Background of the Invention Cathepsin E is an intracellular, non-lysosomal aspartic proteinase belonging to the A1 pepsin-like family. In vivo, Cathepsin E is synthesized at neutral pH as inactive zymogen.

This precursor form is inhibited by binding of its N-terminal pro-sequence in the active site.

Cathepsin E, like most aspartic proteases, auto-activates at acidic pH in a stepwise fashion resulting in the mature, active form of the protease at the end of the activation pathway. The mature enzyme appears to be contained within vesicular structures associated with the endoplasmic reticulum, endosomal compartments of selected cells and the trans-Golgi network. In mature erythrocytes, Cathepsin E is associated with the cytoplasmic face of the plasma membranes. Postulated physiological roles for cathepsin E include the biogenesis of the vasoconstrictor peptide endothelin and the antigen/invariant chain processing. Further, the enzyme might play a role in neurodegeneration associated with brain ischemia and aging. In contrast to all other members of the A1 aspartyl protease family the mature Cathepsin E exists as a disulfide-linked homodimer with a molecular mass of 84 kDa.

However, dimer formation is not required for its catalytic activity.

Other members of the human aspartyl protease family include: BACE, BACE 2, renin, Cathepsin D, Pepsin A, Pepsin C and Napsin A. While structural information is available for BACE, Renin, Cathepsin D, Pepsin A and Pepsin C, there has been no description of the crystal structure of Cathepsin E in any species described prior to the present invention.

The present invention describes for the first time to our knowledge, the three dimensional structure of human Cathepsin E determined by crystallization of Cathepsin E and the use of this structural information for identifying and designing inhibitors for Cathepsin E and other aspartyl protease family members.

Summary of the Invention The present invention provides the three-dimensional structure of Cathepsin E thereby enabling the identification and design of ligands or low molecular weight molecules, particularly inhibitors of aspartyl protease family members.

In one aspect of the invention, a crystal of Cathepsin E comprising a unit cell dimension of a = 61.32 + 5 Angstroms, b = 61.32 5 Angstroms, c = 207.80 5 Angstroms, a= 90.0 degrees 90.0 degrees y = 90 degrees is provided.

In another aspect of the invention, a three-dimensional structure of Cathepsin E comprising the atomic structure coordinates of Table 1 is provided.

In yet another aspect of the invention, a crystal of Cathepsin E comprising the sequence of SEQ ID. No. 1, SEQ ID. No. 2, or a mutant, fragment or a homologue of either SEQ ID No. 1 or SEQ ID No. 2 is provided. In one embodiment, at least the ligand binding site is provided.

In a further aspect of the invention, a crystal of cathepsin E bound to at least one ligand or low molecular weight compound is provided.

In yet another aspect of the invention, a computer readable medium comprising data storage material encoded with computer readable data wherein said data comprises the atomic coordinates of Table 1 comprising Cathepsin E.

The present invention also provides a method for making a crystal of Cathepsin E comprising: (i) expression of Cathepsin E comprising SEQ ID No. 1 or SEQ ID No. 2 in a suitable host cell (ii) purification and, if required, refolding, of Cathepsin E. In one embodiment of the invention, at least the prosequence is expressed together with the mature Cathepsin E in a suitable host cell. In another embodiment of the invention, the prosequence or part of the prosequence is removed prior to crystallisation.

(iii) exposure of the purified and folded Cathepsin E to conditions suitable for crystalisation In a preferred embodiment of the invention, at least the prosequence comprising amino acids 19-53 of SEQ ID No. 1 or amino acids 24-58 of SEQ ID No. 2 is expressed together with the mature Cathepsin E comprising amino acids 54-396 of SEQ ID No. 1 or amino acids 59-401 of SEQ ID No. 2 in a suitable host cell.

In another preferred embodiment of the invention, the prosequence or part of the prosequence comprising amino acids 19-53 of SEQ ID No. 1 or amino acids 24-58 of SEQ ID No. 2 is removed at any step prior to crystallisation.

In another embodiment of the invention, a mutant, fragment or homologue of SEQ ID No. 1 or SEQ ID No. 2 may be used for making a crystal of Cathepsin E.

In yet another embodiment of the invention, at least one ligand or low molecule weight chemical compound may be bound to Cathepsin E at any step prior to crystallisation.

In another aspect, the invention provides a method of determining the three-dimensional structure of Cathepsin E comprising: (i) crystallisation of Cathepsin E comprising SEQ ID No. 1 or SEQ ID No. 2, or a mutant, fragment or homologue thereof (ii) utilizing the atomic coordinates of Table 1 in whole or in part to determine the three- dimensional structure of Cathepsin E.

In a further aspect, the invention provides a method of determining the three-dimensional structure of a complex comprising Cathepsin E (SEQ ID No. 1 or SEQ ID No. 2), a mutant, fragment or homologue thereof bound to at least one ligand comprising: (i) obtaining x-ray diffraction data for crystals of the complex (ii) utilising the atomic coordinates of Table 1 in whole or in part to define the three- dimensional structure of the complex.

In yet a further aspect, the invention provides a method of determining the three dimensional structure of a member of the aspartyl protease family comprising: utilizing the atomic coordinates of Table 1 in whole or in part to determining the three dimensional structure of a member of the aspartyl protease family.

In another aspect, the invention provides a method of identifying a ligand or low molecular weight compound that binds to Cathepsin E or any other aspartyl protease family member comprising: (i) utilising the three dimensional structure of Cathepsin E derived in whole or in part from the set of atomic coordinates in Table 1 to identify a potential ligand or low molecular weight compound that binds to Cathepsin E or any other aspartyl protease family member (ii) selecting those ligands or low molecular weight compound that bind to Cathepsin E or any other aspartyl protease family member.

In another aspect of the invention, a method of identifying a ligand or low molecular weight compound that selectively binds to Cathepsin E is provided comprising: (i) utilising the three dimensional structure of Cathepsin E derived in whole or in part from the set of atomic coordinates in Table 1 to identify a potential ligand or low molecular weight compound that binds selectively to Cathepsin E and to no other aspartyl protease family member (ii) selecting only those ligands or low molecular weight compounds which bind selectively to Cathepsin E and to no other aspartyl protease family member.

In still another aspect of the invention, a method is provided for identifying a ligand or low molecular weight compound which does not bind to Cathepsin E but selectively binds to another aspartyl protease family member comprising: (i) utilising the three dimensional structure of Cathepsin E derived in whole or in part from the set of atomic coordinates in Table 1 to identify a potential ligand or low molecular weight compound that binds selectively to an aspartyl protease family member but not to Cathepsin E (ii) selecting only those ligands or low molecular weight compounds which bind selectively to an aspartyl protease family member but not to Cathepsin E.

In one embodiment of the invention, a ligand or low molecular weight compound which inhibits the biological activity of Cathepsin E or any other aspartyl protease family member is preferred. Most preferred are highly selective inhibitors which inhibit one aspartyl protease family member selectively.

In another aspect of the invention, a method of designing a ligand or low molecular weight compound capable of binding to Cathepsin E or any other aspartyl protease is provided comprising: (i) using the atomic coordinates of Table 1 in whole or in part to determine the three dimensional structure of Cathepsin E (ii) screening said Cathepsin E with candidate ligands or low molecular weight compounds to determine which bind to Cathepsin E or any other aspartyl protease (iii) selecting those ligands or low molecular weight compounds which bind to Cathepsin E or any other aspartyl protease (iv) modifying those ligands or low molecular weight compounds which bind to maximize physical properties such as solubility, affinity, specificity or potency is provided.

In a preferred embodiment of the invention, a ligand or low molecular weight compound is designed which inhibits the activity of Cathepsin E or any other aspartyl protease family.

Most preferred are highly selective inhibitors which inhibit one aspartyl protease family member selectively.

In one embodiment of the invention, the candidate ligands or low molecular weight compounds are screened and designed in silico.

In yet another aspect of the invention, a pharmaceutical composition comprising a ligand identified or designed by any of the aforementioned methods is provided for use in preventing or treating of diseases and conditions involving an aspartyl protease family member.

Description of the Invention The full-length sequence of human Cathepsin E is given by SEQ ID No. 1 (see: Genbank Accession number NP 001901; G1 : 4503145, Swissprot Accession number P14091). Amino acids 1-18 represent the N-terminal signal sequence, amino acids 19-53 represent the pro- sequence and amino acids 54-396 represent the mature Cathepsin E.

A construct of human Cathepsin E is given by SEQ ID No. 2. Amino acids 1-23 represent the N-terminal extension, amino acids 24-58 represent the pro-sequence, amino acids 59-401 represent the mature Cathepsin E and amino acids 402-409 represent the C-terminal extension. The amino acids of the pro-sequence and mature Cathepsin E are identical for SEQ ID. 1 and SEQ ID. No. 2, but have different amino acid numbering due to the difference in the length of the N-terminal sequences.

SEQ ID. No. 3 and SEQ ID No. 4 represent primers to introduce the C-terminal extension.

The C-terminal extension is used to facilitate purification of Cathepsin E.

The present invention provides a crystal of Cathepsin E comprising a unit cell dimension of a = 61.32 + 5 Angstroms, b = 61.32 + 5 Angstroms, c = 207.80 5 Angstroms, a= 90.0 degrees (3 = 90.0 degrees y = 90 degrees. Depending on the particular conditions for crystallization, the parameters characterising the unit cell may vary within a limited range, for example, a, b, c each vary by up to 5 Angstroms. The space group of the present invention is P4i2i2 tetragona !.

The term"unit cell"according to the invention refers to the basic shape block. The entire volume of a crystal is constructed by regular assembly of such blocks. Each unit cell comprises a complete representation of the unit of pattern, the repetition of which builds up the crystal.

The term"space group"according to the invention refers to the arrangement of symmetry elements of a crystal.

The term"ligand"according to the invention, refers to a molecule or group of molecules that bind to one or more specific sites of Cathepsin E or another aspartyl protease family member. Preferred ligands are those that selectively bind to the active site of only one aspartyl protease family member. Most preferred are ligands that selectively bind to the active site of Cathepsin E. Ligands according to the invention are preferably low molecular weight molecules.

The term"low molecular weight compound"according to the invention refers to preferably organic compounds generally having a molecular weight less than about 1000, more preferably less than about 600. Most preferably, said low molecular weight compounds or ligands selectively inhibit biological activity of Cathepsin E or another aspartyl protease family member.

In context of a Cathepsin E inhibitor, the terms"peptide"or"peptide derivative"are intended to embrace a"peptidomimetic"or"peptide analogue"which complement the three- dimensional structure of the binding site of Cathepsin E or can be designed with improved physical or chemical properties to bind with the three-dimensional binding site of the Cathepsin E as provided in the present invention.

The term"mutant"refers to differences within the wild-type sequence of Cathepsin E set forth in SEQ. ID No. 1 by deletion, insertion, extension, or replacement of one or more selected amino acids.

According to the present invention, the term"mutant"also refers to a polypeptide, whose amino acid sequence differs from the sequence given in SEQ ID No. 2 by deletion, insertion or preferably replacement of one or more selected amino acids. For example, a Cathepsin E mutant of the present invention is preferably at least 50% homologous to SEQ ID No. 2, more preferably at least 80% homologous to SEQ ID No. 2 most preferably at least 90% homologous to SEQ ID No. 2.

A"fragment"of Cathepsin E according to the invention comprises more than 50% of the full- length sequence of Cathepsin E according to SEQ ID No. 1 or SEQ ID No. 2, more preferably at least 80% of the full length sequence of Cathepsin E according to SEQ ID No. 1 or SEQ ID No. 2, most preferably at least 90% of the full-length sequence of Cathepsin E according to SEQ ID No. 1 or SEQ ID No. 2.

A"N-terminal extension"of Cathepsin E according to the invention comprises the addition of amino acids at the N terminus of the full length Cathepsin E. For example, the N terminal extension of SEQ ID No. 2 is represent by amino acids 1-23.

A"C-terminal extension"of Cathepsin E according to the invention comprises the addition of 8-10 amino acids at the C-terminus of the full-length Cathepsin E. For example, the C- terminal extension of SEQ ID No. 2 is represented by amino acids 402-409.

Cathepsin E may be crystallisable with or without at least one ligand. It may also be crystallisable with or without the pro-sequence or parts of the pro-sequence of Cathepsin E.

According to the present invention, Cathepsin E crystals are stable if kept under suitable conditions. For example, the crystals are stable in there mother liquor at 20°C for at least 3-4 weeks. Preferable storage is frozen in liquid nitrogen.

In the present invention, Cathepsin E, a mutant, fragment or homologue thereof is advantageously obtained by expressing proCathepsin E in a recombinant host cell culture and subsequent refolding and auto-proteolytic cleavage of the pro-sequence.

According to the invention, Cathepsin E may be prepared by isolation from natural sources, e. g. cultured human cells or preferably by recombinant heterologous expression. Expression of recombinant Cathepsin E is achievable in eukaryotic or prokaryotic systems. For example, recombinant human Cathepsin E may be expressed in bacteria. The protease may be expressed as a Strep-tag fusion protein, a glutathione-S-transferase (GST) fusion protein, a histidine-tagged fusion protein or as an untagged protein. If desired, the fusion partner is removed before crystallization. The heterologously produced Cathepsin E to be used for crystallization is potentially biologically active. Such ability may be determined by morphological, biochemical or viability analysis well-known in the art.

Methods for the preparation of Cathepsin E mutants are commonly known in the art. For example, Cathepsin E mutants may be prepared by expression of Cathepsin E DNA previously modified in its coding region by oligo-nucleotide directed mutagenesis.

In the present invention, purified Cathepsin E is preferably at least 90 % homogeneous.

Protein homogeneity is determinable according to analytical methods well-know in the art, e. g. sequence analysis, electrophoresis, spectroscopic or chromatographic techniques. The purified protein is potentially proteolytically active. Appropriate assays for determining Cathepsin E activity towards a suitable substrate, e. g. a natural substrate or a synthetic substrate, are known in the art. In one embodiment of the invention, at any step prior to crystallization Cathepsin E may be complexed with a low molecular weight compound or ligand which is capable of suitably binding to Cathepsin E. Preferred is a compound inhibiting Cathepsin E activity. Protease inhibition is determinable employing assays known in the art. Suitable inhibitors include protease inhibitors which act on the catalytic site to inhibit Cathepsin E activity.

Various methods of cystallization can be used in the claimed invention including vapor diffusion, dialysis or batch crystallization. In vapor diffusion crystallization, a small volume (i. e. , a few microliters) of protein solution is mixed with a solution containing a precipitant.

This mixed volume is suspended over a well containing a small amount, i. e. about 0.15-1 ml, of precipitant. Vapor diffusion between the drop and the well will result in crystal formation in the drop.

The dialysis method of crystallization utilizes a semipermeable size-exclusion membrane that retains the protein but allows small molecules (i. e. buffers and precipitants) to diffuse in and out. In dialysis, rather than concentrating the protein and the precipitant by evaporation, the precipitant is allowed to slowly diffuse through the membrane and reduce the solubility of the protein while keeping the protein concentration fixed.

The batch method generally involves the slow addition of a precipitant to an aqueous solution of protein until the solution just becomes turbid, at this point the container can be sealed and left undisturbed for a period of time until crystallization occurs. In the batch technique the precipitant and the target molecule solution are simply mixed. Supersaturation is achieved directly rather than by diffusion. Often the batch technique is performed under oil. The oil prevents evaporation and extremely small drops can be used. For this, the term "microbatch"is used. A modification of this technique is not to use paraffin oil (which prevents evaporation completely) but rather use silicone oil or a mixture of silicone and paraffin oils so that a slow evaporation is possible.

The claimed invention can encompass any and all methods of crystallization. One skilled in the art can choose any of such methods and vary the parameters such that the chosen method results in the desired crystals.

One preferred method of crystallization of Cathepsin E involves mixing a Cathepsin E solution with a"reservoir buffer", with a lower concentration of the precipitating agent necessary for crystal formation. For crystal formation, the concentration of the precipitating agent has to be increased, e. g. by addition of precipitating agent, for example by titration, or by allowing the concentration of precipitating agent to balance by diffusion between the crystallization buffer and a reservoir buffer. Under suitable conditions such diffusion of water or volatile precipitating agent occurs along the gradient of precipitating agent, e. g. between the reservoir buffer having a higher concentration of precipitating agent and the crystallization buffer having a lower concentration of precipitating agent. Diffusion may be achieved e. g. by vapour diffusion techniques allowing diffusion of water in the common gas phase. Known techniques are e. g. vapour diffusion methods, such as the"hanging drop"or the"sitting drop"method. In the vapour diffusion method a drop of crystallization buffer containing the protein is hanging above or sitting beside a much larger pool of reservoir buffer. Alternatively, the balancing of the precipitating agent can be achieved through a semipermeable membrane (dialysis method) that separates the crystallization buffer from the reservoir buffer and prevents dilution of the protein into the reservoir buffer.

Formation of Cathepsin E crystals can be achieved under various conditions which are essentially determined by the following parameters: pH, presence of salts and additives, precipitating agent, protein concentration and temperature. The pH may range, for example, from about 3.0 to 11.0.

The present invention also relates to a computer readable medium having stored a model of the Cathepsin E crystal structure. In a preferred embodiment, said model is built from all or part of the X-ray diffraction data. The atomic coordinates are shown in Table 1.

The present invention provides the structure coordinates of human Cathepsin E. The term "structure coordinates"or"atomic coordinates"refers to mathematical coordinates derived from the mathematical equations (Fourier transformation) related to the diffraction pattern obtained on a monochromatic beam of X-rays by the atoms (scattering centers) of a crystal comprising a Cathepsin E. The diffraction data are used to calculate an electron density map of the repeating unit of the crystal. The electron density maps are used to establish the positions of the individual atoms within the unit cell of the crystal.

Structural coordinates of a crystalline composition of this invention may be stored in a machine-readable form on a machine-readable storage medium, e. g. a computer hard drive, diskette, DAT tape, CD, DVD etc. , for display as a three-dimensional shape or for other uses involving computer-assisted manipulation of, or computation based on, the structural coordinates or the three-dimensional structures they define. For example, data defining the three dimensional structure of a protein of Cathepsin E, or portions or structurally similar homologues of such proteins, may be stored in a machine-readable storage medium, and may be displayed as a graphical three-dimensional representation of the protein structure, typically using a computer capable of reading the data from said storage medium and programmed with instructions for creating the representation from such data.

According to the present invention, a three-dimensional Cathepsin E model is obtainable from a Cathepsin E crystal comprising Cathepsin E, mutant, fragment or homologue thereof.

Such a model can be built or refined from all or part of the Cathepsin E structure data of the present invention using the x-ray diffraction coordinates, particularly the atomic structure coordinates of Table 1.

The knowledge obtained from the three-dimensional model of Cathepsin E can be used in various ways. For example, it can be used to identify chemical entities, for example, small organic and bioorganic molecules such as peptidomimetics and synthetic organic molecules that bind to Cathepsin E and preferably block or prevent a Cathepsin E mediated or associated process or event, or that bind to another aspartyl protease or prevent another aspartyl protease mediated or associated process or event. Using the three-dimensional structure of Cathepsin E, the skilled artisan constructs a model of the Cathepsin E. For example, every atom can be depicted as a sphere of the appropriate van der Waals radius, and a detailed surface map of Cathepsin E can be constructed.

Chemical entities that have a surface that mimics the accessible surface of the catalytic binding site of Cathepsin E can be constructed by those skilled in the art. By way of example, the skilled artisan can screen three-dimensional structural databases of compounds to identify those compounds that position appropriate functional groups in similar three dimensional structural arrangement, then build combinatorial chemistry libraries around such chemical entities to identify those with high affinity to the catalytic binding site of Cathepsin E.

Ligands or small molecular compounds can be identified from screening compound databases or libraries and using a computational means to form a fitting operation to a binding site on Cathepsin E. The three dimensional structure of Cathepsin E as provided in the present invention in whole or in part by the structural coordinates of Table 1, can be used together with various docking programs.

The potential inhibitory or binding effect of a chemical entity on Cathepsin E may be analyzed prior to its actual synthesis and testing by the use of computer-modeling techniques. If the theoretical structure of the given chemical entity suggests insufficient interaction and association between it and Cathepsin E, the need for synthesis and testing of the chemical entity is obviated. However, if computer modeling indicates a strong interaction, the molecule may then be synthesized and tested for its ability to bind to Cathepsin E. Thus, expensive and time-consuming synthesis of inoperative compounds may be avoided.

An inhibitory or other binding compound of Cathepsin E 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 sites of Cathepsin E. Thus, one skilled in the art may use one of several methods to screen chemical entities or fragments for their ability to associate with Cathepsin E. This process may begin by visual inspection of, for example, the binding site on a computer screen based on the structural coordinates of Table 1 in whole or in part. Selected fragments or chemical entities may then be positioned in a variety of orientations, or"docked, "within the catalytic binding site of Cathepsin E. Docking may be accomplished using software such as Quanta and SYBYL, followed by energy minimization and molecular dynamics with standard molecular mechanics force fields, such as CHARMM or AMBER. Specialized computer programs may be of use for selecting interesting fragments or chemical entities. These programs include, for example, GRID, available from Oxford University, Oxford, UK; 5 MCSS or CATALYST, available from Molecular Simulations, Burlington, MA; AUTODOCK, available from Scripps Research Institute, La Jolla, CA; DOCK, available from University of California, San Francisco, CA, and XSITE, available from University College of London, UK.

Using molecular replacement to exploit a set of coordinates such as those of Table 1 of the invention, the structure of a crystalline Cathepsin E or portion thereof can for example, be bound to one or more ligands or low molecular weight compounds to form a complex.

The term"molecular replacement"refers to a method that involves generating a preliminary structural model of a crystal whose structural coordinates are unknown, by orienting and positioning a molecule whose structural coordinates are known, e. g., the Cathepsin E coordinates within the unit cell of the unknown crystal, so as to best account for the observed diffraction pattern of the unknown crystal. Phases can then be calculated from this model, and combined with the observed amplitudes to give an approximated Fourier synthesis of the structure whose coordinates are unknown. This in turn can be subject to any of the several forms of refinement to provide a final accurate structure. Using the structural coordinates provided by this invention, molecular replacement may be used to determine the structural coordinates of a crystalline co complex, unknown ligand, mutant, or homolog, or of a different crystalline form of Cathepsin E. Additionally, the claimed crystal and its coordinates may be used to determine the structural coordinates of a chemical entity that associates with Cathepsin E.

"Homology modeling"according to the invention involves constructing a model of an unknown structure using structural coordinates of one or more related proteins, protein domains and/or one subdomain. Homology modeling may be conducted by fitting common or homologous portions of the protein or peptide whose three dimensional structure is to be solved to the three dimensional structure of homologous structural elements. Homology modeling can include rebuilding part or all of a three dimensional structure by replacement of amino acids or other components by those of the related structure to be solved.

Molecular replacement according to the present invention, uses a molecule having a known structure. The three-dimensional structure of Cathepsin E provided in whole or in part in Table 1 in a machine-readable form on a data-carrier can be used as a starting point to model the structure of an unknown crystalline sample. This technique is based on the principle that two molecules which have similar structures, orientations and positions in the unit cell diffract similarly. Molecular replacement involves positioning the known structure in the unit cell in the same location and orientation as the unknown structure. Once positioned, the atoms of the known structure in the unit cell are used to calculate the structure factors that would result from a hypothetical diffraction experiment. This involves rotating the known structure in the six dimensions (three angular and three spatial dimensions) until alignment of the known structure with the experimental data is achieved. This approximate structure can be fine-tuned to yield a more accurate and often higher resolution structure using various refinement techniques. For instance, the resultant model for the structure defined by the experimental data may be subjected to rigid body refinement in which the model is subjected to limited additional rotation in the six dimensions yielding positioning shifts of under about 5%. The refined model may then be further refined using other known refinement methods. The present invention also enables homologues and mutants of Cathepsin E and the solving of their crystal structure. Based on the three-dimensional structure of Cathepsin E as provided in the present invention and using the atomic coordinates of Table 1 in whole or in part, the effects of site-specific mutations can be predicted. More specifically, the structural information provided herein permits the identification of desirable sites for amino acid modification, particularly amino acid mutation resulting in substitutional, insertional or deletion variants. Such variants may be designed to have special properties, particularly properties distinct from wild-type Cathepsin E, such as altered catalytic activity. Substitutions, deletions and insertions may be combined to arrive at a desired variant. Such variants can be prepared by methods well-known in the art, e. g. starting from wild-type Cathepsin E or by de novo synthesis.

Cathepsin E may also crystallize in a form different from the one disclosed herein. The structural information provided, for example, in SEQ ID No. 2 and Table 1 in whole or in part, is also useful for solving the structure of other crystal forms. Furthermore, it may serve to solve the structure of a Cathepsin E mutant, a Cathepsin E co-complex or a sufficiently homologous protein such as another aspartyl protease family member.

The Cathepsin E structural information provided herein is useful for the design of ligands or small molecule compounds which are capable of selectively interacting with Cathepsin E and thereby specifically modulating the biological activity of Cathepsin E. Furthermore, this information can be used to design and prepare Cathepsin E mutants, e. g. mutants with altered catalytic activity, model the three-dimensional structure and solve the crystal structure of proteins, such as Cathepsin E homologues, Cathepsin E mutants or Cathepsin E co-complexes, involving e. g. molecular replacement.

Preferred is a method for designing a Cathepsin E inhibitor which interacts at the active binding site. The present invention also relates to the chemical entity or ligand identified by such method. The present invention may also be used to design ligands or low molecular weight compounds which bind to another aspartyl protease family member using the atomic coordinates of Table 1 in whole or in part to determine the three-dimensional structure of a aspartyl protease family member. The present invention may also be used to design ligands or low molecular weight compounds which specifically inhibit one aspartyl protease family member and which specifically do not bind to Cathepsin E.

One approach enabled by this invention is the use of the structural coordinates of Cathepsin E to design chemical entities that bind to or associate with Cathepsin E and alter the physical properties of the chemical entities in different ways. Thus, properties such as, for example, solubility, affinity, specificity, potency, on/off rates, or other binding characteristics may all be altered and/or maximized. One may design desired chemical entities by probing an Cathepsin E crystal comprising Cathepsin E with a library of different entities to determine optimal sites for interaction between candidate chemical entities and Cathepsin E. For example, high-resolution x-ray diffraction data collected from crystals saturated with solutes allows the determination of where each type of solute molecule adheres. Small molecules that bind tightly to those sites can then be designed and synthesized and tested for the desired activity. Once the desired activity is obtained, the molecule can be further altered to maximize desired properties.

The invention also contemplates computational screening of small-molecule databases or designing of chemical entities that can bind in whole or in part to Cathepsin E. They may also be used to solve the crystal structure of mutants, co-complexes, or the crystalline form of any other molecule homologous to, or capable of associating with, at least a portion of Cathepsin E. One method that may be employed for this purpose is molecular replacement.

An unknown crystal structure, which may be any unknown structure, such as, for example, another crystal form of Cathepsin E, an Cathepsin E mutant or peptide, or a co-complex with Cathepsin E, or any other unknown crystal of a chemical entity that associates with Cathepsin E that is of interest, may be determined using the whole of part of the structural coordinates set forth in Table 1. This method provides an accurate structural form for the unknown crystal far more quickly and efficiently than attempting to determine such information without the invention herein.

In one preferred embodiment of the invention, candidate ligands are screened in silico. The information obtained can be used to obtain specific inhibitors of Cathepsin E or any other aspartyl protease family member. In a most preferred embodiment, a method is provided to select inhibitors specific for only one aspartyl protease family member. For example, an inhibitor which inhibits only Cathepsin E but not other aspartyl protease family members.

In another preferred embodiment of the invention, a method is provided to design ligands which inhibit the activity of Cathepsin E or any other aspartyl protease family member. In a most preferred embodiment, a method is provided to design a selective inhibitor which is specific for only one aspartyl protease family member, for example, specific for only Cathepsin E.

The design of chemical entities that inhibit Cathepsin E generally involves consideration of at least two factors. First, the chemical entity must be capable of physically or structural associating with Cathepsin E, preferably at the catalytic site of Cathepsin E. The association may be any physical, structural, or chemical association, such as, for example, covalent or non-covalent binding, or van der Waals, hydrophobic, or electrostatic interactions. Second, the chemical entity must be able to assume a conformation that allows it to associate with Cathepsin E, preferentially at the catalytic site of Cathepsin E. Although not all portions of the chemical entity will necessarily participate in the association with Cathepsin E, those non-participating portions may still influence the overall conformation of the molecule. This in turn may have a significant impact on the desirability of the chemical entity. Such conformational requirements include the overall three-dimensional structure and orientation of the chemical entity in relation to all or a portion of the binding site.

Once a compound has been designed or selected by the above methods, the efficiency with which that compound may bind to Cathepsin E may be tested and modified for the maximum desired characteristic (s) using computational or experimental evaluation. Various parameters can be maximized depending on the desired result. These include, but are not limited to, specificity, affinity, on/off rates, hydrophobicity, solubility, and other characteristics readily identifiable by the skilled artisan.

The present invention also relates to identification of compounds which inhibit Cathepsin E or any other aspartyl protease family members activity. In particular, said compounds are useful in preventing or treating disorders mediated by Cathepsin E or other aspartyl protease family members, for example, acute or chronic rejection or organ or tissue allografts or xenografts, atherosclerosis, vascular occlusion due to vascular injury such as angioplasty, restenosis, hypertension, heart failure, chronic obstructive pulmonary disease, CNS disease such as Alzheimer disease or amyotrophic lateral sclerosis, cancer, infectious diseases such as AIDS, septic shock or adult respiratory distress syndrome, ischemia/reperfusion injury e. g. myocardial infarction, stroke, gut ischemia, renal failure or hemorrhage shock or traumatic shock. Further, said compounds can be useful in preventing or treating T-cell mediated acute or chronic inflammatory diseases or disorders or autoimmune diseases, for example, rheumatoid arthritis, osteoarthritis, systemic lupus erythematosus, Hashimoto's thyroidis, multiple sclerosis, myasthenia gravis, diabetes type I or 11 and disorders associated therewith, respiratory diseases such as asthma or inflammatory lung injury, inflammatory liver injury, inflammatory glomerular injury, cutaneous manifestations of immunologically- mediated disorders or illnesses, inflammatory and hyperproliferative skin diseases (such as psoriasis, atopic dermatitis, allergic contact dermatitis, irritant contact dermatitis, and further eczematous dermatitis, seberrhoeic dermatitis), inflammatory eye diseases, e. g. Sjoegren's syndrome, keratoconjunctivitis, or uveitis, inflammatory bowel disease, Crohn's disease or ulcerative colitis.

For the above uses, the required dosage will depend on the mode of administration, the particular condition to be treated and the desired effect. In general, satisfactory results are to be obtained systematically at daily dosages from about 0.1 to about 100 mg/kg body weight.

A daily dosage in a larger mammal (e. g. human) is in the range from about 0.5mg to about 2000mg, conveniently administered, for example, in divided doses up to four times a day or in delayed dosage form. The compounds may be administered by any conventional route, in particular enterally e. g. orally, e. g. in the form or tablets or capsules, or parenterally, e. g. in the form of injectable solutions or suspensions, topically, e. g. in the form of lotions, gels, ointments or creams, or in a nasal or a suppository form. Pharmaceutical compositions comprising said compound in free form or in a pharmaceutically acceptable salt form in association with at least one pharmaceutically acceptable carrier or diluent may be manufactured in conventional manner by mixing with a pharmaceutically acceptable carrier or diluent. Unit dosage forms for oral administration contain, for example, from about 0.1 mg to about 500 mg of active substance. Topical administration is e. g. to the skin. A further form of topical administration is to the eye. Compounds may be administered in free form or in a pharmaceutically acceptable salt form. Such salts may be prepared in a conventional manner and exhibit the same order of activity as the free compounds. The present invention enables the use of molecular design techniques, particularly the rational drug design approach, to prepare new or improved chemical entities and compounds, including Cathepsin E inhibitors, capable of irreversibly or reversibly, modulating Cathepsin E activity.

Improved entities or compounds means that these entities or compounds are superior to the "original"or parent compound they are derived from with regard to a property relevant to therapeutic use including suitability for in vivo administration, e. g. cellular uptake, solubility, stability against (enzymatic) degradation, binding affinity or specificity, and the like. For example, on the basis on the information provided herein it is possible to specially design Cathepsin E inhibitors which covalently, or preferably non-covalently, bind to Cathepsin E.

Such inhibitors may act in a competitive or uncompetitive manner, bind at or close to the active site of Cathepsin E or act allosterically.

The design of Cathepsin E modulators the following aspects should be considered: (i) if the candidate compound is capable of physically and structurally associating with Cathepsin E, and/or (ii) if the compound is capable of assuming a conformation allowing it to associate with Cathepsin E. Advantageously, computer modelling techniques are used in the process of assessing these abilities for the modulator as a whole, or a fragment thereof-in order to minimize efforts in the synthesis or testing of unsuccessful candidate compounds.

Specialized computer software is well-know in the art.

Another design approach is to probe a Cathepsin E crystal with a variety of different chemical entities to determine optimal sites for interaction between candidate Cathepsin E inhibitors and the target enzyme. Yet another possibility which arises from the present invention is to screen computationally small molecule data bases for chemical entities or compounds that are capable of binding, in whole or in part, to Cathepsin E catalytic domain.

The quality of fit to the binding site may be judged e. g. by shape complementarity or by estimated interaction energy. Knowledge of the three-dimensional arrangement of the modifications can be then utilized for the design of new Cathepsin E ligands or low molecular weight compounds such as selective inhibitors.

Chemical entities that are capable of associating with the aspartyl protease family member may inhibit its interaction with naturally occurring ligands of the protein and may inhibit biological functions mediated by such interaction. In the case of Cathepsin E, such biological functions include the biogenesis of the vasoconstrictor peptide endothelin and the antigen/invariant chain processing. Such chemical entities are potential drug candidates.

Compounds of the structures selected or designed by any of the foregoing means may be tested for their ability to bind to an aspartyl protease family member, particularly to Cathepsin E, to inhibit the binding to a natural or non-natural ligand therefore, and/or inhibit a biological function mediated by the aspartyl protease family member.

The following examples serve to illustrate embodiments of the present invention but should not be construed as a limitation thereof. Compounds identified by any of the methods described herein are also encompassed by this invention.

Examples Standard protocols in molecular biology are applied, if not otherwise stated. The manufacturer's recommendations are followed when using commercially available kits.

Example 1 : Generation of Cathepsin E variants for expression in E. coli The gene of human pro-cathepsin E is inserted into the expression vector pET22b. Insertion of the pro-Cathepsin E gene into pET22b results in 23 additional amino acids at the N- terminus of pro-Cathepsin E (SEQ ID No. 2). The pro-Cathepsin E gene is C-terminally extended to code for 8 additional amino acid residues (WSHPQFEK) in order to facilitate purification by using the Strep-tag@ system. The sequence of the primers to introduce the C- terminal extension is given by SEQ ID No. 3 and SEQ ID No. 4.

Example 2: Expression of Cathepsin E in E. coli, refolding and purification E. coli cells (BL21 (DE3) pLysS harboring the cathepsin E expression plasmid are induced with IPTG. Cells are resuspended in 50 mM Tris/HCI buffer at pH 8.0 and ruptured by sonication. After centrifugation of the homogenate at 16500g for 15 min, the inclusion body- containing pellet is washed twice with the same buffer and then dissolved in 50 mM Tris/HCI buffer at pH 8.0, containing 8 M guanidinium chloride and 100 mM DTE. Pro-cathepsin E is refolded by diluting the clear supernatant at a ratio of 1: 150 into 50 mM Tris/HCI buffer at pH 9.5, containing 1 mM EDTA, 0.7 M arginine, 0.5 mM oxidized glutathione and 2 mM reduced glutathione, followed by dialysis against 25 mM Tris/HCI buffer, pH 8.0, 1 mM EDTA. For generation of the mature, active enzyme, the protein solution is concentrated 10-fold and the pH adjusted to 3.5 with a 1 M sodium citrate solution, pH 3.1. After 15 minutes incubation at room temperature the pH is increased to 8.0 with 1 M Tris/HCI, pH 9.5, and the precipitated protein removed by centrifugation. The supernatant is loaded onto a Strep-Tactino column. The column is washed with 100 mM Tris/HCI buffer, pH 8.0, containing 1 M NaCI, 1 mM EDTA and 0.1 % (v/v) Tween 20 and the proteins are eluted with buffer A (100 mM Tris/HCI, at pH 8.0, 150 mM NaCI, and 1 mM EDTA) containing 2.5 mM desthiobiotin. The fractions containing active cathepsin E are pooled and loaded onto a Superdex 200 16/60 gel filtration column which is equilibrated and run with buffer A. Pure cathepsin E is then concentrated to 3 mg/mi and subjected to crystallization trials.

Example 3: Crvstallization, data collection and structure determination of human Cathepsin E Crvstallization Human Cathepsin E is crystallized at 20° by the vapor diffusion method in sitting drops using a cartesian robotics and 96 well plates. 200 ni of the protein solution (3 mg/ml Cathepsin E, 100 mM Tris/HCI at pH 8.0, 150 mM NaCI and 1 mM EDTA) are mixed with 200 ni reservoir solution and equilibrated against 150 ul of the respective reservoir solution. Diffracting quality crystals can be obtained after approximately five month in the following two reservoir solutions : a) 16% PEG4000,100 mM Tris/HCI at pH 8.5 and 200 mM MgCI2 b) 30% PEG4000,100 mM sodium citrate at pH 5.6 and 200 mM ammonium sulfate For both crystallization conditions the crystals have a tetragonal bipyramidal morphology.

Data collection For data collection a crystal is cryoprotected by addition of 1 pI reservoir solution and 0. 2 ul Glycerol to the nano drop and flash-frozen in liquid nitrogen. X-ray diffraction data were collected on a Nonius FR591 rotating anode operating at 5 kW (55 kV and 90 mA) with a MAR345 imaging plate detector at 100 K. 38 images are collected with 1. 0° oscillation each, using an exposure time of 60 min per frame and a crystal-to-detector distance of 200 mm.

The raw diffraction data are processed with MOSFLM and scaled with SCALA from the CCP4 suite (Collaborative Computational Project, Number 4,1994). The data collection statistics are summarized in Table 2.

Structure determination and refinement The structure of Cathepsin E can be solved by the molecular replacement method using the program MOLREP (Collaborative Computational Project, Number 4,1994) and the coordinates of human Pepsin A (Protein Data Bank accession code 1PSN, Fujinaga et al., 1995) as a search model. Using a high resolution data cut off of 3.5 A, an unambiguous solution is found in space group P4, 212 with one cathepsin E molecule in the asymmetric unit (correlation coefficient of 0.44, R-factor of 0.48). An initial refinement cycle using the rigid-body and simulated annealing protocols as implemented in CNX version 2000 (Accelrys, San Diego, USA,/Brunger, 1998) results in a model used to calculate the initial electron density map, which is of high quality and allows the unambiguous assignment and building of most amino acids residues using the program O version 7.0 (Jones et al. 1991). Subsequently, alternating cycles of refinement, including restrained individual B-factor refinement, and manual rebuilding resulted in the final model with R-factors of 0.198 and 0.238 (Rfree). Cross-validation is used throughout the refinement process using 10% of the reflections. The water molecules of the final model are placed using the water-pick protocol as implemented in CNX version 2000. The stereochemical quality of the model is analyzed with the programs CNX version 2000 and PROCHECK (Laskowski et al. 1993). The refinement statistics are summarized in Table 3.

Example 4: Crystal Structure of Cathepsin E The overall structure of Cathepsin E (amino acid numbering corresponding to SEQ ID No. 1) comprises the general fold of A1 aspartyl proteases. Cathepsin E contains three topologically distinct reagents, a N-terminal domain (residues Lys67-Val210), a C-terminal domain (residues Thr251-Gln377) and a six-stranded anti-parallel ß-sheet interdomain, connecting the pseudo-twofold-related N-and C-terminal domains. Both, the N-and C- terminal domains contribute an aspartic acid, Asp96 and Asp281 respectively, to the active site. The interdomain consists of amino acids Gly19-Arg27 from the pro-sequence, building the outermost strand of the p-sheet and being non covalently associated to Cathepsin E, amino acids Asp211-Val250, linking the N-and the C-terminal domains, and the C-terminal amino acids Phe378-Val395.

Most amino acids are well defined by the electron density with the following exceptions: The amino acids Arg28-Met53 of the pro-sequence are completely disordered and therefore not visible in the x-ray structure. Additional disordered regions, that have not been considered in the Cathepsin E structure, comprise the N-terminal amino acids lle54-Ala66, amino acids Glu224-Gly225 as well as amino acids Phe344-Met348.

The Cathepsin E structure represents an intermediate 2 state on the activation pathway of aspartyl proteases, similar to that described for Pepsin C with the N-terminal amino acids of mature Cathepsin E (residues Lys67-Glu77) residing in the active site, more precisely, in the unprimed binding site of the active site. The Tyr73 side chain occupies the S1 binding site and makes a hydrogen bond to the carboxylate of Asp96. Leu74 and the backbone carbonyl group of Tyr73 bind to the S3 pocket, while the side chain of Asn72 points towards the S4 pocket. By the insertion of the N-terminal amino acid residues into the active site, the ß- hairpin structure, termed the flap (residues Phe135-Gly146), is displace by approximately 4 A in comparison to the position, observed in known aspartyl protease structures complexed with pepide-based transition state inhibitors. In addition to the displacement of the flap, the loop Val169-Ala179, shielding the combined S1-S3 hydrophobic binding pocked from the solvent, is also displaced to some extend.

The primed binding site of the active site is not occupied and is observed in an active conformation with the Proline rich loop, flanking the S2'binding pocket (residues Gly357- Leu367), in the closed conformation.

Example 5: Identification and Design of Specific Inhibitors to Aspartyl Protease Family Members Using the three dimensional information from Table 1 in whole or in part, one can compare the inhibition of Cathepsin E complexed with an inhibitor to inhibition of another aspartyl protease family member with the same inhibitor to identify any differences in binding. For example, inhibition of Cathepsin E and Cathepsin D can be compared against each other using the same inhibitor. Using known techniques of molecular modeling and/or molecular replacement, modifications can be made such that a specific inhibitor can be designed which does not bind to Cathepsin E but retains inhibitory activity of Cathepsin D.

In the same way, it is possible to design selective inhibitors for BACE1, BACE2, renin, pepsin A, pepsin C, and napsin A by using the structural information from Table 1 in whole or in part to specifically design an inhibitor to a particular aspartyl protease family member.

Table 1: Atomic Coordinates for Cathepsin E crystal structure ATOM 1 CB PRO P 14 29.627-18. 334 22.690 1. 00 31. 04 P C ATOM 2 CG PRO P 14 30.875-17. 489 22.919 1. 00 30. 87 P c ATOM 3 C PRO P 14 29.752-18. 744 20.217 1. 00 31. 89 P C ATOM 4 0 PRO P 14 30.531-18. 014 19.610 1. 00 31. 04 P O ATOM 5 N PRO P 14 31.568-19. 433 21.779 1. 00 31. 38 P N ATOM 6 CD PRO P 14 32.050-18. 484 22.801 1. 00 30. 51 P C ATOM 7 CA PRO P 14 30.104-19. 286 21.602 1. 00 31. 50 P C ATOM 8 N ALA P 15 28.573-19. 109 19.726 1. 00 32. 54 P N ATOM 9 CA ALA P 15 28.106-18. 651 18.424 1. 00 34. 74 P C ATOM 10 CB ALA P 15 26.782-19. 332 18.074 1. 00 34. 66 P C ATOM 11 C ALA P 15 27.908-17. 144 18.480 1. 00 36. 24 P C ATOM 12 O ALA P 15 27.556-16. 600 19.525 1. 00 35. 73 P O ATOM 13 N MET P 16 28.141-16. 462 17.367 1. 00 38. 87 P N ATOM 14 CA MET P 16 27.943-15. 026 17.355 1. 00 43. 22 P C ATOM 15 CB MET P 16 28.898-14. 339 16.378 1. 00 44. 16 P C ATOM 16 CG MET P 16 30.332-14. 213 16.914 1. 00 46. 93 P C ATOM 17 SD MET P 16 30.436-13. 559 18.633 1. 00 48. 73 P S ATOM 18 CE MET P 16 31.214-14. 999 19.530 1. 00 46. 97 P C ATOM 19 C MET P 16 26.491-14. 772 16. 988 1. 00 45. 69 P C ATOM 20 0 MET P 16 26.002-15. 248 15.960 1. 00 45. 44 P O ATOM 21 N ALA P 17 25.805-14. 029 17.857 1.00 48.60 P N ATOM 22 CA ALA P 17 24.386-13. 725 17.695 1. 00 51. 14 P C ATOM 23 CB ALA P 17 23.846-13. 127 18.995 1. 00 50. 50 P C ATOM 24 C ALA P 17 24.023-12. 825 16.523 1. 00 52. 50 P C ATOM 25 O ALA P 17 24.855-12. 087 15.994 1. 00 53. 26 P 0 ATOM 26 N MET P 18 22.761-12. 908 16.120 1. 00 54. 53 P N ATOM 27 CA MET P 18 22.245-12. 088 15.036 1. 00 56. 11 P C ATOM 28 CB MET P 18 21.599-12. 950 13.952 1. 00 57. 70 P C ATOM 29 CG MET P 18 20.985-12. 137 12.810 1.00 60.13 P C ATOM 30 SD MET P 18 22.239-11. 272 11.806 1.00 62.53 P S ATOM 31 CE MET P 18 22.112-9. 500 12.421 1.00 61.40 P C ATOM 32 C MET P 18 21.190-11. 167 15.634 1. 00 56. 05 P C ATOM 33 0 MET P 18 20.502-11. 543 16.586 1. 00 56. 06 P 0 ATOM 34 N GLY P 19 21.075-9. 964 15.075 1. 00 55. 78 P N ATOM 35 CA GLY P 19 20.095-9. 008 15.556 1. 00 54. 66 P C ATOM 36 C GLY P 19 18.803-9. 713 15.909 1. 00 53. 93 P C ATOM 37 0 GLY P 19 18.231-10. 435 15.090 1. 00 54. 52 P 0 ATOM 38 N SER P 20 18.346-9. 517 17.139 1. 00 52. 49 P N ATOM 39 CA SER P 20 17.123-10. 153 17.597 1. 00 50. 72 P C ATOM 40 CB SER P 20 17.416-11. 056 18.800 1. 00 51. 99 P C ATOM 41 OG SER P 20 16.241-11. 716 19.241 1.00 52.79 P O ATOM 42 C SER P 20 16.086-9. 114 17.978 1. 00 48. 52 P C ATOM 43 O SER P 20 16.423-8. 041 18. 481 1. 00 49. 04 P 0 ATOM 44 N LEU P 21 14.822-9. 438 17.726 1.00 44.95 P N ATOM 45 CA LEU P 21 13.729-8. 540 18.055 1. 00 40. 46 P C ATOM 46 CB LEU P 21 12.797-8. 338 16.854 1. 00 39. 93 P C ATOM 47 CG LEU P 21 13.328-7. 632 15.604 1. 00 39. 84 P C ATOM 48 CD1 LEU P 21 12.198-7. 521 14.595 1. 00 39. 47 P C ATOM 49 CD2 LEU P 21 13.875-6. 248 15.953 1. 00 39. 18 P C ATOM 50 C LEU P 21 12.944-9. 149 19.200 1. 00 37. 68 P C ATOM 51 O LEU P 21 12.543-10. 312 19.148 1. 00 37. 35 P O ATOM 52 N HIS P 22 12.727-8. 351 20.234 1. 00 34. 35 P N ATOM 53 CA HIS P 22 11.984-8. 798 21.394 1. 00 30. 79 P C ATOM 54 CB HIS P 22 12.732-8. 350 22.642 1. 00 29. 18 P C ATOM 55 CG HIS P 22 14.156-8. 816 22.656 1. 00 28. 80 P C ATOM 56 CD2 HIS P 22 15.316-8. 146 22.457 1. 00 28. 25 P C ATOM 57 ND1 HIS P 22 14.498-10. 149 22.766 1. 00 28. 76 P N ATOM 58 CE1 HIS P 22 15.807-10. 278 22.631 1. 00 28. 10 P C ATOM 59 NE2 HIS P 22 16.326-9. 078 22.442 1. 00 29. 13 P N ATOM 60 C HIS P 22 10.574-8. 236 21. 291 1. 00 29. 24 P C ATOM 61 O HIS P 22 10.318-7. 068 21.577 1. 00 28. 22 P O ATOM 62 N ARG P 23 9.674-9. 105 20.836 1. 00 28. 38 P N ATOM 63 CA ARG P 23 8.274-8. 781 20.608 1. 00 27. 83 P C ATOM 64 CB ARG P 23 7.731-9. 645 19.468 1. 00 28. 90 P C ATOM 65 CG ARG P 23 8.536-9. 558 18.180 1. 00 30. 04 P C ATOM 66 CD ARG P 23 8.222-10. 742 17.272 1. 00 33. 61 P C ATOM 67 NE ARG P 23 9.046-10. 745 16.064 1. 00 35. 54 P N ATOM 68 CZ ARG P 23 8.776-10. 040 14.969 1. 00 35. 93 P C ATOM 69 NH1 ARG P 23 7.693-9. 271 14. 920 1. 00 35. 81 P N ATOM 70 NH2 ARG P 23 9.593-10. 100 13.924 1. 00 35. 09 P N ATOM 71 C ARG P 23 7.387-8. 953 21.826 1. 00 26. 56 P C ATOM 72 O ARG P 23 7.452-9. 958 22.532 1. 00 25. 52 P O ATOM 73 N VAL P 24 6.541-7. 956 22.040 1. 00 26. 42 P N ATOM 74 CA VAL P 24 5.608-7. 936 23.152 1. 00 26. 38 P C ATOM 75 CB VAL P 24 5.926-6. 763 24.112 1. 00 25. 48 P C ATOM 76 CG1 VAL P 24 4.912-6. 715 25.242 1. 00 23. 14 P C ATOM 77 CG2 VAL P 24 7.336-6. 915 24.657 1. 00 24. 96 P C ATOM 78 C VAL P 24 4.206-7. 752 22.575 1. 00 27. 09 P C ATOM 79 O VAL P 24 3.842-6. 659 22.142 1. 00 27. 39 P O ATOM 80 N PRO P 25 3.409-8. 828 22.547 1. 00 27. 18 P N ATOM 81 CD PRO P 25 3.768-10. 203 22.937 1. 00 27. 25 P C ATOM 82 CA PRO P 25 2.043-8. 775 22.018 1. 00 27. 77 P C ATOM 83 CB PRO P 25 1.547-10. 213 22.188 1. 00 26. 82 P C ATOM 84 CG PRO P 25 2.809-11. 025 22.115 1. 00 26. 50 P C ATOM 85 C PRO P 25 1.181-7. 787 22.795 1. 00 28. 75 P C ATOM 86 0 PRO P 25 1.308-7. 673 24.016 1. 00 28. 64 P O ATOM 87 N LEU P 26 0.312-7. 076 22.083 1. 00 29. 58 P N ATOM 88 CA LEU P 26-0.592-6. 108 22.702 1. 00 31. 73 P C ATOM 89 CB LEU P 26-0.234-4. 681 22.267 1. 00 29. 69 P C ATOM 90 CG LEU P 26 1.217-4. 232 22.453 1. 00 30. 32 P C ATOM 91 CD1 LEU P 26 1.395-2. 860 21.837 1. 00 30. 72 P C ATOM 92 CD2 LEU P 26 1.579-4. 203 23.928 1. 00 30. 19 P C ATOM 93 C LEU P 26-2.011-6. 446 22.243 1. 00 33. 47 P C ATOM 94 0 LEU P 26-2.206-6. 892 21.114 1. 00 33. 17 P 0 ATOM 95 N ARG P 27-2. 997-6.236 23.112 1. 00 36. 18 P N ATOM 96 CA ARG P 27-4.384-6. 535 22.769 1. 00 38. 38 P C ATOM 97 CB ARG P 27-4.838-7. 785 23.516 1.00 40.60 P C ATOM 98 CG ARG P 27-3.912-8. 962 23.355 1.00 43.40 P C ATOM 99 CD ARG P 27-3.904-9. 815 24.618 1.00 48.43 P C ATOM 100 NE ARG P 27-3.497-9. 054 25.804 1. 00 51. 34 P N ATOM 101 CZ ARG P 27-3.298-9. 590 27.008 1. 00 52. 58 P C ATOM 102 NH1 ARG P 27-3. 465-10.895 27. 192 1.00 53.65 P N ATOM 103 NH2 ARG P 27-2.937-8. 824 28.031 1. 00 52. 56 P N ATOM 104 C ARG P 27-5.303-5. 378 23.130 1.00 38.98 P C ATOM 105 0 ARG P 27-4.916-4. 585 24.015 1.00 40.11 P O ATOM 106 OXT ARG P 27-6.404-5. 291 22.542 1. 00 38. 93 P 0 ATOM 107 CB LYS A 67-9.164 12.473 42.655 1. 00 42. 16 A C ATOM 108 CG LYS A 67-9.189 13.738 43.492 1.00 44.71 A C ATOM 109 CD LYS A 67-7.776 14.253 43.727 1.00 47.20 A C ATOM 110 CE LYS A 67-7.749 15.401 44.729 1.00 48.51 A C ATOM 111 NZ LYS A 67-6.348 15.815 45.061 1.00 49.76 A N ATOM 112 C LYS A 67-10.352 10.569 41. 576 1. 00 38. 39 A C ATOM 113 0 LYS A 67-10.496 9.447 42.066 1. 00 37. 71 A O ATOM 114 N LYS A 67-11.189 11.526 43.734 1.00 40.58 A N ATOM 115 CA LYS A 67-10.535 11.829 42.424 1.00 40.26 A C ATOM 116 N GLU A 68-10.036 10.773 40.300 1. 00 36. 63 A N ATOM 117 CA GLU A 68-9.806 9. 680 39.360 1.00 34.14 A C ATOM 118 CB GLU A 68-10.875 9.685 38.268 1. 00 35. 37 A C ATOM 119 CG GLU A 68-12.273 9.393 38.790 1. 00 38. 12 A C ATOM 120 CD GLU A 68-12. 547 7.904 38.951 1.00 40.19 A C ATOM 121 OE1 GLU A 68-11.592 7.135 39.196 1.00 40.67 A O ATOM 122 OE2 GLU A 68-13.726 7.503 38.840 1.00 41.31 A 0 ATOM 123 C GLU A 68-8.426 9.898 38.753 1. 00 32. 04 A C ATOM 124 0 GLU A 68-8. 291 10.437 37.652 1.00 30.71 A O ATOM 125 N PRO A 69-7.377 9.479 39.477 1. 00 30. 08 A N ATOM 126 CD PRO A 69-7.479 8.779 40.768 1. 00 28. 88 A C ATOM 127 CA PRO A 69-5.975 9.602 39.072 1. 00 28. 98 A C ATOM 128 CB PRO A 69-5.228 8.881 40.190 1. 00 28. 51 A C ATOM 129 CG PRO A 69-6.133 9.034 41.362 1. 00 29. 57 A C ATOM 130 C PRO A 69-5.633 9.009 37.710 1. 00 27. 77 A C ATOM 131 0 PRO A 69-4.761 9.523 37.012 1. 00 27. 66 A O ATOM 132 N LEU A 70-6.323 7.938 37.330 1. 00 26. 45 A N ATOM 133 CA LEU A 70-6.031 7.262 36.065 1. 00 26. 49 A C ATOM 134 CB LEU A 70-5.783 5.773 36.339 1. 00 24. 54 A C ATOM 135 CG LEU A 70-4.805 5.474 37.479 1. 00 23. 47 A C ATOM 136 CD1 LEU A 70-4.777 3.973 37.756 1. 00 23. 01 A C ATOM 137 CD2 LEU A 70-3.416 6.003 37.121 1. 00 21. 23 A C ATOM 138 C LEU A 70-7.103 7.391 34.992 1. 00 27. 17 A C ATOM 139 O LEU A 70-7. 129 6.600 34.044 1. 00 26. 34 A 0 ATOM 140 N ILE A 71-7.971 8.389 35.126 1. 00 28. 30 A N ATOM 141 CA ILE A 71-9.063 8.586 34.178 1. 00 29. 43 A C ATOM 142 CB ILE A 71-9. 880 9.842 34.534 1. 00 31. 54 A C ATOM 143 CG2 ILE A 71-9. 061 11.097 34.240 1. 00 31. 19 A C ATOM 144 CG1 ILE A 71-11. 186 9.848 33.735 1.00 32.51 A C ATOM 145 CD1 ILE A 71-12. 104 11.018 34.059 1. 00 36. 03 A C ATOM 146 C ILE A 71-8. 652 8.685 32.708 1. 00 29. 53 A C ATOM 147 O ILE A 71-9. 422 8.327 31.823 1. 00 28. 87 A O ATOM 148 N ASN A 72-7. 447 9.173 32.442 1. 00 30. 63 A N ATOM 149 CA ASN A 72-6.983 9.307 31.063 1. 00 31. 03 A C ATOM 150 CB ASN A 72-5.907 10.393 30.962 1. 00 33. 08 A C ATOM 151 CG ASN A 72-6. 497 11.794 30.926 1. 00 35. 85 A C ATOM 152 OD1 ASN A 72-5.800 12.782 31.176 1. 00 38. 52 A 0 ATOM 153 ND2 ASN A 72-7.785 11.888 30.598 1. 00 35. 31 A N ATOM 154 C ASN A 72-6. 459 8.008 30.484 1. 00 30. 37 A C ATOM 155 O ASN A 72-6.005 7.981 29. 345 1. 00 30. 37 A 0 ATOM 156 N TYR A 73-6.517 6.936 31.272 1. 00 29. 52 A N ATOM 157 CA TYR A 73-6.067 5.623 30.816 1. 00 29. 81 A C ATOM 158 CB TYR A 73-4. 947 5.079 31.712 1. 00 28. 00 A C ATOM 159 CG TYR A 73-3.665 5.865 31.649 1. 00 26. 65 A C ATOM 160 CD1 TYR A 73-3. 423 6.909 32.543 1. 00 26. 24 A C ATOM 161 CE1 TYR A 73-2.258 7.665 32.466 1. 00 26. 02 A C ATOM 162 CD2 TYR A 73-2.705 5.591 30.671 1. 00 24. 53 A C ATOM 163 CE2 TYR A 73-1.538 6.339 30.585 1. 00 24. 65 A C ATOM 164 CZ TYR A 73-1.320 7.377 31.485 1. 00 25. 72 A C ATOM 165 OH TYR A 73-0.180 8.141 31.399 1. 00 25. 49 A 0 ATOM 166 C TYR A 73-7.213 4.615 30.812 1. 00 30. 85 A C ATOM 167 O TYR A 73-7.044 3.479 30.374 1. 00 30. 35 A O ATOM 168 N LEU A 74-8.379 5.036 31.290 1.00 33.53 A N ATOM 169 CA LEU A 74-9.531 4.147 31.373 1. 00 37. 70 A C ATOM 170 CB LEU A 74-10.515 4.677 32.415 1. 00 37. 53 A C ATOM 171 CG LEU A 74-9.877 4.853 33.794 1. 00 39. 31 A C ATOM 172 CD1 LEU A 74-10.952 5.198 34.814 1. 00 40. 69 A C ATOM 173 CD2 LEU A 74-9. 151 3.578 34.196 1. 00 38. 49 A C ATOM 174 C LEU A 74-10.266 3.881 30.065 1. 00 39. 74 A C ATOM 175 O LEU A 74-11. 155 3.033 30.010 1. 00 39. 65 A 0 ATOM 176 N ASP A 75-9.899 4.597 29.011 1.00 42.71 A N ATOM 177 CA ASP A 75-10.547 4.398 27.726 1.00 45.37 A C ATOM 178 CB ASP A 75-10.833 5.747 27.065 1.00 48.03 A C ATOM 179 CG ASP A 75-12.301 6.117 27.136 1.00 51.08 A C ATOM 180 OD1 ASP A 75-13.096 5.509 26.382 1.00 53.32 A O ATOM 181 OD2 ASP A 75-12.664 6.994 27.954 1.00 51.99 A O ATOM 182 C ASP A 75-9.709 3.518 26.820 1.00 45.56 A C ATOM 183 O ASP A 75-8.510 3.370 27.029 1.00 46.56 A O ATOM 184 N MET A 76-10.355 2.934 25.817 1.00 46.24 A N ATOM 185 CA MET A 76-9.702 2.035 24.876 1.00 46.67 A C ATOM 186 CB MET A 76-10.274 2.225 23.464 1.00 49.03 A C ATOM 187 CG MET A 76-10.517 3.666 23.045 1.00 51.71 A C ATOM 188 SD MET A 76-11.067 3.776 21.317 1. 00 54. 92 A S ATOM 189 CE MET A 76-12.657 2.877 21.382 1. 00 53. 96 A C ATOM 190 C MET A 76-8.181 2.128 24. 838 1.00 45.74 A C ATOM 191 O MET A 76-7.604 3.128 24.397 1. 00 46. 47 A O ATOM 192 N GLU A 77-7.540 1.069 25.318 1.00 42.10 A N ATOM 193 CA GLU A 77-6.091 1.004 25.335 1. 00 39. 51 A C ATOM 194 CB GLU A 77-5.564 1.240 26.761 1. 00 40. 15 A C ATOM 195 CG GLU A 77-5.909 2.601 27.350 1. 00 39. 87 A C ATOM 196 CD GLU A 77-4.928 3.693 26.958 1.00 41.20 A C ATOM 197 OE1 GLU A 77-4.250 3.551 25.920 1.00 41.53 A O ATOM 198 OE2 GLU A 77-4.845 4.708 27.686 1. 00 41. 98 A O ATOM 199 C GLU A 77-5.641-0. 371 24.844 1.00 37.01 A C ATOM 200 O GLU A 77-6.454-1. 270 24.609 1. 00 35. 43 A O ATOM 201 N TYR A 78-4.337-0. 510 24.671 1.00 33.48 A N ATOM 202 CA TYR A 78-3.752-1. 767 24.261 1. 00 31. 20 A C ATOM 203 CB TYR A 78-2.746-1. 560 23.128 1. 00 30. 26 A C ATOM 204 CG TYR A 78-3.374-1. 172 21.812 1.00 30.10 A C ATOM 205 CD1 TYR A 78-3.914 0.102 21.615 1. 00 29. 18 A C ATOM 206 CE1 TYR A 78-4.506 0.451 20.396 1. 00 28. 87 A C ATOM 207 CD2 TYR A 78-3.442-2. 088 20.762 1. 00 29. 64 A C ATOM 208 CE2 TYR A 78-4.030-1. 753 19.550 1. 00 29. 03 A C ATOM 209 CZ TYR A 78-4.558-0. 487 19.369 1. 00 28. 48 A C ATOM 210 OH TYR A 78-5.129-0. 172 18.157 1. 00 28. 05 A O ATOM 211 C TYR A 78-3.031-2. 223 25.509 1.00 29.40 A C ATOM 212 O TYR A 78-2.499-1. 397 26.251 1. 00 29. 13 A O ATOM 213 N PHE A 79-3.015-3. 525 25.760 1. 00 27. 59 A N ATOM 214 CA PHE A 79-2.338-4. 017 26.944 1. 00 25. 70 A C ATOM 215 CB PHE A 79-3.341-4. 539 27.967 1. 00 24. 34 A C ATOM 216 CG PHE A 79-4.487-3. 618 28.195 1.00 24.00 A C ATOM 217 CD1 PHE A 79-5.738-3. 905 27.662 1. 00 23. 61 A C ATOM 218 CD2 PHE A 79-4.309-2. 435 28.898 1. 00 22. 84 A C ATOM 219 CE1 PHE A 79-6.794-3. 021 27. 825 1. 00 24. 59 A C ATOM 220 CE2 PHE A 79-5.358-1. 547 29.065 1. 00 24. 18 A C ATOM 221 CZ PHE A 79-6.602-1. 836 28.528 1. 00 23. 88 A C ATOM 222 C PHE A 79-1.348-5. 109 26.627 1. 00 25. 87 A C ATOM 223 O PHE A 79-1.440-5. 785 25.601 1. 00 24. 72 A O ATOM 224 N GLY A 80-0.394-5. 258 27.535 1. 00 25. 37 A N ATOM 225 CA GLY A 80 0.624-6. 273 27.411 1.00 25.04 A C ATOM 226 C GLY A 80 0.771-6. 862 28.796 1. 00 24. 29 A C ATOM 227 0 GLY A 80 0.197-6. 347 29.752 1. 00 24. 78 A O ATOM 228 N THR A 81 1.547-7. 927 28.908 1.00 23.92 A N ATOM 229 CA THR A 81 1.762-8. 594 30. 178 1. 00 23. 26 A C ATOM 230 CB THR A 81 1.331-10. 068 30.081 1. 00 24. 00 A C ATOM 231 OG1 THR A 81-0. 086-10.127 29.893 1.00 27.36 A O ATOM 232 CG2 THR A 81 1.708-10. 829 31.337 1.00 24.06 A C ATOM 233 C THR A 81 3.227-8. 547 30.581 1. 00 22. 25 A C ATOM 234 O THR A 81 4.112-8. 612 29.730 1. 00 21. 17 A O ATOM 235 N ILE A 82 3.473-8. 423 31.883 1.00 21.29 A N ATOM 236 CA ILE A 82 4.832-8. 413 32.408 1.00 20.03 A C ATOM 237 CB ILE A 82 5.337-6. 981 32.738 1.00 20.43 A C ATOM 238 CG2 ILE A 82 5.135-6. 057 31.537 1.00 19. 64 A C ATOM 239 CG1 ILE A 82 4.601-6. 436 33.963 1. 00 18. 25 A C ATOM 240 CD1 ILE A 82 5.207-5. 194 34.521 1.00 16.22 A C ATOM 241 C ILE A 82 4.831-9. 222 33.694 1.00 19.85 A C ATOM 242 0 ILE A 82 3.776-9. 536 34.237 1.00 20.63 A O ATOM 243 N SER A 83 6.017-9. 553 34.181 1.00 20.89 A N ATOM 244 CA SER A 83 6.154-10. 314 35.413 1.00 21.08 A C ATOM 245 CB SER A 83 6.631-11. 731 35.113 1. 00 21. 63 A C ATOM 246 OG SER A 83 5.606-12. 459 34. 481 1.00 27.41 A O ATOM 247 C SER A 83 7.148-9. 650 36.347 1.00 20.21 A C ATOM 248 O SER A 83 8.121-9. 048 35.903 1. 00 21. 12 A O ATOM 249 N ILE A 84 6.902-9. 771 37.644 1.00 18.49 A N ATOM 250 CA ILE A 84 7.795-9. 191 38.630 1.00 17.61 A C ATOM 251 CB ILE A 84 7.188-7. 916 39.242 1.00 16.65 A C ATOM 252 CG2 ILE A 84 8.200-7. 253 40.169 1.00 14.83 A C ATOM 253 CG1 ILE A 84 6.751-6. 958 38.126 1.00 15.33 A C ATOM 254 CD1 ILE A 84 6.089-5. 689 38.637 1.00 10.96 A C ATOM 255 C ILE A 84 8.027-10. 188 39.751 1.00 18.65 A C ATOM 256 O ILE A 84 7.082-10. 820 40.221 1.00 18.90 A O ATOM 257 N GLY A 85 9.282-10. 338 40.169 1.00 19.02 A N ATOM 258 CA GLY A 85 9.590-11. 235 41.269 1.00 20.29 A C ATOM 259 C GLY A 85 9.872-12. 689 40.935 1.00 22.04 A C ATOM 260 0 GLY A 85 9.721-13. 129 39.798 1.00 22.58 A O ATOM 261 N SER A 86 10.287-13. 434 41.953 1.00 22.15 A N ATOM 262 CA SER A 86 10.608-14. 847 41.812 1.00 23.50 A C ATOM 263 CB SER A 86 12.118-15. 052 41.917 1.00 23.46 A C ATOM 264 OG SER A 86 12.791-14. 099 41.124 1.00 27.20 A O ATOM 265 C SER A 86 9.925-15. 599 42.941 1. 00 22. 10 A C ATOM 266 O SER A 86 10.256-15. 394 44.108 1.00 22.73 A O ATOM 267 N PRO A 87 8.948-16. 457 42.614 1. 00 21. 58 A N ATOM 268 CD PRO A 87 8.230-17. 274 43.608 1. 00 21. 27 A C ATOM 269 CA PRO A 87 8.456-16. 737 41.258 1. 00 21. 84 A C ATOM 270 CB PRO A 87 7.553-17. 949 41.468 1. 00 21. 06 A C ATOM 271 CG PRO A 87 7.002-17. 707 42. 840 1. 00 21. 58 A C ATOM 272 C PRO A 87 7.714-15. 547 40.637 1. 00 21. 60 A C ATOM 273 O PRO A 87 7.235-14. 666 41.347 1. 00 22. 43 A 0 ATOM 274 N PRO A 88 7.599-15. 518 39.300 1. 00 21. 46 A N ATOM 275 CD PRO A 88 8.017-16. 560 38.346 1. 00 20. 55 A C ATOM 276 CA PRO A 88 6.915-14. 422 38.601 1. 00 20. 92 A C ATOM 277 CB PRO A 88 7.020-14. 823 37.129 1. 00 20. 43 A C ATOM 278 CG PRO A 88 7.077-16. 309 37.183 1. 00 21. 38 A C ATOM 279 C PRO A 88 5.477-14. 138 39.006 1.00 20.56 A C ATOM 280 O PRO A 88 4.680-15. 049 39.201 1. 00 21. 06 A O ATOM 281 N GLN A 89 5.168-12. 852 39.140 1. 00 20. 07 A N ATOM 282 CA GLN A 89 3.827-12. 393 39.475 1. 00 19. 51 A C ATOM 283 CB GLN A 89 3.859-11. 518 40.740 1. 00 18. 08 A C ATOM 284 CG GLN A 89 4. 013-12. 347 42.032 1. 00 19. 56 A C ATOM 285 CD GLN A 89 4. 097-11. 519 43.318 1. 00 18. 03 A C ATOM 286 OE1 GLN A 89 3.279-10. 637 43.567 1.00 18.64 A O ATOM 287 NE2 GLN A 89 5.086-11. 822 44.143 1.00 17.15 A N ATOM 288 C GLN A 89 3.437-11. 595 38.241 1.00 19.28 A C ATOM 289 O GLN A 89 4.098-10. 617 37.911 1. 00 20. 15 A 0 ATOM 290 N ASN A 90 2.389-12. 026 37.543 1.00 19.27 A N ATOM 291 CA ASN A 90 1.968-11. 351 36.314 1. 00 20. 21 A C ATOM 292 CB ASN A 90 1.295-12. 344 35.362 1. 00 21. 63 A C ATOM 293 CG ASN A 90 2.188-13. 529 35.029 1.00 24.22 A C ATOM 294 OD1 ASN A 90 3.359-13. 364 34.679 1.00 22.89 A 0 ATOM 295 ND2 ASN A 90 1.636-14. 735 35.138 1.00 26.02 A N ATOM 296 C ASN A 90 1.061-10. 142 36.488 1.00 19.38 A C ATOM 297 O ASN A 90 0.238-10. 082 37.393 1.00 19.02 A O ATOM 298 N PHE A 91 1.229-9. 176 35.596 1. 00 18. 32 A N ATOM 299 CA PHE A 91 0.438-7. 966 35.621 1. 00 17. 33 A C ATOM 300 CB PHE A 91 1. 203-6. 859 36.344 1.00 15.81 A C ATOM 301 CG PHE A 91 1.474-7. 161 37.781 1.00 14.65 A C ATOM 302 CD1 PHE A 91 0.525-6. 869 38.759 1.00 13.61 A C ATOM 303 CD2 PHE A 91 2.658-7. 800 38.158 1.00 13.04 A C ATOM 304 CE1 PHE A 91 0.750-7. 215 40.100 1.00 12.86 A C ATOM 305 CE2 PHE A 91 2.889-8. 150 39.487 1.00 13.11 A C ATOM 306 CZ PHE A 91 1.927-7. 856 40.461 1.00 12.53 A C ATOM 307 C PHE A 91 0.144-7. 525 34.198 1.00 18.17 A C ATOM 308 O PHE A 91 0.973-7. 687 33.306 1. 00 18. 68 A O ATOM 309 N THR A 92-1.052-6. 990 33.992 1. 00 18. 58 A N ATOM 310 CA THR A 92-1.447-6. 469 32.692 1. 00 18. 47 A C ATOM 311 CB THR A 92-2.963-6. 619 32.459 1. 00 18. 74 A C ATOM 312 OG1 THR A 92-3.310-8. 011 32.451 1. 00 21. 04 A O ATOM 313 CG2 THR A 92-3.368-5. 983 31.130 1. 00 18. 24 A C ATOM 314 C THR A 92-1.114-4. 988 32.817 1. 00 18. 49 A C ATOM 315 O THR A 92-1.563-4. 326 33.758 1. 00 17. 37 A O ATOM 316 N VAL A 93-0.312-4. 474 31.894 1. 00 18. 39 A N ATOM 317 CA VAL A 93 0.075-3. 065 31.941 1. 00 18. 13 A C ATOM 318 CB VAL A 93 1.565-2. 879 32.361 1. 00 17. 01 A C ATOM 319 CG1 VAL A 93 1.821-3. 500 33.721 1. 00 16. 54 A C ATOM 320 CG2 VAL A 93 2.480-3. 487 31.313 1. 00 16. 64 A C ATOM 321 C VAL A 93-0.085-2. 373 30.601 1. 00 18. 36 A C ATOM 322 0 VAL A 93-0.234-3. 014 29.558 1.00 18.45 A 0 ATOM 323 N ILE A 94-0.044-1. 049 30.647 1.00 18.84 A N ATOM 324 CA ILE A 94-0.123-0. 236 29.449 1. 00 18. 75 A C ATOM 325 CB ILE A 94-1.064 0.954 29.645 1. 00 18. 28 A C ATOM 326 CG2 ILE A 94-1.041 1.825 28.407 1. 00 20. 15 A C ATOM 327 CG1 ILE A 94-2.483 0.462 29.945 1. 00 20. 02 A C ATOM 328 CD1 ILE A 94-3.463 1.581 30.319 1. 00 17. 15 A C ATOM 329 C ILE A 94 1.281 0.308 29.197 1. 00 18. 42 A C ATOM 330 0 ILE A 94 1.909 0.866 30.104 1. 00 17. 57 A O ATOM 331 N PHE A 95 1.788 0.126 27.983 1. 00 18. 12 A N ATOM 332 CA PHE A 95 3.108 0.651 27.651 1. 00 18. 31 A C ATOM 333 CB PHE A 95 3.752-0. 188 26.549 1. 00 17. 65 A C ATOM 334 CG PHE A 95 4.131-1. 562 27.014 1. 00 17. 21 A C ATOM 335 CD1 PHE A 95 3.185-2. 581 27.060 1. 00 17. 49 A C ATOM 336 CD2 PHE A 95 5.411-1. 815 27.503 1. 00 17. 64 A C ATOM 337 CE1 PHE A 95 3.504-3. 842 27.594 1. 00 16. 93 A C ATOM 338 CE2 PHE A 95 5.744-3. 065 28.039 1. 00 17. 93 A C ATOM 339 CZ PHE A 95 4. 783-4.082 28. 084 1. 00 17. 53 A C ATOM 340 C PHE A 95 2.853 2.091 27.244 1. 00 18. 51 A C ATOM 341 O PHE A 95 2.262 2.367 26. 206 1. 00 18. 48 A O ATOM 342 N ASP A 96 3.307 3.002 28.097 1. 00 18. 43 A N ATOM 343 CA ASP A 96 3.046 4.422 27.939 1. 00 18. 61 A C ATOM 344 CB ASP A 96 2.286 4.855 29.206 1. 00 19. 92 A C ATOM 345 CG ASP A 96 1.875 6.305 29.201 1. 00 21. 34 A C ATOM 346 OD1 ASP A 96 1.613 6.861 28.113 1. 00 21. 10 A O ATOM 347 OD2 ASP A 96 1.791 6.880 30.313 1. 00 21. 23 A O ATOM 348 C ASP A 96 4.264 5.306 27.676 1. 00 19. 22 A C ATOM 349 O ASP A 96 5.070 5.558 28.571 1. 00 18. 81 A O ATOM 350 N THR A 97 4.389 5.780 26.438 1. 00 18. 97 A N ATOM 351 CA THR A 97 5.498 6.652 26.075 1. 00 18. 57 A C ATOM 352 CB THR A 97 5.695 6.720 24.549 1.00 19.05 A C ATOM 353 OG1 THR A 97 4.482 7.171 23.931 1.00 19.34 A O ATOM 354 CG2 THR A 97 6.079 5.347 23.992 1.00 16.54 A C ATOM 355 C THR A 97 5.216 8.061 26.591 1.00 19.09 A C ATOM 356 0 THR A 97 6.010 8.979 26.377 1.00 18.31 A O ATOM 357 N GLY A 98 4.074 8.212 27.267 1.00 18.28 A N ATOM 358 CA GLY A 98 3.671 9. 490 27.826 1.00 16.76 A C ATOM 359 C GLY A 98 4.035 9.649 29.294 1.00 17.10 A C ATOM 360 0 GLY A 98 3.720 10.668 29.904 1.00 15.79 A O ATOM 361 N SER A 99 4.681 8.629 29.861 1.00 17.62 A N ATOM 362 CA SER A 99 5.131 8.646 31.252 1.00 17.42 A C ATOM 363 CB SER A 99 4.063 8.067 32.188 1. 00 18. 00 A C ATOM 364 OG SER A 99 3.848 6.689 31.954 1.00 19.97 A 0 ATOM 365 C SER A 99 6.407 7.813 31.312 1.00 18.32 A C ATOM 366 0 SER A 99 6.776 7.179 30.322 1.00 18.38 A O ATOM 367 N SER A 100 7.080 7.794 32.461 1.00 18.59 A N ATOM 368 CA SER A 100 8.334 7.053 32.570 1.00 17.79 A C ATOM 369 CB SER A 100 9.497 8.039 32.557 1.00 17.19 A C ATOM 370 OG SER A 100 9.425 8.869 31.415 1.00 18.32 A O ATOM 371 C SER A 100 8.495 6.116 33.765 1.00 18.67 A C ATOM 372 0 SER A 100 9.555 5.515 33.936 1. 00 19. 44 A 0 ATOM 373 N ASN A 101 7.472 5.994 34.602 1.00 18.62 A N ATOM 374 CA ASN A 101 7.575 5.099 35.749 1. 00 18. 28 A C ATOM 375 CB ASN A 101 7.002 5.734 37.023 1.00 18.79 A C ATOM 376 CG ASN A 101 7.787 6.949 37.490 1. 00 20. 60 A C ATOM 377 OD1 ASN A 101 7.535 8.064 37.055 1. 00 22. 76 A 0 ATOM 378 ND2 ASN A 101 8.746 6.731 38.382 1. 00 21. 99 A N ATOM 379 C ASN A 101 6.831 3.795 35.518 1. 00 18. 00 A C ATOM 380 O ASN A 101 5.910 3.711 34.700 1. 00 17. 09 A O ATOM 381 N LEU A 102 7.252 2.773 36.249 1. 00 17. 55 A N ATOM 382 CA LEU A 102 6.596 1.481 36.215 1.00 17.11 A C ATOM 383 CB LEU A 102 7.589 0.343 35.971 1. 00 15. 06 A C ATOM 384 CG LEU A 102 7.070-1. 072 36.283 1. 00 14. 00 A C ATOM 385 CD1 LEU A 102 5.782-1. 384 35.522 1.00 10.77 A C ATOM 386 CD2 LEU A 102 8.151-2. 074 35.920 1. 00 13. 72 A C ATOM 387 C LEU A 102 6.002 1.337 37.607 1.00 17.99 A C ATOM 388 0 LEU A 102 6.690 1.546 38.610 1. 00 17. 63 A O ATOM 389 N TRP A 103 4.719 1.017 37.673 1.00 18.59 A N ATOM 390 CA TRP A 103 4.078 0.831 38.960 1.00 18.63 A C ATOM 391 CB TRP A 103 3.523 2.157 39.511 1.00 17.76 A C ATOM 392 CG TRP A 103 2.359 2.722 38.735 1.00 19.44 A C ATOM 393 CD2 TRP A 103 0.980 2.322 38.832 1. 00 18. 94 A C ATOM 394 CE2 TRP A 103 0.256 3.087 37.889 1.00 18.15 A C ATOM 395 CE3 TRP A 103 0.290 1.389 39.623 1.00 18.66 A C ATOM 396 CD1 TRP A 103 2.407 3.690 37.768 1. 00 18. 57 A C ATOM 397 NE1 TRP A 103 1.149 3.912 37.257 1. 00 19. 24 A N ATOM 398 CZ2 TRP A 103-1. 127 2.949 37.712 1. 00 17. 85 A C ATOM 399 CZ3 TRP A 103-1. 087 1.251 39.449 1. 00 18. 33 A C ATOM 400 CH2 TRP A 103-1. 781 2.029 38.498 1. 00 18. 43 A C ATOM 401 C TRP A 103 2. 948-0. 161 38.796 1.00 18.78 A C ATOM 402 O TRP A 103 2.358-0. 268 37.721 1. 00 18. 32 A O ATOM 403 N VAL A 104 2.665-0. 893 39.867 1. 00 18. 04 A N ATOM 404 CA VAL A 104 1.586-1. 865 39.873 1. 00 18. 27 A C ATOM 405 CB VAL A 104 2.091-3. 320 39.640 1. 00 17. 81 A C ATOM 406 CG1 VAL A 104 2.583-3. 481 38.206 1. 00 16. 50 A C ATOM 407 CG2 VAL A 104 3.192-3. 658 40.624 1. 00 17. 96 A C ATOM 408 C VAL A 104 0.948-1. 765 41.243 1. 00 18. 39 A C ATOM 409 0 VAL A 104 1.552-1. 232 42.180 1. 00 19. 82 A 0 ATOM 410 N PRO A 105-0.284-2. 267 41.382 1. 00 17. 97 A N ATOM 411 CD PRO A 105-1.173-2. 831 40.352 1. 00 16. 65 A C ATOM 412 CA PRO A 105-0.963-2. 202 42.677 1. 00 17. 56 A C ATOM 413 CB PRO A 105-2.341-2. 794 42. 376 1. 00 17. 80 A C ATOM 414 CG PRO A 105-2.541-2. 491 40.913 1. 00 16. 69 A C ATOM 415 C PRO A 105-0.223-3. 004 43.737 1. 00 18. 58 A C ATOM 416 0 PRO A 105 0.315-4. 078 43.455 1. 00 18. 86 A O ATOM 417 N SER A 106-0.182-2. 471 44.953 1.00 18.85 A N ATOM 418 CA SER A 106 0.466-3. 170 46.048 1.00 18.79 A C ATOM 419 CB SER A 106 1.045-2. 183 47.066 1. 00 18. 87 A C ATOM 420 OG SER A 106 1.476-2. 873 48.235 1. 00 16. 77 A 0 ATOM 421 C SER A 106-0.577-4. 027 46.742 1.00 18.68 A C ATOM 422 0 SER A 106-1.759-3. 677 46.786 1. 00 17. 66 A 0 ATOM 423 N VAL A 107-0. 143-5.154 47.286 1. 00 19. 46 A N ATOM 424 CA VAL A 107-1. 060-6.016 48.008 1. 00 20. 47 A C ATOM 425 CB VAL A 107-0. 362-7.329 48.457 1. 00 20. 96 A C ATOM 426 CG1 VAL A 107 0.665-7. 039 49.548 1.00 19.80 A C ATOM 427 CG2 VAL A 107-1. 407-8.341 48.925 1. 00 21. 28 A C ATOM 428 C VAL A 107-1. 511-5.208 49.229 1.00 20.74 A C ATOM 429 O VAL A 107-2. 515-5.522 49.863 1. 00 21. 68 A O ATOM 430 N TYR A 108-0. 766-4.151 49.545 1. 00 20. 62 A N ATOM 431 CA TYR A 108-1. 113-3. 298 50.676 1. 00 20. 78 A C ATOM 432 CB TYR A 108 0.125-2. 594 51.234 1. 00 18. 74 A C ATOM 433 CG TYR A 108 1.015-3. 512 52.031 1.00 16.76 A C ATOM 434 CD1 TYR A 108 1.942-4. 332 51.399 1. 00 16. 57 A C ATOM 435 CE1 TYR A 108 2.766-5. 186 52.132 1. 00 17. 50 A C ATOM 436 CD2 TYR A 108 0.923-3. 567 53.426 1. 00 17. 66 A C ATOM 437 CE2 TYR A 108 1.737-4. 419 54.170 1. 00 16. 16 A C ATOM 438 CZ TYR A 108 2.658-5. 223 53.512 1. 00 17. 47 A C ATOM 439 OH TYR A 108 3.479-6. 053 54.228 1. 00 18. 91 A 0 ATOM 440 C TYR A 108-2. 186-2.271 50.350 1. 00 21. 31 A C ATOM 441 O TYR A 108-2. 634-1.548 51.240 1.00 20.68 A O ATOM 442 N CYS A 109-2. 582-2.192 49.078 1. 00 23. 00 A N ATOM 443 CA CYS A 109-3. 654-1.282 48.666 1. 00 24. 59 A C ATOM 444 C CYS A 109-4.929-2. 041 49.029 1. 00 24. 65 A C ATOM 445 O CYS A 109-5. 214-3.082 48.445 1. 00 25. 33 A O ATOM 446 CB CYS A 109-3.616-1. 006 47.147 1.00 25.46 A C ATOM 447 SG CYS A 109-5. 064-0.074 46.519 1. 00 28. 61 A S ATOM 448 N THR A 110-5. 680-1.534 50.002 1. 00 25. 31 A N ATOM 449 CA THR A 110-6.906-2. 198 50.441 1. 00 26. 94 A C ATOM 450 CB THR A 110-6.986-2. 274 51.989 1.00 28.52 A C ATOM 451 OG1 THR A 110-6.946-0. 950 52.542 1. 00 29. 31 A O ATOM 452 CG2 THR A 110-5.814-3. 084 52.543 1. 00 29. 24 A C ATOM 453 C THR A 110-8.164-1. 522 49.921 1.00 27.34 A C ATOM 454 O THR A 110-9.272-1. 814 50.371 1. 00 27. 15 A O ATOM 455 N SER A 111-7.994-0. 612 48.971 1. 00 27. 96 A N ATOM 456 CA SER A 111-9.133 0.073 48.383 1. 00 27. 86 A C ATOM 457 CB SER A 111-8.650 1.153 47.416 1. 00 28. 78 A C ATOM 458 OG SER A 111-9.716 1.627 46.614 1. 00 31. 10 A 0 ATOM 459 C SER A 111-9.971-0. 955 47.629 1. 00 27. 71 A C ATOM 460 O SER A 111-9. 439-1.930 47.100 1.00 26.10 A O ATOM 461 N PRO A 112-11.298-0. 762 47.587 1. 00 28. 23 A N ATOM 462 CD PRO A 112-12.090 0.259 48.300 1. 00 28. 77 A C ATOM 463 CA PRO A 112-12.171-1. 703 46.876 1. 00 27. 75 A C ATOM 464 CB PRO A 112-13. 551-1. 068 47.021 1. 00 28. 65 A C ATOM 465 CG PRO A 112-13.460-0. 387 48.375 1.00 28.99 A C ATOM 466 C PRO A 112-11.738-1. 806 45.417 1.00 27.64 A C ATOM 467 0 PRO A 112-11.816-2. 871 44.807 1. 00 27. 23 A 0 ATOM 468 N ALA A 113-11.260-0. 688 44.879 1. 00 26. 75 A N ATOM 469 CA ALA A 113-10.808-0. 613 43.496 1. 00 27. 06 A C ATOM 470 CB ALA A 113-10.509 0.833 43.137 1. 00 26. 13 A C ATOM 471 C ALA A 113-9.590-1. 489 43.181 1.00 27.96 A C ATOM 472 O ALA A 113-9.366-1. 854 42.022 1. 00 28. 34 A 0 ATOM 473 N CYS A 114-8.799-1. 818 44.199 1.00 27.46 A N ATOM 474 CA CYS A 114-7.615-2. 654 43.990 1. 00 28. 09 A C ATOM 475 C CYS A 114-7.929-4. 154 44.105 1.00 27.46 A C ATOM 476 O CYS A 114-7.186-4. 993 43.593 1. 00 26. 03 A 0 ATOM 477 CB CYS A 114-6. 518-2.303 45.010 1. 00 27. 16 A C ATOM 478 SG CYS A 114-5.468-0. 845 44. 665 1.00 30.19 A S ATOM 479 N LYS A 115-9.027-4. 486 44.776 1. 00 27. 89 A N ATOM 480 CA LYS A 115-9.401-5. 882 44.982 1. 00 29. 65 A C ATOM 481 CB LYS A 115-10.645-5. 970 45.870 1. 00 32. 09 A C ATOM 482 CG LYS A 115-10.373-5. 595 47.317 1. 00 36. 41 A C ATOM 483 CD LYS A 115-11.657-5. 270 48.073 1. 00 40. 28 A C ATOM 484 CE LYS A 115-11. 348-4.686 49.454 1.00 40.93 A C ATOM 485 NZ LYS A 115-12. 564-4.142 50.122 1.00 41.96 A N ATOM 486 C LYS A 115-9.617-6. 694 43.716 1. 00 28. 77 A C ATOM 487 O LYS A 115-9.457-7. 910 43.729 1. 00 29. 75 A O ATOM 488 N THR A 116-9. 967-6.033 42.621 1. 00 27. 94 A N ATOM 489 CA THR A 116-10. 202-6.738 41.367 1. 00 26. 99 A C ATOM 490 CB THR A 116-11. 314-6.049 40.558 1. 00 27. 13 A C ATOM 491 OG1 THR A 116-11. 000-4.657 40.412 1. 00 26. 39 A O ATOM 492 CG2 THR A 116-12. 661-6.195 41.267 1. 00 25. 71 A C ATOM 493 C THR A 116 -8. 956-6.851 40.484 1. 00 27. 23 A C ATOM 494 O THR A 116-9. 035-7.350 39.359 1. 00 28. 24 A O ATOM 495 N HIS A 117-7.808-6. 397 40.985 1. 00 25. 32 A N ATOM 496 CA HIS A 117-6.574-6. 454 40.204 1. 00 22. 98 A C ATOM 497 CB HIS A 117-5.934-5. 069 40.084 1. 00 21. 94 A C ATOM 498 CG HIS A 117-6.723-4. 096 39.275 1.00 19.85 A C ATOM 499 CD2 HIS A 117-6. 589-3.693 37.991 1.00 18.68 A C ATOM 500 ND1 HIS A 117-7. 793-3.398 39.788 1. 00 21. 04 A N ATOM 501 CE1 HIS A 117-8.285-2. 604 38.854 1. 00 20. 96 A C ATOM 502 NE2 HIS A 117-7.571-2. 763 37.754 1. 00 19. 61 A N ATOM 503 C HIS A 117-5.522-7. 359 40.806 1. 00 22. 57 A C ATOM 504 O HIS A 117-5.623-7. 768 41.959 1. 00 21. 20 A O ATOM 505 N SER A 118-4.501-7. 658 40.006 1. 00 22. 03 A N ATOM 506 CA SER A 118-3.372-8. 441 40.480 1. 00 21. 12 A C ATOM 507 CB SER A 118-2.472-8. 865 39.313 1. 00 21. 85 A C ATOM 508 OG SER A 118-3. 189-9.607 38.345 1. 00 23. 39 A O ATOM 509 C SER A 118-2.629-7. 421 41.350 1. 00 21. 15 A C ATOM 510 0 SER A 118-2. 449-6.266 40.943 1. 00 19. 07 A O ATOM 511 N ARG A 119-2.213-7. 832 42.541 1. 00 21. 31 A N ATOM 512 CA ARG A 119-1. 512-6.934 43.448 1. 00 22. 35 A C ATOM 513 CB ARG A 119-2.356-6. 707 44.708 1. 00 22. 58 A C ATOM 514 CG ARG A 119-3. 742-6.150 44.409 1. 00 24. 56 A C ATOM 515 CD ARG A 119-4. 514-5.792 45.669 1. 00 27. 79 A C ATOM 516 NE ARG A 119-4. 789-6.950 46.514 1. 00 31. 16 A N ATOM 517 CZ ARG A 119-5.575-7. 967 46.167 1. 00 33. 81 A C ATOM 518 NH1 ARG A 119-6. 181-7.984 44. 985 1. 00 34. 28 A N ATOM 519 NH2 ARG A 119-5. 746-8.978 47.004 1. 00 34. 67 A N ATOM 520 C ARG A 119-0. 162-7.528 43.809 1. 00 22. 93 A C ATOM 521 O ARG A 119-0. 075-8.699 44.184 1. 00 24.58 A O ATOM 522 N PHE A 120 0.895-6. 732 43.701 1. 00 21. 42 A N ATOM 523 CA PHE A 120 2.216-7. 252 44.006 1. 00 21. 08 A C ATOM 524 CB PHE A 120 3.309-6. 257 43.614 1. 00 18. 21 A C ATOM 525 CG PHE A 120 4.691-6. 838 43.693 1. 00 15. 75 A C ATOM 526 CD1 PHE A 120 5.047-7. 916 42.883 1. 00 15. 60 A C ATOM 527 CD2 PHE A 120 5.621-6. 347 44.607 1. 00 15. 17 A C ATOM 528 CE1 PHE A 120 6.316-8. 504 42.985 1. 00 13. 93 A C ATOM 529 CE2 PHE A 120 6.889-6. 925 44.719 1. 00 14. 72 A C ATOM 530 CZ PHE A 120 7.235-8. 007 43.906 1.00 13.43 A C ATOM 531 C PHE A 120 2.391-7. 634 45.471 1. 00 22. 62 A C ATOM 532 O PHE A 120 2.100-6. 851 46.386 1.00 21.89 A O ATOM 533 N GLN A 121 2.899-8. 843 45. 680 1. 00 23. 13 A N ATOM 534 CA GLN A 121 3.124-9. 368 47.019 1. 00 24. 57 A C ATOM 535 CB GLN A 121 2.348-10. 672 47.145 1. 00 26. 76 A C ATOM 536 CG GLN A 121 2.052-11. 141 48.536 1. 00 31. 33 A C ATOM 537 CD GLN A 121 0.861-12. 082 48.539 1.00 34.43 A C ATOM 538 OE1 GLN A 121 0.645-12. 823 47.575 1.00 34.94 A O ATOM 539 NE2 GLN A 121 0. 082-12.063 49.622 1.00 35.44 A N ATOM 540 C GLN A 121 4.633-9. 582 47.212 1. 00 24. 01 A C ATOM 541 O GLN A 121 5.178-10. 625 46.854 1. 00 24. 18 A 0 ATOM 542 N PRO A 122 5.322-8. 585 47.792 1. 00 24. 52 A N ATOM 543 CD PRO A 122 4.711-7. 392 48.406 1. 00 23. 81 A C ATOM 544 CA PRO A 122 6.768-8. 606 48.050 1. 00 24. 11 A C ATOM 545 CB PRO A 122 6.995-7. 325 48.862 1. 00 23. 93 A C ATOM 546 CG PRO A 122 5.869-6. 441 48.459 1. 00 23. 41 A C ATOM 547 C PRO A 122 7.295-9. 836 48.791 1. 00 23. 73 A C ATOM 548 O PRO A 122 8.357-10. 362 48.454 1. 00 23. 12 A O ATOM 549 N SER A 123 6.556-10. 284 49.802 1. 00 22. 90 A N ATOM 550 CA SER A 123 6.976-11. 428 50.607 1. 00 24. 11 A C ATOM 551 CB SER A 123 6.043-11. 598 51.810 1. 00 24. 23 A C ATOM 552 OG SER A 123 4.737-11. 970 51.396 1. 00 26. 25 A O ATOM 553 C SER A 123 7.051-12. 747 49.835 1. 00 24. 20 A C ATOM 554 O SER A 123 7.740-13. 676 50.253 1. 00 24. 39 A O ATOM 555 N GLN A 124 6.349-12. 831 48.712 1. 00 24. 61 A N ATOM 556 CA GLN A 124 6.363-14. 052 47.920 1. 00 25. 47 A C ATOM 557 CB GLN A 124 5.031-14. 217 47.188 1. 00 26. 88 A C ATOM 558 CG GLN A 124 3.856-14. 513 48.102 1. 00 30. 04 A C ATOM 559 CD GLN A 124 4.072-15. 760 48.943 1. 00 32. 69 A C ATOM 560 OE1 GLN A 124 4.395-16. 828 48.420 1.00 34.90 A O ATOM 561 NE2 GLN A 124 3.889-15. 632 50.250 1.00 34.02 A N ATOM 562 C GLN A 124 7.513-14. 080 46.916 1. 00 25. 01 A C ATOM 563 O GLN A 124 7.730-15. 085 46.242 1. 00 24. 91 A O ATOM 564 N SER A 125 8.251-12. 980 46.821 1. 00 23. 79 A N ATOM 565 CA SER A 125 9.370-12. 898 45.888 1. 00 24. 53 A C ATOM 566 CB SER A 125 9.254-11. 639 45.029 1.00 23.13 A C ATOM 567 OG SER A 125 10.477-11. 392 44.360 1.00 22.16 A O ATOM 568 C SER A 125 10.723-12. 894 46.585 1.00 24.71 A C ATOM 569 O SER A 125 11.050-11. 968 47.330 1. 00 26. 77 A O ATOM 570 N SER A 126 11.520-13. 918 46.318 1. 00 25. 20 A N ATOM 571 CA SER A 126 12.842-14. 038 46.925 1.00 26.36 A C ATOM 572 CB SER A 126 13.415-15. 428 46.633 1. 00 26. 29 A C ATOM 573 OG SER A 126 13.394-15. 706 45.240 1. 00 25. 11 A O ATOM 574 C SER A 126 13.842-12. 977 46.461 1. 00 27. 12 A C ATOM 575 0 SER A 126 14.818-12. 697 47.154 1. 00 28. 61 A O ATOM 576 N THR A 127 13.596-12. 380 45.298 1. 00 26. 95 A N ATOM 577 CA THR A 127 14.508-11. 380 44.746 1. 00 26. 12 A C ATOM 578 CB THR A 127 14.687-11. 616 43.241 1. 00 24. 91 A C ATOM 579 OG1 THR A 127 13.400-11. 792 42.630 1.00 25.23 A O ATOM 580 CG2 THR A 127 15.519-12. 862 43.008 1.00 24.07 A C ATOM 581 C THR A 127 14.115-9. 918 44.985 1.00 25.86 A C ATOM 582 O THR A 127 14.729-8. 997 44.439 1. 00 26. 39 A O ATOM 583 N TYR A 128 13.106-9. 709 45.817 1.00 24.62 A N ATOM 584 CA TYR A 128 12. 638-8.363 46.117 1. 00 24. 31 A C ATOM 585 CB TYR A 128 11.174-8. 411 46.558 1.00 22.37 A C ATOM 586 CG TYR A 128 10.639-7. 079 47.036 1. 00 22. 43 A C ATOM 587 CD1 TYR A 128 10.133-6. 142 46.133 1.00 21.45 A C ATOM 588 CE1 TYR A 128 9.649-4. 908 46.572 1. 00 22. 29 A C ATOM 589 CD2 TYR A 128 10.651-6. 749 48.395 1. 00 21. 12 A C ATOM 590 CE2 TYR A 128 10.174-5. 520 48.843 1. 00 21. 02 A C ATOM 591 CZ TYR A 128 9.672-4. 604 47.927 1. 00 21. 72 A C ATOM 592 OH TYR A 128 9.190-3. 391 48.362 1.00 21.72 A O ATOM 593 C TYR A 128 13.453-7. 667 47.205 1. 00 24. 04 A C ATOM 594 0 TYR A 128 13.928-8. 301 48.142 1. 00 23. 97 A O ATOM 595 N SER A 129 13.609-6. 355 47.065 1. 00 24. 68 A N ATOM 596 CA SER A 129 14.317-5. 544 48.050 1. 00 25. 55 A C ATOM 597 CB SER A 129 15.818-5. 477 47.745 1. 00 24. 94 A C ATOM 598 OG SER A 129 16.092-4. 602 46.666 1. 00 28. 67 A O ATOM 599 C SER A 129 13.705-4. 145 48.006 1. 00 25. 49 A C ATOM 600 0 SER A 129 13. 125-3. 743 46.996 1. 00 23. 98 A 0 ATOM 601 N GLN A 130 13.832-3. 413 49.105 1. 00 26. 65 A N ATOM 602 CA GLN A 130 13.285-2. 065 49.203 1. 00 28. 99 A C ATOM 603 CB GLN A 130 12.409-1. 968 50.448 1. 00 28. 57 A C ATOM 604 CG GLN A 130 11.005-1. 496 50.182 1. 00 31. 51 A C ATOM 605 CD GLN A 130 10.101-1. 675 51.384 1. 00 33. 17 A C ATOM 606 OE1 GLN A 130 10.411-1. 211 52.490 1. 00 32. 17 A O ATOM 607 NE2 GLN A 130 8.970-2. 349 51.177 1. 00 32. 52 A N ATOM 608 C GLN A 130 14.378-0. 992 49.262 1. 00 30. 56 A C ATOM 609 0 GLN A 130 15.172-0. 953 50.204 1. 00 30. 90 A O ATOM 610 N PRO A 131 14.430-0. 105 48.255 1. 00 31. 42 A N ATOM 611 CD PRO A 131 13.650-0. 124 47.005 1. 00 31. 36 A C ATOM 612 CA PRO A 131 15.440 0.962 48.224 1. 00 31. 93 A C ATOM 613 CB PRO A 131 15.136 1.689 46.914 1. 00 31. 99 A C ATOM 614 CG PRO A 131 14.563 0.604 46.051 1. 00 32. 24 A C ATOM 615 C PRO A 131 15.310 1.885 49.435 1. 00 32. 35 A C ATOM 616 O PRO A 131 16.293 2.454 49.908 1. 00 32. 88 A o ATOM 617 N GLY A 132 14.085 2.038 49.924 1. 00 32. 71 A N ATOM 618 CA GLY A 132 13.855 2.885 51.079 1. 00 34. 14 A C ATOM 619 C GLY A 132 13.001 4.109 50.809 1. 00 34. 75 A C ATOM 620 O GLY A 132 12.329 4.614 51.711 1.00 36.26 A O ATOM 621 N GLN A 133 13.018 4.586 49.571 1.00 34.28 A N ATOM 622 CA GLN A 133 12.247 5.765 49.199 1. 00 34. 58 A C ATOM 623 CB GLN A 133 12.889 6.440 47.981 1.00 36.14 A C ATOM 624 CG GLN A 133 13.096 5.508 46.800 1.00 40.45 A C ATOM 625 CD GLN A 133 14.566 5.319 46.434 1.00 43.33 A C ATOM 626 OE1 GLN A 133 15.412 5.053 47.299 1. 00 44. 38 A O ATOM 627 NE2 GLN A 133 14.876 5.445 45.141 1. 00 43. 80 A N ATOM 628 C GLN A 133 10.789 5.442 48.895 1. 00 33. 32 A C ATOM 629 O GLN A 133 10.467 4.343 48.452 1. 00 34. 47 A O ATOM 630 N SER A 134 9.901 6.393 49.156 1. 00 31. 22 A N ATOM 631 CA SER A 134 8.490 6.195 48.851 1. 00 30. 59 A C ATOM 632 CB SER A 134 7.601 6.765 49.963 1. 00 30. 74 A C ATOM 633 OG SER A 134 7.695 8.174 50.034 1. 00 32. 32 A O ATOM 634 C SER A 134 8. 253 6.935 47.531 1.00 29.44 A C ATOM 635 O SER A 134 9.190 7.512 46.969 1. 00 27. 97 A O ATOM 636 N PHE A 135 7.025 6.926 47.024 1.00 28.34 A N ATOM 637 CA PHE A 135 6.775 7.609 45.764 1. 00 27. 67 A C ATOM 638 CB PHE A 135 7.045 6.660 44.597 1.00 29.01 A C ATOM 639 CG PHE A 135 5.864 5.828 44.204 1.00 29.26 A C ATOM 640 CD1 PHE A 135 4.942 6.304 43.271 1.00 30.60 A C ATOM 641 CD2 PHE A 135 5.651 4.588 44.784 1. 00 29. 31 A C ATOM 642 CE1 PHE A 135 3.824 5.557 42.924 1. 00 29. 95 A C ATOM 643 CE2 PHE A 135 4.534 3.828 44.446 1. 00 30. 32 A C ATOM 644 CZ PHE A 135 3.618 4.316 43.514 1. 00 30. 67 A C ATOM 645 C PHE A 135 5.385 8.193 45.619 1. 00 27. 10 A C ATOM 646 O PHE A 135 4.460 7.831 46.336 1. 00 27. 05 A O ATOM 647 N SER A 136 5.252 9.097 44.658 1. 00 27. 76 A N ATOM 648 CA SER A 136 3.983 9.746 44.377 1. 00 27. 51 A C ATOM 649 CB SER A 136 3.785 10.935 45.315 1. 00 26. 46 A C ATOM 650 OG SER A 136 2.459 11.415 45.248 1. 00 27. 40 A O ATOM 651 C SER A 136 4.013 10.216 42.930 1. 00 27. 11 A C ATOM 652 O SER A 136 4.938 10.917 42.519 1. 00 27. 92 A O ATOM 653 N ILE A 137 3.013 9.822 42. 150 1. 00 26. 89 A N ATOM 654 CA ILE A 137 2.965 10.224 40. 748 1. 00 26. 53 A C ATOM 655 CB ILE A 137 3.131 9.013 39.811 1. 00 27. 58 A C ATOM 656 CG2 ILE A 137 4.452 8.333 40.078 1. 00 28. 72 A C ATOM 657 CG1 ILE A 137 2.003 8.015 40. 032 1. 00 27. 62 A C ATOM 658 CD1 ILE A 137 2.109 6.802 39.145 1. 00 31. 13 A C ATOM 659 C ILE A 137 1.675 10.943 40.397 1. 00 25. 46 A C ATOM 660 0 ILE A 137 0.638 10.729 41.022 1. 00 25. 42 A O ATOM 661 N GLN A 138 1.751 11.790 39.381 1.00 25.36 A N ATOM 662 CA GLN A 138 0.611 12.577 38.934 1.00 25.81 A C ATOM 663 CB GLN A 138 0.822 14.053 39.307 1.00 27.14 A C ATOM 664 CG GLN A 138-0. 144 14.596 40.351 1.00 33.02 A C ATOM 665 CD GLN A 138 -1. 498 15.005 39.768 1.00 35.12 A C ATOM 666 OE1 GLN A 138-2.167 14.220 39.093 1.00 36.72 A O ATOM 667 NE2 GLN A 138-1.904 16.239 40.036 1.00 37.04 A N ATOM 668 C GLN A 138 0.430 12.453 37.423 1.00 24.77 A C ATOM 669 O GLN A 138 1.382 12.590 36.652 1.00 22.67 A O ATOM 670 N TYR A 139-0. 800 12.185 37.008 1. 00 23. 66 A N ATOM 671 CA TYR A 139-1. 114 12.067 35.599 1. 00 23. 51 A C ATOM 672 CB TYR A 139 -1. 794 10.724 35.321 1. 00 22. 80 A C ATOM 673 CG TYR A 139-0. 850 9.548 35.457 1. 00 21. 74 A C ATOM 674 CD1 TYR A 139 0.243 9.409 34.600 1.00 21.15 A C ATOM 675 CE1 TYR A 139 1.128 8.341 34.725 1.00 20.35 A C ATOM 676 CD2 TYR A 139-1. 036 8.584 36.448 1.00 21.82 A C ATOM 677 CE2 TYR A 139-0. 152 7.506 36.582 1. 00 21. 39 A C ATOM 678 CZ TYR A 139 0.925 7.396 35.716 1.00 19.83 A C ATOM 679 OH TYR A 139 1.812 6.356 35.849 1. 00 18. 69 A O ATOM 680 C TYR A 139-2. 008 13.231 35.206 1. 00 24. 40 A C ATOM 681 O TYR A 139-2. 593 13.245 34.122 1.00 25.66 A O ATOM 682 N GLY A 140-2. 116 14.203 36.109 1. 00 25. 36 A N ATOM 683 CA GLY A 140-2. 909 15.389 35.841 1. 00 26. 11 A C ATOM 684 C GLY A 140-4. 269 15.477 36.500 1.00 27.31 A C ATOM 685 O GLY A 140-4. 893 16.541 36.485 1.00 27.89 A 0 ATOM 686 N THR A 141-4. 739 14.380 37.087 1. 00 27. 64 A N ATOM 687 CA THR A 141-6. 050 14.388 37.721 1.00 26. 80 A C ATOM 688 CB THR A 141-7. 093 13.682 36.826 1.00 28.49 A C ATOM 689 OG1 THR A 141-6. 785 12.282 36.731 1. 00 27. 54 A O ATOM 690 CG2 THR A 141-7. 089 14.301 35.422 1.00 27.29 A C ATOM 691 C THR A 141-6. 059 13.736 39.096 1.00 26.68 A C ATOM 692 O THR A 141 -7. 048 13.117 39.495 1. 00 26. 74 A 0 ATOM 693 N GLY A 142-4. 962 13.882 39.826 1.00 26. 11 A N ATOM 694 CA GLY A 142-4. 888 13.289 41.147 1. 00 26. 29 A C ATOM 695 C GLY A 142-3. 629 12.473 41. 332 1.00 26. 10 A C ATOM 696 O GLY A 142-3. 138 11.855 40.392 1. 00 25. 94 A 0 ATOM 697 N SER A 143-3.110 12.459 42.553 1. 00 26. 18 A N ATOM 698 CA SER A 143-1.890 11.727 42.837 1. 00 26. 52 A C ATOM 699 CB SER A 143-1.087 12.442 43.927 1. 00 27.88 A C ATOM 700 OG SER A 143-1.828 12.514 45.131 1. 00 31. 19 A 0 ATOM 701 C SER A 143-2.119 10.281 43.244 1. 00 25. 78 A C ATOM 702 0 SER A 143-3.158 9.918 43.793 1.00 25. 79 A O ATOM 703 N LEU A 144 -1. 114 9.466 42.957 1. 00 25. 12 A N ATOM 704 CA LEU A 144-1.118 8.048 43.263 1. 00 24. 23 A C ATOM 705 CB LEU A 144-1.062 7.266 41.957 1. 00 24. 50 A C ATOM 706 CG LEU A 144-1.571 5.837 41.937 1. 00 24. 56 A C ATOM 707 CD1 LEU A 144-3.023 5.817 42.381 1. 00 24. 59 A C ATOM 708 CD2 LEU A 144-1. 427 5.286 40.525 1. 00 23. 60 A C ATOM 709 C LEU A 144 0.173 7.854 44.061 1. 00 23. 75 A C ATOM 710 O LEU A 144 1.252 8.205 43.578 1. 00 23. 44 A O ATOM 711 N SER A 145 0.073 7.310 45.271 1. 00 21. 73 A N ATOM 712 CA SER A 145 1.259 7.147 46.102 1. 00 21. 03 A C ATOM 713 CB SER A 145 1. 214 8.140 47.266 1. 00 21. 56 A C ATOM 714 OG SER A 145 1.061 9.462 46.787 1. 00 21. 96 A O ATOM 715 C SER A 145 1.475 5.749 46.654 1. 00 20. 22 A C ATOM 716 O SER A 145 0.541 4.950 46.757 1. 00 20. 37 A O ATOM 717 N GLY A 146 2.725 5.476 47.014 1.00 17.81 A N ATOM 718 CA GLY A 146 3.091 4.186 47.564 1. 00 17. 25 A C ATOM 719 C GLY A 146 4.574 4.195 47.882 1. 00 17. 79 A C ATOM 720 O GLY A 146 5.146 5.252 48.174 1.00 16.62 A O ATOM 721 N ILE A 147 5.206 3.027 47.850 1. 00 17. 71 A N ATOM 722 CA ILE A 147 6.633 2.976 48.111 1. 00 18. 46 A C ATOM 723 CB ILE A 147 6.982 2.135 49.393 1. 00 20. 88 A C ATOM 724 CG2 ILE A 147 6.126 2.581 50.575 1. 00 20. 94 A C ATOM 725 CG1 ILE A 147 6.776 0.647 49.146 1. 00 22. 59 A C ATOM 726 CD1 ILE A 147 8.012-0. 054 48.642 1. 00 24. 57 A C ATOM 727 C ILE A 147 7.303 2.388 46.881 1. 00 18. 10 A C ATOM 728 O ILE A 147 6.640 1.805 46.015 1. 00 16. 81 A O ATOM 729 N ILE A 148 8.617 2.564 46.799 1. 00 18. 22 A N ATOM 730 CA ILE A 148 9.395 2.061 45.677 1.00 16.15 A C ATOM 731 CB ILE A 148 10.553 3.026 45.321 1.00 16.06 A C ATOM 732 CG2 ILE A 148 11.448 2.401 44.263 1. 00 17. 03 A C ATOM 733 CG1 ILE A 148 9.992 4.363 44.828 1. 00 17. 21 A C ATOM 734 CD1 ILE A 148 9.217 4.275 43.512 1. 00 16. 93 A C ATOM 735 C ILE A 148 9.992 0.711 46.025 1. 00 16. 17 A C ATOM 736 0 ILE A 148 10.504 0.511 47.130 1.00 15.23 A O ATOM 737 N GLY A 149 9.921-0. 213 45.072 1.00 16.38 A N ATOM 738 CA GLY A 149 10.479-1. 534 45.271 1. 00 15. 87 A C ATOM 739 C GLY A 149 11.441-1. 868 44.148 1.00 16.39 A C ATOM 740 O GLY A 149 11.456-1. 197 43.111 1. 00 15. 70 A O ATOM 741 N ALA A 150 12.251-2. 902 44.357 1. 00 16. 57 A N ATOM 742 CA ALA A 150 13.214-3. 349 43.363 1. 00 16. 67 A C ATOM 743 CB ALA A 150 14.625-2. 958 43.777 1. 00 16. 93 A C ATOM 744 C ALA A 150 13.101-4. 860 43.254 1. 00 18. 55 A C ATOM 745 O ALA A 150 12.967-5. 560 44.267 1. 00 19. 05 A 0 ATOM 746 N ASP A 151 13.160-5. 361 42.026 1. 00 19. 29 A N ATOM 747 CA ASP A 151 13.044-6. 792 41.784 1. 00 21. 35 A C ATOM 748 CB ASP A 151 11.636-7. 272 42.167 1.00 21.69 A C ATOM 749 CG ASP A 151 11.604-8. 734 42.589 1. 00 23. 80 A C ATOM 750 OD1 ASP A 151 12.261-9. 569 41.928 1. 00 24. 05 A O ATOM 751 OD2 ASP A 151 10.906-9. 047 43.579 1. 00 22. 98 A O ATOM 752 C ASP A 151 13.275-7. 025 40.295 1.00 21.27 A C ATOM 753 0 ASP A 151 13.480-6. 076 39.540 1. 00 21. 18 A O ATOM 754 N GLN A 152 13.232-8. 283 39.877 1. 00 21. 73 A N ATOM 755 CA GLN A 152 13.428-8. 615 38.473 1. 00 22. 09 A C ATOM 756 CB GLN A 152 13.933-10. 052 38.323 1. 00 23. 20 A C ATOM 757 CG GLN A 152 12.992-11. 110 38.863 1.00 24.69 A C ATOM 758 CD GLN A 152 13.578-12. 504 38.770 1. 00 26. 04 A C ATOM 759 OE1 GLN A 152 14.622-12. 793 39.364 1. 00 27. 79 A O ATOM 760 NE2 GLN A 152 12.912-13. 376 38.025 1.00 26.10 A N ATOM 761 C GLN A 152 12.111-8. 452 37.740 1. 00 21. 73 A C ATOM 762 0 GLN A 152 11.078-8. 972 38.170 1. 00 21. 80 A O ATOM 763 N VAL A 153 12.155-7. 712 36.638 1.00 21.10 A N ATOM 764 CA VAL A 153 10.977-7. 456 35.823 1. 00 20. 71 A C ATOM 765 CB VAL A 153 10.732-5. 931 35.670 1. 00 19. 80 A C ATOM 766 CG1 VAL A 153 9.568-5. 675 34.728 1. 00 17. 41 A C ATOM 767 CG2 VAL A 153 10.451-5. 314 37.043 1. 00 18. 32 A C ATOM 768 C VAL A 153 11. 211-8.072 34.457 1. 00 22. 12 A C ATOM 769 O VAL A 153 12.237-7. 803 33.816 1. 00 22. 79 A O ATOM 770 N SER A 154 10.264-8. 901 34.020 1. 00 22. 17 A N ATOM 771 CA SER A 154 10.362-9. 576 32.732 1. 00 22. 83 A C ATOM 772 CB SER A 154 10.193-11. 083 32.902 1. 00 22. 10 A C ATOM 773 OG SER A 154 11.216-11. 611 33.714 1. 00 25. 37 A O ATOM 774 C SER A 154 9.339-9. 084 31.723 1. 00 24. 44 A C ATOM 775 0 SER A 154 8.155-8. 925 32.034 1. 00 24. 06 A O ATOM 776 N VAL A 155 9.819-8. 858 30.507 1. 00 25. 31 A N ATOM 777 CA VAL A 155 9.001-8. 395 29.403 1. 00 27. 61 A C ATOM 778 CB VAL A 155 9.337-6. 941 29.031 1. 00 27. 44 A C ATOM 779 CG1 VAL A 155 8.385-6. 450 27.960 1. 00 29. 12 A C ATOM 780 CG2 VAL A 155 9.259-6. 065 30.255 1. 00 27. 95 A C ATOM 781 C VAL A 155 9.331-9. 280 28.211 1. 00 28. 52 A C ATOM 782 O VAL A 155 10.335-9. 065 27.535 1. 00 29. 37 A O ATOM 783 N GLU A 156 8.490-10. 283 27.983 1. 00 30. 31 A N ATOM 784 CA GLU A 156 8.632-11. 248 26.887 1. 00 32. 11 A C ATOM 785 CB GLU A 156 7.682-10. 881 25.744 1. 00 35. 46 A C ATOM 786 CG GLU A 156 7.217-12. 083 24.928 1.00 41.85 A C ATOM 787 CD GLU A 156 6.212-12. 943 25.681 1.00 44.68 A C ATOM 788 OE1 GLU A 156 5.083-12. 461 25.914 1.00 45.95 A O ATOM 789 OE2 GLU A 156 6.551-14. 094 26.048 1.00 47.04 A O ATOM 790 C GLU A 156 10. 032-11. 450 26. 305 1. 00 31. 02 A C ATOM 791 O GLU A 156 10.399-10. 833 25. 289 1. 00 31. 54 A O ATOM 792 N GLY A 157 10.807-12. 325 26.934 1. 00 28. 19 A N ATOM 793 CA GLY A 157 12.141-12. 604 26.431 1. 00 25. 57 A c ATOM 794 C GLY A 157 13.267-11. 935 27.189 1. 00 23. 66 A c ATOM 795 0 GLY A 157 14.362-12. 473 27.284 1. 00 22. 89 A o ATOM 796 N LEU A 158 13.002-10. 754 27.729 1. 00 22. 84 A N ATOM 797 CA LEU A 158 14.018-10. 027 28.465 1. 00 22. 85 A C ATOM 798 CB LEU A 158 14.163-8. 614 27.891 1.00 22.07 A C ATOM 799 CG LEU A 158 14.536-8. 517 26.412 1.00 20.96 A C ATOM 800 CD1 LEU A 158 14.560-7. 060 25.994 1.00 20.51 A C ATOM 801 CD2 LEU A 158 15.891-9. 173 26.177 1.00 18.81 A C ATOM 802 C LEU A 158 13.684-9. 940 29.946 1. 00 22. 52 A C ATOM 803 0 LEU A 158 12.522-9. 901 30.327 1. 00 24. 30 A O ATOM 804 N THR A 159 14.714-9. 922 30.778 1. 00 21. 54 A N ATOM 805 CA THR A 159 14.528-9. 803 32.211 1. 00 20. 49 A C ATOM 806 CB THR A 159 14.735-11. 152 32.944 1. 00 21. 16 A C ATOM 807 OG1 THR A 159 13.689-12. 062 32.573 1.00 22.06 A O ATOM 808 CG2 THR A 159 14.700-10. 946 34.460 1.00 19.10 A C ATOM 809 C THR A 159 15.518-8. 785 32.754 1.00 20.18 A C ATOM 810 O THR A 159 16. 734-8.966 32.658 1.00 18.91 A 0 ATOM 811 N VAL A 160 14.978-7. 705 33.309 1. 00 20. 10 A N ATOM 812 CA VAL A 160 15.785-6. 642 33.888 1.00 20.65 A C ATOM 813 CB VAL A 160 15.084-5. 276 33.739 1.00 21.57 A C ATOM 814 CG1 VAL A 160 15.934-4. 184 34.360 1.00 23.70 A C ATOM 815 CG2 VAL A 160 14.807-4. 986 32.273 1.00 22.18 A C ATOM 816 C VAL A 160 15.928-6. 941 35.368 1. 00 20. 69 A C ATOM 817 O VAL A 160 14.925-7. 138 36.052 1.00 20.90 A O ATOM 818 N VAL A 161 17.158-6. 981 35.872 1.00 21.21 A N ATOM 819 CA VAL A 161 17.358-7. 251 37.292 1.00 20.51 A C ATOM 820 CB VAL A 161 18.598-8. 147 37.547 1.00 21.25 A C ATOM 821 CG1 VAL A 161 18.531-9. 395 36.671 1.00 18.87 A C ATOM 822 CG2 VAL A 161 19.877-7. 360 37.300 1.00 21.94 A C ATOM 823 C VAL A 161 17.541-5. 941 38.041 1.00 20.69 A C ATOM 824 O VAL A 161 18.112-4. 985 37.512 1.00 21.57 A 0 ATOM 825 N GLY A 162 17.036-5. 891 39.268 1. 00 20. 29 A N ATOM 826 CA GLY A 162 17.168-4. 690 40.068 1.00 19.50 A C ATOM 827 C GLY A 162 16.300-3. 530 39.620 1.00 19.64 A C ATOM 828 0 GLY A 162 16.486-2. 404 40.086 1. 00 20. 58 A O ATOM 829 N GLN A 163 15.352-3. 783 38.725 1.00 18.41 A N ATOM 830 CA GLN A 163 14.474-2. 716 38.260 1.00 18.33 A C ATOM 831 CB GLN A 163 13.525-3. 231 37.181 1.00 17.90 A C ATOM 832 CG GLN A 163 12.460-2. 223 36.760 1.00 15.96 A C ATOM 833 CD GLN A 163 13.025-1. 079 35.946 1.00 17.25 A C ATOM 834 OE1 GLN A 163 13.701-1. 300 34.935 1.00 17.76 A O ATOM 835 NE2 GLN A 163 12. 744 0.152 36.369 1.00 13.19 A N ATOM 836 C GLN A 163 13.647-2. 177 39.424 1. 00 19. 49 A C ATOM 837 O GLN A 163 13.084-2. 949 40.205 1. 00 19. 99 A O ATOM 838 N GLN A 164 13.581-0. 854 39.543 1. 00 18. 66 A N ATOM 839 CA GLN A 164 12.794-0. 232 40.600 1. 00 18. 49 A C ATOM 840 CB GLN A 164 13.493 1.008 41.168 1. 00 18. 54 A C ATOM 841 CG GLN A 164 14.854 0.732 41.779 1. 00 20. 48 A C ATOM 842 CD GLN A 164 15.393 1.913 42.568 1. 00 22. 09 A C ATOM 843 OE1 GLN A 164 15.186 3.071 42.200 1.00 23.13 A 0 ATOM 844 NE2 GLN A 164 16.099 1.625 43.652 1. 00 23. 25 A N ATOM 845 C GLN A 164 11.442 0.158 40.014 1.00 17.95 A C ATOM 846 O GLN A 164 11.339 0.543 38.846 1.00 16.64 A O ATOM 847 N PHE A 165 10.407 0.050 40.833 1.00 16.79 A N ATOM 848 CA PHE A 165 9.066 0.365 40.396 1. 00 16. 81 A C ATOM 849 CB PHE A 165 8.431-0. 871 39.747 1.00 16.05 A C ATOM 850 CG PHE A 165 8.430-2. 084 40.639 1. 00 16. 37 A C ATOM 851 CD1 PHE A 165 9. 586-2. 846 40.801 1. 00 16. 84 A C ATOM 852 CD2 PHE A 165 7.288-2. 438 41.356 1.00 16.97 A C ATOM 853 CE1 PHE A 165 9.608-3. 939 41.664 1.00 15.85 A C ATOM 854 CE2 PHE A 165 7.297-3. 532 42.227 1. 00 16. 21 A C ATOM 855 CZ PHE A 165 8.460-4. 282 42.379 1.00 17.38 A C ATOM 856 C PHE A 165 8.241 0.777 41.605 1.00 17.40 A C ATOM 857 0 PHE A 165 8.644 0.563 42.748 1.00 17.72 A O ATOM 858 N GLY A 166 7.077 1.354 41.346 1.00 17.66 A N ATOM 859 CA GLY A 166 6.219 1.759 42.437 1.00 18.67 A C ATOM 860 C GLY A 166 5.195 0.696 42.796 1.00 19.28 A C ATOM 861 O GLY A 166 4.714-0. 051 41.938 1.00 18.84 A 0 ATOM 862 N GLU A 167 4.899 0.606 44.086 1.00 20.17 A N ATOM 863 CA GLU A 167 3.895-0. 315 44. 613 1. 00 21. 41 A C ATOM 864 CB GLU A 167 4.500-1. 178 45.728 1.00 22.05 A C ATOM 865 CG GLU A 167 5.665-2. 070 45.253 1. 00 20. 92 A C ATOM 866 CD GLU A 167 6.433-2. 720 46.406 1.00 22.61 A C ATOM 867 OE1 GLU A 167 5. 828-3. 496 47.183 1. 00 20. 29 A 0 ATOM 868 OE2 GLU A 167 7.650-2. 454 46.533 1. 00 22. 17 A 0 ATOM 869 C GLU A 167 2.852 0.662 45.163 1.00 21. 17 A C ATOM 870 O GLU A 167 3.009 1.192 46.260 1.00 21.69 A 0 ATOM 871 N SER A 168 1.807 0.923 44.380 1. 00 21. 17 A N ATOM 872 CA SER A 168 0.790 1.892 44.776 1. 00 22. 04 A C ATOM 873 CB SER A 168-0.024 2.348 43.562 1. 00 22. 73 A C ATOM 874 OG SER A 168-0.844 1.299 43.087 1.00 26.64 A 0 ATOM 875 C SER A 168-0.140 1.392 45.861 1. 00 21. 61 A C ATOM 876 O SER A 168-0.604 0.252 45.828 1. 00 21. 47 A 0 ATOM 877 N VAL A 169-0. 420 2.274 46.811 1. 00 21. 31 A N ATOM 878 CA VAL A 169-1. 261 1.952 47.947 1. 00 22. 07 A C ATOM 879 CB VAL A 169-0. 458 2.095 49.255 1.00 22.08 A C ATOM 880 CG1 VAL A 169-1. 314 1.691 50.437 1.00 22.84 A C ATOM 881 CG2 VAL A 169 0.801 1.251 49.181 1.00 21.30 A C ATOM 882 C VAL A 169-2. 510 2.819 48.055 1.00 22.39 A C ATOM 883 O VAL A 169-3.590 2.315 48.337 1.00 23.71 A O ATOM 884 N THR A 170-2. 363 4.119 47.830 1. 00 22. 60 A N ATOM 885 CA THR A 170-3. 493 5.037 47.937 1.00 22.45 A C ATOM 886 CB THR A 170-3. 026 6.512 47.848 1.00 21.96 A C ATOM 887 OG1 THR A 170-2. 461 6.775 46.556 1.00 20.37 A O ATOM 888 CG2 THR A 170-1. 978 6.787 48.926 1.00 20.95 A C ATOM 889 C THR A 170-4. 604 4.801 46.917 1.00 23.21 A C ATOM 890 O THR A 170 -4. 402 4.127 45.898 1. 00 22. 17 A 0 ATOM 891 N GLU A 171-5. 777 5.363 47.218 1.00 23.12 A N ATOM 892 CA GLU A 171-6. 971 5.243 46.382 1. 00 23. 04 A C ATOM 893 CB GLU A 171-8. 063 6.171 46.920 1.00 24.19 A C ATOM 894 CG GLU A 171-9. 342 6.188 46.103 1. 00 27. 06 A C ATOM 895 CD GLU A 171-9. 955 4.809 45.929 1. 00 28. 65 A C ATOM 896 OE1 GLU A 171-10. 125 4.096 46.945 1.00 29.22 A 0 ATOM 897 OE2 GLU A 171-10. 274 4.447 44.775 1.00 28.91 A 0 ATOM 898 C GLU A 171-6. 670 5.556 44.919 1.00 22.24 A C ATOM 899 O GLU A 171-6. 302 6.676 44.576 1. 00 21. 30 A O ATOM 900 N PRO A 172-6.826 4.555 44.037 1.00 22.62 A N ATOM 901 CD PRO A 172-7.207 3.165 44.354 1. 00 22. 11 A C ATOM 902 CA PRO A 172-6.567 4.696 42.602 1.00 22.10 A C ATOM 903 CB PRO A 172-6.268 3.268 42.183 1. 00 20. 68 A C ATOM 904 CG PRO A 172-7. 281 2.513 42.974 1. 00 20. 69 A C ATOM 905 C PRO A 172-7.733 5.287 41.827 1.00 22.52 A C ATOM 906 0 PRO A 172-7.582 5.677 40.672 1. 00 22. 16 A O ATOM 907 N GLY A 173-8. 895 5.348 42.469 1. 00 24. 58 A N ATOM 908 CA GLY A 173-10. 078 5.885 41.822 1.00 25.95 A C ATOM 909 C GLY A 173-11. 120 4.796 41.669 1. 00 27. 60 A C ATOM 910 O GLY A 173-10. 796 3.679 41.258 1. 00 26. 70 A 0 ATOM 911 N GLN A 174-12. 371 5.119 41.991 1. 00 28. 96 A N ATOM 912 CA GLN A 174-13.463 4.156 41.906 1.00 30.80 A C ATOM 913 CB GLN A 174-14.808 4.846 42.154 1. 00 34. 09 A C ATOM 914 CG GLN A 174-15. 951 3.861 42.398 1.00 38.86 A C ATOM 915 CD GLN A 174-17.326 4.488 42.227 1.00 43.51 A C ATOM 916 OE1 GLN A 174-17.651 5.496 42.866 1.00 46.17 A O ATOM 917 NE2 GLN A 174-18.147 3.890 41.360 1.00 43.77 A N ATOM 918 C GLN A 174-13.521 3.423 40.566 1.00 29.55 A C ATOM 919 0 GLN A 174-13. 676 2.204 40.528 1.00 29. 36 A O ATOM 920 N THR A 175-13. 399 4.166 39.472 1.00 28.49 A N ATOM 921 CA THR A 175-13. 456 3.572 38.142 1.00 28.57 A C ATOM 922 CB THR A 175-13. 452 4.659 37.056 1.00 29.47 A C ATOM 923 OG1 THR A 175-12. 414 5.610 37.334 1.00 32.59 A 0 ATOM 924 CG2 THR A 175-14. 799 5.367 37.010 1.00 30.53 A C ATOM 925 C THR A 175-12. 332 2.577 37.846 1. 00 28. 24 A C ATOM 926 0 THR A 175-12. 464 1.726 36.963 1.00 30.02 A O ATOM 927 N PHE A 176-11. 226 2.673 38.572 1. 00 26. 08 A N ATOM 928 CA PHE A 176-10.127 1.745 38.349 1. 00 25. 00 A C ATOM 929 CB PHE A 176-8. 948 2.074 39. 276 1. 00 23. 60 A C ATOM 930 CG PHE A 176-7. 732 1. 208 39.053 1. 00 21. 82 A C ATOM 931 CD1 PHE A 176-7.092 1.187 37.817 1. 00 21. 45 A C ATOM 932 CD2 PHE A 176-7.218 0.427 40.085 1. 00 21. 21 A C ATOM 933 CE1 PHE A 176-5.954 0.397 37.611 1. 00 20. 82 A C ATOM 934 CE2 PHE A 176-6.084-0. 363 39.892 1. 00 19. 91 A C ATOM 935 CZ PHE A 176-5. 449-0.379 38.650 1. 00 19. 84 A C ATOM 936 C PHE A 176-10.622 0.328 38.621 1.00 24.56 A C ATOM 937 O PHE A 176-10. 045-0.644 38.137 1. 00 23. 54 A O ATOM 938 N VAL A 177-11. 707 0.216 39.383 1. 00 25. 05 A N ATOM 939 CA VAL A 177-12. 248-1.093 39.733 1. 00 25. 69 A C ATOM 940 CB VAL A 177-13.586-0. 976 40.514 1. 00 25. 62 A C ATOM 941 CG1 VAL A 177-14.725-0. 640 39.576 1.00 25.38 A C ATOM 942 CG2 VAL A 177-13.869-2. 272 41.247 1.00 25.33 A C ATOM 943 C VAL A 177-12.455-1. 987 38.517 1.00 25.77 A C ATOM 944 O VAL A 177-12.211-3. 192 38.582 1.00 26.39 A 0 ATOM 945 N ASP A 178-12.880-1. 403 37.402 1.00 26.29 A N ATOM 946 CA ASP A 178-13. 112-2.198 36.199 1.00 26.95 A C ATOM 947 CB ASP A 178-14.521-1. 947 35.668 1.00 27. 20 A C ATOM 948 CG ASP A 178-15.593-2. 341 36.667 1.00 28.85 A C ATOM 949 OD1 ASP A 178-15.579-3. 505 37.135 1. 00 28. 08 A 0 ATOM 950 OD2 ASP A 178-16.449-1. 486 36.981 1. 00 29. 95 A 0 ATOM 951 C ASP A 178-12.100-1. 981 35.082 1. 00 27. 80 A C ATOM 952 0 ASP A 178-12.309-2. 443 33.961 1. 00 28. 35 A 0 ATOM 953 N ALA A 179-11.008-1. 283 35.385 1. 00 27. 91 A N ATOM 954 CA ALA A 179-9.969-1. 037 34.392 1. 00 27. 44 A C ATOM 955 CB ALA A 179-8.855-0. 202 34.996 1. 00 27. 10 A C ATOM 956 C ALA A 179-9.435-2. 393 33.967 1. 00 27. 98 A C ATOM 957 O ALA A 179-9.286-3. 290 34.794 1. 00 29. 08 A O ATOM 958 N GLU A 180-9. 155-2.556 32.682 1. 00 28. 63 A N ATOM 959 CA GLU A 180-8.650-3. 832 32.198 1. 00 29. 17 A C ATOM 960 CB GLU A 180-9. 025-4.017 30.721 1. 00 32. 29 A C ATOM 961 CG GLU A 180-10. 534-4.203 30.498 1. 00 36. 39 A C ATOM 962 CD GLU A 180-10. 882-4.713 29.103 1. 00 38. 17 A C ATOM 963 OE1 GLU A 180-10.673-3. 971 28.119 1.00 39.87 A 0 ATOM 964 OE2 GLU A 180-11.365-5. 861 28.991 1.00 38.62 A 0 ATOM 965 C GLU A 180-7. 146-4.017 32.399 1. 00 27. 73 A C ATOM 966 O GLU A 180-6.586-5. 043 32.012 1.00 28.40 A 0 ATOM 967 N PHE A 181-6.497-3. 039 33.023 1. 00 25. 30 A N ATOM 968 CA PHE A 181-5.056-3. 117 33.270 1. 00 23. 01 A C ATOM 969 CB PHE A 181-4.319-2. 013 32.503 1. 00 22. 35 A C ATOM 970 CG PHE A 181-4.646-0. 626 32.973 1. 00 22. 11. A C ATOM 971 CD1 PHE A 181-3. 827 0.022 33.890 1. 00 21. 49 A C ATOM 972 CD2 PHE A 181-5. 791 0.021 32.521 1. 00 21. 66 A C ATOM 973 CE1 PHE A 181-4. 143 1.303 34.352 1. 00 21. 30 A C ATOM 974 CE2 PHE A 181-6. 118 1.297 32.975 1. 00 21. 59 A C ATOM 975 CZ PHE A 181-5.288 1.939 33.895 1. 00 21. 65 A C ATOM 976 C PHE A 181-4.773-2. 986 34.760 1. 00 22. 01 A C ATOM 977 O PHE A 181-5.622-2. 523 35.522 1. 00 20. 50 A O ATOM 978 N ASP A 182-3. 580-3.400 35.172 1. 00 20. 25 A N ATOM 979 CA ASP A 182-3. 204-3.326 36.577 1.00 19.58 A C ATOM 980 CB ASP A 182-2. 523-4.627 37.017 1.00 18.70 A C ATOM 981 CG ASP A 182-3. 411-5.843 36.824 1. 00 18. 23 A C ATOM 982 OD1 ASP A 182-4. 557-5.826 37.319 1.00 19. 40 A 0 ATOM 983 OD2 ASP A 182-2. 964-6.814 36.184 1. 00 17. 53 A O ATOM 984 C ASP A 182-2. 268-2.158 36.832 1.00 18.70 A C ATOM 985 O ASP A 182-2. 407-1.446 37.819 1. 00 18. 71 A O ATOM 986 N GLY A 183-1. 312-1.963 35.932 1.00 18.88 A N ATOM 987 CA GLY A 183-0.364-0. 887 36.111 1. 00 17. 83 A C ATOM 988 C GLY A 183 0.032-0. 256 34.804 1.00 18.50 A C ATOM 989 O GLY A 183-0. 567-0.529 33.764 1.00 19.31 A O ATOM 990 N ILE A 184 1.057 0.582 34. 862 1. 00 17. 47 A N ATOM 991 CA ILE A 184 1.547 1.279 33.694 1.00 16.69 A C ATOM 992 CB ILE A 184 1.147 2.771 33.757 1. 00 18. 12 A C ATOM 993 CG2 ILE A 184 1.777 3.545 32.592 1.00 15.31 A C ATOM 994 CG1 ILE A 184-0. 386 2.882 33.750 1.00 17.61 A C ATOM 995 CD1 ILE A 184-0. 928 4.252 34.085 1.00 18.43 A C ATOM 996 C ILE A 184 3.058 1.154 33.629 1.00 17.10 A C ATOM 997 0 ILE A 184 3.737 1.162 34.657 1.00 16.99 A 0 ATOM 998 N LEU A 185 3.583 1.000 32.417 1.00 17. 42 A N ATOM 999 CA LEU A 185 5.023 0.895 32.226 1. 00 15. 81 A C ATOM 1000 CB LEU A 185 5.390-0. 469 31.616 1.00 13.39 A C ATOM 1001 CG LEU A 185 6.884-0. 836 31.597 1. 00 13. 15 A C ATOM 1002 CD1 LEU A 185 7.056-2. 349 31.494 1. 00 13. 42 A C ATOM 1003 CD2 LEU A 185 7.582-0. 136 30.446 1. 00 11. 61 A C ATOM 1004 C LEU A 185 5.424 2.038 31.297 1. 00 15. 84 A C ATOM 1005 0 LEU A 185 5.267 1.949 30.078 1. 00 16. 06 A 0 ATOM 1006 N GLY A 186 5.929 3.116 31.891 1. 00 15. 83 A N ATOM 1007 CA GLY A 186 6.334 4.282 31.123 1. 00 15. 02 A C ATOM 1008 C GLY A 186 7.564 4.062 30.266 1. 00 15. 36 A C ATOM 1009 0 GLY A 186 8.550 3.466 30.708 1.00 15.71 A O ATOM 1010 N LEU A 187 7.513 4.573 29.039 1. 00 14. 69 A N ATOM 1011 CA LEU A 187 8.610 4.430 28.102 1. 00 13. 86 A C ATOM 1012 CB LEU A 187 8.129 3.662 26.876 1. 00 13. 67 A C ATOM 1013 CG LEU A 187 7.736 2.200 27.122 1. 00 14. 94 A C ATOM 1014 CD1 LEU A 187 6.802 1.734 26.022 1.00 15.10 A C ATOM 1015 CD2 LEU A 187 8.991 1.324 27.178 1.00 12.84 A C ATOM 1016 C LEU A 187 9.197 5.773 27.684 1. 00 14. 44 A C ATOM 1017 O LEU A 187 9.919 5.857 26.687 1.00 14.57 A O ATOM 1018 N GLY A 188 8.891 6.818 28.450 1. 00 14. 20 A N ATOM 1019 CA GLY A 188 9.409 8.144 28.147 1.00 14.51 A C ATOM 1020 C GLY A 188 10.801 8.317 28.724 1.00 15.82 A C ATOM 1021 0 GLY A 188 11.381 7.353 29.234 1.00 16.51 A O ATOM 1022 N TYR A 189 11.338 9.532 28.657 1. 00 15. 81 A N ATOM 1023 CA TYR A 189 12.674 9.809 29.176 1. 00 16. 02 A C ATOM 1024 CB TYR A 189 13.206 11.130 28.627 1.00 16.22 A C ATOM 1025 CG TYR A 189 13.597 11.085 27.173 1. 00 15. 60 A C ATOM 1026 CD1 TYR A 189 12.634 11.162 26.172 1.00 16.49 A C ATOM 1027 CE1 TYR A 189 12. 994 11.165 24.820 1.00 16.66 A C ATOM 1028 CD2 TYR A 189 14.937 11.000 26.799 1.00 14.89 A C ATOM 1029 CE2 TYR A 189 15.310 11.001 25.453 1.00 16.99 A C ATOM 1030 CZ TYR A 189 14.333 11.087 24.468 1. 00 16. 78 A C ATOM 1031 OH TYR A 189 14.693 11.113 23.137 1.00 16.33 A O ATOM 1032 C TYR A 189 12.739 9.856 30.696 1.00 17.25 A C ATOM 1033 O TYR A 189 11.731 10.096 31.364 1. 00 17. 86 A O ATOM 1034 N PRO A 190 13.938 9.634 31.265 1. 00 17. 61 A N ATOM 1035 CD PRO A 190 15.147 9.105 30.610 1.00 16.61 A C ATOM 1036 CA PRO A 190 14.102 9.654 32.722 1.00 18.52 A C ATOM 1037 CB PRO A 190 15.564 9.225 32.926 1. 00 17. 67 A C ATOM 1038 CG PRO A 190 16.210 9.449 31.602 1. 00 18. 69 A C ATOM 1039 C PRO A 190 13.761 10.962 33.428 1. 00 19. 64 A C ATOM 1040 O PRO A 190 13.419 10.955 34.609 1. 00 20. 01 A 0 ATOM 1041 N SER A 191 13.831 12.077 32.713 1. 00 20. 20 A N ATOM 1042 CA SER A 191 13.522 13.373 33.305 1.00 21.60 A C ATOM 1043 CB SER A 191 13.780 14.488 32.294 1.00 22.53 A C ATOM 1044 OG SER A 191 12.771 14.489 31.301 1.00 23.98 A O ATOM 1045 C SER A 191 12.060 13.432 33.739 1.00 22.72 A C ATOM 1046 O SER A 191 11.670 14.264 34.552 1.00 23.45 A 0 ATOM 1047 N LEU A 192 11.252 12.544 33.180 1.00 23.91 A N ATOM 1048 CA LEU A 192 9.834 12.489 33.492 1.00 25.39 A C ATOM 1049 CB LEU A 192 9.075 12.024 32.246 1. 00 26. 23 A C ATOM 1050 CG LEU A 192 7.601 12.356 32.051 1.00 25.91 A C ATOM 1051 CD1 LEU A 192 7.389 13. 867 32.138 1. 00 26. 96 A C ATOM 1052 CD2 LEU A 192 7.166 11.837 30.692 1.00 24.73 A C ATOM 1053 C LEU A 192 9.573 11.531 34.656 1.00 26.23 A C ATOM 1054 O LEU A 192 8.494 11.530 35.242 1.00 27.59 A O ATOM 1055 N ALA A 193 10.569 10.718 34.991 1. 00 26. 83 A N ATOM 1056 CA ALA A 193 10.433 9.750 36.072 1.00 28.91 A C ATOM 1057 CB ALA A 193 11.550 8.715 35.995 1. 00 26. 58 A C ATOM 1058 C ALA A 193 10.443 10.425 37.436 1. 00 31. 06 A C ATOM 1059 O ALA A 193 11.310 11.249 37.729 1. 00 31. 89 A 0 ATOM 1060 N VAL A 194 9.472 10.071 38.270 1. 00 33. 19 A N ATOM 1061 CA VAL A 194 9.378 10.642 39.605 1. 00 34. 53 A C ATOM 1062 CB VAL A 194 7.930 10.558 40.162 1. 00 35. 15 A C ATOM 1063 CG1 VAL A 194 6.961 11.230 39.192 1.00 34.24 A C ATOM 1064 CG2 VAL A 194 7.540 9.101 40.401 1.00 34.35 A C ATOM 1065 C VAL A 194 10.318 9.891 40.535 1. 00 34. 92 A C ATOM 1066 O VAL A 194 10.454 8.672 40.435 1. 00 34. 89 A 0 ATOM 1067 N GLY A 195 10.969 10.634 41.429 1. 00 35. 72 A N ATOM 1068 CA GLY A 195 11.894 10.035 42.377 1. 00 35. 10 A C ATOM 1069 C GLY A 195 13.233 9.663 41.768 1. 00 34. 47 A C ATOM 1070 O GLY A 195 14.048 8.989 42.406 1. 00 33. 06 A O ATOM 1071 N GLY A 196 13.461 10.102 40.534 1. 00 33. 58 A N ATOM 1072 CA GLY A 196 14.708 9.789 39.865 1. 00 34. 30 A C ATOM 1073 C GLY A 196 14.888 8.289 39.707 1. 00 33. 88 A C ATOM 1074 O GLY A 196 16.013 7.784 39.746 1. 00 34. 98 A O ATOM 1075 N VAL A 197 13.776 7.574 39.545 1. 00 31. 55 A N ATOM 1076 CA VAL A 197 13.800 6.119 39.373 1. 00 28. 53 A C ATOM 1077 CB VAL A 197 12.443 5. 521 39.799 1.00 29.25 A C ATOM 1078 CG1 VAL A 197 12.360 4.050 39.435 1. 00 28. 63 A C ATOM 1079 CG2 VAL A 197 12.261 5.713 41.297 1.00 29.05 A C ATOM 1080 C VAL A 197 14.090 5.794 37.903 1. 00 26. 38 A C ATOM 1081 O VAL A 197 13.428 6.318 37.002 1. 00 25. 44 A 0 ATOM 1082 N THR A 198 15.081 4.941 37.659 1. 00 23. 72 A N ATOM 1083 CA THR A 198 15.455 4.590 36.287 1. 00 22. 22 A C ATOM 1084 CB THR A 198 16.752 3.765 36. 245 1. 00 21. 85 A C ATOM 1085 OG1 THR A 198 17.798 4.483 36.905 1. 00 21. 78 A 0 ATOM 1086 CG2 THR A 198 17.171 3.507 34.804 1.00 21.64 A C ATOM 1087 C THR A 198 14.369 3.798 35.568 1.00 20.97 A C ATOM 1088 0 THR A 198 13.954 2.740 36.031 1. 00 21. 54 A 0 ATOM 1089 N PRO A 199 13.895 4.310 34.420 1.00 19.79 A N ATOM 1090 CD PRO A 199 14.263 5.622 33.858 1.00 18.73 A C ATOM 1091 CA PRO A 199 12.849 3.666 33.614 1. 00 18. 06 A C ATOM 1092 CB PRO A 199 12.634 4.652 32.466 1.00 18.94 A C ATOM 1093 CG PRO A 199 13.026 5.979 33.053 1.00 19.45 A C ATOM 1094 C PRO A 199 13.279 2.295 33.103 1.00 18.70 A C ATOM 1095 O PRO A 199 14.466 2.031 32.916 1.00 19.51 A 0 ATOM 1096 N VAL A 200 12.308 1.423 32.867 1.00 18.70 A N ATOM 1097 CA VAL A 200 12. 600 0.088 32.375 1.00 17.45 A C ATOM 1098 CB VAL A 200 11.297-0. 677 32.053 1.00 18.06 A C ATOM 1099 CG1 VAL A 200 11.604-1. 944 31.230 1.00 17.73 A C ATOM 1100 CG2 VAL A 200 10.598-1. 051 33.353 1.00 18.08 A C ATOM 1101 C VAL A 200 13.500 0.090 31.140 1. 00 17. 94 A C ATOM 1102 O VAL A 200 14.534-0. 581 31.130 1.00 17.40 A O ATOM 1103 N PHE A 201 13.131 0.850 30.108 1. 00 17. 41 A N ATOM 1104 CA PHE A 201 13.937 0.861 28.892 1.00 17.20 A C ATOM 1105 CB PHE A 201 13.263 1.663 27.780 1.00 17.65 A C ATOM 1106 CG PHE A 201 13.905 1.458 26.436 1. 00 17. 90 A C ATOM 1107 CD1 PHE A 201 14.006 0.174 25.892 1.00 17.44 A C ATOM 1108 CD2 PHE A 201 14.441 2.528 25.730 1.00 17.31 A C ATOM 1109 CE1 PHE A 201 14.633-0. 046 24.670 1.00 17. 24 A C ATOM 1110 CE2 PHE A 201 15.073 2.323 24.501 1. 00 17. 88 A C ATOM 1111 CZ PHE A 201 15.170 1.030 23.968 1. 00 17. 63 A C ATOM 1112 C PHE A 201 15.359 1.366 29.077 1. 00 18. 00 A C ATOM 1113 0 PHE A 201 16.261 0.938 28.354 1. 00 18. 96 A 0 ATOM 1114 N ASP A 202 15.567 2.277 30.026 1. 00 18. 31 A N ATOM 1115 CA ASP A 202 16.909 2.784 30.286 1. 00 19. 15 A C ATOM 1116 CB ASP A 202 16.870 4.000 31.213 1. 00 20. 62 A C ATOM 1117 CG ASP A 202 16.317 5.238 30.527 1. 00 21. 62 A C ATOM 1118 OD1 ASP A 202 15.106 5.264 30.210 1. 00 21. 53 A 0 ATOM 1119 OD2 ASP A 202 17.101 6.182 30.296 1.00 23.22 A O ATOM 1120 C ASP A 202 17.740 1.672 30.917 1. 00 19. 66 A C ATOM 1121 O ASP A 202 18.946 1.576 30.676 1. 00 20. 28 A 0 ATOM 1122 N ASN A 203 17.100 0. 828 31.722 1. 00 19. 39 A N ATOM 1123 CA ASN A 203 17.817-0. 285 32.334 1. 00 20. 53 A C ATOM 1124 CB ASN A 203 16.998-0. 929 33.463 1. 00 19. 84 A C ATOM 1125 CG ASN A 203 17.096-0. 150 34.765 1. 00 21. 01 A C ATOM 1126 OD1 ASN A 203 18.168 0.336 35.120 1.00 21.03 A 0 ATOM 1127 ND2 ASN A 203 15.983-0. 039 35.488 1.00 19.00 A N ATOM 1128 C ASN A 203 18.139-1. 319 31.258 1. 00 20. 53 A C ATOM 1129 O ASN A 203 19.201-1. 944 31.286 1. 00 21. 26 A O ATOM 1130 N MET A 204 17.223-1. 488 30.307 1. 00 19. 94 A N ATOM 1131 CA MET A 204 17.437-2. 436 29.222 1. 00 20. 85 A C ATOM 1132 CB MET A 204 16.227-2. 485 28.286 1. 00 20. 40 A C ATOM 1133 CG MET A 204 15.010-3. 185 28.879 1. 00 22. 14 A C ATOM 1134 SD MET A 204 13.689-3. 398 27.661 1. 00 21. 29 A S ATOM 1135 CE MET A 204 12.765-1. 939 27.953 1. 00 27. 18 A C ATOM 1136 C MET A 204 18.669-2. 022 28.434 1. 00 20. 62 A C ATOM 1137 0 MET A 204 19. 485-2. 863 28.052 1. 00 21. 30 A 0 ATOM 1138 N MET A 205 18.798-0. 723 28. 183 1. 00 19. 59 A N ATOM 1139 CA MET A 205 19.949-0. 226 27.444 1. 00 19. 24 A C ATOM 1140 CB MET A 205 19.758 1.237 27.057 1. 00 16. 27 A C ATOM 1141 CG MET A 205 18.738 1.474 25.967 1. 00 17. 01 A C ATOM 1142 SD MET A 205 18. 847 3.175 25.384 1.00 18.64 A S ATOM 1143 CE MET A 205 17.766 3.965 26.566 1.00 17. 86 A C ATOM 1144 C MET A 205 21.218-0. 359 28.279 1. 00 19. 85 A C ATOM 1145 0 MET A 205 22.254-0. 799 27.777 1.00 20.30 A O ATOM 1146 N ALA A 206 21.124 0.021 29.552 1. 00 19. 71 A N ATOM 1147 CA ALA A 206 22.259-0. 033 30.462 1.00 20.19 A C ATOM 1148 CB ALA A 206 21.903 0.642 31.789 1.00 18.68 A C ATOM 1149 C ALA A 206 22.700-1. 463 30.708 1. 00 21. 03 A C ATOM 1150 O ALA A 206 23.868-1. 717 30.999 1.00 21.46 A O ATOM 1151 N GLN A 207 21.762-2. 397 30.602 1.00 21.96 A N ATOM 1152 CA GLN A 207 22.066-3. 806 30.819 1.00 22.59 A C ATOM 1153 CB GLN A 207 20.933-4. 451 31.630 1.00 22.82 A C ATOM 1154 CG GLN A 207 21.000-4. 083 33.113 1.00 24.65 A C ATOM 1155 CD GLN A 207 19.799-4. 545 33.939 1.00 25.77 A C ATOM 1156 OE1 GLN A 207 19.170-5. 567 33.650 1.00 26.35 A O ATOM 1157 NE2 GLN A 207 19.496-3. 797 34.993 1.00 25.29 A N ATOM 1158 C GLN A 207 22.311-4. 558 29.505 1.00 22.65 A C ATOM 1159 O GLN A 207 22.362-5. 784 29.485 1.00 22.76 A O ATOM 1160 N ASN A 208 22. 480-3.805 28.418 1.00 23.12 A N ATOM 1161 CA ASN A 208 22.729-4. 351 27.078 1.00 23.83 A C ATOM 1162 CB ASN A 208 24. 171-4. 840 26.954 1. 00 26. 80 A C ATOM 1163 CG ASN A 208 25.173-3. 748 27.228 1.00 31.13 A C ATOM 1164 OD1 ASN A 208 25.029-2. 623 26.737 1. 00 33. 39 A O ATOM 1165 ND2 ASN A 208 26.202-4. 065 28.017 1.00 32.84 A N ATOM 1166 C ASN A 208 21.797-5. 477 26.664 1. 00 22. 75 A C ATOM 1167 O ASN A 208 22.241-6. 494 26.131 1.00 21.60 A O ATOM 1168 N LEU A 209 20.505-5. 289 26.894 1.00 21.51 A N ATOM 1169 CA LEU A 209 19.525-6. 305 26.549 1. 00 21. 17 A C ATOM 1170 CB LEU A 209 18.383-6. 299 27.571 1.00 20.05 A C ATOM 1171 CG LEU A 209 18.793-6. 578 29.018 1. 00 18. 08 A C ATOM 1172 CD1 LEU A 209 17.554-6. 587 29.906 1.00 15.88 A C ATOM 1173 CD2 LEU A 209 19.525-7. 910 29.100 1.00 16.67 A C ATOM 1174 C LEU A 209 18.966-6. 102 25.150 1. 00 20. 87 A C ATOM 1175 0 LEU A 209 18.335-6. 996 24.600 1. 00 20. 99 A O ATOM 1176 N VAL A 210 19.201-4. 928 24.574 1. 00 21. 89 A N ATOM 1177 CA VAL A 210 18.705-4. 628 23.234 1.00 22.04 A C ATOM 1178 CB VAL A 210 17.710-3. 436 23.257 1.00 20.70 A C ATOM 1179 CG1 VAL A 210 16.407-3. 872 23.898 1. 00 19. 37 A C ATOM 1180 CG2 VAL A 210 18.298-2. 269 24.019 1. 00 20. 18 A C ATOM 1181 C VAL A 210 19.843-4. 347 22.253 1.00 23.24 A C ATOM 1182 O VAL A 210 20.880-3. 793 22.632 1. 00 24. 08 A O ATOM 1183 N ASP A 211 19.642-4. 738 20.997 1. 00 24. 38 A N ATOM 1184 CA ASP A 211 20.652-4. 569 19.952 1. 00 26. 29 A C ATOM 1185 CB ASP A 211 20.376-5. 536 18.790 1. 00 27. 14 A C ATOM 1186 CG ASP A 211 20.514-7. 010 19.198 1. 00 29. 20 A C ATOM 1187 OD1 ASP A 211 21.041-7. 303 20.298 1. 00 27. 94 A O ATOM 1188 OD2 ASP A 211 20.104-7. 883 18.405 1.00 30.60 A O ATOM 1189 C ASP A 211 20.757-3. 136 19.429 1. 00 26. 84 A C ATOM 1190 0 ASP A 211 21.817-2. 715 18.951 1. 00 27. 86 A O ATOM 1191 N LEU A 212 19.651-2. 402 19.513 1.00 25.65 A N ATOM 1192 CA LEU A 212 19.595-1. 004 19.093 1. 00 24. 27 A C ATOM 1193 CB LEU A 212 18.892-0. 862 17.738 1. 00 24. 61 A C ATOM 1194 CG LEU A 212 19.664-1. 373 16.515 1. 00 25. 17 A C ATOM 1195 CD1 LEU A 212 18.857-1. 121 15.249 1. 00 23. 53 A C ATOM 1196 CD2 LEU A 212 21.016-0. 670 16.437 1. 00 22. 90 A C ATOM 1197 C LEU A 212 18.814-0. 264 20.174 1.00 23.84 A C ATOM 1198 O LEU A 212 17.797-0. 764 20.667 1. 00 25. 26 A O ATOM 1199 N PRO A 213 19.279 0.934 20. 558 1.00 22.08 A N ATOM 1200 CD PRO A 213 20.419 1.652 19.954 1. 00 20. 78 A C ATOM 1201 CA PRO A 213 18.637 1.751 21.593 1.00 20.97 A C ATOM 1202 CB PRO A 213 19.693 2.818 21.875 1.00 20.53 A C ATOM 1203 CG PRO A 213 20.257 3.063 20.503 1.00 20.42 A C ATOM 1204 C PRO A 213 17.295 2.344 21.168 1.00 20.38 A C ATOM 1205 0 PRO A 213 17.092 3.557 21.201 1. 00 19. 34 A O ATOM 1206 N MET A 214 16.374 1.474 20.780 1. 00 20. 60 A N ATOM 1207 CA MET A 214 15.060 1.910 20.350 1. 00 21. 25 A C ATOM 1208 CB MET A 214 15.105 2.317 18.877 1. 00 22. 54 A C ATOM 1209 CG MET A 214 15.731 1.258 17.984 1. 00 26. 32 A C ATOM 1210 SD MET A 214 15.852 1.711 16.232 1. 00 29. 38 A S ATOM 1211 CE MET A 214 14.978 0.400 15.572 1. 00 28. 40 A C ATOM 1212 C MET A 214 14.028 0.814 20.534 1. 00 21. 22 A C ATOM 1213 0 MET A 214 14.365-0. 342 20.798 1. 00 21. 12 A 0 ATOM 1214 N PHE A 215 12.765 1.202 20.425 1. 00 20. 73 A N ATOM 1215 CA PHE A 215 11.648 0.273 20.508 1. 00 19. 76 A C ATOM 1216 CB PHE A 215 11.073 0.172 21.937 1. 00 17. 84 A C ATOM 1217 CG PHE A 215 10.708 1.495 22.564 1. 00 15. 58 A C ATOM 1218 CD1 PHE A 215 11.659 2.232 23.278 1. 00 14. 66 A C ATOM 1219 CD2 PHE A 215 9.409 1.986 22.473 1. 00 14. 26 A C ATOM 1220 CE1 PHE A 215 11.318 3.441 23.900 1.00 13.89 A C ATOM 1221 CE2 PHE A 215 9.054 3.197 23.089 1.00 15.21 A C ATOM 1222 CZ PHE A 215 10.014 3.925 23.806 1.00 14.13 A C ATOM 1223 C PHE A 215 10.618 0.827 19.542 1. 00 20. 46 A C ATOM 1224 0 PHE A 215 10.665 1.999 19.200 1.00 22.19 A 0 ATOM 1225 N SER A 216 9.702-0. 005 19.075 1.00 21.53 A N ATOM 1226 CA SER A 216 8.708 0.482 18.136 1.00 23.01 A C ATOM 1227 CB SER A 216 9.141 0.167 16.705 1.00 23.35 A C ATOM 1228 OG SER A 216 9.491-1. 196 16.574 1. 00 25. 93 A 0 ATOM 1229 C SER A 216 7.351-0. 121 18.436 1.00 23.91 A C ATOM 1230 O SER A 216 7.256-1. 187 19. 050 1. 00 23. 88 A 0 ATOM 1231 N VAL A 217 6.302 0.572 18.007 1. 00 24. 17 A N ATOM 1232 CA VAL A 217 4.947 0.126 18.269 1. 00 24. 96 A C ATOM 1233 CB VAL A 217 4.242 1.079 19.252 1. 00 24. 83 A C ATOM 1234 CG1 VAL A 217 2.827 0.593 19.536 1.00 25.02 A C ATOM 1235 CG2 VAL A 217 5. 043 1.173 20.539 1.00 26.32 A C ATOM 1236 C VAL A 217 4.068-0. 007 17.040 1.00 26.36 A C ATOM 1237 O VAL A 217 4.012 0.879 16.176 1. 00 25. 55 A 0 ATOM 1238 N TYR A 218 3.378-1. 136 16.977 1. 00 27. 66 A N ATOM 1239 CA TYR A 218 2.457-1. 403 15.892 1.00 29.58 A C ATOM 1240 CB TYR A 218 2.865-2. 642 15.092 1.00 29.69 A C ATOM 1241 CG TYR A 218 1.783-3. 080 14.127 1.00 30.21 A C ATOM 1242 CD1 TYR A 218 1.436-2. 286 13.030 1.00 30.26 A C ATOM 1243 CE1 TYR A 218 0.409-2. 661 12.165 1.00 29.54 A C ATOM 1244 CD2 TYR A 218 1.074-4. 267 14.334 1.00 30.25 A C ATOM 1245 CE2 TYR A 218 0.049-4. 652 13.477 1.00 30.30 A C ATOM 1246 CZ TYR A 218-0. 278-3.845 12.396 1.00 31.06 A C ATOM 1247 OH TYR A 218-1. 291-4.223 11.548 1.00 31.98 A O ATOM 1248 C TYR A 218 1.109-1. 648 16.525 1. 00 29. 04 A C ATOM 1249 O TYR A 218 0.952-2. 574 17.319 1. 00 28. 96 A O ATOM 1250 N MET A 219 0.144-0. 804 16.191 1. 00 30. 34 A N ATOM 1251 CA MET A 219-1.200-0. 951 16.724 1. 00 33. 38 A C ATOM 1252 CB MET A 219-1. 634 0.326 17.448 1. 00 32. 02 A C ATOM 1253 CG MET A 219-0.763 0.650 18.655 1. 00 30. 74 A C ATOM 1254 SD MET A 219-1.265 2.132 19.531 1. 00 30. 51 A S ATOM 1255 CE MET A 219-0.549 1.836 21.159 1. 00 27. 75 A C ATOM 1256 C MET A 219-2.124-1. 269 15.562 1. 00 35. 77 A C ATOM 1257 O MET A 219-2.326-0. 453 14.665 1. 00 34. 92 A O ATOM 1258 N SER A 220-2.659-2. 483 15.585 1.00 40.09 A N ATOM 1259 CA SER A 220-3.545-2. 966 14.540 1.00 44.86 A C ATOM 1260 CB SER A 220-3.580-4. 497 14.561 1. 00 45. 22 A C ATOM 1261 OG SER A 220-4.151-5. 011 13.372 1.00 47.24 A O ATOM 1262 C SER A 220-4.952-2. 420 14.704 1.00 47.82 A C ATOM 1263 O SER A 220-5.506-2. 410 15.807 1.00 47.99 A O ATOM 1264 N SER A 221-5.520-1. 964 13.592 1. 00 51. 76 A N ATOM 1265 CA SER A 221-6.871-1. 420 13.579 1. 00 55. 98 A C ATOM 1266 CB SER A 221-7.046-0. 490 12.377 1. 00 55. 81 A C ATOM 1267 OG SER A 221-6.768-1. 171 11.166 1. 00 57. 12 A O ATOM 1268 C SER A 221-7.887-2. 559 13.511 1. 00 58. 58 A C ATOM 1269 0 SER A 221-8.993-2. 452 14.038 1. 00 59. 13 A O ATOM 1270 N ASN A 222-7. 501-3.648 12.856 1.00 62.00 A N ATOM 1271 CA ASN A 222-8. 362-4.819 12.723 1.00 65.11 A C ATOM 1272 CB ASN A 222-8. 464-5.248 11.251 1.00 66.58 A C ATOM 1273 CG ASN A 222-9. 225-4.244 10.394 1.00 68.18 A C ATOM 1274 OD1 ASN A 222-10. 437-4.067 10.549 1.00 68.67 A 0 ATOM 1275 ND2 ASN A 222-8. 512-3.580 9.486 1.00 68.68 A N ATOM 1276 C ASN A 222-7. 782-5.965 13.552 1.00 66.50 A C ATOM 1277 O ASN A 222-6. 581-5.999 13.821 1. 00 67.09 A O ATOM 1278 N PRO A 223-8.629-6. 918 13.972 1.00 67.64 A N ATOM 1279 CD PRO A 223-8.163-8. 206 14.514 1.00 67.77 A C ATOM 1280 CA PRO A 223-10.075-6. 957 13.714 1.00 67.89 A C ATOM 1281 CB PRO A 223-10.471-8. 359 14.177 1.00 68.16 A C ATOM 1282 CG PRO A 223-9.202-9. 155 13.985 1. 00 68.31 A C ATOM 1283 C PRO A 223-10.834-5. 865 14.467 1.00 67.84 A C ATOM 1284 O PRO A 223-11.777-6. 147 15.207 1.00 67.85 A O ATOM 1285 N GLY A 226-7. 322-5.972 17.016 1.00 48.00 A N ATOM 1286 CA GLY A 226-5. 946-5.594 17.290 1. 00 47. 95 A C ATOM 1287 C GLY A 226-5. 067-6.800 17.558 1.00 47.27 A C ATOM 1288 O GLY A 226-4. 124-6.729 18.347 1. 00 46. 82 A O ATOM 1289 N ALA A 227-5.380-7. 904 16.884 1. 00 46. 59 A N ATOM 1290 CA ALA A 227-4.649-9. 163 17.027 1. 00 45. 29 A C ATOM 1291 CB ALA A 227-5.194-10. 184 16.025 1.00 45.66 A C ATOM 1292 C ALA A 227-3.128-9. 042 16.869 1. 00 43. 89 A C ATOM 1293 O ALA A 227-2.373-9. 325 17.805 1. 00 45. 56 A O ATOM 1294 N GLY A 228-2. 683-8.626 15.686 1. 00 40. 24 A N ATOM 1295 CA GLY A 228-1. 258-8.502 15.433 1.00 35.23 A C ATOM 1296 C GLY A 228-0. 532-7.330 16.068 1.00 32. 23 A C ATOM 1297 O GLY A 228 0.646-7. 120 15.779 1.00 30.94 A O ATOM 1298 N SER A 229-1.208-6. 566 16.926 1. 00 30. 01 A N ATOM 1299 CA SER A 229-0.568-5. 416 17.573 1. 00 28. 36 A C ATOM 1300 CB SER A 229-1.560-4. 664 18.462 1. 00 27. 79 A C ATOM 1301 OG SER A 229-2.593-4. 079 17.697 1. 00 27. 46 A O ATOM 1302 C SER A 229 0.625-5. 853 18.417 1.00 27.55 A C ATOM 1303 O SER A 229 0.543-6. 812 19.192 1. 00 26. 38 A O ATOM 1304 N GLU A 230 1.742-5. 153 18.270 1. 00 26. 03 A N ATOM 1305 CA GLU A 230 2.906-5. 521 19.047 1. 00 25. 46 A C ATOM 1306 CB GLU A 230 3.663-6. 666 18.364 1. 00 26. 10 A C ATOM 1307 CG GLU A 230 4.521-6. 253 17.193 1. 00 27. 86 A C ATOM 1308 CD GLU A 230 5.317-7. 413 16.619 1. 00 30. 56 A C ATOM 1309 OE1 GLU A 230 5.550-8. 400 17.354 1. 00 30. 86 A O ATOM 1310 OE2 GLU A 230 5.725-7. 334 15.439 1.00 30.36 A O ATOM 1311 C GLU A 230 3.865-4. 383 19.321 1. 00 24. 71 A C ATOM 1312 0 GLU A 230 3.922-3. 391 18.587 1.00 24.63 A O ATOM 1313 N LEU A 231 4.613-4. 551 20.404 1.00 24.16 A N ATOM 1314 CA LEU A 231 5.623-3. 603 20.837 1. 00 23. 68 A C ATOM 1315 CB LEU A 231 5.442-3. 290 22.320 1. 00 23. 88 A C ATOM 1316 CG LEU A 231 6.555-2. 478 22.986 1. 00 25. 15 A C ATOM 1317 CD1 LEU A 231 6.415-1. 012 22.641 1. 00 24. 93 A C ATOM 1318 CD2 LEU A 231 6.470-2. 666 24.491 1.00 28.67 A C ATOM 1319 C LEU A 231 6.950-4. 322 20.625 1.00 23.08 A C ATOM 1320 0 LEU A 231 7.080-5. 494 20.967 1. 00 23. 45 A O ATOM 1321 N ILE A 232 7.934-3. 634 20.065 1. 00 22. 05 A N ATOM 1322 CA ILE A 232 9.221-4. 265 19.833 1. 00 22. 38 A C ATOM 1323 CB ILE A 232 9.507-4. 377 18.322 1. 00 22. 98 A C ATOM 1324 CG2 ILE A 232 10.865-5. 031 18.095 1. 00 22. 72 A C ATOM 1325 CG1 ILE A 232 8.396-5. 196 17.655 1.00 23.85 A C ATOM 1326 CD1 ILE A 232 8.446-5. 197 16.143 1. 00 26. 02 A C ATOM 1327 C ILE A 232 10.370-3. 522 20.505 1.00 22.03 A C ATOM 1328 0 ILE A 232 10.605-2. 350 20.230 1.00 21.31 A O ATOM 1329 N PHE A 233 11.078-4. 214 21.392 1.00 21.87 A N ATOM 1330 CA PHE A 233 12.215-3. 630 22.088 1.00 21.61 A C ATOM 1331 CB PHE A 233 12.300-4. 138 23.532 1.00 21.60 A C ATOM 1332 CG PHE A 233 11.316-3. 496 24.474 1.00 21.75 A C ATOM 1333 CD1 PHE A 233 11.402-2. 143 24.775 1.00 21.71 A C ATOM 1334 CD2 PHE A 233 10.313-4. 249 25.073 1.00 22.87 A C ATOM 1335 CE1 PHE A 233 10.505-1. 544 25.657 1. 00 21. 98 A C ATOM 1336 CE2 PHE A 233 9.407-3. 658 25.961 1.00 24.23 A C ATOM 1337 CZ PHE A 233 9.507-2. 300 26.251 1. 00 22. 31 A C ATOM 1338 C PHE A 233 13.486-4. 029 21.359 1. 00 22. 54 A C ATOM 1339 0 PHE A 233 13.726-5. 213 21.119 1. 00 23. 63 A O ATOM 1340 N GLY A 234 14.296-3. 044 20.994 1. 00 22. 03 A N ATOM 1341 CA GLY A 234 15.542-3. 355 20. 322 1. 00 22. 37 A C ATOM 1342 C GLY A 234 15.530-3. 213 18.820 1. 00 21. 96 A C ATOM 1343 O GLY A 234 16.510-3. 547 18.166 1. 00 22. 67 A 0 ATOM 1344 N GLY A 235 14.428-2. 722 18.267 1. 00 22. 68 A N ATOM 1345 CA GLY A 235 14.355-2. 546 16.831 1. 00 24. 70 A C ATOM 1346 C GLY A 235 12.941-2. 344 16.336 1. 00 26. 98 A C ATOM 1347 O GLY A 235 12.054-1. 989 17.114 1. 00 27. 49 A 0 ATOM 1348 N TYR A 236 12.737-2. 558 15.038 1. 00 28. 68 A N ATOM 1349 CA TYR A 236 11.421-2. 429 14.422 1. 00 30. 40 A C ATOM 1350 CB TYR A 236 11.250-1. 038 13.809 1. 00 31. 82 A C ATOM 1351 CG TYR A 236 12.278-0. 674 12.763 1. 00 33. 79 A C ATOM 1352 CD1 TYR A 236 12.270-1. 274 11.503 1.00 34.98 A C ATOM 1353 CE1 TYR A 236 13.207-0. 918 10.530 1.00 35.77 A C ATOM 1354 CD2 TYR A 236 13.250 0.288 13.027 1. 00 34. 15 A C ATOM 1355 CE2 TYR A 236 14.188 0.649 12.069 1.00 34.92 A C ATOM 1356 CZ TYR A 236 14.161 0.045 10.822 1.00 36.17 A C ATOM 1357 OH TYR A 236 15.077 0.420 9.862 1.00 38.06 A 0 ATOM 1358 C TYR A 236 11.228-3. 507 13.356 1. 00 31. 27 A C ATOM 1359 O TYR A 236 12.189-4. 135 12.913 1. 00 30. 81 A O ATOM 1360 N ASP A 237 9.980-3. 715 12.955 1.00 31.84 A N ATOM 1361 CA ASP A 237 9.638-4. 723 11.961 1.00 32.51 A C ATOM 1362 CB ASP A 237 8.510-5. 601 12.504 1. 00 32. 99 A C ATOM 1363 CG ASP A 237 8.295-6. 851 11.680 1. 00 33. 45 A C ATOM 1364 OD1 ASP A 237 8.503-6. 791 10.451 1. 00 32. 53 A o ATOM 1365 OD2 ASP A 237 7.908-7. 887 12.265 1. 00 33. 22 A 0 ATOM 1366 C ASP A 237 9.180-4. 036 10.679 1. 00 33. 26 A c ATOM 1367 0 ASP A 237 8.118-3. 416 10.648 1. 00 33. 41 A O ATOM 1368 N HIS A 238 9.960-4. 157 9.613 1. 00 34. 25 A N ATOM 1369 CA HIS A 238 9.595-3. 502 8.364 1. 00 36. 46 A C ATOM 1370 CB HIS A 238 10.764-3. 529 7.379 1. 00 37. 53 A C ATOM 1371 CG HIS A 238 10.751-2. 390 6.408 1.00 38.69 A C ATOM 1372 CD2 HIS A 238 11.738-1. 564 5.987 1. 00 39. 96 A C ATOM 1373 ND1 HIS A 238 9.608-1. 990 5.749 1. 00 39. 40 A N ATOM 1374 CE1 HIS A 238 9.891-0. 966 4.964 1.00 40.26 A C ATOM 1375 NE2 HIS A 238 11.177-0. 688 5.089 1.00 40.49 A N ATOM 1376 C HIS A 238 8.350-4. 075 7.685 1.00 36.51 A C ATOM 1377 O HIS A 238 7.883-3. 534 6.684 1.00 37.19 A O ATOM 1378 N SER A 239 7.806-5. 159 8.225 1. 00 36. 26 A N ATOM 1379 CA SER A 239 6.612-5. 760 7.643 1. 00 36. 60 A C ATOM 1380 CB SER A 239 6.527-7. 240 8.016 1. 00 36. 33 A C ATOM 1381 OG SER A 239 6.322-7. 384 9.409 1. 00 37. 88 A 0 ATOM 1382 C SER A 239 5.357-5. 040 8.137 1.00 36.52 A C ATOM 1383 O SER A 239 4.247-5. 329 7.687 1.00 35.63 A 0 ATOM 1384 N HIS A 240 5.542-4. 105 9.069 1. 00 36. 39 A N ATOM 1385 CA HIS A 240 4.434-3. 339 9.632 1. 00 35. 07 A C ATOM 1386 CB HIS A 240 4.595-3. 179 11.143 1. 00 35. 73 A C ATOM 1387 CG HIS A 240 4.375-4. 442 11.911 1. 00 36. 51 A C ATOM 1388 CD2 HIS A 240 5.119-5. 046 12.866 1. 00 36. 93 A C ATOM 1389 ND1 HIS A 240 3.255-5. 228 11.743 1. 00 36. 76 A N ATOM 1390 CE1 HIS A 240 3.319-6. 262 12.562 1. 00 37. 56 A C ATOM 1391 NE2 HIS A 240 4.441-6. 175 13.255 1.00 37.72 A N ATOM 1392 C HIS A 240 4.314-1. 959 9.019 1.00 34.69 A C ATOM 1393 O HIS A 240 3.420-1. 198 9.381 1. 00 34. 96 A 0 ATOM 1394 N PHE A 241 5.210-1. 621 8.101 1. 00 33. 71 A N ATOM 1395 CA PHE A 241 5.140-0. 308 7.478 1. 00 33. 82 A C ATOM 1396 CB PHE A 241 5.864 0.729 8.351 1. 00 31. 00 A C ATOM 1397 CG PHE A 241 7.353 0.544 8.422 1. 00 28. 85 A C ATOM 1398 CD1 PHE A 241 8.187 1.123 7.468 1. 00 28. 33 A C ATOM 1399 CD2 PHE A 241 7.928-0. 186 9.459 1. 00 28. 23 A C ATOM 1400 CE1 PHE A 241 9.578 0.983 7.551 1. 00 26. 80 A C ATOM 1401 CE2 PHE A 241 9.317-0. 334 9.549 1. 00 27. 55 A C ATOM 1402 CZ PHE A 241 10.141 0.255 8.591 1. 00 26. 58 A C ATOM 1403 C PHE A 241 5.692-0. 289 6.060 1. 00 34. 54 A C ATOM 1404 O PHE A 241 6.643-1. 002 5.738 1. 00 34. 88 A 0 ATOM 1405 N SER A 242 5.079 0.531 5.215 1. 00 35. 50 A N ATOM 1406 CA SER A 242 5.500 0.650 3.830 1. 00 37. 40 A C ATOM 1407 CB SER A 242 4.281 0.825 2.914 1.00 38.02 A C ATOM 1408 OG SER A 242 3.622 2.060 3.149 1. 00 39. 25 A 0 ATOM 1409 C SER A 242 6.435 1.838 3.669 1. 00 38. 30 A C ATOM 1410 O SER A 242 6.367 2.809 4.429 1. 00 38. 35 A O ATOM 1411 N GLY A 243 7.310 1.751 2.672 1. 00 38. 90 A N ATOM 1412 CA GLY A 243 8.250 2.822 2.416 1. 00 38. 29 A C ATOM 1413 C GLY A 243 9.316 2.904 3.487 1. 00 38. 49 A C ATOM 1414 O GLY A 243 9.416 2.030 4.349 1. 00 38. 52 A 0 ATOM 1415 N SER A 244 10.109 3.968 3.431 1. 00 38. 08 A N ATOM 1416 CA SER A 244 11.183 4.179 4.389 1. 00 37. 17 A C ATOM 1417 CB SER A 244 12.353 4.876 3.692 1. 00 38. 10 A C ATOM 1418 OG SER A 244 13.544 4.761 4.453 1.00 42.25 A O ATOM 1419 C SER A 244 10.686 5.026 5.565 1. 00 36. 05 A C ATOM 1420 O SER A 244 9.706 5.770 5.439 1. 00 35. 62 A 0 ATOM 1421 N LEU A 245 11.358 4.907 6.708 1. 00 33. 55 A N ATOM 1422 CA LEU A 245 10. 974 5.663 7.897 1. 00 31. 65 A C ATOM 1423 CB LEU A 245 11.630 5. 064 9.148 1. 00 30. 86 A C ATOM 1424 CG LEU A 245 11.076 3.750 9.701 1. 00 29. 98 A C ATOM 1425 CD1 LEU A 245 11.960 3.263 10.830 1. 00 30. 34 A C ATOM 1426 CD2 LEU A 245 9.656 3.947 10.186 1. 00 27. 14 A C ATOM 1427 C LEU A 245 11.333 7.147 7.811 1. 00 30. 46 A C ATOM 1428 0 LEU A 245 12.418 7.513 7.358 1. 00 28. 90 A O ATOM 1429 N ASN A 246 10.402 7.995 8.237 1. 00 29. 11 A N ATOM 1430 CA ASN A 246 10.627 9.432 8.254 1. 00 28. 29 A C ATOM 1431 CB ASN A 246 9.346 10.182 7.891 1. 00 28. 61 A C ATOM 1432 CG ASN A 246 8.911 9.924 6.461 1. 00 31. 25 A C ATOM 1433 OD1 ASN A 246 9.639 10.237 5.517 1. 00 32. 15 A 0 ATOM 1434 ND2 ASN A 246 7.727 9.347 6.293 1. 00 30. 48 A N ATOM 1435 C ASN A 246 11.041 9.751 9.684 1. 00 27. 38 A C ATOM 1436 O ASN A 246 10.323 9.416 10.628 1. 00 26. 43 A 0 ATOM 1437 N TRP A 247 12.209 10.367 9.847 1. 00 26. 14 A N ATOM 1438 CA TRP A 247 12.692 10.705 11.177 1. 00 25. 96 A C ATOM 1439 CB TRP A 247 14.195 10.464 11.289 1. 00 26. 04 A C ATOM 1440 CG TRP A 247 14.572 9.017 11.169 1. 00 28. 30 A C ATOM 1441 CD2 TRP A 247 14.365 7.988 12.149 1.00 27.29 A C ATOM 1442 CE2 TRP A 247 14.867 6.784 11.604 1.00 27.62 A C ATOM 1443 CE3 TRP A 247 13.804 7.966 13.435 1.00 27.55 A C ATOM 1444 CD1 TRP A 247 15.171 8.412 10.099 1.00 28. 13 A C ATOM 1445 NE1 TRP A 247 15.351 7.072 10.355 1.00 29.13 A N ATOM 1446 CZ2 TRP A 247 14.829 5.567 12.302 1. 00 26. 74 A C ATOM 1447 CZ3 TRP A 247 13.766 6.750 14.132 1. 00 26. 57 A C ATOM 1448 CH2 TRP A 247 14.277 5.572 13. 562 1.00 25.70 A C ATOM 1449 C TRP A 247 12.363 12.134 11.579 1.00 25.48 A C ATOM 1450 0 TRP A 247 12.442 13.067 10.773 1.00 24.73 A 0 ATOM 1451 N VAL A 248 11.986 12.273 12.846 1.00 24.23 A N ATOM 1452 CA VAL A 248 11.605 13.544 13.444 1. 00 22. 75 A C ATOM 1453 CB VAL A 248 10.116 13.541 13.846 1. 00 21. 92 A C ATOM 1454 CG1 VAL A 248 9.739 14.873 14.464 1. 00 20. 41 A C ATOM 1455 CG2 VAL A 248 9.258 13.218 12.642 1.00 20.31 A C ATOM 1456 C VAL A 248 12.420 13.701 14.706 1. 00 22. 54 A C ATOM 1457 O VAL A 248 12.461 12.800 15.537 1.00 23.15 A O ATOM 1458 N PRO A 249 13.077 14.850 14.876 1. 00 22. 18 A N ATOM 1459 CD PRO A 249 13.192 16.016 13.981 1. 00 21. 63 A C ATOM 1460 CA PRO A 249 13.875 15.032 16.086 1.00 21.62 A C ATOM 1461 CB PRO A 249 14.741 16.236 15.739 1. 00 21. 77 A C ATOM 1462 CG PRO A 249 13.811 17.061 14.893 1. 00 22. 65 A C ATOM 1463 C PRO A 249 13.025 15.281 17.326 1. 00 21. 10 A C ATOM 1464 0 PRO A 249 11.968 15.901 17.245 1. 00 20. 78 A O ATOM 1465 N VAL A 250 13.480 14.765 18.465 1. 00 20. 99 A N ATOM 1466 CA VAL A 250 12.794 14.980 19.734 1. 00 19. 80 A C ATOM 1467 CB VAL A 250 13.213 13.939 20.792 1. 00 20. 01 A C ATOM 1468 CG1 VAL A 250 12.767 14.387 22.179 1.00 19.84 A C ATOM 1469 CG2 VAL A 250 12.590 12.593 20.453 1.00 17.59 A C ATOM 1470 C VAL A 250 13.249 16.372 20.154 1.00 18.73 A C ATOM 1471 0 VAL A 250 14.446 16.639 20.238 1.00 19.53 A 0 ATOM 1472 N THR A 251 12.284 17.257 20.389 1. 00 18. 13 A N ATOM 1473 CA THR A 251 12.557 18.645 20.739 1.00 15.95 A C ATOM 1474 CB THR A 251 11.399 19.540 20. 288 1. 00 16. 04 A C ATOM 1475 OG1 THR A 251 10.183 19.102 20. 915 1. 00 16. 44 A 0 ATOM 1476 CG2 THR A 251 11.244 19.468 18.772 1.00 11.94 A C ATOM 1477 C THR A 251 12.826 18.903 22.203 1.00 16.62 A C ATOM 1478 0 THR A 251 13.569 19.817 22.545 1.00 18.58 A O ATOM 1479 N LYS A 252 12.216 18.103 23.066 1.00 17.15 A N ATOM 1480 CA LYS A 252 12.387 18.233 24.508 1. 00 18. 18 A C ATOM 1481 CB LYS A 252 11.241 19.060 25.100 1. 00 18. 26 A C ATOM 1482 CG LYS A 252 11.356 19.330 26.591 1. 00 21. 10 A C ATOM 1483 CD LYS A 252 10.106 20.034 27.118 1. 00 22. 45 A C ATOM 1484 CE LYS A 252 10.079 20.043 28.635 1. 00 24. 44 A C ATOM 1485 NZ LYS A 252 8.831 20.666 29.175 1. 00 27. 23 A N ATOM 1486 C LYS A 252 12.363 16.815 25.067 1. 00 18. 34 A C ATOM 1487 0 LYS A 252 11.352 16.127 24.959 1. 00 18. 09 A 0 ATOM 1488 N GLN A 253 13.477 16.385 25.659 1. 00 18. 05 A N ATOM 1489 CA GLN A 253 13.592 15.030 26.201 1.00 17.75 A C ATOM 1490 CB GLN A 253 15.065 14.620 26.253 1. 00 18. 46 A C ATOM 1491 CG GLN A 253 15.668 14.368 24.875 1. 00 19. 49 A C ATOM 1492 CD GLN A 253 17.184 14.362 24.879 1. 00 20. 89 A C ATOM 1493 OE1 GLN A 253 17.813 13.782 25.764 1. 00 22. 39 A O ATOM 1494 NE2 GLN A 253 17.780 15.002 23.878 1. 00 20. 59 A N ATOM 1495 C GLN A 253 12.942 14.783 27.556 1. 00 17. 59 A C ATOM 1496 O GLN A 253 13.596 14.849 28.588 1. 00 17. 55 A O ATOM 1497 N ALA A 254 11.645 14.491 27.520 1. 00 17. 84 A N ATOM 1498 CA ALA A 254 10.823 14.191 28.695 1.00 17.48 A C ATOM 1499 CB ALA A 254 10.147 15.457 29.204 1. 00 17. 22 A C ATOM 1500 C ALA A 254 9.797 13.232 28.092 1. 00 17. 32 A C ATOM 1501 O ALA A 254 9.890 12.011 28.250 1.00 17.34 A O ATOM 1502 N TYR A 255 8.817 13.791 27.396 1. 00 17. 22 A N ATOM 1503 CA TYR A 255 7.848 12.967 26.684 1.00 17.17 A C ATOM 1504 CB TYR A 255 6.573 13.750 26.369 1. 00 17. 71 A C ATOM 1505 CG TYR A 255 5.862 14.346 27.552 1. 00 18. 64 A C ATOM 1506 CD1 TYR A 255 5.218 13.538 28.483 1. 00 18. 13 A C ATOM 1507 CE1 TYR A 255 4.537 14.093 29.563 1. 00 19. 71 A C ATOM 1508 CD2 TYR A 255 5.813 15.730 27.729 1. 00 19. 54 A C ATOM 1509 CE2 TYR A 255 5.137 16.297 28.805 1.00 19.42 A C ATOM 1510 CZ TYR A 255 4.501 15.474 29.719 1. 00 20. 35 A C ATOM 1511 OH TYR A 255 3.832 16.028 30.785 1. 00 21. 41 A O ATOM 1512 C TYR A 255 8.590 12.788 25.365 1. 00 16. 41 A C ATOM 1513 O TYR A 255 9.691 13.327 25.188 1. 00 15. 28 A 0 ATOM 1514 N TRP A 256 8.018 12.035 24.440 1. 00 16. 30 A N ATOM 1515 CA TRP A 256 8.650 11.940 23.138 1. 00 17. 27 A C ATOM 1516 CB TRP A 256 8.331 10.614 22.461 1. 00 17. 01 A C ATOM 1517 CG TRP A 256 9.149 9.513 23.026 1. 00 16. 95 A C ATOM 1518 CD2 TRP A 256 10.434 9.085 22.562 1.00 16.57 A C ATOM 1519 CE2 TRP A 256 10.887 8.084 23.451 1.00 15.56 A C ATOM 1520 CE3 TRP A 256 11.249 9.453 21.481 1.00 17.65 A C ATOM 1521 CD1 TRP A 256 8.879 8.773 24.147 1. 00 15. 30 A C ATOM 1522 NE1 TRP A 256 9.920 7.915 24.407 1. 00 15. 82 A N ATOM 1523 CZ2 TRP A 256 12.119 7.447 23.294 1. 00 16. 39 A C ATOM 1524 CZ3 TRP A 256 12.482 8.818 21.326 1. 00 17. 30 A C ATOM 1525 CH2 TRP A 256 12.902 7.826 22.230 1.00 17.14 A C ATOM 1526 C TRP A 256 7.989 13.113 22.431 1.00 18.16 A C ATOM 1527 O TRP A 256 6.999 12.961 21.714 1. 00 18. 78 A 0 ATOM 1528 N GLN A 257 8.533 14.297 22.701 1. 00 18. 98 A N ATOM 1529 CA GLN A 257 8.020 15.557 22.173 1. 00 18. 48 A C ATOM 1530 CB GLN A 257 8.256 16.675 23.195 1. 00 17. 17 A C ATOM 1531 CG GLN A 257 7.361 17.895 23.015 1. 00 17. 40 A C ATOM 1532 CD GLN A 257 7.481 18.867 24.172 1.00 17.54 A C ATOM 1533 OE1 GLN A 257 7.474 18.456 25.331 1. 00 17. 68 A 0 ATOM 1534 NE2 GLN A 257 7.582 20.158 23.867 1. 00 14. 67 A N ATOM 1535 C GLN A 257 8.648 15.942 20.845 1.00 18.67 A C ATOM 1536 0 GLN A 257 9.867 15.873 20.670 1.00 17.86 A 0 ATOM 1537 N ILE A 258 7.792 16.364 19.920 1.00 19.15 A N ATOM 1538 CA ILE A 258 8.210 16.762 18.585 1. 00 19. 46 A C ATOM 1539 CB ILE A 258 7.805 15.691 17.546 1. 00 18. 66 A C ATOM 1540 CG2 ILE A 258 8.519 14.374 17.835 1.00 15.98 A C ATOM 1541 CG1 ILE A 258 6.286 15.485 17.585 1.00 18.26 A C ATOM 1542 CD1 ILE A 258 5.755 14.646 16.429 1.00 17.46 A C ATOM 1543 C ILE A 258 7.541 18.084 18.205 1.00 20.88 A C ATOM 1544 O ILE A 258 6.703 18.609 18.947 1.00 20.22 A. O ATOM 1545 N ALA A 259 7.904 18.612 17.039 1.00 21.49 A N ATOM 1546 CA ALA A 259 7.333 19.866 16.561 1. 00 20. 96 A C ATOM 1547 CB ALA A 259 8.443 20.841 16.200 1.00 21.02 A C ATOM 1548 C ALA A 259 6.440 19.647 15.350 1.00 21.76 A C ATOM 1549 0 ALA A 259 6.779 18.875 14.448 1.00 21.50 A 0 ATOM 1550 N LEU A 260 5.293 20.320 15.345 1.00 22.26 A N ATOM 1551 CA LEU A 260 4.358 20.251 14.229 1. 00 23. 13 A C ATOM 1552 CB LEU A 260 2. 907 20.239 14.714 1.00 22.82 A C ATOM 1553 CG LEU A 260 2.326 19.129 15.581 1. 00 24. 01 A C ATOM 1554 CD1 LEU A 260 0.861 19.459 15.865 1.00 21.61 A C ATOM 1555 CD2 LEU A 260 2.452 17.787 14.869 1.00 24.36 A C ATOM 1556 C LEU A 260 4.559 21.527 13.415 1.00 24.08 A C ATOM 1557 0 LEU A 260 4.673 22.612 13.984 1.00 23.78 A O ATOM 1558 N ASP A 261 4.603 21.404 12.092 1.00 25.52 A N ATOM 1559 CA ASP A 261 4.758 22.578 11.243 1.00 27.21 A C ATOM 1560 CB ASP A 261 5.174 22.186 9.824 1.00 27.73 A C ATOM 1561 CG ASP A 261 6.560 21.595 9.767 1.00 28.44 A C ATOM 1562 OD1 ASP A 261 7.479 22.177 10.372 1.00 29.24 A O ATOM 1563 OD2 ASP A 261 6.733 20.550 9.111 1.00 30.85 A O ATOM 1564 C ASP A 261 3.416 23.280 11.184 1.00 27.96 A C ATOM 1565 0 ASP A 261 3.335 24.507 11.259 1.00 29.62 A O ATOM 1566 N ASN A 262 2.364 22.481 11.043 1.00 28.21 A N ATOM 1567 CA ASN A 262 1.001 22.986 10.970 1.00 28.70 A C ATOM 1568 CB ASN A 262 0.830 23.916 9.755 1.00 28.46 A C ATOM 1569 CG ASN A 262 1.187 23.238 8.434 1.00 28.68 A C ATOM 1570 OD1 ASN A 262 2.130 23.646 7.747 1.00 28.36 A O ATOM 1571 ND2 ASN A 262 0.438 22.198 8.074 1.00 28.45 A N ATOM 1572 C ASN A 262 0.030 21.821 10.854 1.00 29.08 A C ATOM 1573 O ASN A 262 0.425 20.698 10.533 1.00 29.58 A O ATOM 1574 N ILE A 263-1.237 22.097 11.133 1.00 29.97 A N ATOM 1575 CA ILE A 263-2.292 21.099 11.034 1.00 30.87 A C ATOM 1576 CB ILE A 263-2.996 20.872 12.381 1.00 30.00 A C ATOM 1577 CG2 ILE A 263-4.117 19.855 12.212 1.00 29.26 A C ATOM 1578 CG1 ILE A 263-1.985 20.392 13.426 1.00 29.05 A C ATOM 1579 CD1 ILE A 263-2.532 20.369 14.838 1.00 28.24 A C ATOM 1580 C ILE A 263-3.303 21.677 10.057 1.00 32.64 A C ATOM 1581 O ILE A 263-3.730 22.822 10.203 1.00 33.17 A O ATOM 1582 N GLN A 264-3. 684 20.902 9.053 1.00 34.05 A N ATOM 1583 CA GLN A 264-4.644 21.401 8.089 1.00 35.88 A C ATOM 1584 CB GLN A 264-3. 959 21.641 6.740 1.00 36.94 A C ATOM 1585 CG GLN A 264-3. 158 20.469 6. 212 1.00 38.92 A C ATOM 1586 CD GLN A 264-2. 321 20.849 5.002 1.00 40.77 A C ATOM 1587 OE1 GLN A 264-1. 466 21.734 5.080 1.00 40.57 A O ATOM 1588 NE2 GLN A 264-2.563 20.181 3.875 1.00 41.59 A N ATOM 1589 C GLN A 264-5. 840 20.490 7.910 1.00 36.52 A C ATOM 1590 0 GLN A 264-5. 756 19.277 8.128 1.00 37.04 A O ATOM 1591 N VAL A 265-6. 963 21.101 7.540 1.00 37.10 A N ATOM 1592 CA VAL A 265-8. 204 20.380 7.282 1.00 37.14 A C ATOM 1593 CB VAL A 265-9. 357 20.865 8.185 1.00 36.48 A C ATOM 1594 CG1 VAL A 265-10. 590 20.013 7.937 1. 00 36. 48 A C ATOM 1595 CG2 VAL A 265-8. 948 20.797 9.651 1.00 35.81 A C ATOM 1596 C VAL A 265-8. 556 20.687 5.832 1. 00 37. 94 A C ATOM 1597 O VAL A 265-8. 381 21.816 5.369 1. 00 37. 61 A O ATOM 1598 N GLY A 266-9. 036 19.682 5.112 1. 00 38. 83 A N ATOM 1599 CA GLY A 266-9. 383 19.891 3.721 1. 00 39. 67 A C ATOM 1600 C GLY A 266-8. 251 20.531 2.937 1.00 40.27 A C ATOM 1601 O GLY A 266-8. 484 21.405 2.103 1.00 41.39 A 0 ATOM 1602 N GLY A 267-7. 022 20.106 3.215 1.00 40.37 A N ATOM 1603 CA GLY A 267-5.864 20.635 2. 512 1.00 39.69 A C ATOM 1604 C GLY A 267-5. 550 22.098 2.766 1. 00 39. 89 A C ATOM 1605 O GLY A 267-4.802 22.717 2.011 1. 00 39. 52 A 0 ATOM 1606 N THR A 268-6. 117 22.661 3.827 1.00 40.01 A N ATOM 1607 CA THR A 268-5. 868 24.058 4.159 1.00 39.36 A C ATOM 1608 CB THR A 268-7. 125 24.915 3.882 1.00 40.71 A C ATOM 1609 OG1 THR A 268-7. 395 24.911 2.472 1.00 42.88 A O ATOM 1610 CG2 THR A 268-6. 922 26.352 4.350 1.00 40.22 A C ATOM 1611 C THR A 268-5. 442 24.207 5.620 1.00 38.58 A C ATOM 1612 0 THR A 268-6. 097 23.687 6.526 1.00 37.40 A 0 ATOM 1613 N VAL A 269-4. 332 24.910 5.837 1.00 37.93 A N ATOM 1614 CA VAL A 269-3. 803 25.134 7.179 1.00 37.43 A C ATOM 1615 CB VAL A 269-2. 575 26.058 7.151 1.00 36.43 A C ATOM 1616 CG1 VAL A 269-2. 116 26.351 8.573 1.00 34.58 A C ATOM 1617 CG2 VAL A 269-1. 463 25.413 6.337 1.00 35.67 A C ATOM 1618 C VAL A 269-4. 865 25.779 8.049 1.00 38.15 A C ATOM 1619 0 VAL A 269-5. 458 26.789 7.669 1. 00 38. 95 A 0 ATOM 1620 N MET A 270-5.096 25.208 9.224 1.00 38.08 A N ATOM 1621 CA MET A 270-6. 114 25.736 10.113 1.00 39.07 A C ATOM 1622 CB MET A 270-7.332 24.814 10.084 1.00 40.56 A C ATOM 1623 CG MET A 270-8.554 25.359 10.789 1.00 42.85 A C ATOM 1624 SD MET A 270-9.989 24.307 10.504 1.00 45.56 A S ATOM 1625 CE MET A 270-10.228 24.554 8.748 1.00 43.18 A C ATOM 1626 C MET A 270-5.621 25.916 11.542 1.00 38.80 A C ATOM 1627 O MET A 270-6.187 26.697 12.301 1.00 39.76 A O ATOM 1628 N PHE A 271-4. 570 25.194 11.913 1. 00 38. 75 A N ATOM 1629 CA PHE A 271-4. 017 25.309 13.260 1.00 38.63 A C ATOM 1630 CB PHE A 271-4. 541 24.193 14.173 1. 00 38. 66 A C ATOM 1631 CG PHE A 271-6. 036 24.076 14.203 1.00 38.50 A C ATOM 1632 CD1 PHE A 271-6.675 23.045 13.524 1.00 37.61 A C ATOM 1633 CD2 PHE A 271-6.806 24.993 14.911 1.00 38.67 A C ATOM 1634 CE1 PHE A 271-8.061 22.928 13.549 1.00 38.26 A C ATOM 1635 CE2 PHE A 271-8. 195 24.885 14.941 1. 00 38. 38 A C ATOM 1636 CZ PHE A 271-8. 823 23.848 14.258 1. 00 37. 93 A C ATOM 1637 C PHE A 271-2. 501 25.228 13.232 1.00 38.36 A C ATOM 1638 O PHE A 271-1. 920 24.689 12.290 1. 00 37. 83 A O ATOM 1639 N CYS A 272-1. 866 25.759 14.273 1. 00 38. 65 A N ATOM 1640 CA CYS A 272-0. 410 25.719 14.384 1. 00 39. 61 A C ATOM 1641 C CYS A 272 0.245 26.185 13.100 1. 00 39. 02 A C ATOM 1642 O CYS A 272 1.277 25.651 12.695 1. 00 38. 76 A O ATOM 1643 CB CYS A 272 0.048 24.290 14.696 1.00 40.12 A C ATOM 1644 SG CYS A 272-0. 558 23.672 16.294 1.00 43.96 A S ATOM 1645 N SER A 273-0.363 27.176 12.458 1. 00 39. 32 A N ATOM 1646 CA SER A 273 0.160 27.709 11.206 1. 00 38. 72 A C ATOM 1647 CB SER A 273-0.671 28.912 10.764 1. 00 38. 66 A C ATOM 1648 OG SER A 273-0.755 29.874 11.797 1. 00 39. 05 A O ATOM 1649 C SER A 273 1.622 28. 108 11.362 1. 00 38. 56 A C ATOM 1650 0 SER A 273 2.403 28.024 10.414 1. 00 38. 29 A O ATOM 1651 N GLU A 274 1.986 28.525 12.570 1.00 38.16 A N ATOM 1652 CA GLU A 274 3.351 28.935 12.861 1. 00 39. 00 A C ATOM 1653 CB GLU A 274 3.335 30.258 13.631 1.00 42.14 A C ATOM 1654 CG GLU A 274 2.527 31.356 12.937 1.00 47.15 A C ATOM 1655 CD GLU A 274 2.417 32.630 13.763 1. 00 50. 29 A C ATOM 1656 OE1 GLU A 274 3.459 33.287 14.000 1.00 51.41 A O ATOM 1657 OE2 GLU A 274 1.284 32.972 14.177 1.00 51.66 A O ATOM 1658 C GLU A 274 4.077 27.859 13.667 1. 00 37. 45 A C ATOM 1659 0 GLU A 274 5.108 28.117 14.279 1. 00 36. 78 A 0 ATOM 1660 N GLY A 275 3.528 26.650 13.660 1. 00 35. 96 A N ATOM 1661 CA GLY A 275 4.141 25.554 14.385 1. 00 34. 49 A C ATOM 1662 C GLY A 275 3.783 25.488 15.859 1. 00 33. 47 A C ATOM 1663 O GLY A 275 3.537 26.504 16.499 1. 00 34. 20 A 0 ATOM 1664 N CYS A 276 3.745 24.276 16.395 1. 00 33. 29 A N ATOM 1665 CA CYS A 276 3.441 24. 061 17.804 1. 00 33. 14 A C ATOM 1666 C CYS A 276 4.067 22.738 18.236 1. 00 30. 72 A C ATOM 1667 0 CYS A 276 4.557 21.971 17.408 1. 00 28. 75 A 0 ATOM 1668 CB CYS A 276 1.927 24.035 18.045 1. 00 35. 92 A C ATOM 1669 SG CYS A 276 1.052 22.733 17.123 1. 00 42. 56 A S ATOM 1670 N GLN A 277 4.055 22.475 19.536 1. 00 28. 92 A N ATOM 1671 CA GLN A 277 4.644 21. 254 20.059 1. 00 26. 42 A C ATOM 1672 CB GLN A 277 5.353 21.561 21.380 1. 00 26. 63 A C ATOM 1673 CG GLN A 277 6.560 22.494 21.256 1. 00 25. 83 A C ATOM 1674 CD GLN A 277 7.780 21.808 20.654 1.00 26.43 A C ATOM 1675 OE1 GLN A 277 8.173 20.722 21.091 1.00 23.67 A 0 ATOM 1676 NE2 GLN A 277 8.392 22.446 19.653 1. 00 24. 41 A N ATOM 1677 C GLN A 277 3.622 20.133 20.265 1. 00 25. 57 A C ATOM 1678 0 GLN A 277 2.456 20.388 20.564 1. 00 24. 40 A O ATOM 1679 N ALA A 278 4.076 18.892 20.095 1. 00 24. 57 A N ATOM 1680 CA ALA A 278 3.233 17.713 20.281 1. 00 23. 28 A C ATOM 1681 CB ALA A 278 2.582 17.309 18.967 1. 00 22. 35 A C ATOM 1682 C ALA A 278 4.060 16.549 20.820 1. 00 22. 58 A C ATOM 1683 O ALA A 278 5.293 16.610 20.858 1. 00 21. 65 A 0 ATOM 1684 N ILE A 279 3.376 15.492 21.247 1. 00 21. 74 A N ATOM 1685 CA ILE A 279 4.055 14.313 21.760 1. 00 21. 66 A C ATOM 1686 CB ILE A 279 4.015 14.238 23.325 1.00 19.94 A C ATOM 1687 CG2 ILE A 279 4.515 15.541 23.931 1. 00 19. 10 A C ATOM 1688 CG1 ILE A 279 2.596 13.966 23.816 1. 00 19. 64 A C ATOM 1689 CD1 ILE A 279 2.488 13.863 25.332 1. 00 17. 28 A C ATOM 1690 C ILE A 279 3.374 13.080 21.178 1. 00 22. 21 A C ATOM 1691 0 ILE A 279 2. 168 13.100 20.910 1. 00 22. 41 A O ATOM 1692 N VAL A 280 4.157 12.025 20.959 1. 00 20. 99 A N ATOM 1693 CA VAL A 280 3.643 10.774 20.428 1. 00 20. 34 A C ATOM 1694 CB VAL A 280 4.651 10.149 19.458 1. 00 20. 47 A C ATOM 1695 CG1 VAL A 280 4.035 8.949 18.762 1. 00 20. 04 A C ATOM 1696 CG2 VAL A 280 5.074 11.192 18.431 1. 00 19. 83 A C ATOM 1697 C VAL A 280 3.446 9.904 21.659 1. 00 21. 26 A C ATOM 1698 O VAL A 280 4.406 9.414 22.246 1. 00 20. 96 A 0 ATOM 1699 N ASP A 281 2.187 9.727 22.050 1. 00 22. 89 A N ATOM 1700 CA ASP A 281 1.856 8.990 23.265 1. 00 22. 70 A C ATOM 1701 CB ASP A 281 1.218 9.963 24.256 1. 00 22. 29 A C ATOM 1702 CG ASP A 281 0.829 9.300 25.555 1. 00 24. 98 A C ATOM 1703 OD1 ASP A 281 1.346 8.194 25.831 1. 00 25. 10 A 0 ATOM 1704 OD2 ASP A 281 0.015 9.892 26.303 1. 00 24. 92 A 0 ATOM 1705 C ASP A 281 0.972 7.757 23.120 1. 00 22. 34 A C ATOM 1706 O ASP A 281-0. 226 7.858 22.876 1. 00 22. 99 A 0 ATOM 1707 N THR A 282 1.574 6.590 23.311 1. 00 21. 38 A N ATOM 1708 CA THR A 282 0.861 5.328 23.215 1. 00 20. 20 A C ATOM 1709 CB THR A 282 1.836 4.141 23.292 1. 00 19. 91 A C ATOM 1710 OG1 THR A 282 2.674 4.281 24.449 1. 00 20. 45 A O ATOM 1711 CG2 THR A 282 2.700 4.083 22.049 1. 00 18. 14 A C ATOM 1712 C THR A 282-0. 171 5.185 24.327 1. 00 20. 85 A C ATOM 1713 0 THR A 282-1. 121 4.414 24.198 1.00 20.58 A 0 ATOM 1714 N GLY A 283 0.010 5.935 25.410 1. 00 21. 07 A N ATOM 1715 CA GLY A 283-0. 916 5.862 26.529 1. 00 21. 74 A C ATOM 1716 C GLY A 283-2. 186 6.667 26.336 1. 00 22. 86 A c ATOM 1717 O GLY A 283-3. 109 6.591 27.148 1. 00 23. 04 A o ATOM 1718 N THR A 284-2. 232 7.456 25.269 1. 00 23. 13 A N ATOM 1719 CA THR A 284-3. 408 8.263 24.970 1. 00 22. 88 A C ATOM 1720 CB THR A 284-3. 003 9.696 24.575 1.00 23.26 A C ATOM 1721 OG1 THR A 284-2. 428 10.349 25.714 1.00 20.91 A 0 ATOM 1722 CG2 THR A 284-4. 212 10.490 24.072 1.00 20.87 A C ATOM 1723 C THR A 284-4. 166 7.597 23. 825 1. 00 24. 09 A C ATOM 1724 O THR A 284-3. 589 7.292 22.777 1. 00 24. 80 A O ATOM 1725 N SER A 285-5.458 7.374 24.037 1.00 23.97 A N ATOM 1726 CA SER A 285-6.311 6.714 23.057 1. 00 25. 14 A C ATOM 1727 CB SER A 285-7.662 6.382 23.698 1. 00 25. 74 A C ATOM 1728 OG SER A 285-7.488 5.650 24.898 1. 00 28. 81 A O ATOM 1729 C SER A 285-6.558 7.489 21.768 1. 00 24. 60 A C ATOM 1730 O SER A 285-6.403 6.965 20.668 1. 00 24. 94 A O ATOM 1731 N LEU A 286-6.953 8.742 21.907 1.00 25.83 A N ATOM 1732 CA LEU A 286-7. 261 9.565 20.750 1. 00 27. 15 A C ATOM 1733 CB LEU A 286-8.551 10.344 21.028 1. 00 27. 49 A C ATOM 1734 CG LEU A 286-9.698 9.488 21.580 1. 00 28. 94 A C ATOM 1735 CD1 LEU A 286-10. 926 10.356 21.829 1. 00 29. 39 A C ATOM 1736 CD2 LEU A 286-10. 017 8.371 20.596 1. 00 29. 09 A C ATOM 1737 C LEU A 286-6.145 10.542 20.415 1.00 27.12 A C ATOM 1738 O LEU A 286-5.008 10.392 20.860 1.00 28.46 A 0 ATOM 1739 N ILE A 287-6. 480 11.529 19.595 1. 00 26. 31 A N ATOM 1740 CA ILE A 287-5.543 12.578 19.242 1. 00 26. 14 A C ATOM 1741 CB ILE A 287-5.568 12.899 17.733 1. 00 25. 76 A C ATOM 1742 CG2 ILE A 287-4.807 14.182 17.465 1. 00 26. 29 A C ATOM 1743 CG1 ILE A 287-4.954 11.748 16.941 1. 00 25. 41 A C ATOM 1744 CD1 ILE A 287 -4. 955 11.965 15.438 1.00 25.43 A C ATOM 1745 C ILE A 287-6.107 13.756 20.018 1. 00 26. 05 A C ATOM 1746 O ILE A 287-7.265 14.129 19.825 1.00 25.33 A 0 ATOM 1747 N THR A 288-5. 314 14.320 20. 921 1. 00 25. 66 A N ATOM 1748 CA THR A 288 -5. 800 15.446 21.703 1. 00 25. 30 A C ATOM 1749 CB THR A 288-5. 646 15.194 23.217 1. 00 24. 54 A C ATOM 1750 OG1 THR A 288-4. 257 15.162 23.565 1.00 23.71 A O ATOM 1751 CG2 THR A 288-6. 291 13.875 23.598 1.00 23.13 A C ATOM 1752 C THR A 288-5. 109 16.756 21.360 1. 00 25. 47 A C ATOM 1753 O THR A 288-4. 113 16.788 20.635 1. 00 26. 04 A O ATOM 1754 N GLY A 289-5. 657 17.839 21.892 1. 00 25. 57 A N ATOM 1755 CA GLY A 289 -5. 098 19.151 21.655 1. 00 25. 71 A C ATOM 1756 C GLY A 289-5.820 20.141 22. 540 1. 00 25. 66 A C ATOM 1757 0 GLY A 289-6. 738 19.754 23.266 1.00 25.67 A O ATOM 1758 N PRO A 290-5.417 21.419 22.528 1. 00 25. 75 A N ATOM 1759 CD PRO A 290-4.304 22.020 21.773 1. 00 25. 79 A C ATOM 1760 CA PRO A 290-6.086 22.420 23.359 1.00 26.14 A C ATOM 1761 CB PRO A 290-5.480 23.727 22.868 1.00 25.68 A C ATOM 1762 CG PRO A 290-4.080 23.313 22.522 1. 00 26. 70 A C ATOM 1763 C PRO A 290-7.581 22.328 23.083 1. 00 26. 63 A C ATOM 1764 0 PRO A 290-8.018 22.370 21.930 1. 00 26. 11 A O ATOM 1765 N SER A 291-8.355 22.187 24.150 1. 00 27. 10 A N ATOM 1766 CA SER A 291-9.800 22.048 24.049 1. 00 28. 27 A C ATOM 1767 CB SER A 291-10. 421 22.188 25.437 1. 00 27. 09 A C ATOM 1768 OG SER A 291-9.956 23.367 26.069 1. 00 28. 72 A 0 ATOM 1769 C SER A 291-10.477 23.005 23.074 1. 00 28. 81 A C ATOM 1770 O SER A 291-11. 371 22. 597 22.334 1. 00 28. 29 A 0 ATOM 1771 N ASP A 292-10. 058 24.267 23.061 1. 00 30. 59 A N ATOM 1772 CA ASP A 292-10. 666 25.246 22.162 1.00 32.61 A C ATOM 1773 CB ASP A 292-10.177 26.668 22. 486 1.00 34.64 A C ATOM 1774 CG ASP A 292-8.661 26.811 22.405 1.00 37.56 A C ATOM 1775 OD1 ASP A 292-8. 181 27.960 22.291 1.00 38.40 A O ATOM 1776 OD2 ASP A 292-7. 947 25.786 22.468 1.00 38.44 A 0 ATOM 1777 C ASP A 292-10. 408 24.927 20.692 1.00 33.17 A C ATOM 1778 O ASP A 292-11. 322 25.005 19. 868 1.00 33.88 A 0 ATOM 1779 N LYS A 293-9. 169 24.561 20.363 1.00 33.25 A N ATOM 1780 CA LYS A 293-8. 815 24.224 18.987 1.00 33.09 A C ATOM 1781 CB LYS A 293-7. 309 23.949 18.865 1.00 34.53 A C ATOM 1782 CG LYS A 293-6. 377 25.011 19.465 1.00 36.13 A C ATOM 1783 CD LYS A 293-6.110 26.196 18.540 1.00 37.43 A C ATOM 1784 CE LYS A 293-7.268 27.177 18.518 1.00 39.84 A C ATOM 1785 NZ LYS A 293-6.937 28.405 17.737 1.00 41.64 A N ATOM 1786 C LYS A 293-9.585 22. 976 18.548 1.00 32.66 A C ATOM 1787 0 LYS A 293-10. 024 22.882 17.404 1.00 33.11 A 0 ATOM 1788 N ILE A 294-9. 746 22. 018 19.459 1. 00 31. 81 A N ATOM 1789 CA ILE A 294-10. 460 20.786 19.141 1.00 31.86 A C ATOM 1790 CB ILE A 294-10. 416 19.779 20.312 1.00 30.90 A C ATOM 1791 CG2 ILE A 294-11. 284 18.570 19.987 1.00 28.98 A C ATOM 1792 CG1 ILE A 294-8. 972 19.332 20.565 1.00 30.19 A C ATOM 1793 CD1 ILE A 294-8. 330 18.616 19.390 1.00 27.20 A C ATOM 1794 C ILE A 294-11. 913 21.048 18.768 1.00 32.76 A C ATOM 1795 O ILE A 294-12. 433 20.428 17.841 1. 00 32. 12 A 0 ATOM 1796 N LYS A 295-12.575 21.951 19.491 1.00 33.99 A N ATOM 1797 CA LYS A 295-13.963 22.282 19.173 1.00 35.42 A C ATOM 1798 CB LYS A 295-14.494 23.370 20.111 1.00 36.84 A C ATOM 1799 CG LYS A 295-14.718 22.895 21.540 1.00 41. 18 A C ATOM 1800 CD LYS A 295-15.194 24.025 22.444 1.00 43.75 A C ATOM 1801 CE LYS A 295-15.392 23.539 23.876 1.00 45.78 A C ATOM 1802 NZ LYS A 295-15.857 24.630 24.789 1.00 47.45 A N ATOM 1803 C LYS A 295-14.005 22.778 17.728 1.00 35.19 A C ATOM 1804 0 LYS A 295-14.843 22.343 16.933 1.00 34.20 A O ATOM 1805 N GLN A 296-13. 087 23.679 17.389 1.00 34.58 A N ATOM 1806 CA GLN A 296-13.021 24.206 16.033 1.00 34.66 A C ATOM 1807 CB GLN A 296-11. 895 25.229 15.906 1.00 35.67 A C ATOM 1808 CG GLN A 296-12.050 26.463 16.768 1.00 38.32 A C ATOM 1809 CD GLN A 296-10.974 27.487 16. 472 1.00 40.93 A C ATOM 1810 OE1 GLN A 296-10.857 27.971 15.344 1.00 42.75 A O ATOM 1811 NE2 GLN A 296-10.176 27.820 17.480 1.00 42.25 A N ATOM 1812 C GLN A 296-12. 778 23.069 15. 045 1.00 33.95 A C ATOM 1813 0 GLN A 296-13.280 23.095 13.919 1.00 34.01 A O ATOM 1814 N LEU A 297-11. 999 22.076 15.466 1.00 32.67 A N ATOM 1815 CA LEU A 297-11.700 20.937 14.609 1. 00 31.86 A C ATOM 1816 CB LEU A 297-10.490 20.170 15.146 1.00 31.21 A C ATOM 1817 CG LEU A 297-10.085 18.947 14.317 1.00 30.45 A C ATOM 1818 CD1 LEU A 297-9.956 19. 349 12.862 1.00 29.77 A C ATOM 1819 CD2 LEU A 297-8. 775 18.373 14.840 1.00 30.63 A C ATOM 1820 C LEU A 297-12. 899 19.996 14.498 1.00 32.27 A C ATOM 1821 0 LEU A 297-13.151 19.413 13.441 1.00 30.63 A O ATOM 1822 N GLN A 298-13.631 19.855 15.596 1.00 33.37 A N ATOM 1823 CA GLN A 298-14. 804 18.992 15.636 1.00 35.19 A C ATOM 1824 CB GLN A 298-15.412 19.007 17.041 1.00 34.60 A C ATOM 1825 CG GLN A 298-14.480 18.475 18.122 1.00 33.41 A C ATOM 1826 CD GLN A 298-14.296 16.970 18.054 1.00 32.93 A C ATOM 1827 OE1 GLN A 298-14.356 16.370 16.982 1.00 32.14 A O ATOM 1828 NE2 GLN A 298-14.056 16.354 19.203 1.00 32.97 A N ATOM 1829 C GLN A 298-15.860 19.410 14.609 1.00 36.87 A C ATOM 1830 0 GLN A 298-16.297 18.599 13.793 1.00 37. 36 A O ATOM 1831 N ASN A 299-16.266 20.674 14.629 1.00 38.39 A N ATOM 1832 CA ASN A 299-17.283 21.116 13.682 1.00 40.48 A C ATOM 1833 CB ASN A 299-17.986 22.379 14.203 1.00 42.56 A C ATOM 1834 CG ASN A 299-17.019 23.436 14.680 1.00 43.62 A C ATOM 1835 OD1 ASN A 299-17.379 24. 301 15.479 1.00 43.65 A 0 ATOM 1836 ND2 ASN A 299-15.788 23.383 14.185 1.00 45.23 A N ATOM 1837 C ASN A 299-16.754 21.319 12.265 1.00 40.34 A C ATOM 1838 0 ASN A 299-17.529 21.372 11.312 1.00 40.49 A O ATOM 1839 N ALA A 300-15.437 21. 412 12.121 1.00 40.54 A N ATOM 1840 CA ALA A 300-14.839 21.572 10.800 1.00 41.01 A C ATOM 1841 CB ALA A 300-13.388 22.011 10.929 1.00 40.21 A C ATOM 1842 C ALA A 300-14.921 20.238 10.056 1.00 42.36 A C ATOM 1843 0 ALA A 300-15.068 20.209 8.833 1.00 42.09 A 0 ATOM 1844 N ILE A 301-14. 826 19. 135 10.799 1.00 43.34 A N ATOM 1845 CA ILE A 301-14.899 17.805 10.202 1.00 45.30 A C ATOM 1846 CB ILE A 301-14.076 16.754 10.993 1.00 45.06 A C ATOM 1847 CG2 ILE A 301-12.606 17.127 10.979 1.00 44.19 A C ATOM 1848 CG1 ILE A 301-14. 608 16.637 12.423 1.00 44.86 A C ATOM 1849 CD1 ILE A 301-13.942 15.553 13.244 1.00 44.69 A C ATOM 1850 C ILE A 301-16. 343 17.331 10.148 1.00 46.88 A c ATOM 1851 O ILE A 301-16. 674 16.418 9.389 1.00 47.35 A O ATOM 1852 N GLY A 302-17. 195 17.948 10.962 1. 00 48. 37 A N ATOM 1853 CA GLY A 302-18. 601 17.582 10.974 1. 00 50. 33 A C ATOM 1854 C GLY A 302-19. 053 16.790 12.185 1. 00 51. 72 A C ATOM 1855 O GLY A 302-20. 055 16.075 12.124 1. 00 51. 77 A O ATOM 1856 N ALA A 303-18.321 16.910 13.286 1. 00 53. 22 A N ATOM 1857 CA ALA A 303-18.666 16.195 14.509 1. 00 54. 79 A C ATOM 1858 CB ALA A 303-17.411 15.900 15.321 1. 00 54. 96 A C ATOM 1859 C ALA A 303-19.638 17.026 15.331 1. 00 55. 80 A C ATOM 1860 O ALA A 303-19.659 18.251 15.230 1. 00 55. 89 A 0 ATOM 1861 N ALA A 304-20.441 16.356 16.148 1. 00 57. 75 A N ATOM 1862 CA ALA A 304-21.418 17.051 16.973 1. 00 59. 99 A C ATOM 1863 CB ALA A 304-22.810 16.915 16.351 1.00 60. 15 A C ATOM 1864 C ALA A 304-21.436 16.538 18.409 1.00 61.30 A C ATOM 1865 O ALA A 304-21.259 15.344 18.659 1.00 61.45 A 0 ATOM 1866 N PRO A 305-21.650 17.443 19.374 1.00 62.84 A N ATOM 1867 CD PRO A 305-21.691 18.907 19.218 1.00 62.90 A C ATOM 1868 CA PRO A 305-21.693 17.074 20.791 1.00 64.62 A C ATOM 1869 CB PRO A 305-21.869 18.418 21.493 1.00 63.86 A C ATOM 1870 CG PRO A 305-21.197 19.376 20.561 1.00 63.49 A C ATOM 1871 C PRO A 305-22.849 16.123 21.082 1.00 66.49 A C ATOM 1872 O PRO A 305-23.894 16.185 20.432 1.00 66.52 A O ATOM 1873 N VAL A 306-22. 651 15.240 22.055 1.00 68.85 A N ATOM 1874 CA VAL A 306-23. 676 14.279 22.446 1. 00 71. 37 A C ATOM 1875 CB VAL A 306-23. 359 12.858 21.902 1. 00 71. 57 A C ATOM 1876 CG1 VAL A 306-24.584 11.962 22.028 1.00 72.03 A C ATOM 1877 CG2 VAL A 306-22.913 12.939 20.451 1.00 72.05 A C ATOM 1878 C VAL A 306-23. 720 14.243 23.975 1. 00 72. 93 A C ATOM 1879 0 VAL A 306-23. 720 15.291 24.625 1. 00 73. 01 A O ATOM 1880 N ASP A 307-23. 754 13.042 24.547 1. 00 74. 56 A N ATOM 1881 CA ASP A 307-23. 786 12.895 25. 996 1. 00 76. 05 A C ATOM 1882 CB ASP A 307-23. 877 11.415 26.385 1. 00 76. 62 A C ATOM 1883 CG ASP A 307-25. 188 10.773 25.956 1. 00 77. 46 A C ATOM 1884 OD1 ASP A 307-26.262 11.274 26.360 1.00 77.09 A 0 ATOM 1885 OD2 ASP A 307-25.143 9.763 25.219 1.00 77.62 A 0 ATOM 1886 C ASP A 307-22. 516 13.504 26.577 1. 00 76. 72 A C ATOM 1887 0 ASP A 307-22. 569 14.311 27.507 1. 00 77. 10 A O ATOM 1888 N GLY A 308-21. 377 13.115 26.012 1. 00 77. 05 A N ATOM 1889 CA GLY A 308-20. 100 13.626 26.477 1. 00 77. 32 A C ATOM 1890 C GLY A 308-19. 015 13.485 25.425 1. 00 77. 44 A C ATOM 1891 O GLY A 308-17. 898 13.977 25.599 1. 00 77. 39 A O ATOM 1892 N GLU A 309-19. 345 12.809 24.328 1.00 77.21 A N ATOM 1893 CA GLU A 309-18. 397 12.598 23.239 1. 00 76. 67 A C ATOM 1894 CB GLU A 309-18. 201 11.097 22.988 1. 00 77. 94 A C ATOM 1895 CG GLU A 309-18. 839 10.178 24.033 1. 00 80. 14 A C ATOM 1896 CD GLU A 309-18. 322 10.423 25.443 1. 00 81. 44 A C ATOM 1897 OE1 GLU A 309-17.093 10.335 25.657 1.00 81.96 A O ATOM 1898 OE2 GLU A 309-19.147 10.700 26.341 1.00 82.16 A 0 ATOM 1899 C GLU A 309-18. 915 13.261 21.966 1. 00 75. 31 A C ATOM 1900 0 GLU A 309-20. 053 13.726 21.920 1. 00 75. 31 A 0 ATOM 1901 N TYR A 310-18. 076 13.314 20.937 1. 00 73. 62 A N ATOM 1902 CA TYR A 310-18. 483 13.907 19.670 1. 00 71. 78 A C ATOM 1903 CB TYR A 310-17. 395 14.840 19.130 1. 00 71. 35 A C ATOM 1904 CG TYR A 310-17. 308 16.159 19.861 1. 00 70. 68 A C ATOM 1905 CD1 TYR A 310-16.809 16.227 21.162 1.00 70.53 A C ATOM 1906 CE1 TYR A 310-16.745 17.440 21.845 1.00 70.04 A C ATOM 1907 CD2 TYR A 310-17.744 17.339 19. 258 1.00 70.14 A C ATOM 1908 CE2 TYR A 310-17.686 18.554 19.931 1.00 70.04 A C ATOM 1909 CZ TYR A 310-17. 184 18.598 21.223 1. 00 70. 42 A C ATOM 1910 OH TYR A 310-17. 117 19.801 21.889 1. 00 70. 62 A O ATOM 1911 C TYR A 310-18. 777 12.814 18.655 1. 00 70. 86 A C ATOM 1912 O TYR A 310-17. 906 12.010 18.322 1. 00 70. 52 A O ATOM 1913 N ALA A 311-20.012 12.787 18.169 1.00 69.88 A N ATOM 1914 CA ALA A 311-20.425 11.783 17.200 1.00 68.77 A C ATOM 1915 CB ALA A 311-21.798 11.243 17.569 1.00 68.93 A C ATOM 1916 C ALA A 311-20.449 12.339 15.786 1.00 68.00 A C ATOM 1917 O ALA A 311-20.471 13.552 15.581 1.00 67.77 A O ATOM 1918 N VAL A 312-20. 440 11.435 14.813 1.00 67. 52 A N ATOM 1919 CA VAL A 312-20. 473 11.807 13.404 1.00 67.56 A C ATOM 1920 CB VAL A 312-19. 057 11.750 12.762 1.00 67.63 A C ATOM 1921 CG1 VAL A 312-18.094 12.626 13.545 1.00 67.62 A C ATOM 1922 CG2 VAL A 312-18.551 10.316 12.719 1.00 67.37 A C ATOM 1923 C VAL A 312-21. 389 10.835 12.666 1.00 67.37 A C ATOM 1924 O VAL A 312-21. 426 9.645 12.981 1.00 66.95 A O ATOM 1925 N GLU A 313-22.138 11.340 11.694 1.00 67.46 A N ATOM 1926 CA GLU A 313-23.028 10.476 10.935 1.00 67.79 A C ATOM 1927 CB GLU A 313-23.998 11.307 10.092 1.00 69.01 A C ATOM 1928 CG GLU A 313-25.033 10.467 9.359 1. 00 71. 22 A C ATOM 1929 CD GLU A 313-25.800 9.541 10.295 1.00 72.65 A C ATOM 1930 OE1 GLU A 313-26.482 10.051 11.213 1.00 73.36 A O ATOM 1931 OE2 GLU A 313-25.717 8.305 10.115 1.00 72.86 A 0 ATOM 1932 C GLU A 313-22.179 9.585 10.038 1.00 67.14 A C ATOM 1933 0 GLU A 313-21.504 10.071 9.127 1.00 67.01 A 0 ATOM 1934 N CYS A 314-22. 210 8.283 10.311 1.00 66.03 A N ATOM 1935 CA CYS A 314-21. 433 7.310 9.549 1.00 65. 21 A C ATOM 1936 C CYS A 314-21. 580 7.469 8.037 1.00 64.83 A C ATOM 1937 O CYS A 314-20. 637 7.226 7.283 1.00 64.71 A 0 ATOM 1938 CB CYS A 314-21. 846 5.887 9.912 1.00 64.78 A C ATOM 1939 SG CYS A 314-21. 619 5.299 11.625 1.00 64.88 A S ATOM 1940 N ALA A 315-22.770 7.867 7.600 1.00 64.46 A N ATOM 1941 CA ALA A 315-23.056 8.037 6.180 1.00 63.94 A C ATOM 1942 CB ALA A 315-24.527 8.387 5.994 1.00 64.24 A C ATOM 1943 C ALA A 315-22.187 9.077 5.474 1.00 63.61 A C ATOM 1944 O ALA A 315-21.657 8.819 4.392 1.00 63.17 A O ATOM 1945 N ASN A 316-22. 045 10.248 6.090 1.00 63.48 A N ATOM 1946 CA ASN A 316-21. 266 11.344 5.510 1.00 62.93 A C ATOM 1947 CB ASN A 316-21. 661 12.661 6.178 1.00 63.46 A C ATOM 1948 CG ASN A 316-23. 153 12.761 6.419 1.00 64.52 A C ATOM 1949 OD1 ASN A 316-23. 959 12.563 5.506 1.00 64.28 A 0 ATOM 1950 ND2 ASN A 316-23. 531 13.067 7.656 1.00 65. 06 A N ATOM 1951 C ASN A 316-19. 757 11.151 5.628 1.00 62.14 A C ATOM 1952 O ASN A 316-18. 990 12.111 5.548 1.00 61.57 A 0 ATOM 1953 N LEU A 317-19. 332 9.909 5.805 1.00 61.28 A N ATOM 1954'CA LEU A 317-17. 917 9.618 5.942 1.00 60.48 A C ATOM 1955 CB LEU A 317-17. 721 8.133 6.232 1.00 60.79 A C ATOM 1956 CG LEU A 317-16. 378 7.752 6.852 1.00 61.23 A C ATOM 1957 CD1 LEU A 317-16. 220 8.478 8.184 1.00 60.85 A C ATOM 1958 CD2 LEU A 317-16. 311 6.242 7.051 1.00 61.10 A C ATOM 1959 C LEU A 317-17. 135 10.010 4.691 1.00 60.03 A C ATOM 1960 O LEU A 317-16. 073 10.627 4.782 1. 00 59. 93 A 0 ATOM 1961 N ASN A 318-17. 666 9.661 3.524 1.00 59.35 A N ATOM 1962 CA ASN A 318-16.992 9.966 2.264 1.00 58.55 A C ATOM 1963 CB ASN A 318-17. 543 9.077 1.141 1. 00 59. 46 A C ATOM 1964 CG ASN A 318-19. 048 9.204 0.976 1.00 60.62 A C ATOM 1965 OD1 ASN A 318-19.569 10.288 0.704 1.00 60.36 A O ATOM 1966 ND2 ASN A 318-19.755 8.089 1.137 1.00 61.39 A N ATOM 1967 C ASN A 318-17.073 11.433 1.845 1.00 57.39 A C ATOM 1968 O ASN A 318-16. 460 11.835 0.853 1.00 57.13 A 0 ATOM 1969 N VAL A 319-17. 821 12.235 2.596 1. 00 55. 76 A N ATOM 1970 CA VAL A 319-17. 952 13.651 2.273 1. 00 54. 32 A C ATOM 1971 CB VAL A 319-19. 445 14.077 2.211 1.00 54.95 A C ATOM 1972 CG1 VAL A 319-20. 055 14.076 3.609 1.00 54.78 A C ATOM 1973 CG2 VAL A 319-19. 570 15.453 1.568 1.00 55.06 A C ATOM 1974 C VAL A 319-17. 219 14.516 3.300 1. 00 53. 06 A C ATOM 1975 O VAL A 319-17. 258 15.746 3.234 1. 00 53. 17 A O ATOM 1976 N MET A 320-16.548 13.866 4.247 1. 00 51. 19 A N ATOM 1977 CA MET A 320-15.804 14.572 5.284 1.00 48.34 A C ATOM 1978 CB MET A 320-15.807 13.748 6.578 1.00 48.86 A C ATOM 1979 CG MET A 320-17.172 13.731 7.273 1.00 49.23 A C ATOM 1980 SD MET A 320-17.386 12.481 8.568 1. 00 49. 47 A S ATOM 1981 CE MET A 320-16.610 13.280 9.950 1. 00 48. 60 A C ATOM 1982 C MET A 320-14.380 14.864 4.814 1.00 46.45 A C ATOM 1983 0 MET A 320-13.832 14.147 3.977 1. 00 45. 98 A 0 ATOM 1984 N PRO A 321-13.765 15.932 5.345 1.00 44.77 A N ATOM 1985 CD PRO A 321-14.381 16.898 6.274 1.00 44.08 A C ATOM 1986 CA PRO A 321-12.405 16.352 4.993 1.00 43.77 A C ATOM 1987 CB PRO A 321-12.408 17.824 5.374 1. 00 43. 93 A C ATOM 1988 CG PRO A 321-13.218 17.803 6.630 1. 00 44. 27 A C ATOM 1989 C PRO A 321-11.247 15.603 5.655 1.00 42.92 A C ATOM 1990 0 PRO A 321-11.382 15.031 6.733 1. 00 42. 99 A O ATOM 1991 N ASP A 322-10. 100 15.628 4.989 1.00 41.57 A N ATOM 1992 CA ASP A 322-8. 900 14.991 5.495 1. 00 39. 71 A C ATOM 1993 CB ASP A 322-7. 903 14.763 4.357 1. 00 40. 40 A C ATOM 1994 CG ASP A 322-8. 302 13.621 3.448 1.00 41.27 A C ATOM 1995 OD1 ASP A 322-7.652 13.453 2.395 1.00 41.33 A O ATOM 1996 OD2 ASP A 322-9. 254 12.885 3.790 1.00 42.48 A O ATOM 1997 C ASP A 322-8. 264 15.901 6.536 1. 00 38. 55 A C ATOM 1998 0 ASP A 322-8. 311 17.126 6.409 1. 00 39. 02 A O ATOM 1999 N VAL A 323-7. 679 15.299 7.568 1. 00 36. 58 A N ATOM 2000 CA VAL A 323-7. 003 16.050 8.621 1. 00 33. 71 A C ATOM 2001 CB VAL A 323-7. 476 15.614 10. 023 1. 00 33. 10 A C ATOM 2002 CG1 VAL A 323-6. 648 16.311 11.101 1. 00 30. 94 A C ATOM 2003 CG2 VAL A 323-8. 949 15.939 10.191 1. 00 32. 84 A C ATOM 2004 C VAL A 323-5. 523 15.735 8.474 1. 00 33. 11 A C ATOM 2005 0 VAL A 323-5. 107 14.584 8.644 1. 00 33. 15 A O ATOM 2006 N THR A 324-4. 726 16.747 8. 155 1. 00 31. 13 A N ATOM 2007 CA THR A 324-3. 302 16.524 7.971 1. 00 31. 09 A C ATOM 2008 CB THR A 324-2. 877 16.912 6.554 1. 00 30. 38 A C ATOM 2009 OG1 THR A 324-3.453 15.991 5.622 1.00 31.46 A O ATOM 2010 CG2 THR A 324-1.366 16.889 6.419 1. 00 32. 02 A C ATOM 2011 C THR A 324-2. 385 17.228 8.966 1. 00 31. 60 A C ATOM 2012 O THR A 324-2. 510 18.431 9.227 1. 00 32. 17 A O ATOM 2013 N PHE A 325-1. 464 16.445 9.516 1. 00 30. 11 A N ATOM 2014 CA PHE A 325-0. 476 16.922 10.463 1. 00 28. 61 A C ATOM 2015 CB PHE A 325-0. 385 15.959 11.644 1. 00 28. 75 A C ATOM 2016 CG PHE A 325-1. 637 15.897 12.468 1. 00 28. 51 A C ATOM 2017 CD1 PHE A 325-1.823 16.762 13.539 1.00 27.36 A C ATOM 2018 CD2 PHE A 325-2.643 14.993 12.158 1.00 27.80 A C ATOM 2019 CE1 PHE A 325-2.989 16.725 14.284 1.00 26.60 A C ATOM 2020 CE2 PHE A 325-3.814 14.952 12.901 1.00 26.97 A C ATOM 2021 CZ PHE A 325-3. 986 15.820 13.965 1. 00 26. 22 A C ATOM 2022 C PHE A 325 0.839 16.939 9.699 1. 00 29. 15 A C ATOM 2023 O PHE A 325 1.296 15.900 9.220 1. 00 28. 66 A O ATOM 2024 N THR A 326 1.433 18.121 9.568 1.00 29.43 A N ATOM 2025 CA THR A 326 2.693 18.263 8.849 1.00 29.04 A c ATOM 2026 CB THR A 326 2.722 19.588 8.059 1.00 30.05 A C ATOM 2027 OG1 THR A 326 1.590 19.638 7.176 1.00 30.32 A O ATOM 2028 CG2 THR A 326 4.001 19.699 7.246 1.00 28.51 A C ATOM 2029 C THR A 326 3.839 18.221 9.855 1.00 28.93 A C ATOM 2030 O THR A 326 4.010 19.129 10.673 1.00 28.55 A 0 ATOM 2031 N ILE A 327 4.625 17.155 9.786 1.00 28.12 A N ATOM 2032 CA ILE A 327 5.727 16.971 10.713 1.00 26.75 A C ATOM 2033 CB ILE A 327 5.533 15.660 11.517 1.00 25.49 A C ATOM 2034 CG2 ILE A 327 6.626 15.517 12.567 1.00 24.77 A C ATOM 2035 CG1 ILE A 327 4.149 15.670 12.176 1.00 25.24 A C ATOM 2036 CD1 ILE A 327 3.797 14.412 12.932 1.00 23.13 A C ATOM 2037 C ILE A 327 7.062 16.932 9.996 1.00 26.79 A C ATOM 2038 O ILE A 327 7. 290 16.078 9.146 1.00 26.23 A 0 ATOM 2039 N ASN A 328 7.938 17.870 10.341 1.00 28.04 A N ATOM 2040 CA ASN A 328 9.267 17.946 9.744 1.00 28.87 A C ATOM 2041 CB ASN A 328 10.074 16.709 10.150 1.00 30.44 A C ATOM 2042 CG ASN A 328 11.572 16.921 10.058 1.00 31.91 A C ATOM 2043 OD1 ASN A 328 12.073 18.025 10.279 1.00 33.71 A 0 ATOM 2044 ND2 ASN A 328 12.301 15.851 9.760 1.00 32.52 A N ATOM 2045 C ASN A 328 9.152 18.049 8.223 1. 00 29. 41 A C ATOM 2046 O ASN A 328 9.949 17.467 7.481 1. 00 29. 43 A 0 ATOM 2047 N GLY A 329 8.141 18.789 7.772 1. 00 29. 49 A N ATOM 2048 CA GLY A 329 7.925 18.993 6.350 1.00 30.18 A C ATOM 2049 C GLY A 329 7.175 17.889 5.628 1.00 30.97 A C ATOM 2050 O GLY A 329 6.899 18.007 4.435 1.00 32.05 A O ATOM 2051 N VAL A 330 6.844 16.818 6.341 1. 00 30. 83 A N ATOM 2052 CA VAL A 330 6.125 15.693 5.751 1. 00 29. 51 A C ATOM 2053 CB VAL A 330 6.754 14.340 6.173 1. 00 28. 77 A C ATOM 2054 CG1 VAL A 330 6.025 13.193 5.490 1. 00 28. 14 A C ATOM 2055 CG2 VAL A 330 8.236 14.315 5.826 1. 00 25. 59 A C ATOM 2056 C VAL A 330 4.656 15.692 6.171 1. 00 30. 29 A C ATOM 2057 O VAL A 330 4.315 15.968 7.325 1. 00 29. 58 A O ATOM 2058 N PRO A 331 3.760 15.389 5.226 1.00 30.63 A N ATOM 2059 CD PRO A 331 3.986 15.327 3.768 1.00 31.45 A C ATOM 2060 CA PRO A 331 2.331 15.359 5.534 1. 00 30. 00 A C ATOM 2061 CB PRO A 331 1.687 15.686 4.192 1.00 30.13 A C ATOM 2062 CG PRO A 331 2.594 14.985 3.228 1. 00 31. 00 A C ATOM 2063 C PRO A 331 1.881 14.005 6.068 1. 00 29. 91 A C ATOM 2064 O PRO A 331 2.162 12.964 5.469 1. 00 30. 52 A O ATOM 2065 N TYR A 332 1.187 14.028 7.200 1. 00 28. 66 A N ATOM 2066 CA TYR A 332 0.663 12.814 7.807 1. 00 28. 19 A C ATOM 2067 CB TYR A 332 1.210 12.658 9.228 1. 00 26. 70 A C ATOM 2068 CG TYR A 332 2.682 12.305 9.212 1.00 26.31 A C ATOM 2069 CD1 TYR A 332 3.103 11.005 8.938 1.00 25.44 A C ATOM 2070 CE1 TYR A 332 4.455 10.689 8.833 1.00 25.46 A C ATOM 2071 CD2 TYR A 332 3.653 13.285 9.389 1.00 25.68 A C ATOM 2072 CE2 TYR A 332 5.011 12.983 9.286 1.00 27.65 A C ATOM 2073 CZ TYR A 332 5.405 11.684 9.006 1.00 26.86 A C ATOM 2074 OH TYR A 332 6.746 11.393 8.886 1.00 26.55 A O ATOM 2075 C TYR A 332-0. 846 12.982 7.784 1.00 29.00 A C ATOM 2076 O TYR A 332-1. 447 13.569 8.690 1.00 28.73 A O ATOM 2077 N THR A 333-1. 442 12.469 6.712 1.00 29.54 A N ATOM 2078 CA THR A 333-2. 869 12.589 6.484 1.00 30.01 A C ATOM 2079 CB THR A 333-3. 154 12.737 4.989 1.00 29.69 A C ATOM 2080 OG1 THR A 333-2. 499 13.914 4.510 1.00 31.36 A 0 ATOM 2081 CG2 THR A 333-4. 647 12.859 4.729 1.00 29.76 A C ATOM 2082 C THR A 333-3. 733 11.478 7.030 1.00 30.86 A C ATOM 2083 O THR A 333-3. 444 10.295 6.850 1.00 30.59 A O ATOM 2084 N LEU A 334-4. 809 11.891 7.690 1.00 31.31 A N ATOM 2085 CA LEU A 334-5. 777 10.981 8.277 1.00 32.82 A C ATOM 2086 CB LEU A 334-5. 954 11. 289 9.763 1.00 33.68 A C ATOM 2087 CG LEU A 334-4. 697 11.268 10.632 1.00 35.30 A C ATOM 2088 CD1 LEU A 334-5.010 11.902 11. 975 1.00 37.00 A C ATOM 2089 CD2 LEU A 334-4.205 9.841 10.802 1.00 35.15 A C ATOM 2090 C LEU A 334-7. 115 11.171 7.571 1.00 33.64 A C ATOM 2091 O LEU A 334-7. 732 12.234 7.673 1.00 33.18 A 0 ATOM 2092 N SER A 335-7.556 10.155 6.843 1. 00 34. 19 A N ATOM 2093 CA SER A 335-8.838 10.249 6.164 1. 00 36. 13 A C ATOM 2094 CB SER A 335-8.995 9.117 5.153 1.00 35.62 A C ATOM 2095 OG SER A 335-8.852 7.861 5.791 1.00 37.33 A O ATOM 2096 C SER A 335-9.890 10.118 7.252 1.00 37.00 A C ATOM 2097 O SER A 335-9.601 9.618 8.340 1.00 36.65 A 0 ATOM 2098 N PRO A 336-11.120 10. 583 6.989 1.00 38.35 A N ATOM 2099 CD PRO A 336-11.617 11.340 5.829 1.00 39.00 A C ATOM 2100 CA PRO A 336-12.151 10.462 8.023 1.00 39.28 A C ATOM 2101 CB PRO A 336-13.388 11.084 7.364 1.00 39.59 A C ATOM 2102 CG PRO A 336-13.080 11.044 5.880 1.00 39.36 A C ATOM 2103 C PRO A 336-12.356 9.012 8.467 1.00 40.09 A C ATOM 2104 O PRO A 336-12.893 8.743 9.548 1. 00 39. 62 A O ATOM 2105 N THR A 337-11. 916 8.079 7.631 1. 00 40. 40 A N ATOM 2106 CA THR A 337-12. 030 6.667 7.958 1.00 41.39 A C ATOM 2107 CB THR A 337-11. 694 5.784 6.746 1.00 42.16 A C ATOM 2108 OG1 THR A 337-12.760 5.856 5.790 1.00 43.82 A O ATOM 2109 CG2 THR A 337-11.488 4.344 7.178 1.00 41.75 A C ATOM 2110 C THR A 337-11. 038 6.363 9.070 1.00 41.44 A C ATOM 2111 O THR A 337-11. 293 5.528 9.940 1.00 42.05 A O ATOM 2112 N ALA A 338-9.912 7.068 9.037 1. 00 40. 95 A N ATOM 2113 CA ALA A 338-8.847 6.886 10.011 1.00 40.62 A C ATOM 2114 CB ALA A 338-7. 517 7.298 9.394 1.00 41.09 A C ATOM 2115 C ALA A 338-9.055 7.625 11.330 1.00 40.28 A C ATOM 2116 O ALA A 338-8.601 7.158 12.376 1. 00 39. 56 A O ATOM 2117 N TYR A 339-9. 729 8.771 11.294 1.00 40.02 A N ATOM 2118 CA TYR A 339-9. 945 9.528 12.521 1.00 40.59 A C ATOM 2119 CB TYR A 339-9. 593 11.010 12.315 1.00 40.56 A C ATOM 2120 CG TYR A 339-10. 474 11.792 11.354 1.00 40.31 A C ATOM 2121 CD1 TYR A 339-11.824 12.018 11.631 1.00 40.17 A C ATOM 2122 CE1 TYR A 339-12. 618 12.792 10.781 1.00 39.54 A C ATOM 2123 CD2 TYR A 339-9. 938 12.359 10.194 1. 00 39. 99 A C ATOM 2124 CE2 TYR A 339-10. 722 13.136 9.337 1.00 39.19 A C ATOM 2125 CZ TYR A 339-12. 061 13.347 9.638 1.00 39.18 A C ATOM 2126 OH TYR A 339-12. 841 14.107 8.800 1.00 36.83 A 0 ATOM 2127 C TYR A 339-11. 347 9.391 13.091 1.00 41.53 A C ATOM 2128 O TYR A 339-11. 789 10.227 13.880 1.00 41.00 A 0 ATOM 2129 N THR A 340-12. 038 8.325 12.696 1.00 43.47 A N ATOM 2130 CA THR A 340-13. 394 8.056 13.169 1.00 45.39 A C ATOM 2131 CB THR A 340-14. 420 8.136 12.014 1.00 45.51 A C ATOM 2132 OG1 THR A 340-14. 423 9.460 11.467 1.00 46.14 A O ATOM 2133 CG2 THR A 340-15. 818 7.802 12.516 1.00 45.63 A C ATOM 2134 C THR A 340-13. 469 6.663 13.791 1.00 46.52 A C ATOM 2135 O THR A 340-13. 041 5.681 13.190 1. 00 46. 66 A O ATOM 2136 N LEU A 341-14. 019 6.589 14.998 1. 00 48. 43 A N ATOM 2137 CA LEU A 341-14. 149 5.328 15.716 1. 00 50. 20 A C ATOM 2138 CB LEU A 341-14. 005 5.579 17.215 1. 00 49. 53 A C ATOM 2139 CG LEU A 341-12. 758 6.363 17.632 1. 00 50. 26 A C ATOM 2140 CD1 LEU A 341-12. 890 6.822 19.074 1.00 49.45 A C ATOM 2141 CD2 LEU A 341-11.525 5.497 17.445 1.00 49.77 A C ATOM 2142 C LEU A 341-15. 495 4.661 15.436 1.00 52.23 A C ATOM 2143 0 LEU A 341-16. 547 5.295 15.548 1.00 51.94 A O ATOM 2144 N LEU A 342-15. 456 3.381 15.072 1. 00 54. 78 A N ATOM 2145 CA LEU A 342-16.674 2.629 14.788 1.00 57.81 A C ATOM 2146 CB LEU A 342-16. 394 1.497 13.795 1.00 57.98 A C ATOM 2147 CG LEU A 342-15. 946 1.900 12.388 1. 00 59. 28 A C ATOM 2148 CD1 LEU A 342-15.783 0.644 11.546 1.00 59.54 A C ATOM 2149 CD2 LEU A 342-16.964 2.843 11.752 1.00 58.85 A C ATOM 2150 C LEU A 342-17. 258 2.046 16.067 1.00 59.47 A C ATOM 2151 O LEU A 342-18. 365 1.508 16.064 1.00 60.36 A 0 ATOM 2152 N ASP A 343-16.503 2.157 17.156 1.00 61.73 A N ATOM 2153 CA ASP A 343-16.932 1.662 18.461 1.00 63.30 A C ATOM 2154 CB ASP A 343-16.137 2.366 19.569 1.00 64.98 A C ATOM 2155 CG ASP A 343-16.595 1.967 20.962 1.00 66.46 A C ATOM 2156 OD1 ASP A 343-16.425 0.785 21.331 1.00 67.61 A 0 ATOM 2157 OD2 ASP A 343-17.130 2.835 21.685 1.00 67.36 A 0 ATOM 2158 C ASP A 343-18. 426 1.896 18.680 1.00 63.32 A C ATOM 2159 O ASP A 343-19. 257 1.052 18.339 1.00 63.61 A O ATOM 2160 N GLN A 349-21. 762 0.379 16.494 1. 00 73. 44 A N ATOM 2161 CA GLN A 349-22. 759 0.604 15.449 1. 00 73. 03 A C ATOM 2162 CB GLN A 349-24. 133 0.111 15.919 1. 00 74. 30 A C ATOM 2163 CG GLN A 349-24. 132-1.327 16.420 1. 00 76. 06 A C ATOM 2164 CD GLN A 349-25. 462-1.736 17.027 1. 00 77. 24 A C ATOM 2165 OE1 GLN A 349-26. 475-1.828 16.331 1.00 77.46 A O ATOM 2166 NE2 GLN A 349-25.467-1. 978 18.336 1.00 77.44 A N ATOM 2167 C GLN A 349-22. 833 2.091 15.102 1.00 71.22 A C ATOM 2168 0 GLN A 349-23. 418 2.476 14.088 1. 00 70. 92 A 0 ATOM 2169 N PHE A 350-22. 229 2.916 15.954 1.00 69.13 A N ATOM 2170 CA PHE A 350-22. 217 4.360 15.763 1.00 66.79 A C ATOM 2171 CB PHE A 350-22. 680 5.065 17.041 1.00 67.74 A C ATOM 2172 CG PHE A 350-24. 011 4.583 17.552 1.00 69.17 A C ATOM 2173 CD1 PHE A 350-24.135 3.319 18.129 1.00 69.98 A C ATOM 2174 CD2 PHE A 350-25.146 5.382 17.438 1.00 69.66 A C ATOM 2175 CE1 PHE A 350-25.372 2.857 18.585 1.00 70.13 A C ATOM 2176 CE2 PHE A 350-26.389 4.931 17.891 1.00 69.95 A C ATOM 2177 CZ PHE A 350-26. 501 3.665 18.466 1.00 70.27 A C ATOM 2178 C PHE A 350-20. 818 4.841 15.391 1.00 64.54 A C ATOM 2179 O PHE A 350-19. 842 4.107 15.532 1.00 64.04 A 0 ATOM 2180 N CYS A 351-20. 731 6.077 14.912 1.00 61.99 A N ATOM 2181 CA CYS A 351-19. 455 6.663 14.521 1. 00 58. 88 A C ATOM 2182 C CYS A 351-19. 169 7.907 15.360 1.00 56.07 A C ATOM 2183 O CYS A 351-19. 987 8.823 15.430 1.00 55.27 A 0 ATOM 2184 CB CYS A 351-19. 474 6.992 13.017 1.00 60.12 A C ATOM 2185 SG CYS A 351-19. 627 5.474 12.016 1.00 63.31 A S ATOM 2186 N SER A 352-18.012 7.923 16.015 1. 00 52. 95 A N ATOM 2187 CA SER A 352-17.629 9.057 16.853 1.00 49.89 A C ATOM 2188 CB SER A 352-17.621 8.649 18.328 1.00 49.44 A C ATOM 2189 OG SER A 352-16.750 7.557 18.545 1.00 50.16 A 0 ATOM 2190 C SER A 352-16. 267 9.617 16.464 1.00 47.15 A C ATOM 2191 O SER A 352-15.510 8.983 15.730 1.00 47.10 A 0 ATOM 2192 N SER A 353-15.963 10.807 16.973 1.00 44.28 A N ATOM 2193 CA SER A 353-14.709 11.493 16.678 1.00 41.07 A C ATOM 2194 CB SER A 353-14.844 12.982 17.017 1.00 41.14 A C ATOM 2195 OG SER A 353-13.678 13.702 16.653 1.00 39.50 A 0 ATOM 2196 C SER A 353-13.492 10.929 17.402 1.00 39.02 A C ATOM 2197 O SER A 353-13.554 10.600 18. 586 1. 00 38. 78 A 0 ATOM 2198 N GLY A 354-12. 383 10.835 16.674 1. 00 37. 08 A N ATOM 2199 CA GLY A 354-11.148 10.337 17.243 1.00 34.05 A C ATOM 2200 C GLY A 354-10. 328 11.479 17.815 1.00 32.89 A C ATOM 2201 O GLY A 354-9. 168 11.300 18.180 1.00 33.09 A 0 ATOM 2202 N PHE A 355-10. 935 12.660 17.886 1.00 31.12 A N ATOM 2203 CA PHE A 355-10. 274 13.846 18.423 1. 00 30. 03 A C ATOM 2204 CB PHE A 355-10. 353 15.003 17.430 1. 00 28. 03 A C ATOM 2205 CG PHE A 355-9. 663 14.729 16.137 1.00 28.49 A C ATOM 2206 CD1 PHE A 355-8. 277 14.635 16.083 1.00 28.23 A c ATOM 2207 CD2 PHE A 355-10.397 14.538 14.971 1.00 28.51 A C ATOM 2208 CE1 PHE A 355-7. 623 14.353 14.882 1.00 28.44 A C ATOM 2209 CE2 PHE A 355-9. 756 14.255 13.763 1.00 29.93 A C ATOM 2210 CZ PHE A 355-8. 362 14.162 13.719 1.00 29.18 A C ATOM 2211 C PHE A 355-10. 954 14.253 19.718 1.00 29.84 A C ATOM 2212 O PHE A 355-12. 166 14.089 19.870 1.00 30.94 A 0 ATOM 2213 N GLN A 356-10. 173 14.784 20.649 1.00 28.36 A N ATOM 2214 CA GLN A 356-10. 714 15.205 21.927 1. 00 27. 29 A C ATOM 2215 CB GLN A 356-10. 802 14.017 22.874 1. 00 28. 82 A C ATOM 2216 CG GLN A 356-11. 440 14.349 24.205 1.00 31.34 A C ATOM 2217 CD GLN A 356-11. 401 13.182 25.163 1.00 33.84 A C ATOM 2218 OE1 GLN A 356-10. 336 12.806 25.662 1.00 34.17 A 0 ATOM 2219 NE2 GLN A 356-12.563 12.589 25.418 1. 00 35.12 A N ATOM 2220 C GLN A 356-9. 867 16.293 22.568 1. 00 26. 21 A C ATOM 2221 O GLN A 356-8. 650 16.343 22.388 1.00 25.50 A O ATOM 2222 N GLY A 357-10. 523 17.165 23.320 1.00 25.12 A N ATOM 2223 CA GLY A 357-9.816 18.239 23.981 1. 00 24. 95 A C ATOM 2224 C GLY A 357-9. 119 17.768 25.238 1. 00 24. 51 A C ATOM 2225 O GLY A 357-9. 648 16.962 25.998 1.00 23.64 A O ATOM 2226 N LEU A 358-7. 913 18.271 25.448 1.00 24.97 A N ATOM 2227 CA LEU A 358-7. 128 17.922 26.617 1. 00 25. 98 A C ATOM 2228 CB LEU A 358-6. 479 16.553 26.432 1.00 25.45 A C ATOM 2229 CG LEU A 358-5. 619 16.067 27.600 1. 00 26. 84 A C ATOM 2230 CD1 LEU A 358-6.440 16.082 28.880 1.00 28.05 A C ATOM 2231 CD2 LEU A 358-5.097 14.666 27.305 1. 00 26. 37 A C ATOM 2232 C LEU A 358-6. 072 19.005 26.773 1.00 27.54 A C ATOM 2233 0 LEU A 358-5. 096 19.057 26.019 1.00 28.08 A 0 ATOM 2234 N ASP A 359-6. 286 19.879 27.750 1. 00 28. 25 A N ATOM 2235 CA ASP A 359-5. 383 20.989 28.003 1.00 29.62 A C ATOM 2236 CB ASP A 359-6. 190 22.196 28. 486 1.00 30.83 A C ATOM 2237 CG ASP A 359-7. 268 22. 602 27.500 1.00 32.27 A C ATOM 2238 OD1 ASP A 359-6. 925 23.020 26.369 1.00 32.03 A 0 ATOM 2239 OD2 ASP A 359-8. 461 22.494 27.854 1.00 32.86 A 0 ATOM 2240 C ASP A 359-4. 272 20.681 29.000 1. 00 29. 59 A C ATOM 2241 O ASP A 359-4. 519 20.538 30.198 1.00 29.66 A O ATOM 2242 N ILE A 360-3. 048 20.580 28.493 1. 00 29. 68 A N ATOM 2243 CA ILE A 360-1. 885 20.318 29.333 1. 00 30. 12 A C ATOM 2244 CB ILE A 360-0.751 19.646 28.528 1. 00 29. 75 A C ATOM 2245 CG2 ILE A 360 0.445 19.382 29.427 1.00 28.17 A C ATOM 2246 CG1 ILE A 360-1. 254 18.339 27.910 1. 00 29. 69 A C ATOM 2247 CD1 ILE A 360-1.740 17.320 28.923 1.00 30.44 A C ATOM 2248 C ILE A 360-1.409 21.682 29.819 1.00 31.00 A C ATOM 2249 O ILE A 360-1.131 22.569 29.012 1.00 30.30 A O ATOM 2250 N HIS A 361-1.316 21.849 31.132 1.00 32.64 A N ATOM 2251 CA HIS A 361-0.902 23.127 31.697 1.00 35.14 A C ATOM 2252 CB HIS A 361-1.205 23.182 33.199 1.00 37.34 A C ATOM 2253 CG HIS A 361-2.648 22.986 33.538 1.00 40.86 A C ATOM 2254 CD2 HIS A 361-3. 244 22.231 34.493 1.00 41.41 A C ATOM 2255 ND1 HIS A 361-3. 666 23.640 32.876 1.00 42.03 A N ATOM 2256 CE1 HIS A 361-4. 825 23.296 33.408 1.00 43.17 A C ATOM 2257 NE2 HIS A 361-4.597 22.442 34.391 1.00 43.34 A N ATOM 2258 C HIS A 361 0.571 23.460 31.506 1. 00 35. 49 A C ATOM 2259 O HIS A 361 1.431 22.577 31.465 1.00 35.39 A O ATOM 2260 N PRO A 362 0.879 24.756 31.371 1.00 35.58 A N ATOM 2261 CD PRO A 362-0.028 25.873 31.056 1. 00 35. 40 A C ATOM 2262 CA PRO A 362 2.274 25.154 31.203 1.00 35.71 A C ATOM 2263 CB PRO A 362 2.171 26.656 30.971 1. 00 35. 89 A C ATOM 2264 CG PRO A 362 0.861 26.786 30.252 1. 00 35. 61 A C ATOM 2265 C PRO A 362 3.000 24.812 32.507 1. 00 36. 24 A C ATOM 2266 O PRO A 362 2.363 24.573 33.535 1.00 36.21 A O ATOM 2267 N PRO A 363 4.341 24. 771 32.477 1. 00 36. 54 A N ATOM 2268 CD PRO A 363 5.181 24.637 33.683 1. 00 36. 66 A C ATOM 2269 CA PRO A 363 5.165 25.025 31.289 1. 00 35. 62 A C ATOM 2270 CB PRO A 363 6.530 25.349 31.892 1.00 36.32 A C ATOM 2271 CG PRO A 363 6.565 24.443 33.102 1.00 37.41 A C ATOM 2272 C PRO A 363 5.219 23.857 30.289 1.00 34.05 A C ATOM 2273 O PRO A 363 5.699 24.026 29.167 1.00 33.44 A O ATOM 2274 N ALA A 364 4.721 22.687 30.691 1. 00 31. 60 A N ATOM 2275 CA ALA A 364 4.730 21.509 29.821 1.00 30.85 A C ATOM 2276 CB ALA A 364 4.270 20.286 30.591 1.00 29.48 A C ATOM 2277 C ALA A 364 3.859 21.691 28.579 1.00 30.58 A C ATOM 2278 O ALA A 364 4.296 21.436 27.451 1.00 29.62 A O ATOM 2279 N GLY A 365 2.620 22.120 28.798 1.00 29.37 A N ATOM 2280 CA GLY A 365 1.706 22.339 27.694 1.00 27.86 A C ATOM 2281 C GLY A 365 1.780 23.785 27.251 1. 00 26. 81 A C ATOM 2282 O GLY A 365 2.617 24.530 27.759 1.00 27.39 A 0 ATOM 2283 N PRO A 366 0.929 24.219 26.305 1.00 25.83 A N ATOM 2284 CD PRO A 366 0. 892 25.607 25.807 1.00 25.12 A C ATOM 2285 CA PRO A 366-0.089 23.400 25.639 1.00 24.35 A C ATOM 2286 CB PRO A 366-0.923 24.433 24.893 1.00 24.73 A C ATOM 2287 CG PRO A 366 0.096 25.475 24.526 1.00 24.55 A C ATOM 2288 C PRO A 366 0.550 22.389 24.700 1. 00 23. 87 A C ATOM 2289 O PRO A 366 1.635 22.624 24.170 1.00 24.64 A O ATOM 2290 N LEU A 367-0. 122 21.264 24.496 1.00 22.62 A N ATOM 2291 CA LEU A 367 0.396 20.227 23.619 1.00 21.31 A C ATOM 2292 CB LEU A 367 1.104 19.141 24.435 1. 00 20. 14 A C ATOM 2293 CG LEU A 367 2.419 19.420 25.166 1.00 20.21 A C ATOM 2294 CD1 LEU A 367 2.680 18.292 26.161 1.00 19.07 A C ATOM 2295 CD2 LEU A 367 3.567 19.532 24.167 1.00 18.91 A C ATOM 2296 C LEU A 367-0. 698 19.552 22.812 1.00 21.69 A C ATOM 2297 0 LEU A 367-1. 876 19.564 23.183 1.00 22.01 A O ATOM 2298 N TRP A 368-0. 296 18.984 21.684 1.00 21.15 A N ATOM 2299 CA TRP A 368-1. 200 18.211 20.860 1. 00 21. 19 A C ATOM 2300 CB TRP A 368-1. 064 18.575 19.381 1. 00 21. 89 A C ATOM 2301 CG TRP A 368-1. 838 19.806 18.983 1.00 24.13 A C ATOM 2302 CD2 TRP A 368-3. 115 19.843 18.324 1.00 24.49 A C ATOM 2303 CE2 TRP A 368-3.451 21.205 18.141 1.00 25.06 A C ATOM 2304 CE3 TRP A 368-4. 007 18.858 17.872 1. 00 24. 89 A C ATOM 2305 CD1 TRP A 368-1.468 21.107 19.170 1.00 23.03 A C ATOM 2306 NE1 TRP A 368-2. 429 21.952 18.666 1.00 25.45 A N ATOM 2307 CZ2 TRP A 368-4.642 21.611 17.520 1.00 25.07 A C ATOM 2308 CZ3 TRP A 368-5. 195 19.258 17.252 1. 00 25. 77 A C ATOM 2309 CH2 TRP A 368-5. 499 20.626 17.082 1.00 25.15 A C ATOM 2310 C TRP A 368-0. 680 16.797 21.122 1. 00 20. 76 A C ATOM 2311 0 TRP A 368 0. 525 16.592 21.253 1. 00 20. 31 A O ATOM 2312 N ILE A 369-1. 573 15.827 21.238 1. 00 20. 18 A N ATOM 2313 CA ILE A 369-1. 121 14.475 21.501 1.00 19.96 A C ATOM 2314 CB ILE A 369-1. 636 13.961 22.861 1.00 19.08 A C ATOM 2315 CG2 ILE A 369-1. 102 12.564 23.122 1.00 18. 62 A C ATOM 2316 CG1 ILE A 369-1. 174 14.901 23.981 1. 00 19. 49 A C ATOM 2317 CD1 ILE A 369-1.609 14.473 25.372 1.00 18.04 A C ATOM 2318 C ILE A 369-1. 537 13.505 20.410 1. 00 20. 75 A C ATOM 2319 O ILE A 369-2. 732 13.295 20.146 1. 00 22. 02 A O ATOM 2320 N LEU A 370-0. 531 12.926 19.769 1.00 19.48 A N ATOM 2321 CA LEU A 370-0. 754 11.959 18.713 1.00 18.75 A C ATOM 2322 CB LEU A 370 0.408 12.010 17.726 1. 00 16. 19 A C ATOM 2323 CG LEU A 370 0.622 13.426 17.164 1.00 16.74 A C ATOM 2324 CD1 LEU A 370 1.738 13.414 16.126 1. 00 15. 88 A C ATOM 2325 CD2 LEU A 370-0.681 13.946 16.546 1.00 13.35 A C ATOM 2326 C LEU A 370-0. 844 10.608 19.406 1. 00 19. 18 A C ATOM 2327 0 LEU A 370 0.170 9.943 19.646 1.00 17.49 A O ATOM 2328 N GLY A 371-2. 074 10.241 19.760 1. 00 19. 04 A N ATOM 2329 CA GLY A 371-2. 322 8. 989 20.449 1. 00 20. 31 A C ATOM 2330 C GLY A 371-2. 496 7.795 19.534 1.00 21.62 A C ATOM 2331 0 GLY A 371-2. 046 7.807 18.377 1.00 20.77 A O ATOM 2332 N ASP A 372-3.162 6.764 20.053 1. 00 22. 22 A N ATOM 2333 CA ASP A 372-3.378 5.529 19.298 1. 00 23. 68 A C ATOM 2334 CB ASP A 372-4.189 4.533 20.127 1. 00 24. 63 A C ATOM 2335 CG ASP A 372-3.476 4.130 21.407 1. 00 27. 84 A C ATOM 2336 OD1 ASP A 372-2.254 4.388 21.523 1.00 26.22 A O ATOM 2337 OD2 ASP A 372-4.140 3.549 22.294 1.00 28.99 A O ATOM 2338 C ASP A 372-4. 035 5. 738 17.945 1. 00 23. 64 A C ATOM 2339 O ASP A 372-3. 687 5.059 16.981 1. 00 24. 74 A O ATOM 2340 N VAL A 373-4. 980 6.671 17.867 1. 00 23. 77 A N ATOM 2341 CA VAL A 373-5.648 6.965 16.603 1. 00 22. 90 A C ATOM 2342 CB VAL A 373-6.619 8.156 16.746 1. 00 22. 56 A C ATOM 2343 CG1 VAL A 373-7.083 8.629 15.375 1.00 22.51 A C ATOM 2344 CG2 VAL A 373-7.815 7.743 17.582 1.00 23.32 A C ATOM 2345 C VAL A 373-4.621 7.296 15.520 1. 00 22. 69 A C ATOM 2346 O VAL A 373-4. 790 6.932 14.359 1. 00 22. 40 A O ATOM 2347 N PHE A 374-3. 553 7.985 15.907 1. 00 22. 80 A N ATOM 2348 CA PHE A 374-2.511 8.365 14.961 1.00 22. 72 A C ATOM 2349 CB PHE A 374-1. 722 9.551 15.511 1. 00 20. 89 A C ATOM 2350 CG PHE A 374-0. 702 10.105 14.554 1. 00 19. 44 A C ATOM 2351 CD1 PHE A 374-1.069 11.038 13.584 1.00 18.93 A C ATOM 2352 CD2 PHE A 374 0.632 9.708 14.632 1.00 17.62 A C ATOM 2353 CE1 PHE A 374-0. 116 11.573 12.703 1.00 17.99 A C ATOM 2354 CE2 PHE A 374 1.594 10.235 13.757 1.00 17.98 A C ATOM 2355 CZ PHE A 374 1.222 11.169 12.792 1. 00 16. 90 A C ATOM 2356 C PHE A 374-1. 558 7.200 14.707 1. 00 24. 00 A C ATOM 2357 O PHE A 374-1.221 6.886 13.559 1.00 23.12 A O ATOM 2358 N ILE A 375-1.124 6.561 15.789 1.00 25.26 A N ATOM 2359 CA ILE A 375-0.193 5.445 15.692 1. 00 25. 65 A C ATOM 2360 CB ILE A 375 0.221 4.954 17.095 1. 00 25. 30 A C ATOM 2361 CG2 ILE A 375 1.169 3.780 16.975 1.00 24. 53 A C ATOM 2362 CG1 ILE A 375 0.903 6.104 17.854 1. 00 26. 58 A C ATOM 2363 CD1 ILE A 375 1.159 5. 845 19.343 1.00 24.05 A C ATOM 2364 C ILE A 375-0.764 4.297 14.865 1. 00 25. 96 A C ATOM 2365 O ILE A 375-0.022 3.618 14.161 1.00 27.45 A O ATOM 2366 N ARG A 376-2.075 4.080 14.931 1.00 25.47 A N ATOM 2367 CA ARG A 376-2.679 3.013 14.136 1.00 25.66 A C ATOM 2368 CB ARG A 376-4.181 2.885 14.413 1.00 25.03 A C ATOM 2369 CG ARG A 376-4.539 1.799 15.425 1. 00 27. 11 A C ATOM 2370 CD ARG A 376-6.035 1.504 15.432 1. 00 26. 50 A C ATOM 2371 NE ARG A 376-6.831 2.624 15.929 1. 00 28. 30 A N ATOM 2372 CZ ARG A 376-7.016 2.907 17.218 1. 00 28. 43 A C ATOM 2373 NH1 ARG A 376-6.463 2.151 18.159 1.00 27.70 A N ATOM 2374 NH2 ARG A 376-7.757 3.949 17.567 1.00 27.81 A N ATOM 2375 C ARG A 376-2.456 3.293 12.653 1.00 25.60 A C ATOM 2376 O ARG A 376-2.285 2.370 11.858 1. 00 26. 15 A O ATOM 2377 N GLN A 377-2.450 4.569 12.282 1. 00 24. 92 A N ATOM 2378 CA GLN A 377-2.227 4.940 10.892 1. 00 25. 48 A C ATOM 2379 CB GLN A 377-2.887 6.286 10.579 1. 00 26. 70 A C ATOM 2380 CG GLN A 377-4.398 6.253 10.655 1. 00 29. 73 A C ATOM 2381 CD GLN A 377-4.979 5.082 9.884 1. 00 30. 70 A C ATOM 2382 OE1 GLN A 377-4.794 4.974 8.670 1. 00 31. 82 A O ATOM 2383 NE2 GLN A 377-5.679 4.194 10.588 1.00 30.41 A N ATOM 2384 C GLN A 377-0.740 5.022 10.567 1.00 25.49 A C ATOM 2385 O GLN A 377-0.342 4.820 9.418 1. 00 26. 41 A 0 ATOM 2386 N PHE A 378 0.082 5.307 11.573 1. 00 24. 62 A N ATOM 2387 CA PHE A 378 1.516 5.425 11.345 1. 00 24. 96 A C ATOM 2388 CB PHE A 378 1.915 6.900 11.289 1. 00 25. 72 A C ATOM 2389 CG PHE A 378 1.199 7.673 10.225 1. 00 26. 87 A C ATOM 2390 CD1 PHE A 378 0.094 8.456 10.543 1.00 27.05 A C ATOM 2391 CD2 PHE A 378 1.607 7.587 8.897 1. 00 26. 88 A C ATOM 2392 CE1 PHE A 378-0.602 9.145 9.551 1.00 28.77 A C ATOM 2393 CE2 PHE A 378 0.920 8.271 7.892 1.00 28.36 A C ATOM 2394 CZ PHE A 378-0.187 9.051 8.217 1.00 28.42 A C ATOM 2395 C PHE A 378 2.419 4.709 12.337 1.00 25.06 A C ATOM 2396 0 PHE A 378 2.598 5.150 13.477 1.00 25.15 A O ATOM 2397 N TYR A 379 2.994 3.603 11.885 1.00 24.83 A N ATOM 2398 CA TYR A 379 3.916 2.817 12.693 1.00 23.54 A C ATOM 2399 CB TYR A 379 4.653 1.838 11.788 1.00 24.12 A C ATOM 2400 CG TYR A 379 5.574 0. 885 12.496 1.00 25.46 A C ATOM 2401 CD1 TYR A 379 5.072-0. 116 13. 321 1.00 26.15 A C ATOM 2402 CE1 TYR A 379 5.917-1. 042 13.929 1.00 27.44 A C ATOM 2403 CD2 TYR A 379 6.951 0.950 12.299 1.00 26.31 A C ATOM 2404 CE2 TYR A 379 7.809 0.031 12.901 1.00 28.31 A C ATOM 2405 CZ TYR A 379 7.284-0. 965 13.710 1.00 27.61 A C ATOM 2406 OH TYR A 379 8.118-1. 911 14.252 1.00 28.64 A O ATOM 2407 C TYR A 379 4.896 3.818 13.295 1.00 23.65 A C ATOM 2408 0 TYR A 379 5.397 4.695 12.591 1.00 23.17 A O ATOM 2409 N SER A 380 5.167 3.698 14.591 1.00 23.02 A N ATOM 2410 CA SER A 380 6.072 4.634 15.246 1.00 22.71 A C ATOM 2411 CB SER A 380 5.330 5.389 16.348 1.00 22.43 A C ATOM 2412 OG SER A 380 4.178 6.027 15.827 1.00 22.11 A O ATOM 2413 C SER A 380 7.300 3.973 15.833 1.00 22.82 A C ATOM 2414 0 SER A 380 7.212 2.916 16.454 1.00 23.25 A O ATOM 2415 N VAL A 381 8.449 4.612 15.633 1.00 23.14 A N ATOM 2416 CA VAL A 381 9.719 4.114 16.146 1.00 21.61 A C ATOM 2417 CB VAL A 381 10.710 3.862 14.991 1.00 21.32 A C ATOM 2418 CG1 VAL A 381 12.035 3.371 15.531 1.00 19.05 A C ATOM 2419 CG2 VAL A 381 10.124 2.840 14.028 1.00 21.16 A C ATOM 2420 C VAL A 381 10.297 5.155 17.107 1.00 21. 92 A C ATOM 2421 O VAL A 381 10.404 6.336 16.772 1.00 22.51 A O ATOM 2422 N PHE A 382 10.657 4.713 18.307 1.00 20.80 A N ATOM 2423 CA PHE A 382 11.212 5.601 19.325 1.00 19.91 A C ATOM 2424 CB PHE A 382 10.428 5.417 20.620 1.00 18.79 A C ATOM 2425 CG PHE A 382 8.949 5.603 20.449 1.00 17.48 A C ATOM 2426 CD1 PHE A 382 8.363 6.848 20.644 1.00 16.61 A C ATOM 2427 CD2 PHE A 382 8.145 4.539 20.051 1.00 17.85 A C ATOM 2428 CE1 PHE A 382 6.994 7.032 20.443 1.00 17.06 A C ATOM 2429 CE2 PHE A 382 6.772 4.712 19.845 1.00 18.29 A C ATOM 2430 CZ PHE A 382 6.197 5.962 20.042 1.00 17.58 A C ATOM 2431 C PHE A 382 12.679 5.247 19.518 1.00 20.18 A C ATOM 2432 O PHE A 382 13.004 4.197 20.079 1.00 20.29 A O ATOM 2433 N ASP A 383 13.552 6.137 19.052 1.00 20.31 A N ATOM 2434 CA ASP A 383 14.999 5.940 19.093 1.00 19.93 A C ATOM 2435 CB ASP A 383 15.553 6.197 17.690 1.00 20.13 A C ATOM 2436 CG ASP A 383 17.057 6.068 17.616 1. 00 21. 60 A C ATOM 2437 OD1 ASP A 383 17.686 5.744 18.647 1.00 23.41 A O ATOM 2438 OD2 ASP A 383 17.613 6.290 16.520 1. 00 21. 33 A O ATOM 2439 C ASP A 383 15.751 6.804 20.107 1.00 20.85 A C ATOM 2440 O ASP A 383 15.995 7.986 19.863 1.00 21.69 A O ATOM 2441 N ARG A 384 16.136 6.208 21.232 1.00 20.47 A N ATOM 2442 CA ARG A 384 16.872 6.925 22.275 1. 00 20. 68 A C ATOM 2443 CB ARG A 384 16.844 6.132 23.590 1.00 18.72 A C ATOM 2444 CG ARG A 384 15.522 6.195 24.343 1.00 18.36 A C ATOM 2445 CD ARG A 384 15.302 7.587 24.945 1.00 19.10 A C ATOM 2446 NE ARG A 384 16.247 7.886 26.024 1.00 18.20 A N ATOM 2447 CZ ARG A 384 16.156 7.402 27.262 1.00 17.66 A C ATOM 2448 NH1 ARG A 384 15.159 6.595 27.594 1.00 16.38 A N ATOM 2449 NH2 ARG A 384 17.063 7.723 28.172 1.00 16.41 A N ATOM 2450 C ARG A 384 18.328 7.168 21.867 1.00 21.52 A C ATOM 2451 O ARG A 384 18.985 8.085 22.371 1.00 21.29 A O ATOM 2452 N GLY A 385 18.831 6.343 20.955 1.00 21.54 A N ATOM 2453 CA GLY A 385 20.206 6.486 20.516 1.00 22.29 A C ATOM 2454 C GLY A 385 20.461 7.782 19.777 1.00 24.06 A C ATOM 2455 O GLY A 385 21 523 8.389 19.937 1.00 25.35 A 0 ATOM 2456 N ASN A 386 19.488 8.213 18.975 1. 00 23. 31 A N ATOM 2457 CA ASN A 386 19.620 9.445 18.202 1.00 23.07 A C ATOM 2458 CB ASN A 386 19.496 9.138 16.705 1.00 22.78 A C ATOM 2459 CG ASN A 386 20.534 8.140 16. 226 1.00 23.74 A C ATOM 2460 OD1 ASN A 386 21.735 8.417 16.241 1. 00 24. 39 A O ATOM 2461 ND2 ASN A 386 20.075 6.967 15.802 1. 00 22. 59 A N ATOM 2462 C ASN A 386 18.569 10.483 18.595 1. 00 22. 64 A C ATOM 2463 O ASN A 386 18. 482 11.543 17.971 1. 00 20. 69 A O ATOM 2464 N ASN A 387 17.777 10.162 19.621 1. 00 21. 84 A N ATOM 2465 CA ASN A 387 16.717 11.042 20.127 1. 00 21. 29 A C ATOM 2466 CB ASN A 387 17.324 12.241 20.851 1. 00 19. 60 A C ATOM 2467 CG ASN A 387 18.058 11.842 22.107 1. 00 21. 14 A C ATOM 2468 OD1 ASN A 387 17.465 11.297 23.045 1. 00 20. 88 A O ATOM 2469 ND2 ASN A 387 19.360 12.109 22.139 1. 00 21. 45 A N ATOM 2470 C ASN A 387 15.791 11.530 19.023 1. 00 21. 22 A C ATOM 2471 O ASN A 387 15.665 12.733 18.783 1. 00 21. 13 A O ATOM 2472 N ARG A 388 15.125 10.589 18.366 1. 00 21. 31 A N ATOM 2473 CA ARG A 388 14.234 10.928 17.267 1. 00 21. 58 A C ATOM 2474 CB ARG A 388 15.026 10.900 15.960 1. 00 22. 91 A C ATOM 2475 CG ARG A 388 15.687 9.551 15.716 1. 00 24. 16 A C ATOM 2476 CD ARG A 388 16.539 9.541 14.469 1. 00 24. 96 A C ATOM 2477 NE ARG A 388 17.066 8.206 14.214 1. 00 26. 17 A N ATOM 2478 CZ ARG A 388 17.700 7.848 13.102 1. 00 28. 54 A C ATOM 2479 NH1 ARG A 388 17.890 8.731 12.128 1.00 28.21 A N ATOM 2480 NH2 ARG A 388 18.141 6.604 12.964 1.00 27.83 A N ATOM 2481 C ARG A 388 13.073 9.947 17.168 1.00 20.92 A C ATOM 2482 0 ARG A 388 13.085 8.887 17.799 1. 00 19. 86 A 0 ATOM 2483 N VAL A 389 12.074 10.311 16.368 1. 00 19. 84 A N ATOM 2484 CA VAL A 389 10.919 9.456 16.155 1. 00 20. 20 A C ATOM 2485 CB VAL A 389 9.603 10.146 16.587 1. 00 19. 75 A C ATOM 2486 CG1 VAL A 389 8.421 9.233 16.288 1.00 17.65 A C ATOM 2487 CG2 VAL A 389 9.647 10.473 18.078 1.00 18.92 A C ATOM 2488 C VAL A 389 10.821 9.106 14.679 1.00 20.87 A C ATOM 2489 O VAL A 389 11.012 9.959 13.813 1.00 22.18 A 0 ATOM 2490 N GLY A 390 10.539 7.841 14.397 1. 00 21. 62 A N ATOM 2491 CA GLY A 390 10.399 7.395 13. 023 1.00 21.56 A C ATOM 2492 C GLY A 390 8.938 7.092 12.747 1.00 22.22 A C ATOM 2493 O GLY A 390 8.277 6.427 13.547 1. 00 22. 20 A O ATOM 2494 N LEU A 391 8.430 7.582 11.620 1. 00 22. 30 A N ATOM 2495 CA LEU A 391 7.039 7.367 11.248 1. 00 22. 42 A C ATOM 2496 CB LEU A 391 6.233 8.658 11.433 1.00 22.14 A C ATOM 2497 CG LEU A 391 6.291 9.350 12.800 1. 00 22. 34 A C ATOM 2498 CD1 LEU A 391 5.696 10.746 12. 690 1.00 22.31 A C ATOM 2499 CD2 LEU A 391 5.544 8.523 13.834 1.00 21.71 A C ATOM 2500 C LEU A 391 6.953 6.926 9.794 1.00 23.55 A C ATOM 2501 0 LEU A 391 7.760 7.334 8.958 1. 00 24. 48 A O ATOM 2502 N ALA A 392 5.962 6.096 9.501 1. 00 24. 08 A N ATOM 2503 CA ALA A 392 5.742 5.589 8.155 1.00 23.85 A C ATOM 2504 CB ALA A 392 6.814 4. 568 7.795 1. 00 24. 42 A C ATOM 2505 C ALA A 392 4.366 4.940 8.148 1.00 24.86 A C ATOM 2506 O ALA A 392 3.889 4.467 9.180 1. 00 24. 25 A O ATOM 2507 N PRO A 393 3. 700 4.919 6.987 1.00 26.93 A N ATOM 2508 CD PRO A 393 4.103 5.515 5.700 1. 00 27. 24 A C ATOM 2509 CA PRO A 393 2.368 4.317 6.892 1. 00 27. 75 A C ATOM 2510 CB PRO A 393 2.057 4.417 5.405 1. 00 27. 80 A C ATOM 2511 CG PRO A 393 2.773 5.688 5.002 1. 00 26. 87 A C ATOM 2512 C PRO A 393 2.365 2.879 7.391 1. 00 29. 41 A C ATOM 2513 O PRO A 393 3.190 2.075 6.971 1.00 29.06 A O ATOM 2514 N ALA A 394 1.444 2.566 8.298 1. 00 31. 14 A N ATOM 2515 CA ALA A 394 1.341 1.220 8. 849 1.00 34.20 A C ATOM 2516 CB ALA A 394 0.438 1.228 10.077 1.00 33.27 A C ATOM 2517 C ALA A 394 0.795 0.249 7.804 1. 00 35. 94 A C ATOM 2518 O ALA A 394 0.211 0.671 6.809 1. 00 37. 11 A O ATOM 2519 N VAL A 395 0.992-1. 047 8.035 1.00 38.13 A N ATOM 2520 CA VAL A 395 0.517-2. 091 7.125 1.00 39.87 A C ATOM 2521 CB VAL A 395 1.680-2. 780 6.378 1.00 40.55 A C ATOM 2522 CG1 VAL A 395 1.128-3. 861 5.464 1.00 41.02 A C ATOM 2523 CG2 VAL A 395 2.478-1. 767 5.586 1.00 40.46 A C ATOM 2524 C VAL A 395-0.220-3. 176 7.907 1.00 41.21 A C ATOM 2525 0 VAL A 395-1.402-3. 452 7. 592 1.00 42.62 A 0 ATOM 2526 OXT VAL A 395 0.414-3. 748 8.822 1.00 41.06 A O ATOM 2527 OH2 WAT S 1 4.152 5.839 34.653 1.00 12.02 S O ATOM 2528 OH2 WAT S 2 11.023 5.002 36.383 1.00 14.83 S O ATOM 2529 OH2 WAT S 3-3.451 11.760 37.887 1.00 16.97 S O ATOM 2530 OH2 WAT S 4 5.313 10.926 24.760 1.00 12.46 S O ATOM 2531 OH2 WAT S 5 3.297-4. 253 47.162 1.00 22.88 S O ATOM 2532 OH2 WAT S 6-4.445 8.135 45.345 1.00 18.64 S O ATOM 2533 OH2 WAT S 7 12.642 4.993 29.274 1.00 11.54 S 0 ATOM 2534 OH2 WAT S 8 12.581 5.622 26.562 1.00 14.30 S 0 ATOM 2535 OH2 WAT S 9 8.960 16.535 26.509 1.00 15.73 S O ATOM 2536 OH2 WAT S 10-8.666 6.508 38.419 1. 00 22. 02 S O ATOM 2537 OH2 WAT S 11-0.241 8.838 28.485 1. 00 25. 98 S O ATOM 2538 OH2 WAT S 12-3.744 17.695 24.000 1. 00 29. 68 S O ATOM 2539 OH2 WAT S 13 11.222 2.843 29. 981 1. 00 16.45 S O ATOM 2540 OH2 WAT S 14 6.503-14. 225 43.684 1.00 23.64 S O ATOM 2541 OH2 WAT S 15 6.699 9.460 34.905 1.00 12.81 S O ATOM 2542 OH2 WAT S 16 9.609 2.690 33.199 1.00 23.40 S O ATOM 2543 OH2 WAT S 17 11.592 1.788 49.293 1.00 21.26 S O ATOM 2544 OH2 WAT S 18 10.545 1.176 51.729 1.00 29. 52 S 0 ATOM 2545 OH2 WAT S 19 18.553 9.312 24.698 1.00 19.76 S O ATOM 2546 OH2 WAT S 20 10.904 13.400 8.503 1.00 26.06 S O ATOM 2547 OH2 WAT S 21 19.469-8. 084 33.086 1.00 19.08 S 0 ATOM 2548 OH2 WAT S 22 15.278-12. 721 24.725 1.00 24.75 S O ATOM 2549 OH2 WAT S 23 14.541-13. 776 29.654 1.00 20.99 S O ATOM 2550 OH2 WAT S 24 6.445 19.566 27.456 1. 00 21. 56 S O ATOM 2551 OH2 WAT S 25 10.273 17.592 15.887 1.00 17.38 S O ATOM 2552 OH2 WAT S 26-4.252 14.105 44.924 1. 00 41. 54 S O ATOM 2553 OH2 WAT S 27-1.300 10.392 46.776 1. 00 26. 35 S O ATOM 2554 OH2 WAT S 28 15.774-3. 235 13.337 1. 00 26. 47 S O ATOM 2555 OH2 WAT S 29 22.419 11.045 16.423 1. 00 35. 27 S O ATOM 2556 OH2 WAT S 30 8.483 13.436 9.004 1. 00 23. 18 S O ATOM 2557 OH2 WAT S 31-10.757-5. 326 25.285 1.00 50.99 S O ATOM 2558 OH2 WAT S 32-9.989 16.598 2.262 1. 00 30. 70 S O ATOM 2559 OH2 WAT S 33-3.077 2.014 44.788 1. 00 26. 79 S 0 ATOM 2560 OH2 WAT S 34-6.651 5.654 13.056 1. 00 30. 18 S O ATOM 2561 OH2 WAT S 35 0.574-14. 104 38.252 1.00 26.55 S O ATOM 2562 OH2 WAT S 36-10.382-1. 525 27.922 1. 00 28. 41 S O ATOM 2563 OH2 WAT S 37 12.824-12. 772 22.502 1.00 40.35 S O ATOM 2564 OH2 WAT S 38 2.319-9. 174 26.315 1. 00 19. 44 S O ATOM 2565 OH2 WAT S 39 0.117-1. 290 26.033 1. 00 24. 36 S 0 ATOM 2566 OH2 WAT S 40 4.756-14. 784 52.471 1. 00 30. 72 S O ATOM 2567 OH2 WAT S 41 14.214-11. 867 17.143 1. 00 53. 91 S O ATOM 2568 OH2 WAT S 42 10.514-9. 859 50.315 1. 00 31. 05 S O ATOM 2569 OH2 WAT S 43 9.667-11. 823 36.921 1. 00 27. 19 S 0 ATOM 2570 OH2 WAT S 44 18.640 8.117 9.152 1. 00 35. 31 S O ATOM 2571 OH2 WAT S 45 0.620-10. 882 42.559 1. 00 23. 06 S O ATOM 2572 OH2 WAT S 46-9.690 14.014 39.053 1.00 46.44 S O ATOM 2573 OH2 WAT S 47-13.118 7.759 43.067 1. 00 35. 33 S 0 ATOM 2574 OH2 WAT S 48 24.338-8. 314 26.557 1.00 19.33 S 0 ATOM 2575 OH2 WAT S 49 8.313 19.885 12.434 1. 00 25. 77 S 0 ATOM 2576 OH2 WAT S 50 1.087 22.680 21.179 1. 00 21. 41 S O ATOM 2577 OH2 WAT S 51-2.775-10. 664 43.030 1. 00 32. 02 S O ATOM 2578 OH2 WAT S 52 15.243-15. 487 40.805 1. 00 36. 27 S O ATOM 2579 OH2 WAT S 53-13.378 11.643 42.512 1. 00 40. 71 S O ATOM 2580 OH2 WAT S 54 13.581 11.228 7.348 1. 00 31. 94 S 0 ATOM 2581 OH2 WAT S 55 15.186 1.100 38.249 1. 00 26. 25 S 0 ATOM 2582 OH2 WAT S 56-2.835 21.194 25.750 1. 00 30. 98 S 0 ATOM 2583 OH2 WAT S 57-19.849-1. 375 16.938 1. 00 71. 36 S 0 ATOM 2584 OH2 WAT S 58 11.791-12. 980 30.375 1. 00 30.89 S O ATOM 2585 OH2 WAT S 59 3.892-9. 641 50.565 1. 00 21. 46 S 0 ATOM 2586 OH2 WAT S 60-8.321 19.147 29.911 1.00 30.60 S 0 ATOM 2587 OH2 WAT S 61-3.313 29.378 13.931 1. 00 45. 97 S 0 ATOM 2588 OH2 WAT S 62-4.603 29.439 10.334 1.00 48.89 S 0 ATOM 2589 OH2 WAT S 63 16.749-8. 649 40.469 1. 00 23. 42 S 0 ATOM 2590 OH2 WAT S 64 7.235 5.903 4.384 1. 00 47. 90 S O ATOM 2591 OH2 WAT S 65 8.753 4.167 39.344 1. 00 24. 48 S 0 ATOM 2592 OH2 WAT S 66 21.680-6. 958 23.211 1. 00 26. 34 S 0 ATOM 2593 OH2 WAT S 67 0.875 1.015 13.906 1. 00 23. 24 S 0 ATOM 2594 OH2 WAT S 68-12.734 2.628 45.644 1.00 47.81 S O ATOM 2595 OH2 WAT S 69 25.842 0.178 29.121 1. 00 39. 74 S O ATOM 2596 OH2 WAT S 70-6.168 1.977 49.390 1. 00 35. 36 S O ATOM 2597 OH2 WAT S 71 4.160-10. 269 18.486 1.00 34.30 S o ATOM 2598 OH2 WAT S 72 12.722 7.854 44.744 1. 00 37. 06 S O ATOM 2599 OH2 WAT S 73 17.187 11.620 11.924 1. 00 36. 08 S O ATOM 2600 OH2 WAT S 74-17.254 0.970 36.944 1.00 60.28 S 0 ATOM 2601 OH2 WAT S 75-8.224 1.207 29.542 1. 00 20. 42 S 0 ATOM 2602 OH2 WAT S 76-2.980 11.654 32.013 1. 00 48. 50 S 0 ATOM 2603 OH2 WAT S 77 16.632 3.138 39.859 1.00 28.80 S 0 ATOM 2604 OH2 WAT S 78-4.377 0.572 51.648 1.00 28.79 S 0 ATOM 2605 OH2 WAT S 79 17.142-6. 177 20.309 1.00 33.07 S 0 ATOM 2606 OH2 WAT S 80 6.606 24. 758 18.280 1. 00 31. 61 S 0 ATOM 2607 OH2 WAT S 81 18.260-1. 988 42.031 1. 00 26. 56 S O ATOM 2608 OH2 WAT S 82 3.895 24.739 21.151 1. 00 41. 77 S O ATOM 2609 OH2 WAT S 83 20.821 14.834 24.442 1. 00 31. 66 S O ATOM 2610 OH2 WAT S 84 10.876 18.494 12.965 1.00 24.19 S O ATOM 2611 OH2 WAT S 85-3. 563-12. 131 40.006 1.00 37.50 S O ATOM 2612 OH2 WAT S 86-3.193-7. 920 13.067 1.00 61.86 S O ATOM 2613 OH2 WAT S 87 23.180-3. 250 16.436 1. 00 33. 40 S O ATOM 2614 OH2 WAT S 88 18.874 6.859 32.702 1. 00 50. 11 S O ATOM 2615 OH2 WAT S 89-2.654-1. 844 6.211 1. 00 35. 16 S O ATOM 2616 OH2 WAT S 90 16.104-6. 211 44.533 1.00 39.92 S O ATOM 2617 OH2 WAT S 91 18.947-8. 125 22.183 1. 00 25. 41 S 0 ATOM 2618 OH2 WAT S 92 9.985 2.642 37.353 1. 00 19. 41 S 0 ATOM 2619 OH2 WAT S 93-4.243 23.510 26.391 1. 00 30. 63 S O ATOM 2620 OH2 WAT S 94-19.713 7.167 3.614 1.00 44.39 S 0 ATOM 2621 OH2 WAT S 95-3.843 10.276 47.849 1.00 43.01 S O ATOM 2622 OH2 WAT S 96 25.542-3. 627 32.144 1. 00 33.48 S O ATOM 2623 OH2 WAT S 97 17.822 4.274 44.745 1. 00 52. 05 S O ATOM 2624 OH2 WAT S 98 17.118 15.728 18.839 1. 00 38. 23 S O ATOM 2625 OH2 WAT S 99-4.553-7. 086 49.458 1. 00 39. 10 S O ATOM 2626 OH2 WAT S 100-12.825 8. 224 4. 429 1.00 55.15 S 0 ATOM 2627 OH2 WAT S 101-6. 184 6.776 49.587 1.00 28.89 S O ATOM 2628 OH2 WAT S 102 9.239 5.083 52.720 1.00 31.87 S 0 ATOM 2629 OH2 WAT S 103 21.761-0. 876 21.854 1.00 35.04 S O ATOM 2630 OH2 WAT S 104 15.528 12.613 30.197 1.00 32.26 S 0 ATOM 2631 OH2 WAT S 105 10.351 13.667 41.582 1.00 42.33 S 0 ATOM 2632 OH2 WAT S 106-23.034 7.902 15.089 1.00 50.95 S 0 ATOM 2633 OH2 WAT S 107 9.094 20.229 32.233 1.00 45.29 S O ATOM 2634 OH2 WAT S 108-7.379 5.917 4.863 1.00 42.01 S O ATOM 2635 OH2 WAT S 109-0.130-11. 597 39.955 1.00 32.40 S O ATOM 2636 OH2 WAT S 110-10.263-4. 919 37.013 1.00 36.80 S O ATOM 2637 OH2 WAT S 111 17.458 14.179 16.290 1.00 36.48 S O ATOM 2638 OH2 WAT S 112 5.629 26.273 10.845 1.00 26.90 S O ATOM 2639 OH2 WAT S 113-8.779-8. 848 18.574 1.00 40.59 S O ATOM 2640 OH2 WAT S 114-1.630-9. 620 20.202 1.00 44.98 S 0 ATOM 2641 OH2 WAT S 115 23.422-4. 192 24.002 1.00 42.78 S 0 ATOM 2642 OH2 WAT S 116-3.075 24.709 28.847 1.00 42.19 S 0 ATOM 2643 OH2 WAT S 117 16.529 5.837 41.245 1.00 44.17 S O ATOM 2644 OH2 WAT S 118 -11. 768 13.358 2.487 1.00 46.72 S O ATOM 2645 OH2 WAT S 119 16.811-1. 887 46.907 1.00 26.45 S O ATOM 2646 OH2 WAT S 120 1.946-14. 148 45.206 1.00 37.65 S O ATOM 2647 OH2 WAT S 121 5.969 28.560 17.152 1.00 43.17 S O ATOM 2648 OH2 WAT S 122 -9. 596 10.736 1.651 1.00 51.42 S O ATOM 2649 OH2 WAT S 123-12.522 20.444 23.257 1.00 43.85 S O ATOM 2650 OH2 WAT S 124 16.936-11. 403 40.090 1.00 32.89 S 0 ATOM 2651 OH2 WAT S 125-10.869-0. 800 52.653 1.00 40.70 S 0 ATOM 2652 OH2 WAT S 126 12.629-5. 075 9.142 1.00 38.19 S 0 ATOM 2653 OH2 WAT S 127 3.205-16. 239 41.101 1.00 41.70 S O ATOM 2654 OH2 WAT S 128-8.182 4.697 20.300 1.00 46.35 S O ATOM 2655 OH2 WAT S 129-7.825 9.675 24.324 1.00 40.18 S 0 ATOM 2656 OH2 WAT S 130-27.295-3. 512 19.478 1.00 41.90 S 0 ATOM 2657 OH2 WAT S 131-21. 922 20.888 14.712 1.00 38.37 S O ATOM 2658 OH2 WAT S 132-8.512-4. 625 24.266 1.00 37.01 S O ATOM 2659 OH2 WAT S 133 23.550 6.313 18.003 1.00 50.55 S O ATOM 2660 OH2 WAT S 134-6.403-7. 832 36.907 1.00 50.11 S 0 ATOM 2661 OH2 WAT S 135 4. 135 12.495 38.211 1.00 49.64 S O ATOM 2662 OH2 WAT S 136 19.389 3.755 17.297 1.00 27.22 S 0 ATOM 2663 OH2 WAT S 137 16.572 13.745 13.754 1.00 30.96 S 0 ATOM 2664 OH2 WAT S 138 4.096 23.759 24.003 1. 00 28. 02 S O ATOM 2665 OH2 WAT S 139 4.104-15. 174 44.014 1.00 32.91 S O ATOM 2666 OH2 WAT S 140-9.042-7. 092 36.570 1.00 36.91 S O ATOM 2667 OH2 WAT S 141 12.385-12. 256 14.649 1.00 38.72 S 0 ATOM 2668 OH2 WAT S 142-22.955-1. 261 19.145 1.00 40.85 S 0 ATOM 2669 OH2 WAT S 143 4.676-10. 049 26.383 1.00 29.75 S 0 ATOM 2670 OH2 WAT S 144 1.669-6. 038 9.380 1.00 37.48 S 0 ATOM 2671 OH2 WAT S 145-23. 937 19.808 12.898 1.00 40.51 S 0 ATOM 2672 OH2 WAT S 146-10.774-8. 460 16.990 1.00 47.33 S 0 ATOM 2673 OH2 WAT S 147-5.789 11.187 44.039 1.00 33.92 S 0 ATOM 2674 OH2 WAT S 148-16.081-5. 527 42.454 1.00 28.16 S 0 ATOM 2675 OH2 WAT S 149 9.973 21.833 9.267 1.00 36.23 S O ATOM 2676 OH2 WAT S 150 13.508 3.349 7.020 1.00 52.28 S O ATOM 2677 OH2 WAT S 151-13.904-4. 346 45.074 1.00 34.84 S O ATOM 2678 OH2 WAT S 152 21.384 13.687 20.501 1.00 49.39 S 0 ATOM 2679 OH2 WAT S 153-0.283 24.891 20.717 1.00 40.70 S 0 ATOM 2680 OH2 WAT S 154-9.423 4.494 49.428 1.00 50.01 S O ATOM 2681 OH2 WAT S 155-1.107-7. 898 11.215 1.00 37.89 S 0 ATOM 2682 OH2 WAT S 156-1.625 19.825 32.729 1.00 38.83 S O ATOM 2683 OH2 WAT S 157-6.482 2.719 21.755 1.00 40.76 S O ATOM 2684 OH2 WAT S 158 5.752-10. 655 29.403 1.00 31.74 S 0 ATOM 2685 OH2 WAT S 159 10.381-12. 063 20.448 1.00 45.00 S O ATOM 2686 OH2 WAT S 160 19.452 15.466 20.064 1.00 43.02 S 0 ATOM 2687 OH2 WAT S 161-2.769 8.912 29.087 1.00 35.63 S O ATOM 2688 OH2 WAT S 162-5.645 3.117 51.485 1.00 40.92 S 0 ATOM 2689 OH2 WAT S 163-13.527 17.380 22.217 1.00 44.07 S 0 ATOM 2690 OH2 WAT S 164 17.603-0. 711 44.769 1.00 34.92 S 0 ATOM 2691 OH2 WAT S 165-3.046 16.167 44.136 1.00 40.49 S 0 ATOM 2692 OH2 WAT S 166 14.128 0.797 7.246 1.00 50.55 S 0 ATOM 2693 OH2 WAT S 167-9.529 15.329 28.097 1.00 40.51 S 0 ATOM 2694 OH2 WAT S 168-9.442-0. 484 31.247 1.00 37.85 S 0 ATOM 2695 OH2 WAT S 169 4.272 4.235 1.405 1.00 46.39 S 0 ATOM 2696 OH2 WAT S 170 7.542 25.015 15.505 1.00 41.46 S 0 ATOM 2697 OH2 WAT S 171 4.450 13.689 40.720 1.00 45.99 S 0 ATOM 2698 OH2 WAT S 172 1.269 28.745 15.120 1.00 47.58 S 0 ATOM 2699 OH2 WAT S 173 1.025-15. 040 41.364 1.00 40.16 S 0 ATOM 2700 OH2 WAT S 174 17.653 7.604 35.873 1.00 43.38 S 0 ATOM 2701 OH2 WAT S 175 6.109-4. 007 3.970 1.00 46.29 S 0 ATOM 2702 OH2 WAT S 176-25.405 4.252 13.765 1.00 51.47 S 0 ATOM 2703 OH2 WAT S 177 2.552 13.383 42.421 1.00 52.08 S O ATOM 2704 OH2 WAT S 178 33.536-15. 983 20.576 1.00 61.60 S O ATOM 2705 OH2 WAT S 179-2.025-13. 474 36.889 1.00 44.76 S O ATOM 2706 OH2 WAT S 180 4.095-18. 935 40.650 1.00 40.74 S O ATOM 2707 OH2 WAT S 181 19.859 5.845 9.836 1.00 48.44 S O ATOM 2708 OH2 WAT S 182 9.717 16.491 33.584 1.00 44.93 S O ATOM 2709 OH2 WAT S 183-5.164 10.138 33.944 1.00 39.65 S 0 ATOM 2710 OH2 WAT S 184 0.426 1.147 24.382 1.00 40.47 S 0 ATOM 2711 OH2 WAT S 185 6.340 25.775 7.858 1.00 41.27 S 0 ATOM 2712 OH2 WAT S 186-4.009-9. 118 35.479 1.00 41.03 S 0 ATOM 2713 OH2 WAT S 187 21.089 4.758 32.580 1.00 43.64 S 0 ATOM 2714 OH2 WAT S 188-2. 802 1.822 24.962 1.00 38.15 S O ATOM 2715 OH2 WAT S 189 14.858 6.220 6.499 1.00 46.12 S 0 ATOM 2716 OH2 WAT S 190 15.526 8.974 36.558 1.00 42.12 S 0 ATOM 2717 OH2 WAT S 191-14.081 1.239 43.690 1.00 51.82 S 0 ATOM 2718 OH2 WAT S 192 0.299-13. 351 43.176 1.00 36.71 S O ATOM 2719 OH2 WAT S 193-3.456 27.436 16.065 1.00 50.73 S O ATOM 2720 OH2 WAT S 194 23.746-16. 775 15.749 1.00 45.32 S 0 ATOM 2721 OH2 WAT S 195-18.596 5.040 18.767 1.00 50.09 S 0 ATOM 2722 OH2 WAT S 196 20.607 3.837 29.727 1.00 36.67 S 0 ATOM 2723 OH2 WAT S 197-7.679 8.933 44.596 1.00 40.03 S 0 ATOM 2724 OH2 WAT S 198-11.531-3. 878 23.533 1.00 39.51 S 0 ATOM 2725 OH2 WAT S 199 17.555-2. 833 51.080 1.00 48.08 S O ATOM 2726 OH2 WAT S 200-15.624 3.997 5.122 1.00 45. 97 S O ATOM 2727 OH2 WAT S 201-8.950-0. 857 23.782 1.00 47.73 S O ATOM 2728 OH2 WAT S 202-8. 042 9.289-0. 079 1.00 47.59 S 0 ATOM 2729 OH2 WAT S 203 -7. 343-7.440 20.391 1. 00 54. 70 S O ATOM 2730 OH2 WAT S 204-14. 596 9.578 21.448 1.00 54.92 S 0 ATOM 2731 OH2 WAT S 205 -4. 257 17.710 32.242 1. 00 48. 38 S 0 ATOM 2732 OH2 WAT S 206 9.643-16. 650 46.909 1. 00 53. 41 S O ATOM 2733 OH2 WAT S 207 5.917 21.283 4.134 1.00 65.88 S O ATOM 2734 OH2 WAT S 208-17. 908-2.658 39.185 1.00 39.14 S O ATOM 2735 OH2 WAT S 209 3.574 27.249 27.323 1.00 38.67 S O ATOM 2736 OH2 WAT S 210-12. 135 0.926 31.764 1.00 45.72 S O ATOM 2737 OH2 WAT S 211 16.611-13. 921 48.894 1.00 35.36 S O ATOM 2738 OH2 WAT S 212 -S. 004 12.234 0. 014 1. 00 39. 35 S 0 ATOM 2739 OH2 WAT S 213-14. 191 13.419 21.640 1.00 51.36 S 0 ATOM 2740 OH2 WAT S 214 21.328-1. 257 35.465 1.00 46.11 S O Table 2: Crystal Data and X-rav data collection statistics Number of crystals 1 Space group P4i2i2 (tetragona !) Unit cell dimensions a = b = 61. 32 c = 207. 80 A a 3=y=90° Number of monomers/a. u. 1 Packing coefficient 2. 29A3/Da Solvent content 45.8% Resolution range 25.50-2. 35A Number of observations 50202 Number of unique reflections 16976 Mosaicity 0.54 Overall Data redundancy 3.0 Data completeness 98.5% <#/#(I)> 7.2 Rmerge 0.094 Highest resolution shell Resolution range 2.48-2. 35A Completeness for shell 99. 1 % <IIa (I) > 2.0 Rmerge for shell 0.371 Table 3: Refinement Statistics Data used in refinement -resolution range 25. 25-2. 35A -intensity cutoff (Sigma (F) ) 0.0 - number of reflections (working/test set) 15241/1723 - completeness (working + test set) 97.6% -test set 10. 0% Fit to data used in refinement - overall Rcryst 0.198 - overall Rfree 0.238 Fit in the highest resolution bin - resolution range 2.50-2. 35 A - bin completeness (working +test set) 98.9% - bin Rcryst 0.246 - bin Rfree 0.308 Number of non-hydrogen atoms - protein atoms 2526 - waters 214 Overall B value from Wilson plot 26.4 A Overall mean B value 30.6 A2 atoms chain P (pro-sequence) 38.8 Å2 atoms chain A (Cathepsin E) 29.9 A2 water molecules 36.9 A2 Cross-validated estimated coordinate error - from Luzzati plot 0. 32A - from #A 0. 29A Rms deviations from ideal values - bond lengths 0. 007A - bond angles 1. 4° - dihedral angles 26. 3° - improper angles 0. 81° Ramachandran plot Residues in most favorable regions 89. 6 % Residues in additional allowed regions 9. 3 % Residues in generously allowed regions 1. 1 %