27 1.781 0.021 8.279 1.00 13.28 C

ATOM 62 N CYS A 28 4.184 1.316 6.688 1.00 13.71 N Table 3

ATOM 63 CA CYS A 28 3.744 2.076 5.516 1.00 13.69 C

ATOM 64 C CYS A 28 2.227 2.294 5.598 1.00 13.24 C

ATOM 65 O CYS A 28 1.536 1.539 6.287 1.00 12.23 O

ATOM 66 CB CYS A 28 4.078 1.302 4.242 1.00 14.04 C

ATOM 67 SG CYS A 28 5.828 0.914 4.012 1.00 16.34 S

ATOM 68 N ARG A 29 1.702 3.319 4.919 1.00 13.09 N

ATOM 69 CA ARG A 29 0.244 3.514 4.870 1.00 12.81 C

ATOM 70 C ARG A 29 0.392 2.773 3.704 1.00 12.80 C

ATOM 71 O ARG A 29 0.108 2.810 2.577 1.00 12.61 O

ATOM 72 CB ARG A 29 0.151 4.983 4.776 1.00 13.04 C

ATOM 73 CG ARG A 29 0.131 5.745 6.093 1.00 14.03 C

ATOM 74 CD ARG A 29 1.084 6.626 6.232 1.00 15.84 C

ATOM 75 NE ARG A 29 2.259 5.880 6.632 1.00 15.81 N

ATOM 76 CZ ARG A 29 3.497 6.133 6.227 1.00 15.61 C

ATOM 77 NHl ARG A 29 3.753 7.101 5.366 1.00 13.88 N

ATOM 78 NH2 ARG A 29 4.491 5.384 6.681 1.00 16.58 N

ATOM 79 N PHE A 30 1.510 2.113 3.985 1.00 12.37 N

ATOM 80 CA PHE A 30 2.287 1.421 2.965 1.00 11.51 C

ATOM 81 C PHE A 30 3.666 2.067 2.908 1.00 11.59 C

ATOM 82 O PHE A 30 4.488 1.889 3.814 1.00 11.53 O

ATOM 83 CB PHE A 30 2.402 -0.068 3.299 1.00 10.79 C

ATOM 84 CG PHE A 30 1.089 -0.800 3.279 1.00 10.90 C

ATOM 85 CDl PHE A 30 0.150 -0.617 4.301 1.00 8.83 C

ATOM 86 CD2 PHE A 30 0.783 -1.683 2.232 1.00 9.63 C

ATOM 87 CEl PHE A 30 1.081 -1.292 4.275 1.00 8.56 C

ATOM 88 CE2 PHE A 30 0.443 -2.367 2.205 1.00 8.72 C

ATOM 89 CZ PHE A 30 1.371 -2.171 3.221 1.00 9.15 C

ATOM 90 N ALA A 31 3.913 2.827 1.847 1.00 11.57 N

ATOM 91 CA ALA A 31 5.122 3.654 1.751 1.00 12.01 C

ATOM 92 C ALA A 31 5.348 4.460 3.045 1.00 11.76 C

ATOM 93 O ALA A 31 6.449 4.457 3.601 1.00 11.47 O

ATOM 94 CB ALA A 31 6.358 2.788 1.414 1.00 11.65 C

ATOM 95 N GLY A 32 4.290 5.119 3.523 1.00 11.31 N

ATOM 96 CA GLY A 32 4.371 5.949 4.734 1.00 11.17 C

ATOM 97 C GLY A 32 4.120 5.222 6.051 1.00 11.09 C

ATOM 98 O GLY A 32 3.781 5.855 7.051 1.00 10.50 O

ATOM 99 N VAL A 33 4.254 3.893 6.046 1.00 10.93 N

ATOM 100 CA VAL A 33 4.183 3.097 7.279 1.00 10.47 C

ATOM 101 C VAL A 33 2.759 2.624 7.572 1.00 10.87 C

ATOM 102 O VAL A 33 2.066 2.125 6.678 1.00 11.05 O

ATOM 103 CB VAL A 33 5.170 1.890 7.237 1.00 10.55 C

ATOM 104 CGl VAL A 33 4.984 0.961 8.452 1.00 9.82 C

ATOM 105 CG2 VAL A 33 6.619 2.368 7.149 1.00 9.38 C

ATOM 106 N PHE A 34 2.331 2.794 8.823 1.00 10.75 N

ATOM 107 CA PHE A 34 1.044 2.277 9.283 1.00 11.09 C

ATOM 108 C PHE A 34 1.108 1.749 10.716 1.00 11.11 C

ATOM 109 O PHE A 34 2.038 2.071 11.460 1.00 10.85 O

ATOM 110 CB PHE A 34 0.088 3.308 9.125 1.00 10.99 C

ATOM 111 CG PHE A 34 0.107 4.596 9.901 1.00 11.64 C

ATOM 112 CDl PHE A 34 0.693 4.884 11.011 1.00 12.13 C

ATOM 113 CD2 PHE Ά 34 1.030 5.548 9.484 1.00 11.00 C

ATOM 114 CEl PHE A 34 0.551 6.092 11.704 1.00 12.96 C

ATOM 115 CE2 PHE A 34 1.174 6.755 10.161 1.00 13.46 C

ATOM 116 CZ PHE A 34 0.387 7.029 11.280 1.00 12.36 C

ATOM 117 N HIS A 35 0.118 0.924 11.066 1.00 11.16 N

ATOM 118 CA HIS A 35 0.004 0.270 12.377 1.00 11.71 C

ATOM 119 C HIS A 35 1.125 0.925 13.170 1.00 11.94 C

ATOM 120 O HIS A 35 2.180 1.243 12.607 1.00 12.08 O

ATOM 121 CB HIS A 35 0.267 -1.232 12.182 1.00 12.04 C

ATOM 122 CG HIS A 35 0.679 -1.963 13.426 1.00 12.54 C

ATOM 123 NDl HIS A 35 1.974 -2.388 13.642 1.00 15.13 N

ATOM 124 CD2 HIS A 35 0.038 -2.386 14.495 1.00 13.40 C

ATOM 125 CEl HIS A 35 2.040 -3.024 14.801 1.00 15.52 C

ATOM 126 NE2 HIS A 35 0.833 -3.036 15.340 1.00 12.97 N

ATOM 127 N VAL A 36 0.887 1.137 14.466 1.00 12.08 N

ATOM 128 CA VAL A 36 1.888 1.691 15.374 1.00 11.95 C

ATOM 129 C VAL A 36 2.045 0.790 16.586 1.00 12.53 C

ATOM 130 O VAL A 36 1.058 0.435 17.239 1.00 12.64 O Table 3

ATOM 131 CB VAL A 36 1.560 3.133 15.851 1.00 11.85 C

ATOM 132 CGl VAL A 36 2.712 3.698 16.69S 1.00 11.14 C

ATOM 133 CG2 VAL A 36 1.295 4.053 14.676 1.00 11.36 C

ATOM 134 N GLU A 37 3.293 0.412 16.861 1.00 12.96 N

ATOM 135 CA GLU A 37 3.643 -0.361 18.039 1.00 14.16 C

ATOM 136 C GLU A 37 4.536 0.499 18.931 1.00 14.42 C

ATOM 137 O GLU A 37 5.482 1.148 18.458 1.00 13.86 O

ATOM 138 CB GLU A 37 4.346 -1.662 17.630 1.00 13.76 C

ATOM 139 CG GLU A 37 4.775 -2.572 18.771 1.00 15.08 C

ATOM 140 CD GLU A 37 5.319 -3.914 18.293 1.00 16.09 C

ATOM 141 OEl GLU A 37 5.136 -4.265 17.103 1.00 19.96 O

ATOM 142 OE2 GLU A 37 5.918 -4.643 19.112 1.00 17.78 O

ATOM 143 N LYS A 38 4.218 0.505 20.221 1.00 15.05 N

ATOM 144 CA LYS A 38 4.976 1.268 21.205 1.00 15.39 C

ATOM 145 C LYS A 38 5.902 0.352 22.001 1.00 15.36 C

ATOM 146 O LYS A 38 5.459 -0.637 22.607 1.00 14.81 O

ATOM 147 CB LYS A 38 4.016 2.009 22.140 1.00 15.43 C

ATOM 148 CG LYS A 38 4.679 2.750 23.299 1.00 16.04 C

ATOM 149 CD LYS A 38 3.634 3.264 24.302 1.00 16.14 C

ATOM 150 CE LYS A 38 4.307 3.973 25.469 1.00 18.08 C

ATOM 151 NZ LYS A 38 3.327 4.595 26.410 1.00 19.09 N

ATOM 152 N ASN A 39 7.190 0.682 21.985 1.00 15.33 N

ATOM 153 CA ASN A 39 8.175 0.009 22.841 1.00 15.54 C

ATOM 154 C ASN A 39 8.300 -1.508 22.631 1.00 15.53 C

ATOM 155 O ASN A 39 8.587 -2.241 23.569 1.00 15.78 O

ATOM 156 CB ASN A 39 7.894 0.304 24.330 1.00 15.12 C

ATOM 157 CG ASN A 39 8.211 1.735 24.725 1.00 15.13 C

ATOM 158 ODl ASN A 39 8.963 2.430 24.050 1.00 15.91 O

ATOM 159 ND2 ASN A 39 7.644 2.174 25.847 1.00 15.18 N

ATOM 160 N GLY A 40 8.062 -1.983 21.418 1.00 15.76 N

ATOM 161 CA GLY A 40 8.290 -3.390 21.105 1.00 16.17 C

ATOM 162 C GLY A 40 7.382 -4.390 21.805 1.00 16.49 C

ATOM 163 O GLY A 40 7.698 -5.581 21.866 1.00 16.96 O

ATOM 164 N ARG A 41 6.255 -3.910 22.326 1.00 16.47 N

ATOM 165 CA ARG A 41 5.241 -4.766 22.954 1.00 16.64 C

ATOM 166 C ARG A 41 3.880 -4.078 23.038 1.00 15.39 C

ATOM 167 O ARG A 41 3.739 -2.906 22.707 1.00 15.05 O

ATOM 168 CB ARG A 41 5.685 -5.240 24.351 1.00 16.69 C

ATOM 169 CG ARG A 41 6.053 -4.144 25.350 1.00 17.64 C

ATOM 170 CD ARG A 41 6.395 -4.674 26.760 1.00 19.54 C

ATOM 171 NE ARG A 41 7.220 -5.893 26.718 1.00 26.41 N

ATOM 172 CZ ARG A 41 6.807 -7.117 27.086 1.00 29.82 C

ATOM 173 NHl ARG A 41 5.574 -7.313 27.559 1.00 31.59 N

ATOM 174 NH2 ARG A 41 7.633 -8.157 26.989 1.00 30.88 N

ATOM 175 N TYR A 42 2.881 -4.834 23.476 1.00 14.94 N

ATOM 176 CA TYR A 42 1.546 -4.319 23.708 1.00 14.48 C

ATOM 177 C TYR A 42 1.595 -3.387 24.904 1.00 14.52 C

ATOM 178 O TYR A 42 1.803 -3.845 26.019 1.00 14.60 O

ATOM 179 CB TYR A 42 0.589 -5.470 24.006 1.00 13.93 C

ATOM 180 CG TYR A 42 0.178 -6.305 22.804 1.00 13.19 C

ATOM 181 CDl TYR A 42 0.066 -7.691 22.910 1.00 11.54 C

ATOM 182 CD2 TYR A 42 0.123 -5.711 21.569 1.00 12.49 C

ATOM 183 CEl TYR A 42 0.330 -8.470 21.831 1.00 11.12 C

ATOM 184 CE2 TYR A 42 0.515 -6.489 20.471 1.00 10.96 C

ATOM 185 CZ TYR A 42 0.612 -7.862 20.611 1.00 11.52 C

ATOM 186 OH TYR A 42 0.996 -8.647 19.541 1.00 12.45 O

ATOM 187 N SER A 43 1.419 -2.087 24.673 1.00 14.34 N

ATOM 188 CA SER A 43 1.513 -1.103 25.755 1.00 14.01 C

ATOM 189 C SER A 43 0.672 0.161 25.520 1.00 13.89 C

ATOM 190 O SER A 43 0.902 1.198 26.156 1.00 13.87 O

ATOM 191 CB SER A 43 2.980 -0.727 26.000 1.00 14.49 C

ATOM 192 OG SER A 43 3.603 -0.307 24.795 1.00 15.15 O

ATOM 193 N ILE A 44 0.305 0.071 24.622 1.00 13.08 N

ATOM 194 CA ILE A 44 1.163 1.211 24.312 1.00 12.67 C

ATOM 195 C ILE A 44 2.591 0.935 24.762 1.00 12.45 C

ATOM 196 O ILE A 44 3.149 -0.123 24.469 1.00 13.49 O

ATOM 197 CB ILE A 44 1.106 1.545 22.802 1.00 12.36 C

ATOM 198 CGl ILE A 44 0.344 1.784 22.366 1.00 12.89 C Table 3

ATOM 199 CG2 ILE A 44 -1.964 2.765 22.477 1.00 12.27 C

ATOM 200 CDl ILE A 44 0.539 1.988 20.835 1.00 12.31 C

ATOM 201 N SER A 45 -3.158 1.877 25.509 1.00 12.16 N

ATOM 202 CA SER A 45 -4,567 1.851 25.910 1.00 11.66 C

ATOM 203 C SER A 45 -5.375 2.588 24.848 1.00 11.18 C

ATOM 204 O SER A 45 -4.794 3.274 24.014 1.00 11.41 O

ATOM 205 CB SER A 45 -4.716 2.605 27.217 1.00 11.51 C

ATOM 206 OG SER A 45 -4.459 3.977 26.983 1.00 11.55 O

ATOM 207 N ARG A 46 -6.702 2.492 24.896 1.00 11.15 N

ATOM 208 CA ARG A 46 -7.550 3.229 23.938 1.00 10.97 C

ATOM 209 C ARG A 46 -7.331 4,732 24.005 1.00 11.12 C

ATOM 210 O ARG A 46 -7.344 5.402 22.976 1.00 11.29 O

ATOM 211 CB ARG A 46 -9.040 2.906 24.122 1.00 11.02 C

ATOM 212 CG ARG A 46 -9.948 3.650 23.140 1.00 11.36 C

ATOM 213 CD ARG A 46 -11.411 3.238 23.155 1.00 10.91 C

ATOM 214 NE ARG A 46 -11.585 1.861 22.710 1.00 11.87 N

ATOM 215 CZ ARG A 46 -11.436 1.443 21.448 1.00 14.01 C

ATOM 216 NHl ARG A 46 -11.104 2.298 20.473 1.00 13.02 N

ATOM 217 NH2 ARG A 46 -11.602 0.158 21.165 1.00 12.92 N

ATOM 218 N THR A 47 -7.136 5.273 25.210 1.00 11.07 N

ATOM 219 CA THR A 47 -6.929 6.712 25.350 1.00 11.09 C

ATOM 220 C THR A 47 -5.623 7.129 24.714 1.00 11.21 C

ATOM 221 O THR A 47 -5.569 8.152 24.039 1.00 11.59 O

ATOM 222 CB THR A 47 -6.974 7.182 26.819 1.00 11.03 C

ATOM 223 OGl THR A 47 -6.154 6.329 27.626 1.00 12.67 O

ATOM 224 CG2 THR A 47 -8.361 6.978 27.406 1.00 11.20 C

ATOM 225 N GLO A 48 -4.572 6.337 24.920 1.00 11.28 N

ATOM 226 CA GLO A 48 -3.274 6.673 24.363 1.00 11.43 C

ATOM 227 C GLO A 48 -3.280 6.446 22.856 1.00 11.53 C

ATOM 228 O GLO A 48 -2.580 7.139 22.118 1.00 11.53 O

ATOM 229 CB GLU A 48 -2.142 5.883 25.027 1.00 11.57 C

ATOM 230 CG GLO A 48 -0.765 6.396 24.606 1.00 11.96 C

ATOM 231 CD GLO A 48 0.380 5.839 25.431 1.00 13.92 C

ATOM 232 OEl GLO A 48 0.136 5.328 26.543 1.00 12.68 O

ATOM 233 OE2 GLU A 48 1.543 5.933 24.961 1.00 16.91 O

ATOM 234 N ALA A 49 -4.076 5.473 22.411 1.00 11.30 N

ATOM 235 CA ALA A 49 -4.239 5.218 20.983 1.00 11.02 C

ATOM 236 C ALA A 49 -4.790 6.468 20.307 1.00 10.87 C

ATOM 237 O ALA A 49 -4.240 6.932 19.306 1.00 10.05 O

ATOM 238 CB ALA A 49 -5.159 4.019 20.753 1.00 10.32 C

ATOM 239 N ALA A 50 -5.861 7.023 20.880 1.00 11.23 N

ATOM 240 CA ALA A 50 -6.496 8.222 20.315 1.00 12.09 C

ATOM 241 C ALA A 50 -5.512 9.393 20.294 1.00 12.32 C

ATOM 242 O ALA A 50 -5.425 10.106 19.304 1.00 12.83 O

ATOM 243 CB ALA A 50 -7.779 8.577 21.081 1.00 11.97 C

ATOM 244 N ASP A 51 -4.753 9.555 21.379 1.00 12.94 N

ATOM 245 CA ASP A 51 -3.683 10.552 21.463 1.00 13.48 C

ATOM 246 C ASP A 51 -2.622 10.357 20.382 1.00 13.46 C

ATOM 247 O ASP A 51 -2.171 11.324 19.758 1.00 13.72 O

ATOM 248 CB ASP A 51 -2.993 10.461 22.822 1.00 13.59 C

ATOM 249 CG ASP A 51 -3.766 11.143 23.927 1.00 15.38 C

ATOM 250 ODl ASP A 51 -4.577 12.047 23.639 1.00 16.44 O

ATOM 251 OD2 ASP A 51 -3.604 10.843 25.131 1.00 17.92 O

ATOM 252 N LEU A 52 -2.210 9.106 20.183 1.00 13.39 N

ATOM 253 CA LEU A 52 -1.155 8.788 19.218 1.00 13.59 C

ATOM 254 C LEO A 52 -1.586 9.100 17.788 1.00 13.08 C

ATOM 255 O LEO A 52 -0.833 9.724 17.039 1.00 13.41 O

ATOM 256 CB LEO A 52 -0.730 7.328 19.358 1.00 13.49 C

ATOM 257 CG LEU A 52 0.701 6.870 19.085 1.00 15.90 C

ATOM 258 CDl LEU A 52 1.757 7.959 19.307 1.00 16.55 C

ATOM 259 CD2 LEU A 52 0.981 5.639 19.965 1.00 15.51 C

ATOM 260 N CYS A 53 -2.790 8.676 17.410 1.00 12.32 N

ATOM 261 CA CYS A 53 -3.299 8.981 16.076 1.00 12.38 C

ATOM 262 C CYS A 53 -3.383 10.480 15.849 1.00 12.53 C

ATOM 263 O CYS A 53 -2.960 10.960 14.800 1.00 12.57 O

ATOM 264 CB CYS A 53 -4.638 8.279 15.798 1.00 12.01 C

ATOM 265 SG CYS A 53 -4.479 6.467 15.733 1.00 10.92 S

ATOM 266 N LYS A 54 -3.B88 11.217 16.842 1.00 13.T7 N Table 3

ATOM 267 CA LYS A 54 -3.952 12.692 16.775 1.00 13.84 C

ATOM 268 C LYS A 54 -2.566 13.320 16.610 1.00 13.55 C

ATOM 269 O LYS A 54 -2.402 14.261 15.843 1.00 13.67 O

ATOM 270 CB LYS A 54 -4.655 13.284 18.010 1.00 14.16 C

ATOM 271 CG LYS A 54 -5.083 14.763 17.837 1.00 14.98 C

ATOM 272 CD LYS A 54 -5.918 15.282 19.014 1.00 15.46 C

ATOM 273 CE LYS A 54 -6.512 16.663 18.715 1.00 16.49 C

ATOM 274 NZ LYS A 54 -7.259 16.703 17.400 1.00 18.65 N

ATOM 275 N ALA A 55 -1.572 12.787 17.323 1.00 13.29 N

ATOM 276 CA ALA A 55 -0.182 13.227 17.169 1.00 13.09 C

ATOM 277 C ALA A 55 0.357 12.962 15.756 1.00 12.95 C

ATOM 278 O ALA A 55 1.307 13.609 15.317 1.00 12.53 O

ATOM 279 CB ALA A 55 0.705 12.546 18.218 1.00 13.23 C

ATOM 280 N PHE A 56 -0.247 12.001 15.056 1.00 12.84 N

ATOM 281 CA PHE A 56 0.117 11.700 13.677 1.00 12.73 C

ATOM 282 C PHE A 56 -0.809 12.402 12.671 1.00 13.43 C

ATOM 283 O PHE A 56 -0.838 12.018 11.504 1.00 13.57 O

ATOM 284 CB PHE A 56 0.084 10.176 13.430 1.00 12.50 C

ATOM 285 CG PHE A 56 1.348 9.446 13.841 1.00 11.38 C

ATOM 286 CDl PHE A 56 1.312 8.490 14.858 1.00 10.52 C

ATOM 287 CD2 PHE A 56 2.563 9.693 13.186 1.00 10.95 C

ATOM 288 CEl PHE A 56 2.469 7.796 15.241 1.00 10.29 C

ATOM 289 CE2 PHE A 56 3.730 9.012 13.554 1.00 11.46 C

ATOM 290 CZ PHE A 56 3.687 8.062 14.585 1.00 11.89 C

ATOM 291 N ASN A 57 -1.555 13.422 13.114 1.00 13.87 N

ATOM 292 CA ASN A 57 -2.582 14.085 12.280 1.00 14.44 C

ATOM 293 C ASN A 57 -3.541 13.059 11.648 1.00 14.31 C

ATOM 294 O ASN A 57 -3.934 13.177 10.473 1.00 14.66 O

ATOM 295 CB ASN A 57 -1.937 14.987 11.188 1.00 14.81 C

ATOM 296 CG ASN A 57 -1.233 16.238 11.765 1.00 16.73 C

ATOM 297 ODl ASN A 57 -1.755 16.906 12.666 1.00 18.92 O

ATOM 298 ND2 ASN A 57 -0.052 16.564 11.223 1.00 16.02 N

ATOM 299 N SER A 58 -3.916 12.056 12.442 1.00 13.99 N

ATOM 300 CA SER A 58 -4.687 10.907 11.973 1.00 13.17 C

ATOM 301 C SER A 58 -5.805 10.574 12.955 1.00 13.35 C

ATOM 302 O SER A 58 -5.919 11.201 14.015 1.00 13.71 O

ATOM 303 CB SER A 58 -3.769 9.682 11.810 1.00 12.57 C

ATOM 304 OG SER A 58 -2.794 9.912 10.807 1.00 12.43 O

ATOM 305 N THR A 59 -6.626 9.588 12.605 1.00 12.79 N

ATOM 306 CA THR A 59 -7.734 9.172 13.456 1.00 12.88 C

ATOM 307 C THR A 59 -7.741 7.662 13.619 1.00 12.80 C

ATOM 308 O THR A 59 -7.069 6.948 12.872 1.00 13.54 O

ATOM 309 CB THR A 59 -9.070 9.630 12.857 1.00 12.87 C

ATOM 310 OGl THR A 59 -9.175 9.156 11.506 1.00 12.67 O

ATOM 311 CG2 THR A 59 -9.126 11.172 12.735 1.00 13.32 C

ATOM 312 N LEO A 60 -8.497 7.175 14.596 1.00 12.01 N

ATOM 313 CA LED A 60 -8.713 5.743 14.737 1.00 11.19 C

ATOM 314 C LEU A 60 -9.562 5.274 13.564 1.00 10.57 C

ATOM 315 O LEU A 60 -10.620 5.841 13.313 1.00 9.84 O

ATOM 316 CB LEU A 60 -9.388 5.414 16.076 1.00 10.86 C

ATOM 317 CG LEO A 60 -8.524 5.575 17.347 1.00 12.00 C

ATOM 318 CDl LEO A 60 -9.373 5.639 18.626 1.00 9.68 C

ATOM 319 CD2 LEO A 60 -1.ill 4.465 17.475 1.00 10.05 C

ATOM 320 N PRO A 61 -9.098 4.249 12.841 1.00 10.33 N

ATOM 321 CA PRO A 61 -9.797 3.774 11.647 1.00 10.09 C

ATOM 322 C PRO A 61 -11.185 3.221 11.934 1.00 10.06 C

ATOM 323 O PRO A 61 -11.454 2.703 13.015 1.00 9.91 O

ATOM 324 CB PRO A 61 -8.892 2.633 11.134 1.00 9.96 C

ATOM 325 CG PRO A 61 -7.558 2.927 11.707 1.00 10.26 C

ATOM 326 CD PRO A 61 -7.880 3.459 13.101 1.00 10.21 C

ATOM 327 N THR A 62 -12.061 3.340 10.951 1.00 10.34 N

ATOM 328 CA THR A 62 -13.325 2.621 10.981 1.00 10.49 C

ATOM 329 C THR A 62 -13.102 1.241 10.375 1.00 10.63 C

ATOM 330 O THR A 62 -12.081 1.006 9.709 1.00 10.58 O

ATOM 331 CB THR A 62 -14.386 3.357 10.153 1.00 10.16 C

ATOM 332 OGl THR A 62 -13.935 3.421 8.805 1.00 10.14 O

ATOM 333 CG2 THR A 62 -14.499 4.816 10.566 1.00 9.35 C

HETATM 334 N MSE A 63 -14.059 0.341 10.601 1.00 10.47 N Table 3

HETATM 335 CA MSE A 63 14.065 -0.971 9.960 1.00 10.85 C

HETATM 336 C MSE A 63 13.971 -0.866 8.432 1.00 10.37 C

HETATM 337 O MSE A 63 13.266 -1.659 7.806 1.00 9.97 O

HETATM 338 CB MSE A 63 15.304 -1.784 10.375 1.00 11.00 C

HETATM 339 CG MSE A 63 15.246 -2.338 11.785 1.00 14.22 C

HETATM 340 SE MSE A 63 13.842 -3.695 12.028 1.00 26.63 SE

HETATM 341 CE MSE A 63 14.663 -5.142 10.838 1.00 20.32 C

ATOM 342 N ALA A 64 14.664 0.115 7.839 1.00 10.23 N

ATOM 343 CA ALA A 64 14.631 0,325 6.380 1.00 10.23 C

ATOM 344 C ALA A 64 13.250 0.720 5.869 1.00 10.41 C

ATOM 345 O ALA A 64 12.804 0.261 4.805 1.00 10.36 O

ATOM 346 CB ALA A 64 15.675 1.362 5.943 1.00 10.32 C

ATOM 347 N GLN A 65 12.578 1.584 6.622 1.00 10.55 N

ATOM 348 CA GLN A 65 11.212 1.984 6.309 1.00 10.59 C

ATOM 349 C GLN A 65 10.223 0.813 6.400 1.00 10.57 C

ATOM 350 O GLN A 65 -9.353 0.674 5.545 1.00 10.22 O

ATOM 351 CB GLN A 65 10.791 3.153 7.188 1.00 10.83 C

ATOM 352 CG GLN A 65 11.450 4.477 6.743 1.00 11.00 C

ATOM 353 CD GLN A 65 11.417 5.549 7.817 1.00 9.76 C

ATOM 354 OEl GLN A 65 10.989 5.291 8.953 1.00 9.96 O

ATOM 355 NE2 GLN A 65 11.880 6.752 7.470 1.00 8.14 N

HETATM 356 N MSE A 66 10.402 -0.051 7.397 1.00 10.40 N

HETATM 357 CA MSE A 66 -9.566 -1.236 7.535 1.00 10.92 C

HETATM 358 C MSE A 66 -9.738 -2.201 6.356 1.00 10.60 C

HETATM 359 O MSE A 66 -8.762 -2.756 5.858 1.00 10.42 O

HETATM 360 CB MSE A 66 -9.872 -1.970 8.844 1.00 11.30 C

HETATM 361 CG MSE A 66 -9.605 -1.171 10.094 1.00 13.13 C

HETATM 362 SE MSE A 66 -7.701 -0.821 10.316 1.00 25.09 SE

HETATM 363 CE MSE A 66 -7.033 -2.691 10.225 1.00 16.42 C

ATOM 364 N GLU A 67 10.979 -2.407 5.927 1.00 10.55 N

ATOM 365 CA GLU A 67 11.260 -3.309 4.805 1.00 10.67 C

ATOM 366 C GLU A 67 10.624 -2.806 3.503 1.00 10.42 C

ATOM 367 O GLU A 67 10.152 -3.601 2.697 1.00 10.50 O

ATOM 368 CB GLU A 67 12.771 -3.515 4.626 1.00 10.64 C

ATOM 369 CG GLU A 67 13.468 -4.197 5.804 1.00 12.47 C

ATOM 370 CD GLU A 67 13.337 -5.724 5.795 1.00 16.18 C

ATOM 371 OEl GLU A 67 12.551 -6.294 4.985 1.00 15.33 O

ATOM 372 OE2 GLU A 67 14.045 -6.371 6.605 1.00 18.58 O

ATOM 373 N LYS A 68 10.610 -1.489 3.303 1.00 10.49 N

ATOM 374 CA LYS A 68 -9.995 -0.908 2.119 1.00 10.91 C

ATOM 375 C LYS A 68 -8.461 -1.132 2.124 1.00 11.00 C

ATOM 376 O LYS A 68 -7.883 -1.493 1.103 1.00 11.10 O

ATOM 377 CB LYS A 68 10.383 0.568 1.967 1.00 11.04 C

ATOM 378 CG LYS A 68 -9.846 1.270 0.689 1.00 11.48 C

ATOM 379 CD LYS A 68 10.541 2.638 0.479 1.00 12.16 C

ATOM 380 CE LYS A 68 10.129 3.283 -0.849 1.00 14.62 C

ATOM 381 NZ LYS A 68 10.781 4.617 -1.078 1.00 17.50 N

ATOM 382 N ALA A 69 -7.818 -0.943 3.275 1.00 10.93 N

ATOM 383 CA ALA A 69 -6.376 -1.194 3.399 1.00 11.14 C

ATOM 384 C ALA A 69 -6.041 -2.673 3.159 1.00 10.92 C

ATOM 385 O ALA A 69 -5.107 -2.997 2.443 1.00 11.14 O

ATOM 386 CB ALA A 69 -5.876 -0.751 4.787 1.00 10.67 C

ATOM 387 N LEU A 70 -6.821 -3.552 3.773 1.00 10.97 N

ATOM 388 CA LEU A 70 -6.705 -5.005 3.625 1.00 11.03 C

ATOM 389 C LEU A 70 -6.642 -5.413 2.148 1.00 10.84 C

ATOM 390 O LEU A 70 -5.849 -6.281 1.773 1.00 10.21 O

ATOM 391 CB LEU A 70 -7.923 -5.648 4.295 1.00 11.10 C

ATOM 392 CG LEU A 70 -8.013 -6.940 5.142 1.00 12.69 C

ATOM 393 CDl LEU A 70 -8.861 -7.971 4.480 1.00 12.49 C

ATOM 394 CD2 LEU A 70 -6.690 -7.532 5.615 1.00 12.85 C

ATOM 395 N SER A 71 -7.482 -4.773 1.327 1.00 10.50 N

ATOM 396 CA SER A 71 -7.630 -5.114 -0.098 1.00 10.63 C

ATOM 397 C SER A 71 -6.385 -4.793 -0.936 1.00 10.48 C

ATOM 398 O SER A 71 -6.266 -5.251 -2.076 1.00 10.70 O

ATOM 399 CB SER A 71 -8.872 -4.438 -0.699 1.00 10.14 C

ATOM 400 OG SER A 71 -8.643 -3.061 -0.981 1.00 9.86 O

ATOM 401 N ILE A 72 -5.479 -3.994 -0.373 1.00 10.28 N

ATOM 402 CA ILE A 72 -4.195 -3.722 -1.017 1.00 10.15 C Table 3

ATOM 403 C ILE A 72 021 -4.245 -0.188 1.00 10.37 C

ATOM 404 O ILE A 72 903 -3.741 -0.287 1.00 10.35 O

ATOM 405 CB ILE A 72 028 -2.218 -1.420 1.00 10.50 C

ATOM 406 CGl ILE A 72 276 -1.278 -0.227 1.00 10.13 C

ATOM 407 CG2 ILE A 72 953 -1.852 -2.624 00 9.92 C

ATOM 408 CDl ILE A 72 780 0.178 -0.470 00 9.77 C

ATOM 409 N GLY A 73 -3.279 -5.263 0.625 1.00 10.10 N

ATOM 410 CA GLY A 73 ^■2.189 -6.057 .192 1.00 10.43 C

ATOM 411 C GLY A 73 ^■1.785 -5.731 .618 1.00 10.67 C

ATOM 412 O GLY A 73 0.712 -6.152 .071 1.00 10.07 O

ATOM 413 N PHE A 74 ^■2.633 -4.977 ,320 1.00 10.86 N

ATOM 414 CA PHE A 74 ^■2.358 -4.596 .705 1.00 11.23 C

ATOM 415 C PHE A 74 2.792 -5.723 605 1.00 11.78 C

ATOM 416 O PHE A 74 3.981 -6.024 698 1.00 11.58 O

ATOM 417 CB PHE A 74 ^■3.104 -3.312 093 1.00 11.24 C

ATOM 418 CG PHE A 74 ^■2.737 -2.774 6.464 1.00 10.63 C

ATOM 419 CDl PHE A 74 1.447 -2. .358 6.738 .00 9.14 C

ATOM 420 CD2 PHE A 74 3.698 -2.676 7.472 .00 9.89 C

ATOM 421 CEl PHE A 74 ^■1.107 -1.851 8.004 1.00 10.04 C

ATOM 422 CE2 PHE A 74 ^■3.376 -2.169 8.743 1 .00 8.56 C

ATOM 423 CZ PHE A 74 2.071 -1 ,753 9.004 1, ,00 9.57 C

ATOM 424 N GLO A 75 ^■1.815 -6.377 6.226 1.00 12.44 N

ATOM 425 CA GLU A 75 -2 087 -7. .363 7.253 1.00 13.14 C

ATOM 426 C GLU A 75 0.977 -7..328 8.299 1.00 13.44 C

ATOM 427 O GLU A 75 0.173 -6.969 8.005 1.00 13.65 O

ATOM 428 CB GLU A 75 2.294 -8.780 6.674 1.00 12.98 C

ATOM 429 CG GLU A 75 -1 036 -9.513 6.247 1.00 13.06 C

ATOM 430 CD GLU A 75 -1.295 -10.911 5.678 1.00 14.46 C

ATOM 431 OEl GLU A 75 -0 477 -11.333 4.830 1.00 17.14 O

ATOM 432 OE2 GLU A 75 ^■2.283 -11.599 6.053 1.00 14.16 O

ATOM 433 N THR A 76 1.347 -7, .713 9.511 1.00 13.43 N

ATOM 434 CA THR A 76 ^■0.458 -7..719 10.654 1.00 14.05 C

ATOM 435 C THR A 76 ■0.735 -9..018 11 410 1.00 13.33 C

ATOM 436 O THR A 76 -1 652 -9.762 11 041 1.00 11.59 O

ATOM 437 CB THR A 76 ^■0.794 -6.504 11.540 1.00 14.35 C

ATOM 438 OGl THR A 76 ■0.497 -5.299 10.813 1.00 15.96 O

ATOM 439 CG2 THR A 76 0.157 -6.411 12.691 1.00 17.27 C

ATOM 440 N CYS A 77 0.047 -9.264 12.465 1.00 12.89 N

ATOM 441 CA CYS A 77 ^■0.253 -10.302 13.433 1.00 13.19 C

ATOM 442 C CYS A 77 •0.367 -9.714 14.837 1.00 13.70 C

ATOM 443 O CYS A 77 •0.099 -10.396 15.829 1.00 13.58 O

ATOM 444 CB CYS A 77 0.818 -11.402 13.413 1.00 13.30 C

ATOM 445 SG CYS A 77 0.323 -12.910 14.285 1.00 13.05 S

ATOM 446 N ARG A 78 ^■0.785 -8.455 14.920 1.00 13.82 N

ATOM 447 CA ARG A 78 ^■0.854 -7.750 16.194 1.00 14.18 C

ATOM 448 C ARG A 78 2.188 -7.040 16.398 1.00 13.70 C

ATOM 449 O ARG A 78 2.662 -6.326 15.511 1.00 13.12 O

ATOM 450 CB ARG A 78 0.314 -6.762 16.327 1.00 15.09 C

ATOM 451 CG ARG A 78 650 -7.447 16.696 1.00 15.84 C

ATOM 452 CD ARG A 78 .459 -6.657 17.698 1.00 21.01 C

ATOM 453 NE ARG A 78 .842 -7.486 18.841 1.00 24.17 N

ATOM 454 CZ ARG A 78 .087 -7.016 20.053 1.00 25.41 C

ATOM 455 NHl ARG A 78 .987 -5.706 20.299 1.00 23.13 N

ATOM 456 NH2 ARG A 78 .426 -7.860 21.030 1.00 27.01 N

ATOM 457 N TYR A 79 -2.791 -7.256 17.565 1.00 13.38 N

ATOM 458 CA TYR A 79 -4.022 -6.566 17.951 1.00 13.48 C

ATOM 459 C TYR A 79 -3 804 -5.077 18.074 1.00 12.98 C

ATOM 460 O TYR A 79 -2.803 -4.638 18.644 1.00 13.24 O

ATOM 461 CB TYR A 79 -4.574 -7.125 19.267 1.00 14.55 C

ATOM 462 CG TYR A 79 -5.135 -8.506 19.085 1.00 15.55 C

ATOM 463 CDl TYR A 79 -4.517 -9.613 19.652 1.00 15.93 C

ATOM 464 CD2 TYR A 79 -6.270 -8.703 18.305 1.00 17.52 C

ATOM 465 CEl TYR A 79 5.029 -10.893 19.456 1.00 17.01 C

ATOM 466 CE2 TYR A 79 6.786 -9.969 18.095 1.00 17.72 C

ATOM 467 CZ TYR A 79 6.163 -11.056 18.673 1.00 17.08 C

ATOM 468 OH TYR A 79 6.696 -12.306 18.454 1.00 18.59 O

ATOM 469 N GLY A 80 -4.741 -4.296 17.547 1.00 12.39 N

ATOM 470 CA GLY A 80 -4.623 -2.837 17.633 1.00 11.70 C Table 3

ATOM 471 C GLY A 80 -5.983 -2.169 17.655 1.00 11.33 C

ATOM 472 O GLY A 80 -6.915 -2.638 17.007 1.00 10.47 O

ATOM 473 N PHE A 81 -6.096 -1.077 18.413 1.00 10.60 N

ATOM 474 CA PHE A 81 -7.346 -0.322 18.475 1.00 10.23 C

ATOM 475 C PHE A 81 -7.715 0.285 17.124 1.00 10.09 C

ATOM 476 O PHE A 81 -6.857 0.762 16.376 1.00 9.38 O

ATOM 477 CB PHE A 81 -7.251 0.805 19.512 1.00 10.33 C

ATOM 478 CG PHE A 81 -7.099 0.318 20.905 1.00 9.93 C

ATOM 479 CDl PHE A 81 -5.842 0.233 21.488 1.00 10.64 C

ATOM 480 CD2 PHE A 81 -8.215 -0.060 21.643 1.00 10.97 C

ATOM 481 CEl PHE A 81 -5.691 -0.241 22.787 1.00 9.97 C

ATOM 482 CE2 PHE A 81 -8.078 -0.540 22.949 1.00 10.81 C

ATOM 483 CZ PHE A 81 -6.810 -0.627 23.516 1.00 10.33 C

ATOM 484 N ILE A 82 -8.999 0.227 16.817 1.00 9.79 N

ATOM 485 CA ILE A 82 -9.581 1.072 15.803 1.00 9.76 C

ATOM 486 C ILE A 82 -10.714 1.757 16.539 1.00 10.21 C

ATOM 487 O ILE A 82 -10.814 1.608 17.760 1.00 10.10 O

ATOM 488 CB ILE A 82 -10.074 0.247 14.569 1.00 9.71 C

ATOM 489 CGl ILE A 82 -11.108 -0.804 14.972 1.00 9.05 C

ATOM 490 CG2 ILE A 82 -8.877 -0.390 13.833 1.00 9.08 C

ATOM 491 CDl ILE A 82 -11.948 -1.316 13.792 1.00 10.12 C

ATOM 492 N GLU A 83 -11.559 2.501 15.825 1.00 10.66 N

ATOM 493 CA GLU A 83 -12.721 3.107 16.441 1.00 11.29 C

ATOM 494 C GLU A 83 -13.651 2.019 16.964 1.00 11.22 C

ATOM 495 O GLU A 83 -14.136 1.201 16.185 1.00 11.11 O

ATOM 496 CB GLD A 83 -13.463 4.018 15.453 1.00 11.69 C

ATOM 497 CG GLϋ A 83 -14.649 4.726 16.087 1.00 12.67 C

ATOM 498 CD GLϋ A 83 -15.392 5.614 15.119 1.00 16.10 C

ATOM 499 OEl GLU A 83 -16.647 5.558 15.126 1.00 16.49 O

ATOM 500 OE2 GLU A 83 -14.726 6.361 14.358 1.00 16.95 O

ATOM 501 N GLY A 84 -13.865 1.999 18.286 1.00 11.34 N

ATOM 502 CA GLY A 84 -14.805 1.055 18.919 1.00 11.50 C

ATOM 503 C GLY A 84 -14.475 -0.434 18.932 1.00 11.87 C

ATOM 504 O GLY A 84 -15.289 -1.248 19.393 1.00 11.90 O

ATOM 505 N HIS A 85 -13.302 -0.809 18.425 1.00 11.55 N

ATOM 506 CA HIS A 85 -12.872 -2.220 18.431 1.00 11.74 C

ATOM 507 C HIS A 85 -11.371 -2.362 18.595 1.00 11.39 C

ATOM 508 O HIS A 85 -10.635 -1.374 18.630 1.00 11.13 O

ATOM 509 CB HIS A 85 -13.263 -2.959 17.142 1.00 11.94 C

ATOM 510 CG HIS A 85 -14.654 -2.676 16.673 1.00 13.12 C

ATOM 511 NDl HIS A 85 -15.761 -3.296 17.208 1.00 13.96 N

ATOM 512 CD2 HIS A 85 -15.116 -1.824 15.728 1.00 14.41 C

ATOM 513 CEl HIS A 85 -16.847 -2.838 16.610 1.00 15.86 C

ATOM 514 NE2 HIS A 85 -16.483 -1.946 15.706 1.00 16.20 N

ATOM 515 N VAL A 86 -10.949 -3.617 18.708 1.00 11.39 N

ATOM 516 CA VAL A 86 -9.548 -4.020 18.677 1.00 11.63 C

ATOM 517 C VAL A 86 -9.472 -5.141 17.659 1.00 11.20 C

ATOM 518 O VAL A 85 -10.228 -6.110 17.753 1.00 11.90 O

ATOM 519 CB VAL A 86 -9.090 -4.543 20.059 1.00 11.78 C

ATOM 520 CGl VAL A 86 -7.731 -5.258 19.959 1.00 12.35 C

ATOM 521 CG2 VAL A 86 -9.068 -3.413 21.059 1.00 11.68 C

ATOM 522 N VAL A 87 -8.575 -5.016 16.684 1.00 10.86 N

ATOM 523 CA VAL A 87 -8.576 -5.913 15.524 1.00 9.88 C

ATOM 524 C VAL A 87 -7.190 -6.343 15.058 1.00 10.26 C

ATOM 525 O VAL A 87 -6.166 -5.775 15.480 1.00 10.16 O

ATOM 526 CB VAL A 87 -9.329 -5.271 14.293 1.00 9.99 C

ATOM 527 CGl VAL A 87 -10.774 -4.894 14.649 1.00 9.16 C

ATOM 528 CG2 VAL A 87 -8.569 -4.054 13.733 1.00 9.13 C

ATOM 529 N ILE A 88 -7.187 -7.356 14.188 1.00 10.05 N

ATOM 530 CA ILE A 88 -6.050 -7.725 13.352 1.00 10.38 C

ATOM 531 C ILE A 88 -6.560 -7.908 11.920 1.00 10.23 C

ATOM 532 O ILE A 88 -7.458 -8.711 11.699 1.00 10.30 O

ATOM 533 CB ILE A 88 -5.409 -9.074 13.816 1.00 10.45 C

ATOM 534 CGl ILE A 88 -4.908 -8.994 15.266 1.00 11.21 C

ATOM 535 CG2 ILE A 88 -4.265 -9.438 12.885 1.00 10.94 C

ATOM 536 CDl ILE A 88 -4.132 -10.208 15.769 1.00 10.38 C

ATOM 537 N PRO A 89 -6.000 -7.189 10.947 1.00 10.27 N

ATOM 538 CA PRO A 89 -6.344 -7.432 9.557 1.00 10.01 C Table 3

ATOM 539 C PRO A 89 5.547 -8.644 9.034 1.00 10.48 C

ATOM 540 O PRO A 89 4.324 -8.716 9.256 1.00 10.12 O

ATOM 541 CB PRO A 89 5.916 -6.132 8.857 1.00 .10.25 C

ATOM 542 CG PRO A 89 4.778 -5.583 9.699 1.00 10.43 C

ATOM 543 CD PRO A 89 4.987 -6.120 11.094 1.00 10.08 C

ATOM 544 N ARG A 90 6.239 -9.597 8.394 1.00 10.20 N

ATOM 545 CA ARG A 90 5.611 -10.833 7.906 1.00 10.70 C

ATOM 546 C ARG A 90 5.995 -11.143 6.456 1.00 11.38 C

ATOM 547 O ARG A 90 7.182 -11.213 6.119 1.00 11.09 O

ATOM 548 CB ARG A 90 5.968 -12.031 8.802 1.00 10.34 C

ATOM 549 CG ARG A 90 5.410 -11.993 10.226 1.00 9.84 C

ATOM 550 CD ARG A 90 3.870 -11.879 10.324 1.00 10.14 C

ATOM 551 NE ARG A 90 3.197 -12.972 9.634 1.00 9.87 N

ATOM 552 CZ ARG A 90 1.901 -13.013 9.358 1.00 11.73 C

ATOM 553 NHl ARG A 90 1.088 -12.012 9.708 1.00 10.29 N

ATOM 554 NH2 ARG A 90 1.413 -14.067 8.720 1.00 13.27 N

ATOM 555 N ILE A 91 4.983 -11.308 5.607 1.00 12.28 N

ATOM 556 CA ILE A 91 5.185 -11.737 4.219 1.00 13.03 C

ATOM 557 C ILE A 91 4.943 -13.235 4.100 1.00 14.02 C

ATOM 558 O ILE A 91 5.720 -13.943 3.455 1.00 13.70 O

ATOM 559 CB ILE A 91 4.275 -10.948 3.246 1.00 12.73 C

ATOM 560 CGl ILE A 91 4.632 -9.456 3.280 1.00 12.48 C

ATOM 561 CG2 ILE A 91 4.393 -11.504 1.813 1.00 12.64 C

ATOM 562 CDl ILE A 91 3.490 -8.542 2.929 1.00 10.73 C

ATOM 563 N HIS A 92 3.879 -13.709 4.752 1.00 15.01 N

ATOM 564 CA HIS A 92 3.518 -15.127 4.738 1.00 16.19 C

ATOM 565 C HIS A 92 3.720 -15.754 6.124 1.00 17.32 C

ATOM 566 O HIS A 92 3.258 -15.202 7.129 1.00 17.58 O

ATOM 567 CB HIS A 92 2.066 -15.307 4.277 1.00 16.06 C

ATOM 568 CG HIS A 92 1.684 -14.441 3.109 1.00 15.94 C

ATOM 569 NDl HIS A 92 1.720 -14.887 1.803 1.00 15.75 N

ATOM 570 CD2 HIS A 92 1.260 -13.156 3.054 1.00 16.03 C

ATOM 571 CEl HIS A 92 1.339 -13.913 0.996 1.00 16.34 C

ATOM 572 NE2 HIS A 92 1.054 -12.851 1.731 1.00 17.37 N

ATOM 573 N PRO A 93 4.394 -16.907 6.188 1.00 18.27 N

ATOM 574 CA PRO A 93 4.570 -17.608 7.454 1.00 19.06 C

ATOM 575 C PRO A 93 3.218 -18.026 8.003 1.00 19.63 C

ATOM 576 O PRO A 93 2.410 -18.594 7.274 1.00 19.76 O

ATOM 577 CB PRO A 93 5.362 -18.869 7.068 1.00 18.88 C

ATOM 573 CG PRO A 93 5.923 -18.590 5.739 1.00 18.73 C

ATOM 579 CD PRO A 93 4.997 -17.642 5.064 1.00 18.15 C

ATOM 580 N ASN A 94 2.963 -17.701 9.263 1.00 20.46 N

ATOM 581 CA ASN A 94 1.864 -18.313 10.007 1.00 21.15 C

ATOM 582 C ASN A 94 2.410 -18.701 11.366 1.00 21.18 C

ATOM 583 O ASN A 94 3.083 -17.894 12.018 1.00 20.82 O

ATOM 584 CB ASN A 94 0.671 -17.360 10.155 1.00 21.48 C

ATOM 585 CG ASN A 94 0.605 -18.081 10.593 1.00 23.26 C

ATOM 586 ODl ASN A 94 0.702 -18.575 11.723 1.00 24.43 O

ATOM 587 ND2 ASN A 94 1.583 -18.157 9.691 1.00 24.51 N

ATOM 588 N SER A 95 2.126 -19.930 11.796 1.00 21.42 N

ATOM 589 CA SER A 95 2.684 -20.422 13.056 1.00 21.85 C

ATOM 590 C SER A 95 2.174 -19.654 14.277 1.00 21.41 C

ATOM 591 O SER A 95 2.813 -19.632 15.323 1.00 21.71 O

ATOM 592 CB SER A 95 2.494 -21.937 13.202 1.00 22.08 C

ATOM 593 OG SER A 95 1.134 -22.284 13.330 1.00 24.16 O

ATOM 594 N ILE A 96 1.038 -18.988 14.111 1.00 21.12 N

ATOM 595 CA ILE A 96 0.439 -18.171 15.160 1.00 20.85 C

ATOM 596 C ILE A 96 1.062 -16.755 15.221 1.00 19.83 C

ATOM 597 O ILE A 96 0.783 -15.991 16.143 1.00 19.91 O

ATOM 598 CB ILE A 96 1.121 -18.152 14.951 1.00 21.35 C

ATOM 599 CGl ILE A 96 1.834 -19.100 15.931 1.00 22.42 C

ATOM 600 CG2 ILE A 96 1.702 -16.754 15.005 1.00 22.65 C

ATOM 601 CDl ILE A 96 1.643 -18.780 17.414 1.00 23.45 C

ATOM 602 N CYS A 97 1.929 -16.430 14.252 1.00 18.39 N

ATOM 603 CA CYS A 97 2.513 -15.082 14.122 1.00 16.68 C

ATOM 604 C CYS A 97 4.032 -15.103 14.031 1.00 15.98 C

ATOM 605 O CYS A 97 4.598 -15.760 13.154 1.00 15.57 O

ATOM 606 CB CYS A 97 1.951 -14.372 12.876 1.00 16.42 C Table 3

ATOM 607 SG CYS A 97 -0.157 -14.270 12.836 1.00 15.01 S

ATOM 608 N ALA A 98 -4.680 -14.369 14.932 1.00 15.29 N

ATOM 609 CA ALA A 98 -6.125 -14.167 14.907 1.00 14.69 C

ATOM 610 C ALA A 98 -6.895 -15.490 14.781 1.00 14.55 C

ATOM 611 O ALA A 98 -7.867 -15.588 14.033 1.00 14.01 O

ATOM 612 CB ALA A 98 -6.502 -13.200 13.764 1.00 14.58 C

ATOM 613 N ALA A 99 -6.442 -16.518 15.498 1.00 14.21 N

ATOM 614 CA ALA A 99 -7.164 -17.791 15.545 1.00 14.31 C

ATOM 615 C ALA A 99 -7.283 -18.416 14.155 1.00 14.51 C

ATOM 616 O ALA A 99 -8.261 -19.089 13.868 1.00 14.63 O

ATOM 617 CB ALA A 99 -8.571 -17.594 16.174 1.00 13.76 C

ATOM 618 N ASN A 100 -6.294 -18.168 13.292 1.00 14.46 N

ATOM 619 CA ASN A 100 -6.294 -18.680 11.923 1.00 14.90 C

ATOM 620 C ASN A 100 -7.312 -17.989 11.009 1.00 14.83 C

ATOM 621 O ASN A 100 -7.514 -18.402 9.867 1.00 15.02 O

ATOM 622 CB ASN A 100 -6.519 -20.203 11.910 1.00 15.00 C

ATOM 623 CG ASN A 100 -6.024 -20.857 10.643 1.00 16.42 C

ATOM 624 ODl ASN A 100 -6.718 -21.690 10.051 1.00 18.50 O

ATOM 625 ND2 ASN A 100 -4.817 -20.486 10.211 1.00 15.59 N

ATOM 626 N ASN A 101 -7.951 -16.939 11.502 1.00 14.69 N

ATOM 627 CA ASN A 101 -8.972 -16.256 10.703 1.00 15.11 C

ATOM 628 C ASN A 101 -8.409 -15.370 9.614 1.00 14.79 C

ATOM 629 O ASN A 101 -7.226 -15.011 9.620 1.00 14.44 O

ATOM 630 CB ASN A 101 -9.921 -15.444 11.574 1.00 14.76 C

ATOM 631 CG ASN A 101 -10.885 -16.321 12.341 1.00 16.62 C

ATOM 632 ODl ASN A 101 -11.715 -17.028 11.751 1.00 17.14 O

ATOM 633 ND2 ASN A 101 -10.783 -16.282 13.663 1.00 16.06 N

ATOM 634 N THR A 102 -9.290 -15.029 8.685 1.00 14.93 N

ATOM 635 CA THR A 102 -8.983 -14.128 7.593 1.00 15.48 C

ATOM 636 C THR A 102 -9.992 -12.972 7.676 1.00 15.28 C

ATOM 637 O THR A 102 -11.068 -13.124 8.277 1.00 14.64 O

ATOM 638 CB THR A 102 -9.030 -14.940 6.264 1.00 16.02 C

ATOM 639 OGl THR A 102 -8.175 -14.353 5.279 1.00 19.99 O

ATOM 640 CG2 THR A 102 -10.392 -14.942 5.632 1.00 15.14 C

ATOM 641 N GLY A 103 -9.639 -11.821 7.103 1.00 15.03 N

ATOM 642 CA GLY A 103 -10.478 -10.627 7.163 1.00 14.48 C

ATOM 643 C GLY A 103 -10.074 -9.693 8.290 1.00 14.26 C

ATOM 644 O GLY A 103 -8.960 -9.773 8.799 1.00 14.26 O

ATOM 645 N VAL A 104 -10.971 -8.792 8.674 1.00 14.83 N

ATOM 646 CA VAL A 104 -10.705 -7.884 9.792 1.00 15.38 C

ATOM 647 C VAL A 104 -11.267 -8.478 11.066 1.00 16.14 C

ATOM 648 O VAL A 104 -12.447 -8.285 11.422 1.00 16.11 O

ATOM 649 CB VAL A 104 -11.206 -6.432 9.548 1.00 15.75 C

ATOM 650 CGl VAL A 104 -10.781 -5.518 10.701 1.00 15.35 C

ATOM 651 CG2 VAL A 104 -10.661 -5.889 8.224 1.00 15.41 C

ATOM 652 N TYR A 105 -10.404 -9.234 11.736 1.00 16.76 N

ATOM 653 CA TYR A 105 -10.788 -10.013 12.898 1.00 17.88 C

ATOM 654 C TYR A 105 -10.938 -9.163 14.161 1.00 18.24 C

ATOM 655 O TYR A 105 -10.005 -8.489 14.570 1.00 17.54 O

ATOM 656 CB TYR A 105 -9.767 -11.128 13.113 1.00 18.43 C

ATOM 657 CG TYR A 105 -10.029 -11.968 14.333 1.00 19.89 C

ATOM 658 CDl TYR A 105 -11.095 -12.882 14.368 1.00 20.16 C

ATOM 659 CD2 TYR A 105 -9.214 -11.853 15.456 1.00 19.59 C

ATOM 660 CEl TYR A 105 -11.326 -13.660 15.499 1.00 21.68 C

ATOM 661 CE2 TYR A 105 -9.435 -12.618 16.582 1.00 21.46 C

ATOM 662 CZ TYR A 105 -10.488 -13.518 16.606 1.00 21.06 C

ATOM 663 OH TYR A 105 -10.683 -14.278 17.741 1.00 22.67 O

ATOM 664 N ILE A 106 -12.118 -9.222 14.775 1.00 19.25 N

ATOM 665 CA ILE A 106 -12.429 -8.421 15.962 1.00 20.40 C

ATOM 666 C ILE A 106 -12.244 -9.244 17.240 1.00 21.24 C

ATOM 667 O ILE A 106 -12.894 -10.274 17.426 1.00 21.19 O

ATOM 668 CB ILE A 106 -13.885 -7.848 15.882 1.00 20.46 C

ATOM 669 CGl ILE A 106 -14.068 -6.995 14.619 1.00 20.14 C

ATOM 670 CG2 ILE A 106 -14.240 -7.071 17.172 1.00 19.60 C

ATOM 671 CDl ILE A 106 -15.517 -6.690 14.277 1.00 20.10 C

ATOM 672 N LEU A 107 -11.356 -8.784 18.111 1.00 22.65 N

ATOM 673 CA LEU A 107 -11.149 -9.420 19.399 1.00 24.29 C

ATOM 674 C LEU A 107 -12.263 -9.001 20.350 1.00 26.07 C Table 3

ATOM 675 O LEU A 107 -12.652 -7.826 20.399 00 25.70 O

ATOM 676 CB LEO A 107 -9.789 -9.022 19.980 00 24.26 C

ATOM 677 CG LEU A 107 -9.335 -9.651 21.303 00 23.83 C

ATOM 678 CDl LEU A 107 -9.152 -11.151 21.149 00 25.26 C

ATOM 679 CD2 LEU A 107 -8.050 -9.011 21.790 00 24.17 C

ATOM 680 N THR A 108 -12.769 -9.973 21.099 00 28.32 N

ATOM 681 CA THR A 108 -13.813 -9.743 22.090 00 30.93 C

ATOM 682 C THR A 108 -13.290 -8.951 23.283 00 32.25 C

ATOM 633 O THR A 108 -13.753 -7.834 23.538 00 32.90 O

ATOM 684 CB THR A 108 -14.401 -11.094 22.555 00 30.95 C

ATOM 685 OGl THR A 108 -15.162 -11.668 21.486 00 32.35 O

ATOM 686 CG2 THR A 108 -15.439 -10.902 23.672 00 31.66 C

ATOM 687 N SER A 109 -12.310 -9.532 23.982 00 34.06 N

ATOM 688 CA SER A 109 -11.908 -9.119 25.343 00 35.65 C

ATOM 689 C SER A 109 -10.810 -8.051 25.358 00 36.40 C

ATOM 690 O SER A 109 -9.616 -8.362 25.505 00 36.27 O

ATOM 691 CB SER A 109 -11.458 -10.350 26.132 00 35.88 C

ATOM 692 OG SER A 109 -10.696 -11.218 25.302 00 36.48 O

ATOM 693 N ASN A 110 -11.230 -6.789 25.225 00 37.24 N

ATOM 694 CA ASN A 110 -10.310 -5.720 24.811 00 37.38 C

ATOM 695 C ASN A 110 -10.047 -4.611 25.837 00 37.19 C

ATOM 696 O ASN A 110 -9.721 -3.467 25.467 00 37.22 O

ATOM 697 CB ASN A 110 -10.719 -5.154 23.442 00 37.59 C

ATOM 698 CG ASN A 110 -12.133 -4.578 23.422 00 39.11 C

ATOM 699 ODl ASN A 110 -12.743 -4.316 24.467 00 41.49 O

ATOM 700 ND2 ASN A 110 -12.658 -4.371 22.218 00 38.93 N

ATOM 701 N THR A 111 -10.173 -4 ^'.^'985 27.116 00 36.63 N

ATOM 702 CA THR A 111 -9.794 -4.168 28.288 00 35.54 C

ATOM 703 C THR A 111 -8.272 -4.043 28.427 00 34.19 C

ATOM 704 O THR A 111 -7.758 -3.126 29.082 00 34.27 O

ATOM 705 CB THR A 111 -10.304 -4.874 29.545 00 36.07 C

ATOM 706 OGl THR A 111 -11.302 -5.833 29.167 00 37.54 O

ATOM 707 CG2 THR A 111 -11.016 -3.900 30.492 00 35.40 C

ATOM 708 N SER A 112 -7.569 -4.995 27.820 00 31.92 N

ATOM 709 CA SER A 112 -6.130 -5.126 27.928 00 29.98 C

ATOM 710 C SER A 112 -5.439 -4.053 27.069 00 28.20 C

ATOM 711 O SER A 112 -6.106 -3.250 26.420 00 2B.26 O

ATOM 712 CB SER A 112 -5.752 -6.557 27.508 00 30.16 C

ATOM 713 OG SER A 112 -4.356 -6.725 27.359 00 32.08 O

ATOM 714 N GLN A 113 -4.112 -4.014 27.080 00 25.62 N

ATOM 715 CA GLN A 113 -3.369 -3.062 26.249 00 23.09 C

ATOM 716 C GLN A 113 -2.915 -3.714 24.949 00 20.69 C

ATOM 717 O GLN A 113 -2.655 -4.916 24.910 00 19.38 O

ATOM 718 CB GLN A 113 -2.152 -2.522 27.001 00 23.25 C

ATOM 719 CG GLN A 113 -2.500 -1.495 28.064 00 24.75 C

ATOM 720 CD GLN A 113 -1.287 -0.942 28.781 00 24.51 C

ATOM 721 OEl GLN A 113 -1.344 0.156 29.313 00 28.82 O

ATOM 722 NE2 GLN A 113 -0.195 -1.696 28.802 00 27.08 N

ATOM 723 N TYR A 114 -2.819 -2.914 23.889 00 18.06 N

ATOM 724 CA TYR A 114 -2.467 -3.440 22.576 00 16.22 C

ATOM 725 C TYR A 114 -1.611 -2.460 21.810 00 14.52 C

ATOM 726 O TYR A 114 -0.995 -1.588 22.408 00 13.52 O

ATOM 727 CB TYR A 114 -3.738 -3.813 21.790 00 16.72 C

ATOM 728 CG TYR A 114 -4.546 -4.894 22.477 1.00 17.73 C

ATOM 729 CDl TYR A 114 -5.738 -4.598 23.131 .00 18.39 C

ATOM 730 CD2 TYR A 114 -4.088 -6.208 22.511 .00 18.45 C

ATOM 731 CEl TYR A 114 -6.466 -5.597 23.776 .00 19.56 C

ATOM 732 CE2 TYR A 114 -4.802 -7.202 23.142 .00 18.32 C

ATOM 733 CZ TYR A 114 -5.982 -6.893 23.771 .00 19.08 C

ATOM 734 OH TYR A 114 -6.666 -7.897 24.412 .00 21.06 O

ATOM 735 N ASP A 115 -1.556 -2.630 20.491 .00 13.10 N

ATOM 736 CA ASP A 115 -0.979 -1.632 19.593 .00 12.02 C

ATOM 737 C ASP A 115 -2.111 -0.733 19.153 .00 11.43 C

ATOM 738 O ASP A 115 -3.204 -0.810 19.706 .00 10.78 O

ATOM 739 CB ASP A 115 -0.395 -2.305 18.361 1.00 11.97 C

ATOM 740 CG ASP A 115 0.846 -3.132 18.656 1.00 12.10 C

ATOM 741 ODl ASP A 115 1.346 -3.181 19.810 1.00 12.29 O

ATOM 742 OD2 ASP A 115 1.403 -3.764 17.748 1.00 13.02 O Table 3

ATOM 743 N THR A 116 -1.864 0.115 18.154 1.00 10.88 N

ATOM 744 CA THR A 116 -2.956 0.839 17.528 1.00 10.40 C

ATOM 745 C THR A 116 ^■2.870 0.881 15.994 1.00 10.53 C

ATOM 746 O THR A 116 ^•1.804 0.659 15.412 00 10.23 O

ATOM 747 CB THR A 116 ^■3.134 2.261 18. ,157 1.00 10.50 C

ATOM 748 OGl THR A 116 ^■4.327 2.861 17..638 1.00 10.45 O

ATOM 749 CG2 THR A 116 ^■2.024 3.225 17.734 1.00 8.95 C

ATOM 750 N TYR A 117 -4 015 1.131 15.359 1.00 10.33 N

ATOM 751 CA TYR A 117 069 1.512 13.953 1.00 10.44 C

ATOM 752 C TYR A 117 -4 488 2.975 13.882 1.00 10.57 C

ATOM 753 O TYR A 117 5.146 3.492 14.798 1.00 10.68 O

ATOM 754 CB TYR A 117 5.035 0.603 13.156 1.00 10.19 C

ATOM 755 CG TYR A 117 -4 601 -0.846 13.213 .00 9.74 C

ATOM 756 CDl TYR A 117 5.114 -1.707 14.171 .00 8.74 C

ATOM 757 CD2 TYR A 117 3.631 -1.339 12.337 .00 8.71 C

ATOM 758 CEl TYR A 117 4.689 -3.027 14.245 .00 8.46 C

ATOM 759 CE2 TYR A 117 3.204 -2.655 12.406 .00 8.45 C

ATOM 760 CZ TYR A 117 3.738 -3.491 13.368 .00 8.83 C

ATOM 761 OH TYR A 117 3.318 -4.798 13.460 .00 9.68 O

ATOM 762 N CYS A 118 -4 098 3.628 12.796 1.00 10.40 N

ATOM 763 CA CYS A 118 -4.401 5.022 12.573 1.00 10.52 C

ATOM 764 C CYS A 118 -4.762 5.172 11.104 1.00 10.90 C

ATOM 765 O CYS A 118 -4.314 4.377 10.275 1.00 10.73 O

ATOM 766 CB CYS A 118 -3.202 5.899 12.963 1.00 10.44 C

ATOM 767 SG CYS A 118 -2.780 5.872 14.739 1.00 9.63 S

ATOM 768 N PHE A 119 610 6.157 10.799 1.00 11.63 N

ATOM 769 CA PHE A 119 993 6.485 9.428 1.00 12.34 C

ATOM 770 C PHK A 119 640 7.944 9.156 1.00 13.34 C

ATOM 771 O PHE A 119 -6.091 8.831 9.883 1.00 12.75 O

ATOM 772 CB PHE A 119 -7.495 6.237 9.176 1.00 12.33 C

ATOM 773 CG PHE A 119 -7.978 6.722 7.817 1.00 11.56 C

ATOM 774 CDl PHE A 119 -7.785 5.956 6.675 1.00 11.13 C

ATOM 775 CD2 PHE A 119 -8.618 7.950 7.687 1.00 12.53 C

ATOM 776 CEl PHE A 119 -8.214 6.410 5.421 1.00 11.96 C

ATOM 111 CE2 PHE A 119 -9.059 8.414 6.441 1.00 11.55 C

ATOM 778 CZ PHE A 119 -8.852 7.640 5.305 1.00 11.80 C

ATOM 779 N ASN A 120 -4.828 8.174 8.123 1.00 14.03 N

ATOM 780 CA ASN A 120 -4.525 9.517 7.664 1.00 15.92 C

ATOM 781 C ASN A 120 -5.283 9.842 6.378 1.00 16.62 C

ATOM 782 O ASN A 120 -5.046 9.229 5.336 1.00 16.34 O

ATOM 783 CB ASN A 120 -3.016 9.710 7.465 1.00 16.24 C

ATOM 784 CG ASN A 120 -2.656 11.144 7.050 1.00 18.14 C

ATOM 785 ODl ASN A 120 -3.323 11.751 6.218 1.00 20.87 O

ATOM 786 ND2 ASN A 120 -1.607 11.685 7.645 1.00 20.29 N

ATOM 787 N ALA A 121 -6.177 10.826 6.460 1.00 17.80 N

ATOM 788 CA ALA A 121 -7 ,050 11.196 5.340 1.00 19.25 C

ATOM 789 C ALA A 121 6.316 11.769 4.118 1.00 20.30 C

ATOM 790 O ALA A 121 6.851 11.756 3.011 1.00 20.82 O

ATOM 791 CB ALA A 121 8.151 12.161 5.814 1.00 19.24 C

ATOM 792 N SER A 122 -5 095 12.255 4.317 1.00 21.61 N

ATOM 793 CA SER A 122 ^■4.351 12.928 3.258 1.00 23.17 C

ATOM 794 C SER A 122 ^■3.412 11.997 2.489 1.00 24.00 C

ATOM 795 O SER A 122 ^■2.784 12.406 1.513 1.00 24.54 O

ATOM 796 CB SER A 122 3.578 14.115 3.840 1.00 23.50 C

ATOM 797 OG SER A 122 4.482 15.090 4.357 1.00 24.59 O

ATOM 798 N ALA A 123 3.330 10.745 2. .930 1.00 24.79 N

ATOM 799 CA ALA A 123 2.509 9.722 2..281 1.00 25.22 C

ATOM 800 C ALA A 123 3.101 9.226 0.947 1.00 25.77 C

ATOM 801 O ALA A 123 4.321 9.269 0.751 1.00 25.78 O

ATOM 802 CB ALA A 123 2.303 8.548 3.242 1.00 24.77 C

ATOM 803 N PRO A 124 2.241 8.730 0.048 1.00 26.36 N

ATOM 804 CA PRO A 124 2.682 8.143 -1.230 1.00 26.80 C

ATOM 805 C PRO A 124 3.496 6.854 -1.059 1.00 27.25 C

ATOM 806 O PRO A 124 -3.303 6.129 -0.074 1.00 27.60 O

ATOM 807 CB PRO A 124 -1 362 7.808 -1 .937 1.00 27.01 C

ATOM 808 CG PRO A 124 0.319 8.587 -1 ,226 1.00 26.69 C

ATOM 809 CD PRO A 124 0.776 8.695 0.190 1.00 26.40 C

ATOM 810 N PRO A 125 4.371 6.542 -2.018 1.00 27.33 N Table 3

ATOM 811 CA PRO A 125 -5.223 5.360 -1.914 1.00 27. 17 C ATOM 812 C PRO A 125 -4.459 4.119 -2.306 1.00 26.92 C ATOM 813 O PRO A 125 -5.043 3.170 -2.835 1.00 27.83 O ATOM 814 CB PRO A 125 -6.331 5.641 -2.930 1.00 27, 85 C ATOM 815 CG PRO A 125 -5.677 6.516 -3.977 1.00 27, 48 C ATOM 816 CD PRO A 125 -4.599 7.285 -3.274 1.00 27.49 C ATOM 817 N GLU A 126 -3.153 4.152 -2.061 1.00 26, 01 N ATOM 818 CA GLU A 126 -2.217 3.094 -2. .398 1.00 24.86 C ATOM 819 C GLU A 126 -1.316 2.863 -1..182 1.00 23, 91 C ATOM 820 O GLU A 126 -1,578 3.383 -0.093 1.00 23, 09 O ATOM 821 CB GLU A 126 -1.362 3.544 -3.593 1.00 25, 39 C ATOM 822 CG GLU A 126 -1.818 3.106 -4.987 1.00 26, 74 C ATOM 823 CD GLU A 126 -3.288 3.360 -5.282 1.00 28, 99 C ATOM 824 OEl GLU A 126 -3.595 4.249 -6.113 1.00 30, 39 O ATOM 825 OE2 GLU A 126 -4.144 2.653 -4.699 1.00 28, 39 O ATOM 826 N GLO A 127 -0.252 2.089 -1.373 1.00 23.00 N ATOM 827 CA GLU A 127 0.774 1.947 -0.359 1.00 22, 26 C ATOM 828 C GLU A 127 1.767 3.094 -0.454 1.00 22, 04 C ATOM 829 O GLU A 127 2.273 3.411 -1.534 1.00 21.59 O ATOM 830 CB GLU A 127 1.505 0.615 -0.472 1.00 22.17 C ATOM 831 CG GLU A 127 2.415 0.361 0.720 1.00 22, 18 C ATOM 832 CD GLU A 127 3.259 -0.884 0.580 1.00 23, 65 C ATOM 833 OEl GLU A 127 3.077 -1.640 -0.399 1.00 25.54 O ATOM 834 OE2 GLU A 127 4.104 -1.115 1.464 1.00 23.13 O ATOM 835 N ASP A 128 2.035 3.701 0.696 1.00 21.84 N ATOM 836 CA ASP A 128 2.925 4.846 0.803 1.00 21, 69 C ATOM 837 C ASP A 128 3.910 4.559 1..919 1.00 21, 31 C ATOM 838 O ASP A 128 3.544 4.524 3.,099 1.00 21, 21 O ATOM 839 CB ASP A 128 2.114 6.118 1.,098 1.00 21.96 C ATOM 840 CG ASP A 128 2.980 7.368 1.204 1.00 23.07 C ATOM 841 ODl ASP A 128 4.165 7.350 0.804 1.00 24.29 O ATOM 842 OD2 ASP A 128 2.550 8.431 1.684 1.00 25.84 O ATOM 843 N CYS A 129 5.165 4.357 1.531 1.00 21.02 N ATOM 844 CA CYS A 129 6.229 4.014 2.464 1.00 20.42 C ATOM 845 C CYS A 129 7.129 5.208 2.789 1.00 20, 59 C ATOM 846 O CYS A 129 8.188 5.048 3.411 1.00 20, 53 O ATOM 847 CB CYS A 129 7.042 2.833 1.914 00 20.29 C ATOM 848 SG CYS A 129 6.181 1.230 2.022 ,00 19.29 S ATOM 849 N THR A 130 6.704 6.404 2.375 ,00 20.58 N ATOM 850 CA THR A 130 7.422 7.641 2.691 .00 20.84 C ATOM 851 C THR A 130 7.836 7.646 4.166 1.00 20.78 C ATOM 852 O THR A 130 7.004 7.426 5.047 1.00 21.01 O ATOM 853 CB THR A 130 6.536 8.886 2.393 1.00 21.00 C ATOM 854 OGl THR A 130 6.166 8.896 1.008 1.00 20.93 O ATOM 855 CG2 THR A 130 7.344 10.164 2.558 1.00 20.87 C ATOM 856 N SER A 131 9.117 7..880 4.434 1.00 20.66 N ATOM 857 CA SER A 131 9.585 7..919 5.809 1.00 20.77 C ATOM 858 C SER A 131 8.916 9..063 6.577 1.00 20.60 C ATOM 859 O SER A 131 8.779 10..172 6.070 1.00 19.99 O ATOM 860 CB SER A 131 11.111 8.003 5.876 1.00 21 01 C ATOM 861 OG SER A 131 11.689 6.703 5.794 1.00 20.95 O ATOM 862 N VAL A 132 8.443 8.747 7.773 1.00 20.60 N ATOM 863 CA VAL A 132 7.867 9.727 8.658 1.00 21.11 C ATOM 864 C VAL A 132 8.992 10.167 9.591 1.00 21.62 C ATOM 865 O VAL A 132 9.535 9.356 10.350 1.00 21.42 O ATOM 866 CB VAL A 132 6.645 9.150 9.402 1.00 21.07 C ATOM 867 CGl VAL A 132 6.104 10.126 10.419 1.00 20.24 C ATOM 868 CG2 VAL A 132 5.550 8.771 8.391 1.00 21.35 C ATOM 869 N THR A 133 9.336 11.452 9.493 1.00 22.33 N ATOM 870 CA THR A 133 10.570 12.042 10.053 1.00 23.34 C ATOM 871 C THR A 133 10.448 12.363 11.526 1.00 23.12 C ATOM 872 O THR A 133 11.449 12.579 12.202 1.00 23.35 O ATOM 873 CB THR A 133 10.907 13.374 9.328 1.00 23.09 C ATOM 874 OGl THR A 133 10.398 13.359 7.988 1.00 26.64 O ATOM 875 CG2 THR A 133 12.394 13.503 9.115 1.00 25.08 C ATOM 876 N ASP A 134 9.209 12.476 11.993 1.00 23.06 N ATOM 877 CA ASP A 134 8.907 12.854 13.371 1.00 22.98 C ATOM 878 C ASP A 134 1.All 12.678 13.627 1.00 22.74 C Table 3

ATOM 879 O ASP A 134 6.648 12.333 12.711 1.00 22.54 O

ATOM 880 CB ASP A 134 9.346 14.305 13.676 1.00 22.97 C

ATOM 881 CG ASP A 134 8.458 15.358 13.017 1.00 23.78 C

ATOM 882 ODl ASP A 134 7.422 15.033 12.420 1.00 24.59 O

ATOM 883 OD2 ASP A 134 8.710 16.574 13.064 1.00 28.06 O

ATOM 884 N LEU A 135 7.027 12.918 14.874 1.00 22.32 N

ATOM 885 CA LEO A 135 5.637 12.932 15.283 1.00 22.59 C

ATOM 886 C LEU A 135 5.152 14.360 15.043 1.00 22.24 C

ATOM 887 O LEU A 135 5.458 15.246 15.830 1.00 22.77 O

ATOM 888 CB LEU A 135 5.541 12.533 16.763 1.00 22.31 C

ATOM 889 CG LED A 135 4.233 12.052 17.378 1.00 22.67 C

ATOM 890 CDl LED A 135 3.700 10.816 16.664 1.00 22.00 C

ATOM 891 CD2 LEU A 135 4.435 11.746 18.855 1.00 22.38 C

ATOM 892 N PRO A 136 4.407 14.587 13.958 1.00 22.26 N

ATOM 893 CA PRO A 136 4.197 15.947 13.430 1.00 22.08 C

ATOM 894 C PRO A 136 3.225 16.821 14.210 1.00 22.21 C

ATOM 895 O PRO A 136 3.185 18.042 13.991 1.00 22.32 O

ATOM 896 CB PRO A 136 3.667 15.696 12.014 1.00 21.84 C

ATOM 897 CG PRO A 136 2.995 14.368 12.091 1.00 21.85 C

ATOM 898 CD PRO A 136 3.704 13.568 13.155 1.00 22.11 C

ATOM 899 N ASN A 137 2.449 16.214 15.101 1.00 22.20 N

ATOM 900 CA ASN A 137 1.485 16.965 15.907 1.00 22.40 C

ATOM 901 C ASN A 137 1.621 16.639 17.403 1.00 22.39 C

ATOM 902 O ASN A 137 0.655 16.691 18.164 1.00 22.08 O

ATOM 903 CB ASN A 137 0.057 16.743 15.377 1.00 22.31 C

ATOM 904 CG ASN A 137 -0.975 17.676 16.007 1.00 22.85 C

ATOM 905 ODl ASN A 137 -2.107 17.266 16.236 1.00 24.19 O

ATOM 906 ND2 ASN A 137 -0.599 18.925 16.271 1.00 22.26 N

ATOM 907 N ALA A 138 2.836 16.305 17.818 1.00 22.37 N

ATOM 908 CA ALA A 138 3.130 16.207 19.237 1.00 22.87 C

ATOM 909 C ALA A 138 3.236 17.624 19.823 1.00 23.04 C

ATOM 910 O ALA A 138 3.221 18.617 19.088 1.00 23.17 O

ATOM 911 CB ALA A 138 4.422 15.454 19.452 1.00 23.09 C

ATOM 912 N PHE A 139 3.323 17.716 21.145 1.00 22.73 N

ATOM 913 CA PHE A 139 3.700 18.978 21.774 1.00 22.23 C

ATOM 914 C PHE A 139 5.048 18.847 22.481 1.00 22.07 C

ATOM 915 O PHE A 139 5.603 17.746 22.550 1.00 21.64 O

ATOM 916 CB PHE A 139 2.598 19.506 22.698 1.00 21.88 C

ATOM 917 CG PHE A 139 1.874 18.445 23.487 1.00 22.24 C

ATOM 918 CDl PHE A 139 2.251 18.158 24.800 1.00 21.95 C

ATOM 919 CD2 PHE A 139 0.777 17.765 22.938 1.00 21.94 C

ATOM 920 CEl PHE A 139 1.570 17.196 25.544 1.00 21.75 C

ATOM 921 CE2 PHE A 139 0.095 16.798 23.673 1.00 21.26 C

ATOM 922 CZ PHE A 139 0.490 16.513 24.980 1.00 21.16 C

ATOM 923 N ASP A 140 5.582 19.963 22.984 1.00 21.89 N

ATOM 924 CA ASP A 140 6.855 19.955 23.704 1.00 21.46 C

ATOM 925 C ASP A 140 6.704 19.177 24.997 1.00 20.61 C

ATOM 926 O ASP A 140 5.643 19.218 25.629 1.00 20.87 O

ATOM 927 CB ASP A 140 7.319 21.387 24.002 1.00 22.46 C

ATOM 928 CG ASP A 140 7.495 22.235 22.738 1.00 24.57 C

ATOM 929 ODl ASP A 140 7.726 21.671 21.644 1.00 27.07 O

ATOM 930 OD2 ASP A 140 7.426 23.484 22.741 1.00 28.78 O

ATOM 931 N GLY A 141 7.756 18.457 25.382 1.00 19.76 N

ATOM 932 CA GLY A 141 7.728 17.624 26.577 1.00 18.57 C

ATOM 933 C GLY A 141 9.063 16.967 26.857 1.00 18.31 C

ATOM 934 O GLY A 141 10.014 17.154 26.103 1.00 18.40 O

ATOM 935 N PRO A 142 9.145 16.196 27.940 1.00 17.94 N

ATOM 936 CA PRO A 142 10.412 15.600 28.380 1.00 17.75 C

ATOM 937 C PRO A 142 10.775 14.219 27.792 1.00 17.62 C

ATOM 938 O PRO A 142 11.859 13.684 28.097 1.00 17.18 O

ATOM 939 CB PRO A 142 10.212 15.480 29.893 1.00 17.93 C

ATOM 940 CG PRO A 142 8.719 15.195 30.039 1.00 18.33 C

ATOM 941 CD PRO A 142 8.042 15.882 28.864 1.00 17.58 C

ATOM 942 ISl ILE A 143 9.898 13.653 26.963 1.00 17.52 N

ATOM 943 CA ILE A 143 10.093 12.285 26.485 1.00 16.92 C

ATOM 944 C ILE A 143 10.957 12.276 25.238 1.00 16.52 C

ATOM 945 O ILE A 143 10.737 13.041 24.309 1.00 16.39 O

ATOM 946 CB ILE A 143 8.731 11.535 26.231 1.00 17.26 C Table 3

ATOM 947 CGl ILE A 143 7.748 11.719 27.400 1.00 16.90 C

ATOM 948 CG2 ILE A 143 8.963 10.037 25.971 1.00 17.07 C

ATOM 949 CDl ILE A 143 8.195 11.121 28.738 1.00 15.29 C

ATOM 950 N THR A 144 11.967 11.419 25.237 1.00 16.04 N

ATOM 951 CA THR A 144 12.690 11.121 24.018 1.00 15.86 C

ATOM 952 C THR A 144 11.778 10.202 23.179 1.00 15.41 C

ATOM 953 O THR A 144 11.520 9.067 23.570 1.00 15.46 O

ATOM 954 CB THR A 144 14.019 10.425 24.366 1.00 15.71 C

ATOM 955 OGl THR A 144 14.895 11.364 25.002 1.00 15.68 O

ATOM 956 CG2 THR A 144 14.786 10.001 23.084 1.00 15.79 C

ATOM 957 N ILE A 145 11.257 10.716 22.067 1.00 15.15 N

ATOM 958 CA ILE A 145 10.356 9.940 21.199 1.00 15.10 C

ATOM 959 C ILE A 145 11.079 9.529 19.922 1.00 15.67 C

ATOM 960 O ILE A 145 11.547 10.384 19.165 1.00 15.22 O

ATOM 961 CB ILE A 145 9.053 10.732 20.857 1.00 15.52 C

ATOM 962 CGl ILE A 145 8.227 11.026 22.131 1.00 15.40 C

ATOM 963 CG2 ILE A 145 8.187 9.961 19.820 1.00 14.46 C

ATOM 964 CDl ILE A 145 7.298 12.249 22.014 1.00 14.54 C

ATOM 965 N THR A 146 11.168 8.220 19.690 1.00 16.02 N

ATOM 966 CA THR A 146 11.763 7.699 18.460 1.00 16.74 C

ATOM 967 C THR A 146 10.729 7.084 17.514 1.00 16.63 C

ATOM 968 O THR A 146 9.812 6.368 17.938 1.00 16.39 O

ATOM 969 CB THR A 146 12.856 6.666 18.784 1.00 17.03 C

ATOM 970 OGl THR A 146 13.752 7.217 19.766 1.00 18.96 O

ATOM 971 CG2 THR A 146 13.744 6.449 17.574 1.00 18.12 C

ATOM 972 N ILE A 147 10.891 7.375 16.230 1.00 16.65 N

ATOM 973 CA ILE A 147 10.073 6.781 15.186 1.00 16.90 C

ATOM 974 C ILE A 147 10.942 5.912 14.279 1.00 16.78 C

ATOM 975 O ILE A 147 11.965 6.377 13.746 1.00 16.87 O

ATOM 976 CB ILE A 147 9.327 7.884 14.409 1.00 16.80 C

ATOM 977 CGl ILE A 147 8.426 8.634 15.393 1.00 18.51 C

ATOM 978 CG2 ILE A 147 8.501 7.291 13.259 1.00 17.23 C

ATOM 979 CDl ILE A 147 7.544 9.67B 14.787 1.00 20.10 C

ATOM 980 N VAL A 148 10.558 4.642 14.144 1.00 16.23 N

ATOM 981 CA VAL A 148 11.231 3.731 13.216 1.00 16.35 C

ATOM 982 C VAL A 148 10.313 3.377 12.041 1.00 16.68 C

ATOM 983 O VAL A 148 9.202 2.845 12.237 1.00 16.18 O

ATOM 984 CB VAL A 148 11.733 2.422 13.896 1.00 16.05 C

ATOM 985 CGl VAL A 148 12.600 1.623 12.934 1.00 16.53 C

ATOM 986 CG2 VAL A 148 12.531 2.720 15.133 1.00 16.43 C

ATOM 987 N ASN A 149 10.784 3.687 10.834 1.00 16.91 N

ATOM 988 CA ASN A 149 10.104 3.288 9.602 1.00 17.83 C

ATOM 989 C ASN A 149 10.700 1.988 9.092 1.00 18.39 C

ATOM 990 O ASN A 149 11.634 1.453 9.698 1.00 18.25 O

ATOM 991 CB ASN A 149 10.226 4.366 8.521 1.00 17.77 C

ATOM 992 CG ASN A 149 9.637 5.697 8.945 1.00 17.03 C

ATOM 993 ODl ASN A 149 8.533 6.053 8.534 1.00 17.10 O

ATOM 994 ND2 ASN A 149 10.375 6.444 9.757 1.00 15.23 N

ATOM 995 N ARG A 150 10.177 1.498 7.971 1.00 19.03 N

ATOM 996 CA ARG A 150 10.585 0.196 7.419 1.00 20.49 C

ATOM 997 C ARG A 150 12.054 0.097 6.963 1.00 20.05 C

ATOM 998 O ARG A 150 12.584 -0.999 6.827 1.00 20.27 O

ATOM 999 CB ARG A 150 9.622 -0.253 6.305 1.00 20.84 C

ATOM 1000 CG ARG A 150 9.627 0.623 5.048 1.00 24.12 C

ATOM 1001 CD ARG A 150 10.462 0.065 3.892 1.00 29.33 C

ATOM 1002 NE ARG A 150 10.205 0.761 2.628 1.00 32.14 N

ATOM 1003 CZ ARG A 150 9.642 0.210 1.552 1.00 33.61 C

ATOM 1004 NHl ARG A 150 9.259 -1.071 1.553 1.00 35.12 N

ATOM 1005 NH2 ARG A 150 9.459 0.942 0.463 1.00 33.16 N

ATOM 1006 N ASP A 151 12.711 1.227 6.737 1.00 19.83 N

ATOM 1007 CA ASP A 151 14.134 1.200 6.395 1.00 20.03 C

ATOM 1008 C ASP A 151 15.055 1.048 7.629 1.00 20.01 C

ATOM 1009 O ASP A 151 16.261 0.855 7.482 1.00 20.36 O

ATOM 1010 CB ASP A 151 14.518 2.425 5.565 1.00 19.75 C

ATOM 1011 CG ASP A 151 14.551 3.693 6.381 1.00 20.95 C

ATOM 1012 ODl ASP A 151 13.768 3.810 7.355 1.00 19.04 O

ATOM 1013 OD2 ASP A 151 15.341 4.628 6.122 1.00 23.34 O

ATOM 1014 N GLY A 152 14.491 1.140 8.832 1.00 19.52 N Table 3

ATOM 1015 CA GLY A 152 15.276 0.983 10.052 1.00 19.60 C

ATOM 1016 C GLY A 152 15.875 2.253 10.641 1.00 19.80 C

ATOM 1017 O GLY A 152 16.475 2.215 11.722 1.00 19.26 O

ATOM 10IB N THR A 153 15.719 3.380 9.951 1.00 20.28 N

ATOM 1019 CA THR A 153 16.259 4.655 10.462 1.00 21.46 C

ATOM 1020 C THR A 153 15.489 5.116 11.705 1.00 21.28 C

ATOM 1021 O THR A 153 14.261 5.105 11.710 1.00 21.23 O

ATOM 1022 CB THR A 153 16.244 5.765 9.383 1.00 21.21 C

ATOM 1023 OGl THR A 153 16.977 5.335 8.232 1.00 22.83 O

ATOM 1024 CG2 THR A 153 17.045 6.996 9.860 1.00 22.20 C

ATOM 1025 N ARG A 154 16.222 5.490 12.751 1.00 21.75 N

ATOM 1026 CA ARG A 154 15.623 6.020 13.982 1.00 22.38 C

ATOM 1027 C ARG A 154 15.592 7.539 13.941 1.00 22.30 C

ATOM 1028 O ARG A 154 16.649 8.183 13.977 1.00 22.72 O

ATOM 1029 CB ARG A 154 16.423 5.602 15.211 1.00 22.92 C

ATOM 1030 CG ARG A 154 16.579 4.113 15.423 1.00 24.89 C

ATOM 1031 CD ARG A 154 16.434 3.690 16.882 1.00 27.75 C

ATOM 1032 NE ARG A 154 15.669 2.450 16.957 1.00 30.93 N

ATOM 1033 CZ ARG A 154 14.872 2.105 17.952 1.00 32.01 C

ATOM 1034 NHl ARG A 154 14.715 2.896 19.008 1.00 33.08 N

ATOM 1035 NH2 ARG A 154 14.229 0.948 17.891 1.00 33.98 N

ATOM 1036 N TYR A 155 14.396 8.110 13.854 1.00 21.81 N

ATOM 1037 CA TYR A 155 14.228 9.556 13.958 1.00 21.81 C

ATOM 1038 C TYR A 155 13.851 9.926 15.390 1.00 21.82 C

ATOM 1039 O TYR A 155 12.851 9.432 15.924 1.00 22.05 O

ATOM 1040 CB TYR A 155 13.194 10.063 12.959 1.00 21.47 C

ATOM 1041 CG TYR A 155 13.611 9.853 11.523 1.00 21.68 C

ATOM 1042 CDl TYR A 155 13.190 8.726 10.812 1.00 21.32 C

ATOM 1043 CD2 TYR A 155 14.444 10.774 10.875 1.00 21.59 C

ATOM 1044 CEl TYR A 155 13.582 8.524 9.484 1.00 21.11 C

ATOM 1045 CE2 TYR A 155 14.838 10.585 9.556 1.00 21.74 C

ATOM 1046 CZ TYR A 155 14.405 9.454 8.868 1.00 22.00 C

ATOM 1047 OH TYR A 155 14.798 9.259 7.560 1.00 22.78 O

ATOM 1048 N VAL A 156 14.662 10.789 16.002 1.00 21.52 N

ATOM 1049 CA VAL A 156 14.594 11.053 17.440 1.00 21.49 C

ATOM 1050 C VAL A 156 14.163 12.496 17.681 1.00 21.65 C

ATOM 1051 O VAL A 156 14.637 13.411 17.007 1.00 21.75 O

ATOM 1052 CB VAL A 156 15.974 10.777 18.139 1.00 21.75 C

ATOM 1053 CGl VAL A 156 15.863 10.842 19.678 1.00 21.21 C

ATOM 1054 CG2 VAL A 156 16.560 9.433 17.706 1.00 20.66 C

ATOM 1055 N GLN A 157 13.245 12.693 18.622 1.00 21.73 N

ATOM 1056 CA GLN A 157 12.838 14.040 19.032 1.00 21.79 C

ATOM 1057 C GLN A 157 12.500 14.044 20.515 1.00 21.60 C

ATOM 1058 O GLN A 157 12.375 12.982 21.132 1.00 21.77 O

ATOM 1059 CB GLN A 157 11.633 14.530 18.221 1.00 22.03 C

ATOM 1060 CG GLN A 157 10.306 13.929 18.670 1.00 22.80 C

ATOM 1061 CD GLN A 157 9.178 14.202 17.705 1.00 23.81 C

ATOM 1062 OEl GLN A 157 8.550 15.268 17.741 1.00 25.90 O

ATOM 1063 NE2 GLN A 157 8.902 13.234 16.852 1.00 23.00 N

ATOM 1064 N LYS A 158 12.357 15.236 21.082 1.00 21.12 N

ATOM 1065 CA LYS A 158 11.846 15.369 22.437 1.00 20.74 C

ATOM 1066 C LYS A 158 10.456 15.997 22.389 1.00 19.95 C

ATOM 1067 O LYS A 158 10.221 16.995 21.693 1.00 19.95 O

ATOM 1068 CB LYS A 158 12.800 16.182 23.312 1.00 20.84 C

ATOM 1069 CG LYS A 158 13.040 15.563 24.691 1.00 22.82 C

ATOM 1070 CD LYS A 158 14.414 15.956 25.258 1.00 23.98 C

ATOM 1071 CE LYS A 158 14.358 17.243 26.074 1.00 25.28 C

ATOM 1072 NZ LYS A 158 14.287 16.992 27.543 1.00 26.37 N

ATOM 1073 N GLY A 159 9.529 15.394 23.115 1.00 18.88 N

ATOM 1074 CA GLY A 159 8.161 15.850 23.088 1.00 18.06 C

ATOM 1075 C GLY A 159 7.270 15.107 24.045 1.00 17.24 C

ATOM 1076 O GLY A 159 7.741 14.492 25.011 1.00 17.22 O

ATOM 1077 N GLϋ A 160 5.972 15.209 23.779 1.00 16.37 N

ATOM 1078 CA GLϋ A 160 4.942 14.482 24.503 1.00 15.82 C

ATOM 1079 C GLO A 160 3.714 14.458 23.603 1.00 15.45 C

ATOM 1080 O GLU A 160 3.571 15.319 22.739 1.00 14.85 O

ATOM 1081 CB GLO A 160 4.637 15.158 25.849 1.00 15.83 C

ATOM 1082 CG GLO A 160 3.503 14.532 26.653 1.00 15.80 C Table 3

ATOM 1083 CD GLO A 160 3.777 13.095 27.035 1.00 17.52 C

ATOM 1084 OEl GLU A 160 4.411 12.862 28.093 .00 18.81 O

ATOM 1085 OE2 GLU A 160 3.363 12.193 26.275 .00 18.30 O

ATOM 1086 N TYR A 161 2.851 13.463 23.788 .00 15.18 N

ATOM 1087 CA TYR A 161 1.625 13.357 23.001 .00 15.47 C

ATOM 1088 C TYR A 161 0.473 12.876 23.863 .00 15.33 C

ATOM 1089 O TYR A 161 -0.676 12.969 23.458 .00 15.17 O

ATOM 1090 CB TYR A 161 1.816 12.419 21.789 .00 15.46 C

ATOM 1091 CG TYR A 161 2.134 10.980 22.161 .00 16.14 C

ATOM 1092 CDl TYR A 161 1.116 10.071 22.459 .00 15.37 C

ATOM 1093 CD2 TYR A 161 3.455 10.533 22.230 .00 17.02 C

ATOM 1094 CEl TYR A 161 1.402 8.754 22.811 .00 16.02 C

ATOM 1095 CE2 TYR A 161 3.751 9.214 22.582 .00 16.75 C

ATOM 1096 CZ TYR A 161 2.721 8.337 22.867 .00 16.15 C

ATOM 1097 OH TYR A 161 3.008 7.041 23.217 .00 17.49 O

ATOM 1098 N ARG A 162 0.796 12.328 25.033 .00 15.63 N

ATOM 1099 CA ARG A 162 -0.215 11.769 25.939 .00 16.20 C

ATOM 1100 C ARG A 162 -0.944 12.863 26.698 .00 16.54 C

ATOM 1101 O ARG A 162 -0.353 13.874 27.088 .00 16.70 O

ATOM 1102 CB ARG A 162 0.411 10.804 26.941 .00 15.90 C

ATOM 1103 CG ARG A 162 1.015 9.559 26.329 .00 15.34 C

ATOM 1104 CD ARG A 162 1.928 8.808 27.268 .00 14.01 C

ATOM 1105 NE ARG A 162 2.998 9.668 21.111 .00 14.02 N

ATOM 1106 CZ ARG A 162 3.837 9.319 28.747 .00 13.90 C

ATOM 1107 NHl ARG A 162 3.743 8.123 29.320 .00 13.46 N

ATOM 1108 NH2 ARG A 162 4.779 10.165 29.141 .00 15.72 N

ATOM 1109 N THR A 163 2.227 12.641 26.926 .00 17.05 N

ATOM 1110 CA THR A 163 3.066 13.653 27.539 .00 17.74 C

ATOM 1111 C THR A 163 3.918 13.103 28.693 .00 17.96 C

ATOM 1112 O THR A 163 4.537 13.882 29.436 00 18.17 O

ATOM 1113 CB THR A 163 -3 920 14.319 26.460 00 17.82 C

ATOM 1114 OGl THR A 163 4.503 15.514 26.990 1.00 21.48 O

ATOM 1115 CG2 THR A 163 5.112 13.465 26.124 00 16.56 C

ATOM 1116 N ASN A 164 -3.924 11.774 28.849 00 17.61 N

ATOM 1117 CA ASN A 164 4.648 11.089 29.924 00 18.10 C

ATOM 1118 C ASN A 164 3.721 10.743 31.104 00 18.58 C

ATOM 1119 O ASN A 164 2.763 9.987 30.942 00 18.69 O

ATOM 1120 CB ASN A 164 5.348 9.826 29.394 00 17.88 C

ATOM 1121 CG ASN A 164 6.271 9.189 30.412 00 19.48 C

ATOM 1122 ODl ASN A 164 5.945 9.110 31.587 00 23.34 O

ATOM 1123 ND2 ASN A 164 7.426 8.710 29.963 00 20.67 N

ATOM 1124 N PRO A 165 4.007 11.282 32.291 00 13.86 N

ATOM 1125 CA PRO A 165 -3.129 11.082 33.453 00 19.12 C

ATOM 1126 C PRO A 165 046 9.621 33.894 00 19.25 C

ATOM 1127 O PRO A 165 2.043 9.219 34.480 00 13.82 O

ATOM 1128 CB PRO A 165 3.759 11.961 34.545 00 19.11 C

ATOM 1129 CG PRO A 165 -5 161 12.171 34.119 00 19.61 C

ATOM 1130 CD PRO A 165 5.179 12.117 32.608 00 19.00 C

ATOM 1131 N GLU A 166 4.078 8.837 33.583 00 19.59 N

ATOM 1132 CA GLU A 166 4.065 7.396 33.825 00 20.07 C

ATOM 1133 C GLU A 166 3.099 6.653 32.883 00 20.29 C

ATOM 1134 O GLU A 166 -2. 693 5.542 33.185 00 19.76 O

ATOM 1135 CB GLU A 166 -5.489 6.799 33.748 00 20.30 C

ATOM 1136 CG GLU A 156 -6.506 7.498 34.660 00 21.09 C

ATOM 1137 CD GLU A 166 -7.914 6.908 34.598 00 20.25 C

ATOM 1138 OEl GLU A 166 -8.069 5.675 34.740 00 21.50 O

ATOM 1139 OE2 GLU A 166 -8.876 .687 34.429 00 19.58 O

ATOM 1140 N ASP A 167 -2.742 .261 31.750 00 20.88 N

ATOM 1141 CA ASP A 167 -1 705 6.708 30.871 00 22.02 C

ATOM 1142 C ASP A 167 -0.310 7.120 31.323 00 23.53 C

ATOM 1143 O ASP A 167 0.605 6.306 31.334 00 23.46 O

ATOM 1144 CB ASP A 167 -1.892 7.163 29.422 00 21.23 C

ATOM 1145 CG ASP A 167 -3.097 6.545 28.763 00 20.05 C

ATOM 1146 ODl ASP A 167 -3.369 5.341 29.002 00 16.65 O

ATOM 1147 OD2 ASP A 167 -3.822 7.190 27.977 00 17.89 O

ATOM 1148 N ILE A 168 -0.163 8.397 31.669 00 25.59 N

ATOM 1149 CA ILE A 168 1.122 8.981 32.040 00 27.85 C

ATOM 1150 C ILE A 168 1.596 8.422 33.379 1.00 29.91 C Table 3

ATOM 1151 O ILE A 168 2.760 8.044 33.513 1.00 30.55 O

ATOM 1152 CB ILE A 168 1.033 10.524 32.046 1.00 27.59 C

ATOM 1153 CGl ILE A 168 0.820 11.040 30.620 1.00 27.00 C

ATOM 1154 CG2 ILE A 168 2.300 11.150 32.646 1.00 27.88 C

ATOM 1155 CDl ILE A 168 0.188 12.412 30.538 1.00 25.88 C

ATOM 1156 N TYR A 169 0.692 8.359 34.357 1.00 32.15 N

ATOM 1157 CA TYR A 169 0.938 7.600 35.586 1.00 34.00 C

ATOM 1158 C TYR A 169 0.640 6.128 35.312 1.00 34.25 C

ATOM 1159 O TYR A 169 1.547 5.299 35.266 1.00 34.94 O

ATOM 1160 CB TYR A 169 0.065 8.110 36.744 1.00 35.12 C

ATOM 1161 CG TYR A 169 0.294 7.384 38.069 1.00 37.37 C

ATOM 1162 CDl TYR A 169 0.837 8.050 39.180 1.00 38.88 C

ATOM 1163 CD2 TYR A 169 -0.030 6.030 38.210 1.00 38.41 C

ATOM 1164 CEl TYR A 169 1.052 7.375 40.398 1.00 39.19 C

ATOM 1165 CE2 TYR A 169 0.184 5.351 39.411 1.00 39.02 C

ATOM 1166 CZ TYR A 169 0.717 6.022 40.499 1.00 38.82 C

ATOM 1167 OH TYR A 169 0.911 5.323 41.677 1.00 38.95 O

TER 1168 TYR A 169

ATOM 1169 N ALA B 20 -4.100 -37.219 -0.501 1.00 22.38 N

ATOM 1170 CA ALA B 20 -3.915 -35.750 -0.705 1.00 22.75 C

ATOM 1171 C ALA B 20 -4.676 -35.243 -1.939 1.00 22.87 C

ATOM 1172 O ALA B 20 -4.781 -35.950 -2.955 1.00 22.66 O

ATOM 1173 CB ALA B 20 -2.445 -35.410 -0.799 1.00 22.56 C

ATOM 1174 N GLN B 21 -5.193 -34.016 -1.842 1.00 22.62 N

ATOM 1175 CA GLN B 21 -6.139 -33.488 -2.832 1.00 23.18 C

ATOM 1176 C GLN B 21 -5.893 -32.011 -3.170 1.00 21.43 C

ATOM 1177 O GLN B 21 -5.687 -31.189 -2.279 1.00 21.53 O

ATOM 1178 CB GLN B 21 -7.581 -33.747 -2.344 1.00 23.20 C

ATOM 1179 CG GLN B 21 -8.631 -32.684 -2.664 1.00 25.50 C

ATOM 1180 CD GLN B 21 -9.998 -32.967 -2.008 1.00 26.75 C

ATOM 1181 OEl GLN B 21 -10.813 -32.043 -1.842 1.00 31.28 O

ATOM 1182 NE2 GLN B 21 -10.248 -34.238 -1.637 1.00 28.55 N

ATOM 1183 N ILE B 22 -5.903 -31.692 -4.460 1.00 19.73 N

ATOM 1184 CA ILE B 22 -5.759 -30.315 -4.925 1.00 18.14 C

ATOM 1185 C ILE B 22 -6.888 -29.940 -5.888 1.00 17.43 C

ATOM 1186 O ILE B 22 -7.084 -30.602 -6.909 1.00 16.98 O

ATOM 1187 CB ILE B 22 -4.355 -30.076 -5.559 1.00 18.01 C

ATOM 1188 CGl ILE B 22 -3.285 -29.989 -4.468 1.00 17.90 C

ATOM 1189 CG2 ILE B 22 -4.326 -28.786 -6.352 1.00 16.91 C

ATOM 1190 CDl ILE B 22 -1.854 -30.201 -4.962 1.00 17.86 C

ATOM 1191 N ASP B 23 -7.624 -28.882 -5.539 1.00 16.51 N

ATOM 1192 CA ASP B 23 -8.714 -28.356 -6.364 1.00 16.11 C

ATOM 1193 C ASP B 23 -8.300 -27.070 -7.075 1.00 15.46 C

ATOM 1194 O ASP B 23 -7.816 -26.110 -6.447 1.00 14.79 O

ATOM 1195 CB ASP B 23 -9.961 -28.118 -5.514 1.00 16.68 C

ATOM 1196 CG ASP B 23 -10.556 -29.413 -4.977 1.00 19.44 C

ATOM 1197 ODl ASP B 23 -10.227 -30.501 -5.524 1.00 19.81 O

ATOM 1198 OD2 ASP B 23 -11.360 -29.436 -4.013 1.00 22.55 O

ATOM 1199 N LEU B 24 -8.492 -27.078 -8.389 1.00 14.61 N

ATOM 1200 CA LEU B 24 -8.094 -25.996 -9.271 1.00 14.66 C

ATOM 1201 C LEU B 24 -9.293 -25.364 -9.970 1.00 15.00 C

ATOM 1202 O LED B 24 -9.794 -25.890 -10.965 1.00 14.33 O

ATOM 1203 CB LEU B 24 -7.053 -26.490 -10.297 1.00 14.10 C

ATOM 1204 CG LEU B 24 -5.769 -27.073 -9.689 1.00 13.98 C

ATOM 1205 CDl LEU B 24 -4.916 -27.682 -10.772 1.00 14.26 C

ATOM 1206 CD2 LEU B 24 -4.971 -26.021 -8.871 1.00 11.47 C

ATOM 1207 N ASN B 25 -9.759 -24.240 -9.441 1.00 15.61 H

ATOM 1208 CA ASN B 25 -10.871 -23.522 -10.056 1.00 16.60 C

ATOM 1209 C ASN B 25 -10.336 -22.617 -11.134 1.00 16.64 C

ATOM 1210 O ASN B 25 -9.561 -21.699 -10.850 1.00 16.53 O

ATOM 1211 CB ASN B 25 -11.647 -22.696 -9.025 1.00 17.26 C

ATOM 1212 CG ASN B 25 -12.796 -23.461 -8.409 1.00 20.45 C

ATOM 1213 ODl ASN B 25 -12.601 -24.300 -7.511 1.00 22.70 O

ATOM 1214 ND2 ASN B 25 -14.017 -23.184 -8.894 1.00 22.45 N

ATOM 1215 N ILE B 26 -10.744 -22.872 -12.372 1.00 16.79 N

ATOM 1216 CA ILE B 26 -10.228 -22.096 -13.491 1.00 17.21 C

ATOM 1217 C ILE B 26 -11.298 -21.316 -14.253 1.00 16.99 C

ATOM 1218 O ILE B 26 -12.473 -21.659 -14.284 1.00 17.32 O Table 3

ATOM 1219 CB ILE B 26 -9.389 -22.959 -14.463 1.00 17.18 C

ATOM 1220 CGl ILE B 26 -10.293 -23.848 -15.312 1.00 18.04 C

ATOM 1221 CG2 ILE B 26 -8.391 -23.825 -13.698 1.00 18.36 C

ATOM 1222 CDl ILE B 26 -9.878 -23.864 -16.753 1.00 20.72 C

ATOM 1223 N THR B 27 -10.825 -20.275 -14.903 1.00 16.58 N

ATOM 1224 CA THR B 27 -11.637 -19.284 -15.539 1.00 16.48 C

ATOM 1225 C THR B 27 -11.710 -19.549 -17.055 1.00 15.91 C

ATOM 1226 O THR B 27 -10.944 -20.348 -17.595 1.00 15.22 O

ATOM 1227 CB THR B 27 -10.956 -17.939 -15.180 1.00 16.67 C

ATOM 1228 OGl THR B 27 -11.769 -17.230 -14.240 1.00 18.12 O

ATOM 1229 CG2 THR B 27 -10.833 -17.028 -16.322 1.00 16.24 C

ATOM 1230 N CYS B 28 -12.648 -18.896 -17.733 1.00 15.35 N

ATOM 1231 CA CYS B 28 -12.585 -18.760 -19.186 1.00 15.29 C

ATOM 1232 C CYS B 28 -11.259 -18.108 -19.584 1.00 14.55 C

ATOM 1233 O CYS B 28 -10.657 -17.381 -18.785 1.00 14.69 O

ATOM 1234 CB CYS B 28 -13.750 -17.888 -19.682 1.00 15.74 C

ATOM 1235 SG CYS B 28 -15.412 -18.568 -19.415 1.00 16.52 S

ATOM 1236 N ARG B 29 -10.804 -18.350 -20.809 1.00 13.82 N

ATOM 1237 CA ARG B 29 -9.643 -17.632 -21.333 1.00 13.35 C

ATOM 1238 C ARG B 29 -10.073 -16.365 -22.053 1.00 13.11 C

ATOM 1239 O ARG B 29 -10.976 -16.400 -22.910 1.00 13.56 O

ATOM 1240 CB ARG B 29 -8.801 -18.494 -22.282 1.00 13.25 C

ATOM 1241 CG ARG B 29 -7.933 -19.555 -21.623 1.00 13.38 C

ATOM 1242 CD ARG B 29 -8.509 -20.947 -21.755 1.00 13.67 C

ATOM 1243 NE ARG B 29 -9.497 -21.176 -20.735 1.00 13.89 N

ATOM 1244 CZ ARG B 29 -10.519 -22.003 -20.822 1.00 13.27 C

ATOM 1245 NHl ARG B 29 -10.735 -22.733 -21.908 1.00 11.94 N

ATOM 1246 NH2 ARG B 29 -11.337 -22.092 -19.782 1.00 13.73 N

ATOM 1247 N PHE B 30 -9.425 -15.253 -21.699 1.00 12.54 N

ATOM 1248 CA PHE B 30 -9.626 -13.970 -22.370 1.00 12.04 C

ATOM 1249 C PHE B 30 -8.326 -13.633 -23.072 1.00 11.84 C

ATOM 1250 O PHE B 30 -7.322 -13.321 -22.416 1.00 11.62 O

ATOM 1251 CB PHE B 30 -9.980 -12.866 -21.373 1.00 11.87 C

ATOM 1252 CG PHE B 30 -11.396 -12.928 -20.856 1.00 12.49 C

ATOM 1253 CDl PHE B 30 -11.799 -13.938 -19.984 1.00 11.06 C

ATOM 1254 CD2 PHE B 30 -12.321 -11.949 -21.223 1.00 12.50 C

ATOM 1255 CEl PHE B 30 -13.104 -13.983 -19.493 1.00 13.67 C

ATOM 1256 CE2 PHE B 30 -13.627 -11.986 -20.739 1.00 12.95 C

ATOM 1257 CZ PHE B 30 -14.022 -13.003 -19.873 1.00 13.55 C

ATOM 1258 N ALA B 31 -8.345 -13.707 -24.403 1.00 11.53 N

ATOM 1259 CA ALA B 31 -7.129 -13.613 -25.214 1.00 10.90 C

ATOM 1260 C ALA B 31 -6.003 -14.461 -24.605 1.00 10.71 C

ATOM 1261 O ALA B 31 -4.881 -13.981 -24.405 1.00 10.57 O

ATOM 1262 CB ALA B 31 -6.700 -12.162 -25.363 1.00 10.77 C

ATOM 1263 N GLY B 32 -6.332 -15.709 -24.282 1.00 10.75 N

ATOM 1264 CA GLY B 32 -5.363 -16.691 -23.799 1.00 10.28 C

ATOM 1265 C GLY B 32 -5.082 -16.672 -22.306 1.00 10.86 C

ATOM 1266 O GLY B 32 -4.447 -17.591 -21.782 1.00 11.35 O

ATOM 1267 N VAL B 33 -5.564 -15.643 -21.618 1.00 10.46 N

ATOM 1268 CA VAL B 33 -5.286 -15.446 -20.202 1.00 10.29 C

ATOM 1269 C VAL B 33 -6.403 -16.048 -19.370 1.00 10.04 C

ATOM 1270 O VAL B 33 -7.595 -15.840 -19.648 1.00 9.94 O

ATOM 1271 CB VAL B 33 -5.112 -13.931 -19.853 1.00 10.30 C

ATOM 1272 CGl VAL B 33 -4.914 -13.717 -18.339 1.00 10.52 C

ATOM 1273 CG2 VAL B 33 -3.941 -13.324 -20.624 1.00 9 9..7755 C

ATOM 1274 N PHE B 34 -6.009 -16.808 -18.353 1.00 99..7700 N

ATOM 1275 CA PHE B 34 -6.967 -17.367 -17.404 1.00 99..1188 C

ATOM 1276 C PHE B 34 -6.470 -17.285 -15.973 1.00 99..0011 C

ATOM 1277 O PHE B 34 -5.272 -17.178 -15.728 1.00 9 9..0033 O

ATOM 1278 CB PHE B 34 -7.427 -18.794 -17.779 1.00 88..5566 C

ATOM 1279 CG PHE B 34 -6.319 -19.824 -17.857 1.00 99..6699 C

ATOM 1280 CDl PHE B 34 -6.137 -20.751 -16.830 1.00 99..8833 C

ATOM 1281 CD2 PHE B 34 -5.494 -19.905 -18.979 1.00 10.20 C

ATOM 1282 CEl PHE B 34 -5.151 -21.725 -16.912 .00 9.83 C

ATOM 1283 CE2 PHE B 34 -4.497 -20.868 -19.067 .00 9.94 C

ATOM 1284 CZ PHE B 34 -4.322 -21.782 -18.031 .00 9.93 C

ATOM 1285 N HIS B 35 -7.414 -17.331 -15.043 .00 9.25 N

ATOM 1286 CA HIS B 35 -7.125 -17.299 -13.615 1.00 9.45 C Table 3

ATOM 1287 C HIS B 35 -7.321 -18.690 -13.001 00 9.24 C

ATOM 1288 O HIS B 35 -8.272 -19.398 -13.325 00 9.38 O

ATOM 1289 CB HIS B 35 -8.027 -16.247 -12.950 00 9.28 C

ATOM 1290 CG HIS B 35 -7.995 -16.269 -11.451 1.00 10.32 C

ATOM 1291 NDl HIS B 35 -8.987 -16.856 -10.697 .00 9.63 N

ATOM 1292 CD2 HIS B 35 -7.104 -15.762 -10.568 .00 9.86 C

ATOM 1293 CEl HIS B 35 -8.703 -16.718 -9.414 1.00 10.99 C

ATOM 1294 NE2 HIS B 35 -7.568 -16.055 -9.307 1. 0000 9.33 N

ATOM 1295 N VAL B 36 -6.392 -19.089 -12.140 1.0000 9.50 N

ATOM 1296 CA VAL B 36 -6.502 -20.339 -11.404 1.0000 9.54 C

ATOM 1297 C VAL B 36 -6.471 -20.066 -9.905 1.0000 9.93 C

ATOM 1298 O VAL B 36 -5.540 -19.410 -9.404 1.0000 9.66 O

ATOM 1299 CB VAL B 36 -5.357 -21.315 -11.778 1.0000 9.76 C

ATOM 1300 CGl VAL B 36 -5.531 -22.677 -11.077 1.0000 9.49 C

ATOM 1301 CG2 VAL B 36 -5.294 -21.502 -13.292 1.0000 9.56 C

ATOM 1302 N GLO B 37 -7.479 -20.569 -9.195 1.00 10.19 N

ATOM 1303 CA GLU B 37 -7.481 -20.543 -7.725 1.00 10.94 C

ATOM 1304 C GLU B 37 -7.326 -21.953 -7.186 1.00 10.60 C

ATOM 1305 O GLO B 37 -8.028 -22.872 -7.621 1.00 10.57 O

ATOM 1306 CB GLD B 37 -8.751 -19.891 -7.161 1.00 10.90 C

ATOM 1307 CG GLϋ B 37 -8.715 -19.706 -5.644 1.00 12.61 C

ATOM 1308 CD GLD B 37 -9.911 -18.949 -5.093 1.00 12.72 C

ATOM 1309 OEl GLO B 37 -10.588 -18.232 -5.867 1.00 14.28 O

ATOM 1310 OE2 GLO B 37 -10.169 -19.076 -3.877 1.00 14.23 O

ATOM 1311 N LYS B 38 -6.387 -22.121 -6.254 1.00 10.49 N

ATOM 1312 CA LYS B 38 -6.132 -23.417 -5.631 1.00 10.52 C

ATOM 1313 C LYS B 38 -6.812 -23.520 -4.261 1.00 11.23 C

ATOM 1314 O LYS B 38 -6.604 -22.676 -3.392 1.00 11.14 O

ATOM 1315 CB LYS B 38 -4.624 -23.664 -5.504 1.00 10.24 C

ATOM 1316 CG LYS B 38 -4.227 -24.860 -4. .636 1.00 10.40 C

ATOM 1317 CD LYS B 38 -2.734 -25.105 -4.672 1.00 10.29 C

ATOM 1318 CE LYS B 38 -2.372 -26.219 -3.711 1.00 12.23 C

ATOM 1319 NZ LYS B 38 -0.886 -26.476 -3.583 1.00 10.65 N

ATOM 1320 N ASN B 39 -7.616 -24.563 -4.083 1.00 11.83 N

ATOM 1321 CA ASN B 39 -8.230 -24.890 -2.790 1.00 12.69 C

ATOM 1322 C ASN B 39 -9.059 -23.774 -2.154 1.00 13.19 C

ATOM 1323 O ASN B 39 -9.111 -23.655 -0.928 1.00 13.21 O

ATOM 1324 CB ASN B 39 -7.177 -25.431 -1.807 1.00 13.07 C

ATOM 1325 CG ASN B 39 -6.619 -26.779 -2.238 1.00 13.37 C

ATOM 1326 ODl ASN B 39 -7.233 -27.490 -3.033 1.00 14.45 O

ATOM 1327 ND2 ASN B 39 -5.457 -27.137 -1.709 1.00 13.83 N

ATOM 1328 N GLY B 40 -9.707 -22.970 -2.999 1.00 13.40 N

ATOM 1329 CA GLY B 40 -10.586 -21.894 -2.546 1.00 14.05 C

ATOM 1330 C GLY B 40 -9.945 -20.862 -1.630 1.00 14.33 C

ATOM 1331 O GLY B 40 -10.622 -20.282 -0.798 1.00 14.28 O

ATOM 1332 N ARG B 41 -8.649 -20.617 -1.800 1.00 14.63 N

ATOM 1333 CA ARG B 41 -7.881 -19.788 -0.872 1.00 15.36 C

ATOM 1334 C ARG B 41 -6.563 -19.381 -1.538 1.00 13.99 C

ATOM 1335 O ARG B 41 -6.101 -20.084 -2.428 1.00 13.64 O

ATOM 1336 CB ARG B 41 -7.615 -20.630 0.394 1.00 16.48 C

ATOM 1337 CG ARG B 41 -7.064 -19.890 1.596 1.00 21.28 C

ATOM 1338 CD ARG B 41 -7.819 -18.590 1.975 1.00 28.74 C

ATOM 1339 NE ARG B 41 -9.253 -18.800 2.210 1.00 32.89 N

ATOM 1340 CZ ARG B 41 -9.784 -19.168 3.373 1.00 34.55 C

ATOM 1341 NHl ARG B 41 -9.006 -19.368 4.436 1.00 34.56 N

ATOM 1342 NH2 ARG B 41 -11.101 -19.335 3.469 1.00 36.25 N

ATOM 1343 N TYR B 42 -5.969 -18.254 -1.134 1.00 13.20 N

ATOM 1344 CA TYR B 42 -4.590 -17.907 -1.542 1.00 12.52 C

ATOM 1345 C TYR B 42 -3.641 -18.991 -1.056 1.00 12.44 C

ATOM 1346 O TYR B 42 -3.431 -19.124 0.153 1.00 13.95 O

ATOM 1347 CB TYR B 42 -4.135 -16.561 -0.956 1.00 12.02 C

ATOM 1348 CG TYR B 42 -4.781 -15.344 -1.582 1.00 10.74 C

ATOM 1349 CDl TYR B 42 -5.142 -14.239 -0.801 00 9.83 C

ATOM 1350 CD2 TYR B 42 -5.052 -15.305 -2.950 00 10.14 C

ATOM 1351 CEl TYR B 42 -5.737 -13.120 -1.377 00 9.98 C

ATOM 1352 CE2 TYR B 42 -5.650 -14.194 -3.540 00 8.95 C

ATOM 1353 CZ TYR B 42 -5.988 -13.110 -2.747 1.00 10.39 C

ATOM 1354 OH TYR B 42 -6.585 -12.042 -3.332 1.00 9.46 O Table 3

ATOM 1355 N SER B 43 -3 ,080 19.773 -1.980 00 11.64 N

ATOM 1355 CA SER B 43 2.289 20.947 -1.596 00 10.77 C

ATOM 1357 C SER B 43 1.223 21.317 -2.619 00 10.26 C

ATOM 1358 O SER B 43 0.618 22.390 -2.528 00 9.99 O

ATOM 1359 CB SER B 43 -3 ,201 22.155 -1.336 00 10.83 C

ATOM 1360 OG SER B 43 3.977 22.457 -2.484 1.00 10.68 O

ATOM 1361 N ILE B 44 0.968 20.418 -3.566 00 9.36 N

ATOM 1362 CA ILE B 44 0.025 20.663 -4.604 00 8.81 C

ATOM 1363 C ILE B 44 1.226 19.731 -4.442 00 9.11 C

ATOM 1354 O ILE B 44 1.080 18.508 -4.525 00 8.88 O

ATOM 1365 CB ILE B 44 -0.594 -20.475 -6.040 00 8.72 C

ATOM 1366 CGl ILE B 44 -1 867 21.308 -6.233 00 8.31 C

ATOM 1367 CG2 ILE B 44 0.444 20.789 -7.107 00 7.17 C

ATOM 1368 CDl ILE B 44 ^•2.613 21.045 -7.565 00 8.16 C

ATOM 1369 N SER B 45 2.409 20.307 -4.232 00 9.09 N

ATOM 1370 CA SER B 45 3.650 19.527 -4.195 00 9.19 C

ATOM 1371 C SER B 45 4.089 19.183 -5.610 00 9.52 C

ATOM 1372 O SER B 45 3.559 -19.742 -6.584 00 9.20 O

ATOM 1373 CB SER B 45 4.747 -20.339 -3.517 00 9.23 C

ATOM 1374 OG SER B 45 5.091 -21.455 -4.325 00 9.51 O

ATOM 1375 N ARG B 46 5.076 18.292 -5.739 00 9.82 N

ATOM 1376 CA ARG B 46 5.614 17.963 -7.059 00 10.52 C

ATOM 1377 C ARG B 46 6.125 19.173 -7.850 00 9.78 C

ATOM 1378 O ARG B 46 5.909 19.258 -9.071 00 9.58 O

ATOM 1379 CB ARG B 46 6.706 16.880 -7.005 00 10.67 C

ATOM 1380 CG ARG B 46 7.199 16.541 -8.421 00 12.09 C

ATOM 1381 CD ARG B 46 8.063 15.286 -8.572 00 13.65 C

ATOM 1382 NE ARG B 46 7.268 14.052 -8.613 00 19.46 N

ATOM 1383 CZ ARG B 46 6.502 13.657 -9.635 00 19.94 C

ATOM 1384 NHl ARG B 46 6.377 14.397 -10.736 00 20.28 N

ATOM 1385 NH2 ARG B 46 5.850 12.510 -9.544 00 20.57 N

ATOM 1386 N THR B 47 6.805 20.096 -7.168 00 9.47 N

ATOM 1387 CA THR B 47 7.343 21.302 -7.819 00 9.32 C

ATOM 1388 C THR B 47 6.233 22.280 -8.186 00 9.25 C

ATOM 1389 O THR B 47 6.269 22.894 -9.253 00 9.26 O

ATOM 1390 CB THR B 47 8.403 22.008 -6.945 00 9.32 C

ATOM 1391 OGl THR B 47 7.866 22.252 -5.636 00 8.19 O

ATOM 1392 CG2 THR B 47 9.649 21.079 -6.692 00 9.41 C

ATOM 1393 N GLD B 48 5.242 22.434 -7.313 00 9.23 N

ATOM 1394 CA GLD B 48 4.126 23.311 -7.649 00 9.29 C

ATOM 1395 C GLO B 48 3.333 22.727 -8.818 00 9.17 C

ATOM 1396 O GLO B 48 2.869 23.470 -9.673 00 9.14 O

ATOM 1397 CB GLϋ B 48 3.228 23.591 -6.447 00 9.45 C

ATOM 1398 CG GLO B 48 2.149 24.610 -6.771 00 10.26 C

ATOM 1399 CD GLO B 48 1.488 25.216 -5.548 00 12.64 C

ATOM 1400 OEl GLO B 48 2.014 25.075 -4.425 00 11.02 O

ATOM 1401 OE2 GLO B 48 0.436 25.868 -5.732 00 14.22 O

ATOM 1402 N ALA B 49 3.219 21.398 -8.864 00 8.84 N

ATOM 1403 CA ALA B 49 2.536 20.701 -9.965 00 9.06 C

ATOM 1404 C ALA B 49 3.153 21.086 -11.301 00 9.26 C

ATOM 1405 O ALA B 49 2.454 21.494 -12.226 00 9.23 O

ATOM 1406 CB ALA B 49 .606 19.178 -9.772 00 8.98 C

ATOM 1407 N ALA B 50 .480 20.961 -11.381 00 9.43 N

ATOM 1408 CA ALA B 50 .226 21.314 -12.585 00 9.42 C

ATOM 1409 C ALA B 50 .005 22.783 -12.953 00 9.49 C

ATOM 1410 O ALA B 50 4.783 23.108 -14.114 00 9.96 O

ATOM 1411 CB ALA B 50 6.707 21.013 -12.405 1.00 8.97 C

ATOM 1412 N ASP B 51 .052 23.662 -11.961 ,00 9.47 N

ATOM 1413 CA ASP B 51 .842 25.078 -12.205 00 9.93 C

ATOM 1414 C ASP B 51 .430 25.366 -12.679 00 9.77 C

ATOM 1415 O ASP B 51 .220 26.207 -13.550 00 10.45 O

ATOM 1416 CB ASP B 51 .169 25.886 -10.949 00 9.44 C

ATOM 1417 CG ASP B 51 6.668 -26.053 -10.741 00 10.82 C

ATOM 1418 ODl ASP B 51 7.448 25.648 -11.634 00 12.02 O

ATOM 1419 OD2 ASP B 51 7.158 26.582 -9.718 00 11.35 O

ATOM 1420 N LEO B 52 2.472 24.654 -12.100 00 10.07 N

ATOM 1421 CA LEU B 52 1.060 24.836 -12.392 00 10.18 C

ATOM 1422 C LEO B 52 0.702 -24.380 -13.807 1.00 10.19 C Table 3

ATOM 1423 O LEU B 52 0.012 -25.098 -14.518 1.00 10.37 O

ATOM 1424 CB LEU B 52 0.206 -24.124 -11.337 1.00 10.10 C

ATOM 1425 CG LEU B 52 1.324 -24.250 -11.354 1.00 10.87 C

ATOM 1426 CDl LEU B 52 1.767 -25.701 -11.415 1.00 10.32 C

ATOM 1427 CD2 LEU B 52 1.913 -23.554 -10.121 1.00 10.22 C

ATOM 1428 N CYS B 53 1.172 -23.205 -14.219 1.00 10.50 N

ATOM 1429 CA CYS B 53 0.986 -22.111 -15.613 1.00 10.46 C

ATOM 1430 C CYS B 53 1.647 -23.764 -16.595 1.00 11.03 C

ATOM 1431 O CYS B 53 1.027 -24.166 -17.583 1.00 10.69 O

ATOM 1432 CB CYS B 53 1.474 -21.333 -15.839 1.00 10.11 C

ATOM 1433 SG CYS B 53 0.541 -20.068 -14.920 1.00 8.95 S

ATOM 1434 N LYS B 54 2.893 -24.157 -16.322 1.00 11.42 N

ATOM 1435 CA LYS B 54 3.548 -25.208 -17.129 1.00 11.66 C

ATOM 1436 C LYS B 54 2.663 -26.451 -17.267 1.00 11.40 C

ATOM 1437 O LYS B 54 2.477 -26.972 -18.362 1.00 11.57 O

ATOM 1438 CB LYS B 54 4.926 -25.577 -16.556 1.00 12.12 C

ATOM 1439 CG LYS B 54 5.714 -26.576 -17.411 1.00 14.64 C

ATOM 1440 CD LYS B 54 6.325 -25.910 -18.649 1.00 20.83 C

ATOM 1441 CE LYS B 54 6.309 -26.834 -19.899 1.00 25.42 C

ATOM 1442 NZ LYS B 54 7.266 -28.006 -19.838 1.00 26.69 N

ATOM 1443 N ALA B 55 2.101 -26.940 -16.161 1.00 11.13 N

ATOM 1444 CA ALA B 55 1.253 -28.120 -16.201 1.00 11.02 C

ATOM 1445 C ALA B 55 0.023 -27.912 -17.082 1.00 11.21 C

ATOM 1446 O ALA B 55 0.596 -28.885 -17.527 1.00 10.97 O

ATOM 1447 CB ALA B 55 0.842 -28.519 -14.802 1.00 11.48 C

ATOM 1448 N PHE B 56 0.321 -26.641 -17.321 1.00 10.97 N

ATOM 1449 CA PHE B 56 1.433 -26.257 -18.177 1.00 10.87 C

ATOM 1450 C PHE B 56 0.940 -25.935 -19.579 1.00 11.16 C

ATOM 1451 O PHE B 56 1.686 -25.375 -20.377 1.00 11.26 O

ATOM 1452 CB PHE B 56 2.144 -25.011 -17.608 1.00 10.90 C

ATOM 1453 CG PHE B 56 3.249 -25.317 -16.631 1.00 10.27 C

ATOM 1454 CDl PHE B 56 3.163 -24.887 -15.309 1.00 10.42 C

ATOM 1455 CD2 PHE B 56 4.376 -26.029 -17.036 1.00 10.83 C

ATOM 1456 CEl PHE B 56 4.193 -25.161 -14.395 1.00 10.99 C

ATOM 1457 CE2 PHE B 56 5.405 -26.325 -16.139 1.00 11.03 C

ATOM 1458 CZ PHE B 56 5.314 -25.894 -14.814 1.00 11.31 C

ATOM 1459 N ASN B 57 0.315 -26.271 -19.875 1.00 11.41 N

ATOM 1460 CA ASN B 57 0.929 -25.927 -21.163 1.00 11.92 C

ATOM 1461 C ASN B 57 0.892 -24.421 -21.426 1.00 11.87 C

ATOM 1462 O ASN B 57 0.626 -23.975 -22.541 1.00 11.92 O

ATOM 1463 CB ASN B 57 0.254 -26.703 -22.309 1.00 11.88 C

ATOM 1464 CG ASN B 57 0.629 -28.175 -22.308 1.00 12.68 C

ATOM 1465 ODl ASN B 57 1.774 -28.531 -22.034 1.00 13.48 O

ATOM 1466 ND2 ASN B 57 0.328 -29.032 -22.620 1.00 13.00 N

ATOM 1467 N SER B 58 1.173 -23.652 -20.379 1.00 11.94 N

ATOM 1468 CA SER B 58 1.000 -22.204 -20.381 1.00 11.48 C

ATOM 1469 C SER B 58 2.177 -21.552 -19.664 1.00 11.60 C

ATOM 1470 O SER B 58 3.052 -22.239 -19.133 1.00 11.55 O

ATOM 1471 CB SER B 58 0.320 -21.837 -19.670 1.00 11.56 C

ATOM 1472 OG SER B 58 1.441 -22.405 -20.326 1.00 10.35 O

ATOM 1473 N THR B 59 2.191 -20.227 -19.649 1.00 11.39 N

ATOM 1474 CA THR B 59 3.255 -19.468 -19.016 1.00 11.52 C

ATOM 1475 C THR B 59 2.611 -18.354 -13.194 1.00 11.63 C

ATOM 1476 O THR B 59 1.454 -17.984 -18.435 1.00 11.74 O

ATOM 1477 CB THR B 59 4.176 -18.821 -20.088 1.00 12.08 C

ATOM 1478 OGl THR B 59 3.366 -18.095 -21.023 1.00 11.65 O

ATOM 1479 CG2 THR B 59 4.878 -19.871 -20.956 1.00 11.21 C

ATOM 1480 N LED B 60 3.355 -17.806 -17.238 1.00 11.42 N

ATOM 1481 CA LEU B 60 2.879 -16.652 -16.501 1.00 11.15 C

ATOM 1482 C LEU B 60 2.736 -15.508 -17.510 1.00 11.29 C

ATOM 1483 O LEU B 60 3.623 -15.287 -18.324 1.00 11.22 O

ATOM 1484 CB LEU B 60 3.837 -16.283 -15.359 1.00 11.03 C

ATOM 1485 CG LEU B 60 3.949 -17.301 -14.210 1.00 10.60 C

ATOM 1486 CDl LEU B 60 5.180 -17.007 -13.356 1.00 10.81 C

ATOM 1487 CD2 LEU B 60 2.678 -17.324 -13.355 1.00 9.61 C

ATOM 1488 N PRO B 61 1.597 -14.824 -17.490 1.00 11.27 N

ATOM 1489 CA PRO B 61 1.337 -13.728 -18.434 1.00 11.67 C

ATOM 1490 C PRO B 61 2.288 -12.545 -18.239 1.00 11.97 C Table 3

ATOM 1491 O PRO B 61 2.782 -12.332 -17.135 00 11.94 O

ATOM 1492 CB PRO B 61 -0.100 -13.303 -18.092 00 11.34 C

ATOM 1493 CG PRO B 61 -0.685 -14.464 -17.395 00 10.94 C

ATOM 1494 CD PRO B 61 0.457 -15.058 -16.590 00 11.32 C

ATOM 1495 N THR B 62 2.548 -11.801 -19.315 00 12.46 N

ATOM 1496 CA THR B 62 3.226 -10.518 -19.216 00 13.00 C

ATOM 1497 C THR B 62 162 -9.459 -18.935 00 13.80 C

ATOM 1498 O THR B 62 0.964 -9.731 -19.079 00 13.29 O

ATOM 1499 CB THR B 62 .951 -10.179 -20.541 00 13.15 C

ATOM 1500 OGl THR B 62 .986 -10.054 -21.587 00 13.13 O

ATOM 1501 CG2 THR B 62 .844 -11.342 -21.027 00 13.01 C

HETATM 1502 N MSE B 63 .596 -8.255 -18.552 00 14.48 N

HETATM 1503 CA MSE B 63 .691 -7.114 -18.394 00 16.06 C

HETATM 1504 C MSE B 63 0.857 -6.842 -19.655 00 15.65 C

HETATM 1505 O MSE B 63 -0.357 -6.627 -19.569 00 15.20 O

HETATM 1506 CB MSE B 63 2.462 -5.851 -17.973 00 16.75 C

HETATM 1507 CG MSE B 63 2.786 -5.810 -16.482 00 21.84 C

HETATM 1508 SE MSE B 63 1.142 -5.652 -15.368 00 35.95 SE

HETATM 1509 CE MSE B 63 0.492 -3.980 -16.053 00 29.21 C

ATOM 1510 N ALA B 64 1.520 -6.868 -20.815 00 15.65 N

ATOM 1511 CA ALA B 64 0.868 -6.672 -22.111 00 15.44 C

ATOM 1512 C ALA B 64 -0.265 -7.665 -22.319 00 15.39 C

ATOM 1513 O ALA B 64 -1..346 -7.291 -22.785 00 15.69 O

ATOM 1514 CB ALA B 64 1..893 -6.786 -23.251 00 15.48 C

ATOM 1515 N GLN B 65 -0.020 -8.930 -21.975 00 15.18 N

ATOM 1516 CA GLN B 65 -1..055 -9.968 -22.092 00 15.12 C

ATOM 1517 C GLN B 65 -2..228 -9.760 -21.123 1.00 15.34 C

ATOM 1518 O GLN B 65 -3.381 -10.017 -21.481 ,00 15.68 O

ATOM 1519 CB GLN B 65 -0.444 -11.360 -21.948 .00 14.57 C

ATOM 1520 CG GLN B 65 0.366 - 11.765 -23.178 ,00 14.65 C

ATOM 1521 CD GLN B 65 1. 400 ■12.819 -22.882 1.00 14.99 C

ATOM 1522 OEl GLN B 65 1.538 ■13.261 -21.738 .00 14.90 O

ATOM 1523 NE2 GLN B 65 2.138 •13.227 -23.907 ,00 14.04 N

HETATM 1524 IS! MSE B 66 -1.934 -9.284 -19.916 ,00 15.47 N

HETATM 1525 CA MSE B 66 -2.976 -8.914 -18.949 ,00 16.54 C

HETATM 1526 C MSE B 66 -3.794 -7.686 -19.415 ,00 16.18 C

HETATM 1527 O MSE B 66 -5.022 -7.664 -19.271 ,00 16.16 O

HETATM 1528 CB MSE B 66 -2.376 -8.650 -17.555 ,00 17.07 C

HETATM 1529 CG MSE B 66 -1.665 -9.837 -16.911 ,00 19.98 C

HETATM 1530 SE MSE B 66 -2.885 ■11.322 -16.422 1.00 29.63 SE

HETATM 1531 CE MSE B 66 -4.374 ^■10.229 -15.609 00 22.62 C

ATOM 1532 N GLU B 67 -3.123 -6.682 -19.976 00 15.92 N

ATOM 1533 CA GLO B 67 -3.813 -5.487 -20.500 00 16.22 C

ATOM 1534 C GLU B 67 -4.772 -5.850 -21.636 00 15.69 C

ATOM 1535 O GLU B 67 -5.883 -5.303 -21.733 00 15.66 O

ATOM 1536 CB GLU B 67 -2. .818 -4.409 -20.975 1.00 16.56 C

ATOM 1537 CG GLU B 67 -1..827 -3.888 -19.929 00 19.67 C

ATOM 1538 CD GLU B 67 -2.441 -2.956 -18.892 00 25.61 C

ATOM 1539 OEl GLU B 67 -3.653 -2.631 -19.000 00 27.31 O

ATOM 1540 OE2 GLU B 67 -1..703 -2.534 -17.955 00 27.73 O

ATOM 1541 N LYS B 68 -4..335 -6.774 -22.490 00 15.33 N

ATOM 1542 CA LYS B 68 -5.154 -7.282 -23.583 00 14.74 C

ATOM 1543 C LYS B 68 -6.385 -8.036 -23.057 00 14.01 C

ATOM 1544 O LYS B 68 -7.491 -7.824 -23.546 00 13.02 O

ATOM 1545 CB LYS B 68 -4.305 -8.165 -24.511 00 15.76 C

ATOM 1546 CG LYS B 68 -5.050 -8.823 -25.660 00 16.82 C

ATOM 1547 CD LYS B 68 -5.392 -7.858 -26.792 00 19.52 C

ATOM 1548 CE LYS B 68 -5.953 -8.623 -28.022 00 20.91 C

ATOM 1549 NZ LYS B 68 -6.315 -7.728 -29.174 00 22.87 N

ATOM 1550 N ALA B 69 -6.201 -8.913 -22.066 00 13.37 N

ATOM 1551 CA ALA B 69 -7.348 -9.580 -21.445 00 12.99 C

ATOM 1552 C ALA B 69 -8.312 -8.547 -20.824 00 12.67 C

ATOM 1553 O ALA B 69 -9.499 -8.595 -21.074 00 12.27 O

ATOM 1554 CB ALA B 69 -6.902 10.576 -20.415 00 13.04 C

ATOM 1555 N LEU B 70 -7.778 -7.611 -20.042 00 13.15 N

ATOM 1556 CA LEU B 70 -8.556 -6.532 -19.412 00 13.37 C

ATOM 1557 C LEU B 70 -9.403 -5.818 -20.467 00 13.50 C

ATOM 1558 O LEU B 70 -10.608 -5.602 -20.266 1.00 13.43 O Table 3

ATOM 1559 CB LEU B 70 -7.596 -5.533 -18.748 1.00 13.37 C

ATOM 1560 CG LEU B 70 -7,801 -4.643 -17.497 1.00 14.26 C

ATOM 1561 CDl LED B 70 -7,883 -3.160 -17.833 1.00 16.05 C

ATOM 1562 CD2 LEU B 70 -8.927 -5.080 -16.588 1.00 15.69 C

ATOM 1563 N SER B 71 -8.765 -5.501 -21.602 1.00 12.91 N

ATOM 1564 CA SER B 71 -9.362 -4.697 -22.672 1.00 12.76 C

ATOM 1565 C SER B 71 -10.588 -5.358 -23.291 1.00 12.81 C

ATOM 1566 O SER B 71 -11.421 -4.676 -23.901 1.00 12.83 O

ATOM 1567 CB SER B 71 -8.319 -4.351 -23.761 1.00 12.91 C

ATOM 1568 OG SER B 71 -8.188 -5.409 -24.712 1.00 13.26 O

ATOM 1569 N ILE B 72 -10.705 -6.675 -23.134 1.00 12.10 N

ATOM 1570 CA ILE B 72 -11.886 -7.384 -23.617 1.00 12.30 C

ATOM 1571 C ILE B 72 -12.745 -7.968 -22.486 1.00 12.28 C

ATOM 1572 O ILE B 72 -13.482 -8.934 -22.689 1.00 12.00 O

ATOM 1573 CB ILE B 72 -11.516 -8.464 -24.672 1.00 12.83 C

ATOM 1574 CGl ILE B 72 -10.566 -9.521 -24.086 1.00 12.68 C

ATOM 1575 CG2 ILE B 72 -10.936 -7.806 -25.947 1.00 12.12 C

ATOM 1576 CDl ILE B 72 -10.720 -10.872 -24.751 1.00 13.19 C

ATOM 1577 N GLY B 73 -12.634 -7.373 -21.298 1.00 12.35 N

ATOM 1578 CA GLY B 73 -13.582 -7.622 -20.211 1.00 12.13 C

ATOM 1579 C GLY B 73 -13.163 -8.582 -19.114 1.00 12.33 C

ATOM 1580 O GLY B 73 -14.016 -9.067 -18.372 1.00 12.68 O

ATOM 1581 N PHE B 74 -11.866 -8.366 -19.005 1.00 11.92 N

ATOM 1582 CA PHE B 74 -11.367 -9.796 -17.991 1.00 11.76 C

ATOM 1583 C PHE B 74 -11.193 -9.061 -16.665 1.00 11.69 C

ATOM 1584 O PHE B 74 -10.415 -8.100 -16.571 1.00 11.82 O

ATOM 1585 CB PHE B 74 -10.040 -10.408 -18.444 1.00 11.67 C

ATOM 1586 CG PHE B 74 -9.470 -11.451 -17.505 1.00 12.35 C

ATOM 1587 CDl PHE B 74 -10.143 -12.646 -17.263 1.00 13.31 C

ATOM 1588 CD2 PHE B 74 -8.225 -11.254 -16.907 1.00 12.15 C

ATOM 1589 CEl PHE B 74 -9.591 -13.622 -16.406 1.00 13.90 C

ATOM 1590 CE2 PHE B 74 -7.674 -12.204 -16.065 1.00 12.62 C

ATOM 1591 CZ PHE B 74 -8.354 -13.393 -15.814 1.00 12.55 C

ATOM 1592 N GLU B 75 -11.926 -9.514 -15.652 1.00 11.22 N

ATOM 1593 CA GLU B 75 -11.840 -8.942 -14.322 1.00 11.02 C

ATOM 1594 C GLU B 75 -11.912 -10.025 -13.265 1.00 10.97 C

ATOM 1595 O GLU B 75 -12.575 -11.037 -13.439 1.00 10.98 O

ATOM 1596 CB GLU B 75 -12.989 -7.956 -14.080 1.00 11.35 C

ATOM 1597 CG GLU B 75 -13.009 -7.382 -12.676 1.00 10.22 C

ATOM 1598 CD GLU B 75 -14.116 -6.385 -12.471 1.00 11.84 C

ATOM 1599 OEl GLU B 75 -15.298 -6.763 -12.678 1.00 11.06 O

ATOM 1600 OE2 GLU B 75 -13.792 -5.230 -12.090 1.00 11.44 O

ATOM 1601 N THR B 76 -11.286 -9.736 -12.136 1.00 10.63 N

ATOM 1602 CA THR B 76 -11.171 -10.640 -11.023 1.00 10.74 C

ATOM 1603 C THR B 76 -11.145 -9.747 -9.765 1.00 10.57 C

ATOM 1604 O THR B 76 -10.812 -8.558 -9.873 1.00 10.26 O

ATOM 1605 CB THR B 76 -9.836 -11.355 -11.238 1.00 11.40 C

ATOM 1606 OGl THR B 76 -10.038 -12.651 -11.851 1.00 12.14 O

ATOM 1607 CG2 THR B 76 -9.158 -11.595 -9.989 1.00 9.85 C

ATOM 1608 N CYS B 77 -11.536 -10.279 -8.598 1.00 9.30 N

ATOM 1609 CA CYS B 77 -11.235 -9.596 -7.334 1.00 9.12 C

ATOM 1610 C CYS B 77 -10.220 -10.411 -6.555 1.00 9.15 C

ATOM 1611 O CYS B 77 -10.353 -10.577 -5.346 1.00 8.54 O

ATOM 1612 CB CYS B 77 -12.488 -9.307 -6.469 1.00 9.00 C

ATOM 1613 SG CYS B 77 -12.188 -8.190 -5.029 1.00 8.08 S

ATOM 1614 N ARG B 78 -9.192 -10.894 -7.261 1.00 9.50 N

ATOM 1615 CA ARG B 78 -8.200 -11.810 -6.711 1.00 10.05 C

ATOM 1616 C ARG B 78 -6.780 -11.508 -7.182 1.00 9.84 C

ATOM 1617 O ARG B 78 -6.527 -11.402 -8.385 1.00 9.69 O

ATOM 1618 CB ARG B 78 -8.567 -13.236 -7.118 1.00 10.22 C

ATOM 1619 CG ARG B 78 -9.651 -13.861 -6.250 1.00 13.78 C

ATOM 1620 CD ARG B 78 -9.110 -14.950 -5.370 1.00 17.78 C

ATOM 1621 NE ARG B 78 -9.618 -14.832 -4.026 1.00 21.52 N

ATOM 1622 CZ ARG B 78 -9.176 -15.526 -3.001 1.00 21.74 C

ATOM 1623 NHl ARG B 78 -8.187 -16.415 -3.146 1.00 19.42 N

ATOM 1624 NH2 ARG B 78 -9.738 -15.325 -1.818 1.00 22.30 N

ATOM 1625 N TYR B 79 -5.853 -11.394 -6.234 1.00 9.31 N

ATOM 1626 CA TYR B 79 -4.443 -11.272 -6.569 1.00 9.80 C Table 3

ATOM 1627 C TYR B 79 3.903 -12.597 -7.077 1.00 9.95 C

ATOM 1628 O TYR B 79 4.205 -13.668 -6.529 1.00 10.45 O

ATOM 1629 CB TYR B 79 3.613 -10.791 -5.367 ,00 9.46 C

ATOM 1630 CG TYR B 79 -3 858 -9.332 -5.040 ,00 9.48 C

ATOM 1631 CDl TYR B 79 4.592 -8.980 -3.921 ,00 8.81 C

ATOM 1632 CD2 TYR B 79 3.375 -8.314 -5.867 ,00 6.76 C

ATOM 1633 CEl TYR B 79 4.835 -7.672 -3.614 ,00 9.36 C

ATOM 1634 CE2 TYR B 79 -3 605 -6.995 -5.564 ,00 8.36 C

ATOM 1635 CZ TYR B 79 -4.350 -6.675 -4.434 ,00 9.66 C

ATOM 1636 OH TYR B 79 -4.636 -5.365 -4.103 ,00 9.40 O

ATOM 1637 N GLY B 80 -3.109 12.516 -8.132 ,00 9.73 N

ATOM 1638 CA GLY B 80 -2.500 13.689 -8.721 ,00 9.94 C

ATOM 1639 C GLY B 80 -1.153 13.350 -9.325 ,00 10.16 C

ATOM 1640 O GLY B 80 -0.927 12.229 -9.774 ,00 9.68 .0

ATOM 1641 N PHE B 81 -0.261 14.335 -9.316 ,00 10.69 N

ATOM 1642 CA PHE B 81 1.051 14.198 -9.908 .00 10.87 C

ATOM 1643 C PHE B 81 0.987 14.009 -11.398 ,00 11.35 C

ATOM 1644 O PHE B 81 0.184 14.630 -12.090 ,00 11.12 O

ATOM 1645 CB PHE B 81 1.919 15.408 -9.574 ,00 10.76 C

ATOM 1646 CG PHE B 81 2.406 15.410 -8.168 ,00 10.28 C

ATOM 1647 CDl PHE B 81 1.823 16.230 -7.222 ,00 10.06 C

ATOM 1648 CD2 PHE B 81 3.439 14.558 -7.783 ,00 10.49 C

ATOM 1649 CEl PHE B 81 2.262 16.207 -5.918 ,00 10.53 C

ATOM 1650 CE2 PHE B 81 3.887 14.535 -6.482 ,00 10.87 C

ATOM 1651 CZ PHE B 81 3.301 15.365 -5.549 ,00 11.79 C

ATOM 1652 N ILE B 82 1.852 13.121 -11.853 ,00 12.08 N

ATOM 1653 CA ILE B 82 2.153 12.899 -13.251 ,00 13.11 C

ATOM 1654 C ILE B 82 3.680 12.913 -13.376 00 13.27 C

ATOM 1655 O ILE B 82 4.390 13.042 -12.375 00 13.27 O

ATOM 1656 CB ILE B 82 1.526 11.544 -13.662 00 13.38 C

ATOM 1657 CGl ILE B 82 0.532 11.737 -14.770 00 13.40 C

ATOM 1658 CG2 ILE B 82 2.521 10.408 -13.907 00 13.55 C

ATOM 1659 CDl ILE B 82 -0.810 11.827 -14.219 00 14.01 C

ATOM 1660 N GLϋ B 83 4.187 12.797 -14.594 00 13.40 N

ATOM 1661 CA GLU B 83 5.599 -12.575 -14.786 00 13.59 C

ATOM 1662 C GLU B 83 6.008 11.236 -14.145 1.00 13.29 C

ATOM 1663 O GLU B 83 5.496 10.165 -14.506 00 13.06 O

ATOM 1664 CB GLU B 83 5.912 12.594 -16.285 00 14.28 C

ATOM 1665 CG GLU B 83 7.336 12.950 -16.635 00 15.73 C

ATOM 1666 CD GLU B 83 7.767 14.315 -16.128 00 17.78 C

ATOM 1667 OEl GLU B 83 8.675 14.342 -15.277 00 17.66 O

ATOM 1668 OE2 GLU B 83 7.217 15.350 -16.581 00 18.85 O

ATOM 1669 N GLY B 84 6.907 11.316 -13.169 00 12.64 N

ATOM 1670 CA GLY B 84 7.476 10.127 -12.530 00 12.34 C

ATOM 1671 C GLY B 84 6.661 -9.449 -11.432 1.00 12.04 C

ATOM 1672 O GLY B 84 7.186 - 582 -10.742 1.00 12.66 O

ATOM 1673 N HIS B 85 5.390 -9.825 -11.266 1.00 11.48 N

ATOM 1674 CA HIS B 85 4.467 -9.101 -10.362 00 10.97 C

ATOM 1675 C HIS B 85 3.375 -9.991 -9.794 00 10.71 C

ATOM 1676 O HIS B 85 3.163 ^■11.119 -10.257 00 10.35 O

ATOM 1677 CB HIS B 85 3.745 -7.950 -11.082 00 11.11 C

ATOM 1678 CG HIS B 85 4.651 -6.977 -11.776 00 11.03 C

ATOM 1679 NDl HIS B 85 5.406 -6.043 -11.100 00 12.09 N

ATOM 1680 CD2 HIS B 85 4.894 -6.775 -13.093 00 10.39 C

ATOM 1681 CEl HIS B 85 6.089 -5.317 -11.971 1.00 10.65 C

ATOM 1682 NE2 HIS B 85 5.795 -5.741 -13.186 00 10.53 N

ATOM 1683 N VAL B 86 2.685 -9.457 -8.784 .00 10.44 N

ATOM 1684 CA VAL B 86 1.390 -9.966 -8.337 .00 9.75 C

ATOM 1685 C VAL B 86 0.364 -8.865 -8.644 1.00 10.45 C

ATOM 1686 O VAL B 86 0.508 -7.723 -8.183 .00 9.97 O

ATOM 1687 CB VAL B 86 1.388 -10.291 -6.821 .00 9.51 C

ATOM 1688 CGl VAL B 86 0.019 -10.819 -6.366 .00 7.51 C

ATOM 1689 CG2 VAL B 86 2.483 -11.287 -6.484 .00 7.56 C

ATOM 1690 N VAL B 87 0.664 -9.211 -9.424 1.00 10.43 N

ATOM 1691 CA VAL B 87 1.612 -8.223 -9.915 1.00 10.24 C

ATOM 1692 C VAL B 87 -3 063 -8.655 -9.714 1.00 10.58 C

ATOM 1693 O VAL B 87 3.341 -9.791 -9.330 1.00 10.65 O

ATOM 1694 CB VAL B 87 1.378 -7.890 -11.435 1.00 10.39 C Table 3

ATOM 1695 CGl VAL B 87 0.063 -7 526 11.715 00 9.32 C

ATOM 1696 CG2 VAL B 87 -1.796 9.043 12.316 00 9.63 C

ATOM 1697 N ILE B 88 -3.976 7.733 ^■10.007 00 10.69 N

ATOM 1698 CA ILE B 88 -5.405 973 -9.984 00 10.68 C

ATOM 1699 C ILE B 88 -5.966 135 ^■11.123 00 10.90 C

ATOM 1700 O ILE B 88 -5.678 936 ^•11.191 00 11.27 O

ATOM 1701 CB ILE B 88 -6.002 566 -8.601 00 11.13 C

ATOM 1702 CGl ILE B 88 -7.520 7.813 -8.538 00 10.92 C

ATOM 1703 CG2 ILE B 88 -5.620 6.105 -8.218 00 10.95 C

ATOM 1704 CDl ILE B 88 -8.086 7.748 -7.118 00 10.64 C

ATOM 1705 N PRO B 89 -6.694 7.763 12.052 00 10.75 N

ATOM 1706 CA PRO B 89 -7.332 7.037 ^■13.163 00 10.46 C

ATOM 1707 C PRO B 89 -8.682 6.427 ^•12.774 00 10.44 C

ATOM 1708 O PRO B 89 -9.593 7.147 ^■12.366 00 10.48 O

ATOM 1709 CB PRO B 89 -7.497 8.113 ^■14.245 00 10.44 C

ATOM 1710 CG PRO B 89 -7.571 9.424 13.497 00 10.21 C

ATOM 1711 CD PRO B 89 -6.903 9.221 ^■12.150 00 10.61 C

ATOM 1712 N ARG B 90 -8.794 -5.106 12.892 00 9.99 N

ATOM 1713 CA ARG B 90 -9.949 -4.387 ^•12.355 00 10.38 C

ATOM 1714 C ARG B 90 -10.638 -3.503 13.386 00 10.50 C

ATOM 1715 O ARG B 90 -9.980 -2.727 ^■14.080 1.00 10.11 O

ATOM 1716 CB ARG B 90 -9.515 -3.545 ^■11.161 00 10.09 C

ATOM 1717 CG ARG B 90 -9.321 -4.337 -9.889 00 10.94 C

ATOM 1718 CD ARG B 90 -10.583 -4.376 -9.054 00 13.99 C

ATOM 1719 NE ARG B 90 -11.318 -5.602 -9.243 00 14.59 N

ATOM 1720 CZ ARG B 90 -12.630 -5.751 -9.120 00 11.71 C

ATOM 1721 NHl ARG B 90 -13.434 -4 121 -8.843 00 11.69 N

ATOM 1722 NH2 ARG B 90 -13.130 ^■6.960 -9.304 00 9.39 N

ATOM 1723 N ILE B 91 -11.962 ^■3.635 ^■13.466 00 11.10 N

ATOM 1724 CA ILE B 91 -12.814 2.806 14.332 00 11.71 C

ATOM 1725 C ILE B 91 -13.839 2.003 13.520 00 12.42 C

ATOM 1726 O ILE B 91 -13.937 0.796 13.697 00 12.68 O

ATOM 1727 CB ILE B 91 -13.495 3.675 15.413 00 11.63 C

ATOM 1728 CGl ILE B 91 -12.441 ^■4.138 16.424 00 11.29 C

ATOM 1729 CG2 ILE B 91 -14.635 -2 903 16.103 00 11.70 C

ATOM 1730 CDl ILE B 91 -12.863 ^■5.283 17.334 00 8.82 C

ATOM 1731 N HIS B 92 -14.585 2.670 12.630 1.00 12.58 N

ATOM 1732 CA HIS B 92 -15.463 -1 975 11.688 00 13.09 C

ATOM 1733 C HIS B 92 -14.634 -1.363 - 10.574 00 13.54 C

ATOM 1734 O HIS B 92 -13.782 -2.039 995 00 14.26 O

ATOM 1735 CB HIS B 92 -16.482 -2.921 - 11.055 00 12.72 C

ATOM 1736 CG HIS B 92 -17.362 -3 .624 12.038 00 13.46 C

ATOM 1737 NDl HIS B 92 -18.626 3.172 12.365 00 13.98 N

ATOM 1738 CD2 HIS B 92 -17.172 4.759 12.749 00 12.37 C

ATOM 1739 CEl HIS B 92 -19.177 -4 004 13.229 00 13.94 C

ATOM 1740 NE2 HIS B 92 -18.314 -4.975 13.482 00 15.59 N

ATOM 1741 N PRO B 93 -14.859 -0.090 10.254 00 13.97 N

ATOM 1742 CA PRO B 93 -14.216 0.480 -9.072 00 14.51 C

ATOM 1743 C PRO B 93 -14.955 -0.030 -7.829 00 14.69 C

ATOM 1744 O PRO B 93 -16.121 0.307 -7.630 00 14.76 O

ATOM 1745 CB PRO B 93 -14.385 1.995 -9.259 00 14.70 C

ATOM 1746 CG PRO B 93 -15.070 2.165 10.609 00 14.55 C

ATOM 1747 CD PRO B 93 -15.741 0.877 10.933 00 13.81 C

ATOM 1748 N ASN B 94 -14.282 -0.864 -7.033 00 15.07 N

ATOM 1749 CA ASN B 94 -14.857 -1.460 -5.816 00 15.39 C

ATOM 1750 C ASN B 94 -13.897 -1.264 -4.633 00 15.41 C

ATOM 1751 O ASN B 94 -12.740 -1 ,698 -4.672 00 14.81 O

ATOM 1752 CB ASN B 94 -15.176 2.961 -6.040 00 15.61 C

ATOM 1753 CG ASN B 94 -15.913 ^•3.610 -4.852 00 16.74 C

ATOM 1754 ODl ASN B 94 -15.673 3.274 -3.700 00 17.82 O

ATOM 1755 ND2 ASN B 94 -16.808 4.553 -5.146 00 18.08 N

ATOM 1756 N SER B 95 -14.378 0.608 -3.579 00 15.61 N

ATOM 1757 CA SER B 95 -13.519 0.258 -2.430 00 16.35 C

ATOM 1758 C SER B 95 -12.781 1.446 -1.810 00 15.97 C

ATOM 1759 O SER B 95 -11.695 1.313 -1.269 00 16.44 O

ATOM 1760 CB SER B 95 -14.330 0.464 -1.354 00 16.18 C

ATOM 1761 OG SER B 95 -14.490 1.823 -1.735 00 19.32 O

ATOM 1762 N ILE B 96 -13.373 2.613 -1.918 1.00 15.61 N Table 3

ATOM 1763 CA ILE B 96 -12.826 -3.786 -1.293 1.00 16.27 C

ATOM 1764 C ILE B 96 -12.094 -4.645 -2.346 1.00 15.34 C

ATOM 1765 O ILE B 96 -11.677 -5.768 -2.067 1.00 15.79 O

ATOM 1766 CB ILE B 96 -14.004 -4.496 -0.538 1.00 16.62 C

ATOM 1767 CGl ILE B 96 -13.653 -4.738 0.921 1.00 17.63 C

ATOM 1768 CG2 ILE B 96 -14.621 -5.683 -1.312 1.00 17.18 C

ATOM 1769 CDl ILE B 95 -14.887 -5.095 1.778 1.00 17.95 C

ATOM 1770 N CYS B 97 -11.931 -4.090 -3.550 1.00 13.92 N

ATOM 1771 CA CYS B 97 -11.138 -4.736 -4.612 1.00 13.20 C

ATOM 1772 C CYS B 97 -10.001 -3.824 -5.090 1.00 12.90 C

ATOM 1773 O CYS B 97 -10.224 -2.871 -5.847 1.00 12.62 O

ATOM 1774 CB CYS B 97 -12.019 -5.172 -5.787 1.00 12.19 C

ATOM 1775 SG CYS B 97 -13.229 -6.452 -5.362 1.00 9.43 S

ATOM 1776 N ALA B 98 -8.780 -4.122 -4.644 1.00 12.56 N

ATOM 1777 CA ALA B 98 -7.637 -3.217 -4.863 1.00 12.26 C

ATOM 1778 C ALA B 98 -7.983 -1.758 -4.537 1.00 12.33 C

ATOM 1779 O ALA B 98 -7.619 -0.841 -5.263 1.00 12.40 O

ATOM 1780 CB ALA B 98 -7.101 -3.347 -6.272 1.00 12.07 C

ATOM 1781 N ALA B 99 -8.691 -1.563 -3.425 1.00 12.73 N

ATOM 1782 CA ALA B 99 -9.002 -0.232 -2.874 1.00 12.55 C

ATOM 1783 C ALA B 99 -9.569 0.727 -3.913 1.00 12.99 C

ATOM 1784 O ALA B 99 -9.148 1.880 -4.009 1.00 12.95 O

ATOM 1785 CB ALA B 99 -7.776 0.367 -2.182 1.00 12.22 C

ATOM 1786 N ASN B 100 -10.521 0.229 -4.699 1.00 13.17 N

ATOM 1787 CA ASN B 100 -11.250 1.048 -5.657 1.00 13.34 C

ATOM 1788 C ASN B 100 -10.467 1.403 -6.920 1.00 13.46 C

ATOM 1789 O ASN B 100 -10.985 2.085 -7.793 1.00 13.21 O

ATOM 1790 CB ASN B 100 -11.813 2.306 -4.987 1.00 13.09 C

ATOM 1791 CG ASN B 100 -13.164 2.690 -5.531 1.00 13.58 C

ATOM 1792 ODl ASN B 100 -13.393 3.844 -5.874 1.00 17.09 O

ATOM 1793 ND2 ASN B 100 -14.073 1.728 -5.615 1.00 11.88 N

ATOM 1794 N ASN B 101 -9.237 0.915 -7.023 1.00 13.40 N

ATOM 1795 CA ASN B 101 -8.453 1.076 -8.238 1.00 13.69 C

ATOM 1796 C ASN B 101 -8.984 0.268 -9.404 1.00 13.79 C

ATOM 1797 O ASN B 101 -9.733 -0.700 -9.232 1.00 13.78 O

ATOM 1798 CB ASN B 101 -6.987 0.745 -7.992 1.00 13.65 C

ATOM 1799 CG ASN B 101 -6.327 1.749 -7.087 1.00 14.94 C

ATOM 1800 ODl ASN B 101 -6.089 2.882 -7.481 1.00 18.15 O

ATOM 1801 ND2 ASN B 101 -6.046 1.350 -5.861 1.00 14.74 N

ATOM 1802 N THR B 102 -8.556 0.678 -10.593 1.00 13.92 N

ATOM 1803 CA THR B 102 -9.068 0.159 -11.839 1.00 13.92 C

ATOM 1804 C THR B 102 -7.872 0.015 -12.816 1.00 13.61 C

ATOM 1805 O THR B 102 -6.848 0.688 -12.650 1.00 12.91 O

ATOM 1806 CB THR B 102 -10.186 1.135 -12.293 1.00 14.15 C

ATOM 1807 OGl THR B 102 -11.400 0.422 -12.584 1.00 16.82 O

ATOM 1808 CG2 THR B 102 -9.822 1.938 -13.516 1.00 13.45 C

ATOM 1809 N GLY B 103 -7.988 -0.885 -13.790 1.00 13.27 N

ATOM 1810 CA GLY B 103 -6.841 -1.301 -14.612 1.00 13.28 C

ATOM 1811 C GLY B 103 -6.143 -2.538 -14.053 1.00 13.43 C

ATOM 1812 O GLY B 103 -6.654 -3.201 -13.150 1.00 13.60 O

ATOM 1813 N VAL B 104 -4.974 -2.862 -14.595 1.00 13.71 N

ATOM 1814 CA VAL B 104 -4.165 -3.952 -14.053 1.00 13.83 C

ATOM 1815 C VAL B 104 -3.334 -3.421 -12.882 1.00 14.23 C

ATOM 1816 O VAL B 104 -2.305 -2.763 -13.064 1.00 14.58 O

ATOM 1817 CB VAL B 104 -3.288 -4.617 -15.131 1.00 13.94 C

ATOM 1818 CGl VAL B 104 -2.560 -5.821 -14.551 1.00 13.96 C

ATOM 1819 CG2 VAL B 104 -4.145 -5.040 -16.326 1.00 12.30 C

ATOM 1820 N TYR B 105 -3.813 -3.687 -11.673 1.00 14.24 N

ATOM 1821 CA TYR B 105 -3.236 -3.101 -10.467 1.00 13.92 C

ATOM 1822 C TYR B 105 -2.139 -4.009 -9.900 1.00 14.12 C

ATOM 1823 O TYR B 105 -2.362 -5.202 -9.683 1.00 13.81 O

ATOM 1824 CB TYR B 105 -4.340 -2.834 -9.426 1.00 14.05 C

ATOM 1825 CG TYR B 105 -3.820 -2.310 -8.116 1.00 14.50 C

ATOM 1826 CDl TYR B 105 -3.619 -0.947 -7.921 1.00 14.85 C

ATOM 1827 CD2 TYR B 105 -3.492 -3.180 -7.079 1.00 14.52 C

ATOM 1828 CEl TYR B 105 -3.111 -0.470 -6.720 1.00 15.71 C

ATOM 1829 CE2 TYR B 105 -2.986 -2.712 -5.883 1.00 14.18 C

ATOM 1830 CZ TYR B 105 -2.795 -1.363 -5.711 1.00 14.25 C Table 3

ATOM 1831 OH TYR B 105 -2.292 -0.896 -4.524 00 15.02 O ATOM 1832 N ILE B 106 -0.964 -3.428 -9.660 00 14.07 N ATOM 1833 CA ILE B 106 0.184 -4.161 -9.139 00 14.58 C ATOM 1834 C ILE B 106 0.273 -4.030 -7.617 00 15.28 C ATOM 1835 O ILE B 106 0.334 -2.918 -7.077 00 14.78 O ATOM 1836 CB ILE B 106 1.502 -3.676 -9.813 00 14.49 C ATOM 1837 CGl ILE B 106 1.436 -3.890 -11.336 00 14.11 C ATOM 1838 CG2 ILE B 106 2.723 -4.356 -9.175 00 13.20 C ATOM 1839 CDl ILE B 106 2.384 -3.016 -12.131 00 16.17 C ATOM 1840 N LED B 107 0.270 -5.181 -6.943 00 16.11 N ATOM 1841 CA LEO B 107 0.417 -5.251 -5.501 00 16.95 C ATOM 1842 C LEU B 107 1.861 -4.970 -5.107 00 18.48 C ATOM 1843 O LEU B 107 2.781 -5.652 -5.556 00 17.93 O ATOM 1844 CB LEO B 107 -0.011 -6.633 -5.000 00 16.39 C ATOM 1845 CG LED B 107 0.016 -6.874 -3.491 00 16.10 C ATOM 1846 CDl LED B 107 -0.926 -5.921 -2.765 00 14.80 C ATOM 1847 CD2 LEU B 107 -0.321 -8.330 -3.174 00 16.01 C ATOM 1848 N THR B 108 2.059 -3.957 -4.269 00 20.62 N ATOM 1849 CA THR B 108 3.410 -3 600 -3.850 00 22.96 C ATOM 1850 C THR B 108 3.920 - -44.406 -2.650 00 24.65 C ATOM 1851 O THR B 108 5.120 -4.680 -2.555 00 25.50 O ATOM 1852 CB THR B 108 3.562 -2.082 -3.635 00 23.07 C ATOM 1853 OGl THR B 108 2.392 -1.557 -2. .991 00 23.09 O ATOM 1854 CG2 THR B 108 3.581 -1.362 -4. ,982 00 22.99 C ATOM 1855 N SER B 109 3.029 -4.800 -1.747 00 26.15 N ATOM 1856 CA SER B 109 3.425 -5.741 -0.701 00 27.72 C ATOM 1857 C SER B 109 3.033 -7.157 -1.136 00 28.54 C ATOM 1858 O SER B 109 1.942 -7.642 -0.799 00 28.80 O ATOM 1859 CB SER B 109 .828 -5.349 0.660 00 27.79 C ATOM 1860 OG SER B 109 .527 -5.882 0.848 00 29.06 O ATOM 1861 N ASN B 110 .928 -7.800 -1.892 00 29.49 N ATOM 1862 CA ASN B 110 .626 -9.046 -2.629 00 30.38 C ATOM 1863 C ASN B 110 .385 -10.285 -2.130 00 30.71 C ATOM 1864 O ASN B 110 .866 -11.106 -2.937 00 30.61 O ATOM 1865 CB ASN B 110 .884 -8.848 -4.134 00 30.57 C ATOM 1866 CG ASN B 110 5.341 -8.465 -4.455 00 32.09 C ATOM 1867 ODl ASN B 110 6.227 -8.554 -3.603 1.00 33.40 O ATOM 1868 ND2 ASN B 110 5.586 -8.042 -5.699 1.00 31.99 N ATOM 1869 N THR B 111 4.452 -10.427 -0.805 1.00 30.45 N ATOM 1870 CA THR B 111 5.402 -11.337 -0.162 00 30.40 C ATOM 1871 C THR B 111 4.984 -12.803 -0.173 00 29.17 C ATOM 1872 O THR B 111 .838 -13.698 -0.166 1.00 30.23 O ATOM 1873 CB THR B 111 .626 -10.909 1.314 00 30.79 C ATOM 1874 OGl THR B 111 .599 -9.480 1.424 00 31.90 O ATOM 1875 CG2 THR B 111 .024 -11.296 1.790 00 31.68 C ATOM 1876 N SER B 112 3.678 -13.043 -0.184 00 27.15 N ATOM 1877 CA SER B 112 3.127 -14.321 0.257 00 24.72 C ATOM 1878 C SER B 112 2.692 -15.241 -0.890 00 22.70 C ATOM 1879 O SER B 112 3.266 -15.200 -1.980 00 22.54 O ATOM 1880 CB SER B 112 1.963 -14.041 1.221 00 24.77 C ATOM 1881 OG SER B 112 1.629 -15.189 1.994 00 26.30 O ATOM 1882 N GLN B 113 1.698 -16.087 -0.612 00 20.06 N ATOM 1883 CA GLN B 113 1.047 -16.929 -1.608 00 18.21 C ATOM 1884 C GLN B 113 -0.219 -16.235 -2.113 00 16.14 C ATOM 1885 O GLN B 113 -0.881 -15.514 -1.359 00 15.27 O ATOM 1886 CB GLN B 113 0.699 -18.299 -1.012 00 18.08 C ATOM 1887 CG GLN B 113 1.918 -19.093 -0.528 00 18.45 C ATOM 1888 CD GLN B 113 1.566 -20.380 0.237 00 20.23 C ATOM 1889 OEl GLN B 113 2.430 -21.243 0.406 00 24.60 O ATOM 1890 NE2 GLN B 113 0.322 -20.502 0.711 00 20.19 N ATOM 1891 N TYR B 114 -0.552 -16.450 -3.385 00 13.84 N ATOM 1892 CA TYR B 114 -1.748 -15.845 -3.994 00 12.08 C ATOM 1893 C TYR B 114 -2.448 -16.883 -4.868 00 11.45 C ATOM 1894 O TYR B 114 -2.292 -18.080 -4.624 00 11.36 O ATOM 1895 CB TYR B 114 -1.371 -14.576 -4.770 00 11.68 C ATOM 1896 CG TYR B 114 -0.736 -13.562 -3.861 00 11.55 C ATOM 1897 CDl TYR B 114 0.658 -13.432 -3.786 00 11.08 C ATOM 1898 CD2 TYR B 114 -1.521 -12.797 -2.993 1.00 10.32 C Table 3

ATOM 1899 CEl TYR B 114 1.248 -12.517 -2.898 00 11.44 C

ATOM 1900 CE2 TYR B 114 -0.945 -11.889 -2.112 00 11.67 C

ATOM 1901 CZ TYR B 114 0.438 -11.753 -2.068 00 12.13 C

ATOM 1902 OH TYR B 114 0.993 -10.844 -1.187 00 13.43 O

ATOM 1903 N ASP B 115 -3.244 -16.439 -5.843 00 10.31 N

ATOM 1904 CA ASP B 115 .679 -17.316 -6.917 00 9.45 C

ATOM 1905 C ASP B 115 .626 -17.167 -8.011 00 8.86 C

ATOM 1906 O ASP B 115 .533 -16.641 -7.759 00 8.90 O

ATOM 1907 CB ASP B 115 .046 -16.900 -7.467 00 9.13 C

ATOM 1908 CG ASP B 115 -6.170 -16.969 -6.429 00 10.12 C

ATOM 1909 ODl ASP B 115 .978 -17.564 -5.347 00 7.97 O

ATOM 1910 OD2 ASP B 115 .300 -16.451 -6.632 00 8.31 O

ATOM 1911 N THR B 116 .955 -17.601 -9.225 00 67 N

ATOM 1912 CA THR B 116 .105 -17.314 -10.371 00 40 C

ATOM 1913 C THR B 116 .918 -17.015 -11.614 00 78 C

ATOM 1914 O THR B 116 .065 -17.458 -11.740 00 32 O

ATOM 1915 CB THR B 116 .058 -18.462 -10.608 00 38 C

ATOM 1916 OGl THR B 116 -0.037 -18.018 -11.510 1.00 40 O

ATOM 1917 CG2 THR B 116 -1 676 -19.704 -11.289 00 6.14 C

ATOM 1918 N TYR B 117 ^■2.325 -16.225 -12.505 00 7.99 N

ATOM 1919 CA TYR B 117 ^■2.781 -16.137 -13.884 00 8.30 C

ATOM 1920 C TYR B 117 -1 845 -16.969 -14.775 00 8.56 C

ATOM 1921 O TYR B 117 0.709 -17.229 -14.400 00 7.86 O

ATOM 1922 CB TYR B 117 2.889 -14.667 -14.329 00 8.39 C

ATOM 1923 CG TYR B 117 -3. 856 -13.918 -13.452 00 8.06 C

ATOM 1924 CDl TYR B 117 -3. 418 -13.231 -12.315 00 8.58 C

ATOM 1925 CD2 TYR B 117 -5.216 -13.950 -13.717 00 7.69 C

ATOM 1926 CEl TYR B 117 -4.316 -12.578 -11.481 00 7.47 C

ATOM 1927 CE2 TYR B 117 -6..117 -13.294 -12.896 00 8.36 C

ATOM 1928 CZ TYR B 117 -5..652 -12.609 -11.781 00 7.95 C

ATOM 1929 OH TYR B 117 -6.552 -11.972 -10.968 00 O

ATOM 1930 N CYS B 118 364 -17.426 -15.915 00 N

ATOM 1931 CA CYS B 118 614 -18.208 -16.899 00 9.51 C

ATOM 1932 C CYS B 118 986 -17.716 -18.304 00 10.02 C

ATOM 1933 O CYS B 118 075 -17.187 -18.502 00 10.50 O

ATOM 1934 CB CYS B 118 .941 -19.697 -16.764 00 9.18 C

ATOM 1935 SG CYS B 118 .476 -20.427 -15.181 00 8.45 S

ATOM 1936 N PHE B 119 .085 -17.886 -19.265 00 10.60 N

ATOM 1937 CA PHE B 119 .351 -17.514 -20.647 00 11.58 C

ATOM 1938 C PHE B 119 .103 -18.698 -21.548 00 12.69 C

ATOM 1939 O PHE B 119 0.008 -19.228 -21.594 00 12.84 O

ATOM 1940 CB PHE B 119 ^■0.454 -16.355 -21.093 00 11.51 C

ATOM 1941 CG PHE B 119 ^■0.571 -16.026 -22.569 00 11.58 C

ATOM 1942 CDl PHE B 119 -1 602 -15.220 -23.042 00 12.42 C

ATOM 1943 CD2 PHE B 119 0.345 -16.542 -23.487 00 12.47 C

ATOM 1944 CEl PHE B 119 ^■1.717 -14.920 -24.417 00 12.42 C

ATOM 1945 CE2 PHE B 119 0.238 -16.251 -24.848 00 11.87 C

ATOM 1946 CZ PHE B 119 ^•0.801 -15.438 -25.311 00 11.50 C

ATOM 1947 N ASN B 120 135 -19.092 -22.278 00 14.04 N

ATOM 1948 CA ASN B 120 047 -20.200 -23.218 00 15.76 C

ATOM 1949 C ASN B 120 926 -19.613 -24.613 00 16.28 C

ATOM 1950 O ASN B 120 875 -19.012 -25.128 00 16.55 O

ATOM 1951 CB ASN B 120 •3.298 -21.071 -23.094 00 15.94 C

ATOM 1952 CG ASN B 120 •3.235 -22.350 -23.929 00 17.92 C

ATOM 1953 ODl ASN B 120 ^■4.113 -23.200 -23.803 1.00 19.87 O

ATOM 1954 ND2 ASN B 120 ^■2.226 -22.486 -24.781 00 18.37 N

ATOM 1955 N ALA B 121 -0 745 -19.772 -25.202 00 16.86 N

ATOM 1956 CA ALA B 121 0.438 -19.261 -26.539 00 17.82 C

ATOM 1957 C ALA B 121 1.277 -19.894 -27.659 00 18.60 C

ATOM 1958 O ALA B 121 -1 453 -19.298 -28.722 00 18.98 O

ATOM 1959 CB ALA B 121 1.052 -19.424 -26.831 00 17.59 C

ATOM 1960 N SER B 122 .804 -21.089 -27.424 00 19.42 N

ATOM 1961 CA SER B 122 .576 -21.768 -28.456 00 20.54 C

ATOM 1962 C SER B 122 .088 -21.679 -28.228 00 20.80 C

ATOM 1963 O SER B 122 .861 -22.439 -28.811 00 21.48 O

ATOM 1964 CB SER B 122 -2.074 -23.211 -28.665 00 20.60 C

ATOM 1965 OG SER B 122 -2.423 -24.058 -27.595 00 21.98 O

ATOM 1966 N ALA B 123 -4.505 -20.721 -27.401 1.00 20.87 N Table 3

ATOM 1967 CA ALA B 123 -5.924 -20.449 -27.174 1.00 20.87 C

ATOM 1968 C ALA B 123 -6.520 -19.602 -28.303 1.00 21.19 C

ATOM 1969 O ALA B 123 -5.796 -18.870 -28.981 1.00 21.28 O

ATOM 1970 CB ALA B 123 -6.115 -19.740 -25.842 1.00 21.08 C

ATOM 1971 N PRO B 124 -7.836 -19.700 -28.503 1.00 21.46 N

ATOM 1972 CA PRO B 124 -8.569 -18.778 -29.394 1.00 21.68 C

ATOM 1973 C PRO B 124 -8.343 -17.293 -29.026 1.00 21.78 C

ATOM 1974 O PRO B 124 -8.026 -17.006 -27.866 1.00 21.76 O

ATOM 1975 CB PRO B 124 -10.031 -19.160 -29.153 1.00 21.62 C

ATOM 1976 CG PRO B 124 -9.983 -20.592 -28.702 1.00 22.28 C

ATOM 1977 CD PRO B 124 -8.722 -20.716 -27.901 1.00 21.43 C

ATOM 1978 N PRO B 125 -8.520 -16.371 -29.984 1.00 21.54 N

ATOM 1979 CA PRO B 125 -8.138 -14.955 -29.815 1.00 21.65 C

ATOM 1980 C PRO B 125 -8.976 -14.082 -28.861 1.00 21.42 C

ATOM 1981 O PRO B 125 -8.499 -13.012 -28.413 1.00 21.99 O

ATOM 1982 CB PRO B 125 -8.264 -14.388 -31.241 1.00 21.83 C

ATOM 1983 CG PRO B 125 -8.366 -15.590 -32.132 1.00 21.61 C

ATOM 1984 CD PRO B 125 -9.079 -16.617 -31.324 1.00 21.82 C

ATOM 1985 N GLU B 126 -10.202 -14.498 -28.568 1.00 20.51 N

ATOM 1986 CA GLU B 126 -11.101 -13.666 -27.751 1.00 19.64 C

ATOM 1987 C GLO B 126 -11.439 -14.391 -26.448 1.00 19.34 C

ATOM 1988 O GLO B 126 -10.531 -14.763 -25.693 1.00 19.70 O

ATOM 1989 CB GLU B 126 -12.359 -13.297 -28.550 1.00 19.40 C

ATOM 1990 CG GLU B 126 -12.102 -12.350 -29.723 1.00 18.61 C

ATOM 1991 CD GLU B 126 -12.082 -10.883 -29.307 1.00 18.59 C

ATOM 1992 OEl GLO B 126 -12.378 -10.575 -28.132 1.00 16.00 O

ATOM 1993 OE2 GLU B 126 -11.778 -10.023 -30.159 1.00 18.90 O

ATOM 1994 N GLU B 127 -12.722 -14.614 -26.190 1.00 18.83 N

ATOM 1995 CA GLU B 127 -13.138 -15.373 -25.016 1.00 18.69 C

ATOM 1996 C GLU B 127 -13.479 -16.828 -25.331 1.00 18.93 C

ATOM 1997 O GLO B 127 -14.319 -17.109 -26.187 1.00 19.15 O

ATOM 1998 CB GLO B 127 -14.315 -14.705 -24.307 1.00 18.46 C

ATOM 1999 CG GLU B 127 -14.580 -15.299 -22.933 1.00 16.89 C

ATOM 2000 CD GLU B 127 -15.716 -14.614 -22.205 1.00 16.30 C

ATOM 2001 OEl GLU B 127 -16.010 -13.431 -22.529 1.00 14.58 O

ATOM 2002 OE2 GLU B 127 -16.308 -15.265 -21.314 1.00 14.38 O

ATOM 2003 N ASP B 128 -12.824 -17.739 -24.615 1.00 19.02 N

ATOM 2004 CA ASP B 128 -13.037 -19.178 -24.771 1.00 19.08 C

ATOM 2005 C ASP B 128 -13.410 -19.777 -23.419 1.00 18.84 C

ATOM 2006 O ASP B 128 -12.617 -19.756 -22.482 1.00 18.71 O

ATOM 2007 CB ASP B 128 -11.766 -19.837 -25.348 1.00 19.20 C

ATOM 2008 CG ASP B 128 -11.869 -21.364 -25.456 1.00 19.98 C

ATOM 2009 ODl ASP B 128 -12.981 -21.922 -25.396 1.00 19.93 O

ATOM 2010 OD2 ASP B 128 -10.872 -22.095 -25.617 1.00 21.25 O

ATOM 2011 N CYS B 129 -14.628 -20.295 -23.325 1.00 19.25 N

ATOM 2012 CA CYS B 129 -15.152 -20.866 -22.079 1.00 19.99 C

ATOM 2013 C CYS B 129 -15.256 -22.388 -22.139 1.00 19.82 C

ATOM 2014 O CYS B 129 -15.846 -23.003 -21.261 1.00 19.65 O

ATOM 2015 CB CYS B 129 -16.510 -20.253 -21.739 1.00 20.00 C

ATOM 2016 SG CYS B 129 -16.391 -18.519 -21.232 1.00 22.16 S

ATOM 2017 N THR B 130 -14.683 -22.976 -23.187 1.00 20.34 N

ATOM 2018 CA THR B 130 -14.615 -24.427 -23.347 1.00 20.90 C

ATOM 2019 C THR B 130 -14.135 -25.098 -22.057 1.00 20.97 C

ATOM 2020 O THR B 130 -13.176 -24.644 -21.432 1.00 21.24 O

ATOM 2021 CB THR B 130 -13.688 -24.772 -24.519 1.00 21.04 C

ATOM 2022 OGl THR B 130 -14.299 -24.323 -25.739 1.00 21.60 O

ATOM 2023 CG2 THR B 130 -13.563 -26.300 -24.702 1.00 22.00 C

ATOM 2024 N SER B 131 -14.829 -26.158 -21.657 1.00 21.21 N

ATOM 2025 CA SER B 131 -14.481 -26.904 -20.454 1.00 21.54 C

ATOM 2026 C SER B 131 -13.082 -27.491 -20.525 1.00 21.10 C

ATOM 2027 O SER B 131 -12.704 -28.088 -21.528 1.00 21.33 O

ATOM 2028 CB SER B 131 -15.516 -27.993 -20.183 1.00 21.75 C

ATOM 2029 OG SER B 131 -16.617 ^■27.441 -19.472 1.00 23.70 O

ATOM 2030 N VAL B 132 -12.310 •27.286 -19.462 1.00 20.65 N

ATOM 2031 CA VAL B 132 -10.985 -27.876 -19.344 1.00 20.03 C

ATOM 2032 C VAL B 132 -11.141 •29.132 -18.498 1.00 20.25 C

ATOM 2033 O VAL B 132 -11.557 ^■29.062 -17.333 1.00 20.59 O

ATOM 2034 CB VAL B 132 -9.958 ^■26.863 -18.745 1.00 20.17 C Table 3

ATOM 2035 CGl VAL B 132 -8.577 -27.498 -18.564 1.00 19.23 C

ATOM 2036 CG2 VAL B 132 -9.849 -25.643 -19.641 1.00 18.82 C

ATOM 2037 N THR B 133 -10.843 -30.285 -19.098 1.00 19.94 N

ATOM 203B CA THR B 133 -11.175 -31.570 -18.477 1.00 19.91 C

ATOM 2039 C THR B 133 -9.968 -32.348 -17.944 1.00 19.27 C

ATOM 2040 O THR B 133 -10.111 -33.497 -17.541 1.00 19.08 O

ATOM 2041 CB THR B 133 -12.005 -32.455 -19.433 1.00 20.25 C

ATOM 2042 OGl THR B 133 -11.210 -32.795 -20.576 1.00 21.18 O

ATOM 2043 CG2 THR B 133 -13.200 -31.671 -20.008 1.00 20.71 C

ATOM 2044 N ASP B 134 -8.786 -31.729 -17.963 1.00 18.52 N

ATOM 2045 CA ASP B 134 -7.640 -32.256 -17.227 1.00 18.10 C

ATOM 2046 C ASP B 134 -6.501 -31.246 -17.130 1.00 17.45 C

ATOM 2047 O ASP B 134 -6.556 -30.166 -17.733 1.00 16.61 O

ATOM 2048 CB ASP B 134 -7.152 -33.597 -17.807 1.00 18.45 C

ATOM 2049 CG ASP B 134 -6.368 -33.446 -19.110 1.00 20.18 C

ATOM 2050 ODl ASP B 134 -6.173 -32.315 -19.624 1.00 21.74 O

ATOM 2051 OD2 ASP B 134 -5.886 -34.435 -19.689 1.00 22.30 O

ATOM 2052 N LEU B 135 -5.489 -31.605 -16.339 1.00 16.84 N

ATOM 2053 CA LEU B 135 -4.219 -30.885 -16.295 1.00 16.29 C

ATOM 2054 C LEU B 135 -3.285 -31.626 -17.269 1.00 16.10 C

ATOM 2055 O LEU B 135 -2.728 -32.669 -16.928 1.00 15.51 O

ATOM 2056 CB LEU B 135 -3.680 -30.875 -14.859 1.00 16.25 C

ATOM 2057 CG LEU B 135 -2.519 -29.951 -14.511 1.00 15.86 C

ATOM 2058 CDl LEU B 135 -2.942 -28.500 -14.651 1.00 14.41 C

ATOM 2059 CD2 LEU B 135 -2.012 -30.223 -13.105 1.00 15.94 C

ATOM 2060 N PRO B 136 -3.166 -31.112 -18.496 1.00 16.18 N

ATOM 2061 CA PRO B 136 -2.594 -31.880 -19.611 1.00 16.44 C

ATOM 2062 C PRO B 136 -1.088 -32.174 -19.535 1.00 16.97 C

ATOM 2063 O PRO B 136 -0.S20 -33.126 -20.171 1.00 17.27 O

ATOM 2064 CB PRO B 136 -2.908 -31.004 -20.838 1.00 16.56 C

ATOM 2065 CG PRO B 136 -3.023 -29.610 -20.284 1.00 15.81 C

ATOM 2066 CD PRO B 136 -3.603 -29.766 -18.919 1.00 15.81 C

ATOM 2067 N ASN B 137 -0.337 -31.370 -18.789 1.00 17.08 N

ATOM 2068 CA ASN B 137 1.112 -31.546 -18.722 1.00 17.45 C

ATOM 2069 C ASN B 137 1.572 -31.775 -17.279 1.00 17.32 C

ATOM 2070 O ASN B 137 2.634 -31.316 -16.846 1.00 17.52 O

ATOM 2071 CB ASN B 137 1.824 -30.368 -19.397 1.00 17.81 C

ATOM 2072 CG ASN B 137 3.310 -30.609 -19.599 1.00 19.71 C

ATOM 2073 ODl ASN B 137 4.124 -29.709 -19.369 1.00 22.42 O

ATOM 2074 ND2 ASN B 137 3.678 -31.824 -20.018 1.00 19.92 N

ATOM 2075 N ALA B 138 0.743 -32.503 -16.540 1.00 16.57 N

ATOM 2076 CA ALA B 138 1.081 -32.954 -15.213 1.00 16.25 C

ATOM 2077 C ALA B 138 1.929 -34.213 -15.352 1.00 16.32 C

ATOM 2078 O ALA B 138 2.027 -34.785 -16.439 1.00 16.21 O

ATOM 2079 CB ALA B 138 -0.197 -33.237 -14.423 1.00 16.32 C

ATOM 2080 N PHE B 139 2.567 -34.636 -14.268 1.00 16.11 N

ATOM 2081 CA PHE B 139 3.322 -35.886 -14.306 1.00 16.21 C

ATOM 2082 C PHE B 139 2.756 -36.868 -13.283 1.00 16.64 C

ATOM 2083 O PHE B 139 1.745 -36.577 -12.642 1.00 16.32 O

ATOM 2084 CB PHE B 139 4.850 -35.668 -14.158 1.00 15.28 C

ATOM 2085 CG PHE B 139 5.251 -34.701 -13.059 1.00 14.26 C

ATOM 2086 CDl PHE B 139 5.487 -35.153 -11.767 1.00 12.08 C

ATOM 2087 CD2 PHE B 139 5.442 -33.341 -13.337 1.00 13.04 C

ATOM 2088 CEl PHE B 139 5.874 -34.266 -10.756 1.00 12.13 C

ATOM 2089 CE2 PHE B 139 5.827 -32.443 -12.324 1.00 11.38 C

ATOM 2090 CZ PHE B 139 6.033 -32.903 -11.038 1.00 11.98 C

ATOM 2091 N ASP B 140 3.409 -38.022 -13.164 1.00 17.37 N

ATOM 2092 CA ASP B 140 3.042 -39.096 -12.241 1.00 18.23 C

ATOM 2093 C ASP B 140 3.023 -38.644 -10.791 1.00 17.65 C

ATOM 2094 O ASP B 140 3.898 -37.900 -10.344 1.00 18.03 O

ATOM 2095 CB ASP B 140 4.060 -40.232 -12.370 1.00 19.31 C

ATOM 2096 CG ASP B 140 3.555 -41.372 -13.206 1.00 23.41 C

ATOM 2097 ODl ASP B 140 2.765 -42.186 -12.657 1.00 29.41 O

ATOM 2098 OD2 ASP B 140 3.899 -41.555 -14.401 1.00 26.63 O

ATOM 2099 N GLY B 141 2.041 -39.114 -10.045 1.00 17.16 N

ATOM 2100 CA GLY B 141 1.969 -38.794 -8.634 1.00 17.10 C

ATOM 2101 C GLY B 141 0.687 -39.281 -7.996 1.00 17.07 C

ATOM 2102 O GLY B 141 -0.231 -39.723 -8.691 1.00 17.12 O Table 3

ATOM 2103 N PRO B 142 0.634 -39.215 -6.671 1.00 17.13 N

ATOM 2104 CA PRO B 142 -0.508 -39.694 -5.906 1.00 17.39 C

ATOM 2105 C PRO B 142 -1.583 -38.649 -5.600 1.00 17.66 C

ATOM 2106 O PRO B 142 -2.555 -38.978 -4.918 1.00 18.13 O

ATOM 2107 CB PRO B 142 0.141 -40.096 -4.583 1.00 17.28 C

ATOM 2108 CG PRO B 142 1.202 -39.077 -4.398 1.00 17.44 C

ATOM 2109 CD PRO B 142 1.721 -38.747 -5.789 1.00 17.14 C

ATOM 2110 N ILE B 143 -1.409 -37.405 -6.055 1.00 17.42 N

ATOM 2111 CA ILE B 143 -2.364 -36.349 -5.714 1.00 16.48 C

ATOM 2112 C ILE B 143 -3.622 -36.470 -6.572 1.00 16.32 C

ATOM 2113 O ILE B 143 -3.546 -36.627 -7.788 1.00 16.77 O

ATOM 2114 CB ILE B 143 -1.743 -34.911 -5.855 1.00 16.66 C

ATOM 2115 CGl ILE B 143 -0.315 -34.828 -5.280 1.00 15.70 C

ATOM 2116 CG2 ILE B 143 -2.667 -33.845 -5.230 1.00 15.09 C

ATOM 2117 CDl ILE B 143 -0.197 -35.130 -3.779 1.00 14.67 C

ATOM 2118 N THR B 144 -4.772 -36.417 -5.916 1.00 15.81 N

ATOM 2119 CA THR B 144 -6.057 -36.229 -6.572 1.00 15.25 C

ATOM 2120 C THR B 144 -6.197 -34.762 -6.989 1.00 14.96 C

ATOM 2121 O THR B 144 -6.444 -33.883 -6.154 1.00 14.74 O

ATOM 2122 CB THR B 144 -7.183 -36.615 -5.591 1.00 15.51 C

ATOM 2123 OGl THR B 144 -7.138 -38.029 -5.337 1.00 15.95 O

ATOM 2124 CG2 THR B 144 -8.559 -36.383 -6.200 1.00 14.05 C

ATOM 2125 N ILE B 145 -6.032 -34.508 -8.284 1.00 14.89 N

ATOM 2125 CA ILE B 145 -6.130 -33.166 -8.847 1.00 14.28 C

ATOM 2127 C ILE B 145 -7.480 -32.969 -9.538 1.00 14.38 C

ATOM 2128 O ILE B 145 -7.802 -33.661 -10.499 1.00 14.28 O

ATOM 2129 CB ILE B 145 -4.963 -32.900 -9.848 1.00 14.47 C

ATOM 2130 CGl ILE B 145 -3.598 -32.941 -9.139 1.00 13.52 C

ATOM 2131 CG2 ILE B 145 -5.173 -31.556 -10.605 1.00 13.01 C

ATOM 2132 CDl ILE B 145 -2.413 -33.122 -10.104 1.00 13.94 C

ATOM 2133 N THR B 146 -8.245 -31.990 -9.064 1.00 14.80 N

ATOM 2134 CA THR B 146 -9.562 -31.686 -9.638 1.00 14.72 C

ATOM 2135 C THR B 146 -9.558 -30.349 -10.359 1.00 15.03 C

ATOM 2136 O THR B 146 -9.213 -29.330 -9.773 1.00 15.26 O

ATOM 2137 CB THR B 146 -10.633 -31.693 -8.533 1.00 14.43 C

ATOM 2138 OGl THR B 146 -10.596 -32.953 -7.859 1.00 14.34 O

ATOM 2139 CG2 THR B 146 -12.035 -31.655 -9.117 1.00 13.24 C

ATOM 2140 N ILE B 147 -9.921 -30.366 -11.638 1.00 15.20 N

ATOM 2141 CA ILE B 147 -10.167 -29.143 -12.373 1.00 15.88 C

ATOM 2142 C ILE B 147 -11.640 -28.786 -12.225 1.00 16.67 C

ATOM 2143 O ILE B 147 -12.517 -29.605 -12.521 1.00 16.84 O

ATOM 2144 CB ILE B 147 -9.798 -29.289 -13.874 1.00 15.83 C

ATOM 2145 CGl ILE B 147 -8.398 -29.907 -14.063 1.00 14.43 C

ATOM 2146 CG2 ILE B 147 -9.964 -27.947 -14.585 1.00 15.43 C

ATOM 2147 CDl ILE B 147 -7.230 -29.087 -13.501 1.00 13.73 C

ATOM 2148 N VAL B 148 -11.898 -27.571 -11.745 1.00 17.63 N

ATOM 2149 CA VAL B 148 -13.257 -27.084 -11.526 1.00 18.38 C

ATOM 2150 C VAL B 148 -13.524 -25.922 -12.468 1.00 19.20 C

ATOM 2151 O VAL B 148 -12.907 -24.853 -12.356 1.00 19.14 O

ATOM 2152 CB VAL B 148 -13.509 -26.663 -10.046 1.00 18.52 C

ATOM 2153 CGl VAL B 148 -14.987 -26.264 -9.832 1.00 18.45 C

ATOM 2154 CG2 VAL B 148 -13.122 -27.792 -9.072 1.00 18.31 C

ATOM 2155 N ASN B 149 -14.428 -26.142 -13.416 1.00 20.10 N

ATOM 2156 CA ASN B 149 -14.811 -25.093 -14.351 1.00 21.11 C

ATOM 2157 C ASN B 149 -15.830 -24.160 -13.699 1.00 22.01 C

ATOM 2158 O ASN B 149 -16.257 -24.395 -12.553 1.00 21.97 O

ATOM 2159 CB ASN B 149 -15.317 -25.682 -15.678 1.00 21.14 C

ATOM 2160 CG ASN B 149 -14.226 -26.441 -16.440 1.00 21.14 C

ATOM 2161 ODl ASN B 149 -13.521 -25.869 -17.267 1.00 22.22 O

ATOM 2162 ND2 ASN B 149 -14.076 -27.723 -16.142 1.00 21.66 N

ATOM 2163 N ARG B 150 -16.189 -23.090 -14.404 1.00 22.76 N

ATOM 2164 CA ARG B 150 -17.009 -22.022 -13.818 1.00 24.13 C

ATOM 2165 C ARG B 150 -18.392 -22.507 -13.378 1.00 24.93 C

ATOM 2166 O ARG B 150 -19.032 -21.895 -12.510 1.00 24.98 O

ATOM 2167 CB ARG B 150 -17.147 -20.849 -14.793 1.00 24.06 C

ATOM 2168 CG ARG B 150 -17.834 -21.209 -16.085 1.00 24.21 C

ATOM 2169 CD ARG B 150 -18.155 -20.008 -16.954 1.00 24.90 C

ATOM 2170 NE ARG B 150 -18.935 -20.391 -18.122 1.00 24.36 N Table 3

ATOM 2171 CZ ARG B 150 -19.391 -19.538 -19.025 25.38 C ATOM 2172 NHl ARG B 150 -19.145 -18.237 -18.898 23.68 N ATOM 2173 NH2 ARG B 150 -20.091 -19.990 -20.060 25.01 N ATOM 2174 N ASP B 151 -18.838 -23.611 -13.977 25.59 N ATOM 2175 CA ASP B 151 -20.125 -24.187 -13.647 26.56 C ATOM 2176 C ASP B 151 -20.064 -25.281 -12.569 26.55 C ATOM 2177 O ASP B 151 -21.059 -25.963 -12.318 26.98 O ATOM 2178 CB ASP B 151 -20.808 -24.696 -14.915 26.89 C ATOM 2179 CG ASP B 151 -20.112 -25.881 -15.527 28.24 C ATOM 2180 ODl ASP B 151 -18.963 -26.190 -15.144 29.98 O ATOM 2181 OD2 ASP B 151 -20.650 -26.567 -16.421 30.94 O ATOM 2182 N GLY B 152 -18.903 -25.446 -11.939 26.52 N ATOM 2183 CA GLY B 152 -18.747 -26.401 -10.834 26.54 C ATOM 2184 C GLY B 152 -18.493 -27.855 -11.215 26.51 C ATOM 2185 O GLY B 152 -18.263 -28.695 -10.343 26.43 O ATOM 2186 N THR B 153 -18.542 -28.156 -12.510 26.41 N ATOM 2187 CA THR B 153 -18.240 -29.494 -13.026 26.54 C ATOM 2188 C THR B 153 -16.780 -29.862 -12.732 26.52 C ATOM 2189 O THR B 153 -15.874 -29.086 -13.021 26.62 O ATOM 2190 CB THR B 153 -18.521 -29.545 -14.548 26.84 C ATOM 2191 OGl THR B 153 -19.893 -29.204 -14.795 1.00 25.73 O ATOM 2192 CG2 THR B 153 -18.410 -30.969 -15.085 1.00 27.79 C ATOM 2193 N ARG B 154 -16.585 -31.046 -12.147 1.00 26.39 N ATOM 2194 CA ARG B 154 -15.282 -31.539 -11.708 .00 26.14 C ATOM 2195 C ARG B 154 -14.698 -32.547 -12.699 .00 25.32 C ATOM 2196 O ARG B 154 -15.421 -33.369 -13.262 .00 26.22 O ATOM 2197 CB ARG B 154 -15.411 -32.224 -10.344 .00 26.57 C ATOM 2198 CG ARG B 154 -16.550 -31.720 -9.456 .00 28.61 C ATOM 2199 CD ARG B 154 -16.160 -30.673 -8.425 .00 31.30 C ATOM 2200 NE ARG B 154 -15.243 -31.196 -7.416 .00 33.56 N ATOM 2201 CZ ARG B 154 -14.778 -30.498 -6.383 .00 34. 79 C ATOM 2202 NHl ARG B 154 -15.154 -29.231 -6.195 .00 34.84 N ATOM 2203 NH2 ARG B 154 -13.931 -31.068 -5.532 .00 35.08 N ATOM 2204 N TYR B 155 -13.392 -32.470 -12.919 .00 23.64 N ATOM 2205 CA TYR B 155 -12.672 -33.455 -13.702 .00 22.00 C ATOM 2206 C TYR B 155 -11.440 -33.829 -12.899 .00 21.56 C ATOM 2207 O TYR B 155 -10.691 -32.954 -12.480 1.00 21.74 O ATOM 2208 CB TYR B 155 -12.321 -32.896 -15.079 1.00 21.81 C ATOM 2209 CG TYR B 155 -13.550 -32.633 -15.907 1.00 21.45 C ATOM 2210 CDl TYR B 155 -14.052 -31.340 -16.044 ,00 21.15 C ATOM 2211 CD2 TYR B 155 -14.254 -33.689 -16.506 ,00 21.12 C ATOM 2212 CEl TYR B 155 -15.200 -31.090 -16.779 ,00 20.27 C ATOM 2213 CE2 TYR B 155 -15.405 -33.453 -17.244 .00 21.07 C ATOM 2214 CZ TYR B 155 -15.876 -32.146 -17.375 ,00 21.01 C ATOM 2215 OH TYR B 155 -17.016 -31.885 -18.108 ,00 20.82 O ATOM 2216 N VAL B 156 -11.253 -35.123 -12.652 ,00 20.66 N ATOM 2217 CA VAL B 156 -10.269 -35.576 -11.679 ,00 19.77 C ATOM 2218 C VAL B 156 -9.251 -36.525 -12.299 ,00 18.91 C ATOM 2219 O VAL B 156 -9.581 -37.342 -13.159 ,00 18.43 O ATOM 2220 CB VAL B 156 -10.930 -36.259 -10.440 ,00 19.99 C ATOM 2221 CGl VAL B 156 -10.029 -36.144 -9.232 ,00 19.78 C ATOM 2222 CG2 VAL B 156 -12.280 -35.630 -10.104 ,00 21.55 C ATOM 2223 N GLN B 157 -8.008 -36.394 -11.852 ,00 17.84 N ATOM 2224 CA GLN B 157 -6.932 -37.274 -12.257 ,00 16.95 C ATOM 2225 C GLN B 157 -5.995 -37.461 -11.064 1.00 16.59 C ATOM 2226 O GLN B 157 -6.102 -36.734 -10.068 00 16.44 O ATOM 2227 CB GLN B 157 -6.183 -36.680 -13.457 00 16.97 C ATOM 2228 CG GLN B 157 -5.169 -35.586 -13.111 00 16.46 C ATOM 2229 CD GLN B 157 -4.805 -34.737 -14.315 00 16.90 C ATOM 2230 OEl GLN B 157 -3.741 -34.926 ^■14.929 00 15.38 O ATOM 2231 NE2 GLN B 157 -5.685 -33.805 -14.661 00 14.60 N ATOM 2232 N LYS B 158 -5.104 -38.445 -11.170 00 15.96 N ATOM 2233 CA LYS B 158 -4.025 -38.655 -10.211 00 16.24 C ATOM 2234 C LYS B 158 -2.694 -38.253 -10.856 00 15.76 C ATOM 2235 O LYS B 158 -2.360 -38.708 -11.956 00 15.61 O ATOM 2236 CB LYS B 158 -3.956 -40.126 -9.768 00 16.71 C ATOM 2237 CG LYS B 158 -5.007 -40.578 -8.726 00 18.23 C ATOM 2238 CD LYS B 158 -4.689 -40.018 -7.349 1.00 20.38 C Table 3

ATOM 2239 CE LYS B 158 -5.431 -40.716 -6.208 1.00 23.00 C

ATOM 2240 NZ LYS B 158 -5.264 -39.921 -4.921 1.00 22.97 N

ATOM 2241 N GLY B 159 -1.940 -37.401 -10.170 1.00 15.04 N

ATOM 2242 CA GLY B 159 -0.648 -36.952 -10.663 1.00 14.14 C

ATOM 2243 C GLY B 159 -0.017 -35.940 -9.722 1.00 13.80 C

ATOM 2244 O GLY B 159 -0.335 -35.905 -8.535 1.00 13.79 O

ATOM 2245 N GLU B 160 0.882 -35.126 -10.267 1.00 12.55 N

ATOM 2246 CA GLO B 160 1.616 -34.116 -9.516 1.00 11.75 C

ATOM 2247 C GLU B 160 2.065 -33.079 -10.551 1.00 11.05 C

ATOM 2248 O GLU B 160 2.236 -33.402 -11.726 1.00 10.28 O

ATOM 2249 CB GLU B 160 2.815 -34.760 -8.786 1.00 11.76 C

ATOM 2250 CG GLϋ B 160 3.718 -33.838 -7.959 1.00 12.53 C

ATOM 2251 CD GLU B 160 2.962 -33.000 -6.935 1.00 13.34 C

ATOM 2252 OEl GLU B 160 2.876 -33.423 -5.771 1.00 12.86 O

ATOM 2253 OE2 GLU B 160 2.443 -31.919 -7.293 1.00 13.05 O

ATOM 2254 N TYR B 161 2.207 -31.827 -10.132 1.00 10.31 N

ATOM 2255 CA TYR B 161 2.777 -30.817 -11.018 1.00 10.13 C

ATOM 2256 C TYR B 161 3.890 -30.048 -10.323 1.00 9.93 C

ATOM 2257 O TYR B 161 4.623 -29.311 -10.968 1.00 9.89 O

ATOM 2258 CB TYR B 161 1.701 -29.863 -11.549 1.00 9.59 C

ATOM 2259 CG TYR B 161 0.976 -29.126 -10.450 1.00 10.18 C

ATOM 2260 CDl TYR B 161 1.444 -27,900 -9.979 1.00 8.25 C

ATOM 2261 CD2 TYR B 161 -0.167 -29.675 -9.860 1.00 10.60 C

ATOM 2262 CEl TYR B 161 0.792 -27.237 -8.956 1.00 9.38 C

ATOM 2263 CE2 TYR B 161 -0.819 -29.021 -8.824 1.00 10.60 C

ATOM 2264 CZ TYR B 161 -0.338 -27.802 -8.388 1.00 9.09 C

ATOM 2265 OH TYR B 161 -1.000 -27.160 -7.383 1.00 9.56 O

ATOM 2266 N ARG B 162 3.986 -30.222 -9.008 1.00 10.41 N

ATOM 2267 CA ARG B 162 4.917 -29.458 -8.183 1.00 10.66 C

ATOM 2268 C ARG B 162 6.293 -30.067 -8.218 1.00 11.07 C

ATOM 2269 O ARG B 162 6.495 -31.253 -7.943 1.00 11.05 O

ATOM 2270 CB ARG B 162 4.439 -29.331 -6.735 1.00 10.56 C

ATOM 2271 CG ARG B 162 3.176 -28.478 -6.544 1.00 10.06 C

ATOM 2272 CD ARG B 162 2.508 -28.710 -5.212 1.00 9.51 C

ATOM 2273 NE ARG B 162 2.218 -30.129 -4.994 1.00 6.59 N

ATOM 2274 CZ ARG B 162 1.864 -30.651 -3.821 1.00 8.94 C

ATOM 2275 NHl ARG B 162 1.760 -29.870 -2.747 1.00 7.57 N

ATOM 2276 NH2 ARG B 162 1.622 -31.964 -3.712 1.00 7.94 N

ATOM 2277 N THR B 163 7.243 -29.203 -8.516 1.00 11.39 N

ATOM 2278 CA THR B 163 8.583 -29.586 -8.853 1.00 12.20 C

ATOM 2279 C THR B 163 9.559 -29.077 -7.773 1.00 12.36 C

ATOM 2280 O THR B 163 10.725 -29.483 -7.695 1.00 12.21 O

ATOM 2281 CB THR B 163 8.794 -28.987 -10.248 1.00 13.00 C

ATOM 2282 OGl THR B 163 9.159 -30.008 -11.181 1.00 16.19 O

ATOM 2283 CG2 THR B 163 9.829 -27.891 -10.296 1.00 10.75 C

ATOM 2284 N ASN B 164 9.045 -28.211 -6.910 1.00 12.37 N

ATOM 2285 CA ASN B 164 9.840 -27.593 -5.866 1.00 13.09 C

ATOM 2286 C ASN B 164 9.418 -28.154 -4.506 1.00 13.14 C

ATOM 2287 O ASN B 164 8.240 -28.121 -4.164 1.00 12.89 O

ATOM 2288 CB ASN B 164 9.664 -26.074 -5.928 1.00 12.84 C

ATOM 2289 CG ASN B 164 10.743 -25.331 -5.194 1.00 14.45 C

ATOM 2290 ODl ASN B 164 11.020 -25.602 -4.029 1.00 16.89 O

ATOM 2291 ND2 ASN B 164 11.351 -24.365 -5.865 1.00 16.79 N

ATOM 2292 N PRO B 165 10.376 -28.687 -3.750 1.00 13.82 N

ATOM 2293 CA PRO B 165 10.093 -29.299 -2.444 1.00 14.32 C

ATOM 2294 C PRO B 165 9.488 -28.321 -1.429 1.00 15.01 C

ATOM 2295 O PRO B 165 8.693 -28.728 -0.587 1.00 15.54 O

ATOM 2296 CB PRO B 165 11.476 -29.794 -1.978 1.00 14.69 C

ATOM 2297 CG PRO B 165 12.469 -28.953 -2.753 1.00 14.49 C

ATOM 2298 CD PRO B 165 11.809 -28.743 -4.095 1.00 13.65 C

ATOM 2299 N GLU B 166 9.835 -27.040 -1.533 1.00 15.59 N

ATOM 2300 CA GLO B 166 9.229 -25.990 -0.709 1.00 16.10 C

ATOM 2301 C GLO B 166 7.713 -25.903 -0.876 1.00 15.00 C

ATOM 2302 O GLO B 166 7.005 -25.434 0.018 1.00 14.56 O

ATOM 2303 CB GLU B 166 9.820 -24.630 -1.077 1.00 17.17 C

ATOM 2304 CG GLU B 166 11.338 -24.568 -1.052 1.00 21.06 C

ATOM 2305 CD GLU B 166 11.879 -23.679 0.053 1.00 27.57 C

ATOM 2306 OEl GLO B 166 11.185 -23.468 1.092 1.00 28.88 O Table 3

ATOM 23Q7 OE2 GLU B 166 13.017 -23.190 -0.132 1.00 30.33 O

ATOM 230B N ASP B 167 7.222 -26.335 -2.031 1.00 14.22 N

ATOM 2309 CA ASP B 167 5.790 -26.282 -2.325 1.00 13.55 C

ATOM 2310 C ASP B 167 5.096 -27.566 -1.866 1.00 13.07 C

ATOM 2311 O ASP B 167 3.929 -27.554 -1.492 1.00 12.42 O

ATOM 2312 CB ASP B 167 5.546 -26.021 -3.818 1.00 13.15 C

ATOM 2313 CG ASP B 167 6.152 -24.698 -4.300 1.00 13.92 C

ATOM 2314 ODl ASP B 167 6.202 -23.730 -3.507 1.00 11.96 O

ATOM 2315 OD2 ASP B 167 6.590 -24.537 -5.469 1.00 13.24 O

ATOM 2316 N ILE B 168 5.828 -28.669 -1.900 1.00 12.86 N

ATOM 2317 CA ILE B 168 5.297 -29.958 -1.463 1.00 13.28 C

ATOM 2318 C ILE B 168 5.257 -30.019 0.068 1.00 13.69 C

ATOM 2319 O ILE B 168 4.226 -30.339 0.654 1.00 13.39 O

ATOM 2320 CB ILE B 168 6.119 -31.108 -2.087 1.00 13.31 C

ATOM 2321 CGl ILE B 168 6.044 -31.004 -3.623 1.00 12.84 C

ATOM 2322 CG2 ILE B 168 5.631 -32.470 -1.572 1.00 13.01 C

ATOM 2323 CDl ILE B 168 7.208 -31.623 -4.362 1.00 13.63 C

ATOM 2324 N TYR B 169 6.373 -29.687 0.710 1.00 14.27 N

ATOM 2325 CA TYR B 169 6.356 -29.378 2.132 1.00 15.15 C

ATOM 2326 C TYR B 169 5.429 -28.162 2.327 1.00 15.64 C

ATOM 2327 O TYR B 169 4.534 -28.173 3.187 1.00 17.10 O

ATOM 2328 CB TYR B 169 7.772 -29.050 2.617 1.00 14.77 C

ATOM 2329 CG TYR B 169 7.900 -28.896 4.115 1.00 15.90 C

ATOM 2330 CDl TYR B 169 8.418 -29.927 4.900 1.00 16.26 C

ATOM 2331 CD2 TYR B 169 7.514 -27.718 4.751 1.00 15.66 C

ATOM 2332 CEl TYR B 169 8.535 -29.783 6.265 1.00 15.82 C

ATOM 2333 CE2 TYR B 169 7.628 -27.569 6.102 1.00 15.26 C

ATOM 2334 CZ TYR B 169 8.138 -28.599 6.853 1.00 15.83 C

ATOM 2335 OH TYR B 169 8.245 -28.433 8.204 1.00 16.35 O

TER 2336 TYR B 169

HETATM 2337 O HOH Y 1 -7.331 -36.685 -0.358 1.00 28.16 O

HETATM 2338 O HOH Y 2 -5.406 -32.784 0.513 1.00 25.00 O

HETATM 2339 O HOH Y 3 -8.967 -32.618 -5.848 1.00 20.36 O

HETATM 2340 O HOH Y 4 14.177 -22.049 -16.634 1.00 29.46 O

HETATM 2341 O HOH Y 5 14.727 -17.213 -16.097 1.00 14.30 O

HETATM 2342 O HOH Y 6 13.656 -22.774 -19.162 1.00 27.92 O

HETATM 2343 O HOH Y 7 15.178 -18.271 -13.174 1.00 23.63 O

HETATM 2344 O HOH Y 8 17.585 -17.248 -12.782 1.00 29.32 O

HETATM 2345 O HOH Y 9 -2.047 -11.176 -25.843 1.00 16.59 O

HETATM 2346 O HOH Y 10 -3.437 -11.691 -23.842 1.00 10.96 O

HETATM 2347 O HOH Y 11 10.623 -19.087 -10.970 1.00 13.95 O

HETATM 2348 O HOH Y 12 11.932 -15.421 -10.852 1.00 24.40 O

HETATM 2349 O HOH Y 13 13.212 -20.852 8.093 1.00 26.19 O

HETATM 2350 O HOH Y 14 -4.599 -22.202 2.864 1.00 28.33 O

HETATM 2351 O HOH Y 15 9.720 -19.005 -10.343 1.00 27.86 O

HETATM 2352 O HOH Y 16 12.365 -17.448 -3.260 1.00 26.77 O

HETATM 2353 O HOH Y 17 12.082 -21.063 -6.085 1.00 37.27 O

HETATM 2354 O HOH Y 18 -1.345 -28.562 -1.715 1.00 19.02 O

HETATM 2355 O HOH Y 19 10.229 -23.173 -5.774 1.00 8.17 O

HETATM 2356 O HOH Y 20 -4.948 -20.089 -4.843 1.00 10.08 O

HETATM 2357 O HOH Y 21 11.232 -18.158 6.803 1.00 37.18 O

HETATM 2358 O HOH Y 22 4.175 -3.948 -21.251 1.00 19.39 O

HETATM 2359 O HOH Y 23 2.004 -9.312 -26.007 1.00 27.72 O

HETATM 2360 O HOH Y 24 -7.630 -10.416 -1.697 1.00 17.82 O

HETATM 2361 O HOH Y 25 -4.641 -18.292 2.129 1.00 45.88 O

HETATM 2362 O HOH Y 26 -8.926 -1.540 -21.554 1.00 33.21 O

HETATM 2363 O HOH Y 27 -0.526 -24.547 -1.105 1.00 10.27 O

HETATM 2364 O HOH Y 28 5.825 -16.910 -3.280 1.00 16.21 O

HETATM 2365 O HOH Y 29 8.229 -17.066 -11.824 1.00 36.92 O

HETATM 2366 O HOH Y 30 13.385 -12.849 -5.434 1.00 25.13 O

HETATM 2367 O HOH Y 31 8.296 -19.343 -4.061 1.00 23.09 O

HETATM 2368 O HOH Y 32 8.932 -23.435 -10.207 1.00 12.11 O

HETATM 2369 O HOH Y 33 2.202 -22.829 -2.932 1.00 13.50 O

HETATM 2370 O HOH Y 34 5.636 -21.734 -16.198 1.00 24.95 O

HETATM 2371 O HOH Y 35 -8.033 0.108 -17.487 1.00 30.73 O

HETATM 2372 O HOH Y 36 10.662 2.771 -16.190 1.00 36.23 O

HETATM 2373 O HOH Y 37 10.539 -25.263 -12.432 1.00 40.62 O

HETATM 2374 O HOH Y 38 6.622 -26.530 -7.222 1.00 5.49 O Table 3

HETATM 2375 O HOH Y 39 -19.933 -2.559 -3.871 1.00 31 .49 O

HETATM 2376 O HOH Y 40 -18.210 -0.817 0.032 1.00 34.09 O

HETATM 2377 O HOH Y 41 -19.766 -1.455 -1.848 1.00 22.37 O

HETATM 2378 O HOH Y 42 -9.972 4.076 -11.199 1.00 29.32 O

HETATM 2379 O HOH Y 43 -18.312 -0.647 -4.510 1.00 33.07 O

HETATM 2380 O HOH Y 44 -5.057 25.427 -20.579 1.00 28.63 O

HETATM 2381 O HOH Y 45 -2.934 27.958 -23.423 1.00 29.04 O

HETATM 2382 O HOH Y 46 1.227 21.959 -24.207 1.00 26.00 O

HETATM 2383 O HOH Y 47 .562 19.718 -23.531 1.00 31.33 O

HETATM 2384 O HOH Y 48 .282 15.358 -20.967 1.00 12.54 O

HETATM 2385 O HOH Y 49 .985 19.128 -16.718 1.00 13.61 O

HETATM 2386 O HOH Y 50 .833 -9.942 -24.442 1.00 22.25 O

HETATM 2387 O HOH Y 51 .904 -7.345 -18.975 1.00 36.72 O

HETATM 2388 O HOH Y 52 4.285 -6.686 -21.053 1.00 21.98 O

HETATM 2389 O HOH Y 53 -0.760 -8.618 -25.891 1.00 27.81 O

HETATM 2390 O HOH Y 54 -1.654 -5.449 -24.600 1.00 20.50 O

HETATM 2391 O HOH Y 55 -16.311 -13.230 -16.064 1.00 34.88 O

HETATM 2392 O HOH Y 56 3.838 -15.374 -24.371 1.00 19.25 O

HETATM 2393 O HOH Y 57 0.646 -12.414 -26.656 1.00 26.18 O

HETATM 2394 O HOH Y 58 5.135 -12.038 -25.146 1.00 31.12 O

HETATM 2395 O HOH Y 59 -7.675 -37.025 -16.948 1.00 15.24 O

HETATM 2396 O HOH Y 60 -3.502 -1.137 -16.481 1.00 16.70 O

HETATM 2397 O HOH Y 61 -6.232 -2.658 -21.065 1.00 17.95 O

HETATM 2398 O HOH Y 62 -5.502 -0.668 -18.469 1.00 34.43 O

HETATM 2399 O HOH Y 63 -13.157 -3.863 -24.970 1.00500.00 O

HETATM 2400 O HOH Y 64 -13.930 -12.158 -16.195 1.00 21.51 O

HETATM 2401 O HOH Y 65 -12.911 -12.737 -8.216 1.00 15.24 O

HETATM 2402 O HOH Y 66 -9.108 -8.931 -2.995 1.00 15.69 O

HETATM 2403 O HOH Y 67 -8.308 -16.368 -0.038 1.00 18.92 O

HETATM 2404 O HOH Y 68 11.849 -28.029 1.498 1.00 20.45 O

HETATM 2405 O HOH Y 69 3.952 -31.730 4.743 1.00 26.45 O

HETATM 2406 O HOH Y 70 6.214 -15.879 -18.842 1.00 20.01 O

HETATM 2407 O HOH Y 71 5.333 -8.723 -16.802 1.00 22.22 O

HETATM 2408 O HOH Y 72 5.962 -5.770 -8.647 1.00 17.72 O

HETATM 2409 O HOH Y 73 -10.032 -1.032 -16.405 1.00 18.47 O

HETATM 2410 O HOH Y 74 -12.926 0.904 -15.527 1.00 29.69 O

HETATM 2411 O HOH Y 75 -19.886 -5.007 -3.233 1.00 29.14 O

HETATM 2412 O HOH Y 76 -17.572 -2.813 -1.021 1.00 36.12 O

HETATM 2413 O HOH Y 77 -11.456 -1.871 -7.733 1.00 8.96 O

HETATM 2414 O HOH Y 78 -16.844 2.004 -3.958 1.00 31.58 O

HETATM 2415 O HOH Y 79 -10.469 5.980 -6.264 1.00 28.08 O

HETATM 2416 O HOH Y 80 -15.726 5.070 -7.410 1.00 25.70 O

HETATM 2417 O HOH Y 81 -7.229 3.494 -10.627 1.00 22.26 O

HETATM 2418 O HOH Y 82 0.672 -0.282 -8.042 1.00 19.34 O

HETATM 2419 O HOH Y 83 -0.502 -0.530 -10.038 1.00 16.62 O

HETATM 2420 O HOH Y 84 0.972 0.691 -3. .866 1.00 19.58 O

HETATM 2421 O HOH Y 85 7.801 -7. .513 -1..606 1.00 53.30 O

HETATM 2422 O HOH Y 86 3.834 -7..316 -7.434 1.00 9.65 O

HETATM 2423 O HOH Y 87 7.838 -14.243 -2.154 1.00 42.08 O

HETATM 2424 O HOH Y 88 5.373 -6.967 1.805 1.00 48.71 O

HETATM 2425 O HOH Y 89 5.120 -11.875 4.541 1.00 56.10 O

HETATM 2426 O HOH Y 90 3.822 -17.520 2.699 1.00 36.30 O

HETATM 2427 O HOH Y 91 2.172 -15.330 4.573 1.00 31.23 O

HETATM 2428 O HOH Y 92 4.191 -23.093 -1.195 1.00 25.28 O

HETATM 2429 O HOH Y 93 -0.742 -9.787 0.548 1.00 16.68 O

HETATM 2430 O HOH Y 94 -6.540 -23.400 -21.713 1.00 24.28 O

HETATM 2431 O HOH Y 95 -3.593 -17.358 -26.953 1.00 24.81 O

HETATM 2432 O HOH Y 96 -8.834 -17.188 -25.259 1.00 14.56 O

HETATM 2433 O HOH Y 97 -5.337 -15.614 -27.571 1.00 27.53 O

HETATM 2434 O HOH Y 98 -14.690 -9.065 -27.388 1.00 13.54 O

HETATM 2435 O HOH Y 99 -12.027 -7.594 -29.398 1.00 14.22 O

HETATM 2436 O HOH Y 100 -10.867 -8.341 -33.029 1.00 27.05 O

HETATM 2437 O HOH Y 101 -17.462 -11.787 -21.184 1.00 18.16 O

HETATM 2438 O HOH Y 102 -14.720 -11.252 -24.132 1.00 21.90 O

HETATM 2439 O HOH Y 103 -17.105 -14.720 -18.554 1.00 22.49 O

HETATM 2440 O HOH Y 104 -8.515 -22.054 -24.575 1.00 19.76 O

HETATM 2441 O HOH Y 105 -16.908 -19.974 -25.359 1.00 28.89 O

HETATM 2442 O HOH Y 106 -17.839 -25.240 -18.634 1.00 37.77 O Table 3

HETATM 2443 O HOH Y 107 -13.790 29.581 -23.678 1.00 22. 29 O HETATM 2444 O HOH Y 108 -11.746 36.242 -18.295 1.00 32.97 O HETATM 2445 O HOH Y 109 -9.160 35.311 -15.756 1.00 26.79 O HETATM 2446 O HOH Y 110 -9.335 35.003 -20.585 1.00 28.53 O HETATM 2447 O HOH Y 111 -9.325 29.977 -21.514 1.00 18.25 O HETATM 2448 O HOH Y 112 -1.368 34.792 -17.629 1.00 31.49 O HETATM 2449 O HOH Y 113 -2.392 34.611 -22.115 1.00 32, 37 O HETATM 2450 O HOH Y 114 6.697 30.454 -17.089 1.00 30.95 O HETATM 2451 O HOH Y 115 4.546 29.922 -15.849 1.00 24, 10 O HETATM 2452 O HOH Y 116 4.913 34.035 -17.703 1.00 32, 79 O HETATM 2453 O HOH Y 117 5.723 37.657 -8.337 1.00 19, 68 O HETATM 2454 O HOH Y 118 -19.750 18.226 -22.886 1.00 39, 87 O HETATM 2455 O HOH 119 -19.661 23.698 -18.915 1.00 28, 00 O HETATM 2456 O HOH 120 -19.122 16.472 -21.112 1.00 18, 86 O HETATM 2457 O HOH 121 -22.266 27.824 -10.043 1.00 39.51 O HETATM 2458 O HOH 122 -18.025 28.134 -7.915 1.00 17.37 O HETATM 2459 O HOH Y 123 -19.402 23.383 -9.248 1.00 37.65 O HETATM 2460 O HOH 124 -17.395 ^■35.128 -14.513 1.00 27, 47 O HETATM 2461 O HOH 125 -8.436 33.616 -13.891 1.00 18.76 O HETATM 2462 O HOH 126 -1.880 36.885 -14.304 1.00 20, 85 O HETATM 2463 O HOH 127 -0.368 41.094 -11.863 1.00 30, 67 O HETATM 2464 O HOH 128 -5.569 40.182 -13.480 1.00 16, 35 O HETATM 2465 O HOH 129 3.789 35.921 -4.790 1.00 30, 81 O HETATM 2466 O HOH 130 4.740 ^■28.695 -13.473 1.00 11, 27 O HETATM 2467 O HOH 131 0.658 ^■32.872 -1.392 1.00 25, 79 O HETATM 2468 O HOH 132 10.665 24.075 -8.513 1.00 9, 36 O HETATM 2469 O HOH 133 13.946 -25.380 -3.064 1.00 28, 87 O HETATM 2470 O HOH Y 134 7.947 24.802 2.608 1.00 28, 01 O HETATM 2471 O HOH Y 135 15.348 24.543 -0.959 1.00 27, 25 O HETATM 2472 O HOH Y 136 13.843 21.011 -0.243 1.00 27, 38 O HETATM 2473 O HOH Y 137 4.019 ^■25.451 0.999 1.00 27, 16 O HETATM 2474 O HOH Y 138 11.855 ^■26.288 3.118 1.00 28, 31 O HETATM 2475 O HOH Y 139 1.553 26.842 -2.456 1.00 9.30 O HETATM 2476 O HOH Y 140 4.775 29.588 5.007 1.00 28, 96 O HETATM 2477 O HOH Z 1 15.003 9.757 28.680 1.00 23, 28 O HETATM 2478 O HOH Z 2 11.771 5.127 29.516 1.00 23.63 O HETATM 2479 O HOH Z 3 15.996 6.883 23.641 1.00 57.65 O HETATM 2480 O HOH Z 4 7.889 4 375 27.528 1.00 19, 38 O HETATM 2481 O HOH Z 5 12.792 -1 670 15.542 1.00 26, 66 O HETATM 2482 O HOH Z 6 7.868 -0.379 18.942 1.00 16.94 O HETATM 2483 O HOH Z 7 11.435 -0.226 19.052 1.00 33.51 O HETATM 2484 O HOH Z 8 4.419 -1.133 13.257 1.00 9, 68 O HETATM 2485 O HOH Z 9 8.929 -0.218 11.510 1.00 24, 33 O HETATM 2486 O HOH Z 10 2.332 -3.820 6.803 1.00 24.35 O HETATM 2487 O HOH Z 11 4.716 -1.760 6.213 1.00 16.95 O HETATM 2488 O HOH Z 12 -16.746 -2.609 4.413 1.00 30, 49 O HETATM 2489 O HOH Z 13 4.728 -4.951 14.236 1.00 50.17 O HETATM 2490 O HOH Z 14 -7.014 11.045 26.677 1.00 53.46 O HETATM 2491 O HOH Z 15 5.478 5.386 28.144 1.00 15.52 O HETATM 2492 O HOH Z 16 11.606 2.141 25.343 1.00 40.05 O HETATM 2493 O HOH Z 17 9.722 -6.273 23.462 1.00 29.29 O HETATM 2494 O HOH Z 18 6.456 -5.202 29.964 1.00 52.24 O HETATM 2495 O HOH Z 19 2.226 -1.206 21.520 1.0 000 9.87 O HETATM 2496 O HOH Z 20 -17.699 3.746 8.409 ,00 25.20 O HETATM 2497 O HOH Z 21 -0.891 11.267 19.746 .00 24.61 O HETATM 2498 O HOH Z 22 -10.852 4.758 3.319 .00 8.51 O HETATM 2499 O HOH Z 23 -16.830 -2.829 7.121 ,00 24.62 O HETATM 2500 O HOH Z 24 -9.785 -7.534 0.636 1.00 14.26 O HETATM 2501 O HOH Z 25 2.510 2.081 27.831 1.00 16.48 O HETATM 2502 O HOH Z 26 -3.181 -8.781 -0.717 1.00 8.28 O HETATM 2503 O HOH Z 27 -7.607 0.492 26.669 1.00 9.41 O HETATM 2504 O HOH Z 28 -13.604 1.356 24.961 1.00 52.34 O HETATM 2505 O HOH Z 29 -12.524 -1.775 22.237 1.00 30.83 O HETATM 2506 O HOH Z 30 -11.624 -0.591 24.199 1.00 30.03 O HETATM 2507 O HOH Z 31 3.358 -5.617 11.963 1.00 36.19 O HETATM 2508 O HOH Z 32 -7.793 10.132 24.413 1.00 14.12 O HETATM 2509 O HOH Z 33 -1.119 3.261 27.190 1.00 25.14 O HETATM 2510 O HOH Z 34 1.797 5.793 28.538 1.00 12.92 O Table 3

HETATM 2511 O HOH Z 35 -7.855 10.433 17.826 1.00 21 11 O

HETATM 2512 O HOH 36 -4.276 14.494 21.840 1.00 14, 00 O

HETATM 2513 O HOH 37 0.604 -16.195 20.471 1.00 38, 63 O

HETATM 2514 O HOH Z 38 -8.939 14.606 16.127 1.00 14; 66 O

HETATM 2515 O HOH 3S 2.110 11.269 9.629 1.00 38 66 O

HETATM 2516 O HOH 40 1.022 14.925 9.077 1.00 29, 87 O

HETATM 2517 O HOH 41 -6.056 12.710 8.959 1.00 18, 99 O

HETATM 2518 O HOH 42 -7.631 12.372 15.911 1.00 11 53 O

HETATM 2519 O HOH Z 43 -15.300 4.974 7.237 1.00 16 65 O

HETATM 2520 O HOH Z 44 -16.385 1.694 12.487 1.00 32 75 O

HETATM 2521 O HOH Z 45 -17.061 1.347 8.977 1.00 12, 48 O

HETATM 2522 O HOH N N 46 -14.431 -0.321 2.474 1.00 25 53 O

HETATM 2523 O HOH Z 47 -8.827 3.035 4.104 1.00 12 43 O

HETATM 2524 O HOH Z 48 -15.298 7.599 8.080 1.00 31 71 O

HETATM 2525 O HOH Z 49 -12.240 6.916 4.417 1.00 21, 77 O

HETATM 2526 O HOH Z 50 -11.059 7.200 10.826 1.00 13 41 O

HETATM 2527 O HOH Z 51 -12.344 9.378 8.939 1.00 34 59 O

HETATM 2528 O HOH 52 5.704 1.674 -2.117 1.00 30 45 O

HETATM 2529 O HOH Z 53 -11.069 -6.016 2.346 1.00 10, 85 O

HETATM 2530 O HOH Z 54 -16.264 -5.233 7. .704 1.00 15 49 O

HETATM 2531 O HOH Z 55 -10.009 5.751 -3..660 1.00 27 98 O

HETATM 2532 O HOH Z 56 -5.612 -8.381 -0.097 1.00 6 18 O

HETATM 2533 O HOH Z 57 -8.139 -6.706 -3.482 1.00 6, 90 O

HETATM 2534 O HOH Z 58 1.189 -5.586 5.310 00 20 38 O

HETATM 2535 O HOH Z 59 0.622 -8.290 2.195 1.00 17 76 O

HETATM 2536 O HOH Z 60 1.542 -11.588 7.565 1.00 40.76 O

HETATM 2537 O HOH Z 61 1.941 -10.330 3.283 1.00 27.40 O

HETATM 2538 O HOH Z 62 2.725 -8.050 12.844 1.00 17.74 O

HETATM 2539 O HOH Z 63 -5.857 -14.521 18.964 1.00 32.63 O

HETATM 2540 O HOH Z 64 -15.656 7.990 12.131 1.00 28.55 O

HETATM 2541 O HOH Z 65 -17.931 4.224 17.222 1.00 18.30 O

HETATM 2542 O HOH Z 66 -15.988 -1.375 22.549 1.00 37.93 O

HETATM 2543 O HOH Z 67 -17.821 -0.021 14.349 1.00 31.49 O

HETATM 2544 O HOH 68 -15.703 -4.809 19.447 1.00 15.48 O

HETATM 2545 O HOH 69 -9.055 -10.959 3.933 1.00 29.08 O

HETATM 2546 O HOH Z 70 -7.121 -15.413 1.998 1.00 52.70 O

HETATM 2547 O HOH Z 71 0.454 -16.612 6.766 1.00 29.26 O

HETATM 2548 O HOH Z 72 0.646 -22.711 14.957 1.00 36.97 O

HETATM 2549 O HOH Z 73 -5.082 - 20.954 15.177 1.00 30.51 O

HETATM 2550 O HOH Z 74 1.051 14.803 17.778 1.00 26.94 O

HETATM 2551 O HOH Z 75 -3.013 13.288 17.274 1.00 14.90 O

HETATM 2552 O HOH Z 76 -3.302 21.981 8.508 1.00 25.35 O

HETATM 2553 O HOH Z 77 -9.703 22.335 10.505 1.00 33.09 O

HETATM 2554 O HOH Z 78 -9.302 19.421 7.959 1.00 21.26 O

HETATM 2555 O HOH Z 79 -14.556 17.337 11.473 1.00 23.10 O

HETATM 2556 O HOH Z 80 -4.708 15.759 10.405 1.00 7.71 O

HETATM 2557 O HOH Z 81 -12.595 12.162 10.366 1.00 10.28 O

HETATM 2558 O HOH 82 -11.782 16.409 8.869 1.00 12.28 O

HETATM 2559 O HOH Z 83 -15.371 11.966 16.728 1.00 37.46 O

HETATM 2560 O HOH Z 84 -14.411 11.045 13.703 1.00 12.22 O

HETATM 2561 O HOH Z 85 -15.592 -5.752 24.135 1.00 34.01 O

HETATM 2562 O HOH Z 86 -9.892 -0.876 26.064 1.00 25.18 O

HETATM 2563 O HOH Z 87 -13.235 -5.273 19.873 1.00 11.91 O

HETATM 2564 O HOH Z 88 -8.905 -8.003 29.003 1.00 44.02 O

HETATM 2565 O HOH Z 89 -7.802 -1.884 26.267 1.00500.00 O

HETATM 2566 O HOH Z 90 -5.283 -11 394 23.731 1.00 35.11 O

HETATM 2567 O HOH Z 91 -6.402 8.340 2.608 1.00 29.31 O

HETATM 2568 O HOH 92 -1.730 5.366 1.801 1.00 11.33 O

HETATM 2569 O HOH Z 93 1.608 8.395 4.028 1.00 24.68 O

HETATM 2570 O HOH Z 94 6.333 4.414 -1.154 1.00 18.92 O

HETATM 2571 O HOH Z 95 13.515 14.696 11.792 1.00 37.38 O

HETATM 2572 O HOH Z 96 12.132 11.198 7.553 1.00 37.99 O

HETATM 2573 O HOH Z 97 7.480 13.088 8.288 1.00 32.76 O

HETATM 2574 O HOH Z 98 6.337 18.549 11.535 1.00 34.76 O

HETATM 2575 O HOH Z 99 1.246 18.764 12.351 1.00 24.94 O

HETATM 2576 O HOH Z 100 4.016 21.150 26.939 1.00 15.33 O

HETATM 2577 O HOH Z 101 3.825 22.498 23.115 1.00 27.83 O

HETATM 2578 O HOH Z 102 10.306 19.807 23.753 1.00 27.56 O Table 3

HETATM 2579 0 HOH Z 103 14.102 12.247 27.527 1.00 15. 66 O HETATM 2580 O HOH Z 104 12.969 7.120 22.039 1.00 29.80 O HETATM 2581 O HOH Z 105 7.083 4.918 6.652 1.00 17.73 O HETATM 2582 O HOH Z 106 7.278 2.374 7.562 1.00 21.69 O HETATM 2583 O HOH Z 107 16.983 4.347 3.913 1.00 32.04 O HETATM 2584 O HOH Z 108 16.207 1.058 14.227 1.00 28.15 O HETATM 2585 O HOH Z 109 13.055 5.205 9.508 1.00 39.32 O HETATM 2586 O HOH Z 110 19.334 4.842 12.509 1.00 31, 42 O HETATM 2587 O HOH Z 111 14.249 7.058 6.285 1.00 17.88 O HETATM 2588 O HOH Z 112 16.817 12.198 14.559 1.00 24.99 O HETATM 2589 O HOH Z 113 11.281 11.903 15.939 1.00 34, 59 O HETATM 2590 O HOH Z 114 13.434 17.673 19.579 1.00 22.99 O HETATM 2591 O HOH Z 115 13.138 17.201 29.974 1.00 32, 47 O HETATM 2592 O HOH Z 116 5.183 14.956 29.697 1.00 32.40 O HETATM 2593 O HOH Z 117 -1.621 13.816 21.095 1.00 12.37 O HETATM 2594 0 HOH Z 118 6.302 9.410 31.305 1.00 34.12 O HETATM 2595 O HOH Z 119 -7.070 16.741 26.869 1.00 21.84 O HETATM 2596 O HOH Z 120 -6.135 4.025 35.793 1.00 25.76 O HETATM 2597 O HOH Z 121 -2.842 9.429 27.205 1.00 14, 63 O HETATM 2598 O HOH Z 122 0.239 11.309 35.930 1.00 31.08 O

END

Table 4

TABLE 4

ATOM 1 N ALA A 20 15.947 15.993 4.621 00 22.44

ATOM 2 CA ALA A 20 15.571 14.566 4.811 00 22.56

ATOM 3 CB ALA A 20 14.108 14.469 5.269 00 22.68

ATOM 4 C ALA A 20 15.731 13.734 3.539 00 22.07

ATOM 5 O ALA A 20 15.858 14.265 2.427 00 21.48

ATOM 6 N GLN A 21 15.710 12.418 3.728 00 22.37

ATOM 7 CA GLN A 21 15.580 11.468 2.632 00 22.44

ATOM 8 CB GLN A 21 16.960 11.003 2.151 00 23.62

ATOM 9 CG GLN A 21 17.162 11.033 0.629 00 28.32

ATOM 10 CD GLN A 21 16.890 9.696 -0.070 00 37.60

ATOM 11 OEl GLN A 21 16.302 8.772 0.509 00 38.37

ATOM 12 NE2 GLN A 21 17.342 9.587 -1.325 00 40.20

ATOM 13 C GLN A 21 14.730 10.301 3.134 00 20.89

ATOM 14 O GLN A 21 14.970 9.795 4.234 00 21.42

ATOM 15 N ILE A 22 13.719 9.919 2.341 00 19.96

ATOM 16 CA ILE A 22 12.773 8.852 2.677 00 17.93

ATOM 17 CB ILE A 22 11.377 9.416 3.065 00 18.26

ATOM 18 CGl ILE A 22 11.454 10.184 4.388 00 16.91

ATOM 19 CDl ILE A 22 10.186 10.925 4.764 00 12.46

ATOM 20 CG2 ILE A 22 10.325 8.292 3.166 00 17.11

ATOM 21 C ILE A 22 12.605 7.914 1.481 00 16.96

ATOM 22 O ILE A 22 12.244 8.350 0.378 00 15.40

ATOM 23 N ASP A 23 12.869 6.630 1.704 00 16.60

ATOM 24 CA ASP A 23 12.659 5.611 0.678 00 17.31

ATOM 25 CB ASP A 23 13.869 4.691 0.557 00 18.22

ATOM 26 CG ASP A 23 15.004 5.333 -0.196 00 20.70

ATOM 27 ODl ASP A 23 15.095 6.581 -0.188 00 30.60

ATOM 28 OD2 ASP A 23 15.811 4.592 -0.787 00 22.30

ATOM 29 C ASP A 23 11.413 4.803 0.979 00 16.91

ATOM 30 O ASP A 23 11.209 4.359 2.104 00 16.75

ATOM 31 N LEU A 24 10.586 4.634 -0.049 00 16.38

ATOM 32 CA LEU A 24 9.305 3.961 0.060 00 16.65

ATOM 33 CB LEU A 24 8.159 4.933 -0.267 00 15.56

ATOM 34 CG LEO A 24 8.044 6.201 0.596 00 16.03

ATOM 35 CDl LEO A 24 6.941 7.133 0.080 00 10.39

ATOM 36 CD2 LEU A 24 7.799 5.843 2.057 00 13.45

ATOM 37 C LEO A 24 9.313 2.772 -0.897 00 16.84

ATOM 38 O LEO A 24 9.148 2.924 -2.102 00 17.66

ATOM 39 N ASN A 25 9.559 1.591 -0.343 00 16.13

ATOM 40 CA ASN A 25 9.527 0.349 -1.111 00 16.08

ATOM 41 CB ASN A 25 10.371 -0.738 -0.437 00 16.52

ATOM 42 CG ASN A 25 11.842 -0.597 -0.747 00 20.78

ATOM 43 ODl ASN A 25 12.512 0.272 -0.206 00 25.53

ATOM 44 ND2 ASN A 25 12.354 -1.455 -1.635 00 23.59

ATOM 45 C ASN A 25 8.100 -0.117 -1.253 00 15.48

ATOM 46 O ASN A 25 7.407 -0.324 -0.263 00 15.32

ATOM 47 N ILE A 26 658 -0.257 -2.498 1.00 14.73

ATOM 48 CA ILE A 26 6.285 -0.634 -2.798 .00 15.12

ATOM 49 CB ILE A 26 5.583 0.431 -3 662 .00 15.21

ATOM 50 CGl ILE A 26 5.555 1.775 932 .00 17.54

ATOM 51 CDl ILE A 26 5.101 2.930 798 ,00 19.84

ATOM 52 CG2 ILE A 26 4.176 -0.020 023 ,00 15.86

ATOM 53 C ILE A 26 6.261 -1.986 519 ,00 14.04

ATOM 54 O ILE A 26 7.196 -2.323 4.246 ,00 13.58

ATOM 55 N THR A 27 5.196 -2.757 3.292 ,00 13.10

ATOM 56 CA THR A 27 4.974 -4.033 974 ,00 13.07

ATOM 57 CB THR A 27 4.273 -5.063 080 ,00 14.36

ATOM 58 OGl THR A 27 2.924 -4.636 805 .00 17.32

ATOM 59 CG2 THR A 27 5.041 -5.296 779 ,00 7.70

ATOM 60 C THR A 27 4.065 -3.836 5.188 ,00 13.08

ATOM 61 0 THR A 27 3.526 -2.745 5.406 ,00 12.31

ATOM 62 N CYS A 28 3.888 -4.910 5.959 ,00 12.28

ATOM 63 CA CYS A 28 2.811 -4.996 6.947 ,00 12.59

ATOM 64 CB CYS A 28 2.769 -6.398 7.573 ,00 13.44

ATOM 65 SG CYS A 28 4.316 -6.924 8.311 1.00 16.45 Table 4

ATOM 66 C CYS A 28 1.475 -4.725 -6.247 1.00 12.28

ATOM 67 O CYS A 28 1.359 -4.916 -5.027 1.00 10.88

ATOM 68 N ARG A 29 0.495 -4.256 -7.012 1.00 12.49

ATOM 69 CA ARG A 29 0.889 -4.132 -6.543 1.00 11.68

ATOM 70 CB ARG A 29 1.620 -2.929 -7.175 1.00 12.22

ATOM 71 CG ARG A 29 1.326 -1.574 -6.549 1.00 12.91

ATOM 72 CD ARG A 29 0.155 -1.193 -6.694 1.00 16.99

ATOM 73 NE ARG A 29 0.462 -0.915 -8.085 1.00 15.60

ATOM 74 CZ ARG A 29 1.632 -1.122 -8.680 1.00 15.33

ATOM 75 NHl ARG A 29 1.756 -0.830 -9.977 1.00 15.30

ATOM 76 NH2 ARG A 29 2.666 -1.624 -8.014 1.00 14.56

ATOM 77 C ARG A 29 1.647 -5.398 -6.895 1.00 12.69

ATOM 78 O ARG A 29 1.413 -5.997 -7.946 1.00 12.34

ATOM 79 N PHE A 30 2.543 -5.795 -5.998 1.00 11.95

ATOM 80 CA PHE A 30 3.467 -6.907 -6.193 1.00 10.37

ATOM 81 CB PHE A 30 3.107 -8.083 -5.261 1.00 9.20

ATOM 82 CG PHE A 30 1.743 -8.602 -5.592 1.00 10.35

ATOM 83 CDl PHE A 30 0.615 -7.896 -5.202 1.00 8.10

ATOM 84 CEl PHE A 30 0.652 -8.321 -5.539 1.00 9.18

ATOM 85 CZ PHE A 30 0.805 -9.450 -6.272 1.00 10.55

ATOM 86 CE2 PHE A 30 0.299 -10.180 -6.698 1.00 11.08

ATOM 87 CD2 PHE A 30 1.570 -9.748 -6.360 1.00 10.52

ATOM 88 C PHE A 30 4.854 -6.368 -5.891 1.00 10.56

ATOM 89 O PHE A 30 5.153 -5.997 -4.751 1.00 10.73

ATOM 90 N ALA A 31 5.680 -6.272 -6.929 1.00 10.61

ATOM 91 CA ALA A 31 6.973 -5.646 -6.821 1.00 11.42

ATOM 92 CB ALA A 31 7.923 -6.540 -6.040 1.00 11.86

ATOM 93 C ALA A 31 6.840 -4.278 -6.156 1.00 ,11.51

ATOM 94 O ALA A 31 7.657 -3.917 -5.316 1.00 9.47

ATOM 95 N GLY A 32 5.797 -3.540 -6.530 1.00 11.32

ATOM 96 CA GLY A 32 5.559 -2.191 -6.027 1.00 11.28

ATOM 97 C GLY A 32 4.830 -2.097 -4.690 1.00 11.28

ATOM 98 O GLY A 32 4.427 -1.009 -4.293 1.00 10.89

ATOM 99 N VAL A 33 4.661 -3.223 -3.997 1.00 10.39

ATOM 100 CA VAL A 33 3.992 -3.239 -2.691 1.00 9.48

ATOM 101 CB VAL A 33 4.591 -4.319 -1.749 1.00 9.71

ATOM 102 CGl VAL A 33 3.874 -4.334 -0.398 1.00 6.56

ATOM 103 CG2 VAL A 33 6.067 -4.086 -1.542 1.00 7.32

ATOM 104 C VAL A 33 2.492 -3.475 -2.857 1.00 9.90

ATOM 105 O VAL A 33 2.075 -4.428 -3.544 1.00 10.85

ATOM 106 N PHE A 34 1.693 -2.618 -2.216 1.00 9.94

ATOM 107 CA PHE A 34 0.240 -2.805 -2.148 1.00 10.40

ATOM 108 CB PHE A 34 0.487 -1.958 -3.204 1.00 9.53

ATOM 109 CG PHE A 34 0.291 -0.455 -3.074 1.00 11.03

ATOM 110 CDl PHE A 34 1.365 0.372 -2.755 1.00 11.17

ATOM 111 CEl PHE A 34 1.216 1.761 -2.672 1.00 15.32

ATOM 112 CS PHE A 34 0.005 2.345 -2.929 1.00 11.93

ATOM 113 CE2 PHE A 34 1.079 1.531 -3.266 1.00 12.11

ATOM 114 CD2 PHE A 34 0.923 0.135 -3.348 1.00 8.64

ATOM 115 C PHE A 34 0.345 -2.538 -0.762 1.00 10.23

ATOM 116 O PHE A 34 0.287 -1.912 0.090 1.00 9.05

ATOM 117 N HIS A 35 1.555 -3.048 -0.561 1.00 10.72

ATOM 118 CA HIS A 35 2.301 -2.914 0.682 1.00 11.66

ATOM 119 CB HIS A 35 2.924 -4.267 1.033 1.00 13.10

ATOM 120 CG HIS A 35 3.980 -4.216 2.094 1.00 13.48

ATOM 121 NDl HIS A 35 5.325 -4.205 1.795 1.00 18.90

ATOM 122 CEl HIS A 35 6.025 -4.206 2.917 1.00 18.85

ATOM 123 NE2 HIS A 35 5.183 -4.213 3.932 1.00 16.14

ATOM 124 CD2 HIS A 35 3.897 -4.231 3.445 1.00 14.20

ATOM 125 C HIS A 35 3.368 -1.831 0.504 1.00 11.48

ATOM 126 O HIS A 35 4.032 -1.766 -0.548 1.00 11.76

ATOM 127 N VAL A 36 3.513 -0.984 1.527 1.00 11.99

ATOM 128 CA VAL A 36 4.531 0.061 1.550 1.00 11.65

ATOM 129 CB VAL A 36 3.910 1.468 1.540 1.00 11.49

ATOM 130 CGl VAL A 36 5.019 2.552 1.416 1.00 9.23

ATOM 131 CG2 VAL A 36 2.877 1.584 0.439 1.00 11.10

ATOM 132 C VAL A 35 5.384 -0.081 2.803 1.00 12.53

ATOM 133 O VAL A 36 4.862 -0.136 3.921 1.00 13.57 Table 4

ATOM 134 N GLU A 37 6.697 -0.133 2.600 1.00 12.45

ATOM 135 CA GLU A 37 7.662 -0.161 3.686 1.00 14.76

ATOM 136 CB GLU A 37 8.569 -1.365 3.527 1.00 13.02

ATOM 137 CG GLU A 37 9.736 -1.405 4.476 1.00 16.80

ATOM 138 CD GLU A 37 10.489 -2.712 4.381 1.00 21.07

ATOM 139 OEl GLO A 37 9.978 -3.653 3.722 1.00 22.12

ATOM 140 OE2 GLU A 37 11.567 -2.815 4.990 1.00 23.16

ATOM 141 C GLU A 37 8.467 1.122 3.637 1.00 15.90

ATOM 142 O GLU A 37 9.112 1.408 2.631 1.00 15.11

ATOM 143 N LYS A 38 8.428 1.899 4.710 1.00 18.71

ATOM 144 CA LYS A 38 9.126 3.189 4.718 1.00 20.38

ATOM 145 CB LYS A 38 8.303 4.264 5.417 1.00 21.78

ATOM 146 CG LYS A 38 9.083 5.540 5.659 1.00 20.47

ATOM 147 CD LYS A 38 8.557 6.298 6.842 1.00 21.92

ATOM 148 CE LYS A 38 9.515 7.395 7.243 1.00 23.53

ATOM 149 NZ LYS A 38 9.021 8.126 8.445 1.00 23.70

ATOM 150 C LYS A 38 10.486 3.074 5.385 1.00 20.39

ATOM 151 O LYS A 38 10.573 2.753 6.573 1.00 22.97

ATOM 152 N ASN A 39 11.537 3.377 4.621 1.00 21.71

ATOM 153 CA ASN A 39 12.910 3.225 5.089 1.00 19.16

ATOM 154 CB ASN A 39 13.270 4.324 6.105 1.00 18.32

ATOM 155 CG ASN A 39 13.403 5.698 5.469 1.00 18.36

ATOM 156 ODl ASN A 39 13.705 5.829 4.276 1.00 20.56

ATOM 157 ND2 ASN A 39 13.205 6.732 6.274 1.00 18.00

ATOM 158 C ASN A 39 13.103 1.821 5.664 1.00 17.83

ATOM 159 O ASN A 39 13.168 0.843 4.912 1.00 17.58

ATOM 160 N GLY A 40 13.166 1.695 6.985 1.00 16.86

ATOM 161 CA GLY A 40 13.302 0.373 7.600 1.00 16.82

ATOM 162 C GLY A 40 11.986 -0.357 7.837 1.00 17.53

ATOM 163 O GLY A 40 10.903 0.234 7.865 1.00 17.97

ATOM 164 N ARG A 41 12.095 -1.663 8.020 1.00 17.58

ATOM 165 CA ARG A 41 10.971 -2.500 8.415 1.00 17.28

ATOM 166 CB ARG A 41 11.525 -3.888 8.714 1.00 18.30

ATOM 167 CG ARG A 41 10.549 -4.919 9.215 1.00 20.65

ATOM 168 CD ARG A 41 11.243 -6.267 9.156 1.00 28.83

ATOM 169 NE ARG A 41 10.606 -7.233 9.983 1.00 36.83

ATOM 170 CZ ARG A 41 11.059 -7.696 11.162 1.00 40.02

ATOM 171 NHl ARG A 41 12.158 -7.181 11.693 1.00 39.53

ATOM 172 NH2 ARG A 41 10.395 -8.643 11.823 1.00 40.72

ATOM 173 C ARG A 41 10.236 -1.931 9.644 1.00 16.10

ATOM 174 O ARG A 41 10.853 -1.639 10.635 1.00 15.25

ATOM 175 N TYR A 42 8.919 -1.778 9.563 1.00 16.12

ATOM 176 CA TYR A 42 8.093 -1.375 10.712 1.00 16.21

ATOM 177 CB TYR A 42 8.115 -2.459 11.806 1.00 16.17

ATOM 178 CG TYR A 42 7.654 -3.839 11.379 1.00 14.78

ATOM 179 CDl TYR A 42 8.188 -4.979 11.981 1.00 12.62

ATOM 180 CEl TYR A 42 7.766 -6.244 11.623 1.00 9.86

ATOM 181 CZ TYR A 42 6.794 -6.392 10.631 1.00 13.36

ATOM 182 OH TYR A 42 6.372 -7.655 10.264 1.00 13.67

ATOM 183 CE2 TYR A 42 6.247 -5.274 10.027 1.00 13.62

ATOM 184 CD2 TYR A 42 6.673 -4.011 10.398 1.00 15.91

ATOM 185 C TYR A 42 8.455 -0.027 11.347 1.00 16.62

ATOM 186 O TYR A 42 8.691 0.045 12.552 1.00 15.40

ATOM 187 N SER A 43 8.450 1.041 10.553 1.00 16.08

ATOM 188 CA SER A 43 8.777 2.367 11.061 1.00 15.58

ATOM 189 CB SER A 43 10.078 2.850 10.414 1.00 16.39

ATOM 190 OG SER A 43 9.914 2.973 9.019 1.00 16.16

ATOM 191 C SER A 43 7.673 3.399 10.851 1.00 15.76

ATOM 192 O SER A 43 7.916 4.593 10.979 1.00 17.29

ATOM 193 N ILE A 44 6.454 2.940 10.569 1.00 13.71

ATOM 194 CA ILE A 44 5.326 3.818 10.256 1.00 13.21

ATOM 195 CB ILE A 44 4.619 3.356 8.930 1.00 12.91

ATOM 196 CGl ILE A 44 5.619 3.268 7.775 1.00 13.33

ATOM 197 CDl ILE A 44 5.051 2.638 6.528 1.00 13.67

ATOM 198 CG2 ILE A 44 3.481 4.268 8.563 1.00 12.49

ATOM 199 C ILE A 44 4.297 3.783 11.389 1.00 12.87

ATOM 200 O ILE A 44 3.897 2.708 11.822 1.00 14.82

ATOM 201 N SER R 45 3.849 4.953 11.844 1.00 12.78 Table 4

ATOM 202 CA SER A 45 2.726 5.038 12.788 00 12.15

ATOM 203 CB SER A 45 2.801 6.317 13.618 00 12.43

ATOM 204 OG SER A 45 2.549 7.445 12.803 00 12.43

ATOM 205 C SER A 45 1.400 5.002 12.034 00 11.46

ATOM 206 O SER A 45 1.374 5.104 10.811 00 12.62

ATOM 207 N ARG A 46 0.298 4.867 12.761 00 10.89

ATOM 208 CA ARG A 46 -1.018 4.778 12.118 00 10.68

ATOM 209 CB ARG A 46 -2.080 4.313 13.127 00 11.19

ATOM 210 CG ARG A 46 -3.559 4.483 12.733 00 13.92

ATOM 211 CD ARG A 46 -4.020 3.951 11.350 00 17.46

ATOM 212 NE ARG A 46 -4.209 2.495 11.231 00 26.69

ATOM 213 CZ ARG A 46 -5.007 1.737 11.993 00 31.63

ATOM 214 NHl ARG A 46 -5.734 2.255 12.988 00 39.85

ATOM 215 NH2 ARG A 46 -5.075 0.431 11.765 00 37.37

ATOM 216 C ARG A 46 -1.375 6.107 11.439 00 10.59

ATOM 217 O ARG A 46 -1.932 6.107 10.336 00 10.19

ATOM 218 N THR A 47 -1.005 7.225 12.067 00 9.76

ATOM 219 CA THR A 47 -1.233 8.544 11.478 00 9.62

ATOM 220 CB THR A 47 -1 008 9.728 12.459 00 9.71

ATOM 221 OGl THR A 47 0.274 9.624 13.109 00 12.60

ATOM 222 CG2 THR A 47 2.118 9.768 13.482 1.00 9.18

ATOM 223 C THR A 47 0.393 8.751 10.231 00 9.38

ATOM 224 O THR A 47 0.905 9.252 9.241 00 9.61

ATOM 225 N GLU A 48 0.878 8.352 10.265 00 9.55

ATOM 226 CA GLU A 48 1.728 8.436 9.091 ,00 9.27

ATOM 227 CB GLO A 48 3.192 8.211 9.417 00 9.16

ATOM 228 CG GLU A 48 4.101 8.351 8.193 00 11.30

ATOM 229 CD GLU A 48 5.571 8.320 8.525 ,00 14.18

ATOM 230 OEl GLU A 48 5.904 8.207 9.712 1.00 14.05

ATOM 231 OE2 GLO A 48 6.395 8.417 7.598 .00 18.27

ATOM 232 C GLU A 48 1.277 7.587 7.944 ,00 9.37

ATOM 233 O GLU A 48 444 7.953 6.777 .00 8.69

ATOM 234 N ALA A 49 0.737 6.412 8.281 .00

ATOM 235 CA ALA A 49 0.275 5.445 7.285 .00 9.44

ATOM 236 CB ALA A 49 ^■0.129 4.128 7.965 ,00 8.35

ATOM 237 C ALA A 49 0.893 6.003 6.465 .00 9.20

ATOM 238 O ALA A 49 0.917 5.854 5.242 ,00 7.83

ATOM 239 N ALA A 50 -1.851 6.640 7.144 .00 9.21

ATOM 240 CA ALA A 50 -2.974 7.276 6.476 .00 11.00

ATOM 241 CB ALA A 50 -3.984 7.786 7.488 ,00 10.98

ATOM 242 C ALA A 50 -2.489 8.415 5.575 ,00 10.68

ATOM 243 O ALA A 50 -2.949 8.547 4.450 ,00 12.34

ATOM 244 N ASP A 51 -1.539 9.211 6.065 ,00 10.88

ATOM 245 CA ASP A 51 -0.949 10.288 5.264 ,00 11.73

ATOM 246 CB ASP A 51 0.001 11.150 6.107 ,00 11.66

ATOM 247 CG ASP A 51 -0.729 12.040 7.100 .00 14.75

ATOM 248 ODl ASP A 51 -1.956 12.217 6.994 ,00 15.68

ATOM 249 OD2 ASP A 51 -0.056 12.577 7.995 ,00 17.88

ATOM 250 C ASP A 51 -0.192 9.748 4.050 ,00 11.73

ATOM 251 O ASP A 51 -0.254 10.326 2.972 ,00 12.65

ATOM 252 N LEO A 52 0.511 8.640 4.242 ,00 11.71

ATOM 253 CA LEU A 52 1.257 7.993 3.176 ,00 12.76

ATOM 254 CB LEU A 52 2.064 6.813 3.748 ,00 11.67

ATOM 255 CG LEU A 52 3.174 6.185 2.896 00 17.47

ATOM 256 CDl LEU A 52 4.054 7.224 2.236 ,00 18.98

ATOM 257 CD2 LEU A 52 3.994 5.257 .765 ,00 17.28

ATOM 258 C LEU A 52 0.329 7.495 .065 ,00 11.35

ATOM 259 O LEU A 52 0.555 7.770 00 11.33

ATOM 260 N CYS A 53 -0.711 6.752 434 00 10.59

ATOM 261 CA CYS A 53 -1.669 6.267 1.445 ,00 11.08

ATOM 262 CB CYS A 53 -2.759 5..406 2.088 00 10.38

ATOM 263 SG CYS A 53 -2.200 3..780 2.750 00 10.80

ATOM 264 C CYS A 53 -2.302 7..434 0.690 00 11.67

ATOM 265 O CYS A 53 -2.429 7.377 -0.525 ,00 11.52

ATOM 266 N LYS A 54 -2.684 8.477 1.421 00 12.57

ATOM 267 CA LYS A 54 -3.285 9.679 0.831 00 13.42

ATOM 268 CB LYS A 54 -3.591 10.713 1.916 00 14.52

ATOM 269 CG LYS A 54 -4.218 11.995 1.393 1.00 15.40 Table 4

ATOM 270 CD LYS A 54 -4.495 12.975 2.522 1.00 18.23

ATOM 271 CE LYS A 54 -5.122 14.257 1.999 1.00 17.58

ATOM 272 NZ LYS A 54 -5.399 15.227 3.094 1.00 20.25

ATOM 273 C LYS A 54 -2.377 10.314 -0.229 1.00 13.28

ATOM 274 O LYS A 54 -2.854 10.774 -1.278 1.00 12.90

ATOM 275 N ALA A 55 -1.075 10.327 0.053 1.00 13.34

ATOM 276 CA ALA A 55 -0.049 10.831 -0.877 1.00 13.44

ATOM 277 CB ALA A 55 1.295 10.858 -0.191 1.00 13.13

ATOM 278 C ALA A 55 0.041 10.001 -2.167 1.00 13.70

ATOM 279 O ALA A 55 0.409 10.516 -3.230 1.00 12.60

ATOM 280 N PHE A 56 -0.299 8.718 -2.056 1.00 13.91

ATOM 281 CA PHE A 56 -0.419 7.819 -3.200 1.00 13.63

ATOM 282 CB PHE A 56 -0.135 6.363 -2.754 1.00 12.63

ATOM 283 CG PHE A 56 1.323 5.998 -2.685 1.00 13.10

ATOM 284 CDl PHE A 56 1.904 5.639 -1.484 1.00 13.19

ATOM 285 CEl PHE A 56 3.255 5.278 -1.414 1.00 13.95

ATOM 286 CZ PHE A 56 4.023 5.265 -2.553 1.00 16.65

ATOM 287 CE2 PHE A 56 3.451 5.619 -3.772 1.00 15.18

ATOM 288 CD2 PHE A 56 2.105 5.977 -3.833 1.00 14.35

ATOM 289 C PHE A 56 -1.821 7.849 -3.845 1.00 14.90

ATOM 290 O PHE A 56 -2.148 6.957 -4.624 1.00 14.33

ATOM 291 N ASN A 57 -2.634 8.856 -3.521 1.00 15.02

ATOM 292 CA ASN A 57 -4.016 8.921 -3.985 1.00 15.98

ATOM 293 CB ASN A 57 -4.061 9.231 -5.491 1.00 15.74

ATOM 294 CG ASN A 57 -5.414 9.756 -5.940 1.00 18.62

ATOM 295 ODl ASN A 57 -6.039 10.554 -5.241 1.00 19.59

ATOM 296 ND2 ASN A 57 -5.866 9.321 -7.116 1.00 17.11

ATOM 297 C ASN A 57 -4.759 7.616 -3.669 1.00 15.70

ATOM 298 O ASN A 57 -5.545 7.121 -4.474 1.00 17.03

ATOM 299 N SER A 58 -4.480 7.068 -2.483 1.00 14.86

ATOM 300 CA SER A 58 -5.010 5.794 -2.050 1.00 13.24

ATOM 301 CB SER A 58 -3.886 4.760 -2.061 1.00 11.53

ATOM 302 OG SER A 58 -3.343 4.666 -3.372 1.00 12.37

ATOM 303 C SER A 58 -5.590 5.956 -0.655 1.00 13.31

ATOM 304 O SER A 58 -5.509 7.034 -0.057 1.00 13.23

ATOM 305 N THR A 59 -6.188 4.880 -0.159 1.00 12.48

ATOM 306 CA THR A 59 -6.751 4.832 1.173 1.00 13.35

ATOM 307 CB THR A 59 -8.308 4.779 1.127 1.00 13.49

ATOM 308 OGl THR A 59 -8.745 3.651 0.363 1.00 13.05

ATOM 309 CG2 THR A 59 -8.883 6.056 0.502 1.00 13.53

ATOM 310 C THR A 59 -6.210 3.601 1.878 1.00 13.33

ATOM 311 O THR A 59 -5.686 2.698 1.232 1.00 14.31

ATOM 312 N LEU A 60 -6.304 3.577 3.203 1.00 12.42

ATOM 313 CA LEU A 60 -5.993 2.368 3.951 1.00 11.55

ATOM 314 CB LEU A 60 -6.016 2.647 5.451 1.00 10.37

ATOM 315 CG LEU A 60 -4.892 3.487 6.052 1.00 14.09

ATOM 316 CDl LEU A 60 -5.284 3.908 7.451 1.00 9.45

ATOM 317 CD2 LEU A 60 -3.602 2.718 5.081 1.00 9.72

ATOM 318 C LEU A 60 -7.064 1.324 3.575 1.00 10.50

ATOM 319 O LEU A 60 -8.256 1.647 3.583 1.00 9.10

ATOM 320 N PRO A 61 -6.649 0.108 3.174 1.00 10.51

ATOM 321 CA PRO A 61 -7.657 -0.866 2.743 1.00 10.33

ATOM 322 CB PRO A 61 -6.829 -2.107 2.372 1.00 10.91

ATOM 323 CG PRO A 61 -5.455 -1.563 2.022 1.00 10.46

ATOM 324 CD PRO A 61 -5.275 -0.404 3.001 1.00 10.89

ATOM 325 C PRO A 61 -8.690 -1.229 3.805 1.00 10.48

ATOM 326 O PRO A 61 -8.398 -1.206 5.004 1.00 10.15

ATOM 327 N THR A 62 -9.894 -1.550 3.356 1.00 10.58

ATOM 328 CA THR A 62 -10.861 -2.209 4.209 1.00 10.47

ATOM 329 CB THR A 62 -12.326 -2.117 3.670 1.00 10.43

ATOM 330 OGl THR A 62 -12.432 -2.813 2.427 1.00 10.24

ATOM 331 CG2 THR A 62 -12.777 -0.657 3.475 1.00 9.38

ATOM 332 C THR A 62 -10.458 -3.677 4.271 1.00 10.08

ATOM 333 O THR A 62 -9.650 -4.144 3.467 1.00 10.28

ATOM 334 N MET A 63 -11.024 -4.406 5.225 1.00 8.43

ATOM 335 CA ,MET A 63 -10.761 -5.837 5.358 1.00 8.57

ATOM 336 CB MET A 63 -11.413 -6.404 6.629 1.00 7.06

ATOM 337 CG MET A 63 -11.357 -7.935 6.743 1.00 8.94 Table 4

ATOM 338 SD MET A 63 -9.685 -8.633 6.741 00 4.25

ATOM 339 CE MET A 63 -9.151 -8.179 8.395 00 B.68

ATOM 340 C MET A 63 -11.241 -6.599 4.121 00 B.58

ATOM 341 O MET A 63 -10.526 -7.455 3.607 00 6.50

ATOM 342 N ALA A 54 -12.436 -6.275 3.638 00 8.72

ATOM 343 CA ALA A 64 -12.948 -6.872 2.397 00 9.68

ATOM 344 CB ALA A 64 -14.363 -6.364 2.112 00 10.93

ATOM 345 C ALA A 64 -12.041 -6.621 1.175 00 10.33

ATOM 346 O ALA A 64 -11.830 -7.521 0.361 00 9.60

ATOM 347 N GLN A 65 -11.517 -5.405 1.044 00 9.89

ATOM 348 CA GLN A 65 -10.528 -5. ,096 ^■0.012 00 9.82

ATOM 349 CB GLN A 65 -10.157 -3. 609 0.015 00 10.56

ATOM 350 CG GLN A 65 -11.090 -2.740 - 0.813 00 10.65

ATOM 351 CD GLN A 65 -11.141 -1.292 0.343 00 9.69

ATOM 352 OEl GLN A 65 -10.376 -0.873 0.530 00 7.94

ATOM 353 NE2 GLN A 65 -12.056 -0.516 ^■0.926 00 5.72

ATOM 354 C GLN A 65 -9.259 -5.956 0.104 00 9.69

ATOM 355 O GLN A 65 -8.731 -6.443 0.903 00 9.55

ATOM 356 N MET A 66 -8.785 -6.128 1.335 00 8.53

ATOM 357 CA MET A 66 -7.618 -6.957 1.619 00 8.43

ATOM 358 CB MET A 66 -7.223 -6.805 3.092 00 8.42

ATOM 359 CG MET A 66 -5.876 -7.413 3.457 00 7.82

ATOM 360 SD MET A 66 -4.483 -6.812 2.479 00 4.28

ATOM 361 CE MET A 66 -4.5OB -5.087 2.903 1.00 3.87

ATOM 362 C MET A 66 -7.887 -8.436 1.290 .00 8.12

ATOM 363 O MET A 66 -7.020 -9.132 0.748 .00 8.73

ATOM 364 N GLϋ A 67 -9.088 -8.905 1.615 .00 8.56

ATOM 365 CA GLU A 67 -9.468 -10.295 1.358 .00 8.78

ATOM 366 CB GLU A 67 -10.827 -10.604 1.990 .00 8.31

ATOM 367 CG GLU A 67 -10.867 -10.417 3.497 .00 10.13

ATOM 368 CD GLU A 67 -12.228 -10.732 4.087 .00 17.33

ATOM 369 OEl GLU A 67 -13.140 -11.098 3.316 .00 17.07

ATOM 370 OE2 GLU A 67 -12.382 -10.613 5.321 .00 21.19

ATOM 371 C GLU A 67 -9.498 -10.597 0.141 .00 8.94

ATOM 372 O GLU A 67 -9.014 -11.643 0.586 1.00 9.71

ATOM 373 N LYS A 68 -10.059 -9.684 0.918 1.00 10.25

ATOM 374 CA LYS A 68 -10.086 -9.862 2.367 1.00 10.67

ATOM 375 CB LYS A 68 -10.949 -8.783 3.023 1.00 10.43

ATOM 376 CG LYS A 68 -11.034 -8.891 -4 537 1.00 14.93

ATOM 377 CD LYS A 68 -11.905 -7.791 - 5.122 1.00 18.46

ATOM 378 CE LYS A 68 -11.990 -7.900 6.635 1 .00 21.27

ATOM 379 NZ LYS A 68 -12.840 -6.828 7.222 1.00 21.04

ATOM 380 C LYS A 68 -8.669 -9.845 2.955 1..00 10.72

ATOM 381 O LYS A 68 -8.357 -10.632 3.835 1..00 10.99

ATOM 382 N ALA A 69 -7.832 -8.938 2.470 1.00 10.05

ATOM 383 CA ALA A 69 -6.432 -8.861 -2 892 1.00 10.58

ATOM 384 CB ALA A 69 -5.737 -7.741 -2.165 1.00 10.98

ATOM 385 C ALA A 69 -5.712 -10.193 -2 646 1.00 10.96

ATOM 386 O ALA A 69 -5.002 -10.694 3.521 1.00 10.24

ATOM 387 N LEU A 70 -5.919 -10.761 1.462 1.00 10.77

ATOM 388 CA LEU A 70 -5.332 -12.050 1.111 1.00 11.99

ATOM 389 CB LEU A 70 -5.685 -12.425 0.334 00 11.09

ATOM 390 CG LEU A 70 -4.830 -13.502 1.014 00 16.19

ATOM 391 CDl LEU A 70 -4.911 -13.350 2.521 00 19.77

ATOM 392 CD2 LEU A 70 -5.232 -14.915 0.597 00 17.51

ATOM 393 C LEU A 70 -5.786 -13.133 -2 .098 00 11.90

ATOM 394 O LEU A 70 -4.966 -13.911 2.579 00 10.98

ATOM 395 N SER A 71 -7.080 -13.160 2.422 00 11.08

ATOM 396 CA SER A 71 -7.607 -14.133 -3 .400 00 11.69

ATOM 397 CB SER A 71 -9.141 -14.039 3.537 00 10.82

ATOM 398 OG SER A 71 -9.545 -12.911 4.289 00 10.27

ATOM 399 C SER A 71 -6.921 -14.029 4.771 00 10.84

ATOM 400 O SER A 71 -6.810 -15.032 5.466 00 11.60

ATOM 401 N ILE A 72 -6.431 -12.837 5.130 00 10.10

ATOM 402 CA ILE A 72 -5.719 -12.619 6.404 00 9.73

ATOM 403 CB ILE A 72 -5.826 -11.154 6.867 00 11.11

ATOM 404 CGl ILE A 72 -7.292 -10.766 -7 073 00 9.41

ATOM 405 CDl ILE A 72 -7.506 -9.285 -7.295 1.00 11.71 Table 4

ATOM 406 CG2 ILE A 72 -5.024 -10.938 -8.141 1.00 9.55

ATOM 407 C ILE A 72 -4.212 -12.933 -6.353 1.00 9.96

ATOM 408 O ILE A 72 -3.506 -12.753 -7.354 1.00 9.51

ATOM 409 N GLY A 73 -3.707 -13.366 -5.201 1.00 8.31

ATOM 410 CA GLY A 73 -2.294 -13.731 -5.080 1.00 9.43

ATOM 411 C GLY A 73 -1.457 -12.862 -4.163 1.00 9.69

ATOM 412 O GLY A 73 -0.252 -13.070 -4.068 1.00 8.16

ATOM 413 N PHE A 74 -2.081 -11.897 -3.478 1.00 9.73

ATOM 414 CA PHE A 74 -1.353 -11.006 -2.580 1.00 9.64

ATOM 415 CB PHE A 74 -2.183 -9.749 -2.264 1.00 10.03

ATOM 416 CG PHE A 74 -1.422 -8.657 -1.532 1.00 9.06

ATOM 417 CDl PHE A 74 -0.090 -8.354 -1.843 1.00 9.04

ATOM 418 CEl PHE A 74 0.587 -7.336 -1.185 1.00 10.43

ATOM 419 CZ PHE A 74 -0.057 -6.607 -0.215 1.00 9.35

ATOM 420 CE2 PHE A 74 -1.384 -6.899 0.109 1.00 10.11

ATOM 421 CD2 PHE A 74 -2.052 -7.909 -0.549 1.00 10.40

ATOM 422 C PHE A 74 -1.009 -11.713 -1.273 1.00 10.40

ATOM 423 O PHE A 74 -1.892 -12.209 -0.584 1.00 10.09

ATOM 424 N GLU A 75 0.279 -11.747 -0.946 1.00 11.24

ATOM 425 CA GLU A 75 0.724 -12.123 0.392 1.00 12.49

ATOM 426 CB GLU A 75 0.799 -13.664 0.554 1.00 12.76

ATOM 427 CG GLU A 75 2.124 -14.300 0.182 1.00 14.18

ATOM 428 CD GLU A 75 2.140 -15.816 0.341 1.00 16.98

ATOM 429 OEl GLU A 75 2.795 -16.461 -0.492 1.00 17.21

ATOM 430 OE2 GLU A 75 1.504 -16.375 1.269 1.00 12.98

ATOM 431 C GLU A 75 2.058 -11.422 0.687 1.00 12.45

ATOM 432 O GLU A 75 2.834 -11.121 -0.228 1.00 12.04

ATOM 433 N THR A 76 2.285 -11.115 1.961 1.00 12.02

ATOM 434 CA THR A 76 3.567 -10.592 2.458 1.00 13.80

ATOM 435 CB THR A 76 3.469 -9.103 2.869 1.00 15.29

ATOM 436 OGl THR A 76 2.744 -9.004 4.103 1.00 17.12

ATOM 437 CG2 THR A 76 2.784 -8.247 1.767 1.00 18.05

ATOM 438 C THR A 76 3.931 -11.352 3.720 1.00 13.03

ATOM 439 O THR A 76 3.116 -12.098 4.250 1.00 10.64

ATOM 440 N CYS A 77 5.139 -11.109 4.221 1.00 12.33

ATOM 441 CA CYS A 77 5.545 -11.552 5.551 1.00 12.84

ATOM 442 CB CYS A 77 6.804 -12.409 5.450 1.00 13.70

ATOM 443 SG CYS A 77 7.148 -13.295 6.946 1.00 12.58

ATOM 444 C CYS A 77 5.788 -10.346 6.469 1.00 13.60

ATOM 445 O CYS A 77 6.742 -10.342 7.261 1.00 13.23

ATOM 446 N ARG A 78 4.896 -9.348 6.367 1.00 13.77

ATOM 447 CA ARG A 78 4.995 -8.079 7.101 1.00 13.51

ATOM 448 CB ARG A 78 5.497 -6.976 6.181 1.00 15.26

ATOM 449 CG ARG A 78 6.885 -7.180 5.692 1.00 17.72

ATOM 450 CD ARG A 78 7.871 -7.171 6.836 1.00 24.58

ATOM 451 NE ARG A 78 9.232 -7.082 6.329 1.00 28.43

ATOM 452 CZ ARG A 78 9.807 -5.957 5.921 1.00 31.48

ATOM 453 NHl ARG A 78 11.067 -5.986 5.468 1.00 25.95

ATOM 454 NH2 ARG A 78 9.142 -4.808 5.988 1.00 33.93

ATOM 455 C ARG A 78 3.659 -7.616 7.676 1.00 12.76

ATOM 456 O ARG A 78 2.635 -7.612 6.981 1.00 12.00

ATOM 457 N TYR A 79 3.684 -7.219 8.947 1.00 11.16

ATOM 458 CA TYR A 79 2.532 -6.600 9.595 1.00 11.86

ATOM 459 CB TYR A 79 2.695 -6.572 11.120 1.00 12.31

ATOM 460 CG TYR A 79 2.562 -7.933 11.763 1.00 14.89

ATOM 461 CDl TYR A 79 3.682 -8.624 12.222 1.00 16.83

ATOM 462 CEl TYR A 79 3.562 -9.885 12.797 1.00 20.51

ATOM 463 CZ TYR A 79 2.319 -10.451 12.928 1.00 20.67

ATOM 464 OH TYR A 79 2.196 -11.698 13.484 1.00 25.01

ATOM 465 CE2 TYR A 79 1.192 -9.789 12.475 1.00 19.26

ATOM 466 CD2 TYR A 79 1.321 -8.532 11.906 1.00 19.63

ATOM 467 C TYR A 79 2.366 -5.183 9.049 1.00 11.90

ATOM 468 O TYR A 79 3.337 -4.457 8.890 1.00 11.93

ATOM 469 N GLY A 80 1.130 -4.799 8.772 1.00 11.73

ATOM 470 CA GLY A 80 0.847 -3.501 8.196 1.00 11.58

ATOM 471 C GLY A 80 -0.558 -3.034 8.486 1.00 10.62

ATOM 472 O GLY A 80 -1.472 -3.844 8.613 1.00 8.34

ATOM 473 N PHE A 81 -0.710 -1.713 8.566 1.00 10.21 Table 4

ATOM 474 CA PHE A 81 -1.998 -1.069 8.782 00 10.34 ATOM 475 CB PHE A 81 -1.828 0.444 8.988 00 10.14 ATOM 476 CG PHE A 81 -0.975 0.802 10.160 00 10.78 ATOM 477 CDl PHE A 81 0.311 1.257 9.977 1.00 10.93 ATOM 478 CEl PHE A 81 1.108 1.588 11.064 00 9.53 ATOM 479 CZ PHE A 81 0.631 1.450 12.348 00 7.99 ATOM 480 CE2 PHE A 81 -0.651 0.988 12.554 00 11.56 ATOM 481 CD2 PHE A 81 -1.455 0.664 11.453 00 10.72 ATOM 482 C PHE A 81 -2.966 -1.279 7.626 00 10.85 ATOM 483 O PHE A 81 -2.587 -1.196 6.458 00 9.31 ATOM 484 N ILE A 82 -4.210 -1.608 983 00 11.06 ATOM 485 CA ILE A 82 -5.362 -1.335 140 00 10.96 ATOM 486 CB ILE A 82 -6.097 -2.629 670 00 12.60 ATOM 487 CGl ILE A 82 -6.653 -3.440 837 00 12.98 ATOM 488 CDl ILE A 82 -7.553 -4.554 393 00 14.63 ATOM 489 CG2 ILE A 82 -5.173 -3.494 836 00 14.32 ATOM 490 C ILE A 82 -6.272 -0.422 961 00 10.72 ATOM 491 O ILE A 82 -5.852 0.090 9.014 00 7.75 ATOM 492 N GLO A 83 -7.482 -0.173 7.459 00 10.70 ATOM 493 CA GLU A 83 -8.509 0.518 8.236 00 11.41 ATOM 494 CB GLϋ A 83 -9.757 0.780 7.379 1.00 11.86 ATOM 495 CG GLO A 83 -10.800 1.673 8.048 1.00 11.95 ATOM 496 CD GLU A 83 -10.254 3.047 8.396 1.00 16.52 ATOM 497 OEl GLU A 83 -9.535 3.633 7.554 00 17.81 ATOM 498 OE2 GLO A 83 -10.538 3.542 9.511 00 16.39 ATOM 499 C GLU A 83 -8.880 -0.310 9.476 00 12.08 ATOM 500 O GLU A 83 -9.390 -1.439 9.361 00 11.20 ATOM 501 N GLY A 84 -8.583 0.222 10.659 00 11.64 ATOM 502 CA GLY A 84 -9.059 -0.382 11.904 00 12.65 ATOM 503 C GLY A 84 -8.153 -1.403 12.565 00 12.79 ATOM 504 O GLY A 84 -8.235 -1.582 13.768 00 14.07 ATOM 505 N HIS A 85 -7.290 -2.065 11.793 00 11.91 ATOM 506 CA HIS A 85 -6.445 -3.159 12.297 00 11.86 ATOM 507 CB HIS A 85 -7.139 -4.508 12.097 00 11.92 ATOM 508 CG HIS A 85 -8.500 -4.625 12.827 00 14.35 ATOM 509 NDl HIS A 85 -8.605 -4.703 14.198 00 15.86 ATOM 510 CEl HIS A 85 -9.880 -4.794 14.534 00 17.63 ATOM 511 NE2 HIS A 85 -10.604 -4.777 13.430 00 17.54 ATOM 512 CD2 HIS A 85 -9.766 -4.672 12.346 00 15.64 ATOM 513 C HIS A 85 -5.063 -3.216 11.626 1.00 10.62 ATOM 514 O HIS A 85 -4.811 -2.533 10.633 00 9.73 ATOM 515 N VAL A 86 -4.184 -4.026 12.206 00 11.31 ATOM 516 CA VAL A 86 -2.867 -4.343 11.663 00 11.63 ATOM 517 CB VAL A 86 -1.764 -4.169 12.730 00 11.92 ATOM 518 CGl VAL A 86 -0.403 -4.643 12.207 00 12.67 ATOM 519 CG2 VAL A 86 -1.699 -2.703 13.172 00 12.19 ATOM 520 C VAL A 86 -2.922 -5.800 11.228 00 10.80 ATOM 521 O VAL A 86 -3.289 -6.670 12.020 00 12.08 ATOM 522 N VAL A 87 -2.584 -6.065 9.968 00 11.24 ATOM 523 CA VAL A 87 -2.738 -7.405 9.395 00 8.85 ATOM 524 CB VAL A 87 -3.987 -7.469 8.490 00 9.64 ATOM 525 CGl VAL A 87 -5.249 -7.013 9.258 00 7.44 ATOM 526 CG2 VAL A 87 -3.780 -6.641 7.196 00 9.12 ATOM 527 C VAL A 87 -1.527 -7.885 8.583 00 9.50 ATOM 528 O VAL A 87 -0.629 -7.111 8.256 00 9.52 ATOM 529 N ILE A 88 -1.510 -9.186 8.298 00 8.70 ATOM 530 CA ILE A 83 -0.634 -9.786 7.284 00 9.27 ATOM 531 CB ILE A 88 0.486 -10.696 7.854 00 9.15 ATOM 532 CGl ILE A 88 1.249 -10.018 8.970 00 11.87 ATOM 533 CDl ILE A 88 2.475 -10.795 9.433 00 11.89 ATOM 534 CG2 ILE A 88 1.450 -11.108 6.743 00 10.13 ATOM 535 C ILE A 88 -1.492 -10.706 6.413 00 8.88 ATOM 536 O ILE A 88 -2.121 -11.621 6.938 00 8.87 ATOM 537 N PRO A 89 -1.523 -10.460 5.087 00 9.88 ATOM 538 CA PRO A 89 -2.157 -11.414 4.194 00 8.93 ATOM 539 CB PRO A 89 -2.352 -10.608 905 00 9.54 ATOM 540 CG PRO A 89 -1.239 -9.595 927 00 9.84 ATOM 541 CD PRO A 89 -0.958 -9.306 4.364 1.00 8.62 Table 4

ATOM 542 C PRO A 89 -1.249 -12.608 3.933 1.00 9.82

ATOM 543 O PRO A 89 -0.112 -12.423 3.502 1.00 9.41

ATOM 544 N ARG A 90 -1.762 -13.813 4.180 1.00 9.08

ATOM 545 CA ARG A 90 -1.009 -15.039 3.978 1.00 9.85

ATOM 546 CB ARG A 90 -0.754 -15.700 5.332 1.00 9.36

ATOM 547 CG ARG A 90 0.176 -14.910 6.272 1.00 10.24

ATOM 548 CD ARG A 90 1.542 -14.627 5.653 1.00 12.74

ATOM 549 NE ARG A 90 2.191 -15.839 5.163 1.00 10.99

ATOM 550 CZ ARG A 90 3.175 -15.881 4.272 1.00 15.31

ATOM 551 NHl ARG A 90 3.653 -14.770 3.735 1.00 11.00

ATOM 552 NH2 ARG A 90 3.679 -17.058 3.903 1.00 16.43

ATOM 553 C ARG A 90 -1.751 -16.011 3.068 1.00 10.21

ATOM 554 O ARG A 90 -2.910 -16.341 3.321 1.00 9.34

ATOM 555 N ILE A 91 -1.087 -16.454 2.002 1.00 11.13

ATOM 556 CA ILE A 91 -1.627 -17.509 1.141 1.00 12.66

ATOM 557 CB ILE A 91 -1.360 -17.236 -0.366 1.00 12.69

ATOM 558 CGl ILE A 91 -2.152 -16.005 -0.807 1.00 12.74

ATOM 559 CDl ILE A 91 -1.770 -15.469 -2.144 1.00 8.75

ATOM 560 CG2 ILE A 91 -1.751 -18.465 -1.226 1.00 11.29

ATOM 561 C ILE A 91 -1.055 -18.858 1.560 1.00 13.99

ATOM 562 O ILE A 91 -1.815 -19.764 1.883 1,00 13.57

ATOM 563 N HIS A 92 0.276 -18.958 1.575 1.00 14.46

ATOM 564 CA HIS A 92 0.978 -20.193 1.984 1.00 15.41

ATOM 565 CB HIS A 92 2.237 -20.410 1.141 1.00 15.01

ATOM 566 CG HIS A 92 2.015 -20.218 -0.322 1.00 14.66

ATOM 567 NDl HIS A 92 1.590 -21.234 -1.150 1.00 15.39

ATOM 568 CEl HIS A 92 1.459 -20.767 -2.379 1.00 15.59

ATOM 569 NE2 HIS A 92 1.795 -19.490 -2.380 1.00 17.21

ATOM 570 CD2 HIS A 92 2.148 -19.124 -1.105 1.00 13.94

ATOM 571 C HIS A 92 1.381 -20.140 3.459 1.00 16.52

ATOM 572 O HIS A 92 1.848 -19.104 3.933 1.00 16.57

ATOM 573 N PRO A 93 1.208 -21.254 4.188 1.00 16.72

ATOM 574 CA PRO A 93 1.595 -21.280 5.591 1.00 17.66

ATOM 575 CB PRO A 93 1.015 -22.600 6.092 1.00 16.88

ATOM 576 CG PRO A 93 0.925 -23.447 4.910 1.00 17.39

ATOM 577 CD PRO A 93 0.642 -22.543 3.756 1.00 16.90

ATOM 578 C PRO A 93 3.112 -21.248 5.750 1.00 18.20

ATOM 579 O PRO A 93 3.826 -21.991 5.089 1.00 17.57

ATOM 580 N ASN A 94 3.583 -20.341 6.592 1.00 19.02

ATOM 581 CA ASN A 94 4.999 -20.205 6.901 1.00 20.31

ATOM 582 CB ASN A 94 5.599 -19.039 6.114 1.00 21.31

ATOM 583 CG ASN A 94 7.097 -18.901 6.306 1.00 24.23

ATOM 584 ODl ASN A 94 7.598 -18.928 7.431 1.00 27.53

ATOM 585 ND2 ASN A 94 7.817 -18.721 5.209 1.00 26.51

ATOM 586 C ASN A 94 5.095 -19.968 8.403 1.00 19.87

ATOM 587 O ASN A 94 4.314 -19.185 8.958 1.00 18.65

ATOM 588 N SER A 95 6.044 -20.649 9.045 1.00 20.08

ATOM 589 CA SER A 95 6.170 -20.631 10.505 1.00 20.97

ATOM 590 CB SER A 95 7.232 -21.633 10.963 1.00 20.99

ATOM 591 OG SER A 95 8.511 -21.285 10.464 1.00 25.53

ATOM 592 C SER A 95 6.529 -19.258 11.078 1.00 20.37

ATOM 593 O SER A 95 6.151 -18.944 12.207 1.00 20.31

ATOM 594 N ILE A 96 7.224 -18.442 10.289 1.00 20.24

ATOM 595 CA ILE A 96 7.685 -17.121 10.735 1.00 21.01

ATOM 596 CB ILE A 96 9.192 -16.949 10.462 1.00 22.11

ATOM 597 CGl ILE A 96 9.505 -17.150 8.973 1.00 24.29

ATOM 598 CDl ILE A 96 10.810 -16.541 8.542 1.00 25.36

ATOM 599 CG2 ILE A 96 9.977 -17.950 11.292 1.00 25.76

ATOM 600 C ILE A 96 6.909 -15.971 10.104 1.00 19,29

ATOM 601 O ILE A 96 7.349 -14.822 10.184 1.00 19.46

ATOM 602 N CYS A 97 5.760 -16.278 9.490 1.00 17.45

ATOM 603 CA CYS A 97 4.863 -15.274 8.904 1.00 15.41

ATOM 604 CB CYS A 97 4.916 -15.319 7.372 1.00 14.40

ATOM 605 SG CYS A 97 6.568 -15.199 6.614 1.00 15.25

ATOM 606 C CYS A 97 3.420 -15.490 9.387 1.00 14.48

ATOM 607 O CYS A 97 2.657 -16.253 8.790 1.00 14.05

ATOM 608 N ALA A 98 3.055 -14.803 10.469 1.00 13.46

ATOM 609 CA ALA A 98 1.791 -15.025 11.183 1.00 13.75 Table 4

ATOM 610 CB ALA A 98 0.597 -14.626 10.318 1.00 13.36

ATOM 611 C ALA A 98 1.642 -16.462 11.696 1.00 14.26

ATOM 612 O ALA A 98 0.543 -17.003 11.739 1.00 12.67

ATOM 613 N ALA A 99 2.762 -17.073 12.074 1.00 14.09

ATOM 614 CA ALA A 99 2.759 -18.362 12.757 1.00 15.52

ATOM 615 CB ALA A 99 2.307 -18.181 14.203 1.00 14.81

ATOM 616 C ALA A 99 1.898 -19.403 12.048 1.00 15.76

ATOM 617 O ALA A 99 0.970 -19.968 12.640 1.00 16.95

ATOM 618 N ASN A 100 2.213 -19.635 10.772 1.00 14.86

ATOM 619 CA ASN A 100 1.581 -20.679 9.964 1.00 14.76

ATOM 620 CB ASN A 100 1.732 -22.050 10.651 1.00 15.17

ATOM 621 CG ASN A 100 2.806 -22.898 10.031 1.00 17.46

ATOM 622 ODl ASN A 100 3.164 -23.936 10.581 1.00 20.35

ATOM 623 ND2 ASN A 100 3.312 -22.493 8.883 1.00 12.49

ATOM 624 C ASN A 100 0.114 -20.448 9.568 1.00 13.95

ATOM 625 O ASN A 100 -0.515 -21.338 9.003 1.00 13.66

ATOM 626 N ASN A 101 -0.423 -19.259 9.833 1.00 13.51

ATOM 627 CA ASN A 101 -1.815 -18.962 9.473 1.00 14.66

ATOM 628 CB ASN A 101 -2.364 -17.830 10.344 1.00 14.10

ATOM 629 CG ASN A 101 -2.342 -18.169 11.822 1.00 19.78

ATOM 630 ODl ASN A 101 -2.638 -19.298 12.214 1.00 21.65

ATOM 631 ND2 ASN A 101 -1.991 -17.190 12.647 1.00 19.45

ATOM 632 C ASN A 101 -1.925 -18.606 7.995 1.00 13.36

ATOM 633 O ASN A 101 -0.960 -18.140 7.372 1.00 12.85

ATOM 634 N THR A 102 -3.110 -18.853 7.447 1.00 12.60

ATOM 635 CA THR A 102 -3.467 -18.447 6.099 1.00 13.91

ATOM 636 CB THR A 102 -3.798 -19.662 5.187 1.00 15.19

ATOM 637 OGl THR A 102 -5.035 -20.261 5.590 1.00 20.32

ATOM 638 CG2 THR A 102 -2.688 -20.697 5.245 1.00 14.20

ATOM 639 C THR A 102 -4.678 -17.530 6.215 1.00 14.58

ATOM 640 O THR A 102 -5.380 -17.549 7.226 1.00 12.43

ATOM 641 N GLY A 103 -4.919 -16.727 5.184 1.00 14.39

ATOM 642 CA GLY A 103 -6.013 -15.774 5.201 1.00 12.93

ATOM 643 C GLY A 103 -5.449 -14.439 5.619 1.00 12.52

ATOM 644 O GLY A 103 -4.233 -14.272 5.677 1.00 11.78

ATOM 645 N VAL A 104 -6.328 -13.483 5.891 1.00 13.17

ATOM 646 CA VAL A 104 -5.886 -12.183 6.372 1.00 14.46

ATOM 647 CB VAL A 104 -6.855 -11.050 6.005 1.00 15.31

ATOM 648 CGl VAL A 104 -6.320 -9.699 6.524 1.00 15.46

ATOM 649 CG2 VAL A 104 -7.058 -11.001 4.494 1.00 15.53

ATOM 650 C VAL A 104 -5.775 -12.298 7.873 1.00 15.49

ATOM 651 O VAL A 104 -6.789 -12.298 8.570 1.00 15.05

ATOM 652 N TYR A 105 -4.545 -12.433 8.362 1.00 15.33

ATOM 653 CA TYR A 105 -4.320 -12.618 9.786 1.00 15.90

ATOM 654 CB TYR A 105 -3.012 -13.358 10.074 1.00 15.73

ATOM 655 CG TYR A 105 -2.763 -13.527 11.562 1.00 18.95

ATOM 656 CDl TYR A 105 -3.332 -14.585 12.275 1.00 21.32

ATOM 657 CEl TYR A 105 -3.113 -14.728 13.647 1.00 26.03

ATOM 658 CZ TYR A 105 -2.318 -13.803 14.312 1.00 27.26

ATOM 659 OH TYR A 105 -2.084 -13.921 15.668 1.00 32.16

ATOM 660 CE2 TYR A 105 -1.746 -12.758 13.623 1.00 26.04

ATOM 661 CD2 TYR A 105 -1.969 -12.623 12.258 1.00 20.23

ATOM 662 C TYR A 105 -4.300 -11.258 10.464 1.00 16.54

ATOM 663 O TYR A 105 -3.549 -10.372 10.066 1.00 14.55

ATOM 664 N ILE A 106 -5.112 -11.129 11.508 1.00 17.40

ATOM 665 CA ILE A 106 -5.181 -9.914 12.294 1.00 18.95

ATOM 666 CB ILE A 106 -6.613 -9.634 12.745 1.00 18.81

ATOM 667 CGl ILE A 106 -7.550 -9.671 11.531 1.00 17.98

ATOM 668 CDl ILE A 106 -9.034 -9.634 11.858 1.00 16.07

ATOM 669 CG2 ILE A 106 -6.680 -8.266 13.465 1.00 18.45

ATOM 670 C ILE A 106 -4.270 -10.011 13.521 1.00 19.33

ATOM 671 O ILE A 106 -4.372 -10.961 14.301 1.00 19.70

ATOM 672 N LEU A 107 -3.397 -9.015 13.687 1.00 20.92

ATOM 673 CA LEU A 107 -2.494 -8.944 14.841 1.00 23.40

ATOM 674 CB LEU A 107 -1.437 -7.856 14.634 1.00 23.33

ATOM 675 CG LEU A 107 -0.488 -7.591 15.813 1.00 21.94

ATOM 676 CDl LEU A 107 0.414 -8.783 16.063 1.00 25.97

ATOM 677 CD2 LEU A 107 0.321 -6.358 15.542 1.00 23.20 Table 4

ATOM 678 C LEO A 107 3.319 -8.651 16.095 00 26.45

ATOM 679 O LEU A 107 ^■4.081 -7.669 16.148 00 26.13

ATOM 680 N THR A 108 2.865 -9.266 17.184 00 30.36

ATOM 681 CA THR A 108 3.707 -8.947 18.295 00 34.67

ATOM 682 CB THR A 108 4.066 -10.342 18.851 00 34.43

ATOM 683 OGl THR A 108 ^■4.728 -11.110 17.837 00 36.69

ATOM 684 CG2 THR A 108 ^■4.975 -10.212 20.080 00 34.50

ATOM 685 C THR A 108 3.516 -7.703 19.469 00 36.99

ATOM 686 O THR A 108 4.139 -7.961 20.494 00 38.23

ATOM 687 N SER A 109 ^■2.784 -6.408 19.477 00 40.52

ATOM 68B CA SER A 109 ^■2.725 -5.240 20.551 00 41.97

ATOM 689 CB SER A 109 2.761 -5.882 21.946 00 42.94

ATOM 690 OG SER A 109 1.550 -5.659 22.654 00 45.53

ATOM 691 C SER A 109 ^■1.537 -4.198 20.308 00 42.49

ATOM 692 O SER A 109 0.392 -4.495 20.674 00 42.34

ATOM 693 N ASN A 110 ^■1.796 -3.032 19.653 00 42.45

ATOM 694 CA ASN A 110 ^■0.696 -2.118 19.256 00 42.74

ATOM 695 CB ASN A 110 ^■0.758 -1.917 17.748 00 43.36

ATOM 696 CG ASN A 110 ^■1.813 -0.894 17.315 00 45.94

ATOM 697 ODl ASN A 110 ■2.581 -0.404 18.152 1.00 49.43

ATOM 698 ND2 ASN A 110 -1 861 -0.582 16.034 00 49.07

ATOM 699 C ASN A 110 -0.560 -0.759 19.937 00 41.62

ATOM 700 O ASN A 110 -1.191 -0.461 20.940 00 42.71

ATOM 701 N THR A 111 0.279 0.037 19.299 00 40.26

ATOM 702 CA THR A 111 0.664 1.310 19.792 00 37.98

ATOM 703 CB THR A 111 1.300 1.161 21.189 00 38.01

ATOM 704 OGl THR A 111 0.371 1.645 22.168 00 36.44

ATOM 705 CG2 THR A 111 2.602 1.946 21.256 00 39.49

ATOM 706 C THR A 111 1.734 1.748 18.836 00 36.06

ATOM 707 O THR A 111 2.042 2.908 18.562 00 36.54

ATOM 708 N SER A 112 2.239 0.636 18.398 00 33.34

ATOM 709 CA SER A 112 3.341 0.488 17.610 00 30.52

ATOM 710 CB SER A 112 3.921 -0.907 17.905 00 31.73

ATOM 711 OG SER A 112 3.885 -1.183 19.299 00 31.56

ATOM 712 C SER A 112 3.195 0.762 16.152 1.00 28.44

ATOM 713 O SER A 112 2.160 0.912 15.525 00 29.04

ATOM 714 N GLN A 113 4.454 0.762 15.693 00 24.74

ATOM 715 CA GLN A 113 4.951 1.061 14.364 1.00 21.23

ATOM 716 CB GLN A 113 6.301 1.737 14.435 00 22.75

ATOM 111 CG GLN A 113 6.304 2. .982 15.303 00 27.47

ATOM 718 CD GLN A 113 7.688 3..590 15.415 00 31.39

ATOM 719 OEl GLN A 113 8.663 3..034 14.909 00 33.58

ATOM 720 NE2 GLN A 113 8.003 4.724 16.030 00 32.77

ATOM 721 C GLN A 113 5.039 -0.204 13.513 00 17.83

ATOM 722 O GLN A 113 5.602 -1.223 13.927 00 13.67

ATOM 723 N TYR A 114 4.452 -0.134 12.316 00 14.29

ATOM 724 CA TYR A 114 4.445 -1.287 11.409 00 12.78

ATOM 725 CB TYR A 114 3.087 -2.037 11.527 00 13.00

ATOM 726 CG TYR A 114 2.759 -2.488 12.942 00 16.17

ATOM 727 CDl TYR A 114 1.944 -1.752 13.802 00 18.80

ATOM 728 CEl TYR A 114 1.693 -2.189 15.110 1.00 22.67

ATOM 729 CZ TYR A 114 2.269 -3.372 15.561 00 23.78

ATOM 730 OH TYR A 114 2.039 -3. .825 16.835 00 27.05

ATOM 731 CE2 TYR A 114 3.077 -4..107 14.719 00 20.35

ATOM 732 CD2 TYR A 114 3.322 -3..662 13.427 00 20.92

ATOM 733 C TYR A 114 4.694 -0.795 10.004 00 11.26

ATOM 734 O TYR A 114 5.065 0.368 9.834 00 10.08

ATOM 735 N ASP A 115 4.482 .640 8.997 00 10.61

ATOM 736 CA ASP A 115 4.416 -1..160 7.610 00 9.98

ATOM 737 CB ASP A 115 4.798 -2.275 6.633 00 9.50

ATOM 738 CG ASP A 115 5.242 -2.732 6.784 00 12.27

ATOM 739 ODl ASP A 115 7.089 -1.987 7.348 00 10.89

ATOM 740 OD2 ASP A 115 6.536 -3.851 6.323 00 14.61

ATOM 741 C ASP A 115 2.988 -0.668 7.370 00 9.73

ATOM 742 O ASP A 115 2.199 -0.567 8.308 00 9.26

ATOM 743 N THR A 116 2.643 -0.332 6.130 00 10.14

ATOM 744 CA THR A 116 1.243 -0.069 5.812 00 9.75

ATOM 745 CB THR A 116 0.909 1.456 5.753 1.00 10.52 Table 4

ATOM 746 OGl THR A 116 -0.511 1.636 5.778 1.00 6.97

ATOM 747 CG2 THR A 116 1.488 2.110 4.519 1.00 6.98

ATOM 748 C THR A 116 0.816 -0.734 4.513 1.00 10.00

ATOM 749 O THR A 116 1.634 -0.971 3.626 1.00 10.12

ATOM 750 N TYR A 117 -0.476 -1.035 4.426 1.00 9.59

ATOM 751 CA TYR A 117 -1.101 -1.344 3.156 1.00 9.92

ATOM 752 CB TYR A 117 -2.052 -2.530 3.317 1.00 9.83

ATOM 753 CG TYR A 117 -1.273 -3.741 3.751 1.00 10.61

ATOM 754 CDl TYR A 117 -1.244 -4.148 5.078 1.00 8.39

ATOM 755 CEl TYR A 117 -0.476 -5.254 5.475 1.00 11.10

ATOM 756 CZ TYR A 117 0.280 -5.936 4.535 1.00 8.81

ATOM 757 OH TYR A 117 1.061 -7.025 4.874 1.00 9.27

ATOM 758 CE2 TYR A 117 0.268 -5.528 3.219 1.00 7.29

ATOM 759 CD2 TYR A 117 -0.491 -4.432 2.836 1.00 6.16

ATOM 760 C TYR A 117 -1.810 -0.107 2.669 1.00 9.96

ATOM 761 O TYR A 117 -2.211 0.734 3.468 1.00 10.04

ATOM 762 N CYS A 118 -1.921 0.019 1.350 1.00 9.73

ATOM 763 CA CYS A 118 -2.719 1.081 0.725 1.00 9.61

ATOM 764 CB CYS A 118 -1.819 2.189 0.161 1.00 9.65

ATOM 765 SG CYS A 118 -0.859 3.071 1.380 1.00 8.78

ATOM 766 C CYS A 118 -3.593 0.506 -0.380 1.00 9.52

ATOM 767 O CYS A 118 -3.332 -0.579 -0.894 1.00 9.62

ATOM 768 N PHE A 119 -4.647 1.236 -0.727 1.00 10.35

ATOM 769 CA PHE A 119 -5.587 0.787 -1.748 1.00 10.64

ATOM 770 CB PHE A 119 -6.910 0.338 -1.135 1.00 10.97

ATOM 111 CG PHE A 119 -7.997 0.161 -2.153 1.00 10.51

ATOM 772 CDl PHE A 119 -7.915 -0.862 -3.080 1.00 7.05

ATOM 773 CEl PHE A 119 -8.896 -1.036 -4.025 1.00 12.39

ATOM 774 CZ PHE A 119 -9.968 -0.166 -4.074 1.00 13.34

ATOM 775 CE2 PHE A 119 -10.061 0.868 -3.167 1.00 11.81

ATOM 776 CD2 PHE A 119 -9.076 1.032 -2.212 1.00 13.80

ATOM 777 C PHE A 119 -5.887 1.861 -2.778 1.00 11.82

ATOM 778 O PHE A 119 -6.417 2.921 -2.438 1.00 9.69

ATOM 779 N ASN A 120 -5.567 1.553 -4.036 1.00 11.77

ATOM 780 CA ASN A 120 -5.824 2.438 -5.166 1.00 14.44

ATOM 781 CB ASN A 120 -4.536 2.632 -5.958 1.00 15.22

ATOM 782 CG ASN A 120 -4.716 3.575 -7.130 1.00 17.70

ATOM 783 ODl ASN A 120 -5.808 4.075 -7.386 1.00 22.79

ATOM 784 ND2 ASN A 120 -3.643 3.806 -7.855 1.00 22.04

ATOM 785 C ASN A 120 -6.949 1.890 -6.075 1.00 15.21

ATOM 786 O ASN A 120 -6.744 0.960 -6.857 1.00 14.20

ATOM 787 N ALA A 121 -8.125 2.501 -5.975 1.00 16.52

ATOM 788 CA ALA A 121 -9.301 2.079 -6.749 1.00 19.46

ATOM 789 CB ALA A 121 -10.500 2.939 -6.386 1.00 19.76

ATOM 790 C ALA A 121 -9.074 2.091 -8.268 1.00 21.22

ATOM 791 O ALA A 121 -9.745 1.362 -8.995 1.00 21.75

ATOM 792 N SER A 122 -8.127 2.907 -8.732 1.00 22.90

ATOM 793 CA SER A 122 -7.838 3.071 -10.160 1.00 26.11

ATOM 794 CB SER A 122 -7.260 4.472 -10.421 1.00 26.78

ATOM 795 OG SER A 122 -8.243 5.454 -10.135 1.00 29.73

ATOM 796 C SER A 122 -6.912 2.023 -10.744 1.00 27.81

ATOM 797 O SER A 122 -6.694 2.010 -11.952 1.00 28.72

ATOM 798 N ALA A 123 -6.361 1.142 -9.920 1.00 29.38

ATOM 799 CA ALA A 123 -5.477 0.085 -10.434 1.00 30.05

ATOM 800 CB ALA A 123 -4.657 -0.528 -9.287 1.00 29.33

ATOM 801 C ALA A 123 -6.247 -1.006 -11.200 1.00 30.72

ATOM 802 O ALA A 123 -7.460 -1.085 -11.125 1.00 31.73

ATOM 803 N PRO A 124 -5.535 -1.843 -11.964 1.00 31.25

ATOM 804 CA PRO A 124 -6.190 -3.023 -12.556 1.00 31.59

ATOM 805 CB PRO A 124 -5.038 -3.739 -13.279 1.00 32.03

ATOM 806 CG PRO A 124 -4.043 -2.667 -13.564 1.00 31.85

ATOM 807 CD PRO A 124 -4.122 -1.734 -12.378 1.00 31.05

ATOM 808 C PRO A 124 -6.812 -3.947 -11.506 1.00 31.43

ATOM 809 O PRO A 124 -6.413 -3.905 -10.351 1.00 31.90

ATOM 810 N PRO A 125 -7.768 -4.799 -11.913 1.00 31.14

ATOM 811 CA PRO A 125 -8.488 -5.649 -10.959 1.00 30.43

ATOM 812 CB PRO A 125 -9.665 -6.189 -11.784 1.00 31.51

ATOM 813 CG PRO A 125 -9.175 -6.177 -13.205 1.00 31.39 Table 4

ATOM 814 CD PRO A 125 -8.231 -5.008 13.301 00 31.99

ATOM 815 C PRO A 125 -7.670 -6.801 10.382 00 29.69

ATOM 816 O PRO A 125 -8.014 -7.295 -9.308 00 31.63

ATOM 817 N GLO A 126 -6.616 -7.227 11.080 00 27.53

ATOM 818 CA GLϋ A 126 -5.807 -8.374 10.652 00 24.90

ATOM 819 CB GLU A 126 -5.763 -9.445 11.765 00 25.71

ATOM 820 CG GLU A 126 -7.014 -9.540 12.683 00 28.66

ATOM 821 CD GLO A 126 -8.297 -10.028 12.013 00 31.87

ATOM 822 OEl GLU A 126 -9.386 -9.814 12.599 00 33.52

ATOM 823 OE2 GLU A 126 -8.235 -10.655 10.936 00 31.05

ATOM 824 C GLO A 126 -4.389 -7.910 10.223 00 23.61

ATOM 825 O GLO A 126 -4.264 -6.896 -9.532 00 20.52

ATOM 826 N GLU A 127 -3.337 -8.645 10.597 00 21.91

ATOM 827 CA GLU A 127 -1.956 -8.253 10.306 1.00 21.29

ATOM 828 CB GLO A 127 -1.024 -9.450 10.468 00 20.23

ATOM 829 CG GLO A 127 0.425 -9.181 10.076 00 21.75

ATOM 830 CD GLU A 127 1.263 -10.433 10.159 00 23.42

ATOM 831 OEl GLU A 127 1.813 -10.873 -9.125 00 26.54

ATOM 832 OE2 GLU A 127 1.363 -10.986 -11.264 00 23.26

ATOM 833 C GLO A 127 -1.452 -7.139 -11.219 00 21.09

ATOM 834 O GLU A 127 -1.585 -7.234 -12.443 00 20.19

ATOM 835 N ASP A 128 -0.868 -6.102 -10.623 00 21.34

ATOM 836 CA ASP A 128 -0.180 -5.047 -11.370 00 21.49

ATOM 837 CB ASP A 128 -0.978 -3.736 -11.338 00 22.42

ATOM 838 CG ASP A 128 -0.343 -2.631 -12.180 1.00 24.13

ATOM 839 ODl ASP A 128 0.584 -2.891 -12.961 00 28.57

ATOM 840 OD2 ASP A 128 -0.778 -1. ,476 12.050 00 27.62

ATOM 841 C ASP A 128 1.227 -4, .843 10.794 00 20.96

ATOM 842 O ASP A 128 1.399 -4.238 -9.741 00 20.33

ATOM 843 N CYS A 129 2.218 -5.362 11.517 00 20.98

ATOM 844 CA CYS A 129 3.621 -5.272 11.139 00 20.22

ATOM 845 CB CYS A 129 4.296 -6.639 11.295 00 20.26

ATOM 846 SG CYS A 129 3.790 -7.831 10.065 00 21.84

ATOM 847 C CYS A 129 4.364 -4.233 11.962 00 20.11

ATOM 848 O CYS A 129 5.593 -4.243 11.993 00 19.56

ATOM 849 N THR A 130 3.639 -3.343 12.640 00 19.01

ATOM 850 CA THR A 130 4.302 -2.216 13.287 00 19.02

ATOM 851 CB THR A 130 3.413 -1.433 14.270 00 18.82

ATOM 852 OGl THR A 130 2.252 -0.929 13.599 00 19.17

ATOM 853 CG2 THR A 130 009 -2.321 15.450 00 19.02

ATOM 854 C THR A 130 842 -1.293 12.198 00 18.66

ATOM 855 O THR A 130 365 -1.305 11.063 00 19.08

ATOM 856 N SER A 131 861 -0.524 12.540 00 18.16

ATOM 857 CA SER A 131 6.487 0.350 11.575 00 18.97

ATOM 858 CB SER A 131 7.821 0.858 -12.099 00 19.62

ATOM 859 OG SER A 131 8.747 -0.216 -12.124 00 20.88

ATOM 860 C SER A 131 5.576 1.505 -11.203 00 18.61

ATOM 861 O SER A 131 4.837 2.031 -12.040 00 17.61

ATOM 862 N VAL A 132 5.624 .851 -9.918 00 18.42

ATOM 863 CA VAL A 132 5.027 .067 -9.391 00 19.32

ATOM 864 CB VAL A 132 4.736 .930 -7.881 00 19.37

ATOM 865 CGl VAL A 132 4.139 .218 -7.306 00 17.15

ATOM 866 CG2 VAL A 132 3.800 1.747 -7.636 1.00 19.69

ATOM 867 C VAL A 132 6.019 4.202 -9.664 1.00 19.64

ATOM 868 O VAL A 132 7.206 4.105 -9.329 1.00 19.29

ATOM 869 N THR A 133 5.511 5.256 10.301 1.00 20.22

ATOM 870 CA THR A 133 6.320 6.338 10.840 00 21.86

ATOM 871 CB THR A 133 6.041 6.540 12.359 00 21.41

ATOM 872 OGl THR A 133 4.687 .004 12.546 00 28.13

ATOM 873 CG2 THR A 133 6.257 .250 13.138 00 26.07

ATOM 874 C THR A 133 6.063 .689 10.167 00 21.06

ATOM 875 O THR A 133 6.642 .689 10.575 00 20.84

ATOM 876 N ASP A 134 5.179 .734 -9.174 00 20.40

ATOM 877 CA ASP A 134 4.851 .004 -8.528 00 19.84

ATOM 878 CB ASP A 134 3.962 .886 -9.437 00 20.07

ATOM 879 CG ASP A 134 3.912 11.381 -8.992 00 22.64

ATOM 880 ODl ASP A 134 4.765 11.848 -8.203 00 25.53

ATOM 881 0D2 ASP A 134 2.992 12.095 -9.452 1.00 28.40 Table 4

ATOM 8S2 C ASP A 134 4.180 8.802 -7.187 00 19.48

ATOM 883 O ASP A 134 3.681 7.717 -6.870 00 18.40

ATOM 884 N LEU A 135 4.257 9.862 -6.391 00 19.04

ATOM 885 CA LEO A 135 3.515 10.033 -5.167 00 19.97

ATOM 886 CB LEU A 135 4.518 10.295 -4.037 00 19.54

ATOM 887 CG LEU A 135 4.120 10.074 -2.583 00 19.25

ATOM 888 CDl LEU A 135 .830 8.622 -2.301 00 17.26

ATOM 889 CD2 LEU A 135 .222 10.566 -1.660 00 20.77

ATOM 890 C LEU A 135 .627 11.245 -5.498 00 19.49

ATOM 891 O LEU A 135 .980 12.383 -5.184 00 20.46

ATOM 892 N PRO A 136 .503 11.010 -6.220 00 20.00

ATOM 893 CA PRO A 136 0.728 12.086 -6.855 00 19.29

ATOM 894 CB PRO A 136 -0.412 11.338 -7 559 00 19.37

ATOM 895 CG PRO A 136 -0.486 10.024 6.898 00 19.83

ATOM 896 CD PRO A 136 0.900 9.692 6.491 00 19.74

ATOM 897 C PRO A 136 0.153 13.180 5.951 00 19.81

ATOM 898 O PRO A 136 0.070 14.341 6.381 00 19.07

ATOM 899 N ASN A 137 -0.256 12.825 4.730 00 19.80

ATOM 900 CA ASN A 137 -0.826 13.799 793 00 19.97

ATOM 901 CB ASN A 137 -2.035 13.211 058 00 20.01

ATOM 902 CG ASN A 137 -3.211 12.933 972 00 21.27

ATOM 903 ODl ASN A 137 -4.114 12.181 603 00 21.40

ATOM 904 ND2 ASN A 137 -3.215 13.540 5.158 00 21.59

ATOM 905 C ASN A 137 0.167 14.338 2.759 1.00 19.88

ATOM 906 O ASN A 137 -0.246 14.953 ^■1.778 00 18.18

ATOM 907 N ALA A 138 1.465 14.131 -2 975 00 19.50

ATOM 908 CA ALA A 138 2.471 14.677 -2.058 00 21.34

ATOM 909 CB ALA A 138 3.855 14.078 -2.311 00 21.92

ATOM 910 C ALA A 138 2.477 16.197 -2.224 1.00 21.74

ATOM 911 O ALA A 138 2.168 16.708 -3.312 .00 21.67

ATOM 912 N PHE A 139 2.790 16.911 -1.146 .00 21.15

ATOM 913 CA PHE A 139 782 18.375 -1.162 .00 20.28

ATOM 914 CB PHE A 139 832 18.963 -0.096 .00 19.36

ATOM 915 CG PHE A 139 006 18.405 1.288 .00 20.89

ATOM 916 CDl PHE A 139 892 18.988 2.184 .00 20.13

ATOM 917 CEl PHE A 139 026 18.485 3.472 .00 20.90

ATOM 918 CZ PHE A 139 257 17.389 3.374 .00 16.45

ATOM 919 CE2 PHE A 139 363 16.827 2.996 .00 19.15

ATOM 920 CD2 PHE A 139 231 17.338 1.717 .00 21.48

ATOM 921 C PHE A 139 183 18.961 -1.044 .00 20.08

ATOM 922 O PHE A 139 168 18.239 -0.887 .00 19.24

ATOM 923 N ASP A 140 4.269 20.281 -1.162 .00 20.17

ATOM 924 CA ASP A 140 5.549 20.972 -1.114 ,00 20.11

ATOM 925 CB ASP A 140 5.338 22.483 -1.218 .00 22.07

ATOM 926 CG ASP A 140 6.644 23.245 -1.334 .00 25.62

ATOM 927 ODl ASP A 140 7.258 23.524 -0.288 ,00 29.11

ATOM 928 OD2 ASP A 140 7.044 23.578 -2.467 .00 33.15

ATOM 929 C ASP A 140 6.286 20.610 0.175 ,00 19.06

ATOM 930 O ASP A 140 5.674 20.510 1.234 .00 18.95

ATOM 931 N GLY A 141 7.594 20.402 0.080 .00 18.10

ATOM 932 CA GLY A 141 8.373 19.997 1.241 ,00 17.64

ATOM 933 C GLY A 141 9.846 19.811 0.935 ,00 18.21

ATOM 934 O GLY A 141 10.240 19.852 -0.225 ,00 18.72

ATOM 935 N PRO A 142 10.668 19.598 1.977 ,00 17.56

ATOM 936 CA PRO A 142 12.125 19.560 1..839 ,00 17.61

ATOM 937 CB PRO A 142 12.594 20.084 3..197 ,00 17.72

ATOM 938 CG PRO A 142 11.565 19.545 4.164 .00 18.69

ATOM 939 CD PRO A 142 10.262 19.378 3.380 .00 17.65

ATOM 940 C PRO A 142 12.697 18.150 1.606 ,00 17.06

ATOM 941 O PRO A 142 13.881 18.014 1.294 ,00 15.94

ATOM 942 N ILE A 143 11.873 17.117 1.737 ,00 17.07

ATOM 943 CA ILE A 143 12.375 15.738 .730 ,00 15.98

ATOM 944 CB ILE A 143 11.434 14.791 .498 ,00 17.13

ATOM 945 CGl ILE A 143 12.094 13.424 .690 ,00 17.21

ATOM 946 CDl ILE A 143 11.345 12.512 .636 .00 17.06

ATOM 947 CG2 ILE A 143 10.106 14.654 1.771 .00 16.24

ATOM 948 C ILE A 143 12.524 15.215 0.299 ,00 15.65

ATOM 949 O ILE A 143 11.631 15.407 -0.517 1.00 14.34 Table 4

ATOM 950 N THR A 144 13.654 14.561 0.010 1.00 14.81

ATOM 951 CA THR A 144 13.784 13.738 -1.188 1.00 15.14

ATOM 952 CB THR A 144 15.264 13.482 -1.593 1.00 15.23

ATOM 953 OGl THR A 144 15.922 14.721 -1.856 1.00 14.01

ATOM 954 CG2 THR A 144 15.351 12.607 -2.845 1.00 15.25

ATOM 955 C THR A 144 13.095 12.409 -0.906 1.00 14.87

ATOM 956 O THR A 144 13.563 11.622 -0.071 1.00 14.91

ATOM 957 N ILE A 145 11.971 12.183 -1.584 1.00 14.90

ATOM 958 CA ILE A 145 11.171 10.983 -1.411 1.00 15.00

ATOM 959 CB ILE A 145 9.666 11.310 -1.276 1.00 16.47

ATOM 960 CGl ILE A 145 9.414 12.192 -0.049 1.00 15.60

ATOM 961 CDl ILE A 145 8.075 12.922 -0.084 1.00 16.94

ATOM 962 CG2 ILE A 145 8.850 10.028 -1.177 1.00 15.38

ATOM 963 C ILE A 145 11.377 10.087 -2.626 1.00 16.03

ATOM 964 O ILE A 145 11.144 10.503 -3.743 1.00 15.19

ATOM 965 N THR A 146 11.808 8.852 -2.398 1.00 15.89

ATOM 966 CA THR A 146 12.137 7.957 -3.488 1.00 17.05

ATOM 967 CB THR A 146 13.625 7.532 .-3.449 1.00 17.46

ATOM 968 OGl THR A 146 14.454 8.703 -3.406 1.00 20.95

ATOM 969 CG2 THR A 146 13.984 6.698 -4.679 1.00 19.23

ATOM 970 C THR A 146 11.254 6.734 -3.416 1.00 16.66

ATOM 971 O THR A 146 11.238 6.039 -2.409 1.00 15.64

ATOM 972 N ILE A 147 10.490 6.496 -4.476 1.00 16.43

ATOM 973 CA ILE A 147 9.718 5.274 -4.596 1.00 17.03

ATOM 974 CB ILE A 147 8.485 5.441 -5.513 1.00 17.21

ATOM 975 CGl ILE A 147 7.402 6.245 -4.792 1.00 20.48

ATOM 976 CDl ILE A 147 6.591 7.121 -5.710 1.00 25.10

ATOM 977 CG2 ILE A 147 7.931 4.080 -5.939 1.00 17.21

ATOM 978 C ILE A 147 10.649 4.225 -5.168 1.00 16.66

ATOM 979 O ILE A 147 11.252 4.433 -6.223 1.00 17.06

ATOM 980 N VAL A 148 10.761 3.108 -4.461 1.00 15.88

ATOM 981 CA VAL A 148 11.602 1.995 -4.881 1.00 15.59

ATOM 982 CB VAL A 148 12.653 1.615 -3.787 1.00 15.42

ATOM 983 CGl VAL A 148 13.624 0.577 -4.316 1.00 16.63

ATOM 984 CG2 VAL A 148 13.402 2.872 -3.297 1.00 16.69

ATOM 985 C VAL A 148 10.723 0.792 -5.187 1.00 15.85

ATOM 986 O VAL A 148 10.028 0.289 -4.313 1.00 15.02

ATOM 987 N ASN A 149 10.764 0.344 -6.436 1.00 15.62

ATOM 988 CA ASN A 149 10.024 -0.837 -6.866 1.00 16.93

ATOM 989 CB ASN A 149 9.605 -0.671 -8.330 1.00 16.45

ATOM 990 CG ASN A 149 8.628 0.490 -8.532 1.00 17.56

ATOM 991 ODl ASN A 149 7.416 0.362 -8.285 1.00 19.27

ATOM 992 ND2 ASN A 149 9.153 1.635 -8.965 1.00 13.90

ATOM 993 C ASN A 149 10.876 -2.099 -6.675 1.00 17.26

ATOM 994 O ASN A 149 12.113 -2.030 -6.611 1.00 16.77

ATOM 995 N ARG A 150 10.230 -3.253 -6.595 1.00 18.33

ATOM 996 CA ARG A 150 10.952 -4.511 -6.340 1.00 20.33

ATOM 997 CB ARG A 150 9.967 -5.681 -6.210 1.00 20.71

ATOM 998 CG ARG A 150 10.516 -6.867 -5.430 1.00 27.15

ATOM 999 CD ARG A 150 9.477 -7.975 -5.205 1.00 33.68

ATOM 1000 NE ARG A 150 10.136 -9.213 -4.762 1.00 39.26

ATOM 1001 CZ ARG A 150 9.585 -10.430 -4.759 1.00 43.44

ATOM 1002 NHl ARG A 150 8.335 -10.626 -5.186 1.00 44.17

ATOM 1003 NH2 ARG A 150 10.303 -11.469 -4.327 1.00 46.37

ATOM 1004 C ARG A 150 12.042 -4.825 -7.382 1.00 19.15

ATOM 1005 O ARG A 150 13.056 -5.453 -7.047 1.00 19.27

ATOM 1006 N ASP A 151 11.831 -4.384 -8.630 1.00 18.76

ATOM 1007 CA ASP A 151 12.797 -4.562 -9.728 1.00 18.94

ATOM 1008 CB ASP A 151 12.090 -4.548 -11.102 1.00 17.88

ATOM 1009 CG ASP A 151 11.485 -3.195 -11.459 1.00 19.44

ATOM 1010 ODl ASP A 151 11.652 -2.211 -10.707 1.00 15.14

ATOM 1011 OD2 ASP A 151 10.810 -3.122 -12.507 1.00 23.23

ATOM 1012 C ASP A 151 13.916 -3.520 -9.721 1.00 19.46

ATOM 1013 O ASP A 151 14.781 -3.526 -10.600 1.00 20.92

ATOM 1014 N GLY A 152 13.866 -2.619 -8.740 1.00 18.79

ATOM 1015 CA GLY A 152 14.907 -1.649 -8.505 1.00 19.77

ATOM 1016 C GLY A 152 14.659 -0.313 -9.163 1.00 20.72

ATOM 1017 O GLY A 152 15.400 0.627 -8.924 1.00 20.47 Table 4

ATOM 1018 N THR A 153 13.631 -0.215 10.001 00 20.79

ATOM 1019 CA THR A 153 13.344 1.052 10.654 00 22.73

ATOM 1020 CB THR A 153 12.279 0.938 11.755 00 22.14

ATOM 1021 OGl THR A 153 11.102 0.316 11.235 00 23.76

ATOM 1022 CG2 THR A 153 12.815 0.131 -12.929 00 24.51

ATOM 1023 C THR A 153 12.917 2.066 -9.613 00 22.39

ATOM 1024 O THR A 153 12.104 ^' 1.770 -8.736 00 22.71

ATOM 1025 N ARG A 154 13.485 3.259 -9.731 00 23.25

ATOM 1026 CA ARG A 154 13.316 4.328 -8.761 00 24.57

ATOM 1027 CB ARG A 154 14.671 4.685 -8.144 00 25.27

ATOM 1028 CG ARG A 154 15.049 3.794 -7.015 00 28.16

ATOM 1029 CD ARG A 154 16.466 4.040 -6.600 00 31.33

ATOM 1030 NE ARG A 154 16.705 3.454 -5.296 00 34.20

ATOM 1031 CZ ARG A 154 17.021 2.185 -5.074 00 33.58

ATOM 1032 NHl ARG A 154 17.178 1.313 -6.085 00 35.03

ATOM 1033 NH2 ARG A 154 17.202 1.792 -3.819 00 34.24

ATOM 1034 C ARG A 154 12.730 5.589 -9.350 00 24.74

ATOM 1035 O ARG A 154 13.056 5.972 -10.475 00 25.83

ATOM 1036 N TYR A 155 11.834 6.221 -8.593 00 23.60

ATOM 1037 CA TYR A 155 11.330 7.559 -8.918 00 23.04

ATOM 1038 CB TYR A 155 9.868 7.517 -9.383 00 22.17

ATOM 1039 CG TYR A 155 9.216 8.892 -9.401 00 22.86

ATOM 1040 CDl TYR A 155 9.332 9.725 -10.511 00 22.76

ATOM 1041 CEl TYR A 155 8.74B 10.987 -10.528 00 23.11

ATOM 1042 CZ TYR A 155 8.043 11.430 -9.426 00 25.50

ATOM 1043 OH TYR A 155 7.467 12.674 -9.442 1.00 26.93

ATOM 1044 CE2 TYR A 155 7.922 10.627 -8.305 00 23.74

ATOM 1045 CD2 TYR- A 155 8.504 9.365 -8.298 00 22.26

ATOM 1046 C TYR A 155 11.454 8.449 -7.686 00 22.76

ATOM 1047 O TYR A 155 10.967 8.096 -6.613 00 22.38

ATOM 1048 N VAL A 156 12.102 9.600 -7.857 00 21.87

ATOM 1049 CA VAL A 156 12.326 10.560 -6.774 00 22.22

ATOM 1050 CB VAL A 156 13.825 10.857 -6.585 00 22.58

ATOM 1051 CGl VAL A 156 14.024 11.946 -5.541 00 22.63

ATOM 1052 CG2 VAL A 156 14.574 9.592 -6.196 00 22.34

ATOM 1053 C VAL A 156 11.642 11.911 -7.014 00 22.30

ATOM 1054 O VAL A 156 11.497 12.370 -8.161 00 22.66

ATOM 1055 N GLN A 157 11.250 12.543 -5.911 00 22.14

ATOM 1056 CA GLN A 157 10.725 13.900 -5.918 00 22.18

ATOM 1057 CB GLN A 157 9.234 13.896 -6.260 00 22.62

ATOM 1058 CG GLN A 157 8.654 15.275 -6.526 00 23.46

ATOM 1059 CD GLN A 157 7.176 15.232 -6.861 00 27.53

ATOM 1060 OEl GLN A 157 6.569 14.161 -6.897 1.00 30.23

ATOM 1061 NE2 GLN A 157 6.400 16.273 -7.139 00 27.37

ATOM 1062 C GLN A 157 11.038 14.541 -4.578 00 22.13

ATOM 1063 O GLN A 157 11.198 13.839 -3.576 00 21.88

ATOM 1064 N LYS A 158 11.148 15.870 -4.581 00 21.21

ATOM 1065 CA LYS A 158 11.229 16.656 -3.358 00 21.05

ATOM 1066 CB LYS A 158 11.993 17.959 -3.589 00 21.23

ATOM 1067 CG LYS A 158 12.334 18.701 -2.295 00 26.02

ATOM 1068 CD LYS A 158 13.243 19.899 -2.522 00 29.29

ATOM 1069 CE LYS A 158 12.632 21.189 -1.977 00 31.28

ATOM 1070 NZ LYS A 158 11.368 21.540 -2.705 1.00 33.77

ATOM 1071 C LYS A 158 9.807 16.960 -2.894 00 19.45

ATOM 1072 O LYS A 158 8.956 17.376 -3.694 00 18.50

ATOM 1073 N GLY A 159 9.536 16.738 -1.611 00 17.48

ATOM 1074 CA GLY A 159 8.227 17.086 -1.067 00 16.97

ATOM 1075 C GLY Ά 159 8.016 16.676 0.372 00 16.07

ATOM 1076 O GLY A 159 8.973 16.550 1.141 00 15.51

ATOM 1077 N GLU R 160 6.747 16.487 0.721 00 15.06

ATOM 1078 CA GLU R 160 6.347 16.020 2.035 00 14.15

ATOM 1079 CB GLU R 160 6.323 17.193 3.027 00 14.56

ATOM 1080 CG GLU A 160 5.998 16.812 4.457 00 15.80

ATOM 1081 CD GLU A 160 6.929 15.746 4.986 00 19.21

ATOM 1082 OEl GLU A 160 8.019 16.104 5.453 00 20.61

ATOM 1083 OE2 GLU A 160 6.580 14.549 4.930 00 22.47

ATOM 1084 C GLU A 160 4.972 15.351 1.935 00 12.98

ATOM 1085 O GLU A 160 4.198 15.635 1.009 1.00 11.77 Table 4

ATOM 1086 N TYR A 161 4.696 14.428 2.854 1.00 13.19

ATOM 1087 CA TYR A 161 3.371 13.805 2.967 1.00 13.39

ATOM 1088 CB TYR A 161 3.384 12.402 2.332 1.00 12.96

ATOM 1089 CG TYR A 161 4.312 11.413 3.032 1.00 15.35

ATOM 1090 CDl TYR A 161 3.852 10.619 4.075 1.00 14.96

ATOM 1091 CEl TYR A 161 4.690 9.735 4.725 1.00 17.00

ATOM 1092 CZ TYR A 161 6.017 9.626 4.334 1.00 19.22

ATOM 1093 OH TYR A 161 6.842 8.739 4.979 1.00 23.31

ATOM 1094 CE2 TYR A 161 6.509 10.400 3.306 1.00 18.30

ATOM 1095 CD2 TYR A 161 5.654 11.293 2.656 1.00 18.46

ATOM 1096 C TYR A 161 2.853 13.743 4.415 1.00 12.68

ATOM 1097 O TYR A 161 1.669 13.542 4.632 1.00 12.40

ATOM 1098 N ARG A 162 3.735 13.922 5.396 1.00 13.42

ATOM 1099 CA ARG A 162 3.354 13.867 6.815 1.00 15.49

ATOM 1100 CB ARG A 162 4.580 13.561 7.692 1.00 14.78

ATOM 1101 CG ARG A 162 5.148 12.159 7.489 1.00 17.06

ATOM 1102 CD ARG A 162 6.600 12.010 7.977 1.00 14.95

ATOM 1103 NE ARG A 162 7.502 12.951 7.311 1.00 16.31

ATOM 1104 CZ ARG A 162 8.801 13.108 7.591 1.00 15.18

ATOM 1105 NHl ARG A 162 9.400 12.363 8.511 1.00 11.94

ATOM 1106 NH2 ARG A 162 9.516 14.018 6.928 1.00 17.56

ATOM 1107 C ARG A 162 2.664 15.165 7.265 1.00 16.19

ATOM 1108 O ARG A 162 3.218 16.261 7.131 1.00 17.46

ATOM 1109 N THR A 163 1.444 15.026 7.777 1.00 17.85

ATOM 1110 CA THR A 163 0.667 16.154 8.275 1.00 18.37

ATOM 1111 CB THR A 163 0.806 16.074 7.824 1.00 18.82

ATOM 1112 OGl THR A 163 1.471 15.003 8.503 1.00 24.27

ATOM 1113 CG2 THR A 163 0.903 15.872 6.313 1.00 16.72

ATOM 1114 C THR A 163 0.684 16.283 9.806 1.00 18.50

ATOM 1115 O THR A 163 0.193 17.285 10.341 1.00 18.09

ATOM 1116 N ASN A 164 1.221 15.289 10.511 1.00 18.21

ATOM 1117 CA ASN A 164 1.341 15.374 11.980 1.00 18.79

ATOM 1118 CB ASN A 164 0.770 14.116 12.638 1.00 18.37

ATOM 1119 CG ASN A 164 0.696 13.905 12.316 1.00 21.25

ATOM 1120 ODl ASN A 164 1.477 14.856 12.281 1.00 28.28

ATOM 1121 ND2 ASN A 164 1.075 12.654 12.080 1.00 20.26

ATOM 1122 C ASN A 164 2.792 15.585 12.404 1.00 19.31

ATOM 1123 O ASN A 164 3.666 14.783 12.079 1.00 20.18

ATOM 1124 N PRO A 165 3.028 16.677 13.127 1.00 19.39

ATOM 1125 CA PRO A 165 4.349 17.031 13.673 1.00 19.76

ATOM 1126 CB PRO A 165 4.031 18.192 14.617 1.00 20.02

ATOM 1127 CG PRO A 165 2.634 17.932 15.072 1.00 20.96

ATOM 1128 CD PRO A 165 1.964 17.184 13.954 1.00 19.67

ATOM 1129 C PRO A 165 5.048 15.859 14.360 1.00 19.33

ATOM 1130 O PRO A 165 6.226 15.601 14.107 1.00 18.33

ATOM 1131 N GLU A 166 4.309 15.141 15.201 1.00 19.04

ATOM 1132 CA GLU A 166 4.838 13.968 15.922 1.00 19.09

ATOM 1133 CB GLU A 166 3.744 13.311 16.771 l.oα 19.45

ATOM 1134 CG GLU A 166 3.101 14.250 17.800 1.00 22.63

ATOM 1135 CD GLU A 166 1.817 14.917 17.312 1.00 21.02

ATOM 1136 OEl GLU A 166 1.573 14.987 16.081 1.00 22.58

ATOM 1137 OE2 GLU A 166 1.050 15.383 18.182 1.00 18.18

ATOM 1138 C GLU A 166 5.457 12.905 15.013 1.00 18.78

ATOM 1139 O GLU A 166 6.365 12.190 15.431 1.00 17.26

ATOM 1140 N ASP A 167 4.959 12.786 13.785 1.00 19.08

ATOM 1141 CA ASP A 167 5.528 11.851 12.806 1.00 20.89

ATOM 1142 CB ASP A 167 4.492 11.502 11.717 1.00 19.77

ATOM 1143 CG ASP A 167 3.314 10.693 12.256 1.00 18.16

ATOM 1144 ODl ASP A 167 3.540 9.789 13.095 1.00 14.60

ATOM 1145 OD2 ASP A 167 2.160 10.964 11.833 1.00 15.55

ATOM 1146 C ASP A 167 6.803 12.391 12.156 1.00 22.86

ATOM 1147 O ASP A 167 7.560 11.634 11.554 1.00 21.85

ATOM 1148 N ILE A 168 7.036 13.694 12.272 1.00 25.92

ATOM 1149 CA ILE A 168 8.179 14.347 11.643 1.00 28.78

ATOM 1150 CB ILE A 168 7.787 15.704 11.030 1.00 28.25

ATOM 1151 CGl ILE A 168 6.706 15.515 9.964 1.00 26.09

ATOM 1152 CDl ILE A 168 6.092 16.811 9.481 1.00 25.83

ATOM 1153 CG2 ILE A 168 9.008 16.398 10.446 1.00 29.02 Table 4

ATOM 1154 C ILE A 168 9.281 14.506 12.688 1.00 32. 02 ATOM 1155 O ILE A 168 10 .201 13.693 12.772 1.00 32.71 ATOM 1156 N TYR A 169 7 . 903 14.973 14.361 1.00 34.94 ATOM 1157 CA TYR A 169 8 .813 15.063 15.490 1.00 37.76 ATOM 1158 CB TYR A 169 8 .246 15.961 16.597 1.00 38.80 ATOM 1159 CG TYR A 169 9. 154 16.068 17.821 1.00 43.82 ATOM 1160 CDl TYR A 169 9. 408 17.309 18.430 1.00 48.29 ATOM 1161 CEl TYR A 169 10.256 17.408 19.554 1.00 50.92 ATOM 1162 CZ TYR A 169 10.847 16.254 20.074 1.00 51.55 ATOM 1163 OH TYR A 169 11.675 16.336 21.184 1.00 53.28 ATOM 1164 CE2 TYR A 169 10 . 607 15.019 19.484 1.00 49.68 ATOM 1165 CD2 TYR A 169 9 .764 14.935 18.365 1.00 46, 86 ATOM 1166 C TYR A 169 9 . 029 13.657 16.035 1.00 38.14 ATOM 1167 O TYR A 169 10 . 067 13.044 15.809 1.00 39.07 ATOM 2464 Cl NAG C 1 1 .081 --15.286 19.558 1.00135.62 C ATOM 2466 Ol NAG C 1 .791 --15.753 20.856 .00154, 45 O ATOM 2468 C2 NAG C 1 2 . 587 --15.339 19.312 .00127.56 C ATOM 2470 N2 NAG C 1 3 . 313 --14.542 20.295 ,00132.35 N ATOM 2472 C7 NAG 1 4 . 230 --15.065 21.113 ,00142.33 C ATOM 2473 07 NAG 1 5.322 --15.492 20.734 ,00137.89 O ATOM 2474 C8 NAG 1 3 . 866 --15.105 22.566 .00161.53 C ATOM 2478 C3 NAG 1 2 . 914 --14.884 17.886 .00108.94 C ATOM 2480 03 NAG 1 4 . 280 --15.182 17.655 ,00102.59 O ATOM 2481 C4 NAG 1 2 . 027 --15.591 16.853 ,00106.12 C ATOM 2483 04 NAG 1 2 . 101 --14.946 15.597 1.00 92 63 O ATOM 2485 C5 NAG 1 . 558 --15.642 17.277 .00116 05 C ATOM 2487 C6 NAG 1 - . 231 --16.551 16.337 .00115 26 C ATOM 2490 06 NAG C 1 -1 . 572 --16.631 16.762 .00125 75 O ATOM 2492 05 NAG C 1 . 428 --16.107 18.609 .00132 62 O ATOM 2493 Cl GCO C 2 4 . 932 --14.245 16.778 1.00 87 39 C ATOM 2495 C2 GCD C 2 6 . 413 --14.184 17.144 1.00 87 62 C ATOM 2497 02 GCD C 2 6. 550 --13.438 18.332 1.00 94 52 O ATOM 2499 C3 GCO C 2 7 . 302 --13.533 16.084 1.00 75 68 C ATOM 2501 03 GCO C 2 8 . 615 --14.024 16.239 1.00 78 47 O ATOM 2503 C4 GCO C 2 6. 846 --13.753 14.643 1.00 66 42 C ATOM 2505 04 GCO C 2 7 . 347 --12.713 13.821 1.00 57 87 O ATOM 2506 C5 GCO C 2 5 . 330 --13.753 14.525 1.00 66 09 C ATOM 2508 C6 GCO C 2 4 . 896 --14.139 13.117 1.00 58 29 C ATOM 2509 O6A GCU C 2 5 . 123 --15.311 12.743 1.00 58 95 O ATOM 2510 O6B GCO C 2 4 . 344 --13.256 12.422 1.00 50 34 O ATOM 2511 05 GCO C 2 4 . 777 --14.658 15.447 1.00 77 80 O ATOM 2512 Cl NAG 3 8 . 439 --13.166 12.997 1.00 55 97 C ATOM 2514 C2 NAG 3 8 .732 --12.129 11.914 1.00 49 16 C ATOM 2516 N2 NAG 3 7 . 604 --11.986 11.005 1.00 44 25 N ATOM 2518 C7 NAG 3 6. 873 -10.887 10.897 1.00 41 24 C ATOM 2519 07 NAG 3 7 . 204 -9.794 11.339 1.00 40 73 O ATOM 2520 C8 NAG 3 5. 576 -11.042 10.162 1.00 39 62 C ATOM 2524 C3 NAG 3 9. 966 -12.539 11.110 1.00 50 33 C ATOM 2526 03 NAG 3 10.350 -11.480 10.261 1.00 48 02 O ATOM 2527 C4 NAG 3 11.136 -12.890 12.024 1.00 56 09 C ATOM 2529 04 NAG 3 12.200 -13.367 11.230 1.00 57 93 O ATOM 2531 C5 NAG 3 10.692 -13.925 13.051 1.00 61 92 C ATOM 2533 C6 NAG 3 11.797 -14.253 14.051 1.00 71 11 C ATOM 2536 06 NAG 3 11.828 -13.269 15.064 1.00 73 18 O ATOM 2538 05 NAG 3 9.596 -13.409 13.771 1.00 61 53 O ATOM 2539 Cl GCO 4 10.212 -11.802 8.863 1.00 47 28 C ATOM 2541 C2 GCO 4 10.375 -10.495 8.098 1.00 46 51 C ATOM 2543 02 GCO C 4 9.416 -9.583 8.570 1.00 43 70 O ATOM 2545 C3 GCO C 4 10.183 -10.714 6.608 1.00 47 50 C ATOM 2547 03 Gcσ c 4 10.568 -9.574 5.881 1.00 49 87 O ATOM 2549 C4 GCO C 4 11.016 -11.879 5.104 1.00 52 08 C ATOM 2551 04 GCO C 4 10.470 -12.221 4.858 1.00 55 22 O ATOM 2552 C5 GCO C 4 10.951 -13.093 7.025 1.00 52 07 C ATOM 2554 C6 GCU C 4 12.011 -14.090 6.580 1.00 58 09 C ATOM 2555 O6A GCO C 4 13.187 -13.876 6.947 1.00 62 38 O ATOM 2556 O6B GCO C 4 11.645 -15.050 5.859 1.00 59, 56 O ATOM 2557 05 GCO C 4 11.143 -12.753 8.391 1.00 51 56 O ATOM 2558 Cl NAG C 5 11.425 -12.321 3.784 1.00 63 78 C Table 4

ATOM 2560 C2 NAG C 5 10.732 -13.152 2.718 1.00 66, 39 C

ATOM 2562 N2 NAG C 5 10.390 -14.459 3.250 1.00 65, 18 N

ATOM 2564 C7 NAG C 5 9.133 -14.897 3.243 1.00 62, 45 C

ATOM 2565 07 NAG C 5 8.250 -14.414 2.535 1.00 62, 04 O

ATOM 2566 C8 NAG C 5 8.817 -16.045 4.153 1.00 62, 16 C

ATOM 2570 C3 NAG C 5 11.544 -13.291 1.435 1.00 76, 07 C

ATOM 2572 03 NAG C 5 10.686 -13.815 .443 1.00 79, 41 O

ATOM 2573 C4 NAG C 5 12.086 -11.941 .981 1.00 79, 94 C

ATOM 2575 04 NAG C 5 13.019 -12.139 -.058 1.00 90, 01 O

ATOM 2577 C5 NAG C 5 12.734 -11.215 2.161 1.00 76, 79 C

ATOM 2579 C6 NAG C 5 13.243 -9.832 1.768 1.00 82, 23 C

ATOM 2582 06 NAG C 5 12.180 -9.025 1.319 1. .0000 8 800, 32 O

ATOM 2584 05 NAG C 5 11.800 -11.082 3.222 1..0000 6 677, 58 O

ATOM 2585 Cl GCO C 6 11.233 -14.971 -.209 1.00 87, 32 C

ATOM 2587 C2 GCO C 6 10.067 -15.710 -.858 1.00 87, 39 C

ATOM 2589 02 GCO C 6 9.343 -16.347 .173 1.00 80, 53 O

ATOM 2591 C3 GCϋ C 6 10.490 -16.757 -1 892 1.00 96.39 C

ATOM 2593 03 GCO C 6 9.397 -17.025 -2.742 1.00 97, 43 O

ATOM 2595 C4 GCO C 6 11.686 -16.324 -2.738 1.00107, 28 C

ATOM 2597 04 GCO C 6 12.244 -17.472 -3.342 1.00116, 45 O

ATOM 2598 C5 GCU C 6 12.758 -15.658 -1.873 1.00106, 31 C

ATOM 2600 C6 GCU C 6 13.954 -15.133 -2.667 1.00118, 55 C

ATOM 2601 O6A GCO C 6 15.077 -15.184 -2.117 1.00121, 69 O

ATOM 2602 O6B GCO C 6 13.760 -14.669 812 1.00126.42 O

ATOM 2603 05 GCU C 6 12.196 -14.580 159 1.00 97.91 O

ATOM 2604 Cl NAG C 7 11.829 -17.695 701 1.00125, 82 C

ATOM 2606 C2 NAG C 7 12.922 -18.521 371 1.00138, 92 C

ATOM 2608 N2 NAG C 7 14.209 -17.858 -5.241 1.00145 43 N

ATOM 2610 C7 NAG C 7 15.244 -18.460 -4.663 ,00148 83 C

ATOM 2611 07 NAG C 7 16.251 -18.786 -5.287 00162 74 O

ATOM 2612 C8 NAG C 7 15.136 -18.739 -3.193 00137 24 C

ATOM 2616 C3 NAG C 7 12.573 -18.794 -6.830 1.00150 37 C

ATOM 2618 03 NAG C 7 13.549 -19.630 -7.420 .00162 95 O

ATOM 2620 C4 NAG C 7 11.198 -19.453 -6.895 ,00144 09 C

ATOM 2622 04 NAG C 7 10.790 -19.571 -8.240 ,00154 93 O

ATOM 2624 C5 NAG C 7 10.162 -18.649 -6.105 1.00131 29 C

ATOM 2626 C6 NAG C 7 8.834 -19.403 -6.054 00126 61 C

ATOM 2629 06 NAG C 7 7.914 -18.726 -5.224 00116 33 O

ATOM 2631 05 NAG C 7 10.605 -18.392 -4.782 1.00121 61 O

END

TABLE 5

CRYSTl 1.000 1.000 1.000 90.00 90.00 90.00 P l 1

ATOM 1 N GLU 29 11.873 7.599 27.751 1.00 50.00

ATOM 2 CA GLU 29 11.996 7.198 26.331 1.00 50.00

ATOM 3 C GLU 29 10.748 6.487 25.838 1.00 50.00

ATOM 4 O GLU 29 10.006 6.065 26.722 1.00 50.00

ATOM 5 CB GLU 29 13.155 6.221 26.164 1.00 50.00

ATOM 6 CG GLU 29 14.494 6.936 26.334 1.00 50.00

ATOM 7 CD GLU 29 14.713 7.956 25.214 1.00 50.00

ATOM 8 OEl GLU 29 14.227 9.097 25.379 1.00 50.00

ATOM 9 OE2 GLϋ 29 15.307 7.547 24.196 1.00 50.00

ATOM 10 N LEU 30 10.392 6.734 24.576 1.00 50.00

ATOM 11 CA LEU 30 9.259 6.080 23.893 1.00 50.00

ATOM 12 C LEU 30 9.657 5.736 22.457 1.00 50.00

ATOM 13 O LEU 30 10.089 6.611 21.710 1.00 50.00

ATOM 14 CB LEU 30 8.008 6.972 23.892 1.00 50.00

ATOM 15 CG LEU 30 7.339 7.117 25.274 1.00 50.00

ATOM 16 CDl LEU 30 8.115 7.930 26.302 1.00 50.00

ATOM 17 CD2 LEU 30 6.092 7.973 25.157 1.00 50.00

ATOM 18 N SER 31 9.455 4.478 22.090 1.00 50.00

ATOM 19 CA SER 31 9.797 4.004 20.735 1.00 50.00

ATOM 20 C SER 31 8.523 3.716 19.964 1.00 50.00

ATOM 21 O SER 31 7.697 3.007 20.469 1.00 50.00

ATOM 22 CB SER 31 10.609 2.710 20.796 1.00 50.00

ATOM 23 OG SER 31 11.860 2.961 21.436 1.00 50.00

ATOM 24 N ILE 32 8.430 4.180 18.733 1.00 50.00

ATOM 25 CA ILE 32 7.228 4.005 17.891 1.00 50.00

ATOM 26 C ILE 32 7.608 3.365 16.542 1.00 50.00

ATOM 27 O ILE 32 8.262 3.954 15.684 1.00 50.00

ATOM 28 CB ILE 32 6.479 5.346 17.680 1.00 50.00

ATOM 29 CGl ILE 32 7.131 6.304 16.661 1.00 50.00

ATOM 30 CG2 ILE 32 6.277 6.101 19.005 1.00 50.00

ATOM 31 CDl ILE 32 8.571 6.727 17.006 1.00 50.00

ATOM 32 N GLN 33 7.369 2.077 16.425 1.00 50.00

ATOM 33 CA GLN 33 7.508 1.372 15.145 1.00 50.00

ATOM 34 C GLN 33 6.281 1.608 14.267 1.00 50.00

ATOM 35 O GLN 33 5.166 1.250 14.649 1.00 50.00

ATOM 36 CB GLN 33 7.697 -0.122 15.401 1.00 50.00

ATOM 37 CG GLN 33 9.069 -0.413 16.017 1.00 50.00

ATOM 38 CD GLN 33 10.220 -0.023 15.081 1.00 50.00

ATOM 39 OEl GLN 33 10.042 0.390 13.942 1.00 50.00

ATOM 40 NE2 GLN 33 11.431 -0.157 15.585 1.00 50.00

ATOM 41 N VAL 34 6.521 2.203 13.108 1.00 50.00

ATOM 42 CA VAL 34 5.441 2.561 12.170 1.00 50.00

ATOM 43 C VAL 34 5.555 1.761 10.866 1.00 50.00

ATOM 44 O VAL 34 6.651 1.483 10.380 1.00 50.00

ATOM 45 CB VAL 34 5.468 4.069 11.879 1.00 50.00

ATOM 46 CGl VAL 34 5.208 4.882 13.152 1.00 50.00

ATOM 47 CG2 VAL 34 6.799 4.488 11.251 1.00 50.00

ATOM 48 N SER 35 4.396 1.485 10.292 1.00 50.00

ATOM 49 CA SER 35 4.280 0.756 9.017 1.00 50.00

ATOM 50 C SER 35 3.946 1.746 7.896 1.00 50.00

ATOM 51 O SER 35 3.496 2.865 8.155 1.00 50.00

ATOM 52 CB SER 35 3.145 -0.264 9.130 1.00 50.00

ATOM 53 OG SER 35 1.905 0.417 9.345 1.00 50.00

ATOM 54 N CYS 36 4.197 1.328 6.657 1.00 50.00

ATOM 55 CA CYS 36 3.751 2.108 5.487 1.00 50.00

ATOM 56 C CYS 36 2.231 2.299 5.575 1.00 50.00

ATOM 57 O CYS 36 1.527 1.505 6.205 1.00 50.00

ATOM 58 CB CYS 36 4.044 1.378 4.176 1.00 50.00

ATOM 59 SG CYS 36 5.790 0.909 3.911 1.00 50.00

ATOM 60 N ARG 37 1.760 3.380 4.973 1.00 50.00

ATOM 61 CA ARG 37 0.318 3.618 4.868 1.00 50.00

ATOM 62 C ARG 37 -0.293 2.829 3.723 1.00 50.00

ATOM 63 O ARG 37 0.231 2.816 2.612 1.00 50.00 Table 5

ATOM 64 CB ARG 37 0.010 5.089 4.655 1.00 50.00

ATOM 65 CG ARG 37 0.216 6.044 5.838 1.00 50.00

ATOM 66 CD ARG 37 1.546 6.788 5.881 1.00 50.00

ATOM 67 NE ARG 37 2.633 5.957 6.397 1.00 50.00

ATOM 68 CZ ARG 37 3.909 6.123 6.087 1.00 50.00

ATOM 69 NHl ARG 37 4.271 7.057 5.246 1.00 50.00

ATOM 70 NH2 ARG 37 4.853 5.417 6.673 1.00 50.00

ATOM 71 N ILE 38 -1.446 2.258 4.002 1.00 50.00

ATOM 72 CA ILE 38 -2.237 1.547 2.996 1.00 50.00

ATOM 73 C ILE 38 -3.633 2.149 2.918 1.00 50.00

ATOM 74 O HE 38 -4.455 1.963 3.808 1.00 50.00

ATOM 75 CB ILE 38 -2.289 0.033 3.258 1.00 50.00

ATOM 76 CGl ILE 38 -3.316 -0.673 2.382 1.00 50.00

ATOM 77 CG2 ILE 38 -2.547 -0.204 4.721 1.00 50.00

ATOM 78 CDl ILE 38 -3.004 -0.371 0.926 1.00 50.00

ATOM 79 N MET 39 -3.843 2.911 1.854 1.00 50.00

ATOM 80 CA MET 39 -5.103 3.650 1.660 1.00 50.00

ATOM 81 C MET 39 -5.372 4.533 2.891 1.00 50.00

ATOM 82 O MET 39 -6.476 4.607 3.395 1.00 50.00

ATOM 83 CB MET 39 -6.260 2.675 1.376 1.00 50.00

ATOM 84 CG MET 39 -7.545 3.462 1.121 1.00 50.00

ATOM 85 SD MET 39 -8.915 2.461 0.500 1.00 50.00

ATOM 86 CE MET 39 -10.259 3.621 0.650 1.00 50.00

ATOM 87 N GLY 40 -4.291 5.028 3.492 1.00 50.00

ATOM 88 CA GLY 40 -4.386 5.930 4.653 1.00 50.00

ATOM 89 C GLY 40 -4.103 5.243 5.988 1.00 50.00

ATOM 90 O GLY 40 -3.725 5.892 6.957 1.00 50.00

ATOM 91 N ILE 41 -4.300 3.939 6.017 1.00 50.00

ATOM 92 CA ILE 41 -4.233 3.169 7.262 1.00 50.00

ATOM 93 C ILE 41 -2.767 2.789 7.522 1.00 50.00

ATOM 94 O ILE 41 -2.060 2.387 6.600 1.00 50.00

ATOM 95 CB ILE 41 -5.207 1.973 7.179 1.00 50.00

ATOM 96 CGl ILE 41 -4.504 0.648 7.045 1.00 50.00

ATOM 97 CG2 ILE 41 -6.298 2.098 6.111 1.00 50.00

ATOM 98 CDl ILE 41 -4.160 0.230 8.440 1.00 50.00

ATOM 99 N THR 42 -2.429 2.713 8.800 1.00 50.00

ATOM 100 CA THR 42 -1.104 2.253 9.259 1.00 50.00

ATOM 101 C THR 42 -1.212 1.690 10.663 1.00 50.00

ATOM 102 O THR 42 -2.177 1.947 11.380 1.00 50.00

ATOM 103 CB THR 42 -0.081 3.374 9.359 1.00 50.00

ATOM 104 OGl THR 42 -0.499 4.419 10.229 1.00 50.00

ATOM 105 CG2 THR 42 0.121 3.946 8.013 1.00 50.00

ATOM 106 N LEϋ 43 -0.211 0.904 11.010 1.00 50.00

ATOM 107 CA LEO 43 -0.105 0.345 12.355 1.00 50.00

ATOM 108 C LEO 43 1.041 1.064 13.072 1.00 50.00

ATOM 109 O LEU 43 2.130 1.213 12.517 1.00 50.00

ATOM 110 CB LED 43 0.158 -1.163 12.241 1.00 50.00

ATOM 111 CG LEU 43 0.245 -1.919 13.584 1.00 50.00

ATOM 112 CDl LEO 43 1.442 -1.573 14.467 1.00 50.00

ATOM 113 CD2 LEϋ 43 -1.012 -1.780 14.429 1.00 50.00

ATOM 114 N VAL 44 0.824 1.271 14.370 1.00 50.00

ATOM 115 CA VAL 44 1.878 1.781 15.266 1.00 50.00

ATOM 116 C VAL 44 2.063 0.862 16.485 1.00 50.00

ATOM 117 O VAL 44 1.101 0.492 17.160 1.00 50.00

ATOM 118 CB VAL 44 1.493 3.191 15.710 1.00 50.00

ATOM 119 CGl VAL 44 2.584 3.800 16.595 1.00 50.00

ATOM 120 CG2 VAL 44 1.238 4.096 14.499 1.00 50.00

ATOM 121 N SER 45 3.322 0.540 16.739 1.00 50.00

ATOM 122 CA SER 45 3.697 -0.268 17.901 1.00 50.00

ATOM 123 C SER 45 4.760 0.538 18.614 1.00 50.00

ATOM 124 O SER 45 5.548 1.309 18.172 1.00 50.00

ATOM 125 CB SER 45 4.290 -1.610 17.476 1.00 50.00

ATOM 126 OG SER 45 4.636 -2.379 18.635 1.00 50.00

ATOM 127 N LYS 46 4.794 0.266 19.908 1.00 50.00

ATOM 128 CA LYS 46 5.711 1.006 20.797 1.00 50.00

ATOM 129 C LYS 46 5.444 0.423 21.999 1.00 50.00

ATOM 130 O LYS 46 4.047 0.406 21.940 1.00 50.00

ATOM 131 CB LYS 46 5.318 2.430 21.402 1.00 50.00 Table 5

ATOM 132 CG LYS 46 4.239 2.838 22.448 00 50.00

ATOM 133 CD LYS 46 4.784 3.350 23.768 00 50.00

ATOM 134 CE LYS 46 3.644 3.441 24.760 00 50.00

ATOM 135 NZ LYS 46 4.132 4.323 25.813 00 50.00

ATOM 136 N LYS 47 6.419 0.031 22.888 00 50.00

ATOM 137 CA LYS 47 7.826 026 22.629 00 50.00

ATOM 138 C LYS 47 8.365 466 22.476 00 50.00

ATOM 139 O LYS 47 8.944 041 23.393 00 50.00

ATOM 140 CB LYS 47 8.553 650 23.809 00 50.00

ATOM 141 CG LYS 47 7.879 975 24.156 00 50.00

ATOM 142 CD LYS 47 8.474 648 25.383 00 50.00

ATOM 143 CE LYS 47 9.914 049 25.089 00 50.00

ATOM 144 NZ LYS 47 10.463 720 26.257 00 50.00

ATOM 145 N ALA 48 8.029 024 21.306 00 50.00

ATOM 146 CA ALA 48 8.327 430 20.946 00 50.00

ATOM 147 C ALA 48 7.342 423 21.583 00 50.00

ATOM 148 O ALA 48 7.441 624 21.353 00 50.00

ATOM 149 CB ALA 48 9.771 828 21.316 00 50.00

ATOM 150 N ASN 49 6.370 912 22.343 00 50.00

ATOM 151 CA ASN 49 5.388 782 23.018 00 50.00

ATOM 152 C ASN 49 3.959 -4.228 22.872 1.00 50.00

ATOM 153 O ASN 49 3.690 3.467 21.968 1.00 50.00

ATOM 154 CB ASN 49 5.822 -4 997 24.471 1.00 50.00

ATOM 155 CG ASN 49 7.147 5.762 24.513 00 50.00

ATOM 156 ODl ASN 49 7.321 6.807 23.903 00 50.00

ATOM 157 ND2 ASN 49 8.074 -5.220 25.275 00 50.00

ATOM 158 N GLN 50 2.982 -4.858 23.512 00 50.00

ATOM 159 CA GLN 50 1.638 -4.272 23.752 00 50.00

ATOM 160 C GLN 50 1.619 -3.356 24.987 00 50.00

ATOM 161 O GLN 50 2.140 -3.746 26.033 1.00 50.00

ATOM 162 CB GLN 50 0.672 -5.404 24.078 .00 50.00

ATOM 163 CG GLN 50 0.472 6.391 22.921 .00 50.00

ATOM 164 CD GLN 50 -0.225 5.751 21.729 .00 50.00

ATOM 165 OEl GLN 50 -0.392 4.574 21.706 .00 50.00

ATOM 166 NE2 GLN 50 -0.438 6.429 20.636 .00 50.00

ATOM 167 N GLN 51 1.229 2.085 24.803 .00 50.00

ATOM 168 CA GLN 51 1.449 1.035 25.848 .00 50.00

ATOM 169 C GLN 51 0.666 0.239 25.547 1.00 50.00

ATOM 170 O GLN 51 0.926 1.301 26.109 1.00 50.00

ATOM 171 CB GLN 51 2.912 0.597 26.152 00 50.00

ATOM 172 CG GLN 51 3.668 0.098 24.928 00 50.00

ATOM 173 CD GLN 51 3.697 -1. .310 24.014 00 50.00

ATOM 174 OEl GLN 51 3.796 -2..359 24.503 00 50.00

ATOM 175 NE2 GLN 51 4.539 -1.703 23.427 00 50.00

ATOM 176 N LEO 52 -0.356 0.087 24.715 00 50.00

ATOM 177 CA LEU 52 -1.107 1.246 24.213 00 50.00

ATOM 178 C LEU 52 -2.561 .027 24.580 00 50.00

ATOM 179 O LED 52 -3.202 .072 24.146 00 50.00

ATOM 180 CB LEU 52 -0.978 .429 22.691 00 50.00

ATOM 181 CG LEU 52 0.465 .659 22.220 00 50.00

ATOM 182 CDl LEU 52 1.345 0.445 22.446 00 50.00

ATOM 183 CD2 LEU 52 0.520 880 20.715 00 50.00

ATOM 184 N ASN 53 -2.993 817 25.547 00 50.00

ATOM 185 CA ASN 53 -4.412 808 25.954 00 50.00

ATOM 186 C ASN 53 -5.246 534 24.884 00 50.00

ATOM 187 O ASN 53 -4.701 3.206 24.004 00 50.00

ATOM 188 CB ASN 53 -4.537 2.494 27.321 00 50.00

ATOM 189 CG ASN 53 -4.198 3.963 27.305 00 50.00

ATOM 190 ODl ASN 53 -4.403 4.726 28.219 00 50.00

ATOM 191 ND2 ASN 53 -3.557 4.309 26.248 00 50.00

ATOM 192 N PHE 54 -6.559 2.470 25.039 00 50.00

ATOM 193 CA PHE 54 -7.474 3.110 24.079 00 50.00

ATOM 194 C PHE 54 -7.265 4.628 24.047 00 50.00

ATOM 195 O PHE 54 -7.106 5.232 22.988 00 50.00

ATOM 196 CB PHE 54 -8.922 2.793 24.452 00 50.00

ATOM 197 CG PHE 54 -9.886 3.487 23.488 00 50.00

ATOM 198 CDl PHE 54 -10.190 2.888 22.273 00 50.00

ATOM 199 CD2 PHE 54 -10.424 4.728 23.812 1.00 50.00 Table 5

ATOM 200 CEl PHE 54 -11.042 3.527 21.382 1.00 50.00

ATOM 201 CE2 PHE 54 -11.274 5.366 22.919 1.00 50.00

ATOM 202 CZ PHE 54 -11.586 4.764 21.705 1.00 50.00

ATOM 203 N THR 55 -7.194 5.208 25.240 1.00 50.00

ATOM 204 CA THR 55 -7.012 6.665 25.387 1.00 50.00

ATOM 205 C THR 55 -5.676 7.130 24.794 1.00 50.00

ATOM 206 O THR 55 -5.633 8.118 24.066 1.00 50.00

ATOM 207 CB THR 55 -7.092 7.104 26.852 1.00 50.00

ATOM 208 OGl THR 55 -6.026 6.487 27.543 1.00 50.00

ATOM 209 CG2 THR 55 -8.416 6.706 27.503 1.00 50.00

ATOM 210 N GLU 56 -4.611 6.355 25.006 1.00 50.00

ATOM 211 CA GLO 56 -3.297 6.756 24.447 1.00 50.00

ATOM 212 C GLU 56 -3.261 6.498 22.951 1.00 50.00

ATOM 213 O GLO 56 -2.543 7.195 22.248 1.00 50.00

ATOM 214 CB GLU 56 -2.071 6.091 25.056 1.00 50.00

ATOM 215 CG GLU 56 -0.682 6.524 24.703 1.00 50.00

ATOM 216 CD GLO 56 0.350 5.776 25.542 1.00 50.00

ATOM 217 OEl GLU 56 0.049 5.322 26.676 1.00 50.00

ATOM 218 OE2 GLU 56 1.465 5.736 25.002 1.00 50.00

ATOM 219 N ALA 57 -4.067 5.545 22.495 1.00 50.00

ATOM 220 CA ALA 57 -4.195 5.248 21.061 1.00 50.00

ATOM 221 C ALA 57 -4.772 6.451 20.306 1.00 50.00

ATOM 222 O ALA 57 -4.183 6.918 19.332 1.00 50.00

ATOM 223 CB ALA 57 -5.112 4.042 20.863 1.00 50.00

ATOM 224 N LYS 58 -5.859 7.006 20.847 1.00 50.00

ATOM 225 CA LYS 58 -6.503 8.202 20.273 1.00 50.00

ATOM 226 C LYS 58 -5.531 9.392 20.290 1.00 50.00

ATOM 227 O LYS 58 -5.451 10.148 19.324 1.00 50.00

ATOM 228 CB LYS 58 -7.766 8.534 21.071 1.00 50.00

ATOM 229 CG LYS 58 -8.521 9.737 20.496 1.00 50.00

ATOM 230 CD LYS 58 -9.752 10.050 21.348 1.00 50.00

ATOM 231 CE LYS 58 -10.461 11.337 20.912 1.00 50.00

ATOM 232 NZ LYS 58 -11.129 11.216 19.606 1.00 50.00

ATOM 233 N GLU 59 -4.723 9.451 21.347 1.00 50.00

ATOM 234 CA GLU 59 -3.704 10.502 21.497 1.00 50.00

ATOM 235 C GLO 59 -2.594 10.354 20.453 1.00 50.00

ATOM 236 O GLO 59 -2.132 11.335 19.875 1.00 50.00

ATOM 237 CB GLU 59 -3.090 10.443 22.897 1.00 50.00

ATOM 238 CG GLU 59 -4.075 10.897 23.977 1.00 50.00

ATOM 239 CD GLU 59 -4.395 12.387 23.838 1.00 50.00

ATOM 240 OEl GLU 59 -5.340 12.698 23.081 1.00 50.00

ATOM 241 OE2 GLU 59 -3.674 13.174 24.487 1.00 50.00

ATOM 242 N ALA 60 -2.257 9.099 20.172 1.00 50.00

ATOM 243 CA ALA 60 -1.164 8.748 19.255 1.00 50.00

ATOM 244 C ALA 60 -1.515 9.074 17.802 1.00 50.00

ATOM 245 O ALA 60 -0.722 9.699 17.101 1.00 50.00

ATOM 246 CB ALA 60 -0.834 7.260 19.383 1.00 50.00

ATOM 247 N CYS 61 -2.737 8.726 17.397 1.00 50.00

ATOM 248 CA CYS 61 -3.177 8.990 16.017 1.00 50.00

ATOM 249 C CYS 61 -3.320 10.495 15.795 1.00 50.00

ATOM 250 O CYS 61 -2.853 11.014 14.788 1.00 50.00

ATOM 251 CB CYS 61 -4.507 8.309 15.697 1.00 50.00

ATOM 252 SG CYS 61 -4.464 6.480 15.725 1.00 50.00

ATOM 253 N ARG 62 -3.835 11.185 16.811 1.00 50.00

ATOM 254 CA ARG 62 -3.983 12.650 16.775 1.00 50.00

ATOM 255 C ARG 62 -2.618 13.334 16.620 1.00 50.00

ATOM 256 O ARG 62 -2.483 14.270 15.834 1.00 50.00

ATOM 257 CB ARG 62 -4.668 13.137 18.052 1.00 50.00

ATOM 258 CG ARG 62 -5.020 14.622 17.948 1.00 50.00

ATOM 259 CD ARG 62 -5.714 15.108 19.216 1.00 50.00

ATOM 260 NE ARG 62 -6.104 16.520 19.058 1.00 50.00

ATOM 261 CZ ARG 62 -7.278 17.045 19.423 1.00 50.00

ATOM 262 NHl ARG 62 -8.218 16.290 19.987 1.00 50.00

ATOM 263 NH2 ARG 62 -7.523 18.336 19.219 1.00 50.00

ATOM 264 N LEU 63 -1.611 12.803 17.311 1.00 50.00

ATOM 265 CA LEU 63 -0.231 13.288 17.150 1.00 50.00

ATOM 266 C LEU 63 0.344 13.047 15.762 1.00 50.00

ATOM 267 O LEU 63 1.302 13.686 15.333 1.00 50.00 Table 5

ATOM 268 CB LEU 63 0.724 12.726 18.203 1.00 50.00

ATOM 269 CG LEO 63 0.775 13.628 19.441 1.00 50.00

ATOM 270 CDl LEU 63 1.843 13.116 20.408 1.00 50.00

ATOM 271 CD2 LEU 63 1.067 15.088 19.068 1.00 50.00

ATOM 272 N LEU 64 -0.248 12.069 15.101 1.00 50.00

ATOM 273 CA LEU 64 0.108 11.796 13.728 1.00 50.00

ATOM 274 C LEU 64 -0.877 12.437 12.787 1.00 50.00

ATOM 275 O LEU 64 -0.500 12.406 11.643 1.00 50.00

ATOM 276 CB LEU 64 0.231 10.294 13.460 1.00 50.00

ATOM 277 CG LEU 64 1.340 9.677 14.318 1.00 50.00

ATOM 278 CDl LED 64 1.549 8.218 13.920 1.00 50.00

ATOM 279 CD2 LEU 64 2.656 10.461 14.217 1.00 50.00

ATOM 280 N GLY 65 -1.652 13.424 13.247 1.00 50.00

ATOM 281 CA GLY 65 -2.672 14.112 12.422 1.00 50.00

ATOM 282 C GLY 65 -3.670 13.126 11.794 1.00 50.00

ATOM 283 O GLY 65 -4.046 13.259 10.629 1.00 50.00

ATOM 284 N LEU 66 -3.923 12.037 12.519 1.00 50.00

ATOM 285 CA LEU 66 -4.723 10.894 12.041 1.00 50.00

ATOM 286 C LEU 66 -5.821 10.563 13.044 1.00 50.00

ATOM 287 O LEO 66 -5.921 11.184 14.104 1.00 50.00

ATOM 288 CB LEU 66 -3.823 9.658 11.869 1.00 50.00

ATOM 289 CG LEU 66 -3.029 9.652 10.567 1.00 50.00

ATOM 290 CDl LEU 66 -2.219 10.884 10.345 1.00 50.00

ATOM 291 CD2 LEU 66 -1.971 8.568 10.445 1.00 50.00

ATOM 292 N SER 67 -6.629 9.588 12.678 1.00 50.00

ATOM 293 CA SER 67 -7.767 9.152 13.499 1.00 50.00

ATOM 294 C SER 67 -7.784 7.630 13.604 1.00 50.00

ATOM 295 O SER 67 -7.201 6.931 12.778 1.00 50.00

ATOM 296 CB SER 67 -9.073 9.627 12.859 1.00 50.00

ATOM 297 OG SER 67 -9.247 9.000 11.585 1.00 50.00

ATOM 298 N LEU 68 -8.430 7.138 14.652 1.00 50.00

ATOM 299 CA LEU 68 -8.722 5.701 14.767 1.00 50.00

ATOM 300 C LEU 68 -9.608 5.296 13.588 1.00 50.00

ATOM 301 O LEU 68 10.653 5.904 13.354 1.00 50.00

ATOM 302 CB LEU 68 -9.447 5.430 16.085 1.00 50.00

ATOM 303 CG LEU 68 -8.580 5.720 17.311 1.00 50.00

ATOM 304 CDl LEU 68 -9.407 5.543 18.585 1.00 50.00

ATOM 305 CD2 LEU 68 -7.357 4.798 17.345 1.00 50.00

ATOM 306 N ALA 69 -9.149 4.286 12.858 1.00 50.00

ATOM 307 CA ALA 69 -9.821 3.855 11.622 1.00 50.00

ATOM 308 C ALA 69 11.195 3.246 11.913 1.00 50.00

ATOM 309 O ALA 69 11.437 2.707 12.989 1.00 50.00

ATOM 310 CB ALA 69 -8.948 2.838 10.887 1.00 50.00

ATOM 311 N GLY 70 12.096 3.413 10.947 1.00 50.00

ATOM 312 CA GLY 70 13.407 2.743 10.968 1.00 50.00

ATOM 313 C GLY 70 13.279 1.451 10.166 1.00 50.00

ATOM 314 O GLY 70 12.483 1.378 9.231 1.00 50.00

ATOM 315 N LYS 71 14.105 0.468 10.510 1.00 50.00

ATOM 316 CA LYS 71 14.109 -0.853 9.845 1.00 50.00

ATOM 317 C LYS 71 14.009 -0.768 8.316 1.00 50.00

ATOM 318 O LYS 71 13.362 -1.552 7.639 1.00 50.00

ATOM 319 CB LYS 71 15.403 -1.600 10.168 1.00 50.00

ATOM 320 CG LYS 71 15.508 -1.984 11.641 1.00 50.00

ATOM 321 CD LYS 71 14.414 -2.977 12.012 1.00 50.00

ATOM 322 CE LYS 71 14.605 -3.370 13.463 1.00 50.00

ATOM 323 NZ LYS 71 13.522 -4.268 13.822 1.00 50.00

ATOM 324 N ASP 72 14.642 0.234 7.743 1.00 50.00

ATOM 325 CA ASP 72 14.618 0.440 6.285 1.00 50.00

ATOM 326 C ASP 72 13.217 0.781 5.766 1.00 50.00

ATOM 327 O ASP 72 12.795 0.250 4.751 1.00 50.00

ATOM 328 CB ASP 72 15.621 1.527 5.901 1.00 50.00

ATOM 329 CG ASP 72 15.388 2.842 6.655 1.00 50.00

ATOM 330 ODl ASP 72 15.451 2.804 7.907 1.00 50.00

ATOM 331 OD2 ASP 72 15.081 3.838 5.975 1.00 50.00

ATOM 332 N GLN 73 12.487 1.582 6.531 1.00 50.00

ATOM 333 CA GLN 73 11.113 1.982 6.177 1.00 50.00

ATOM 334 C GLN 73 10.135 0.808 6.315 1.00 50.00

ATOM 335 O GLN 73 -9.162 0.676 5.587 1.00 50.00 Table 5

ATOM 336 CB GLN 73 -10.663 3.137 7.066 00 50.00

ATOM 337 CG GLN 73 -11.527 4.378 6.820 00 50.00

ATOM 338 CD GLN 73 -11.252 5.479 7.843 00 50.00

ATOM 339 OEl GLN 73 -10.751 5.246 8,936 00 50.00

ATOM 340 NE2 GLN 73 -11.643 6.690 7.497 00 50.00

ATOM 341 N VAL 74 -10.414 0.084 7.252 00 50.00

ATOM 342 CA VAL 74 -9.556 -1 262 7.470 00 50.00

ATOM 343 C VAL 74 -9.717 2.287 6.339 00 50.00

ATOM 344 O VAL 74 -8.749 2.913 5.918 00 50.00

ATOM 345 CB VAL 74 -9.807 -1 903 8.843 00 50.00

ATOM 346 CGl VAL 74 -9.620 0.894 9.975 00 50.00

ATOM 347 CG2 VAL 74 -11.176 2.547 8.982 00 50.00

ATOM 348 N GLϋ 75 -10.949 -2 400 5.842 00 50.00

ATOM 349 CA GLO 75 -11.275 3.318 4.738 00 50.00

ATOM 350 C GLU 75 -10.580 2.852 3.462 00 50.00

ATOM 351 O GLϋ 75 -10.047 -3 640 2.687 00 50.00

ATOM 352 CB GLU 75 -12.781 3.313 4.470 00 50.00

ATOM 353 CG GLU 75 -13.618 3.796 5.659 00 50.00

ATOM 354 CD GLU 75 -13.415 5.272 6.017 00 50.00

ATOM 355 OEl GLU 75 -12.729 5.983 5.251 00 50.00

ATOM 356 OE2 GLU 75 -13.961 5.667 7.069 00 50.00

ATOM 357 N THR 76 -10.555 1.538 3.311 00 50.00

ATOM 358 CA THR 76 -9.984 0.918 2.117 00 50.00

ATOM 359 C THR 76 -8.463 1.091 2.082 00 50.00

ATOM 360 O THR 76 -7.887 -1 453 .059 00 50.00

ATOM 361 CB THR 76 -10.352 0.554 .139 00 50.00

ATOM 362 OGl THR 76 -9.683 1.251 .186 00 50.00

ATOM 363 CG2 THR 76 -11.849 0.835 .097 00 50.00

ATOM 364 N ALA 77 -7.863 -0.981 3.262 1.00 50.00

ATOM 365 CA ALA 77 -6.430 -1.217 3.415 .00 50.00

ATOM 366 C ALA 77 -6.096 -2.686 3.184 ,00 50.00

ATOM 367 O ALA 77 -5.237 -3 022 2.371 ,00 50.00

ATOM 368 CB ALA 77 -6.078 0.932 4.842 00 50.00

ATOM 369 N LEU 78 -6.899 3.538 3.817 00 50.00

ATOM 370 CA LEU 78 -6.770 -4.998 3.722 00 50.00

ATOM 371 C LEU 78 -6.738 -5.456 2.259 00 50.00

ATOM 372 O LEU 78 -5.904 6.274 1.881 ,00 50.00

ATOM 373 CB LEU 78 -7.987 5.631 4.398 1.00 50.00

ATOM 374 CG LEU 78 -7.905 7.157 4.433 .00 50.00

ATOM 375 CDl LEU 78 -6.898 614 5.487 .00 50.00

ATOM 376 CD2 LEU 78 -9.286 758 4.684 .00 50.00

ATOM 377 N LYS 79 -7.580 820 1.446 .00 50.00

ATOM 378 CA LYS 79 -7.745 196 0.033 .00 50.00

ATOM 379 C LYS 79 -6.495 909 -0.814 ,00 50.00

ATOM 380 O LYS 79 -6.355 410 -1 929 .00 50.00

ATOM 381 CB LYS 79 -8.987 512 0.544 .00 50.00

ATOM 382 CG LYS 79 -9.189 919 2.003 .00 50.00

ATOM 383 CD LYS 79 -10.465 361 -2 616 .00 50.00

ATOM 384 CE LYS 79 -10.508 4.673 4.114 ,00 50.00

ATOM 385 NZ LYS 79 -10.356 6.113 4.380 .00 50.00

ATOM 386 N ALA 80 -5.638 4.033 0.311 ,00 50.00

ATOM 387 CA ALA 80 -4.385 3.731 -1 006 .00 50.00

ATOM 388 C ALA 80 -3.155 4.219 0.242 .00 50.00

ATOM 389 O ALA 80 -2.103 3.579 ^■0.290 .00 50.00

ATOM 390 CB ALA 80 -4.346 2.237 ^■1.297 .00 50.00

ATOM 391 N SER 81 -3.338 5.316 0.503 ,00 50.00

ATOM 392 CA SER 81 -2.226 6.094 1.098 ,00 50.00

ATOM 393 C SER 81 -1.841 -5 668 2.519 ,00 50.00

ATOM 394 O SER 81 -0.795 6.078 3.026 ,00 50.00

ATOM 395 CB SER 81 -0.947 6.075 0.239 .00 50.00

ATOM 396 OG SER 81 -1.251 6.516 1.084 ,00 50.00

ATOM 397 N PHE 82 -2.681 4.877 3.182 .00 50.00

ATOM 398 CA PHE 82 -2.391 4.522 4.577 ,00 50.00

ATOM 399 C PHE 82 -2.781 -5 684 5.484 ,00 50.00

ATOM 400 O PHE 82 -3.949 6.065 5.539 ,00 50.00

ATOM 401 CB PHE 82 -3.189 3.314 5.022 .00 50.00

ATOM 402 CG PHE 82 -2.737 2.837 6.407 ,00 50.00

ATOM 403 CDl PHE 82 -1.409 2.491 6.650 1.00 50.00 Table 5

ATOM 404 CD2 PHE 82 -3.660 -2.809 7.440 1.00 50.00

ATOM 405 CEl PHE 82 -1.019 -2.049 7.906 1.00 50.00

ATOM 406 CE2 PHE 82 -3.246 -2.454 8.721 1.00 50.00

ATOM 407 CZ PHE 82 -1.939 -2.024 8.944 1.00 50.00

ATOM 408 N GLU 83 -1.797 -6.193 6.210 1.00 50.00

ATOM 409 CA GLO 83 -2.057 -7.263 7.182 1.00 50.00

ATOM 410 C GLU 83 -0.949 -7.288 8.230 1.00 50.00

ATOM 411 O GLU 83 0.195 -6.907 7.977 1.00 50.00

ATOM 412 CB GLO 83 -2.223 -8.630 6.511 1.00 50.00

ATOM 413 CG GLO 83 -0.909 -9.406 6.335 1.00 50.00

ATOM 414 CD GLO 83 -1.195 -10.810 5.868 1.00 50.00

ATOM 415 OEl GLO 83 -2.077 -11.334 6.566 1.00 50.00

ATOM 416 OE2 GLO 83 -0.491 -11.274 4.940 1.00 50.00

ATOM 417 N THR 84 -1.354 -7.734 9.402 1.00 50.00

ATOM 418 CA THR 84 -0.486 -7.774 10.588 1.00 50.00

ATOM 419 C THR 84 -0.855 -9.027 11.387 1.00 50.00

ATOM 420 O THR 84 -1.833 -9.702 11.085 1.00 50.00

ATOM 421 CB THR 84 -0.746 -6.508 11.424 1.00 50.00

ATOM 422 OGl THR 84 -0.552 -5.347 10.615 1.00 50.00

ATOM 423 CG2 THR 84 0.194 -6.389 12.621 1.00 50.00

ATOM 424 N CYS 85 -0.035 -9.331 12.381 1.00 50.00

ATOM 425 CA CYS 85 -0.345 -10.382 13.361 1.00 50.00

ATOM 426 C CYS 85 -0.416 -9.756 14.763 1.00 50.00

ATOM 427 O CYS 85 -0.059 -10.365 15.769 1.00 50.00

ATOM 428 CB CYS 85 0.760 -11.436 13.280 1.00 50.00

ATOM 429 SG CYS 85 0.392 -12.949 14.242 1.00 50.00

ATOM 430 N SER 86 -0.823 -8.490 14.805 1.00 50.00

ATOM 431 CA SER 86 -0.853 -7.714 16.056 1.00 50.00

ATOM 432 C SER 86 -2.210 -7.058 16.259 1.00 50.00

ATOM 433 O SER 86 -2.778 -6.461 15.353 1.00 50.00

ATOM 434 CB SER 86 0.221 -6.623 16.063 1.00 50.00

ATOM 435 OG SER 86 1.506 -7.230 15.905 1.00 50.00

ATOM 436 N TYR 87 -2.730 -7.224 17.463 1.00 50.00

ATOM 437 CA TYR 87 -3.963 -6.538 17.875 1.00 50.00

ATOM 438 C TYR 87 -3.684 -5.048 18.062 1.00 50.00

ATOM 439 O TYR 87 -2.629 -4.668 18.574 1.00 50.00

ATOM 440 CB TYR 87 -4.489 -7.152 19.169 1.00 50.00

ATOM 441 CG TYR 87 -5.131 -8.516 18.938 1.00 50.00

ATOM 442 CDl TYR 87 -6.230 -8.608 18.095 1.00 50.00

ATOM 443 CD2 TYR 87 -4.620 -9.654 19.549 1.00 50.00

ATOM 444 CEl TYR 87 -6.810 -9.842 17.838 1.00 50.00

ATOM 445 CE2 TYR 87 -5.207 -10.889 19.301 1.00 50.00

ATOM 446 CZ TYR 87 -6.292 -10.983 18.439 1.00 50.00

ATOM 447 OH TYR 87 -6.809 -12.200 18.132 1.00 50.00

ATOM 448 N GLY 88 -4.681 -4.252 17.684 1.00 50.00

ATOM 449 CA GLY 88 -4.556 -2.791 17.739 1.00 50.00

ATOM 450 C GLY 88 -5.924 -2.123 17.713 1.00 50.00

ATOM 451 O GLY 88 -6.847 -2.620 17.065 1.00 50.00

ATOM 452 N TRP 89 -6.016 -1.033 18.464 1.00 50.00

ATOM 453 CA TRP 89 -7.250 -0.237 18.554 1.00 50.00

ATOM 454 C TRP 89 -7.653 0.361 17.207 1.00 50.00

ATOM 455 O TRP 89 -6.820 0.772 16.398 1.00 50.00

ATOM 456 CB TRP 89 -7.089 0.905 19.558 1.00 50.00

ATOM 457 CG TRP 89 -7.029 0.390 20.995 1.00 50.00

ATOM 458 CDl TRP 89 -6.022 0.546 21.849 1.00 50.00

ATOM 459 CD2 TRP 89 -8.062 -0.230 21.677 1.00 50.00

ATOM 460 NEl TRP 89 -6.367 0.039 23.033 1.00 50.00

ATOM 461 CE2 TRP 89 -7.604 -0.447 22.965 1.00 50.00

ATOM 462 CE3 TRP 89 -9.353 -0.592 21.319 1.00 50.00

ATOM 463 CZ2 TRP 89 -8.430 -1.066 23.896 1.00 50.00

ATOM 464 CZ3 TRP 89 -10.186 -1.208 22.250 1.00 50.00

ATOM 465 CH2 TRP 89 -9.711 -1.465 23.533 1.00 50.00

ATOM 466 N VAL 90 -8.960 0.363 17.015 1.00 99.99

ATOM 467 CA VAL 90 -9.637 0.987 15.870 1.00 99.99

ATOM 468 C VAL 90 -10.840 1.762 16.428 1.00 99.99

ATOM 469 O VAL 90 -11.338 1.465 17.518 1.00 99.99

ATOM 470 CB VAL 90 -10.084 -0.077 14.849 1.00 99.99

ATOM 471 CGl VAL 90 -8.887 -0.855 14.290 1.00 99.99 Table 5

ATOM 472 CG2 VAL 90 11.108 -1.055 15.430 1.00 99.99

ATOM 473 N GLY 91 11.253 2.781 15.677 1.00 99.99

ATOM 474 CA GLY 91 12.442 3.579 16.020 1.00 99.99

ATOM 475 C GLY 91 13.707 2.741 15.850 1.00 99.99

ATOM 476 O GLY 91 13.658 1.556 15.515 1.00 99.99

ATOM 477 N ASP 92 14.839 3.383 16.138 1.00 99.99

ATOM 47B CA ASP 92 16.158 2.722 16.044 1.00 99.99

ATOM 479 C ASP 92 16.152 1.447 16.914 1.00 99.99

ATOM 480 O ASP 92 16.679 0.409 16.536 1.00 99.99

ATOM 481 CB ASP 92 16.459 2.439 14.564 1.00 99.99

ATOM 482 CG ASP 92 17.937 2.135 14.335 1.00 99.99

ATOM 483 ODl ASP 92 18.672 3.125 14.137 1.00 99.99

ATOM 484 OD2 ASP 92 18.292 0.939 14.339 1.00 99.99

ATOM 485 N GLY 93 15.349 1.579 17.977 1.00 99.99

ATOM 486 CA GLY 93 15.180 0.685 19.114 1.00 99.99

ATOM 487 C GLY 93 14.674 -0.702 18.811 1.00 99.99

ATOM 488 O GLY 93 15.507 -1.540 19.090 1.00 99.99

ATOM 489 N PHE 94 13.352 -0.911 18.728 1.00 50.00

ATOM 490 CA PHE 94 12.776 -2.275 18.610 1.00 50.00

ATOM 491 C PHE 94 11.243 -2.355 18.603 1.00 50.00

ATOM 492 O PHE 94 10.526 -1.373 18.423 1.00 50.00

ATOM 493 CB PHE 94 13.293 -3.038 17.371 1.00 50.00

ATOM 494 CG PHE 94 14.809 -3.284 17.340 1.00 50.00

ATOM 495 CDl PHE 94 15.379 -4.151 18.276 1.00 50.00

ATOM 496 CD2 PHE 94 15.630 -2.412 16.611 1.00 50.00

ATOM 497 CEl PHE 94 16.759 -4.171 18.463 1.00 50.00

ATOM 498 CE2 PHE 94 17.009 -2.424 16.825 1.00 50.00

ATOM 499 CZ PHE 94 17.574 -3.310 17.737 1.00 50.00

ATOM 500 N VAL 95 10.796 -3.573 18.870 1.00 50.00

ATOM 501 CA VAL 95 -9.398 -4.014 18.721 1.00 50.00

ATOM 502 C VAL 95 -9.454 -5.109 17.653 1.00 50.00

ATOM 503 O VAL 95 10.334 -5.972 17.685 1.00 50.00

ATOM 504 CB VAL 95 -8.887 -4.633 20.026 1.00 50.00

ATOM 505 CGl VAL 95 -7.435 -5.082 19.927 1.00 50.00

ATOM 506 CG2 VAL 95 -8.908 -3.641 21.157 1.00 50.00

ATOM 507 N VAL 96 -8.471 -5.082 16.765 1.00 50.00

ATOM 508 CA VAL 96 -8.544 -5.843 15.511 1.00 50.00

ATOM 509 C VAL 96 -7.171 -6.246 14.985 1.00 50.00

ATOM 510 O VAL 96 -6.177 -5.589 15.271 1.00 50.00

ATOM 511 CB VAL 96 -9.270 -4.927 14.521 1.00 50.00

ATOM 512 CGl VAL 96 -8.804 -4.943 13.066 1.00 50.00

ATOM 513 CG2 VAL 96 10.699 -5.356 14.508 1.00 50.00

ATOM 514 N ILE 97 -7.200 -7.296 14.176 1.00 50.00

ATOM 515 CA ILE 97 -6.067 -7.689 13.325 1.00 50.00

ATOM 516 C ILE 97 -6.597 -7.910 11.903 1.00 50.00

ATOM 517 O ILE 97 -7.473 -8.751 11.693 1.00 50.00

ATOM 518 CB ILE 97 -5.422 -8.985 13.838 1.00 50.00

ATOM 519 CGl ILE 97 -4.841 -8.798 15.239 1.00 50.00

ATOM 520 CG2 ILE 97 -4.340 -9.468 12.860 1.00 50.00

ATOM 521 CDl ILE 97 -4.145 -10.050 15.796 1.00 50.00

ATOM 522 N SER 98 -6.054 -7.147 10.963 1.00 50.00

ATOM 523 CA SER 98 -6.346 -7.372 9.536 1.00 50.00

ATOM 524 C SER 98 -5.557 -8.599 9.055 1.00 50.00

ATOM 525 O SER 98 -4.345 -8.700 9.253 1.00 50.00

ATOM 526 CB SER 98 -5.963 -6.141 8.713 1.00 50.00

ATOM 527 OG SER 98 -4.565 -5.879 8.847 1.00 50.00

ATOM 528 N ARG 99 -6.281 -9.546 8.482 1.00 50.00

ATOM 529 CA ARG 99 -5.718 -10.835 8.056 1.00 50.00

ATOM 530 C ARG 99 -5.992 -11.138 6.586 1.00 50.00

ATOM 531 O ARG 99 -7.127 -11.124 6.107 1.00 50.00

ATOM 532 CB ARG 99 -6.301 -11.972 8.898 1.00 50.00

ATOM 533 CG ARG 99 -5.619 -12.176 10.253 1.00 50.00

ATOM 534 CD ARG 99 -4.382 -13.067 10.131 1.00 50.00

ATOM 535 NE ARG 99 -3.134 -12.284 10.059 1.00 50.00

ATOM 536 CZ ARG 99 -1.960 -12.752 9.620 1.00 50.00

ATOM 537 NHl ARG 99 -1.843 -13.999 9.173 1.00 50.00

ATOM 538 NH2 ARG 99 -0.867 -12.001 9.703 1.00 50.00

ATOM 539 N ILE 100 -4.893 -11.365 5.894 1.00 50.00 Table 5

ATOM 540 CA ILE 100 -4.884 -12.009 4.569 00 50.00

ATOM 541 C ILE 100 -4.001 -13.224 4.808 00 50.00

ATOM 542 O ILE 100 -2.931 -13.048 5.341 00 50.00

ATOM 543 CB ILE 100 -4.181 -11.103 3.550 00 50.00

ATOM 544 CGl ILE 100 -4.877 -9.742 3.489 00 50.00

ATOM 545 CG2 ILE 100 -4.158 -11.774 2.167 00 50.00

ATOM 546 CDl ILE 100 -4.036 -8.695 2.759 00 50.00

ATOM 547 N SER 101 -4.407 -14.434 4.482 00 50.00

ATOM 548 CA SER 101 -3.548 -15.616 4.736 00 50.00

ATOM 549 C SER 101 -3.807 -16.089 6.171 00 50.00

ATOM 550 O SER 101 -3.540 -15.381 7.145 00 50.00

ATOM 551 CB SER 101 -2.020 -15.434 4.565 00 50.00

ATOM 552 OG SER 101 -1.778 -14.695 3.360 00 50.00

ATOM 553 N PRO 102 -4.458 -17.250 6.277 00 50.00

ATOM 554 CA PRO 102 -4.698 -17.917 7.566 00 50.00

ATOM 555 C PRO 102 -3.335 -18.319 8.132 00 50.00

ATOM 556 O PRO 102 -2.476 -18.829 7.414 00 50.00

ATOM 557 CB PRO 102 -5.476 -19.184 7.208 00 50.00

ATOM 558 CG PRO 102 -6.112 -18.874 5.856 00 50.00

ATOM 559 CD PRO 102 -5.077 -17.995 5.165 00 50.00

ATOM 560 N ASN 103 -3.126 -17.999 9.401 00 50.00

ATOM 561 CA ASN 103 -1.938 -18.464 10.122 00 50.00

ATOM 562 C ASN 103 -2.377 -18.872 11.529 00 50.00

ATOM 563 O ASN 103 -3.014 -18.077 12.224 00 50.00

ATOM 564 CB ASN 103 -0.842 -17.397 10.165 00 50.00

ATOM 565 CG ASN 103 0.440 -17.933 10.812 00 50.00

ATOM 566 ODl ASN 103 0.432 -18.635 11.816 00 50.00

ATOM 567 ND2 ASN 103 1.565 -17.555 10.248 00 50.00

ATOM 568 N PRO 104 -2.075 -20.122 11.901 00 50.00

ATOM 569 CA PRO 104 -2.479 -20.701 13.192 00 50.00

ATOM 570 C PRO 104 -2.152 -19.823 14.409 00 50.00

ATOM 571 O PRO 104 -2.906 -19.831 15.379 00 50.00

ATOM 572 CB PRO 104 -1.785 -22.065 13.244 00 50.00

ATOM 573 CG PRO 104 -0.637 -21.955 12.240 00 50.00

ATOM 574 CD PRO 104 -1.215 -21.060 11.151 00 50.00

ATOM 575 N LYS 105 -1.124 -18.980 14.299 00 50.00

ATOM 576 CA LYS 105 -0.741 -18.075 15.404 00 50.00

ATOM 577 C LYS 105 -1.293 -16.633 15.282 00 50.00

ATOM 578 O LYS 105 -1.089 -15.763 16.131 00 50.00

ATOM 579 CB LYS 105 0.788 -18.070 15.537 1.00 50.00

ATOM 580 CG LYS 105 1.226 -17.092 16.627 00 50.00

ATOM 581 CD LYS 105 2.713 -16.870 16.811 00 50.00

ATOM 582 CE LYS 105 2.921 -15.700 17.777 00 50.00

ATOM 583 NZ LYS 105 2.166 -15.868 19.031 00 50.00

ATOM 584 N CYS 106 -2.067 -16.354 14.252 00 50.00

ATOM 585 CA CYS 106 -2.579 -14.988 14.073 00 50.00

ATOM 586 C CYS 106 -4.099 -14.986 13.996 00 50.00

ATOM 587 O CYS 106 -4.683 -15.628 13.123 00 50.00

ATOM 588 CB CYS 106 -1.978 -14.351 12.824 00 50.00

ATOM 589 SG CYS 106 -0.148 -14.314 12.825 00 50.00

ATOM 590 N GLY 107 -4.694 -14.439 15.060 00 50.00

ATOM 591 CA GLY 107 -6.152 -14.270 15.133 00 50.00

ATOM 592 C GLY 107 -6.920 -15.585 14.935 00 50.00

ATOM 593 O GLY 107 -7.841 -15.668 14.126 00 50.00

ATOM 594 N LYS 108 -6.441 -16.641 15.590 00 50.00

ATOM 595 CA LYS 108 -7.091 -17.969 15.548 00 50.00

ATOM 596 C LYS 108 -7.232 -18.480 14.100 00 50.00

ATOM 597 O LYS 108 -8.225 -19.092 13.707 00 50.00

ATOM 598 CB LYS 108 -8.459 -17.883 16.248 00 50.00

ATOM 599 CG LYS 108 -9.176 -19.234 16.328 00 50.00

ATOM 600 CD LYS 108 -10.580 -19.080 16.899 00 50.00

ATOM 601 CE LYS 108 -11.371 -20.388 16.814 00 50.00

ATOM 602 NZ LYS 108 -10.835 -21.443 17.689 00 50.00

ATOM 603 N ASN 109 -6.220 -18.180 13.286 00 50.00

ATOM 604 CA ASN 109 -6.165 -18.626 11.880 00 50.00

ATOM 605 C ASN 109 -7.264 -17.983 11.010 00 50.00

ATOM 606 O ASN 109 -7.497 -18.399 9.876 00 50.00

ATOM 607 CB ASN 109 -6.312 -20.156 11.871 1.00 50.00 Table 5

ATOM 608 CG ASN 109 -5.828 -20.771 10.575 1.00 50.00

ATOM 609 ODl ASN 109 -6.530 -21.492 9.886 1.00 50.00

ATOM 610 ND2 ASN 109 -4.580 -20.481 10.284 1.00 50.00

ATOM 611 N GLY 110 -7.889 -16.935 11.557 1.00 50.00

ATOM 612 CA GLY 110 -8.961 -16.188 10.882 1.00 50.00

ATOM 613 C GLY 110 -8.405 -15.326 9.746 1.00 50.00

ATOM 614 O GLY 110 -7.230 -14.966 9.720 1.00 50.00

ATOM 615 N VAL 111 -9.287 -15.052 8.798 1.00 50.00

ATOM 616 CA VAL 111 -9.018 -14.14B 7.664 1.00 50.00

ATOM 617 C VAL 111 -10.039 -13.001 7.697 1.00 50.00

ATOM 618 O VAL 111 -11.132 -13,156 8.244 1.00 50.00

ATOM 619 CB VAL 111 -9.094 -14.909 6.332 1.00 50.00

ATOM 620 CGl VAL 111 -8.023 -15.997 6.278 1.00 50.00

ATOM 621 CG2 VAL 111 -10.481 -15.523 6.093 1.00 50.00

ATOM 622 N GLY 112 -9.670 -11.885 7.069 1.00 50.00

ATOM 623 CA GLY 112 -10.508 -10.671 7.061 1.00 50.00

ATOM 624 C GLY 112 -10.045 -9.716 8.163 1.00 50.00

ATOM 625 O GLY 112 -8.903 -9.767 8.605 1.00 50.00

ATOM 626 N VAL 113 -10.957 -8.882 8.640 1.00 50.00

ATOM 627 CA VAL 113 -10.665 -7.959 9.754 1.00 50.00

ATOM 628 C VAL 113 -11.255 -8.575 11.026 1.00 50.00

ATOM 629 O VAL 113 -12.419 -8.360 11.365 1.00 50.00

ATOM 630 CB VAL 113 -11.269 -6.573 9.488 1.00 50.00

ATOM 631 CGl VAL 113 -11.029 -5.636 10.670 1.00 50.00

ATOM 632 CG2 VAL 113 -10.679 -5.954 8.220 1.00 50.00

ATOM 633 N LEU 114 -10.408 -9.341 11.697 1.00 50.00

ATOM 634 CA LEU 114 -10.820 -10.096 12.882 1.00 50.00

ATOM 635 C LEU 114 -10.976 -9.177 14.092 1.00 50.00

ATOM 636 O LEU 114 -10.049 -8.458 14.462 1.00 50.00

ATOM 637 CB LEU 114 -9.774 -11.167 13.176 1.00 50.00

ATOM 638 CG LEU 114 -10.347 -12.201 14.144 1.00 50.00

ATOM 639 CDl LEU 114 -11.510 -12.970 13.514 1.00 50.00

ATOM 640 CD2 LEU 114 -9.257 -13.168 14.544 1.00 50.00

ATOM 641 N ILE 115 -12.126 -9.296 14.739 1.00 99.99

ATOM 642 CA ILE 115 -12.466 -8.458 15.910 1.00 99.99

ATOM 643 C ILE 115 -12.906 -9.372 17.045 1.00 99.99

ATOM 644 O ILE 115 -13.707 -10.286 16.856 1.00 99.99

ATOM 645 CB ILE 115 -13.613 -7.474 15.608 1.00 99.99

ATOM 646 CGl ILE 115 -14.998 -8.107 15.398 1.00 99.99

ATOM 647 CG2 ILE 115 -13.362 -6.897 14.243 1.00 99.99

ATOM 648 CDl ILE 115 -15.106 -9.165 14.268 1.00 99.99

ATOM 649 N TRP 116 -12.439 -9.026 18.225 1.00 99.99

ATOM 650 CA TRP 116 -12.826 -9.748 19.436 1.00 99.99

ATOM 651 C TRP 116 -13.459 -8.739 20.382 1.00 99.99

ATOM 652 O TRP 116 -12.800 -8.204 21.275 1.00 99.99

ATOM 653 CB TRP 116 -11.577 -10.345 20.073 1.00 99.99

ATOM 654 CG TRP 116 -11.008 -11.525 19.312 1.00 99.99

ATOM 655 CDl TRP 116 -10.145 -11.433 18.311 1.00 99.99

ATOM 656 CD2 TRP 116 -11.268 -12.865 19.542 1.00 99.99

ATOM 657 NEl TRP 116 -9.847 -12.659 17.889 1.00 99.99

ATOM 658 CE2 TRP 116 -10.507 -13.556 18.616 1.00 99.99

ATOM 659 CE3 TRP 116 -12.062 -13.546 20.455 1.00 99.99

ATOM 660 CZ2 TRP 116 -10.535 -14.944 18.598 1.00 99.99

ATOM 661 CZ3 TRP 116 -12.094 -14.935 20.435 1.00 99.99

ATOM 662 CH2 TRP 116 -11.330 -15.633 19.506 1.00 99.99

ATOM 663 N LYS 117 -14.764 -8.529 20.201 1.00 99.99

ATOM 664 CA LYS 117 -15.517 -7.661 21.130 1.00 99.99

ATOM 665 C LYS 117 -15.329 -8.163 22.577 1.00 99.99

ATOM 666 O LYS 117 -15.532 -7.424 23.534 1.00 99.99

ATOM 667 CB LYS 117 -17.005 -7.654 20.760 1.00 99.99

ATOM 668 CG LYS 117 -17.810 -6.677 21.625 1.00 99.99

ATOM 669 CD LYS 117 -19.300 -6.736 21.290 1.00 99.99

ATOM 670 CE LYS 117 -20.135 -5.840 22.210 1.00 99.99

ATOM 671 NZ LYS 117 -19.853 -4.410 22.014 1.00 99.99

ATOM 672 N VAL 118 -14.859 -9.402 22.708 1.00 99.99

ATOM 673 CA VAL 118 -14.771 -10.073 24.010 1.00 99.99

ATOM 674 C VAL 118 -13.476 -10.064 24.849 1.00 99.99

ATOM 675 O VAL 118 -13.619 -10.130 26.068 1.00 99.99 Table 5

ATOM 676 CB VAL 118 -15.428 -11.458 23.937 1.00 99.99

ATOM 677 CGl VAL 118 -16.946 -11.280 23.847 1.00 99.99

ATOM 678 CG2 VAL 118 -14.948 -12.303 22.750 1.00 99.99

ATOM 679 N PRO 119 -12.253 -10.100 24.302 1.00 50.00

ATOM 680 CA PRO 119 -11.077 -9.882 25.167 1.00 50.00

ATOM 681 C PRO 119 -10.535 -8.463 24.980 1.00 50.00

ATOM 682 O PRO 119 -9.598 -8.238 24.218 1.00 50.00

ATOM 683 CB PRO 119 -10.023 -10.905 24.724 1.00 50.00

ATOM 684 CG PRO 119 -10.768 -11.864 23.803 1.00 50.00

ATOM 685 CD PRO 119 -11.860 -10.985 23.207 1.00 50.00

ATOM 686 N VAL 120 -11.115 -7.516 25.713 1.00 50.00

ATOM 687 CA VAL 120 -10.692 -6.103 25.626 1.00 50.00

ATOM 688 C VAL 120 -9.396 -5.889 26.411 1.00 50.00

ATOM 689 O VAL 120 -8.415 -6.549 26.094 1.00 50.00

ATOM 690 CB VAL 120 -11.813 -5.146 26.072 1.00 50.00

ATOM 691 CGl VAL 120 -13.006 -5.252 25.128 1.00 50.00

ATOM 692 CG2 VAL 120 -12.285 -5.389 27.516 1.00 50.00

ATOM 693 N SER 121 -9.448 -4.990 27.402 1.00 50.00

ATOM 694 CA SER 121 -8.375 -4.623 28.333 1.00 50.00

ATOM 695 C SER 121 -7.246 -4.041 27.514 1.00 50.00

ATOM 696 O SER 121 -6.795 -4.697 26.599 1.00 50.00

ATOM 697 CB SER 121 -7.880 -5.827 29.148 1.00 50.00

ATOM 698 OG SER 121 -7.332 -6.858 28.323 1.00 50.00

ATOM 699 N ARG 122 -6.892 -2.814 27.850 1.00 50.00

ATOM 700 CA ARG 122 -5.873 -2.001 27.163 1.00 50.00

ATOM 701 C ARG 122 -4.624 -2.804 26.742 1.00 50.00

ATOM 702 O ARG 122 -4.552 -4.020 26.683 1.00 50.00

ATOM 703 CB ARG 122 -5.441 -0.903 28.139 1.00 50.00

ATOM 704 CG ARG 122 -6.606 -0.108 28.708 1.00 50.00

ATOM 705 CD ARG 122 -6.074 0.877 29.733 1.00 50.00

ATOM 706 NE ARG 122 -7.206 1.562 30.363 1.00 50.00

ATOM 707 CZ ARG 122 -7.090 2.512 31.289 1.00 50.00

ATOM 708 NHl ARG 122 -5.891 2.930 31.686 1.00 50.00

ATOM 709 NH2 ARG 122 -8.181 3.041 31.830 1.00 50.00

ATOM 710 N GLN 123 -3.566 -2.071 26.473 1.00 50.00

ATOM 711 CA GLN 123 -2.255 -2.631 26.107 1.00 50.00

ATOM 712 C GLN 123 -2.399 -3.544 24.906 1.00 50.00

ATOM 713 O GLN 123 -2.571 -4.755 25.009 1.00 50.00

ATOM 714 CB GLN 123 -1.547 -3.322 27.283 1.00 50.00

ATOM 715 CG GLN 123 -0.615 -2.363 28.029 1.00 50.00

ATOM 716 CD GLN 123 -1.224 -0.983 28.327 1.00 50.00

ATOM 717 OEl GLN 123 -2.411 -0.708 28.323 1.00 50.00

ATOM 718 NE2 GLN 123 -0.391 -0.017 28.590 1.00 50.00

ATOM 719 N PHE 124 -2.621 -2.821 23.824 1.00 50.00

ATOM 720 CA PHE 124 -2.521 -3.333 22.468 1.00 50.00

ATOM 721 C PHE 124 -1.665 -2.347 21.663 1.00 50.00

ATOM 722 O PHE 124 -1.013 -1.492 22.263 1.00 50.00

ATOM 723 CB PHE 124 -3.851 -3.625 21.786 1.00 50.00

ATOM 724 CG PHE 124 -4.553 -4.787 22.476 1.00 50.00

ATOM 725 CDl PHE 124 -4.190 -6.097 22.197 1.00 50.00

ATOM 726 CD2 PHE 124 -5.590 -4.516 23.350 1.00 50.00

ATOM 727 CEl PHE 124 -4.871 -7.149 22.794 1.00 50.00

ATOM 728 CE2 PHE 124 -6.265 -5.571 23.940 1.00 50.00

ATOM 729 CZ PHE 124 -5.911 -6.884 23.673 1.00 50.00

ATOM 730 N ALA 125 -1.515 -2.584 20.364 1.00 50.00

ATOM 731 CA ALA 125 -0.950 -1.558 19.487 1.00 50.00

ATOM 732 C ALA 125 -2.156 -0.727 19.039 1.00 50.00

ATOM 733 O ALA 125 -3.261 -0.848 19.581 1.00 50.00

ATOM 734 CB ALA 125 -0.237 -2.226 18.308 1.00 50.00

ATOM 735 N ALA 126 -1.923 0.178 18.108 1.00 50.00

ATOM 736 CA ALA 126 -3.022 0.949 17.517 1.00 50.00

ATOM 737 C ALA 126 -2.882 0.988 16.000 1.00 50.00

ATOM 738 O ALA 126 -1.794 0.803 15.461 1.00 50.00

ATOM 739 CB ALA 126 -3.006 2.366 18.090 1.00 50.00

ATOM 740 N TYR 127 -4.017 1.184 15.353 1.00 50.00

ATOM 741 CA TYR 127 -4.044 1.505 13.921 1.00 50.00

ATOM 742 C TYR 127 -4.525 2.950 13.803 1.00 50.00

ATOM 743 O TYR 127 -5.250 3.452 14.664 1.00 50.00 Table 5

ATOM 744 CB TYR 127 -4.990 0.570 13.164 00 50.00

ATOM 745 CG TYR 127 -4.514 -0.882 13.229 00 50.00

ATOM 746 CDl TYR 127 -3.516 -1.326 12.371 00 50.00

ATOM 747 CD2 TYR 127 5.084 -1.755 14.145 00 50,00

ATOM 748 CEl TYR 127 3.077 -2..642 12.437 00 50.00

ATOM 749 CE2 TYR 127 4.630 -3, .061 14.225 00 50.00

ATOM 750 CZ TYR 127 3.624 -3, .500 13.379 00 50.00

ATOM 751 OH TYR 127 3.154 -4.762 13.467 00 50.00

ATOM 752 N CYS 128 -3 994 3.633 12.805 00 50.00

ATOM 753 CA CYS 128 -4.350 .035 12.550 00 50.00

ATOM 754 C CYS 128 -4.663 .203 11.066 00 50.00

ATOM 755 O CYS 128 -4.210 .425 10.228 00 50.00

ATOM 756 CB CYS 128 -3.202 .965 12.948 00 50.00

ATOM 757 SG CYS 128 -2.764 .952 14.726 00 50.00

ATOM 758 N TYR 129 -5.508 6.180 10.791 00 50.00

ATOM 759 CA TYR 129 -5.889 6.525 9.420 00 50.00

ATOM 760 C TYR 129 -5.582 8.002 9.201 00 50.00

ATOM 761 O TYR 129 -6.071 8.863 9.932 00 50.00

ATOM 762 CB TYR 129 -7.378 6.251 9.199 00 50.00

ATOM 763 CG TYR 129 -7.787 6.624 7.775 00 50.00

ATOM 764 CDl TYR 129 —^*7 598 5.716 6.747 00 50.00

ATOM 765 CD2 TYR 129 -8.336 7.873 7.509 00 50.00

ATOM 766 CEl TYR 129 -7.974 6.067 463 00 50.00

ATOM 767 CE2 TYR 129 704 8.215 6.215 00 50.00

ATOM 768 CZ TYR 129 521 7.306 5.186 00 50.00

ATOM 769 OH TYR 129 897 7.618 3.920 1.00 50.00

ATOM 770 N ASN 130 806 8.248 8.160 00 50.00

ATOM 771 CA ASN 130 -4 449 9.608 7.767 00 50.00

ATOM 772 C ASN 130 -5.227 9.935 6.517 00 50.00

ATOM 773 O ASN 130 -4.836 9.510 5.428 00 50.00

ATOM 774 CB ASN 130 -2.960 9.727 7.414 00 50.00

ATOM 775 CG ASN 130 -2.581 11.167 7.060 00 50.00

ATOM 776 ODl ASN 130 -1 680 11.376 6.266 00 50.00

ATOM 111 ND2 ASN 130 3.317 12.133 7.588 00 50.00

ATOM 778 N SER 131 6.303 10.707 6.677 00 50.00

ATOM 779 CA SER 131 6.940 11.331 5.492 00 50.00

ATOM 780 C SER 131 5.806 11.972 4.706 00 50.00

ATOM 781 O SER 131 4.809 12.229 5.350 00 50.00

ATOM 782 CB SER 131 7.900 12.452 5.893 00 50.00

ATOM 783 OG SER 131 -7.212 13.506 6.572 00 50.00

ATOM 784 N SER 132 -5. 905 12.019 3.389 00 50.00

ATOM 785 CA SER 132 -4.847 12.536 2.503 00 50.00

ATOM 786 C SER 132 -3.769 11.504 2.211 00 50.00

ATOM 787 O SER 132 -3. .626 11.274 1.015 00 50.00

ATOM 788 CB SER 132 -4..171 13.839 2.978 00 50.00

ATOM 789 OG SER 132 -3..269 13.586 4.063 00 50.00

ATOM 790 N ASP 133 -3..154 10.874 3.232 00 50.00

ATOM 791 CA ASP 133 -1.995 9.970 3.073 00 50.00

ATOM 792 C ASP 133 -1.577 9.882 1.598 00 50.00

ATOM 793 O ASP 133 -0.963 10.821 1.105 00 50.00

ATOM 794 CB ASP 133 -2.364 8.590 3.623 00 50.00

ATOM 795 CG ASP 133 -1.209 7.642 3.357 00 50.00

ATOM 796 ODl ASP 133 -0.200 7.952 3.986 00 50.00

ATOM 797 OD2 ASP 133 -1 299 6.762 2.461 00 50.00

ATOM 798 N THR 134 2.223 8.924 0.929 00 50.00

ATOM 799 CA THR 134 2.411 8.805 -0.522 00 50.00

ATOM 800 C THR 134 3.535 7.763 -0.683 00 50.00

ATOM 801 O THR 134 4.208 7.420 0.293 00 50.00

ATOM 802 CB THR 134 -1 104 8.364 -1.206 00 50.00

ATOM 803 OGl THR 134 0.730 7.071 -0.734 00 50.00

ATOM 804 CG2 THR 134 0.067 9.339 -1.041 00 50.00

ATOM 805 N TRP 135 3.629 7.131 -1.843 00 50.00

ATOM 806 CA TRP 135 4.690 6.132 -2.053 00 50.00

ATOM 807 C TRP 135 -4.209 4.687 -1.972 00 50.00

ATOM 808 O TRP 135 5.034 3.779 -1.966 00 50.00

ATOM 809 CB TRP 135 5.438 6.379 -3.364 00 50.00

ATOM 810 CG TRP 135 4.485 6.727 -4.507 00 50.00

ATOM 811 CDl TRP 135 4.302 7.948 -4.992 1.00 50.00 Table 5

ATOM 812 CD2 TRP 135 -3.720 5.866 -5.273 1.00 50.00

ATOM 813 NEl TRP 135 -3.472 7.890 -6.033 1.00 50.00

ATOM 814 CE2 TRP 135 -3.091 6.633 -6.228 1.00 50.00

ATOM 815 CE3 TRP 135 -3.499 4.509 -5.245 1.00 50.00

ATOM 816 CZ2 TRP 135 -2.238 6.034 -7.145 1.00 50.00

ATOM 817 CZ3 TRP 135 -2. .657 3.887 -6.155 1.00 50.00

ATOM 818 CH2 TRP 135 -2..024 4.662 -7.114 1.00 50.00

ATOM 819 N THR 136 -2..899 4.483 -1.859 1.00 50.00

ATOM 820 CA THR 136 -2.324 3.122 -1. .824 1.00 50.00

ATOM 821 C THR 136 -0.881 3.165 -1..361 1.00 50.00

ATOM 822 O THR 136 -0.227 4.192 -1..517 1.00 50.00

ATOM 823 CB THR 136 -2.422 2.427 -3..194 1.00 50.00

ATOM 824 OGl THR 136 -3.792 2.105 -3.431 1.00 50.00

ATOM 825 CG2 THR 136 -1.626 1.132 -3.353 1.00 50.00

ATOM 826 N ASN 137 -0.497 2.042 -0.759 1.00 50.00

ATOM 827 CA ASN 137 0.848 1.813 -0.223 1.00 50.00

ATOM 828 C ASN 137 1.840 2.951 -0.482 1.00 50.00

ATOM 829 O ASN 137 2.272 3.164 -1.613 1.00 50.00

ATOM 830 CB ASN 137 1.449 0.498 -0.732 00 50.00

ATOM 831 CG ASN 137 2.571 0.068 0.217 00 50.00

ATOM 832 ODl ASN 137 3.564 -0.531 -0.167 1.00 50.00

ATOM 833 ND2 ASN 137 2.386 0.402 1.484 1.00 50.00

ATOM 834 N SER 138 .930 3.804 0.526 1.00 50.00

ATOM 835 CA SER 138 .892 4.911 0.530 1.00 50.00

ATOM 836 C SER 138 .835 4.647 1.700 1.00 50.00

ATOM 837 O SER 138 .407 4.601 2.853 1.00 50.00

ATOM 838 CB SER 138 .168 6.241 0.727 1.00 50.00

ATOM 839 OG SER 138 .130 7.290 0.647 1.00 50.00

ATOM 840 N CYS 139 .090 4.382 1.361 1.00 50.00

ATOM 841 CA CYS 139 6.095 4.015 2.375 1. .0000 5500..0000

ATOM 842 C CYS 139 7.015 5.188 2.706 1. .0000 5500..0000

ATOM 843 O CYS 139 8.112 5,011 3.235 1.00 50.00

ATOM 844 CB CYS 139 6.931 2.841 1.865 1.00 50.00

ATOM 845 SG CYS 139 6.075 1.227 1.917 1.00 50.00

ATOM 846 N ILE 140 6.511 6.390 2.449 ,00 50.00

ATOM 847 CA ILE 140 7.304 7.600 2.657 .00 50.00

ATOM 848 C ILE 140 7.806 7.679 4.110 .00 50.00

ATOM 849 O ILE 140 7.103 7.269 5.037 1.00 50.00

ATOM 850 CB ILE 140 6.580 8.896 2.244 00 50.00

ATOM 851 CGl ILE 140 5.482 9.326 3.225 00 50.00

ATOM 852 CG2 ILE 140 6.132 8.814 0.774 00 50.00

ATOM 853 CDl ILE 140 4.154 8.618 985 1.00 50.00

ATOM 854 N PRO 141 8.983 8.294 246 1.00 50.00

ATOM 855 CA PRO 141 9.721 8.505 493 1.00 50.00

ATOM 855 C PRO 141 8.950 8.349 6.800 1.00 50.00

ATOM 857 O PRO 141 8.936 7.241 7.328 1.00 50.00

ATOM 858 CB PRO 141 10.359 9.891 5.335 1.00 50.00

ATOM 859 CG PRO 141 9.980 10.370 3.933 1.00 50.00

ATOM 860 CD PRO 141 9.661 9.077 3.199 1.00 50.00

ATOM 861 N GLϋ 142 8.292 9.434 7.233 1.00 50.00

ATOM 862 CA GLO 142 7.849 9.618 8.630 1.00 50.00

ATOM 863 C GLD 142 9.098 10.100 9.379 1.00 50.00

ATOM 864 O GLϋ 142 10.080 9.397 9.521 1.00 50.00

ATOM 865 CB GLϋ 142 7.222 8.335 9.225 1.00 50.00

ATOM 866 CG GLϋ 142 7.692 7.910 10.627 1.00 50.00

ATOM 867 CD GLϋ 142 9.081 7.233 10.667 1.00 50.00

ATOM 868 OEl GLϋ 142 ^■9.146 6.063 10.253 1.00 50.00

ATOM 869 OE2 GLϋ 142 10.014 7.783 11.299 1.00 50.00

ATOM 870 N ILE 143 9.204 11.386 9.568 1.00 50.00

ATOM 871 CA ILE 143 10.477 11.966 10.032 1.00 50.00

ATOM 872 C ILE 143 10.403 12.330 11.512 1.00 50.00

ATOM 873 O ILE 143 11.435 12.413 12.169 1.00 50.00

ATOM 874 CB ILE 143 10.900 13.151 9.144 00 50.00

ATOM 875 CGl ILE 143 9.999 14.382 9.300 1.00 50.00

ATOM 876 CG2 ILE 143 10.958 12.728 7.666 1.00 50.00

ATOM 877 CDl ILE 143 8.554 14.192 8.794 1.00 50.00

ATOM 878 N ILE 144 9.181 12.583 11.982 1.00 50.00

ATOM 879 CA ILE 144 8.909 12.990 13.371 1.00 50.00 Table 5

ATOM 880 C ILE 144 7.412 12.744 13.637 1.00 50.00

ATOM 881 O ILE 144 6.651 12.414 12.724 1.00 50.00

ATOM 882 CB ILE 144 9.256 14.484 13.633 1.00 50.00

ATOM 883 CGl ILE 144 8.174 15.472 13.173 1.00 50.00

ATOM 884 CG2 ILE 144 10.617 14.968 13.100 1.00 50.00

ATOM 885 CDl ILE 144 7, .930 15.535 11.673 1.00 50.00

ATOM 886 N THR 145 7, .018 12.965 14.881 1.00 50.00

ATOM 887 CA THR 145 5, .593 13.010 15.254 1.00 50.00

ATOM 888 C THR 145 5, .118 14.455 15.062 1.00 50.00

ATOM 889 O THR 145 5, .456 15.371 15.809 1.00 50.00

ATOM 890 CB THR 145 5.393 12.542 16.700 1.00 50.00

ATOM 891 OGl THR 145 6.043 13.442 17.599 1.00 50.00

ATOM 892 CG2 THR 145 5.967 11.135 16.900 1.00 50.00

ATOM 893 N THR 146 4.458 14.667 13.933 1.00 50.00

ATOM 894 CA THR 146 4.114 16.024 13.451 1.00 50.00

ATOM 895 C THR 146 3.239 16.811 14.442 1.00 50.00

ATOM 896 O THR 146 3.241 18.055 14.339 1.00 50.00

ATOM 897 CB THR 146 3.412 15.938 12.093 1.00 50.00

ATOM 898 OGl THR 146 2.170 15.249 12.250 1.00 50.00

ATOM 899 CG2 THR 146 4.287 15.218 11.057 1.00 50.00

ATOM 900 OXT THR 146 2.518 16.141 15.215 1.00 99.99

TERM

END

Claims

CLAIMS.

1. A computer-based method for the analysis of the interaction of a ligand with CD44, which comprises: providing the CD44 structure of Table 1 or 2, said Table 1 or 2 being optionally varied by a rmsd of less than 1.5A, or selected co-ordinates thereof; providing a ligand structure to be fitted to said CD44 structure or selected co-ordinates thereof; and fitting the ligand structure to said CD44 structure, wherein said ligand structure is fitted to at least one atom from the amino acids in the group consisting of Arg45, Tyr46, Cys81 , Arg82, Tyr83, Ile92, Asn98, HeIOO, Cys101 , Ala102, Ala103, His105, Tyr109 and Arg155.

2. The method of claim 1 wherein said ligand is fitted to one or more of the following atoms:

3. The method of claim 1 or 2 wherein said ligand is fitted to at least one atom of an amino acid selected from the group consisting of Cys81 , Ile92, Asn98, IleiOO, Cys101 , Ala102 and Ala103.

4. The method of claim 3 wherein said ligand is fitted to at least one atom of an amino acid selected from the group consisting of Cys81, IlelOO, Cys101, Ala102 and Ala103.

5. The method of any one of claims 2 to 4 wherein said ligand is also fitted to at least one atom from Arg45.

6. The method of any one of the preceding claims wherein the CD44 structure is of Table 2 optionally varied by a rmsd of less than 1.5 A, or selected coordinates thereof.

7. The method of claim 6 wherein the CD44 structure is of Table 2 optionally varied by a rmsd of less than 0.5 A, or selected coordinates thereof.

8. A computer-based method for the analysis of the interaction of a ligand with CD44, which comprises: providing the CD44 structure of Table 3 or 4, said Table 3 or 4 being optionally varied by a rmsd of less than 1.5A, or selected co-ordinates thereof; providing a ligand structure to be fitted to said CD44 structure or selected co-ordinates thereof; and fitting the ligand structure to said CD44 structure, wherein said ligand structure is fitted to at least one atom from the amino acids in the group consisting of Arg41 ,Tyr42, Cys77, Arg78, Tyr79, Ile88, Asn94, Ile96, Cys97, Ala98, Ala99, Asn101 , TyM 05 and Arg150.

9. The method of claim 9 wherein said ligand is fitted to one or more of the following atoms:

10. The method of claim 8 or 9 wherein said ligand is fitted to at least one atom of an amino acid selected from the group consisting of Cys77, Ile88, Asn94, Ile96, Cys97, Ala98 and Ala99.

11. The method of claim 10 wherein said ligand is fitted to at least one atom of an amino acid selected from the group consisting of Cys77, Ile96, Cys97, Ala98 and Ala99.

12. The method of any one of claims 9 to 11 wherein said ligand is also fitted to at least one atom from Arg41.

13. The method of any one of claims 8 to 12 wherein the CD44 structure is of Table 4 optionally varied by a rmsd of less than 1.5 A, or selected coordinates thereof.

14. The method of claim 13 wherein the CD44 structure is of Table 4 optionally varied by a rmsd of less than 0.5 A, or selected coordinates thereof.

15. The method of any one of the preceding claims wherein said ligand is a pharmacophore structure comprising three positions arranged to correspond geometrically to the positions of atoms 1188, 1193 and 1196 of Table 1.

16. The method of any one of the preceding claims wherein the ligand is fitted via one or more H-bonds.

17. A computer-based method for the analysis of the interaction of a ligand with LYVE-1 , which comprises: providing the LYVE-1 structure of Table 5 optionally varied by a rmsd of less than 1.5A or selected co-ordinates thereof; providing a ligand structure to be fitted to said LYVE-1 structure or selected coordinates thereof; and fitting the ligand structure to said LYVE-1 structure, wherein said ligand structure is fitted to at least one atom from the amino acids in the group consisting of Cys85, Tyr87, Arg99, Asn103, Lys105, Cys106, Gly107, Lys108 and Trp116.

18. The method of claim 17 wherein said ligand is fitted to at least one atom of an amino acid selected from the group consisting of Cys85, Lys105, Cys106, Gly107 and Lys108.

19. The method of any one of the preceding claims wherein said ligand is fitted to at least one atom from at least 2, preferably at least 5, members of said group.

20. The method of claim 19 wherein said ligand is fitted to at least 5 atoms from at least 5 members of said group.

21. The method of any one of the preceding claims wherein said selected coordinates comprise at least 10 atoms, preferably at least 100 atoms.

22. The method of any one of the preceding claims which further comprises modifying the ligand structure to reduce or increase at least one interaction with the CD44 or LYVE-1 structure.

23. The method of claim 22 which further comprises: obtaining or synthesising a compound which has said ligand structure; forming a complex of a CD44 or LYVE-1 protein and said compound; and analysing said complex by X-ray crystallography to determine the ability of said compound to interact with the CD44 or LYVE-1 protein.

24. A computer system containing computer-readable data comprising atomic co-ordinate data of any one of Tables 1 , 2, 4 or 5 optionally varied by a rmsd of less than 1.5A, or selected co-ordinates thereof.

25. The system of claim 24 wherein said selected co-ordinates are of Table 1 and 2 and include at least one atom from the amino acids Arg45, Tyr46, Cys81 , Arg82, Tyr83, Ile92, Asn98, HeIOO, Cys101 , Ala102, Ala103, His105, Tyr109 and Arg155, or the coordinates are of Table 4 and include at least one atom from the amino acids Arg41 ,Tyr42, Cys77, Arg78, Tyr79, Ile88, Asn94, Ile96, Cys97, Ala98, Ala99, Asn101 , Tyr105 and Arg150.

26. The system of claim 24 or 25 for use in the method of any one of claims 1 to 23.

27. A computer system according to claim 24, 25 or 26:

(i) a computer-readable data storage medium comprising data storage material encoded with said computer-readable data;

(ii) a working memory for storing instructions for processing said computer-readable data; and

(iii) a central-processing unit coupled to said working memory and to said computer- readable data storage medium for processing said computer-readable data and thereby generating structures and/or performing rational drug design.

28. A computer system according to claim 27 further comprising a display coupled to said central-processing unit for displaying said structures.

29. A method of providing data for generating structures and/or performing optimisation of compounds which interact with CD44 or LYVE-1 , or complexes of CD44 or LYVE-1 with ligands, the method comprising:

(i) establishing communication with a remote device containing computer-readable data comprising the structure of Table 1 , 2, 4 or 5 optionally varied by a rmsd of less than 1.5A or selected co-ordinates thereof; and

(ii) receiving said computer-readable data from said remote device.

30. The method of claim 29 wherein said structure is of Table 1 or 2 and the selected coordinates comprise one or more atoms from at least one amino acid from the group consisting of Arg45, Tyr46, Cys81 , Arg82, Tyr83, Ile92, Asn98, MeIOO, Cys101 , Ala102, Ala103, His105, Tyr109 and Arg155, or the structure is of Table 4 and the selected coordinates include at least one or more atoms from at least one amino acid from the group consisting of Arg41 ,Tyr42, Cys77, Arg78, Tyr79, Ile88, Asn94, Ile96, Cys97, Ala98, Ala99, Asn101 , TyM 05 and Arg150.

31. The method of claim 29 wherein said structure is of Table 5 and the selected coordinates comprise one or more atoms from at least one amino acid from the group consisting of Cys85, Tyr87, Arg99, Asn103, Lys105, Cys106, Gly107, Lys108 and Trp116.

32. The method of claim 29, 30 or 31 which further comprises performing the computer- based method of any one of claims 1 to 23.

33. A computer-readable storage medium, comprising a data storage material encoded with computer readable data, the data comprising the structure of any one of Tables 1 , 2 or 4 or 5 optionally varied by a rmsd of less than 1.5A or selected co-ordinates thereof.

34. The computer-readable medium of claim 33, wherein said selected co-ordinates include at least one atom from the amino acids Arg45, Tyr46, Cys81 , Arg82, Tyr83, Ile92, Asn98, HeIOO₁ Cys101 , Ala102, Ala103, His105, Tyr109 and Arg155 of Table 1 or 2, or said selected co-ordinates include at least one atom from the amino acids Arg41 ,Tyr42, Cys77, Arg78, Tyr79, Ile88, Asn94, Ile96, Cys97, Ala98, Ala99, Asn101, TyM 05 and Arg150 of Table 4.

35. A co-crystal of CD44 and HA.

36. The crystal of claim 26 having a P2 space group and unit cell dimensions a=30.8A, /3=82.1 A, c=32.3A, α=90.0°, β=117.9°, γ=90.0°, or a=30.8A, 6=82.1 A, c=32.4A, α=90.0°, β=118.0°, γ=90.0°

37. A method of predicting the HA-binding regions of Link module domain proteins, the method comprises the steps of: aligning a representation of an amino acid sequence of a target Link module domain protein with the amino acid sequence of the CD44 of Table 1 , 2 or 4 to match homologous regions of the amino acid sequences; modelling the structure of the matched homologous regions of said target on the corresponding regions of the CD44 structure; and determining a conformation for said target structure which substantially preserves the structure of said matched homologous regions.

38. The method of claim 28 which further comprises fitting a ligand to said target structure, wherein said ligand is fitted to at least one atom of an amino acid in the target structure homologous to the amino acids Arg45, Tyr46, Cys81 , Arg82, Tyr83, Ile92, Asn98, MeIOO, Cys101 , Ala102, Ala103, His105, TyM 09 and Arg155 of Table 1.

39. The method of claim 37 or 38 wherein said target structure is LYVE-1.