WO2001083769A9 - Crystallization of 4-diphosphocytidyl-2-c-methylerythritol synthesis - Google Patents

Abstract

The present invention provides the structure of the enzyme 4-diphosphocytidyl-2-C-methylerythritol (CDP-ME) synthase, a member of the cytidyltransferase family of enzymes. CDP-ME is a critical intermediate in the mevalonate-independent pathway for isoprenoid biosynthesis in a number of prokaryotic organisms, in algae, in the plastids of plants, and in the malaria parasite. Since vertebrates synthesize isoprenoid precursors using a mevalonate pathway, CDP-ME synthase and other enzymes of the mevalonate-independent pathway for isoprenoid production represent attractive targets for the structure-based design of selective antibacterial, herbicidal, and antimalarial drugs. Accordingly, the present invention provides methods for screening for compounds that inhibit enzymes of the mevalonate-independent pathway and pharmaceutical compositions and antibacterial formulations thereof. Further provided are methods of inhibiting the enzymes of the pathway and bacterial terpenoid synthesis and methods for treating a subject suffering from a bacterial infection.

Description

MODULATION OF MEVALONATE-INDEPENDENT ISOPRENOID BIOSYNTHETIC PATHWAY

RELATED APPLICATIONS

This application claims the benefit of U.S. Provisional Application No. 60/201,589, filed May 3, 2000, and U.S. Provisional Application No. 60/255,088, filed December 12, 2000, the contents of both of which are hereby incorporated by reference herein in their entirety.

ACKNOWLEDGMENT

This invention was made with United States Government support under Grant No. GM-54029, awarded by the National Institutes of Health. The Government has certain rights in the invention.

FIELD OF THE INVENTION

The present invention relates to the structures of crystallized enzymes, methods of identifying enzyme inhibitors, and compositions and methods for the use thereof. In a particular aspect, the invention relates to modulation of the mevalonate- independent isoprenoid biosynthetic pathway for the treatment of bacterial infections.

BACKGROUND OF THE INVENTION

Isopentenyl diphosphate (IPP) and the isomeric compound, dimethylallyl diphosphate (DMAPP) are the fundamental building blocks of isoprenoids in all organisms. The isoprenoids include more than 23,000 naturally occurring molecules of both primary and secondary metabolism (Sacchettini, J.C. & Poulter, CD., 1997). The chemical diversity of this natural product class reflects their wide-ranging physiological roles in all living systems (Connolly, J.D. & Hill, R.A., 1991).' Isoprenoids include hopane triterpenes, ubiquinones and menaquinones in bacteria, carotenoids, plastoquinones, mono-, sesqui-, di-, and tri-terpenes, and the prenyl side chains of chlorophylls in plants, and quinones, dolichols, steroids and retinoids in mammals (Edwards, P.A. & Ericcson, J. 1999).

Until recently it was generally assumed that IPP was derived solely from mevalonate synthesized from the condensation of three molecules of acetyl-CoA (McGarvey, DJ. & Croteau, R., 1995). However, recent independent studies demonstrated the existence of a novel, mevalonate-independent pathway for IPP synthesis known as the 1-deoxy-D-xylulose 5-phosphate / 2-C-methyl-D-erythritol 4- phosphate (DXP/MEP) pathway (Rohmer, M. et al., 1993; Rohmer, M., 1999; Schwender, J. et al, 1996; Eisenreich, W. et al., 1998). This latter mevalonate- independent pathway utilizes pyruvate and glyceraldehyde 3-phosphate as starting materials for production of IPP (Rohmer, M. et al., 1996) (Figure 1).

Since vertebrates synthesize isoprenoid precursors using a mevalonate pathway, enzymes of the mevalonate-independent (DXP/MEP) pathway for isoprenoid production represent attractive targets for the structure-based design of selective pharmaceutical compounds. The DXP/MEP pathway occurs in a variety of eubacteria that includes several pathogenic species such as Mycobacterium tuberculosis, in algae (Rohmer, M., 1999), in the plastids of plant cells (Schwender, J. et al, 1999) and in the apicoplast of Plasmodium falciparum (the parasite that causes malaria) (Jomaa, H. et al, 1999; Vial, H.J., 2000). Given the essential nature of the DXP/MEP pathway in these organisms and the absence of this pathway in mammals, the enzymes comprising the DXP/MEP pathway represent unique targets for the generation of selective antibacterial (Rohmer, M., 1998; Kuzuyama, T. et al, 1998), antimalarial (Jomaa, H. et al, 1999; Vial, H.J., 2000; Ridley, R.G., 1999), and herbicidal (Lichtenthaler, H.K. et al, 2000) molecules.

For example, the YgbP protein of E. coli encodes the enzyme 4- diphosphocytidyl-2-C-methylerythritol (CDP-ME) synthase (Rohdick, F. et al, 1999; Kuzuyama, T. et al, 2000). CDP-ME synthase belongs to the cytidyltransf erase family of enzymes but utilizes a distinct architecture and a novel set of active site residues for CDP-ME formation. CDP-ME is a critical intermediate in the mevalonate-independent pathway for isoprenoid biosynthesis in a number of prokaryotic organisms, in algae, in the plastids of plants, and in the malaria parasite, catalyzing the formation of CDP-ME from 2-C-methyl-D-erythritol-4-phosphate (Koppisch, A.T. et al, 2000) and cytidine tiiphosphate (CTP). Accordingly, there is a need in the art for the three dimensional protein structures of E. coli CDP-ME synthase and related proteins in order to reveal the stereochemical principles underlying substrate recognition and catalysis in CDP-ME synthase.

BRIEF SUMMARY OF THE INVENTION

In accordance with the present invention, the three dimensional atomic resolution structures of E. coli CDP-ME synthase have been solved in the apo form (enzyme alone) and complexed with CTP^»Mg²⁺ and CDP-ME ^«Mg²⁺. These atomic resolution structures reveal active site features responsible for the conformational and stereochemical control of the cytidyltransferase reaction of CDP-ME synthase and serve as three dimensional templates for inhibitor design. The invention reveals the stereochemical principles underlying substrate recognition and catalysis in CDP- ME synthase and provides an understanding of the mechanistic features of this pathway for the design of novel antibacterial and antimalarial agents. Since this pathway does not operate in animal cells, the enzymes which comprise it represent unique and important targets for new medicinal agents identified in accordance with the present invention.

CDP-ME synthase is a functional homodimer in solution (Rohdich, F. et al,

1999) with each polypeptide comprising 237 residues. The E. coli CDP-ME synthase gene was isolated by PCR amplification from total genomic DNA obtained from E. coli K12. The recombinant protein was expressed in E. coli with a thrombin cleavable N-terminal octahistidine tag and purified by Ni²⁺-affinity and gel filtration chromatography. Crystals were readily obtained and the apo structure solved by multiple isomorphous replacement (MIR). Subsequent complexes were obtained using difference Fourier analysis. Mutations of CDP-ME synthase were similarly generated and studied to assess the roles of specific active site residues in the catalytic mechanism of the larger cytidyltransferase family of enzymes.

The present invention provides the first three dimensional view of intermediate formation in the non-mevalonate isoprenoid biosynthesis pathway (DXP/MEP pathway) by solving the three dimensional structures of E. coli CDP-ME synthase complexed with both substrate and product. In another aspect of the present invention, selective mutants have been shown to critically impair the catalytic activity of CDP-ME synthase. In a preferred embodiment of this invention, these structures can be used as structural templates for the identification of effective inhibitors of the DXP/MEP pathway for isoprenoid biosynthesis. Such inhibitors are useful for inhibiting the activity of the target enzyme in a cell-free environment or within a cell, either in vitro or in vivo. In turn, these inhibitors provide novel drugs directed against pathogenic bacteria and the malaria parasite by modulating cell growth via the inhibition of terpenoid synthesis.

BRIEF DESCRIPTION OF THE FIGURES

Figure 1 illustrates the biosynthesis of the isoprenoid precursor IPP via the alternative, non-mevalonate DXP/MEP pathway. The synthesis of the C5 IPP skeleton begins with the condensation of a C2 moiety from the decarboxylation of pyruvate (1) and a C3 moiety from glyceraldehyde 3-phosphate (2), to form 1-deoxy- D-xylulose 5-phosphate (DXP, 3) by the action of DXP synthase (Sprenger, G.A. et al. 1997; Lois, L.M. et al, 1997; Harker, M. & Bramley, P.M., 1999; Lois, L.M. et al, 2000; Kuzuyama, T. et al, 2000) (DXPS; also referred to as DXS). Next DXP is converted into 2-C-methyl-D-erythritol 4-phosphate (MEP, 4) by DXP reductoisomerase (Kuzuyama, T. et al, 1998; Takahashi, S. et al. 1998; Lange B.M. & Croteau, R., 1999; Kuzuyama, T. et al, 2000) (DXPR; sometimes referred to as DXR), and subsequently transformed into 4-diphosphocytidyl-2-C-methyl-D-erythritol (CDP-ME, 5) by CDP- ME synthase (Rohdich, F. et al, 1999; Kuzuyama, T. et al, 2000; Rohdich, F. et al, 2000) (YgbP protein) in a Mg²⁺ and CTP dependent reaction. CDP-ME is phosphorylated on the 2-hydroxy group to form 4-diphosphocytidyl-2-C-methyl-D- erythritol 2-phosphate (CDP-MEP, 6) in an ATP-dependent reaction by the enzyme CDP-ME kinase encoded by the yclϊB gene of E. coli (Luttgen, H. et al, 2000; Kuzuyama, T. et al, 2000). Subsequent formation of 2-C-methyl-D-erythritol 2,4- cyclodiphosphate (7) is catalyzed by the enzyme MECDP synthase encoded by the gene ygbB (Herz, S. et al, 2000; Takagi, M. et al, 2000). Additional steps, which remain to be elucidated, ultimately form isopentenyl diphosphate (IPP, 8).

Figures 2A and 2B collectively depict the overall architecture of E. coli CDP- ME synthase and Neisseria meningitidis CMP-NeuAc synthetase (CMP acyl neuraminate synthetase). The molecules are shown as a ribbon representation of the homodimers complexed with CTP»Mg²⁺. The secondary structure is annotated according to the cytidyltransf erases nomenclature which is based on the CMP- NeuAc synthetase structure aligned with CDP-ME synthase, depicted in Figure 2B. A partially disordered CDP acting as a substrate analog is also shown in Figure 2B.

Figure 3 provides a combined surface and ribbon view of CDP-ME synthase complexed with CDP-ME ^#Mg²⁺. The molecular surface representation of monomer A (left) was calculated with GRASP (Esnouf, R., 1997). Monomer B (right) is represented in ribbon mode, with the side chains of Thr 140 and Arg 157 shown as rendered sticks. This orientation is derived from the view depicted in Figure 2 after a 180 degree rotation around the horizontal axis.

Figure 4 depicts a family of cytidyltransf erases as a topology diagram for GCT (CTP:glycerol-i3-phosphate cytidyltransferase), CDP-ME synthase (ygbP) and CMP-NeuAc synthetase monomers. The diagram was generated with TOPS (Westhead, D.R. et al, 1999); helices are represented as circles and β-strands as triangles.

Figure 5 presents evidence of contrasting CTP binding modes in GCT and CDP-ME synthase. In CDP-ME synthase, CTP binds on the top of βl with the triphosphate arm resting against the P-loop and the cytosine base residing against the β5-αE loop. In GCT, CTP binds on the top of β4 with the triphosphate moiety contacting the β5-αE loop and the cytosine base in contact with the β5-αE loop. The overall orientation of CDP-ME synthase depicted is derived from the view shown in Figure 2A following a 90 degree clockwise rotation in the plane of the figure and a 45 degree rotation around the horizontal axis. In GCT, His 14 and His 17 form hydrogen bonds with the α- and β-phosphate oxygens, respectively (Weber, CH. et al, 1999). Lys 27 and Lys 213 of CDP-ME synthase are spatially equivalent to His 14 and His 17 of GCT.

Figure 6 provides a schematic representation of the CTP»Mg²⁺ binding site of the CDP-ME synthase active site, showing the hydrogen and coordination bonds to CTP and Mg²⁺, respectively.

Figure 7 provides a schematic representation of the CDP-ME»Mg²⁺ binding site of the CDP-ME synthase active site. Recognition of the CDP-ME product is accomphshed using an extensive set of hydrogen-bonding interactions that includes residues from both polypeptide chains of the CDP-ME synthase homodimer. This subset of interactions partially maps the putative MEP binding site in CDP-ME synthase. The carboxyl group of Asp 106 forms a hydrogen bond with the C2 hydroxyl group of the MEP portion of CDP-ME, the backbone amide of Thr 140 from the dyad related monomer hydrogen bonds with the Cl hydroxyl group of CDP-ME, and the side chain δ-guanido group of Asp 157 from the dyad related monomer provides hydrogen bonds to both the C3 hydroxyl group and two phosphate oxygens of MEP.

Figures 8A-8E collectively provide a rendered view of the ground state complexes of CDP-ME synthase. The apo form of CDP-ME synthase is shown in Figure 8A, the CTP«Mg²⁺ complex in Figure 8B and the CDP-ME»Mg²⁺ complex in Figure 8E. The model for the MEP«CTP«Mg²⁺ complex shown in Figure 8C is based on the observed positions of CTP and the MEP-derived portion of CDP-ME. The model for the product complex that includes diphosphate (PPi) shown in Figure 8D is based on the observed position of the β and γ phosphates of CTP. These close-up views are shown in an orientation identical to the views depicted in Figure 3. Figure 9 illustrates a putative role of side chains in the catalytic mechanism of CDP-ME synthase. The curved black arrows represent hypothetical electron flow during both the nucleophilic attack on the CTP α-phosphate as well as the breakdown of the putative pentacoordinate transition state.

Figure 10 provides a model for the same reaction pathway as shown in Figure 9, in CMP-NeuAc synthetase based upon the chemical equivalence of portions of the MEP substrate of CDP-ME synthase and the acymeurarninate substrate of CMP- NeuAc synthetase. Notably, Asp 209, which is equivalent to Lys 213 in CDP-ME synthase, is ideally positioned to act as a general base next to the 2-OH group of acylneuraminate in CMP-NeuAc synthetase.

DETAILED DESCRIPTION OF THE INVENTION

In accordance with the present invention, there are provided compositions comprising 4-diphosphocytidyl-2-C-methylerythritol synthases (CDP-ME synthase) in crystalline form. In accordance with another embodiment of the present invention, the high resolution structures of CDP-ME synthases complexed with CTP^»Mg²⁺ and CDP-ME ^»Mg²⁺ are described, providing compositions comprising a substrate, substrate r irnic or inhibitor of CDP-ME synthase. The discovered structure of a CDP-ME synthase provides the first three dimensional view of the structural basis for intermediate formation in the DXP/MEP pathway for isoprenoid biosynthesis using a mevalonate-independent pathway. The structures of CDP-ME synthase complexed with CTP • Mg²⁺ and CDP-ME • Mg²⁺ respectively, reveal the stereochemical principles underlying both substrate and product recognition as well as catalysis in CDP-ME synthase.

In accordance with the present invention, the apo form of CDP-ME synthase has been refined to 1.55 A resolution, the complex with CTP • Mg²⁺ to 1.5 A resolution (Figure 2), and the complex with CDP-ME »Mg²⁺ to 1.81 A resolution (Figure 3). YgbP crystals belong to space group C2 with one subunit per asymmetric unit and cell parameters of about a = 130.6 A, b = 47.1 A, c = 38.1 A and β= 94 °. The complete X-ray data coordinates for the apo form of CDP-ME synthase are set forth in Appendix 1; for the complex with CTP^#Mg²⁺ in Appendix 2; and for the complex with CDP-ME »Mg²⁺ in Appendix 3.

The crystallographic data for CDP-ME synthase used for phasing and refinement follows in Tables 1 and 2. Diffraction data was collected on a single crystal grown from SeMet containing CDP-ME synthase co-crystallized with CTP, to a resolution of 1.5 A (Table 1). A single crystal of CDP-ME synthase was co- crystallized with CTP to a resolution of 1.5 A, co-crystallized with MEP (referred to as the apo form) to a resolution of 1.55 A, and co-crystallized with CDP-ME to a resolution of 1.81 A, all on a 180/345 mm MAR imaging plate system detector (Table 2).

Table 1 Crystallographic data used for phasing

Native SeMet,λl SeMet,λ2 SeMet,λ3 Hg₂(OAc) KAu(CN₄)

Wavelength (A) 0.9848 0.9797 0.9795 0.8952 1.5418 1.5418

Resolution (A) 90-1.24 90-1.35 90-1.35 90-1.35 90-1.65 90-1.75

Unique reflections¹ 59518 94279 93977 94976 51709 41116

(1539) (4556) (4277) (4529) (1714) (1502)

Completeness ¹(%) 86.4 94.5 94.2 95.2 94.6 91.7

(44.9) (91.4) (85.8) (90.3) (64.3) (66.3)

I/σl¹ 22.5 (2.3) 20.1 (1.8) 20.8 (1.8) 19.7 (1.5) 33 (3) 27.4 (2.5)

Rs m ' (%) 3.5 (37.9) 2.7 (35.6) 2.6 (35.8) 2.9 (43.2) 3.4 (34.0) 3.1 (31.0)

No of sites 4 5

Phasing power³ centric iso 0.626 1.466 acentric iso 1.384 1.066 acentric ano 1.184 0.806 l^cullis centric iso 0.846 0.911 acentric iso 0.815 0.917 acentric ano 0.715 0.831

'Number in parenthesis is for highest resolution shell.

²R-sym ⁼ Σ_h|Ih " "^ H / Σ_h0h)_> where <I > is the average intensity over symmetry equivalent reflections.

³Phasing power = <|Fjj(_caι_c)| / |E|>, where Fπ(calc) is the calculated difference and E is the estimated lack-of- closure error, where iso is isomorphous and ano is anomalous.

⁴Rcullis = Σ|E| / ∑|Fp_H - Fp|.

Table 2 Crystallographic data and refinement statistics

CTP^»Mg^z+ Apo CDP-ME*Mg .^'2+

Wavelength (A) 1.08 1.08 0.773

Resolution (A) 90 - 1.5A 90 - 1.55 90 - 1.81

Unique reflections 34216 (1353) 30652 (880) 20268 (641)

Redundancy 4.7 (3.9) 3.2 (2.1) 2.8 (2.9)

Completeness¹ (%) 92.2 (72.6) 90.3 (51.8) 98.6 (98.6)

I/σ¹ 25.6 (1.9) 32.7 (6) 26.4 (2.7)

Rsym ' (%) 4.5 (34.5) 2.6 (13.4) 2.6 (30.8)

Rcryst / Rfree (%) 22.7 / 24.8 24.6 / 26.8 23.0 / 28.8

Missing residues [1-4] [1-4], [16-27] [1-4]

[229-236] [229-236] [229-236]

Protein atoms 1713 1625

Water molecules 328 370 96

Ions bound l Mg²⁺ l Ca²⁺ l Mg²⁺ l Ca²⁺

Ligand atoms⁵ 29 0 33

R.m.s.d. bonds (A) 0.0092 0.0051 0.0068

R.m.s.d. angles (°) 1.535 1.23 1.20

Average B-factor (A²)

Protein 24.9 25.6 35.0

Water 38.3 39.8 43.5

Ligand 32.3 30.0

dumber in parenthesis is for highest resolution shell.

²R-sym ⁼ ∑_bKh " ^<^h^>l / ∑ι h_> where </_n> is the average intensity over symmetry equivalent reflections.

³Rcryst ⁼ Σ|F₀bs - Fcaicl / ∑F₀bs_> where summation is over the data used for refinement.

⁴R_ftee factor is R^_t calculated using 5% of data (test set) excluded from refinement.

⁵Ligand atoms refer to a CTP molecule in the CTP«Mg²⁺ complex and to a CDP-ME molecule in the CDP-

ME'Mg -2+ complex. One aspect of the invention resides in obtaining crystals of an enzyme of the DXP/MEP pathway for isoprenoid biosynthesis of sufficient quality to determine the three dimensional structure of the protein by X-ray diffraction methods. X-ray crystallography is a method of solving the three dimensional structures of molecules. The structure of a molecule is calculated from X-ray diffraction patterns using a crystal as a diffraction grating. Three dimensional structures of protein molecules arise from crystals grown from a concentrated solution of that protein. The process of X-ray crystallography can include the following steps:

(a) synthesizing and isolating a polypeptide; (b) growing a crystal from a solution comprising the polypeptide with or without a compound, modulator, ligand, or ligand analog; and

(c) collecting X-ray diffraction patterns from the crystals, deterrruning unit cell dimensions and symmetry, determining electron density, fitting the amino acid sequence of the polypeptide to the electron density, and refining the structure.

The term "crystalline form" refers to a crystal formed from a solution comprising a purified polypeptide corresponding to all or part of CDP-ME synthase. In preferred embodiments, a crystalline form may also be formed from a purified polypeptide corresponding to all or part of CDP-ME synthase in a complex with one or more substrates, substrate rrtirnics or inhibitors of CDP-ME synthase.

The term "substrate" refers to a compound whose activity is typically enhanced by an enzyme. Enzymes can catalyze a specific reaction on a specific substrate. For example, CDP-ME synthase can catalyze the formation of CDP-ME from 2-C-methyl-D-erythritol-4-phosphate and CTP. The term "substrate mimic" refers to a compound that is structurally similar, but not identical, to a substrate. The term "inhibitor" refers to a compound causes inhibition of one or more biochemical events which the enzyme may catalyze.

The term "X-ray coordinates" or "X-ray data coordinates" as used herein refers to a data set that defines the three dlrnensional structure of a molecule, for example, as set forth in Appendices 1, 2 and 3. The data sets are derived from mathematical equations related to the patterns obtained on diffraction of a monochromatic beam of X-rays by the atoms (scattering centers) of a protein molecule in crystal form. The diffraction data are used to calculate an electron density map of the repeating unit of the crystal cell. Structural coordinates can be slightly modified and still render nearly identical three dimensional structures. A measure of a unique set of structural coordinates is the root-mean-square (r.m.s.) deviation of the resulting structure. Structural coordinates that render three dimensional structures that deviated from one another by a r.m.s. deviation of less than about 1.5 A may be viewed by a person of ordinary skill in the art as identical since they have little effect on the overall structure, and would not significantly alter the nature of binding associations. Furthermore, those of skill in the art understand that a set of coordinates for an enzyme or complex thereof, is a relative set of points that define the three dimensional shape of said enzyme or enzyme complex. As such, it is possible that an entirely different set of coordinates could define a similar or identical shape. Hence, the structural coordinates set forth in Tables 1 and 2, and Appendices 1, 2 and 3 are not limited to the express values set forth therein.

The use of X-ray crystallography can elucidate the three dimensional structure of crystalline forms according to the invention. Typically, the first characterization of crystalline forms by X-ray crystallography can determine the unit cell shape and its orientation in the crystal. The term "unit cell" refers to the smallest and simplest volume element of a crystal that is completely representative of the unit of pattern of the crystal. The dimensions of the unit cell are defined by six numbers: dimensions a, b and c and angles α, β and γ. A crystal can be viewed as an efficiently packed array of multiple unit cells. Detailed descriptions of crystallographic terms are described in Hahn, 1996, Tlie International Tables for Crystallography, Volume A, Fourth Edition, Kluwer Academic Publishers; and Shmueli, Tlie International Tables or Crystallography, Volume B, First Edition, Kluwer Academic Publishers. The term "space group" refers to the symmetry of a unit cell. In a space group designation (e.g., C2) the capital letter indicates the lattice type and the other symbols represent symmetry operations that can be carried out on the unit cell without changing its appearance. The knowledge obtained from X-ray diffraction patterns can be used in the determination of the three dimensional structure of the binding sites of other homologous enzymes. This is achieved through the use of commercially available software known in the art that is capable of generating three dimensional graphical representations of molecules or portions thereof from a set of structure coordinates. The binding domain can also be predicted by various computer models. Based on the structural X-ray coordinates of the solved structure, small molecules which mimic the functional binding of an enzyme to its substrate can be designed and synthesized as potential drugs. Another approach to such "rational" drug design is based on a lead compound that is discovered using high throughput screens; the lead compound is further modified based on a crystal structure of the binding regions of the molecule in question using the points of interaction between the compound and target molecule.

Accordingly, in one embodiment of the present invention, there is provided a computer for producing a three-dimensional representation of a molecule or molecular complex or a homologue of said molecule or molecular complex, wherein said molecule or molecular complex or a homologue of said molecule or molecular complex comprises an active site defined by structure coordinates of Appendix 1, 2 or 3, wherein said computer comprises:

(i) a computer-readable data storage medium comprising a data storage material encoded with computer-readable data, wherein said data comprises the structure coordinates of Appendix 1, 2 or 3; (ii) a working memory for storing instructions for processing said computer-readable data;

(iii) a central-processing unit coupled to said working memory and to said computer-readable data storage medium for processing said computer-machine readable data into said three-dimensional representation; and

(iv) a display coupled to said central-processing unit for displaying said three-dimensional representation. According to an alternative embodiment there is provided a computer for deterrrviriing at least a portion of the structure coordinates corresponding to X-ray diffraction data obtained from a molecule or molecular complex or a homologue of said molecule or molecular complex, wherein said computer comprises:

(i) a computer-readable data storage medium comprising a data storage material encoded with machine-readable data, wherein said data comprises at least a portion of the structural coordinates of Appendix 1, 2 or 3; (ii) a computer-readable data storage medium comprising a data storage material encoded with computer-readable data, wherein said data comprises X-ray diffraction data obtained from said molecule or molecular complex or a homologue of said molecule or molecular complex;

(iii) a working memory for storing instructions for processing said computer-readable data of (i) and (ii);

(iv) a central-processing unit coupled to said working memory and to said computer-readable data storage medium of (i) and (ii) for performing a Fourier transform of the machine readable data of (i) and for processing said computer-readable data of (ii) into structure coordinates; and (v) a display coupled to said central-processing unit for displaying said structure coordinates of said molecule or molecular complex.

The term "computer" as used herein can be composed of a central processing unit (for example, the Pentium III from Intel Corporation, or similar processor from Sun, Motorola, Compaq, AMD or International Business Machines, and the like), a working memory which may be random-access memory or core memory, mass storage memory (for example, one or more floppy disk drives, compact disk drives or magnetic tape containing data recorded thereon), at least one display terminal, at least one keyboard and accompanying input and output devices and connections therefor. The computer typically includes a mechanism for processing, accessing and manipulating input data. A skilled artisan can readily appreciate that any one of the currently available computer systems are suitable. It should also be noted that the computer can be linked to other computer systems in a network or wide area network to provide centralized access to the information contained within the computer.

Contemplated input devices for entering machine readable data include, for example, telephone modem lines, cable modems, CD-ROMs, a keyboard or disk drives. The computer may advantageously include or be programmed with appropriate software for reading the data from the data storage component or input device, for example computational programs for use in rational drug design that are described in detail below. Contemplated output devices include conventional systems known in the art, for example, display terminals, printers, or disk drives for further storage of output.

In a further embodiment of the present invention, there are provided methods for screening for compounds that inhibit the mevalonate-independent isoprenoid biosynthesis pathway. These methods comprise deterrriining the points of interaction between any one or more enzymes in this pathway, with a substrate or substrate mimic therefor; selecting compound(s) having similar interaction with said one or more enzymes; and testing the selected compound for the ability to inhibit the activity of any one or more enzymes in the non-mevalonate isoprenoid biosynthesis pathway.

The term "points of interaction" refers to hydrophobic, aromatic, and ionic forces and hydrogen bonds formed between atoms. Such interactions can be "intramolecular," or within the same molecule, or "intermolecular," or between separate molecules. Compounds with similar points of interaction are preferably selected by docking a three dimensional representation of a structure of a compound with a three dimensional representation of the target enzyme in the non-mevalonate isoprenoid biosynthesis pathway, for example, CDP-ME synthase. The computer representation of the target enzyme can be defined in a variety of ways, for example, by atomic X-ray coordinates. For example, from the crystal structure of CDP-ME synthase it was determined that CTP and CDP-ME are sequestered by a glycine rich loop spanning Pro 13 to Arg 20. Selectivity for the pyrimidine base is achieved through hydrogen bonding interactions and steric constrictions in the base-binding pocket, which do not allow for the sequestration of larger purine bases (Weber, CH. et al, 1999). This selectivity is specifically achieved through hydrogen bonds formed between the backbone amides of Ala 14 and Ala 15, the carbonyl oxygens of Gly 82 and Asp 83, and the hydroxyl group of Ser 88. The cytosine base is stacked between the flexible loop spanning βl and β2, and the methylene portion of the Arg 85 side chain projecting outward from the β5-αE catalytic loop. The 2' and 3' hydroxyl groups of the ribose moiety are involved in backbone hydrogen bonding interactions with Pro 13, Gly 16, and Ala 107 (Figures 6 and 7).

Furthermore, the main chain monomers of CDP-ME synthase superpose with a root mean square (r.m.s) deviation of 0.264 A, 0.773 A, and 0.754 A between the apo and CTP»Mg²⁺, apo and CDP-ME'Mg²⁺, and CTP»Mg²⁺ and CDP-ME^«Mg²⁺ bound forms, respectively. The largest backbone differences occur in the loop linking βl and β2 supporting the Sio-helices, Al and A2. In CMP-NeuAc synthetase, this so- called P-loop (Mossimann, S.C. et al., 2000) responsible for phosphate recognition, together with the residues following β5, enclose the mononucleotide binding pocket. In CDP-ME synthase, the P-loop comprising residues 17-25 is not defined in the apo form and poorly defined in the CDP-ME^»Mg²⁺ complex. In both CDP-ME synthase and CMP-NeuAc synthetase, the P-loop undergoes a dramatic ordering upon binding of CDP in CMP-NeuAc synthetase or CTP^»Mg²⁺ in CDP-ME synthase. The rest of the nucleotide binding pocket responsible for base recognition and ribose binding are well defined in the electron density maps of the apo form and both the CTP^»Mg²⁺ and CDP-ME^»Mg²⁺ complexes.

In addition, the side chain amino group of Lys 27 is in direct contact with the α-phosphates of CTP and CDP-ME (Figure 6). Arg 20 through both its backbone amide and its side chain δ-guanido moiety forms an elaborate series of hydrogen bonding interactions with the α and γ phosphate oxygens (Figure 6). Given their positions near the α-phosphate of CTP, their absolute conservation in the CDP-ME enzyme family, and the potential accumulation of negative charges in the pentacoordinate transition state for CDP-ME formation, Arg 20 and Lys 27 may play important roles in transition state stabilization during CDP-ME formation.

Mg²⁺, which is essential for cytidyltransferase activity (Rohdich, F. et al., 1999), forms coordination bonds with the α, β, and γ phosphate oxygens of CTP and the α phosphate oxygen of CDP-ME. The Mg²⁺ ion coordinates with regular octahedral geometry to CTP with water molecules occupying the coordination sites not occupied by the phosphate oxygens. No coordination bonds between CDP-ME synthase and Mg ⁺ occur in any of the complexes examined to date. Lys 213, together with Arg 157 from the dyad related subunit, does not participate in hydrogen bonds with CTP, but both are in direct contact with the MEP derived portions of CDP-ME (Figure 7).

Thus, the structural analysis of the substrate and product complexes suggest that MEP does not bind in the absence of CTP as all attempts to obtain an MEP complex in the absence of CTP failed to reveal any density in the CDP-ME synthase active site. In cytidyltransferases, as in class I aminoacyl-tRNA synthetases, the CTP or ATP substrates bind first followed by the second substrate prior to product formation through a pentacoordinate (associative mechanism) transition state (Veitch, D.P. & Cornell, R.B., 1996; Veitch, D.P. et al, 1998). The MEP-derived portion of the CDP-ME molecule contacts the protein through hydrogen bonds between MEP's three hydroxyl groups and the side chain carboxyl group of Asp 106, the δ-guanido moiety of Arg 109, the main chain amide of Thr 140, and the side chain δ-guanido moiety of Arg 157. Finally, the C4 methyl group of CDP-ME is nestled in a hydrophobic pocket formed by the side chain methyl groups of Thr 165 and Ala 163 (Figure 7). Notably, it is the polypeptide chain of the dyad related subunit which contains Thr 140 and Arg 157. Methods of using crystal structure data to design inhibitors of enzyme activity are known in the art. Thus, the crystal structure data provided herein can be used in the design of new or improved enzymatic inhibitors. For example, the CDP- ME synthase binding site X-ray coordinates, provided herein, can be superimposed onto other available coordinates of similar enzymes which have inhibitors bound to them to give an approximation of the way these and related inhibitors might bind to CDP-ME synthase. Alternatively, computer programs employed in the practice of rational drug design can be used to identify compounds that reproduce interaction characteristics similar to those found between the enzyme and its substrate or product. For, example, the CDP-ME synthase coordinates when complexed with CTP^»Mg²⁺ and CDP-ME ^»Mg²⁺, provided herein, can be used to model beneficial points of interaction in a potential drug compound. Furthermore, detailed knowledge of the nature of binding site interactions allows for the modification of compounds to alter or improve solubility, pharmokinetics, etc. without affecting binding activity.

Computer programs are widely available that are capable of carrying out the activities necessary to design compounds using the crystal structure information provided herein. Examples include, but are not limited to, the computer programs listed below:

Catalyst Databases™ - an information retrieval program accessing chemical databases such as BioByte Master File, Derwent WDI and ACD; Catalyst/ HYPO™ - generates models of compounds and hypotheses to explain variations of activity with the structure of drug candidates; Ludi™ - fits molecules into the active site of a protein by identifying and matching complementary polar and hydrophobic groups;

Leapfrog™ - "grows" new Hgands using an algorithm with parameters under the control of the user.

In addition, various general purpose machines may be used with programs written in accordance with the teachings herein, or it may be more convenient to construct more specialized apparatus to perform the operations. However, preferably this is implemented in one or more computer programs executing on programmable systems each comprising at least one processor, at least one data storage system (including volatile and non-volatile memory and/ or storage elements), at least one input device, and at least one output device. The program is executed on the processor to perform the functions described herein.

For the first time, the present invention permits the use of molecular design techniques to design, select and synthesize chemical entities and compounds, including inhibitory compounds, capable of binding to the active site of the enzymes of the mevalonate-independent isoprenoid biosynthetic pathway.

One approach contemplated by this invention is to use the structure coordinates set forth in Appendices 1, 2 and 3 to design compounds that bind to the enzyme and alter the physical properties of the compounds in different ways, e.g., solubility. For example, this invention enables the design of compounds that act as competitive inhibitors of CDP-ME synthase by binding to the identified active site. In another approach, the active site of a crystal of an enzyme is probed with molecules composed of a variety of different chemical entities to deterrnine optimal sites for interaction. For example, these molecules could mimic substrate compounds, or enzyme inhibitors.

In another embodiment, an approach made possible and enabled by this invention is to screen computationally small molecule data bases for chemical entities or compounds that can bind to the active site of a target enzyme. In this screening, the quality of fit of such entities or compounds to the binding site may be judged either by shape complementarity or by estimated interaction energy (Meng, E. C. et al, 1992).

In addition, in accordance with the present invention, enzyme mutants may be crystallized in co-complex with known binding agents, substrates, or inhibitors. The crystal structures of a series of such complexes may then be solved by molecular replacement and compared with that of a wild-type enzyme. Potential sites for modification within the enzyme's active site may thus be identified. This information provides an additional tool for determining the most efficient bmding interactions, for example, increased hydrophobic interactions, between an active site residue and a chemical entity or compound.

All of the complexes referred to above may be studied using well-known X-ray diffraction techniques and may be refined versus 2-3 A resolution X-ray data to an R value of about 0.20 or less using computer software, such as X-PLOR (Yale University, 1992, distributed by Molecular Simulations, Inc.). See, e.g., Methods in Enzymology, 1985). This information may thus be used to optimize known classes of enzyme binding agents (e.g., inhibitors), and to design and synthesize novel classes of active site agents (e.g., inhibitors).

The design of binding agents that bind or otherwise associate with or inhibit the active site of an enzyme according to the invention generally involves consideration of two factors. First, the compound or binding agent must be capable of physically and structurally associating with the target enzyme. Non-covalent molecular interactions important in the association of an enzyme with a substrate include hydrogen bonding, van der Waals and hydrophobic interactions.

Second, the compound or binding agent must be able to assume a conformation that allows it to associate with the active site. Although certain portions of the compound or binding agent will not directly participate in this association, those portions may still influence the overall conformation of the molecule. This, in turn, may have a significant impact on potency. Such conformational requirements include the overall three-dimensional structure and orientation of the chemical entity or compound in relation to all or a portion of the bmding site, or the spacing between functional groups of a compound comprising several chemical entities that directly interact with an active site.

The potential inhibitory or binding effect of a chemical compound on an active site may be analyzed prior to its actual synthesis and testing by the use of computer modeling techniques. If the theoretical structure of the given compound suggests insufficient interaction and association between it and the active site, synthesis and testing of the compound may be obviated. However, if computer modeling indicates a strong interaction, the molecule may then be tested in efforts to confirm its ability to bind to the target enzyme. Methods of assaying for enzymatic activity are known in the art. Methods for assaying the effect of a potential binding agent can be performed in the presence of a known binding agent of the target enzyme. For example, the effect of the potential binding agent can be assayed by measuring the ability of the potential binding agent to compete with a known binding agent.

An inhibitory or other binding compound of the target enzyme may be computationally evaluated and designed by means of a series of steps in which chemical entities or fragments are screened and selected for their ability to associate with the individual binding pockets or other areas of the active site of the target enzyme.

One skilled in the art may use one of several methods to screen chemical entities or fragments for their ability to associate with the target active site. This process may begin by visual inspection of, for example, the active site on the computer screen based on the X-ray coordinates of the enzyme. Selected fragments or chemical entities may then be positioned in a variety of orientations, or docked, within an individual binding pocket of an active site. Docking may be accomplished using software such as Quanta and Sybyl, followed by energy miriimization and molecular dynamics with standard molecular mechanics forcefields, such as CHARMM and AMBER.

Specialized computer programs may also assist in the process of selecting fragments or chemical entities. These include:

1. GRID (Goodford, P. J., 1985). GRID is available from Oxford University, Oxford, UK.

2. MCSS (Miranker, A. and Karplus,M., 1991). MCSS is available from Molecular Simulations, Burlington, Mass. 3. AUTODOCK (Goodsell, D. S. and Olsen, A. J., 1990). AUTODOCK is available from Scripps Research Institute, La Jolla, Calif. 4. DOCK (Kuntz, I. D. e£βZ., 1982). DOCK is available from University of California, San Francisco, Calif.

Once suitable chemical entities or fragments have been selected, they can be assembled into a single compound or binding agent (e.g., an inhibitor). Assembly may be performed by visual inspection of the relationship of the fragments to each other on the three-dimensional image displayed on a computer screen in relation to the structure coordinates of the enzyme. This would be followed by manual model building using software such as Quanta or Sybyl.

Useful programs to aid one of skill in the art in connecting the individual chemical entities or fragments include:

1. CAVEAT (Bartlett, P. A. et al, 1989). CAVEAT is available from the University of California, Berkeley, Calif. 2. 3D Database systems such as MACCS-3D (MDL Information Systems, San

Leandro, Calif.). This area is reviewed in Martin, Y. C, 1992).

3. HOOK (available from Molecular Simulations, Burlington, Mass.).

In addition to the method of building or identifing a binding agent in a step- wise fashion one fragment or chemical entity at a time as described above, inhibitory or other active site binding compounds may be designed as a whole or "de novo" using either an empty active site or optionally including some portion(s) of a known inhibitor(s). These methods include:

1. LUDI (Bohm, H.-J., 1992). LUDI is available from Biosym Technologies, San Diego, Calif.

2. LEGEND (Nishibata, Y. and Itai, A., 1991). LEGEND is available from Molecular Simulations, Burlington, Mass.

3. LeapFrog (available from Tripos Associates, St. Louis, Mo.).

Other molecular modeling techniques may also be employed in accordance with this invention. See, e.g., Cohen, N. C. et al, 1990. See also, Navia, M. A. and Murcko, M. A., 1992. Once a compound or binding agent has been designed or selected by the above methods, the efficiency with which that compound may bind to an enzyme's active site may be tested and optimized by computational evaluation.

A compound designed or selected as an active site binding agent may be further computationally optimized so that in its bound state it would preferably lack repulsive electrostatic interaction with the target site. Such non-complementary (e.g., electrostatic) interactions include repulsive charge-charge, dipole-dipole and charge- dipole interactions. Specifically, the sum of all electrostatic interactions between the binding agent and the active site when the bmding agent is bound to it, preferably make a neutral or favorable contribution to the enthalpy of binding.

Specific computer software is available in the art to evaluate compound deformation energy and electrostatic interaction. Examples of programs designed for such uses include: Gaussian 92, revision C (M. J. Frisch, Gaussian, Inc., Pittsburgh, Pa., 1992); AMBER, version 4.0 (P. A. Kollman, University of California at San Francisco, 1994); QUANTA/ CHARMM (Molecular Simulations, Inc., Burlington, Mass. 1994); and Insight π/ Discover (Biosysm Technologies Inc., San Diego, Calif., 1994). These programs may be implemented, for example, using a Silicon Graphics workstation, IRIS 4D/35 or IBM RISC/ 6000 workstation model 550. Other hardware systems and software packages will be known to those skilled in the art of which the speed and capacity are continually modified.

Once an active site binding agent has been selected or designed, as described above, substitutions may then be made in some of its atoms or side groups in order to improve or modify its binding properties. Generally, initial substitutions are conservative, e.g., the replacement group will have approximately the same size, shape, hydrophobicity and charge as the original group. Such substituted chemical compounds may then be analyzed for efficiency of fit to an active site by the same computer methods described above. In accordance with another aspect of the present invention, there are provided methods for inhibiting the activity of any one or more enzymes in the non- mevalonate isoprenoid biosynthesis pathway comprising contacting said one or more enzymes with an effective amount of an inhibitory compound in a cell-free environment or in a cell. Such cellular contact may be in vitro or in vivo. In a preferred embodiment of the invention, the cell's growth is modulated by contact with the inhibitory compound. In another preferred embodiment of the invention, the cell is a bacterial cell.

The term "growth of the cell" refers to the rate at which a cell divides. A compound can modulate growth by either increasing or decreasing cell division rates. Cell division rates can be readily measured by methods known in the art.

In accordance with another embodiment of the present invention there are provided compounds identified as inhibitors of the mevalonate-independent isoprenoid biosynthesis pathway and pharmaceutical compositions thereof in a pharmaceutically acceptable carrier. In a preferred embodiment of the invention there is provided an antibacterial formulation containing at least one inhibitory compound in a suitable carrier.

In accordance with yet another aspect of the present invention, there are provided methods for inhibiting bacterial terpenoid synthesis comprising contacting bacteria with an effective amount of at least one inhibitory compound.

The term "effective amount" as used herein refers to the amount of inhibitor required to biologically inhibit terpenoid synthesis via inhibition of any enzyme involved along the mevalonate-independent isoprenoid biosynthetic pathway.

In accordance with yet another aspect of the present invention, there are provided methods for treating a subject suffering from a bacterial infection. These methods comprise administering to the subject an effective amount of at least one inhibitory compound. In a preferred embodiment of the present invention, the subject is suffering from an E. coli infection or a streptococcal infection.

Bacterial infections contemplated for treatment using invention compounds and methods include infections caused by both gram-positive and gram-negative bacteria, including infections caused by Staphylococcus, Clostridium, Streptococcus, Enterococcus, Diplococcus, Hemophilus, Neisseria, Erysipelothricosis, Listeria, Bacillus, Salmonella, Shigella, Escherichia, Klebsiella, Enterobacter, Serratia, Proteus, Morganella, Providencia, Yersinia, Camphylobacter, Mycobacteria, and the like. Infection by such organisms causes a wide variety of disorders including pneumonia, diarrhea and dysentery, anthrax, rheumatic fever, toxic shock syndrome, mastoiditis, meningitis, gonorrhea, typhoid fever, gastroenteritis, brucellosis, cholera, bubonic plague, tetanus, tuberculosis, Lyme disease, and the like.

The particular invention compound(s) selected for therapeutic use as taught herein can be administered to a subject either alone or in a pharmaceutical composition where the compound(s) is mixed with suitable carriers or excipient(s). In treating a subject, a therapeutically effective dose of compound (i.e., active ingredient) is administered. A therapeutically effective dose refers to that amount of the active ingredient that produces ameUoration of symptoms or a prolongation of survival of a subject.

Toxicity and therapeutic efficacy of a compound can be determined by standard pharmaceutical procedures in cell culture or experimental animals. Cell culture assays and animal studies can be used to determine the LD50 (the dose lethal to 50% of a population) and the ED50 (the dose therapeutically effective in 50% of a population). The dose ratio between toxic and therapeutic effects is the therapeutic index, which can be expressed as the ratio LD50/ED50. Compounds which exhibit large therapeutic indices are preferred. The data obtained from these cell culture assays and animal studies can be used in formulating a range of dosages suitable for use in humans. The dosage of such compounds lies preferably within a range of circulating concentrations that include the ED₅₀ with little or no toxicity. The dosage may vary within this range depending upon a variety of factors, e.g., the dosage form employed, the route of adrninistration utilized, the condition of the subject, and the like.

For any compound used in the method of the invention, the therapeutically effective dose can be estimated initially from cell culture assays by determining an IC50 (le., the concentration of the test substance which achieves a half-maximal inhibition of PPIase activity). A dose can then be formulated in animal models to achieve a circulating plasma concentration range that includes the IC50 as determined in cell culture. Such information can be used to more accurately determine useful doses in humans. Levels in plasma may be measured, for example, by HPLC. The exact formulation, route of administration and dosage can be chosen by the individual physician in view of the patient's condition. (See e.g. Fingl et al, 1975).

It should be noted that the attending physician would know how to and when to terrrrinate, interrupt, or adjust administration due to toxicity, to organ dysfunction, and the like. Conversely, the attending physician would also know to adjust treatment to higher levels if the clinical response were not adequate (precluding toxicity). The magnitude of an administered dose in the management of the disorder of interest will vary with the severity of the condition to be treated, with the route of administration, and the like. The severity of the condition may, for example, be evaluated, in part, by standard prognostic evaluation methods. Further, the dose and perhaps dose frequency will also vary according to the age, body weight, and response of the individual patient. Typically, the dose will be between about 1-10 mg/kg of body weight. About 1 mg to about 50 mg will be administered to a child, and between about 25 mg and about 1000 mg will be administered to an adult. A program comparable to that discussed above may be used in veterinary medicine.

Depending on the specific conditions being treated, such agents may be formulated and administered systemically or locally. Techniques for formulation and administration may be found in "Remington's Pharmaceutical Sciences," 1990, 18th ed., Mack PubUshing Co., Easton, PA. Suitable routes may include oral, rectal, transdermal, vaginal, transmucosal, or intestinal administration; parenteral delivery, including intramuscular, subcutaneous, intramedullary injections, as well as intrathecal, direct intraventricular, intravenous, intraperitoneal, intranasal, or intraocular injections, just to name a few.

For injection, compounds of the invention may be formulated in aqueous solutions, preferably in physiologically compatible buffers such as Hank's solution, Ringer's solution, or physiological saline buffer. For transmucosal administration, penetrants appropriate to the barrier to be permeated are used in the formulation. Such penetrants are generally known in the art.

Use of pharmaceutically acceptable carriers to formulate the compounds herein disclosed into dosages suitable for systemic administration is within the scope of the invention. With proper choice of carrier and suitable manufacturing practice, the compositions of the present invention, in particular those formulated as solutions, may be administered parenterally, such as by intravenous injection. The compounds can be readily formulated using pharmaceutically acceptable carriers well known in the art into dosages suitable for oral administration. Such carriers enable the compounds of the invention to be formulated as tablets, pills, capsules, dragees, liquids, gels, syrups, slurries, suspensions, and the like, for oral ingestion by a subject to be treated.

Agents intended to be administered intracellularly may be administered using techniques well known to those of ordinary skill in the art. For example, such agents may be encapsulated into liposomes, then administered as described above. Liposomes are spherical lipid bilayers with aqueous interiors. All molecules present in an aqueous solution at the time of liposome formation are incorporated into the aqueous interior. The liposomal contents are both protected from the external microenvironment and, because liposomes fuse with cell membranes, are efficiently delivered into the cell cytoplasm. Delivery systems involving liposomes are discussed in International Patent Publication No. WO 91/02805 and International Patent PubHcation No. WO 91/19501, as weU as U.S. Patent No.4,880,635 to Janoff et al. These pubHcations and patents provide useful descriptions of techniques for liposome drug deHvery and are incorporated by reference herein in their entirety.

Pharmaceutical compositions contemplated for use in the present invention include compositions wherein the active ingredients are contained in an amount effective to achieve the intended purpose. Determination of an effective amount is weU within the capabiHty of those skilled in the art, especially in light of the detailed disclosure provided herein.

In addition to the active ingredients, these pharmaceutical compositions may contain suitable pharmaceuticaHy acceptable excipients and auxiliaries which facilitate processing of the active compounds into preparations which can be used pharmaceutically.

The pharmaceutical compositions of the present invention may be manufactured in a manner that is itself known, e.g., by means of conventional mixing, dissolving, granulating, dragee-making, levigating, emulsifying, encapsulating, entrapping, lyophiHzing processes, or the Hke.

Pharmaceutical formulations for parenteral administration include aqueous solutions of the active compounds in water-soluble form. Additionally, suspensions of the active compounds may be prepared as appropriate oily injection suspensions. Suitable HpophiHc solvents or vehicles include fatty oils such as sesame oil, or synthetic fatty acid esters, such as ethyl oleate or triglycerides, or liposomes.

Aqueous injection suspensions may contain compounds which increase the viscosity of the suspension, such as sodium carboxymethyl cellulose, sorbitol, dextran, or the like. OptionaHy, the suspension may also contain suitable stabiHzers or agents which increase the solubility of the compounds to allow for the preparation of highly concentrated solutions. Pharmaceutical preparations for oral use can be obtained by combining the active compounds with soHd excipient, optionally grinding the resulting mixture, and processing the mixture of granules, after adding suitable auxiliaries, if desired, to obtain tablets or dragee cores.

Suitable excipients are, in particular, fillers such as sugars, including lactose, sucrose, mannitol, sorbitol, and the like; cellulose preparations such as, for example, maize starch, wheat starch, rice starch, potato starch, gelatin, gum tragacanth, methyl ceHulose, hydroxypropylmethylceUulose, sodium carboxymethylceUulose, polyvinylpyrrolidone (PVP), and the like, as well as mixtures of any two or more thereof. If desired, disintegrating agents may be added, such as cross-linked polyvinyl pyrrolidone, agar, alginic acid or a salt thereof such as sodium alginate, and the like.

Dragee cores are provided with suitable coatings. For this purpose, concentrated sugar solutions may be used, which may optionally contain gum arabic, talc, polyvinyl pyrrolidone, carbopol gel, polyethylene glycol, titanium dioxide, lacquer solutions, suitable organic solvents or solvent mixtures, and the like. Dyestuffs or pigments may be added to the tablets or dragee coatings for identification or to characterize different combinations of active compound doses.

Pharmaceutical preparations which can be used oraHy include push-fit capsules made of gelatin, as weU as soft, sealed capsules made of gelatin and a plasticizer, such as glycerol or sorbitol. The push-fit capsules can contain the active ingredients in admixture with fiUer such as lactose, binders such as starches, and/ or lubricants such as talc or magnesium stearate and, optionaUy, stabilizers. In soft capsules, the active compounds may be dissolved or suspended in suitable Hquids, such as fatty oils, Hquid paraffin, or Hquid polyethylene glycols. In addition, stabiHzers may be added.

A detailed description of CDP-ME synthase structure is provided below as a preferred embodiment of the invention. The present invention may suitably be practice in the absence of any element or limitation not specifically disclosed herein. The terms and expressions employed herein have been used as terms of description to faciHtate enablement and not of Hmitation, and there is no intention in the use of such terms and expressions of excluding any equivalents of the features shown and described or portions thereof, but it is recognized that various modifications are possible within the scope of the invention claimed. Thus it should be understood that although the present invention has been specifically disclosed by preferred embodiments and optional features, modification and variation of the inventions embodied herein disclosed may be resorted to by those skilled in the art, and that such modifications and variations are considered to be within the scope of this invention.

CDP-ME synthase packs as a homodimer in the crystalline state with each monomer related by a crystallographic two-fold axis, in accordance with its hydrodynamic characterization. The dimeric arrangement is beHeved to represent the physiologicaHy relevant dimeric arrangement for two reasons. Firstly, oHgomerization buries 3750 A² of surface area, a value typical of dimeric proteins. Secondly, the polypeptide chain of each monomer contributes residues to the active site of the dyad related monomer, lending mechanistic relevance to this oligomeric arrangement (Figure 3).

Each monomer is comprised of two structuraHy distinct domains. The larger core-domain (residues 1 to 136 and 160 to 236) is globular in shape and maintains an α/β structure that resembles a Rossman fold (Rossman, MG. et al, 1975), but which displays a distinct α/ β connectivity pattern including an insertion of two β-strands, β7 and βlO, into a canonical 3-2-1-4-5 type of parallel β-sheet topology (strands β5, β4, βl, β6 and βll in Figure 4). The second much smaller lobe or subdomain (residues 137 to 159) resembles a curved arm that interlocks in trans with its symmetry related arm to mediate dimer formation. Moreover, the interlocking arms form a significant fraction of the MEP binding site, and organize portions of the catalytic surface responsible for cytidyltransf erase activity (Figure 3). In CDP-ME synthase, the connecting loops, βl-β2 and βll-αl, become ordered upon CTP binding and form the upper section of the catalytic pocket responsible for CTP recognition (Figure 2). The lower half of this catalytic crevice is extended across the dimer interface through a conserved network of salt bridges.

A PSI-BLAST (Altschul, S .F. et al. , 1997) search of the non-redundant sequence database with E. coli CDP-MΕ synthase retrieved a large number of similar sequences from a variety of organisms. These sequences exhibit several highly conserved regions that, when viewed with reference to the structure of the E. coli enzyme, support their role as vital active site residues utilized for substrate recognition and catalysis in CDP-MΕ synthase. A search for related three dimensional structures in the Protein Data Bank (Berman, H.M. et al, 2000) using the DALI (Holm, L. & Sander C, 1993) server retrieved a number of enzyme cores containing a mononucleotide binding fold. Currently, three cytidyltransferase structures have been described and include capsule specific CMP:2-keto-3-deoxy-m<3«no-octonic acid synthetase (Jelakovic, S. et al., 1996) (K-CKS), CTP:glycerol-3-phosphate cytidyltransferase (GCT) (Weber, CH. et al., 1999), and most recently CMP acylneuraminate synthetase (CMP-NeuAc synthetase) (Mossimann, S.C. et al., 2000).

CDP-MΕ synthase, CMP-NeuAc synthetase, and GCT share similarly folded cores (Figures 2 and 5). However, the five parallel β-strands of GCT, which maintain a 3-2-1-4-5 topology, are interrupted in CDP-MΕ synthase and CMP-NeuAc synthetase by the insertion of two antiparallel β-strands (β7 and βlO) between strands 4 and 5 (β6 and βl 1) of the core β-sheet (Figure 4). This insertion extends the central β-sheet leading to a structural alteration of the nucleotide binding region and subsequent formation of a distinct and spatially non-overlapping CTP binding motif in CDP-MΕ synthase, CMP-NeuAc synthetase, and presumably K-CKS. While all earlier cytidyltransferase structures described to date have lacked bound product, the currently described CDP-MΕ synthase structures with Mg²⁺, substrates, and products bound accurately map the complete cytidyltransferase active site. Notably, the inserted β-strands, β7 and βlO, position the extended arm lobe of CDP-MΕ synthase that modulates formation of the MΕP binding site in trans through dimerization. By superimposing GCT and CDP-ME synthase to constrain the connectivity pattern of the central β-sheets and the surrounding α-helices, the GCT and CDP-ME synthase active sites reside on the same C-terminal side of the central β-sheets, but the orientations of the bound CTP molecules in each enzyme are arranged in opposite fashions (Figure 5). In contrast, alignments of the two structures using the bound CTP molecules as a guide reveals an internal pseudosymmetry in the core α/β fold of both GCT and CDP-ME synthase (Figure 5). Indeed, it appears that this pseudosymmetric folding pattern can be utilized for two distinct modes of binding the CTP substrate partially dictated by the extension of the parallel 3-2-1-4-5 β-strand topology in CDP-ME synthase by two antiparallel β-strands.

While the cytidine base and ribose exhibit nearly identical orientations in GCT and CDP-ME synthase, the curved triphosphate ends of the bound CTP molecules pucker in opposite directions. These alternative orientations of the triphosphate tail of CTP position each of the α-phosphates of the CTP substrates for nucleophilic attack by MEP in CDP-ME synthase and glycerol 3 -phosphate in GCT. The structure of CMP-NeuAc synthetase was solved in the apo form and complexed to a partially disordered CDP molecule which serves as a mimic of the true CTP substrate. Structural alignments of E. coli CDP-ME synthase ox Neisseria meningitidis CMP- NeuAc synthetase with GCT reveal that the catalytic machinery of CDP-ME synthase and CMP-NeuAc synthetase are spatially conserved but not shared with the GCT family of CTP-dependent cytidyltransferases (Bork, P. et al, 1995; Park, Y.S. et al, 1997; Veitch, D.P. & Cornell, R.B., 1996; Veitch, D.P. et al, 1998). While there are similarities between the two sub-families including spatial correspondence of the putative catalytic residues His 14 / His 17 of GCT with Lys 27 / Lys 213 of CDP-ME synthase and Lys 21 / Asp 209 of CMP-NeuAc synthetase, there is very little correspondence at the primary amino acid level.

Two catalytic mechanisms are likely in the cytidyltransferase family of enzymes. The first encompasses a dissociative pathway that results in the transient formation of a reactive metaphosphate intermediate at the α-phosphate position of CTP. Subsequent capture of the reactive metaphosphate intermediate by the 4- phosphate group of MEP would form CDP-ME. The second mechanism mirrors the associative pathway described for a number of GTPases and ATPases. This pathway forms a negatively charged pentacoordinate transition state upon nucleophilic attack on the α-phosphate of CTP by the 4-phosphate of MEP. Collapse of this charged state would lead to pyrophosphate release and CDP-ME formation. The large number of positive charges surrounding the active site cavity suggest that CDP-ME synthase is organized to stabilize the negatively charged pentacoordinate transition state characteristic of associative type mechanisms. The substrate and product bound structures that include Mg²⁺ ions provide a useful model to assess the roles of specific residues in the catalytic mechanism of the larger cytidyltransferase family of enzymes which includes CDP-ME synthase and CMP-NeuAc synthetase.

The roles of both Lys 27 and Lys 213 have been examined by mutating Lys 27 to Ala and Ser, respectively, and Lys 213 has been mutated to Ser. Assays conducted on these mutants and compared to the wild type protein indicate that Lys 27 plays an essential role in catalysis. This observation supports the absolute conservation of this residue in the active sites of CDP-ME family members and Lys 27 's postulated role in stabilization of the negatively charged pentacoordinate transition state. While the activity of the K213S mutant is severely compromised, it retains the ability to form the CDP-ME product albeit with significantly reduced efficiency.

In addition to the utility of the substrate and product complexes in assessing the role of specific residues of CDP-ME synthase in substrate recognition and catalysis (Figures 8 and 9), comparison of these structures with the previously described structure of CMP-NeuAc synthetase (Mossimann, S.C et al, 2000) lends further support to the role of specific residues in cytidyltransferase activity. Arg 20, Lys 27, Arg 157, and Lys 213 in CDP-ME synthase are spatially equivalent to Arg 12, Lys 21, Arg 165, and Asp 209, respectively, in CMP-NeuAc synthetase (Figures 9 and 10). Arg 20 (Arg 12 in CMP-NeuAc synthetase) interacts with the α and β- phosphates of CTP, positioning the α-phosphate for nucleophilic attack, and together with Lys 27 (Lys 21 in CMP-NeuAc synthetase) and Mg²⁺, serve as complementary charges for the negatively charged pentacoordinate transition state during CMP transfer. Arg 157 (Arg 165 in CMP-NeuAc synthetase) positioned on the dyad- related subunits most likely position the attacking nucleophiles near the α-phosphates of the respective CTP substrates in CDP-ME synthase and CMP-NeuAc synthetase. Lys 213 (Asp 209 in CMP-NeuAc synthetase) may act as an electrostatic guide for the MEP phosphate prior to nucleophilic attack on CTP (Figures 8 and 9).

Notably, in CMP-NeuAc synthetase, Asp 209, which is spatially equivalent to

Lys 213 in CDP-ME synthase, is ideally positioned to act as a general base during activation of the 2-OH of the acylneuraminate substrate in CMP-NeuAc synthetase (Figure 10). The close resemblance between the MEP derived portions of CDP-ME and the acylneuraminate substrate of CMP-NeuAc synthetase provided a starting point for the modeling of the ground state complex of CMP-NeuAc synthetase (Figure 10). This model, based upon the close chemical similarity of MEP and acylneuraminate, assigns distinct roles to Asp 209 than an earlier proposal where Asp 209 was thought to act as a Mg²⁺ binding site while the identity of the general base responsible for proton abstraction from the 2-OH group of acylneuraminate was attributed to an ordered water molecule (Mossimann, S.C. et al, 2000). It is clear in all of the CDP-ME synthase structures determined to date that the Mg²⁺ ion does not contact any side chain in the active site of CDP-ME synthase.

The invention will now be described in greater detail by reference to the following non-limiting examples.

EXAMPLE 1 Subcloning of the E. coli ygbP gene encoding CDP-ME synthase and mutations thereof

The E. coli ygbP gene (GenBank accession number AP002562) was cloned by PCR amplification of total genomic DNA isolated from E. coli K12 strain, NovaBlue using oHgonucleotides designed for Hgation into the E. coli expression vector pHIS8. The 5' and 3' ends of E. coli ygbP were taken from the deposited genome sequence of E. coli. The sense oligo, 5'- CC GTA TGC CAT GGC ATG GCA ACC ACT CAT TTG GAT G -3', (Nco I site underlined and the translation start site in bold - Sequence ID. No. 1) and antisense oHgo, 5'- ATG CCG GAA TTC TTA TGT ATT CTC CTG ATG GAT GG - 3', (BamH I site underlined and the stop codon in bold - Sequence ID. No. 2) amplified the coding sequence of ygbP (711 base pairs) which was efficiently ligated into the E. coli expression vector pHIS8. The 0.7 kb PCR product was digested with Nco I and BamH I, gel purified, and Hgated with Nco I/BamH I digested pHIS8 to generate the expression vector. The pET-28a(+) expression vector and E. coli strain BL21(DE3) were purchased from Novagen. All oHgonucleotides were ordered from Operon, Inc. NuSieve GTG agarose was obtained from FMC BioProducts. Restriction endonucleases, T4 DNA ligase, and dNTPs were from New England

Biolabs. Ni²⁺-NTA was bought from Qiagen. Benzamidine-Sepharose and the Superdex-200 FPLC column were from Pharmacia. Thrombin was purchased from Sigma. The CDP-ME synthase K27S, K27A and K213S mutants were generated with the QuickChange (Stratagene) PCR method. EXAMPLE 2 Expression and purification of E. coli CDP-ME synthase

A set of three sense: δ'-dCATGAAACACCACCACCACCAC-S' (Sequence ID. No. 3),

5'-dCACCACCACGGTGGTCTG-3' (Sequence ID. No.4), 5'-dGTTCCGCGTGGTTCCCATGGCG-3' (Sequence I.D. No. 5) and three antisense:

5'-dGATCCGCCATGGGAACCACG-3' (Sequence I.D. No. 6), 5'-dCGGAACCAGACCACCGTG-3' (Sequence ID. No. 7),

5'-dGTGCTGGTGGTGGTGGTGGTGTTT-3' (Sequence I.D. No. 8) overlapping oHgonucleotides were used to introduce an Nco I site after the thrombin cleavage site of pET-28a(+) and to extend the N-terminal hexahistidyl-coding sequence to eight histidines. The new sequence uses E. coli preferred codons and an AAA codon at the +2 site. The second and third sense and the second and third anti- sense strands were phosphorylated using T4 polynucleotide kinase, followed by incubation of all six oHgonucleotides with T4 ligase. The 62 bp fragment was isolated from a 3% NuSieve GTG agarose gel. pET-28a(+) was cut with Nde I and BamH I and the resulting 5279 bp product gel purified. The synthetic 62 bp fragment was then Hgated into the Nde l/BanιH I digested pET-28a(+). Automated nucleotide sequencing (Salk Institute DNA sequencing facility) verified the sequence of the pHIS8 construct.

Constructs of pHIS8-ygbP were transformed into E. coli BL21(DE3). Transformed E. coli were grown at 37 °C in Terrific broth containing 50 μg/ml kanamycin until A600nm ⁼ l-2. After induction with 0.5 mM isopropyl 1-thio-β-D- galactopyranoside, the cultures were grown at 20 °C for four hours. CeUs were pelleted, harvested, and resuspended in 50 mM Tris-HCl (pH 8.0), 500 mM NaCl, 20 mM imidazole (pH 8.0), 20 mM β-mercaptoethanol, 10% (v/v) glycerol, and 1% (v/v) Tween-20. After sonication and centrifugation, the supernatant was passed over a Ni²⁺-NTA column, the column was washed with 10 bed volumes of lysis buffer, 10 bed volumes of lysis buffer minus Tween-20, then the His8-tagged protein was eluted with lysis buffer minus Tween-20 but containing 250 mM imidazole (pH 8.0). Incubation with thrombin during dialysis for 24 hours at 4 °C against the lysis buffer without Tween-20 removed the amino-terrninal His8-tag. Dialyzed protein was reloaded on a Ni²⁺-NTA column and the flow-through depleted of thrombin using a benzamidine-Sepharose column. Gel filtration on a Superdex-200 FPLC column equiHbrated with 25 mM HEPES (pH 7.5), 100 mM NaCl, and 5 mM dithiothreitol (DTT) was the final step. Fractions containing ygbP were pooled, concentrated to 35 mg/ml, and stored at -80 °C in 12.5 mM HEPES (pH 7.5), 50 mM NaCl, 10 mM MgCl₂, 1 mM CTP, and 2 mM DTT after buffer exchange. The CDP-ME synthase K27S, K27A and K213S mutants were similarly expressed and purified as His8- tagged proteins.

EXAMPLE 3 Synthesis of methyl-D-erythritol-4-phosphate (MEP)

MEP was prepared on a 2 mmol scale by a one-pot, coupled enzymatic synthesis using malate as source of pyruvate, fructose-1,6- diphosphate as the source of glyceraldehyde-3-phosphate, and a NADPH recycling system involving malic enzyme and deoxyxylulose-5-phosphate reductoisomerase (DXPR). The reaction mixture contained: fructose 1,6-diphosphate (10.0 mmol), malate (20.0 mmol), pyruvate (2 mmol), NADP⁺ (1.24 mmol), MgCl₂ (0.5 mmol), Tris-Cl pH 7.5 (40 mmol), DTT (0.1 mmol), TPP (0.06 mmol), aldolase (570 units), isomerase (9700 units), maHc enzyme (50 units), DXPS2 (deoxyxylulose phosphate synthase from Streptomyces coelicolor (Cane, D.E. et al, 2001) (50 units) and DXPR («50units from S. coelicolor (Cane, D.E. et al, 2001)) in total volume of 100 ml. This solution was incubated for 3 days at 30 °C.

The crude reaction mixture was mixed with activated charcoal (10 g) and stirred at room temperature for 10 min, then passed through a 0.45 μm filter to remove the charcoal. The charcoal was then washed with distilled water (50 ml) and the filtrates were combined. This solution (150 ml) was passed through a cation exchange column (DOWEX 50W-X8, 2.5 x 50 cm) in the H⁺ form to remove the Tris buffer, which was the major contaminant identified by Η-NMR analysis. The column was eluted until the pH of the eluent was neutral. The eluate was titrated to pH 7 with NaOH, as MEP is unstable at low pH, then concentrated to 20 ml by rotary evaporation under reduced pressure. An aliquot of the concentrated solution (5 ml) was loaded onto a cellulose column (2.5 x 50 cm) equilibrated with a acetonitrile:water:TFA mixture (90:10:1) and eluted with the same solvent. Fractions containing pure MEP were pooled and concentrated to 50 ml. The material was filtered and appHed onto an anion exchange column (DOWEX 1X8-100, formate form, 2.5 x 16.5 cm) in 10 ml aHquots. The column was washed with 150 ml water and eluted with 150 ml of a 1:1 mixture of ammonium formate (1 M) and formic acid. The MEP-containing fractions were combined and lyophilized to dryness. Analysis by Η-NMR showed the yield of MEP to be 11.0 mmol (53% yield based on the fructose-1,6- diphosphate starting material), with a purity of >85%.

EXAMPLE 4

Synthesis of 4-diphosphocytidyl-2-C-methylerythritol (CDP-ME)

CDP-ME was prepared on a 0.1 mmol scale. The reaction mixture contained 104 μmol MEP, (purified as described above), CTP (104 μmol), MgCl₂ (16.8 μmol), Tris-HCl pH 7.8 (168 μmol), NaOH (120 μmol), 1.3 mg of E. coli CDP-ME synthase, and inorganic phosphatase (20 units) in a total volume of 1.68 ml. This solution was incubated for 3 hr at 37 °C. Approximately 80% of the MEP was converted to CDP- ME as determined by TLC analysis (siHca plates, n-propanol:ethyl acetate:water / 35:10:5 eluant, anysaldehyde:sulphuric acid:ethanol / 4:2:94 staining solution). The crude reaction mixture was deproteinized (500 NMWL filter,

MilHpore), lyophiHzed, and dissolved in 100 μL of an aqueous solution containing 40% methanol and 0.1 M ammonium formate. AHquots of 10 μl were loaded onto an ion exchange analytical HPLC column (Nucleosil SBlOO-104.6 x 250 mm, Macherey Nagel) and eluted with the same solution (Herz, S. et al, 1999). The eluate was monitored by UV spectiophotometry at λ = 260 nm. The peak detected at 35 min corresponded to CDP-ME. Upon repeated lyophiHzations (to remove the formate), CDP-ME was obtained in 30% overaU yield and >85% purity as determined by ^αH NMR analysis.

EXAMPLE 5 Enzymatic analysis of CDP-ME synthase

Assay mixtures at 25 °C contained 30 μg/ml CDP-ME synthase, 600 μM CTP, 600 μM MEP, 5 mM MgCl₂ and 0.2 μCi/ml [α-³ψ]CTP (400 Ci/mmol), in 0.1 M Tris-HCl pH 8.0, 2 mM DTT in a final volume of 25 μl. Reactions were initiated by adding CDP-ME synthase at a stock concentration of 2.25 mg/ml. After incubation for 2 hr, the samples were boiled for 5 min, and 5 μl aHquots were spotted on polyethyleneimine (PEI)-ceUulose TLC plates previously activated by immersion in 10% (w/v) NaCl for 10 min, dried with cool air, then soaked in deionized water for 10 min and dried again. After appHcation of the samples, the plates were dried with warm air, soaked for 10 min in 500 ml of methanol and dried. Before proceeding with ascending chromatography, the plates were pre-developed for 5 cm in methanol to prevent tiailing of the nucleotides. Ascending chromatography was accomphshed at 4 °C in rectangular glass tanks containing 100 ml of 0.8 M (NH₄)₂ SO₄ and plates developed to within 1 cm of the top. The plate was dried with hot, exposed for 8 hr with an imaging plate, and scanned with a Molecular Dynamics' Phosphorlmager.

Thin layer chromatography assays were used to compare the enzymatic activity of CDP-ME synthase wild type to CDP-ME synthase mutants K27A, K27S, and K213S. Assays were standardized using controls with no enzyme added and either added CTP, or added CTP and MEP. CDP-ME synthase activity was determined using a concentration of 30-60 μg/ml; mutant CDP-ME synthases were added at a concentration of 30 μg/ml. The quantity of CDP-ME produced by the K27S, K213A, and K27A mutants were 1.5%, 25% and 1.5%, respectively, normaHzed to 100% for wild type CDP-ME synthase formed over 2 hr. The reaction with wild type protein is complete within 1-2 minutes. EXAMPLE 6 Crystallization of CDP-ME synthase

Crystals of CDP-ME synthase (800 μm x 600 μm x 200 μm) were obtained by the vapor diffusion method at 4 °C. 2 μl hanging drops containing a 1:1 mixture of the protein solution and crystallization buffer (10% [w/v] PEG 8000, 0.2 M calcium acetate, 2 mM DTT, 0.1 M PIPES pH 6.5) produced well diffracting crystals that grew overnight. Crystallization of CDP-ME synthase was accomplished in the presence of up to 19% (v/v) ethylene glycol used both as a cryoprotectant and as an additive to improve crystal size and morphology. Crystals were stabihzed in 15% (w/v) PEG 8000, 15% (v/v) ethylene glycol, 0.2 M calcium acetate, 0.1 M PIPES pH 6.5 (no DTT), and flash frozen in Hquid nitrogen prior to data coUection. CDP-ME synthase crystals belong to space group C2 with unit cell dimensions of a = 130.6 A, b = 47.1 A, c = 38.1 A, β = 94°, with one monomer per asymmetric unit, and a solvent content of 42%. Complexes of CDP-ME synthase with CTP or CDP-ME were obtained as above by crystalHzation in the presence of 10 mM CTP / 10 mM MgCl₂ and 10 mM CDP- ME / 10 mM MgCl₂ , respectively.

EXAMPLE 7 CrystaHography data collection and analysis

A data set was coUected on beamline 9.2 (λ 0.9848 A) of the Stanford Synchrotron Radiation Laboratory (SSRL) equipped with an ADSC Quantum 4 CCD detector on a single crystal co-crystallized with 1 mM CTP, to a resolution of 1.24 A. A MAD data set with minirnal signal was coUected on beamHne 9-2 (selenium edge with λi = 0.9797 A, λ₂ = 0.9795 A, λ₃ = 0.8952 A) at SSRL on a single crystal grown from Se-met containing CDP-ME synthase (three potential methionines) co- crystaUized with 1 mM CTP, to a resolution of 1.5 A (Table 1). FinaUy, diffraction data were coUected on beamHne 7-1 (λ = 1.08 A) at SSRL on a single crystal co- crystallized with 10 mM CTP to a resolution of 1.5 A, on a crystal co-crystallized with 10 mM MEP (referred to as the apo form) to a resolution of 1.55 A, and on a crystal co-crystallized with 10 mM CDP-ME to a resolution of 1.8 A, aU on a 180/345 mm MAR imaging plate system detector (Table 2). Heavy atom derivatives were obtained by soaking native crystals for 12-16 hr in the cryopreservation solution in the presence of either 13 mM KAu(CN)₄ or a saturated solution of dimercurial acetate (DMA). MIR data sets were collected in-house at 100 K using a DIP 2030 imaging plate system (Mac Science Corporation, Japan) and CuK_α radiation produced by a rotating anode operated at 45 kV and 100 mA and equipped with double-focusing Pt/Ni coated mirrors (Table 1). AU data were indexed and integrated using DENZO (Otwinowski, Z. & Minor, W., 1997) and scaled with the program SCALEPACK (French, G.S. & Wilson, K.S., 1978). Intensities were transformed into ampHtudes using TRUNCATE (CCP4, 1994). The heavy atom derivative data sets were scaled against the 1.24 A resolution native data set with the program SCALEIT (CCP4, 1994).

AU crystaUographic calculations were performed using the CCP4 suite of programs (CCP4, 1994) unless stated otherwise. MAD experiments attempting to solve the structure of Se-met containing CDP-ME synthase yielded two potential Se sites and low quality experimental maps that did not permit chain tracing. However, the phases obtained from SHARP (La Fortelle, E. de & Bricogne, G, 1997) were sufficient to identify initial metal-binding sites for the Au and Hg derivatives by difference Fourier analysis. These initial sites were verified by inspection of difference Patterson maps using XTALVIEW (McRee, D.E., 1992), and initiaUy refined using MLPHARE (Otwinowski, Z., 1991). Final refinement of heavy atom parameters, identification of minor heavy atom binding sites, and phase-angle calculations were performed with the program SHARP (La ForteUe, E. de & Bricogne, G., 1997) using the 1.24 A resolution native data set. Solvent flipping using the CCP4 program SOLOMON (CCP4, 1994) significantly improved and extended phases to 1.24 A.

The initial atomic model was generated using wARP (Perrakis, A. et al, 1997). Subsequent model building was carried out with the program O (Jones, T.A. &

Kjeldgaard, M.O., 1997), and refinement steps consisting of bulk-solvent correction, positional, torsion angle simulated annealing, and B-factor refinement were carried out with CNS (Brunger, A.T. et al, 1998). However, due to the low occupancy of the CTP binding site and the corresponding partial disorder surrounding this site further refinement using the .1.24 A data set was halted. Subsequent building and refinement steps were carried out using data obtained from a crystal co-crystalHzed with 10 mM CTP and 10 mM MgCl₂. This data set yielded a weU-ordered CTP • Mg²⁺ binding site with full occupancy. This refined model served as the starting model for construction and refinement of the apo form and CDP-ME ^»Mg²⁺ complex. PROCHECK (Laskowski, R.A. et al, 1993) analysis of aU models shows 92% of the main chain torsion angles in the most favored regions, and no residues in the disallowed regions. The current apo model includes residues 5 to 228 with the loop sparming Ala 16 to Phe 26 absent due to disorder. The CTP^»Mg²⁺ complex includes residues 5 to 229. The CDP-ME ^»Mg²⁺ complex includes residues 5 to 228 with the loop spanning Phe 17 to Glu 24 poorly defined in the density due to disorder. Figures were generated using MOLSCRIPT (Kraulis, P.J., 1991) and BOBSCRIPT (Esnouf, R., 1997) and rendered with POV-RAY (Amundsen, S., 1997) . The electrostatic surface potential was generated using GRASP (Nicholls, A. & Honig, B. (1991).

While the invention has been described in detaU with reference to certain preferred embodiments thereof, it wiU be understood that modifications and variations are within the spirit and scope of that which is described and claimed.

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Otwinowski, Z. Maximum Hkelihood refinement of heavy-atom parameters in isomorphous replacement and anomalous scattering. Proceedings ofCCP4 Study Weekend, Warrington UK, 307-326 (1991).

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Perrakis, A., Sixma, T.K., Wilson K.S. & Lamzin, V.S. wARP: improvement and extension of crystaUographic phases by weighted averaging of multiple refined dummy atomic models. Acta Cnjstallogr. D 53, 448-455 (1997). Ridley, R.G. Planting the seeds of new antimalarial drugs. Science 285, 1502-1503 (1999).

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APPENDIX 1 X-RAY DATA COORDINATES FOR THE APO FORM OF CDP-ME SYNTHASE

REMARK coordinates from minimization and B-factor refinement REMARK refinement resolution: 90 - 1.50 A

REMARK starting r= .3521 free_r= .3557

REMARK final r= .2462 free_r= .2682

REMARK rmsd bonds= .005120 rmsd angles= 1.23322

REMARK B rmsd for bonded mainchain atoms= 1.636 target= 1.5 REMARK B rmsd for bonded sidechain atoms= 2.269 target= 2.0

REMARK B rmsd for angle mainchain atoms= 2.510 target= 2.0

REMARK B rmsd for angle sidechain atoms= 3.370 target= 2.5

REMARK target= mlf final wa= .542348

REMARK final r eight= .0659 (with wa= .542348) REMARK md-method= torsion annealing schedule= constant

REMARK starting temperature= 2000 total md steps= 1 * 100

REMARK cycles= 2 coordinate steps= 20 B-factor steps= 10

REMARK sg= C2 a= 130.297 b= 47.328 c= 38.146 alpha= 90 beta= 94.179 gamma= 90

REMARK topology file 1 : CNS_TOPPAR:protein.top REMARK topology file 2 : CNS_TOPPAR:dna-rna.top

REMARK topology file 3 : CNS_TOPPAR:water.top

REMARK topology file 4 : CNS_TOPPAR:ion.top

REMARK topology file 5 : CNSPAR:ctp.top

REMARK parameter file 1 : CNS_TOPPAR:protein_rep.param REMARK parameter file 2 : CNS_TOPPAR:dna-rna_rep.param

REMARK parameter file 3 : CNS_TOPPAR:water_rep.param

REMARK parameter file 4 : CNS_TOPPAR:ion.param

REMARK parameter file 5 : CNSPAR:ctp.param

REMARK molecular structure file: generate. mtf REMARK input coordinates: rigid. pdb

REMARK reflection file= ssrljun.xpl

REMARK ncs= none

REMARK B-correction resolution: 6.0 - 1.50

REMARK initial B-factor correction applied to fobs : REMARK B11 = 4.766 B22= -4.733 B33= -.033

REMARK B12= .000 B13= -.644 B23= .000

REMARK B-factor correction applied to coordinate array B: -2.541

REMARK bulk solvent: density ievel= .361117 e/A^Λ3, B-factor= 41.4891 A^Λ2

REMARK reflections with |Fobs|/sigma_F < 0.0 rejected REMARK reflections with JFobsj > 10000 * rms(Fobs) rejected

REMARK theoretical total number of refl. in resol. range: 37283 ( 100.0 % )

REMARK number of unobserved reflections (no entry or |F|=0): 5238 ( 14.0 % )

REMARK number of reflections rejected: 0 ( .0 % )

REMARK total number of reflections used: 32045 ( 86.0 % ) REMARK number of reflections in working set: 30422 ( 81.6 % )

REMARK number of reflections in test set: 1623 ( 4.4 % )

CRYST1 130.297 47.328 38.146 90.00 94.18 90.00 C 2

REMARK FILENAME="refine.pdb"

REMARK DATE:24-Jun-00 18:09:09 created by user: richard

REMARK VERSION:1.0

ATOM 1 CB HIS A 5 29.232 - •18.834 9.984 1.00 40.47 A

ATOM 2 CG HIS A 5 30.635 - -19.194 9.613 1.00 42.58 A

ATOM 3 CD2 HIS A 5 31.438 -18.753 8.613 1.00 42.79 A

ATOM 4 ND1 HIS A 5 31.393 -20.079 10.347 1.00 44.08 A

ATOM 5 CE1 HIS A 5 32.602 -20.168 9.821 1.00 43.60 A ATOM 6 NE2HISA 5 32.653-19.372 8.767 1.0043.39 A

ATOM 7 C HIS A 5 30.334-17.383 11.680 1.0036.12 A

ATOM 80 HISA 5 31.173-17.732 12.504 1.0036.81 A

ATOM 9 N HISA 5 27.797-17.559 11.547 1.0038.66 A ATOM 10 CA HISA 5 29.106-18.255 11.398 1.0037.92 A

ATOM 11 N LEU A 6 30.431 -16.255 10.984 1.0033.83 A

ATOM 12 CA LEU A 6 31.565-15.346 11.109 1.0030.96 A

ATOM 13 CB LEU A 6 31.508-14.303 9.982 1.0032.34 A

ATOM 14 CG LEU A 6 31.539-14.816 8.536 1.0034.10 A ATOM 15 CD1 LEUA 6 31.367-13.648 7.575 1.0033.98 A

ATOM 16 CD2LEUA 6 32.852-15.537 8.262 1.0034.60 A

ATOM 17 C LEU A 6 31.761 -14.627 12.451 1.0027.83 A

ATOM 18 O LEU A 6 32.767-13.947 12.635 1.0024.00 A

ATOM 19 N ASP A 7 30.818-14.762 13.380 1.0025.51 A ATOM 20 CA ASP A 7 30.936-14.101 14.682 1.0024.34 A

ATOM 21 CB ASP A 7 29.602-14.179 15.432 1.0027.72 A

ATOM 22 CG ASP A 7 28.579-13.180 14.915 1.0030.36 A

ATOM 23 0D1ASPA 7 28.738-12.686 13.781 1.0029.91 A

ATOM 24 OD2ASPA 7 27.612-12.895 15.646 1.0033.40 A ATOM 25 C ASP A 7 32.045-14.727 15.535 1.0020.74 A

ATOM 26 O ASP A 7 32.094-15.946 15.707 1.0023.22 A

ATOM 27 N VAL A 8 32.924-13.890 16.080 1.0016.44 A

ATOM 28 CA VAL A 8 34.037-14.384 16.896 1.0013.60 A

ATOM 29 CB VAL A 8 35.396-14.105 16.203 1.0013.39 A ATOM 30 CG1VALA 8 36.553-14.486 17.132 1.0014.55 A

ATOM 31 CG2VALA 8 35.486-14.876 14.903 1.0012.40 A

ATOM 32 C VAL A 8 34.092-13.707 18.250 1.0013.03 A

ATOM 33 O VAL A 8 33.872-12.500 18.342 1.0013.92 A

ATOM 34 N CYSA 9 34.385-14.483 19.296 1.0011.76 A ATOM 35 CA CYSA 9 34.526-13.920 20.636 1.0013.89 A

ATOM 36 CB CYSA 9 33.658-14.65421.661 1.0013.63 A

ATOM 37 SG CYSA 9 33.746-13.953 23.345 1.0018.72 A

ATOM 38 C CYSA 9 35.989-14.082 21.011 1.0012.22 A

ATOM 39 0 CYSA 9 36.568-15.150 20.799 1.0014.47 A ATOM 40 N ALA A 10 36.586-13.032 21.562 1.0011.63 A

ATOM 41 CA ALAA 10 37.992-13.091 21.955 1.00 9.91 A

ATOM 42 CB ALAA 10 38.729-11.816 21.504 1.0013.37 A

ATOM 43 C ALAA 10 38.067-13.251 23.467 1.0011.15 A

ATOM 44 O ALAA 10 37.177-12.804 24.194 1.0012.46 A ATOM 45 N VAL A 11 39.109-13.935 23.929 1.0012.85 A

ATOM 46 CA VALA 11 39.328-14.151 25.350 1.0012.20 A

ATOM 47 CB VALA 11 39.169-15.63425.736 1.0010.33 A

ATOM 48 CG1VALA 11 39.583-15.848 27.196 1.0013.90 A

ATOM 49 CG2VALA 11 37.708-16.052 25.539 1.0014.62 A ATOM 50 C VALA 11 40.748-13.711 25.647 1.0011.20 A

ATOM 51 O VALA 11 41.680-14.094 24.950 1.0011.80 A

ATOM 52 N VALA 12 40.917-12.887 26.667 1.0011.27 A

ATOM 53 CA VALA 12 42.241 -12.42427.018 1.0012.65 A

ATOM 54 CB VALA 12 42.362-10.89426.821 1.0010.70 A ATOM 55 CG1VALA 12 43.724-10.41527.298 1.0012.07 A

ATOM 56 CG2VALA 12 42.169-10.54725.343 1.0013.88 A

ATOM 57 C VALA 12 42.495-12.777 28.475 1.0015.37 A

ATOM 58 O VALA 12 41.864-12.221 29.373 1.0015.08 A

ATOM 59 N PROA 13 43.384-13.746 28.727 1.0015.67 A ATOM 60 CD PROA 13 44.010-14.701 27.797 1.0016.20 A

ATOM 61 CA PROA 13 43.660-14.10030.121 1.0018.92 A

ATOM 62 CB PROA 13 44.298-15.48430.005 1.0019.01 A ATOM 63 CG PROA 13 44.988-15.436 28.682 1.0020.83 A

ATOM 64 C PROA 13 44.595-13.038 30.700 1.0019.22 A

ATOM 65 O PROA 13 45.765-12.967 30.331 1.0024.43 A

ATOM 66 N ALAA 14 44.067-12.201 31.589 1.0022.71 A ATOM 67 CA ALAA 14 44.849-11.121 32.184 1.0022.14 A

ATOM 68 CB ALAA 14 44.327 -9.776 31.690 1.0023.57 A

ATOM 69 C ALAA 14 44.819-11.170 33.704 1.0024.27 A

ATOM 70 O ALAA 14 44.759-10.131 34.365 1.0022.98 A

ATOM 71 N ALAA 15 44.862-12.386 34.243 1.0025.27 A ATOM 72 CA ALAA 15 44.832-12.611 35.685 1.0028.94 A

ATOM 73 CB ALAA 15 43.717-13.592 36.026 1.0028.54 A

ATOM 74 C ALAA 15 46.173-13.151 36.172 1.0030.75 A

ATOM 75 O ALAA 15 46.237-14.229 36.768 1.0034.10 A

ATOM 76 N LYSA 27 52.712 -6.297 34.117 1.0033.96 A ATOM 77 CA LYS A 27 53.241 -5.852 32.835 1.0032.52 A

ATOM 78 CB LYS A 27 53.984 -7.007 32.162 1.0034.49 A

ATOM 79 CG LYS A 27 53.209 -8.311 32.199 1.0035.39 A

ATOM 80 CD LYS A 27 54.114 -9.517 32.053 1.0036.37 A

ATOM 81 CE LYS A 27 53.467-10.748 32.672 1.0036.69 A ι ATOM 82 NZ LYS A 27 54.372-1 .935 32.698 1.0037.00 A

ATOM 83 C LYS A 27 52.130 -5.336 31.923 1.0030.49 A

ATOM 84 O LYS A 27 52.309 -4.360 31.196 1.0028.46 A

ATOM 85 N GLNA 28 50.978 -5.996 31.973 1.0028.92 A

ATOM 86 CA GLNA 28 49.836 -5.610 31.156 1.0027.87 A ATOM 87 CB GLNA 28 48.687 -6.593 31.377 1.0029.40 A

ATOM 88 CG GLNA 28 48.245 -6.675 32.830 1.0031.65 A

ATOM 89 CD GLNA 28 47.270 -7.798 33.097 1.0032.55 A

ATOM 90 OE1 GLNA 28 47.564 -8.955 32.826 1.0033.79 A

ATOM 91 NE2GLNA 28 46.092 -7.458 33.618 1.0032.72 A ATOM 92 C GLN A 28 49.364 -4.202 31.493 1.0026.39 A

ATOM 93 O GLNA 28 48.715 -3.537 30.681 1.0022.92 A

ATOM 94 N TYR A 29 49.685 -3.735 32.694 1.0026.86 A

ATOM 95 CA TYR A 29 49.258 -2.404 33.097 1.0026.87 A

ATOM 96 CB TYR A 29 48.768 -2.437 34.548 1.0027.42 A ATOM 97 CG TYR A 29 47.439 -3.152 34.685 1.0027.42 A

ATOM 98 CD1 TYRA 29 47.291 -4.242 35.537 1.0027.12 A

ATOM 99 CE1TYRA 29 46.077 -4.921 35.632 1.0027.04 A

ATOM 100 CD2TYRA 29 46.333 -2.751 33.933 1.0027.62 A

ATOM 101 CE2TYRA 29 45.116 -3.421 34.020 1.0025.89 A ATOM 102 CZ TYR A 29 44.996 -4.505 34.874 1.0026.62 A

ATOM 103 OH TYR A 29 43.792 -5.165 34.956 1.0025.35 A

ATOM 104 C TYR A 29 50.294 -1.311 32.887 1.0028.28 A

ATOM 105 O TYR A 29 50.041 -.14733.198 1.0029.12 A

ATOM 106 N LEU A 30 51.460 -1.685 32.368 1.0030.06 A ATOM 107 CA LEU A 30 52.497 -.704 32.065 1.0031.18 A

ATOM 108 CB LEU A 30 53.805 -1.398 31.674 1.0032.65 A

ATOM 109 CG LEU A 30 54.590 -2.085 32.796 1.0033.29 A

ATOM 110 CD1 LEU A 30 55.792 -2.817 32.215 1.0034.40 A

ATOM 111 CD2LEUA 30 55.035 -1.041 33.805 1.0034.54 A ATOM 112 C LEU A 30 51.921 .04630.868 1.0031.86 A

ATOM 113 0 LEUA 30 51.067 -.492 30.157 1.0030.51 A

ATOM 114 N SERA 31 52.372 1.273 30.638 1.0031.64 A

ATOM 115 CA SERA 31 51.836 2.040 29.527 1.0032.60 A

ATOM 116 CB SERA 31 51.154 3.310 30.043 1.0032.26 A ATOM 117 OG SERA 31 49.994 2.992 30.787 1.0033.99 A

ATOM 118 C SERA 31 52.822 2.408 28.431 1.0033.15 A

ATOM 119 0 SERA 31 54.030 2.50528.654 1.0032.44 A ATOM 120 N ILE A 32 52.275 2.612 27.238 1.00 33.49 A

ATOM 121 CA ILE A 32 53.052 2.980 26.067 1.00 33.65 A

ATOM 122 CB ILE A 32 53.303 1.755 25.159 1.00 34.90 A

ATOM 123 CG2 ILE A 32 54.099 2.175 23.925 1.00 35.04 A

ATOM 124 CG1 ILE A 32 54.046 .671 25.946 1.00 35.29 A

ATOM 125 CD1 ILE A 32 54.283 -.605 25.165 1.00 36.39 A

ATOM 126 C ILE A 32 52.245 4.023 25.301 1.00 34.63 A

ATOM 127 O ILE A 32 51.408 3.684 24.467 1.00 33.63 A

ATOM 128 N GLY A 33 52.482 5.294 25.606 1.00 35.97 A

ATOM 129 CA GLY A 33 51.766 6.359 24.928 1.00 37.07 A

ATOM 130 C GLY A 33 50.423 6.724 25.532 1.00 38.65 A

ATOM 131 O GLY A 33 49.454 6.946 24.811 1.00 39.47 A

ATOM 132 N ASN A 34 50.370 6.789 26.857 1.00 38.53 A

ATOM 133 CA ASN A 34 49.149 7.145 27.578 1.00 39.06 A

ATOM 134 CB ASN A 34 48.610 8.495 27.069 1.00 39.04 A

ATOM 135 CG ASN A 34 47.283 8.369 26.335 1.00 39.17 A

ATOM 136 OD1 ASN A 34 47.227 7.890 25.201 1.00 40.92 A

ATOM 137 ND2 ASN A 34 46.203 8.800 26.987 1.00 39.47 A

ATOM 138 C ASN A 34 48.069 6.065 27.507 1.00 37.59 A

ATOM 139 O ASN A 34 46.950 6.259 27.976 1.00 38.69 A

ATOM 140 N GLN A 35 48.414 4.925 26.920 1.00 36.07 A

ATOM 141 CA GLN A 35 47.485 3.806 26.817 1.00 33.51 A

ATOM 142 CB GLN A 35 47.093 3.574 25.357 1.00 37.81 A

ATOM 143 CG GLN A 35 45.970 2.569 25.162 1.00 40.31 A

ATOM 144 CD GLN A 35 45.446 2.538 23.736 1.00 42.32 A

ATOM 145 OE1 GLN A 35 44.979 3.549 23.213 1.00 43.92 A

ATOM 146 NE2 GLN A 35 45.524 1.374 23.100 1.00 42.96 A

ATOM 147 C GLN A 35 48.201 2.582 27.384 1.00 29.12 A

ATOM 148 O GLN A 35 49.381 2.369 27.103 1.00 27.11 A

ATOM 149 N THR A 36 47.502 1.788 28.192 1.00 25.58 A

ATOM 150 CA THR A 36 48.113 .607 28.794 1.00 21.98 A

ATOM 151 CB THR A 36 47.253 .041 29.956 1.00 23.65 A

ATOM 152 OG1 THR A 36 46.058 -.557 29.432 1.00 19.94 A

ATOM 153 CG2 THR A 36 46.877 1.153 30.937 1.00 23.71 A

ATOM 154 C THR A 36 48.316 -.506 27.771 1.00 19.97 A

ATOM 155 O THR A 36 47.643 -.541 26.740 1.00 18.41 A

ATOM 156 N ILE A 37 49.258 -1.400 28.058 1.00 18.97 A

ATOM 157 CA ILE A 37 49.547 -2.522 27.168 1.00 18.40 A

ATOM 158 CB ILE A 37 50.659 -3.425 27.747 1.00 20.64 A

ATOM 159 CG2 ILE A 37 50.775 -4.709 26.940 1.00 21.89 A

ATOM 160 CG1 ILE A 37 51.995 -2.671 27.728 1.00 24.96 A

ATOM 161 CD1 ILE A 37 53.148 -3.438 28.333 1.00 26.64 A

ATOM 162 C ILE A 37 48.277 -3.342 26.946 1.00 17.58 A

ATOM 163 O ILE A 37 47.981 -3.758 25.823 1.00 15.85 A

ATOM 164 N LEU A 38 47.515 -3.555 28.011 1.00 16.79 A

ATOM 165 CA LEU A 38 46.269 -4.305 27.902 1.00 15.19 A

ATOM 166 CB LEU A 38 45.563 -4.380 29.263 1.00 16.96 A

ATOM 167 CG LEU A 38 44.184 -5.061 29.283 1.00 18.73 A

ATOM 168 CD1 LEU A 38 44.269 -6.480 28.730 1.00 17.43 A

ATOM 169 CD2 LEU A 38 43.660 -5.082 30.708 1.00 20.08 A

ATOM 170 C LEU A 38 45.353 -3.639 26.878 1.00 16.35 A

ATOM 171 O LEU A 38 44.763 -4.317 26.040 1.00 15.22 A

ATOM 172 N GLU A 39 45.242 -2.313 26.935 1.00 18.16 A

ATOM 173 CA GLU A 39 44.389 -1.601 25.992 1.00 17.53 A

ATOM 174 CB GLU A 39 44.252 -.128 26.396 1.00 19.59 A

ATOM 175 CG GLU A 39 43.479 .047 27.690 1.00 22.26 A

ATOM 176 CD GLU A 39 43.546 1.454 28.231 1.00 24.79 A ATOM 177 OE1 GLU A 39 42.673 2.277 27.885 1.00 27.84 A

ATOM 178 OE2 GLU A 39 44.490 1.721 28.991 1.00 22.15 A

ATOM 179 C GLU A 39 44.906 -1.726 24.561 1.00 16.62 A

ATOM 180 O GLU A 39 44.123 -1.936 23.642 1.00 16.23 A ATOM 181 N HIS A 40 46.218 -1.610 24.368 1.00 17.52 A

ATOM 182 CA HIS A 40 46.779 -1.745 23.021 1.00 16.85 A

ATOM 183 CB HIS A 40 48.304 -1.627 23.049 1.00 19.55 A

ATOM 184 CG HIS A 40 48.808 -.225 23.194 1.00 18.43 A

ATOM 185 CD2 HIS A 40 49.420 .397 24.227 1.00 20.94 A ATOM 186 ND1 HIS A 40 48.713 .709 22.184 1.00 22.67 A

ATOM 187 CE1 HIS A 40 49.247 1.847 22.591 1.00 20.57 A

ATOM 188 NE2 HIS A 40 49.684 1.686 23.826 1.00 19.25 A

ATOM 189 C HIS A 40 46.410 -3.131 22.502 1.00 17.48 A

ATOM 190 O HIS A 40 46.026 -3.314 21.348 1.00 17.24 A ATOM 191 N SER A 41 46.553 -4.107 23.386 1.00 15.78 A

ATOM 192 CA SER A 41 46.253 -5.490 23.074 1.00 14.98 A

ATOM 193 CB SE A 41 46.587 -6.345 24.285 1.00 17.90 A

ATOM 194 OG SER A 41 47.987 -6.506 24.398 1.00 20.39 A

ATOM 195 C SER A 41 44.800 -5.723 22.657 1.00 15.59 A ATOM 196 O SER A 41 44.513 -6.275 21.589 1.00 15.02 A

ATOM 197 N VAL A 42 43.886 -5.289 23.512 1.00 15.11 A

ATOM 198 CA VAL A 42 42.460 -5.453 23.280 1.00 15.70 A

ATOM 199 CB VAL A 42 41.673 -5.037 24.541 1.00 15.99 A

ATOM 200 CG1 VAL A 42 40.173 -5.005 24.254 1.00 16.82 A ATOM 201 CG2 VAL A 42 41.980 -6.015 25.669 1.00 18.02 A

ATOM 202 C VAL A 42 41.982 -4.666 22.079 1.00 16.05 A

ATOM 203 O VAL A 42 41.160 -5.148 21.298 1.00 13.89 A

ATOM 204 N HIS A 43 42.502 -3.458 21.910 1.00 14.79 A

ATOM 205 CA HIS A 43 42.089 -2.651 20.764 1.00 17.35 A ATOM 206 CB HIS A 43 42.629 -1.224 20.914 1.00 22.33 A

ATOM 207 CG HIS A 43 41.912 -.425 21.963 1.00 27.03 A

ATOM 208 CD2 HIS A 43 42.378 .316 22.997 1.00 29.13 A

ATOM 209 ND1 HIS A 43 40.537 -.320 22.008 1.00 28.36 A

ATOM 210 CE1 HIS A 43 40.187 .450 23.023 1.00 30.53 A ATOM 211 NE2 HIS A 43 41.286 .849 23.639 1.00 30.65 A

ATOM 212 C HIS A 43 42.506 -3.287 19.434 1.00 15.29 A

ATOM 213 O HIS A 43 41.822 -3.117 18.425 1.00 16.83 A

ATOM 214 N ALA A 44 43.608 -4.036 19.429 1.00 13.99 A

ATOM 215 CA ALA A 44 44.034 -4.697 18.196 1.00 13.80 A ATOM 216 CB ALA A 44 45.407 -5.338 18.378 1.00 14.31 A

ATOM 217 C ALA A 44 42.998 -5.762 17.803 1.00 14.04 A

ATOM 218 O ALA A 44 42.714 -5.955 16.626 1.00 15.04 A

ATOM 219 N LEU A 45 42.440 -6.453 18.796 1.00 11.85 A

ATOM 220 CA LEU A 45 41.441 -7.476 18.542 1.00 12.91 A ATOM 221 CB LEU A 45 41.161 -8.284 19.816 1.00 12.72 A

ATOM 222 CG LEU A 45 42.365 -8.955 20.479 1.00 11.52 A

ATOM 223 CD1 LEU A 45 41.944 -9.631 21.773 1.00 15.00 A

ATOM 224 CD2 LEU A 45 42.963 -9.952 19.518 1.00 13.77 A

ATOM 225 C LEU A 45 40.142 -6.846 18.049 1.00 14.25 A ATOM 226 0 LEU A 45 39.557 -7.298 17.070 1.00 12.38 A

ATOM 227 N LEU A 46 39.700 -5.788 18.722 1.00 14.49 A

ATOM 228 CA LEU A 46 38.449 -5.132 18.362 1.00 13.26 A

ATOM 229 CB LEU A 46 38.044 -4.135 19.458 1.00 14.66 A

ATOM 230 CG LEU A 46 37.545 -4.736 20.780 1.00 17.75 A ATOM 231 CD1 LEU A 46 37.360 -3.634 21.805 1.00 20.21 A

ATOM 232 CD2 LEU A 46 36.236 -5.473 20.542 1.00 17.48 A

ATOM 233 C LEU A 46 38.505 -4.429 17.010 1.00 16.05 A ATOM 234 O LEU A 46 37.463 -4.052 16.467 1.00 14.62 A

ATOM 235 N ALA A 47 39.705 -4.257 16.456 1.00 16.24 A

ATOM 236 CA ALA A 47 39.834 -3.600 15.156 1.00 16.68 A

ATOM 237 CB ALA A 47 41.297 -3.287 14.854 1.00 15.62 A

ATOM 238 C ALA A 47 39.246 -4.448 14.039 1.00 18.38 A

ATOM 239 O ALA A 47 38.759 -3.918 13.040 1.00 18.79 A

ATOM 240 N HIS A 48 39.298 -5.765 14.196 1.00 15.91 A

ATOM 241 CA HIS A 48 38.743 -6.638 13.167 1.00 16.07 A

ATOM 242 CB HIS A 48 39.375 -8.026 13.231 1.00 16.30 A

ATOM 243 CG HIS A 48 39.142 -8.841 11.998 1.00 19.16 A

ATOM 244 CD2 HIS A 48 39.985 -9.209 11.003 1.00 22.54 A

ATOM 245 ND1 HIS A 48 37.905 -9.345 11.656 1.00 16.89 A

ATOM 246 CE1 HIS A 48 37.995 -9.990 10.506 1.00 21.46 A

ATOM 247 NE2 HIS A 48 39.247 -9.922 10.089 1.00 23.03 A

ATOM 248 C HIS A 48 37.227 -6.739 13.343 1.00 16.16 A

ATOM 249 O HIS A 48 36.739 -7.027 14.437 1.00 14.25 A

ATOM 250 N PRO A 49 36.464 -6.504 12.264 1.00 17.59 A

ATOM 251 CD PRO A 49 36.956 -6.131 10.927 1.00 20.42 A

ATOM 252 CA PRO A 49 34.999 -6.552 12.276 1.00 18.90 A

ATOM 253 CB PRO A 49 34.635 -6.369 10.803 1.00 19.01 A

ATOM 254 CG PRO A 49 35.716 -5.516 10.297 1.00 21.90 A

ATOM 255 C PRO A 49 34.371 -7.815 12.849 1.00 16.68 A

ATOM 256 O PRO A 49 33.301 -7.753 13.454 1.00 17.25 A

ATOM 257 N ARG A 50 35.020 -8.960 12.649 1.00 13.28 A

ATOM 258 CA ARG A 50 34.473 -10.223 13.128 1.00 13.07 A

ATOM 259 CB ARG A 50 35.205 -11.401 12.486 1.00 14.41 A

ATOM 260 CG ARG A 50 34.816 -11.641 11.030 1.00 12.99 A

ATOM 261 CD ARG A 50 35.516 -12.872 10.463 1.00 14.15 A

ATOM 262 NE ARG A 50 35.131 -14.100 11.168 1.00 14.34 A

ATOM 263 CZ ARG A 50 35.733 -15.270 10.994 1.00 15.46 A

ATOM 264 NH1 ARG A 50 36.743 -15.371 10.140 1.00 15.57 A

ATOM 265 NH2 ARG A 50 35.330 -16.332 11.671 1.00 15.84 A

ATOM 266 C ARG A 50 34.496 -10.368 14.642 1.00 13.13 A

ATOM 267 O ARG A 50 33.716 -11.139 15.193 1.00 14.18 A

ATOM 268 N VAL A 51 35.382 -9.645 15.319 1.00 11.76 A

ATOM 269 CA VAL A 51 35.439 -9.741 16.774 1.00 11.60 A

ATOM 270 CB VAL A 51 36.795 -9.222 17.302 1.00 10.24 A

ATOM 271 CG1 VAL A 51 36.811 -9.245 18.820 1.00 13.77 A

ATOM 272 CG2 VAL A 51 37.920 -10.083 16.754 1.00 13.31 A

ATOM 273 C VAL A 51 34.273 -8.936 17.356 1.00 13.81 A

ATOM 274 O VAL A 51 34.309 -7.712 17.392 1.00 16.63 A

ATOM 275 N LYS A 52 33.241 -9.644 17.805 1.00 14.11 A

ATOM 276 CA LYS A 52 32.030 -9.022 18.351 1.00 14.27 A

ATOM 277 CB LYS A 52 30.794 -9.876 18.032 1.00 15.62 A

ATOM 278 CG LYS A 52 30.689 -10.374 16.588 1.00 14.74 A

ATOM 279 CD LYS A 52 30.765 -9.227 15.593 1.00 17.23 A

ATOM 280 CE LYS A 52 30.481 -9.680 14.169 1.00 17.95 A

ATOM 281 NZ LYS A 52 30.622 -8.531 13.231 1.00 17.92 A

ATOM 282 C LYS A 52 32.093 -8.866 19.860 1.00 14.99 A

ATOM 283 O LYS A 52 31.310 -8.127 20.465 1.00 16.43 A

ATOM 284 N ARG A 53 33.015 -9.586 20.474 1.00 13.53 A

ATOM 285 CA ARG A 53 33.135 -9.538 21.917 1.00 16.50 A

ATOM 286 CB ARG A 53 32.102 -10.472 22.538 1.00 19.39 A

ATOM 287 CG ARG A 53 32.162 -10.536 24.046 1.00 30.17 A

ATOM 288 CD ARG A 53 31.320 -11.684 24.543 1.00 35.75 A

ATOM 289 NE ARG A 53 30.210 -11.241 25.369 1.00 41.81 A

ATOM 290 CZ ARG A 53 29.213 -12.032 25.748 1.00 44.74 A ATOM 291 NH1 ARG A 53 29.197-13.30025.367 1.0044.68 A ATOM 292 NH2 ARG A 53 28.236 -11.56026.514 1.0046.41 A

ATOM 293 C ARG A 53 34.515 -9.927 22.408 1.0016.44 A

ATOM 294 O ARG A 53 35.197-10.753 21.808 1.0015.60 A

ATOM 295 N VALA 54 34.924 -9.296 23.499 1.0013.78 A

ATOM 296 CA VALA 54 36.201 -9.60524.120 1.0011.86 A

ATOM 297 CB VALA 54 37.228 -8.458 23.978 1.0013.19 A

ATOM 298 CG1 VALA 54 38.543 -8.843 24.669 1.0015.00 A

ATOM 299 CG2VALA 54 37.469 -8.161 22.507 1.0012.35 A A ATTOOMM 3 30000 C C VVAALLAA 5544 35.924 -9.846 25.595 1.0012.49 A

ATOM 301 O VALA 54 35.371 -8.98426.284 1.0014.55 A

ATOM 302 N VALA 55 36.282-11.03726.061 1.0011.41 A

ATOM 303 CA VALA 55 36.113-11.40327.464 1.0013.16 A

ATOM 304 CB VALA 55 35.576-12.84527.635 1.0012.88 A A ATTOOMM 3 30055 C CGG11 VVAALLAA 5555 35.428-13.15429.122 1.0014.18 A

ATOM 306 CG2VALA 55 34.214-13.00026.942 1.0016.91 A

ATOM 307 C VAL A 55 37.503-11.31528.082 1.0012.11 A

ATOM 308 O VALA 55 38.430-11.996 27.648 1.0012.20 A

ATOM 309 N ILEA 56 37.643-10.466 29.093 1.0012.87 A A ATTOOMM 3 31100 C CAA IILLEEAA 5566 38.922-10.28629.761 1.0010.55 A

ATOM 311 CB ILEA 56 39.271 -8.78529.889 1.0013.40 A

ATOM 312 CG2 ILE A 56 40.625 -8.612 30.554 1.0014.69 A

ATOM 313 CG1 ILE A 56 39.284 -8.13328.503 1.0013.13 A

ATOM 314 CD1 ILEA 56 39.575 -6.654 28.529 1.0016.74 A A ATTOOMM 3 31155 C C IILLEEAA 5566 38.817-10.908 31.143 1.0013.77 A

ATOM 316 O ILEA 56 37.924-10.561 31.909 1.0017.04 A

ATOM 317 N ALAA 57 39.706-11.849 31.439 1.0013.75 A

ATOM 318 CA ALAA 57 39.709-12.528 32.734 1.0014.15 A

ATOM 319 CB ALAA 57 40.064-13.993 32.553 1.0015.75 A A ATTOOMM 3 32200 C C AALLAAAA 5577 40.746-11.841 33.608 1.0015.77 A

ATOM 321 O ALAA 57 41.922-11.788 33.257 1.0016.85 A

ATOM 322 N ILEA 58 40.311 -11.299 34.738 1.0017.31 A

ATOM 323 CA ILE A 58 41.234-10.620 35.625 1.0019.97 A

ATOM 324 CB ILE A 58 40.852 -9.144 35.813 1.0021.83 A A ATTOOMM 3 32255 C CGG22 IILLEE AA 5588 40.880 -8.429 34.470 1.0021.64 A

ATOM 326 CG1 ILEA 58 39.471 -9.040 36.452 1.0023.30 A

ATOM 327 CD1 ILEA 58 39.056 -7.618 36.797 1.0024.64 A

ATOM 328 C ILEA 58 41.259-11.29736.985 1.0020.60 A

ATOM 329 O ILE A 58 40.306 -11.97737.373 1.0020.19 A A ATTOOMM 3 33300 N N SSEERRAA 5599 42.351 -11.109 37.711 1.0022.78 A

ATOM 331 CA SERA 59 42.466-11.711 39.029 1.0025.59 A

ATOM 332 CB SERA 59 43.909-11.59039.529 1.0027.11 A

ATOM 333 OG SERA 59 44.007-11.991 40.886 1.0030.40 A

ATOM 334 C SERA 59 41.525-11.010 39.998 1.0026.65 A A ATTOOMM 3 33355 0 O SSEERRAA 5599 41.275 -9.815 39.872 1.0026.71 A

ATOM 336 N PRO A 60 40.958-11.75540.956 1.0026.74 A

ATOM 337 CD PROA 60 41.023-13.20841.184 1.0028.96 A

ATOM 338 CA PRO A 60 40.060-11.10641.913 1.0029.64 A

ATOM 339 CB PROA 60 39.521 -12.27842.733 1.0029.61 A A ATTOOMM 3 34400 C CGG PPRROOAA 6600 40.615-13.30742.633 1.0030.49, A

ATOM 341 C PRO A 60 40.912-10.141 42.733 1.0029.86 A

ATOM 342 O PROA 60 42.033-10.471 43.113 1.0030.44 A

ATOM 343 N GLY A 61 40.398 -8.94642.987 1.0031.62 A

ATOM 344 CA GLY A 61 41.176 -7.97843.739 1.0035.17 A A ATTOOMM 3 34455 C C GGLLYY AA 6611 41.895 -7.00242.818 1.0036.30 A

ATOM 346 O GLY A 61 42.428 -5.981 43.264 1.0037.09 A

ATOM 347 N ASP A 62 41.921 -7.32641.528 1.0036.07 A ATOM 348 CA ASP A 62 42.547 -6.473 40.525 1.00 36.11 A

ATOM 349 CB ASP A 62 42.561 -7.193 39.169 1.00 35.94 A

ATOM 350 CG ASP A 62 43.081 -6.319 38.043 1.00 36.92 A

ATOM 351 OD1 ASP A 62 43.629 -5.233 38.327 1.00 36.70 A ATOM 352 OD2 ASP A 62 42.952 -6.725 36.869 1.00 36.51 A

ATOM 353 C ASP A 62 41.709 -5.200 40.448 1.00 36.34 A

ATOM 354 O ASP A 62 40.633 -5.195 39.853 1.00 35.76 A

ATOM 355 N SER A 63 42.206 -4.126 41.054 1.00 36.41 A

ATOM 356 CA SER A 63 41.485 -2.858 41.081 1.00 36.94 A ATOM 357 CB SER A 63 41.635 -2.212 42.461 1.00 37.51 A

ATOM 358 OG SER A 63 43.001 -1.981 42.767 1.00 39.09 A

ATOM 359 C SER A 63 41.900 -1.848 40.012 1.00 36.43 A

ATOM 360 O SER A 63 41.419 -.715 40.012 1.00 37.48 A

ATOM 361 N ARG A 64 42.781 -2.252 39.104 1.00 35.61 A ATOM 362 CA ARG A 64 43.240 -1.350 38.056 1.00 34.85 A

ATOM 363 CB ARG A 64 44.667 -1.713 37.641 1.00 35.80 A

ATOM 364 CG ARG A 64 45.671 -1.604 38.779 1.00 39.19 A

ATOM 365 CD ARG A 64 47.080 -1.983 38.350 1.00 40.53 A

ATOM 366 NE ARG A 64 48.016 -1.867 39.465 1.00 43.86 A ATOM 367 CZ ARG A 64 49.299 -2.205 39.407 1.00 45.50 A

ATOM 368 NH1 ARG A 64 49.811 -2.688 38.281 1.00 46.56 A

ATOM 369 NH2 ARG A 64 50.071 -2.063 40.477 1.00 45.56 A

ATOM 370 C ARG A 64 42.329 -1.363 36.832 1.00 33.04 A

ATOM 371 O ARG A 64 42.029 -.316 36.261 1.00 32.70 A ATOM 372 N PHE A 65 41.886 -2.552 36.438 1.00 32.15 A

ATOM 373 CA PHE A 65 41.023 -2.709 35.273 1.00 31.23 A

ATOM 374 CB PHE A 65 40.545 -4.157 35.169 1.00 29.22 A

ATOM 375 CG PHE A 65 39.684 -4.420 33.970 1.00 29.52 A

ATOM 376 CD1 PHE A 65 40.256 -4.607 32.716 1.00 28.67 A ATOM 377 CD2 PHE A 65 38.298 -4.427 34.083 1.00 28.69 A

ATOM 378 CE1 PHE A 65 39.460 -4.806 31.593 1.00 29.30 A

ATOM 379 CE2 PHE A 65 37.492 -4.623 32.966 1.00 29.54 A

ATOM 380 CZ PHE A 65 38.076 -4.808 31.718 1.00 28.72 A

ATOM 381 C PHE A 65 39.802 -1.791 35.270 1.00 31.31 A ATOM 382 0 PHE A 65 39.527 -1.117 34.279 1.00 29.65 A

ATOM 383 N ALA A 66 39.069 -1.787 36.380 1.00 32.21 A

ATOM 384 CA ALA A 66 37.859 -.986 36.522 1.00 33.16 A

ATOM 385 CB ALA A 66 37.280 -1.173 37.918 1.00 32.79 A

ATOM 386 C ALA A 66 38.077 .493 36.248 1.00 34.02 A ATOM 387 O ALA A 66 37.134 1.214 35.920 1.00 33.96 A

ATOM 388 N GLN A 67 39.317 .948 36.381 1.00 34.36 A

ATOM 389 CA GLN A 67 39.630 2.352 36.143 1.00 36.22 A

ATOM 390 CB GLN A 67 40.719 2.817 37.113 1.00 38.52 A

ATOM 391 CG GLN A 67 40.355 2.639 38.583 1.00 42.27 A ATOM 392 CD GLN A 67 39.039 3.306 38.958 1.00 44.93 A

ATOM 393 OE1 GLN A 67 38.857 4.508 38.752 1.00 46.46 A

ATOM 394 NE2 GLN A 67 38.109 2.524 39.504 1.00 46.05 A

ATOM 395 C GLN A 67 40.057 2.618 34.698 1.00 36.36 A

ATOM 396 O GLN A 67 40.520 3.714 34.374 1.00 36.17 A ATOM 397 N LEU A 68 39.903 1.612 33.837 1.00 36.05 A

ATOM 398 CA LEU A 68 40.243 1.739 32.419 1.00 35.55 A

ATOM 399 CB LEU A 68 40.969 .481 31.917 1.00 34.55 A

ATOM 400 CG LEU A 68 42.292 .065 32.565 1.00 34.55 A

ATOM 401 CD1 LEU A 68 42.789 -1.223 31.920 1.00 33.68 A ATOM 402 CD2 LEU A 68 43.317 1.173 32.404 1.00 33.49 A

ATOM 403 C LEU A 68 38.959 1.915 31.611 1.00 35.60 A

ATOM 404 O LEU A 68 37.877 1.544 32.063 1.00 35.15 A ATOM 405 N PRO A 69 39.062 2.491 30.403 1 .00 36.84 A

ATOM 406 CD PRO A 69 40.232 3.190 29.845 1 .00 36.87 A

ATOM 407 CA PRO A 69 37.882 2.694 29.554 1 .00 36.73 A

ATOM 408 CB PRO A 69 38.439 3.491 28.376 1 .00 37.94 A

ATOM 409 CG PRO A 69 39.583 4.248 28.991 1 .00 38.08 A

ATOM 410 C PRO A 69 37.264 1.368 29.1 1 1 1.00 36.14 A

ATOM 411 O PRO A 69 36.081 1.297 28.785 1.00 36.69 A

ATOM 412 N LEU A 70 38.079 .319 29.100 1.00 35.78 A

ATOM 413 CA LEU A 70 37.620 -1.006 28.696 1.00 35.23 A

ATOM 414 CB LEU A 70 38.783 -2.000 28.732 1.00 35.52 A

ATOM 415 CG LEU A 70 40.045 -1.634 27.952 1 .00 34.99 A

ATOM 416 CD1 LEU A 70 41.103 -2.685 28.206 1.00 33.53 A

ATOM 417 CD2 LEU A 70 39.735 -1.526 26.469 1.00 34.62 A

ATOM 418 C LEU A 70 36.513 - ^■1 .515 29.614 1 .00 34.82 A

ATOM 419 O LEU A 70 35.705 ^{■ ■}2.352 29.220 1.00 33.40 A

ATOM 420 N ALA A 71 36.485 - 1.001 30.840 1 .00 33.96 A

ATOM 421 CA ALA A 71 35.502 -1.415 31.831 1 .00 34.10 A

ATOM 422 CB ALA A 71 35.847 -.803 33.185 1.00 34.46 A

ATOM 423 C ALA A 71 34.055 - 1.084 31.465 1.00 33.64 A

ATOM 424 O ALA A 71 33.132 - ^■1 .735 31.949 1 .00 34.20 A

ATOM 425 N ASN A 72 33.852 -.075 30.623 1 .00 32.18 A

ATOM 426 CA ASN A 72 32.499 .308 30.237 1.00 30.99 A

ATOM 427 CB ASN A 72 32.217 1.749 30.675 1.00 35.07 A

ATOM 428 CG ASN A 72 32.299 1.926 32.178 1 .00 38.53 A

ATOM 429 OD1 ASN A 72 33.383 2.100 32.736 1 .00 41.67 A

ATOM 430 ND2 ASN A 72 31.151 1.862 32.845 1.00 39.73 A

ATOM 431 C ASN A 72 32.221 .158 28.745 1.00 29.14 A

ATOM 432 O ASN A 72 31.247 .700 28.223 1 .00 28.74 A

ATOM 433 N HIS A 73 33.080 - .588 28.064 1.00 24.55 A

ATOM 434 CA HIS A 73 32.931 -.819 26.633 1.00 19.09 A

ATOM 435 CB HIS A 73 34.244 ^■ -1.347 26.069 1.00 18.76 A

ATOM 436 CG HIS A 73 34.309 -1.341 24.574 1.00 18.54 A

ATOM 437 CD2 HIS A 73 35.074 -.623 23.716 1 .00 18.98 A

ATOM 438 ND1 HIS A 73 33.521 -2.157 23.794 1 .00 18.72 A

ATOM 439 CE1 HIS A 73 33.796 -1.944 22.517 1.00 18.17 A

ATOM 440 NE2 HIS A 73 34.735 -1.017 22.444 1 .00 16.64 A

ATOM 441 C HIS A 73 31.799 -' 1.824 26.410 1.00 16.88 A

ATOM 442 O HIS A 73 31.751 -: 2.874 27.050 1.00 17.17 A

ATOM 443 N PRO A 74 30.869 -1.517 25.492 1.00 15.50 A

ATOM 444 CD PRO A 74 30.798 -.335 24.615 1.00 16.52 A

ATOM 445 CA PRO A 74 29.752 -2.427 25.237 1 .00 16.03 A

ATOM 446 CB PRO A 74 28.876 -1.634 24.258 1 .00 17.38 A

ATOM 447 CG PRO A 74 29.860 -.802 23.515 1.00 16.74 A

ATOM 448 C PRO A 74 30.124 -3.807 24.715 1.00 15.02 A

ATOM 449 O PRO A 74 29.352 -4.753 24.872 1 .00 17.79 A

ATOM 450 N GLN A 75 31.306 ^{■ ■}3.937 24.114 1.00 15.57 A

ATOM 451 CA GLN A 75 31.722 -5.228 23.564 1 .00 14.87 A

ATOM 452 CB GLN A 75 32.374 -5.045 22.190 1 .00 14.55 A

ATOM 453 CG GLN A 75 31.425 -4.520 21.107 1 .00 14.95 A

ATOM 454 CD GLN A 75 32.155 -4.175 19.827 1.00 16.12 A

ATOM 455 OE1 GLN A 75 33.020 -3.300 19.810 1 .00 18.32 A

ATOM 456 NE2 GLN A 75 31.793 -4.836 18.745 1 .00 18.00 A

ATOM 457 C GLN A 75 32.686 ^■ ■5.964 24.472 1.00 16.57 A

ATOM 458 O GLN A 75 33.185 ^■ -7.021 24.100 1 .00 18.71 A

ATOM 459 N ILE A 76 32.939 -5.418 25.659 1 .00 17.02 A

ATOM 460 CA ILE A 76 33.868 - 6.043 26.590 1.00 19.52 A

ATOM 461 CB ILE A 76 34.989 - 5.054 26.983 1 .00 19.64 A ATOM 462 CG2 ILE A 76 35.946 -5.709 27.971 1.00 19.62 A

ATOM 463 CG1 ILE A 76 35.729 -4.595 25.716 1.00 20.83 A

ATOM 464 CD1 ILE A 76 36.846 -3.598 25.971 1.00 22.79 A

ATOM 465 C ILE A 76 33.173 -6.546 27.844 1.00 19.71 A

ATOM 466 O ILE A 76 32.400 -5.823 28.477 1.00 19.91 A

ATOM 467 N THR A 77 33.450 -7.799 28.185 1.00 19.66 A

ATOM 468 CA THR A 77 32.885 -8.430 29.370 1.00 19.52 A

ATOM 469 CB THR A 77 32.070 -9.692 28.995 1.00 23.46 A

ATOM 470 OG1 THR A 77 30.985 -9.325 28.131 1.00 23.56 A A ATTOOMM 4 47711 C CGG22 TTHHRR AA 7777 31.514 -10.362 30.248 1.00 23.02 A

ATOM 472 C THR A 77 34.051 -8.832 30.270 1.00 20.50 A

ATOM 473 O THR A 77 35.046 -9.367 29.796 1.00 16.50 A

ATOM 474 N VAL A 78 33.943 -8.555 31.564 1.00 19.73 A

ATOM 475 CA VAL A 78 35.013 -8.914 32.479 1.00 22.76 A A ATTOOMM 4 47766 C CBB VVAALL AA 7788 35.449 -7.696 33.335 1.00 24.42 A

ATOM 477 CG1 VAL A 78 34.281 -7.221 34.188 1.00 25.84 A

ATOM 478 CG2 VAL A 78 36.627 -8.068 34.205 1.00 25.51 A

ATOM 479 C VAL A 78 34.572 -10.053 33.390 1.00 21.99 A

ATOM 480 O VAL A 78 33.422 -10.092 33.836 1.00 22.76 A A ATTOOMM 4 48811 N N VVAALL AA 7799 35.484 -10.990 33.639 1.00 22.09 A

ATOM 482 CA VAL A 79 35.204 -12.135 34.502 1.00 22.55 A

ATOM 483 CB VAL A 79 34.860 -13.407 33.672 1.00 23.54 A

ATOM 484 CG1 VAL A 79 33.746 -13.103 32.679 1.00 24.21 A

ATOM 485 CG2 VAL A 79 36.096 -13.922 32.945 1.00 23.72 A A ATTOOMM 4 48866 C C VVAALL AA 7799 36.431 -12.420 35.362 1.00 22.28 A

ATOM 487 O VAL A 79 37.540 -11.995 35.031 1.00 18.82 A

ATOM 488 N ASP A 80 36.237 -13.120 36.476 1.00 24.78 A

ATOM 489 CA ASP A 80 37.363 -13.452 37.345 1.00 26.08 A

ATOM 490 CB ASP A 80 36.887 -13.843 38.749 1.00 28.75 A A ATTOOMM 4 49911 C CGG AASSPP AA 8800 36.275 -12.681 39.507 1.00 32.43 A

ATOM 492 OD1 ASP A 80 36.794 -11.545 39.392 1.00 32.71 A

ATOM 493 OD2 ASP A 80 35.286 -12.907 40.240 1.00 34.64 A

ATOM 494 C ASP A 80 38.149 -14.611 36.747 1.00 24.74 A

ATOM 495 O ASP A 80 37.572 -15.632 36.368 1.00 23.08 A A ATTOOMM 4 49966 N N GGLLYY AA 8811 39.464 -14.442 36.668 1.00 26.37 A

ATOM 497 CA GLY A 81 40.320 -15.478 36.126 1.00 29.20 A

ATOM 498 C GLY A 81 40.706 -16.488 37.190 1.00 32.90 A

ATOM 499 O GLY A 81 40.111 -16.510 38.267 1.00 32.69 A

ATOM 500 N GLY A 82 41.707 -17.314 36.900 1.00 34.71 A A ATTOOMM 5 50011 C CAA GGLLYY AA 8822 42.132 -18.318 37.858 1.00 37.44 A

ATOM 502 C GLY A 82 43.603 -18.273 38.213 1.00 38.81 A

ATOM 503 O GLY A 82 44.282 -17.271 37.991 1.00 38.78 A

ATOM 504 N ASP A 83 44.095 -19.377 38.770 1.00 41.09 A

ATOM 505 CA ASP A 83 45.495 -19.485 39.182 1.00 41.46 A A ATTOOMM 5 50066 C CBB AASSPP AA 8833 45.643 -20.595 40.229 1.00 44.43 A

ATOM 507 CG ASP A 83 44.495 -20.612 41.220 1.00 46.67 A

ATOM 508 OD1 ASP A 83 44.130 -19.527 41.731 1.00 47.68 A

ATOM 509 OD2 ASP A 83 43.965 -21.708 41.498 1.00 47.42 A

ATOM 510 C ASP A 83 46.419 -19.771 38.001 1.00 40.47 A A ATTOOMM 5 51111 O O AASSPP AA 8833 47.537 -19.257 37.935 1.00 40.46 A

ATOM 512 N GLU A 84 45.941 -20.599 37.076 1.00 39.89 A

ATOM 513 CA GLU A 84 46.710 -20.979 35.894 1.00 37.95 A

ATOM 514 CB GLU A 84 46.679 -22.504 35.725 1.00 40.74 A

ATOM 515 CG GLU A 84 47.079 -23.291 36.972 1.00 44.79 A A ATTOOMM 5 51166 C CDD GGLLUU AA 8844 48.532 -23.100 37.361 1.00 46.56 A

ATOM 517 OE1 GLU A 84 48.941 -21.948 37.613 1.00 48.27 A

ATOM 518 OE2 GLU A 84 49.275 -24.107 37.393 1.00 48.94 A ATOM 519 C GLU A 84 46.124-20.314 34.647 1.0035.78 A

ATOM 520 O GLU A 84 44.976-19.861 34.656 1.0034.26 A

ATOM 521 N ARG A 85 46.906-20.271 33.572 1.0033.23 A

ATOM 522 CA ARG A 85 46.445-19.658 32.330 1.0032.01 A

ATOM 523 CB ARG A 85 47.542-19.702 31.260 1.0031.90 A

ATOM 524 CG ARG A 85 47.170-18.952 29.984 1.0032.74 A

ATOM 525 CD ARG A 85 48.125-19.250 28.839 1.0034.27 A

ATOM 526 NE ARG A 85 47.629-18.689 27.583 1.0033.13 A

ATOM 527 CZ ARG A 85 47.706-17.403 27.252 1.0035.58 A A ATTOOMM 5 52288 N NHH11 AARRGG AA 8855 48.268-16.534 28.080 1.0034.76 A

ATOM 529 NH2 ARG A 85 47.208-16.983 26.098 1.0034.83 A

ATOM 530 C ARG A 85 45.198-20.363 31.805 1.0031.18 A

ATOM 531 O ARG A 85 44.194-19.720 31.498 1.0028.04 A

ATOM 532 N ALAA 86 45.265-21.689 31.716 1.0029.25 A A ATTOOMM 5 53333 C CAA AALLAAAA 8866 44.142-22.481 31.222 1.0028.41 A

ATOM 534 CB ALAA 86 44.484-23.965 31.271 1.0028.98 A

ATOM 535 C ALAA 86 42.891 -22.203 32.048 1.0027.56 A

ATOM 536 O ALAA 86 41.775-22.221 31.529 1.0024.46 A

ATOM 537 N ASP A 87 43.091 -21.959 33.339 1.0027.52 A A ATTOOMM 5 53388 C CAA AASSPP AA 8877 41.993-21.663 34.235 1.0028.00 A

ATOM 539 CB ASP A 87 42.507-21.521 35.667 1.0032.81 A

ATOM 540 CG ASP A 87 42.645-22.852 36.381 1.0036.33 A

ATOM 541 OD1 ASP A 87 43.153-22.856 37.524 1.0038.82 A

ATOM 542 OD2 ASP A 87 42.245-23.885 35.813 1.0037.71 A A ATTOOMM 5 54433 C C AASSPP AA 8877 41.284-20.378 33.817 1.0025.37 A

ATOM 544 O ASP A 87 40.058-20.331 33.740 1.0022.36 A

ATOM 545 N SERA 88 42.060-19.338 33.540 1.0022.64 A

ATOM 546 CA SERA 88 41.490-18.060 33.136 1.0020.83 A

ATOM 547 CB SERA 88 42.571-16.976 33.118 1.0020.52 A A ATTOOMM 5 54488 O OGG SSEERRAA 8888 43.094-16.763 34.419 1.0021.95 A

ATOM 549 C SERA 88 40.823-18.150 31.767 1.0019.20 A

ATOM 550 O SERA 88 39.808-17.500 31.518 1.0018.81 A

ATOM 551 N VALA 89 41.388-18.953 30.876 1.0020.32 A

ATOM 552 CA VALA 89 40.793-19.098 29.559 1.0020.47 A A ATTOOMM 5 55533 C CBB VVAALLAA 8899 41.733-19.841 28.597 1.0020.38 A

ATOM 554 CG1 VALA 89 41.023-20.119 27.279 1.0021.06 A

ATOM 555 CG2 VAL A 89 42.969-18.993 28.344 1.0021.76 A

ATOM 556 C VALA 89 39.458-19.827 29.652 1.0021.97 A

ATOM 557 O VALA 89 38.503-19.477 28.959 1.0020.86 A A ATTOOMM 5 55588 N N LLEEUU AA 9900 39.382-20.836 30.514 1.0021.28 A

ATOM 559 CA LEU A 90 38.130-21.571 30.685 1.0022.19 A

ATOM 560 CB LEU A 90 38.329-22.758 31.639 1.0024.45 A

ATOM 561 CG LEU A 90 39.000-23.996 31.017 1.0027.30 A

ATOM 562 CD1 LEU A 90 39.320-25.028 32.085 1.0028.23 A A ATTOOMM 5 56633 C CDD22 LLEEUU AA 9900 38.077 -24.589 29.963 1.0028.41 A

ATOM 564 C LEU A 90 37.059-20.632 31.234 1.0021.98 A

ATOM 565 O LEU A 90 35.904-20.684 30.813 1.0021.69 A

ATOM 566 N ALAA 91 37.443-19.772 32.174 1.0020.86 A

ATOM 567 CA ALAA 91 36.503-18.817 32.752 1.0022.55 A A ATTOOMM 5 56688 C CBB AALLAAAA 9911 37.177-18.013 33.866 1.0023.99 A

ATOM 569 C ALAA 91 36.001 -17.881 31.654 1.0023.91 A

ATOM 570 O ALAA 91 34.822-17.536 31.609 1.0024.34 A

ATOM 571 N GLY A 92 36.907-17.473 30.770 1.0023.93 A

ATOM 572 CA GLY A 92 36.525-16.591 29.678 1.0023.53 A A ATTOOMM 5 57733 C C GGLLYY AA 9922 35.536-17.258 28.740 1.0023.71 A

ATOM 574 O GLY A 92 34.570-16.637 28.304 1.0021.27 A

ATOM 575 N LEU A 93 35.776-18.529 28.428 1.0023.99 A ATOM 576 CA LEU A 93 34.898-19.279 27.536 1.0026.50 A

ATOM 577 CB LEU A 93 35.461 -20.683 27.299 1.0027.50 A

ATOM 578 CG LEU A 93 36.800-20.75926.559 1.0028.66 A

ATOM 579 CD1 LEU A 93 37.261 -22.211 26.476 1.0028.62 A

ATOM 580 CD2 LEU A 93 36.646-20.16925.163 1.0029.21 A

ATOM 581 C LEU A 93 33.460-19.384 28.046 1.0029.37 A

ATOM 582 O LEU A 93 32.530-19.552 27.255 1.0027.96 A

ATOM 583 N LYS A 94 33.277-19.290 29.362 1.0030.59 A

ATOM 584 CA LYS A 94 31.940-19.37429.945 1.0032.14 A

ATOM 585 CB LYS A 94 32.032-19.562 31.463 1.0035.43 A

ATOM 586 CG LYS A 94 32.427-20.969 31.890 1.0039.25 A

ATOM 587 CD LYS A 94 32.481-21.109 33.410 1.0043.48 A

ATOM 588 CE LYS A 94 31.180-20.634 34.060 1.0044.76 A

ATOM 589 NZ LYS A 94 29.975-21.339 33.526 1.0047.14 A

ATOM 590 C LYS A 94 31.086-18.152 29.623 1.0032.08 A

ATOM 591 O LYS A 94 29.857-18.224 29.643 1.0032.09 A

ATOM 592 N ALAA 95 31.733-17.031 29.324 1.0030.04 A

ATOM 593 CA ALA A 95 31.005-15.810 28.995 1.0031.62 A

ATOM 594 CB ALAA 95 31.533-14.649 29.825 1.0032.04 A

ATOM 595 C ALAA 95 31.136-15.495 27.510 1.0030.34 A

ATOM 596 O ALAA 95 30.870-14.376 27.082 1.0030.27 A

ATOM 597 N ALAA 96 31.531-16.500 26.733 1.0030.03 A

ATOM 598 CA ALA A 96 31.721-16.34425.297 1.0030.96 A

ATOM 599 CB ALAA 96 32.749-17.35324.803 1.0027.94 A

ATOM 600 C ALAA 96 30.429-16.492 24.505 1.0031.70 A

ATOM 601 O ALAA 96 30.447-16.53323.273 1.0031.99 A

ATOM 602 N GLY A 97 29.306-16.567 25.209 1.0031.51 A

ATOM 603 CA GLY A 97 28.029-16.70524.534 1.0031.57 A

ATOM 604 C GLY A 97 27.970-17.909 23.613 1.0031.63 A

ATOM 605 O GLY A 97 28.521 -18.964 23.916 1.0030.08 A

ATOM 606 N ASP A 98 27.307-17.751 22.474 1.0031.65 A

ATOM 607 CA ASP A 98 27.174-18.847 21.525 1.0031.00 A

ATOM 608 CB ASP A 98 25.748-18.877 20.970 1.0034.71 A

ATOM 609 CG ASP A 98 25.234-17.498 20.617 1.0038.19 A

ATOM 610 OD1 ASP A 98 25.886-16.809 19.803 1.0040.60 A

ATOM 611 OD2 ASP A 98 24.178-17.101 21.159 1.0040.66 A

ATOM 612 C ASP A 98 28.182-18.773 20.382 1.0028.36 A

ATOM 613 O ASP A 98 27.992-19.389 19.338 1.0027.07 A

ATOM 614 N ALAA 99 29.255-18.01720.588 1.0025.77 A

ATOM 615 CA ALAA 99 30.294-17.874 19.575 1.0025.01 A

ATOM 616 CB ALAA 99 31.440-17.03720.117 1.0024.89 A

ATOM 617 C ALAA 99 30.804-19.243 19.146 1.0021.39 A

ATOM 618 O ALAA 99 31.094-20.100 19.980 1.0022.80 A

ATOM 619 N GLN A 100 30.911-19.443 17.839 1.0019.59 A

ATOM 620 CA GLN A 100 31.378-20.712 17.293 1.0018.74 A

ATOM 621 CB GLN A 100 30.834-20.890 15.881 1.0023.69 A

ATOM 622 CG GLN A 100 29.354-21.239 15.812 1.0027.57 A

ATOM 623 CD GLN A 100 28.845-21.221 14.385 1.0029.17 A

ATOM 624 OE1 GLN A 100 29.543-21.644 13.465 1.0029.53 A

ATOM 625 NE2GLNA100 27.625-20.744 14.195 1.0032.90 A

ATOM 626 C GLN A 100 32.895-20.818 17.266 1.0014.95 A

ATOM 627 O GLN A 100 33.434-21.921 17.319 1.0015.67 A

ATOM 628 N TRP A 101 33.564-19.672 17.168 1.0015.59 A

ATOM 629 CA TRP A 101 35.021-19.616 17.133 1.0014.13 A

ATOM 630 CB TRP A 101 35.503-19.196 15.748 1.00 9.98 A

ATOM 631 CG TRP A 101 35.472-20.296 14.731 1.0013.76 A

ATOM 632 CD2TRPA101 36.591 -21.064 14.292 1.0011.85 A ATOM 633 CE2TRPA101 36.111 -22.004 13.353 1.0013.01 A

ATOM 634 CE3TRPA101 37.950-21.064 14.616 1.0014.42 A

ATOM 635 CD1 TRP A 101 34.384-20.775 14.053 1.00 9.90 A

ATOM 636 NE1 TRPA101 34.765-21.802 13.220 1.0015.17 A ATOM 637 CZ2 TRP A 101 36.961 -22.922 12.719 1.0015.51 A

ATOM 638 CZ3 TRP A 101 38.792-21.980 13.987 1.0012.11 A

ATOM 639 CH2TRPA101 38.292-22.899 13.054 1.0014.04 A

ATOM 640 C TRPA101 35.525-18.613 18.164 1.0013.20 A

ATOM 641 0 , TRP A 101 34.943-17.540 18.325 1.0012.54 A ATOM 642 N VAL A 102 36.610-18.970 18.852 1.0012.58 A

ATOM 643 CA VALA102 37.199-18.121 19.887 1.0010.82 A

ATOM 644 CB VALA102 37.119-18.81021.296 1.0013.14 A

ATOM 645 CG1 VAL A 102 37.809-20.170 21.263 1.0015.75 A

ATOM 646 CG2 VAL A 102 37.751 -17.922 22.344 1.0017.16 A ATOM 647 C VALA102 38.650-17.776 19.566 1.0011.95 A

ATOM 648 O VALA 102 39.394-18.606 19.064 1.00 8.83 A

ATOM 649 N LEU A 103 39.032-16.537 19.855 1.0011.68 A

ATOM 650 CA LEU A 103 40.374-16.027 19.603 1.0013.25 A

ATOM 651 CB LEU A 103 40.260-14.725 18.807 1.0016.43 A ATOM 652 CG LEU A 103 41.492-14.099 18.164 1.0020.77 A

ATOM 653 CD1 LEU A 103 41.968-14.963 17.003 1.0017.90 A

ATOM 654 CD2 LEU A 103 41.143-12.704 17.664 1.0019.39 A

ATOM 655 C LEU A 103 41.013-15.740 20.955 1.0012.79 A

ATOM 656 0 LEUA103 40.579-14.83021.654 1.0018.49' A ATOM 657 N VAL A 104 42.023-16.515 21.343 1.0011.23 A

ATOM 658 CA VAL A 104 42.678-16.286 22.635 1.0012.47 A

ATOM 659 CB VAL A 104 43.035-17.616 23.338 1.0013.28 A

ATOM 660 CG1 VALA 104 43.495-17.34324.771 1.0012.32 A

ATOM 661 CG2 VAL A 104 41.831 -18.53923.328 1.0014.21 A ATOM 662 C VAL A 104 43.958-15.483 22.395 1.0011.66 A

ATOM 663 O VAL A 104 44.813-15.892 21.609 1.0011.55 A

ATOM 664 N HIS A 105 44.084-14.341 23.068 1.00 9.57 A

ATOM 665 CA HIS A 105 45.245-13.474 22.893 1.0012.12 A

ATOM 666 CB HIS A 105 44.846-12.252 22.054 1.0013.69 A ATOM 667 CG HIS A 105 46.007-11.401 21.646 1.0012.98 A

ATOM 668 CD2HISA105 47.217-11.73521.139 1.0011.07 A

ATOM 669 ND1 HIS A 105 46.009-10.030 21.775 1.0016.81 A

ATOM 670 CE1 HISA105 47.176 -9.555 21.370 1.0013.31 A

ATOM 671 NE2 HIS A 105 47.926-10.57020.982 1.0016.29 A ATOM 672 C HISA105 45.868-13.004 24.210 1.0011.88 A

ATOM 673 0 HISA105 45.157-12.65725.146 1.0014.50 A

ATOM 674 N ASPA106 47.199-12.997 24.260 1.0014.51 A

ATOM 675 CA ASP A 106 47.950-12.560 25.440 1.0016.77 A

ATOM 676 CB ASP A 106 49.456-12.713 25.207 1.0019.46 A ATOM 677 CG ASP A 106 49.930-14.148 25.305 1.0025.68 A

ATOM 678 OD1 ASPA106 51.126-14.38625.045 1.0027.29 A

ATOM 679 OD2 ASP A 106 49.119-15.03525.647 1.0028.74 A

ATOM 680 C ASPA106 47.683-11.101 25.800 1.0017.71 A

ATOM 681 O ASP A 106 47.667-10.22924.937 1.0017.66 A ATOM 682 N ALAA 107 47.506-10.837 27.087 1.0018.96 A

ATOM 683 CA ALA A 107 47.253 -9.48627.556 1.0016.60 A

ATOM 684 CB ALA A 107 46.922 -9.51329.044 1.0018.05 A

ATOM 685 C ALAA 107 48.469 -8.590 27.309 1.0018.01 A

ATOM 686 0 ALAA 107 48.325 -7.382 27.121 1.0019.04 A ATOM 687 N ALAA108 49.653 -9.194 27.293 1.0018.15 A

ATOM 688 CA ALAA 108 50.909 -8.464 27.120 1.0019.18 A

ATOM 689 CB ALAA 108 51.934 -8.988 28.121 1.0018.64 A ATOM 690 C ALA A 108 51.519 - 8.469 25.721 1.00 18.92 A

ATOM 691 O ALA A 108 52.737 - ^■8.345 25.572 1.00 20.22 A

ATOM 692 N ARG A 109 50.686 -8.616 24.700 1 .00 17.71 A

ATOM 693 CA ARG A 109 51.155 -8.602 23.319 1.00 18.18 A

ATOM 694 CB ARG A 109 50.842 -9.934 22.638 1.00 19.45 A

ATOM 695 CG ARG A 109 51.798 -11.058 22.986 1.00 19.92 A

ATOM 696 CD ARG A 109 51.473 -12.301 22.174 1.00 23.69 A

ATOM 697 NE ARG A 109 52.216 -13.469 22.630 1.00 24.1 1 A

ATOM 698 CZ ARG A 109 53.478 -13.739 22.309 1.00 25.77 A

ATOM 699 NH1 ARG A 109 54.16Ξ 1 -12.928 21.516 1.00 26.52 A

ATOM 700 NH2 ARG A 109 54.062 ! -14.827 22.791 1.00 27.51 A

ATOM 701 C ARG A 109 50.432 -7.460 22.609 1.00 16.63 A

ATOM 702 O ARG A 109 49.456 -7.682 21.891 1.00 18.47 A

ATOM 703 N PRO A 1 10 50.915 -6.220 22.798 1.00 17.10 A

ATOM 704 CD PRO A 110 52.039 -5.870 23.691 1.00 18.96 A

ATOM 705 CA PRO A 110 50.333 -5.018 22.207 1.00 16.23 A

ATOM 706 CB PRO A 110 50.769 -3.938 23.180 1.00 17.38 A

ATOM 707 CG PRO A 110 52.189 -4.357 23.481 1.00 18.64 A

ATOM 708 C PRO A 1 10 50.733 -4.674 20.782 1.00 17.09 A

ATOM 709 O PRO A 1 10 50.193 -3.727 20.218 1.00 19.37 A

ATOM 710 N CYS A 111 51.656 ^■ -5.433 20.198 1.00 14.99 A

ATOM 71 1 CA CYS A 11 1 52.128 -5.125 18.849 1.00 17.77 A

ATOM 712 CB CYS A 1 1 1 53.644 -5.313 18.783 1 .00 17.59 A

ATOM 713 SG CYS A 11 1 54.537 -4.31 1 19.974 1.00 18.48 A

ATOM 714 C CYS A 111 51.474 • -5.883 17.701 1.00 15.78 A

ATOM 715 O CYS A 111 51.935 -5.795 16.561 1.00 20.08 A

ATOM 716 N LEU A 112 50.398 - ^■6.608 17.998 1.00 16.26 A

ATOM 717 CA LEU A 112 49.667 -7.377 16.990 1.00 16.16 A

ATOM 718 CB LEU A 1 12 48.443 -8.052 17.627 1.00 12.66 A

ATOM 719 CG LEU A 112 47.468 -8.791 16.698 1 .00 16.58 A

ATOM 720 CD1 LEU A 112 48.210 -9.871 15.924 1.00 16.49 A

ATOM 721 CD2 LEU A 112 46.325 -9.395 17.513 1.00 14.62 A

ATOM 722 C LEU A 1 12 49.21 1 - •6.495 15.833 1.00 16.47 A

ATOM 723 O LEU A 1 12 48.654 ^■ •5.417 16.051 1.00 17.96 A

ATOM 724 N HIS A 113 49.443 -( 3.965 14.608 1.00 17.36 A

ATOM 725 CA HIS A 113 49.059 ^■ -6.238 13.394 1.00 20.09 A

ATOM 726 CB HIS A 1 13 50.197 • -6.260 12.374 1.00 25.35 A

ATOM 727 CG HIS A 1 13 51.254 -5.232 12.631 1.00 32.50 A

ATOM 728 CD2 HIS A 1 13 51.434 -4.380 13.669 1.00 34.74 A

ATOM 729 ND1 HIS A 113 52.283 -4.985 11.750 1.00 35.42 A

ATOM 730 CE1 HIS A 1 13 53.052 -4.024 12.232 1.00 36.57 A

ATOM 731 NE2 HIS A 113 52.558 -3.640 13.395 1.00 36.42 A

ATOM 732 C HIS A 113 47.808 -( 3.823 12.755 1.00 19.36 A

ATOM 733 O HIS A 1 13 47.582 -I 3.029 12.801 1.00 16.81 A

ATOM 734 N GLN A 114 47.013 ^■ -5.956 12.136 1.00 18.97 A

ATOM 735 CA GLN A 1 14 45.773 -6.347 11.490 1 .00 18.43 A

ATOM 736 CB GLN A 1 14 45.044 -5.099 10.994 1.00 19.15 A

ATOM 737 CG GLN A 114 44.577 -4.208 12.125 1.00 19.02 A

ATOM 738 CD GLN A 114 43.71 1 -4.972 13.114 1.00 20.79 A

ATOM 739 OE1 GLN A 1 14 42.679 -5.536 12.740 1.00 18.91 A

ATOM 740 NE2 GLN A 114 44.132 -5.006 14.378 1.00 19.10 A

ATOM 741 C GLN A 114 45.906 ^■ -7.347 10.354 1.00 16.93 A

ATOM 742 O GLN A 1 14 45.015 ^■ -8.174 10.158 1.00 17.61 A

ATOM 743 N ASP A 115 46.996 - ■7.284 9.595 1.00 20.42 A

ATOM 744 CA ASP A 115 47.148 -8.231 8.501 1.00 19.94 A

ATOM 745 CB ASP A 1 15 48.328 -7.857 7.595 1.00 26.74 A

ATOM 746 CG ASP A 115 49.501 -7.295 8.361 1.00 33.24 A ATOM 747 OD1 ASPA115 49.731 -7.729 9.509 1.0036.12 A

ATOM 748 OD2 ASP A 115 50.203 -6.421 7.803 1.0037.38 A

ATOM 749 C ASP A 115 47.316 -9.650 9.038 1.0017.93 A

ATOM 750 O ASP A 115 46.716-10.580 8.515 1.0018.48 A ATOM 751 N ASPA116 48.130 -9.814 10.079 1.0017.16 A

ATOM 752 CA ASPA116 48.325-11.137 10.670 1.0013.43 A

ATOM 753 CB ASP A 116 49.367-11.106 11.797 1.0015.71 A

ATOM 754 CG ASP A 116 50.785-10.956 11.282 1.0018.25 A

ATOM 755 OD1 ASP A 1.16 51.021 -11.177 10.071 1.0022.27 A ATOM 756 OD2ASPA116 51.672-10.644 12.102 1.0021.50 A

ATOM 757 C ASP A 116 46.998-11.630 11.244 1.0013.26 A

ATOM 758 0 ASPA116 46.587-12.783 11.031 1.0013.86 A

ATOM 759 N LEU A 117 46.317-10.753 11.972 1.0013.44 A

ATOM 760 CA LEU A 117 45.046-11.119 12.574 1.0012.31 A ATOM 761 CB LEUA117 44.467 -9.940 13.361 1.0013.58 A

ATOM 762 CG LEU A 117 43.093-10.181 14.006 1.0011.80 A

ATOM 763 CD1 LEUA117 43.134-11.466 14.837 1.0015.45 A

ATOM 764 CD2LEUA117 42.717 -8.986 14.887 1.0013.79 A

ATOM 765 C LEUA117 44.056-11.576 11.514 1.0012.12 A ATOM 766 0 LEUA117 43.411 -12.599 11.681 1.0012.32 A

ATOM 767 N ALAA 118 43.958-10.827 10.415 1.0013.60 A

ATOM 768 CA ALAA118 43.034-11.177 9.349 1.0011.41 A

ATOM 769 CB ALAA 118 43.026-10.072 8.282 1.0012.83 A

ATOM 770 C ALAA118 43.352-12.532 8.714 1.0013.87 A ATOM 771 O ALAA118 42.445-13.302 8.390 1.0014.88 A

ATOM 772 N ARGA119 44.635-12.833 8.548 1.0013.87 A.

ATOM 773 CA ARGA119 45.028-14.106 7.952 1.0015.14 A

ATOM 774 CB ARG A 119 46.508-14.062 7.568 1.0015.90 A

ATOM 775 CG ARG A 119 46.744-13.247 6.286 1.0020.12 A ATOM 776 CD ARG A 119 48.216-13.054 5.963 1.0022.73 A

ATOM 777 NE ARG A 119 48.949 14.297 6.123 1.0027.58 A

ATOM 778 CZ ARG A 119 49.855-14.510 7.070 1.0027.85 A

ATOM 779 NH1 ARGA119 50.147-13.550 7.939 1.0029.62 A

ATOM 780 NH2ARGA119 50.450-15.691 7.159 1.0027.30 A ATOM 781 C ARGA119 44.739-15.251 8.916 1.0014.62 A

ATOM 782 0 ARGA119 44.417-16.363 8.495 1.0015.97 A

ATOM 783 N LEUA120 44.842-14.972 10.213 1.0013.88 A

ATOM 784 CA LEU A 120 44.555-15.989 11.210 1.0012.37 A

ATOM 785 CB LEU A 120 44.937-15.499 12.607 1.0011.78 A ATOM 786 CG LEU A 120 44.670-16.502 13.741 1.00 8.70 A

ATOM 787 CD1 LEUA120 45.526-17.749 13.544 1.0013.27 A

ATOM 788 CD2LEUA120 44.990-15.846 15.084 1.0010.15 A

ATOM 789 C LEUA120 43.066-16.328 11.182 1.0014.67 A

ATOM 790 O LEUA120 42.683-17.503 11.169 1.0010.18 A ATOM 791 N LEU A 121 42.222-15.300 11.155 1.0013.67 A

ATOM 792 CA LEU A 121 40.778-15.515 11.141 1.0013.47 A

ATOM 793 CB LEU A 121 40.035-14.182 11.284 1.0014.29 A

ATOM 794 CG LEU A 121 40.298-13.500 12.630 1.0017.41 A

ATOM 795 CD1 LEUA121 39.610-12.153 12.646 1.0019.73 A ATOM 796 CD2LEUA121 39.813-14.377 13.774 1.0021.64 A

ATOM 797 C LEUA121 40.276-16.257 9.911 1.0012.02 A

ATOM 798 0 LEU A 121 39.204-16.862 9.947 1.0012.55 A

ATOM 799 N ALAA 122 41.043-16.224 8.827 1.0014.76 A

ATOM 800 CA ALA A 122 40.634-16.926 7.614 1.0014.23 A ATOM 801 CB ALAA 122 41.604-16.624 6.473 1.0018.76 A

ATOM 802 C ALAA 122 40.548-18.438 7.845 1.0015.49 A

ATOM 803 O ALAA 122 39.884-19.142 7.096 1.0015.88 A ATOM 804 N LEU A 123 41.220-18.933 8.884 1.0013.57 A

ATOM 805 CA LEU A 123 41.199-20.355 9.178 1.0014.42 A

ATOM 806 CB LEU A 123 42.078-20.663 10.392 1.0015.14 A

ATOM 807 CG LEU A 123 43.584-20.476 10.225 1.0017.02 A ATOM 808 CD1 LEUA123 44.263-20.668 11.578 1.0018.65 A

ATOM 809 CD2 LEU A 123 44.131 -21.471 9.208 1.0018.23 A

ATOM 810 C LEU A 123 39.807-20.940 9.407 1.0015.97 A

ATOM 811 O LEU A 123 39.604-22.127 9.181 1.0017.79 A

ATOM 812 N SERA 124 38.842-20.134 9.844 1.0014.36 A ATOM 813 CA SERA124 37.504-20.679 10.080 1.0017.77 A

ATOM 814 CB SERA 124 36.617-19.670 10.840 1.0016.39 A

ATOM 815 OG SERA 124 36.484-18.444 10.156 1.0017.43 A

ATOM 816 C SERA 124 36.814-21.135 8.800 1.0021.52 A

ATOM 817 O SER A 124 35.833-21.872 8.857 1.0022.89 A ATOM 818 N GLU A 125 37.331-20.720 7.648 1.0025.43 A

ATOM 819 CA GLU A 125 36.728-21.098 6.371 1.0030.20 A

ATOM 820 CB GLU A 125 36.746-19.906 5.413 1.0033.50 A

ATOM 821 CG GLU A 125 36.392-18.583 6.076 1.0038.90 A

ATOM 822 CD GLU A 125 34.984-18.560 6.637 1.0042.32 A ATOM 823 OE1 GLU A 125 34.805-18.063 7.773 1.0042.43 A

ATOM 824 OE2GLUA125 34.055-19.029 5.941 1.0042.68 A

ATOM 825 C GLU A 125 37.441-22.279 5.711 1.0032.83 A

ATOM 826 O GLU A 125 36.950-22.835 4.723 1.0033.97 A

ATOM 827 N THR A 126 38.596-22.663 6.251 1.0033.85 A ATOM 828 CA THR A 126 39.364-23.765 5.677 1.0035.96 A

ATOM 829 CB THR A 126 40.602-23.241 4.932 1.0037.11 A

ATOM 830 OG1 THR A 126 41.457-22.546 5.849 1.0037.88 A

ATOM 831 CG2THRA126 40.193-22.299 3.817 1.0039.26 A

ATOM 832 C THR A 126 39.846-24.802 6.688 1.0036.26 A ATOM 833 O THR A 126 40.568-25.732 6.326 1.0036.88 A

ATOM 834 N SERA 127 39.455-24.651 7.948 1.0033.28 A

ATOM 835 CA SER A 127 39.886-25.590 8.979 1.0032.06 A

ATOM 836 CB SER A 127 41.133-25.044 9.681 1.0031.98 A

ATOM 837 OG SER A 127 41.516-25.867 10.768 1.0030.61 A ATOM 838 C SERA 127 38.810-25.882 10.020 1.0031.11 A

ATOM 839 O SERA 127 37.950-25.048 10.290 1.0030.07 A

ATOM 840 N ARG A 128 38.861-27.077 10.597 1.0031.72 A

ATOM 841 CA ARG A 128 37.909-27.462 11.632 1.0032.38 A

ATOM 842 CB ARG A 128 37.206-28.775 11.273 1.0035.73 A ATOM 843 CG ARG A 128 36.128-28.655 10.208 1.0038.72 A

ATOM 844 CD ARG A 128 35.500-30.010 9.925 1.0041.24 A

ATOM 845 NE ARG A 128 34.516-29.955 8.847 1.0042.38 A

ATOM 846 CZ ARG A 128 33.311 -29.404 8.954 1.0042.29 A

ATOM 847 NH1 ARG A 128 32.925-28.855 10.099 1.0040.71 A ATOM 848 NH2ARGA128 32.489-29.402 7.913 1.0041.94 A

ATOM 849 C ARG A 128 38.646-27.630 12.953 1.0030.99 A

ATOM 850 O ARG A 128 38.054-28.015 13.955 1.0030.26 A

ATOM 851 N THR A 129 39.945-27.337 12.944 1.0028.93 A

ATOM 852 CA THR A 129 40.766-27.461 14.142 1.0027.52 A ATOM 853 CB THR A 129 41.988-28.365 13.872 1.0029.50 A

ATOM 854 OG1 THR A 129 41.535-29.671 13.495 1.0030.04 A

ATOM 855 CG2THRA129 42.862-28.477 15.110 1.0031.06 A

ATOM 856 C THR A 129 41.248-26.095 14.618 1.0025.08 A

ATOM 857 O THR A 129 41.413-25.872 15.816 1.0025.13 A ATOM 858 N GLYA130 41.461-25.182 13.674 1.0020.33 A

ATOM 859 CA GLY A 130 41.933-23.852 14.025 1.0019.42 A

ATOM 860 C GLYA130 43.440-23.749 13.856 1.0015.78 A ATOM 861 O GLY A 130 44.050-24.609 13.234 1.0017.44 A

ATOM 862 N GLY A 131 44.048-22.715 14.427 1.0012.10 A

ATOM 863 CA GLY A 131 45.483-22.538 14.287 1.0012.38 A

ATOM 864 C GLY A 131 46.004-21.365 15.096 1.0012.12 A

ATOM 865 O GLY A 131 45.257-20.765 15.855 1.0010.17 A

ATOM 866 N ILE A 132 47.280-21.035 14.936 1.0012.54 A

ATOM 867 CA ILE A 132 47.883-19.948 15.691 1.0013.32 A

ATOM 868 CB ILE A 132 48.668-20.476 16.903 1.0013.35 A

ATOM 869 CG2ILEA132 47.801-21.432 17.696 1.0013.94 A

ATOM 870 CG1 ILE A 132 49.926-21.200 16.434 1.0013.72 A

ATOM 871 CD1 ILE A 132 50.884-21.599 17.560 1.0013.89 A

ATOM 872 C ILE A 132 48.861-19.136 14.859 1.0013.30 A

ATOM 873 O ILE A 132 ^* 49.316-19.573 13.793 1.0010.62 A

ATOM 874 N LEU A 133 49.169-17.938 15.340 1.0011.52 A

ATOM 875 CA LEU A 133 50.168-17.107 14.681 1.0010.97 A

ATOM 876 CB LEU A 133 49.993-15.635 15.058 1.0014.16 A

ATOM 877 CG LEU A 133 48.889-14.879 14.303 1.0012.06 A

ATOM 878 CD1 LEU A 133 48.904-13.406 14.726 1.0014.52 A

ATOM 879 CD2LEUA133 49.116-15.002 12.785 1.0014.14 A

ATOM 880 C LEU A 133 51.513-17.615 15.183 1.0013.35 A

ATOM 881 O LEU A 133 51.670-17.937 16.360 1.0012.40 A

ATOM 882 N ALAA 134 52.468-17.721 14.270 1.0011.69 A

ATOM 883 CA ALA A 134 53.807-18.198 14.607 1.0012.80 A

ATOM 884 CB ALA A 134 53.869-19.726 14.510 1.0014.58 A

ATOM 885 C ALAA 134 54.853-17.578 13.693 1.0015.81 A

ATOM 886 O ALAA 134 54.554-17.153 12.576 1.0016.25 A

ATOM 887 N ALAA 135 56.085-17.528 14.181 1.0015.38 A

ATOM 888 CA ALAA 135 57.180-16.963 13.413 1.0018.24 A

ATOM 889 CB ALAA 135 57.779-15.782 14.152 1.0018.05 A

ATOM 890 C ALAA 135 58.211 -18.056 13.228 1.0019.21 A

ATOM 891 O ALAA 135 58.537-18.771 14.172 1.0017.25 A

ATOM 892 N PRO A 136 58.716-18.225 12.000 1.0021.79 A

ATOM 893 CD PRO A 136 58.266-17.601 10.743 1.0024.33 A

ATOM 894 CA PRO A 136 59.718-19.262 11.736 1.0023.21 A

ATOM 895 CB PRO A 136 59.898-19.192 10.219 1.0024.80 A

ATOM 896 CG PRO A 136 58.575-18.673 9.735 1.0026.80 A

ATOM 897 C PRO A 136 61.031-19.010 12.480 1.0023.50 A

ATOM 898 O PRO A 136 61.458-17.867 12.641 1.0023.63 A

ATOM 899 N VAL A 137 61.668-20.079 12.943 1.0023.67 A

ATOM 900 CA VAL A 137 62.935-19.943 13.648 1.0026.07 A

ATOM 901 CB VAL A 137 63.324-21.259 14.356 1.0025.68 A

ATOM 902 CG1 VAL A 137 64.699-21.126 15.003 1.0026.40 A

ATOM 903 CG2VALA137 62.284-21.598 15.401 1.0026.39 A

ATOM 904 C VAL A 137 64.033-19.564 12.656 1.0026.57 A

ATOM 905 O VALA 137 64.162-20.172 11.592 1.0025.54 A

ATOM 906 N ARG A 138 64.817-18.554 13.010 1.0029.06 A

ATOM 907 CA ARG A 138 65.900-18.079 12.158 1.0032.25 A

ATOM 908 CB ARG A 138 65.889-16.548 12.110 1.0035.01 A

ATOM 909 CG ARG A 138 64.535-15.923 11.793 1.0038.28 A

ATOM 910 CD ARG A 138 64.017-16.329 10.422 1.0041.58 A

ATOM 911 NE ARG A 138 62.809-15.584 10.064 1.0044.85 A

ATOM 912 CZ ARG A 138 62.180-15.684 8.896 1.0045.49 A

ATOM 913 NH1 ARG A 138 62.636-16.501 7.957 1.0045.87 A

ATOM 914 NH2ARGA138 61.094-14.959 8.666 1.0046.20 A

ATOM 915 C ARG A 138 67.258-18.560 12.669 1.0031.97 A

ATOM 916 O ARG A 138 68.027-19.177 11.935 1.0035.21 A

ATOM 917 N ASP A 139 67.541 -18.274 13.933 1.0032.82 A ATOM 918 CA ASP A 139 68.803-18.650 14.555 1.0031.03 A

ATOM 919 CB ASP A 139 68.837-18.127 15.991 1.0035.68 A

ATOM 920 CG ASP A 139 68.474-16.654 16.090 1.0039.16 A

ATOM 921 OD1 ASP A 139 69.320-15.803 15.747 1.0041.17 A

ATOM 922 OD2ASPA139 67.332-16.361 16.503 1.0043.42 A

ATOM 923 C ASP A 139 69.046-20.154 14.590 1.0027.87 A

ATOM 924 O ASP A 139 68.112-20.952 14.509 1.0027.06 A

ATOM 925 N THR A 140 70.314-20.530 14.703 1.0024.30 A

ATOM 926 CA THR A 140 70.680-21.928 14.810 1.0021.14 A

ATOM 927 CB THR A 140 72.187-22.139 14.561 1.0022.23 A

ATOM 928 OG1 THR A 140 72.475-21.885 13.182 1.0021.88 A

ATOM 929 CG2THRA140 72.603-23.561 14.919 1.0022.96 A

ATOM 930 C THR A 140 70.342-22.272 16.254 1.0021.73 A

ATOM 931 O THR A 140 70.667-21.516 17.172 1.0018.42 A

ATOM 932 N MET A 141 69.678-23.403 16.463 1.0018.59 A

ATOM 933 CA MET A 141 69.283-23.806 17.808 1.0019.96 A

ATOM 934 CB MET A 141 67.811 -24.230 17.811 1.0021.51 A

ATOM 935 CG MET A 141 66.856-23.184 17.241 1.0025.41 A

ATOM 936 SD MET A 141 66.986-21.560 18.060 1.0017.06 A

ATOM 937 CE MET A 141 66.221 -21.915 19.563 1.0027.99 A

ATOM 938 C MET A 141 70.133-24.937 18.352 1.0019.10 A

ATOM 939 O MET A 141 70.534-25.833 17.612 1.0018.10 A

ATOM 940 N LYS A 142 70.403-24.886 19.651 1.0017.32 A

ATOM 941 CA LYS A 142 71.192-25.91520.313 1.0018.18 A

ATOM 942 CB LYS A 142 72.483-25.32420.893 1.0019.02 A

ATOM 943 CG LYS A 142 73.368-24.569 19.910 1.0017.78 A

ATOM 944 CD LYS A 142 73.942-25.472 18.833 1.0015.70 A

ATOM 945 CE LYS A 142 74.884-24.686 17.938 1.0015.17 A

ATOM 946 NZ LYS A 142 75.530-25.531 16.897 1.0015.59 A

ATOM 947 C LYS A 142 70.407-26.53321.468 1.0018.62 A

ATOM 948 O LYS A 142 69.684-25.84022.181 1.0017.28 A

ATOM 949 N ARG A 143 70.552-27.84021.642 1.0022.22 A

ATOM 950 CA ARG A 143 69.911 -28.53822.743 1.0023.73 A

ATOM 951 CB ARG A 143 69.330-29.87722.286 1.0026.64 A

ATOM 952 CG ARG A 143 68.822-30.75923.423 1.0031.34 A

ATOM 953 CD ARG A 143 67.630-30.13624.130 1.0033.12 A

ATOM 954 NE ARG A 143 66.473 -30.04923.242 1.0033.98 A

ATOM 955 CZ ARG A 143 65.340 -29.42723.548 1.0035.27 A

ATOM 956 NH1 ARG A 143 65.206-28.83224.724 1.0034.19 A

ATOM 957 NH2ARGA143 64.341 -29.40222.675 1.0035.32 A

ATOM 958 C ARG A 143 71.038-28.78623.730 1.0024.33 A

ATOM 959 O ARG A 143 72.062 -29.37023.370 1.0022.85 A

ATOM 960 N ALA A 144 70.864-28.331 24.964 1.0024.49 A

ATOM 961 CA ALA A 144 71.887-28.51625.985 1.0027.63 A

ATOM 962 CB ALAA 144 71.717-27.48027.090 1.0027.11 A

ATOM 963 C ALA A 144 71.788-29.913 26.569 1.0030.21 A

ATOM 964 O ALAA 144 70.735-30.54926.505 1.0028.83 A

ATOM 965 N GLU A 145 72.891-30.39527.124 1.0032.42 A

ATOM 966 CA GLU A 145 72.888-31.71027.736 1.0035.15 A

ATOM 967 CB GLU A 145 74.317-32.20027.952 1.0036.58 A

ATOM 968 CG GLU A 145 75.078-32.35226.654 1.0040.24 A

ATOM 969 CD GLU A 145 76.378-33.10526.817 1.0043.79 A

ATOM 970 OE1 GLU A 145 77.244 -32.64327.591 1.0044.06 A

ATOM 971 OE2GLUA145 76.527-34.16726.174 1.0045.67 A

ATOM 972 C GLU A 145 72.152-31.59429.060 1.0035.81 A

ATOM 973 O GLU A 145 72.264 -30.58429.756 1.0035.23 A

ATOM 974 N PRO A 146 71.383-32.62929.423 1.0036.57 A ATOM 975 CD PRO A 146 71.317-33.945 28.765 1.0037.78 A

ATOM 976 CA PRO A 146 70.620-32.630 30.672 1.0038.88 A

ATOM 977 CB PRO A 146 70.002-34.029 30.694 1.0038.91 A

ATOM 978 CG PRO A 146 70.985-34.851 29.916 1.0039.01 A ATOM 979 C PRO A 146 71.426-32.321 31.928 1.0038.94 A

ATOM 980 O PRO A 146 72.326-33.071 32.299 1.0039.80 A

ATOM 981 N GLYA147 71.101 -31.200 32.565 1.0039.50 A

ATOM 982 CA GLY A 147 71.779-30.820 33.788 1.0040.63 A

ATOM 983 C GLY A 147 72.932-29.841 33.691 1.0041.03 A ATOM 984 O GLY A 147 73.437-29.394 34.723 1.0041.24 A

ATOM 985 N LYS A 148 73.362-29.494 32.481 1.0040.80 A

ATOM 986 CA LYS A 148 74.478-28.559 32.350 1.0041.09 A

ATOM 987 CB LYS A 148 75.804-29.315 32.487 1.0043.02 A

ATOM 988 CG LYS A 148 75.922-30.559 31.634 1.0044.82 A ATOM 989 CD LYS A 148 77.203-31.304 31.973 1.0046.04 A

ATOM 990 CE LYS A 148 77.309-32.616 31.212 1.0047.64 A

ATOM 991 NZ LYS A 148 78.531 -33.375 31.613 1.0048.80 A

ATOM 992 C LYS A 148 74.485-27.718 31.080 1.0039.86 A

ATOM 993 O LYS A 148 73.754-27.997 30.133 1.0038.94 A ATOM 994 N ASN A 149 75.322-26.684 31.079 1.0039.20 A

ATOM 995 CA ASN A 149 75.438-25.778 29.942 1.0038.48 A

ATOM 996 CB ASN A 149 75.851-24.379 30.420 1.0040.65 A

ATOM 997 CG ASN A 149 74.692-23.591 31.007 1.0042.32 A

ATOM 998 OD1 ASN A 149 74.838-22.41331.339 1.0044.71 A ATOM 999 ND2ASNA149 73.535-24.233 31.133 1.0042.35 A

ATOM 1000 C ASN A 149 76.405-26.247 28.859 1.0036.56 A

ATOM 1001 O ASN A 149 77.265-25.490 28.415 1.0035.90 A

ATOM 1002 N ALA A 150 76.265-27.500 28.443 1.0034.82 A

ATOM 1003 CA ALAA 150 77.105-28.054 27.390 1.0031.22 A ATOM 1004 CB ALAA 150 77.848-29.28527.891 1.0032.48 A

ATOM 1005 C ALAA 150 76.171-28.428 26.243 1.0030.16 A

ATOM 1006 O ALA A 150 75.058-28.904 26.474 1.0026.62 A

ATOM 1007 N ILE A 151 76.615-28.197 25.010 1.0026.58 A

ATOM 1008 CA ILE A 151 75.805-28.504 23.837 1.0025.41 A ATOM 1009 CB ILE A 151 76.349-27.801 22.573 1.0026.65 A

ATOM 1010 CG2 ILEA 151 75.533-28.219 21.356 1.0027.05 A

ATOM 1011 CG1 ILEA 151 76.305-26.282 22.759 1.0026.83 A

ATOM 1012 CD1 ILEA 151 76.862-25.510 21.581 1.0026.44 A

ATOM 1013 C ILE A 151 75.738-29.998 23.544 1.0025.85 A ATOM 1014 O ILE A 151 76.760-30.641 23.306 1.0022.07 A

ATOM 1015 N ALA A 152 74.527-30.543 23.558 1.0024.82 A

ATOM 1016 CA ALAA 152 74.327-31.95423.256 1.0025.61 A

ATOM 1017 CB ALAA 152 72.971 -32.419 23.793 1.0026.97 A

ATOM 1018 C ALAA 152 74.379-32.115 21.738 1.0024.46 A ATOM 1019 O ALA A 152 75.088-32.970 21.211 1.0023.85 A

ATOM 1020 N HIS A 153 73.617-31.283 21.036 1.0024.67 A

ATOM 1021 CA HIS A 153 73.580-31.322 19.583 1.0024.68 A

ATOM 1022 CB HIS A 153 72.908-32.610 19.095 1.0028.30 A

ATOM 1023 CG HIS A 153 71.510-32.790 19.599 1.0029.87 A ATOM 1024 CD2 HIS A 153 70.317-32.447 19.058 1.0031.70 A

ATOM 1025 ND1 HIS A 153 71.226-33.363 20.821 1.0031.07 A

ATOM 1026 CE1 HIS A 153 69.918-33.36521.010 1.0032.69 A

ATOM 1027 NE2HISA153 69.344-32.814 19.955 1.0031.92 A

ATOM 1028 C HIS A 153 72.797-30.120 19.073 1.0023.95 A ATOM 1029 O HIS A 153 72.210-29.374 19.860 1.0022.59 A

ATOM 1030 N THR A 154 72.800-29.932 17.759 1.0021.70 A

ATOM 1031 CA THRA154 72.075-28.832 17.134 1.0024.21 A ATOM 1032 CB THR A 154 72.782-28.354 15.847 1.0024.72 A

ATOM 1033 OG1THRA154 74.059-27.797 16.180 1.0021.79 A

ATOM 1034 CG2THRA154 71.954-27.297 15.135 1.0024.37 A

ATOM 1035 C THR A 154 70.677-29.316 16.769 1.0024.31 A ATOM 1036 O THR A 154 70.514-30.412 16.237 1.0025.51 A

ATOM 1037 N VAL A 155 69.671-28.501 17.068 1.0024.64 A

ATOM 1038 CA VAL A 155 68.289-28.846 16.754 1.0026.89 A

ATOM 1039 CB VALA 155 67.327-28.285 17.823 1.0027.09 A

ATOM 1040 CG1 VAL A 155 65.883-28.450 17.369 1.0026.63 A ATOM 1041 CG2VALA155 67.548-29.009 19.150 1.0026.37 A

ATOM 1042 C VAL A 155 67.925-28.263 15.393 1.0027.39 A

ATOM 1043 O VALA 155 68.016-27.056 15.191 1.0028.03 A

ATOM 1044 N ASP A 156 67.517-29.123 14.463 1.0028.13 A

ATOM 1045 CA ASPA156 67.144-28.686 13.123 1.0030.49 A ATOM 1046 CB ASP A 156 66.578-29.863 12.327 1.0033.54 A

ATOM 1047 CG ASP A 156 66.654-29.644 10.828 1.0036.97 A

ATOM 1048 OD1 ASP A 156 66.264-28.557 10.361 1.0036.97 A

ATOM 1049 OD2 ASP A 156 67.101-30.564 10.117 1.0040.34 A

ATOM 1050 C ASP A 156 66.087-27.592 13.231 1.0030.33 A ATOM 1051 O ASP A 156 64.991 -27.835 13.734 1.0028.83 A

ATOM 1052 N ARG A 157 66.412-26.392 12.760 1.0030.07 A

ATOM 1053 CA ARG A 157 65.469-25.282 12.835 1.0031.99 A

ATOM 1054 CB ARG A 157 66.210-23.942 12.824 1.0032.24 A

ATOM 1055 CG ARG A 157 66.844-23.559 11.496 1.0035.50 A ATOM 1056 CD ARG A 157 67.567-22.225 11.623 1.0036.83 A

ATOM 1057 NE ARG A 157 68.201 -21.799 10.380 1.0039.56 A

ATOM 1058 CZ ARG A 157 67.542-21.450 9.279 1.0041.25 A

ATOM 1059 NH1 ARG A 157 66.216-21.476 9.257 1.0041.35 A

ATOM 1060 NH2ARGA157 68.212-21.067 8.200 1.0041.73 A ATOM 1061 C ARG A 157 64.443-25.307 11.711 1.0032.45 A

ATOM 1062 O ARG A 157 63.503-24.515 11.706 1.0030.04 A

ATOM 1063 N ASN A 158 64.625-26.214 10.760 1.0032.54 A

ATOM 1064 CA ASN A 158 63.696-26.335 9.647 1.0033.71 A

ATOM 1065 CB ASN A 158 64.305-27.205 8.546 1.0037.98 A ATOM 1066 CG ASN A 158 63.351 -27.436 7.389 1.0041.42 A

ATOM 1067 OD1 ASN A 158 62.845-26.489 6.783 1.0043.61 A

ATOM 1068 ND2ASNA158 63.108-28.703 7.070 1.0043.14 A

ATOM 1069 C ASN A 158 62.393-26.950 10.152 1.0031.21 A

ATOM 1070 O ASN A 158 62.379-28.070 10.663 1.0030.10 A ATOM 1071 N GLY A 159 61.298-26.212 10.008 1.0028.44 A

ATOM 1072 CA GLY A 159 60.016-26.705 10.473 1.0026.58 A

ATOM 1073 C GLY A 159 59.798-26.386 11.942 1.0024.02 A

ATOM 1074 O GLY A 159 58.865-26.886 12.564 1.0021.02 A

ATOM 1075 N LEU A 160 60.670-25.550 12.496 1.0022.36 A ATOM 1076 CA LEUA160 60.573-25.149 13.896 1.0021.71 A

ATOM 1077 CB LEU A 160 61.952-25.171 14.554 1.0022.54 A

ATOM 1078 CG LEU A 160 61.982-25.095 16.081 1.0023.43 A

ATOM 1079 CD1 LEU A 160 61.317-26.329 16.678 1.0022.78 A

ATOM 1080 CD2LEUA160 63.429-24.994 16.553 1.0023.28 A ATOM 1081 C LEU A 160 60.004-23.737 13.906 1.0020.61 A

ATOM 1082 O LEU A 160 60.465-22.867 13.164 1.0020.82 A

ATOM 1083 N TRPA161 59.005-23.512 14.753 1.0019.44 A

ATOM 1084 CA TRP A 161 58.342-22.216 14.818 1.0018.39 A

ATOM 1085 CB TRP A 161 56.937-22.317 14.198 1.0018.58 A ATOM 1086 CG TRP A 161 56.879-22.686 12.730 1.0021.47 A

ATOM 1087 CD2 TRP A 161 56.373-21.868 11.670 1.0022.44 A

ATOM 1088 CE2 TRP A 161 56.491-22.611 10.472 1.0023.10 A ATOM 1089 CE3TRPA161 55.823-20.580 11.617 1.0024.37 A

ATOM 1090 CD1 TRP A 161 57.280 -23.862 12.147 ι1.0022.79 A

ATOM 1091 NE1TRPA161 57.048-23.821 10.791 oO 22.67 A

ATOM 1092 CZ2TRPA161 56.089-22.100 9.230 1.0026.00 A ATOM 1093 CZ3TRPA161 55.423-20.073 10.387 1.0026.39 A

ATOM 1094 CH2TRPA161 55.555-20.835 9.209 1.0027.16 A

ATOM 1095 C TRPA161 58.183-21.670 16.231 1.0015.37 A

ATOM 1096 O TRPA161 58.079-22.427 17.189 1.0015.87 A

ATOM 1097 N HISA162 58.173-20.344 16.343 1.0016.40 A ATOM 1098 CA HISA162 57.949-19.664 17.607 1.0017.13 A

ATOM 1099 CB HISA162 58.565-18.263 17.590 1.0019.43 A

ATOM 1100 CG HIS A 162 60.046-18.243 17.775 1.0024.18 A

ATOM 1101 CD2HISA162 60.797-18.004 18.873 1.0023.64 A

ATOM 1102 ND1 HIS A 162 60.932-18.472 16.744 1.0027.34 A ATOM 1103 CE1 HIS A 162 62.167-18.372 17.202 1.0026.03 A

ATOM 1104 NE2HISA162 62.113-18.088 18.490 1.0027.35 A

ATOM 1105 C HIS A 162 56.427-19.509 17.706 1.0015.26 A

ATOM 1106 O HIS A 162 55.823-18.880 16.840 1.0017.66 A

ATOM 1107 N ALA A 163 55.809-20.073 18.738 1.0013.97 A ATOM 1108 CA ALA A 163 54.362-19.952 18.902 1.0013.57 A

ATOM 1109 CB ALAA 163 53.862-20.976 19.901 1.0014.57 A

ATOM 1110 C ALAA163 54.034-18.552 19.391 1.0014.53 A

ATOM 1111 0 ALA A 163 54.675-18.042 20.314 1.0016.45 A

ATOM 1112 N LEUA164 53.065-17.898 18.757 1.0013.14 A ATOM 1113 CA LEUA164 52.670-16.553 19.204 1.0011.47 A

ATOM 1114 CB LEU A 164 52.984-15.514 18.120 1.0013.09 A

ATOM 1115 CG LEU A 164 54.448-15.463 17.633 1.0014.10 A

ATOM 1116 CD1 LEU A 164 54.539-14.520 16.440 1.0017.90 A

ATOM 1117 CD2 LEU A 164 55.363-15.000 18.753 1.0016.79 A ATOM 1118 C LEUA164 51.169-16.600 19.463 1.0012.44 A

ATOM 1119 0 LEUA164 50.603-17.681 19.589 1.0012.56 A

ATOM 1120 N THRA165 50.534-15.445 19.620 1.0012.78 A

ATOM 1121 CA THRA165 49.085-15.391 19.802 1.0011.52 A

ATOM 1122 CB THRA165 48.645-15.233 21.300 1.0011.71 A ATOM 1123 OG1 THR A 165 48.793-13.876 21.724 1.0012.61 A

ATOM 1124 CG2 THR A 165 49.488-16.113 22.200 1.0014.85 A

ATOM 1125 C THRA165 48.659-14.175 18.981 1.0011.86 A

ATOM 1126 0 THRA165 49.478-13.303 18.681 1.0012.37 A

ATOM 1127 N PROA166 47.373-14.082 18.628 1.0010.19 A ATOM 1128 CD PRO A 166 46.851-12.904 17.917 1.0011.81 A

ATOM 1129 CA PROA166 46.275-14.997 18.941 1.0010.40 A

ATOM 1130 CB PRO A 166 45.063-14.307 18.315 1.0012.38 A

ATOM 1131 CG PRO A 166 45.404-12.891 18.365 1.0011.90 A

ATOM 1132 C PRO A 166 46.364-16.441 18.469 1.0012.81 A ATOM 1133 0 PROA166 47.119-16.791 17.550 1.0010.98 A

ATOM 1134 N GLNA167 45.540-17.251 19.129 1.0011.38 A

ATOM 1135 CA GLN A 167 45.376-18.666 18.848 1.0010.22 A

ATOM 1136 CB GLN A 167 45.898-19.489 20.026 1.0011.32 A

ATOM 1137 CG GLNA167 47.367-19.167 20.284 1.0011.76 A ATOM 1138 CD GLN A 167 48.173-20.327 20.833 1.0013.08 A

ATOM 1139 OE1 GLN A 167 47.624-21.33221.292 1.0014.71 A

ATOM 1140 NE2 GLN A 167 49.494-20.18420.797 1.0013.26 A

ATOM 1141 C GLN A 167 43.863-18.754 18.636 1.0011.42 A

ATOM 11420 GLNA167 43.078-18.354 19.490 1.0013.10 A ATOM 1143 N PHEA168 43.485-19.262 17.469 1.0010.38 A

ATOM 1144 CA PHE A 168 42.104-19.303 16.997 1.00 9.78 A

ATOM 1145 CB PHEA168 42.121 -18.586 15.638 1.00 9.64 A ATOM 1146 CG PHE A 168 40.775-18.236 15.103 1.00 9.45 A

ATOM 1147 CD1 PHE A 168 39.814-17.659 15.917 1.0010.13 A

ATOM 1148 CD2 PHE A 168 40.469-18.471 13.770 1.0013.27 A

ATOM 1149 CE1 PHE A 168 38.566-17.315 15.412 1.0011.77 A ATOM 1150 CE2 PHE A 168 39.225-18.129 13.262 1.0012.71 A

ATOM 1151 CZ PHE A 168 38.270-17.554 14.084 1.0013.44 A

ATOM 1152 C PHE A 168 41.526-20.710 16.862 1.00 9.50 A

ATOM 1153 O PHE A 168 41.988-21.484 16.030 1.0011.15 A

ATOM 1154 N PHE A 169 40.513-21.049 17.655 1.0011.61 A ATOM 1155 CA PHE A 169 39.950-22.400 17.565 1.0011.09 A

ATOM 1156 CB PHE A 169 40.533-23.312 18.663 1.0013.00 A

ATOM 1157 CG PHE A 169 42.023-23.199 18.853 1.0015.57 A

ATOM 1158 CD1 PHE A 169 42.542-22.401 19.861 1.0016.47 A

ATOM 1159 CD2 PHE A 169 42.897-23.947 18.074 1.0018.54 A ATOM 1160 CE1 PHE A 169 43.907-22.348 20.093 1.0018.21 A

ATOM 1161 CE2PHEA169 44.272-23.902 18.297 1.0018.21 A

ATOM 1162 CZ PHE A 169 44.773-23.104 19.314 1.0016.26 A

ATOM 1163 C PHE A 169 38.436-22.442 17.740 1.0011.01 A

ATOM 1164 O PHE A 169 37.827-21.490 18.205 1.0012.13 A ATOM 1165 N PROA170 37.803-23.552 17.333 1.0013.08 A

ATOM 1166 CD PRO A 170 38.293-24.621 16.447 1.0013.96 A

ATOM 1167 CA PRO A 170 36.351 -23.636 17.523 1.0013.24 A

ATOM 1168 CB PRO A 170 36.010-25.010 16.953 1.0013.11 A

ATOM 1169 CG PRO A 170 36.996-25.159 15.834 1.0013.87 A ATOM 1170 C PROA170 36.168-23.573 19.055 1.0014.27 A

ATOM 1171 O PRO A 170 36.904-24.223 19.793 1.0015.64 A

ATOM 1172 N ARG A 171 35.203-22.784 19.516 1.0015.38 A

ATOM 1173 CA ARG A 171 34.944-22.56820.943 1.0016.47 A

ATOM 1174 CB ARG A 171 33.707-21.671 21.089 1.0019.58 A ATOM 1175 CG ARG A 171 33.499-21.04522.464 1.0024.53 A

ATOM 1176 CD ARG A 171 32.538-21.84323.341 1.0032.28 A

ATOM 1177 NE ARG A 171 31.163-21.82522.837 1.0039.17 A

ATOM 1178 CZ ARG A 171 30.141 -22.43323.433 1.0041.43 A

ATOM 1179 NH1 ARG A 171 30.329-23.110 24.558 1.0043.39 A ATOM 1180 NH2ARGA171 28.930-22.36422.904 1.0043.43 A

ATOM 1181 C ARG A 171 34.773-23.82321.798 1.0015.64 A

ATOM 1182 O ARGA171 35.511 -24.041 22.765 1.0015.62 A

ATOM 1183 N GLU A 172 33.811-24.66521.443 1.0016.65 A

ATOM 1184 CA GLU A 172 33.586-25.851 22.249 1.0015.38 A ATOM 1185 CB GLU A 172 32.235-26.506 21.879 1.0014.49 A

ATOM 1186 CG GLU A 172 31.091 -25.81022.641 1.0017.62 A

ATOM 1187 CD GLU A 172 29.674-26.221 22.232 1.0015.62 A

ATOM 1188 OE1 GLU A 172 29.455-27.37921.803 1.0016.63 A

ATOM 1189 OE2 GLU A 172 28.765-25.38222.373 1.0016.16 A ATOM 1190 C GLU A 172 34.758-26.82422.220 1.0015.30 A

ATOM 1191 O GLU A 172 35.094-27.42623.244 1.0015.03 A

ATOM 1192 N LEUA173 35.404-26.96421.066 1.0015.19 A

ATOM 1193 CA LEU A 173 36.556-27.86520.957 1.0015.54 A

ATOM 1194 CB LEU A 173 37.074-27.912 19.515 1.0016.17 A ATOM 1195 CG LEU A 173 38.302-28.780 19.253 1.0019.39 A

ATOM 1196 CD1 LEU A 173 37.989-30.242 19.554 1.0022.96 A

ATOM 1197 CD2LEUA173 38.736-28.613 17.800 1.0021.76 A

ATOM 1198 C LEUA173 37.664-27.38721.893 1.0016.30 A

ATOM 1199 O LEUA173 38.293-28.19622.577 1.0016.75 A ATOM 1200 N LEU A 174 37.902-26.076 21.923 1.0015.80 A

ATOM 1201 CA LEU A 174 38.935-25.52622.802 1.0017.81 A

ATOM 1202 CB LEU A 174 39.064-24.00722.613 1.0018.63 A ATOM 1203 CG LEU A 174 40.204-23.35323.424 1.0020.38 A

ATOM 1204 CD1 LEU A 174 41.551 -23.921 22.968 1.0022.36 A

ATOM 1205 CD2 LEU A 174 40.196-21.840 23.223 1.0020.45 A

ATOM 1206 C LEU A 174 38.560-25.82424.243 1.0018.39 A ATOM 1207 O LEU A 174 39.398-26.230 25.041 1.0019.22 A

ATOM 1208 N HISA175 37.289-25.616 24.571 1.0016.07 A

ATOM 1209 CA HIS A 175 36.804-25.87525.922 1.0018.44 A

ATOM 1210 CB HIS A 175 35.301 -25.59526.002 1.0020.30 A

ATOM 1211 CG HIS A 175 34.657-26.07427.267 1.0026.13 A ATOM 1212 CD2 HIS A 175 34.076-27.259 27.578 1.0024.95 A

ATOM 1213 ND1 HIS A 175 34.573-25.29928.403 1.0027.10 A

ATOM 1214 CE1 HIS A 175 33.970-25.98329.359 1.0027.70 A

ATOM 1215 NE2 HIS A 175 33.659-27.17628.884 1.0028.69 A

ATOM 1216 C HISA175 37.060-27.32626.325 1.0018.42 A ATOM 1217 O HIS A 175 37.607-27.59327.393 1.0020.46 A

ATOM 1218 N ASP A 176 36.663-28.260 25.470 1.0020.15 A

ATOM 1219 CA ASP A 176 36.829-29.671 25.783 1.0018.85 A

ATOM 1220 CB ASP A 176 36.087-30.52424.757 1.0019.63 A

ATOM 1221 CG ASP A 176 34.597-30.27024.777 1.0020.97 A ATOM 1222 OD1 ASP A 176 34.129-29.69325.777 1.0020.22 A

ATOM 1223 OD2 ASP A 176 33.912-30.64423.801 1.0021.93 A

ATOM 1224 C ASP A 176 38.275-30.12225.894 1.0019.46 A

ATOM 1225 0 ASP A 176 38.631 -30.88026.799 1.0020.15 A

ATOM 1226 N CYSA177 39.113-29.63524.989 1.0018.28 A ATOM 1227 CA CYS A 177 40.522-30.00324.996 1.0020.61 A ATOM 1228 CB CYS A 177 41.215-29.469 23.750 1.0019.81 A

ATOM 1229 SG CYS A 177 40.782-30.39322.277 1.0016.88 A

ATOM 1230 C CYSA177 41.261 -29.51226.226 1.0022.14 A

ATOM 1231 O CYSA177 42.071 -30.23626.802 1.0021.55 A ATOM 1232 N LEU A 178 40.995-28.27826.624 1.0022.35 A

ATOM 1233 CA LEU A 178 41.663-27.74327.795 1.0026.07 A

ATOM 1234 CB LEU A 178 41.582-26.21727.795 1.0028.55 A

ATOM 1235 CG LEU A 178 42.714-25.64026.937 1.0031.41 A

ATOM 1236 CD1 LEU A 178 42.177-24.63425.944 1.0035.20 A ATOM 1237 CD2 LEU A 178 43.759-25.012 27.835 1.0033.45 A

ATOM 1238 C LEU A 178 41.083-28.339 29.070 1.0025.60 A

ATOM 1239 O LEU A 178 41.780-28.489 30.077 1.0025.60 A

ATOM 1240 N THR A 179 39.810-28.70329.020 1.0024.95 A

ATOM 1241 CA THRA179 39.165-29.306 30.177 1.0025.40 A ATOM 1242 CB THR A 179 37.649-29.43329.960 1.0024.57 A

ATOM 1243 OG1 THR A 179 37.037-28.14930.145 1.0022.07 A

ATOM 1244 CG2 THR A 179 37.049-30.43730.942 1.0025.77 A

ATOM 1245 C THR A 179 39.759-30.690 30.411 1.0027.23 A

ATOM 1246 O THR A 179 40.062-31.057 31.546 1.0027.48 A ATOM 1247 N ARG A 180 39.934-31.45029.334 1.0028.52 A

ATOM 1248 CA ARG A 180 40.488-32.79529.440 1.0031.50 A

ATOM 1249 CB ARG A 180 40.269-33.56628.136 1.0033.72 A

ATOM 1250 CG ARG A 180 40.901-34.947 28.138 1.0036.92 A

ATOM 1251 CD ARG A 180 40.499-35.75726.916 1.0040.93 A ATOM 1252 NE ARG A 180 41.208-37.032 26.861 1.0043.91 A

ATOM 1253 CZ ARG A 180 40.912-38.02226.026 1.0045.94 A

ATOM 1254 NH1 ARG A 180 39.911-37.89325.167 1.0046.67 A

ATOM 1255 NH2 ARG A 180 41.618-39.14626.052 1.0047.09 A

ATOM 1256 C ARG A 180 41.974-32.77729.786 1.0032.83 A ATOM 1257 O ARG A 180 42.429-33.549 30.628 1.0033.15 A

ATOM 1258 N ALAA 181 42.723-31.89229.135 1.0033.00 A

ATOM 1259 CA ALAA 181 44.159-31.77829.377 1.0034.41 A ATOM 1260 CB ALAA 181 44.744-30.651 28.523 1.0032.92 A

ATOM 1261 C ALAA 181 44.448-31.521 30.854 1.0035.71 A

ATOM 1262 O ALAA 181 45.376-32.097 31.423 1.0034.97 A

ATOM 1263 N LEU A 182 43.649-30.654 31.467 1.0036.77 A ATOM 1264 CA LEU A 182 43.818-30.31932.876 1.0039.13 A

ATOM 1265 CB LEU A 182 42.981 -29.091 33.232 1.0038.77 A

ATOM 1266 CG LEU A 182 43.462-27.746 32.688 1.0040.00 A

ATOM 1267 CD1 LEU A 182 42.441 -26.672 33.019 1.0039.19 A

ATOM 1268 CD2 LEU A 182 44.821 -27.39633.293 1.0039.21 A ATOM 1269 C LEU A 182 43.435-31.470 33.800 1.0041.08 A

ATOM 1270 O LEU A 182 44.134-31.750 34.774 1.0041.29 A

ATOM 1271 N ASNA183 42.321 -32.12833.495 1.0042.14 A

ATOM 1272 CA ASN A 183 41.845-33.242 34.305 1.0044.22 A

ATOM 1273 CB ASN A 183 40.520-33.77633.755 1.0045.30 A ATOM 1274 CG ASN A 183 39.970-34.92934.578 1.0047.82 A

ATOM 1275 OD1 ASN A 183 39.182-35.739 34.086 1.0049.08 A

ATOM 1276 ND2ASNA183 40.376-35.001 35.843 1.0049.10 A

ATOM 1277 C ASN A 183 42.858-34.378 34.341 1.0044.98 A

ATOM 1278 O ASN A 183 43.010-35.057 35.358 1.0045.78 A ATOM 1279 N GLU A 184 43.546-34.58933.225 1.0044.35 A

ATOM 1280 CA GLU A 184 44.536-35.653 33.136 1.0044.82 A

ATOM 1281 CB GLU A 184 44.546-36.23631.720 1.0045.55 A

ATOM 1282 CG GLU A 184 43.309-37.058 31.391 1.0047.02 A

ATOM 1283 CD GLU A 184 43.304-37.57529.968 1.0047.31 A ATOM 1284 OE1 GLU A 184 44.341 -38.10329.517 1.0049.13 A

ATOM 1285 OE2 GLU A 184 42.259-37.46529.297 1.0049.40 A

ATOM 1286 C GLU A 184 45.934-35.18733.524 1.0044.36 A

ATOM 1287 O GLU A 184 46.915-35.89833.307 1.0044.23 A

ATOM 1288 N GLYA185 46.017-33.992 34.101 1.0044.38 A ATOM 1289 CA GLY A 185 47.299-33.45434.524 1.0044.47 A

ATOM 1290 C GLY A 185 48.365-33.401 33.444 1.0044.39 A

ATOM 1291 O GLY A 185 49.514-33.776 33.680 1.0044.75 A

ATOM 1292 N ALAA 186 47.994-32.929 32.259 1.0043.68 A

ATOM 1293 CA ALAA186 48.936-32.827 31.154 1.0042.71 A ATOM 1294 CB ALAA 186 48.192-32.899 29.826 1.0042.94 A

ATOM 1295 C ALAA186 49.722-31.52531.242 1.0041.91 A

ATOM 1296 0 ALAA 186 49.251 -30.545 31.818 1.0041.89 A

ATOM 1297 N THR A 187 50.925-31.52630.678 1.0041.92 A

ATOM 1298 CA THRA187 51.776-30.341 30.675 1.0041.18 A ATOM 1299 CB THR A 187 53.240-30.708 30.364 1.0042.41 A

ATOM 1300 OG1 THR A 187 53.703-31.67731.313 1.0044.02 A

ATOM 1301 CG2THRA187 54.128-29.473 30.431 1.0043.11 A

ATOM 1302 C THR A 187 51.268-29.386 29.602 1.0039.68 A

ATOM 1303 O THR A 187 51.479-29.611 28.411 1.0040.32 A ATOM 1304 N ILE A 188 50.602-28.320 30.031 1.0037.50 A

ATOM 1305 CA ILE A 188 50.043-27.34429.104 1.0035.51 A

ATOM 1306 CB ILE A 188 48.575-27.02529.469 1.0036.05 A

ATOM 1307 CG2 ILE A 188 47.942-26.16428.385 1.0036.62 A

ATOM 1308 CG1 ILEA 188 47.789-28.32529.624 1.0037.60 A ATOM 1309 CD1 ILE A 188 46.371-28.12730.108 1.0038.78 A

ATOM 1310 C ILE A 188 50.827-26.032 29.074 1.0032.55 A

ATOM 1311 O ILE A 188 51.164-25.472 30.119 1.0032.59 A

ATOM 1312 N THRA189 51.115-25.55427.867 1.0027.88 A

ATOM 1313 CA THR A 189 51.819-24.29627.681 1.0025.45 A ATOM 1314 CB THR A 189 53.035-24.45826.742 1.0024.62 A

ATOM 1315 OG1 THR A 189 52.666-25.25525.612 1.0022.11 A

ATOM 1316 CG2 THR A 189 54.191 -25.13527.478 1.0025.89 A ATOM 1317 C THR A 189 50.816-23.314 27.089 1.0023.45 A

ATOM 1318 O THR A 189 50.216-22.523 27.822 1.0024.18 A

ATOM 1319 N ASPA190 50.614-23.36525.775 1.0020.98 A

ATOM 1320 CA ASP A 190 49.642-22.47525.143 1.0017.54 A ATOM 1321 CB ASP A 190 50.218-21.83823.865 1.0016.47 A

ATOM 1322 CG ASP A 190 50.681-22.85422.830 1.0016.26 A

ATOM 1323 OD1 ASP A 190 50.635-24.06823.075 1.0015.78 A

ATOM 1324 OD2 ASP A 190 51.111 -22.432 21.730 '1.0015.44 A

ATOM 1325 C ASP A 190 48.357-23.257 24.833 1.0015.97 A ATOM 1326 O ASPA190 48.256-24.436 25.149 1.0017.40 A

ATOM 1327 N GLU A 191 47.368-22.58224.257 1.0016.07 A

ATOM 1328 CA GLUA191 46.110-23.221 23.938 1.0015.95 A

ATOM 1329 CB GLU A 191 45.088-22.20523.413 1.0015.82 A

ATOM 1330 CG GLU A 191 44.532-21.24324.467 1.0020.72 A ATOM 1331 CD GLU A 191 45.597-20.32525.049 1.0019.71 A

ATOM 1332 OE1 GLU A 191 46.362-19.73824.266 1.0019.33 A

ATOM 1333 OE2 GLU A 191 45.658-20.17626.281 1.0021.42 A

ATOM 1334 C GLU A 191 46.322-24.32222.906 1.0014.63 A

ATOM 1335 O GLUA191 45.683-25.382 22.958 1.0016.14 A ATOM 1336 N ALAA192 47.230-24.094 21.968 1.0014.56 A

ATOM 1337 CA ALAA 192 47.496-25.094 20.944 1.0013.41 A

ATOM 1338 CB ALAA 192 48.591 -24.596 19.993 1.0017.89 A

ATOM 1339 C ALAA192 47.918-26.40321.598 1.0016.28 A

ATOM 1340 O ALAA 192 47.444-27.46321.217 1.0016.63 A ATOM 1341 N SERA 193 48.782-26.323 22.606 1.0016.39 A

ATOM 1342 CA SERA 193 49.261-27.533 23.276 1.0015.48 A

ATOM 1343 CB SER A 193 50.290-27.182 24.359 1.0013.46 A

ATOM 1344 OG SER A 193 49.689-26.58525.484 1.0017.16 A

ATOM 1345 C SERA193 48.129-28.35723.885 1.0017.93 A ATOM 1346 0 SERA193 48.295-29.54824.115 1.0017.02 A

ATOM 1347 N ALAA194 46.988-27.730 24.154 1.0016.15 A

ATOM 1348 CA ALAA 194 45.861-28.464 24.716 1.0018.81 A

ATOM 1349 CB ALAA 194 44.854-27.51625.334 1.0019.68 A

ATOM 1350 C ALAA 194 45.219-29.28723.602 1.0018.96 A ATOM 1351 O ALAA 194 44.805-30.43523.813 1.0019.05 A

ATOM 1352 N LEUA195 45.135-28.70522.411 1.0018.92 A

ATOM 1353 CA LEU A 195 44.575-29.41821.267 1.0020.22 A

ATOM 1354 CB LEU A 195 44.428-28.47420.066 1.0021.80 A

ATOM 1355 CG LEU A 195 43.147-27.642 19.922 1.0026.42 A ATOM 1356 CD1 LEU A 195 42.016-28.540 19.487 1.0029.21 A

ATOM 1357 CD2 LEU A 195 42.828-26.93521.226 1.0025.36 A

ATOM 1358 C LEU A 195 45.501-30.568 20.898 1.0019.61 A

ATOM 1359 O LEU A 195 45.053-31.676 20.597 1.0019.39 A

ATOM 1360 N GLU A 196 46.801-30.29520.928 1.0018.68 A ATOM 1361 CA GLUA196 47.819-31.290 20.595 1.0019.13 A

ATOM 1362 CB GLU A 196 49.207-30.654 20.728 1.0020.13 A

ATOM 1363 CG GLU A 196 49.504-29.573 19.687 1.0018.83 A

ATOM 1364 CD GLU A 196 50.605-28.62520.124 1.0020.54 A

ATOM 1365 OE1 GLU A 196 51.591-29.09220.733 1.0018.89 A ATOM 1366 OE2 GLU A 196 50.496-27.408 19.848 1.0017.61 A

ATOM 1367 C GLUA196 47.710-32.49821.519 1.0021.16 A

ATOM 1368 O GLU A 196 47.795-33.635 21.070 1.0019.34 A

ATOM 1369 N TYR A 197 47.516-32.237 22.807 1.0022.93 A

ATOM 1370 CA TYR A 197 47.400-33.301 23.796 1.0026.31 A ATOM 1371 CB TYRA 197 47.220-32.701 25.186 1.0028.90 A

ATOM 1372 CG TYR A 197 47.015-33.727 26.272 1.0034.05 A

ATOM 1373 CD1 TYRA 197 48.059-34.55026.688 1.0036.50 A ATOM 1374 CE1 TYR A 197 47.866-35.50627.683 1.0039.04 A

ATOM 1375 CD2 TYR A 197 45.770-33.88326.876 1.0035.94 A

ATOM 1376 CE2 TYR A 197 45.565-34.836 27.869 1.0038.21 A

ATOM 1377 CZ TYR A 197 46.617-35.64328.267 1.0038.24 A ATOM 1378 OH TYR A 197 46.416-36.58729.248 1.0039.16 A

ATOM 1379 C TYR A 197 46.235-34.24323.495 1.0026.99 A

ATOM 1380 O TYR A 197 46.293-35.43623.795 1.0025.99 A

ATOM 1381 N CYSA198 45.175-33.69622.911 1.0025.50 A

ATOM 1382 CA CYS A 198 43.990-34.47022.571 1.0027.08 A ATOM 1383 CB CYS A 198 42.740-33.59922.758 1.0026.29 A

ATOM 1384 SG CYS A 198 42.546-32.95324.467 1.0021.86 A

ATOM 1385 C CYSA198 44.019-35.05521.155 1.0026.83 A

ATOM 1386 0 CYS A 198 42.986-35.48220.631 1.0027.50 A

ATOM 1387 N GLY A 199 45.197-35.04920.533 1.0025.56 A ATOM 1388 CA GLY A 199 45.352-35.623 19.207 1.0024.91 A

ATOM 1389 C GLYA199 45.151 -34.718 18.008 1.0024.69 A

ATOM 1390 O GLY A 199 45.142-35.193 16.870 1.0022.99 A

ATOM 1391 N PHE A 200 44.992-33.421 18.247 1.0024.89 A

ATOM 1392 CA PHE A 200 44.795-32.475 17.161 1.0026.64 A ATOM 1393 CB PHE A 200 43.781-31.407 17.576 1.0027.11 A

ATOM 1394 CG PHE A 200 42.405-31.949 17.824 1.0027.64 A

ATOM 1395 CD1 PHE A 200 42.003-32.314 19.101 1.0027.27 A

ATOM 1396 CD2PHEA200 41.525-32.139 16.768 1.0028.29 A

ATOM 1397 CE1 PHEA200 40.741-32.865 19.324 1.0028.86 A ATOM 1398 CE2 PHE A 200 40.262-32.690 16.980 1.0027.76 A

ATOM 1399 CZ PHE A 200 39.874-33.052 18.260 1.0027.71 A

ATOM 1400 C PHEA200 46.091 -31.814 16.704 1.0026.07 A

ATOM 1401 O PHE A 200 47.083-31.786 17.435 1.0025.11 A

ATOM 1402 N HISA201 46.072-31.283 15.485 1.0024.41 A ATOM 1403 CA HIS A 201 47.238-30.621 14.915 1.0024.83 A

ATOM 1404 CB HIS A 201 47.883-31.532 13.867 1.0026.07 A

ATOM 1405 CG HIS A 201 48.320-32.857 14.412 1.0029.20 A

ATOM 1406 CD2HISA201 49.551 -33.337 14.706 1.0029.26 A

ATOM 1407 ND1 HIS A 201 47.430-33.850 14.760 1.0031.82 A ATOM 1408 CE1 HIS A 201 48.093-34.884 15.245 1.0030.34 A

ATOM 1409 NE2 HIS A 201 49.382-34.599 15.223 1.0031.15 A

ATOM 1410 C HISA201 46.855-29.278 14.288 1.0022.68 A

ATOM 1411 O HIS A 201 46.620-29.192 13.085 1.0022.47 A

ATOM 1412 N PRO A 202 46.778-28.214 15.106 1.0021.92 A ATOM 1413 CD PRO A 202 46.948-28.234 16.569 1.0020.50 A

ATOM 1414 CA PRO A 202 46.421 -26.866 14.649 1.0020.93 A

ATOM 1415 CB PROA202 46.502-26.036 15.926 1.0021.46 A

ATOM 1416 CG PRO A 202 46.157-27.025 16.996 1.0021.32 A

ATOM 1417 C PROA202 47.350-26.322 13.564 1.0019.09 A ATOM 1418 0 PROA202 48.537-26.664 13.504 1.0018.10 A

ATOM 1419 N GLN A 203 46.803-25.456 12.718 1.0018.45 A

ATOM 1420 CA GLN A 203 47.574-24.859 11.640 1.0019.50 A

ATOM 1421 CB GLNA203 46.637-24.302 10.562 1.0023.14 A

ATOM 1422 CG GLN A 203 45.946-25.375 9.744 1.0030.02 A ATOM 1423 CD GLN A 203 46.934-26.212 8.953 1.0032.83 A

ATOM 1424 OE1 GLN A 203 47.670-25.694 8.114 1.0036.02 A

ATOM 1425 NE2GLNA203 46.955-27.512 9.219 1.0036.60 A

ATOM 1426 C GLNA203 48.500-23.753 12.125 1.0019.54 A

ATOM 1427 O GLNA203 48.240-23.095 13.130 1.0017.94 A ATOM 1428 N LEUA204 49.597-23.578 11.401 1.0016.93 A

ATOM 1429 CA LEU A 204 50.578-22.545 11.698 1.0016.07 A

ATOM 1430 CB LEUA204 51.990-23.132 11.612 1.0015.88 A ATOM 1431 CG LEUA204 52.360-24.074 12.759 1.0015.91 A

ATOM 1432 CD1 LEU A 204 53.520-24.980 12.362 1.0016.95 A

ATOM 1433 CD2 LEU A 204 52.715-23.234 13.974 1.0015.31 A

ATOM 1434 C LEUA204 50.400-21.451 10.651 1.0016.94 A ATOM 1435 0 LEU A 204 50.551 -21.701 9.459 1.0020.31 A

ATOM 1436 N VALA205 50.050-20.251 11.097 1.0017.13 A

ATOM 1437 CA VALA205 49.866-19.120 10.197 1.0016.22 A

ATOM 1438 CB VAL A 205 48.526-18.400 10.465 1.0017.00 A

ATOM 1439 CG1 VAL A 205 48.372-17.207 9.540 1.0017.28 A ATOM 1440 CG2 VAL A 205 47.373-19.374 10.264 1.0016.18 A

ATOM 1441 C VALA205 51.013-18.172 10.492 1.0016.18 A

ATOM 1442 O VAL A 205 51.099-17.623 11.590 1.0015.45 A

ATOM 1443 N GLUA206 51.901 -17.984 9.523 1.0017.10 A

ATOM 1444 CA GLU A206 53.047-17.114 9.738 1.0017.75 A ATOM 1445 CB GLU A 206 53.991 -17.161 8.531 1.0019.99 A

ATOM 1446 CG GLU A 206 55.038-16.060 8.553 1.0025.62 A

ATOM 1447 CD GLUA206 56.265-16.393 7.735 1.0027.02 A

ATOM 1448 OE1 GLU A 206 56.125-17.075 6.701 1.0029.15 A

ATOM 1449 OE2 GLU A 206 57.363-15.951 8.123 1.0028.29 A ATOM 1450 C GLUA206 52.669-15.674 10.057 1.0019.85 A

ATOM 1451 O GLU A 206 51.857-15.056 9.366 1.0020.61 A

ATOM 1452 N GLYA207 53.274-15.155 11.118 1.0019.73 A

ATOM 1453 CA GLY A 207 53.014-13.794 11.536 1.0018.34 A

ATOM 1454 C GLYA207 54.311-13.044 11.756 1.0021.80 A ATOM 1455 O GLY A 207 55.392-13.636 11.751 1.0020.99 A

ATOM 1456 N ARG A 208 54.206-11.736 11.945 1.0021.05 A

ATOM 1457 CA ARG A 208 55.379-10.898 12.161 1.0022.72 A

ATOM 1458 CB ARG A 208 54.971 -9.427 12.172 1.0024.14 A

ATOM 1459 CG ARG A 208 54.277 -8.934 10.918 1.0027.47 A ATOM 1460 CD ARG A 208 53.736 -7.535 11.164 1.0031.07 A

ATOM 1461 NE ARG A 208 54.793 -6.636 11.628 1.0034.68 A

ATOM 1462 CZ ARGA208 55.476 -5.817 10.835 1.0037.65 A

ATOM 1463 NH1 ARG A 208 55.207 -5.776 9.536 1.0038.90 A

ATOM 1464 NH2 ARG A 208 56.436 -5.051 11.336 1.0038.25 A ATOM 1465 C ARGA208 56.091 -11.224 13.471 1.0022.28 A

ATOM 1466 0 ARGA208 55.454-11.461 14.498 1.0019.54 A

ATOM 1467 N ALA A 209 57.419-11.207 13.435 1.0021.98 A

ATOM 1468 CA ALAA209 58.218-11.501 14.614 1.0022.60 A

ATOM 1469 CB ALA A 209 59.658-11.794 14.202 1.0024.37 A ATOM 1470 C ALAA209 58.191 -10.361 15.631 1.0023.23 A

ATOM 1471 O ALAA209 58.589-10.548 16.778 1.0024.96 A

ATOM 1472 N ASPA210 57.722 -9.185 15.217 1.0023.89 A

ATOM 1473 CA ASPA210 57.664 -8.033 16.117 1.0024.37 A

ATOM 1474 CB ASP A 210 57.625 -6.723 15.319 1.0027.21 A ATOM 1475 CG ASP A 210 56.384 -6.589 14.458 1.0030.03 A

ATOM 1476 OD1 ASP A 210 55.760 -7.611 14.145 1.0029.12 A

ATOM 1477 OD2ASPA210 56.042 -5.447 14.085 1.0035.48 A

ATOM 1478 C ASP A 210 56.468 -8.111 17.066 1.0022.67 A

ATOM 1479 O ASPA210 56.244 -7.218 17.877 1.0020.42 A ATOM 1480 N ASNA211 55.710 -9.198 16.964 1.0022.16 A

ATOM 1481 CA ASNA211 54.551 -9.429 17.825 1.0019.71 A

ATOM 1482 CB ASNA211 53.572-10.363 17.102 1.0019.96 A

ATOM 1483 CG ASNA211 52.345-10.706 17.929 1.0018.74 A

ATOM 1484 OD1ASNA211 51.998-10.015 18.886 1.0017.61 A ATOM 1485 ND2 ASN A 211 51.664-11.774 17.539 1.0014.44 A

ATOM 1486,C ASNA211 55.100-10.064 19.102 1.0021.24 A

ATOM 1487 O ASNA211 54.931 -11.257 19.342 1.0023.32 A ATOM 1488 N ILE A 212 55.768 -9.247 19.915 1.00 20.62 A

ATOM 1489 CA ILE A 212 56.385 -9.722 21.149 1.00 21.93 A

ATOM 1490 CB ILE A 212 57.712 -8.977 21.413 1.00 23.60 A

ATOM 1491 CG2 ILE A 212 58.679 -9.235 20.269 1.00 23.98 A

ATOM 1492 CG1 ILE A 212 57.443 -7.475 21.573 1.00 24.67 A

ATOM 1493 CD1 ILE A 212 58.609 -6.690 22.159 1.00 27.58 A

ATOM 1494 C ILE A 212 55.513 -9.586 22.393 1.00 21.40 A

ATOM 1495 O ILE A 212 54.555 -8.815 22.417 1.00 19.12 A

ATOM 1496 N LYS A 213 55.860 -10.345 23.429 1.00 21.31 A

ATOM 1497 CA LYS A 213 55.140 -10.301 24.692 1.00 22.16 A

ATOM 1498 CB LYS A 213 54.839 -11.714 25.199 1.00 24.13 A

ATOM 1499 CG LYS A 213 54.059 -11.730 26.507 1.00 29.39 A

ATOM 1500 CD LYS A 213 53.540 -13.114 26.861 1.00 32.17 A

ATOM 1501 CE LYS A 213 54.660 -14.092 27.132 1.00 35.45 A

ATOM 1502 NZ LYS A 213 54.126 -15.437 27.504 1.00 37.54 A

ATOM 1503 C LYS A 213 56.008 -9.574 25.704 1.00 24.21 A

ATOM 1504 O LYS A 213 57.155 -9.954 25.933 1.00 24.13 A

ATOM 1505 N VAL A 214 55.464 -8.519 26.297 1.00 23.37 A

ATOM 1506 CA VAL A 214 56.204 -7.746 27.284 1.00 24.37 A

ATOM 1507 CB VAL A 214 55.561 -6.363 27.504 1.00 24.05 A

ATOM 1508 CG1 VAL A 214 56.376 -5.561 28.506 1.00 22.70 A

ATOM 1509 CG2 VAL A 214 55.478 -5.619 26.177 1.00 21.93 A

ATOM 1510 C VAL A 214 56.239 -8.510 28.601 1.00 25.84 A

ATOM 1511 O VAL A 214 55.227 -8.623 29.297 1.00 26.39 A

ATOM 1512 N THR A 215 57.413 -9.037 28.936 1.00 28.69 A

ATOM 1513 CA THR A 215 57.582 -9.805 30.161 1.00 30.70 A

ATOM 1514 CB THR A 215 57.914 -11.273 29.835 1.00 32.16 A

ATOM 1515 OG1 THR A 215 56.933 -11.800 28.930 1.00 34.81 A

ATOM 1516 CG2 THR A 215 57.915 -12.108 31.103 1.00 34.57 A

ATOM 1517 C THR A 215 58.691 -9.232 31.039 1.00 31.82 A

ATOM 1518 O THR A 215 58.587 -9.234 32.265 1.00 31.35 A

ATOM 1519 N ARG A 216 59.754 -8.749 30.405 1.00 33.48 A

ATOM 1520 CA ARG A 216 60.879 -8.175 31.132 1.00 35.00 A

ATOM 1521 CB ARG A 216 62.202 -8.770 30.640 1.00 37.32 A

ATOM 1522 CG ARG A 216 62.455 -10.216 31.056 1.00 41.78 A

ATOM 1523 CD ARG A 216 61.952 -11.214 30.024 1.00 44.93 A

ATOM 1524 NE ARG A 216 62.276 -12.587 30.413 1.00 48.03 A

ATOM 1525 CZ ARG A 216 62.047 -13.662 29.663 1.00 49.21 A

ATOM 1526 NH1 ARG A 216 61.488 -13.541 28.466 1.00 49.67 A

ATOM 1527 NH2 ARG A 216 62.384 -14.864 30.113 1.00 50.23 A

ATOM 1528 C ARG A 216 60.913 -6.659 30.967 1.00 35.48 A

ATOM 1529 O ARG A 216 60.348 -6.114 30.019 1.00 34.18 A

ATOM 1530 N PRO A 217 61.587 -5.956 31.891 1.00 35.81 A

ATOM 1531 CD PRO A 217 62.304 -6.517 33.051 1.00 35.99 A

ATOM 1532 CA PRO A 217 61.708 -4.496 31.868 1.00 35.89 A

ATOM 1533 CB PRO A 217 62.783 -4.233 32.918 1.00 35.87 A

ATOM 1534 CG PRO A 217 62.509 -5.299 33.925 1.00 36.63 A

ATOM 1535 C PRO A 217 ■ 62.077 -3.916 30.502 1.00 35.07 A

ATOM 1536 O PRO A 217 61.461 -2.952 30.043 1.00 36.13 A

ATOM 1537 N GLU A 218 63.074 -4.509 29.851 1.00 35.38 A

ATOM 1538 CA GLU A 218 63.526 -4.031 28.549 1.00 35.94 A

ATOM 1539 CB GLU A 218 64.802 -4.764 28.121 1.00 39.06 A

ATOM 1540 CG GLU A 218 64.606 -6.250 27.848 1.00 42.32 A

ATOM 1541 CD GLU A 218 64.882 -7.114 29.063 1.00 44.84 A

ATOM 1542 OE1 GLU A 218 64.414 -6.763 30.170 1.00 45.70 A

ATOM 1543 OE2 GLU A 218 65.559 -8.153 28.906 1.00 45.53 A

ATOM 1544 C GLU A 218 62.477 -4.194 27.458 1.00 35.05 A ATOM 1545 O GLU A 218 62.481 -3.455 26.473 1.00 34.92 A

ATOM 1546 N ASP A 219 61.585 -5.165 27.628 1.00 33.36 A

ATOM 1547 CA ASP A 219 60.545 -5.416 26.632 1.00 33.06 A

ATOM 1548 CB ASP A 219 59.690 -6.626 27.025 1.00 33.66 A ATOM 1549 CG ASP A 219 60.470 -7.927 26.995 1.00 34.71 A

ATOM 1550 OD1 ASP A 219 61.406 -8.047 26.173 1.00 37.33 A

ATOM 1551 OD2 ASP A 219 60.135 -8.839 27.778 1.00 34.59 A

ATOM 1552 C ASP A 219 59.633 -4.218 26.388 1.00 31.76 A

ATOM 1553 O ASP A 219 59.133 -4.038 25.280 1.00 29.92 A ATOM 1554 N LEU A 220 59.412 -3.401 27.413 1.00 31.37 A

ATOM 1555 CA LEU A 220 58.538 -2.240 27.263 1.00 30.75 A

ATOM 1556 CB LEU A 220 58.382 -1.508 28.598 1.00 32.54 A

ATOM 1557 CG LEU A 220 57.313 -.412 28.637 1.00 33.38 A

ATOM 1558 CD1 LEU A 220 55.932 -1.037 28.462 1.00 34.72 A ATOM 1559 CD2 LEU A 220 57.386 .329 29.961 1.00 35.06 A

ATOM 1560 C LEU A 220 59.078 -1.276 26.214 1.00 29.90 A

ATOM 1561 O LEU A 220 58.361 -.871 25.297 1.00 27.81 A

ATOM 1562 N ALA A 221 60.349 -.913 26.354 1.00 29.87 A

ATOM 1563 CA ALA A 221 60.990 .007 25.422 1.00 30.00 A ATOM 1564 CB ALA A 221 62.424 .276 25.863 1.00 31.39 A

ATOM 1565 C ALA A 221 60.973 -.549 24.000 1.00 27.88 A

ATOM 1566 O ALA A 221 60.763 .191 23.042 1.00 28.09 A

ATOM 1567 N LEU A 222 61.194 -1.854 23.871 1.00 27.19 A

ATOM 1568 CA LEU A 222 61.196 -2.499 22.565 1.00 27.07 A ATOM 1569 CB LEU A 222 61.704 -3.941 22.679 1.00 26.82 A

ATOM 1570 CG LEU A 222 61.769 -4.762 21.386 1.00 28.14 A

ATOM 1571 CD1 LEU A 222 62.620 -4.041 20.351 1.00 28.77 A

ATOM 1572 CD2 LEU A 222 62.349 -6.137 21.675 1.00 29.45 A

ATOM 1573 C LEU A 222 59.797 -2.492 21.956 1.00 26.03 A ATOM 1574 O LEU A 222 59.632 -2.252 20.757 1.00 23.89 A

ATOM 1575 N ALA A 223 58.790 -2.763 22.779 1.00 26.12 A

ATOM 1576 CA ALA A 223 57.410 -2.773 22.300 1.00 25.66 A

ATOM 1577 CB ALA A 223 56.463 -3.138 23.438 1.00 26.82 A

ATOM 1578 C ALA A 223 57.058 -1.396 21.747 1.00 27.62 A ATOM 1579 O ALA A 223 56.443 -1.278 20.687 1.00 25.06 A

ATOM 1580 N GLU A 224 57.460 -.355 22.469 1.00 29.02 A

ATOM 1581 CA GLU A 224 57.191 1.010 22.038 1.00 32.44 A

ATOM 1582 CB GLU A 224 57.702 2.002 23.081 1.00 34.38 A

ATOM 1583 CG GLU A 224 57.622 3.447 22.633 1.00 38.78 A ATOM 1584 CD GLU A 224 57.905 4.420 23.758 1.00 41.08 A

ATOM 1585 OE1 GLU A 224 58.903 4.219 24.484 1.00 42.44 A

ATOM 1586 OE2 GLU A 224 57.135 5.389 23.908 1.00 42.70 A

ATOM 1587 C GLU A 224 57.858 1.274 20.693 1.00 32.65 A

ATOM 1588 O GLU A 224 57.294 1.947 19.833 1.00 32.02 A ATOM 1589 N PHE A 225 59.061 .734 20.522 1.00 31.71 A

ATOM 1590 CA PHE A 225 59.802 .896 19.281 1.00 33.18 A

ATOM 1591 CB PHE A 225 61.172 .221 19.392 1.00 33.18 A

ATOM 1592 CG PHE A 225 61.914 .138 18.089 1.00 33.06 A

ATOM 1593 CD1 PHE A 225 62.406 1.288 17.479 1.00 32.57 A ATOM 1594 CD2 PHE A 225 62.082 -1.086 17.448 1.00 33.06 A

ATOM 1595 CE1 PHE A 225 63.059 1.222 16.249 1.00 31.85 A

ATOM 1596 CE2 PHE A 225 62.733 -1.165 16.218 1.00 32.49 A

ATOM 1597 CZ PHE A 225 63.219 -.007 15.615 1.00 32.15 A

ATOM 1598 C PHE A 225 59.016 .276 18.130 1.00 33.56 A ATOM 1599 O PHE A 225 58.845 .893 17.080 1.00 33.86 A

ATOM 1600 N TYR A 226 58.539 -.948 18.336 1.00 33.55 A

ATOM 1601 CA TYR A 226 57.769 -1.661 17.318 1.00 34.87 A ATOM 1602 CB TYR A 226 57.500 -3.097 17.777 1.00 33.17 A ATOM 1603 CG TYR A 226 58.694 -4.014 17.672 1.00 31.78 A ATOM 1604 CD1 TYR A 226 58.857 -5.074 18.557 1.00 31.15 A ATOM 1605 CE1 TYR A 226 59.939 -5.941 18.449 1.00 31.98 A ATOM 1606 CD2 TYR A 226 59.646 -3.841 16.668 1.00 32.61 A ATOM 1607 CE2 TY A 226 60.732 -4.702 16.549 1.00 31.90 A ATOM 1608 CZ TYR A 226 60.872 -5.749 17.440 1.00 33.04 A ATOM 1609 OH TYR A 226 61.938 -6.611 17.328 1.00 32.47 A ATOM 1610 C TYR A 226 56.445 -.976 17.005 1.00 36.55 A ATOM 1611 O TYR A 226 56.068 -.834 15.842 1.00 36.93 A ATOM 1612 N LEU A 227 55.744 -.559 18.053 1.00 37.47 A ATOM 1613 CA LEU A 227 54.454 .104 17.899 1.00 39.20 A ATOM 1614 CB LEU A 227 53.811 .311 19.274 1.00 38.91 A ATOM 1615 CG LEU A 227 52.283 .282 19.351 1.00 39.64 A ATOM 1616 CD1 LEU A 227 51.778 -1.076 18.887 1.00 39.00 A ATOM 1617 CD2 LEU A 227 51.839 .536 20.784 1.00 39.27 A ATOM 1618 C LEU A 227 54.639 1.446 17.193 1.00 40.78 A ATOM 1619 O LEU A 227 54.016 1.714 16.163 1.00 40.32 A ATOM 1620 N ALA A 228 55.514 2.277 17.749 1.00 41.39 A ATOM 1621 CA ALA A 228 55.799 3.594 17.192 1.00 43.00 A ATOM 1622 CB ALA A 228 55.149 4.677 18.050 1.00 43.48 A ATOM 1623 C ALA A 228 57.305 3.818 17.122 1.00 43.48 A ATOM 1624 O ALA A 228 57.819 4.606 17.947 1.00 42.74 A ATOM 1625 OXT ALA A 228 57.952 3.185 16.259 1.00 43.89 A ATOM 1626 OH2 WAT W 1 69.246 -24.960 14.039 1.00 16.05 W ATOM 1627 OH2 WAT W 2 51.412 -9.069 14.203 1.00 19.33 W ATOM 1628 OH2 WAT W 3 35.037 -2.630 18.322 1.00 13.13 W ATOM 1629 OH2 WAT W 4 33.748 -26.657 18.710 1.00 16.51 W ATOM 1630 OH2 WAT W 5 52.514 -12.208 14.605 1.00 18.96 W ATOM 1631 OH2 WAT W 6 52.791 -8.03820.626 1.00 17.33 W ATOM 1632 OH2 WAT W 7 49.029 -3.382 17.928 1.00 23.46 W ATOM 1633 OH2 WAT W 8 46.563 -3.796 14.936 1.00 21.91 W ATOM 1634 OH2 WAT W 9 44.272 -9.13936.843 1.00 21.18 W ATOM 1635 OH2 WAT W 10 30.303 -29.396 23.277 1.00 22.44 W ATOM 1636 OH2 WAT W 11 33.949 -22.983 10.665 1.00 20.27 W ATOM 1637 OH2 WAT W 12 53.381 -7.638 15.068 1.00 21.63 W ATOM 1638 OH2 WAT W 13 32.469 -24.357 18.629 1.00 17.27 W ATOM 1639 OH2 WAT W 14 63.026 -22.205 10.528 1.00 33.09 W ATOM 1640 OH2 WAT W 15 64.631 -17.261 15.851 1.00 27.29 W ATOM 1641 OH2 WAT W 16 32.049 -1.046 18.852 1.00 37.69 W ATOM 1642 OH2 WAT W 17 53.112 -27.95925.937 1.00 23.38 W ATOM 1643 OH2 WAT W 18 58.315 -12.110 23.219 1.00 26.86 W ATOM 1644 OH2 WAT W 19 47.971 -3.165 11.920 1.00 35.46 W ATOM 1645 OH2 WAT W 20 37.748 -13.724 7.999 1.00 19.98 W ATOM 1646 OH2 WAT W 21 52.663-31.199 22.016 1.00 21.59 W ATOM 1647 OH2 WAT W 22 64.593 -30.93520.354 1.00 31.09 W ATOM 1648 OH2 WAT W 23 31.537 -28.451 25.450 1.00 25.90 W ATOM 1649 OH2 WAT W 24 56.920 -25.364 8.547 1.00 28.30 W ATOM 1650 OH2 WAT W 25 60.221 -22.855 10.260 1.00 30.69 W ATOM 1651 OH2 WAT W 26 28.249 -17.443 27.700 1.00 30.74 W ATOM 1652 OH2 WAT W 27 35.751 -9.923 37.506 1.00 38.23 W ATOM 1653 OH2 WAT W 28 40.037 -12.109 8.097 1.00 25.74 W ATOM 1654 OH2 WAT W 29 57.693 -14.172 10.121 1.00 31.89 w ATOM 1655 OH2 WAT W 30 56.673 -10.411 33.450 1.00 38.51 w ATOM 1656 OH2 WAT W 31 42.642 -7.374 10.869 1.00 25.99 w ATOM 1657 OH2 WAT W 32 46.509 -1.896 19.137 1.00 30.71 w ATOM 1658 OH2 WAT W 33 31.660 -6.561 32.171 1.00 39.12 w ATOM 1659 OH2 WAT W 34 45.041 -18.191 6.632 1.00 34.41 W

ATOM 1660 OH2 WAT W 35 62.244 -9.089 19.040 1.00 36.42 W

ATOM 1661 OH2 WAT W 36 39.869 -1.182 17.753 1.00 24.63 W

ATOM 1662 OH2 WAT W 37 55.325 -18.507 22.980 1.00 30.20 W

ATOM 1663 OH2 WAT W 38 46.156 -4.753 39.342 1.00 38.96 W

ATOM 1664 OH2 WAT W 39 46.623 -9.090 37.980 1.00 36.77 W

ATOM 1665 OH2 WAT W 40 33.385 -17.307 13.423 1.00 27.98 W

ATOM 1666 OH2 WAT W 41 38.813 -3.666 38.631 1.00 30.14 W

ATOM 1667 OH2 WAT W 42 61.918 -.691 28.844 1.00 41.06 W

ATOM 1668 OH2 WAT W 43 70.827 -22.840 11.042 1.00 33.42 W

ATOM 1669 OH2 WAT W 44 48.517 -22.087 7.775 1.00 41.59 W

ATOM 1670 OH2 WAT W 45 58.815 -11.050 10.913 1.00 39.68 W

ATOM 1671 OH2 WAT W 46 30.062 -6.577 16.316 1.00 46.22 W

ATOM 1672 OH2 WAT W 47 33.178 -16.966 33.557 1.00 39.38 W

ATOM 1673 OH2 WAT W 48 43.790 -31.676 13.603 1.00 38.62 W

ATOM 1674 OH2 WAT W 49 30.057 -17.713 15.587 1.00 33.32 W

ATOM 1675 OH2 WAT W 50 64.863 -3.352 24.837 1.00 38.40 W

ATOM 1676 OH2 WAT W 51 69.853 -33.381 25.729 1.0042.24 W

ATOM 1677 OH2 WAT W 52 76.383 -35.990 20.525 1.00 50.00 W

ATOM 1678 OH2 WAT W 53 34.974 2.235 26.442 1.00 44.13 W

ATOM 1679 OH2 WAT W 54 48.235 -22.793 32.601 1.00 41.34 W

ATOM 1680 OH2 WAT W 55 34.621 -30.605 21.183 1.00 41.63 W

ATOM 1681 OH2 WAT W 56 51.250 -18.678 6.709 1.00 33.65 W

ATOM 1682 OH2 WAT W 57 70.565 -13.545 16.284 1.00 43.91 W

ATOM 1683 OH2 WAT W 58 40.644 1.975 25.990 1.00 39.90 w

ATOM 1684 OH2 WAT W 59 41.777 -36.084 16.783 1.00 42.92 w

ATOM 1685 OH2 WAT W 60 38.635 -.149 20.191 1.00 38.28 w

ATOM 1686 OH2 WAT W 61 48.417 -34.017 18.551 1.00 27.72 w

ATOM 1687 OH2 WAT W 62 26.991 -13.329 11.995 1.00 48.57 w

ATOM 1688 OH2 WAT W 63 66.842 -31.824 15.221 1.00 38.52 w

ATOM 1689 OH2 WAT W 64 36.537 -28.187 32.627 1.00 49.21 w

ATOM 1690 OH2 WAT W 65 46.636 -23.459 28.167 1.00 47.17 w

ATOM 1691 OH2 WAT W 66 48.616 -4.648 9.478 1.00 44.89 w

ATOM 1692 OH2 WAT W 67 62.533 -30.691 10.230 1.00 49.40 w

ATOM 1693 OH2 WAT W 68 38.365 -21.636 35.248 1.00 38.43 w

ATOM 1694 OH2 WAT W 69 30.506 -10.319 10.891 1.00 48.05 w

ATOM 1695 OH2 WAT W 70 61.229 2.971 23.053 1.00 33.07 w

ATOM 1696 OH2 WAT W 71 70.839 -28.021 30.557 1.00 36.36 w

ATOM 1697 OH2 WAT W 72 41.046 -4.390 10.686 1.00 39.11 w

ATOM 1698 OH2 WAT W 73 60.331 -4.338 13.393 1.00 42.66 w

ATOM 1699 OH2 WAT W 74 25.455 -16.974 14.799 1.00 47.52 w

ATOM 1700 OH2 WAT W 75 38.240 -8.792 40.148 1.00 50.64 w

ATOM 1701 OH2 WAT W 76 35.251 -25.503 10.720 1.00 40.38 w

ATOM 1702 OH2 WAT W 77 43.525 .230 44.626 1.00 50.93 w

ATOM 1703 OH2 WAT W 78 31.161 -3.158 29.730 1.00 39.26 w

ATOM 1704 OH2 WAT W 79 44.692 4.129 30.103 1.00 42.10 w

ATOM 1705 OH2 WAT W 80 47.730 .629 19.833 1.00 41.81 w

ATOM 1706 OH2 WAT W 81 28.983 -6.441 19.015 1.00 37.15 w

ATOM 1707 OH2 WAT W 82 53.059 -2.671 16.337 1.00 48.52 w

ATOM 1708 OH2 WAT W 83 35.652 -28.960 14.519 1.00 38.10 w

ATOM 1709 OH2 WAT W 84 40.625 -36.991 20.735 1.00 40.38 w

ATOM 1710 OH2 WAT W 85 58.845 -7.979 12.466 1.00 39.38 w

ATOM 1711 OH2 WAT W 86 45.002 -4.273 41.882 1.00 47.19 w

ATOM 1712 OH2 WAT W 87 33.718 -26.477 8.515 1.00 50.48 w

ATOM 1713 OH2 WAT W 88 50.069 -20.338 34.203 1.00 43.55 w

ATOM 1714 OH2 WAT W 89 29.960 -14.517 21.721 1.00 52.73 w

ATOM 1715 OH2 WAT W 90 43.458 -20.448 5.549 1.00 45.96 w ATOM 1716 OH2WATW 91 43.340 4.923 27.531 1.0053.92 W

ATOM 1717 OH2 WAT W 92 70.329 -30.549 13.073 1.0044.38 W

ATOM 1718 OH2WATW 93 60.087 -10.44524.204 1.0057.72 W

ATOM 1719 OH2 WAT W 94 41.834 -26.671 3.843 1.0048.97 W

ATOM 1720 OH2WATW 95 72.976 -35.458 21.556 1.0045.34 W

ATOM 1721 OH2 WAT W 96 50.294 -30.96424.830 1.0040.42 W

ATOM 1722 OH2 WAT W 97 55.485 5.461 26.072 1.0044.52 W

ATOM 1723 OH2 WAT W 98 34.294 .687 35.910 1.0049.18 W

ATOM 1724 OH2 WAT W 99 46.604 -17.402 23.217 1.0037.43 W

ATOM 1725 OH2WATW100 26.889 -14.00727.811 1.0051.68 W

ATOM 1726 OH2WATW101 53.058 2.171 12.804 1.0051.67 W

ATOM 1727 OH2WATW102 28.899 .012 31.657 1.0052.77 W

ATOM 1728 OH2WATW103 48.126 4.68530.317 1.0046.21 W

ATOM 1729 OH2WATW104 37.897 -1.208 12.423 1.0052.60 W

ATOM 1730 OH2WATW105 48.969 -17.333 5.205 1.0050.86 W

ATOM 1731 OH2WATW106 43.189 -37.13924.550 1.0050.37 W

ATOM 1732 OH2WATW107 29.336 -21.901 27.551 1.0057.38 W

ATOM 1733 OH2WATW108 43.569 4.40734.810 1.0048.40 W

ATOM 1734 OH2WATW109 69.798 -14.989 13.364 1.0053.72 W

ATOM 1735 OH2WATW110 42.224 -16.23442.400 1.0051.54 W

ATOM 1736 OH2 WAT W 111 44.370 1.938 36.110 1.0048.40 W

ATOM 1737 OH2WATW112 28.429 -8.132 25.215 1.0050.57 W

ATOM 1738 OH2WATW113 50.216 -27.28532.630 1.0042.37 W

ATOM 1739 OH2WATW114 72.500 -26.010 33.414 1.0049.65 W

ATOM 1740 OH2WATW115 44.925 -9.21342.403 1.0050.21 W

ATOM 1741 OH2WATW116 68.600 -26.791 9.097 1.0055.95 W

ATOM 1742 OH2WATW117 33.246 -4.312 32.699 1.0049.49 w

ATOM 1743 OH2WATW118 40.392 -29.158 8.379 1.0057.65 w

ATOM 1744 OH2WATW119 74.338 -35.936 29.115 1.0055.95 w

ATOM 1745 OH2WATW120 34.835 -23.884 33.240 1.0050.81 w

ATOM 1746 OH2WATW121 35.803 -3.411 13.833 1.0015.14 w

ATOM 1747 OH2WATW122 26.307 -24.145 18.144 1.0019.74 w

ATOM 1748 OH2WATW123 35.171 -5.592 15.997 1.0015.31 w

ATOM 1749 OH2WATW124 46.436 -17.60434.520 1.0043.83 w

ATOM 1750 OH2WATW125 75.516 -33.855 16.538 1.0034.44 w

ATOM 1751 OH2WATW126 34.150 -2.386 11.946 1.0027.16 w

ATOM 1752 OH2WATW127 36.533 -1.226 16.007 1.0019.22 w

ATOM 1753 OH2WATW128 27.964 -4.64821.057 1.0030.15 w

ATOM 1754 OH2WATW129 45.265 -1.633 16.733 1.0038.55 w

ATOM 1755 OH2WATW130 61.843 -15.164 14.022 1.0042.32 w

ATOM 1756 OH2WATW131 69.549 -26.025 11.790 1.0045.61 w

ATOM 1757 OH2WATW132 35.664 -2.029 9.458 1.0046.62 w

ATOM 1758 OH2WATW133 50.695 -34.08523.768 1.0037.68 w

ATOM 1759 OH2WATW134 52.795 -30.33424.553 1.0035.10 w

ATOM 1760 OH2WATW135 32.104 -22.60529.298 1.0039.30 w

ATOM 1761 OH2WATW136 51.901 -18.86622.741 1.0042.51 w

ATOM 1762 OH2WATW137 39.919 -10.349 6.223 1.0044.77 w

ATOM 1763 OH2WATW138 41.482 -6.465 8.651 1.0040.84 ' w

ATOM 1764 OH2WATW139 71.700 -35.48425.298 1.0049.21 w

ATOM 1765 OH2WATW140 46.543 7.381 22.804 1.0042.24 w

ATOM 1766 OH2WATW141 52.204 -16.52924.520 1.0044.86 w

ATOM 1767 OH2WATW142 65.365 1.801 25.939 1.0049.53 w

ATOM 1768 OH2WATW143 60.813 1.92229.123 1.0044.60 w

ATOM 1769 OH2WATW144 33.851 -31.795 17.243 1.0046.91 w

ATOM 1770 OH2WATW145 71.305 -28.383 11.480 1.0049.64 w

ATOM 1771 OH2WATW146 59.135 -23.485 7.953 1.0050.51 w

ATOM 1772 OH2WATW147 46.587 -7.295 39.929 1.0044.36 w ATOM 1773 OH2WATW148 46.090 3.644 33.046 1.0045.41 W

ATOM 1774 OH2WATW149 64.392 -32.060 25.629 1.0047.04 W

ATOM 1775 OH2WATW150 42.269 -39.619 18.398 1.0051.63 W

ATOM 1776 OH2WATW151 68.730 -29.270 29.988 1.0046.16 W

ATOM 1777 OH2WATW152 34.281 -17.141 21.416 1.0043.61 W

ATOM 1778 OH2WATW153 34.715 -17.426 37.366 1.0051.97 W

ATOM 1779 OH2WATW154 27.111 -10.281 13.095 1.0046.34 W

ATOM 1780 OH2WATW155 50.360 -1.990 15.586 1.0046.73 W

ATOM 1781 OH2WATW156 36.674 -4.854 37.623 1.0043.24 W

ATOM 1782 OH2WATW157 47.144 -19.749 6.293 1.0040.87 W

ATOM 1783 OH2WATW158 52.276 -14.076 36.660 1.0048.83 W

ATOM 1784 OH2WATW159 38.671 .36641.137 1.0049.19 W

ATOM 1785 OH2WATW160 36.709 -9.669 4.795 1.0050.52 W

ATOM 1786 OH2WATW161 43.244 -38.273 16.427 1.0042.30 W

ATOM 1787 OH2WATW162 27.735 -15.226 30.946 1.0052.66 W

ATOM 1788 OH2WATW163 51.486 -18.198 29.962 1.0040.73 W

ATOM 1789 OH2WATW164 46.701 .969 36.381 1.0044.14 W

ATOM 1790 OH2WATW165 66.661 -31.968 21.121 1.0056.65 W

ATOM 1791 OH2WATW166 51.184 -4.445 34.952 1.0045.62 W

ATOM 1792 OH2WATW167 34.768 -3.534 36.003 1.0048.51 W

ATOM 1793 OH2WATW168 59.415 -16.211 6.406 1.0051.14 W

ATOM 1794 OH2WATW169 40.259 -20.791 37.003 1.0057.12 W

ATOM 1795 OH2WATW170 46.872 7.453 32.080 1.0060.54 W

ATOM 1796 OH2WATW171 56.470 3.618 27.841 1.0054.22 w

ATOM 1797 OH2WATW172 70.936 -18.836 10.804 1.0046.77 w

ATOM 1798 OH2WATW173 36.773 -15.453 41.856 1.0046.98 w

ATOM 1799 OH2WATW174 30.603 -7.262 10.669 1.0044.40 w

ATOM 1800 OH2WATW175 36.480 -36.175 34.173 1.0053.09 w

ATOM 1801 OH2WATW176 49.148 -37.067 21.108 1.0050.34 w

ATOM 1802 OH2WATW177 70.687 -23.652 35.226 1.0053.19 w

ATOM 1803 OH2WATW178 36.694 -15.622 6.575 1.0048.97 w

ATOM 1804 OH2WATW179 54.045 -18.467 5.276 1.0046.62 w

ATOM 1805 OH2WATW180 30.765 -11.541 33.596 1.0046.71 w

ATOM 1806 OH2WATW181 61.475 -10.906 17.507 1.0044.41 w

ATOM 1807 OH2WATW182 50.659 2.850 33.354 1.0054.62 w

ATOM 1808 OH2WATW183 56.116 2.097 12.131 1.0054.36 w

ATOM 1809 OH2WATW184 44.396 -15.03541.417 1.0052.33 w

ATOM 1810 OH2WATW185 50.049 -10.978 7.022 1.0046.47 w

ATOM 1811 OH2WATW186 43.833 -23.761 1.923 1.0061.71 w

ATOM 1812 OH2WATW187 79.402 -34.752 27.411 1.0054.01 w

ATOM 1813 OH2WATW188 37.293 -31.403 14.941 1.0049.95 w

ATOM 1814 OH2WATW189 70.203 -17.062 18.317 1.0054.79 w

ATOM 1815 OH2WATW190 65.151 -5.728 23.873 1.0061.57 w

ATOM 1816 OH2WATW191 37.853 -33.800 25.789 1.0046.69 w

ATOM 1817 OH2WATW192 39.680 -18.112 .455 1.0058.93 w

ATOM 1818 OH2WATW193 54.731 6.739 14.744 1.0051.68 w

ATOM 1819 OH2WATW194 53.212 -36.559 31.398 1.0050.96 w

ATOM 1820 OH2WATW195 36.525 -20.445 1.537 1.0051.26 w

ATOM 1821 OH2WATW196 49.123 -7.88541.693 1.0063.54 w

ATOM 1822 OH2WATW197 66.656 -10.031 31.191 1.0052.70 w

ATOM 1823 OH2WATW198 61.761 -8.146 13.688 1.0053.54 w

ATOM 1824 OH2WATW199 48.878 -18.750 24.972 1.0050.02 w

ATOM 1825 OH2 WAT W 200 28.047 -16.163 13.561 1.0029.63 w

ATOM 1826 OH2WATW201 38.951 -33.62221.898 1.0039.34 w

ATOM 1827 OH2 WAT W 202 33.058 -22.788 26.401 1.0036.35 w

ATOM 1828 OH2 WAT W 203 26.220 -20.034 17.663 1.0032.93 w

ATOM 1829 OH2 WAT W 204 42.937 .449 17.390 1.0036.78 w ATOM 1830 OH2WATW205 73.381 -35.387 31.582 1.0036.40 W

ATOM 1831 OH2WATW206 68.297 -33.469 11.365 1.0039.32 W

ATOM 1832 OH2WATW207 27.299 -15.490 17.962 1.0039.35 W

ATOM 1833 OH2WATW208 38.576 -22.452 1.220 1.0037.72 W ATOM 1834 OH2WATW209 68.126 -28.62432.747 1.0037.95 W

ATOM 1835 OH2WATW210 55.448 -37.767 30.587 1.0038.91 W

ATOM 1836 OH2WATW211 75.053 -33.823 34.010 1.0038.15 W

ATOM 1837 OH2WATW212 52.212 -33.92032.727 1.0037.10 W

ATOM 1838 OH2WATW213 51.093 -21.328 30.470 1.0036.93 W ATOM 1839 OH2WATW214 81.957 -34.96328.344 1.0038.58 W

ATOM 1840 OH2WATW215 45.291 3.543 19.935 1.0035.30 W

ATOM 1841 OH2WATW216 62.130 -33.797 26.548 1.0039.66 W

ATOM 1842 OH2WATW217 45.208 -28.641 10.874 1.0033.55 W

ATOM 1843 OH2WATW218 39.604 16.72840.866 1.0031.75 W ATOM 1844 OH2WATW219 60.602 15.681 11.964 1.0039.59 w

ATOM 1845 OH2WATW220 36.103 -22.302 34.761 1.0037.39 w

ATOM 1846 OH2WATW221 76.463 -33.946 18.868 1.0030.75 w

ATOM 1847 OH2WATW222 50.498 -31.97027.034 1.0036.59 w

ATOM 1848 OH2WATW223 58.236 -13.487 19.226 1.0040.48 w ATOM 1849 OH2WATW224 32.488 -8.773 9.666 1.0035.60 w

ATOM 1850 OH2WATW225 51.230 -4.501 9.393 1.0036.04 w

ATOM 1851 OH2WATW226 35.085 -7.502 38.101 1.0036.81 w

ATOM 1852 OH2WATW227 34.519 -23.05530.435 1.0026.83 w

ATOM 1853 OH2WATW228 42.459 -40.490 20.916 1.0038.83 w ATOM 1854 OH2WATW229 35.846 -11.183 7.433 1.0038.58 w

ATOM 1855 OH2WATW230 61.749 -10.10021.568 1.0035.63 w

ATOM 1856 OH2WATW231 48.088 2.114 34.545 1.0038.92 w

ATOM 1857 OH2WATW232 51.384 .229 12.259 1.0040.35 w

ATOM 1858 OH2WATW233 39.510 ^■23.97635.730 1.0039.65 w ATOM 1859 OH2WATW234 67.706 -18.336 9.774 1.0038.00 w

ATOM 1860 OH2WATW235 61.049 -12.499 21.206 1.0036.84 w

ATOM 1861 OH2WATW236 43.438 -27.522 9.385 1.0033.00 w

ATOM 1862 OH2WATW237 43.402 -24.214 6.938 1.0027.53 w

ATOM 1863 OH2WATW238 41.835 -1.867 11.137 1.0039.67 w ATOM 1864 OH2WATW239 51.610 -34.621 28.404 1.0036.38 w

ATOM 1865 OH2WATW240 28.732 -13.03829.510 1.0037.25 w

ATOM 1866 OH2WATW241 30.870 -15.792 34.118 1.0037.46 w

ATOM 1867 OH2WATW242 34.612 3.88631.054 1.0037.30 w

ATOM 1868 OH2WATW243 45.928 -13.903 39.327 1.0040.97 w ATOM 1869 OH2WATW244 40.562 -36.401 23.262 1.0037.22 w

ATOM 1870 OH2WATW245 54.642 -1.209 10.634 1.0038.84 w

ATOM 1871 OH2WATW246 47.537 -29.261 33.487 1.0035.12 w

ATOM 1872 OH2WATW247 65.770 -33.74324.370 1.0035.53 w

ATOM 1873 OH2WATW248 71.323 -27.195 8.289 1.0034.44 w ATOM 1874 OH2WATW249 38.691 -7.996 7.691 1.0037.45 w

ATOM 1875 OH2WATW250 26.635 -21.801 19.402 1.0040.94 w

ATOM 1876 OH2WATW251 59.792 -4.179 9.401 1.0039.95 w

ATOM 1877 OH2WATW252 34.266 -30.99528.659 1.0033.29 w

ATOM 1878 OH2WATW253 45.488 -39.518 19.690 1.0038.10 w ATOM 1879 OH2WATW254 50.380 -38.17829.545 1.0038.65 w

ATOM 1880 OH2WATW255 49.055 5.53022.440 1.0036.29 w

ATOM 1881 OH2WATW256 25.993 -14.592 22.542 1.0036.63 w

ATOM 1882 OH2WATW257 37.021 -3.914 8.037 1.0039.14 w

ATOM 1883 OH2WATW258 46.433 -30.547 9.040 1.0040.62 w ATOM 1884 OH2WATW259 61.922 -11.81226.540 1.0038.87 w

ATOM 1885 OH2WATW260 67.352 -28.635 35.330 1.0038.57 w

ATOM 1886 OH2WATW261 33.327 -1.623 36.746 1.0035.17 w ATOM 1887 OH2 WAT W 262 67.245 -15.018 21.815 1.00 38.13 W

ATOM 1888 OH2 WAT W 263 63.140 -10.794 15.625 1.00 37.48 W

ATOM 1889 OH2 WAT W 264 44.444 6.021 .36.984 1.00 37.46 W

ATOM 1890 OH2 WAT W 265 48.915 -36.830 23.991 1.00 34.41 W

ATOM 1891 OH2 WAT W 266 53.177 6.584 28.788 1.00 37.55 W

ATOM 1892 OH2 WAT W 267 70.033 -6.803 29.472 1.0041.07 W

ATOM 1893 OH2 WAT W 268 31.037 -24.101 27.627 1.00 35.03 W

ATOM 1894 OH2 WAT W 269 22.643 -16.819 15.031 1.00 35.15 W

ATOM 1895 OH2 WAT W 270 60.672 -32.913 10.688 1.00 37.73 W

ATOM 1896 OH2 WAT W 271 71.897 -33.555 14.885 1.00 37.96 W

ATOM 1897 OH2 WAT W 272 32.489 -5.999 36.729 1.00 38.27 W

ATOM 1898 OH2 WAT W 273 51.397 -14.486 39.300 1.00 40.75 W

ATOM 1899 OH2 WAT W 274 73.215 -35.263 16.494 1.00 35.26 W

ATOM 1900 OH2 WAT W 275 43.450 -27.121 6.183 1.00 42.76 W

ATOM 1901 OH2 WAT W 276 42.886 -20.713 1.544 1.00 36.42 W

ATOM 1902 OH2 WAT W 277 57.540 -7.214 45.424 1.00 44.20 W

ATOM 1903 OH2 WAT W 278 33.091 -10.337 36.900 1.00 39.10 W

ATOM 1904 OH2 WAT W 279 66.306 -14.561 18.687 1.00 41.44 W

ATOM 1905 OH2 WAT W 280 63.990 -15.269 18.044 1.00 38.04 W

ATOM 1906 OH2 WAT W 281 76.897 -37.735 23.633 1.00 41.53 W

ATOM 1907 OH2 WAT W 282 80.276 -32.365 34.015 1.00 39.33 W

ATOM 1908 OH2 WAT W 283 54.173 -11.914 8.067 1.00 26.94 w

ATOM 1909 OH2 WAT W 284 47.730 -13.279 28.873 1.00 21.23 W

ATOM 1910 OH2 WAT W 285 46.244 -8.593 23.770 1.00 32.34 w

ATOM 1911 OH2 WAT W 286 34.478 -15.466 35.653 1.0047.84 w

ATOM 1912 OH2 WAT W 287 68.461 -30.111 27.640 1.00 31.10 w

ATOM 1913 OH2 WAT W 288 29.982 -8.197 23.061 1.00 32.62 w

ATOM 1914 OH2 WAT W 289 50.221 -11.963 28.572 1.00 32.60 w

ATOM 1915 OH2 WAT W 290 31.124 -26.176 26.158 1.00 36.05 w

ATOM 1916 OH2 WAT W 291 52.051 -20.208 28.464 1.00 31.51 w

ATOM 1917 OH2 WAT W 292 31.899 -5.559 8.582 1.00 37.99 w

ATOM 1918 OH2 WAT W 293 38.422 -34.999 23.754 1.00 46.66 w

ATOM 1919 OH2 WAT W 294 31.113 -13.932 35.960 1.00 30.82 w

ATOM 1920 OH2 WAT W 295 60.269 -13.415 11.203 1.00 36.12 w

ATOM 1921 OH2 WAT W 296 53.027 -20.763 26.247 1.00 35.30 w

ATOM 1922 OH2 WAT W 297 44.908 1.001 20.320 1.00 38.21 w

ATOM 1923 OH2 WAT W 298 40.914 -23.590 .763 ' 1.00 38.18 w

ATOM 1924 OH2 WAT W 299 45.909 -15.058 33.218 1.00 32.70 w

ATOM 1925 OH2 WAT W 300 39.131 -11.896 4.216 1.00 42.04 w

ATOM 1926 OH2 WAT W 301 30.715 -7.770 26.017 1.00 32.31 w

ATOM 1927 OH2 WAT W 302 42.143 -5.186 45.743 1.00 33.54 w

ATOM 1928 OH2 WAT W 303 54.825 -3.349 14.625 1.00 34.04 w

ATOM 1929 OH2 WAT W 304 36.344 -32.589 28.083 1.00 40.75 w

ATOM 1930 OH2 WAT W 305 58.825 -4.134 30.659 1.00 37.98 w

ATOM 1931 OH2 WAT W 306 29.365 -13.663 33.162 1.00 46.20 w

ATOM 1932 OH2 WAT W 307 37.798 1.648 25.154 1.00 34.01 w

ATOM 1933 OH2 WAT W 308 29.169 2.302 30.871 1.00 38.60 w

ATOM 1934 OH2 WAT W 309 39.113 -30.014 34.574 1.0040.12 w

ATOM 1935 OH2 WAT W 310 28.202 -15.234 11.198 1.00 35.80 w

ATOM 1936 OH2 WAT W 311 34.013 -12.223 5.796 1.00 36.73 w

ATOM 1937 OH2 WAT W 312 65.135 -12.527 30.842 1.00 36.35 w

ATOM 1938 OH2 WAT W 313 61.610 -13.358 24.438 1.00 42.16 w

ATOM 1939 OH2 WAT W 314 51.277 -38.295 22.003 1.00 39.14 w

ATOM 1940 OH2 WAT W 315 44.367 8.114 25.280 1.00 41.86 w

ATOM 1941 OH2 WAT W 316 33.263 -13.718 37.313 1.00 40.67 w

ATOM 1942 OH2 WAT W 317 75.035 -36.306 22.610 1.00 36.93 w

ATOM- 1943 OH2 WAT W 318 54.307 2.638 32.199 1.00 36.42 w ATOM 1944 OH2 WAT W 319 29.958 -2.096 33.043 1.00 46.25 W ATOM 1945 OH2 WAT W 320 53.620 -19.427 24.395 1.00 42.64 W ATOM 1946 OH2 WAT W 321 30.025 -20.253 25.528 1.00 32.25 W ATOM 1947 OH2 WAT W 322 44.310 -21.503 27.957 1.00 42.09 W ATOM 1948 OH2 WAT W 323 62.771 -13.033 17.232 1.00 41.08 W ATOM 1949 OH2 WAT W 324 51.001 -10.704 31.086 1.00 39.54 W ATOM 1950 OH2 WAT W 325 59.319 -6.706 35.798 1.00 41.35 W ATOM 1951 OH2 WAT W 326 52.805 -6.529 8.419 1.00 41.00 W ATOM 1952 OH2 WAT W 327 38.766 2.762 19.345 1.00 34.39 W ATOM 1953 OH2 WAT W 328 37.103 -5.581 42.654 1.00 42.22 W ATOM 1954 OH2 WAT W 329 34.817 -31.236 15.066 1.00 42.18 W ATOM 1955 OH2 WAT W 330 71.453 -21.515 32.130 1.0040.73 W ATOM 1956 OH2 WAT W 331 41.272 -23.472 28.333 1.00 43.59 W ATOM 1957 OH2 WAT W 332 33.573 -3.860 30.030 1.00 41.68 W ATOM 1958 OH2 WAT W 333 67.262 -28.470 7.896 1.00 43.23 W ATOM 1959 OH2 WAT W 334 55.197 -3.726 36.467 1.00 43.19 W ATOM 1960 OH2 WAT W 335 55.295 -7.671 6.528 1.00 37.53 W ATOM 1961 OH2 WAT W 336 48.832 -8.496 39.036 1.00 41.02 W ATOM 1962 OH2 WAT W 337 35.234 -26.229 32.390 1.00 39.19 W ATOM 1963 OH2 WAT W 338 47.493 -16.818 36.560 1.00 47.08 W ATOM 1964 OH2 WAT W 339 48.819 -12.951 41.747 1.00 42.03 W ATOM 1965 OH2 WAT W 340 43.882 -38.716 22.504 1.00 44.02 W ATOM 1966 OH2 WAT W 341 46.578 -1.977 43.191 1.00 42.24 w ATOM 1967 OH2 WAT W 342 72.531 -31.605 12.468 1.00 38.62 w ATOM 1968 OH2 WAT W 343 40.079 -33.999 38.820 1.00 42.63 w ATOM 1969 OH2 WAT W 344 58.324 -6.292 33.262 1.00 46.55 w ATOM 1970 OH2 WAT W 345 59.594 -15.109 29.299 1.00 37.79 w ATOM 1971 OH2 WAT W 346 35.944 -32.471 21.864 1.00 38.04 w ATOM 1972 OH2 WAT W 347 38.115 -27.656 34.427 1.00 36.95 w ATOM 1973 OH2 WAT W 348 36.574 5.056 35.584 1.00 42.65 w ATOM 1974 OH2 WAT W 349 25.506 -14.859 25.508 1.00 41.43 w ATOM 1975 OH2 WAT W 350 50.547 2.686 18.569 1.00 44.73 w ATOM 1976 OH2 WAT W 351 38.816 -35.639 31.130 1.00 44.62 w ATOM 1977 OH2 WAT W 352 34.952 -.329 41.304 1.00 38.63 w ATOM 1978 OH2 WAT W 353 46.443 -23.548 7.404 1.00 42.33 w ATOM 1979 OH2 WAT W 354 47.114 -6.665 42.494 1.00 41.73 w ATOM 1980 OH2 WAT W 355 67.809 -12.662 20.880 1.00 52.33 w ATOM 1981 OH2 WAT W 356 63.121 4.774 27.064 1.00 38.29 w ATOM 1982 OH2 WAT W 357 39.688 -31.762 10.395 1.00 37.01 w ATOM 1983 OH2 WAT W 358 28.870 -23.345 18.011 1.00 47.78 w ATOM 1984 OH2 WAT W 359 60.870 -31.947 8.435 1.00 33.76 w ATOM 1985 OH2 WAT W 360 37.501 -35.144 36.269 1.00 37.97 w ATOM 1986 OH2 WAT W 361 70.220 -24.991 9.266 1.00 40.70 w ATOM 1987 OH2 WAT W 362 35.817 -17.655 2.516 1.00 45.68 w ATOM 1988 OH2 WAT W 363 68.321 -33.612 16.959 1.00 43.51 w ATOM 1989 OH2 WAT W 364 46.092 -1.435 11.021 1.00 42.43 w ATOM 1990 OH2 WAT W 365 33.745 .630 17.603 1.00 51.36 w ATOM 1991 OH2 WAT W 366 82.055 •37.490 30.372 1.00 41.66 w ATOM 1992 OH2 WAT W 367 57.994 -8.837 38.009 1.00 44.43 w ATOM 1993 OH2 WAT W 368 33.895 -2.783 39.558 1.00 39.11 w ATOM 1994 OH2 WAT W 369 51.828 -1.923 36.682 1.00 41.88 w ATOM 1995 OH2 WAT W 370 68.164 ■35.713 18.711 1.00 37.62 w ATOM 1996 CA+2 CA2 C 1 35.316 •3.287 16.067 1 00 65.43 END APPENDIX 2

X-RAY DATA COORDINATES FOR CDP-ME SYNTHASE COMPLEXED WITH CTP^«Mg²⁺ REMARK coordinates from minimization and B-factor refinement

REMARK refinement resolution: 90 - 1.5 A

REMARK starting r= .2933 free_r= .2909

REMARK final r= .2270 free_r= .2494

REMARK rmsd bonds= .009964 rmsd angles= 1.59282 REMARK B rmsd for bonded mainchain atoms= 1.428 target= 1.5

REMARK B rmsd for bonded sidechain atoms= 2.284 target= 2.0

REMARK B rmsd for angle mainchain atoms= 2.182 target= 2.0

REMARK B rmsd for angle sidechain atoms= 3.167 target= 2.5

REMARK target= mlf final wa= 2.11827 REMARK final rweight= .1856 (with wa= 2.11827)

REMARK md-method= torsion annealing schedule= constant

REMARK starting temperature= 2000 total md steps= 1 * 100

REMARK cycles= 2 coordinate steps= 20 B-factor steps= 10

REMARK sg= C2 a= 130.564 b= 47.074 c= 38.105 alpha= 90 beta= 93.784 gamma= 90 REMARK topology file 1 : ,CNS_TOPPAR:protein.top

REMARK topology file 2 : CNS_TOPPAR:dna-rna.top

REMARK topology file 3 : CNS__TOPPAR:water.top

REMARK topology file 4 : CNS_TOPPAR:ion.top

REMARK topology file 5 : CNSPAR:ctp.top REMARK parameter file 1 : CNS_TOPPAR:protein_rep.param

REMARK parameter file 2 : CNS_TOPPAR:dna-rna_rep.param

REMARK parameter file 3 : CNS_TOPPAR:water_rep.param

REMARK parameter file 4 : CNS_TOPPAR:ion.param

REMARK parameter file 5 : CNSPAR:ctp.param REMARK molecular structure file: generate. mtf

REMARK input coordinates: generate.pdb

REMARK reflection file= ygbp2.xpl

REMARK ncs= none

REMARK B-correction resolution: 6.0 - 1.5 REMARK initial B-factor correction applied to fobs :

REMARK B11 = 7.197 B22= -7.860 B33= .663

REMARK B12= .000 B13= .143 B23= .000

REMARK B-factor correction applied to coordinate array B: -.741

REMARK bulk solvent: density level= .365386 e/A^Λ3, B-factor= 45.0858 A^Λ2 REMARK reflections with |Fobs|/sigma_F < 0.0 rejected

REMARK reflections with JFobsj > 10000 * rms(Fobs) rejected

REMARK theoretical total number of refl. in resol. range: 37155 ( 100.0 % )

REMARK number of unobserved reflections (no entry or |F|=0): 2741 ( 7.4 % )

REMARK number of reflections rejected: 0 ( .0 % ) REMARK total number of reflections used: 34414 ( 92.6 % )

REMARK number of reflections in working set: 32682 ( 88.0 % )

REMARK number of reflections in test set: 1732 ( 4.7 % )

CRYST1 130.564 47.074 38.105 90.00 93.78 90.00 C 2

REMARK FILENAME="refine.pdb" REMARK DATE:24-Oct-00 14:14:42 created by user: richard

REMARK VERSION:1.0

ATOM 1 CB HIS A 5 29.154 -18.768 10.052 1.00 35.33 A

ATOM 2 CG HIS A 5 30.545 -19.141 9.646 1.00 38.47 A

ATOM 3 CD2 HIS A 5 31.312 -18.732 8.608 1.00 38.22 A A ATTOOMM 4 4 N NDD11 HHIISS AA 5 5 31.340 -19.974 10.405 1.00 38.98 A ATOM 5 CE1 HISA 5 32.537-20.058 9.853 1.0039.06 A

ATOM 6 NE2HISA 5 32.547-19.314 8.764 1.0038.86 A

ATOM 7 C HISA 5 30.439-17.272 11.579 1.0032.77 A

ATOM 8 O HISA 5 31.369-17.814 12.176 1.0032.69 A ATOM 9 N HISA 5 27.910-17.076 11.383 1.0033.62 A

ATOM 10 CA HISA 5 29.097-17.994 11.377 1.0034.27 A

ATOM 11 N LEU A 6 30.524-16.049 11.075 1.0030.52 A

ATOM 12 CA LEU A 6 31.750-15.270 11.141 1.0027.09 A

ATOM 13 CB LEU A 6 31.784-14.282 9.966 1.0029.57 A ATOM 14 CG LEU A 6 31.822-14.886 8.551 1.0030.37 A

ATOM 15 CD1 LEUA 6 31.767-13.761 7.509 1.0032.24 A

ATOM 16 CD2LEUA 6 33.091-15.695 8.364 1.0031.47 A

ATOM 17 C LEU A 6 31.980-14.530 12.456 1.0024.41 A

ATOM 18 O LEU A 6 32.988-13.856 12.619 1.0021.54 A ATOM 19 N ASP A 7 31.052-14.646 13.396 1.0022.72 A

ATOM 20 CA ASP A 7 31.204-13.966 14.689 1.0021.73 A

ATOM 21 CB ASP A 7 29.892-14.029 15.478 1.0024.18 A

ATOM 22 CG ASP A 7 28.825-13.072 14.948 1.0029.36 A

ATOM 23 OD1ASPA 7 28.909-12.639 13.786 1.0028.09 A ATOM 24 OD2ASPA 7 27.898-12.775 15.722 1.0033.58 A

ATOM 25 C ASPA 7 32.301 -14.661 15.505 1.0021.28 A

ATOM 26 O ASPA 7 32.302-15.884 15.645 1.0023.50 A

ATOM 27 N VALA 8 33.237-13.876 16.023 1.0017.05 A

ATOM 28 CA VALA 8 34.340-14.399 16.837 1.0014.95 A ATOM 29 CB VALA 8 35.711-14.038 16.185 1.0013.56 A

ATOM 30 CG1VALA 8 36.878-14.405 17.102 1.0014.57 A

ATOM 31 CG2VALA 8 35.830-14.770 14.869 1.0015.46 A

ATOM 32 C VALA 8 34.335-13.739 18.220 1.0015.86 A

ATOM 33 O VALA 8 34.042-12.537 18.343 1.0015.09 A ATOM 34 N CYSA 9 34.639-14.509 19.264 1.0014.35 A

ATOM 35 CA CYSA 9 34.790-13.934 20.598 1.0015.35 A

ATOM 36 CB CYSA 9 33.944-14.672 21.638 1.0014.95 A

ATOM 37 SG CYSA 9 34.106-13.99523.322 1.0022.28 A

ATOM 38 C CYSA 9 36.282-14.074 20.948 1.0016.35 A ATOM 39 O CYSA 9 36.871 -15.098 20.682 1.0015.32 A

ATOM 40 N ALAA 10 36.886-13.034 21.498 1.0014.31 A

ATOM 41 CA ALAA 10 38.291 -13.11521.907 1.0013.64 A

ATOM 42 CB ALAA 10 39.016-11.88521.503 1.0014.82 A

ATOM 43 C ALAA 10 38.375-13.281 23.424 1.0014.28 A ATOM 44 O ALAA 10 37.501-12.80324.161 1.0015.32 A

ATOM 45 N VALA 11 39.406-14.004 23.879 1.0013.95 A

ATOM 46 CA VALA 11 39.636-14.18025.312 1.0013.66 A

ATOM 47 CB VALA 11 39.544-15.65825.765 1.0013.48 A

ATOM 48 CG1VALA 11 40.004-15.761 27.237 1.0015.44 A ATOM 49 CG2VALA 11 38.089-16.126 25.664 1.0015.73 A

ATOM 50 C VALA 11 41.078-13.710 25.544 1.0012.91 A

ATOM 51 O VALA 11 42.009-14.16524.857 1.0013.54 A

ATOM 52 N VALA 12 41.255-12.802 26.497 1.0012.18 A

ATOM 53 CA VALA 12 42.567-12.25026.825 1.0013.20 A ATOM 54 CB VALA 12 42.555-10.696 26.643 1.0014.61 A

ATOM 55 CG1VALA 12 43.878-10.102 27.089 1.0016.25 A

ATOM 56 CG2VALA 12 42.319-10.343 25.163 1.0015.42 A

ATOM 57 C VALA 12 42.936-12.576 28.275 1.0015.56 A

ATOM 58 0 VALA 12 42.367-11.99429.201 1.0016.10 A ATOM 59 N PROA 13 43.818-13.56528.488 1.0015.73 A

ATOM 60 CD PROA 13 44.352-14.568 27.549 1.0015.57 A

ATOM 61 CA PROA 13 44.201-13.86629.877 1.0017.87 A ATOM 62 CB PROA 13 44.963-15.18329.765 1.0018.98 A

ATOM 63 CG PROA 13 45.440-15.24228.360 1.0019.82 A

ATOM 64 C PROA 13 45.087-12.704 30.351 1.0018.36 A

ATOM 65 O PROA 13 46.126-12.403 29.737 1.0020.50 A ATOM 66 N ALAA 14 44.658-12.036 31.420 1.0018.05 A

ATOM 67 CA ALAA 14 45.363-10.877 31.946 1.0017.96 A

ATOM 68 CB ALAA 14 44.705 -9.599 31.422 1.0019.55 A

ATOM 69 C ALAA 14 45.312-10.889 33.465 1.0019.04 A

ATOM 70 O ALAA 14 45.187 -9.84234.099 1.0017.63 A ATOM 71 N ALAA 15 45.438-12.080 34.032 1.0018.99 A

ATOM 72 CA ALAA 15 45.348-12.268 35.476 1.0021.55 A

ATOM 73 CB ALAA 15 44.415-13.423 35.769 1.0022.46 A

ATOM 74 C ALAA 15 46.698-12.500 36.140 1.0024.97 A

ATOM 75 O ALAA 15 46.767-12.730 37.349 1.0026.39 A ATOM 76 N GLY A 16 47.769-12.408 35.356 1.0024.66 A

ATOM 77 CA GLY A 16 49.104-12.592 35.900 1.0026.91 A

ATOM 78 C GLY A 16 49.602-11.337 36.589 1.0027.01 A

ATOM 79 O GLY A 16 48.979-10.270 36.499 1.0026.91 A

ATOM 80 N PHE A 17 50.745-11.472 37.263 1.0028.01 A ATOM 81 CA PHE A 17 51.372-10.385 38.024 1.0028.35 A

ATOM 82 CB PHE A 17 51.674-10.872 39.464 1.0028.66 A

ATOM 83 CG PHE A 17 50.485-11.47740.190 1.0028.93 A

ATOM 84 CD1 PHEA 17 50.685-12.43341.187 1.0030.11 A

ATOM 85 CD2PHEA 17 49.183-11.079 39.907 1.0027.69 A ATOM 86 CE1 PHEA 17 49.612-12.98541.882 1.0027.93 A

ATOM 87 CE2PHEA 17 48.089-11.62540.600 1.0027.62 A

ATOM 88 CZ PHE A 17 48.306-12.57641.583 1.0028.48 A

ATOM 89 C PHE A 17 52.683 -9.856 37.392 1.0028.54 A

ATOM 90 O PHE A 17 53.252 -8.868 37.869 1.0027.85 A ATOM 91 N GLYA 18 53.159-10.513 36.334 1.0029.85 A

ATOM 92 CA GLYA 18 54.386-10.074 35.683 1.0030.89 A

ATOM 93 C GLYA 18 55.523 -9.889 36.671 1.0031.81 A

ATOM 94 O GLYA 18 56.138 -8.812 36.759 1.0031.37 A

ATOM 95 N ARG A 19 . 55.804-10.949 37.418 1.0031.59 A ATOM 96 CA ARG A 19 56.864-10.911 38.426 1.0033.23 A

ATOM 97 CB ARG A 19 56.865-12.222 39.209 1.0032.02 A

ATOM 98 CG ARG A 19 57.897-12.31440.328 1.0034.02 A

ATOM 99 CD ARG A 19 58.464-13.733 40.386 1.0033.39 A

ATOM 100 NE ARG A 19 57.534-14.660 39.726 1.0033.01 A ATOM 101 CZ ARG A 19 57.803-15.927 39.426 1.0031.50 A

ATOM 102 NH1 ARG A 19 58.985-16.471 39.721 1.0033.70 A

ATOM 103 NH2ARGA 19 56.882-16.655 38.821 1.0035.56 A

ATOM 104 C ARG A 19 58.243-10.665 37.795 1.0033.26 A

ATOM 105 O ARG A 19 59.107-10.04938.410 1.0034.50 A ATOM 106 N ARG A 20 58.445-11.142 36.567 1.0033.73 A

ATOM 107 CA ARG A 20 59.722-10.942 35.884 1.0033.83 A

ATOM 108 CB ARG A 20 59.843-11.906 34.700 1.0034.00 A

ATOM 109 CG ARG A 20 60.001 -13.375 35.108 1.0033.35 A

ATOM 110 CD ARG A 20 60.002-14.302 33.887 1.0034.51 A ATOM 111 NE ARG A 20 58.650-14.687 33.456 1.0034.45 A

ATOM 112 CZ ARG A 20 58.386-15.420 32.371 1.0033.96 A

ATOM 113 NH1 ARG A 20 59.375-15.850 31.593 1.0033.51 A

ATOM 114 NH2 ARG A 20 57.131 -15.739 32.067 1.0034.23 A

ATOM 115 C ARG A 20 59.983 -9.499 35.409 1.0034.78 A ATOM 116 O ARG A 20 61.030 -9.224 34.803 1.0034.95 A

ATOM 117 N MET A 21 59.055 -8.579 35.685 1.0034.67 A

ATOM 118 CA MET A 21 59.228 -7.179 35.274 1.0034.61 A ATOM 1 19 CB MET A 21 57.895 -6.584 34.790 1.00 33.13 A

ATOM 120 CG MET A 21 57.401 -7.1 15 33.452 1.00 30.27 A

ATOM 121 SD MET A 21 58.443 -6.679 32.046 1.00 20.98 A

ATOM 122 CE MET A 21 58.542 -4.942 32.181 1.00 25.33 A

ATOM 123 C MET A 21 59.808 -6.263 36.349 1.00 36.15 A

ATOM 124 O MET A 21 60.202 -5.143 36.043 1 .00 37.80 A

ATOM 125 N ALA A 22 59.854 - 6.719 37.600 1.00 37.34 A

ATOM 126 CA ALA A 22 60.394 -5.889 38.685 1.00 38.25 A

ATOM 127 CB ALA A 22 61.671 -5.171 38.232 1.00 40.10 A

ATOM 128 C ALA A 22 59.419 - 4.838 39.187 1.00 38.85 A

ATOM 129 O ALA A 22 59.606 - ^■4.290 40.273 1.00 40.70 A

ATOM 130 N THR A 23 58.397 -4.530 38.401 1.00 39.16 A

ATOM 131 CA THR A 23 57.440 -3.516 38.818 1.00 38.94 A

ATOM 132 CB THR A 23 56.774 -2.820 37.592 1.00 39.69 A

ATOM 133 OG1 THR A 23 56.054 I -3.788 36.815 1.00 40.37 A

ATOM 134 CG2 THR A 23 57.824 ■ -2.151 36.715 1.00 38.43 A

ATOM 135 C THR A 23 56.353 ^■ -4.109 39.71 1 1.00 38.99 A

ATOM 136 O THR A 23 55.928 -5.263 39.538 1.00 39.51 A

ATOM 137 N GLU A 24 55.937 • -3.337 40.704 1.00 38.56 A

ATOM 138 CA GLU A 24 54.881 -3.798 41 .581 1.00 37.98 A

ATOM 139 CB GLU A 24 54.820 -2.933 42.841 1.00 39.72 A

ATOM 140 CG GLU A 24 53.568 -3.148 43.681 1 .00 41.57 A

ATOM 141 CD GLU A 24 53.718 -2.627 45.104 1.00 43.73 A

ATOM 142 OE1 GLU A 24 54.435 -1.608 45.289 1.00 43.87 A

ATOM 143 OE2 GLU A 24 53.109 -3.229 46.030 1.00 44.04 A

ATOM 144 C GLU A 24 53.593 ^■ -3.685 40.760 1.00 36.95 A

ATOM 145 O GLU A 24 52.598 -4.341 41.049 1.00 38.13 A

ATOM 146 N CYS A 25 53.623 ^■ -2.843 39.733 1.00 35.90 A

ATOM 147 CA CYS A 25 52.471 -2.684 38.857 1.00 33.76 A

ATOM 148 CB CYS A 25 52.547 -1.335 38.121 1.00 33.99 A

ATOM 149 SG CYS A 25 51.294 -1.072 36.811 1.00 33.82 A

ATOM 150 C CYS A 25 52.495 ^■ -3.838 37.851 1.00 32.91 A

ATOM 151 O CYS A 25 53.534 -4.124 37.241 1.00 31.82 A

ATOM 152 N PRO A 26 51.364 -4.551 37.696 1.00 30.12 A

ATOM 153 CD PRO A 26 50.1 12 -4.502 38.473 1.00 30.73 A

ATOM 154 CA PRO A 26 51.340 -5.660 36.736 1 .00 29.73 A

ATOM 155 CB PRO A 26 49.899 -6.158 36.816 1.00 29.49 A

ATOM 156 CG PRO A 26 49.547 -5.892 38.249 1.00 31 .19 A

ATOM 157 C PRO A 26 51.706 -5.104 35.360 1.00 26.87 A

ATOM 158 O PRO A 26 51.210 -4.051 34.952 1.00 27.18 A

ATOM 159 N LYS A 27 52.584 - 5.810 34.658 1.00 26.55 A

ATOM 160 CA LYS A 27 53.065 -5.362 33.358 1 .00 25.90 A

ATOM 161 CB LYS A 27 53.979 -6.420 32.756 1 .00 25.18 A

ATOM 162 CG LYS A 27 53.280 -7.695 32.334 1.00 23.47 A

ATOM 163 CD LYS A 27 54.317 -8.694 31.896 1.00 24.07 A

ATOM 164 CE LYS A 27 • 53.709 - ■10.025 31.580 1.00 25.87 A

ATOM 165 NZ LYS A 27 54.758 - ^■10.930 31.026 1.00 25.14 A

ATOM 166 C LYS A 27 51.986 - 4.989 32.360 1.00 26.12 A

ATOM 167 O LYS A 27 52.164 - ■4.057 31.567 1.00 25.02 A

ATOM 168 N GLN A 28 50.868 ^• -5.712 32.383 1.00 25.08 A

ATOM 169 CA GLN A 28 49.798 -5.385 31.444 1.00 24.50 A

ATOM 170 CB GLN A 28 48.654 -6.435 31.490 1.00 25.05 A

ATOM 171 CG GLN A 28 47.919 -6.597 32.824 1.00 25.83 A

ATOM 172 CD GLN A 28 48.597 -7.620 33.704 1.00 25.85 A

ATOM 173 OE1 GLN A 28 49.816 -7.645 33.775 1.00 25.91 A

ATOM 174 NE2 GLN A 28 47.820 -8.466 34.379 1.00 25.23 A

ATOM 175 C GLN A 28 49.252 ^■ -3.989 31.719 1.00 25.09 A ATOM 176 O GLN A 28 48.536 -3.430 30.897 1.00 23.92 A

ATOM 177 N TYR A 29 49.596 - ■3.411 32.871 1.00 24.17 A

ATOM 178 CA TYR A 29 49.106 -2.083 33.187 1.00 24.33 A

ATOM 179 CB TYR A 29 48.494 -2.043 34.602 1.00 25.67 A

ATOM 180 CG TYR A 29 47.210 -2.852 34.722 1.00 24.85 A

ATOM 181 CD1 TYR A 29 47.181 -4.075 35.398 1.00 24.71 A

ATOM 182 CE1 TYR A 29 46.013 -4.846 35.447 1.00 23.38 A

ATOM 183 CD2 TYR A 29 46.047 -2.429 34.100 1.00 24.91 A

ATOM 184 CE2 TYR A 29 44.883 -3.200 34.133 1.00 25.03 A

ATOM 185 CZ TYR A 29 44.876 -4.403 34.809 1.00 24.59 A

ATOM 186 OH TYR A 29 43.719 -5.143 34.840 1.00 25.01 A

ATOM 187 C TYR A 29 50.184 - ^■1.014 33.020 1.00 24.55 A

ATOM 188 O TYR A 29 49.963 .157 33.345 1.00 25.65 A

ATOM 189 N LEU A 30 51.345 - ^■1.421 32.518 1.00 24.86 A

ATOM 190 CA LEU A 30 52.410 -.474 32.240 1.00 25.87 A

ATOM 191 CB LEU A 30 53.752 -1.171 32.038 1.00 25.35 A

ATOM 192 CG LEU A 30 54.330 -1.819 33.287 1.00 28.75 A

ATOM 193 CD1 LEU A 30 55.608 -2.547 32.933 1.00 28.54 A

ATOM 194 CD2 LEU A 30 54.584 -.748 34.360 1.00 28.94 A

ATOM 195 C LEU A 30 51.974 .178 30.949 1.00 26.56 A

ATOM 196 O LEU A 30 51.209 -.405 30.164 1.00 23.47 A

ATOM 197 N SER A 31 52.453 1.389 30.712 1.00 27.10 A

ATOM 198 CA SER A 31 52.037 2.082 29.517 1.00 28.58 A

ATOM 199 CB SER A 31 51.427 3.428 29.896 1.00 29.76 A

ATOM 200 OG SER A 31 50.314 3.264 30.750 1.00 33.82 A

ATOM 201 C SER A 31 53.072 2.308 28.446 1.00 29.16 A

ATOM 202 O SER A 31 54.277 2.317 28.692 1.00 29.41 A

ATOM 203 N ILE A 32 52.553 2.463 27.234 1.00 28.68 A

ATOM 204 CA ILE A 32 53.338 2.786 26.067 1.00 29.30 A

ATOM 205 CB ILE A 32 53.482 1.628 25.101 1.00 29.81 A

ATOM 206 CG2 ILE A 32 54.253 2.098 23.864 1.00 31.20 A

ATOM 207 CG1 ILE A 32 54.242 .493 25.796 1.00 30.08 A

ATOM 208 CD1 ILE A 32 54.568 -.661 24.889 1.00 32.54 A

ATOM 209 C ILE A 32 52.510 3.898 25.453 1.00 30.33 A

ATOM 210 O ILE A 32 51.378 3.695 24.997 1.00 25.79 A

ATOM 211 N GLY A 33 53.078 5.099 25.471 1.00 31.92 A

ATOM 212 CA GLY A 33 52.354 6.249 24.980 1.00 34.62 A

ATOM 213 C GLY A 33 51.560 6.707 26.187 1.00 36.21 A

ATOM 214 O GLY A 33 52.117 7.287 27.129 1.00 40.13 A

ATOM 215 N ASN A 34 50.262 6.443 26.164 1.00 35.33 A

ATOM 216 CA ASN A 34 49.368 6.794 27.265 1.00 35.76 A

ATOM 217 CB ASN A 34 48.767 8.165 27.059 1.00 36.00 A

ATOM 218 CG ASN A 34 49.252 8.785 25.814 1.00 34.71 A

ATOM 219 OD1 ASN A 34 50.242 9.530 25.826 1.00 37.75 A

ATOM 220 ND2 ASN A 34 48.600 8.447 24.690 1.00 37.02 A

ATOM 221 C ASN A 34 48.262 5.767 27.269 1.00 35.51 A

ATOM 222 O ASN A 34 47.159 6.017 27.753 1.00 36.99 A

ATOM 223 N GLN A 35 48.565 4.623 26.678 1.00 33.00 A

ATOM 224 CA GLN A 35 47.641 3.508 26.656 1.00 30.33 A

ATOM 225 CB GLN A 35 47.326 3.106 25.231 1.00 34.12 A

ATOM 226 CG GLN A 35 45.874 2.836 25.015 1.00 37.20 A

ATOM 227 CD GLN A 35 45.536 2.633 23.558 1.00 39.52 A

ATOM 228 OE1 GLN A 35 45.514 3.582 22.773 1.00 41.95 A

ATOM 229 NE2 GLN A 35 45.304 1.385 23.177 1.00 41.18 A

ATOM 230 C GLN A 35 48.396 2.381 27.336 1.00 26.79 A

ATOM 231 O GLN A 35 49.606 2.279 27.173 1.00 24.51 A

ATOM 232 N THR A 36 47.696 1.545 28.104 1.00 23.04 A ATOM 233 CA THR A 36 48.348 .435 28.781 1.00 21.21 A

ATOM 234 CB THR A 36 47.459 -.158 29.892 1.00 21.39 A

ATOM 235 0G1 THR A 36 46.212 -.586 29.333 1.0020.25 A

ATOM 236 CG2 THR A 36 47.186 .869 30.982 1.00 23.04 A ATOM 237 C THR A 36 48.604 -.676 27.773 1.00 19.28 A

ATOM 238 O THR A 36 47.974 -.710 26.707 1.00 19.13 A

ATOM 239 N ILE A 37 49.540 -1.564 28.111 1.00 17.97 A

ATOM 240 CA ILE A 37 49.856 -2.713 27.265 1.00 17.40 A

ATOM 241 CB ILE A 37 50.906 -3.642 27.960 1.00 18.43 A ATOM 242 CG2 ILE A 37 51.067 -4.944 27.202 1.00 20.24 A

ATOM 243 CG1 ILE A 37 52.271 -2.940 28.017 1.00 21.81 A

ATOM 244 CD1 ILE A 37 52.702 -2.402 26.714 1.00 25.97 A

ATOM 245 C ILE A 37 48.546 -3.486 27.022 1.00 15.83 A

ATOM 246 O ILE A 37 48.262 -3.904 25.889 1.00 15.77 A ATOM 247 N LEU A 38 47.741 -3.671 28.067 1.00 15.45 A

ATOM 248 CA LEU A 38 46.469 -4.384 27.907 1.00 15.80 A

ATOM 249 CB LEU A 38 45.740 -4.463 29.256 1.00 17.12 A

ATOM 250 CG LEU A 38 44.335 -5.061 29.212 1.00 17.44 A

ATOM 251 CD1 LEU A 38 44.397 -6.499 28.683 1.00 18.18 A ATOM 252 CD2 LEU A 38 43.726 -5.035 30.604 1.00 19.06 A

ATOM 253 C LEU A 38 45.587 -3.672 26.851 1.00 15.36 A

ATOM 254 O LEU A 38 44.980 -4.316 25.989 1.00 15.75 A

ATOM 255 N GLU A 39 45.525 -2.342 26.886 1.00 15.93 A

ATOM 256 CA GLU A 39 44.707 -1.625 25.912 1.00 17.21 A ATOM 257 CB GLU A 39 44.595 -.143 26.285 1.00 18.21 A

ATOM 258 CG GLU A 39 43.635 .056 27.456 1.00 20.61 A

ATOM 259 CD GLU A 39 43.759 1.412 28.105 1.00 23.58 A

ATOM 260 OE1 GLU A 39 42.848 2.256 27.871 1.00 28.16 A

ATOM 261 OE2 GLU A 39 44.757 1.628 28.834 1.00 22.14 A ATOM 262 C GLU A 39 45.229 -1.789 24.489 1.00 15.58 A

ATOM 263 O GLU A 39 44.442 -2.033 23.556 1.00 18.20 A

ATOM 264 N HIS A 40 46.542 -1.676 24.292 1.00 17.07 A

ATOM 265 CA HIS A 40 47.081 -1.882 22.938 1.00 16.87 A

ATOM 266 CB HIS A 40 48.608 -1.831 22.939 1.00 17.54 A ATOM 267 CG HIS A 40 49.184 -.455 23.081 1.00 18.22 A

ATOM 268 CD2 HIS A 40 49.786 .146 24.130 1.00 19.94 A

ATOM 269 ND1 HIS A 40 49.184 .467 22.054 1.00 21.68 A

ATOM 270 CE1 HIS A 40 49.763 1.581 22.470 1.00 21.75 A

ATOM 271 NE2 HIS A 40 50.136 1.415 23.728 1.00 20.48 A ATOM 272 C HIS A 40 46.663 -3.265 22.421 1.00 15.95 A

ATOM 273 0 HIS A 40 46.213 -3.419 21.280 1.00 17.34 A

ATOM 274 N SER A 41 46.819 -4.283 23.271 1.00 14.78 A

ATOM 275 CA SER A 41 46.460 -5.629 22.894 1.00 15.60 A

ATOM 276 CB SER A 41 46.833 -6.611 24.014 1.00 16.56 A ATOM 277 OG SER A 41 48.215 -6.590 24.205 1.0020.21 A

ATOM 278 C SER A 41 44.987 -5.796 22.542 1.00 16.38 A

ATOM 279 O SER A 41 44.636 -6.355 21.496 1.00 15.32 A

ATOM 280 N VAL A 42 44.117 -5.310 23.421 1.00 14.52 A

ATOM 281 CA VAL A 42 42.684 -5.430 23.231 1.00 15.98 A ATOM 282 CB VAL A 42 41.966 -4.917 24.495 1.00 14.93 A

ATOM 283 CG1 VAL A 42 40.478 -4.764 24.257 1.00 16.23 A

ATOM 284 CG2 VAL A 42 42.228 -5.882 25.623 1.00 15.67 A

ATOM 285 C VAL A 42 42.222 -4.671 22.008 1.00 15.24 A

ATOM 286 O VAL A 42 41.402 -5.158 21.209 1.00 15.34 A ATOM 287 N HIS A 43 42.749 -3.470 21.835 1.00 15.87 A

ATOM 288 CA HIS A 43 42.321 -2.704 20.680 1.00 17.76 A

ATOM 289 CB HIS A 43 42.759 -1.252 20.840 1.00 20.59 A ATOM 290 CG HIS A 43 41.973 -.521 21.891 1.00 25.11 A

ATOM 291 CD2 HIS A 43 42.368 .213 22.959 1.00 26.37 A

ATOM 292 ND1 HIS A 43 40.592 -.492 21.898 1.00 24.93 A

ATOM 293 CE1 HIS A 43 40.173 .230 22.924 1.00 27.12 A ATOM 294 NE2 HIS A 43 41.230 .671 23.583 1.00 26.59 A

ATOM 295 C HIS A 43 42.762 -3.321 19.370 1.00 16.08 A

ATOM 296 O HIS A 43 42.074 -3.159 18.348 1.00 16.83 A

ATOM 297 N ALA A 44 43.870 -4.067 19.363 1.00 15.17 A

ATOM 298 CA ALA A 44 44.266 -4.687 18.097 1.00 15.38 A ATOM 299 CB ALA A 44 45.690 -5.285 18.189 1.00 16.25 A

ATOM 300 C ALA A 44 43.234 -5.772 17.724 1.00 14.81 A

ATOM 301 O ALA A 44 42.915 -5.951 16.562 1.00 15.91 A

ATOM 302 N LEU A 45 42.702 -6.489 18.712 1.00 13.33 A

ATOM 303 CA LEU A 45 41.694 -7.494 18.431 1.00 14.68 A ATOM 304 CB LEU A 45 41.400 -8.305 19.701 1.00 14.24 A

ATOM 305 CG LEU A 45 42.639 -8.968 20.321 1.00 13.57 A

ATOM 306 CD1 LEU A 45 42.273 -9.555 21.675 1.00 17.66 A

ATOM 307 CD2 LEU A 45 43.186 -10.019 19.397 1.00 15.75 A

ATOM 308 C LEU A 45 40.387 -6.840 17.946 1.00 14.57 A ATOM 309 O LEU A 45 39.772 -7.330 17.007 1.00 14.75 A

ATOM 310 N LEU A 46 39.964 -5.776 18.622 1.00 15.14 A

ATOM 311 CA LEU A 46 38.707 -5.110 18.275 1.00 16.70 A

ATOM 312 CB LEU A 46 38.294 -4.113 19.373 1.00 15.91 A

ATOM 313 CG LEU A 46 37.851 -4.769 20.680 1.00 17.28 A ATOM 314 CD1 LEU A 46 37.588 -3.731 21.759 1.00 19.07 A

ATOM 315 CD2 LEU A 46 36.615 -5.612 20.409 1.00 19.67 A

ATOM 316 C LEU A 46 38.747 -4.426 16.921 1.00 18.12 A

ATOM 317 O LEU A 46 37.689 -4.039 16.381 1.00 17.11 A

ATOM 318 N ALA A 47 39.944 -4.256 16.362 1.00 17.31 A ATOM 319 CA ALA A 47 40.040 -3.612 15.054 1.00 16.97 A

ATOM 320 CB ALA A 47 41.490 -3.210 14.750 1.00 16.64 A

ATOM 321 C ALA A 47 39.502 -4.494 13.942 1.00 18.74 A

ATOM 322 O ALA A 47 39.043 -3.988 12.918 1.00 20.37 A

ATOM 323 N HIS A 48 39.548 -5.810 14.112 1.00 15.77 A ATOM 324 CA HIS A 48 39.035 -6.676 13.060 1.00 15.79 A

ATOM 325 CB HIS A 48 39.679 -8.064 13.127 1.00 14.19 A

ATOM 326 CG HIS A 48 39.359 -8.899 11.934 1.00 16.96 A

ATOM 327 CD2 HIS A 48 40.134 -9.352 10.919 1.00 19.54 A

ATOM 328 ND1 HIS A 48 38.072 -9.282 11.638 1.00 15.40 A ATOM 329 CE1 HIS A 48 38.060 -9.936 10.488 1.00 18.80 A

ATOM 330 NE2 HIS A 48 39.303 -9.993 10.033 1.00 20.46 A

ATOM 331 C HIS A 48 37.516 -6.788 13.207 1.00 16.85 A

ATOM 332 O HIS A 48 37.013 -7.122 14.288 1.00 15.48 A

ATOM 333 N PRO A 49 36.747 -6.520 12.128 1.00 17.76 A ATOM 334 CD PRO A 49 37.136 -6.136 10.755 1.00 20.07 A

ATOM 335 CA PRO A 49 35.283 -6.598 12.238 1.00 17.87 A

ATOM 336 CB PRO A 49 34.800 -6.352 10.797 1.00 18.38 A ATOM 337 CG PRO A 49 35.831 -5.498 10.237 1.00 20.52 A

ATOM 338 C PRO A 49 34.644 -7,849 12.799 1.00 16.63 A ATOM 339 O PRO A 49 33.567 -7.779 13.358 1.00 17.87 A

ATOM 340 N ARG A 50 35.291 -9.000 12.628 1.00 15.65 A

ATOM 341 CA ARG A 50 34.705 -10.237 13.099 1.00 14.52 A

ATOM 342 CB ARG A 50 35.371 -11.447 12.431 1.00 14.72 A

ATOM 343 CG ARG A 50 34.991 -11.653 10.957 1.00 15.70 A ATOM 344 CD ARG A 50 35.700 -12.871 10.356 1.00 16.30 A

ATOM 345 NE ARG A 50 35.314 -14.097 11.063 1.00 15.60 A

ATOM 346 CZ ARG A 50 35.924 -15.264 10.920 1.00 15.54 A ATOM 347 NH1 ARG A 50 36.960-15.400 10.075 1.0016.64 A

ATOM 348 NH2 ARG A 50 35.522-16.296 11.658 1.0016.95 A

ATOM 349 C ARG A 50 34.762-10.379 14.622 1.0015.56 A

ATOM 350 O ARG A 50 34.024-11.174 15.189 1.0015.79 A ATOM 351 N VALA 51 35.622 -9.627 15.280 1.0013.34 A

ATOM 352 CA VALA 51 35.687 -9.735 16.736 1.0012.40 A

ATOM 353 CB VALA 51 37.064 -9.314 17.255 1.0012.17 A

ATOM 354 CG1 VALA 51 37.093 -9.505 18.780 1.0015.31 A

ATOM 355 CG2VALA 51 38.133-10.139 16.603 1.0013.45 A ATOM 356 C VALA 51 34.543 -8.931 17.364 1.0014.50 A

ATOM 357 O VALA 51 34.577 -7.713 17.472 1.0016.52 A

ATOM 358 N LYS A 52 33.526 -9.655 17.797 1.0014.51 A

ATOM 359 CA LYS A 52 32.327 -9.029 18.361 1.0015.31 A

ATOM 360 CB LYS A 52 31.080 -9.870 18.039 1.0016.47 A ATOM 361 CG LYS A 52 30.985-10.359 16.588 1.0016.59 A

ATOM 362 CD LYS A 52 31.072 -9.195 15.594 1.0016.24 A

ATOM 363 CE LYS A 52 30.781 -9.656 14.183 1.0018.96 A

ATOM 364 NZ LYS A 52 30.848 -8.511 13.240 1.0021.54 A

ATOM 365 C LYS A 52 32.365 -8.862 19.870 1.0016.57 A ATOM 366 O LYS A 52 31.569 -8.111 20.452 1.0018.90 A

ATOM 367 N ARG A 53 33.261 -9.589 20.496 1.0015.64 A

ATOM 368 CA ARG A 53 33.345 -9.556 21.941 1.0017.52 A

ATOM 369 CB ARG A 53 32.425-10.616 22.511 1.0021.74 A

ATOM 370 CG ARG A 53 32.315-10.59724.011 1.0029.80 A ATOM 371 CD ARG A 53 31.452 -11.756 24.450 1.0034.62 A

ATOM 372 NE ARG A 53 30.917-11.551 25.783 1.0038.19 A

ATOM 373 CZ ARG A 53 30.005-12.341 26.340 1.0041.59 A

ATOM 374 NH1 ARG A 53 29.538-13.38825.667 1.0041.75 A

ATOM 375 NH2 ARG A 53 29.545-12.07827.559 1.0042.21 A ATOM 376 C ARG A 53 34.734 -9.874 22.414 1.0017.34 A

ATOM 377 O ARG A 53 35.479-10.588 21.751 1.0016.17 A

ATOM 378 N VALA 54 35.094 -9.330 23.568 1.0015.82 A

ATOM 379 CA VALA 54 36.386 -9.681 24.142 1.0013.98 A

ATOM 380 CB VALA 54 37.427 -8.580 24.020 1.0014.23 A ATOM 381 CG1 VAL A 54 38.756 -9.02524.600 1.0015.34 A

ATOM 382 CG2VALA 54 37.622 -8.25922.549 1.0013.83 A

ATOM 383 C VALA 54 36.129 -9.909 25.622 1.0015.48 A

ATOM 384 O VALA 54 35.528 -9.074 26.292 1.0019.41 A

ATOM 385 N VALA 55 36.562-11.068 26.096 1.0013.36 A ATOM 386 CA VALA 55 36.437-11.42727.499 1.0013.37 A

ATOM 387 CB VALA 55 35.913-12.866 27.674 1.0015.78 A

ATOM 388 CG1 VAL A 55 35.793-13.15929.169 1.0016.54 A

ATOM 389 CG2 VAL A 55 34.541 -13.046 27.017 1.0015.99 A

ATOM 390 C VALA 55 37.852-11.345 28.073 1.0013.11 A ATOM 391 O VALA 55 38.753-12.054 27.606 1.0013.82 A

ATOM 392 N ILEA 56 38.045-10.498 29.082 1.0013.16 A

ATOM 393 CA ILEA 56 39.347-10.313 29.725 1.0014.31 A

ATOM 394 CB ILEA 56 39.671 -8.831 29.838 1.0015.14 A

ATOM 395 CG2ILEA 56 41.054 -8.641 30.405 1.0016.24 A ATOM 396 CG1 ILEA 56 39.537 -8.186 28.445 1.0015.56 A

ATOM 397 CD1 ILEA 56 39.853 -6.692 28.442 1.0017.36 A

ATOM 398 C ILEA 56 39.317-10.935 31.119 1.0015.62 A

ATOM 399 O ILEA 56 38.454-10.597 31.918 1.0016.74 A

ATOM 400 N ALA A 57 40.238-11.854 31.395 1.0014.35 A ATOM 401 CA ALAA 57 40.266-12.508 32.705 1.0016.52 A

ATOM 402 CB ALAA 57 40.695-13.962 32.554 1.0014.74 A

ATOM 403 C ALAA 57 41.287-11.760 33.533 1.0017.14 A ATOM 404 O ALAA 57 42.436-11.640 33.109 1.0018.16 A

ATOM 405 N ILEA 58 40.884-11.303 34.723 1.0018.41 A

ATOM 406 CA ILEA 58 41.789-10.568 35.582 1.0017.97 A ATOM 407 CB ILEA 58 41.322 -9.116 35.765 1.0019.92 A ATOM 408 CG2ILEA 58 41.287 -8.41334.404 1.0020.37 A

ATOM 409 CG1 ILEA 58 39.915 -9.06436.362 1.0018.48 A

ATOM 410 CD1 ILEA 58 39.473 -7.64736.748 1.0021.10 A

ATOM 411 C ILEA 58 41.884-11.263 36.943 1.0018.45 A

ATOM 412 0 ILEA 58 41.062-12.117 37.281 1.0019.54 A ATOM 413 N SERA 59 42.900-10.90937.713 1.0020.22 A

ATOM 414 CA SERA 59 43.068-11.52339.020 1.0021.73 A

ATOM 415 CB SERA 59 44.435-11.14439.591 1.0021.16 A

ATOM 416 OG SERA 59 44.549-11.59940.931 1.0027.61 A

ATOM 417 C SERA 59 41.997-11.001 39.951 1.0020.98 A ATOM 418 0 SERA 59 41.516 -9.899 39.771 1.0021.86 A

ATOM 419 N PROA 60 41.560-11.81040.932 1.0022.36 A

ATOM 420 CD PROA 60 41.661 -13.26941.077 1.0024.77 A

ATOM 421 CA PROA 60 40.544-11.24441.825 1.0024.69 A

ATOM 422 CB PROA 60 40.165-12.42042.742 1.0026.73 A ATOM 423 CG PROA 60 41.186-13.47342.493 1.0026.33 A

ATOM 424 C PROA 60 41.243-10.09742.581 1.0026.73 A

ATOM 425 0 PROA 60 42.444-10.14942.819 1.0027.75 A

ATOM 426 N GLYA 61 40.524 -9.051 42.952 1.0030.12 A

ATOM 427 CA GLYA 61 41.215 -7.96243.634 1.0032.79 A ATOM 428 C GLYA 61 41.865 -6.92242.714 1.0033.94 A

ATOM 429 O GLYA 61 42.068 -5.77443.135 1.0034.84 A

ATOM 430 N ASPA 62 42.219 -7.321 41.483 1.0033.01 A

ATOM 431 CA ASP A 62 42.796 -6.40740.481 1.0032.37 A

ATOM 432 CB ASPA 62 42.736 -7.05339.075 1.0031.25 A ATOM 433 CG ASPA 62 43.210 -6.113 37.955 1.0031.73 A

ATOM 434 OD1 ASPA 62 43.309 -4.893 38.171 1.0032.93 A

ATOM 435 OD2ASPA 62 43.471 -6.598 36.842 1.0028.27 A

ATOM 436 C ASPA 62 41.919 -5.15740.494 1.0031.28 A

ATOM 437 O ASPA 62 40.794 -5.18339.989 1.0033.15 A ATOM 438 N SERA 63 42.429 -4.07041.074 1.0032.19 A

ATOM 439 CA SERA 63 41.685 -2.81441.163 1.0033.27 A

ATOM 440 CB SERA 63 41.974 -2.13042.505 1.0034.57 A

ATOM 441 OG SERA 63 43.370 -1.98542.702 1.0036.92 A

ATOM 442 C SERA 63 42.009 -1.83640.037 1.0032.43 A ATOM 443 0 SERA 63 41.453 -.74039.964 1.0034.16 A

ATOM 444 N ARG A 64 42.911 -2.222 39.155 1.0030.86 A

ATOM 445 CA ARG A 64 43.294 -1.33338.069 1.0029.54 A

ATOM 446 CB ARG A 64 44.712 -1.65937.604 1.0031.18 A

ATOM 447 CG ARG A 64 45.786 -1.33038.635 1.0033.85 A ATOM 448 CD ARG A 64 47.174 -1.582 38.070 1.0034.86 A

ATOM 449 NE ARG A 64 48.245 -1.21438.995 1.0038.00 A

ATOM 450 CZ ARG A 64 48.511 -1.84940.130 1.0039.31 A

ATOM 451 NH1ARGA 64 47.781 -2.89040.496 1.0040.37 A

ATOM 452 NH2 ARG A 64 49.527 -1.45440.890 1.0042.22 A ATOM 453 C ARG A 64 42.367 -1.376 36.875 1.0029.02 A

ATOM 454 0 ARG A 64 42.015 -.33336.321 1.0026.60 A

ATOM 455 N PHE A 65 41.978 -2.578 36.470 1.0026.58 A

ATOM 456 CA PHE A 65 41.116 -2.713 35.310 1.0027.19 A

ATOM 457 CB PHE A 65 40.584 -4.140 35.189 1.0025.73 A ATOM 458 CG PHE A 65 39.777 -4.37433.943 1.0025.26 A

ATOM 459 CD1 PHE A 65 40.415 -4.543 32.711 1.0024.66 A

ATOM 460 CD2PHEA 65 38.389 -4.41533.995 1.0024.69 A ATOM 461 CE1 PHE A 65 39.682 -4.751 31.553 1.00 26.53 A

ATOM 462 CE2 PHE A 65 37.638 -4.624 32.840 1.00 26.25 A

ATOM 463 CZ PHE A 65 38.292 -4.792 31.610 1.00 26.41 A

ATOM 464 C PHE A 65 39.928 ■ -1.769 35.334 1.00 27.84 A

ATOM 465 O PHE A 65 39.634 -1.105 34.343 1.00 27.31 A

ATOM 466 N ALA A 66 39.237 - 1.718 36.469 1.00 27.80 A

ATOM 467 CA ALA A 66 38.052 -.891 36.586 1.00 29.41 A

ATOM 468 CB ALA A 66 37.468 -1.003 37.992 1.00 29.97 A

ATOM 469 C ALA A 66 38.289 .561 36.235 1.00 30.45 A

ATOM 470 O ALA A 66 37.352 1.256 35.849 1.00 30.58 A

ATOM 471 N GLN A 67 39.533 1.023 36.342 1.00 30.88 A

ATOM 472 CA GLN A 67 39.827 2.425 36.037 1.00 34.01 A

ATOM 473 CB GLN A 67 40.967 2.923 36.929 1.00 35.63 A

ATOM 474 CG GLN A 67 40.685 2.745 38.409 1.00 38.59 A

ATOM 475 CD GLN A 67 39.308 3.256 38.792 1.00 40.38 A

ATOM 476 OE1 GLN A 67 38.970 4.417 38.537 1.00 42.52 A

ATOM 477 NE2 GLN A 67 38.501 2.393 39.407 1.00 40.21 A

ATOM 478 C GLN A 67 40.161 2.725 34.567 1.00 34.08 A

ATOM 479 O GLN A 67 40.475 3.871 34.215 1.00 35.16 A

ATOM 480 N LEU A 68 40.092 1.704 33.715 1.00 33.17 A

ATOM 481 CA LEU A 68 40.382 1.879 32.293 1.00 31.98 A

ATOM 482 CB LEU A 68 41.154 .666 31.753 1.00 30.47 A

ATOM 483 CG LEU A 68 42.464 .265 32.426 1.00 30.28 A

ATOM 484 CD1 LEU A 68 42.987 -1.026 31.797 1.00 29.38 A

ATOM 485 CD2 LEU A 68 43.479 1.392 32.286 1.00 31.14 A

ATOM 486 C LEU A 68 39.080 2.014 31.502 1.00 32.32 A

ATOM 487 O LEU A 68 38.023 1.596 31.965 1.00 32.34 A

ATOM 488 N PRO A 69 39.146 2.593 30.289 1.00 33.02 A

ATOM 489 CD PRO A 69 40.317 3.302 29.735 1.00 33.95 A

ATOM 490 CA PRO A 69 37.959 2.766 29.435 1.00 33.11 A

ATOM 491 CB PRO A 69 38.511 3.528 28.233 1.00 34.68 A

ATOM 492 CG PRO A 69 39.671 4.319 28.835 1.00 35.12 A

ATOM 493 C PRO A 69 37.357 1.407 29.044 1.00 33.26 A

ATOM 494 O PRO A 69 36.162 1.276 28.800 1.00 33.69 A

ATOM 495 N LEU A 70 38.197 .388 28.989 1.00 32.17 A

ATOM 496 CA LEU A 70 37.729 -.945 28.634 1.00 31.80 A

ATOM 497 CB LEU A 70 38.885 -1.923 28.678 1.00 30.79 A

ATOM 498 CG LEU A 70 40.110 -1.613 27.834 1.00 30.22 A

ATOM 499 CD1 LEU A 70 41.099 -2.734 28.068 1.00 28.58 A

ATOM 500 CD2 LEU A 70 39.743 -1.497 26.364 1.00 28.70 A

ATOM 501 C LEU A 70 36.649 - 1.471 29.557 1.00 31.86 A

ATOM 502 O LEU A 70 35.858 - ^■2.332 29.174 1.00 32.33 A

ATOM 503 N ALA A 71 36.640 -.963 30.786 1.00 32.20 A

ATOM 504 CA ALA A 71 35.692 -1.395 31.797 1.00 31.87 A

ATOM 505 CB ALA A 71 36.047 -.754 33.139 1.00 32.57 A

ATOM 506 C ALA A 71 34.241 - 1.097 31.437 1.00 30.89 A

ATOM 507 O ALA A 71 33.336 - 1.777 31.916 1.00 31.74 A

ATOM 508 N ASN A 72 34.019 -.097 30.589 1.00 28.33 A

ATOM 509 CA ASN A 72 32.658 .277 30.202 1.00 27.96 A

ATOM 510 CB ASN A 72 32.399 1.728 30.614 1.00 32.03 A

ATOM 511 CG ASN A 72 32.427 1.916 32.123 1.00 34.86 A

ATOM 512 OD1 ASN A 72 33.043 2.856 32.638 1.00 39.66 A

ATOM 513 ND2 ASN A 72 31.743 1.031 32.839 1.00 35.66 A

ATOM 514 C ASN A 72 32.341 .095 28.716 1.00 25.17 A

ATOM 515 O ASN A 72 31.312 .570 28.217 1.00 24.91 A

ATOM 516 N HIS A 73 33.218 - .618 28.019 1.00 21.98 A

ATOM 517 CA HIS A 73 33.070 -.866 26.593 1.00 18.90 A ATOM 518 CB HIS A 73 34.404 -1.355 26.069 1.00 18.25 A

ATOM 519 CG HIS A 73 34.465 -1.459 24.583 1.00 18.07 A

ATOM 520 CD2 HIS A 73 33.730 -2.195 23.725 1.00 16.10 A

ATOM 521 ND1 HIS A 73 35.361 -.746 23.811 1.00 18.96 A

ATOM 522 CE1 HIS A 73 35.163 -1.039 22.538 1.00 15.21 A

ATOM 523 NE2 HIS A 73 34.180 -1.914 22.459 1.00 19.78 A

ATOM 524 C HIS A 73 31.976 -1.903 26.366 1.00 17.23 A

ATOM 525 O HIS A 73 31.986 -2.967 26.975 1.00 18.97 A

ATOM 526 N PRO A 74 31.038 -1.629 25.439 1.00 16.35 A

ATOM 527 CD PRO A 74 30.960 -.463 24.541 1.00 17.25 A

ATOM 528 CA PRO A 74 29.949 -2.571 25.197 1.00 16.24 A

ATOM 529 CB PRO A 74 29.007 -1.793 24.251 1.00 16.50 A

ATOM 530 CG PRO A 74 29.911 -.882 23.513 1.00 16.03 A

ATOM 531 C PRO A 74 30.336 -3.935 24.683 1.00 16.81 A

ATOM 532 O PRO A 74 29.564 -4.898 24.831 1.00 18.71 A

ATOM 533 N GLN A 75 31.541 -4.058 24.123 1.00 16.14 A

ATOM 534 CA GLN A 75 31.968 -5.355 23.590 1.00 17.00 A

ATOM 535 CB GLN A 75 32.655 -5.177 22.233 1.00 14.34 A

ATOM 536 CG GLN A 75 31.683 -4.634 21.150 1.00 15.60 A

ATOM 537 CD GLN A 75 32.390 -4.254 19.842 1.00 15.43 A

ATOM 538 OE1 GLN A 75 33.241 -3.358 19.800 1.00 19.31 A

ATOM 539 NE2 GLN A 75 32.038 -4.930 18.785 1.00 18.09 A

ATOM 540 C GLN A 75 32.920 -6.095 24.526 1.00 17.88 A

ATOM 541 O GLN A 75 33.370 -7.182 24.173 1.00 18.66 A

ATOM 542 N ILE A 76 33.185 -5.543 25.716 1.00 17.28 A

ATOM 543 CA ILE A 76 34.116 -6.163 26.642 1.00 17.98 A

ATOM 544 CB ILE A 76 35.257 -5.193 26.956 1.00 17.24 A

ATOM 545 CG2 ILE A 76 36.261 -5.848 27.910 1.00 19.78 A

ATOM 546 CG1 ILE A 76 35.985 -4.838 25.650 1.00 19.19 A

ATOM 547 CD1 ILE A 76 37.026 -3.762 25.826 1.00 22.62 A

ATOM 548 C ILE A 76 33.470 -6.624 27.934 1.00 19.13 A

ATOM 549 O ILE A 76 32.742 -5.874 28.570 1.00 20.34 A

ATOM 550 N THR A 77 33.788 -7.856 28.317 1.00 18.36 A

ATOM 551 CA THR A 77 33.261 -8.498 29.515 1.00 18.73 A

ATOM 552 CB THR A 77 32.465 -9.755 29.124 1.00 22.50 A

ATOM 553 OG1 THR A 77 31.385 -9.378 28.254 1.00 25.58 A

ATOM 554 CG2 THR A 77 31.924 -10.460 30.353 1.00 23.93 A

ATOM 555 C THR A 77 34.471 -8.926 30.335 1.00 19.00 A

ATOM 556 O THR A 77 35.433 -9.434 29.786 1.00 18.50 A

ATOM 557 N VAL A 78 34.436 -8.719 31.642 1.00 19.40 A

ATOM 558 CA VAL A 78 35.564 -9.116 32.469 1.00 19.89 A

ATOM 559 CB VAL A 78 36.031 -7.928 33.337 1.00 23 75 A

ATOM 560 CG1 VAL A 78 34.920 -7.524 34.299 1.00 24.68 A

ATOM 561 CG2 VAL A 78 37.284 -8.286 34.105 1.00 25.87 A

ATOM 562 C VAL A 78 35.140 -10.268 33.374 1.00 19.37 A

ATOM 563 O VAL A 78 33.985 -10.345 33.782 1.00 20.50 A

ATOM 564 N VAL A 79 36.069 -11.171 33.662 1.00 18.53 A

ATOM 565 CA VAL A 79 35.803 -12.290 34.555 1.00 19.64 A

ATOM 566 CB VAL A 79 35.526 -13.592 33.787 1.00 21.64 A

ATOM 567 CG1 VAL A 79 34.347 -13.384 32.829 1.00 20.90 A

ATOM 568 CG2 VAL A 79 36.764 -14.042 33.027 1.00 21.64 A

ATOM 569 C VAL A 79 37.053 -12.484 35.388 1.00 18.59 A

ATOM 570 O VAL A 79 38.114 -11.965 35.056 1.00 17.18 A

ATOM 571 N ASP A 80 36.936 -13.224 36.484 1.00 20.90 A

ATOM 572 CA ASP A 80 38.104 -13.474 37.302 1.00 21.87 A

ATOM 573 CB ASP A 80 37.728 -13.836 38.753 1.00 24.61 A

ATOM 574 CG ASP A 80 37.342 -12.630 39.593 1.00 28.38 A ATOM 575 OD1 ASP A 80 37.433-11.47739.113 1.0029.26 A

ATOM 576 OD2 ASP A 80 36.936-12.82840.767 1.0030.57 A

ATOM 577 C ASPA 80 38.861 -14.645 36.700 1.0020.01 A

ATOM 578 0 ASPA 80 38.271 -15.665 36.330 1.0021.81 A ATOM 579 N GLYA 81 40.173-14.482 36.605 1.0022.14 A

ATOM 580 CA GLYA 81 41.024-15.536 36.091 1.0023.88 A

ATOM 581 C GLYA 81 41.384-16.498 37.223 1.0027.85 A

ATOM 582 O GLYA 81 40.781-16.433 38.311 1.0026.32 A

ATOM 583 N GLYA 82 42.365-17.367 36.979 1.0028.98 A ATOM 584 CA GLYA 82 42.765-18.364 37.969 1.0032.02 A

ATOM 585 C GLYA 82 44.245-18.422 38.301 1.0033.56 A

ATOM 586 O GLYA 82 44.993-17.506 37.973 1.0032.84 A

ATOM 587 N ASP A 83 44.670-19.505 38.956 1.0035.24 A

ATOM 588 CA ASPA 83 46.069-19.673 39.360 1.0035.35 A ATOM 589 CB ASPA 83 46.225-20.948 40.199 1.0039.08 A

ATOM 590 CG ASPA 83 45.158-21.07341.264 1.0041.85 A

ATOM 591 OD1ASPA 83 44.854-20.051 41.922 1.0044.29 A

ATOM 592 OD2ASPA 83 44.633-22.19441.454 1.0044.06 A

ATOM 593 C ASPA 83 47.084-19.694 38.216 1.0033.53 A ATOM 594 0 ASP A 83 48.151 -19.075 38.306 1.0032.73 A

ATOM 595 N GLU A 84 46.755-20.425 37.157 1.0033.17 A

ATOM 596 CA GLU A 84 47.620 -20.529 35.989 1.0032.63 A

ATOM 597 CB GLU A 84 48.028-21.981 35.754 1.0035.36 A

ATOM 598 CG GLU A 84 48.925-22.522 36.838 1.0039.82 A ATOM 599 CD GLU A 84 49.532-23.836 36.448 1.0042.75 A

ATOM 600 OE1 GLUA 84 50.117-23.908 35.340 1.0045.64 A

ATOM 601 OE2 GLU A 84 49.434-24.79437.245 1.0045.57 A

ATOM 602 C GLU A 84 46.910-19.986 34.755 1.0030.41 A

ATOM 603 O GLU A 84 45.684-19.822 34.745 1.0029.29 A ATOM 604 N ARG A 85 47.679-19.724 33.708 1.0030.64 A

ATOM 605 CA ARG A 85 47.111-19.171 32.484 1.0028.58 A

ATOM 606 CB ARG A 85 48.225-19.01531.439 1.0028.67 A

ATOM 607 CG ARG A 85 47.774-18.365 30.137 1.0027.63 A

ATOM 608 CD ARG A 85 48.977-17.96629.299 1.0028.41 A ATOM 609 NE ARG A 85 48.558-17.41028.019 1.0028.39 A

ATOM 610 CZ ARGA 85 47.925-18.11727.093 1.0028.68 A

ATOM 611 NH1ARGA 85 47.659-19.38927.311 1.0027.16 A

ATOM 612 NH2ARGA 85 47.544-17.549 25.964 1.0027.49 A

ATOM 613 C ARG A 85 45.953-20.00431.929 1.0027.39 A ATOM 614 O ARG A 85 44.926-19.468 31.522 1.0025.90 A

ATOM 615 N ALAA 86 46.113-21.318 31.905 1.0027.24 A

ATOM 616 CA ALAA 86 45.064-22.18531.385 1.0027.02 A

ATOM 617 CB ALAA 86 45.521 -23.631 31.413 1.0028.51 A

ATOM 618 C ALAA 86 43.751 -22.034 32.152 1.0027.35 A ATOM 619 O ALAA 86 42.656-22.120 31.574 1.0025.26 A

ATOM 620 N ASPA 87 43.852-21.811 33.460 1.0028.02 A

ATOM 621 CA ASPA 87 42.660-21.636 34.271 1.0026.98 A

ATOM 622 CB ASPA 87 43.036-21.583 35.746 1.0030.14 A

ATOM 623 CG ASPA 87 43.703-22.871 36.220 1.0032.77 A ATOM 624 OD1 ASP A 87 43.020-23.91236.237 1.0033.68 A

ATOM 625 OD2ASPA 87 44.903-22.836 36.554 1.0034.65 A

ATOM 626 C ASPA 87 41.967-20.345 33.864 1.0026.42 A

ATOM 627 O ASP A 87 40.740 -20.274 33.766 1.0024.39 A

ATOM 628 N SERA 88 42.765-19.319 33.611 1.0024.13 A ATOM 629 CA SERA 88 42.206-18.039 33.221 1.0022.11 A

ATOM 630 CB SERA 88 43.285-16.958 33.267 1.0020.60 A

ATOM 631 OG SERA 88 43.785-16.795 34.587 1.0022.43 A ATOM 632 C SERA 88 41.572-18.125 31.837 1.0019.85 A

ATOM 633 O SERA 88 40.532-17.521 31.590 1.0018.26 A

ATOM 634 N VAL A 89 42.185-18.873 30.931 1.0020.60 A

ATOM 635 CA VALA 89 41.593-18.99329.607 1.0020.90 A

ATOM 636 CB VALA 89 42.528-19.738 28.629 1.0022.14 A

ATOM 637 CG1 VAL A 89 41.826-19.951 27.305 1.0023.04 A

ATOM 638 CG2 VAL A 89 43.811 -18.926 28.454 1.0022.44 A

ATOM 639 C VAL A 89 40.252-19.711 29.705 1.0022.92 A

ATOM 640 O VALA 89 39.279-19.306 29.070 1.0023.26 A

ATOM 641 N LEU A 90 40.183-20.769 30.515 1.0024.29 A

ATOM 642 CA LEU A 90 38.922-21.509 30.691 1.0024.22 A

ATOM 643 CB LEU A 90 39.112-22.708 31.641 1.0026.68 A

ATOM 644 CG LEU A 90 39.373-24.077 31.006 1.0029.09 A

ATOM 645 CD1 LEU A 90 39.606-25.116 32.109 1.0029.18 A

ATOM 646 CD2 LEU A 90 38.197-24.494 30.153 1.0027.80 A

ATOM 647 C LEU A 90 37.816-20.622 31.231 1.0024.32 A

ATOM 648 O LEU A 90 36.681 -20.721 30.796 1.0023.54 A

ATOM 649 N ALAA 91 38.152-19.770 32.198 1.0022.19 A

ATOM 650 CA ALAA 91 37.189-18.860 32.792 1.0022.94 A

ATOM 651 CB ALAA 91 37.833-18.058 33.914 1.0022.32 A

ATOM 652 C ALAA 91 36.703-17.928 31.693 1.0022.09 A

ATOM 653 O ALAA 91 35.538-17.608 31.629 1.0022.86 A

ATOM 654 N GLYA 92 37.615-17.481 30.834 1.0021.50 A

ATOM 655 CA GLYA 92 37.200-16.620 29.743 1.0020.45 A

ATOM 656 C GLYA 92 36.310-17.37528.766 1.0021.11 A

ATOM 657 O GLYA 92 35.303-16.83428.315 1.0020.68 A

ATOM 658 N LEU A 93 36.664-18.621 28.439 1.0021.79 A

ATOM 659 CA LEU A 93 35.857-19.415 27.506 1.0024.32 A

ATOM 660 CB LEU A 93 36.518-20.772 27.238 1.0024.66 A

ATOM 661 CG LEU A 93 37.863-20.723 26.505 1.0027.53 A

ATOM 662 CD1 LEU A 93 38.431 -22.134 26.413 1.0028.96 A

ATOM 663 CD2 LEU A 93 37.676-20.157 25.086 1.0028.17 A

ATOM 664 C LEU A 93 34.423-19.61728.018 1.0026.57 A

ATOM 665 O LEU A 93 33.481 -19.72727.225 1.0027.96 A

ATOM 666 N LYS A 94 34.256-19.67429.341 1.0027.71 A

ATOM 667 CA LYS A 94 32.933-19.82029.949 1.0029.06 A

ATOM 668 CB LYS A 94 33.041 -19.993 31.475 1.0032.51 A

ATOM 669 CG LYS A 94 33.760-21.241 31.966 1.0036.19 A

ATOM 670 CD LYS A 94 32.776-22.303 32.449 1.0039.18 A

ATOM 671 CE LYS A 94 33.477-23.388 33.292 1.0040.84 A

ATOM 672 NZ LYS A 94 34.604-24.106 32.586 1.0041.60 A

ATOM 673 C LYS A 94 32.033-18.61829.672 1.0029.36 A

ATOM 674 O LYS A 94 30.820-18.75529.657 1.0029.33 A

ATOM 675 N ALAA 95 32.606-17.43729.455 1.0027.40 A

ATOM 676 CA ALAA 95 31.789-16.261 29.204 1.0028.45 A

ATOM 677 CB ALAA 95 32.259-15.09830.065 1.0031.33 A

ATOM 678 C ALAA 95 31.772-15.83427.745 1.0028.46 A

ATOM 679 O ALAA 95 31.276-14.75627.416 1.0028.85 A

ATOM 680 N ALAA 96 32.280-16.70426.880 1.0028.53 A

ATOM 681 CA ALAA 96 32.371 -16.43725.448 1.0029.07 A

ATOM 682 CB ALAA 96 33.356-17.411 24.811 1.0027.22 A

ATOM 683 C ALAA 96 31.065-16.47724.679 1.0029.41 A

ATOM 684 O ALAA 96 31.060-16.320 23.455 1.0030.31 A

ATOM 685 N GLYA 97 29.955-16.70925.369 1.0029.55 A

ATOM 686 CA GLYA 97 28.679-16.755 24.677 1.0029.21 A

ATOM 687 C GLYA 97 28.538-17.94023.737 1.0028.92 A

ATOM 688 O GLYA 97 29.065-19.01724.012 1.0029.22 A ATOM 689 N ASP A 98 27.846-17.74222.613 1.0027.73 A

ATOM 690 CA ASPA 98 27.635-18.823 21.650 1.0027.76 A

ATOM 691 CB ASPA 98 26.182-18.822 21.162 1.0031.55 A

ATOM 692 CG ASPA 98 25.708-17.45320.711 1.0035.48 A ATOM 693 OD1 ASP A 98 26.489-16.715 20.079 1.0036.29 A

ATOM 694 OD2 ASP A 98 24.533-17.111 20.981 1.0038.12 A

ATOM 695 C ASPA 98 28.580-18.771 20.449 1.0025.53 A

ATOM 696 0 ASPA 98 28.384-19.461 19.450 1.0024.06 A

ATOM 697 N ALAA 99 29.622-17.959 20.563 1.0024.35 A ATOM 698 CA ALAA 99 30.600-17.831 19.496 1.0023.88 A

ATOM 699 CB ALAA 99 31.789-17.020 19.992 1.0026.04 A

ATOM 700 C ALAA 99 31.084-19.199 19.027 1.0021.02 A

ATOM 701 O ALAA 99 31.442-20.046 19.833 1.0022.54 A

ATOM 702 N GLNA100 31.116-19.425 17.726 1.0019.11 A ATOM 703 CA GLN A 100 31.594-20.725 17.257 1.0018.49 A

ATOM 704 CB GLN A 100 31.113-20.987 15.833 1.0020.50 A

ATOM 705 CG GLN A 100 29.620-21.301 15.743 1.0025.56 A

ATOM 706 CD GLN A 100 29.106-21.210 14.329 1.0025.31 A

ATOM 707 OE1 GLN A 100 29.810-21.528 13.384 1.0028.35 A ATOM 708 NE2GLNA100 27.859-20.784 14.180 1.0029.57 A

ATOM 709 C GLN A 100 33.109-20.832 17.282 1.0016.63 A

ATOM 710 O GLN A 100 33.651 -21.933 17.426 1.0015.49 A

ATOM 711 N TRPA101 33.785-19.690 17.116 1.0015.31 A

ATOM 712 CA TRPA101 35.246-19.641 17. 00 1.0015.64 A ATOM 713 CB TRPA101 35.734-19.218 15.711 1.0014.31 A

ATOM 714 CG TRPA101 35.695-20.313 14.699 1.0016.23 A

ATOM 715 CD2TRPA101 36.808-21.089 14.262 1.0013.03 A

ATOM 716 CE2TRPA101 36.337-22.010 13.298 1.0015.27 A

ATOM 717 CE3TRPA101 38.168-21.089 14.586 1.0013.69 A ATOM 718 CD1 TRP A 101 34.603-20.784 14.005 1.0015.41 A

ATOM 719 NE1 TRPA101 34.987-21.802 13.161 1.0015.92 A

ATOM 720 CZ2 TRP A 101 37.190-22.932 12.671 1.0015.19 A

ATOM 721 CZ3 TRP A 101 39.012-21.995 13.956 1.0014.28 A

ATOM 722 CH2 TRP A 101 38.525-22.902 13.009 1.0014.21 A ATOM 723 C TRPA101 35.763-18.644 18.134 1.0015.17 A

ATOM 724 O TRP A 101 35.143-17.600 18.337 1.0013.62 A

ATOM 725 N VAL A 102 36.884-18.975 18.779 1.0013.64 A

ATOM 726 CA VAL A 102 37.470-18.094 19.787 1.0014.03 A

ATOM 727 CB VAL A 102 37.368-18.730 21.192 1.0015.13 A ATOM 728 CG1 VALA 102 38.107-20.046 21.218 1.0017.37 A

ATOM 729 CG2 VAL A 102 37.898-17.786 22.217 1.0018.27 A

ATOM 730 C VALA102 38.929-17.796 19.481 1.0014.11 A

ATOM 731 O VAL A 102 39.664-18.647 19.002 1.0011.94 A

ATOM 732 N LEU A 103 39.325-16.560 19.771 1.0013.71 A ATOM 733 CA LEU A 103 40.673-16.052 19.536 1.0016.36 A

ATOM 734 CB LEU A 103 40.551-14.701 18.847 1.0017.08 A

ATOM 735 CG LEU A 103 41.634-13.976 18.091 1.0022.42 A

ATOM 736 CD1 LEU A 103 42.073-14.827 16.888 1.0017.83 A

ATOM 737 CD2 LEU A 103 41.046-12.630 17.615 1.0018.34 A ATOM 738 C LEU A 103 41.280-15.83220.909 1.0015.87 A

ATOM 739 O LEU A 103 40.765-15.02421.650 1.0020.10 A

ATOM 740 N VAL A 104 42.358-16.526 21.266 1.0014.32 A

ATOM 741 CA VAL A 104 42.957-16.31522.586 1.0014.36 A

ATOM 742 CB VAL A 104 43.296-17.64523.287 1.0015.31 A ATOM 743 CG1 VAL A 104 43.832-17.344 24.687 1.0014.73 A

ATOM 744 CG2 VAL A 104 42.043-18.520 23.370 1.0016.32 A

ATOM 745 C VAL A 104 44.248-15.521 22.368 1.0013.00 A ATOM 746 O VAL A 104 45.111 -15.941 21.596 1.00 13.68 A

ATOM 747 N HIS A 105 44.378 -14.397 23.067 1.00 12.73 A

ATOM 748 CA HIS A 105 45.524 -13.519 22.895 1.00 13.25 A

ATOM 749 CB HIS A 105 45.103 -12.289 22.064 1.00 13.67 A

ATOM 750 CG HIS A 105 46.268 -11.465 21.615 1.00 15.84 A

ATOM 751 CD2 HIS A 105 47.421 -11.844 21.024 1.00 12.69 A

ATOM 752 ND1 HIS A 105 46.380 -10.110 21.847 1.00 19.95 A

ATOM 753 CE1 HIS A 105 47.562 -9.693 21.420 1.00 14.81 A

ATOM 754 NE2 HIS A 105 48.213 -10.729 20.919 1.00 18.87 A

ATOM 755 C HIS A 105 46.108 -13.027 24.208 1.00 13.77 A

ATOM 756 O HIS A 105 45.380 -12.535 25.059 1.00 15.58 A

ATOM 757 N ASP A 106 47.430 -13.126 24.353 1.00 15.17 A

ATOM 758 CA ASP A 106 48.090 -12.661 25.580 1.00 18.01 A

ATOM 759 CB ASP A 106 49.577 -12.972 25.559 1.00 21.72 A

ATOM 760 CG ASP A 106 49.873 -14.410 25.862 1.00 27.57 A

ATOM 761 OD1 ASP A 106 49.010 -15.097 26.445 1.00 28.66 A

ATOM 762 OD2 ASP A 106 50.990 -14.823 25.521 1.00 31.37 A

ATOM 763 C ASP A 106 47.960 -11.161 25.787 1.00 17.91 A

ATOM 764 O ASP A 106 48.175 -10.391 24.870 1.00 17.99 A

ATOM 765 N ALA A 107 47.607 -10.735 26.982 1.00 18.20 A

ATOM 766 CA ALA A 107 47.506 -9.308 27.242 1.00 17.03 A

ATOM 767 CB ALA A 107 47.062 -9.065 28.699 1.00 21.46 A

ATOM 768 C ALA A 107 48.892 -8.657 27.006 1.00 19.42 A

ATOM 769 O ALA A 107 48.972 -7.490 26.626 1.00 23.53 A

ATOM 770 N ALA A 108 49.962 -9.430 27.182 1.00 18.19 A

ATOM 771 CA ALA A 108 51.317 -8.918 27.070 1.00 19.32 A

ATOM 772 CB ALA A 108 52.226 -9.721 27.994 1.00 22.61 A

ATOM 773 C ALA A 108 51.935 -8.840 25.685 1.00 20.72 A

ATOM 774 O ALA A 108 53.166 -8.647 25.563 1.00 20.01 A

ATOM 775 N ARG A 109 51.119 -9.015 24.644 1.00 18.60 A

ATOM 776 CA ARG A 109 51.609 -8.931 23.264 1.00 19.61 A

ATOM 777 CB ARG A 109 51.315 -10.236 22.532 1.00 18.96 A

ATOM 778 CG ARG A 109 52.288 -11.344 22.860 1.00 18.85 A

ATOM 779 CD ARG A 109 51.911 -12.627 22.120 1.00 22.53 A

ATOM 780 NE ARG A 109 52.712 -13.773 22.552 1.00 25.67 A

ATOM 781 CZ ARG A 109 53.972 -14.006 22.189 1.00 25.25 A

ATOM 782 NH1 ARG A 109 54.606 -13.181 21.370 1.00 28.44 A

ATOM 783 NH2 ARG A 109 54.614 -15.078 22.646 1.00 28.17 A

ATOM 784 C ARG A 109 50.879 -7.763 22.603 1.00 19.28 A

ATOM 785 O ARG A 109 49.928 -7.957 21.825 1.00 21.88 A

ATOM 786 N PRO A 1 10 51.348 -6.533 22.867 1.00 17.30 A

ATOM 787 CD PRO A 110 52.555 -6.170 23.635 1.00 19.28 A

ATOM 788 CA PRO A 110 50.717 -5.336 22.319 1.00 16.05 A

ATOM 789 CB PRO A 110 51.176 -4.257 23.280 1.00 18.08 A

ATOM 790 CG PRO A 110 52.635 -4.631 23.462 1.00 18.84 A

ATOM 791 C PRO A 110 51.055 -4.951 20.899 1.00 16.91 A

ATOM 792 O PRO A 110 50.436 -4.024 20.372 1.00 18.13 A

ATOM 793 N CYS A 111 51.976 -5.671 20.272 1.00 14.89 A

ATOM 794 CA CYS A 111 52.440 -5.300 18.946 1.00 16.65 A

ATOM 795 CB CYS A 111 53.960 -5.494 18.872 1.00 18.20 A

ATOM 796 SG CYS A 111 54.803 -4.496 20.100 1.00 21.59 A

ATOM 797 C CYS A 111 51.777 -5.994 17.786 1.00 17.24 A

ATOM 798 O CYS A 111 52.241 -5.871 16.655 1.00 19.05 A

ATOM 799 N LEU A 112 50.675 -6.701 18.041 1.00 15.71 A

ATOM 800 CA LEU A 112 49.954 -7.402 16.967 1.00 16.48 A

ATOM 801 CB LEU A 112 48.709 -8.088 17.545 1.00 13.99 A

ATOM 802 CG LEU A 112 47.816 -8.897 16.601 1.00 16.31 A ATOM 803 CD1 LEU A 112 48.581 -10.078 16.004 1.0016.00 A

ATOM 804 CD2LEUA112 46.590 -9.401 17.400 1.0016.60 A

ATOM 805 C LEU A 112 49.513 -6.532 15.794 1.0015.46 A

ATOM 806 O LEU A 112 48.894 -5.495 15.982 1.0016.88 A

ATOM 807 N HISA113 49.817 -6.988 14.585 1.0016.60 A

ATOM 808 CA HIS A 113 49.437 -6.287 13.364 1.0019.95 A

ATOM 809 CB HISA 113 50.538 -6.392 12.321 1.0019.94 A

ATOM 810 CG HIS A 113 51.686 -5.468 12.569 1.0028.23 A

ATOM 811 CD2HISA113 52.271 -5.063 13.716 1.0029.35 A

ATOM 812 ND1 HISA113 52.369 -4.846 11.545 1.0029.63 A

ATOM 813 CE1 HIS A 113 53.326 -4.095 12.058 1.0031.75 A

ATOM 814 NE2HISA113 53.289 -4.208 13.374 1.0031.40 A

ATOM 815 C HIS A 113 48.146 -6.822 12.748 1.0018.44 A

ATOM 816 O HISA113 47.831 -8.000 12.833 1.0017.33 A

ATOM 817 N GLNA114 47.402 -5.940 12.096 1.0018.12 A

ATOM 818 CA GLN A 114 46.157 -6.351 11.485 1.0017.59 A

ATOM 819 CB GLN A 114 45.380 -5.133 10.958 1.0016.61 A

ATOM 820 CG GLN A 114 44.918 -4.179 12.061 1.0016.97 A

ATOM 821 CD GLN A 114 44.030 -4.891 13.059 1.0018.29 A

ATOM 822 OE1 GLN A 114 42.947 -5.372 12.709 1.0019.05 A

ATOM 823 NE2GLNA114 44.502 -4.991 14.309 1.0015.72 A

ATOM 824 C GLN A 114 46.277 -7.366 10.370 1.0017.30 A

ATOM 825 O GLN A 114 45.386 -8.200 10.179 1.0019.13 A

ATOM 826 N ASP A 115 47.351 -7.312 9.594 1.0018.29 A

ATOM 827 CA ASP A 115 47.466 -8.274 8.510 1.0019.16 A

ATOM 828 CB ASPA 115 48.629 -7.892 7.572 1.0023.11 A

ATOM 829 CG ASP A 115 49.967 -7.852 8.278 1.0030.27 A

ATOM 830 OD1 ASP A 115 50.039 -7.318 9.409 1.0032.83 A

ATOM 831 OD2ASPA115 50.961 -8.339 7.690 1.0036.96 A

ATOM 832 C ASPA 115 47.612 -9.701 9.053 1.0017.53 A

ATOM 833 O ASP A 115 46.986-10.643 8.543 1.0018.94 A

ATOM 834 N ASP A 116 48.411 -9.871 10.104 1.0016.45 A

ATOM 835 CA ASP A 116 48.579-11.202 10.729 1.0015.17 A

ATOM 836 CB ASPA 116 49.610-11.162 11.884 1.0014.46 A

ATOM 837 CG ASPA 116 51.054-11.109 11.411 1.0018.54 A

ATOM 838 OD1 ASP A 116 51.331 -11.283 10.194 1.0019.68 A

ATOM 839 OD2ASPA116 51.924-10.897 12.284 1.0019.69 A

ATOM 840 C ASP A 116 47.239-11.671 11.315 1.0013.56 A

ATOM 841 O ASP A 116 46.831 -12.828 11.144 1.0013.81 A

ATOM 842 N LEU A 117 46.555-10.765 12.007 1.0013.13 A

ATOM 843 CA LEU A 117 45.282-11.106 12.631 1.0012.99 A

ATOM 844 CB LEU A 117 44.709 -9.918 13.399 1.0014.37 A

ATOM 845 CG LEU A 117 43.334-10.159 14.026 1.0014.86 A

ATOM 846 CD1 LEU A 117 43.388-11.441 14.887 1.0016.99 A

ATOM 847 CD2LEUA117 42.920 -8.951 14.904 1.0016.37 A

ATOM 848 C LEU A 117 44.298-11.574 11.575 1.0013.28 A

ATOM 849 O LEU A 117 43.629-12.606 11.728 1.0013.19 A

ATOM 850 N ALA A 118 44.223-10.847 10.457 1.0014.50 A

ATOM 851 CA ALAA 118 43.297-11.228 9.392 1.0014.59 A

ATOM 852 CB ALAA 118 43.243-10.114 8.325 1.0014.44 A

ATOM 853 C ALAA 118 43.631-12.566 8.745 1.0015.13 A '

ATOM 854 O ALAA 118 42.724-13.314 8.405 1.0016.65 A

ATOM 855 N ARG A 119 44.921-12.876 8.582 1.0015.00 A

ATOM 856 CA ARG A 119 45.301 -14.145 7.979 1.0015.50 A

ATOM 857 CB ARG A 119 46.775-14.122 7.623 1.0015.31 A

ATOM 858 CG ARG A 119 46.982-13.277 6.349 1.0019.88 A

ATOM 859 CD ARG A 119 48.438-13.062 5.960 1.0021.65 A ATOM 860 NE ARG A 119 49.198-14.273 6.139 1.0024.65 A

ATOM 861 CZ ARG A 119 50.129-14.432 7.067 1.0025.09 A

ATOM 862 NH1 ARG A 119 50.433-13.433 7.894 1.0022.58 A

ATOM 863 NH2ARGA119 50.714-15.615 7.191 1.0025.34 A

ATOM 864 C ARG A 119 44.976-15.283 8.940 1.0015.31 A

ATOM 865 O ARG A 119 44.605-16.368 8.511 1.0016.31 A

ATOM 866 N LEU A 120 45.114-15.020 10.240 1.0015.11 A

ATOM 867 CA LEU A 120 44.791 -16.045 11.228 1.0014.94 A

ATOM 868 CB LEU A 120 45.170-15.573 12.638 1.0013.19 A

ATOM 869 CG LEU A 120 44.849-16.629 13.709 1.0013.92 A

ATOM 870 CD1 LEU A 120 45.621 -17.909 13.444 1.0015.86 A

ATOM 871 CD2LEUA120 45.167-16.060 15.088 1.0013.77 A

ATOM 872 C LEU A 120 43.291 -16.362 11.188 1.0014.09 A

ATOM 873 O LEU A 120 42.886-17.538 11.206 1.0014.24 A

ATOM 874 N LEU A 121 42.452-15.322 11.132 1.0014.24 A

ATOM 875 CA LEU A 121 41.001 -15.521 11.098 1.0015.32 A

ATOM 876 CB LEU A 121 40.282-14.175 11.179 1.0015.34 A

ATOM 877 CG LEU A 121 40.518-13.499 12.516 1.0017.74 A

ATOM 878 CD1 LEU A 121 39.767-12.176 12.606 1.0020.95 A

ATOM 879 CD2LEUA121 40.085-14.457 13.605 1.0022.13 A

ATOM 880 C LEU A 121 40.512-16.280 9.864 1.0014.44 A

ATOM 881 O LEU A 121 39.446-16.911 9.887 1.0014.00 A

ATOM 882 N ALAA 122 41.247-16.197 8.774 1.0017.61 A

ATOM 883 CA ALAA 122 40.831 -16.918 7.578 1.0018.71 A

ATOM 884 CB ALAA 122 41.763-16.576 6.408 1.0019.05 A

ATOM 885 C ALAA 122 40.772-18.433 7.805 1.0019.32 A

ATOM 886 O ALAA 122 40.137-19.150 7.044 1.0018.19 A

ATOM 887 N LEU A 123 41.423-18.931 8.863 1.0017.64 A

ATOM 888 CA LEU A 123 41.402-20.356 9.146 1.0017.24 A

ATOM 889 CB LEU A 123 42.220-20.688 10.390 1.0018.69 A

ATOM 890 CG LEU A 123 43.737-20.593 10.212 1.0017.82 A

ATOM 891 CD1 LEU A 123 44.389-20.942 11.551 1.0020.65 A

ATOM 892 CD2LEUA123 44.227-21.539 9.099 1.0019.95 A

ATOM 893 C LEU A 123 40.006-20.922 9.353 1.0017.87 A

ATOM 894 O LEU A 123 39.770-22.116 9.105 1.0020.15 A

ATOM 895 N SERA 124 39.064-20.092 9.793 1.0016.28 A

ATOM 896 CA SER A 124 37.729-20.638 10.020 1.0018.28 A

ATOM 897 CB SER A 124 36.874-19.633 10.797 1.0016.16 A

ATOM 898 OG SER A 124 36.601-18.466 10.060 1.0018.89 A

ATOM 899 C SERA 124 37.031 -21.072 8.731 1.0020.71 A

ATOM 900 O SER A 124 36.046-21.812 8.777 1.0022.36 A

ATOM 901 N GLU A 125 37.545-20.628 7.590 1.0023.42 A

ATOM 902 CA GLU A 125 36.937-20.984 6.314 1.0027.79 A

ATOM 903 CB GLU A 125 36.971 -19.768 5.372 1.0031.02 A

ATOM 904 CG GLU A 125 35.635-19.042 5.164 1.0036.90 A

ATOM 905 CD GLU A 125 34.712-19.047 6.388 1.0039.97 A

ATOM 906 OE1 GLU A 125 35.121 -18.643 7.512 1.0039.39 A

ATOM 907 OE2GLUA125 33.547-19.461 6.216 1.0041.50 A

ATOM 908 C GLU A 125 37.643-22.173 5.667 1.0031.06 A

ATOM 909 O GLU A 125 37.181 -22.709 4.651 1.0032.43 A

ATOM 910 N THR A 126 38.748-22.607 6.263 1.0031.62 A

ATOM 911 CA THR A 126 39.520-23.696 5.676 1.0033.91 A

ATOM 912 CB THR A 126 40.740-23.140 4.958 1.0035.03 A

ATOM 913 OG1 THR A 126 41.408-24.203 4.276 1.0039.67 A

ATOM 914 CG2THRA126 41.712-22.516 5.971 1.0034.52 A

ATOM 915 C THR A 126 40.027-24.764 6.637 1.0033.01 A

ATOM 916 O THR A 126 40.761 -25.658 6.218 1.0035.04 A ATOM 917 N SERA 127 39.649-24.675 7.911 1.0030.59 A

ATOM 918 CA SER A 127 40.101-25.634 8.919 1.0029.20 A

ATOM 919 CB SER A 127 41.304-25.058 9.681 1.0030.71 A

ATOM 920 OG SER A 127 41.598-25.827 10.845 1.0030.55 A

ATOM 921 C SERA 127 39.022-25.981 9.933 1.0029.41 A

ATOM 922 O SER A 127 38.142-25.172 10.197 1.0029.20 A

ATOM 923 N ARG A 128 39.086 -27182 10.499 1.0029.24 A

ATOM 924 CA ARG A 128 38.131-27.562 11.530 1.0030.11 A

ATOM 925 CB ARG A 128 37.421-28.879 11.211 1.0033.02 A

ATOM 926 CG ARG A 128 36.149-28.704 10.402 1.0035.30 A

ATOM 927 CD ARG A 128 35.557-30.049 10.047 1.0037.21 A

ATOM 928 NE ARG A 128 34.675-29.961 8.894 1.0037.57 A

ATOM 929 CZ ARG A 128 33.470-29.404 8.912 1.0037.49 A

ATOM 930 NH1 ARGA128 33.001 -28.879 10.039 1.0036.16 A

ATOM 931 NH2ARGA128 32.727-29.388 7.806 1.0036.56 A

ATOM 932 C ARG A 128 38.872-27.700 12.837 1.0029.93 A

ATOM 933 O ARG A 128 38.287-28.050 13.861 1.0030.50 A

ATOM 934 N THR A 129 40.175-27.426 12.805 1.0028.24 A

ATOM 935 CA THR A 129 40.988-27.527 14.013 1.0027.39 A

ATOM 936 CB THR A 129 42.241-28.414 13.777 1.0029.11 A

ATOM 937 OG1 THR A 129 41.816-29.723 13.375 1.0031.63 A

ATOM 938 CG2THRA129 43.077-28.531 15.059 1.0030.87 A

ATOM 939 C THR A 129 41.438-26.153 14.484 1.0025.89 A

ATOM 940 O THR A 129 41.483-25.896 15.670 1.0026.66 A

ATOM 941 N GLY A 130 41.748-25.269 13.549 1.0021.52 A

ATOM 942 CA GLYA 130 42.215-23.960 13.952 1.0020.18 A

ATOM 943 C GLYA 130 43.721 -23.865 13.820 1.0017.98 A

ATOM 944 O GLY A 130 44.350-24.687 13.153 1.0020.03 A

ATOM 945 N GLY A 131 44.303-22.852 14.450 1.0015.56 A

ATOM 946 CA GLYA 131 45.743-22.682 14.363 1.0014.28 A

ATOM 947 C GLY A 131 46.252-21.488 15.150 1.0014.43 A

ATOM 948 O GLY A 131 45.526-20.889 15.917 1.0014.30 A

ATOM 949 N ILE A 132 47.512-21.136 14.919 1.0014.15 A

ATOM 950 CA ILE A 132 48.178-20.068 15.653 1.0015.03 A

ATOM 951 CB ILE A 132 49.083-20.648 16.791 1.0015.19 A

ATOM 952 CG2ILEA132 48.251 -21.573 17.675 1.0016.70 A

ATOM 953 CG1 ILEA 132 50.275-21.412 16.215 1.0014.76 A

ATOM 954 CD1 ILEA 132 51.306-21.832 17.277 1.0016.71 A

ATOM 955 C ILE A 132 49.102-19.249 14.779 1.0014.47 A

ATOM 956 O ILE A 132 49.509-19.694 13.693 1.0014.56 A

ATOM 957 N LEU A 133 49.401-18.029 15.231 1.0013.78 A

ATOM 958 CA LEU A 133 50.409-17.229 14.540 1.0013.97 A

ATOM 959 CB LEU A 133 50.306-15.748 14.917 1.0015.26 A

ATOM 960 CG LEU A 133 49.157-14.976 14.267 1.0016.40 A

ATOM 961 CD1 LEU A 133 49.173-13.543 14.788 1.0017.99 A

ATOM 962 CD2LEUA133 49.319-15.013 12.747 1.0019.04 A

ATOM 963 C LEU A 133 51.723-17.812 15.084 1.0015.68 A

ATOM 964 O LEU A 133 51.838-18.153 16.274 1.0013.89 A

ATOM 965 N ALAA 134 52.702-17.894 14.205 1.0014.52 A

ATOM 966 CA ALA A 134 53.999-18.432 14.575 1.0014.76 A

ATOM 967 CB ALA A 134 53.989-19.952 14.437 1.0014.84 A

ATOM 968 C ALAA 134 55.074-17.828 13.691 1.0016.49 A

ATOM 969 O ALAA 134 54.796-17.424 12.551 1.0017.53 A

ATOM 970 N ALAA 135 56.302-17.726 14.207 1.0016.59 A

ATOM 971 CA ALAA 135 57.391 -17.164 13.407 1.0018.51 A

ATOM 972 CB ALA A 135 57.960-15.927 14.084 1.0018.92 A

ATOM 973 C- ALAA 135 58.447-18.241 13.262 1.0018.74 A ATOM 974 O ALAA 135 58.768-18.942 14.231 1.0017.60 A

ATOM 975 N PRO A 136 58.986-18.401 12.043 1.0021.29 A

ATOM 976 CD PRO A 136 58.640-17.711 10.791 1.0022.92 A

ATOM 977 CA PRO A 136 60.004-19.421 11.814 1.0021.33 A

ATOM 978 CB PRO A 136 60.267-19.336 10.311 1.0022.92 A

ATOM 979 CG PRO A 136 59.053-18.736 9.747 1.0025.51 A

ATOM 980 C PRO A 136 61.272-19.172 12.605 1.0021.46 A

ATOM 981 O PRO A 136 61.688-18.033 12.815 1.0022.13 A

ATOM 982 N VAL A 137 61.911-20.244 13.035 1.0022.32 A

ATOM 983 CA VAL A 137 63.164-20.091 13.752 1.0024.03 A

ATOM 984 CB VAL A 137 63.581 -21.399 14.401 1.0024.30 A

ATOM 985 CG1 VAL A 137 65.031-21.284 14.890 1.0024.89 A

ATOM 986 CG2VALA137 62.657-21.694 15.574 1.0023.94 A

ATOM 987 C VAL A 137 64.250-19.654 12.779 1.0024.59 A

ATOM 988 O VAL A 137 64.377-20.211 11.685 1.0024.89 A

ATOM 989 N ARG A 138 65.025-18.651 13.188 1.0026.49 A

ATOM 990 CA ARG A 138 66.116-18.117 12.377 1.0028.95 A

ATOM 991 CB ARG A 138 66.065-16.584 12.356 1.0031.56 A

ATOM 992 CG ARG A 138 64.767-15.997 11.824 1.0033.59 A

ATOM 993 CD ARG A 138 64.388-16.611 10.483 1.0036.03 A

ATOM 994 NE ARG A 138 63.269-15.910 9.847 1.0039.10 A

ATOM 995 CZ ARG A 138 62.707-16.293 8.704 1.0039.60 A

ATOM 996 NH1 ARG A 138 63.155-17.376 8.079 1.0040.83 A

ATOM 997 NH2ARGA138 61.712-15.590 8.176 1.0039.74 A

ATOM 998 C ARG A 138 67.500-18.549 12.879 1.0028.27 A

ATOM 999 O ARG A 138 68.356-18.904 12.087 1.0030.47 A

ATOM 1000 N ASP A 139 67.735-18.516 14.186 1.0028.91 A

ATOM 1001 CA ASP A 139 69.057-18.894 14.694 1.0027.49 A

ATOM 1002 CB ASP A 139 69.236-18.414 16.142 1.0031.28 A

ATOM 1003 CG ASP A 139 69.529-16.918 16.243 1.0035.12 A

ATOM 1004 OD1 ASP A 139 70.384-16.421 15.479 1.0035.84 A

ATOM 1005 OD2ASPA139 68.921-16.253 17.108 1.0036.04 A

ATOM 1006 C ASP A 139 69.343-20.400 14.663 1.0024.95 A

ATOM 1007 O ASP A 139 68.430-21.219 14.640 1.0024.43 A

ATOM 1008 N THR A 140 70.618-20.763 14.648 1.0022.15 A

ATOM 1009 CA THR A 140 70.996-22.156 14.744 1.0021.63 A

ATOM 1010 CB THR A 140 72.501-22.329 14.454 1.0019.03 A

ATOM 1011 OG1 THR A 140 72.722-22.157 13.042 1.0022.95 A

ATOM 1012 CG2THRA140 72.974-23.697 14.882 1.0021.28 A

ATOM 1013 C THR A 140 70.652-22.461 16.209 1.0020.48 A

ATOM 1014 O THR A 140 70.922-21.651 17.089 1.0022.89 A

ATOM 1015 N MET A 141 70.004-23.588 16.474 1.0020.63 A

ATOM 1016 CA MET A 141 69.619-23.944 17.830 1.0018.91 A

ATOM 1017 CB MET A 141 68.129-24.298 17.882 1.0021.88 A

ATOM 1018 CG MET A 141 67.232-23.284 17.243 1.0022.65 A

ATOM 1019 SD MET A 141 67.311-21.705 18.151 1.0019.81 A

ATOM 1020 CE MET A 141 65.446-21.341 18.409 1.0029.38 A

ATOM 1021 C MET A 141 70.422-25.104 18.373 1.0020.58 A

ATOM 1022 O MET A 141 70.755-26.046 17.639 1.0020.90 A

ATOM 1023 N LYS A 142 70.751-25.013 19.658 1.0018.27 A

ATOM 1024 CA LYS A 142 71.527-26.043 20.334 1.0019.93 A

ATOM 1025 CB LYS A 142 72.808-25.459 20.954 1.0019.53 A

ATOM 1026 CG LYS A 142 73.695-24.690 19.993 1.0017.98 A

ATOM 1027 CD LYS A 142 74.232-25.573 18.867 1.0018.48 A

ATOM 1028 CE LYS A 142 75.202-24.816 17.988 1.0017.34 A

ATOM 1029 NZ LYS A 142 75.826-25.675 16.952 1.0019.58 A

ATOM 1030 C LYS A 142 70.737-26.656 21.472 1.0021.18 A ATOM 1031 O LYS A 142 70.035-25.96322.200 1.0021.57 A

ATOM 1032 N ARG A 143 70.867-27.96421.615 1.0022.95 A

ATOM 1033 CA ARG A 143 70.251 -28.67722.715 1.0023.82 A

ATOM 1034 CB ARG A 143 69.668-30.00522.230 1.0026.85 A

ATOM 1035 CG ARG A 143 69.123-30.90623.330 1.0029.45 A

ATOM 1036 CD ARG A 143 67.619-30.95623.259 1.0033.88 A

ATOM 1037 NE ARG A 143 67.006-30.009 24.166 1.0035.29 A

ATOM 1038 CZ ARG A 143 65.802-29.46823.990 1.0031.12 A

ATOM 1039 NH1 ARG A 143 65.054 -29.76422.928 1.0030.99 A

ATOM 1040 NH2ARGA143 65.351-28.628 24.891 1.0032.03 A

ATOM 1041 C ARG A 143 71.402-28.92923.677 1.0024.39 A

ATOM 1042 O ARG A 143 72.472-29.391 23.258 1.0024.74 A

ATOM 1043 N ALAA 144 71.191 -28.62324.954 1.0024.49 A

ATOM 1044 CA ALAA 144 72.222-28.80225.972 1.0026.27 A

ATOM 1045 CB ALAA 144 72.018-27.80627.102 1.0026.21 A

ATOM 1046 C ALA A 144 72.159-30.19826.533 1.0028.36 A

ATOM 1047 O ALAA 144 71.119-30.85526.467 1.0028.32 A

ATOM 1048 N GLU A 145 73.279-30.65627.082 1.0029.88 A

ATOM 1049 CA GLU A 145 73.302-31.96527.702 1.0032.20 A

ATOM 1050 CB GLU A 145 74.735-32.43627.944 1.0033.38 A

ATOM 1051 CG GLU A 145 75.478 -32.68626.656 1.0036.34 A

ATOM 1052 CD GLU A 145 76.847-33.29326.860 1.0040.24 A

ATOM 1053 OE1 GLU A 145 77.616-32.78427.701 1.0041.95 A

ATOM 1054 OE2GLUA145 77.162-34.27826.165 1.0042.63 A

ATOM 1055 C GLU A 145 72.566-31.811 29.021 1.0032.59 A

ATOM 1056 O GLU A 145 72.650-30.77329.679 1.0031.56 A

ATOM 1057 N PRO A 146 71.807-32.84029.412 1.0033.23 A

ATOM 1058 CD PRO A 146 71.654-34.11228.686 1.0034.06 A

ATOM 1059 CA PRO A 146 71.033-32.84330.653 1.0034.96 A

ATOM 1060 CB PRO A 146 70.656-34.31730.812 1.0034.85 A

ATOM 1061 CG PRO A 146 70.481 -34.761 29.402 1.0034.53 A

ATOM 1062 C PRO A 146 71.768-32.28831.877 1.0035.35 A

ATOM 1063 O PRO A 146 72.800-32.81332.288 1.0037.03 A

ATOM 1064 N GLYA 147 71.225-31.21232.435 1.0036.02 A

ATOM 1065 CA GLYA 147 71.790-30.59833.622 1.0036.61 A

ATOM 1066 C GLY A 147 73.090-29.831 33.491 1.0037.30 A

ATOM 1067 O GLY A 147 73.556 -29.25734.475 1.0038.20 A

ATOM 1068 N LYS A 148 73.674-29.803 32.296 1.0035.74 A

ATOM 1069 CA LYS A 148 74.933 -29.09732.087 1.0036.67 A

ATOM 1070 CB LYS A 148 76.045-30.09631.782 1.0037.18 A

ATOM 1071 CG LYS A 148 76.436-30.93632.977 1.0040.35 A

ATOM 1072 CD LYS A 148 77.755-31.65432.751 1.0041.13 A

ATOM 1073 CE LYS A 148 78.857-30.708 32.253 1.0043.39 A

ATOM 1074 NZ LYS A 148 78.878-30.57530.757 1.0044.66 A

ATOM 1075 C LYS A 148 74.856-28.08230.961 1.0035.85 A

ATOM 1076 O LYS A 148 74.061 -28.236 30.037 1.0036.15 A

ATOM 1077 N ASN A 149 75.696-27.051 31.029 1.0035.99 A

ATOM 1078 CA ASN A 149 75.702-26.02929.985 1.0034.60 A

ATOM 1079 CB ASN A 149 75.993-24.65230.601 1.0036.41 A

ATOM 1080 CG ASN A 149 74.795-24.094 31.375 1.0038.46 A

ATOM 1081 OD1 ASN A 149 74.941-23.572 32.479 1.0040.11 A

ATOM 1082 ND2ASN A 149 73.601 -24.201 30.785 1.0037.85 A

ATOM 1083 C ASN A 149 76.694-26.35228.869 1.0032.98 A

ATOM 1084 O ASN A 149 77.489-25.51228.466 1.0032.18 A

ATOM 1085 N ALAA 150 76.636-27.58628.383 1.0032.00 A

ATOM 1086 CA ALAA 150 77.488-28.05327.298 1.0029.93 A

ATOM 1087 CB ALAA 150 78.337-29.211 27.763 1.0031.12 A ATOM 1088 C ALAA 150 76.559-28.50626.176 1.0028.65 A

ATOM 1089 O ALAA 150 75.491 -29.056 26.438 1.0026.31 A

ATOM 1090 N ILE A 151 76.949-28.261 24.929 1.0025.44 A

ATOM 1091 CA ILE A 151 76.125-28.649 23.790 1.0024.98 A

ATOM 1092 CB ILE A 151 76.640-28.000 22.492 1.0024.68 A

ATOM 1093 CG2 ILEA 151 75.865-28.536 21.300 1.0024.20 A

ATOM 1094 CG1 ILEA 151 76.486-26.481 22.582 1.0025.06 A

ATOM 1095 CD1 ILE A 151 77.161 -25.721 21.433 1.0024.42 A

ATOM 1096 C ILE A 151 76.064-30.150 23.548 1.0025.48 A

ATOM 1097 O ILE A 151 77.092-30.795 23.426 1.0023.92 A

ATOM 1098 N ALAA 152 74.857 -30.70423.481 1.0024.21 A

ATOM 1099 CA ALA A 152 74.689-32.12023.181 1.0026.01 A

ATOM 1100 CB ALA A 152 73.347-32.611 23.687 1.0026.00 A

ATOM 1101 C ALAA 152 74.740-32.228 21.665 1.0025.71 A

ATOM 1102 O ALAA 152 75.495-33.01421.112 1.0026.57 A

ATOM 1103 N HIS A 153 73.922-31.433 20.983 1.0025.10 A

ATOM 1104 CA HIS A 153 73.907-31.445 19.527 1.0024.64 A

ATOM 1105 CB HIS A 153 73.260-32.737 19.001 1.0026,68 A

ATOM 1106 CG HIS A 153 71.838-32.907 19.433 1.0028.74 A

ATOM 1107 CD2 HISA 153 70.686-32.425 18.909 1.0030.39 A

ATOM 1108 ND1 HISA 153 71.482-33.586 20.580 1.0030.13 A

ATOM 1109 CE1 HIS A 153 70.172-33.51020.744 1.0031.06 A

ATOM 1110 NE2HISA153 69.666-32.809 19.744 1.0030.80 A

ATOM 1111 C HIS A 153 73.101 -30.249 19.036 1.0022.38 A

ATOM 1112 O HIS A 153 72.482-29.545 19.830 1.0023.29 A

ATOM 1113 N THR A 154 73.143-30.016 17.736 1.0021.21 A

ATOM 1114 CA THR A 154 72.397-28.928 17.118 1.0023.03 A

ATOM 1115 CB THR A 154 73.072-28.459 15.821 1.0024.28 A

ATOM 1116 OG1 THR A 154 74.327-27.844 16.139 1.0023.30 A

ATOM 1117 CG2THRA154 72.219-27.446 15.096 1.0024.75 A

ATOM 1118 C THR A 154 71.011-29.465 16.781 1.0024.02 A

ATOM 1119 O THR A 154 70.881 -30.589 16.296 1.0025.55 A

ATOM 1120 N VAL A 155 69.983-28.668 17.050 1.0022.12 A

ATOM 1121 CA VAL A 155 68.601 -29.062 16.752 1.0024.49 A

ATOM 1122 CB VAL A 155 67.642-28.516 17.853 1.0024.92 A

ATOM 1123 CG1 VAL A 155 66.177-28.780 17.472 1.0025.18 A

ATOM 1124 CG2VALA155 67.950-29.189 19.186 1.0025.03 A

ATOM 1125 C VALA 155 68.210-28.488 15.380 1.0025.30 A

ATOM 1126 O VAL A 155 68.313-27.288 15.167 1.0026.20 A

ATOM 1127 N ASP A 156 67.773-29.350 14.459 1.0025.66 A

ATOM 1128 CA ASP A 156 67.375-28.931 13.110 1.0027.01 A

ATOM 1129 CB ASP A 156 66.771-30.112 12.344 1.0029.76 A

ATOM 1130 CG ASP A 156 66.616-29.840 10.844 1.0033.42 A

ATOM 1131 OD1 ASP A 156 66.601-28.671 10.415 1.0033.74 A

ATOM 1132 OD2ASPA156 66.503-30.822 10.091 1.0037.18 A

ATOM 1133 C ASP A 156 66.312-27.848 13.237 1.0026.63 A

ATOM 1134 O ASP A 156 65.240-28.107 13.794 1.0024.84 A

ATOM 1135 N ARG A 157 66.587-26.655 12.716 1.0026.74 A

ATOM 1136 CA ARG A 157 65.615-25.569 12.805 1.0028.26 A

ATOM 1137 CB ARG A 157 66.326 -24.214 12.857 1.0029.24 A

ATOM 1138 CG ARG A 157 66.907 -23.721 11.541 1.0031.76 A

ATOM 1139 CD ARG A 157 67.639 -22.400 11.754 1.0033.25 A

ATOM 1140 NE ARG A 157 68.343-21.955 10.562 1.0033.91 A

ATOM 1141 CZ ARG A 157 67.753-21.491 9.467 1.0037.71 A

ATOM 1142 NH1 ARG A 157 66.426-21.399 9.408 1.0037.76 A

ATOM 1143 NH2ARGA157 68.491 -21.138 8.417 1.0038.65 A

ATOM 1144 C ARG A 157 64.606-25.576 11.665 1.0029.90 A ATOM 1145 O ARG A 157 63.664-24.775 11.658 1.0027.95 A

ATOM ^'1146 N ASN A 158 64.796-26.475 10.710 1.0029.32 A

ATOM 1147 CA ASN A158 63.889-26.594 9.578 1.0031.14 A

ATOM 1148 CB ASN A 158 64.519-27.513 8.535 1.0035.18 A ATOM 1149 CG ASN A 158 63.591 -27.829 7.399 1.0038.59 A

ATOM 1150 OD1 ASN A 158 63.145-26.936 6.669 1.0041.93 A

ATOM 1151 ND2ASNA158 63.284-29.111 7.236 1.0040.45 A

ATOM 1152 C ASN A 158 62.559-27.159 10.090 1.0029.06 A

ATOM 1153 O ASN A 158 62.509-28.257 10.645 1.0028.91 A ATOM 1154 N GLYA 159 61.485-26.393 9.915 1.0026.63 A

ATOM 1155 CA GLYA159 60.183-26.827 10.389 1.0025.19 A

ATOM 1156 C GLYA 159 59.989-26.516 11.872 1.0023.97 A

ATOM 1157 O GLY A 159 '59.081 -27.042 12.509 1.0024.61 A

ATOM 1158 N LEU A 160 60.840-25.662 12.426 1.0022.10 A ATOM 1159 CA LEUA160 60.737-25.305 13.833 1.0021.20 A

ATOM 1160 CB LEU A 160 62.111 -25.392 14.484 1.0020.15 A

ATOM 1161 CG LEU A 160 62.133-25.249 15.999 1.0020.47 A

ATOM 1162 CD1 LEUA160 61.452-26.478 16.659 1.0019.89 A

ATOM 1163 CD2LEUA160 63.591-25.126 16.429 1.0021.08 A ATOM 1164 C LEU A 160 60.190-23.888 13.899 1.0020.97 A

ATOM 11650 LEUA160 60.650-23.000 13.177 1.0019.28 A

ATOM 1166 N TRPA161 59.225-23.662 14.792 1.0018.62 A

ATOM 1167 CA TRP A 161 58.561 -22.362 14.883 1.0017.91 A

ATOM 1168 CB TRP A 161 57.146-22.480 14.287 1.0018.07 A ATOM 1169 CG TRP A 161 57.050-22.821 12.823 1.0020.11 A

ATOM 1170 CD2TRPA161 56.663-21.938 11.763 1.0020.69 A

ATOM 1171 CE2TRPA161 56.702-22.686 10.565 1.0021.93 A

ATOM 1172 CE3TRPA161 56.283-20.584 11.713 1.0022.55 A

ATOM 1173 CD1 TRPA161 57.305-24.036 12.237 1.0019.91 A ATOM 1174 NE1 TRP A 161 57.098-23.958 10.889 1.0022.38 A

ATOM 1175 CZ2 TRP A 161 56.374-22.127 9.320 1.0024.31 A

ATOM 1176 CZ3 TRP A 161 55.961-20.029 10.484 1.0023.64 A

ATOM 1177 CH2TRPA161 56.006-20.801 9.300 1.0026.06 A

ATOM 1178 C TRPA161 58.397-21.826 16.306 1.0016.59 A ATOM 1179 0 TRP A 161 58.209-22.598 17.250 1.0016.89 A

ATOM 1180 N HIS A 162 58.462-20.499 16.436 1.0017.09 A

ATOM 1181 CA HISA162 58.188-19.829 17.710 1.0016.99 A

ATOM 1182 CB HIS A 162 58.743-18.399 17.715 1.0018.89 A

ATOM 1183 CG HIS A 162 60.225-18.295 17.846 1.0022.18 A ATOM 1184 CD2 HISA 162 60.996-18.063 18.932 1.0021.07 A

ATOM 1185 ND1 HISA 162 61.081 -18.334 16.764 1.0025.27 A

ATOM 1186 CE1 HISA 162 62.317-18.125 17.182 1.0021.66 A

ATOM 1187 NE2 HIS A 162 62.292-17.956 18.494 1.0025.42 A

ATOM 1188 C HIS A 162 56.644-19.669 17.765 1.0017.23 A ATOM 1189 0 HISA162 56.086-19.053 16.873 1.0017.47 A

ATOM 1190 N ALA A 163 55.978-20.225 18.767 1.0015.41 A

ATOM 1191 CA ALAA163 54.533-20.082 18.901 1.0015.78 A

ATOM 1192 CB ALA A 163 54.004-21.105 19.880 1.0016.71 A

ATOM 1193 C ALAA163 54.231-18.681 19.402 1.0017.87 A ATOM 1194 0 ALAA163 54.854-18.202 20.356 1.0019.80 A

ATOM 1195 N LEU A 164 53.297-17.990 18.749 1.0014.59 A

ATOM 1196 CA LEUA164 52.924-16.627 19.202 1.0015.17 A

ATOM 1197 CB LEUA164 53.180-15.612 18.086 1.0015.44 A

ATOM 1198 CG LEU A 164 54.604-15.645 17.485 1.0017.07 A ATOM 1199 CD1 LEU A 164 54.675-14.727 16.264 1.0017.59 A

ATOM 1200 CD2 LEU A 164 55.632-15.233 18.533 1.0018.12 A

ATOM 1201 C LEU A 164 51.434-16.647 19.505 1.0013.85 A ATOM 1202 O LEU A 164 50.823-17.707 19.582 1.0013.66 A

ATOM 1203 N THRA165 50.828-15.484 19.752 1.0015.09 A

ATOM 1204 CA THRA 165 49.378-15.439 19.888 1.0015.28 A

ATOM 1205 CB THRA165 48.854-15.291 21.368 1.0017.09 A ATOM 1206 OG1 THR A 165 49.004-13.940 21.814 1.0016.05 A

ATOM 1207 CG2 THRA 165 49.605-16.27622.320 1.0018.30 A

ATOM 1208 C THRA165 48.968-14.241 19.006 1.0014.90 A

ATOM 1209 O THRA 165 49.798-13.372 18.698 1.0014.74 A

ATOM 1210 N PROA166 47.690-14.140 18.641 1.0012.97 A ATOM 1211 CD PRO A 166 47.227-13.048 17.773 1.0014.13 A

ATOM 1212 CA PROA166 46.579-15.033 18.963 1.0013.39 A

ATOM 1213 CB PROA166 45.365-14.340 18.338 1.0013.43 A

ATOM 1214 CG PROA166 45.781 -12.944 18.168 1.0014.27 A

ATOM 1215 C PROA166 46.664-16.460 18.460 1.0013.60 A ATOM 1216 0 PROA166 47.418-16.776 17.531 1.0012.79 A

ATOM 1217 N GLNA167 45.813-17.271 19.080 1.0012.21 A

ATOM 1218 CA GLNA167 45.646-18.680 18.739 1.0013.45 A

ATOM 1219 CB GLN A 167 46.191-19.554 19.861 1.0014.14 A

ATOM 1220 CG GLN A 167 47.661 -19.278 20.054 1.0012.95 A ATOM 1221 CD GLN A 167 48.430-20.42020.660 1.0015.02 A

ATOM 1222 OE1 GLN A 167 47.843-21.402 21.152 1.0016.34 A

ATOM 1223 NE2 GLN A 167 49.759-20.302 20.638 1.0014.86 A

ATOM 1224 C GLNA167 44.129-18.753 18.555 1.0013.08 A

ATOM 12250 GLNA167 43.349-18.261 19.371 1.0016.16 A ATOM 1226 N PHEA168 43.729-19.334 17.428 1.0011.35 A

ATOM 1227 CA PHEA168 42.334-19.351 16.988 1.0013.22 A

ATOM 1228 CB PHE A 168 42.346-18.609 15.652 1.0013.34 A

ATOM 1229 CG PHE A 168 41.018-18.318 15.082 1.0011.46 A

ATOM 1230 CD1 PHEA168 40.024-17.696 15.835 1.0011.80 A ATOM 1231 CD2 PHE A 168 40.793-18.614 13.729 1.0013.34 A

ATOM 1232 CE1 PHE A 168 38.789-17.347 15.245 1.0012.04 A

ATOM 1233 CE2 PHE A 168 39.583-18.284 13.136 1.0014.21 A

ATOM 1234 CZ PHEA 168 38.575-17.652 13.871 1.0012.79 A

ATOM 1235 C PHEA168 41.758-20.742 16.819 1.0013.32 A ATOM 1236 0 PHEA168 42.252-21.524 15.997 1.0013.53 A

ATOM 1237 N PHEA169 40.707-21.039 17.572 1.0013.68 A

ATOM 1238 CA PHE A 169 40.141 -22.400 17.512 1.0013.48 A

ATOM 1239 CB PHE A 169 40.656-23.229 18.687 1.0015.51 A

ATOM 1240 CG PHEA169 42.127-23.307 18.772 1.0014.70 A ATOM 1241 CD1 PHEA169 42.834 -22.482 19.634 1.0018.78 A

ATOM 1242 CD2PHEA169 42.806-24.219 17.998 1.0016.86 A

ATOM 1243 CE1 PHE A 169 44.217-22.569 19.719 1.0018.31 A

ATOM 1244 CE2 PHE A 169 44.185-24.318 18.074 1.0020.03 A

ATOM 1245 CZ PHE A 169 44.876-23.478 18.944 1.0017.40 A ATOM 1246 C PHE A 169 38.652-22.438 17.675 1.0014.22 A

ATOM 12470 PHEA169 38.050-21.488 18.153 1.0013.93 A

ATOM 1248 N PROA170 38.015-23.551 17.246 1.0014.23 A

ATOM 1249 CD PROA170 38.512-24.610 16.352 1.0014.76 A

ATOM 1250 CA PROA170 36.565-23.649 17.444 1.0013.15 A ATOM 1251 CB PROA170 36.236-25.043 16.900 1.0014.44 A

ATOM 1252 CG PROA170 37.229-25.216 15.809 1.0013.86 A

ATOM 1253 C PRO A 170 36.428-23.593 18.994 1.0014.51 A

ATOM 1254 O PRO A 170 37.169-24.246 19.723 1.0015.77 A

ATOM 1255 N ARG A 171 35.477-22.815 19.475 1.0014.72 A ATOM 1256 CA ARG A 171 35.256-22.568 20.895 1.0015.83 A

ATOM 1257 CB ARG A 171 34.022-21.680 21.047 1.0018.65 A

ATOM 1258 CG ARG A 171 33.937-20.866 22.355 1.0025.90 A ATOM 1259 CD ARG A 171 32.704-21.17923.181 1.0031.83 A

ATOM 1260 NE ARG A 171 31.488-21.219 22.377 1.0036.10 A

ATOM 1261 CZ ARG A 171 30.424-21.953 22.681 1.0038.37 A

ATOM 1262 NH1 ARGA171 30.424-22.692 23.782 1.0040.28 A

ATOM 1263 NH2ARGA171 29.384-21.997 21.855 1.0039.67 A

ATOM 1264 C ARG A 171 35.082-23.813 21.766 1.0017.37 A

ATOM 1265 O ARG A 171 35.822-24.043 22.734 1.0018.69 A

ATOM 1266 N GLU A 172 34.106-24.642 21.418 1.0018.97 A

ATOM 1267 CA GLU A 172 33.865-25.811 22.264 1.0016.09 A A ATTOOMM 1 1226688 C CBB GGLLUU AA 117722 32.479-26.425 21.949 1.0016.45 A

ATOM 1269 CG GLU A 172 31.308-25.452 22.174 1.0015.53 A

ATOM 1270 CD GLU A 172 29.908-26.08222.129 1.0016.53 A

ATOM 1271 OE1 GLU A 172 29.747-27.219 21.651 1.0016.05 A

ATOM 1272 OE2GLUA172 28.948-25.442 22.589 1.0018.55 A A ATTOOMM 1 1227733 C C GGLLUUAA117722 34.992-26.851 22.181 1.0014.98 A

ATOM 1274 O GLU A 172 35.335-27.509 23.189 1.0015.75 A

ATOM 1275 N LEU A 173 35.631 -26.971 21.018 1.0015.02 A

ATOM 1276 CA LEU A 173 36.745-27.921 20.904 1.0014.35 A

ATOM 1277 CB LEU A 173 37.253-28.000 19.452 1.0017.88 A A ATTOOMM 1 1227788 C CGG LLEEUU AA 117733 38.467-28.895 19.204 1.0019.94 A

ATOM 1279 CD1 LEU A 173 38.155-30.312 19.644 1.0023.00 A

ATOM 1280 CD2LEUA173 38.860-28.891 17.718 1.0022.40 A

ATOM 1281 C LEU A 173 37.869-27.444 21.843 1.0016.58 A

ATOM 1282 O LEU A 173 38.445-28.242 22.553 1.0017.31 A A ATTOOMM 1 1228833 N N LLEEUUAA117744 38.153-26.138 21.859 1.0016.39 A

ATOM 1284 CA LEU A 174 39.209-25.622 22.725 1.0017.86 A

ATOM 1285 CB LEU A 174 39.422-24.121 22.547 1.0017.46 A

ATOM 1286 CG LEU A 174 40.490-23.579 23.527 1.0016.50 A

ATOM 1287 CD1 LEU A 174 41.823-24.280 23.354 1.0016.77 A A ATTOOMM 1 1228888 C CDD22 LLEEUU AA 117744 40.650-22.087 23.267 1.0018.40 A

ATOM 1289 C LEU A 174 38.858-25.857 24.174 1.0016.75 A

ATOM 1290 O LEU A 174 39.693-26.313 24.956 1.0019.65 A

ATOM 1291 N HIS A 175 37.623-25.524 24.541 1.0016.32 A

ATOM 1292 CA HIS A 175 37.170-25.711 25.909 1.0017.93 A A ATTOOMM 1 1229933 C CBB HHIISS AA 117755 35.694-25.33326.001 1.0018.40 A

ATOM 1294 CG HIS A 175 35.058-25.70027.297 1.0024.23 A

ATOM 1295 CD2HISA175 34.753-24.952 28.381 1.0024.69 A

ATOM 1296 ND1 HIS A 175 34.699-26.997 27.603 1.0022.69 A

ATOM 1297 CE1 HIS A 175 34.205-27.02928.830 1.0024.69 A A ATTOOMM 1 1229988 N NEE22 HHIISS AA 117755 34.228-25.802 29.323 1.0025.90 A

ATOM 1299 C HIS A 175 37.365-27.186 26.321 1.0018.61 A

ATOM 1300 O HIS A 175 37.916-27.492 27.394 1.0021.69 A

ATOM 1301 N ASP A 176 36.926-28.110 25.474 1.0020.32 A

ATOM 1302 CA ASP A 176 37.040-29.528 25.793 1.0020.36 A A ATTOOMM 1 1330033 C CBB AASSPP AA 117766 36.307-30.384 24.756 1.0019.54 A

ATOM 1304 CG ASP A 176 34.811 -30.203 24.827 1.0021.78 A

ATOM 1305 OD1 ASP A 176 34.318-29.598 25.811 1.0019.43 A

ATOM 1306 OD2ASPA176 34.141 -30.670 23.884 1.0024.34 A

ATOM 1307 C ASP A 176 38.468-30.019 25.931 1.0020.70 A A ATTOOMM 1 1330088 O O AASSPP AA 117766 38.781 -30.763 26.862 1.0021.08 A

ATOM 1309 N CYS A 177 39.340-29.571 25.027 1.0020.09 A

ATOM 1310 CA CYS A 177 40.748-29.992 25.047 1.0020.88 A

ATOM 1311 CB CYS A 177 41.448-29.547 23.763 1.0020.76 A

ATOM 1312 SG CYS A 177 40.917-30.449 22.321 1.0022.54 A A ATTOOMM 1 1331133 C C CCYYSS AA 117777 41.490-29.440 26.273 1.0021.77 A

ATOM 1314 O CYS A 177 42.289-30.170 26.877 1.0022.18 A

ATOM 1315 N LEU A 178 41.212-28.185 26.649 1.0021.32 A ATOM 1316 CA LEUA178 41.844-27.58427.826 1.0023.70 A

ATOM 1317 CB LEU A 178 41.492-26.11027.938 1.0025.76 A

ATOM 1318 CG LEU A 178 42.438-25.10727.297 1.0029.21 A

ATOM 1319 CD1 LEU A 178 41.779-23.72827.235 1.0028.84 A ATOM 1320 CD2 LEU A 178 43.738-25.06928.106 1.0029.51 A

ATOM 1321 C LEU A 178 41.330-28.28829.064 1.0024.65 A

ATOM 1322 O LEU A 178 42.067-28.517 30.032 1.0025.16 A

ATOM 1323 N THRA 179 40.053-28.632 29.036 1.0022.96 A

ATOM 1324 CA THRA 179 39.464-29.287 30.187 1.0024.69 A ATOM 1325 CB THR A 179 37.942-29.40530.040 1.0023.46 A

ATOM 1326 OG1 THR A 179 37.344-28.106 30.165 1.0024.30 A

ATOM 1327 CG2THRA179 37.373-30.312 31.132 1.0025.38 A

ATOM 1328 C THRA 179 40.074-30.662 30.396 1.0025.03 A

ATOM 1329 O THRA179 40.410-31.01831.523 1.0026.66 A ATOM 1330 N ARGA180 40.241 -31.41729.318 1.0026.02 A

ATOM 1331 CA ARG A 180 40.814-32.75929.402 1.0028.99 A

ATOM 1332 CB ARG A 180 40.683-33.50028.068 1.0031.28 A

ATOM 1333 CG ARGA180 41.251 -34.91728.111 1.0035.07 A

ATOM 1334 CD ARG A 180 41.087-35.67826.795 1.0038.12 A ATOM 1335 NE ARGA180 41.055-37.119 27.047 1.0040.37 A

ATOM 1336 CZ ARG A 180 40.946-38.062 26.113 1.0042.33 A

ATOM 1337 NH1 ARG A 180 40.859-37.733 24.827 1.0040.95 A

ATOM 1338 NH2 ARG A 180 40.906-39.34526.473 1.0040.62 A

ATOM 1339 C ARG A 180 42.283-32.71529.794 1.0030.47 A ATOM 1340 O ARG A 180 42.716-33.455 30.680 1.0031.09 A

ATOM 1341 N ALAA181 43.041-31.84529.131 1.0029.77 A

ATOM 1342 CA ALAA181 44.469-31.71629.401 1.0031.21 A

ATOM 1343 CB ALAA 181 45.076-30.60828.525 1.0029.92 A

ATOM 1344 C ALAA 181 44.710-31.421 30.876 1.0032.21 A ATOM 1345 O ALAA181 45.545-32.06531.510 1.0032.96 A

ATOM 1346 N LEU A 182 43.971-30.462 31.418 1.0032.52 A

ATOM 1347 CA LEU A 182 44.107-30.09032.817 1.0034.94 A

ATOM 1348 CB LEU A 182 43.259-28.861 33.122 1.0034.14 A

ATOM 1349 CG LEU A 182 43.839-27.495 32.730 1.0035.40 A ATOM 1350 CD1 LEU A 182 42.780-26.40632.905 1.0034.56 A

ATOM 1351 CD2 LEU A 182 45.058-27.197 33.607 1.0036.57 A

ATOM 1352 C LEUA182 43.714-31.219 33.763 1.0036.85 A

ATOM 1353 O LEU A 182 44.402-31.464 34.753 1.0038.12 A

ATOM 1354 N ASN A 183 42.608-31.899 33.462 1.0038.78 A ATOM 1355 CA ASN A 183 42.125-32.994 34.300 1.0040.37 A

ATOM 1356 CB ASN A 183 40.733-33.451 33.822 1.0041.20 A

ATOM 1357 CG ASN A 183 40.163-34.613 34.651 1.0043.88 A

ATOM 1358 OD1ASNA183 40.477-35.784 34.406 1.0044.85 A

ATOM 1359 ND2 ASN A 183 39.323-34.28635.637 1.0044.80 A ATOM 1360 C ASN A 183 43.109-34.15934.305 1.0040.66 A

ATOM 1361 O ASN A 183 43.280-34.825 35.328 1.0042.26 A

ATOM 1362 N GLU A 184 43.771 -34.399 33.175 1.0040.71 A

ATOM 1363 CA GLU A 184 44.742-35.49033.090 1.0040.79 A

ATOM 1364 CB GLU A 184 44.781 -36.067 31.671 1.0041.32 A ATOM 1365 CG GLU A 184 43.549-36.877 31.309 1.0042.20 A

ATOM 1366 CD GLU A 184 43.689-37.612 29.996 1.0043.64 A

ATOM 1367 OE1 GLU A 184 44.768-38.18629.728 1.0044.91 A

ATOM 1368 OE2 GLU A 184 42.705-37.64629.233 1.0045.31 A

ATOM 1369 C GLU A 184 46.147-35.06033.509 1.0040.44 A ATOM 1370 O GLU A 184 47.114-35.792 33.299 1.0039.99 A

ATOM 1371 N GLYA 185 46.254-33.876 34.101 1.0040.16 A

ATOM 1372 CA GLYA 185 47.550-33.379 34.540 1.0040.35 A ATOM 1373 C GLYA 185 48.603-33.250 33.447 1.0040.25 A

ATOM 1374 O GLYA 185 49.793-33.47733.680 1.0040.74 A

ATOM 1375 N ALAA 186 48.186-32.876 32.245 1.0039.05 A

ATOM 1376 CA ALAA 186 49.147-32.719 31.163 1.0038.44 A

ATOM 1377 CB ALA A 186 48.435-32.768 29.810 1.0039.17 A

ATOM 1378 C ALAA 186 49.897-31.390 31.317 1.0037.45 A

ATOM 1379 O ALAA 186 49.428-30.472 31.986 1.0036.32 A

ATOM 1380 N THRA 187 51.069-31.30930.700 1.0037.15 A

ATOM 1381 CA THR A 187 51.883-30.100 30.733 1.0036.95 A A ATTOOMM 1 1338822 C CBB TTHHRR AA 118877 53.362-30.444 30.489 1.0038.24 A

ATOM 1383 OG1 THRA 187 53.862-31.165 31.620 1.0040.23 A

ATOM 1384 CG2 THRA 187 54.193-29.185 30.271 1.0039.65 A

ATOM 1385 C THRA 187 51.379-29.16729.642 1.0034.75 A

ATOM 1386 O THRA 187 51.599-29.401 28.458 1.0036.28 A A ATTOOMM 1 1338877 N N IILLEEAA 118888 50.702-28.106 30.052 1.0032.87 A

ATOM 1388 CA ILE A 188 50.138-27.14629.112 1.0030.65 A

ATOM 1389 CB ILE A 188 48.708-26.76829.541 1.0030.86 A

ATOM 1390 CG2ILEA188 48.147-25.65928.650 1.0033.36 A

ATOM 1391 CG1 ILE A 188 47.834-28.01529.480 1.0032.82 A A ATTOOMM 1 1339922 C CDD11 IILLEE AA 118888 46.464-27.79630.017 1.0035.08 A

ATOM 1393 C ILEA 188 50.969-25.881 29.019 1.0028.60 A

ATOM 1394 O ILE A 188 51.329-25.298 30.047 1.0029.73 A

ATOM 1395 N THRA 189 51.297-25.47927.795 1.0024.39 A

ATOM 1396 CA THRA 189 52.036-24.241 27.565 1.0023.54 A A ATTOOMM 1 1339977 C CBB TTHHRRAA 118899 53.261 -24.46426.653 1.0021.74 A

ATOM 1398 OG1 THRA 189 52.904-25.29725.540 1.0022.87 A

ATOM 1399 CG2THRA189 54.395-25.142 27.458 1.0024.44 A

ATOM 1400 C THRA 189 51.033-23.280 26.933 1.0021.79 A

ATOM 1401 O THRA 189 50.459-22.460 27.645 1.0023.55 A A ATTOOMM 1 1440022 N N AASSPP AA 119900 50.768-23.410 25.630 1.0020.46 A

ATOM 1403 CA ASP A 190 49.792-22.531 25.000 1.0017.65 A

ATOM 1404 CB ASPA 190 50.354-21.90223.707 1.0018.83 A

ATOM 1405 CG ASP A 190 50.819-22.92822.698 1.0020.10 A

ATOM 1406 OD1 ASP A 190 50.733-24.15722.966 1.0018.81 A A ATTOOMM 1 1440077 O ODD22AASSPPAA119900 51.293-22.53821.605 1.0020.63 A

ATOM 1408 C ASP A 190 48.494-23.280 24.706 1.0018.73 A

ATOM 1409 O ASP A 190 48.363-24.46325.042 1.0018.88 A

ATOM 1410 N GLU A 191 47.535-22.59824.075 1.0017.62 A

ATOM 1411 CA GLU A 191 46.275-23.25623.753 1.0018.22 A A ATTOOMM 1 1441122 C CBB GGLLUU AA 119911 45.251 -22.27023.186 1.0017.72 A

ATOM 1413 CG GLU A 191 44.624-21.336 24.234 1.0020.18 A

ATOM 1414 CD GLU A 191 45.658-20.49824.949 1.0019.25 A

ATOM 1415 OE1 GLU A 191 46.405-19.74924.284 1.0021.27 A

ATOM 1416 OE2GLUA191 45.746-20.57926.183 1.0024.43 A A ATTOOMM 1 1441177 C C GGLLUUAA119911 46.494-24.386 22.766 1.0017.25 A

ATOM 1418 O GLU A 191 45.845-25.433 22.858 1.0017.71 A

ATOM 1419 N ALAA 192 47.414-24.211 21.824 1.0017.27 A ^'

ATOM 1420 CA ALA A 192 47.667-25.262 20.863 1.0014.57 A

ATOM 1421 CB ALA A 192 48.683-24.803 19.815 1.0017.75 A A ATTOOMM 1 1442222 C C AALLAAAA119922 48.146-26.52921.551 1.0018.49 A

ATOM 1423 O ALAA 192 47.779-27.623 21.129 1.0018.39 A

ATOM 1424 N SER A 193 48.931 -26.40322.623 1.0019.16 A

ATOM 1425 CA SERA 193 49.425-27.60723.295 1.0018.15 A

ATOM 1426 CB SERA 193 50.432-27.27524.407 1.0017.82 A A ATTOOMM 1 1442277 O OGG SSEERR AA 119933 49.854-26.67625.523 1.0020.35 A

ATOM 1428 C SER A 193 48.271 -28.441 23.860 1.0018.39 A

ATOM 1429 O SERA 193 48.417-29.65524.001 1.0020.89 A ATOM 1430 N ALAA194 47.150-27.81224.183 1.0017.06 A

ATOM 1431 CA ALAA 194 45.998-28.581 24.695 1.0019.00 A

ATOM 1432 CB ALAA 194 44.961 -27.66525.316 1.0019.48 A

ATOM 1433 C ALAA 194 45.392-29.38723.548 1.0020.61 A ATOM 1434 O ALAA 194 45.004-30.552 23.723 1.0021.17 A

ATOM 1435 N LEU A 195 45.267-28.77622.372 1.0019.88 A

ATOM 1436 CA LEU A 195 44.747-29.50321.217 1.0020.46 A

ATOM 1437 CB LEU A 195 44.644-28.607 19.978 1.0020.87 A

ATOM 1438 CG LEU A 195 43.408-27.733 19.733 1.0022.89 A ATOM 1439 CD1 LEU A 195 42.301 -28.615 19.240 1.0025.41 A

ATOM 1440 CD2 LEU A 195 43.017-26.95821.007 1.0022.27 A

ATOM 1441 C LEU A 195 45.714-30.62420.887 1.0020.06 A

ATOM 1442 O LEUA195 45.312-31.713 20.497 1.0021.99 A

ATOM 1443 N GLUA196 47.001 -30.341 21.014 1.0020.14 A ATOM 1444 CA GLU A 196 48.004-31.341 20.698 1.0021.08 A

ATOM 1445 CB GLU A 196 49.401 -30.74620.838 1.0021.85 A

ATOM 1446 CG GLU A 196 49.719-29.755 19.730 1.0020.85 A

ATOM 1447 CD GLU A 196 50.810-28.79020.131 1.0023.06 A

ATOM 1448 OE1 GLU A 196 51.783-29.25920.748 1.0022.15 A ATOM 1449 OE2GLUA196 50.689-27.569 19.839 1.0020.84 A

ATOM 1450 C GLUA196 47.865-32.53321.593 1.0021.44 A

ATOM 1451 O GLUA196 47.936-33.66421.125 1.0023.67 A

ATOM 1452 N TYRA 197 47.651-32.28322.873 1.0022.86 A

ATOM 1453 CA TYRA 197 47.529-33.37223.825 1.0024.81 A ATOM 1454 CB TYRA 197 47.294-32.81525.217 1.0026.70 A

ATOM 1455 CG TYRA 197 47.145-33.87626.272 1.0030.94 A

ATOM 1456 CD1 TYR A 197 48.255-34.55626.771 1.0034.41 A

ATOM 1457 CE1 TYRA 197 48.113-35.531 27.760 1.0036.74 A

ATOM 1458 CD2 TYR A 197 45.892-34.20026.776 1.0032.36 A ATOM 1459 CE2 TYR A 197 45.739-35.17627.762 1.0035.27 A

ATOM 1460 CZ TYRA 197 46.854-35.83228.251 1.0036.98 A

ATOM 1461 OH TYRA 197 46.707-36.75929.261 1.0038.43 A

ATOM 1462 C TYR A 197 46.388-34.313 23.454 1.0026.65 A

ATOM 1463 O TYRA 197 46.479-35.517 23.679 1.0028.06 A ATOM 1464 N CYS A 198 45.323-33.75822.882 1.0025.61 A

ATOM 1465 CA CYS A 198 44.137-34.53422.494 1.0026.39 A

ATOM 1466 CB CYS A 198 42.890-33.65422.676 1.0025.99 A

ATOM 1467 SG CYSA198 42.661 -33.11824.389 1.0025.29 A

ATOM 1468 C CYS A 198 44.185-35.14721.082 1.0027.48 A ATOM 1469 O CYS A 198 43.175-35.65520.555 1.0028.61 A

ATOM 1470 N GLYA 199 45.363-35.101 20.467 1.0025.51 A

ATOM 1471 CA GLYA199 45.522-35.692 19.154 1.0026.35 A

ATOM 1472 C GLYA 199 45.333-34.790 17.960 1.0025.23 A

ATOM 1473 O GLYA 199 45.368-35.251 16.826 1.0026.02 A ATOM 1474 N PHEA200 45.131-33.496 18.192 1.0026.46 A

ATOM 1475 CA PHE A 200 44.965-32.591 17.071 1.0025.13 A

ATOM 1476 CB PHE A 200 43.935-31.515 17.410 1.0025.59 A

ATOM 1477 CG PHEA200 42.571 -32.073 17.663 1.0024.68 A

ATOM 1478 CD1 PHE A 200 42.137-32.323 18.952 1.0025.33 A ATOM 1479 CD2 PHE A 200 41.741 -32.406 16.607 1.0025.88 A

ATOM 1480 CE1 PHE A 200 40.892-32.903 19.193 1.0026.86 A

ATOM 1481 CE2 PHE A 200 40.481 -32.995 16.838 1.0024.95 A

ATOM 1482 CZ PHE A 200 40.072-33.237 18.132 1.0025.93 A

ATOM 1483 C PHE A 200 46.274-31.965 16.637 1.0026.98 A ATOM 1484 O PHEA200 47.274-31.979 17.380 1.0026.59 A

ATOM 1485 N HISA201 46.258-31.424 15.422 1.0025.31 A

ATOM 1486 CA HIS A 201 47.422-30.789 14.834 1.0024.70 A ATOM 1487 CB HIS A 201 48.016-31.716 13.774 1.0025.44 A

ATOM 1488 CG HIS A 201 48.545-33.001 14.336 1.0028.40 A

ATOM 1489 CD2HISA201 49.774-33.327 14.799 1.0026.07 A

ATOM 1490 ND1 HIS A 201 47.756-34.117 14.528 1.0029.46 A

ATOM 1491 CE1 HIS A 201 48.478-35.073 15.086 1.0028.32 A

ATOM 1492 NE2HISA201 49.705-34.618 15.261 1.0030.32 A

ATOM 1493 C HIS A 201 47.049-29.437 14.233 1.0022.38 A

ATOM 1494 O HIS A 201 46.786-29.330 13.037 1.0023.23 A

ATOM 1495 N PRO A 202 47.036-28.382 15.066 1.0021.62 A

ATOM 1496 CD PRO A 202 47.358-28.400 16.500 1.0021.55 A

ATOM 1497 CA PRO A 202 46.691 -27.019 14.644 1.0020.94 A

ATOM 1498 CB PRO A 202 46.811 -26.210 15.936 1.0021.83 A

ATOM 1499 CG PRO A 202 46.573-27.219 17.011 1.0022.80 A

ATOM 1500 C PRO A 202 47.603-26.460 13.555 1.0019.04 A

ATOM 1501 O PRO A 202 48.770-26.846 13.421 1.0019.03 A

ATOM 1502 N GLN A 203 47.053-25.539 12.772 1.0017.57 A

ATOM 1503 CA GLN A 203 47.803-24.926 11.696 1.0019.99 A

ATOM 1504 CB GLN A 203 46.848-24.346 10.648 1.0021.19 A

ATOM 1505 CG GLN A 203 46.137-25.385 9.805 1.0028.17 A

ATOM 1506 CD GLN A 203 47.084-26.137 8.868 1.0031.04 A

ATOM 1507 OE1 GLN A 203 47.813-25.532 8.075 1.0033.76 A

ATOM 1508 NE2GLNA203 47.060-27.464 8.945 1.0035.67 A

ATOM 1509 C GLN A 203 48.737-23.822 12.181 1.0018.74 A

ATOM 1510 O GLN A 203 48.462-23.146 13.179 1.0020.08 A

ATOM 1511 N LEU A 204 49.832-23.662 11.452 1.0018.05 A

ATOM 1512 CA LEU A 204 50.821-22.628 11.727 1.0017.82 A

ATOM 1513 CB LEU A 204 52.236-23.213 11.603 1.0017.49 A

ATOM 1514 CG LEU A 204 52.599-24.184 12.732 1.0017.60 A

ATOM 1515 CD1 LEU A 204 53.704-25.173 12.316 1.0020.96 A

ATOM 1516 CD2 LEU A 204 53.044-23.364 13.933 1.0019.49 A

ATOM 1517 C LEU A 204 50.597-21.550 10.665 1.0018.49 A

ATOM 1518 O LEU A 204 50.682-21.814 9.470 1.0021.23 A

ATOM 1519 N VAL A 205 50.275-20.337 11.097 1.0019.02 A

ATOM 1520 CA VAL A 205 50.063-19.241 10.171 1.0017.25 A

ATOM 1521 CB VAL A 205 48.734-18.535 10.485 1.0016.67 A

ATOM 1522 CG1 VAL A 205 48.608-17.262 9.690 1.0019.67 A

ATOM 1523 CG2 VAL A 205 47.583-19.464 10.150 1.0016.36 A

ATOM 1524 C VAL A 205 51.235-18.323 10.428 1.0018.86 A

ATOM 1525 O VAL A 205 51.377-17.792 11.527 1.0015.99 A

ATOM 1526 N GLU A 206 52.095-18.136 9.439 1.0016.73 A

ATOM 1527 CA GLU A 206 53.265-17.306 9.682 1.0017.54 A

ATOM 1528 CB GLU A 206 54.227-17.361 8.490 1.0018.17 A

ATOM 1529 CG GLU A 206 55.401 -16.413 8.677 1.0020.97 A

ATOM 1530 CD GLU A 206 56.567-16.677 7.733 1.0024.77 A

ATOM 1531 OE1 GLU A 206 56.420-17.506 6.818 1.0029.05 A

ATOM 1532 OE2 GLU A 206 57.625-16.044 7.926 1.0027.53 A

ATOM 1533 C GLU A 206 52.927-15.860 10.000 1.0019.59 A

ATOM 1534 O GLU A 206 52.153-15.218 9.284 1.0019.39 A

ATOM 1535 N GLY A 207 53.519-15.357 11.079 1.0018.50 A

ATOM 1536 CA GLY A 207 53.296-13.985 11.501 1.0019.21 A

ATOM 1537 C GLY A 207 54.589-13.216 11.737 1.0019.02 A

ATOM 1538 O GLY A 207 55.679-13.784 11.712 1.0021.77 A

ATOM 1539 N ARG A 208 54.465-11.911 11.927 1.0019.15 A

ATOM 1540 CA ARG A 208 55.630-11.051 12.140 1.0019.87 A

ATOM 1541 CB ARG A 208 55.194 -9.589 12.173 1.0021.67 A

ATOM 1542 CG ARG A 208 54.474 -9.119 10.943 1.0021.90 A

ATOM 1543 CD ARG A 208 53.919 -7.747 11.214 1.0026.13 A ATOM 1544 NE ARG A 208 54.981 -6.822 11.567 1.0029.70 A

ATOM 1545 CZ ARG A 208 55.640 -6.090 10.675 1.0033.00 A

ATOM 1546 NH1ARGA208 55.321 -6.177 9.388 1.0033.75 A

ATOM 1547 NH2ARGA208 56.634 -5.306 11.066 1.0033.49 A ATOM 1548 C ARG A 208 56.359-11.375 13.431 1.0021.32 A

ATOM 1549 O ARG A 208 55.743-11.581 14.486 1.0020.27 A

ATOM 1550 N ALA A 209 57.685-11.360 13.365 1.0020.28 A

ATOM 1551 CA ALAA209 58.484-11.665 14.541 1.0022.16 A

ATOM 1552 CB ALAA209 59.905-12.025 14.120 1.0022.70 A ATOM 1553 C ALAA209 58.511-10.552 15.590 1.0021.24 A

ATOM 1554 O ALA A 209 58.946-10.785 16.713 1.0022.67 A

ATOM 1555 N ASP A 210 58.037 -9.357 15.234 1.0021.21 A

ATOM 1556 CA ASPA210 58.009 -8.253 16.180 1.0022.11 A

ATOM 1557 CB ASP A 210 58.143 -6.884 15.494 1.0023.53 A ATOM 1558 CG ASP A 210 57.169 -6.676 14.354 1.0027.09 A

ATOM 1559 OD1 ASP A 210 56.127 -7.358 14.281 1.0022.40 A

ATOM 1560 OD2ASPA210 57.470 -5.791 13.524 1.0030.11 A

ATOM 1561 C ASP A 210 56.767 -8.272 17.058 1.0020.66 A

ATOM 1562 O ASP A 210 56.526 -7.357 17.828 1.0020.26 A ATOM 1563 N ASN A 211 55.992 -9.344 16.936 1.0020.39 A

ATOM 1564 CA ASN A211 54.802 -9.540 17.768 1.0018.95 A

ATOM 1565 CB ASN A 211 53.877-10.546 17.057 1.0017.97 A

ATOM 1566 CG ASNA211 52.625-10.856 17.842 1.0017.29 A

ATOM 1567 OD1 ASN A 211 52.333-10.214 18.843 1.0017.93 A ATOM 1568 ND2ASNA211 51.877-11.849 17.382 1.0014.78 A

ATOM 1569 C ASNA211 55.394-10.140 19.059 1.0019.68 A

ATOM 1570 O ASN A 211 55.260-11.338 19.312 1.0022.87 A

ATOM 1571 N ILEA212 56.063 -9.321 19.870 1.0018.72 A

ATOM 1572 CA ILE A 212 56.716 -9.809 21.095 1.0020.21 A ATOM 1573 CB ILEA212 58.016 -8.997 21.383 1.0021.90 A

ATOM 1574 CG2ILEA212 58.999 -9.171 20.232 1.0024.05 A

ATOM 1575 CG1 ILE A 212 57.666 -7.51521.623 1.0021.14 A

ATOM 1576 CD1 ILE A 212 58.801 -6.708 22.291 1.0025.97 A

ATOM 1577 C ILE A 212 55.881 -9.764 22.360 1.0020.50 A ATOM 1578 0 ILEA212 54.895 -9.041 22.426 1.0018.71 A

ATOM 1579 N LYS A 213 56.295-10.54523.368 1.0020.71 A

ATOM 1580 CA LYS A 213 55.629-10.582 24.655 1.0021.21 A

ATOM 1581 CB LYS A 213 55.459-12.012 25.163 1.0021.58 A

ATOM 1582 CG LYS A 213 54.520-12.12026.351 1.0025.52 A ATOM 1583 CD LYSA213 54.131 -13.56326.609 1.0027.46 A

ATOM 1584 CE LYS A 213 55.364-14.429 26.712 1.0032.41 A

ATOM 1585 NZ LYSA213 54.991 -15.85026.895 1.0035.18 A

ATOM 1586 C LYS A 213 56.524 -9.823 25.614 1.0020.88 A

ATOM 1587 O LYSA213 57.711-10.118 25.739 1.0023.26 A ATOM 1588 N VALA214 55.954 -8.821 26.246 1.0019.25 A

ATOM 1589 CA VAL A 214 56.689 -8.01427.199 1.0021.63 A

ATOM 1590 CB VAL A 214 55.902 -6.728 27.441 1.0021.92 A

ATOM 1591 CG1VALA214 56.568 -5.87828.501 1.0022.59 A

ATOM 1592 CG2 VAL A 214 55.798 -5.95826.114 1.0019.13 A ATOM 1593 C VALA214 56.791 -8.892 28.435 1.0021.12 A

ATOM 1594 O VAL A 214 55.777 -9.236 29.043 1.0023.74 A

ATOM 1595 N THR A 215 58.012 -9.272 28.801 1.0023.14 A

ATOM 1596 CA THRA215 58.233-10.17229.927 1.0024.52 A

ATOM 1597 CB THR A 215 58.722-11.55029.426 1.0025.23 A ATOM 1598 OG1 THR A 215 57.842-12.02928.391 1.0029.30 A

ATOM 1599 CG2THRA215 58.739-12.557 30.577 1.0028.71 A

ATOM 1600 C THR A 215 59.267 -9.645 30.906 1.0025.65 A ATOM 1601 O THR A 215 59.132 -9.835 32.118 1.00 25.68 A

ATOM 1602 N ARG A 216 60.308 -9.009 30.365 1.00 26.81 A

ATOM 1603 CA ARG A 216 61.399 -8.451 31.167 1.00 28.70 A

ATOM 1604 CB ARG A 216 62.762 -9.009 30.738 1.00 31.94 A ATOM 1605 CG ARG A 216 63.023 -10.452 31.106 1.00 36.40 A

ATOM 1606 CD ARG A 216 62.506 -11.398 30.046 1.00 41.09 A

ATOM 1607 NE ARG A 216 62.570 -12.780 30.512 1.00 43.98 A

ATOM 1608 CZ ARG A 216 62.201 -13.841 29.800 1.00 44.60 A

ATOM 1609 NH1 ARG A 216 61.734 -13.697 28.561 1.00 44.81 A ATOM 1610 NH2 ARG A 216 62.293 -15.051 30.340 1.00 45.00 A

ATOM 1611 C ARG A 216 61.441 -6.946 31.018 1.00 28.78 A

ATOM 1612 0 ARG A 216 60.928 -6.391 30.051 1.00 27.46 A

ATOM 1613 N PRO A 217 62.108 -6.261 31.950 1.00 28.34 A

ATOM 1614 CD PRO A 217 62.833 -6.767 33.130 1.00 30.01 A ATOM 1615 CA PRO A 217 62.186 -4.804 31.883 1.00 30.03 A

ATOM 1616 CB PRO A 217 63.222 -4.477 32.947 1.00 28.68 A

ATOM 1617 CG PRO A 217 62.933 -5.514 33.980 1.00 29.57 A

ATOM 1618 C PRO A 217 62.535 -4.201 30.530 1 .00 29.07 A

ATOM 1619 O PRO A 217 61.881 -3.266 30.084 1.00 31.81 A ATOM 1620 N GLU A 218 63.546 -4.750 29.872 1.00 30.64 A

ATOM 1621 CA GLU A 218 63.985 -4.234 28.587 1.00 30.48 A

ATOM 1622 CB GLU A 218 65.256 -4.959 28.147 1.00 33.28 A

ATOM 1623 CG GLU A 218 65.069 -6.466 28.032 1.00 38.91 A

ATOM 1624 CD GLU A 218 65.516 -7.238 29.269 1.00 41.24 A ATOM 1625 OE1 GLU A 218 65.181 -6.830 30.410 1.00 40.90 A

ATOM 1626 OE2 GLU A 218 66.196 -8.272 29.087 1.00 42.62 A

ATOM 1627 C GLU A 218 62.936 -4.351 27.494 1.00 29.13 A

ATOM 1628 O GLU A 218 62.960 -3.598 26.510 1.00 27.03 A

ATOM 1629 N ASP A 219 62.017 -5.298 27.659 1.00 26.62 A ATOM 1630 CA ASP A 219 60.968 -5.508 26.669 1.00 25.98 A

ATOM 1631 CB ASP A 219 60.140 -6.750 27.014 1.00 26.06 A

ATOM 1632 CG ASP A 219 60.950 -8.023 26.961 1.00 26.52 A

ATOM 1633 OD1 ASP A 219 61.988 -8.039 26.277 1.00 31.84 A

ATOM 1634 OD2 ASP A 219 60.550 -9.028 27.581 1.00 27.31 A ATOM 1635 C ASP A 219 60.040 -4.321 26.510 1.00 25.26 A

ATOM 1636 0 ASP A 219 59.484 -4.130 25.451 1.00 22.56 A

ATOM 1637 N LEU A 220 59.868 -3.518 27.551 1.00 25.27 A

ATOM 1638 CA LEU A 220 58.987 -2.375 27.446 1.00 26.84 A

ATOM 1639 CB LEU A 220 58.895 -1.650 28.781 1.00 28.83 A ATOM 1640 CG LEU A 220 57.759 -.631 28.884 1.00 30.20 A

ATOM 1641 CD1 LEU A 220 56.406 -1.338 28.717 1.00 30.95 A

ATOM 1642 CD2 LEU A 220 57.832 .054 30.243 1.00 31.79 A

ATOM 1643 C LEU A 220 '59.455 -1.397 26.374 1.00 25.87 A

ATOM 1644 0 LEU A 220 58.678 -.973 25.536 1.00 25.32 A ATOM 1645 N ALA A 221 60.737 -1.037 26.408 1.00 27.07 A

ATOM 1646 CA ALA A 221 61.266 -.101 25.435 1.00 25.56 A

ATOM 1647 CB ALA A 221 62.656 .363 25.852 1.00 26.78 A

ATOM 1648 C ALA A 221 61.289 -.711 24.038 1.00 23.26 A

ATOM 1649 O ALA A 221 61.087 -.013 23.058 1.00 24.63 A ATOM 1650 N LEU A 222 61.504 -2.013 23.938 1.00 23.08 A

ATOM 1651 CA LEU A 222 61.503 -2.661 22.628 1.0023.30 A

ATOM 1652 CB LEU A 222 62.014 -4.101 22.728 1.00 21.55 A

ATOM 1653 CG LEU A 222 62.050 -4.926 21.437 1.00 23.49 A

ATOM 1654 CD1 LEU A 222 62.997 -4.286 20.417 1.00 23.59 A ATOM 1655 CD2 LEU A 222 62.533 -6.326 21.761 1.00 24.91 A

ATOM 1656 C LEU A 222 60.091 -2.655 22.056 1.00 23.53 A

ATOM 1657 O LEU A 222 59.904 -2.391 20.867 1.00 21.82 A ATOM 1658 N ALA A 223 59.100 -2.951 22.896 1.00 23.35 A

ATOM 1659 CA ALA A 223 57.718 -2.947 22.420 1.00 23.76 A

ATOM 1660 CB ALA A 223 56.778 -3.378 23.528 1.00 24.49 A

ATOM 1661 C ALA A 223 57.366 -1.552 21.934 1.00 24.90 A ATOM 1662 O ALA A 223 56.734 -1.389 20.894 1.00 24.19 A

ATOM 1663 N GLU A 224 57.801 -.541 22.684 1.00 26.47 A

ATOM 1664 CA GLU A 224 57.547 .847 22.314 1.00 28.65 A

ATOM 1665 CB GLU A 224 58.106 1.779 23.388 1.00 31.36 A

ATOM 1666 CG GLU A 224 58.017 3.242 23.027 1.00 36.03 A ATOM 1667 CD GLU A 224 58.625 4.139 24.097 1.00 37.40 A

ATOM 1668 OE1 GLU A 224 59.707 3.810 24.630 1.00 40.58 A

ATOM 1669 OE2 GLU A 224 58.023 5.181 24.390 1.00 39.57 A

ATOM 1670 C GLU A 224 58.182 1.162 20.955 1.00 29.18 A

ATOM 1671 O GLU A 224 57.601 1.875 20.138 1.00 27.89 A ATOM 1672 N PHE A 225 59.371 .612 20.715 1.00 28.71 A

ATOM 1673 CA PHE A 225 60.078 .815 19.451 1.00 28.52 A

ATOM 1674 CB PHE A 225 61.475 .176 19.524 1.00 28.57 A

ATOM 1675 CG PHE A 225 62.178 .085 18.187 1.00 27.70 A

ATOM 1676 CD1 PHE A 225 62.774 1.207 17.616 1.00 29.44 A ATOM 1677 CD2 PHE A 225 62.211 -1.122 17.480 1.00 28.27 A

ATOM 1678 CE1 PHE A 225 63.380 1.130 16.370 1.00 27.78 A

ATOM 1679 CE2 PHE A 225 62.820 -1.205 16.229 1.00 28.89 A

ATOM 1680 CZ PHE A 225 63.404 -.078 15.671 1.00 28.69 A

ATOM 1681 C PHE A 225 59.281 .182 18.307 1.00 30.36 A ATOM 1682 O PHE A 225 59.064 .799 17.262 1.00 30.81 A

ATOM 1683 N TYR A 226 58.836 -1.056 18.493 1.00 29.52 A

ATOM 1684 CA TYR A 226 58.079 -1.730 17.440 1.00 30.72 A

ATOM 1685 CB TYR A 226 57.796 -3.188 17.824 1.00 29.06 A

ATOM 1686 CG TYR A 226 59.000 -4.098 17.729 1.00 27.52 A ATOM 1687 CD 1 TYR A 226 59.185 -5.113 18.653 1.00 28.12 A

ATOM 1688 CE1 TYR A 226 60.248 -5.993 18.561 1.00 29.18 A

ATOM 1689 CD2 TYR A 226 59.928 -3.983 16.686 1.00 29.15 A

ATOM 1690 CE2 TYR A 226 61.005 -4.867 16.585 1.00 28.48 A

ATOM 1691 CZ TYR A 226 61.158 -5.866 17.520 1.00 29.84 A ATOM 1692 OH TYR A 226 62.203 -6.761 17.462 1.00 31.49 A

ATOM 1693 C TYR A 226 56.765 -1.020 17.096 1.00 32.01 A

ATOM 1694 O TYR A 226 56.400 -.924 15.918 1.00 32.48 A

ATOM 1695 N LEU A 227 56.043 -.544 18.108 1.00 33.13 A

ATOM 1696 CA LEU A 227 54.784 .155 17.843 1.00 35.84 A ATOM 1697 CB LEU A 227 54.136 .606 19.162 1.00 35.21 A

ATOM 1698 CG LEU A 227 53.498 -.535 19.968 1.00 34.38 A

ATOM 1699 CD1 LEU A 227 53.211 -.093 21.393 1.00 36.57 A

ATOM 1700 CD2 LEU A 227 52.226 -.985 19.280 1.00 31.83 A

ATOM 1701 C LEU A 227 55.075 1.352 16.918 1.00 38.28 A ATOM 1702 O LEU A 227 54.316 1.624 15.978 1.00 38.83 A

ATOM 1703 N ALA A 228 56.195 2.030 17.178 1.00 39.66 A

ATOM 1704 CA ALA A 228 56.647 3.179 16.385 1.00 41.19 A

ATOM 1705 CB ALA A 228 55.458 4.010 15.931 1.00 42.11 A

ATOM 1706 C ALA A 228 57.617 4.063 17.165 1.00 41.86 A ATOM 1707 O ALA A 228 57.670 3.999 18.397 1.00 43.53 A

ATOM 1708 N ARG A 229 58.388 4.883 16.445 1.00 42.26 A

ATOM 1709 CA ARG A 229 59.347 5.813 17.067 1.00 42.80 A

ATOM 1710 CB ARG A 229 60.517 5.049 17.712 1.00 42.26 A

ATOM 1711 CG ARG A 229 61.470 4.368 16.711 1.00 41.20 A ATOM 1712 CD ARG A 229 62.923 4.350 17.224 1.00 40.43 A

ATOM 1713 NE ARG A 229 63.616 5.639 17.075 1.00 41.57 A

ATOM 1714 CZ ARG A 229 64.884 5.861 17.439 1.00 40.59 A ATOM 1715 NH1 ARG A 229 65.604 4.875 17.982 1.00 39.90 A

ATOM 1716 NH2 ARG A 229 65.441 7.060 17.245 1.00 38.59 A

ATOM 1717 C ARG A 229 59.927 6.835 16.076 1.0043.60 A

ATOM 1718 O ARG A 229 61.020 7.381 16.389 1.00 44.29 A

ATOM 1719 OXT ARG A 229 59.290 7.088 15.018 1.00 44.84 A

ATOM 1720 OH2 WAT W 1 69.448 -25.156 14.038 1.00 19.25 W

ATOM 1721 OH2 WAT W 2 51.629 -9.080 14.253 1.00 19.44 W

ATOM 1722 OH2 WAT W 3 35.094 -2.771 18.279 1.00 19.45 W

ATOM 1723 OH2 WAT W 4 33.976 -26.705 18.662 1.00 17.10 W

ATOM 1724 OH2 WAT W 5 52.813 -12.455 14.557 1.00 16.38 W

ATOM 1725 OH2 WAT W 6 53.187 -8.229 20.463 1.00 19.20 W

ATOM 1726 OH2 WAT W 7 49.268 -3.449 17.985 1.00 22.05 W

ATOM 1727 OH2 WAT W 8 46.964 -3.745 15.057 1.00 21.55 W

ATOM 1728 OH2 WAT W 9 44.646 -8.817 36.606 1.00 23.99 W

ATOM 1729 OH2 WAT W 10 30.477 -29.293 23.227 1.00 23.15 W

ATOM 1730 OH2 WAT W 11 34.173 -22.952 10.668 1.00 24.71 W

ATOM 1731 OH2 WAT W 12 53.670 -7.692 15.168 1.0022.43 W

ATOM 1732 OH2 WAT W 13 32.609 -24.270 18.778 1.00 21.27 W

ATOM 1733 OH2 WAT W 14 63.052 -22.277 10.587 1.00 33.72 W

ATOM 1734 OH2 WAT W 15 65.031 -17.416 16.052 1.00 25.01 W

ATOM 1735 OH2 WAT W 16 32.872 -.430 19.340 1.00 25.07 W

ATOM 1736 OH2 WAT W 17 53.296 -27.934 26.071 1.00 23.84 W

ATOM 1737 OH2 WAT W 18 58.482 -12.425 22.987 1.00 28.79 W

ATOM 1738 OH2 WAT W 19 48.329 -3.258 11.821 1.00 29.93 W

ATOM 1739 OH2 WAT W 20 37.906 -13.579 7.975 1.00 24.45 W

ATOM 1740 OH2 WAT W 21 52.857 -31.323 22.008 1.0026.31 W

ATOM 1741 OH2 WAT W 22 64.836 -31.087 20.394 1.00 29.98 W

ATOM 1742 OH2 WAT W 23 31.920 -28.284 25.506 1.00 28.02 W

ATOM 1743 OH2 WAT W 24 57.175 -25.382 8.480 1.00 30.36 W

ATOM 1744 OH2 WAT W 25 60.385 -22.881 10.307 1.00 31.03 w

ATOM 1745 OH2 WAT W 26 28.837 -17.540 27.739 1.0028.41 w

ATOM 1746 OH2 WAT W 27 36.224 -10.019 37.482 1.00 33.45 w

ATOM 1747 OH2 WAT W 28 40.247 -12.011 8.115 1.00 25.12 >w

ATOM 1748 OH2 WAT W 29 57.911 -14.191 10.103 1.00 27.69 w

ATOM 1749 OH2 WAT W 30 56.765 -10.849 33.082 1.00 24.56 w

ATOM 1750 OH2 WAT W 31 42.902 -7.474 10.867 1.00 26.36 w

ATOM 1751 OH2 WAT W 32 46.979 -2.034 19.107 1.00 31.70 w

ATOM 1752 OH2 WAT W 33 32.230 -6.221 32.176 1.00 36.61 w

ATOM 1753 OH2 WAT W 34 45.253 -18.307 6.591 1.00 32.11 w

ATOM 1754 OH2 WAT W 35 62.705 -9.347 19.162 1.00 30.56 w

ATOM 1755 OH2 WAT W 36 40.108 -1.214 17.645 1.00 26.43 w

ATOM 1756 OH2 WAT W 37 55.363 -18.633 23.017 1.00 28.90 w

ATOM 1757 OH2 WAT W 38 46.034 -4.757 39.584 1.00 32.73 w

ATOM 1758 OH2 WAT W 39 47.165 -8.807 37.988 1.00 26.93 w

ATOM 1759 OH2 WAT W 40 33.578 -17.230 13.377 1.0024.83 w

ATOM 1760 OH2 WAT W 41 39.144 -3.601 38.556 1.00 28.45 w

ATOM 1761 OH2 WAT W 42 62.456 -.794 28.993 1.00 34.38 w

ATOM 1762 OH2 WAT W 43 71.052 -22.967 11.198 1.00 26.39 w

ATOM 1763 OH2 WAT W 44 48.533 -22.257 7.819 1.00 40.61 w

ATOM 1764 OH2 WAT W 45 58.944 -11.053 10.727 1.00 33.19 w

ATOM 1765 OH2 WAT W 46 30.123 -6.475 16.324 1.00 43.29 w

ATOM 1766 OH2 WAT W 47 34.004 -17.324 33.764 1.00 35.82 w

ATOM 1767 OH2 WAT W 48 44.071 -31.670 13.539 1.00 35.88 w

ATOM 1768 OH2 WAT W 49 30.210 -17.690 15.712 1.00 33.61 w

ATOM 1769 OH2 WAT W 50 65.239 -3.633 24.753 1.00 33.85 w

ATOM 1770 OH2 WAT W 51 70.276 -33.334 25.730 1.0040.63 w

ATOM 1771 OH2 WAT W 52 76.400 -36.099 20.668 1.00 45.57 w ATOM 1772 OH2 WAT W 53 35.088 2.210 26.432 1 .00 39.60 W

ATOM 1773 OH2 WAT W 54 48.956 ^■ -22.613 32.043 1.00 33.99 W

ATOM 1774 OH2 WAT W 55 35.005 -31.090 21 .279 1 .00 36.47 W

ATOM 1775 OH2 WAT W 56 51.619 -18.908 6.646 1 .00 32.67 W

ATOM 1776 OH2 WAT W 57 70.171 -13.596 17.282 1 .00 37.33 W

ATOM 1777 OH2 WAT W 58 41.071 1.986 25.759 1.00 35.25 W

ATOM 1778 OH2 WAT W 59 41.954 - -36.091 16.951 1 .00 38.23 W

ATOM 1779 OH2 WAT W 60 38.880 -.276 19.849 1.00 33.93 W

ATOM 1780 OH2 WAT W 61 48.770 -34.232 18.536 1 .00 28.36 W

ATOM 1781 OH2 WAT W 62 27.373 -13.659 11.856 1.00 44.81 W

ATOM 1782 OH2 WAT W 63 67.113 -32.058 15.222 1.00 35.19 W

ATOM 1783 OH2 WAT W 64 36.028 -26.826 32.399 1.00 44.47 W

ATOM 1784 OH2 WAT W 65 27.443 -22.432 24.743 1.00 45.82 W

ATOM 1785 OH2 WAT W 66 46.041 -22.664 27.737 1.00 39.93 W

ATOM 1786 OH2 WAT W 67 48.911 -4.662 9.464 1.00 40.99 W

ATOM 1787 OH2 WAT W 68 62.896 -30.845 10.163 1.00 47.19 W

ATOM 1788 OH2 WAT W 69 38.979 -21.653 35.297 1.00 34.19 W

ATOM 1789 OH2 WAT W 70 30.860 -10.334 10.875 1.00 45.08 W

ATOM 1790 OH2 WAT W 71 61.598 2.792 22.912 1 .00 30.93 W

ATOM 1791 OH2 WAT W 72 70.989 -28.099 30.502 1.00 35.60 W

ATOM 1792 OH2 WAT W 73 41.470 -4.255 10.603 1.00 38.04 W

ATOM 1793 OH2 WAT W 74 60.498 -4.583 13.363 1.00 36.79 W

ATOM 1794 OH2 WAT W 75 25.770 ^■ -16.859 14.722 1.00 41.59 W

ATOM 1795 OH2 WAT W 76 38.461 -8.889 40.013 1 .00 45.19 W

ATOM 1796 OH2 WAT W 77 35.499 ^■ -25.365 10.662 1 .00 33.83 W

ATOM 1797 OH2 WAT W 78 43.480 .173 44.832 1.00 42.02 w

ATOM 1798 OH2 WAT W 79 31.524 -3.075 29.751 1 .00 35.54 w

ATOM 1799 OH2 WAT W 80 45.075 4.120 30.144 1.00 38.37 w

ATOM 1800 OH2 WAT W 81 48.180 .505 19.595 1.00 35.81 w

ATOM 1801 OH2 WAT W 82 29.171 -6.346 18.717 1.00 28.48 w

ATOM 1802 OH2 WAT W 83 53.483 -2.873 16.260 1.00 43.90 w

ATOM 1803 OH2 WAT W 84 35.821 ^■ -28.944 14.638 1 .00 35.73 w

ATOM 1804 OH2 WAT W 85 40.906 ^■ -36.893 20.980 1.00 35.50 w

ATOM 1805 OH2 WAT W 86 59.031 -8.257 12.538 1.00 35.32 w

ATOM 1806 OH2 WAT W 87 45.069 -4.274 41.958 1.00 42.19 w

ATOM 1807 OH2 WAT W 88 33.935 -26.360 8.450 1.00 46.56 w

ATOM 1808 OH2 WAT W 89 50.726 -19.821 34.058 1.00 34.18 w

ATOM 1809 OH2 WAT W 90 30.250 -14.642 21.689 1.00 46.63 w

ATOM 1810 OH2 WAT W 91 43.569 -20.524 5.629 1.00 41 .80 w

ATOM 181 1 OH2 WAT W 92 43.598 4.858 27.547 1 .00 48.67 w

ATOM 1812 OH2 WAT W 93 70.776 -30.681 13.045 1.00 39.65 w

ATOM 1813 OH2 WAT W 94 61.250 -9.574 23.706 1.00 53.54 w

ATOM 1814 OH2 WAT W 95 42.048 -26.632 3.893 1.00 44.43 w

ATOM 1815 OH2 WAT W 96 73.449 ^■ -35.614 21.545 1.00 43.76 w

ATOM 1816 OH2 WAT W 97 50.473 ^■ -31.183 24.728 1.00 35.59 w

ATOM 1817 OH2 WAT W 98 55.802 5.390 25.935 1.00 41.22 w

ATOM 1818 OH2 WAT W 99 34.348 .839 36.171 1.00 45.05 w

ATOM 1819 OH2 WAT W 100 46.884 -17.753 22.952 1.00 35.80 w

ATOM 1820 OH2 WAT W 101 26.922 -14.1 17 27.132 1.00 48.51 w

ATOM 1821 OH2 WAT W 102 53.597 .015 13.685 1.00 46.00 w

ATOM 1822 OH2 WAT W 103 29.284 .348 31.420 1.00 47.14 w

ATOM 1823 OH2 WAT W 104 48.259 4.708 29.823 1.00 41.93 w

ATOM 1824 OH2 WAT W 105 38.149 -1.183 12.378 1 .00 49.01 w

ATOM 1825 OH2 WAT W 106 49.201 -17.271 4.613 1 .00 45.33 w

ATOM 1826 OH2 WAT W 107 49.073 1.385 38.522 1.00 52.18 w

ATOM 1827 OH2 WAT W 108 43.631 -37.270 24.443 1.00 45.09 w

ATOM 1828 OH2 WAT W 109 29.607 -21.946 27.582 1.00 54.17 w ATOM 1829 OH2WATW110 43.992 4.341 34.902 1.0040.51 W

ATOM 1830 OH2 WAT W 111 69.856 -15.066 13.446 1.0047.79 W

ATOM 1831 OH2WATW112 42.488 -17.308 40.806 1.0048.50 W

ATOM 1832 OH2WATW113 44.339 1.922 36.321 1.0043.77 W

ATOM 1833 OH2WATW114 29.531 -8.002 25.167 1.0047.17 W

ATOM 1834 OH2WATW115 50.410 -27.360 32.747 1.0038.17 W

ATOM 1835 OH2WATW116 72.814 -25.951 33.355 1.0044.83 W

ATOM 1836 OH2WATW117 45.342 -9.204 42.273 1.0045.61 W

ATOM 1837 OH2WATW118 68.809 -26.532 9.279 1.0052.23 W

ATOM 1838 OH2WATW119 57.553 -16.365 29.345 1.0053.39 W

ATOM 1839 OH2WATW120 33.819 -4.277 32.940 1.0044.22 W

ATOM 1840 OH2WATW121 41.602 -28.871 9.657 1.0052.21 W

ATOM 1841 OH2WATW122 76.991 -34.057 30.451 1.0051.83 W

ATOM 1842 OH2WATW123 35.454 -23.777 36.483 1.0044.51 W

ATOM 1843 OH2WATW124 35.956 -3.455 13.747 1.0020.11 W

ATOM 1844 OH2WATW125 26.420 -24.149 18.076 1.0021.34 W

ATOM 1845 OH2WATW126 35.334 -5.667 15.906 1.0017.94 W

ATOM 1846 OH2WATW127 51.836 -17.626 32.782 1.0029.22 W

ATOM 1847 OH2WATW128 75.887 -33.979 16.553 1.0034.80 W

ATOM 1848 OH2WATW129 34.342 -2.331 11.862 1.0028.03 W

ATOM 1849 OH2WATW130 36.621 -1.176 16.079 1.0024.77 W

ATOM 1850 OH2WATW131 28.212 -4.740 21.363 1.0027.12 W

ATOM 1851 OH2WATW132 45.780 -1.666 16.693 1.0033.94 W

ATOM 1852 OH2WATW133 61.756 -15.215 13.972 1.0036.57 w

ATOM 1853 OH2WATW134 70.339 -25.918 11.680 1.0041.19 w

ATOM 1854 OH2WATW135 35.992 -1.863 9.266 1.0042.97 w

ATOM 1855 OH2WATW136 50.974 -34.015 23.709 1.0036.59 w

ATOM 1856 OH2WATW137 52.968 -30.322 24.594 1.0033.07 w

ATOM 1857 OH2WATW138 32.457 -22.711 29.325 1.0041.34 w

ATOM 1858 OH2WATW139 52.360 -18.647 22.969 1.0040.41 w

ATOM 1859 OH2WATW140 40.111 -10.431 6.148 1.0039.66 w

ATOM 1860 OH2WATW141 50.498 -10.197 33.090 1.0027.16 w

ATOM 1861 OH2WATW142 41.341 -6.537 8.677 1.0038.44 w

ATOM 1862 OH2WATW143 71.957 -35.628 25.409 1.0045.01 w

ATOM 1863 OH2WATW144 46.276 7.530 23.751 1.0035.30 w

ATOM 1864 OH2WATW145 52.457 -16.102 24.301 1.0035.80 w

ATOM 1865 OH2WATW146 65.653 1.880 25.790 1.0045.54 w

ATOM 1866 OH2WATW147 60.922 1.944 29.217 1.0042.43 w

ATOM 1867 OH2WATW148 33.963 -31.564 17.274 1.0042.53 w

ATOM 1868 OH2WATW149 71.503 -28.467 11.200 1.0047.55 w

ATOM 1869 OH2WATW150 22.889 -23.504 23.317 1.0046.29 w

ATOM 1870 OH2WATW151 61.185 -24.301 7.822 1.0048.60 w

ATOM 1871 OH2WATW152 46.876 -7.023 40.154 1.0035.08 w

ATOM 1872 OH2WATW153 46.438 3.775 32.997 1.0040.75 w

ATOM 1873 OH2WATW154 64.718 -32.295 25.408 1.0042.98 w

ATOM 1874 OH2WATW155 42.473 -39.610 18.372 1.0046.94 w

ATOM 1875 OH2WATW156 69.222 -29.469 29.868 1.0040.57 w

ATOM 1876 OH2WATW157 34.446 -16.952 21.371 1.0038.02 w

ATOM 1877 OH2WATW158 34.991 -18.870 36.219 1.0043.38 w

ATOM 1878 OH2WATW159 27.403 -10.163 12.857 1.0043.36 w

ATOM 1879 OH2WATW160 50.552 -2.554 15.092 1.0043.22 w

ATOM 1880 OH2WATW161 36.848 -4.712 37.819 1.0038.63 w

ATOM 1881 OH2WATW162 47.421 -19.832 6.445 1.0034.37 w

ATOM 1882 OH2WATW163 52.088 -13.745 37.632 1.0038.45 w

ATOM 1883 OH2WATW164 39.009 .40641.089 ' 1.0045.81 w

ATOM 1884 OH2WATW165 38.735 -5.971 7.602 1.0044.46 w

ATOM 1885 OH2WATW166 43.315 -38.052 16.613 1.0031.70 w ATOM 1886 OH2WATW167 28.029 -15.136 30.655 1.0046.08 W

ATOM 1887 OH2WATW168 52.118 -18.161 30.268 1.0034.55 W

ATOM 1888 OH2WATW169 54.611 -15.578 39.069 1.0049.12 W

ATOM 1889 OH2WATW170 47.011 1.112 36.528 1.0039.43 W ATOM 1890 OH2WATW171 66.939 -32.091 20.971 1.0052.76 W

ATOM 1891 OH2WATW172 54.817 -6.405 36.064 1.0039.35 W

ATOM 1892 OH2 WAT W 173 35.310 -3.699 36.035 1.0043.30 W

ATOM 1893 OH2WATW174 44.315 -39.693 32.948 1.0048.37 W

ATOM 1894 OH2WATW175 59.742 -16.330 6.340 1.0046.29 W ATOM 1895 OH2WATW176 39.508 -19.813 37.366 1.0048.68 W

ATOM 1896 OH2WATW177 47.206 7.430 31.997 1.0055.90 W

ATOM 1897 OH2WATW178 57.228 2.950 27.978 1.0050.55 W

ATOM 1898 OH2 WAT W 179 71.642 -18.769 10.660 1.0044.57 W

ATOM 1899 OH2 WAT W 180 37.162 -15.558 41.938 1.0042.54 W ATOM 1900 OH2 WAT W 181 30.882 -7.180 10.669 1.0039.77 W

ATOM 1901 OH2WATW182 37.267 -36.743 34.407 1.0047.56 W

ATOM 1902 OH2WATW183 49.384 -36.706 21.424 1.0046.44 W

ATOM 1903 OH2WATW184 53.237 -11.013 8.153 1.0046.36 W

ATOM 1904 OH2WATW185 70.954 -24.207 35.281 1.0048.28 W ATOM 1905 OH2WATW186 66.735 -35.337 14.211 1.0049.52 W

ATOM 1906 OH2WATW187 37.554 -15.247 5.842 1.0043.58 W

ATOM 1907 OH2WATW188 54.383 -18.359 5.274 1.0040.83 W

ATOM 1908 OH2 WAT W 189 31.174 -11.621 33.508 1.0042.08 w

ATOM 1909 OH2WATW190 61.773 -11.468 17.554 1.0039.47 w ATOM 1910 OH2WATW191 50.934 2.770 33.359 1.0050.16 w

ATOM 1911 OH2WATW192 56.642 1.618 12.516 1.0050.38 w

ATOM 1912 OH2WATW193 45.142 -14.488 41.340 1.0046.57 w

ATOM 1913 OH2WATW194 50.164 -11.058 6.895 1.0044.72 w

ATOM 1914 OH2WATW195 44.049 -23.801 1.940 1.0056.77 w ATOM 1915 OH2WATW196 30.026 -21.121 32.514 1.0050.64 w

ATOM 1916 OH2WATW197 79.798 -34.870 27.305 1.0050.13 w

ATOM 1917 OH2WATW198 37.302 -31.443 15.126 1.0046.26 w

ATOM 1918 OH2WATW199 68.876 -15.087 19.694 1.0048.70 w

ATOM 1919 OH2WATW200 65.534 -6.053 23.933 1.0056.28 w ATOM 1920 OH2WATW201 46.408 1.708 46.434 1.0050.11 w

ATOM 1921 OH2WATW202 54.541 -12.954 41.868 1.0044.25 w

ATOM 1922 OH2WATW203 38.264 -34.103 25.307 1.0044.15 w

ATOM 1923 OH2WATW204 39.636 -18.372 -.362 1.0050.52 w

ATOM 1924 OH2WATW205 55.146 6.711 14.832 1.0045.80 w ATOM 1925 OH2WATW206 58.491 -5.32242.521 1.0048.34 w

ATOM 1926 OH2WATW207 54.006 -36.570 31.956 1.0043.54 w

ATOM 1927 OH2WATW208 36.814 -20.783 1.406 1.0047.70 w

ATOM 1928 OH2WATW209 49.487 -8.123 41.799 1.0058.41 w

ATOM 1929 OH2WATW210 51.485 .847 40.395 1.0049.26 w ATOM 1930 OH2WATW211 34.265 -15.199 40.327 1.0055.47 w

ATOM 1931 OH2WATW212 26.486 -14.582 34.221 1.0050.72 w

ATOM 1932 OH2WATW213 66.916 -10.088 31.137 1.0047.49 w

ATOM 1933 OH2WATW214 61.880 -8.393 13.804 1.0048.18 w

ATOM 1934 OH2WATW215 52.178 -17.094 27.375 1.0045.11 w ATOM 1935 OH2WATW216 49.521 -18.66724.459 1.0049.30 w

ATOM 1936 OH2WATW217 53.886 -17.906 35.573 1.0055.93 w

ATOM 1937 OH2WATW218 55.084 -18.233 33.255 1.0039.30 w

ATOM 1938 OH2WATW219 28.371 -16.056 13.349 1.0031.78 w

ATOM 1939 OH2WATW220 32.932 -14.472 37.055 1.0042.97 w ATOM 1940 OH2WATW221 39.410 -34.086 22.291 1.0037.76 w

ATOM 1941 OH2WATW222 33.275 -22.371 26.097 1.0035.53 w

ATOM 1942 OH2WATW223 26.542 -20.324 17.962 1.0032.09 w ATOM 1943 OH2WATW224 48.390 -21.762 29.306 1.0034.05 W

ATOM 1944 OH2WATW225 60.310 -20.076 6.547 1.0037.28 W

ATOM 1945 OH2WATW226 43.094 .669 17.220 1.0033.70 W

ATOM 1946 OH2WATW227 73.860 -35.372 31.469 1.0037.49 W ATOM 1947 OH2WATW228 68.956 -33.959 11.475 1.0036.68 W

ATOM 1948 OH2WATW229 23.816 -21.242 21.882 1.0036.45 W

ATOM 1949 OH2WATW230 27.318 -15.732 17.360 1.0038.35 W

ATOM 1950 OH2WATW231 39.409 -22.802 .775 1.0036.89 W

ATOM 1951 OH2WATW232 58.232 -18.569 34.405 1.0039.91 W ATOM 1952 OH2WATW233 68.355 -28.762 32.730 1.0037.69 W

ATOM 1953 OH2WATW234 55.936 -37.730 30.398 1.0039.68 W

ATOM 1954 OH2WATW235 45.260 -25.648 37.188 1.0036.59 W

ATOM 1955 OH2WATW236 75.374 -33.981 34.034 1.0037.73 W

ATOM 1956 OH2WATW237 52.239 -34.063 32.671 1.0037.84 W ATOM 1957 OH2WATW238 51.841 -21.005 30.156 1.0037.29 W

ATOM 1958 OH2WATW239 82.007 -35.370 28.582 1.0037.20 W

ATOM 1959 OH2WATW240 63.489 -10.399 34.778 1.0038.65 W

ATOM 1960 OH2WATW241 45.527 3.090 19.799 1.0035.95 W

ATOM 1961 OH2WATW242 62.245 -33.868 26.786 1.0038.85 W ATOM 1962 OH2WATW243 52.342 -32.049 35.064 1.0040.47 W

ATOM 1963 OH2WATW244 62.770 -7.476 38.022 1.0017.00 W

ATOM 1964 OH2WATW245 31.655 -8.160 32.543 1.0033.60 W

ATOM 1965 OH2WATW246 50.142 -9.332 30.522 1.0028.82 W

ATOM 1966 OH2WATW247 45.439 -28.519 10.822 1.0033.23 W ATOM 1967 OH2WATW248 40.072 -16.759 40.869 1.0033.87 W

ATOM 1968 OH2WATW249 52.184 -16.062 36.269 1.0037.48 W

ATOM 1969 OH2WATW250 61.003 -15.817 11.647 1.0036.41 W

ATOM 1970 OH2WATW251 36.495 -22.153 34.743 1.0036.46 W

ATOM 1971 OH2WATW252 76.770 -34.127 18.874 1.0034.34 W ATOM 1972 OH2WATW253 62.770 -12.201 38.022 1.0017.00 W

ATOM 1973 OH2WATW254 50.484 -31.854 26.997 1.0036.81 W

ATOM 1974 OH2WATW255 58.581 -12.809 18.088 1.0039.04 W

ATOM 1975 OH2WATW256 32.594 -8.771 9.643 1.0036.26 W

ATOM 1976 OH2WATW257 51.336 -4.634 9.213 1.0034.53 W ATOM 1977 OH2WATW258 35.798 -7.331 37.946 1.0037.03 W

ATOM 1978 OH2WATW259 35.260 -23.001 30.377 1.0033.67 W

ATOM 1979 OH2WATW260 34.896 -13.902 37.589 1.0039.31 W

ATOM 1980 OH2WATW261 42.162 -40.928 20.985 1.0037.46 W

ATOM 1981 OH2WATW262 36.322 -11.110 7.752 1.0036.11 W ATOM 1982 OH2WATW263 61.892 -10.371 21.398 1.0036.91 W

ATOM 1983 OH2WATW264 47.802 2.206 34.276 1.0036.71 W

ATOM 1984 OH2WATW265 52.001 -.402 12.062 1.0036.46 W

ATOM 1985 OH2WATW266 40.513 -23.612 36.250 1.0037.12 W

ATOM 1986 OH2WATW267 67.809 -18.565 9.806 1.0037.96 W ATOM 1987 OH2WATW268 26.113 -15.588 12.746 1.0037.09 W

ATOM 1988 OH2WATW269 61.053 -12.542 21.269 1.0037.13 W

ATOM 1989 OH2WATW270 43.529 -27.397 9.657 1.0034.48 W

ATOM 1990 OH2WATW271 43.736 -24.233 6.927 1.0033.17 W

ATOM 1991 OH2WATW272 42.219 -2.100 11.107 1.0039.63 W ATOM 1992 OH2WATW273 43.467 2.251 39.320 1.0037.05 W

ATOM 1993 OH2WATW274 51.766 -33.764 28.769 1.0035.16 W

ATOM 1994 OH2WATW275 29.480 -13.446 29.674 1.0038.86 W

ATOM 1995 OH2WATW276 31.438 -15.875 33.929 1.0035.54 W

ATOM 1996 OH2WATW277 34.840 3.87531.200 1.0037.50 W ATOM 1997 OH2WATW278 45.787 -14.113 39.075 1.0040.19 W

ATOM 1998 OH2WATW279 40.321 -35.999 23.191 1.0039.97 W

ATOM 1999 OH2WATW280 51.237 -19.654 26.273 1.0034.90 W ATOM 2000 OH2WATW281 54.804 -.729 11.647 1.0038.99 W

ATOM 2001 OH2WATW282 47.778-29.403 33.616 1.0035.73 W

ATOM 2002 OH2WATW283 66.355-33.697 24.644 1.0037.66 W

ATOM 2003 OH2WATW284 71.418-27.396 8.830 1.0037.88 W ATOM 2004 OH2WATW285 39.188 -8.324 7.787 1.0037.51 W

ATOM 2005 OH2WATW286 27.966-22.317 19.638 1.0031.50 W

ATOM 2006 OH2WATW287 59.662 -3.852 9.894 1.0035.74 W

ATOM 2007 OH2 WAT W 288 34.463-30.80028.613 1.0033.15 W

ATOM 2008 OH2WATW289 45.611 -39.424 19.799 1.0039.36 W ATOM 2009 OH2WATW290 50.384-38.201 29.658 1.0036.52 W

ATOM 2010 OH2WATW291 59.847 4.646 11.852 1.0038.17 W

ATOM 2011 OH2WATW292 49.189 5.51822.494 1.0034.19 W

ATOM 2012 OH2WATW293 46.776 4.104 39.072 1.0038.69 W

ATOM 2013 OH2WATW294 26.962-14.646 22.181 1.0037.33 W ATOM 2014 OH2WATW295 37.661 -3.844 8.058 1.0036.35 W

ATOM 2015 OH2WATW296 46.623-30.625 9.429 1.0038.96 W

ATOM 2016 OH2WATW297 61.594-12.343 26.315 1.0036.48 W

ATOM 2017 OH2WATW298 67.747-28.627 35.305 1.0037.90 W

ATOM 2018 OH2WATW299 33.799 -2.015 36.646 1.0036.15 W ATOM 2019 OH2WATW300 67.746-14.88521.797 1.0036.04 W

ATOM 2020 OH2WATW301 58.854 8.524 12.900 1.0038.09 W

ATOM 2021 OH2WATW302 32.978 -3.974 8.453 1.0033.93 W

ATOM 2022 OH2WATW303 63.322-10.751 15.598 1.0033.79 W

ATOM 2023 OH2WATW304 44.768 5.928 36.747 1.0038.29 W ATOM 2024 OH2 WAT W 305 49.391 -36.589 23.806 1.0037.09 W

ATOM 2025 OH2WATW306 64.421 -35.095 16.907 1.0035.24 W

ATOM 2026 OH2WATW307 53.513 6.511 28.897 1.0039.31 W

ATOM 2027 OH2WATW308 68.782 -5.972 28.982 1.0038.08 W

ATOM 2028 OH2WATW309 31.389-24.047 27.685 1.0035.97 W ATOM 2029 OH2WATW310 78.419-34.694 34.315 1.0039.67 W

ATOM 2030 OH2WATW311 38.578 -6.45240.994 1.0037.44 W

ATOM 2031 OH2WATW312 22.842-16.703 15.039 1.0037.09 W

ATOM 2032 OH2WATW313 60.802-32.616 10.210 1.0034.91 W

ATOM 2033 OH2WATW314 57.183-16.736 35.580 1.0033.74 W ATOM 2034 OH2WATW315 45.641 -3.90644.243 1.0040.89 W

ATOM 2035 OH2WATW316 71.745-33.932 14.736 1.0038.44 W

ATOM 2036 OH2WATW317 55.459-34.280 32.056 1.0039.08 W

ATOM 2037 OH2WATW318 32.848 -5.963 36.209 1.0035.86 W

ATOM 2038 OH2 WAT W 319 52.516-14.14740.227 1.0039.85 W ATOM 2039 OH2WATW320 73.383-35.309 16.496 1.0035.71 W

ATOM 2040 OH2WATW321 44.817-27.535 6.162 1.0040.86 W

ATOM 2041 OH2WATW322 42.999-20.760 1.675 1.0036.03 W

ATOM 2042 OH2 WAT W 323 57.370 -7.78242.721 1.0037.02 W

ATOM 2043 OH2WATW324 33.548-10.260 36.904 1.0037.56 W ATOM 2044 OH2WATW325 66.504-14.765 18.547 1.0040.28 W

ATOM 2045 OH2WATW326 64.126-15.395-18.074 1.0035.23 W

ATOM 2046 OH2WATW327 77.176-37.936 23.428 1.0038.41 W

ATOM 2047 OH2WATW328 80.622-32.273 34.010 1.0039.04 W

ATOM 2048 N1 CTP T 1 48.100-14.923 32.848 1.0025.48 T ATOM 2049 C2 CTP T 1 46.837-15.097 33.378 1.0026.99 T

ATOM 2050 N3 CTP T 1 46.607-15.831 34.480 1.0027.82 T

ATOM 2051 C4 CTP T 1 47.659-16.454 35.121 1.0029.02 T

ATOM 2052 C5 CTP T 1 48.972-16.329 34.645 1.0027.87 T

ATOM 2053 C6 CTP T 1 49.140-15.556 33.504 1.0029.45 T ATOM 2054 02 CTP T 1 45.826-14.571 32.865 1.0023.95 T

ATOM 2055 N4 CTP T 1 47.371 -17.178 36.218 1.0026.76 T

ATOM 2056 C1*CTPT 1 48.318-14.103 31.612 1.0026.60 T ATOM 2057 C2* CTP T 1 49.212-12.919 31.883 1.0024.63 T ATOM 2058 02* CTP T 1 48.509-11.86532.543 1.0026.02 T ATOM 2059 C3* CTP T 1 49.729-12.600 30.509 1.0027.12 T ATOM 2060 C4* CTP T 1 49.682-13.91729.722 1.0028.21 T ATOM 2061 04* CTP T 1 49.060-14.83730.665 1.0026.00 T ATOM 2062 03* CTP T 1 48.907-11.720 29.762 1.0024.59 T ^* ATOM 2063 C5* CTP T 1 51.145-14.101 29.547 1.0033.59 T ATOM 2064 05* CTP T 1 51.687-15.046 30.419 1.0036.44 T ATOM 2065 PA CTPT 1 53.060-14.696 31.313 1.0038.24 T ATOM 2066 OIACTPT 1 53.690-13.420 30.710 1.0040.22 T ATOM 2067 02A CTP T 1 53.998-15.908 31.123 1.0041.49 T ATOM 2068 03A CTP T 1 52.578-14.60532.919 1.0042.18 T ATOM 2069 PB CTPT 1 I 52.743-13.27833.891 1.0035.17 T ATOM 2070 01 B CTPT 1 52.149-13.768 35.226 1.0043.39 T ATOM 2071 02B CTP T 1 51.920-12.092 33.338 1.0043.09 T ATOM 2072 03B CTP T 1 54.360-12.876 34.128 1.0033.74 T ATOM 2073 PG CTPT 1 55.354-13.686 35.212 1.0028.19 T ATOM 2074 OIGCTPT 1 54.735-13.510 36.647 1.0030.67 T ATOM 2075 02G CTP T 1 56.741 -12.988 35.065 1.0028.63 T ATOM 2076 03G CTP T 1 55.358-15.171 34.773 1.0028.76 T ATOM 2077 CA+2 CA2 C 1 35.514 -3.246 16.059 1.0016.73 C ATOM 2078 MG+2MG2M 1 53.667-16.446 33.965 1.0020.91 M END

APPENDIX 3

X-RAY DATA COORDINATES FOR CDP-ME SYNTHASE COMPLEXED WITH CDP-ME «Mg2⁺ REMARK coordinates from minimization and B-factor refinement

REMARK refinement resolution: 90 - 1.82 A

REMARK starting r= .2368 free_r= .2626

REMARK final r= .2214 free_r= .2743

REMARK rmsd bonds= .008991 rmsd angles= 1.35025 REMARK B rmsd for bonded mainchain atoms= 3.296 target= 1.5

REMARK B rmsd for bonded sidechain atoms= 4.641 target= 2.0

REMARK B rmsd for angle mainchain atoms= 4.298 target= 2.0

REMARK B rmsd for angle sidechain atoms= 5.838 target= 2.5

REMARK target= mlf final wa= 2.46162 REMARK final rweight= .0200 (with wa= 2.46162)

REMARK md-method= torsion annealing schedule= constant

REMARK starting temperature= 2000 total md steps= 1 * 100

REMARK cydes= 2 coordinate steps= 20 B-factor steps= 10

REMARK sg= C2 a= 129.990 b= 46.764 c= 38.387 alpha= 90 beta= 92.638 gamma= 90 REMARK topology file 1 : CNS_TOPPAR:protein.top

REMARK topology file 2 : CNS_TOPPAR:dna-ma.top

REMARK topology file 3 : CNS_TOPPAR:water.top

REMARK topology file 4 : CNS_TOPPAR:ion.top

REMARK topology file 5 : CNSPAR:prd2.top REMARK parameter file 1 : CNS_TOPPAR:protein_rep.param

REMARK parameter file 2 : CNS_TOPPAR:dna-rna_rep.param

REMARK parameter file 3 : CNS_TOPPAR:water_rep.param

REMARK parameter file 4 : CNS_TOPPAR:ion.param

REMARK parameter file 5 : CNSPAR:prd2.param REMARK molecular structure file: generate. mtf

REMARK input coordinates: generate. pdb

REMARK reflection file= ygbp_cdpme03_freer.xpl

REMARK ncs= none

REMARK B-correction resolution: 6.0 - 1.82 REMARK initial B-factor correction applied to fobs :

REMARK B11 = 7.881 B22= -4.981 B33= -2.899

REMARK B12= .000 B13= 1.914 B23= .000

REMARK B-factor correction applied to coordinate array B: .411

REMARK bulk solvent: density level= .368214 e/A^Λ3, B-factor= 44.6998 A^Λ2 REMARK reflections with |Fobs|/sigma_F < 0.0 rejected

REMARK reflections with JFobsj > 10000 * rms(Fobs) rejected

REMARK theoretical total number of refl. in resol. range: 20834 ( 100.0 % )

REMARK number of unobserved reflections (no entry or |F|=0): 3690 ( 17.7 % )

REMARK number of reflections rejected: 0 ( .0 % ) REMARK total number of reflections used: 17144 ( 82.3 % )

REMARK number of reflections in working set: 16278 ( 78.1 % )

REMARK number of reflections in test set: 866 ( 4.2 % )

CRYST1 129.990 46.764 38.387 90.00 92.64 90.00 C 2

REMARK FILENAME="refine.pdb" REMARK DATE: 5-Apr-01 14:49:24 created by user: richard

REMARK VERSION:1.0

ATOM 1 CB THR A 4 25.657 -16.403 13.519 1.00 45.99 A

ATOM 2 OG1 THR A 4 25.992 -16.520 14.909 1.00 50.29 A

ATOM 3 CG2 THR A 4 25.422 -17.805 12.934 1.00 48.97 A A ATTOOMM 4 4 C C TTHHRR AA 44 28.030 -16.608 12.693 1.00 43.82 A ATOM 5 O THRA 4 28.821 -16.686 13.631 1.0038.41 ^•A

ATOM 6 N THRA 4 26.378-15.298 11.382 1.0047.34 A

ATOM 7 CA THRA 4 26.804-15.685 12.762 1.0046.78 A

ATOM 8 N HISA 5 28.189-17.300 11.570 1.0042.34 A

ATOM 9 CA HISA 5 29.324-18.199 11.378 1.0040.58 A

ATOM 10 CB HISA 5 29.235-18.845 9.996 1.0035.11 A

ATOM 11 CG HISA 5 30.545-19.342 9.473 1.0041.58 A

ATOM 12 CD2HISA 5 31.190-19.097 8.307 1.0044.21 A

ATOM 13 ND1 HISA 5 31.354-20.201 10.185 1.0047.30 A

ATOM 14 CE1 HISA 5 32.442-20.465 9.482 1.0047.54 A

ATOM 15 NE2HISA 5 32.367-19.807 8.339 1.0052.31 A

ATOM 16 C HISA 5 30.666-17.485 11.518 1.0038.26 A

ATOM 17 O HISA 5 31.631 -18.046 12.048 1.0038.36 A

ATOM 18 N LEU A 6 30.731 -16.250 11.036 1.0033.44 A

ATOM 19 CA LEU A 6 31.976-15.493 11.103 1.0033.00 A

ATOM 20 CB LEU A 6 32.007-14.428 9.997 1.0031.48 A

ATOM 21 CG LEU A 6 32.091 -14.960 8.559 1.0036.77 A

ATOM 22 CD1 LEU A 6 31.946-13.793 7.562 1.0041.82 A

ATOM 23 CD2LEUA 6 33.416-15.672 8.352 1.0034.18 A

ATOM 24 C LEU A 6 32.276-14.839 12.447 1.0028.86 A

ATOM 25 O LEU A 6 33.380-14.342 12.643 1.0027.45 A

ATOM 26 N ASPA 7 31.312-14.827 13.366 1.0029.60 A

ATOM 27 CA ASP A 7 31.525-14.200 14.685 1.0022.98 A

ATOM 28 CB ASPA 7 30.269-14.293 15.550 1.0030.56 A

ATOM 29 CG ASPA 7 29.205-13.300 15.138 1.0041.80 A

ATOM 30 OD1 ASP A 7 29.319-12.748 14.026 1.0036.86 A

ATOM 31 OD2ASPA 7 28.263-13.092 15.920 1.0042.70 A

ATOM 32 C ASPA 7 32.649-14.891 15.433 1.0017.00 A

ATOM 33 O ASPA 7 32.694-16.121 15.502 1.0023.97 A

ATOM 34 N VALA 8 33.520-14.084 16.019 1.0022.13 A

ATOM 35 CA VAL A 8 34.665-14.583 16.762 1.0019.66 A

ATOM 36 CB VALA 8 35.983-14.193 16.043 1.0018.02 A

ATOM 37 CG1 VAL A 8 37.203-14.600 16.879 1.0021.86 A

ATOM 38 CG2VALA 8 36.043-14.897 14.672 1.0029.40 A

ATOM 39 C VALA 8 34.683-14.027 18.168 1.0019.90 A

ATOM 40 O VALA 8 34.405-12.844 18.389 1.0024.28 A

ATOM 41 N CYSA 9 34.988-14.883 19.137 1.0019.63 A

ATOM 42 CA CYS A 9 35.090-14.392 20.509 1.0019.16 A

ATOM 43 CB CYSA 9 34.306-15.266 21.496 1.0021.92 A

ATOM 44 SG CYSA 9 34.497-14.61523.199 1.0029.21 A

ATOM 45 C CYSA 9 36.576-14.442 20.841 1.0019.88 A

ATOM 46 O CYSA 9 37.236-15.407 20.503 1.0021.87 A

ATOM 47 N ALAA 10 37.104-13.418 21.497 1.0018.71 A

ATOM 48 CA ALAA 10 38.526-13.40821.825 1.0016.26 A

ATOM 49 CB ALAA 10 39.148-12.071 21.408 1.0022.53 A

ATOM 50 C ALAA 10 38.705-13.620 23.321 1.0023.88 A

ATOM 51 O ALAA 10 37.860-13.203 24.128 1.0022.39 A

ATOM 52 N VALA 11 39.789-14.302 23.677 1.0018.67 A

ATOM 53 CA VAL A 11 40.116-14.540 25.062 1.0015.63 A

ATOM 54 CB VALA 11 40.143-16.043 25.390 1.0024.35 A

ATOM 55 CG1 VALA 11 40.647-16.25226.823 1.0022.63 A

ATOM 56 CG2VALA 11 38.744-16.62825.237 1.0025.61 A

ATOM 57 C VALA 11 41.514-13.964 25.272 1.0019.47 A

ATOM 58 O VALA 11 42.422-14.25024.505 1.0021.26 A

ATOM 59 N VALA 12 41.677-13.118 26.287 1.0018.88 A

ATOM 60 CA VALA 12 42.985-12.52726.565 1.0018.68 A

ATOM 61 CB VALA 12 42.948-10.97426.406 1.0016.69 A ATOM 62 CG1 VALA 12 44.224-10.33426.973 1.0018.29 A

ATOM 63 CG2VALA 12 42.763-10.619 24.953 1.0022.46 A

ATOM 64 C VALA 12 43.463-12.869 27.978 1.0023.85 A

ATOM 65 O VALA 12 42.954-12.337 28.967 1.0024.74 A

ATOM 66 N PROA 13 44.435-13.791 28.088 1.0020.81 A

ATOM 67 CD PROA 13 44.914-14.725 27.050 1.0014.87 A

ATOM 68 CA PROA 13 44.943-14.151 29.411 1.0026.70 A

ATOM 69 CB PROA 13 45.742-15.44029.144 1.0024.55 A

ATOM 70 CG PROA 13 46.156-15.336 27.688 1.0019.23 A

ATOM 71 C PROA 13 45.807-12.987 29.908 1.0023.46 A

ATOM 72 O PROA 13 46.808-12.638 29.285 1.0025.64 A

ATOM 73 N ALAA 14 45.389-12.376 31.009 1.0024.83 A

ATOM 74 CA ALAA 14 46.093-11.233 31.582 1.0027.83 A

ATOM 75 CB ALAA 14 45.403 -9.947 31.157 1.0028.84 A

ATOM 76 C ALAA 14 46.117-11.315 33.104 1.0029.28 A

ATOM 77 O ALAA 14 46.051-10.289 33.788 1.0029.13 A

ATOM 78 N ALAA 15 46.213-12.531 33.625 1.0027.61 A

ATOM 79 CA ALAA 15 46.203-12.745 35.064 1.0034.10 A

ATOM 80 CB ALAA 15 45.293-13.919 35.400 1.0032.07 A

ATOM 81 C ALAA 15 47.596-12.984 35.625 1.0037.58 A

ATOM 82 O ALAA 15 47.744-13.290 36.803 1.0045.94 A

ATOM 83 N GLYA 16 48.607-12.847 34.772 1.0037.57 A

ATOM 84 CA GLYA 16 49.973-13.043 35.208 1.0046.44 A

ATOM 85 C GLYA 16 50.445-11.930 36.127 1.0049.84 A

ATOM 86 O GLYA 16 50.105-10.759 35.935 1.0047.72 A

ATOM 87 N PHEA 17 51.218-12.306 37.142 1.0056.23 A

ATOM 88 CA PHEA 17 51.765-11.354 38.106 1.0062.35 A

ATOM 89 CB PHEA 17 52.025-12.057 39.442 1.0059.95 A

ATOM 90 CG PHEA 17 50.803-12.701 40.034 1.0063.20 A

ATOM 91 CD1 PHEA 17 50.921-13.63641.060 1.0062.21 A

ATOM 92 CD2PHEA 17 49.530-12.387 39.552 1.0061.71 A

ATOM 93 CE1 PHEA 17 49.796-14.25341.597 1.0062.78 A

ATOM 94 CE2PHEA 17 48.397-12.99740.082 1.0065.70 A

ATOM 95 CZ PHEA 17 48.530-13.93541.108 1.0065.41 A

ATOM 96 C PHEA 17 53.071 -10.818 37.529 1.0064.91 A

ATOM 97 O PHEA 17 53.606 -9.805 37.989 1.0065.52 A

ATOM 98 N GLYA 18 53.571 -11.521 36.516 1.0064.92 A

ATOM 99 CA GLYA 18 54.796-11.129 35.848 1.0069.16 A

ATOM 100 C GLYA 18 55.994-10.869 36.739 1.0073.00 A

ATOM 101 O GLYA 18 56.595 -9.790 36.675 1.0073.79 A

ATOM 102 N ARG A 19 56.356-11.840 37.574 1.0072.63 A

ATOM 103 CA ARG A 19 57.513-11.640 38.426 1.0072.94 A

ATOM 104 CB ARG A 19 57.387-12.401 39.747 1.0073.83 A

ATOM 105 CG ARG A 19 58.378-11.89540.778 1.0072.01 A

ATOM 106 CD ARG A 19 58.020-12.31542.187 1.0071.92 A

ATOM 107 NE ARG A 19 59.105-11.98643.110 1.0076.20 A

ATOM 108 CZ ARG A 19 59.054-12.16244.427 1.0074.46 A

ATOM 109 NH1 ARG A 19 57.962-12.66744.986 1.0071.84 A

ATOM 110 NH2ARGA 19 60.097-11.831 45.182 1.0073.96 A

ATOM 111 C ARG A 19 58.765-12.058 37.663 1.0075.19 A

ATOM 112 O ARG A 19 59.386-13.091 37.925 1.0074.73 A

ATOM 113 N ARG A 20 59.080-11.215 36.685 1.0075.66 A

ATOM 114 CA ARG A 20 60.226-11.31435.791 1.0074.89 A

ATOM 115 CB ARG A 20 59.969-12.31434.655 1.0073.64 A

ATOM 116 CG ARG A 20 60.304-13.756 35.019 1.0074.15 A

ATOM 117 CD ARG A 20 60.081 -14.695 33.849 1.0074.85 A

ATOM 118 NE ARG A 20 58.669-14.758 33.471 1.0074.80 A ATOM 119 CZ ARG A 20 58.197 -15.442 32.434 1.00 74.15 A

ATOM 120 NH1 ARG A 20 59.021 I -16.132 31.654 1.00 73.69 A

ATOM 121 NH2 ARG A 20 56.897 -15.436 32.178 1 .00 67.39 A

ATOM 122 C ARG A 20 60.302 -9.888 35.256 1.00 75.49 A

ATOM 123 O ARG A 20 61.081 -9.563 34.355 1.00 74.77 A

ATOM 124 N MET A 21 59.454 -9.048 35.846 1 .00 75.51 A

ATOM 125 CA MET A 21 59.357 -7.630 35.524 1.00 76.50 A

ATOM 126 CB MET A 21 57.891 -7.219 35.345 1.00 72.76 A

ATOM 127 CG MET A 21 57.331 -7.493 33.966 1.00 74.55 A

ATOM 128 SD MET A 21 58.326 -6.681 32.705 1.00 78.64 A

ATOM 129 CE MET A 21 58.264 -4.965 33.269 1.00 73.09 A

ATOM 130 C MET A 21 59.968 -6.836 36.673 1.00 77.13 A

ATOM 131 O MET A 21 60.268 -5.648 36.532 1.00 78.49 A

ATOM 132 N ALA A 22 60.144 - ^•7.509 37.809 1.00 76.42 A

ATOM 133 CA ALA A 22 60.719 -6.903 39.007 1.00 75.39 A

ATOM 134 CB ALA A 22 62.069 -6.250 38.676 1 .00 74.18 A

ATOM 135 C ALA A 22 59.780 - •5.877 39.642 1.00 74.55 A

ATOM 136 O ALA A 22 59.506 ^{■ ■}5.942 40.841 1 .00 75.98 A

ATOM 137 N THR A 23 59.290 -4.934 38.840 1.00 73.51 A

ATOM 138 CA THR A 23 58.389 -3.899 39.342 1.00 75.29 A

ATOM 139 CB THR A 23 58.014 -2.867 38.230 1.00 74.54 A

ATOM 140 OG1 THR A 23 57.42c i -3.544 37.1 12 1 .00 74.36 A

ATOM 141 CG2 THR A 23 59.254 [ -2.107 37.768 1.00 72.43 A

ATOM 142 C THR A 23 57.103 -4.490 39.922 1.00 75.01 A

ATOM 143 O THR A 23 56.609 -5.519 39.456 1 .00 75.20 A

ATOM 144 N GLU A 24 56.575 -3.830 40.950 1.00 72.71 A

ATOM 145 CA GLU A 24 55.347 -4.265 41.608 1.00 70.58 A

ATOM 146 CB GLU A 24 55.179 -3.518 42.934 1.00 70.84 A

ATOM 147 CG GLU A 24 54.368 -4.264 43.986 1 .00 72.99 A

ATOM 148 CD GLU A 24 54.099 -3.413 45.220 1.00 73.23 A

ATOM 149 OE1 GLU A 24 53.198 ; -2.548 45.160 1.00 71.07 A

ATOM 150 OE2 GLU A 24 54.798 : -3.601 46.243 1.00 68.68 A

ATOM 151 C GLU A 24 54.152 • -3.978 40.689 1.00 69.02 A

ATOM 152 O GLU A 24 53.000 -4.263 41.033 1 .00 65.27 A

ATOM 153 N CYS A 25 54.445 ^■ -3.402 39.523 1.00 64.03 A

ATOM 154 CA CYS A 25 53.427 -3.076 38.527 1.00 61.19 A

ATOM 155 CB CYS A 25 53.647 -1.671 37.960 1.00 63.72 A

ATOM 156 SG CYS A 25 52.616 -1.304 36.51 1 1.00 67.26 A

ATOM 157 C CYS A 25 53.466 ^■ -4.074 37.379 1.00 58.70 A

ATOM 158 O CYS A 25 54.463 -4.166 36.659 1 .00 56.84 A

ATOM . 159 N PRO A 26 52.373 -4.830 37.186 1.00 57.00 A

ATOM 160 CD PRO A 26 51 .131 -4.830 37.980 1.00 50.95 A

ATOM 161 CA PRO A 26 52.299 -5.825 36.112 1 .00 52.99 A

ATOM 162 CB PRO A 26 50.844 -6.274 36.164 1.00 54.39 A

ATOM 163 CG PRO A 26 50.535 -6.176 37.626 1.00 52.36 A

ATOM 164 C PRO A 26 52.689 -5.259 34.756 1.00 46.91 A

ATOM 165 O PRO A 26 52.393 -4.108 34.441 1 .00 48.18 A

ATOM 166 N LYS A 27 53.361 - 6.082 33.963 1.00 43.17 A

ATOM 167 CA LYS A 27 53.812 -5.689 32.638 1 .00 42.02 A

ATOM 168 CB LYS A 27 54.554 -6.864 31.995 1 .00 50.63 A

ATOM 169 CG LYS A 27 53.792 -8.185 32.089 1.00 57.39 A

ATOM 170 CD LYS A 27 54.672 -9.390 31.778 1.00 60.25 A

ATOM 171 CE LYS A 27 53.914 - ■10.695 32.003 1.00 62.39 A

ATOM 172 NZ LYS A 27 54.762 - ■1 1.885 31.722 1.00 66.15 A

ATOM 173 C LYS A 27 52.665 - 5.225 31.735 1.00 40.66 A

ATOM 174 O LYS A 27 52.813 - 4.256 30.981 1.00 35.61 A

ATOM 175 N GLN A 28 51.519 ^■ -5.899 31.812 1.00 34.44 A ATOM 176 CA GLN A 28 50.386 -5.512 30.966 1.00 37.28 A

ATOM 177 CB GLN A 28 49.252 -6.551 31.031 1.00 41.23 A

ATOM 178 CG GLN A 28 48.654 -6.782 32.422 1.00 49.20 A

ATOM 179 CD GLN A 28 49.386 -7.855 33.206 1.0049.95 A

ATOM 180 OE1 GLN A 28 50.617 -7.875 33.259 1.00 51.37 A

ATOM 181 NE2 GLN A 28 48.630 -8.751 33.825 1.00 45.76 A

ATOM 182 C GLN A 28 49.830 ^• -4.129 31.309 1.00 42.28 A

ATOM 183 O GLN A 28 49.137 -3.498 30.497 1.00 37.80 A

ATOM 184 N TYR A 29 50.140 ^{■ ■}3.647 32.508 1.00 41.29 A

ATOM 185 CA TYR A 29 49.650 -2.340 32.926 1.00 42.26 A

ATOM 186 CB TYR A 29 49.178 -2.393 34.376 1.00 40.62 A

ATOM 187 CG TYR A 29 47.887 -3.158 34.544 1.00 40.31 A

ATOM 188 CD1 TYR A 29 47.829 -4.318 35.317 1.00 38.03 A

ATOM 189 CE1 TYR A 29 46.639 -5.040 35.443 1.00 34.00 A

ATOM 190 CD2 TYR A 29 46.722 -2.733 33.903 1.00 43.65 A

ATOM 191 CE2 TYR A 29 45.537 -3.443 34.022 1.00 42.57 A

ATOM 192 CZ TYR A 29 45.503 -4.597 34.792 1.00 30.68 A

ATOM 193 OH TYR A 29 44.323 -5.304 34.887 1.00 35.99 A

ATOM 194 C TYR A 29 50.649 - ■1.205 32.731 1.00 46.82 A

ATOM 195 O TYR A 29 50.366 -.054 33.064 1.00 46.09 A

ATOM 196 N LEU A 30 51.818 - ■1.530 32.189 1.00 45.82 A

ATOM 197 CA LEU A 30 52.816 -.513 31.906 1.00 46.62 A

ATOM 198 CB LEU A 30 54.144 -1.152 31.496 1.00 48.83 A

ATOM 199 CG LEU A 30 54.859 -1.993 32.558 1.00 54.67 A

ATOM 200 CD1 LEU A 30 56.097 -2.666 31.953 1.00 54.11 A

ATOM 201 CD2 LEU A 30 55.242 -1.103 33.729 1.00 52.34 A

ATOM 202 C LEU A 30 52.232 .258 30.734 1.00 49.75 A

ATOM 203 O LEU A 30 51.361 -.257 30.026 1.00 48.00 A

ATOM 204 N SER A 31 52.707 1.477 30.509 1.00 47.95 A

ATOM 205 CA SER A 31 52.166 2.274 29.417 1.00 50.26 A

ATOM 206 CB SER A 31 51.570 3.579 29.960 1.00 53.05 A

ATOM 207 OG SER A 31 50.439 3.321 30.775 1.00 54.25 A

ATOM 208 C SER A 31 53.119 2.608 28.285 1.00 48.62 A

ATOM 209 O SER A 31 54.301 2.868 28.488 1.00 45.89 A

ATOM 210 N ILE A 32 52.567 2.596 27.081 1.00 49.08 A

ATOM 211 CA ILE A 32 53.293 2.931 25.869 1.0045.90 A

ATOM 212 CB ILE A 32 53.514 1.686 24.979 1.00 49.67 A

ATOM 213 CG2 ILE A 32 54.172 2.087 23.671 1.0049.58 A

ATOM 214 CG1 ILE A 32 54.401 .668 25.703 .1.00 47.94 A

ATOM 215 CD ILE A 32 55.822 1.130 25.940 1.00 46.89 A

ATOM 216 C ILE A 32 52.381 3.931 25.161 1.0048.90 A

ATOM 217 O ILE A 32 51.257 3.602 24.764 1.00 39.74 A

ATOM 218 N GLY A 33 52.856 5.164 25.020 1.00 49.17 A

ATOM 219 CA GLY A 33 52.039 6.182 24.389 1.0043.64 A

ATOM 220 C GLY A 33 50.933 6.535 25.359 1.00 45.95 A

ATOM 221 O GLY A 33 51.175 6.628 26.564 1.00 50.72 A

ATOM 222 N ASN A 34 49.717 6.713 24.855 1.00 47.83 A

ATOM 223 CA ASN A 34 48.601 7.062 25.724 1.00 51.66 A

ATOM 224 CB ASN A 34 47.711 8.128 25.052 1.00 56.21 A

ATOM 225 CG ASN A 34 46.941 7.595 23.843 1.00 57.14 A

ATOM 226 OD1 ASN A 34 47.517 7.285 22.805 1.00 60.54 A

ATOM 227 ND2 ASN A 34 45.629 7.493 23.983 1.00 61.15 A

ATOM 228 C ASN A 34 47.763 5.843 26.094 1.00 50.82 A

ATOM 229 O ASN A 34 46.545 5.947 26.239 1.00 54.75 A

ATOM 230 N GLN A 35 48.410 4.691 26.266 1.00 51.16 A

ATOM 231 CA GLN A 35 47.683 3.463 26.597 1.00 43.73 A

ATOM 232 CB GLN A 35 47.084 2.842 25.332 1.0047.91 A ATOM 233 CG GLN A 35 45.814 3.473 24.839 1.00 52.52 A

ATOM 234 CD GLN A 35 45.162 2.646 23.756 1.00 55.94 A

ATOM 235 OE1 GLN A 35 44.088 i 2.995 23.253 1.00 56.83 A

ATOM 236 NE2 GLN A 35 45.807 1.538 23.388 1.00 47.85 A

ATOM 237 C GLN A 35 48.495 2.380 27.289 1.00 38.15 A

ATOM 238 O GLN A 35 49.723 2.313 27.167 1.00 34.45 A

ATOM 239 N THR A 36 47.798 1.507 28.011 1.00 33.80 A

ATOM 240 CA THR A 36 48.483 .409 28.672 1.00 28.77 A

ATOM 241 CB THR A 36 47.654 -.172 29.850 1.00 34.00 A

ATOM 242 OG1 THR A 36 46.418 -.701 29.361 1.00 31.58 A

ATOM 243 CG2 THR A 36 47.354 I .922 30.882 1.00 39.71 A

ATOM 244 C THR A 36 48.730 -.690 27.643 1.00 29.16 A

ATOM 245 O THR A 36 48.078 -.721 26.595 1.00 26.77 A

ATOM 246 N ILE A 37 49.682 -' 1.574 27.937 1.00 29.17 A

ATOM 247 CA ILE A 37 50.014 - •2.689 27.061 1.00 30.81 A

ATOM 248 CB ILE A 37 51.107 - ^■3.581 27.700 1.00 27.58 A

ATOM 249 CG2 ILE A 37 51.295 -4.855 26.906 1.00 28.55 A

ATOM 250 CG1 ILE A 37 52.432 -2.813 27.758 1.00 39.15 A

ATOM 251 CD ILE A 37 52.981 • ■2.449 26.385 1.00 39.56 A

ATOM 252 C ILE A 37 48.742 -3.506 26.819 1.00 27.27 A

ATOM 253 O ILE A 37 48.453 -; 3.904 25.680 1.00 25.35 A

ATOM 254 N LEU A 38 47.977 • ■3.735 27.888 1.00 28.92 A

ATOM 255 CA LEU A 38 46.714 -4.483 27.793 1.00 26.13 A

ATOM 256 CB LEU A 38 45.990 -4.541 29.148 1.00 28.58 A

ATOM 257 CG LEU A 38 44.600 -5.222 29.138 1.00 27.57 A

ATOM 258 CD1 LEU A 38 44.728 -6.699 28.687 1.00 24.81 A

ATOM 259 CD2 LEU A 38 44.004 -5.162 30.552 1.00 25.59 A

ATOM 260 C LEU A 38 45.779 ^■ ■3.840 26.780 1.00 26.34 A

ATOM 261 O LEU A 38 45.232 ■ -4.524 25.908 1.00 29.38 A

ATOM 262 N GLU A 39 45.602 -2.523 26.879 1.00 24.93 A

ATOM 263 CA GLU A 39 44.711 -1.834 25.949 1.00 23.02 A

ATOM 264 CB GLU A 39 44.526 -.371 26.364 1.00 21.65 A

ATOM 265 CG GLU A 39 43.799 -.216 27.696 1.00 24.98 A

ATOM 266 CD GLU A 39 43.944 1.191 28.275 1.00 30.75 A

ATOM 267 OE1 GLU A 39 43.007 ^' 2.006 28.126 1.00 35.65 A

ATOM 268 OE2 GLU A 39 45.003 i 1.467 28.861 1.00 31.83 A

ATOM 269 C GLU A 39 45.196 -1.938 24.499 1.00 22.79 A

ATOM 270 O GLU A 39 44.389 -2.081 23.595 1.00 21.73 A

ATOM 271 N HIS A 40 46.509 - 1.868 24.297 1.00 22.53 A

ATOM 272 CA HIS A 40 47.088 -1.999 22.965 1.00 26.18 A

ATOM 273 CB HIS A 40 48.613 -1.872 23.043 1.00 27.87 A

ATOM 274 CG HIS A 40 49.095 -.459 23.159 1.00 28.60 A

ATOM 275 CD2 HIS A 40 49.782 .172 24.140 1.00 23.74 A

ATOM 276 ND1 HIS A 40 48.909 .475 22.162 1.00 34.50 A

ATOM 277 CE1 HIS A 40 49.463 1.618 22.522 1.00 32.98 A

ATOM 278 NE2 HIS A 40 50.000 1.460 23.718 1.00 32.31 A

ATOM 279 C HIS A 40 46.707 -: 3.371 22.387 1.00 22.32 A

ATOM 280 O HIS A 40 46.211 - 3.465 21.267 1.00 23.85 A

ATOM 281 N SER A 41 46.933 -4.424 23.170 1.00 23.42 A

ATOM 282 CA SER A 41 46.618 -5.785 22.755 1.00 22.49 A

ATOM 283 CB SER A 41 47.031 -6.785 23.840 1.00 24.91 A

ATOM 284 OG SER A 41 48.430 -6.745 24.042 1.00 31.40 A

ATOM 285 C SER A 41 45.141 -5.969 22.422 1.00 26.91 A

ATOM 286 O SER A 41 44.784 -6.518 21.369 1.00 22.29 A

ATOM 287 N VAL A 42 44.281 - •5.499 23.318 1.00 22.22 A

ATOM 288 CA VAL A 42 42.841 -5.610 23.120 1.00 18.27 A

ATOM 289 CB VAL A 42 42.086 -5.179 24.392 1.00 20.36 A ATOM 290 CG1 VAL A 42 40.569 -5.169 24.121 1.00 23.44 A

ATOM 291 CG2 VAL A 42 42.428 -6.128 25.532 1.00 25.04 A

ATOM 292 C VAL A 42 42.341 -4.800 21.921 1.00 24.29 A

ATOM 293 O VAL A 42 41.494 -5.269 21.162 1.00 19.73 A ATOM 294 N HIS A 43 42.857 -3.586 21.733 1.00 23.56 A

ATOM 295 CA HIS A 43 42.417 -2.796 20.585 1.00 24.18 A

ATOM 296 CB HIS A 43 42.963 -1.365 20.662 1.00 33.22 A

ATOM 297 CG HIS A 43 42.327 -.542 21.740 1.00 45.05 A

ATOM 298 CD2 HIS A 43 42.860 .322 22.635 1.00 45.86 A ATOM 299 ND1 HIS A 43 40.970 -.561 21.988 1.00 46.89 A

ATOM 300 CE1 HIS A 43 40.695 .254 22.991 1.00 44.15 A

ATOM 301 NE2 HIS A 43 41.825 .803 23.403 1.00 48.24 A

ATOM 302 C HIS A 43 42.818 -3.439 19.258 1.00 20.96 A

ATOM 303 O HIS A 43 42.121 -3.281 18.252 1.00 23.87 A ATOM 304 N ALA A 44 43.912 -4.192 19.255 1.00 20.69 A

ATOM 305 CA ALA A 44 44.356 -4.842 18.022 1.00 24.37 A

ATOM 306 CB ALA A 44 45.721 -5.518 18.246 1.00 21.74 A

ATOM 307 C ALA A 44 43.313 -5.879 17.598 1.00 23.68 A

ATOM 308 O ALA A 44 43.028 -6.045 16.413 1.00 22.13 A ATOM 309 N LEU A 45 42.761 -6.591 18.577 1.00 20.35 A

ATOM 310 CA LEU A 45 41.734 -7.592 18.292 1.00 19.40 A

ATOM 311 CB LEU A 45 41.516 -8.472 19.519 1.00 22.27 A

ATOM 312 CG LEU A 45 42.780 -9.078 20.163 1.00 20.62 A

ATOM 313 CD1 LEU A 45 42.403 -9.707 21.487 1.00 17.38 A ATOM 314 CD2 LEU A 45 43.421 -10.084 19.247 1.00 26.24 A

ATOM 315 C LEU A 45 40.406 -6.925 17.913 1.00 19.87 A

ATOM 316 O LEU A 45 39.706 -7.362 16.998 1.00 19.24 A

ATOM 317 N LEU A 46 40.056 -5.870 18.638 1.00 21.01 A

ATOM 318 CA LEU A 46 38.785 -5.186 18.377 1.00 25.21 A ATOM 319 CB LEU A 46 38.480 -4.178 19.499 1.00 29.53 A

ATOM 320 CG LEU A 46 38.044 -4.724 20.881 1.00 28.23 A

ATOM 321 CD1 LEU A 46 38.026 -3.595 21.895 1.00 32.92 A

ATOM 322 CD2 LEU A 46 36.687 -5.378 20.799 1.00 26.62 A

ATOM 323 C LEU A 46 38.772 -4.483 17.018 1.00 28.20 A ATOM 324 0 LEU A 46 37.692 -4.175 16.481 1.00 27.75 A

ATOM 325 N ALA A 47 39.961 -4.236 16.473 1.00 29.10 A

ATOM 326 CA ALA A 47 40.111 -3.583 15.173 1.00 29.73 A

ATOM 327 CB ALA A 47 41.587 -3.266 14.907 1.00 33.23 A

ATOM 328 C ALA A 47 39.540 -4.430 14.035 1.00 35.37 A ATOM 329 0 ALA A 47 39.191 -3.899 12.983 1.00 32.46 A

ATOM 330 N HIS A 48 39.442 -5.744 14.233 1.00 28.63 A

ATOM 331 CA HIS A 48 38.880 -6.601 13.187 1.00 29.03 A

ATOM 332 CB HIS A 48 39.556 -7.974 13.137 1.00 31.65 A

ATOM 333 CG HIS A 48 39.175 -8.767 11.926 1.00 33.48 A ATOM 334 CD2 HIS A 48 37.992 -9.316 11.559 1.00 29.09 A

ATOM 335 ND1 HIS A 48 40.050 -9.014 10.894 1.00 41.87 A

ATOM 336 CE1 HIS A 48 39.426 -9.683 9.940 1.00 34.30 A

ATOM 337 NE2 HIS A 48 38.177 -9.878 10.318 1.00 35.40 A

ATOM 338 C HIS A 48 37.383 -6.787 13.424 1.00 27.28 A ATOM 339 O HIS A 48 36.948 -7.135 14.524 1.00 22.76 A

ATOM 340 N PRO A 49 36.571 -6.553 12.380 1.00 29.00 A

ATOM 341 CD PRO A 49 37.053 -6.198 11.033 1.00 28.21 A

ATOM 342 CA PRO A 49 35.107 -6.657 12.391 1.00 28.19 A

ATOM 343 CB PRO A 49 34.734 -6.471 10.921 1.00 32.09 A ATOM 344 CG PRO A 49 35.823 -5.620 10.397 1.00 32.98 A

ATOM 345 C PRO A 49 34.536 -7.956 12.934 1.00 27.93 A

ATOM 346 O PRO A 49 33.472 -7.967 13.555 1.00 31.44 A ATOM 347 N ARG A 50 35.236 -9.055 12.688 1.0024.08 A

ATOM 348 CA ARG A 50 34.750-10.341 13.155 1.0020.78 A

ATOM 349 CB ARG A 50 35.516-11.476 12.477 1.0025.42 A

ATOM 350 CG ARG A 50 35.168-11.630 11.009 1.0026.36 A ATOM 351 CD ARGA 50 35.913-12.783 10.385 1.0021.91 A

ATOM 352 NE ARG A 50 35.555-14.056 11.000 1.0023.38 A

ATOM 353 CZ ARG A 50 36.150-15.214 10.729 1.0025.64 A

ATOM 354 NH1 ARG A 50 37.136-15.266 9.848 1.0029.67 A

ATOM 355 NH2ARGA 50 35.773-16.324 11.347 1.0026.15 A ATOM 356 C ARG A 50 34.787-10.545 14.661 1.0020.63 A

ATOM 357 O ARG A 50 34.009-11.338 15.193 1.0020.99 A

ATOM 358 N VALA 51 35.679 -9.832 15.336 1.0021.47 A

ATOM 359 CA VALA 51 35.821 -9.982 16.778 1.0023.76 A

ATOM 360 CB VALA 51 37.194 -9.499 17.251 1.0022.80 A ATOM 361 CG1 VALA 51 37.330 -9.716 18.750 1.0022.07 A

ATOM 362 CG2VALA 51 38.270-10.234 16.512 1.0024.63 A

ATOM 363 C VALA 51 34.726 -9.199 17.466 1.0021.48 A

ATOM 364 O VALA 51 34.824 -7.994 17.646 1.0024.10 A

ATOM 365 N LYS A 52 33.688 -9.921 17.857 1.0019.47 A ATOM 366 CA LYS A 52 32.522 -9.325 18.483 1.0026.74 A

ATOM 367 CB LYS A 52 31.296-10.194 18.192 1.0024.55 A

ATOM 368 CG LYS A 52 31.148-10.574 16.732 1.0031.23 A

ATOM 369 CD LYS A 52 31.074 -9.330 15.862 1.0027.79 A

ATOM 370 CE LYS A 52 30.950 -9.685 14.388 1.0028.49 A ATOM 371 NZ LYS A 52 31.024 -8.462 13.559 1.0032.39 A

ATOM 372 C LYS A 52 32.637 -9.136 19.981 1.0023.13 A

ATOM 373 O LYS A 52 32.044 -8.218 20.546 1.0023.25 A

ATOM 374 N ARG A 53 33.419 -9.995 20.618 1.0027.50 A

ATOM 375 CA ARG A 53 33.547 -9.955 22.062 1.0027.17 A ATOM 376 CB ARG A 53 32.569-10.963 22.661 1.0026.89 A

ATOM 377 CG ARG A 53 32.494-11.022 24.167 1.0040.61 A

ATOM 378 CD ARG A 53 31.025-11.188 24.589 1.0048.88 A

ATOM 379 NE ARG A 53 30.899-11.710 25.945 1.0052.86 A

ATOM 380 CZ ARG A 53 30.985-12.998 26.257 1.0046.37 A ATOM 381 NH1 ARGA 53 31.188-13.89925.306 1.0047.93 A

ATOM 382 NH2 ARG A 53 30.873-13.38427.522 1.0055.68 A

ATOM 383 C ARG A 53 34.951 -10.313 22.479 1.0025.51 A

ATOM 384 O ARG A 53 35.629-11.075 21.796 1.0024.30 A

ATOM 385 N VALA 54 35.391 -9.733 23.584 1.0023.87 A ATOM 386 CA VALA 54 36.713-10.044 24.115 1.0023.37 A

ATOM 387 CB VALA 54 37.695 -8.857 23.939 1.0021.46 A

ATOM 388 CG1 VALA 54 38.995 -9.129 24.706 1.0022.36 A

ATOM 389 CG2VALA 54 37.984 -8.631 22.462 1.0023.74 A

ATOM 390 C VAL A 54 36.567-10.348 25.610 1.0021.98 A ATOM 391 O VALA 54 36.078 -9.520 26.378 1.0024.45 A

ATOM 392 N VAL A 55 36.989-11.545 26.009 1.0020.32 A

ATOM 393 CA VALA 55 36.932-11.938 27.404 1.0023.01 A

ATOM 394 CB VALA 55 36.486-13.418 27.575 1.0027.45 A

ATOM 395 CG1 VALA 55 36.497-13.790 29.058 1.0025.08 A ATOM 396 CG2VALA 55 35.068-13.614 26.998 1.0024.70 A

ATOM 397 C VALA 55 38.349-11.795 27.942 1.0020.26 A

ATOM 398 O VALA 55 39.276-12.403 27.408 1.0021.32 A

ATOM 399 N ILE A 56 38.514-10.967 28.967 1.0021.16 A

ATOM 400 CA ILEA 56 39.821 -10.750 29.583 1.0017.91 A ATOM 401 CB ILEA 56 40.100 -9.241 29.741 1.0017.25 A

ATOM 402 CG2ILEA 56 41.513 -9.004 30.355 1.0022.83 A

ATOM 403 CG1 ILEA 56 40.017 -8.568 28.367 1.0022.48 A ATOM 404 CD ILE A 56 40.125 -7.023 28.418 1.00 20.35 A

ATOM 405 C ILE A 56 39.868 -11.425 30.961 1.00 20.20 A

ATOM 406 O ILE A 56 38.999 -11.190 31.804 1.00 24.59 A

ATOM 407 N ALA A 57 40.864 -12.286 31.164 1.00 21.29 A

ATOM 408 CA ALA A 57 41.043 -12.988 32.439 1.00 24.90 A

ATOM 409 CB ALA A 57 41.502 -14.424 32.204 1.00 22.96 A

ATOM 410 C ALA A 57 42.100 -12.225 33.228 1.00 26.18 A

ATOM 411 O ALA A 57 43.203 -11.984 32.727 1.00 24.29 A

ATOM 412 N ILE A 58 41.750 -11.830 34.447 1.00 26.72 A

ATOM 413 CA ILE A 58 42.651 -11.081 35.320 1.00 27.24 A

ATOM 414 CB ILE A 58 42.106 -9.666 35.613 1.00 26.58 A

ATOM 415 CG2 ILE A 58 42.077 -8.823 34.324 1.00 28.78 A

ATOM 416 CG1 ILE A 58 40.703 -9.771 36.213 1.00 27.10 A

ATOM 417 CD ILE A 58 40.140 -8.441 36.726 1.00 30.53 A

ATOM 418 C ILE A 58 42.814 -11.778 36.667 1.00 31.88 A

ATOM 419 O ILE A 58 42.094 -12.735 36.983 1.00 31.48 A

ATOM 420 N SER A 59 43.761 -11.289 37.461 1.00 32.09 A

ATOM 421 CA SER A 59 43.987 -11.848 38.798 1.00 33.42 A

ATOM 422 CB SER A 59 45.351 -11.421 39.351 1.00 41.32 A

ATOM 423 OG SER A 59 45.428 -11.706 40.754 1.00 38.99 A

ATOM 424 C SER A 59 42.900 -11.365 39.757 1.00 29.69 A

ATOM 425 O SER A 59 42.459 -10.228 39.679 1.00 31.54 A

ATOM 426 N PRO A 60 42.463 -12.225 40.681 1.00 34.36 A

ATOM 427 CD PRO A 60 42.859 -13.633 40.849 1.00 35.71 A

ATOM 428 CA PRO A 60 41.427 -11.851 41.649 1.00 38.23 A

ATOM 429 CB PRO A 60 41.338 -13.082 42.540 1.00 39.62 A

ATOM 430 CG PRO A 60 41.691 -14.195 41.587 1.00 42.51 A

ATOM 431 C PRO A 60 41.822 -10.600 42.434 1.00 37.96 A

ATOM 432 O PRO A 60 40.969 -9.817 42.858 1.00 38.56 A

ATOM 433 N GLY A 61 43.125 -10.415 42.616 1.00 39.00 A

ATOM 434 CA GLY A 61 43.610 -9.259 43.350 1.00 45.99 A

ATOM 435 C GLY A 61 43.915 -8.077 42.449 1.00 47.20 A

ATOM 436 O GLY A 61 44.503 -7.091 42.895 1.00 44.19 A

ATOM 437 N ASP A 62 43.509 -8.178 41.183 1.00 45.96 A

ATOM 438 CA ASP A 62 43.737 -7.118 40.202 1.00 44.62 A

ATOM 439 CB ASP A 62 43.538 -7.655 38.779 1.00 43.13 A

ATOM 440 CG ASP A 62 43.867 -6.624 37.709 1.00 48.53 A

ATOM 441 OD1 ASP A 62 43.666 -5.413 37.954 1.00 44.68 A

ATOM 442 OD2 ASP A 62 44.317 -7.027 36.615 1.00 50.65 A

ATOM 443 C ASP A 62 42.776 -5.959 40.446 1.00 45.58 A

ATOM 444 O ASP A 62 41.557 -6.105 40.338 1.00 48.49 A

ATOM 445 N SER A 63 43.332 -4.799 40.766 1.00 47.96 A

ATOM 446 CA SER A 63 42.508 -3.637 41.025 1.00 51.71 A

ATOM 447 CB SER A 63 42.737 -3.155 42.463 1.00 50.92 A

ATOM 448 OG SER A 63 44.106 -3.246 42.824 1.00 49.99 A

ATOM 449 C SER A 63 42.729 -2.495 40.034 1.00 49.41 A

ATOM 450 O SER A 63 42.064 -1.463 40.123 1.00 50.09 A

ATOM 451 N ARG A 64 43.650 -2.665 39.089 1.00 45.40 A

ATOM 452 CA ARG A 64 43.871 -1.599 38.122 1.00 43.93 A

ATOM 453 CB ARG A 64 45.342 -1.500 37.701 1.00 46.70 A

ATOM 454 CG ARG A 64 45.721 -.046 37.395 1.00 57.12 A

ATOM 455 CD ARG A 64 46.928 .146 36.479 1.00 57.01 . A

ATOM 456 NE ARG A 64 46.863 1.473 35.854 1.00 58.33 A

ATOM 457 CZ ARG A 64 47.526 1.840 34.759 1.00 62.35 A

ATOM 458 NH1 ARG A 64 48.329 .983 34.144 1.00 59.24 A

ATOM 459 NH2 ARG A 64 47.368 3.064 34.263 1.00 57.91 A

ATOM 460 C ARG A 64 42.994 -1.742 36.878 1.00 38.62 A ATOM 461 O ARG A 64 42.765 -.766 36.168 1.00 36.54 A

ATOM 462 N PHE A 65 42.488 ■ -2.943 36.611 1.00 34.78 A

ATOM 463 CA PHE A 65 41.639 -3.126 35.438 1.00 37.30 A

ATOM 464 CB PHE A 65 41.175 -4.577 35.291 1.00 39.72 A

ATOM 465 CG PHE A 65 40.394 -4.825 34.026 1.00 35.70 A

ATOM 466 CD1 PHE A 65 41.054 -5.037 32.818 1.00 32.35 A

ATOM 467 CD2 PHE A 65 39.001 -4.799 34.031 1.00 37.72 A

ATOM 468 CE1 PHE A 65 40.340 -5.215 31.637 1.00 33.09 A

ATOM 469 CE2 PHE A 65 38.284 -4.974 32.858 1.00 43.12 A

ATOM 470 CZ PHE A 65 38.953 -5.182 31.657 1.00 40.50 A

ATOM 471 C PHE A 65 40.404 ■ -2.243 35.492 1.00 37.84 A

ATOM 472 O PHE A 65 40.084 ■ -1.565 34.518 1.00 40.04 A

ATOM 473 N ALA A 66 39.707 - 2.253 36.624 1.00 39.01 A

ATOM 474 CA ALA A 66 38.493 -1.458 36.764 1.00 38.77 A

ATOM 475 CB ALA A 66 37.841 -1.728 38.115 1.00 42.87 A

ATOM 476 C ALA A 66 38.725 .037 36.579 1.00 39.97 A

ATOM 477 O ALA A 66 37.774 .798 36.429 1.00 37.02 A

ATOM 478 N GLN A 67 39.982 .469 36.582 1.00 39.65 A

ATOM 479 CA GLN A 67 40.256 1.891 36.397 1.00 45.99 A

ATOM 480 CB GLN A 67 41.387 2.345 37.326 1.00 47.02 A

ATOM 481 CG GLN A 67 41.128 2.039 38.800 1.00 52.64 A

ATOM 482 CD GLN A 67 39.710 2.403 39.224 1.00 54.11 A

ATOM 483 OE1 GLN A 67 39.268 3.541 39.045 1.00 60.55 A

ATOM 484 NE2 GLN A 67 38.988 1.432 39.786 1.00 52.40 A

ATOM 485 C GLN A 67 40.601 2.228 34.944 1.00 47.66 A

ATOM 486 O GLN A 67 40.991 3.352 34.637 1.00 45.96 A

ATOM 487 N LEU A 68 40.464 1.252 34.051 1.00 46.35 A

ATOM 488 CA LEU A 68 40.751 1.482 32.635 1.00 47.73 A

ATOM 489 CB LEU A 68 41.533 .297 32.050 1.00 43.82 A

ATOM 490 CG LEU A 68 42.913 .016 32.644 1.00 38.71 A

ATOM 491 CD1 LEU A 68 43.422 -1.326 32.145 1.00 41.50 A

ATOM 492 CD2 LEU A 68 43.874 1.140 32.290 1.00 40.32 A

ATOM 493 C LEU A 68 39.446 1.670 31.855 1.00 44.97 A

ATOM 494 O LEU A 68 38.391 1.183 32.264 1.00 44.55 A

ATOM 495 N PRO A 69 39.502 2.392 30.724 1.00 48.13 A

ATOM 496 CD PRO A 69 40.634 3.228 30.287 1.00 46.43 A

ATOM 497 CA PRO A 69 38.316 2.633 29.888 1.00 50.32 A

ATOM 498 CB PRO A 69 38.867 3.491 28.753 1.00 46.96 A

ATOM 499 CG PRO A 69 39.953 4.266 29.424 1.00 48.61 A

ATOM 500 C PRO A 69 37.692 1.331 29.371 1.00 50.50 A

ATOM 501 O PRO A 69 36.498 1.271 29.055 1.00 54.51 A

ATOM 502 N LEU A 70 38.513 .291 29.279 1.00 48.11 A

ATOM 503 CA LEU A 70 38.058 -1.009 28.798 1.00 46.44 A

ATOM 504 CB LEU A 70 39.246 -1.958 28.656 1.00 46.67 A

ATOM 505 CG LEU A 70 40.286 -1.624 27.595 1.00 46.22 A

ATOM 506 CD1 LEU A 70 41.386 -2.679 27.659 1.00 53.95 A

ATOM 507 CD2 LEU A 70 39.646 -1.611 26.213 1.00 47.43 A

ATOM 508 C LEU A 70 37.043 - 1.641 29.742 1.00 47.63 A

ATOM 509 O LEU A 70 36.203 - 2.448 29.328 1.00 44.03 A

ATOM 510 N ALA A 71 37.147 - 1.282 31.017 1.00 43.51 A

ATOM 511 CA ALA A 71 36.262 -1.806 32.048 1.00 44.73 A

ATOM 512 CB ALA A 71 36.551 -1.102 33.383 1.00 46.97 A

ATOM 513 C ALA A 71 34.780 - 1.672 31.699 1.00 43.18 A

ATOM 514 O ALA A 71 33.987 - 2.563 32.010 1.00 43.61 A

ATOM 515 N ASN A 72 34.415 -.572 31.045 1.00 39.33 A

ATOM 516 CA ASN A 72 33.020 -.310 30.682 1.00 41.21 A

ATOM 517 CB ASN A 72 32.657 1.127 31.078 1.00 48.12 A ATOM 518 CG ASNA 72 32.538 1.311 32.581 1.0053.17 A

ATOM 519 OD1 ASN A 72 32.752 2.410 33.102 1.0060.98 A

ATOM 520 ND2 ASN A 72 32.182 .240 33.287 1.0053.98 A

ATOM 521 C ASN A 72 32.653 -.525 29.209 1.0034.56 A ATOM 522 0 ASN A 72 31.555 -.160 28.781 1.0033.75 A

ATOM 523 N HISA 73 33.565 -1.118 28.451 1.0033.12 A

ATOM 524 CA HISA 73 33.376 -1.376 27.025 1.0028.82 A

ATOM 525 CB HISA 73 34.719 -1.812 26.428 1.0024.68 A

ATOM 526 CG HISA 73 34.742 -1.828 24.936 1.0023.50 A ATOM 527 CD2 HIS A 73 34.066 -2.59024.043 1.0020.40 A

ATOM 528 ND1 HISA 73 35.527 -.971 24.194 1.0026.71 A

ATOM 529 CE1 HISA 73 35.333 -1.204 22.909 1.0018.95 A

ATOM 530 NE2 HIS A 73 34.451 -2.182 22.791 1.0029.15 A

ATOM 531 C HISA 73 32.302 -2.444 26.790 1.0023.21 A ATOM 532 O HISA 73 32.364 -3.531 27.353 1.0023.04 A

ATOM 533 N PROA 74 31.295 -2.145 25.949 1.0025.87 A

ATOM 534 CD PROA 74 31.163 -.929 25.130 1.0021.86 A

ATOM 535 CA PROA 74 30.222 -3.11025.672 1.0025.59 A

ATOM 536 CB PROA 74 29.261 -2.32924.763 1.0029.21 A ATOM 537 CG PROA 74 30.134 -1.33824.069 1.0027.34 A

ATOM 538 C PROA 74 30.641 -4.465 25.071 1.0025.90 A

ATOM 539 O PROA 74 29.904 -5.445 25.164 1.0022.37 A

ATOM 540 N GLNA 75 31.825 -4.533 24.476 1.0020.86 A

ATOM 541 CA GLNA 75 32.269 -5.785 23.882 1.0024.40 A ATOM 542 CB GLNA 75 32.978 -5.513 22.546 1.0021.14 A

ATOM 543 CG GLNA 75 32.071 -4.896 21.490 1.0019.80 A

ATOM 544 CD GLNA 75 32.774 -4.628 20.179 1.0023.19 A

ATOM 545 OE1 GLNA 75 33.333 -3.564 19.976 1.0024.50 A

ATOM 546 NE2GLNA 75 32.753 -5.602 19.287 1.0031.14 A ATOM 547 C GLNA 75 33.193 -6.546 24.816 1.0021.67 A

ATOM 548 O GLNA 75 33.602 -7.665 24.514 1.0027.60 A

ATOM 549 N ILEA 76 33.500 -5.951 25.963 1.0023.36 A

ATOM 550 CA ILEA 76 34.414 -6.598 26.908 1.0030.20 A

ATOM 551 CB ILEA 76 35.479 -5.601 27.416 1.0027.04 A ATOM 552 CG2ILEA 76 36.504 -6.319 28.292 1.0024.98 A

ATOM 553 CG1 ILEA 76 36.189 -4.951 26.224 1.0033.88 A

ATOM 554 CD ILEA 76 36.766 -5.922 25.251 1.0044.83 A

ATOM 555 C ILEA 76 33.777 -7.256 28.129 1.0032.32 A

ATOM 556 O ILEA 76 32.922 -6.669 28.789 1.0030.27 A ATOM 557 N THRA 77 34.201 -8.487 28.402 1.0029.84 A

ATOM 558 CA THRA 77 33.747 -9.243 29.566 1.0033.65 A

ATOM 559 CB THRA 77 33.072-10.57529.165 1.0031.54 A

ATOM 560 OG1 THRA 77 31.836-10.29928.493 1.0037.01 A

ATOM 561 CG2THRA 77 32.793-11.434 30.391 1.0040.33 A ATOM 562 C THRA 77 34.999 -9.562 30.389 1.0029.66 A

ATOM 563 O THR A 77 36.053 -9.870 29.827 1.0026.78 A

ATOM 564 N VALA 78 34.894 -9.462 31.710 1.0028.20 A

ATOM 565 CA VALA 78 36.026 -9.748 32.589 1.0032.24 A

ATOM 566 CB VALA 78 36.381 -8.500 33.460 1.0037.97 A ATOM 567 CG1 VALA 78 35.172 -8.068 34.269 1.0046.27 A

ATOM 568 CG2 VAL A 78 37.546 -8.814 34.386 1.0040.25 A

ATOM 569 C VALA 78 35.753-10.946 33.504 1.0036.17 A

ATOM 570 O VALA 78 34.666-11.063 34.067 1.0037.86 A

ATOM 571 N VALA 79 36.728-11.855 33.613 1.0033.28 A ATOM 572 CA VALA 79 36.616-13.030 34.491 1.0032.17 A

ATOM 573 CB VALA 79 36.325-14.335 33.703 1.0031.78 A

ATOM 574 CG1 VALA 79 35.010-14.186 32.892 1.0029.67 A ATOM 575 CG2VALA 79 37.497-14.668 32.779 1.0033.24 A

ATOM 576 C VALA 79 37.937-13.209 35.242 1.0032.36 A

ATOM 577 O VALA 79 38.939-12.590 34.889 1.0030.86 A

ATOM 578 N ASP A 80 37.960-14.04536.276 1.0036.84 A

ATOM 579 CA ASP A 80 39.211-14.251 36.994 1.0036.68 A

ATOM 580 CB ASP A 80 38.962-14.630 38.455 1.0046.47 A

ATOM 581 CG ASP A 80 38.352-13.495 39.260 1.0049.17 A

ATOM 582 OD1 ASP A 80 38.764-12.327 39.080 1.0048.56 A

ATOM 583 OD2 ASP A 80 37.462-13.778 40.087 1.0056.98 A

ATOM 584 C ASP A 80 40.038-15.337 36.332 1.0030.30 A

ATOM 585 O ASPA 80 39.503-16.341 35.862 1.0035.11 A

ATOM 586 N GLYA 81 41.347-15.130 36.286 1.0030.07 A

ATOM 587 CA GLYA 81 42.236-16.121 35.696 1.0035.52 A

ATOM 588 C GLYA 81 42.631-17.182 36.718 1.0039.60 A

ATOM 589 O GLYA 81 42.069-17.212 37.814 1.0040.21 A

ATOM 590 N GLYA 82 43.586-18.044 36.363 1.0038.16 A

ATOM 591 CA GLYA 82 44.032-19.109 37.261 1.0037.54 A

ATOM 592 C GLYA 82 45.517-19.109 37.591 1.0036.16 A

ATOM 593 O GLYA 82 46.210-18.140 37.307 1.0035.33 A

ATOM 594 N ASP A 83 46.022-20.204 38.162 1.0036.60 A

ATOM 595 CA ASPA 83 47.427-20.270 38.549 1.0040.12 A

ATOM 596 CB ASPA 83 47.718-21.564 39.312 1.0047.09 A

ATOM 597 CG ASPA 83 46.806-21.751 40.510 1.0048.31 A

ATOM 598 OD1 ASP A 83 46.399-20.726 41.105 1.0047.48 A

ATOM 599 OD2 ASP A 83 46.512-22.920 40.860 1.0055.48 A

ATOM 600 C ASPA 83 48.409-20.142 37.403 1.0041.27 A

ATOM 601 O ASP A 83 49.411 -19.439 37.516 1.0044.03 A

ATOM 602 N GLU A 84 48.137-20.841 36.308 1.0037.31 A

ATOM 603 CA GLU A 84 49.007-20.78735.143 1.0033.84 A

ATOM 604 CB GLU A 84 49.513-22.189 34.798 1.0029.93 A

ATOM 605 CG GLU A 84 50.406-22.809 35.862 1.0042.85 A

ATOM 606 CD GLU A 84 51.674-22.010 36.073 1.0050.91 A

ATOM 607 OE1 GLU A 84 52.415-21.798 35.092 1.0052.77 A

ATOM 608 OE2 GLU A 84 51.936-21.589 37.218 1.0061.59 A

ATOM 609 C GLU A 84 48.235-20.203 33.961 1.0036.91 A

ATOM 610 O GLU A 84 47.004-20.041 34.014 1.0029.78 A

ATOM 611 N ARG A 85 48.956-19.892 32.889 1.0033.20 A

ATOM 612 CA ARG A 85 48.320-19.311 31.701 1.0035.71 A

ATOM 613 CB ARG A 85 49.354-19.112 30.587 1.0030.05 A

ATOM 614 CG ARG A 85 48.795-18.460 29.314 1.0027.03 A

ATOM 615 CD ARG A 85 49.903-18.248 28.281 1.0023.61 A

ATOM 616 NE ARG A 85 49.388-17.637 27.050 1.0025.32 A

ATOM 617 CZ ARG A 85 48.692-18.293 26.130 1.0024.50 A

ATOM 618 NH1 ARG A 85 48.437-19.583 26.300 1.0022.31 A

ATOM 619 NH2 ARG A 85 48.238-17.662 25.054 1.0027.83 A

ATOM 620 C ARG A 85 47.183-20.19531.194 1.0035.28 A

ATOM 621 O ARG A 85 46.085-19.711 30.936 1.0034.51 A

ATOM 622 N ALAA 86 47.454-21.491 31.051 1.0031.83 A

ATOM 623 CA ALAA 86 46.440-22.417 30.564 1.0027.37 A

ATOM 624 CB ALAA 86 47.002-23.844 30.518 1.0025.12 A

ATOM 625 C ALAA 86 45.148-22.362 31.391 1.0025.65 A

ATOM 626 O ALAA 86 44.057-22.536 30.845 1.0031.22 A

ATOM 627 N ASPA 87 45.264-22.107 32.694 1.0028.65 A

ATOM 628 CA ASPA 87 44.091-22.024 33.564 1.0030.05 A

ATOM 629 CB ASPA 87 44.494-22.051 35.052 1.0032.92 A

ATOM 630 CG ASP A 87 45.321 -23.271 35.422 1.0038.45 A

ATOM 631 OD1 ASPA 87 44.826-24.407 35.251 1.0039.62 A ATOM 632 OD2 ASP A 87 46.471 -23.086 35.882 1.0033.03 A

ATOM 633 C ASP A 87 43.322-20.731 33.285 1.0027.42 A

ATOM 634 O ASP A 87 42.086-20.718 33.238 1.0026.57 A

ATOM 635 N SERA 88 44.045-19.635 33.109 1.0029.80 A

ATOM 636 CA SERA 88 43.383-18.36332.831 1.0029.86 A

ATOM 637 CB SERA 88 44.410-17.231 32.816 1.0031.10 A

ATOM 638 OG SERA 88 45.118-17.166 34.050 1.0038.96 A

ATOM 639 C SERA 88 42.665-18.450 31.479 1.0028.97 A

ATOM 640 O SERA 88 41.549-17.953 31.325 1.0022.94 A

ATOM 641 N VAL A 89 43.308-19.093 30.511 1.0025.19 A

ATOM 642 CA VAL A 89 42.724-19.241 29.180 1.0027.04 A

ATOM 643 CB VALA 89 43.758-19.86828.199 1.0024.62 A

ATOM 644 CG1 VAL A 89 43.084-20.26326.878 1.0024.12 A

ATOM 645 CG2VALA 89 44.898-18.85727.942 1.0019.91 A

ATOM 646 C VAL A 89 41.448-20.082 29.231 1.0030.57 A

ATOM 647 O VALA 89 40.453-19.783 28.551 1.0026.11 A

ATOM 648 N LEU A 90 41.473-21.130 30.051 1.0033.66 A

ATOM 649 CA LEU A 90 40.309-22.00030.199 1.0030.39 A

ATOM 650 CB LEU A 90 40.657-23.21531.075 1.0031.24 A

ATOM 651 CG LEU A 90 40.039-24.56230.683 1.0037.85 A

ATOM 652 CD1 LEU A 90 39.968-25.45831.928 1.0037.27 A

ATOM 653 CD2 LEU A 90 38.665-24.386 30.094 1.0044.28 A

ATOM 654 C LEU A 90 39.121-21.243 30.806 1.0028.41 A

ATOM 655 O LEU A 90 37.979-21.40530.369 1.0031.48 A

ATOM 656 N ALAA 91 39.390-20.403 31.802 1.0030.15 A

ATOM 657 CA ALAA 91 38.336-19.633 32.452 1.0026.73 A

ATOM 658 CB ALAA 91 38.902-18.89733.664 1.0028.58 A

ATOM 659 C ALAA 91 37.739-18.643 31.457 1.0032.09 A

ATOM 660 O ALAA 91 36.542-18.363 31.491 1.0032.74 A

ATOM 661 N GLYA 92 38.585-18.09930.584 1.0029.47 A

ATOM 662 CA GLYA 92 38.091-17.17829.568 1.0020.98 A

ATOM 663 C GLYA 92 37.202-17.901 28.560 1.0024.16 A

ATOM 664 O GLY A 92 36.165-17.372 28.108 1.0029.29 A

ATOM 665 N LEU A 93 37.603-19.11728.196 1.0025.01 A

ATOM 666 CA LEU A 93 36.842-19.92927.241 1.0026.69 A

ATOM 667 CB LEU A 93 37.565-21.24526.933 1.0029.62 A

ATOM 668 CG LEU A 93 38.832-21.21026.082 1.0033.50 A

ATOM 669 CD1 LEU A 93 39.368-22.63525.968 1.0028.72 A

ATOM 670 CD2 LEU A 93 38.537 -20.63224.704 1.0024.48 A

ATOM 671 C LEU A 93 35.441-20.264 27.744 1.0034.31 A

ATOM 672 O LEU A 93 34.492-20.34926.960 1.0036.53 A

ATOM 673 N LYS A 94 35.308 -20.44729.050 1.0036.53 A

ATOM 674 CA LYS A 94 34.014-20.79029.620 1.0040.92 A

ATOM 675 CB LYS A 94 34.191 -21.251 31.069 1.0041.10 A

ATOM 676 CG LYS A 94 34.965-22.55531.156 1.0040.25 A

ATOM 677 CD LYS A 94 35.070-23.078 32.575 1.0047.86 A

ATOM 678 CE LYS A 94 35.818-24.40332.602 1.0045.88 A

ATOM 679 NZ LYS A 94 36.170-24.81433.987 1.0047.89 A

ATOM 680 C LYS A 94 33.000-19.662 29.523 1.0041.14 A

ATOM 681 O LYS A 94 31.795-19.890 29.648 1.0035.75 A

ATOM 682 N ALAA 95 33.482-18.449 29.274 1.0038.84 A

ATOM 683 CA ALA A 95 32.598-17.30529.137 1.0038.03 A

ATOM 684 CB ALAA 95 33.051 -16.19530.063 1.0031.00 A

ATOM 685 C ALAA 95 32.575-16.802 27.689 1.0037.80 A

ATOM 686 O ALAA 95 32.087-15.707 27.417 1.0034.89 A

ATOM 687 N ALAA 96 33.097-17.611 26.770 1.0037.52 A

ATOM 688 CA ALAA 96 33.170-17.25225.350 1.0043.22 A ATOM 689 CB ALAA 96 33.999-18.296 24.587 1.0037.72 A

ATOM 690 C ALAA 96 31.817-17.083 24.677 1.0046.74 A

ATOM 691 O ALAA 96 31.656-16.238 23.794 1.0051.56 A

ATOM 692 N GLY A 97 30.853-17.900 25.091 1.0047.52 A ATOM 693 CA GLYA 97 29.520-17.825 24.527 1.0043.87 A

ATOM 694 C GLYA 97 29.230-18.92823.530 1.0043.13 A

ATOM 695 0 GLYA 97 29.623-20.084 23.717 1.0045.18 A

ATOM 696 N ASP A 98 28.540-18.572 22.454 1.0044.45 A

ATOM 697 CA ASPA 98 28.200-19.541 21.426 1.0039.02 A ATOM 698 CB ASPA 98 26.727-19.389 21.014 1.0049.37 A

ATOM 699 CG ASPA 98 25.771 -19.804 22.112 1.0058.89 A

ATOM 700 OD1 ASP A 98 25.760-21.00322.472 1.0065.50 A

ATOM 701 OD2 ASP A 98 25.031 -18.933 22.619 1.0065.41 A

ATOM 702 C ASP A 98 29.088-19.374 20.207 1.0036.49 A ATOM 703 O ASP A 98 28.898-20.058 19.204 1.0034.10 A

ATOM 704 N ALAA 99 30.039-18.449 20.279 1.0031.01 A

ATOM 705 CA ALAA 99 30.964-18.229 19.164 1.0036.13 A

ATOM 706 CB ALAA 99 32.129-17.317 19.610 1.0036.52 A

ATOM 707 C ALAA 99 31.509-19.581 18.693 1.0028.33 A ATOM 708 O ALAA 99 31.834-20.435 19.511 1.0027.94 A

ATOM 709 N GLN A 100 31.605-19.771 17.382 1.0018.99 A

ATOM 710 CA GLNA100 32.108-21.023 16.827 1.0022.75 A

ATOM 711 CB GLNA100 31.647-21.186 15.374 1.0019.92 A

ATOM 712 CG GLN A 100 30.134-21.531 15.224 1.0028.75 A ATOM 713 CD GLN A 100 29.586-21.377 13.797 1.0026.62 A

ATOM 714 OE1 GLNA100 30.268-21.644 12.812 1.0030.00 A

ATOM 715 NE2 GLN A 100 28.331-20.962 13.697 1.0035.35 A

ATOM 716 C GLNA100 33.626-21.109 16.881 1.0023.35 A

ATOM 717 O GLN A 100 34.195-22.193 17.040 1.0022.70 A ATOM 718 N TRP A 101 34.264-19.956 16.741 1.0023.27 A

ATOM 719 CA TRPA101 35.705-19.876 16.749 1.0015.64 A

ATOM 720 CB TRP A 101 36.196-19.441 15.365 1.0022.35 A

ATOM 721 CG TRPA101 36.138-20.513 14.327 1.0024.23 A

ATOM 722 CD2TRPA101 37.249-21.271 13.844 1.0027.32 A ATOM 723 CE2TRPA101 36.745-22.181 12.886 1.0028.01 A

ATOM 724 CE3TRPA101 38.628-21.269 14.131 1.0024.94 A

ATOM 725 CD1TRPA101 35.029-20.973 13.660 1.0025.04 A

ATOM 726 NE1 TRP A 101 35.394-21.978 12.791 1.0025.95 A

ATOM 727 CZ2TRPA101 37.572-23.080 12.211 1.0023.73 A ATOM 728 CZ3TRPA101 39.450-22.161 13.458 1.0027.04 A

ATOM 729 CH2TRPA101 38.913-23.060 12.508 1.0025.03 A

ATOM 730 C TRP A 101 36.222-18.901 17.820 1.0021.75 A

ATOM 731 O TRP A 101 35.608-17.866 18.081 1.0023.21 A

ATOM 732 N VAL A 102 37.356-19.229 18.434 1.0021.20 A ATOM 733 CA VAL A 102 37.899-18.360 19.468 1.0020.90 A

ATOM 734 CB VAL A 102 37.822-19.048 20.865 1.0024.10 A

ATOM 735 CG1 VALA 102 38.660-20.32720.867 1.0020.39 A

ATOM 736 CG2 VAL A 102 38.289-18.08421.948 1.0025.04 A

ATOM 737 C VALA102 39.323-17.962 19.134 1.0018.89 A ATOM 738 O VAL A 102 40.086-18.727 18.540 1.0021.86 A

ATOM 739 N LEUA103 39.655-16.734 19.505 1.0019.38 A

ATOM 740 CA LEUA103 40.974-16.172 19.257 1.0023.93 A

ATOM 741 CB LEU A 103 40.804-14.807 18.592 1.0022.17 A

ATOM 742 CG LEU A 103 41.959-14.186 17.825 1.0037.54 A ATOM 743 CD1 LEU A 103 42.251 -14.993 16.546 1.0027.30 A

ATOM 744 CD2LEUA103 41.599-12.749 17.489 1.0040.17 A

ATOM 745 C LEU A 103 41.584-15.986 20.639 1.0017.92 A ATOM 746 O LEU A 103 40.967 -15.355 21.482 1.00 22.00 A

ATOM 747 N VAL A 104 42.770 -16.544 20.887 1.00 18.56 A

ATOM 748 CA VAL A 104 43.399 -16.379 22.207 1.00 19.29 A

ATOM 749 CB VAL A 104 43.759 -17.743 22.856 1.00 18.67 A

ATOM 750 CG1 VAL A 104 44.339 -17.506 24.261 1.00 20.13 A

ATOM 751 CG2 VAL A 104 42.494 -18.617 22.936 1.00 14.94 A

ATOM 752 C VAL A 104 44.666 -15.589 21.978 1.00 20.36 A

ATOM 753 O VAL A 104 45.512 -15.986 21.178 1.00 17.88 A

ATOM 754 N HIS A 105 44.785 -14.457 22.656 1.00 19.74 A

ATOM 755 CA HIS A 105 45.937 -13.597 22.447 1.00 19.79 A

ATOM 756 CB HIS A 105 45.489 -12.413 21.556 1.00 17.21 A

ATOM 757 CG HIS A 105 46.578 -11.448 21.221 1.00 16.62 A

ATOM 758 CD2 H1S A 105 46.671 -10.111 21.426 1.00 18.79 A

ATOM 759 ND1 HIS A 105 47.754 -11.827 20.615 1.00 17.54 A

ATOM 760 CE1 HIS A 105 48.532 -10.769 20.470 1.00 18.17 A

ATOM 761 NE2 HIS A 105 47.898 -9.714 20.958 1.00 21.82 A

ATOM 762 C HIS A 105 46.531 -13.109 23.775 1.00 16.42 A

ATOM 763 O HIS A 105 45.828 -12.588 24.652 1.00 16.02 A

ATOM 764 N ASP A 106 47.843 -13.267 23.937 1.00 17.10 A

ATOM 765 CA ASP A 106 48.510 -12.794 25.156 1.00 19.32 A

ATOM 766 CB ASP A 106 50.039 -13.001 25.105 1.00 18.74 A

ATOM 767 CG ASP A 106 50.450 -14.462 25.086 1.00 24.98 A

ATOM 768 OD1 ASP A 106 49.737 -15.298 25.673 1.00 24.55 A

ATOM 769 OD2 ASP A 106 51.506 -14.764 24.487 1.00 23.72 A

ATOM 770 C ASP A 106 48.306 -11.295 25.384 1.00 23.60 A

ATOM 771 O ASP A 106 48.451 -10.476 24.456 1.00 20.97 A

ATOM 772 N ALA A 107 47.973 -10.908 26.612 1.00 17.70 A

ATOM 773 CA ALA A 107 47.805 -9.476 26.887 1.00 20.48 A

ATOM 774 CB ALA A 107 47.376 -9.284 28.308 1.00 21.67 A

ATOM 775 C ALA A 107 49.143 -8.754 26.652 1.00 28.20 A

ATOM 776 O ALA A 107 49.184 -7.579 26.274 1.00 22.84 A

ATOM 777 N ALA A 108 50.230 -9.495 26.847 1.00 26.69 A

ATOM 778 CA ALA A 108 51.596 -8.973 26.729 1.00 29.71 A

ATOM 779 CB ALA A 108 52.511 -9.828 27.571 1.00 30.45 A

ATOM 780 C ALA A 108 52.191 -8.815 25.326 1.00 32.03 A

ATOM 781 O ALA A 108 53.392 -8.537 25.178 1.00 25.61 A

ATOM 782 N ARG A 109 51.377 -9.017 24.297 1.00 28.09 A

ATOM 783 CA ARG A 109 51.850 -8.860 22.928 1.00 21.72 A

ATOM 784 CB ARG A 109 51.667 -10.160 22.139 1.00 23.48 A

ATOM 785 CG ARG A 109 52.630 -11.283 22.511 1.00 26.58 A

ATOM 786 CD ARG A 109 52.364 -12.493 21.627 1.00 21.06 A

ATOM 787 NE ARG A 109 53.134 -13.677 22.028 1.00 27.47 A

ATOM 788 CZ ARG A 109 54.420 -13.874 21.755 1.00 26.76 A

ATOM 789 NH1 ARG A 109 55.115 -12.965 21.071 1.00 30.79 A

ATOM 790 NH2 ARG A 109 55.014 -14.988 22.158 1.00 31.54 A

ATOM 791 C ARG A 109 51.056 -7.730 22.288 1.00 21.53 A

ATOM 792 O ARG A 109 50.129 -7.971 21.529 1.00 24.06 A

ATOM 793 N PRO A 110 51.432 -6.470 22.573 1.00 25.30 A

ATOM 794 CD PRO A 110 52.499 -6.067 23.509 1.00 28.30 A

ATOM 795 CA PRO A 110 50.742 -5.295 22.039 1.00 25.40 A

ATOM 796 CB PRO A 110 51.072 -4.223 23.067 1.00 28.00 A

ATOM 797 CG PRO A 110 52.512 -4.546 23.382 1.00 33.07 A

ATOM 798 C PRO A 110 51.104 -4.844 20.635 1.00 24.93 A

ATOM 799 O PRO A 110 50.488 -3.915 20.126 1.00 31.54 A

ATOM 800 N CYS A 111 52.056 -5.507 19.990 1.00 23.29 A

ATOM 801 CA CYS A 111 52.476 -5.059 18.672 1.00 29.21 A

ATOM 802 CB CYS A 111 54.015 -5.148 18.569 1.00 23.05 A ATOM 803 SG CYSA 111 54.829 -4.140 19.846 1.0036.29 A

ATOM 804 C CYSA 111 51.816 -5.742 17.482 1.0032.48 A

ATOM 805 O CYSA 111 52.276 -5.587 16.353 1.0030.99 A

ATOM 806 N LEU A 112 50.731 ^■ -6.473 17.735 1.0025.40 A

ATOM 807 CA LEU A 112 50.005 -7.178 16.690 1.0023.18 A

ATOM 808 CB LEU A 112 48.801 -7.911 17.295 1.0020.02 A

ATOM 809 CG LEU A 112 47.864 -8.609 16.305 1.0024.91 A

ATOM 810 CD1 LEU A 112 48.608 -9.742 15.593 1.0027.53 A

ATOM 811 CD2LEUA112 46.657 -9.163 17.068 1.0023.60 A

ATOM 812 C LEU A 112 49.513 ^■ -6.274 15.564 1.0024.34 A

ATOM 813 O LEU A 112 48.836 -5.278 15.821 1.0028.28 A

ATOM 814 N HISA113 49.829 - 6.642 14.325 1.0026.98 A

ATOM 815 CA HISA 113 49.405 -5.887 13.140 1.0031.14 A

ATOM 816 CB HISA 113 50.502 -5.876 12.061 1.0032.41 A

ATOM 817 CG HIS A 113 51.625 -4.932 12.349 1.0037.39 A

ATOM 818 CD2 HISA 113 52.197 -4.553 13.516 1.0038.82 A

ATOM 819 ND1 HISA113 52.302 -4.262 11.353 1.0041.80 A

ATOM 820 CE1 HISA113 53.242 -3.507 11.897 1.0048.05 A

ATOM 821 NE2HISA113 53.201 -3.666 13.209 1.0043.59 A

ATOM 822 C HISA113 48.142 -ι 6.487 12.537 1.0026.49 A

ATOM 823 O HISA113 47.926 - 7.700 12.601 1.0023.11 A

ATOM 824 N GLN A 114 47.311 -5.639 11.933 1.0022.66 A

ATOM 825 CA GLN A 114 46.066 -6.109 11.334 1.0024.25 A

ATOM 826 CB GLN A 114 45.232 -4.906 10.853 1.0025.32 A

ATOM 827 CG GLN A 114 44.741 -4.041 12.006 1.0025.37 A

ATOM 828 CD GLN A 114 43.858 -4.843 12.972 1.0023.76 A

ATOM 829 OE1 GLN A 114 42.784 ■ -5.345 12.603 1.0024.75 A

ATOM 830 NE2GLNA114 44.328 -4.988 14.207 1.0023.83 A

ATOM 831 C GLN A 114 46.227 -7.114 10.192 1.0021.45 A

ATOM 832 O GLN A 114 45.401 -8.003 10.041 1.0025.80 A

ATOM 833 N ASP A 115 47.275 ^■ -6.985 9.388 1.0023.01 A

ATOM 834 CA ASP A 115 47.437 -7.923 8.286 1.0024.77 A

ATOM 835 CB ASP A 115 48.562 -7.478 7.339 1.0028.75 A

ATOM 836 CG ASPA 115 49.896 -7.327 8.036 1.0037.85 A

ATOM 837 OD1 ASP A 115 49.951 -7.323 9.291 1.0046.17 A

ATOM 838 OD2ASPA115 50.898 l -7.194 7.314 1.0046.05 A

ATOM 839 C ASP A 115 47.692 ^■ -9.328 8.796 1.0020.79 A

ATOM 840 O ASP A 115 47.152- 10.280 8.256 1.0024.47 A

ATOM 841 N ASP A 116 48.502 • -9.451 9.846 1.0022.82 A

ATOM 842 CA ASPA 116 48.784 -10.758 10.419 1.0022.69 A

ATOM 843 CB ASPA 116 49.807 -10.660 11.552 1.0024.90 A

ATOM 844 CG ASP A 116 51.238 -10.628 11.045 1.0023.96 A

ATOM 845 OD1 ASP A 116 51.428 1-10.821 9.832 1.0031.59 A

ATOM 846 OD2ASPA116 52.158 i -10.430 11.865 1.0026.58 A

ATOM 847 C ASP A 116 47.483 - 11.317 10.968 1.0021.60 A

ATOM 848 O ASP A 116 47.171 - 12.468 10.739 1.0020.34 A

ATOM 849 N LEU A 117 46.735 - 10.487 11.690 1.0023.95 A

ATOM 850 CA LEU A 117 45.468 -10.917 12.269 1.0022.01 A

ATOM 851 CB LEU A 117 44.850 -9.783 13.084 1.0020.85 A

ATOM 852 CG LEU A 117 43.479 -10.068 13.713 1.0018.62 A

ATOM 853 CD1 LEUA117 43.495 -11.377 14.508 1.0022.76 A

ATOM 854 CD2LEUA117 43.132 -8.889 14.600 1.0022.77 A

ATOM 855 C LEU A 117 44.467 - 11.406 11.221 1.0020.47 A

ATOM 856 O LEU A 117 43.850 - 12.478 11.378 1.0022.04 A

ATOM 857 N ALAA 118 44.291 -^■ 10.624 10.159 1.0021.07 A

ATOM 858 CA ALAA 118 43.363 ^■ -11.009 9.100 1.0024.78 A

ATOM 859 CB ALAA 118 43.244 -9.887 8.048 1.0023.53 A ATOM 860 C ALAA 118 43.802-12.317 8.441 1.0023.04 A

ATOM 861 O ALAA 118 42.958-13.151 8.115 1.0026.43 A

ATOM 862 N ARG A 119 45.102-12.519 8.246 1.0027.95 A

ATOM 863 CA ARG A 119 45.533-13.760 7.616 1.0029.19 A

ATOM 864 CB ARG A 119 47.024-13.709 7.237 1.0030.71 A

ATOM 865 CG ARG A 119 47.278-13.113 5.845 1.0036.65 A

ATOM 866 CD ARG A 119 48.737-13.242 5.375 1.0034.57 A

ATOM 867 NE ARG A 119 49.659-12.656 6.332 1.0040.01 A

ATOM 868 CZ ARG A 119 50.588-13.339 6.991 1.0041.63 A

ATOM 869 NH1 ARG A 119 50.732-14.646 i 6.788 1.0045.99 A

ATOM 870 NH2ARGA119 51.349 -12.71 £ i 7.878 1.0037.56 A

ATOM 871 C ARG A 119 45.242-14.962 8.506 1.0028.69 A

ATOM 872 O ARG A 119 44.893-16.031 8.012 1.0026.98 A

ATOM 873 N LEU A 120 45.382-14.787 9.816 1.0026.20 A

ATOM 874 CA LEU A 120 45.090-15.864 10.766 1.0023.00 A

ATOM 875 CB LEU A 120 45.503-15.450 12.180 1.0018.65 A

ATOM 876 CG LEU A 120 45.296-16.530 13.263 ^"1.0024.57 A

ATOM 877 CD1 LEU A 120 46.285-17.670 13.008 1.0024.89 A

ATOM 878 CD2LEUA120 45.497-15.962 14.663 1.0019.06 A

ATOM 879 C LEU A 120 43.597-16.198 ^■ 10.785 1.0022.34 A

ATOM 880 O LEU A 120 43.196-17.371 10.832 1.0022.65 A

ATOM 881 N LEU A 121 42.773-15.156 ^■ 10.779 1.0020.79 A

ATOM 882 CA LEU A 121 41.338-15.333 10.816 1.0019.64 A

ATOM 883 CB LEU A 121 40.651 -13.967 10.982 1.0017.53 A

ATOM 884 CG LEU A 121 40.695-13.410 12.401 1.0032.93 A

ATOM 885 CD1 LEU A 121 40.194-11.969 12.442 1.0026.55 A

ATOM 886 CD2LEUA121 39.848-14.292 13.293 1.0028.08 A

ATOM 887 C LEU A 121 40.802-16.063 9.586 1.0022.73 A

ATOM 888 O LEU A 121 39.760-16.715 9.651 1.0020.18 A

ATOM 889 N ALAA 122 41.513-15.963 8.469 1.0022.06 A

ATOM 890 CA ALAA 122 41.068-16.626 7.247 1.0028.96 A

ATOM 891 CB ALA A 122 41.977-16.256 6.085 1.0034.80 A

ATOM 892 C ALAA 122 41.029-18.140 7.418 1.0033.12 A

ATOM 893 O ALAA 122 40.282-18.833 6.716 1.0031.70 A

ATOM 894 N LEU A 123 41.813-18.657 8.367 1.0027.58 A

ATOM 895 CA LEU A 123 41.855-20.106 8.612 1.0029.07 A

ATOM 896 CB LEU A 123 42.783 -20.434 9.789 1.0029.67 A

ATOM 897 CG LEU A 123 44.279-20.218 9.566 1.0032.03 A

ATOM 898 CD1 LEU A 123 45.039 -20.698 10.807 1.0032.57 A

ATOM 899 CD2LEUA123 44.741 -21.000 8.334 1.0036.08 A

ATOM 900 C LEU A 123 40.497 -20.779 8.864 1.0030.01 A

ATOM 901 O LEU A 123 40.328-21.975 8.596 1.0026.68 A

ATOM 902 N SERA 124 39.530 -20.028 9.379 1.0027.40 A

ATOM 903 CA SERA 124 38.220 -20.609 9.651 1.0025.54 A

ATOM 904 CB SER A 124 37.334-19.624 10.419 1.0029.50 A

ATOM 905 OG SERA 124 37.048-18.472 9.639 1.0026.90 A

ATOM 906 C SERA 124 37.505-21.035 8.365 1.0027.69 A

ATOM 907 O SERA 124 36.549-21.808 8.404 1.0031.33 A

ATOM 908 N GLU A 125 37.966 -20.527 7.231 1.0033.28 A

ATOM 909 CA GLU A 125 37.344 -20.863 5.957 1.0038.91 A

ATOM 910 CB GLU A 125 37.070-19.585 5.160 1.0037.88 A

ATOM 911 CG GLU A 125 36.360-18.520 5.986 1.0042.24 A

ATOM 912 CD GLU A 125 35.156-19.084 6.731 1.0043.92 A

ATOM 913 OE1 GLU A 125 35.048-18.867 7.959 1.0035.48 A

ATOM 914 OE2GLUA125 34.315-19.750 ι 6.089 1.0049.24 A

ATOM 915 C GLU A 125 38.215-21.811 5.143 1.0044.07 A

ATOM 916 O GLU A 125 37.932 -22.081 3.978 1.0053.04 A ATOM 917 N THRA 126 39.277-22.321 5.750 1.0043.05 A

ATOM 918 CA THRA126 40.157-23.234 5.039 1.0045.62 A

ATOM 919 CB THRA126 41.361 -22.482 4.415 1.0043.90 A

ATOM 920 OG1 THRA126 42.176-21.917 5.453 1.0045.54 A ATOM 921 CG2THRA126 40.875-21.364 3.503 1.0044.96 A

ATOM 922 C THR A 126 40.682-24.328 5.955 1.0048.52 A

ATOM 923 O THR A 126 41.397-25.224 5.507 1.0049.07 A

ATOM 924 N SERA 127 40.317-24.257 7.233 1.0045.05 A

ATOM 925 CA SER A 127 40.776-25.228 8.217 1.0045.95 A ATOM 926 CB SER A 127 41.895-24.629 9.080 1.0044.81 A

ATOM 927 OG SERA 127 42.250-25.515 10.131 1.0049.63 A

ATOM 928 C SERA 127 39.670-25.717 9.131 1.0044.97 A

ATOM 929 O SER A 127 38.686-25.020 9.380 1.0047.08 A

ATOM 930 N ARG A 128 39.855-26.933 9.626 1.0043.89 A ATOM 931 CA ARGA128 38.918-27.567 10.533 1.0042.93 A

ATOM 932 CB ARG A 128 38.604-28.990 10.042 1.0051.95 A

ATOM 933 CG ARG A 128 37.366-29.115 9.154 1.0054.74 A

ATOM 934 CD ARG A 128 36.093-29.168 10.004 1.0060.19 A

ATOM 935 NE ARG A 128 34.879-29.330 9.207 1.0062.65 A ATOM 936 CZ ARG A 128 34.401 -28.412 8.368 1.0068.49 A

ATOM 937 NH1 ARG A 128 35.035-27.257 8.212 1.0067.91 A

ATOM 938 NH2ARGA128 33.284-28.647 7.688 1.0067.50 A

ATOM 939 C ARG A 128 39.517-27.627 11.941 1.0042.19 A

ATOM 940 O ARG A 128 38.809-27.880 12.919 1.0044.76 A ATOM 941 N THR A 129 40.820-27.399 12.052 1.0041.39 A

ATOM 942 CA THR A 129 41.450-27.465 13.361 1.0040:78 A

ATOM 943 CB THR A 129 42.582-28.510 13.390 1.0042.20 A

ATOM 944 OG1THRA129 43.617-28.133 12.475 1.0050.78 A

ATOM 945 CG2 THRA 129 42.038-29.872 13.003 1.0040.95 A ATOM 946 C THRA 129 41.987-26.126 13.826 1.0034.67 A

ATOM 947 O THR A 129 42.095-25.884 15.022 1.0043.67 A

ATOM 948 N GLY A 130 42.312-25.250 12.888 1.0027.96 A

ATOM 949 CA GLY A 130 42.816-23.945 13.277 1.0025.79 A

ATOM 950 C GLY A 130 44.315-23.800 13.112 1.0026.64 A ATOM 951 O GLY A 130 44.957-24.641 12.489 1.0023.28 A

ATOM 952 N GLY A 131 44.872-22.727 13.664 1.0024.45 A

ATOM 953 CA GLY A 131 46.311 -22.504 13.550 1.0020.41 A

ATOM 954 C GLYA131 46.781 -21.350 14.417 1.0020.76 A

ATOM 955 O GLY A 131 46.020-20.813 15.226 1.0021.17 A ATOM 956 N ILE A 132 48.045-20.971 14.244 1.0021.83 A

ATOM 957 CA ILE A 132 48.640-19.893 15.024 1.0020.95 A

ATOM 958 CB ILE A 132 49.471 -20.449 16.226 1.0020.47 A

ATOM 959 CG21LEA132 48.697-21.537 16.941 1.0017.28 A

ATOM 960 CG1 ILEA132 50.786-21.066 15.717 1.0021.17 A ATOM 961 CD ILE A 132 51.801 -21.349 16.845 1.0021.54 A

ATOM 962 C ILEA132 49.591 -19.028 14.197 1.0017.76 A

ATOM 963 O ILE A 132 50.073-19.453 13.151 1.0023.88 A

ATOM 964 N LEU A 133 49.848-17.816 14.685 1.0021.08 A

ATOM 965 CA LEU A 133 50.792-16.913 14.050 1.0024.05 A ATOM 966 CB LEU A 133 50.607-15.488 14.564 1.0021.48 A

ATOM 967 CG LEU A 133 49.440-14.759 13.896 1.0023.30 A

ATOM 968 CD1 LEU A 133 49.384-13.275 14.336 1.0025.14 A

ATOM 969 CD2LEUA133 49.634-14.843 12.358 1.0025.37 A

ATOM 970 C LEU A 133 52.118-17.478 14.523 1.0025.59 A ATOM 971 O LEU A 133 52.216-17.977 15.649 1.0020.11 A

ATOM 972 N ALAA 134 53.140-17.402 13.677 1.0023.59 A

ATOM 973 CA ALA A 134 54.438-17.963 14.030 1.0025.45 A ATOM 974 CB ALA A 134 54.424-19.500 13.784 1.0023.71 A

ATOM 975 C ALAA 134 55.575-17.325 13.242 1.0027.73 A

ATOM 976 O ALA A 134 55.365-16.848 12.124 1.0024.04 A

ATOM 977 N ALAA 135 56.778-17.339 13.814 1.0023.49 A ATOM 978 CA ALA A 135 57.940-16.755 13.132 1.0025.63 A

ATOM 979 CB ALAA135 58.421 -15.478 13.869 1.0023.16 A

ATOM 980 C ALAA 135 59.072-17.768 13.033 1.0028.82 A

ATOM 981 O ALA A 135 59.425-18.420 14.013 1.0028.05 A

ATOM 982 N PRO A 136 59.663-17.906 11.838 1.0034.33 A ATOM 983 CD PRO A 136 59.348-17.142 10.618 1.0029.79 A

ATOM 984 CA PRO A 136 60.768-18.847 11.603 1.0031.03 A

ATOM 985 CB PRO A 136 61.129-18.594 10.141 1.0034.78 A

ATOM 986 CG PRO A 136 59.851 -18.048 9.546 1.0032.53 A

ATOM 987 C PRO A 136 61.973-18.611 12.518 1.0026.42 A ATOM 988 O PRO A 136 62.317-17.471 12.810 1.0023.61 A

ATOM 989 N VAL A 137 62.629-19.684 12.955 1.0025.72 A

ATOM 990 CA VALA137 63.804-19.563 13.816 1.0023.16 A

ATOM 991 CB VAL A 137 64.093-20.908 14.554 1.0024.83 A

ATOM 992 CG1 VAL A 137 65.507-20.897 15.190 1.0023.13 A ATOM 993 CG2VALA137 63.052-21.108 15.676 1.0024.16 A

ATOM 994 C VAL A 137 64.996-19.161 12.940 1.0027.04 A

ATOM 995 0 VALA137 65.161-19.683 11.836 1.0030.50 A

ATOM 996 N ARG A 138 65.803-18.223 13.432 1.0027.80 A

ATOM 997 CA ARGA138 66.971 -17.728 12.711 1.0031.83 A ATOM 998 CB ARG A 138 66.970-16.201 12.681 1.0034.01 A

ATOM 999 CG ARG A 138 65.773-15.562 12.000 1.0045.82 A

ATOM 1000 CD ARG A 138 65.929-14.040 12.029 1.0051.85 A

ATOM 1001 NE ARG A 138 64.853-13.351 11.321 1.0060.52 A

ATOM 1002 CZ ARG A 138 64.933-12.099 10.882 1.0059.91 A ATOM 1003 NH1 ARG A 138 66.046-11.398 11.082 1.0051.33 A

ATOM 1004 NH2ARGA138 63.904-11.558 10.239 1.0056.45 A

ATOM 1005 C ARG A 138 68.318-18.196 13.269 1.0031.64 A

ATOM 1006 O ARG A 138 69.192-18.599 12.510 1.0033.64 A

ATOM 1007 N ASP A 139 68.498-18.136 14.582 1.0027.62 A ATOM 1008 CA ASPA139 69.766-18.562 15.157 1.0027.35 A

ATOM 1009 CB ASP A 139 69.933-18.050 16.585 1.0031.60 A

ATOM 1010 CG ASP A 139 70.006-16.554 16.667 1.0027.85 A

ATOM 1011 OD1 ASPA139 70.589-15.936 15.751 1.0030.40 A

ATOM 1012 OD2ASPA139 69.488-16.012 17.671 1.0035.49 A ATOM 1013 C ASP A 139 69.892-20.068 15.217 1.0025.50 A

ATOM 1014 O ASP A 139 68.904-20.797 15.131 1.0025.21 A

ATOM 1015 N THR A 140 71.124-20.531 15.384 1.0024.74 A

ATOM 1016 CA THRA140 71.357-21.960 15.535 1.0025.72 A

ATOM 1017 CB THR A 140 72.876-22.279 15.523 1.0019.91 A ATOM 1018 OG1 THRA 140 73.375-22.103 14.197 1.0028.24 A

ATOM 1019 CG2 THRA 140 73.155-23.710 15.961 1.0020.51 A

ATOM 1020 C THR A 140 70.779-22.208 16.930 1.0025.65 A

ATOM 1021 O THRA 140 70.972-21.392 17.824 1.0024.08 A

ATOM 1022 N MET A 141 70.070-23.314 17.125 1.0023.51 A ATOM 1023 CA MET A 141 69.502-23.614 18.426 1.0022.08 A

ATOM 1024 CB META141 68.016-24.018 18.288 1.0019.77 A

ATOM 1025 CG MET A 141 66.989-22.902 18.021 1.0030.65 A

ATOM 1026 SD META141 66.965-21.538 19.189 1.0018.93 A

ATOM 1027 CE META141 67.771-20.517 18.219 1.0023.08 A ATOM 1028 C MET A 141 70.290-24.746 19.090 1.0028.16 A

ATOM 1029 O MET A 141 70.800-25.643 18.413 1.0028.96 A

ATOM 1030 N LYS A 142 70.407-24.681 20.419 1.0023.59 A ATOM 1031 CA LYS A 142 71.124 -25.698 21.186 1.00 25.71 A

ATOM 1032 CB LYS A 142 72.390 -25.115 21.821 1.00 25.60 A

ATOM 1033 CG LYS A 142 73.367 -24.457 20.872 1.00 30.53 A

ATOM 1034 CD LYS A 142 73.906 -25.424 19.831 1.00 25.24 A

ATOM 1035 CE LYS A 142 74.976 -24.730 18.994 1.00 29.76 A

ATOM 1036 NZ LYS A 142 75.561 -25.590 17.933 1.00 21.43 A

ATOM 1037 C LYS A 142 70.287 -26.269 22.329 1.00 26.37 A

ATOM 1038 O LYS A 142 69.632 -25.525 23.070 1.00 26.20 A

ATOM 1039 N ARG A 143 70.339 -27.588 22.490 1.00 27.82 A

ATOM 1040 CA ARG A 143 69.646 -28.259 23.579 1.00 30.30 A

ATOM 1041 CB ARG A 143 69.094 -29.612 23.110 1.00 30.18 A

ATOM 1042 CG ARG A 143 68.646 -30.519 24.239 1.00 35.06 A

ATOM 1043 CD ARG A 143 67.373 -29.999 24.867 1.00 29.87 A

ATOM 1044 NE ARG A 143 66.283 -29.964 23.895 1.00 29.44 A

ATOM 1045 CZ ARG A 143 65.186 -29.228 24.045 1.00 24.15 A

ATOM 1046 NH1 ARG A 143 65.041 -28.473 25.128 1.00 24.69 A

ATOM 1047 NH2 ARG A 143 64.244 -29.251 23.119 1.00 25.98 A

ATOM 1048 C ARG A 143 70.706 -28.486 24.670 1.00 30.42 A

ATOM 1049 O ARG A 143 71.766 -29.064 24.407 1.00 28.79 A

ATOM 1050 N ALA A 144 70.432 -28.019 25.883 1.00 26.70 A

ATOM 1051 CA ALA A 144 71.360 -28.182 26.995 1.00 32.38 A

ATOM 1052 CB ALA A 144 71.086 -27.125 28.056 1.00 31.20 A

ATOM 1053 C ALA A 144 71.226 -29.564 27.618 1.00 37.80 A

ATOM 1054 O ALA A 144 70.181 -30.208 27.500 1.00 30.99 A

ATOM 1055 N GLU A 145 72.287 -30.010 28.281 1.00 33.68 A

ATOM 1056 CA GLU A 145 72.267 -31.299 28.956 1.00 33.78 A

ATOM 1057 CB GLU A 145 73.681 -31.746 29.315 1.00 39.72 A

ATOM 1058 CG GLU A 145 74.519 -32.054 28.088 1.00 36.69 A

ATOM 1059 CD GLU A 145 75.874 -32.660 28.419 1.00 50.16 A

ATOM 1060 OE1 GLU A 145 76.564 -32.141 29.329 1.00 44.36 A

ATOM 1061 OE2 GLU A 145 76.257 -33.654 27.761 1.00 48.24 A

ATOM 1062 C GLU A 145 71.416 -31.131 30.201 1.00 41.12 A

ATOM 1063 O GLU A 145 71.443 -30.072 30.841 1.00 33.17 A

ATOM 1064 N PRO A 146 70.643 -32.175 30.554 1.00 42.14 A

ATOM 1065 CD PRO A 146 70.796 -33.533 29.998 1.00 44.90 A

ATOM 1066 CA PRO A 146 69.750 -32.202 31.712 1.00 48.22 A

ATOM 1067 CB PRO A 146 69.701 -33.682 32.066 1.00 45.99 A

ATOM 1068 CG PRO A 146 69.694 -34.308 30.708 1.00 48.46 A

ATOM 1069 C PRO A 146 70.161 -31.328 32.882 1.00 49.31 A

ATOM 1070 O PRO A 146 69.526 -30.313 33.155 1.00 55.93 A

ATOM 1071 N GLY A 147 71.227 -31.705 33.571 1.00 49.59 A

ATOM 1072 CA GLY A 147 71.635 -30.915 34.715 1.00 58.44 A

ATOM 1073 C GLY A 147 72.964 -30.225 34.529 1.00 60.62 A

ATOM 1074 O GLY A 147 73.829 -30.295 35.403 1.00 64.08 A

ATOM 1075 N LYS A 148 73.129 -29.548 33.400 1.00 54.83 A

ATOM 1076 CA LYS A 148 74.381 -28.869 33.121 1.00 54.32 A

ATOM 1077 CB LYS A 148 75.412 -29.892 32.626 1.00 58.05 A

ATOM 1078 CG LYS A 148 75.897 -30.848 33.726 1.00 61.10 A

ATOM 1079 CD LYS A 148 76.162 -32.259 33.205 1.00 64.34 A

ATOM 1080 CE LYS A 148 76.558 -33.201 34.339 1.00 62.92 A

ATOM 1081 NZ LYS A 148 76.784 -34.601 33.874 1.00 64.16 A

ATOM 1082 C LYS A 148 74.195 -27.743 32.108 1.00 53.05 A

ATOM 1083 O LYS A 148 73.197 -27.696 31.388 1.00 54.61 A

ATOM 1084 N ASN A 149 75.143 -26.817 32.070 1.00 48.31 A

ATOM 1085 CA ASN A 149 75.047 -25.712 31.136 1.00 47.84 A

ATOM 1086 CB ASN A 149 75.366 -24.391 31.837 1.00 48.75 A

ATOM 1087 CG ASN A 149 74.133 -23.520 32.024 1.00 54.19 A ATOM 1088 OD1 ASN A 149 74.231 -22.380 32.466 1.0065.56 A

ATOM 1089 ND2ASNA149 72.964-24.057 31.684 1.0050.82 A

ATOM 1090 C ASN A 149 75.993-25.94729.972 1.0044.48 A

ATOM 1091 O ASN A 149 76.721 -25.056 29.551 1.0050.18 A ATOM 1092 N ALA A 150 75.977-27.17429.473 1.0041.41 A

ATOM 1093 CA ALAA 150 76.800-27.573 28.355 1.0036.46 A

ATOM 1094 CB ALAA 150 77.733-28.694 28.776 1.0039.25 A

ATOM 1095 C ALAA 150 75.863-28.042 27.243 1.0032.20 A

ATOM 1096 O ALA A 150 74.743-28.49527.495 1.0035.67 A ATOM 1097 N ILE A 151 76.326-27.929 26.009 1.0029.49 A

ATOM 1098 CA ILE A 151 75.537-28.333 24.863 1.0028.87 A

ATOM 1099 CB ILE A 151 76.115-27.73023.589 1.0027.43 A

ATOM 1100 CG2 ILE A 151 75.277-28.14322.385 1.0026.12 A

ATOM 1101 CG1 ILEA 151 76.160-26.19823.727 1.0025.51 A ATOM 1102 CD ILEA 151 76.771 -25.52322.531 1.0024.00 A

ATOM 1103 C ILEA 151 75.445-29.843 24.663 1.0026.67 A

ATOM 1104 O ILEA 151 76.464-30.532 24.582 1.0028.74 A

ATOM 1105 N ALA A 152 74.221 -30.35324.593 1.0025.35 A

ATOM 1106 CA ALAA 152 73.999-31.777 24.349 1.0027.34 A ATOM 1107 CB ALAA 152 72.581 -32.169 24.759 1.0031.23 A

ATOM 1108 C ALAA152 74.176-31.98722.855 1.0026.66 A

ATOM 1109 O ALA A 152 75.011 -32.780 22.423 1.0028.64 A

ATOM 1110 N HIS A 153 73.359-31.273 22.080 1.0025.29 A

ATOM 1111 CA HIS A 153 73.397-31.313 20.622 1.0029.62 A ATOM 1112 CB HISA153 72.727-32.58520.081 1.0032.35 A

ATOM 1113 CG HIS A 153 71.321 -32.76920.554 1.0036.67 A

ATOM 1114 CD2 HISA 153 70.146-32.311 20.062 1.0033.31 A

ATOM 1115 ND1 HISA153 71.014-33.426 21.728 1.0036.91 A

ATOM 1116 CE1 HISA153 69.713-33.35521.941 1.0038.35 A ATOM 1117 NE2 HISA 153 69.162-32.682 20.946 1.0037.49 A

ATOM 1118 C HIS A 153 72.676-30.094 20.038 1.0024.65 A

ATOM 1119 O HIS A 153 72.005-29.34320.748 1.0027.25 A

ATOM 1120 N THRA 154 72.834-29.900 18.735 1.0027.29 A

ATOM 1121 CA THR A 154 72.204-28.798 18.047 1.0027.85 A ATOM 1122 CB THR A 154 72.983-28.443 16.773 1.0023.93 A

ATOM 1123 OG1 THRA 154 74.177-27.747 17.134 1.0024.26 A

ATOM 1124 CG2 THRA 154 72.163-27.588 15.842 1.0024.63 A

ATOM 1125 C THRA 154 70.795-29.202 17.656 1.0022.25 A

ATOM 11260 THRA 154 70.558-30.353 17.297 1.0024.48 A ATOM 1127 N VAL A 155 69.866-28.260 17.749 1.0022.22 A

ATOM 1128 CA VAL A 155 68.481 -28.522 17.361 1.0028.08 A

ATOM 1129 CB VAL A 155 67.489-27.906 18.373 1.0030.09 A

ATOM 1130 CG1 VAL A 155 66.046-28.191 17.935 1.0027.84 A

ATOM 1131 CG2VALA155 67.738-28.486 19.746 1.0033.47 A ATOM 1132 C VAL A 155 68.305-27.871 15.997 1.0025.10 A

ATOM 1133 0 VAL A 155 68.446-26.661 15.873 1.0026.47 A

ATOM 1134 N ASP A 156 67.980-28.665 14.981 1.0025.79 A

ATOM 1135 CA ASPA156 67.824-28.143 13.616 1.0030.12 A

ATOM 1136 CB ASP A 156 67.407-29.286 12.672 1.0034.60 A ATOM 1137 CG ASP A 156 67.442-28.881 11.210 1.0036.20 A

ATOM 1138 OD1 ASP A 156 67.863-27.737 10.930 1.0036.63 A

ATOM 1139 OD2 ASP A 156 67.055-29.703 10.345 1.0043.11 A

ATOM 1140 C ASP A 156 66.843-26.965 13.509 1.0025.62 A

ATOM 1141 O ASP A 156 65.664-27.111 13.794 1.0027.19 A ATOM 1142 N ARG A 157 67.350-25.801 13.106 1.0028.06 A

ATOM 1143 CA ARGA157 66.518-24.595 12.995 1.0030.65 A

ATOM 1144 CB ARG A 157 67.392-23.334 12.920 1.0035.87 A ATOM 1145 CG ARG A 157 68.297-23.270 11.703 1.0031.98 A

ATOM 1146 CD ARGA157 69.134-22.009 11.701 1.0032.68 A

ATOM 1147 NE ARG A 157 70.160-22.038 10.662 1.0034.98 A

ATOM 1148 CZ ARG A 157 71.187-21.197 10.604 1.0040.01 A ATOM 1149 NH1 ARG A 157 71.321 -20.257 11.535 1.0030.29 A

ATOM 1150 NH2ARGA157 72.082-21.304 9.624 1.0031.13 A

ATOM 1151 C ARG A 157 65.587-24.632 11.791 1.0034.05 A

ATOM 1152 O ARG A 157 64.653-23.826 11.683 1.0030.56 A

ATOM 1153 N ASNA158 65.861 -25.551 10.872 1.0036.16 A ATOM 1154 CA ASN A 158 65.025-25.689 9.690 1.0038.54 A

ATOM 1155 CB ASN A 158 65.744-26.533 8.618 1.0041.88 A

ATOM 1156 CG ASN A 158 67.038-25.876 8.112 1.0053.99 A

ATOM 1157 OD1 ASN A 158 67.030-24.747 7.599 1.0051.76 A

ATOM 1158 ND2ASNA158 68.155-26.587 8.255 1.0053.26 A ATOM 1159 C ASN A 158 63.728-26.354 10.144 1.0032.84 A

ATOM 1160 O ASN A 158 63.758-27.370 10.834 1.0030.73 A

ATOM 1161 N GLYA 159 62.594-25.750 9.782 1.0033.23 A

ATOM 1162 CA GLYA159 61.295-26.282 10.164 1.0031.87 A

ATOM 1163 C GLY A 159 60.939-25.965 11.612 1.0028.76 A ATOM 1164 O GLYA 159 59.938-26.439 12.136 1.0029.41 A

ATOM 1165 N LEU A 160 61.769-25.158 12.264 1.0028.69 A

ATOM 1166 CA LEU A 160 61.524-24.795 13.649 1.0023.98 A

ATOM 1167 CB LEU A 160 62.838-24.809 14.435 1.0026.54 A

ATOM 1168 CG LEU A 160 62.706-24.798 15.957 1.0024.94 A ATOM 1169 CD1 LEU A 160 62.018-26.065 16.457 1.0029.00 A

ATOM 1170 CD2LEUA160 64.083-24.693 16.566 1.0028.96 A

ATOM 1171 C LEU A 160 60.897-23.400 13.684 1.0027.29 A

ATOM 1172 O LEU A 160 61.370-22.482 13.010 1.0023.82 A

ATOM 1173 N TRP A 161 59.832-23.248 14.467 1.0023.84 A ATOM 1174 CA TRPA161 59.124-21.968 14.551 1.0020.56 A

ATOM 1175 CB TRP A 161 57.748-22.070 13.872 1.0020.57 A

ATOM 1176 CG TRP A 161 57.796-22.329 12.396 1.0027.92 A

ATOM 1177 CD2TRPA161 57.439-21.415 11.357 1.0025.22 A

ATOM 1178 CE2 TRP A 161 57.601 -22.095 10.125 1.0029.23 A ATOM 1179 CE3TRPA161 56.980-20.089 11.341 1.0025.62 A

ATOM 1180 CD1 TRP A 161 58.167-23.493 11.774 1.0028.31 A

ATOM 1181 NE1 TRPA161 58.054-23.360 10.413 1.0030.05 A

ATOM 1182 CZ2TRPA161 57.337-21.494 8.892 1.0029.35 A

ATOM 1183 CZ3TRPA161 56.714-19.488 10.112 1.0035.71 A ATOM 1184 CH2TRPA161 56.890-20.198 8.902 1.0034.04 A

ATOM 1185 C TRP A 161 58.893-21.473 15.965 1.0023.31 A

ATOM 1186 O TRP A 161 58.779-22.250 16.927 1.0025.66 A

ATOM 1187 N HISA162 58.841 -20.149 16.058 1.0027.90 A

ATOM 1188 CA HIS A 162 58.535-19.433 17.283 1.0023.36 A ATOM 1189 CB HIS A 162 59.014-17.981 17.203 1.0022.62 A

ATOM 1190 CG HIS A 162 60.473-17.783 17.465 1.0023.65 A

ATOM 1191 CD2 HISA 162 61.517-17.631 16.616 1.0029.38 A

ATOM 1192 ND1 HIS A 162 60.980-17.631 18.735 1.0029.50 A

ATOM 1193 CE1 HISA162 62.277-17.388 18.659 1.0031.62 A ATOM 1194 NE2HISA162 62.630-17.383 17.386 1.0022.48 A

ATOM 1195 C HIS A 162 57.006-19.362 17.294 1.0025.86 A

ATOM 1196 O HIS A 162 56.422-18.812 16.369 1.0024.70 A

ATOM 1197 N ALA A 163 56.352-19.912 18.306 1.0026.24 A

ATOM 1198 CA ALAA163 54.904-19.800 18.341 1.0024.70 A ATOM 1199 CB ALAA 163 54.310-20.898 19.212 1.0020.38 A

ATOM 1200 C ALAA163 54.574-18.411 18.913 1.0020.12 A

ATOM 1201 O ALAA 163 55.160-17.979 19.919 1.0019.24 A . ATOM 1202 N LEU A 164 53.658-17.704 18.263 1.0016.87 A

ATOM 1203 CA LEU A 164 53.252-16.387 18.727 1.0021.64 A

ATOM 1204 CB LEU A 164 53.516-15.358 17.628 1.0022.15 A

ATOM 1205 CG LEU A 164 54.945-15.331 17.060 1.0028.58 A

ATOM 1206 CD1 LEU A 164 55.004-14.419 15.851 1.0026.97 . A

ATOM 1207 CD2LEUA164 55.930-14.853 18.132 1.0020.89 A

ATOM 1208 C LEU A 164 51.744-16.475 18.991 1.0020.46 A

ATOM 1209 O LEU A 164 51.180-17.563 19.031 1.0020.16 A

ATOM 1210 N THRA 165 51.097-15.335 19.183 1.0017.73 A

ATOM 1211 CA THRA 165 49.643-15.314 19.347 1.0018.75 A

ATOM 1212 CB THR A 165 49.146-15.226 20.847 1.0016.44 A

ATOM 1213 OG1 THR A 165 49.411-13.931 21.370 1.0018.30 A

ATOM 1214 CG2THRA165 49.813-16.295 21.731 1.0019.63 A

ATOM 1215 C THRA 165 49.218-14.074 18.578 1.0018.15 A

ATOM 1216 O THRA 165 50.025-13.171 18.344 1.0021.96 A

ATOM 1217 N PRO A 166 47.933-13.987 18.227 1.0018.69 A

ATOM 1218 CD PRO A 166 47.384-12.825 17.515 1.0018.60 A

ATOM 1219 CA PRO A 166 46.884-14.967 18.512 1.0018.06 A

ATOM 1220 CB PRO A 166 45.607-14.312 17.951 1.0018.16 A

ATOM 1221 CG PRO A 166 45.922-12.879 17.929 1.0019.78 A

ATOM 1222 C PRO A 166 47.021 -16.378 17.963 1.0021.86 A

ATOM 1223 O PRO A 166 47.753-16.656 17.014 1.0017.92 A

ATOM 1224 N GLN A 167 46.228-17.243 18.580 1.0019.50 A

ATOM 1225 CA GLN A 167 46.095-18.648 18.237 1.0018.36 A

ATOM 1226 CB GLN A 167 46.644-19.508 19.377 1.0016.46 A

ATOM 1227 CG GLN A 167 48.132-19.176 19.601 1.0015.32 A

ATOM 1228 CD GLN A 167 48.952-20.34620.175 1.0021.79 A

ATOM 1229 OE1 GLN A 167 48.398-21.377 20.587 1.0020.55 A

ATOM 1230 NE2GLNA167 50.285-20.181 20.201 1.0020.06 A

ATOM 1231 C GLN A 167 44.582-18.767 18.047 1.0024.49 A

ATOM 1232 O GLN A 167 43.813-18.398 18.929 1.0021.28 A

ATOM 1233 N PHEA 168 44.177-19.277 16.885 1.0021.99 A

ATOM 1234 CA PHE A 168 42.766-19.341 16.481 1.0021.35 A

ATOM 1235 CB PHE A 168 42.687-18.572 15.151 1.0017.98 A

ATOM 1236 CG PHE A 168 41.290-18.240 14.693 1.0017.59 A

ATOM 1237 CD1 PHE A 168 40.375-17.698 15.584 1.0020.08 A

ATOM 1238 CD2PHEA168 40.919-18.392 13.358 1.0024.64 A

ATOM 1239 CE1 PHEA 168 39.100-17.297 15.155 1.0016.26 A

ATOM 1240 CE2 PHEA 168 39.634-17.995 12.912 1.0018.20 A

ATOM 1241 CZ PHE A 168 38.733-17.447 13.819 1.0025.36 A

ATOM 1242 C PHE A 168 42.247-20.777 16.335 1.0020.20 A

ATOM 1243 O PHEA 168 42.785-21.537 15.528 1.0022.22 A

ATOM 1244 N PHE A 169 41.219-21.143 17.098 1.0020.89 A

ATOM 1245 CA PHE A 169 40.696-22.514 17.040 1.0020.61 A

ATOM 1246 CB PHE A 169 41.331 -23.372 18.147 1.0022.37 A

ATOM 1247 CG PHE A 169 42.818-23.508 18.036 1.0021.21 A

ATOM 1248 CD1 PHE A 169 43.663-22.754 18.847 1.0025.39 A

ATOM 1249 CD2PHEA169 43.371-24.382 17.117 1.0024.72 A

ATOM 1250 CE1 PHE A 169 45.059-22.871 18.742 1.0024.15 A

ATOM 1251 CE2PHEA169 44.747-24.510 17.000 1.0029.52 A

ATOM 1252 CZ PHE A 169 45.594-23.751 17.814 1.0024.47 A

ATOM 1253 C PHE A 169 39.199-22.596 17.222 1.0020.32 A

ATOM 1254 O PHE A 169 38.574-21.651 17.682 1.0020.19 A

ATOM 1255 N PRO A 170 38.602-23.742 16.850 1.0025.60 A

ATOM 1256 CD PRO A 170 39.166-24.827 16.024 1.0021.64 A

ATOM 1257 CA PRO A 170 37.156-23.897 17.031 1.0022.96 A

ATOM 1258 CB PRO A 170 36.868-25.292 16.456 1.0019.67 A ATOM 1259 CG PRO A 170 37.909-25.446 15.369 1.0025.84 A

ATOM ' 1260 C PRO A 170 37.019-23.851 18.557 1.0023.02 A

ATOM 1261 O PRO A 170 37.823-24.455 19.270 1.0020.61 A

ATOM ' 1262 N ARG A 171 36.013-23.135 19.046 1.0019.58 A

ATOM 1263 CA ARG A 171 35.795-22.939 20.479 1.0027.75 A

ATOM ' 1264 CB ARG A 171 34.553 -22.067 20.679 1.0031.50 A

ATOM ' 265 CG ARG A 171 34.529-21.272 21.967 1.0033.72 A

ATOM ' 1266 CD ARG A 171 33.110-21.075 22.502 1.0046.03 A

ATOM ' 1267 NE ARG A 171 32.620 -22.300 23.125 1.0045.83 A

ATOM 1268 CZ ARG A 171 31.709-23.103 22.593 1.0040.61 A

ATOM ' 1269 NH1 ARG A 171 31.167-22.810 21.422 1.0047.16 A

ATOM 1270 NH2ARGA171 31.368-24.222 23.216 1.0048.85 A

ATOM ' 1271 C ARG A 171 35.672-24.181 21.367 1.0021.21 A

ATOM 1272 O ARG A 171 36.435-24.371 22.325 1.0026.16 A

ATOM ^• 1273 N GLU A 172 34.694-25.027 21.064 1.0021.99 A

ATOM 1274 CA GLU A 172 34.489-26.22621.877 1.0023.36 A

ATOM ' 1275 CB GLU A 172 33.154-26.903 21.491 1.0030.61 A

ATOM ' 1276 CG GLU A 172 32.513-27.736 22.624 1.0034.68 A

ATOM ' 1277 CD GLU A 172 31.185-28.391 22.213 1.0044.59 A

ATOM ' 1278 OE1 GLU A 172 31.191 -29.590 21.840 1.0038.35 A

ATOM 1279 OE2GLUA172 30.139-27.698 22.256 1.0038.39 A

ATOM ' 1280 C GLU A 172 35.661 -27.216 21.783 1.0023.87 A

ATOM 1281 O GLU A 172 36.039-27.831 22.784 1.0025.07 A

ATOM ' 1282 N LEU A 173 36.246-27.362 20.596 1.0022.72 A

ATOM 1283 CA LEU A 173 37.383-28.25620.432 1.0024.14 A

ATOM ' 1284 CB LEU A 173 37.858-28.276 18.964 1.0026.48 A

ATOM 1285 CG LEU A 173 39.029-29.209 18.636 1.0026.96 A

ATOM ' 1286 CD1 LEU A 173 38.695-30.618 19.100 1.0031.40 A

ATOM ' 1287 CD2LEUA173 39.317-29.206 17.141 1.0023.02 A

ATOM 1288 C LEU A 173 38.518-27.786 21.350 1.0022.61 A

ATOM ' 1289 O LEU A 173 39.086-28.581 22.120 1.0025.96 A

ATOM 1290 N LEU A 174 38.843-26.498 21.290 1.0022.40 A

ATOM ' 1291 CA LEU A 174 39.913-25.963 22.142 1.0023.75 A

ATOM 1292 CB LEU A 174 40.124-24.45621.868 1.0020.05 A

ATOM ' 1293 CG LEU A 174 41.183-23.786 22.750 1.0028.30 A

ATOM 1294 CD1 LEU A 174 42.520-24.541 22.588 1.0029.73 A

ATOM ' 1295 CD2LEUA174 41.349-22.299 22.379 1.0022.03 A

ATOM 1296 C LEU A 174 39.547-26.178 23.611 1.0023.44 A

ATOM ' 1297 O LEU A 174 40.363-26.63524.411 1.0024.58 A

ATOM 1298 N HIS A 175 38.313-25.840 23.961 1.0025.20 A

ATOM 1299 CA HIS A 175 37.852-26.001 25.331 1.0027.11 A

ATOM 1300 CB HIS A 175 36.381-25.610 25.427 1.0032.98 A

ATOM 1301 CG HIS A 175 35.760-25.91826.752 1.0038.21 A

ATOM ' 1302 CD2HISA175 35.470-25.119 27.805 1.0037.72 A

ATOM 1303 ND1 HIS A 175 35.388-27.193 27.121 1.0036.09 A

ATOM ' 1304 CE1 HIS A 175 34.899-27.166 28.348 1.0036.63 A

ATOM 1305 NE2HISA175 34.939-25.92028.786 1.0037.11 A

ATOM ' 1306 C HIS A 175 38.039-27.433 25.845 1.0023.87 A

ATOM 1307 O HIS A 175 38.566-27.658 26.944 1.0026.85 A

ATOM ' 1308 N ASP A 176 37.605-28.401 25.047 1.0027.06 A

ATOM 1309 CA ASP A 176 37.708-29.799 25.426 1.0028.12 A

ATOM 1310 CB ASP A 176 36.839-30.663 24.501 1.0028.42 A

ATOM ' 1311 CG ASP A 176 35.352-30.343 24.629 1.0033.87 A

ATOM 1312 OD1 ASP A 176 34.951-29.71225.634 1.0031.79 A

ATOM ' 1313 OD2ASPA176 34.577-30.732 23.734 1.0031.04 A

ATOM 1314 C ASP A 176 39.130-30.33825.460 1.0031.20 A

ATOM ' 1315 O ASP A 176 39.488-31.103 26.365 1.0029.68 A ATOM 1316 N CYS A 177 39.950-29.94724.487 1.0024.43 A

ATOM 1317 CA CYS A 177 41.336-30.411 24.463 1.0024.37 A

ATOM 1318 CB CYS A 177 41.997-30.028 23.136 1.0026.45 A

ATOM 1319 SG CYSA177 41.321-30.860 21.704 1.0031.85 A ATOM 1320 C CYS A 177 42.123-29.82525.641 1.0029.28 A

ATOM 1321 O CYS A 177 42.929-30.516 26.272 1.0024.42 A

ATOM 1322 N LEU A 178 41.876-28.55325.954 1.0027.82 A

ATOM 1323 CA LEU A 178 42.578-27.93327.068 1.0029.15 A

ATOM 1324 CB LEU A 178 42.313-26.42527.096 1.0024.68 A ATOM 1325 CG LEU A 178 43.103-25.587 28.103 1.0028.29 A

ATOM 1326 CD1 LEU A 178 44.609-25.729 27.858 1.0024.01 A

ATOM 1327 CD2LEUA178 42.670-24.142 27.986 1.0031.36 A

ATOM 1328 C LEU A 178 42.148-28.583 28.390 1.0033.36 A

ATOM 1329 O LEU A 178 42.983-28.896 29.234 1.0027.27 A ATOM 1330 N THRA 179 40.848-28.808 28.561 1.0035.46 A

ATOM 1331 CA THR A 179 40.348-29.428 29.777 1.0032.88 A

ATOM 1332 CB THR A 179 38.818-29.60329.743 1.0036.98 A

ATOM 1333 OG1 THRA 179 38.197-28.319 29.682 1.0032.55 A

ATOM 1334 CG2 THRA 179 38.332-30.345 30.991 1.0033.89 A ATOM 1335 C THR A 179 40.968-30.808 29.942 1.0031.51 A

ATOM 1336 O THRA 179 41.447-31.158 31.020 1.0034.69 A

ATOM 1337 N ARG A 180 40.952-31.59428.872 1.0027.44 A

ATOM 1338 CA ARG A 180 41.511 -32.944 28.925 1.0032.63 A

ATOM 1339 CB ARG A 180 41.259-33.67627.591 1.0038.39 A ATOM 1340 CG ARGA180 41.797-35.111 27.498 1.0038.63 A

ATOM 1341 CD ARG A 180 41.378-35.747 26.163 1.0048.42 A

ATOM 1342 NE ARG A 180 42.468-36.44225.473 1.0052.71 A

ATOM 1343 CZ ARG A 180 42.484-36.704 24.162 1.0057.37 A

ATOM 1344 NH1 ARG A 180 41.469-36.330 23.393 1.0058.81 A ATOM 1345 NH2ARGA180 43.520-37.333 23.612 1.0057.50 A

ATOM 1346 C ARG A 180 43.007-32.932 29.265 1.0036.27 A

ATOM 1347 O ARG A 180 43.453-33.66530.161 1.0034.74 A

ATOM 1348 N ALAA 181 43.779-32.089 28.576 1.0027.46 A

ATOM 1349 CA ALAA 181 45.216-32.02228.828 1.0034.07 A ATOM 1350 CB ALAA 181 45.886-31.032 27.874 1.0030.80 A

ATOM 1351 C ALAA 181 45.507-31.638 30.274 1.0038.88 A

ATOM 1352 O ALAA 181 46.304-32.294 30.954 1.0037.81 A

ATOM 1353 N LEU A 182 44.863-30.574 30.740 1.0033.28 A

ATOM 1354 CA LEUA182 45.056-30.119 32.109 1.0037.15 A ATOM 1355 CB LEU A 182 44.258-28.835 32.366 1.0035.37 A

ATOM 1356 CG LEU A 182 44.836-27.580 31.684 1.0037.20 A

ATOM 1357 CD1 LEU A 182 43.861 -26.409 31.829 1.0038.56 A

ATOM 1358 CD2LEUA182 46.188-27.235 32.302 1.0042.55 A

ATOM 1359 C LEU A 182 44.654-31.200 33.118 1.0043.30 A ATOM 1360 O LEU A 182 45.323-31.379 34.129 1.0040.78 A

ATOM 1361 N ASN A 183 43.565-31.915 32.842 1.0042.67 A

ATOM 1362 CA ASNA183 43.117-32.981 33.734 1.0045.95 A

ATOM 1363 CB ASN A 183 41.773-33.552 33.271 1.0042.58 A

ATOM 1364 CG ASN A 183 40.584-32.730 33.754 1.0043.14 A ATOM 1365 OD1 ASN A 183 39.444-33.005 33.390 1.0046.52 A

ATOM 1366 ND2ASNA183 40.846-31.726 34.584 1.0047.13 A

ATOM 1367 C ASN A 183 44.148-34.107 33.791 1.0047.24 A

ATOM 1368 O ASN A 183 44.375-34.701 34.844 1.0046.63 A

ATOM 1369 N GLU A 184 44.770-34.39332.654 1.0046.16 A ATOM 1370 CA GLU A 184 45.772-35.442 32.575 1.0043.60 A

ATOM 1371 CB GLU A 184 45.720-36.090 31.186 1.0038.52 A

ATOM 1372 CG GLU A 184 44.554-37.069 31.022 1.0030.01 A ATOM 1373 CD GLU A 184 44.204-37.37429.565 1.0039.87 A

ATOM 1374 OE1 GLU A 184 45.109-37.34828.704 1.0043.83 A

ATOM 1375 OE2 GLU A 184 43.018-37.66229.280 1.0040.89 A

ATOM 1376 C GLU A 184 47.172-34.91432.902 1.0044.99 A ATOM 1377 O GLU A 184 48.183-35.56532.629 1.0044.80 A

ATOM 1378 N GLY A 185 47.211 -33.72533.500 1.0045.32 A

ATOM 1379 CA GLYA 185 48.463-33.102 33.899 1.0046.40 A

ATOM 1380 C GLY A 185 49.537-32.950 32.843 1.0046.00 A

ATOM 1381 O GLYA185 50.714-33.17933.121 1.0049.53 A ATOM 1382 N ALAA186 49.152-32.55531.635 1.0042.61 A

ATOM 1383 CA ALAA 186 50.123-32.379 30.562 1.0042.07 A

ATOM 1384 CB ALAA 186 49.463-32.64829.214 1.0047.06 A

ATOM 1385 C ALAA 186 50.720-30.96930.589 1.0040.77 A

ATOM 1386 O ALAA 186 50.160-30.062 31.204 1.0040.17 A ATOM 1387 N THR A 187 51.860-30.797 29.925 1.0040.52 A

ATOM 1388 CA THR A 187 52.537-29.501 29.854 1.0043.28 A

ATOM 1389 CB THRA 187 54.032-29.668 29.529 1.0043.23 A

ATOM 1390 OG1 THR A 187 54.640-30.55530.479 1.0048.91 A

ATOM 1391 CG2THRA187 54.733-28.326 29.581 1.0036.64 A ATOM 1392 C THRA 187 51.908-28.68328.730 1.0036.95 A

ATOM 1393 O THRA 187 52.054-29.030 27.559 1.0038.01 A

ATOM 1394 N ILEA188 51.233-27.59529.081 1.0038.12 A

ATOM 1395 CA ILE A 188 50.557-26.76328.084 1.0033.23 A

ATOM 1396 CB ILE A 188 49.039-26.80828.317 1.0031.44 A ATOM 1397 CG2 ILE A 188 48.297-26.08527.197 1.0030.91 A

ATOM 1398 CG1 ILE A 188 48.581 -28.260 28.354 1.0035.10 A

ATOM 1399 CD ILE A 188 47.399-28.46229.274 1.0046.06 A

ATOM 1400 C ILEA188 51.016-25.312 28.135 1.0030.03 A

ATOM 1401 O ILE A 188 50.564-24.550 28.984 1.0033.74 A ATOM 1402 N THRA 189 51.893-24.923 27.212 1.0027.65 A

ATOM 1403 CA THRA 189 52.401-23.55527.189 1.0024.61 A

ATOM 1404 CB THRA 189 53.911-23.52826.905 1.0020.05 A

ATOM 1405 OG1 THR A 189 54.168-24.149 25.642 1.0023.58 A

ATOM 1406 CG2 THR A 189 54.665-24.27627.998 1.0024.86 A ATOM 1407 C THRA 189 51.691-22.632 26.212 1.0026.56 A

ATOM 1408 O THRA189 51.950-21.424 26.172 1.0025.97 A

ATOM 1409 N ASP A 190 50.826-23.20525.388 1.0023.70 A

ATOM 1410 CA ASP A 190 50.015-22.401 24.486 1.0028.06 A

ATOM 1411 CB ASPA190 50.824-21.86823.284 1.0022.09 A ATOM 1412 CG ASP A 190 51.194-22.919 22.275 1.0024.30 A

ATOM 1413 OD1ASPA190 50.987-24.131 22.509 1.0024.69 A

ATOM 1414 OD2ASPA190 51.707-22.508 21.200 1.0021.73 A

ATOM 1415 C ASP A 190 48.787-23.221 24.099 1.0023.26 A

ATOM 1416 O ASPA190 48.623-24.34424.582 1.0021.66 A ATOM 1417 N GLU A 191 47.896-22.653 23.297 1.0023.73 A

ATOM 1418 CA GLU A 191 46.672-23.36322.920 1.0022.24 A

ATOM 1419 CB GLU A 191 45.630-22.385 22.375 1.0023.88 A

ATOM 1420 CG GLU A 191 45.059-21.45723.435 1.0022.31 A

ATOM 1421 CD GLU A 191 46.152-20.61624.129 1.0026.32 A ATOM 1422 OE1 GLU A 191 46.870-19.860 23.437 1.0023.45 A

ATOM 1423 OE2GLUA191 46.266-20.711 25.355 1.0027.07 A

ATOM 1424 C GLU A 191 46.923-24.44021.893 1.0021.29 A

ATOM 1425 O GLU A 191 46.234-25.46821.870 1.0023.52 A

ATOM 1426 N ALAA 192 47.906-24.19821.034 1.0023.27 A ATOM 1427 CA ALAA 192 48.242-25.17320.019 1.0021.56 A

ATOM 1428 CB ALAA 192 49.380-24.672 19.153 1.0026.07 A

ATOM 1429 C ALAA 192 48.639-26.46820.715 1.0026.60 A ATOM 1430 O ALAA 192 48.306 -27.56220.245 1.0024.52 A

ATOM 1431 N SER A 193 49.321 -26.33421.854 1.0021.47 A

ATOM 1432 CA SERA 193 49.764-27.50522.614 1.0021.96 A

ATOM 1433 CB SERA 193 50.577-27.098 23.853 1.0021.25 A

ATOM 1434 OG SERA 193 51.806-26.53423.455 1.0035.21 A

ATOM 1435 C SERA 193 48.623-28.413 23.035 1.0024.96 A

ATOM 1436 O SERA 193 48.801-29.63523.099 1.0026.33 A

ATOM 1437 N ALAA 194 47.459 -27.83323.320 1.0023.72 A

ATOM 1438 CA ALA A 194 46.296-28.629 23.713 1.0024.70 A A ATTOOMM 1 1443399 C CBB AALLAAAA 119944 45.201-27.73624.319 1.0022.78 A

ATOM 1440 C ALAA 194 45.766-29.39622.506 1.0027.04 A

ATOM 1441 O ALAA 194 45.469-30.58722.626 1.0031.64 A

ATOM 1442 N LEU A 195 45.648-28.753 21.343 1.0023.86 A

ATOM 1443 CA LEU A 195 45.189-29.507 20.184 1.0026.36 A A ATTOOMM 1 1444444 C CBB LLEEUU AA 119955 45.068-28.643 18.926 1.0026.34 A

ATOM 1445 CG LEU A 195 43.775-27.832 18.766 1.0032.93 A

ATOM 1446 CD1 LEU A 195 42.598-28.765 18.505 1.0036.27 A

ATOM 1447 CD2LEUA195 43.552-27.01520.019 1.0025.88 A

ATOM 1448 C LEU A 195 46.184-30.619 19.903 1.0032.46 A A ATTOOMM 1 1444499 O O LLEEUU AA 119955 45.798-31.726 19.539 1.0029.89 A

ATOM 1450 N GLU A 196 47.469-30.33520.089 1.0025.64 A

ATOM 1451 CA GLU A 196 48.494-31.340 19.816 1.0026.61 A

ATOM 1452 CB GLU A 196 49.878-30.71620.010 1.0029.48 A

ATOM 1453 CG GLU A 196 50.276-29.743 18.902 1.0023.90 A A ATTOOMM 1 1445544 C CDD GGLLUU AA 119966 51.340-28.773 19.348 1.0019.56 A

ATOM 1455 OE1 GLU A 196 52.289-29.22620.016 1.0027.52 A

ATOM 1456 OE2GLUA196 51.224-27.570 19.019 1.0026.47 A

ATOM 1457 C GLU A 196 48.341-32.56520.704 1.0028.89 A

ATOM 1458 O GLU A 196 48.459-33.69920.244 1.0032.12 A A ATTOOMM 1 1445599 N N TTYYRRAA119977 48.075-32.32421.978 1.0026.74 A

ATOM 1460 CA TYR A 197 47.909-33.398 22.941 1.0036.58 A

ATOM 1461 CB TYR A 197 47.641-32.79824.325 1.0025.07 A

ATOM 1462 CG TYR A 197 47.626-33.811 25.434 1.0039.30 A

ATOM 1463 CD1 TYR A 197 48.762-34.56025.725 1.0041.22 A A ATTOOMM 1 1446644 C CEE11 TTYYRR AA 119977 48.750-35.52626.719 1.0049.25 A

ATOM 1465 CD2TYRA197 46.469-34.047 26.174 1.0041.12 A

ATOM 1466 CE2TYRA197 46.441-35.01227.174 1.0041.42 A

ATOM 1467 CZ TYR A 197 47.583-35.75227.442 1.0049.85 A

ATOM 1468 OH TYR A 197 47.553-36.73628.414 1.0052.93 A A ATTOOMM 1 1446699 C C TTYYRRAA 119977 46.761 -34.338 22.535 1.0042.35 A

ATOM 1470 O TYRA 197 46.794-35.54322.803 1.0042.54 A

ATOM 1471 N CYS A 198 45.757-33.78021.870 1.0041.70 A

ATOM 1472 CA CYS A 198 44.604-34.55921.460 1.0039.46 A

ATOM 1473 CB CYS A 198 43.344-33.70521.589 1.0040.51 A A ATTOOMM 1 1447744 S SGG CCYYSS AA 119988 43.039-33.26823.338 1.0050.71 A

ATOM 1475 C CYS A 198 44.741-35.14220.069 1.0037.98 A

ATOM 1476 O CYS A 198 43.773-35.635 19.487 1.0041.21 A

ATOM 1477 N GLYA 199 45.953-35.065 19.534 1.0034.97 A

ATOM 1478 CA GLYA 199 46.226-35.638 18.228 1.0029.64 A A ATTOOMM 1 1447799 C C GGLLYYAA 119999 46.136-34.786 16.989 1.0034.39 A

ATOM 1480 O GLY A 199 46.313-35.312 15.889 1.0030.26 A

ATOM 1481 N PHE A 200 45.861-33.491 17.138 1.0029.22 A

ATOM 1482 CA PHE A 200 45.757-32.615 15.976 1.0033.43 A

ATOM 1483 CB PHE A 200 44.645-31.577 16.181 1.0030.59 A A ATTOOMM 1 1448844 C CGG PPHHEE AA 220000 43.309-32.184 16.543 1.0034.93 A

ATOM 1485 CD1 PHE A 200 42.961-32.403 17.876 1.0037.37 A

ATOM 1486 CD2PHEA200 42.412-32.557 15.549 1.0039.78 A ATOM 1487 CE1 PHE A 200 41.738-32.984 18.210 1.0036.62 A

ATOM 1488 CE2 PHE A 200 41.186-33.139 15.872 1.0040.74 A

ATOM 1489 CZ PHE A 200 40.852-33.351 17.203 1.0033.30 A

ATOM 1490 C PHEA200 47.071 -31.905 15.666 1.0036.21 A ATOM 1491 O PHE A 200 48.003-31.904 16.470 1.0033.02 A

ATOM 1492 N HIS A 201 47.122-31.291 14.490 1.0038.02 A

ATOM 1493 CA HISA201 48.303-30.583 14.024 1.0035.10 A

ATOM 1494 CB HISA201 49.028-31.458 12.996 1.0037.66 A

ATOM 1495 CG HISA201 49.460-32.783 13.547 1.0036.76 A ATOM 1496 CD2 HIS A 201 50.671-33.217 13.967 1.0036.43 A

ATOM 1497 ND1 HISA201 48.577-33.812 13.798 1.0040.22 A

ATOM 1498 CE1 HIS A 201 49.226-34.822 14.351 1.0032.04 A

ATOM 1499 NE2HISA201 50.498-34.486 14.465 1.0043.81 A

ATOM 1500 C HIS A 201 47.910-29.232 13.413 1.0035.64 A ATOM 1501 O HISA201 47.678-29.133 12.195 1.0032.21 A

ATOM 1502 N PRO A 202 47.834-28.174 14.252 1.0031.52 A

ATOM 1503 CD PRO A 202 47.952-28.211 15.721 1.0024.33 A

ATOM 1504 CA PRO A 202 47.461 -26.828 13.804 1.0028.33 A

ATOM 1505 CB PRO A 202 47.494-26.008 15.088 1.0025.14 A ATOM 1506 CG PRO A 202 47.134-27.016 16.129 1.0025.77 A

ATOM 1507 C PROA202 48.340-26.242 12.723 1.0028.77 A

ATOM 1508 O PROA202 49.514-26.582 12.614 1.0028.13 A

ATOM 1509 N GLN A 203 47.750-25.354 11.930 1.0026.19 A

ATOM 1510 CA GLN A 203 48.441 -24.694 10.835 1.0028.01 A ATOM 1511 CB GLNA203 47.395-24.123 9.868 1.0033.27 A

ATOM 1512 CG GLN A 203 47.563-24.515 8.396 1.0043.96 A

ATOM 1513 CD GLN A 203 47.902-25.993 8.198 1.0048.25 A

ATOM 1514 OE1 GLN A 203 47.216-26.884 8.709 1.0048.41 A

ATOM 1515 NE2 GLN A 203 48.969-26.255 7.445 1.0056.65 A ATOM 1516 C GLN A 203 49.358-23.586 11.353 1.0027.73 A

ATOM 1517 O GLNA203 49.095-22.978 12.391 1.0024.02 A

ATOM 1518 N LEU A 204 50.451 -23.350 10.633 1.0029.08 A

ATOM 1519 CA LEU A 204 51.412-22.312 10.984 1.0027.46 A

ATOM 1520 CB LEU A 204 52.845-22.865 10.906 1.0032.07 A ATOM 1521 CG LEU A 204 53.306-23.825 12.013 1.0030.57 A

ATOM 1522 CD1 LEU A 204 54.559-24.571 11.565 1.0033.73 A

ATOM 1523 CD2 LEU A 204 53.579-23.068 13.271 1.0025.87 A

ATOM 1524 C LEU A 204 51.252-21.148 10.009 1.0028.09 A

ATOM 15250 LEU A 204 51.411 -21.317 8.804 1.0029.63 A ATOM 1526 N VALA205 50.903-19.979 10.531 1.0026.87 A

ATOM 1527 CA VAL A 205 50.732-18.785 9.709 1.0025.63 A

ATOM 1528 CB VAL A 205 49.362-18.117 9.941 1.0028.90 A

ATOM 1529 CG1 VAL A 205 49.269-16.823 9.127 1.0035.28 A

ATOM 1530 CG2VALA205 48.253-19.056 9.530 1.0024.69 A ATOM 1531 C VAL A 205 51.823-17.797 10.072 1.0023.72 A

ATOM 1532 O VAL A 205 51.844-17.256 11.179 1.0027.68 A

ATOM 1533 N GLUA206 52.728-17.561 9.126 1.0026.74 A

ATOM 1534 CA GLU A 206 53.855-16.678 9.367 1.0025.64 A

ATOM 1535 CB GLU A 206 54.816-16.689 8.170 1.0027.77 A ATOM 1536 CG GLU A 206 56.135-16.029 8.506 1.0029.82 A

ATOM 1537 CD GLU A 206 57.209-16.218 7.450 1.0032.28 A

ATOM 1538 OE1 GLU A 206 57.076-17.123 6.598 1.0041.46 A

ATOM 1539 OE2GLUA206 58.195-15.460 7.500 1.0038.20 A

ATOM 1540 C GLUA206 53.410-15.267 9.657 1.0026.76 A ATOM 1541 O GLU A 206 52.614-14.701 8.922 1.0030.35 A

ATOM 1542 N GLY A 207 53.905-14.710 10.759 1.0022.65 A

ATOM 1543 CA GLY A 207 53.547-13.349 11.110 1.0028.88 A ATOM 1544 C GLY A 207 54.823 -12.580 11.332 1.00 26.30 A

ATOM 1545 O GLY A 207 55.901 -13.167 11.271 1.00 33.22 A

ATOM 1546 N ARG A 208 54.719 -11.283 11.586 1.00 28.30 A

ATOM 1547 CA ARG A 208 55.896 -10.468 11.825 1.00 26.20 A

ATOM 1548 CB ARG A 208 55.510 -8.989 11.863 1.00 27.69 A

ATOM 1549 CG ARG A 208 54.576 -8.520 10.767 1.00 31.85 A

ATOM 1550 CD ARG A 208 53.963 -7.181 11.169 1.00 30.58 A

ATOM 1551 NE ARG A 208 55.003 -6.193 11.486 1.00 36.20 A

ATOM 1552 CZ ARG A 208 55.603 -5.425 10.581 1.00 42.15 A

ATOM 1553 NH1 ARG A 208 55.259 -5.528 9.301 1.00 45.96 A

ATOM 1554 NH2 ARG A 208 56.540 -4.561 10.955 1.00 40.62 A

ATOM 1555 C ARG A 208 56.536 -10.845 13.163 1.00 32.96 A

ATOM 1556 O ARG A 208 55.835 -11.118 14.152 1.00 28.29 A

ATOM 1557 N ALA A 209 57.868 -10.831 13.188 1.00 27.58 A

ATOM 1558 CA ALA A 209 58.637 -11.162 14.383 1.00 31.10 A

ATOM 1559 CB ALA A 209 60.074 -11.538 14.002 1.00 31.86 A

ATOM 1560 C ALA A 209 58.652 -9.998 15.361 1.00 29.50 A

ATOM 1561 O ALA A 209 59.119 -10.140 16.497 1.00 30.70 A

ATOM 1562 N ASP A 210 58.155 -8.841 14.938 1.00 25.17 A

ATOM 1563 CA ASP A 210 58.113 -7.702 15.857 1.00 30.72 A

ATOM 1564 CB ASP A 210 58.128 -6.369 15.080 1.00 30.47 A

ATOM 1565 CG ASP A 210 56.811 -6.052 14.389 1.00 39.40 A

ATOM 1566 OD1 ASP A 210 56.204 -6.946 13.776 1.00 34.28 A

ATOM 1567 OD2 ASP A 210 56.388 -4.875 14.451 1.00 50.59 A

ATOM 1568 C ASP A 210 56.892 -7.805 16.795 1.00 25.97 A

ATOM 1569 O ASP A 210 56.662 -6.950 17.649 1.00 25.64 A

ATOM 1570 N ASN A 211 56.134 -8.879 16.632 1.00 24.15 A

ATOM 1571 CA ASN A 211 54.967 -9.151 17.471 1.00 26.21 A

ATOM 1572 CB ASN A 211 54.018 -10.075 16.714 1.00 25.38 A

ATOM 1573 CG ASN A 211 52.789 -10.483 17.526 1.00 26.91 A

ATOM 1574 OD1 ASN A 211 52.443 -9.856 18.519 1.00 27.63 A

ATOM 1575 ND2 ASN A 211 52.118 -11.547 17.079 1.00 22.69 A

ATOM 1576 C ASN A 211 55.533 -9.841 18.717 1.00 32.24 A

ATOM 1577 O ASN A 211 55.288 -11.028 18.960 1.00 31.21 A

ATOM 1578 N ILE A 212 56.294 -9.086 19.505 1.00 28.92 A

ATOM 1579 CA ILE A 212 56.937 -9.639 20.682 1.00 32.34 A

ATOM 1580 CB ILE A 212 58.262 -8.882 21.004 1.00 42.77 A

ATOM 1581 CG2 ILE A 212 59.118 -8.757 19.752 1.00 38.38 A

ATOM 1582 CG1 ILE A 212 57.955 -7.498 21.587 1.00 34.48 A

ATOM 1583 CD ILE A 212 57.329 -6.554 20.615 1.00 44.22 A

ATOM 1584 C ILE A 212 56.096 -9.666 21.950 1.00 35.03 A

ATOM 1585 O ILE A 212 55.056 -9.018 22.042 1.00 35.44 A

ATOM 1586 N LYS A 213 56.580 -10.427 22.925 1.00 26.32 A

ATOM 1587 CA LYS A 213 55.931 -10.568 24.222 1.00 28.76 A

ATOM 1588 CB LYS A 213 55.879 -12.045 24.628 1.00 34.04 A

ATOM 1589 CG LYS A 213 55.150 -12.298 25.943 1.00 38.37 A

ATOM 1590 CD LYS A 213 55.058 -13.789 26.283 1.00 36.08 A

ATOM 1591 CE LYS A 213 56.381 -14.330 26.833 1.00 38.22 A

ATOM 1592 NZ LYS A 213 57.058 -15.228 25.858 1.00 42.03 A

ATOM 1593 C LYS A 213 56.737 -9.780 25.255 1.00 35.01 A

ATOM 1594 O LYS A 213 57.947 -9.972 25.380 1.00 32.48 A

ATOM 1595 N VAL A 214 56.070 -8.883 25.976 1.00 29.53 A

ATOM 1596 CA VAL A 214 56.726 -8.072 26.999 1.00 38.83 A

ATOM 1597 CB VAL A 214 56.016 -6.712 27.172 1.00 39.03 A

ATOM 1598 CG1 VAL A 214 56.717 -5.891 28.273 1.00 39.43 A

ATOM 1599 CG2 VAL A 214 56.039 -5.949 25.849 1.00 35.04 A

ATOM 1600 C VAL A 214 56.709 -8.806 28.334 1.00 42.88 A ATOM 1601 O VAL A 214 55.665 -8.913 28.972 1.0040.58 A

ATOM 1602 N THR A 215 57.864 -9.309 28.758 1.0046.63 A

ATOM 1603 CA THR A 215 57.942-10.04430.016 1.0050.56 A

ATOM 1604 CB THR A 215 58.288-11.52529.780 1.0053.56 A ATOM 1605 OG1 THR A 215 57.581 -12.011 28.631 1.0050.16 A

ATOM 1606 CG2 THR A 215 57.888-12.349 30.994 1.0054.02 A

ATOM 1607 C THR A 215 59.004 -9.464 30.937 1.0056.61 A

ATOM 1608 O THR A 215 58.834 -9.419 32.158 1.0053.65 A

ATOM 1609 N ARGA216 60.101 -9.02030.332 1.0055.86 A ATOM 1610 CA ARG A216 61.222 -8.45031.064 1.0055.27 A

ATOM 1611 CB ARG A 216 62.541 -8.938 30.457 1.0053.61 A

ATOM 1612 CG ARG A 216 63.407 -9.72231.411 1.0062.74 A

ATOM 1613 CD ARGA216 63.419-11.202 31.078 1.0061.82 A

ATOM 1614 NE ARG A 216 62.088-11.802 31.095 1.0061.33 A ATOM 1615 CZ ARGA216 61.866-13.10430.953 1.0067.39 A

ATOM 1616 NH1 ARG A216 62.891-13.933 30.790 1.0062.86 A

ATOM 1617 NH2ARGA216 60.628-13.575 30.966 1.0068.72 A

ATOM 1618 C ARGA216 61.185 -6.92831.036 1.0056.05 A

ATOM 16190 ARGA216 60.529 -6.330 30.187 1.0056.49 A ATOM 1620 N PROA217 61.901 -6.27931.970 1.0057.08 A

ATOM 1621 CD PRO A 217 62.666 -6.880 33.079 1.0054.70 A

ATOM 1622 CA PRO A 217 61.942 -4.813 32.041 1.0054.45 A

ATOM 1623 CB PROA217 62.961 -4.552 33.151 1.0056.69 A

ATOM 1624 CG PRO A 217 62.778 -5.72734.054 1.0056.67 A ATOM 1625 C PROA217 62.346 -4.151 30.720 1.0050.89 A

ATOM 16260 PROA217 61.714 -3.18930.284 1.0051.43 A

ATOM 1627 N GLU A 218 63.394 -4.672 30.087 1.0050.91 A

ATOM 1628 CA GLUA218 63.868 -4.10828.826 1.0053.84 A

ATOM 1629 CB GLU A 218 65.211 -4.73528.418 1.0058.08 A ATOM 1630 CG GLU A 218 65.854 -4.06827.190 1.0064.79 A

ATOM 1631 CD GLUA218 66.975 -4.901 26.557 1.0072.12 A

ATOM 1632 OE1 GLU A 218 66.755 -6.11326.326 1.0071.16 A

ATOM 1633 OE2 GLU A 218 68.065 -4.34526.275 1.0067.83 A

ATOM 1634 C GLU A 218 62.865 -4.28727.690 1.0049.59 A ATOM 16350 GLUA218 62.864 -3.51326.733 1.0050.18 A

ATOM 1636 N ASP A 219 62.010 -5.29927.790 1.0045.70 A

ATOM 1637 CA ASP A 219 61.028 -5.54026.736 1.0045.36 A

ATOM 1638 CB ASP A 219 60.144 -6.751 27.066 1.0043.64 A

ATOM 1639 CG ASP A 219 60.920 -8.04327.109 1.0045.39 A ATOM 1640 OD1 ASP A 219 61.961 -8.12726.416 1.0049.21 A

ATOM 1641 OD2 ASP A 219 60.489 -8.98227.823 1.0036.59 A

ATOM 1642 C ASP A 219 60.151 -4.321 26.514 1.0042.03 A

ATOM 1643 O ASPA219 59.735 -4.048 25.392 1.0041.73 A

ATOM 1644 N LEU A 220 59.870 -3.588 27.585 1.0043.58 A ATOM 1645 CA LEU A 220 59.032 -2.40027.483 1.0040.64 A

ATOM 1646 CB LEU A 220 58.957 -1.68528.830 1.0045.60 A

ATOM 1647 CG LEU A 220 58.270 -.31528.833 1.0048.05 A

ATOM 1648 CD1 LEU A 220 56.755 -.46728.706 1.0046.41 A

ATOM 1649 CD2 LEU A 220 58.622 .411 30.135 1.0053.44 A ATOM 1650 C LEU A 220 59.582 -1.43626.453 1.0040.17 A

ATOM 1651 0 LEU A 220 58.885 -1.04225.524 1.0034.63 A

ATOM 1652 N ALA A 221 60.839 -1.044 26.640 1.0042.34 A

ATOM 1653 CA ALA A 221 61.493 -.10625.733 1.0045.60 A

ATOM 1654 CB ALA A 221 62.961 .078 26.136 1.0045.74 A ATOM 1655 C ALA A 221 61.398 -.589 24.293 1.0041.75 A

ATOM 1656 0 ALAA221 61.035 .17523.396 1.0036.25 A

ATOM 1657 N LEU A 222 61.717 -1.86424.081 1.0039.59 A ATOM 1658 CA LEU A 222 61.660 -2.456 22.747 1.00 38.28 A

ATOM 1659 CB LEU A 222 62.132 -3.916 22.798 1.00 39.70 A

ATOM 1660 CG LEU A 222 62.087 -4.707 21.487 1.00 39.68 A

ATOM 1661 CD1 LEU A 222 63.047 -4.099 20.489 1.00 43.78 A ATOM 1662 CD2 LEU A 222 62.437 -6.150 21.745 1.00 40.10 A

ATOM 1663 C LEU A 222 60.247 -2.389 22.162 1.00 42.22 A

ATOM 1664 0 LEU A 222 60.068 -2.057 20.987 1.00 43.92 A

ATOM 1665 N ALA A 223 59.241 -2.713 22.970 1.00 41.63 A

ATOM 1666 CA ALA A 223 57.862 -2.674 22.482 1.00 44.91 A ATOM 1667 CB ALA A 223 56.901 -3.134 23.572 1.00 40.65 A

ATOM 1668 C ALA A 223 57.525 -1.255 22.030 1.00 42.30 A

ATOM 1669 O ALA A 223 56.879 -1.059 20.999 1.00 40.78 A

ATOM 1670 N GLU A 224 57.970 -.266 22.800 1.00 43.74 A

ATOM 1671 CA GLU A 224 57.719 1.125 22.441 1.00 46.16 A ATOM 1672 CB GLU A 224 58.304 2.071 23.484 1.00 44.87 A

ATOM 1673 CG GLU A 224 58.311 3.513 23.017 1.00 55.07 A

ATOM 1674 CD GLU A 224 58.260 4.512 24.153 1.00 57.49 A

ATOM 1675 OE1 GLU A 224 59.249 4.601 24.922 1.00 51.86 A

ATOM 1676 OE2 GLU A 224 57.217 5.205 24.271 1.00 60.96 A ATOM 1677 C GLU A 224 58.326 1.440 21.076 1.00 47.29 A

ATOM 1678 O GLU A 224 57.695 2.085 20.237 1.00 47.20 A

ATOM 1679 N PHE A 225 59.555 .977 20.869 1.00 50.18 A

ATOM 1680 CA PHE A 225 60.268 1.177 19.614 1.00 47.05 A

ATOM 1681 CB PHE A 225 61.597 .415 19.642 1.00 48.91 A ATOM 1682 CG PHE A 225 62.339 .431 18.331 1.00 49.43 A

ATOM 1683 CD1 PHE A 225 62.994 1.581 17.897 1.00 51.99 A

ATOM 1684 CD2 PHE A 225 62.374 -.705 17.523 1.00 49.62 A

ATOM 1685 CE1 PHE A 225 63.673 1.602 16.673 1.00 44.11 A

ATOM 1686 CE2 PHE A 225 63.047 -.699 16.299 1.00 43.16 A ATOM 1687 CZ PHE A 225 63.698 .456 15.872 1.00 48.09 A

ATOM 1688 C PHE A 225 59.429 .673 18.450 1.00 47.63 A

ATOM 1689 O PHE A 225 59.208 1.389 17.477 1.00 48.88 A

ATOM 1690 N TYR A 226 58.966 -.567 18.551 1.00 49.30 A

ATOM 1691 CA TYR A 226 58.165 -1.166 17.490 1.00 48.89 A ATOM 1692 CB TYR A 226 57.886 -2.637 17.813 1.00 50.20 A

ATOM 1693 CG TYR A 226 59.064 -3.556 17.585 1.00 44.80 A

ATOM 1694 CD1 TYR A 226 59.369 -4.564 18.499 1.0046.11 A

ATOM 1695 CE1 TYR A 226 60.435 -5.435 18.279 1.00 47.03 A

ATOM 1696 CD2 TYR A 226 59.858 -3.440 16.440 1.00 43.72 A ATOM 1697 CE2 TYR A 226 60.927 -4.308 16.209 1.00 43.50 A

ATOM 1698 CZ TYR A 226 61.209 -5.302 17.132 1.00 43.61 A

ATOM 1699 OH TYR A 226 62.261 -6.165 16.917 1.00 44.48 A

ATOM 1700 C TYR A 226 56.856 -.439 17.228 1.00 49.19 A

ATOM 1701 O TYR A 226 56.389 -.388 16.088 1.00 46.23 A ATOM 1702 N LEU A 227 56.262 .123 18.276 1.00 51.04 A

ATOM 1703 CA LEU A 227 54.995 .846 18.135 1.00 55.54 A

ATOM 1704 CB LEU A 227 54.249 .877 19.476 1.00 57.70 A

ATOM 1705 CG LEU A 227 53.603 -.419 19.977 1.00 55.63 A

ATOM 1706 CD1 LEU A 227 53.114 -.236 21.409 1.00 53.74 A ATOM 1707 CD2 LEU A 227 52.452 -.799 19.058 1.00 54.22 A

ATOM 1708 C LEU A 227 55.226 2.274 17.656 1.00 53.48 A

ATOM 1709 O LEU A 227 54.300 3.075 17.607 1.00 55.24 A

ATOM 1710 N THR A 228 56.463 2.578 17.283 1.00 55.39 A

ATOM 1711 CA THR A 228 56.823 3.923 16.841 1.00 55.53 A ATOM 1712 CB THR A 228 58.049 4.411 17.654 1.00 55.92 A

ATOM 1713 OG1 THR A 228 57.748 4.315 19.052 1.00 57.68 A

ATOM 1714 CG2 THR A 228 58.395 5.855 17.330 1.00 52.13 A ATOM 1715 C THRA228 57.106 4.065 15.334 1.0055.95 A

ATOM 1716 OT1 THR A 228 57.397 3.046 14.671 1.0053.29 A

ATOM 1717 OXT THR A 228 57.039 5.213 14.832 1.0055.13 A

ATOM 1718 OH2WATW 1 53.847 -7.444 15.008 1.0028.25 W ATOM 1719 OH2WATW 2 47.027 -3.691 14.794 1.0027.00 W

ATOM 1720 OH2WATW 3 45.444 -9.337 36.235 1.0030.05 W

ATOM 1721 OH2WATW 4 33.922 .643 18.800 1.0046.44 W

ATOM 1722 OH2WATW 5 29.022 .031 27.797 1.0033.48 W

ATOM 1723 OH2WATW 6 49.115 -3.454 18.135 1.0034.94 W ATOM 1724 OH2 WAT W 7 42.749 -7.436 10.961 1.0028.12 W

ATOM 1725 OH2 WAT W 8 48.242 -2.786 11.852 1.0033.73 W

ATOM 1726 OH2WATW 9 38.166-13.364 7.759 1.0026.24 W

ATOM 1727 OH2WATW 10 70.200-13.434 18.230 1.0027.23 W

ATOM 1728 OH2WATW 11 32.460 -8.229 32.731 1.0045.56 W ATOM 1729 OH2WATW 12 59.016-11.798 22.216 1.0032.91 W

ATOM 1730 OH2WATW 13 60.995-13.831 10.396 1.0046.99 W

ATOM 1731 OH2WATW 14 49.286-34.083 17.618 1.0030.47 W

ATOM 1732 OH2WATW 15 33.791 -17.472 13.391 1.0032.71 W

ATOM 1733 OH2WATW 16 30.947 -5.854 12.464 1.0038.93 W ATOM 1734 OH2WATW 17 46.728 -1.736 18.777 1.0038.92 W

ATOM 1735 OH2WATW 18 28.006-21.02527.775 1.0048.34 W

ATOM 1736 OH2WATW 19 58.466-13.965 10.078 1.0039.44 W

ATOM 1737 OH2WATW 20 41.247 -6.716 8.377 1.0045.81 W

ATOM 1738 OH2WATW 21 58.906-13.109 17.325 1.0042.74 W ATOM 1739 OH2WATW 22 69.328-24.424 14.872 1.0051.19 W

ATOM 1740 OH2WATW 23 26.850-10.998 14.095 1.0050.74 W

ATOM 1741 OH2WATW 24 46.592-22.926 26.823 1.0033.88 W

ATOM 1742 OH2WATW 25 69.780-25.888 10.403 1.0057.17 W

ATOM 1743 OH2WATW 26 45.111-26.02837.762 1.0046.34 W ATOM 1744 OH2WATW 27 60.710-15.221 6.454 1.0049.35 W

ATOM 1745 OH2WATW 28 68.617-14.221 14.947 1.0039.32 W

ATOM 1746 OH2WATW 29 35.082 -5.686 16.665 1.0030.26 W

ATOM 1747 OH2WATW 30 32.135-23.281 28.156 1.0071.05 W

ATOM 1748 OH2WATW 31 33.020-14.898 35.681 1.0038.98 W ATOM 1749 OH2WATW 32 44.423 2.273 36.015 1.0053.68 W

ATOM 1750 OH2WATW 33 33.459-11.487 36.757 1.0052.78 W

ATOM 1751 OH2WATW 34 36.437-16.867 36.394 1.0054.25 W

ATOM 1752 OH2WATW 35 49.491-37.974 15.120 1.0075.95 W

ATOM 1753 OH2WATW 36 59.826-17.334 5.348 1.0058.58 W ATOM 1754 OH2WATW 37 34.090-31.163 18.062 1.0045.16 W

ATOM 1755 OH2WATW 38 31.474-26.26926.034 1.0047.13 W

ATOM 1756 OH2WATW 39 33.485-25.60734.333 1.0061.09 W

ATOM 1757 OH2WATW 40 41.501 -3.527 10.668 1.0043.25 W

ATOM 1758 OH2WATW 41 58.424 7.398 25.955 1.0052.89 W ATOM 1759 OH2WATW 42 45.178-31.571 12.324 1.0040.69 W

ATOM 1760 OH2WATW 43 40.434-12.172 7.724 1.0037.51 W

ATOM 1761 OH2WATW 44 36.432-27.375 31.518 1.0045.12 W

ATOM 1762 OH2WATW 45 38.394-36.117 34.325 1.0061.82 W

ATOM 1763 OH2WATW 46 63.449-32.687 24.761 1.0050.76 W ATOM 1764 OH2WATW 47 53.209-31.42621.007 1.0030.89 W

ATOM 1765 OH2WATW 48 57.450-25.595 24.104 1.0056.01 W

ATOM 1766 OH2WATW 49 38.837-33.859 23.542 1.0057.69 W

ATOM 1767 OH2WATW 50 51.023-26.542 32.249 1.0062.14 W

ATOM 1768 OH2WATW 51 30.280-22.322 25.792 1.0069.26 W ATOM 1769 OH2WATW 52 64.004-21.598 10.616 1.0033.97 W

ATOM 1770 OH2WATW 53 40.490 1.862 25.889 1.0064.76 W

ATOM 1771 OH2WATW 54 52.502-21.666 31.069 1.0039.06 W ATOM 1772 OH2 WAT W 55 70.054 -27.529 31.630 1.00 46.25 W ATOM 1773 OH2 WAT W 56 59.563 -7.794 12.066 1.00 39.75 W ATOM 1774 OH2 WAT W 57 51.756 -18.437 36.423 1.00 50.57 W ATOM 1775 OH2 WAT W 58 67.957 -29.464 28.996 1.00 38.73 W ATOM 1776 OH2 WAT W 59 53.377 -27.213 25.693 1.00 33.12 W ATOM 1777 OH2 WAT W 60 35.027 -17.956 33.841 1.00 47.36 W ATOM 1778 OH2 WAT W 61 34.699 .015 36.542 1.00 54.16 W ATOM 1779 OH2 WAT W 62 49.063 -21.870 27.908 1.00 29.93 W ATOM 1780 OH2 WAT W 63 43.825 5.170 28.220 1.00 46.89 W ATOM 1781 OH2 WAT W 64 33.220 -24.741 18.208 1.00 26.03 W ATOM 1782 OH2 WAT W 65 69.838 -24.974 30.604 1.00 38.88 W ATOM 1783 OH2 WAT W 66 64.094 -14.214 18.283 1.00 55.93 W ATOM 1784 OH2 WAT W 67 53.048 -12.059 14.317 1.00 24.60 W ATOM 1785 OH2 WAT W 68 66.367 -31.832 21.573 1.00 37.27 W ATOM 1786 OH2 WAT W 69 34.520 -27.015 18.111 1.00 27.09 W ATOM 1787 OH2 WAT W 70 36.890 -.419 16.622 1.00 57.10 W ATOM 1788 OH2 WAT W 71 52.781 -34.086 20.553 1.00 38.70 W ATOM 1789 OH2 WAT W 72 53.288 -1.345 9.327 1.00 55.98 W ATOM 1790 OH2 WAT W 73 34.173 -12.450 5.882 1.00 48.44 W ATOM 1791 OH2 WAT W 74 30.528 -17.942 15.418 1.00 34.06 W ATOM 1792 OH2 WAT W 75 42.189 1.121 18.812 1.00 44.27 W ATOM 1793 OH2 WAT W 76 43.424 -.609 12.645 1.00 40.00 W ATOM 1794 OH2 WAT W 77 51.611 -4.183 8.587 1.00 44.46 W ATOM 1795 OH2 WAT W 78 42.365 -24.866 35.053 1.00 41.89 w ATOM 1796 OH2 WAT W 79 52.460 -18.464 6.314 1.00 42.10 w ATOM 1797 OH2 WAT W 80 29.549 -8.429 24.951 1.00 49.93 w ATOM 1798 OH2 WAT W 81 45.708 -20.606 43.804 1.00 50.97 w ATOM 1799 OH2 WAT W 82 48.759 -4.126 9.313 1.00 38.92 w ATOM 1800 OH2 WAT W 83 69.186 -32.976 14.262 1.0047.91 w ATOM 1801 OH2 WAT W 84 45.989 -18.009 6.140 1.00 40.93 w ATOM 1802 OH2 WAT W 85 56.927 -26.566 26.449 1.00 59.64 w ATOM 1803 OH2 WAT W 86 36.811 -32.057 33.335 1.00 45.03 w ATOM 1804 OH2 WAT W 87 29.983 -15.853 36.792 1.00 51.41 w ATOM 1805 OH2 WAT W 88 27.309 -2.621 27.741 1.00 40.84 w ATOM 1806 OH2 WAT W 89 51.895 -19.984 33.020 1.00 34.45 w ATOM 1807 OH2 WAT W 90 43.526 -19.558 5.099 1.00 54.75 w ATOM 1808 OH2 WAT W 91 49.330 -29.216 33.581 1.00 52.42 w ATOM 1809 OH2 WAT W 92 46.912 -4.742 39.215 1.00 58.61 w ATOM 1810 OH2 WAT W 93 59.739 -18.695 32.277 1.00 52.62 w ATOM 1811 OH2 WAT W 94 47.594 -39.154 17.313 1.00 62.20 w ATOM 1812 OH2 WAT W 95 55.288 6.323 26.048 1.00 63.96 w ATOM 1813 OH2 WAT W 96 43.413 -35.485 13.897 1.00 54.83 w ATOM 1814 OH2 WAT W 97 36.760 -10.358 37.741 1.00 42.77 w ATOM 1815 OH2 WAT W 98 37.400 -5.550 37.108 1.00 48.75 w ATOM 1816 OH2 WAT W 100 32.447 -17.305 33.447 1.00 56.24 w ATOM 1817 OH2 WAT W 102 72.661 -35.327 22.942 1.0047.31 w ATOM 1818 OH2 WAT W 103 33.696 -26.412 31.300 1.00 64.91 w ATOM 1819 OH2 WAT W 104 45.761 -40.125 19.803 1.00 62.37 w ATOM 1820 OH2 WAT W 111 43.033 -36.570 16.978 1.00 60.28 w ATOM 1821 N1 PRD 48, ,972 -15..320 32. ,129 1.00 28.74 ATOM 1822 C2 PRD 47 ,711 -15..455 32 ,800 1.00 29.39 ATOM 1823 N3 PRD 47 ,604 -16..211 33 ,929 1.00 32.53 ATOM 1824 C4 PRD 48 ,759 -16..883 34 ,469 1.00 38.68 ATOM 1825 C5 PRD 50, 037 -16.794 33..854 1.00 37.19 ATOM 1826 C6 PRD 50, 086 -16.008 32.703 1.00 36.55 ATOM 182702 PRD 46.649 -14.916 32 ,422 1.00 26.35 ATOM 1828 N4 PRD 48, 591 -17 609 35 589 1.00 40.89 ATOM 1829 C1*PRD 1 49.134-14.495 30.891 1.0024.92

ATOM 1830 C2*PRD 1 50.055-13.319 31.132 1.0022.59

ATOM 1831 02* PRD 1 49.351 -12.350 31.855 1.0027.79

ATOM 1832 C3*PRD 1 50.529-12.941 29.743 1.0031.02 ATOM 1833 C4* PRD 1 50.336-14.252 28.943 1.0025.94

ATOM 1834 04* PRD 1 49.735-15.210 29.845 1.0025.94

ATOM 183503* PRD 1 49.677-11.980 29.080 1.0028.50

ATOM 1836 C5*PRD 1 51.739-14.679 28.527 1.0024.84

ATOM 183705* PRD 1 52.433-15.08229.674 1.0033.73 ATOM 1838 PA PRD 1 54.056-15.077 29.828 1.0034.41

ATOM 1839 01 A PRD 1 54.488-13.61629.398 1.0036.75

ATOM 184002A PRD 1 54.497-16.13428.879 1.0036.37

ATOM 1841 03APRD 1 54.346-15.458 31.470 1.0041.01

ATOM 1842 PB PRD 1 54.585-17.612 28.672 1.0032.13 ATOM 184301 B PRD 1 53.337-18.26529.179 1.0038.59

ATOM 1844 02B PRD 1 55.839-18.08729.434 1.0031.11

ATOM 1845 03B PRD 1 54.687-18.20027.300 1.0039.60

ATOM 1846 C1M PRD 1 53.636-17.82726.427 1.0028.82

ATOM 1847 C2M PRD 1 54.008-18.44025.091 1.0024.91 ATOM 184802M PRD 1 53.969-19.941 25.302 1.0020.93

ATOM 1849 C3M PRD 1 53.045-18.056 23.911 1.0027.33

ATOM 185003M PRD 1 53.182-16.59723.532 1.0025.46

ATOM 1851 C5MPRD 1 51.561 -18.347 24.271 1.0022.50

ATOM 1852 C4M PRD 1 53.514-18.842 22.709 1.0026.78 ATOM 185304M PRD 1 54.967-18.442 22.335 1.0025.55

ATOM 1854MG+2MG2 1 54.167-17.365 33.325 1.0063.74 END

Claims

That which is claimed is:

1. A composition comprising 4-diphosphocy tidyl-2-C-methylery thritol synthase in crystalline form.

2. A composition according to claim 1 further comprising a substrate, substrate mimic or inhibitor of said synthase.

3. A composition according to claim 1 as described by the X-ray coordinates set forth in Appendix 1, 2 or 3.

4. A composition according to claim 2 as described by the X-ray coordinates set forth in Appendix 1, 2 or 3.

5. A composition according to claim 2 wherein th crystals have a monoclinic space group C2 with unit cell dimensions of about: a = 130 A, b = 47 A, c = 38 A, α = 90°, β = 94°, and γ = 90°.

6. A composition according to claim 2 wherein the crystals have a monoclinic space group C2 with unit cell dimensions: a = 130.3 A, b = 47.3 A, c = 38.1 A, α = 90°, β = 94.2°, and γ = 90°.

7. A composition according to claim 2 wherein the crystals have a monoclinic space group C2 with unit cell dimensions: a = 130.0 A, b = 46.8 A, c = 38.4 A, α = 90°, β = 92.6°, and γ = 90°.

8. A composition according to claim 2 wherein the crystals have a monoclinic space group C2 with unit cell dimensions: a = 130.6 A, b = 47.1 A, c = 38.1 A, α = 90°, β = 93.8°, and γ = 90°.

9. A computer for producing a three-dimensional representation of a molecule or molecular complex or a homologue of said molecule or molecular complex, wherein said molecule or molecular complex or a homologue of said molecule or molecular complex comprises an active site defined by structure coordinates of Appendix 1, 2 or 3, wherein said computer comprises:

(i) a computer-readable data storage medium comprising a data storage material encoded with computer-readable data, wherein said data comprises the structure coordinates of Appendix 1, 2 or 3;

(ii) a working memory for storing instructions for processing said computer-readable data;

(iii) a central-processing unit coupled to said working memory and to said computer-readable data storage medium for processing said computer-machine readable data into said three-dimensional representation; and (iv) a display coupled to said central-processing unit for displaying said three-dimensional representation.

10. A computer for determining at least a portion of the structure coordinates corresponding to X-ray diffraction data obtained from a molecule or molecular complex or a homologue of said molecule or molecular complex, wherein said computer comprises:

(i) a computer-readable data storage medium comprising a data storage material encoded with machine-readable data, wherein said data comprises at least a portion of the structural coordinates of Appendix 1, 2 or 3;

(ii) a computer-readable data storage medium comprising a data storage material encoded with computer-readable data, wherein said data comprises X-ray diffraction data obtained from said molecule or molecular complex or a homologue of said molecule or molecular complex;

(iii) a working memory for storing instructions for processing said computer-readable data of (i) and (ii); (iv) a central-processing unit coupled to said working memory and to said computer-readable data storage medium of (i) and (ii) for performing a Fourier transform of the machine readable data of (i) and for processing said computer-readable data of (ii) into structure coordinates; and

(v) a display coupled to said central-processing unit for displaying said structure coordinates of said molecule or molecular complex.

11. A method for screening for compounds that inhibit the nonmevalonate isoprenoid biosynthesis pathway, said method comprising: a) determining the points of interaction between any one or more enzymes in the non-mevalonate isoprenoid biosynthesis pathway, and substrate or substrate mimic therefor; b) selecting compound(s) having similar interaction with said one or more enzymes; and c) testing the selected compound for the ability to inhibit the activity of any one or more enzymes in the non-mevalonate isoprenoid biosynthesis pathway.

12. A method for screening for compounds that inhibit the nonmevalonate isoprenoid biosynthesis pathway, said method comprising: a) selecting compound(s) having points of interaction with any one or more enzymes in the non-mevalonate isoprenoid biosynthesis pathway, wherein similar points of interaction have been determined between said enzymes and a substrate or substrate mimic therefor; and b) testing the selected compound for the ability to inhibit the activity of any said enzymes.

13. A method for screening for compounds that inhibit the nonmevalonate isoprenoid biosynthesis pathway, said method comprising: testing a compound for the ability to inhibit the activity of any one or more enzymes in the non-mevalonate isoprenoid biosynthesis pathway, wherein said compound has been selected as having points of interaction with said enzymes, and wherein similar points of interaction have been determined between said enzymes and a substrate or substrate rnimic therefor.

14. A compound identified by the method of claim 11.

15. A pharmaceutical composition comprising a compound identified by the method of claim 11 and a pharmaceutically acceptable carrier therefor.

16. A method for inhibiting the activity of any one or more enzymes in the non-mevalonate isoprenoid biosynthesis pathway, said method comprising contacting said one or more enzymes with an effective amount of a compound identified by the method of claixn 11.

17. A method according to claim 14 wherein said one or more enzymes is in a cell-free environment.

18. A method according to claim 14 wherein said one or more enzymes is in a cell.

19. A method according to claim 16 wherein said contacting occurs in vitro.

20. A method according to claim 16 wherein said contacting occurs in vivo.

21. A method according to claim 16 wherein said contacting modulates growth of the cell.

22. A method according to claim 19 wherein the cell is a bacterial cell.

23. An antibacterial formulation comprising at least one compound identified by the method of claim 11 and a suitable carrier therefor.

24. A method for inhibiting bacterial terpenoid synthesis, said method comprising contacting said bacteria with an effective amount of at least one compound identified by the method of claim 11.

25. A method for treating a subject suffering from a bacterial infection, said method comprising administering to said subject an effective amount of at least one compound identified by the method of claim 11.

26. A method according to claim 23 wherein said bacterial infection is an E-coli infection or a streptococcal infection.