WO2008109871A2 - Crystal structure of proprotein convertase 9 (pcsk9) and uses thereof - Google Patents

Abstract

The invention provides a crystallized PCSK9 molecule. The three-dimensional coordinates of the crystal structure of PCSK9 are obtained by X-ray diffraction. The coordinates can be used for studying the PCSK9 structure and designing, screening and developing compounds that modulate PCSK9 activity.

Description

CRYSTAL STRUCTURE OF PROPROTEIN CONVERTASE 9 (PCSK9) AND

USESTHEREOF

CROSS-REFERENCE TO RELATED APPLICATIONS

[0001] This application claims the benefit of priority to U.S. Provisional Patent

Application Number 60/893,828, filed 08 March 2007. The full disclosure of this application is incorporated herein by reference in its entirety and for all purposes.

BACKGROUND OF THE INVENTION

Field of the Invention

[0002] The invention provides a crystallized PCSK9 molecule. The three- dimensional coordinates of the crystal structure of PCSK9 are obtained by X-ray diffraction. The coordinates can be used for studying the PCSK9 structure and designing, screening and developing compounds that modulate PCSK9 activity.

Back2round

[0003] Proprotein convertase subtilisin kexin like 9 (PCSK9) is a 692 residue extra cellular protein expressed primarily in the kidneys, liver and intestines and represents the 9^th member of the secretory subtilase family. The full length sequence consists of three domains; the first two domains correspond to an inhibitory pro-domain (amino acids 1-152) and a serine protease domain (amino acids 153-452) of the proteinase K subfamily member of the secretory subtilisin-like serine proteases, respectively. The third domain is 210 residues in length (amino acids 453-692), rich in cysteine residues and was thought to play an analogous role to the P-(processing) domains of other Furin/Kexin/Subtilisin-like serine proteases which appears to be essential for folding and regulation of the activated protease. Mutations in PCSK9 are strongly associated with levels of low density lipoprotein cholesterol (LDL-c) in the blood plasma and thereby occurrence or resistance to atherosclerosis and coronary heart disease. [0004] The PCSK9 three dimensional coordinates of the invention can be used to design, screen and develop compounds that associate with and modulate the activity of PCSK9. Summary of the Invention

[0005] The present invention provides the three-dimensional structure of

PCSK9 thereby enabling identification and design of ligands, biopharmaceuticals or low molecular weight molecules that specifically bind to and modulate the activity of PCSK9.

[0006] The present invention relates to:

[0007] (i) a crystal of the PCSK9 polypeptide comprising the catalytic site with or without a ligand or low molecular weight compound;

[0008] (ii) a method of crystallizing the PCSK9 polypeptide; and

[0009] (iii) methods of using the three dimensional coordinates derived from said PCSK9 polypeptide crystal to identify/design small molecules/biotherapeutics capable of modulating PCSK9 activity.

BRIEF DESCRIPTION OF FIGURES

[0010] FIG. 1 : A ribbon diagram of PCSK9 detailing the overall fold of the molecule, the pro (auto-inhibitory domain) is colored red, the catalytic domain blue and the disulfide rich C-terminal domain green. Disulfide bonds within the molecule are represented as yellow sticks.

[0011] FIG. 2: A representation of the electrostatic surface of the PCSK9 substrate binding site. Surface is colored red, blue and white to indicate electronegative, electropositive and charge neutral areas, respectively.

DETAILED DESCRIPTION OF THE INVENTION

Definitions

[0012] The term "binding partner" according to the invention refers to a ligand or low molecular weight molecule that associates with PCSK9 and either enhances the ability of PCSK9 to crystallize or modulates the activity of PCSK9.

[0013] The term "PCSK9" means "proprotein convertase subtilisin kexin like

9" and is also known as neural apoptosis-regulated convertase, NARC-I.

[0014] The term "space group" according to the invention refers to the arrangement of symmetry elements of the crystal. [0015] The term "structure coordinates" or "three-dimensional coordinates" refers to mathematical coordinates derived from the placement of a polypeptide chain (and the individual atoms thereof) in an electron density map. The electron density map is derived from mathematical equations related to the pattern obtained on diffraction of a monochromatic beam of X-rays by the atoms of a crystal of the invention. [0016] The term "unit cell" according to the invention, refers to the basic shape block. The entire volume of a crystal can be constructed by regular assembly of such blocks. Each unit cell comprises a complete representation of the unit cell pattern, the repetition of which builds the crystal.

Embodiments

[0017] The present invention relates to a PCSK9 polypeptide, a method of crystallizing a PCSK9 polypeptide and a PCSK9 polypeptide crystal. The invention further relates to the X-ray coordinates (also referred to as three dimensional or structural coordinates) of the structure of a PCSK9 polypeptide elucidated from a PCSK9 polypeptide crystal. Still further, the present invention relates to using the coordinates of a PCSK9 polypeptide to design and developing compounds that modulate the activity of said PCSK9 polypeptide.

[0018] The full length sequence of human PCSK9 is known and is set forth in

Genbank Accession Number gi: 119627065, gb | EAXO 6660 . 1, which are incorporated herein by reference. As used herein, the PCSK9 polypeptide refers to that of SEQ. ID. No.: 1.

SEP. ID. No.: 1 :

MGTVSSRRSWWPLPLLLLLLLLLGP AGARAQEDEDGD YEEL VL ALRSEEDGLAEAPEHGTTATFHRCAKD PWRLPGTYVVVLKEETHLSQSERTARRLQAQAARRGYLTKILHVFHGLLPGFLVKMSGDLLELALKLPHV DYIEEDSSVFAQSIPWNLERITPPRYRADEYQPPDGGSLVEVYLLDTSIQSDHREIEGRVMVTDFENVPE EDGTRFHRQASKCDSHGTHLAGVVSGRDAGVAKGASMRSLR VLNCQGKGTVSGTLIGLEFIRKSQLVQPV GPLVVLLPLAGGYSRVLNAACQRLARAGVVLVTAAGNFRDDACL YSPASAPEVITVGATNAQDQPVTLGT LGTNFGRCVDLFAPGEDIIGASSDCSTCFVSQSGTSQAAAHVAGIAAMMLS AEPELTL AELRQRLIHFSA KD VINEAWFPEDQRVLTPNL VAALPPSTHGAGWQLFCRTVWSAHSGPTRMATAIARCAPDEELLSCSSFS RSGKRRGERMEAQGGKLVCRAHNAFGGEGVYAIARCCLLPQANCSVHTAPPAEASMGTRVHCHQQGHVLT GCSSHWEVEDLGTHKPPVLRPRGQPNQCVGHREASIHASCCHAPGLECKVKEHGIPAPQEQVTVACEEGW TLTGCSALPGTSHVLGAYAVDNTCVVRSRDVSTTGSTSEEAVTAVAICCRSRHLAQASQELQ

[0020] According to the invention, cDNA encoding PCSK9 (i.e., amino acid residues detailed in SEQ. ID No: 1) is inserted into a suitable expression vector and expressed in a suitable cell line. The cDNA also can include other regions that facilitate expression or achieve other objects, such as flanking regions, that otherwise do not depart from the essence of the invention. The cDNAs encoding the PCSK9 polypeptide, or functional portions thereof, can be altered by addition, substitution, deletion, or insertion.

Such alterations can be made, for example, to prevent glycosolation, prevent formation of incorrect or undesired disulfide bridges, and to enhance expression, purification and/or crystallization.

[0021] Recombinant expression vectors containing the nucleotide sequence encoding PCSK9, or a portion thereof, can be prepared using methods known to those of skill in the art. Suitable host cells for expression of PCSK9 polypeptides include prokaryotic, yeast, and higher eukaryotic cells. Further examples of suitable expression systems that can be employed to express recombinant PCSK9 according to the present invention including mammalian or insect host cell culture expression systems, including baculovirus systems in insect cells and mammalian cell lines.

[0022] In one aspect of the invention, there is provided a composition comprising a polypeptide in crystalline form, wherein the polypeptide is a PCSK9 polypeptide.

[0023] In a further embodiment, the PCSK9 polypeptide is the expression product of a polynucleotide encoded by the amino acid residues of SEQ. ID No.: 1, or fragments and/or homologs thereof.

[0024] In a further embodiment of the invention, the composition above further comprises an optional binding partner suitable for co-crystallization with PCSK9.

[0025] In a further embodiment, the binding partner is a small molecule or polypeptide binding partner.

[0026] In a further embodiment, the binding partner is a small molecule or an antibody (or fragment thereof).

[0027] One aspect of the invention relates to a method of crystallizing a

PCSK9 polypeptide with or without a binding partner. Crystals can be grown or formed by any suitable crystallization method such as vapor diffusion, sitting drop and the like (see Ducruix and Giege "Crystallization of Nucleic Acids and Proteins: A Practical Approach", Oxford University Press, 1992) and can be set up manually or automatically (using robotics) known in the art. The crystallization buffer can optionally comprise a number of elements that include, without limitation, buffers, salts, organics, additives, precipitating agents, etc. The pH can range, for example from about 4.0 to about 9.0. The claimed invention can encompass any and all methods of crystallization. One skilled in the art can choose any such methods and vary the parameters such that the chosen method results in the desired crystals. Crystals of the invention are screened for their ability to diffract X-rays to a resolution of 3.0 A or better and a complete data set can be collected from one or more crystals.

[0028] In a further aspect of the invention, is provided a method for crystallizing a PCSK9 polypeptide, comprising mixing a solution comprising a PCSK9 polypeptide, optionally a binding partner and a crystallization buffer, or soaking an existing binding partner into a preformed PCSK9 crystals.

[0029] In a further embodiment, the method of crystallization is by sitting drop, the crystallization precipitant can be PEG-6000 or PEG-8000 at a concentration between 14 and 28% with a CAPS or CHES buffer at a pH ranging from about pH 8.0 to about pH 11.0 with or without additional salts such as 0.1M-0.4M Sodium Chloride. The PCSK9 polypeptide is at a final concentration of 10 mg/mL and the crystals are prepared in a temperature ranging from about 4 to about 20 ⁰C. A detailed description of the crystallization of the PCSK9 polypeptide of the invention is described in Example 1, infra.

[0030] In a further aspect, a PCSK9 crystal of the invention diffracts X-rays to a resolution of at least 3.0 A, is of space group V2{Σ{Σ_\ with unit cell dimensions: a=62.5 +5A, b=70.1 +5 A, c=148.6.0 +5 A, α =90 degrees, β =90 degrees and γ =90 degrees. Depending on the particular conditions for crystallization, the parameters characterizing the unit cell can vary with a limited range, for example, a, b, and c each vary by up to IOA and α, β and γ vary by up to 10 degrees.

[0031] Another aspect of the invention relates to the atomic structure of

PCSK9. The three dimensional coordinates of PCSK9 can be determined utilizing a crystal comprising a PCSK9 polypeptide of the invention. According to the present invention, the structure of PCSK9 is determined using X-ray crystallography. Any suitable X-ray diffraction method for obtaining three-dimensional structural coordinates of a polypeptide can be used (see, for example, International Tables for Crystallography: Volume F: Crystallography of biological macromolecules, editor M. G. Rossmann. For the present invention, see Example 2 (infra) for a detailed description of the structure determination of PCSK9.

[0032] In a further embodiment of the invention, the crystalline PCSK9 polypeptide has a three-dimensional structure characterized by the atomic structure coordinates given in Table 1 , infra.

[0033] In another aspect of the invention is provided a computer-readable medium (such as, for example, a floppy disc, a hard disc, computer tape, RAM, ROM, CD, DVD, a magnetic disk, an optical disk, and the like) having recorded thereon structural coordinate data for PCSK9 (such as set forth in Table 1), or a portion thereof. [0034] In one embodiment, the computer-readable medium has recorded thereon machine-readable data, wherein the computer-readable medium, when used in conjunction with a machine programmed with instructions for using the data, is capable of generating image signals for depicting a graphical, three-dimensional representation of the PCSK9 polypeptide, or portion thereof.

[0035] In a further embodiment of the invention, there is provided a system for studying a PCSK9 polypeptide, said system comprising (a) a memory capable of storing information representing at least a portion of the PCSK9 polypeptide, wherein said memory comprises at least one first-type storage region, including a set of spatial coordinates specifying a location in a three dimensional space, and at least one second- type storage region comprising information representing a characteristic of one of a plurality of amino acids, said second-type storage regions being logically associated with said first-type storage regions in said memory to represent a geometric arrangement of at least one characteristic of said PCSK9 peptide in said three dimensional space; (b) a processor coupled to said memory to access said first-type storage regions and said second-type storage regions, wherein the processor generates image signals for depicting a visual image representing three dimensional image of said PCSK9 polypeptide in said three dimensional space based on data from said memory; and (c) a display coupled to said processor to receive said image signals, wherein the display depicts a visual three dimensional image of said PCSK9 polypeptide in said three dimensional space based on said image signals.

[0036] The use of X-ray structure determination, molecular design and selection and synthesis of compounds that associate with other polypeptides is known in the art. This invention, however, for the first time allows the use of structural coordinates from the PCSK9 polypeptide of SEQ. ID. No.: 1 for molecular design, and selection and synthesis of compounds that associate with PCSK9.

[0037] In one aspect of the invention, the structure coordinates of the invention can be displayed as, or converted to, a graphical representation, including three-dimensional shape representations. This can be accomplished using commercially available computer programs capable of generating graphical representations of molecules, or parts thereof, from a set of structural coordinates. Examples of computer programs capable of generating graphical representations of molecules, or parts thereof, from a set of structural coordinates are O (Alwyn Jones), Xf it, PyMOL, RasMol, and the like.

[0038] In another aspect of the invention, the structure of PCSK9 can be compared to, or superimposed over, other similar molecules, such as PCSK9-like molecules. Comparison of PCSK9 and other molecules for which a graphical structure or three- dimensional structural coordinates are available can be carried out with the aide of available software applications, such as the Molecular Similarity application of QUANTA (Molecular Simulations, Inc., Waltham, Mass.).

[0039] Compounds that associate with PCSK9 can also be computationally evaluated and designed by screening and selecting chemical entities or fragments thereof for their ability to associate with PCSK9. Several methods can be used to accomplish this aspect of the invention.

[0040] In one embodiment, one may visually inspect a computer-generated model of PCSK9 based on the structure coordinates described herein. Computer generated models of chemical entities or specific chemical moieties can then be positioned in or around the catalytic domain and evaluated based on energy minimization and molecular dynamics, using, for example, available programs such as CHARMM or AMBER. Positioning of the chemical entity or fragment can be accomplished, for example, with docking software such as Quanta and Sybyl. Additionally, known and commercially available computer programs can be used in selecting chemical entities or fragments. Once suitable chemical entities or fragments are selected, they can be assembled into a single compound, such as an inhibitor, mediator, or other regulatory compound. Known and commercially available model building software may assist in assembly.

[0041] In one aspect of the invention, compounds that associate with PCSK9 can be designed as a whole, rather than by assembly of specific chemical moieties or chemical entities. This embodiment can be carried out using computer programs such as LUDI (Biosym Technologies, San Diego, Calif.), LEGEND (Molecular Simulations, Burlington, Mass.), and Leap Frog (Tripos Associates, St. Louis, Mo.).

[0042] In one embodiment, a candidate compound is chosen based upon the desired sites of interaction with PCSK9 and the candidate compound in light of the sites of interaction identified previously. Once the specific candidate compound-PC S K9 interactions are determined, docking studies, using commercially available docking software, are performed to provide preliminary "modeled" complexes of selected candidate compound with PCSK9.

[0043] Constrained conformational analysis is performed using, for example, molecular dynamics (MD) to check the integrity of the modeled PCSK9-compound complex. Once the complex reaches its most favorable conformational state, the structure as proposed by the MD study is analyzed visually to ensure that the modeled complex complies with known experimental SAR/QSAR (structure-activity relationship/quantitative structure- activity relationship) based on measured binding affinities.

[0044] Other modeling techniques can also be used in accordance with the invention. Examples of these techniques are disclosed in Cohen et al., "Molecular Modeling Software and Methods for Medicinal Chemistry," J. Med. Chem., 33:883-894 (1990) and Navia et al., "The Use of Structural Information in Drug Design," Current Opinions in Structural Biology, 2:202-210 (1992), "Structure Based Drug Design", editor Verapandian herein incorporated by reference in the entirety.

[0045] Compounds developed or designed to associate with PCSK9 can be optimized or the efficiency of association can be tested using a number of methods known in the art. For example, the deformation energy and electrostatic interactions can be determined and optimized. Known and commercially available software and hardware systems can be used. Structure-based analoging for optimization of the PCSK9 associating compound's potency, selectivity and physical drug-like properties in an iterative manner can also be performed by one skilled in the art of drug design.

[0046] Substitutions can also be made to selected or designed compounds. These substitutions can be made to improve or modify the association properties of the compound. Such substitutions can be made, for example, in side groups or particular atoms of the compounds. Generally, one should begin with conservative substitutions that have approximately the same size, shape, charge and other characteristics of the original group or atom. Substituted compounds can be further analyzed and optimized as described above. [0047] In a further aspect of the invention, the potential inhibitory, mediatory, regulatory, or other binding effect of a compound can be analyzed and evaluated, using, for example, commercially available computer software, prior to actual synthesis and testing of such compound. In this way, one can evaluate the probability of synthesizing and testing of inoperative compounds.

[0048] In a further aspect of the invention, there is provided a method of identifying a compound that associates with PCSK9, comprising: (a) designing an associating compound for said polypeptide that forms a bond with a site on the PCSK9 molecule based on all or part of the coordinates of a PCSK9 polypeptide crystal (Table 1); (b) synthesizing said compound; and (c) determining the capability of said compound to modulate the activity of said PCSK9 polypeptide.

[0049] In one embodiment, the identified compound or polypeptide interacts with a site on PCSK9 defined by at least one of the sets of amino acids listed in Table 3. [0050] As used herein, "associate" means that the compounds may bind to or interact with PCSK9 ionically, covalently, via hydrogen bonding, Van der Waals interactions, salt bridges, steric interactions, hydrophilic interactions and/or hydrophobic interactions. Moreover, the term "associate" encompasses associations with any portion of PCSK9. For example, compounds that associate with PCSK9 can be compounds that act as competitive inhibitors, un-competitive inhibitors, and non-competitive inhibitors. Compounds that associate with PCSK9 can also be compounds that act as mediators or other regulatory compounds. Compounds that associate with PCSK9 can also be compounds that isomerize to short-lived reaction intermediates in the chemical reaction of a substrate with PCSK9. In particular, compounds designed to associate with PCSK9 can be used therapeutically as modulators of PCSK9 activity, such as inhibitors, mediators and other regulatory compounds.

[0051] In vitro procedures for measuring the effect compounds have on modulating the activity of PCSK9 generally are known in the art and are described in Example 3, infra.

Description of PCSK9 Structure

[0052] The crystal structure contains residues 29 to residues 692 of SEQ. ID 1.

For this structure, the construct contains a serine as residue 29 (replaces an alanine of residue 29 in SEQ. ID 1). Of these residues 29 to 60, 168 to 175, 213 to 219, 450 to 451, 572 to 583, 617 to 618, 640 to 641, 660 to 670 and 683 to 692 are not visible in the electron density and are not included in the three dimensional co-ordinates of table 1. [0053] The three dimensional PCSK9 molecule of the invention can be described, with reference to the Figures.

[0054] FIG. 1 is a ribbon diagram of PCSK9: Ribbon diagram of PCSK9 molecule detailing the overall fold of the molecule, the pro (auto-inhibitory domain) is colored red, the catalytic domain blue and the disulfide rich C-terminal domain green. Disulfide bonds within the molecule are represented as yellow sticks. Figure produced with Pymol (www.pymol.org).

[0055] FIG. 2 is a surface representation: Electrostatic surface representation of

PCSK9. Surface is colored red, blue and white to indicate electronegativity, electropositivity and neutrality respectively. Figure produced with PYMOL (www.pymol.org).

[0056] In designing and developing compounds that modulate PCSK9 activity, such as inhibitors, polypeptides, mediators and other compounds having activities with biological significance, that associate with PCSK9, it is desirable to select compounds with a view toward the particular surface contour, charge, shape, and other physical characteristics of PCSK9. Generally, the compounds should be capable of physically and structurally associating with PCSK9. [0057] The PCSK9 crystal structure of the invention demonstrates several structural peculiarities regarding surface contour, charge and shape, which facilitates the design of potent selective modulators of PCSK9 activity, particularly modulators that associate with the residues (or sets thereof) described in Table 3.

[0058] Mutations in PCSK9 are strongly associated with levels of low density lipoprotein cholesterol (LDL-c) in the blood plasma and thereby occurrence or resistance to atherosclerosis and coronary heart disease. Linkage to autosomal dominant familial hypercholesterolemia (ADH) via various genetic observations have suggested that gain of function mutations increase plasma levels of LDL-c whilst nonsense or missense mutations which interfere with folding or targeting of PCSK9 lead to a reduction of plasma levels of LDL-c. Over expression of PCSK9 in mice results in degradation of LDL-R and increased plasma LDL-c, suggesting that PCSK9 is involved in the regulation of LDL-R and its ability to clear LDL-c from the plasma.

[0059] The present invention is a crystal structure of a full-length construct of

PCSK-9 solved to 1.9A resolution. This represents the first structure of a full length mammalian pro-protein convertase enzyme and the first showing of an intact auto-inhibitory pro-domain. The structure contains a fully folded C-terminal disulfide rich domain (DRD), which differs in size, orientation and topology to the P domains of its eukaryotic relatives but shows a distinct structural similarity to the resistin homo-trimer, a small cytokine associated with obesity and diabetes. This structural relationship between the DRD of PCSK9 and resistin is not observed in primary sequence comparisons. The three-dimensional structure of the present invention gives insight into the function of PCSK9 at the molecular level and provides further association of PCSK9 with CHD, emphasizing its importance as a potential therapeutic target.

[0060] The core of the structure, conforms to a standard subtilisin-like serine protease domain, an alpha/beta protein consisting of a seven stranded parallel beta strand sandwiches between sets of helices, inhibited by its pro-domain. A C-terminal, accessory disulfide rich domain (DRD) is situated next to the catalytic domain forming a clover leaf of three sub-domains displaying clear pseudo-threefold axis. The DRD is loosely attached to the catalytic domain occluding a surface area of 1450A² at the interface between the protease domain. Despite the relatively weak binding between the domains and the presence of a flexible linker between them, it seems likely that this is the physiological conformation of the molecule as indicated by the solution and rigid body refinement of a structure at much lower resolution structure (-4.0A) in an unrelated space group which exhibited the same conformation (data not shown). Both chains are well defined in the electron density with the backbone clearly traced between Thr61-Arg 682 of the 692 residues in the full length construct. The exceptions are residues of loops 168-175 and 213-219 in the protease domain, the linker residues between the protease and the DRD (449-452) and two loops of this domain (572-583, 660-672) which are undefined in the electron density. A calcium atom is located in one of the known calcium binding sights co-ordinate by the side chains of Asp360 and Thr335 and the carbonyl side chain interactions of Ala 328, Ala 330, VaI 333 and Cys 358. [0061] The structure is closely aligned in both sequence and structure to the

Furin/Kexin/Subtilisin-like family of serine proteases. The structures of both murine Furin and yeast Kexin (Kex2) have been previously determined. As would be expected the structural homology between Kex2 and Furin is much closer (48% sequence identical) than that of PCSK9, (22 and 21% sequence identity respectively) with the root mean square deviations between Furin and Kex2 being to 0.95 A (on 301 aligned Ca s) as opposed to 1.57 and 1.51 A with PCSK9 (on 192 and 172 aligned Ca).

[0062] Seven of the characterized mammalian pro-protein convertases, including

Furin and Kex2 show a preference for mono- and di -basic substrate residues at the S 1 pocket of the enzyme whilst one other family member, PCSK8 (also known as SKI-I and Site-1 protease) shows preference for non-basic substrate residues at the S 1 pocket. The catalytic triad of PCSK9 (H224, S386 and D186) is conserved and completely superimposable with all serine protease active sites suggesting that in the absence of the inhibitory pro-domain, PCSK9 would be an active protease. The active site of PCSK9 contains the consensus sequence, GTS(A/V)(A/S)P, found in the S8B clan of proteases that contains the active serine nucleophile S386 with the exception that the C-terminal proline is substituted by an alanine and the traditionally aliphatic A/V residue is a glutamine. The DDG motif associated with the active site D384 is not conserved in PCSK9 showing instead a DTS motif and the HGTR, containing (H226), motif is altered at the C-terminal position by a histidine. Relative to the other members of the proprotein convertase family PCSK9 is an outlier, the only known physiologic substrate, the auto-processing sequence LVFAQISIPWN and structure suggest a preference in the Pl site for a glutamine or glutamic acid followed by hydrophobic residues in P2, P3 and P4. The active site of Furin is more occluded at the Pl position largely due to the insertion of two loops relative to PCSK9. In contrast to the Kex2 proteases Asp306 at the bottom of the Pl pocket is substituted by a tyrosine residue (325) excluding the possibility of a non-basic Pl specificity for PCSK9. The inhibitory Glnl52 from the pro-domain does not extend far into the S 1 pocket but instead the side chain is directed to the side of the pocket by a side chain oxygen and main chain nitrogen (Asn317) hydrogen bond (2.7A). An alanine positioned at the P2 position, of the prodomain peptide fits tightly within the hydrophobic lined S2 pocket suggesting a preference for a small residue. The site of the naturally occurring human loss-of-function mutation L253F is present in the catalytic S2 pocket suggesting that this highly conserved residue is essential for correct functioning of the molecule and is sensitive to mutation.

[0063] A number of structures of bacterial subtilisin-like proteases complexed with their prodomain inhibitors are publicly available. These proteins are expressed as a single chain with the pro-domain constituting the first 70 or so residues of the N-terminus. This pro-domain appears to be essential for proper folding of the intact molecule. Maturation of the protease is a two step process initiated by an auto-cleavage event whereby the immature protease cleaves itself, (at site LVF AQISIPWN in PCSK9) into a two chain molecule leaving the C-terminus of the pro-domain in the active site and the pro-domain attached to the head of the protease domain. The second maturation step is generally achieved via further proteolytic processing or a change in environmental stimulus, such as a change in pH or increase in Ca²⁺ concentration. The PCSK9 catalytic/pro-domain pair is structurally very similar to the bacterial structures (rmsds 1.59 A and 1.60A with pdb ids lscj and lspb on 293 and 286 aligned Ca atoms respectively). An ordered motif at the N-terminal end of the PCSK9 pro-domain exists relative to the bacterial structures (aa 61-76). This serves to extend the central pro-domain beta sheet from four to fives strands and to form a "cover" over the active site. These ancillary residues increase the occluded area between the two domains from 2180 A² in the bacterial proteases to 2638 A² in PCSK9 and contribute a number of additional interactions with the catalytic domain.

[0064] Other members of the subtilisin/kexin family have a conserved 150 residue

P-domain mostly present in eukaryotic proprotein convertases/kexins. The presence of this domain appears to have arisen at the same time the protein's specificity for basic resides was established. The P-domain appears to be necessary for the correct functioning/folding of the protein. Of the two eukaryotic proteases solved furin and Kex2 both adopt the same conformation for the 150 residues P-domain which exhibits a jelly roll like fold consisting of two four-stranded anti-parallel beta sheets with a single helix. As a result of its jelly roll beta structure the domain shares a loose topological homology to many beta-barrel structures. In contrast to this, PCSK-9 has a larger C-terminal domain of around 240 residues (residues 453-692) containing a large number of cysteine residues paired to form nine disulfide bonds. There are some similarities between the C-terminal domains from Furin and PCSK9 in that both contain jelly roll type structures. However, the C-terminal domain from PCSK9 consists of three, three-stranded beta domains arranged in a pseudo-threefold with no helices whereas the P-domain of furin has one four stranded anti-parallel beta sheet. In addition the disulfide rich C-terminal domain (DRD) of PCSK9 is positioned in a different orientation relative to the P-domain of Furin and does not appear to form the tight binding interface that Furin shares with its P-domain. Each of the sub-domains in the DRD of PCSK9 consists of three structurally conserved disulfide bonds, arranged such that the six cysteines are bonded in a 1- 6,2-5,3-4 arrangement with a consensus pattern of C(aal8-20)C(aa9-10)C(aa23- 26)C(aal8)CC within each sub-domain. Searching the human proteome for this pattern reveals a number of plasma proteins which display this motif. Domains from Fibronectin, the ADAM family of proteins and the urokinase type plasminogen Activator (uPA) receptor (uPA) contain the motif but do not exhibit the same fold. Other proprotein convertase family members also include the motif, proprotein convertase-5 and proprotein convertase-6, both basic paired proteases, contain only one instance. Indeed, excluding proteins from the extremely cysteine rich keratin family only PCSK9 and a hypothetical protein (genbank accession number XP_001133083.1) contain this motif exactly three times. Of those proteins found which match the cysteine pattern and whose structures are known, none are structurally homologous, with the exception of a remarkably similarity seen between one of the jelly roll "sub-domains" of the DRD and the C-terminal 70 residues of the structure of resistin (FIZZ3, pdb reference IRHF), the only other six-stranded beta barrel known. Recently, the adipocytokine resistin has been linked with Type II diabetes and is thought to antagonize insulin secretion. The resistin protein is characterized by an approximately 30 residue three- stranded alpha helical coiled-coil topped by a 70 residue six-stranded beta strand jelly roll structure. This results in a homo-trimeric arrangement of the molecule with each monomer containing five disulfide bonds of which three are in the six stranded jelly role "head" domain. The remaining disulfides occur in the alpha helical coiled coil segment the N- terminal disulfide contributing to an inter-chain disulfide responsible for the formation of resistin hexamers. In comparison to this, the DRD C-terminal domain of PCSK-9 contains two hundred and ten residues and forms a hetero-pseudotrimeric structure, completely structurally equivalent to the resistin homo-trimer but without the alpha helical "tails" of resistin. The sequence identity between the hetero- and homo-trimer is 15.28%, whereas a structural alignment over the whole hetero- verses homo-trimer produces an rmsd of 1.9A on aligned Ca atoms. This coupled with the identical positions of the disulfides within the primary sequence and the structure, insinuates that the two have an evolutionary relationship and indicates a receptor-like function for the DRD. The most obvious candidate region for interaction region being the head region containing the nine loops of the beta turns surrounding the deep cleft at the center of the pseudo-threefold. The topological arrangement of beta strands between the two molecules is identical but the loops connecting the beta strands to the head of the trimer in resistin of the molecule are conformationally divergent suggesting an alternative binding partner. An RGD primary sequence motif present in the P- domains (residues 496-498, RGE) is situated in the beta sheet of the second lobe of the first sub-domain of the DRD and is largely occluded from the solvent. [0065] A number of genetic studies of naturally occurring variants of PCSK9 have indicated that loss-of- function results in the maintenance of very low plasma levels of LDL-c whilst gain-of-function mutations are associated with hypercholerolemia and risk of coronary heart disease. If the general model that PCSK9 is responsible for plasma LDL-R levels and thus plasma LDL-c levels, then loss-of-function mutations can be linked with nonsense mutations or those mutation related to processing/folding/active site abnormalities within PCSK9 which thus increase levels of LDL-R. One example in the DRD is the nonsense mutation C679X; this mutation occurs in the penultimate disulfide bond suggesting a disruption in the folding pattern of the DRD and thus a loss-of-function from incorrect processing or folding of the molecule. Gain-of-function mutations are likely more diverse in their phenotypic action, the general hypothesis being that the mutations increase the binding affinity for substrates or decrease the affinity of pro-domain inhibitors thus providing a more active molecule. There are three main regions of gain-of-function mutations: one region at the negatively charged lip of the active site where D374T presumably increases the binding affinity for its substrate; one mutation in the prodomain S127R almost certainly increasing the susceptibility of the domain to cleavage by proteases such as furin; and one region at both the front and back ends of the first sub-domain of the DRD. Those in the DRD are particularly interesting and validate the importance of the DRD in function. The two mutations R469W and F515L occur in the putative binding region of the DRD at the head of the domain within the first monomer of the hetero-trimer.

[0066] The structure of the present invention provides valuable insight into its specificity and function and the structural relationship to other cellular proteins, involved in similar interactions. Given the orientation of the DRD C-terminal domain and the enzymatic binding site it can be suggested that the C-terminal domain provides a means to localize the protease to the substrate molecule (LDL-R) or a receptor which localizes function, allowing the PCSK9 protease domain to facilitate degradation or removal of LDL-R. An alternative hypothesis would be the absence of proteolytic activity in PCSK9 altogether whereby binding of the DRD to the LDL-R (or other receptor) provides a signal to lower LDL-R levels. A non-proteolytic mechanism has been shown to exist in proteases of the trypsin family such as hepatocyte growth factor (HGF) whereby the protease has lost catalytic activity but functions as a growth factor receptor. An analogous situation may occur in PCSK9, with the exception that positive selection for the maintenance of the active site is apparent, as the protein must auto-cleave itself to enable the correct folding and secretion of the protein. This connection between structure and disease may be important to dissecting the complex pathway of PCSK9 in CHD.

Examples:

[0067] The following examples serve to illustrate the present invention but should not be construed as a limitation thereof.

Example 1

Expression and Crystallization of PCSK9

[0068] The full length DNA sequence encoding PCSK9 is amplified from a full length construct in the baculovirus expression vector pFastBacl by PCR. The full length baculovirus construct includes a fused hexa-histadine C-terminal affinity tag and the honeybee mellitin secretion signal substituted for the native signal peptide. The forward primer (5'-CCC AAG CTT GCC GCC ACC ATG AAA TTC TTA GTC AAC-3') incorporates a 5' HindIII restriction site and Kozak sequence. The reverse primer (5'-GC TCT AGA TCA GTG GTG GTG GTG GTG GTG GTG CTG GAG-3') includes a 3' Xbal restriction site and introduces a TGA stop codon. The amplified PCR product is purified, digested with HindIII and Xbal, and cloned into these respective sites of the pRS5a mammalian expression vector.

[0069] PCSK9 is expressed in a transient mammalian expression system. Two

500 mL HEK293 Freestyle (Invitrogen) suspension cultures at a density equal to 1 x 10⁶ cells/mL are prepared in IL vented shake flasks (Corning). The transfection mixture is prepared with 1 mg PCSK9 plasmid DNA and 1.5 mL 293fectin (Invitrogen). Each component is diluted separately in 50 mL OptiMEM I reduced serum free medium (Invitrogen). The 293fectin-OptiMEM I mixture is incubated for 5 minutes at room temperature before adding to the DNA-OptiMEM I mixture. The transfection mixture is incubated at room temperature for 30 minutes. 50 mL of the DNA-lipid complex is added to each HEK293 Freestyle suspension culture. Cultures are incubated at 37°C with 5% CO₂ on an orbital shaking platform at 125 rpm.

[0070] Forty-eight hours post-transfection, cultures are harvested by centrifugation at 1,200 rpm. The supernatant is reserved for affinity purification. Supernatant is loaded directly on to a 4 mL NiNTA (QIAGEN) gravity column equilibrated with 50 mM TrisHCl pH 7.4, 300 mM NaCl, 1 mM CaCl₂, 2 mM β-mercaptoethanol. The column is washed with 20 mL of equilibration buffer plus 20 mM imidazole. Bound PCSK9 is eluted in 12 mL of 50 mM TrisHCl pH 7.4, 250 mM imidazole, 300 mM NaCl, 1 mM CaCl₂, 2 mM β-mercaptoethanol. The protein is analyzed by SDS-PAGE and the identity verified by Western Blot with a PCSK9 specific antibody.

[0071] The eluted PCSK9 protein is subsequently dialyzed against 50 mM

TrisHCl pH 7.4, 150 mM NaCl, 1 mM CaCl₂, 2 mM β-mercaptoethanol and concentrated to 10 mg/mL in a 30,000 MWCO spin concentrator (Amicon).

[0072] Sitting drop vapour diffusion crystallization trials are set up in low profile

Greiner 96 well crystallization plates. A reservoir of 50μl of crystallization solution is added to the well reservoir whilst equal volumes of protein and crystallization solution (25OnI) are added to the crystallization shelf. Crystals formed within 3 weeks in a variety conditions all involving 16-26% w/v PEG-8000 and a pH greater than about 8.0. Example 2

Structure Determination of PCSK9

[0073] Data for the PCSK9 structure is collected at a synchrotron X-ray source or on a rotating anode system. Data are processed with standard data reduction packages such as Mosflm or HKL2000 and diffract in excess of 3.θA resolution. The three dimensional structure is solved using the molecular replacement method using two ensembles of a pro-domain structure (PDB identification: lscj and lspb) and one containing five representatives from the subtilisin-like serine protease family (PDB identifications: lcnm, Ish7, 2b6n, Ip8j, Ir64) and all data to 4.0A resolution. The structure is then built and refined until convergence with the crystallographic refinement program Refmac5. [0074] The structure coordinates obtained from a PCSK9 crystal of the invention are detailed in Table 1 , infra. Data collection and refinement statistics for a crystal of the invention are detailed in table 2, infra.

Example 3

Assay of PCSK9 Activity

[0075] Cell-based assays can be used for screening "loss of PCSK9 function" mediated by small molecule or polypeptides. The following list of cell-based assay strategies are applied to screen small molecule or polypeptides (therapeutic antibodies) that suppress PCSK9 function in low density lipoprotein receptor (LDLR) down- regulation: (1) PCSK9 secretion assay; (2) LDLR assay with adenoviral expression of PCSK9 or with exogenously added PCSK9 protein; (3) LDL-C uptake assay with adenoviral expression of PCSK9 or with exogenously added PCSK9 protein. [0076] (1) PCSK9 secretion assay: This assay is based on evidence that secreted PCSK9 plays an important role in LDLR down-regulation and only the auto- processed PCSK9 is secreted. Therefore, inhibition of PCSK9 auto-processing and/or the subsequent intracellular trafficking will reduce the level of PCSK9 secreted into medium. To enable a high throughput screen, HTRF readouts have been established to detect secreted PCSK9-His-Strep-3xFlag using anti-His^E7anti-Flag^XL or using anti- Pcsk9^Cy5/anti-His^Eu. Stable HEK293 and HepG2 cell lines constitutively expressing this PCSK fusion construct are generated and used for small molecule inhibitor screening. [0077] (2) LDLR assay with adenoviral expression of PCSK9 or with exogenously added PCSK9 protein: PCSK9 exerts its function in lipid regulation mainly by down-regulating hepatic LDLR level as shown with in vivo mouse studies using adenoviral expression or parabiosis. In cultured hepatocytes such as HepG2, either adenoviral expression of PCSK9 or addition of isolated PCSK9 protein decreases total intracellular or surface level of LDLR. The change in LDLR level has been detected by ELISA, flow cytometry, immunofluorescence or other traditional methods. To support small molecule and polypeptide screening, HTRF readout has been established for endogenous LDLR as well as for the HA-Strep-His-LDLR fusion protein. The LDLR- HTRF assay is being used to screen small molecule and polypeptide inhibitors using the native HepG2 or a HEK293 clone constitutively expressing HA-Strep-His-LDLR. [0078] (3) LDL-C uptake assay with adenoviral expression of PCSK9 or with exogenously added PCSK9 protein: LDLR is the major cellular receptor that internalizes the circulating LDL-C. The level of LDL-C uptake correlates well with the total or surface level of LDLR. Therefore, LDL-C uptake is used as the surrogate confirmation readout for regulation of LDLR mediated by PCSK9 expression or recombinant PCSK9 protein. Human or mouse hepatocytes are infected by adenovirus to endogenously express PCSK9 or incubated with exogenously added PCSK9 protein prior to exposure to LDL-DiI. The cells are then washed and subjected to FACS measurement for the internalized LDL-DiI.

Table 1

[0079] From left to right the columns of table 1 detail the atom number, the atom (for example nitrogen (N), and the like), the three dimensional amino acid code (for example, Threonine (THR), and the like), chain identifier (A, B, C, and the like; W for water molecules, residue number, 3 dimensional coordinates (next 3 columns), occupancy and atomic displacement factors.

ATOM 1 N THR A 61 46.124 28.260 51.047 1.00 40.07

ATOM 2 CA THR A 61 45.734 28.183 49.607 1.00 40.27

ATOM 4 CB THR A 61 46.472 26.973 48.861 1.00 42.02

ATOM 6 OGl THR A 61 46.374 25.761 49.638 1.00 47.94

ATOM 8 CG2 THR A 61 47.947 27.272 48.598 1.00 44.99

ATOM 12 C THR A 61 44.196 28.074 49.375 1.00 35.75

ATOM 13 O THR A 61 43.765 27.962 48.221 1.00 37.30

ATOM 17 N ALA A 62 43.370 28.055 50.424 1.00 30.10

ATOM 18 CA ALA A 62 41.922 27.828 50.210 1.00 27.58

ATOM 20 CB ALA A 62 41.241 27.287 51.447 1.00 28.06

ATOM 24 C ALA A 62 41.274 29.133 49.813 1.00 25.74

ATOM 25 O ALA A 62 41.530 30.139 50.457 1.00 21.65 ATOM 27 N THR A 63 40.450 29.132 48.759 1.00 22.80

ATOM 28 CA THR A 63 39.885 30.379 48.258 1.00 21.63

ATOM 30 CB THR A 63 40.441 30.689 46.821 1.00 21.88

ATOM 32 OGl THR A 63 40.197 29.561 45.970 1.00 19.67

ATOM 34 CG2 THR A 63 41.975 30.996 46.902 1.00 20.54

ATOM 38 C THR A 63 38.359 30.345 48.236 1.00 19.79

ATOM 39 O THR A 63 37.735 29.293 48.230 1.00 16.19

ATOM 41 N PHE A 64 37.765 31.521 48.192 1.00 18.87

ATOM 42 CA PHE A 64 36.330 31.672 48.180 1.00 18.58

ATOM 44 CB PHE A 64 35.921 32.631 49.300 1.00 18.73

ATOM 47 CG PHE A 64 34.455 32.909 49.347 1.00 19.19

ATOM 48 CDl PHE A 64 33.527 31.876 49.323 1.00 17.66

ATOM 50 CEl PHE A 64 32.148 32.148 49.351 1.00 14.67

ATOM 52 CZ PHE A 64 31.708 33.458 49.374 1.00 18.59

ATOM 54 CE 2 PHE A 64 32.614 34.493 49.369 1.00 16.94

ATOM 56 CD2 PHE A 64 33.977 34.239 49.359 1.00 18.27

ATOM 58 C PHE A 64 35.873 32.282 46.843 1.00 20.49

ATOM 59 O PHE A 64 36.534 33.192 46.291 1.00 22.00

ATOM 61 N HIS A 65 34.721 31.841 46.370 1.00 17.01

ATOM 62 CA HIS A 65 34.196 32.293 45.126 1.00 18.21

ATOM 64 CB HIS A 65 34.542 31.301 44.004 1.00 17.04

ATOM 67 CG HIS A 65 35.993 30.972 43.932 1.00 21.26

ATOM 68 NDl HIS A 65 36.900 31.738 43.236 1.00 21.01

ATOM 70 CEl HIS A 65 38.110 31.233 43.395 1.00 22.80

ATOM 72 NE 2 HIS A 65 38.022 30.171 44.178 1.00 18.66

ATOM 74 CD2 HIS A 65 36.711 30.001 44.544 1.00 23.03

ATOM 76 C HIS A 65 32.715 32.424 45.200 1.00 18.13

ATOM 77 O HIS A 65 32.023 31.563 45.754 1.00 19.70

ATOM 79 N ARG A 66 32.204 33.473 44.587 1.00 16.77

ATOM 80 CA ARG A 66 30.789 33.587 44.403 1.00 17.07

ATOM 82 CB ARG A 66 30.160 34.401 45.521 1.00 18.51

ATOM 85 CG ARG A 66 30.499 35.849 45.495 1.00 19.27

ATOM 88 CD ARG A 66 30.107 36.382 46.807 1.00 22.69

ATOM 91 NE ARG A 66 30.129 37.812 46.886 1.00 24.76

ATOM 93 CZ ARG A 66 30.034 38.463 48.048 1.00 29.10

ATOM 94 NHl ARG A 66 29.952 37.804 49.224 1.00 30.76

ATOM 97 NH2 ARG A 66 30.039 39.760 48.025 1.00 25.28

ATOM 100 C ARG A 66 30.461 34.208 43.061 1.00 17.38

ATOM 101 O ARG A 66 31.298 34.784 42.419 1.00 17.97

ATOM 103 N CYS A 67 29.216 34.039 42.679 1.00 18.77

ATOM 104 CA CYS A 67 28.754 34.350 41.349 1.00 19.72

ATOM 106 CB CYS A 67 27.304 33.939 41.194 1.00 19.83

ATOM 109 SG CYS A 67 26.668 34.117 39.563 1.00 22.90

ATOM 111 C CYS A 67 28.949 35.841 41.136 1.00 19.21

ATOM 112 O CYS A 67 28.659 36.661 42.023 1.00 19.12

ATOM 114 N ALA A 68 29.546 36.155 39.989 1.00 19.35

ATOM 115 CA ALA A 68 29.768 37.547 39.557 1.00 21.27

ATOM 117 CB ALA A 68 30.692 37.567 38.367 1.00 18.69

ATOM 121 C ALA A 68 28.458 38.234 39.191 1.00 21.44

ATOM 122 O ALA A 68 28.364 39.453 39.266 1.00 22.05

ATOM 124 N LYS A 69 27.473 37.467 38.726 1.00 23.30

ATOM 125 CA LYS A 69 26.148 37.998 38.386 1.00 24.17

ATOM 127 CB LYS A 69 25.406 37.100 37.379 1.00 26.65

ATOM 130 CG LYS A 69 26.163 36.723 36.100 1.00 32.44

ATOM 133 CD LYS A 69 25.743 37.555 34.898 1.00 39.94

ATOM 136 CE LYS A 69 26.635 37.283 33.656 1.00 38.40

ATOM 139 NZ LYS A 69 26.973 38.572 33.008 1.00 34.53

ATOM 143 C LYS A 69 25.397 38.051 39.697 1.00 24.94

ATOM 144 O LYS A 69 24.807 37.058 40.127 1.00 22.43

ATOM 146 N ASP A 70 25.431 39.207 40.358 1.00 24.62

ATOM 147 CA ASP A 70 24.951 39.305 41.739 1.00 26.48 ATOM 149 CB ASP A 70 25.096 40.745 42.294 1.00 27.40

ATOM 152 CG ASP A 70 25.299 40.780 43.806 1.00 31.37

ATOM 153 ODl ASP A 70 26.377 40.350 44.288 1.00 33.70

ATOM 154 OD2 ASP A 70 24.409 41.282 44.503 1.00 35.38

ATOM 155 C ASP A 70 23.519 38.797 41.939 1.00 25.68

ATOM 156 O ASP A 70 23.272 38.099 42.926 1.00 25.70

ATOM 158 N PRO A 71 22.587 39.094 41.009 1.00 26.11

ATOM 159 CA PRO A 71 21.204 38.592 41.158 1.00 25.50

ATOM 161 CB PRO A 71 20.498 39.125 39.894 1.00 24.92

ATOM 164 CG PRO A 71 21.362 40.245 39.412 1.00 28.03

ATOM 167 CD PRO A 71 22.738 39.873 39.762 1.00 26.69

ATOM 170 C PRO A 71 21.064 37.067 41.189 1.00 24.59

ATOM 171 O PRO A 71 20.040 36.555 41.651 1.00 26.36

ATOM 172 N TRP A 72 22.076 36.349 40.706 1.00 22.35

ATOM 173 CA TRP A 72 21.984 34.887 40.601 1.00 20.96

ATOM 175 CB TRP A 72 22.669 34.438 39.354 1.00 22.05

ATOM 178 CG TRP A 72 21.976 34.904 38.113 1.00 21.32

ATOM 179 CDl TRP A 72 20.777 35.555 38.021 1.00 23.10

ATOM 181 NEl TRP A 72 20.468 35.785 36.713 1.00 24.49

ATOM 183 CE 2 TRP A 72 21.452 35.251 35.926 1.00 23.62

ATOM 184 CD2 TRP A 72 22.418 34.692 36.783 1.00 23.69

ATOM 185 CE 3 TRP A 72 23.520 34.059 36.225 1.00 20.82

ATOM 187 CZ 3 TRP A 72 23.658 34.054 34.858 1.00 25.03

ATOM 189 CH2 TRP A 72 22.691 34.620 34.037 1.00 24.58

ATOM 191 CZ2 TRP A 72 21.579 35.214 34.551 1.00 26.39

ATOM 193 C TRP A 72 22.579 34.176 41.802 1.00 20.82

ATOM 194 O TRP A 72 22.515 32.952 41.894 1.00 19.40

ATOM 196 N ARG A 73 23.156 34.952 42.710 1.00 19.01

ATOM 197 CA ARG A 73 23.741 34.417 43.927 1.00 20.90

ATOM 199 CB ARG A 73 24.528 35.503 44.643 1.00 20.26

ATOM 202 CG ARG A 73 25.732 36.060 43.893 1.00 20.50

ATOM 205 CD ARG A 73 26.345 37.219 44.679 1.00 22.84

ATOM 208 NE ARG A 73 26.510 36.851 46.098 1.00 20.75

ATOM 210 CZ ARG A 73 26.513 37.716 47.099 1.00 24.89

ATOM 211 NHl ARG A 73 26.648 37.296 48.347 1.00 21.53

ATOM 214 NH2 ARG A 73 26.416 39.007 46.868 1.00 23.83

ATOM 217 C ARG A 73 22.666 33.889 44.877 1.00 20.94

ATOM 218 O ARG A 73 21.566 34.384 44.886 1.00 19.47

ATOM 220 N LEU A 74 23.016 32.886 45.688 1.00 22.01

ATOM 221 CA LEU A 74 22.134 32.331 46.698 1.00 23.08

ATOM 223 CB LEU A 74 21.636 30.939 46.274 1.00 23.51

ATOM 226 CG LEU A 74 20.786 30.909 44.997 1.00 23.71

ATOM 228 CDl LEU A 74 20.561 29.477 44.579 1.00 21.07

ATOM 232 CD2 LEU A 74 19.409 31.649 45.175 1.00 19.29

ATOM 236 C LEU A 74 22.919 32.237 47.996 1.00 23.33

ATOM 237 O LEU A 74 23.330 31.154 48.406 1.00 24.13

ATOM 239 N PRO A 75 23.133 33.383 48.652 1.00 24.14

ATOM 240 CA PRO A 75 23.889 33.481 49.882 1.00 24.26

ATOM 242 CB PRO A 75 23.693 34.943 50.315 1.00 24.21

ATOM 245 CG PRO A 75 23.171 35.658 49.145 1.00 24.55

ATOM 248 CD PRO A 75 22.600 34.686 48.203 1.00 24.14

ATOM 251 C PRO A 75 23.288 32.564 50.940 1.00 24.53

ATOM 252 O PRO A 75 22.093 32.250 50.887 1.00 25.54

ATOM 253 N GLY A 76 24.109 32.125 51.871 1.00 22.90

ATOM 254 CA GLY A 76 23.636 31.281 52.950 1.00 23.50

ATOM 257 C GLY A 76 23.802 29.794 52.720 1.00 22.12

ATOM 258 O GLY A 76 23.574 29.032 53.639 1.00 20.23

ATOM 260 N THR A 77 24.178 29.368 51.504 1.00 21.36

ATOM 261 CA THR A 77 24.510 27.951 51.241 1.00 20.60

ATOM 263 CB THR A 77 23.401 27.275 50.453 1.00 22.94

ATOM 265 OGl THR A 77 22.176 27.409 51.177 1.00 26.25 ATOM 267 CG2 THR A 77 23.700 25.773 50.207 1.00 25.19

ATOM 271 C THR A 77 25.788 27.936 50.448 1.00 19.96

ATOM 272 O THR A 77 25.936 28.746 49.532 1.00 15.71

ATOM 274 N TYR A 78 26.721 27.071 50.837 1.00 17.04

ATOM 275 CA TYR A 78 28.072 27.047 50.328 1.00 17.28

ATOM 277 CB TYR A 78 29.057 27.619 51.373 1.00 19.45

ATOM 280 CG TYR A 78 28.711 29.024 51.682 1.00 19.64

ATOM 281 CDl TYR A 78 29.234 30.068 50.900 1.00 21.78

ATOM 283 CEl TYR A 78 28.858 31.375 51.114 1.00 21.39

ATOM 285 CZ TYR A 78 27.996 31.696 52.140 1.00 21.66

ATOM 286 OH TYR A 78 27.688 33.047 52.299 1.00 24.77

ATOM 288 CE 2 TYR A 78 27.455 30.700 52.946 1.00 19.70

ATOM 290 CD2 TYR A 78 27.805 29.346 52.696 1.00 24.39

ATOM 292 C TYR A 78 28.453 25.620 49.984 1.00 17.56

ATOM 293 O TYR A 78 28.123 24.666 50.729 1.00 15.34

ATOM 295 N VAL A 79 29.119 25.482 48.843 1.00 16.89

ATOM 296 CA VAL A 79 29.737 24.234 48.431 1.00 16.96

ATOM 298 CB VAL A 79 29.566 24.005 46.905 1.00 15.47

ATOM 300 CGl VAL A 79 30.168 22.691 46.501 1.00 17.82

ATOM 304 CG2 VAL A 79 28.104 24.012 46.524 1.00 19.40

ATOM 308 C VAL A 79 31.211 24.250 48.836 1.00 16.73

ATOM 309 O VAL A 79 32.008 25.103 48.365 1.00 18.86

ATOM 311 N VAL A 80 31.579 23.336 49.728 1.00 14.56

ATOM 312 CA VAL A 80 32.903 23.254 50.260 1.00 15.07

ATOM 314 CB VAL A 80 32.942 23.019 51.786 1.00 16.71

ATOM 316 CGl VAL A 80 34.416 22.833 52.279 1.00 14.49

ATOM 320 CG2 VAL A 80 32.271 24.198 52.502 1.00 18.68

ATOM 324 C VAL A 80 33.578 22.180 49.495 1.00 17.77

ATOM 325 O VAL A 80 33.159 20.993 49.547 1.00 17.28

ATOM 327 N VAL A 81 34.557 22.600 48.689 1.00 15.64

ATOM 328 CA VAL A 81 35.246 21.675 47.838 1.00 17.24

ATOM 330 CB VAL A 81 35.400 22.200 46.415 1.00 18.07

ATOM 332 CGl VAL A 81 36.092 21.156 45.580 1.00 17.37

ATOM 336 CG2 VAL A 81 34.026 22.652 45.855 1.00 16.77

ATOM 340 C VAL A 81 36.592 21.349 48.411 1.00 17.70

ATOM 341 O VAL A 81 37.418 22.219 48.659 1.00 17.75

ATOM 343 N LEU A 82 36.817 20.056 48.627 1.00 19.11

ATOM 344 CA LEU A 82 38.032 19.607 49.255 1.00 18.52

ATOM 346 CB LEU A 82 37.729 18.517 50.276 1.00 18.66

ATOM 349 CG LEU A 82 36.703 18.851 51.369 1.00 18.46

ATOM 351 CDl LEU A 82 36.510 17.700 52.321 1.00 21.45

ATOM 355 CD2 LEU A 82 37.058 20.116 52.120 1.00 20.91

ATOM 359 C LEU A 82 39.020 19.154 48.188 1.00 19.65

ATOM 360 O LEU A 82 38.642 18.986 47.042 1.00 19.85

ATOM 362 N LYS A 83 40.276 18.954 48.565 1.00 20.15

ATOM 363 CA LYS A 83 41.318 18.645 47.606 1.00 24.36

ATOM 365 CB LYS A 83 42.704 18.715 48.244 1.00 26.15

ATOM 368 CG LYS A 83 43.128 20.153 48.628 1.00 31.52

ATOM 371 CD LYS A 83 44.236 20.093 49.673 1.00 35.75

ATOM 374 CE LYS A 83 44.766 21.468 50.058 1.00 39.37

ATOM 377 NZ LYS A 83 45.177 21.428 51.529 1.00 43.52

ATOM 381 C LYS A 83 41.059 17.284 47.006 1.00 25.08

ATOM 382 O LYS A 83 40.482 16.440 47.652 1.00 22.66

ATOM 384 N GLU A 84 41.472 17.123 45.757 1.00 27.88

ATOM 385 CA GLU A 84 41.138 15.982 44.902 1.00 31.24

ATOM 387 CB GLU A 84 42.116 15.979 43.718 1.00 31.58

ATOM 390 CG GLU A 84 41.916 14.831 42.745 1.00 38.76

ATOM 393 CD GLU A 84 42.379 15.166 41.324 1.00 48.02

ATOM 394 OEl GLU A 84 42.520 16.376 40.999 1.00 51.76

ATOM 395 OE 2 GLU A 84 42.579 14.213 40.530 1.00 50.52

ATOM 396 C GLU A 84 41.166 14.596 45.542 1.00 31.83 ATOM 397 O GLU A 84 40.267 13.775 45.337 1.00 34.86

ATOM 399 N GLU A 85 42.199 14.301 46.282 1.00 32.26

ATOM 400 CA GLU A 85 42.347 12.914 46.760 1.00 33.71

ATOM 402 CB GLU A 85 43.831 12.534 46.751 1.00 34.02

ATOM 405 CG GLU A 85 44.447 12.504 45.302 1.00 40.71

ATOM 408 CD GLU A 85 45.922 12.993 45.235 1.00 40.42

ATOM 409 OEl GLU A 85 46.183 14.237 45.290 1.00 50.83

ATOM 410 OE 2 GLU A 85 46.822 12.121 45.104 1.00 53.51

ATOM 411 C GLU A 85 41.652 12.697 48.128 1.00 28.90

ATOM 412 O GLU A 85 41.686 11.610 48.704 1.00 29.09

ATOM 414 N THR A 86 40.945 13.710 48.607 1.00 24.66

ATOM 415 CA THR A 86 40.237 13.605 49.890 1.00 22.50

ATOM 417 CB THR A 86 39.556 14.916 50.257 1.00 21.92

ATOM 419 OGl THR A 86 40.543 15.960 50.191 1.00 19.83

ATOM 421 CG2 THR A 86 38.971 14.819 51.642 1.00 21.98

ATOM 425 C THR A 86 39.205 12.484 49.877 1.00 21.35

ATOM 426 O THR A 86 38.409 12.351 48.938 1.00 18.96

ATOM 428 N HIS A 87 39.224 11.692 50.938 1.00 19.62

ATOM 429 CA HIS A 87 38.349 10.537 51.054 1.00 20.66

ATOM 431 CB HIS A 87 39.037 9.445 51.879 1.00 19.67

ATOM 434 CG HIS A 87 38.345 8.126 51.827 1.00 21.72

ATOM 435 NDl HIS A 87 37.291 7.792 52.657 1.00 25.25

ATOM 437 CEl HIS A 87 36.896 6.558 52.392 1.00 24.05

ATOM 439 NE 2 HIS A 87 37.646 6.087 51.406 1.00 19.08

ATOM 441 CD2 HIS A 87 38.567 7.043 51.043 1.00 21.68

ATOM 443 C HIS A 87 37.024 10.911 51.702 1.00 20.82

ATOM 444 O HIS A 87 36.948 11.837 52.543 1.00 21.25

ATOM 446 N LEU A 88 35.959 10.212 51.309 1.00 18.24

ATOM 447 CA LEU A 88 34.640 10.451 51.886 1.00 18.74

ATOM 449 CB LEU A 88 33.681 9.348 51.476 1.00 19.56

ATOM 452 CG LEU A 88 32.306 9.458 52.083 1.00 17.20

ATOM 454 CDl LEU A 88 31.669 10.841 51.823 1.00 14.60

ATOM 458 CD2 LEU A 88 31.413 8.319 51.566 1.00 18.58

ATOM 462 C LEU A 88 34.672 10.552 53.425 1.00 19.42

ATOM 463 O LEU A 88 33.990 11.388 54.006 1.00 17.71

ATOM 465 N SER A 89 35.397 9.658 54.088 1.00 19.06

ATOM 466 CA SER A 89 35.481 9.704 55.548 1.00 19.73

ATOM 468 CB SER A 89 36.348 8.569 56.084 1.00 19.70

ATOM 471 OG SER A 89 35.636 7.347 56.051 1.00 22.04

ATOM 473 C SER A 89 36.074 11.040 56.023 1.00 19.99

ATOM 474 O SER A 89 35.629 11.599 57.033 1.00 21.65

ATOM 476 N GLN A 90 37.073 11.533 55.305 1.00 19.97

ATOM 477 CA GLN A 90 37.695 12.810 55.642 1.00 21.64

ATOM 479 CB GLN A 90 39.001 13.012 54.880 1.00 22.89

ATOM 482 CG GLN A 90 40.092 11.990 55.190 1.00 24.91

ATOM 485 CD GLN A 90 41.258 12.077 54.224 1.00 24.49

ATOM 486 OEl GLN A 90 41.103 11.958 53.014 1.00 23.77

ATOM 487 NE 2 GLN A 90 42.434 12.302 54.763 1.00 30.91

ATOM 490 C GLN A 90 36.703 13.942 55.361 1.00 21.04

ATOM 491 O GLN A 90 36.609 14.879 56.145 1.00 21.41

ATOM 493 N SER A 91 35.924 13.865 54.275 1.00 19.52

ATOM 494 CA SER A 91 34.898 14.893 53.989 1.00 17.58

ATOM 496 CB SER A 91 34.226 14.662 52.604 1.00 18.24

ATOM 499 OG SER A 91 35.197 14.633 51.574 1.00 17.59

ATOM 501 C SER A 91 33.835 14.978 55.076 1.00 19.62

ATOM 502 O SER A 91 33.452 16.075 55.532 1.00 18.65

ATOM 504 N GLU A 92 33.360 13.820 55.516 1.00 19.15

ATOM 505 CA GLU A 92 32.367 13.776 56.562 1.00 19.86

ATOM 507 CB GLU A 92 31.879 12.330 56.758 1.00 19.73

ATOM 510 CG GLU A 92 31.041 11.837 55.646 1.00 21.15

ATOM 513 CD GLU A 92 30.666 10.339 55.740 1.00 23.18 ATOM 514 OEl GLU A 92 31.281 9.605 56.544 1.00 21.93

ATOM 515 OE 2 GLU A 92 29.751 9.917 54.981 1.00 29.46

ATOM 516 C GLU A 92 32.929 14.338 57.872 1.00 20.32

ATOM 517 O GLU A 92 32.251 15.089 58.566 1.00 21.04

ATOM 519 N ARG A 93 34.155 13.950 58.215 1.00 20.28

ATOM 520 CA ARG A 93 34.786 14.465 59.405 1.00 22.23

ATOM 522 CB ARG A 93 36.118 13.788 59.641 1.00 22.64

ATOM 525 CG ARG A 93 35.936 12.388 60.186 1.00 25.89

ATOM 528 CD ARG A 93 37.230 11.630 60.193 1.00 34.60

ATOM 531 NE ARG A 93 36.985 10.197 60.093 1.00 41.42

ATOM 533 CZ ARG A 93 37.860 9.317 59.615 1.00 44.83

ATOM 534 NHl ARG A 93 39.049 9.710 59.154 1.00 47.13

ATOM 537 NH2 ARG A 93 37.528 8.028 59.581 1.00 46.63

ATOM 540 C ARG A 93 34.991 15.967 59.310 1.00 21.23

ATOM 541 O ARG A 93 34.844 16.663 60.287 1.00 20.77

ATOM 543 N THR A 94 35.348 16.450 58.132 1.00 21.12

ATOM 544 CA THR A 94 35.514 17.905 57.932 1.00 21.24

ATOM 546 CB THR A 94 36.188 18.194 56.631 1.00 21.22

ATOM 548 OGl THR A 94 37.481 17.597 56.669 1.00 21.29

ATOM 550 CG2 THR A 94 36.346 19.720 56.431 1.00 20.81

ATOM 554 C THR A 94 34.202 18.658 58.089 1.00 19.88

ATOM 555 O THR A 94 34.156 19.715 58.739 1.00 22.72

ATOM 557 N ALA A 95 33.119 18.103 57.578 1.00 17.95

ATOM 558 CA ALA A 95 31.810 18.672 57.781 1.00 19.53

ATOM 560 CB ALA A 95 30.756 17.902 57.019 1.00 18.04

ATOM 564 C ALA A 95 31.436 18.751 59.244 1.00 21.80

ATOM 565 O ALA A 95 30.897 19.757 59.681 1.00 24.23

ATOM 567 N ARG A 96 31.668 17.666 59.978 1.00 22.17

ATOM 568 CA ARG A 96 31.364 17.613 61.392 1.00 23.01

ATOM 570 CB ARG A 96 31.642 16.204 61.969 1.00 25.38

ATOM 573 CG ARG A 96 30.864 15.056 61.307 1.00 31.81

ATOM 576 CD ARG A 96 29.474 15.434 60.700 1.00 40.78

ATOM 579 NE ARG A 96 29.210 14.700 59.449 1.00 43.63

ATOM 581 CZ ARG A 96 28.140 14.830 58.673 1.00 41.98

ATOM 582 NHl ARG A 96 27.138 15.648 58.995 1.00 40.63

ATOM 585 NH2 ARG A 96 28.067 14.098 57.560 1.00 43.83

ATOM 588 C ARG A 96 32.200 18.619 62.144 1.00 20.36

ATOM 589 O ARG A 96 31.697 19.257 63.029 1.00 23.81

ATOM 591 N ARG A 97 33.459 18.765 61.781 1.00 21.26

ATOM 592 CA ARG A 97 34.335 19.698 62.434 1.00 22.35

ATOM 594 CB ARG A 97 35.723 19.549 61.885 1.00 24.23

ATOM 597 CG ARG A 97 36.744 20.409 62.572 1.00 30.00

ATOM 600 CD ARG A 97 38.081 20.151 61.974 1.00 40.83

ATOM 603 NE ARG A 97 39.043 21.121 62.485 1.00 49.89

ATOM 605 CZ ARG A 97 39.808 20.946 63.559 1.00 52.36

ATOM 606 NHl ARG A 97 39.782 19.803 64.247 1.00 56.64

ATOM 609 NH2 ARG A 97 40.639 21.913 63.927 1.00 53.15

ATOM 612 C ARG A 97 33.803 21.117 62.278 1.00 23.46

ATOM 613 O ARG A 97 33.674 21.849 63.255 1.00 22.37

ATOM 615 N LEU A 98 33.434 21.481 61.052 1.00 22.70

ATOM 616 CA LEU A 98 32.786 22.755 60.787 1.00 21.01

ATOM 618 CB LEU A 98 32.398 22.825 59.298 1.00 20.40

ATOM 621 CG LEU A 98 31.662 24.097 58.945 1.00 21.66

ATOM 623 CDl LEU A 98 32.512 25.329 59.478 1.00 18.63

ATOM 627 CD2 LEU A 98 31.415 24.106 57.454 1.00 21.66

ATOM 631 C LEU A 98 31.554 22.984 61.655 1.00 22.15

ATOM 632 O LEU A 98 31.392 24.054 62.267 1.00 22.68

ATOM 634 N GLN A 99 30.673 22.002 61.740 1.00 21.87

ATOM 635 CA GLN A 99 29.437 22.180 62.497 1.00 23.30

ATOM 637 CB GLN A 99 28.536 20.976 62.366 1.00 24.75

ATOM 640 CG GLN A 99 27.944 20.735 60.978 1.00 27.62 ATOM 643 CD GLN A 99 26.695 19.915 61.074 1.00 30.39

ATOM 644 OEl GLN A 99 26.760 18.696 61.274 1.00 28.23

ATOM 645 NE2 GLN A 99 25.539 20.571 60.950 1.00 29.68

ATOM 648 C GLN A 99 29.746 22.382 63.976 1.00 23.44

ATOM 649 O GLN A 99 29.045 23.121 64.647 1.00 25.44

ATOM 651 N ALA A 100 30.764 21.682 64.469 1.00 25.47

ATOM 652 CA ALA A 100 31.208 21.793 65.874 1.00 26.77

ATOM 654 CB ALA A 100 32.207 20.707 66.207 1.00 25.56

ATOM 658 C ALA A 100 31.829 23.159 66.140 1.00 27.48

ATOM 659 O ALA A 100 31.506 23.814 67.114 1.00 25.92

ATOM 661 N GLN A 101 32.750 23.558 65.268 1.00 28.11

ATOM 662 CA GLN A 101 33.402 24.867 65.370 1.00 28.47

ATOM 664 CB GLN A 101 34.500 24.997 64.338 1.00 28.73

ATOM 667 CG GLN A 101 35.713 24.157 64.649 1.00 28.34

ATOM 670 CD GLN A 101 36.786 24.288 63.618 1.00 32.66

ATOM 671 OEl GLN A 101 36.598 24.960 62.607 1.00 34.10

ATOM 672 NE2 GLN A 101 37.939 23.649 63.857 1.00 37.34

ATOM 675 C GLN A 101 32.403 25.991 65.230 1.00 28.38

ATOM 676 O GLN A 101 32.513 27.011 65.919 1.00 31.09

ATOM 678 N ALA A 102 31.415 25.810 64.364 1.00 26.27

ATOM 679 CA ALA A 102 30.315 26.776 64.221 1.00 26.30

ATOM 681 CB ALA A 102 29.428 26.416 63.008 1.00 24.45

ATOM 685 C ALA A 102 29.467 26.876 65.490 1.00 28.17

ATOM 686 O ALA A 102 29.185 27.967 65.988 1.00 27.47

ATOM 688 N ALA A 103 29.029 25.722 65.983 1.00 30.23

ATOM 689 CA ALA A 103 28.211 25.620 67.195 1.00 31.50

ATOM 691 CB ALA A 103 27.912 24.154 67.552 1.00 31.13

ATOM 695 C ALA A 103 28.877 26.275 68.359 1.00 32.17

ATOM 696 O ALA A 103 28.205 26.887 69.149 1.00 33.96

ATOM 698 N ARG A 104 30.184 26.153 68.462 1.00 34.27

ATOM 699 CA ARG A 104 30.929 26.792 69.538 1.00 37.26

ATOM 701 CB ARG A 104 32.380 26.316 69.552 1.00 37.13

ATOM 704 CG ARG A 104 32.542 24.885 70.031 1.00 40.21

ATOM 707 CD ARG A 104 34.011 24.570 70.346 1.00 43.53

ATOM 710 NE ARG A 104 34.613 23.629 69.386 1.00 50.51

ATOM 712 CZ ARG A 104 35.491 23.932 68.425 1.00 53.48

ATOM 713 NHl ARG A 104 35.921 25.185 68.212 1.00 52.59

ATOM 716 NH2 ARG A 104 35.938 22.949 67.649 1.00 54.70

ATOM 719 C ARG A 104 30.907 28.314 69.405 1.00 36.44

ATOM 720 O ARG A 104 31.108 29.030 70.385 1.00 36.87

ATOM 722 N ARG A 105 30.679 28.807 68.198 1.00 34.92

ATOM 723 CA ARG A 105 30.601 30.237 67.983 1.00 34.30

ATOM 725 CB ARG A 105 31.266 30.616 66.660 1.00 34.97

ATOM 728 CG ARG A 105 32.746 30.370 66.669 1.00 37.96

ATOM 731 CD ARG A 105 33.399 30.989 65.466 1.00 47.66

ATOM 734 NE ARG A 105 34.836 30.726 65.445 1.00 52.43

ATOM 736 CZ ARG A 105 35.759 31.528 64.907 1.00 54.43

ATOM 737 NHl ARG A 105 35.438 32.690 64.349 1.00 55.32

ATOM 740 NH2 ARG A 105 37.037 31.167 64.944 1.00 54.39

ATOM 743 C ARG A 105 29.176 30.725 68.011 1.00 33.41

ATOM 744 O ARG A 105 28.922 31.889 67.721 1.00 33.89

ATOM 746 N GLY A 106 28.239 29.842 68.332 1.00 31.85

ATOM 747 CA GLY A 106 26.834 30.211 68.429 1.00 31.48

ATOM 750 C GLY A 106 26.067 30.134 67.122 1.00 31.96

ATOM 751 O GLY A 106 24.960 30.649 67.036 1.00 32.62

ATOM 753 N TYR A 107 26.637 29.468 66.109 1.00 31.03

ATOM 754 CA TYR A 107 26.031 29.380 64.788 1.00 30.11

ATOM 756 CB TYR A 107 27.106 29.640 63.738 1.00 29.61

ATOM 759 CG TYR A 107 27.522 31.082 63.633 1.00 28.69

ATOM 760 CDl TYR A 107 26.989 31.903 62.645 1.00 27.49

ATOM 762 CEl TYR A 107 27.371 33.221 62.523 1.00 28.65 ATOM 764 CZ TYR A 107 28.285 33.739 63.394 1.00 29.50

ATOM 765 OH TYR A 107 28.654 35.056 63.263 1.00 30.48

ATOM 767 CE 2 TYR A 107 28.846 32.943 64.389 1.00 27.99

ATOM 769 CD2 TYR A 107 28.461 31.629 64.502 1.00 30.28

ATOM 771 C TYR A 107 25.405 28.015 64.519 1.00 29.88

ATOM 772 O TYR A 107 26.039 27.006 64.745 1.00 30.39

ATOM 774 N LEU A 108 24.171 28.010 64.036 1.00 30.30

ATOM 775 CA LEU A 108 23.515 26.820 63.519 1.00 32.25

ATOM 111 CB LEU A 108 21.992 27.007 63.489 1.00 32.68

ATOM 780 CG LEU A 108 21.326 27.106 64.^; 1.00 39.70

ATOM 782 CDl LEU A 108 19.986 27.843 64.^; 1.00 40.95

ATOM 786 CD2 LEU A 108 21.153 25.726 65.505 1.00 41.98

ATOM 790 C LEU A 108 24.055 26.552 62.101 1.00 31.53

ATOM 791 O LEU A 108 24.299 27.482 61.338 1.00 32.12

ATOM 793 N THR A 109 24.301 25.290 61.793 1.00 30.07

ATOM 794 CA THR A 109 24.663 24.880 60.443 1.00 29.19

ATOM 796 CB THR A 109 26.145 24.566 60.319 1.00 29.51

ATOM 798 OGl THR A 109 26.510 23.574 61.276 1.00 30.19

ATOM 800 CG2 THR A 109 26.970 25.806 60.551 1.00 28.82

ATOM 804 C THR A 109 23.853 23.658 60.044 1.00 28.65

ATOM 805 O THR A 109 23.315 22.955 60.886 1.00 27.97

ATOM 807 N LYS A 110 23.748 23.417 58.749 1.00 26.86

ATOM 808 CA LYS A 110 23.123 22.213 58.264 1.00 26.84

ATOM 810 CB LYS A 110 21.686 22.509 57.860 1.00 25.55

ATOM 813 CG LYS A 110 20.771 21.310 57.919 1.00 34.50

ATOM 816 CD LYS A 110 19.290 21.692 57.659 1.00 35.04

ATOM 819 CE LYS A 110 18.599 20.651 56.757 1.00 41.97

ATOM 822 NZ LYS A 110 17.314 21.164 56.137 1.00 44.90

ATOM 826 C LYS A 110 23.948 21.720 57.099 1.00 23.77

ATOM 827 O LYS A 110 24.216 22.480 56.154 1.00 20.20

ATOM 829 N ILE A 111 24.391 20.460 57.196 1.00 22.69

ATOM 830 CA ILE A 111 25.090 19.798 56.123 1.00 22.55

ATOM 832 CB ILE A 111 26.141 18.762 56.616 1.00 21.81

ATOM 834 CGl ILE A 111 27.087 19.399 57.639 1.00 24.46

ATOM 837 CDl ILE A 111 28.017 20.503 57.092 1.00 22.90

ATOM 841 CG2 ILE A 111 26.967 18.165 55.459 1.00 22.65

ATOM 845 C ILE A 111 24.006 19.171 55.287 1.00 24.00

ATOM 846 O ILE A 111 23.380 18.164 55.668 1.00 24.00

ATOM 848 N LEU A 112 23.781 19.767 54.132 1.00 22.11

ATOM 849 CA LEU A 112 22.731 19.323 53.245 1.00 21.19

ATOM 851 CB LEU A 112 22.337 20.452 52.302 1.00 20.79

ATOM 854 CG LEU A 112 21.931 21.785 52.956 1.00 21.21

ATOM 856 CDl LEU A 112 21.566 22.802 51.894 1.00 23.96

ATOM 860 CD2 LEU A 112 20.784 21.584 53.913 1.00 23.24

ATOM 864 C LEU A 112 23.095 18.095 52.435 1.00 20.03

ATOM 865 O LEU A 112 22.225 17.379 52.006 1.00 21.02

ATOM 867 N HIS A 113 24.368 17.877 52.184 1.00 20.26

ATOM 868 CA HIS A 113 24.816 16.835 51.255 1.00 19.13

ATOM 870 CB HIS A 113 24.502 17.216 49.797 1.00 18.30

ATOM 873 CG HIS A 113 24.741 16.102 48.822 1.00 14.94

ATOM 874 NDl HIS A 113 25.902 15.982 48.096 1.00 20.54

ATOM 876 CEl HIS A 113 25.858 14.864 47.388 1.00 19.48

ATOM 878 NE 2 HIS A 113 24.712 14.262 47.631 1.00 21.61

ATOM 880 CD2 HIS A 113 24.007 15.007 48.542 1.00 18.43

ATOM 882 C HIS A 113 26.318 16.694 51.420 1.00 18.82

ATOM 883 O HIS A 113 27.002 17.682 51.657 1.00 18.40

ATOM 885 N VAL A 114 26.825 15.467 51.340 1.00 16.87

ATOM 886 CA VAL A 114 28.256 15.233 51.307 1.00 17.73

ATOM 888 CB VAL A 114 28.757 14.305 52.438 1.00 18.30

ATOM 890 CGl VAL A 114 30.252 13.995 52.280 1.00 15.74

ATOM 894 CG2 VAL A 114 28.435 14.903 53.853 1.00 18.88 ATOM 898 C VAL A 114 28.538 14.651 49.955 1.00 17.51

ATOM 899 O VAL A 114 27.917 13.660 49.547 1.00 18.33

ATOM 901 N PHE A 115 29.443 15.308 49.245 1.00 19.67

ATOM 902 CA PHE A 115 29.791 14.986 47.915 1.00 19.19

ATOM 904 CB PHE A 115 30.342 16.188 47.187 1.00 19.66

ATOM 907 CG PHE A 115 29.306 17.178 46.815 1.00 19.52

ATOM 908 CDl PHE A 115 28.401 16.896 45.792 1.00 15.32

ATOM 910 CEl PHE A 115 27.451 17.813 45.430 1.00 18.69

ATOM 912 CZ PHE A 115 27.357 19.009 46.117 1.00 19.14

ATOM 914 CE 2 PHE A 115 28.244 19.295 47.155 1.00 20.26

ATOM 916 CD2 PHE A 115 29.224 18.377 47.474 1.00 20.21

ATOM 918 C PHE A 115 30.853 13.925 47.941 1.00 22.74

ATOM 919 O PHE A 115 31.849 14.038 48.648 1.00 22.79

ATOM 921 N HIS A 116 30.645 12.895 47.142 1.00 23.93

ATOM 922 CA HIS A 116 31.738 12.014 46.801 1.00 27.66

ATOM 924 CB HIS A 116 31.985 11.001 47.909 1.00 27.91

ATOM 927 CG HIS A 116 30.943 9.936 48.013 1.00 29.99

ATOM 928 NDl HIS A 116 29.710 10.158 48.585 1.00 32.35

ATOM 930 CEl HIS A 116 29.000 9.044 48.544 1.00 33.35

ATOM 932 NE 2 HIS A 116 29.745 8.098 47.996 1.00 34.28

ATOM 934 CD2 HIS A 116 30.971 8.626 47.665 1.00 28.95

ATOM 936 C HIS A 116 31.437 11.353 45.457 1.00 28.33

ATOM 937 O HIS A 116 30.283 11.132 45.107 1.00 30.47

ATOM 939 N GLY A 117 32.471 11.090 44.686 1.00 29.53

ATOM 940 CA GLY A 117 32.251 10.426 43.395 1.00 30.30

ATOM 943 C GLY A 117 32.684 11.251 42.216 1.00 29.68

ATOM 944 O GLY A 117 33.132 10.705 41.211 1.00 31.20

ATOM 946 N LEU A 118 32.536 12.565 42.313 1.00 28.81

ATOM 947 CA LEU A 118 33.154 13.444 41.327 1.00 28.48

ATOM 949 CB LEU A 118 32.086 14.246 40.591 1.00 28.90

ATOM 952 CG LEU A 118 31.282 13.484 39.542 1.00 24.46

ATOM 954 CDl LEU A 118 30.218 14.416 38.927 1.00 20.55

ATOM 958 CD2 LEU A 118 32.229 12.909 38.471 1.00 22.65

ATOM 962 C LEU A 118 34.145 14.363 42.013 1.00 27.75

ATOM 963 O LEU A 118 35.342 14.329 41.734 1.00 30.09

ATOM 965 N LEU A 119 33.618 15.184 42.910 1.00 25.75

ATOM 966 CA LEU A 119 34.384 16.092 43.719 1.00 25.53

ATOM 968 CB LEU A 119 33.843 17.516 43.571 1.00 25.93

ATOM 971 CG LEU A 119 34.118 18.256 42.261 1.00 30.52

ATOM 973 CDl LEU A 119 33.602 19.670 42.359 1.00 32.32

ATOM 977 CD2 LEU A 119 35.630 18.268 41.885 1.00 33.49

ATOM 981 C LEU A 119 34.150 15.645 45.150 1.00 23.19

ATOM 982 O LEU A 119 33.037 15.272 45.502 1.00 23.12

ATOM 984 N PRO A 120 35.183 15.676 45.984 1.00 21.09

ATOM 985 CA PRO A 120 34.872 15.530 47.400 1.00 19.69

ATOM 987 CB PRO A 120 36.164 14.982 47.973 1.00 19.25

ATOM 990 CG PRO A 120 37.223 15.510 47.141 1.00 21.58

ATOM 993 CD PRO A 120 36.624 15.798 45.751 1.00 21.48

ATOM 996 C PRO A 120 34.527 16.878 48.042 1.00 19.05

ATOM 997 O PRO A 120 35.079 17.913 47.661 1.00 18.18

ATOM 998 N GLY A 121 33.631 16.854 49.015 1.00 17.31

ATOM 999 CA GLY A 121 33.247 18.051 49.723 1.00 18.89

ATOM 1002 C GLY A 121 31.875 17.874 50.329 1.00 18.22

ATOM 1003 O GLY A 121 31.389 16.754 50.504 1.00 17.63

ATOM 1005 N PHE A 122 31.234 18.998 50.603 1.00 15.51

ATOM 1006 CA PHE A 122 29.918 18.996 51.173 1.00 15.94

ATOM 1008 CB PHE A 122 29.959 18.712 52.667 1.00 17.86

ATOM 1011 CG PHE A 122 30.896 19.595 53.457 1.00 15.14

ATOM 1012 CDl PHE A 122 32.191 19.253 53.630 1.00 16.64

ATOM 1014 CEl PHE A 122 33.039 20.050 54.396 1.00 19.92

ATOM 1016 CZ PHE A 122 32.560 21.188 54.968 1.00 14.91 ATOM 1018 CE 2 PHE A 122 31.264 21.529 54.810 1.00 14.44

ATOM 1020 CD2 PHE A 122 30.429 20.732 54.056 1.00 18.95

ATOM 1022 C PHE A 122 29.180 20.297 50.859 1.00 15.80

ATOM 1023 O PHE A 122 29.790 21.304 50.527 1.00 14.99

ATOM 1025 N LEU A 123 27.876 20.247 50.964 1.00 15.69

ATOM 1026 CA LEU A 123 27.046 21.400 50.779 1.00 17.50

ATOM 1028 CB LEU A 123 25.831 21.034 49.936 1.00 16.92

ATOM 1031 CG LEU A 123 24.776 22.100 49.635 1.00 20.69

ATOM 1033 CDl LEU A 123 25.438 23.264 48.823 1.00 18.86

ATOM 1037 CD2 LEU A 123 23.613 21.409 48.851 1.00 17.69

ATOM 1041 C LEU A 123 26.580 21.753 52.165 1.00 17.89

ATOM 1042 O LEU A 123 26.021 20.911 52.828 1.00 17.98

ATOM 1044 N VAL A 124 26.732 23.015 52.558 1.00 16.86

ATOM 1045 CA VAL A 124 26.387 23.457 53.915 1.00 16.90

ATOM 1047 CB VAL A 124 27.644 23.595 54.763 1.00 16.52

ATOM 1049 CGl VAL A 124 28.619 24.564 54.097 1.00 16.77

ATOM 1053 CG2 VAL A 124 27.323 23.987 56.295 1.00 19.09

ATOM 1057 C VAL A 124 25.574 24.754 53.901 1.00 18.64

ATOM 1058 O VAL A 124 25.861 25.711 53.126 1.00 15.90

ATOM 1060 N LYS A 125 24.524 24.753 54.709 1.00 18.61

ATOM 1061 CA LYS A 125 23.692 25.917 54.952 1.00 20.01

ATOM 1063 CB LYS A 125 22.230 25.531 55.045 1.00 20.52

ATOM 1066 CG LYS A 125 21.323 26.680 55.238 1.00 27.43

ATOM 1069 CD LYS A 125 19.889 26.325 54.906 1.00 35.56

ATOM 1072 CE LYS A 125 18.932 27.449 55.374 1.00 42.11

ATOM 1075 NZ LYS A 125 17.521 26.975 55.562 1.00 48.29

ATOM 1079 C LYS A 125 24.170 26.528 56.214 1.00 21.10

ATOM 1080 O LYS A 125 24.135 25.899 57.280 1.00 18.90

ATOM 1082 N MET A 126 24.715 27.735 56.089 1.00 21.18

ATOM 1083 CA MET A 126 25.344 28.408 57.199 1.00 21.77

ATOM 1085 CB MET A 126 26.749 27.871 57.498 1.00 21.97

ATOM 1088 CG MET A 126 27.779 28.110 56.411 1.00 22.35

ATOM 1091 SD MET A 126 29.363 27.485 56.820 1.00 24.40

ATOM 1092 CE MET A 126 30.427 28.364 55.674 1.00 23.86

ATOM 1096 C MET A 126 25.441 29.879 56.845 1.00 22.77

ATOM 1097 O MET A 126 25.360 30.272 55.668 1.00 21.00

ATOM 1099 N SER A 127 25.698 30.663 57.864 1.00 22.49

ATOM 1100 CA SER A 127 26.022 32.058 57.668 1.00 23.32

ATOM 1102 CB SER A 127 26.015 32.793 59.011 1.00 25.01

ATOM 1105 OG SER A 127 26.694 34.054 58.921 1.00 22.15

ATOM 1107 C SER A 127 27.377 32.201 57.015 1.00 21.95

ATOM 1108 O SER A 127 28.340 31.501 57.334 1.00 23.54

ATOM 1110 N GLY A 128 27.480 33.163 56.116 1.00 22.67

ATOM 1111 CA GLY A 128 28.764 33.475 55.480 1.00 22.62

ATOM 1114 C GLY A 128 29.793 33.982 56.465 1.00 21.95

ATOM 1115 O GLY A 128 30.981 33.975 56.186 1.00 22.07

ATOM 1117 N ASP A 129 29.339 34.425 57.634 1.00 23.16

ATOM 1118 CA ASP A 129 30.258 34.758 58.726 1.00 22.49

ATOM 1120 CB ASP A 129 29.473 34.942 60.022 1.00 22.51

ATOM 1123 CG ASP A 129 28.638 36.197 60.029 1.00 27.90

ATOM 1124 ODl ASP A 129 28.472 36.856 58.971 1.00 26.60

ATOM 1125 OD2 ASP A 129 28.126 36.500 61.110 1.00 29.81

ATOM 1126 C ASP A 129 31.284 33.671 58.963 1.00 23.78

ATOM 1127 O ASP A 129 32.403 33.942 59.338 1.00 25.24

ATOM 1129 N LEU A 130 30.886 32.416 58.786 1.00 22.71

ATOM 1130 CA LEU A 130 31.788 31.296 59.056 1.00 22.02

ATOM 1132 CB LEU A 130 30.947 30.040 59.303 1.00 20.82

ATOM 1135 CG LEU A 130 29.975 30.132 60.473 1.00 22.58

ATOM 1137 CDl LEU A 130 28.964 28.990 60.429 1.00 23.45

ATOM 1141 CD2 LEU A 130 30.784 30.136 61.763 1.00 19.20

ATOM 1145 C LEU A 130 32.784 30.997 57.953 1.00 22.31 ATOM 1146 O LEU A 130 33.521 30.016 58.061 1.00 22.55

ATOM 1148 N LEU A 131 32.815 31.778 56.866 1.00 21.98

ATOM 1149 CA LEU A 131 33.674 31.391 55.752 1.00 20.41

ATOM 1151 CB LEU A 131 33.405 32.239 54.514 1.00 21.40

ATOM 1154 CG LEU A 131 32.137 31.923 53.754 1.00 19.24

ATOM 1156 CDl LEU A 131 31.827 33.079 52.774 1.00 24.38

ATOM 1160 CD2 LEU A 131 32.316 30.527 53.043 1.00 19.51

ATOM 1164 C LEU A 131 35.153 31.438 56.047 1.00 21.28

ATOM 1165 O LEU A 131 35.890 30.600 55.599 1.00 20.68

ATOM 1167 N GLU A 132 35.613 32.442 56.765 1.00 23.13

ATOM 1168 CA GLU A 132 37.007 32.469 57.178 1.00 25.27

ATOM 1170 CB GLU A 132 37.314 33.713 58.001 1.00 25.87

ATOM 1173 CG GLU A 132 37.704 34.917 57.200 1.00 28.36

ATOM 1176 CD GLU A 132 38.071 36.124 58.109 1.00 32.76

ATOM 1177 OEl GLU A 132 37.639 36.138 59.294 1.00 40.57

ATOM 1178 OE 2 GLU A 132 38.780 37.060 57.632 1.00 42.25

ATOM 1179 C GLU A 132 37.344 31.225 58.009 1.00 24.01

ATOM 1180 O GLU A 132 38.381 30.632 57.835 1.00 26.42

ATOM 1182 N LEU A 133 36.464 30.849 58.918 1.00 24.18

ATOM 1183 CA LEU A 133 36.675 29.626 59.703 1.00 24.40

ATOM 1185 CB LEU A 133 35.557 29.481 60.714 1.00 23.85

ATOM 1188 CG LEU A 133 35.491 28.227 61.602 1.00 28.48

ATOM 1190 CDl LEU A 133 36.770 28.039 62.378 1.00 34.21

ATOM 1194 CD2 LEU A 133 34.311 28.358 62.543 1.00 27.10

ATOM 1198 C LEU A 133 36.742 28.383 58.780 1.00 23.51

ATOM 1199 O LEU A 133 37.655 27.569 58.888 1.00 23.74

ATOM 1201 N ALA A 134 35.772 28.300 57.867 1.00 22.81

ATOM 1202 CA ALA A 134 35.632 27.188 56.930 1.00 23.23

ATOM 1204 CB ALA A 134 34.347 27.332 56.151 1.00 22.63

ATOM 1208 C ALA A 134 36.818 27.038 56.001 1.00 22.64

ATOM 1209 O ALA A 134 37.226 25.920 55.676 1.00 21.99

ATOM 1211 N LEU A 135 37.372 28.161 55.552 1.00 21.14

ATOM 1212 CA LEU A 135 38.529 28.118 54.706 1.00 20.36

ATOM 1214 CB LEU A 135 38.846 29.513 54.147 1.00 20.52

ATOM 1217 CG LEU A 135 37.810 29.995 53.116 1.00 19.46

ATOM 1219 CDl LEU A 135 37.903 31.524 52.938 1.00 21.93

ATOM 1223 CD2 LEU A 135 37.893 29.190 51.746 1.00 17.11

ATOM 1227 C LEU A 135 39.747 27.566 55.402 1.00 20.31

ATOM 1228 O LEU A 135 40.710 27.214 54.743 1.00 21.25

ATOM 1230 N LYS A 136 39.745 27.536 56.737 1.00 20.33

ATOM 1231 CA LYS A 136 40.875 27.020 57.484 1.00 22.47

ATOM 1233 CB LYS A 136 41.055 27.845 58.752 1.00 24.55

ATOM 1236 CG LYS A 136 41.638 29.189 58.454 1.00 27.65

ATOM 1239 CD LYS A 136 41.595 30.060 59.682 1.00 38.13

ATOM 1242 CE LYS A 136 42.482 31.282 59.517 1.00 41.57

ATOM 1245 NZ LYS A 136 42.939 31.809 60.830 1.00 45.94

ATOM 1249 C LYS A 136 40.704 25.535 57.827 1.00 23.72

ATOM 1250 O LYS A 136 41.569 24.939 58.417 1.00 24.76

ATOM 1252 N LEU A 137 39.599 24.931 57.432 1.00 24.07

ATOM 1253 CA LEU A 137 39.417 23.503 57.692 1.00 25.02

ATOM 1255 CB LEU A 137 38.018 23.057 57.297 1.00 25.39

ATOM 1258 CG LEU A 137 36.821 23.593 58.072 1.00 23.72

ATOM 1260 CDl LEU A 137 35.512 23.400 57.241 1.00 21.38

ATOM 1264 CD2 LEU A 137 36.720 22.957 59.436 1.00 22.04

ATOM 1268 C LEU A 137 40.417 22.670 56.923 1.00 26.38

ATOM 1269 O LEU A 137 40.858 23.038 55.824 1.00 24.11

ATOM 1271 N PRO A 138 40.718 21.466 57.451 1.00 27.87

ATOM 1272 CA PRO A 138 41.626 20.615 56.716 1.00 27.68

ATOM 1274 CB PRO A 138 41.781 19.387 57.624 1.00 27.70

ATOM 1277 CG PRO A 138 40.535 19.384 58.473 1.00 32.57

ATOM 1280 CD PRO A 138 40.225 20.837 58.685 1.00 28.24 ATOM 1283 C PRO A 138 41.020 20.204 55.386 1.00 24.72

ATOM 1284 O PRO A 138 39.820 20.058 55.279 1.00 24.52

ATOM 1285 N HIS A 139 41.866 19.961 54.413 1.00 24.02

ATOM 1286 CA HIS A 139 41.443 19.470 53.108 1.00 23.65

ATOM 1288 CB HIS A 139 40.552 18.225 53.223 1.00 24.23

ATOM 1291 CG HIS A 139 41.078 17.195 54.186 1.00 26.62

ATOM 1292 NDl HIS A 139 42.271 16.530 53.986 1.00 31.10

ATOM 1294 CEl HIS A 139 42.495 15.712 55.000 1.00 29.89

ATOM 1296 NE2 HIS A 139 41.498 15.831 55.857 1.00 25.88

ATOM 1298 CD2 HIS A 139 40.596 16.751 55.368 1.00 29.57

ATOM 1300 C HIS A 139 40.753 20.461 52.205 1.00 22.71

ATOM 1301 O HIS A 139 40.497 20.093 51.064 1.00 21.21

ATOM 1303 N VAL A 140 40.473 21.694 52.652 1.00 20.59

ATOM 1304 CA VAL A 140 39.706 22.603 51.803 1.00 20.07

ATOM 1306 CB VAL A 140 39.142 23.821 52.580 1.00 21.66

ATOM 1308 CGl VAL A 140 38.391 24.794 51.642 1.00 17.13

ATOM 1312 CG2 VAL A 140 38.232 23.342 53.719 1.00 22.97

ATOM 1316 C VAL A 140 40.521 23.055 50.587 1.00 18.81

ATOM 1317 O VAL A 140 41.658 23.545 50.707 1.00 19.20

ATOM 1319 N ASP A 141 39.917 22.909 49.414 1.00 17.61

ATOM 1320 CA ASP A 141 40.480 23.487 48.191 1.00 17.16

ATOM 1322 CB ASP A 141 40.222 22.532 47.028 1.00 16.43

ATOM 1325 CG ASP A 141 41.063 22.842 45.828 1.00 20.04

ATOM 1326 ODl ASP A 141 41.854 23.799 45.857 1.00 23.18

ATOM 1327 OD2 ASP A 141 40.899 22.148 44.820 1.00 23.66

ATOM 1328 C ASP A 141 39.886 24.896 47.959 1.00 16.76

ATOM 1329 O ASP A 141 40.620 25.894 47.911 1.00 18.31

ATOM 1331 N TYR A 142 38.557 24.987 47.897 1.00 15.46

ATOM 1332 CA TYR A 142 37.879 26.251 47.796 1.00 17.14

ATOM 1334 CB TYR A 142 37.959 26.805 46.358 1.00 18.35

ATOM 1337 CG TYR A 142 37.462 25.851 45.302 1.00 13.69

ATOM 1338 CDl TYR A 142 38.285 24.876 44.760 1.00 17.10

ATOM 1340 CEl TYR A 142 37.796 23.968 43.769 1.00 18.36

ATOM 1342 CZ TYR A 142 36.485 24.103 43.336 1.00 21.76

ATOM 1343 OH TYR A 142 35.948 23.259 42.382 1.00 19.25

ATOM 1345 CE2 TYR A 142 35.671 25.083 43.879 1.00 20.48

ATOM 1347 CD2 TYR A 142 36.161 25.939 44.843 1.00 18.44

ATOM 1349 C TYR A 142 36.439 26.070 48.241 1.00 18.58

ATOM 1350 O TYR A 142 35.947 24.934 48.412 1.00 16.62

ATOM 1352 N ILE A 143 35.776 27.197 48.465 1.00 16.86

ATOM 1353 CA ILE A 143 34.410 27.232 48.827 1.00 16.07

ATOM 1355 CB ILE A 143 34.228 27.740 50.277 1.00 17.56

ATOM 1357 CGl ILE A 143 34.949 26.818 51.281 1.00 14.57

ATOM 1360 CDl ILE A 143 34.939 27.330 52.778 1.00 15.60

ATOM 1364 CG2 ILE A 143 32.746 27.818 50.617 1.00 17.34

ATOM 1368 C ILE A 143 33.688 28.164 47.835 1.00 17.37

ATOM 1369 O ILE A 143 34.164 29.287 47.551 1.00 14.89

ATOM 1371 N GLU A 144 32.557 27.692 47.313 1.00 15.14

ATOM 1372 CA GLU A 144 31.733 28.491 46.431 1.00 16.42

ATOM 1374 CB GLU A 144 31.804 27.877 45.000 1.00 15.98

ATOM 1377 CG GLU A 144 30.997 28.658 43.931 1.00 18.89

ATOM 1380 CD GLU A 144 31.126 28.087 42.528 1.00 19.87

ATOM 1381 OEl GLU A 144 32.266 27.673 42.222 1.00 19.84

ATOM 1382 OE2 GLU A 144 30.087 28.069 41.764 1.00 23.17

ATOM 1383 C GLU A 144 30.317 28.677 46.962 1.00 17.06

ATOM 1384 O GLU A 144 29.653 27.733 47.355 1.00 15.66

ATOM 1386 N GLU A 145 29.843 29.921 46.967 1.00 16.78

ATOM 1387 CA GLU A 145 28.501 30.233 47.379 1.00 16.23

ATOM 1389 CB GLU A 145 28.314 31.734 47.443 1.00 17.29

ATOM 1392 CG GLU A 145 26.949 32.186 47.836 1.00 18.63

ATOM 1395 CD GLU A 145 26.790 33.653 47.598 1.00 25.65 ATOM 1396 OEl GLU A 145 26.716 34.052 46.426 1.00 22.04

ATOM 1397 OE2 GLU A 145 26.789 34.398 48.578 1.00 21.17

ATOM 1398 C GLU A 145 27.593 29.641 46.321 1.00 18.48

ATOM 1399 O GLU A 145 27.887 29.730 45.110 1.00 16.69

ATOM 1401 N ASP A 146 26.472 29.066 46.738 1.00 17.98

ATOM 1402 CA ASP A 146 25.553 28.484 45.772 1.00 19.19

ATOM 1404 CB ASP A 146 24.430 27.721 46.499 1.00 19.86

ATOM 1407 CG ASP A 146 23.797 26.627 45.663 1.00 23.29

ATOM 1408 ODl ASP A 146 24.218 26.395 44.512 1.00 20.21

ATOM 1409 OD2 ASP A 146 22.825 26.008 46.164 1.00 23.57

ATOM 1410 C ASP A 146 24.994 29.611 44.905 1.00 20.15

ATOM 1411 O ASP A 146 25.014 30.780 45.299 1.00 20.88

ATOM 1413 N SER A 147 24.516 29.256 43.728 1.00 20.91

ATOM 1414 CA SER A 147 23.959 30.201 42.776 1.00 20.54

ATOM 1416 CB SER A 147 25.066 30.856 41.984 1.00 21.84

ATOM 1419 OG SER A 147 25.711 29.882 41.178 1.00 27.64

ATOM 1421 C SER A 147 22.975 29.539 41.844 1.00 19.61

ATOM 1422 O SER A 147 22.812 28.324 41.850 1.00 17.81

ATOM 1424 N SER A 148 22.299 30.366 41.060 1.00 19.03

ATOM 1425 CA SER A 148 21.187 29.952 40.218 1.00 19.46

ATOM 1427 CB SER A 148 20.160 31.093 40.134 1.00 20.12

ATOM 1430 OG SER A 148 19.538 31.292 41.364 1.00 19.29

ATOM 1432 C SER A 148 21.629 29.561 38.795 1.00 16.83

ATOM 1433 O SER A 148 22.616 30.107 38.256 1.00 17.26

ATOM 1435 N VAL A 149 20.954 28.558 38.247 1.00 16.78

ATOM 1436 CA VAL A 149 21.076 28.197 36.838 1.00 17.21

ATOM 1438 CB VAL A 149 21.752 26.788 36.666 1.00 16.21

ATOM 1440 CGl VAL A 149 23.208 26.844 37.175 1.00 18.06

ATOM 1444 CG2 VAL A 149 20.941 25.706 37.382 1.00 16.50

ATOM 1448 C VAL A 149 19.690 28.216 36.269 1.00 17.76

ATOM 1449 O VAL A 149 18.698 28.170 37.015 1.00 19.13

ATOM 1451 N PHE A 150 19.602 28.320 34.943 1.00 18.00

ATOM 1452 CA PHE A 150 18.352 28.542 34.277 1.00 16.87

ATOM 1454 CB PHE A 150 18.213 30.035 33.933 1.00 18.62

ATOM 1457 CG PHE A 150 18.346 30.924 35.124 1.00 17.98

ATOM 1458 CDl PHE A 150 17.226 31.240 35.878 1.00 19.96

ATOM 1460 CEl PHE A 150 17.328 32.040 37.007 1.00 20.59

ATOM 1462 CZ PHE A 150 18.548 32.552 37.362 1.00 19.20

ATOM 1464 CE2 PHE A 150 19.681 32.244 36.607 1.00 20.00

ATOM 1466 CD2 PHE A 150 19.574 31.433 35.500 1.00 21.39

ATOM 1468 C PHE A 150 18.284 27.765 32.993 1.00 16.70

ATOM 1469 O PHE A 150 19.269 27.628 32.289 1.00 16.22

ATOM 1471 N ALA A 151 17.089 27.263 32.706 1.00 16.44

ATOM 1472 CA ALA A 151 16.748 26.591 31.480 1.00 17.92

ATOM 1474 CB ALA A 151 15.215 26.372 31.460 1.00 17.84

ATOM 1478 C ALA A 151 17.107 27.466 30.309 1.00 18.02

ATOM 1479 O ALA A 151 16.757 28.641 30.315 1.00 17.97

ATOM 1481 N GLN A 152 17.740 26.910 29.280 1.00 17.44

ATOM 1482 CA GLN A 152 18.103 27.717 28.127 1.00 18.99

ATOM 1484 CB GLN A 152 19.600 27.607 27.815 1.00 19.14

ATOM 1487 CG GLN A 152 20.474 28.166 28.904 1.00 19.32

ATOM 1490 CD GLN A 152 20.181 29.635 29.225 1.00 21.76

ATOM 1491 OEl GLN A 152 20.311 30.487 28.372 1.00 18.80

ATOM 1492 NE2 GLN A 152 19.761 29.920 30.462 1.00 15.35

ATOM 1495 C GLN A 152 17.219 27.347 26.952 1.00 20.98

ATOM 1496 O GLN A 152 17.564 27.443 25.773 1.00 18.27

ATOM 1498 OXT GLN A 152 16.054 26.982 27.213 1.00 23.34

ATOM 1499 N SER B 153 7.638 18.191 4 . 804 1.00 39.93

ATOM 1500 CA SER B 153 7.059 17.662 6 . 072 1.00 40.03

ATOM 1502 CB SER B 153 6.305 16.368 5 . 819 1.00 40.68

ATOM 1505 OG SER B 153 7.204 15.395 5 . 299 1.00 44.13 ATOM 1507 C SER I3 153 8.142 17.402 7.139 1.00 37.73

ATOM 1508 O SER I 3 153 7.865 17.600 8.332 1.00 39.18

ATOM 1512 N ILE I 3 154 9.348 16.964 6.731 1.00 33.52

ATOM 1513 CA ILE I 3 154 10.461 16.786 7.691 1.00 30.21

ATOM 1515 CB ILE I 3 154 11.788 16.310 7.036 1.00 31.11

ATOM 1517 CGl ILE I 3 154 11.641 14.949 6.324 1.00 32.31

ATOM 1520 CDl ILE I 3 154 11.339 13.754 7.226 1.00 32.28

ATOM 1524 CG2 ILE I 3 154 12.931 16.187 8.095 1.00 32.05

ATOM 1528 C ILE I 3 154 10.700 18.152 8.355 1.00 26.79

ATOM 1529 O ILE I 3 154 10.890 19.146 7.663 1.00 26.19

ATOM 1531 N PRO I 3 155 10.674 18.221 9.692 1.00 23.55

ATOM 1532 CA PRO I 3 155 11.082 19.470 10.330 1.00 22.56

ATOM 1534 CB PRO I 3 155 11.200 19.073 11.785 1.00 21.02

ATOM 1537 CG PRO I 3 155 10.200 18.004 11.978 1.00 24.79

ATOM 1540 CD PRO I 3 155 10.288 17.206 10.687 1.00 24.46

ATOM 1543 C PRO I 3 155 12.420 19.964 9.808 1.00 20.28

ATOM 1544 O PRO I 3 155 13.306 19.173 9.599 1.00 23.58

ATOM 1545 N TRP I 3 156 12.554 21.265 9.595 1.00 19.87

ATOM 1546 CA TRP I 3 156 13.726 21.868 8.952 1.00 18.61

ATOM 1548 CB TRP I 3 156 13.582 23.411 8.950 1.00 18.00

ATOM 1551 CG TRP I 3 156 13.972 24.130 10.265 1.00 18.20

ATOM 1552 CDl TRP I 3 156 13.143 24.547 11.252 1.00 18.53

ATOM 1554 NEl TRP I 3 156 13.857 25.137 12.268 1.00 19.97

ATOM 1556 CE 2 TRP I 3 156 15.187 25.152 11.920 1.00 18.24

ATOM 1557 CD2 TRP I 3 156 15.297 24.524 10.664 1.00 17.74

ATOM 1558 CE 3 TRP I 3 156 16.558 24.390 10.089 1.00 20.64

ATOM 1560 CZ3 TRP I 3 156 17.646 24.890 10.755 1.00 19.41

ATOM 1562 CH2 TRP I 3 156 17.505 25.507 12.001 1.00 16.28

ATOM 1564 CZ 2 TRP I 3 156 16.291 25.622 12.606 1.00 19.41

ATOM 1566 C TRP I 3 156 15.044 21.487 9.627 1.00 17.64

ATOM 1567 O TRP I 3 156 16.059 21.346 8.991 1.00 15.73

ATOM 1569 N ASN I 3 157 14.987 21.412 10.947 1.00 16.99

ATOM 1570 CA ASN I 3 157 16.136 21.137 11.794 1.00 15.68

ATOM 1572 CB ASN I 3 157 15.784 21.397 13.257 1.00 13.09

ATOM 1575 CG ASN I 3 157 14.536 20.731 13.692 1.00 18.68

ATOM 1576 ODl ASN I 3 157 13.458 21.085 13.244 1.00 20.07

ATOM 1577 ND2 ASN I 3 157 14.643 19.812 14.644 1.00 15.33

ATOM 1580 C ASN I 3 157 16.650 19.753 11.622 1.00 16.79

ATOM 1581 O ASN I 3 157 17.862 19.517 11.658 1.00 16.10

ATOM 1583 N LEU I 3 158 15.737 18.819 11.438 1.00 17.71

ATOM 1584 CA LEU I 3 158 16.148 17.436 11.206 1.00 19.42

ATOM 1586 CB LEU I 3 158 14.996 16.481 11.528 1.00 20.61

ATOM 1589 CG LEU I 3 158 14.431 16.459 12.942 1.00 23.16

ATOM 1591 CDl LEU I 3 158 13.293 15.440 13.028 1.00 22.45

ATOM 1595 CD2 LEU I 3 158 15.576 16.153 13.914 1.00 20.65

ATOM 1599 C LEU I 3 158 16.673 17.254 9.790 1.00 19.94

ATOM 1600 O LEU I 3 158 17.623 16.494 9.574 1.00 20.75

ATOM 1602 N GLU I 3 159 16.138 18.000 8.821 1.00 20.59

ATOM 1603 CA GLU I 3 159 16.762 18.042 7.514 1.00 20.18

ATOM 1605 CB GLU I 3 159 15.878 18.766 6.491 1.00 20.12

ATOM 1608 CG GLU I 3 159 16.312 18.554 5.043 1.00 24.15

ATOM 1611 CD GLU I 3 159 16.459 17.044 4.644 1.00 30.99

ATOM 1612 OEl GLU I 3 159 15.529 16.203 4.917 1.00 36.32

ATOM 1613 OE 2 GLU I 3 159 17.528 16.697 4.064 1.00 31.09

ATOM 1614 C GLU I 3 159 18.157 18.715 7.570 1.00 20.79

ATOM 1615 O GLU I 3 159 19.107 18.305 6.907 1.00 18.87

ATOM 1617 N ARG I 3 160 18.291 19.751 8.375 1.00 21.53

ATOM 1618 CA ARG I 3 160 19.533 20.502 8.397 1.00 20.93

ATOM 1620 CB ARG I 3 160 19.391 21.696 9.317 1.00 20.43

ATOM 1623 CG ARG I 3 160 20.535 22.681 9.227 1.00 21.82

ATOM 1626 CD ARG I 3 160 20.714 23.220 7.849 1.00 24.51 ATOM 1629 NE ARG I3 160 19.410 23.613 7.276 1.00 35.05

ATOM 1631 CZ ARG I 3 160 18.927 24.859 7.244 1.00 31.36

ATOM 1632 NHl ARG I 3 160 19.633 25.871 7.726 1.00 33.05

ATOM 1635 NH2 ARG I 3 160 17.734 25.095 6.708 1.00 31.88

ATOM 1638 C ARG I 3 160 20.724 19.635 8.842 1.00 19.10

ATOM 1639 O ARG I 3 160 21.829 19.809 8.365 1.00 19.18

ATOM 1641 N ILE I 3 161 20.477 18.724 9.772 1.00 17.91

ATOM 1642 CA ILE I 3 161 21.518 17.873 10.312 1.00 18.20

ATOM 1644 CB ILE I 3 161 21.269 17.563 11.821 1.00 15.17

ATOM 1646 CGl ILE I 3 161 19.949 16.861 12.051 1.00 18.43

ATOM 1649 CDl ILE I 3 161 19.917 15.986 13.209 1.00 15.58

ATOM 1653 CG2 ILE I 3 161 21.271 18.854 12.629 1.00 15.43

ATOM 1657 C ILE I 3 161 21.694 16.573 9.517 1.00 19.49

ATOM 1658 O ILE I 3 161 22.574 15.743 9.821 1.00 19.04

ATOM 1660 N THR I 3 162 20.869 16.399 8.490 1.00 20.94

ATOM 1661 CA THR I 3 162 20.976 15.242 7.617 1.00 22.52

ATOM 1663 CB THR I 3 162 19.663 14.964 6.877 1.00 22.75

ATOM 1665 OGl THR I 3 162 18.644 14.694 7.850 1.00 21.80

ATOM 1667 CG2 THR I 3 162 19.803 13.757 5.886 1.00 22.47

ATOM 1671 C THR I 3 162 22.084 15.480 6.615 1.00 23.41

ATOM 1672 O THR I 3 162 22.085 16.461 5.895 1.00 24.92

ATOM 1674 N PRO I 3 163 23.015 14.540 6.531 1.00 24.83

ATOM 1675 CA PRO I 3 163 24.179 14.700 5.715 1.00 24.85

ATOM 1677 CB PRO I 3 163 25.088 13.589 6.212 1.00 25.41

ATOM 1680 CG PRO I 3 163 24.204 12.566 6.659 1.00 24.27

ATOM 1683 CD PRO I 3 163 22.994 13.231 7.197 1.00 23.37

ATOM 1686 C PRO I 3 163 23.850 14.529 4.224 1.00 26.58

ATOM 1687 O PRO I 3 163 22.753 14.098 3.879 1.00 24.53

ATOM 1688 N PRO I 3 164 24.780 14.920 3.363 1.00 28.57

ATOM 1689 CA PRO I 3 164 24.576 14.887 1.925 1.00 31.24

ATOM 1691 CB PRO I 3 164 25.822 15.589 1.381 1.00 30.93

ATOM 1694 CG PRO I 3 164 26.354 16.364 2.514 1.00 32.47

ATOM 1697 CD PRO I 3 164 26.098 15.498 3.692 1.00 30.33

ATOM 1700 C PRO I 3 164 24.483 13.476 1.376 1.00 31.99

ATOM 1701 O PRO I 3 164 24.123 13.303 0.226 1.00 32.79

ATOM 1702 N ARG I 3 165 24.841 12.488 2.186 1.00 32.74

ATOM 1703 CA ARG I 3 165 24.714 11.113 1.815 1.00 33.89

ATOM 1705 CB ARG I 3 165 26.046 10.614 1.262 1.00 34.65

ATOM 1708 CG ARG I 3 165 26.228 9.126 1.324 1.00 39.62

ATOM 1711 CD ARG I 3 165 25.314 8.428 0.387 1.00 46.57

ATOM 1714 NE ARG I 3 165 25.925 8.285 -0.936 1.00 53.24

ATOM 1716 CZ ARG I 3 165 26.663 7.248 -1.328 1.00 54.08

ATOM 1717 NHl ARG I 3 165 26.931 6.244 -0.491 1.00 57.66

ATOM 1720 NH2 ARG I 3 165 27.152 7.218 -2.566 1.00 49.65

ATOM 1723 C ARG I 3 165 24.287 10.315 3.018 1.00 34.38

ATOM 1724 O ARG I 3 165 24.944 10.354 4.062 1.00 32.89

ATOM 1726 N TYR I 3 166 23.192 9.581 2.890 1.00 35.19

ATOM 1727 CA TYR I 3 166 22.706 8.815 4.025 1.00 36.84

ATOM 1729 CB TYR I 3 166 21.934 9.714 4.985 1.00 36.96

ATOM 1732 CG TYR I 3 166 20.659 10.256 4.434 1.00 36.43

ATOM 1733 CDl TYR I 3 166 20.674 11.299 3.541 1.00 35.09

ATOM 1735 CEl TYR I 3 166 19.522 11.820 3.037 1.00 38.50

ATOM 1737 CZ TYR I 3 166 18.315 11.293 3.414 1.00 38.49

ATOM 1738 OH TYR I 3 166 17.170 11.839 2.876 1.00 40.10

ATOM 1740 CE2 TYR I 3 166 18.258 10.248 4.307 1.00 39.17

ATOM 1742 CD2 TYR I 3 166 19.435 9.725 4.805 1.00 38.40

ATOM 1744 C TYR I 3 166 21.869 7.602 3.649 1.00 39.08

ATOM 1745 O TYR I 3 166 21.407 7.460 2.507 1.00 38.27

ATOM 1747 N ARG I 3 167 21.696 6.745 4.648 1.00 40.73

ATOM 1748 CA ARG I 3 167 21.148 5.407 4.505 1.00 42.73

ATOM 1750 CB ARG I 3 167 22.210 4.399 4.957 1.00 43.56 ATOM 1753 CG ARG I3 167 21.873 2.949 4.765 1.00 48.59

ATOM 1756 CD ARG I 3 167 22.456 2.397 3.470 1.00 55.13

ATOM 1759 NE ARG I 3 167 22.039 1.010 3.257 1.00 59.51

ATOM 1761 CZ ARG I 3 167 22.551 0.191 2.338 1.00 61.37

ATOM 1762 NHl ARG I 3 167 22.095 -1.053 2.244 1.00 62.36

ATOM 1765 NH2 ARG I 3 167 23.519 0.601 1.517 1.00 61.68

ATOM 1768 C ARG I 3 167 19.914 5.291 5.374 1.00 42.89

ATOM 1769 O ARG I 3 167 19.144 6.245 5.505 1.00 43.23

ATOM 1771 N GLY I 3 176 18.180 5.522 15.981 1.00 42.38

ATOM 1772 CA GLY I 3 176 19.579 5.253 16.276 1.00 42.22

ATOM 1775 C GLY I 3 176 19.852 5.596 17.722 1.00 41.02

ATOM 1776 O GLY I 3 176 18.931 5.970 18.450 1.00 41.84

ATOM 1778 N GLY I 3 177 21.109 5.463 18.133 1.00 39.74

ATOM 1779 CA GLY I 3 177 21.526 5.816 19.489 1.00 38.96

ATOM 1782 C GLY I 3 177 21.322 4.803 20.620 1.00 39.06

ATOM 1783 O GLY I 3 177 21.409 5.197 21.769 1.00 40.51

ATOM 1785 N SER I 3 178 21.105 3.510 20.329 1.00 38.16

ATOM 1786 CA SER I 3 178 20.522 2.542 21.321 1.00 37.26

ATOM 1788 CB SER I 3 178 19.845 1.430 20.551 1.00 38.19

ATOM 1791 OG SER I 3 178 20.771 0.890 19.617 1.00 39.55

ATOM 1793 C SER I 3 178 21.482 1.897 22.349 1.00 34.79

ATOM 1794 O SER I 3 178 21.118 1.568 23.468 1.00 34.98

ATOM 1796 N LEU I 3 179 22.708 1.705 21.927 1.00 33.15

ATOM 1797 CA LEU I 3 179 23.830 1.295 22.749 1.00 30.93

ATOM 1799 CB LEU I 3 179 24.925 1.004 21.716 1.00 31.42

ATOM 1802 CG LEU I 3 179 26.400 0.769 21.914 1.00 35.64

ATOM 1804 CDl LEU I 3 179 26.905 -0.079 20.770 1.00 33.28

ATOM 1808 CD2 LEU I 3 179 27.141 2.088 21.975 1.00 39.93

ATOM 1812 C LEU I 3 179 24.236 2.421 23.763 1.00 28.34

ATOM 1813 O LEU I 3 179 24.913 2.187 24.756 1.00 24.28

ATOM 1815 N VAL I 3 180 23.806 3.645 23.475 1.00 27.32

ATOM 1816 CA VAL I 3 180 24.125 4.828 24.239 1.00 26.77

ATOM 1818 CB VAL I 3 180 24.409 5.991 23.252 1.00 27.32

ATOM 1820 CGl VAL I 3 180 24.640 7.315 23.973 1.00 28.14

ATOM 1824 CG2 VAL I 3 180 25.557 5.627 22.372 1.00 25.87

ATOM 1828 C VAL I 3 180 22.931 5.201 25.104 1.00 27.57

ATOM 1829 O VAL I 3 180 21.787 4.994 24.720 1.00 27.44

ATOM 1831 N GLU I 3 181 23.207 5.795 26.256 1.00 27.27

ATOM 1832 CA GLU I 3 181 22.183 6.370 27.090 1.00 27.77

ATOM 1834 CB GLU I 3 181 22.228 5.723 28.470 1.00 27.82

ATOM 1837 CG GLU I 3 181 20.980 4.969 28.810 1.00 37.21

ATOM 1840 CD GLU I 3 181 21.099 4.208 30.112 1.00 42.56

ATOM 1841 OEl GLU I 3 181 21.686 4.753 31.068 1.00 40.96

ATOM 1842 OE 2 GLU I 3 181 20.613 3.061 30.161 1.00 49.28

ATOM 1843 C GLU I 3 181 22.427 7.870 27.191 1.00 26.52

ATOM 1844 O GLU I 3 181 23.572 8.294 27.358 1.00 26.25

ATOM 1846 N VAL I 3 182 21.360 8.661 27.074 1.00 24.62

ATOM 1847 CA VAL I 3 182 21.433 10.113 27.196 1.00 21.86

ATOM 1849 CB VAL I 3 182 20.743 10.814 26.053 1.00 21.55

ATOM 1851 CGl VAL I 3 182 21.260 10.243 24.697 1.00 17.66

ATOM 1855 CG2 VAL I 3 182 20.931 12.334 26.166 1.00 19.52

ATOM 1859 C VAL I 3 182 20.760 10.492 28.490 1.00 23.04

ATOM 1860 O VAL I 3 182 19.558 10.251 28.684 1.00 24.67

ATOM 1862 N TYR I 3 183 21.514 11.075 29.405 1.00 21.90

ATOM 1863 CA TYR I 3 183 20.905 11.637 30.627 1.00 20.05

ATOM 1865 CB TYR I 3 183 21.883 11.581 31.758 1.00 20.97

ATOM 1868 CG TYR I 3 183 21.906 10.267 32.498 1.00 18.96

ATOM 1869 CDl TYR I 3 183 21.172 10.108 33.662 1.00 22.07

ATOM 1871 CEl TYR I 3 183 21.214 8.934 34.381 1.00 17.81

ATOM 1873 CZ TYR I 3 183 21.970 7.880 33.937 1.00 22.08

ATOM 1874 OH TYR I 3 183 21.965 6.695 34.662 1.00 23.31 ATOM 1876 CE 2 TYR B 183 22.708 7.984 32.765 1.00 22.41

ATOM 1878 CD2 TYR B 183 22.674 9.204 32.049 1.00 21.30

ATOM 1880 C TYR B 183 20.481 13.086 30.396 1.00 20.23

ATOM 1881 O TYR B 183 21.200 13.823 29.752 1.00 21.09

ATOM 1883 N LEU B 184 19.328 13.478 30.918 1.00 19.83

ATOM 1884 CA LEU B 184 18.835 14.854 30.781 1.00 19.80

ATOM 1886 CB LEU B 184 17.474 14.857 30.103 1.00 20.40

ATOM 1889 CG LEU B 184 16.769 16.209 29.920 1.00 21.76

ATOM 1891 CDl LEU B 184 15.353 15.996 29.328 1.00 21.45

ATOM 1895 CD2 LEU B 184 17.598 17.170 29.023 1.00 19.56

ATOM 1899 C LEU B 184 18.736 15.465 32.162 1.00 19.58

ATOM 1900 O LEU B 184 18.026 14.947 33.009 1.00 19.35

ATOM 1902 N LEU B 185 19.382 16.598 32.398 1.00 19.22

ATOM 1903 CA LEU B 185 19.204 17.304 33.673 1.00 18.87

ATOM 1905 CB LEU B 185 20.545 17.678 34.283 1.00 19.35

ATOM 1908 CG LEU B 185 21.255 16.515 34.961 1.00 24.53

ATOM 1910 CDl LEU B 185 21.874 15.665 33.905 1.00 29.83

ATOM 1914 CD2 LEU B 185 22.289 17.038 35.909 1.00 29.34

ATOM 1918 C LEU B 185 18.360 18.554 33.397 1.00 20.60

ATOM 1919 O LEU B 185 18.813 19.484 32.718 1.00 21.55

ATOM 1921 N ASP B 186 17.118 18.585 33.857 1.00 18.61

ATOM 1922 CA ASP B 186 16.194 19.595 33.298 1.00 20.48

ATOM 1924 CB ASP B 186 15.756 19.147 31.903 1.00 20.01

ATOM 1927 CG ASP B 186 15.438 20.303 30.955 1.00 29.91

ATOM 1928 ODl ASP B 186 14.726 21.278 31.305 1.00 35.34

ATOM 1929 OD2 ASP B 186 15.866 20.197 29.800 1.00 42.82

ATOM 1930 C ASP B 186 15.020 19.731 34.232 1.00 19.19

ATOM 1931 O ASP B 186 15.130 19.456 35.396 1.00 20.15

ATOM 1933 N THR B 187 13.905 20.206 33.712 1.00 21.33

ATOM 1934 CA THR B 187 12.651 20.288 34.425 1.00 20.10

ATOM 1936 CB THR B 187 11.625 21.147 33.650 1.00 20.41

ATOM 1938 OGl THR B 187 11.351 20.520 32.393 1.00 23.91

ATOM 1940 CG2 THR B 187 12.117 22.555 33.432 1.00 17.39

ATOM 1944 C THR B 187 12.100 18.892 34.510 1.00 21.34

ATOM 1945 O THR B 187 12.674 17.964 33.988 1.00 20.55

ATOM 1947 N SER B 188 10.963 18.745 35.170 1.00 23.51

ATOM 1948 CA SER B 188 10.282 17.468 35.126 1.00 24.41

ATOM 1950 CB SER B 188 9.113 17.515 36.060 1.00 25.53

ATOM 1953 OG SER B 188 8.361 18.670 35.798 1.00 32.10

ATOM 1955 C SER B 188 9.832 17.233 33.680 1.00 23.69

ATOM 1956 O SER B 188 9.847 18.147 32.860 1.00 22.48

ATOM 1958 N ILE B 189 9.526 16.000 33.341 1.00 23.61

ATOM 1959 CA ILE B 189 9.107 15.706 31.976 1.00 23.32

ATOM 1961 CB ILE B 189 10.162 14.941 31.200 1.00 23.80

ATOM 1963 CGl ILE B 189 10.289 13.520 31.698 1.00 27.64

ATOM 1966 CDl ILE B 189 11.064 12.652 30.755 1.00 34.45

ATOM 1970 CG2 ILE B 189 11.597 15.685 31.223 1.00 20.33

ATOM 1974 C ILE B 189 7.767 14.953 32.002 1.00 25.00

ATOM 1975 O ILE B 189 7.463 14.230 32.964 1.00 23.76

ATOM 1977 N GLN B 190 6.997 15.094 30.930 1.00 25.33

ATOM 1978 CA GLN B 190 5.793 14.290 30.727 1.00 26.35

ATOM 1980 CB GLN B 190 4.807 15.083 29.875 1.00 24.39

ATOM 1983 CG GLN B 190 3.366 14.543 29.805 1.00 31.67

ATOM 1986 CD GLN B 190 2.605 15.084 28.578 1.00 32.69

ATOM 1987 OEl GLN B 190 3.145 15.080 27.457 1.00 47.96

ATOM 1988 NE 2 GLN B 190 1.347 15.516 28.775 1.00 44.09

ATOM 1991 C GLN B 190 6.245 12.996 30.051 1.00 26.28

ATOM 1992 O GLN B 190 6.298 12.896 28.830 1.00 24.60

ATOM 1994 N SER B 191 6.588 11.992 30.855 1.00 26.26

ATOM 1995 CA SER B 191 7.221 10.787 30.324 1.00 28.14

ATOM 1997 CB SER B 191 7.833 9.974 31.470 1.00 28.22 ATOM 2000 OG SER B 191 6.888 9.802 32.495 1.00 30.87

ATOM 2002 C SER B 191 6.297 9.860 29.518 1.00 28.60

ATOM 2003 O SER B 191 6.776 8.955 28.835 1.00 27.43

ATOM 2005 N ASP B 192 4.998 10.095 29.602 1.00 30.41

ATOM 2006 CA ASP B 192 4.004 9.327 28.852 1.00 32.72

ATOM 2008 CB ASP B 192 2.733 9.182 29.691 1.00 34.20

ATOM 2011 CG ASP B 192 2.975 8.399 30.982 1.00 40.62

ATOM 2012 ODl ASP B 192 3.968 7.633 31.043 1.00 49.18

ATOM 2013 OD2 ASP B 192 2.195 8.562 31.952 1.00 53.45

ATOM 2014 C ASP B 192 3.658 9.945 27.493 1.00 32.61

ATOM 2015 O ASP B 192 2.855 9.400 26.758 1.00 31.88

ATOM 2017 N HIS B 193 4.253 11.076 27.147 1.00 31.19

ATOM 2018 CA HIS B 193 4.052 11.620 25.823 1.00 29.09

ATOM 2020 CB HIS B 193 4.864 12.903 25.650 1.00 30.00

ATOM 2023 CG HIS B 193 4.463 13.711 24.459 1.00 24.99

ATOM 2024 NDl HIS B 193 3.675 14.833 24.559 1.00 27.86

ATOM 2026 CEl HIS B 193 3.495 15.342 23.349 1.00 23.52

ATOM 2028 NE 2 HIS B 193 4.129 14.586 22.474 1.00 24.92

ATOM 2030 CD2 HIS B 193 4.742 13.555 23.148 1.00 23.22

ATOM 2032 C HIS B 193 4.469 10.580 24.801 1.00 29.92

ATOM 2033 O HIS B 193 5.420 9.842 25.004 1.00 28.20

ATOM 2035 N ARG B 194 3.766 10.521 23.676 1.00 31.25

ATOM 2036 CA ARG B 194 3.987 9.413 22.738 1.00 31.66

ATOM 2038 CB ARG B 194 2.790 9.263 21.795 1.00 33.84

ATOM 2041 CG ARG B 194 1.443 9.267 22.526 1.00 39.06

ATOM 2044 CD ARG B 194 1.107 7.904 23.177 1.00 50.44

ATOM 2047 NE ARG B 194 0.320 8.090 24.406 1.00 56.22

ATOM 2049 CZ ARG B 194 0.710 7.759 25.644 1.00 58.63

ATOM 2050 NHl ARG B 194 1.884 7.176 25.872 1.00 59.40

ATOM 2053 NH2 ARG B 194 -0.092 8.013 26.677 1.00 58.85

ATOM 2056 C ARG B 194 5.281 9.501 21.937 1.00 30.75

ATOM 2057 O ARG B 194 5.744 8.513 21.371 1.00 29.72

ATOM 2059 N GLU B 195 5.879 10.690 21.870 1.00 29.92

ATOM 2060 CA GLU B 195 7.189 10.826 21.253 1.00 29.61

ATOM 2062 CB GLU B 195 7.601 12.303 21.193 1.00 29.61

ATOM 2065 CG GLU B 195 7.071 13.026 19.976 1.00 29.12

ATOM 2068 CD GLU B 195 7.816 12.637 18.745 1.00 27.54

ATOM 2069 OEl GLU B 195 7.432 11.624 18.129 1.00 29.33

ATOM 2070 OE 2 GLU B 195 8.805 13.329 18.390 1.00 28.87

ATOM 2071 C GLU B 195 8.231 10.066 22.018 1.00 28.56

ATOM 2072 O GLU B 195 9.199 9.604 21.443 1.00 28.39

ATOM 2074 N ILE B 196 8.047 9.967 23.331 1.00 29.09

ATOM 2075 CA ILE B 196 9.107 9.479 24.214 1.00 29.15

ATOM 2077 CB ILE B 196 9.710 10.643 25.004 1.00 29.75

ATOM 2079 CGl ILE B 196 8.661 11.299 25.906 1.00 29.12

ATOM 2082 CDl ILE B 196 9.223 12.367 26.852 1.00 28.82

ATOM 2086 CG2 ILE B 196 10.319 11.677 24.022 1.00 27.67

ATOM 2090 C ILE B 196 8.697 8.341 25.164 1.00 30.72

ATOM 2091 O ILE B 196 9.563 7.634 25.671 1.00 29.17

ATOM 2093 N GLU B 197 7.391 8.149 25.365 1.00 32.34

ATOM 2094 CA GLU B 197 6.856 6.980 26.084 1.00 34.63

ATOM 2096 CB GLU B 197 5.422 6.694 25.599 1.00 34.70

ATOM 2099 CG GLU B 197 4.954 5.254 25.801 1.00 40.31

ATOM 2102 CD GLU B 197 3.726 4.916 24.960 1.00 41.68

ATOM 2103 OEl GLU B 197 3.822 4.910 23.702 1.00 48.28

ATOM 2104 OE 2 GLU B 197 2.659 4.660 25.579 1.00 54.66

ATOM 2105 C GLU B 197 7.693 5.733 25.899 1.00 32.48

ATOM 2106 O GLU B 197 7.938 5.311 24.786 1.00 31.88

ATOM 2108 N GLY B 198 8.126 5.133 27.006 1.00 34.67

ATOM 2109 CA GLY B 198 8.899 3.885 26.955 1.00 36.01

ATOM 2112 C GLY B 198 10.370 4.060 26.576 1.00 37.17 ATOM 2113 O GLY B 198 11.131 3.098 26.560 1.00 38.71

ATOM 2115 N ARG B 199 10.779 5.271 26.240 1.00 36.80

ATOM 2116 CA ARG B 199 12.172 5.510 25.897 1.00 37.64

ATOM 2118 CB ARG B 199 12.291 6.091 24.481 1.00 38.72

ATOM 2121 CG ARG B 199 12.018 5.067 23.366 1.00 46.22

ATOM 2124 CD ARG B 199 12.870 3.791 23.539 1.00 55.59

ATOM 2127 NE ARG B 199 12.964 3.027 22.296 1.00 61.07

ATOM 2129 CZ ARG B 199 12.028 2.191 21.835 1.00 64.76

ATOM 2130 NHl ARG B 199 10.899 1.976 22.509 1.00 66.28

ATOM 2133 NH2 ARG B 199 12.222 1.556 20.682 1.00 64.09

ATOM 2136 C ARG B 199 12.871 6.391 26.928 1.00 35.61

ATOM 2137 O ARG B 199 14.083 6.289 27.068 1.00 36.14

ATOM 2139 N VAL B 200 12.115 7.220 27.645 1.00 33.60

ATOM 2140 CA VAL B 200 12.654 8.002 28.744 1.00 33.84

ATOM 2142 CB VAL B 200 12.192 9.478 28.703 1.00 34.15

ATOM 2144 CGl VAL B 200 12.856 10.281 29.822 1.00 34.37

ATOM 2148 CG2 VAL B 200 12.532 10.105 27.347 1.00 37.10

ATOM 2152 C VAL B 200 12.273 7.386 30.094 1.00 33.84

ATOM 2153 O VAL B 200 11.096 7.153 30.381 1.00 34.28

ATOM 2155 N MET B 201 13.276 7. Ill 30.916 1.00 32.29

ATOM 2156 CA MET B 201 13.041 6.732 32.296 1.00 34.15

ATOM 2158 CB MET B 201 14.006 5.635 32.705 1.00 33.49

ATOM 2161 CG MET B 201 13.694 5.077 34.106 1.00 38.48

ATOM 2164 SD MET B 201 15.081 5.152 35.250 1.00 46.27

ATOM 2165 CE MET B 201 15.689 6.810 34.976 1.00 47.30

ATOM 2169 C MET B 201 13.228 7.938 33.200 1.00 31.09

ATOM 2170 O MET B 201 14.317 8.543 33.222 1.00 29.86

ATOM 2172 N VAL B 202 12.187 8.280 33.961 1.00 28.56

ATOM 2173 CA VAL B 202 12.261 9.331 34.977 1.00 27.49

ATOM 2175 CB VAL B 202 10.882 9.936 35.339 1.00 27.71

ATOM 2177 CGl VAL B 202 11.008 10.967 36.430 1.00 23.95

ATOM 2181 CG2 VAL B 202 10.231 10.566 34.129 1.00 28.16

ATOM 2185 C VAL B 202 12.911 8.726 36.227 1.00 27.46

ATOM 2186 O VAL B 202 12.416 7.771 36.797 1.00 25.25

ATOM 2188 N THR B 203 14.040 9.294 36.632 1.00 26.32

ATOM 2189 CA THR B 203 14.811 8.719 37.704 1.00 25.48

ATOM 2191 CB THR B 203 16.261 9.295 37.728 1.00 25.49

ATOM 2193 OGl THR B 203 16.202 10.725 37.870 1.00 24.05

ATOM 2195 CG2 THR B 203 17.022 8.916 36.465 1.00 23.68

ATOM 2199 C THR B 203 14.120 9.033 39.028 1.00 25.59

ATOM 2200 O THR B 203 14.357 8.356 40.034 1.00 25.69

ATOM 2202 N ASP B 204 13.329 10.105 39.003 1.00 24.87

ATOM 2203 CA ASP B 204 12.763 10.787 40.159 1.00 25.87

ATOM 2205 CB ASP B 204 11.747 9.914 40.904 1.00 27.22

ATOM 2208 CG ASP B 204 10.438 9.747 40.134 1.00 30.34

ATOM 2209 ODl ASP B 204 9.904 10.763 39.625 1.00 34.20

ATOM 2210 OD2 ASP B 204 9.945 8.601 40.038 1.00 32.63

ATOM 2211 C ASP B 204 13.823 11.377 41.095 1.00 25.22

ATOM 2212 O ASP B 204 13.525 11.764 42.206 1.00 23.80

ATOM 2214 N PHE B 205 15.062 11.489 40.623 1.00 25.15

ATOM 2215 CA PHE B 205 15.983 12.415 41.251 1.00 22.16

ATOM 2217 CB PHE B 205 17.355 12.366 40.635 1.00 23.22

ATOM 2220 CG PHE B 205 18.267 13.400 41.193 1.00 21.32

ATOM 2221 CDl PHE B 205 19.082 13.109 42.274 1.00 21.25

ATOM 2223 CEl PHE B 205 19.902 14.091 42.806 1.00 21.45

ATOM 2225 CZ PHE B 205 19.891 15.379 42.294 1.00 18.23

ATOM 2227 CE 2 PHE B 205 19.068 15.685 41.245 1.00 19.72

ATOM 2229 CD2 PHE B 205 18.266 14.687 40.683 1.00 19.83

ATOM 2231 C PHE B 205 15.420 13.815 41.061 1.00 22.70

ATOM 2232 O PHE B 205 15.015 14.168 39.965 1.00 23.82

ATOM 2234 N GLU B 206 15.381 14.574 42.134 1.00 22.59 ATOM 2235 CA GLU B 206 14.907 15.937 42.107 1.00 23.79

ATOM 2237 CB GLU B 206 13.434 15.937 42.474 1.00 24.54

ATOM 2240 CG GLU B 206 12.834 17.261 42.735 1.00 32.80

ATOM 2243 CD GLU B 206 11.324 17.159 42.898 1.00 43.05

ATOM 2244 OEl GLU B 206 10.678 16.515 42.035 1.00 43.70

ATOM 2245 OE2 GLU B 206 10.793 17.723 43.887 1.00 51.80

ATOM 2246 C GLU B 206 15.678 16.745 43.088 1.00 23.70

ATOM 2247 O GLU B 206 15.758 16.390 44.288 1.00 24.09

ATOM 2249 N ASN B 207 16.245 17.852 42.624 1.00 21.65

ATOM 2250 CA ASN B 207 16.849 18.814 43.528 1.00 19.96

ATOM 2252 CB ASN B 207 18.339 18.530 43.725 1.00 20.00

ATOM 2255 CG ASN B 207 18.902 19.241 44.937 1.00 20.57

ATOM 2256 ODl ASN B 207 18.991 20.469 44.963 1.00 24.19

ATOM 2257 ND2 ASN B 207 19.257 18.480 45.970 1.00 20.50

ATOM 2260 C ASN B 207 16.640 20.191 42.928 1.00 19.56

ATOM 2261 O ASN B 207 17.333 20.569 41.978 1.00 20.13

ATOM 2263 N VAL B 208 15.620 20.882 43.386 1.00 21.26

ATOM 2264 CA VAL B 208 15.224 22.136 42.755 1.00 21.87

ATOM 2266 CB VAL B 208 13.967 21.984 41.882 1.00 23.13

ATOM 2268 CGl VAL B 208 14.205 20.967 40.762 1.00 21.63

ATOM 2272 CG2 VAL B 208 12.744 21.598 42.753 1.00 27.61

ATOM 2276 C VAL B 208 14.939 23.158 43.829 1.00 23.68

ATOM 2277 O VAL B 208 14.464 22.816 44.900 1.00 22.08

ATOM 2279 N PRO B 209 15.190 24.438 43.529 1.00 25.08

ATOM 2280 CA PRO B 209 14.868 25.486 44.500 1.00 26.20

ATOM 2282 CB PRO B 209 15.665 26.682 43.981 1.00 24.91

ATOM 2285 CG PRO B 209 15.693 26.475 42.457 1.00 23.24

ATOM 2288 CD PRO B 209 15.706 24.976 42.253 1.00 25.66

ATOM 2291 C PRO B 209 13.339 25.734 44.485 1.00 28.51

ATOM 2292 O PRO B 209 12.671 25.363 43.535 1.00 27.22

ATOM 2293 N GLU B 210 12.780 26.336 45.525 1.00 32.75

ATOM 2294 CA GLU B 210 11.332 26.607 45.535 1.00 37.13

ATOM 2296 CB GLU B 210 10.874 27.109 46.923 1.00 37.56

ATOM 2299 CG GLU B 210 11.558 28.395 47.429 1.00 42.41

ATOM 2302 CD GLU B 210 10.983 28.855 48.778 1.00 43.34

ATOM 2303 OEl GLU B 210 9.886 29.473 48.778 1.00 52.09

ATOM 2304 OE2 GLU B 210 11.626 28.580 49.825 1.00 53.62

ATOM 2305 C GLU B 210 10.973 27.632 44.471 1.00 37.93

ATOM 2306 O GLU B 210 11.803 28.464 44.121 1.00 36.74

ATOM 2308 N GLU B 211 9.747 27.562 43.947 1.00 40.62

ATOM 2309 CA GLU B 211 9.287 28.518 42.932 1.00 42.76

ATOM 2311 CB GLU B 211 7.925 28.098 42.338 1.00 43.56

ATOM 2314 CG GLU B 211 7.990 27.010 41.229 1.00 42.69

ATOM 2317 CD GLU B 211 8.311 25.629 41.771 1.00 46.11

ATOM 2318 OEl GLU B 211 8.289 25.487 43.008 1.00 51.60

ATOM 2319 OE2 GLU B 211 8.604 24.689 40.986 1.00 40.22

ATOM 2320 C GLU B 211 9.218 29.916 43.551 1.00 45.72

ATOM 2321 O GLU B 211 9.116 30.031 44.757 1.00 46.29

ATOM 2323 N ASP B 212 9.313 30.966 42.733 1.00 49.37

ATOM 2324 CA ASP B 212 9.389 32.356 43.224 1.00 51.73

ATOM 2326 CB ASP B 212 10.720 32.616 43.943 1.00 52.74

ATOM 2329 CG ASP B 212 11.914 32.698 42.979 1.00 58.17

ATOM 2330 ODl ASP B 212 12.054 31.803 42.108 1.00 64.75

ATOM 2331 OD2 ASP B 212 12.722 33.652 43.110 1.00 62.05

ATOM 2332 C ASP B 212 9.236 33.383 42.106 1.00 52.46

ATOM 2333 O ASP B 212 8.262 33.354 41.350 1.00 54.12

ATOM 2335 N ALA B 220 1.386 21.910 35.528 1.00 50.44

ATOM 2336 CA ALA B 220 2.038 20.637 35.269 1.00 51.17

ATOM 2338 CB ALA B 220 1.131 19.475 35.625 1.00 51.38

ATOM 2342 C ALA B 220 2.440 20.577 33.800 1.00 51.88

ATOM 2343 O ALA B 220 3.568 20.210 33.486 1.00 52.98 ATOM 2345 N SER B 221 1.508 20.931 32.913 1.00 50.92

ATOM 2346 CA SER B 221 1.806 21.233 31.514 1.00 49.86

ATOM 2348 CB SER B 221 0.548 21.765 30.829 1.00 49.82

ATOM 2351 OG SER B 221 0.870 22.382 29.593 1.00 53.18

ATOM 2353 C SER B 221 2.941 22.271 31.384 1.00 48.49

ATOM 2354 O SER B 221 3.854 22. Ill 30.578 1.00 49.82

ATOM 2356 N LYS B 222 2.879 23.330 32.180 1.00 45.88

ATOM 2357 CA LYS B 222 3.920 24.357 32.183 1.00 43.08

ATOM 2359 CB LYS B 222 3.401 25.604 32.891 1.00 44.08

ATOM 2362 CG LYS B 222 4.457 26.674 33.159 1.00 46.97

ATOM 2365 CD LYS B 222 4.167 27.455 34.444 1.00 49.04

ATOM 2368 CE LYS B 222 5.447 27.707 35.224 1.00 48.68

ATOM 2371 NZ LYS B 222 6.529 28.245 34.340 1.00 47.93

ATOM 2375 C LYS B 222 5.215 23.875 32.851 1.00 40.40

ATOM 2376 O LYS B 222 6.313 24.128 32.333 1.00 39.24

ATOM 2378 N CYS B 223 5.086 23.201 33.999 1.00 36.98

ATOM 2379 CA CYS B 223 6.239 22.676 34.737 1.00 34.97

ATOM 2381 CB CYS B 223 5.823 21.842 35.957 1.00 35.37

ATOM 2384 SG CYS B 223 5.091 22.836 37.262 1.00 44.07

ATOM 2386 C CYS B 223 7.142 21.811 33.892 1.00 31.35

ATOM 2387 O CYS B 223 8.350 21.890 34.047 1.00 32.43

ATOM 2389 N ASP B 224 6.580 20.973 33.033 1.00 27.58

ATOM 2390 CA ASP B 224 7.402 20.022 32.279 1.00 26.95

ATOM 2392 CB ASP B 224 6.978 18.573 32.511 1.00 29.49

ATOM 2395 CG ASP B 224 5.511 18.358 32.470 1.00 37.39

ATOM 2396 ODl ASP B 224 4.808 19.099 31.733 1.00 48.29

ATOM 2397 OD2 ASP B 224 5.079 17.419 33.191 1.00 41.62

ATOM 2398 C ASP B 224 7.539 20.345 30.789 1.00 23.68

ATOM 2399 O ASP B 224 7.901 19.507 29.965 1.00 23.36

ATOM 2401 N SER B 225 7.268 21.587 30.467 1.00 21.42

ATOM 2402 CA SER B 225 7.305 22.019 29.108 1.00 21.65

ATOM 2404 CB SER B 225 6.813 23.458 29.055 1.00 21.72

ATOM 2407 OG SER B 225 7.154 24.034 27.820 1.00 26.20

ATOM 2409 C SER B 225 8.729 21.899 28.534 1.00 21.04

ATOM 2410 O SER B 225 8.955 21.291 27.462 1.00 21.55

ATOM 2412 N HIS B 226 9.699 22.469 29.236 1.00 19.91

ATOM 2413 CA HIS B 226 11.093 22.537 28.693 1.00 18.34

ATOM 2415 CB HIS B 226 11.907 23.411 29.614 1.00 18.03

ATOM 2418 CG HIS B 226 13.316 23.648 29.175 1.00 17.21

ATOM 2419 NDl HIS B 226 14.397 23.058 29.807 1.00 21.58

ATOM 2421 CEl HIS B 226 15.519 23.483 29.248 1.00 19.36

ATOM 2423 NE 2 HIS B 226 15.205 24.357 28.303 1.00 21.10

ATOM 2425 CD2 HIS B 226 13.835 24.477 28.239 1.00 17.46

ATOM 2427 C HIS B 226 11.703 21.147 28.552 1.00 18.14

ATOM 2428 O HIS B 226 12.154 20.758 27.477 1.00 19.23

ATOM 2430 N GLY B 227 11.677 20.378 29.633 1.00 17.66

ATOM 2431 CA GLY B 227 12.250 19.050 29.645 1.00 18.03

ATOM 2434 C GLY B 227 11.594 18.122 28.648 1.00 17.81

ATOM 2435 O GLY B 227 12.266 17.369 27.932 1.00 17.29

ATOM 2437 N THR B 228 10.266 18.163 28.598 1.00 17.16

ATOM 2438 CA THR B 228 9.546 17.271 27.676 1.00 18.16

ATOM 2440 CB THR B 228 8.009 17.383 27.842 1.00 17.28

ATOM 2442 OGl THR B 228 7.658 17.147 29.212 1.00 21.19

ATOM 2444 CG2 THR B 228 7.307 16.384 26.966 1.00 17.57

ATOM 2448 C THR B 228 9.939 17.558 26.239 1.00 15.21

ATOM 2449 O THR B 228 10.168 16.647 25.452 1.00 17.17

ATOM 2451 N HIS B 229 10.029 18.830 25.888 1.00 18.00

ATOM 2452 CA HIS B 229 10.401 19.202 24.523 1.00 15.34

ATOM 2454 CB HIS B 229 10.348 20.726 24.350 1.00 16.03

ATOM 2457 CG HIS B 229 10.509 21.180 22.919 1.00 14.56

ATOM 2458 NDl HIS B 229 11.724 21.510 22.373 1.00 16.07 ATOM 2460 CEl HIS B 229 11.567 21.860 21.108 1.00 13.30

ATOM 2462 NE2 HIS B 229 10.282 21.765 20.806 1.00 15.38

ATOM 2464 CD2 HIS B 229 9.597 21.348 21.929 1.00 16.01

ATOM 2466 C HIS B 229 11.783 18.670 24.166 1.00 16.38

ATOM 2467 O HIS B 229 12.001 18.134 23.104 1.00 16.39

ATOM 2469 N LEU B 230 12.728 18.812 25.084 1.00 16.05

ATOM 2470 CA LEU B 230 14.114 18.446 24.830 1.00 15.82

ATOM 2472 CB LEU B 230 15.008 19.019 25.929 1.00 15.94

ATOM 2475 CG LEU B 230 15.067 20.537 25.989 1.00 17.34

ATOM 2477 CDl LEU B 230 15.953 20.871 27.196 1.00 21.40

ATOM 2481 CD2 LEU B 230 15.593 21.105 24.733 1.00 18.77

ATOM 2485 C LEU B 230 14.314 16.929 24.760 1.00 15.67

ATOM 2486 O LEU B 230 15.053 16.446 23.918 1.00 18.03

ATOM 2488 N ALA B 231 13.627 16.188 25.618 1.00 17.55

ATOM 2489 CA ALA B 231 13.614 14.711 25.497 1.00 19.40

ATOM 2491 CB ALA B 231 12.771 14.115 26.584 1.00 20.60

ATOM 2495 C ALA B 231 13.116 14.298 24.102 1.00 19.38

ATOM 2496 O ALA B 231 13.667 13.389 23.460 1.00 20.70

ATOM 2498 N GLY B 232 12.149 15.046 23.594 1.00 20.68

ATOM 2499 CA GLY B 232 11.612 14.826 22.266 1.00 19.87

ATOM 2502 C GLY B 232 12.549 15.206 21.165 1.00 20.24

ATOM 2503 O GLY B 232 12.605 14.510 20.174 1.00 21.29

ATOM 2505 N VAL B 233 13.258 16.336 21.305 1.00 19.28

ATOM 2506 CA VAL B 233 14.315 16.670 20.358 1.00 17.98

ATOM 2508 CB VAL B 233 14.909 18.070 20.611 1.00 18.38

ATOM 2510 CGl VAL B 233 16.009 18.353 19.596 1.00 16.54

ATOM 2514 CG2 VAL B 233 13.804 19.115 20.542 1.00 17.08

ATOM 2518 C VAL B 233 15.415 15.589 20.328 1.00 17.70

ATOM 2519 O VAL B 233 15.881 15.170 19.234 1.00 17.74

ATOM 2521 N VAL B 234 15.789 15.087 21.489 1.00 18.46

ATOM 2522 CA VAL B 234 16.871 14.076 21.530 1.00 19.86

ATOM 2524 CB VAL B 234 17.468 13.890 22.937 1.00 19.90

ATOM 2526 CGl VAL B 234 18.486 12.737 22.956 1.00 17.67

ATOM 2530 CG2 VAL B 234 18.118 15.209 23.399 1.00 16.21

ATOM 2534 C VAL B 234 16.393 12.744 20.969 1.00 21.68

ATOM 2535 O VAL B 234 17.012 12.216 20.045 1.00 23.25

ATOM 2537 N SER B 235 15.257 12.258 21.452 1.00 23.20

ATOM 2538 CA SER B 235 14.879 10.863 21.227 1.00 24.87

ATOM 2540 CB SER B 235 15.069 10.103 22.554 1.00 25.88

ATOM 2543 OG SER B 235 14.160 10.571 23.529 1.00 28.18

ATOM 2545 C SER B 235 13.462 10.623 20.675 1.00 26.03

ATOM 2546 O SER B 235 13.071 9.482 20.511 1.00 25.55

ATOM 2548 N GLY B 236 12.712 11.684 20.349 1.00 27.03

ATOM 2549 CA GLY B 236 11.292 11.561 19.988 1.00 26.93

ATOM 2552 C GLY B 236 11.072 10.679 18.769 1.00 28.09

ATOM 2553 O GLY B 236 11.784 10.796 17.773 1.00 26.27

ATOM 2555 N ARG B 237 10.078 9.793 18.818 1.00 31.52

ATOM 2556 CA ARG B 237 9.945 8.804 17.718 1.00 34.32

ATOM 2558 CB ARG B 237 8.952 7.680 18.039 1.00 34.45

ATOM 2561 CG ARG B 237 7.505 8.088 18.340 1.00 39.37

ATOM 2564 CD ARG B 237 6.651 6.815 18.642 1.00 42.02

ATOM 2567 NE ARG B 237 7.312 5.970 19.653 1.00 50.71

ATOM 2569 CZ ARG B 237 6.807 5.598 20.832 1.00 53.20

ATOM 2570 NHl ARG B 237 5.568 5.920 21.198 1.00 55.83

ATOM 2573 NH2 ARG B 237 7.555 4.856 21.650 1.00 53.75

ATOM 2576 C ARG B 237 9.660 9.439 16.368 1.00 32.55

ATOM 2577 O ARG B 237 10.149 8.949 15.357 1.00 33.65

ATOM 2579 N ASP B 238 8.935 10.546 16.346 1.00 32.79

ATOM 2580 CA ASP B 238 8.652 11.249 15.084 1.00 32.82

ATOM 2582 CB ASP B 238 7.219 11.781 15.058 1.00 33.87

ATOM 2585 CG ASP B 238 6.166 10.682 14.849 1.00 39.24 ATOM 2586 ODl ASP B 238 6.501 9.561 14.395 1.00 47.70

ATOM 2587 OD2 ASP B 238 4.976 10.961 15.125 1.00 43.68

ATOM 2588 C ASP B 238 9.597 12.424 14.807 1.00 31.42

ATOM 2589 O ASP B 238 10.006 12.627 13.675 1.00 34.31

ATOM 2591 N ALA B 239 9.928 13.221 15.819 1.00 28.02

ATOM 2592 CA ALA B 239 10.657 14.464 15.586 1.00 25.76

ATOM 2594 CB ALA B 239 9.800 15.654 15.980 1.00 25.09

ATOM 2598 C ALA B 239 12.022 14.519 16.288 1.00 25.27

ATOM 2599 O ALA B 239 12.640 15.582 16.372 1.00 23.73

ATOM 2601 N GLY B 240 12.513 13.373 16.746 1.00 24.70

ATOM 2602 CA GLY B 240 13.785 13.319 17.462 1.00 24.75

ATOM 2605 C GLY B 240 14.961 13.145 16.541 1.00 24.53

ATOM 2606 O GLY B 240 14.802 12.739 15.385 1.00 25.27

ATOM 2608 N VAL B 241 16.161 13.397 17.070 1.00 23.46

ATOM 2609 CA VAL B 241 17.383 13.232 16.315 1.00 22.38

ATOM 2611 CB VAL B 241 18.500 14.198 16.850 1.00 21.54

ATOM 2613 CGl VAL B 241 19.886 13.890 16.226 1.00 20.26

ATOM 2617 CG2 VAL B 241 18.108 15.639 16.567 1.00 13.44

ATOM 2621 C VAL B 241 17.861 11.771 16.346 1.00 24.35

ATOM 2622 O VAL B 241 18.268 11.209 15.320 1.00 25.23

ATOM 2624 N ALA B 242 17.863 11.200 17.537 1.00 24.34

ATOM 2625 CA ALA B 242 18.352 9.854 17.767 1.00 25.81

ATOM 2627 CB ALA B 242 19.351 9.830 18.898 1.00 23.63

ATOM 2631 C ALA B 242 17.088 9.110 18.123 1.00 27.82

ATOM 2632 O ALA B 242 16.860 8.773 19.280 1.00 26.33

ATOM 2634 N LYS B 243 16.243 8.906 17.108 1.00 31.40

ATOM 2635 CA LYS B 243 14.853 8.466 17.341 1.00 35.61

ATOM 2637 CB LYS B 243 14.104 8.210 16.023 1.00 35.56

ATOM 2640 CG LYS B 243 13.981 9.445 15.165 1.00 38.14

ATOM 2643 CD LYS B 243 13.050 9.272 13.973 1.00 37.68

ATOM 2646 CE LYS B 243 12.605 10.619 13.423 1.00 40.31

ATOM 2649 NZ LYS B 243 13.734 11.459 12.910 1.00 38.68

ATOM 2653 C LYS B 243 14.797 7.255 18.262 1.00 36.62

ATOM 2654 O LYS B 243 13.964 7.178 19.163 1.00 38.72

ATOM 2656 N GLY B 244 15.710 6.321 18.084 1.00 38.67

ATOM 2657 CA GLY B 244 15.847 5.222 19.062 1.00 39.67

ATOM 2660 C GLY B 244 16.007 5.632 20.531 1.00 40.99

ATOM 2661 O GLY B 244 15.173 5.285 21.391 1.00 41.66

ATOM 2663 N ALA B 245 17.033 6.449 20.771 1.00 39.28

ATOM 2664 CA ALA B 245 17.805 6.485 22.013 1.00 36.45

ATOM 2666 CB ALA B 245 18.671 7.731 22.039 1.00 37.64

ATOM 2670 C ALA B 245 17.059 6.382 23.337 1.00 34.10

ATOM 2671 O ALA B 245 15.992 6.951 23.523 1.00 33.55

ATOM 2673 N SER B 246 17.697 5.693 24.271 1.00 30.34

ATOM 2674 CA SER B 246 17.227 5.618 25.643 1.00 28.64

ATOM 2676 CB SER B 246 17.821 4.388 26.304 1.00 29.07

ATOM 2679 OG SER B 246 17.459 3.243 25.526 1.00 34.00

ATOM 2681 C SER B 246 17.658 6.855 26.394 1.00 26.09

ATOM 2682 O SER B 246 18.793 7.315 26.232 1.00 25.12

ATOM 2684 N MET B 247 16.752 7.393 27.203 1.00 24.66

ATOM 2685 CA MET B 247 17.065 8.527 28.045 1.00 23.12

ATOM 2687 CB MET B 247 16.331 9.763 27.554 1.00 22.25

ATOM 2690 CG MET B 247 16.574 10.106 26.110 1.00 24.78

ATOM 2693 SD MET B 247 15.878 11.745 25.706 1.00 27.44

ATOM 2694 CE MET B 247 17.035 12.864 26.551 1.00 25.93

ATOM 2698 C MET B 247 16.694 8.262 29.498 1.00 23.84

ATOM 2699 O MET B 247 15.785 7.466 29.800 1.00 23.89

ATOM 2701 N ARG B 248 17.401 8.938 30.389 1.00 20.61

ATOM 2702 CA ARG B 248 17.067 8.985 31.800 1.00 21.16

ATOM 2704 CB ARG B 248 18.088 8.204 32.626 1.00 21.92

ATOM 2707 CG ARG B 248 18.289 6.756 32.146 1.00 24.64 ATOM 2710 CD ARG B 248 19.062 5.969 33.181 1.00 35.33

ATOM 2713 NE ARG B 248 19.263 4.589 32.780 1.00 38.66

ATOM 2715 CZ ARG B 248 18.312 3.648 32.812 1.00 45.14

ATOM 2716 NHl ARG B 248 18.590 2.403 32.421 1.00 45.75

ATOM 2719 NH2 ARG B 248 17.081 3.931 33.233 1.00 48.53

ATOM 2722 C ARG B 248 17.032 10.436 32.216 1.00 21.02

ATOM 2723 O ARG B 248 17.934 11.224 31.850 1.00 20.78

ATOM 2725 N SER B 249 16.012 10.821 32.970 1.00 19.87

ATOM 2726 CA SER B 249 15.840 12.238 33.292 1.00 20.22

ATOM 2728 CB SER B 249 14.473 12.726 32.862 1.00 21.06

ATOM 2731 OG SER B 249 13.505 11.754 33.137 1.00 25.26

ATOM 2733 C SER B 249 15.999 12.474 34.778 1.00 21.77

ATOM 2734 O SER B 249 15.486 11.686 35.590 1.00 19.25

ATOM 2736 N LEU B 250 16.706 13.565 35.105 1.00 19.71

ATOM 2737 CA LEU B 250 16.877 14.063 36.471 1.00 20.22

ATOM 2739 CB LEU B 250 18.350 14.182 36.866 1.00 19.27

ATOM 2742 CG LEU B 250 19.156 12.908 37.132 1.00 22.70

ATOM 2744 CDl LEU B 250 19.357 12.124 35.882 1.00 22.97

ATOM 2748 CD2 LEU B 250 20.526 13.265 37.748 1.00 21.41

ATOM 2752 C LEU B 250 16.271 15.462 36.484 1.00 19.76

ATOM 2753 O LEU B 250 16.396 16.222 35.485 1.00 19.27

ATOM 2755 N ARG B 251 15.597 15.792 37.580 1.00 17.73

ATOM 2756 CA ARG B 251 14.972 17.071 37.693 1.00 18.06

ATOM 2758 CB ARG B 251 13.563 16.984 38.282 1.00 19.18

ATOM 2761 CG ARG B 251 12.861 18.316 38.279 1.00 21.53

ATOM 2764 CD ARG B 251 11.574 18.298 39.059 1.00 26.60

ATOM 2767 NE ARG B 251 10.865 19.566 38.892 1.00 28.22

ATOM 2769 CZ ARG B 251 9.980 20.068 39.749 1.00 26.37

ATOM 2770 NHl ARG B 251 9.393 21.221 39.487 1.00 31.60

ATOM 2773 NH2 ARG B 251 9.673 19.430 40.873 1.00 32.51

ATOM 2776 C ARG B 251 15.846 17.973 38.510 1.00 19.61

ATOM 2777 O ARG B 251 16.002 17.783 39.731 1.00 20.34

ATOM 2779 N VAL B 252 16.441 18.954 37.837 1.00 19.82

ATOM 2780 CA VAL B 252 17.226 19.953 38.529 1.00 18.92

ATOM 2782 CB VAL B 252 18.737 19.826 38.220 1.00 19.07

ATOM 2784 CGl VAL B 252 19.191 18.390 38.408 1.00 19.18

ATOM 2788 CG2 VAL B 252 19.059 20.250 36.809 1.00 18.18

ATOM 2792 C VAL B 252 16.723 21.361 38.268 1.00 18.96

ATOM 2793 O VAL B 252 17.302 22.317 38.821 1.00 19.45

ATOM 2795 N LEU B 253 15.623 21.475 37.505 1.00 16.50

ATOM 2796 CA LEU B 253 14.981 22.738 37.241 1.00 16.03

ATOM 2798 CB LEU B 253 15.009 23.036 35.741 1.00 13.30

ATOM 2801 CG LEU B 253 16.376 23.216 35.087 1.00 13.33

ATOM 2803 CDl LEU B 253 16.198 23.568 33.590 1.00 20.46

ATOM 2807 CD2 LEU B 253 17.365 24.173 35.855 1.00 16.69

ATOM 2811 C LEU B 253 13.558 22.691 37.737 1.00 18.15

ATOM 2812 O LEU B 253 12.828 21.712 37.507 1.00 19.38

ATOM 2814 N ASN B 254 13.178 23.744 38.439 1.00 19.54

ATOM 2815 CA ASN B 254 11.824 23.903 38.928 1.00 20.65

ATOM 2817 CB ASN B 254 11.784 24.807 40.160 1.00 20.51

ATOM 2820 CG ASN B 254 11.953 26.300 39.855 1.00 23.05

ATOM 2821 ODl ASN B 254 11.833 26.749 38.712 1.00 21.24

ATOM 2822 ND2 ASN B 254 12.238 27.074 40.905 1.00 16.35

ATOM 2825 C ASN B 254 10.834 24.306 37.820 1.00 22.49

ATOM 2826 O ASN B 254 11.172 24.361 36.603 1.00 20.91

ATOM 2828 N CYS B 255 9.592 24.524 38.221 1.00 23.99

ATOM 2829 CA CYS B 255 8.539 24.815 37.270 1.00 25.54

ATOM 2831 CB CYS B 255 7.187 24.903 37.972 1.00 27.13

ATOM 2834 SG CYS B 255 6.668 23.304 38.531 1.00 33.60

ATOM 2836 C CYS B 255 8.767 26.095 36.536 1.00 24.98

ATOM 2837 O CYS B 255 8.150 26.304 35.502 1.00 26.60 ATOM 2839 N GLN B 256 9.619 26.962 37.062 1.00 23.95

ATOM 2840 CA GLN B 256 9.935 28.213 36.376 1.00 25.63

ATOM 2842 CB GLN B 256 10.052 29.352 37.382 1.00 25.36

ATOM 2845 CG GLN B 256 8.694 29.753 38.019 1.00 29.22

ATOM 2848 CD GLN B 256 8.834 30.614 39.270 1.00 30.53

ATOM 2849 OEl GLN B 256 9.716 30.401 40.091 1.00 39.63

ATOM 2850 NE 2 GLN B 256 7.930 31.576 39.435 1.00 41.64

ATOM 2853 C GLN B 256 11.226 28.101 35.570 1.00 24.21

ATOM 2854 O GLN B 256 11.713 29.108 35.052 1.00 22.29

ATOM 2856 N GLY B 257 11.781 26.885 35.473 1.00 21.45

ATOM 2857 CA GLY B 257 13.048 26.658 34.796 1.00 19.96

ATOM 2860 C GLY B 257 14.278 27.093 35.552 1.00 20.19

ATOM 2861 O GLY B 257 15.301 27.310 34.939 1.00 18.71

ATOM 2863 N LYS B 258 14.194 27.188 36.887 1.00 18.44

ATOM 2864 CA LYS B 258 15.287 27.617 37.712 1.00 18.95

ATOM 2866 CB LYS B 258 14.887 28.826 38.550 1.00 18.90

ATOM 2869 CG LYS B 258 16.054 29.451 39.278 1.00 27.42

ATOM 2872 CD LYS B 258 15.643 30.770 40.014 1.00 25.50

ATOM 2875 CE LYS B 258 15.124 30.531 41.432 1.00 37.19

ATOM 2878 NZ LYS B 258 15.218 31.798 42.255 1.00 37.59

ATOM 2882 C LYS B 258 15.816 26.487 38.591 1.00 17.89

ATOM 2883 O LYS B 258 15.040 25.682 39.156 1.00 15.91

ATOM 2885 N GLY B 259 17.139 26.402 38.644 1.00 17.74

ATOM 2886 CA GLY B 259 17.825 25.409 39.453 1.00 18.44

ATOM 2889 C GLY B 259 18.948 26.044 40.235 1.00 17.77

ATOM 2890 O GLY B 259 19.110 27.283 40.268 1.00 15.21

ATOM 2892 N THR B 260 19.750 25.192 40.851 1.00 15.87

ATOM 2893 CA THR B 260 20.898 25.663 41.576 1.00 15.79

ATOM 2895 CB THR B 260 20.731 25.502 43.096 1.00 17.33

ATOM 2897 OGl THR B 260 20.725 24.108 43.447 1.00 17.97

ATOM 2899 CG2 THR B 260 19.427 26.155 43.608 1.00 17.26

ATOM 2903 C THR B 260 22.160 24.950 41.093 1.00 16.27

ATOM 2904 O THR B 260 22.105 23.852 40.533 1.00 15.69

ATOM 2906 N VAL B 261 23.308 25.591 41.309 1.00 15.64

ATOM 2907 CA VAL B 261 24.558 24.952 41.046 1.00 16.51

ATOM 2909 CB VAL B 261 25.749 25.888 41.246 1.00 18.01

ATOM 2911 CGl VAL B 261 27.057 25.086 41.328 1.00 18.73

ATOM 2915 CG2 VAL B 261 25.786 26.934 40.104 1.00 13.24

ATOM 2919 C VAL B 261 24.677 23.707 41.909 1.00 16.29

ATOM 2920 O VAL B 261 25.056 22.648 41.410 1.00 15.83

ATOM 2922 N SER B 262 24.339 23.801 43.193 1.00 16.49

ATOM 2923 CA SER B 262 24.419 22.620 44.040 1.00 16.93

ATOM 2925 CB SER B 262 24.114 22.984 45.505 1.00 16.60

ATOM 2928 OG SER B 262 22.780 23.433 45.665 1.00 16.37

ATOM 2930 C SER B 262 23.512 21.463 43.567 1.00 17.49

ATOM 2931 O SER B 262 23.931 20.314 43.570 1.00 20.66

ATOM 2933 N GLY B 263 22.270 21.752 43.197 1.00 18.15

ATOM 2934 CA GLY B 263 21.373 20.721 42.712 1.00 16.96

ATOM 2937 C GLY B 263 21.938 20.085 41.462 1.00 17.83

ATOM 2938 O GLY B 263 21.882 18.872 41.289 1.00 15.63

ATOM 2940 N THR B 264 22.562 20.893 40.612 1.00 17.55

ATOM 2941 CA THR B 264 23.157 20.384 39.359 1.00 17.76

ATOM 2943 CB THR B 264 23.568 21.537 38.434 1.00 19.13

ATOM 2945 OGl THR B 264 22.437 22.418 38.283 1.00 21.69

ATOM 2947 CG2 THR B 264 23.997 21.013 37.051 1.00 21.13

ATOM 2951 C THR B 264 24.346 19.466 39.682 1.00 18.18

ATOM 2952 O THR B 264 24.457 18.426 39.084 1.00 16.68

ATOM 2954 N LEU B 265 25.208 19.871 40.618 1.00 16.60

ATOM 2955 CA LEU B 265 26.326 19.046 41.103 1.00 17.85

ATOM 2957 CB LEU B 265 27.104 19.746 42.219 1.00 19.68

ATOM 2960 CG LEU B 265 27.800 21.103 41.947 1.00 19.76 ATOM 2962 CDl LEU B 265 28.380 21.645 43.225 1.00 14.87

ATOM 2966 CD2 LEU B 265 28.896 20.896 40.936 1.00 19.21

ATOM 2970 C LEU B 265 25.834 17.720 41.661 1.00 18.41

ATOM 2971 O LEU B 265 26.420 16.683 41.368 1.00 17.21

ATOM 2973 N ILE B 266 24.785 17.778 42.496 1.00 17.14

ATOM 2974 CA ILE B 266 24.210 16.581 43.095 1.00 16.99

ATOM 2976 CB ILE B 266 23.213 16.948 44.194 1.00 17.87

ATOM 2978 CGl ILE B 266 23.952 17.630 45.343 1.00 16.08

ATOM 2981 CDl ILE B 266 23.035 18.315 46.403 1.00 19.37

ATOM 2985 CG2 ILE B 266 22.475 15.670 44.690 1.00 16.80

ATOM 2989 C ILE B 266 23.654 15.669 41.976 1.00 17.80

ATOM 2990 O ILE B 266 23.850 14.441 41.974 1.00 15.44

ATOM 2992 N GLY B 267 23.070 16.281 40.953 1.00 16.00

ATOM 2993 CA GLY B 267 22.587 15.553 39.776 1.00 16.33

ATOM 2996 C GLY B 267 23.701 14.870 39.015 1.00 17.58

ATOM 2997 O GLY B 267 23.602 13.681 38.751 1.00 15.57

ATOM 2999 N LEU B 268 24.777 15.612 38.696 1.00 17.31

ATOM 3000 CA LEU B 268 25.940 15.035 38.017 1.00 17.00

ATOM 3002 CB LEU B 268 27.024 16.098 37.751 1.00 17.02

ATOM 3005 CG LEU B 268 26.620 17.218 36.779 1.00 16.08

ATOM 3007 CDl LEU B 268 27.614 18.390 36.907 1.00 12.54

ATOM 3011 CD2 LEU B 268 26.560 16.683 35.369 1.00 21.33

ATOM 3015 C LEU B 268 26.535 13.913 38.821 1.00 17.02

ATOM 3016 O LEU B 268 26.846 12.867 38.287 1.00 16.54

ATOM 3018 N GLU B 269 26.608 14.102 40.125 1.00 15.43

ATOM 3019 CA GLU B 269 27.113 13.076 40.993 1.00 16.57

ATOM 3021 CB GLU B 269 27.203 13.628 42.414 1.00 16.60

ATOM 3024 CG GLU B 269 27.797 12.631 43.365 1.00 20.80

ATOM 3027 CD GLU B 269 27.672 13.106 44.794 1.00 26.71

ATOM 3028 OEl GLU B 269 26.569 12.967 45.335 1.00 24.34

ATOM 3029 OE2 GLU B 269 28.665 13.614 45.329 1.00 30.28

ATOM 3030 C GLU B 269 26.227 11.828 40.967 1.00 16.03

ATOM 3031 O GLU B 269 26.721 10.690 40.934 1.00 16.16

ATOM 3033 N PHE B 270 24.923 12.032 40.951 1.00 16.45

ATOM 3034 CA PHE B 270 23.972 10.930 40.864 1.00 17.03

ATOM 3036 CB PHE B 270 22.563 11.505 40.897 1.00 18.70

ATOM 3039 CG PHE B 270 21.512 10.499 40.784 1.00 20.40

ATOM 3040 CDl PHE B 270 20.993 9.905 41.919 1.00 23.73

ATOM 3042 CEl PHE B 270 19.996 8.954 41.804 1.00 24.58

ATOM 3044 CZ PHE B 270 19.529 8.588 40.540 1.00 21.89

ATOM 3046 CE 2 PHE B 270 20.041 9.175 39.423 1.00 26.65

ATOM 3048 CD2 PHE B 270 21.035 10.131 39.539 1.00 16.27

ATOM 3050 C PHE B 270 24.169 10.101 39.612 1.00 18.22

ATOM 3051 O PHE B 270 24.090 8.875 39.628 1.00 16.13

ATOM 3053 N ILE B 271 24.408 10.763 38.497 1.00 18.38

ATOM 3054 CA ILE B 271 24.703 10.047 37.251 1.00 18.10

ATOM 3056 CB ILE B 271 24.920 11.047 36.092 1.00 19.72

ATOM 3058 CGl ILE B 271 23.637 11.822 35.802 1.00 22.36

ATOM 3061 CDl ILE B 271 23.833 13.004 34.769 1.00 20.94

ATOM 3065 CG2 ILE B 271 25.428 10.316 34.842 1.00 17.92

ATOM 3069 C ILE B 271 25.945 9.167 37.394 1.00 17.68

ATOM 3070 O ILE B 271 25.981 8.002 36.944 1.00 16.61

ATOM 3072 N ARG B 272 26.985 9.723 37.993 1.00 17.62

ATOM 3073 CA ARG B 272 28.228 8.991 38.166 1.00 16.92

ATOM 3075 CB ARG B 272 29.332 9.904 38.690 1.00 15.25

ATOM 3078 CG ARG B 272 30.675 9.218 38.982 1.00 19.10

ATOM 3081 CD ARG B 272 31.161 8.442 37.759 1.00 18.53

ATOM 3084 NE ARG B 272 32.504 7.908 37.967 1.00 21.50

ATOM 3086 CZ ARG B 272 33.097 7.045 37.141 1.00 22.96

ATOM 3087 NHl ARG B 272 32.513 6.672 36.050 1.00 17.41

ATOM 3090 NH2 ARG B 272 34.307 6.614 37.381 1.00 20.61 ATOM 3093 C ARG B 272 28.052 7.781 39.089 1.00 17.93

ATOM 3094 O ARG B 272 28.539 6.693 38.774 1.00 17.03

ATOM 3096 N LYS B 273 27.327 7.971 40.183 1.00 18.92

ATOM 3097 CA LYS B 273 27.017 6.873 41.100 1.00 22.34

ATOM 3099 CB LYS B 273 26.293 7.377 42.346 1.00 21.55

ATOM 3102 CG LYS B 273 27.141 8.299 43.205 1.00 26.69

ATOM 3105 CD LYS B 273 26.388 8.760 44.462 1.00 27.81

ATOM 3108 CE LYS B 273 27.342 9.008 45.629 1.00 36.02

ATOM 3111 NZ LYS B 273 26.784 10.060 46.521 1.00 39.85

ATOM 3115 C LYS B 273 26.174 5.798 40.433 1.00 22.94

ATOM 3116 O LYS B 273 26.427 4.607 40.621 1.00 22.86

ATOM 3118 N SER B 274 25.177 6.212 39.652 1.00 22.74

ATOM 3119 CA SER B 274 24.369 5.253 38.908 1.00 23.90

ATOM 3121 CB SER B 274 23.302 5.984 38.107 1.00 24.17

ATOM 3124 OG SER B 274 22.444 6.679 38.999 1.00 29.16

ATOM 3126 C SER B 274 25.237 4.406 37.983 1.00 22.56

ATOM 3127 O SER B 274 25.102 3.195 37.926 1.00 21.83

ATOM 3129 N GLN B 275 26.164 5.040 37.285 1.00 22.07

ATOM 3130 CA GLN B 275 27.034 4.349 36.375 1.00 21.25

ATOM 3132 CB GLN B 275 27.898 5.375 35.659 1.00 22.38

ATOM 3135 CG GLN B 275 28.671 4.878 34.492 1.00 24.80

ATOM 3138 CD GLN B 275 29.697 5.894 34.017 1.00 27.71

ATOM 3139 OEl GLN B 275 30.016 6.854 34.711 1.00 28.63

ATOM 3140 NE 2 GLN B 275 30.217 5.678 32.846 1.00 30.24

ATOM 3143 C GLN B 275 27.903 3.324 37.078 1.00 21.38

ATOM 3144 O GLN B 275 28.083 2.230 36.579 1.00 21.88

ATOM 3146 N LEU B 276 28.464 3.699 38.227 1.00 20.98

ATOM 3147 CA LEU B 276 29.344 2.823 39.038 1.00 20.73

ATOM 3149 CB LEU B 276 29.903 3.591 40.247 1.00 19.14

ATOM 3152 CG LEU B 276 30.989 4.615 39.895 1.00 19.29

ATOM 3154 CDl LEU B 276 31.238 5.522 41.093 1.00 19.13

ATOM 3158 CD2 LEU B 276 32.288 3.962 39.482 1.00 18.31

ATOM 3162 C LEU B 276 28.634 1.589 39.543 1.00 20.82

ATOM 3163 O LEU B 276 29.231 0.517 39.612 1.00 21.43

ATOM 3165 N VAL B 277 27.362 1.753 39.877 1.00 21.37

ATOM 3166 CA VAL B 277 26.558 0.693 40.434 1.00 23.58

ATOM 3168 CB VAL B 277 25.347 1.263 41.218 1.00 23.95

ATOM 3170 CGl VAL B 277 24.455 0.120 41.672 1.00 27.24

ATOM 3174 CG2 VAL B 277 25.809 2.112 42.434 1.00 27.16

ATOM 3178 C VAL B 277 26.039 -0.237 39.333 1.00 24.27

ATOM 3179 O VAL B 277 25.906 -1.449 39.552 1.00 25.29

ATOM 3181 N GLN B 278 25.716 0.335 38.172 1.00 23.89

ATOM 3182 CA GLN B 278 25.203 -0.443 37.059 1.00 25.35

ATOM 3184 CB GLN B 278 23.658 -0.504 37.092 1.00 27.39

ATOM 3187 CG GLN B 278 22.940 0.848 37.198 1.00 36.05

ATOM 3190 CD GLN B 278 22.278 1.136 38.582 1.00 45.81

ATOM 3191 OEl GLN B 278 21.732 0.228 39.255 1.00 50.62

ATOM 3192 NE 2 GLN B 278 22.291 2.420 38.978 1.00 36.00

ATOM 3195 C GLN B 278 25.738 0.078 35.721 1.00 24.85

ATOM 3196 O GLN B 278 25.067 0.833 35.016 1.00 25.49

ATOM 3198 N PRO B 279 26.975 -0.327 35.384 1.00 24.17

ATOM 3199 CA PRO B 279 27.705 0.153 34.223 1.00 23.50

ATOM 3201 CB PRO B 279 29.043 -0.579 34.312 1.00 21.89

ATOM 3204 CG PRO B 279 29.119 -1.133 35.683 1.00 25.96

ATOM 3207 CD PRO B 279 27.759 -1.293 36.178 1.00 23.35

ATOM 3210 C PRO B 279 26.962 -0.217 32.958 1.00 23.55

ATOM 3211 O PRO B 279 26.419 -1.318 32.862 1.00 20.25

ATOM 3212 N VAL B 280 26.892 0.723 32.022 1.00 21.97

ATOM 3213 CA VAL B 280 26.268 0.469 30.744 1.00 22.21

ATOM 3215 CB VAL B 280 24.896 1.170 30.604 1.00 22.93

ATOM 3217 CGl VAL B 280 23.905 0.546 31.550 1.00 27.39 ATOM 3221 CG2 VAL B 280 25.014 2.678 30.875 1.00 27.20

ATOM 3225 C VAL B 280 27.293 0.865 29.703 1.00 21.02

ATOM 3226 O VAL B 280 28.468 0.666 29.942 1.00 21.37

ATOM 3228 N GLY B 281 26.871 1.349 28.533 1.00 20.32

ATOM 3229 CA GLY B 281 27.808 1.755 27.500 1.00 20.81

ATOM 3232 C GLY B 281 28.090 3.247 27.592 1.00 21.06

ATOM 3233 O GLY B 281 27.991 3.842 28.666 1.00 20.35

ATOM 3235 N PRO B 282 28.407 3.858 26.458 1.00 20.46

ATOM 3236 CA PRO B 282 28.653 5.297 26.411 1.00 21.00

ATOM 3238 CB PRO B 282 28.736 5.579 24.923 1.00 21.46

ATOM 3241 CG PRO B 282 29.084 4.298 24.296 1.00 21.09

ATOM 3244 CD PRO B 282 28.588 3.225 25.143 1.00 20.35

ATOM 3247 C PRO B 282 27.501 6.065 26.984 1.00 19.84

ATOM 3248 O PRO B 282 26.368 5.721 26.723 1.00 19.08

ATOM 3249 N LEU B 283 27.813 7.126 27.723 1.00 19.27

ATOM 3250 CA LEU B 283 26.829 8.014 28.285 1.00 19.73

ATOM 3252 CB LEU B 283 26.963 8.060 29.800 1.00 21.66

ATOM 3255 CG LEU B 283 26.100 7.209 30.711 1.00 26.79

ATOM 3257 CDl LEU B 283 25.957 5.791 30.197 1.00 28.67

ATOM 3261 CD2 LEU B 283 26.649 7.265 32.176 1.00 22.49

ATOM 3265 C LEU B 283 27.030 9.413 27.740 1.00 18.75

ATOM 3266 O LEU B 283 28.168 9.905 27.652 1.00 17.80

ATOM 3268 N VAL B 284 25.912 10.030 27.372 1.00 16.74

ATOM 3269 CA VAL B 284 25.854 11.426 27.001 1.00 16.11

ATOM 3271 CB VAL B 284 25.281 11.648 25.586 1.00 15.80

ATOM 3273 CGl VAL B 284 25.203 13.165 25.288 1.00 14.77

ATOM 3277 CG2 VAL B 284 26.116 10.933 24.576 1.00 14.94

ATOM 3281 C VAL B 284 24.980 12.131 28.007 1.00 16.11

ATOM 3282 O VAL B 284 23.884 11.667 28.369 1.00 17.91

ATOM 3284 N VAL B 285 25.482 13.243 28.529 1.00 16.51

ATOM 3285 CA VAL B 285 24.728 14.003 29.513 1.00 14.98

ATOM 3287 CB VAL B 285 25.508 14.122 30.816 1.00 16.39

ATOM 3289 CGl VAL B 285 24.754 15.060 31.832 1.00 16.39

ATOM 3293 CG2 VAL B 285 25.792 12.711 31.349 1.00 17.44

ATOM 3297 C VAL B 285 24.452 15.335 28.924 1.00 15.44

ATOM 3298 O VAL B 285 25.375 16.043 28.558 1.00 14.70

ATOM 3300 N LEU B 286 23.160 15.663 28.820 1.00 17.15

ATOM 3301 CA LEU B 286 22.694 16.913 28.301 1.00 17.28

ATOM 3303 CB LEU B 286 21.452 16.692 27.452 1.00 18.58

ATOM 3306 CG LEU B 286 20.811 17.898 26.766 1.00 19.37

ATOM 3308 CDl LEU B 286 21.807 18.632 25.902 1.00 14.20

ATOM 3312 CD2 LEU B 286 19.631 17.374 25.901 1.00 15.88

ATOM 3316 C LEU B 286 22.341 17.817 29.447 1.00 16.70

ATOM 3317 O LEU B 286 21.505 17.496 30.282 1.00 19.35

ATOM 3319 N LEU B 287 22.958 18.989 29.431 1.00 17.68

ATOM 3320 CA LEU B 287 22.789 20.040 30.416 1.00 16.97

ATOM 3322 CB LEU B 287 24.152 20.345 31.019 1.00 18.11

ATOM 3325 CG LEU B 287 24.656 19.285 31.995 1.00 21.31

ATOM 3327 CDl LEU B 287 26.163 19.345 32.130 1.00 23.48

ATOM 3331 CD2 LEU B 287 23.967 19.525 33.322 1.00 22.14

ATOM 3335 C LEU B 287 22.242 21.260 29.699 1.00 18.35

ATOM 3336 O LEU B 287 23.004 22.116 29.237 1.00 16.83

ATOM 3338 N PRO B 288 20.916 21.321 29.529 1.00 19.25

ATOM 3339 CA PRO B 288 20.237 22.406 28.802 1.00 20.16

ATOM 3341 CB PRO B 288 18.916 21.752 28.398 1.00 20.93

ATOM 3344 CG PRO B 288 18.654 20.812 29.534 1.00 20.59

ATOM 3347 CD PRO B 288 19.971 20.298 29.986 1.00 19.60

ATOM 3350 C PRO B 288 19.960 23.620 29.688 1.00 18.10

ATOM 3351 O PRO B 288 18.801 24.078 29.805 1.00 19.63

ATOM 3352 N LEU B 289 21.012 24.103 30.323 1.00 17.28

ATOM 3353 CA LEU B 289 20.938 25.098 31.397 1.00 17.63 ATOM 3355 CB LEU B 289 20.655 24.415 32.745 1.00 17.47

ATOM 3358 CG LEU B 289 21.679 23.373 33.243 1.00 19.42

ATOM 3360 CDl LEU B 289 22.948 23.993 33.786 1.00 17.36

ATOM 3364 CD2 LEU B 289 21.048 22.412 34.250 1.00 19.17

ATOM 3368 C LEU B 289 22.218 25.875 31.494 1.00 16.27

ATOM 3369 O LEU B 289 23.251 25.416 30.998 1.00 16.52

ATOM 3371 N ALA B 290 22.156 27.056 32.130 1.00 16.51

ATOM 3372 CA ALA B 290 23.341 27.925 32.309 1.00 15.15

ATOM 3374 CB ALA B 290 23.651 28.797 31.040 1.00 14.85

ATOM 3378 C ALA B 290 23.152 28.837 33.523 1.00 15.74

ATOM 3379 O ALA B 290 22.039 29.241 33.889 1.00 15.62

ATOM 3381 N GLY B 291 24.272 29.134 34.145 1.00 17.44

ATOM 3382 CA GLY B 291 24.363 30.193 35.131 1.00 17.44

ATOM 3385 C GLY B 291 25.625 30.930 34.777 1.00 17.06

ATOM 3386 O GLY B 291 26.219 30.674 33.745 1.00 17.20

ATOM 3388 N GLY B 292 26.065 31.822 35.648 1.00 16.97

ATOM 3389 CA GLY B 292 27.316 32.473 35.445 1.00 16.67

ATOM 3392 C GLY B 292 28.479 31.514 35.597 1.00 17.38

ATOM 3393 O GLY B 292 28.316 30.309 35.919 1.00 19.36

ATOM 3395 N TYR B 293 29.680 32.008 35.332 1.00 16.87

ATOM 3396 CA TYR B 293 30.855 31.176 35.469 1.00 15.50

ATOM 3398 CB TYR B 293 32. Ill 31.998 35.279 1.00 16.18

ATOM 3401 CG TYR B 293 33.354 31.172 35.324 1.00 16.93

ATOM 3402 CDl TYR B 293 33.898 30.633 34.158 1.00 22.03

ATOM 3404 CEl TYR B 293 35.049 29.853 34.203 1.00 23.46

ATOM 3406 CZ TYR B 293 35.660 29.619 35.421 1.00 19.79

ATOM 3407 OH TYR B 293 36.806 28.854 35.452 1.00 21.00

ATOM 3409 CE2 TYR B 293 35.141 30.133 36.567 1.00 19.63

ATOM 3411 CD2 TYR B 293 34.016 30.928 36.526 1.00 15.87

ATOM 3413 C TYR B 293 30.880 30.553 36.877 1.00 13.83

ATOM 3414 O TYR B 293 30.763 31.255 37.862 1.00 15.94

ATOM 3416 N SER B 294 31.033 29.249 36.962 1.00 15.24

ATOM 3417 CA SER B 294 31.134 28.564 38.254 1.00 15.64

ATOM 3419 CB SER B 294 29.833 27.809 38.570 1.00 17.21

ATOM 3422 OG SER B 294 30.046 26.832 39.610 1.00 14.68

ATOM 3424 C SER B 294 32.337 27.633 38.260 1.00 16.45

ATOM 3425 O SER B 294 32.409 26.681 37.491 1.00 16.53

ATOM 3427 N ARG B 295 33.281 27.877 39.169 1.00 18.16

ATOM 3428 CA ARG B 295 34.442 27.037 39.259 1.00 17.23

ATOM 3430 CB ARG B 295 35.349 27.558 40.390 1.00 17.74

ATOM 3433 CG ARG B 295 36.583 26.774 40.535 1.00 20.63

ATOM 3436 CD ARG B 295 37.479 27.342 41.548 1.00 17.92

ATOM 3439 NE ARG B 295 38.659 26.512 41.626 1.00 20.25

ATOM 3441 CZ ARG B 295 39.696 26.749 42.413 1.00 20.48

ATOM 3442 NHl ARG B 295 39.686 27.791 43.207 1.00 20.44

ATOM 3445 NH2 ARG B 295 40.736 25.933 42.394 1.00 20.49

ATOM 3448 C ARG B 295 33.991 25.622 39.572 1.00 15.83

ATOM 3449 O ARG B 295 34.438 24.666 38.942 1.00 16.90

ATOM 3451 N VAL B 296 33.113 25.471 40.576 1.00 17.72

ATOM 3452 CA VAL B 296 32.779 24.122 41.038 1.00 17.67

ATOM 3454 CB VAL B 296 32.078 24.092 42.431 1.00 18.61

ATOM 3456 CGl VAL B 296 30.709 24.717 42.370 1.00 18.71

ATOM 3460 CG2 VAL B 296 31.997 22.679 42.919 1.00 18.03

ATOM 3464 C VAL B 296 31.971 23.375 39.980 1.00 16.69

ATOM 3465 O VAL B 296 32.216 22.179 39.736 1.00 18.49

ATOM 3467 N LEU B 297 31.064 24.055 39.284 1.00 17.25

ATOM 3468 CA LEU B 297 30.285 23.361 38.274 1.00 18.07

ATOM 3470 CB LEU B 297 29.106 24.196 37.799 1.00 19.22

ATOM 3473 CG LEU B 297 28.145 23.535 36.815 1.00 21.95

ATOM 3475 CDl LEU B 297 27.600 22.195 37.376 1.00 18.64

ATOM 3479 CD2 LEU B 297 27.010 24.512 36.537 1.00 17.55 ATOM 3483 C LEU B 297 31.214 22.961 37.129 1.00 18.01

ATOM 3484 O LEU B 297 31.194 21.830 36.651 1.00 18.28

ATOM 3486 N ASN B 298 32.069 23.877 36.697 1.00 17.58

ATOM 3487 CA ASN B 298 33.035 23.530 35.672 1.00 15.65

ATOM 3489 CB ASN B 298 33.884 24.729 35.325 1.00 16.44

ATOM 3492 CG ASN B 298 33.142 25.718 34.453 1.00 16.19

ATOM 3493 ODl ASN B 298 31.932 25.584 34.176 1.00 17.86

ATOM 3494 ND2 ASN B 298 33.884 26.691 33.952 1.00 17.93

ATOM 3497 C ASN B 298 33.920 22.378 36.096 1.00 15.86

ATOM 3498 O ASN B 298 34.210 21.481 35.283 1.00 14.60

ATOM 3500 N ALA B 299 34.308 22.342 37.384 1.00 15.85

ATOM 3501 CA ALA B 299 35.199 21.284 37.851 1.00 15.85

ATOM 3503 CB ALA B 299 35.786 21.651 39.273 1.00 16.64

ATOM 3507 C ALA B 299 34.500 19.926 37.860 1.00 16.08

ATOM 3508 O ALA B 299 35.097 18.885 37.540 1.00 15.74

ATOM 3510 N ALA B 300 33.221 19.933 38.216 1.00 16.25

ATOM 3511 CA ALA B 300 32.451 18.714 38.297 1.00 17.35

ATOM 3513 CB ALA B 300 31.138 18.995 38.930 1.00 16.86

ATOM 3517 C ALA B 300 32.256 18.129 36.904 1.00 18.00

ATOM 3518 O ALA B 300 32.319 16.913 36.692 1.00 17.64

ATOM 3520 N CYS B 301 31.970 19.010 35.959 1.00 17.98

ATOM 3521 CA CYS B 301 31.874 18.628 34.555 1.00 18.65

ATOM 3523 CB CYS B 301 31.413 19.861 33.758 1.00 18.28

ATOM 3526 SG CYS B 301 29.682 20.301 34.038 1.00 20.98

ATOM 3528 C CYS B 301 33.169 18.021 34.023 1.00 18.94

ATOM 3529 O CYS B 301 33.165 16.986 33.347 1.00 18.46

ATOM 3531 N GLN B 302 34.281 18.683 34.303 1.00 20.74

ATOM 3532 CA GLN B 302 35.578 18.206 33.887 1.00 22.34

ATOM 3534 CB GLN B 302 36.646 19.169 34.360 1.00 21.88

ATOM 3537 CG GLN B 302 38.052 18.918 33.850 1.00 26.92

ATOM 3540 CD GLN B 302 39.058 20.011 34.364 1.00 29.48

ATOM 3541 OEl GLN B 302 38.815 20.678 35.392 1.00 47.49

ATOM 3542 NE2 GLN B 302 40.170 20.167 33.675 1.00 34.78

ATOM 3545 C GLN B 302 35.838 16.833 34.473 1.00 20.71

ATOM 3546 O GLN B 302 36.319 15.945 33.794 1.00 17.42

ATOM 3548 N ARG B 303 35.542 16.668 35.763 1.00 19.89

ATOM 3549 CA ARG B 303 35.771 15.393 36.393 1.00 20.76

ATOM 3551 CB ARG B 303 35.508 15.520 37.876 1.00 21.29

ATOM 3554 CG ARG B 303 35.729 14.246 38.618 1.00 33.08

ATOM 3557 CD ARG B 303 37.146 14.143 39.157 1.00 48.33

ATOM 3560 NE ARG B 303 37.252 13.026 40.101 1.00 55.74

ATOM 3562 CZ ARG B 303 38.386 12.627 40.667 1.00 60.25

ATOM 3563 NHl ARG B 303 39.535 13.252 40.395 1.00 63.38

ATOM 3566 NH2 ARG B 303 38.371 11.596 41.510 1.00 60.81

ATOM 3569 C ARG B 303 34.888 14.330 35.753 1.00 18.93

ATOM 3570 O ARG B 303 35.318 13.186 35.519 1.00 19.75

ATOM 3572 N LEU B 304 33.654 14.679 35.421 1.00 18.67

ATOM 3573 CA LEU B 304 32.761 13.691 34.860 1.00 18.89

ATOM 3575 CB LEU B 304 31.303 14.150 34.991 1.00 18.62

ATOM 3578 CG LEU B 304 30.199 13.209 34.552 1.00 19.56

ATOM 3580 CDl LEU B 304 30.239 11.851 35.295 1.00 22.63

ATOM 3584 CD2 LEU B 304 28.813 13.856 34.668 1.00 19.84

ATOM 3588 C LEU B 304 33.191 13.370 33.438 1.00 20.27

ATOM 3589 O LEU B 304 33.116 12.200 32.993 1.00 21.71

ATOM 3591 N ALA B 305 33.691 14.385 32.732 1.00 20.02

ATOM 3592 CA ALA B 305 34.251 14.179 31.377 1.00 21.39

ATOM 3594 CB ALA B 305 34.627 15.498 30.743 1.00 19.90

ATOM 3598 C ALA B 305 35.478 13.272 31.462 1.00 22.57

ATOM 3599 O ALA B 305 35.612 12.323 30.694 1.00 22.17

ATOM 3601 N ARG B 306 36.344 13.526 32.440 1.00 24.43

ATOM 3602 CA ARG B 306 37.572 12.721 32.581 1.00 25.75 ATOM 3604 CB ARG B 306 38.538 13.381 33.564 1.00 26.46

ATOM 3607 CG ARG B 306 39.044 14.690 33.005 1.00 34.85

ATOM 3610 CD ARG B 306 40.202 15.303 33.769 1.00 45.29

ATOM 3613 NE ARG B 306 40.455 16.636 33.232 1.00 50.75

ATOM 3615 CZ ARG B 306 40.992 16.883 32.036 1.00 54.41

ATOM 3616 NHl ARG B 306 41.389 15.886 31.240 1.00 58.55

ATOM 3619 NH2 ARG B 306 41.152 18.142 31.631 1.00 51.70

ATOM 3622 C ARG B 306 37.275 11.291 32.967 1.00 25.14

ATOM 3623 O ARG B 306 38.023 10.391 32.646 1.00 25.01

ATOM 3625 N ALA B 307 36.126 11.096 33.597 1.00 26.28

ATOM 3626 CA ALA B 307 35.641 9.796 33.966 1.00 26.37

ATOM 3628 CB ALA B 307 34.593 9.950 35.101 1.00 26.65

ATOM 3632 C ALA B 307 35.068 9.054 32.765 1.00 26.01

ATOM 3633 O ALA B 307 34.641 7.917 32.907 1.00 27.58

ATOM 3635 N GLY B 308 35.047 9.700 31.585 1.00 25.20

ATOM 3636 CA GLY B 308 34.616 9.066 30.316 1.00 23.33

ATOM 3639 C GLY B 308 33.140 9.275 29.937 1.00 23.28

ATOM 3640 O GLY B 308 32.573 8.508 29.165 1.00 23.95

ATOM 3642 N VAL B 309 32.488 10.294 30.482 1.00 23.06

ATOM 3643 CA VAL B 309 31.091 10.577 30.129 1.00 21.39

ATOM 3645 CB VAL B 309 30.267 10.886 31.410 1.00 20.73

ATOM 3647 CGl VAL B 309 28.881 11.456 31.051 1.00 23.05

ATOM 3651 CG2 VAL B 309 30.127 9.618 32.334 1.00 19.94

ATOM 3655 C VAL B 309 31.131 11.787 29.180 1.00 20.17

ATOM 3656 O VAL B 309 31.913 12.704 29.401 1.00 20.65

ATOM 3658 N VAL B 310 30.316 11.798 28.126 1.00 19.95

ATOM 3659 CA VAL B 310 30.306 12.910 27.197 1.00 18.42

ATOM 3661 CB VAL B 310 29.933 12.461 25.774 1.00 19.30

ATOM 3663 CGl VAL B 310 29.635 13.669 24.879 1.00 18.19

ATOM 3667 CG2 VAL B 310 30.997 11.593 25.164 1.00 16.99

ATOM 3671 C VAL B 310 29.263 13.915 27.711 1.00 18.62

ATOM 3672 O VAL B 310 28.115 13.543 28.018 1.00 18.85

ATOM 3674 N LEU B 311 29.646 15.183 27.825 1.00 16.29

ATOM 3675 CA LEU B 311 28.734 16.215 28.291 1.00 15.70

ATOM 3677 CB LEU B 311 29.280 16.896 29.562 1.00 15.71

ATOM 3680 CG LEU B 311 29.027 16.189 30.896 1.00 18.68

ATOM 3682 CDl LEU B 311 29.905 15.008 31.001 1.00 25.60

ATOM 3686 CD2 LEU B 311 29.298 17.132 32.057 1.00 19.86

ATOM 3690 C LEU B 311 28.486 17.238 27.194 1.00 14.15

ATOM 3691 O LEU B 311 29.433 17.665 26.533 1.00 13.58

ATOM 3693 N VAL B 312 27.219 17.582 26.981 1.00 12.17

ATOM 3694 CA VAL B 312 26.800 18.567 25.994 1.00 14.60

ATOM 3696 CB VAL B 312 25.978 17.926 24.856 1.00 13.39

ATOM 3698 CGl VAL B 312 25.564 18.952 23.829 1.00 12.58

ATOM 3702 CG2 VAL B 312 26.788 16.847 24.204 1.00 16.78

ATOM 3706 C VAL B 312 25.972 19.604 26.761 1.00 15.13

ATOM 3707 O VAL B 312 25.118 19.265 27.552 1.00 17.44

ATOM 3709 N THR B 313 26.271 20.879 26.581 1.00 16.08

ATOM 3710 CA THR B 313 25.558 21.908 27.274 1.00 15.51

ATOM 3712 CB THR B 313 26.416 22.495 28.407 1.00 18.31

ATOM 3714 OGl THR B 313 25.606 23.262 29.342 1.00 18.19

ATOM 3716 CG2 THR B 313 27.516 23.341 27.827 1.00 13.51

ATOM 3720 C THR B 313 25.153 23.004 26.304 1.00 16.15

ATOM 3721 O THR B 313 25.715 23.149 25.225 1.00 12.09

ATOM 3723 N ALA B 314 24.181 23.789 26.744 1.00 16.69

ATOM 3724 CA ALA B 314 23.730 24.960 26.034 1.00 15.08

ATOM 3726 CB ALA B 314 22.390 25.416 26.576 1.00 14.11

ATOM 3730 C ALA B 314 24.772 26.058 26.181 1.00 14.78

ATOM 3731 O ALA B 314 25.321 26.231 27.268 1.00 14.51

ATOM 3733 N ALA B 315 25.050 26.774 25.094 1.00 12.63

ATOM 3734 CA ALA B 315 25.928 27.959 25.163 1.00 13.78 ATOM 3736 CB ALA B 315 26.163 28.536 23.814 1.00 13.05

ATOM 3740 C ALA B 315 25.402 29.061 26.082 1.00 13.08

ATOM 3741 O ALA B 315 26.203 29.834 26.571 1.00 13.30

ATOM 3743 N GLY B 316 24.065 29.157 26.226 1.00 12.71

ATOM 3744 CA GLY B 316 23.409 30.254 26.939 1.00 12.41

ATOM 3747 C GLY B 316 22.692 31.166 25.940 1.00 13.26

ATOM 3748 O GLY B 316 23.132 31.301 24.797 1.00 13.20

ATOM 3750 N ASN B 317 21.627 31.800 26.398 1.00 13.73

ATOM 3751 CA ASN B 317 20.755 32.619 25.570 1.00 14.33

ATOM 3753 CB ASN B 317 19.319 32.234 25.826 1.00 14.53

ATOM 3756 CG ASN B 317 19.012 30.832 25.419 1.00 14.04

ATOM 3757 ODl ASN B 317 19.714 30.216 24.592 1.00 14.47

ATOM 3758 ND2 ASN B 317 17.840 30.357 25.877 1.00 12.33

ATOM 3761 C ASN B 317 20.918 34.134 25.840 1.00 15.42

ATOM 3762 O ASN B 317 19.965 34.886 25.711 1.00 15.17

ATOM 3764 N PHE B 318 22.141 34.555 26.155 1.00 15.64

ATOM 3765 CA PHE B 318 22.397 35.910 26.666 1.00 16.34

ATOM 3767 CB PHE B 318 23.193 35.813 27.955 1.00 17.47

ATOM 3770 CG PHE B 318 22.522 34.936 28.999 1.00 19.40

ATOM 3771 CDl PHE B 318 21.406 35.366 29.655 1.00 26.12

ATOM 3773 CEl PHE B 318 20.787 34.552 30.594 1.00 23.34

ATOM 3775 CZ PHE B 318 21.270 33.298 30.829 1.00 23.98

ATOM 3777 CE 2 PHE B 318 22.339 32.852 30.151 1.00 20.79

ATOM 3779 CD2 PHE B 318 22.970 33.674 29.249 1.00 19.58

ATOM 3781 C PHE B 318 23.079 36.805 25.679 1.00 15.58

ATOM 3782 O PHE B 318 23.462 37.907 26.027 1.00 16.72

ATOM 3784 N ARG B 319 23.179 36.356 24.434 1.00 16.37

ATOM 3785 CA ARG B 319 23.888 37.072 23.395 1.00 17.51

ATOM 3787 CB ARG B 319 23.029 38.182 22.810 1.00 18.57

ATOM 3790 CG ARG B 319 23.453 38.545 21.421 1.00 21.29

ATOM 3793 CD ARG B 319 22.688 39.753 20.897 1.00 29.42

ATOM 3796 NE ARG B 319 22.615 39.671 19.450 1.00 38.20

ATOM 3798 CZ ARG B 319 22.268 40.672 18.652 1.00 46.05

ATOM 3799 NHl ARG B 319 22.028 41.911 19.138 1.00 50.21

ATOM 3802 NH2 ARG B 319 22.209 40.435 17.345 1.00 42.94

ATOM 3805 C ARG B 319 25.193 37.619 23.907 1.00 16.62

ATOM 3806 O ARG B 319 25.508 38.807 23.751 1.00 16.62

ATOM 3808 N ASP B 320 25.973 36.725 24.491 1.00 15.44

ATOM 3809 CA ASP B 320 27.161 37.086 25.244 1.00 16.60

ATOM 3811 CB ASP B 320 26.742 37.201 26.717 1.00 15.46

ATOM 3814 CG ASP B 320 27.673 38.024 27.560 1.00 21.03

ATOM 3815 ODl ASP B 320 28.645 38.618 27.039 1.00 20.09

ATOM 3816 OD2 ASP B 320 27.452 38.008 28.805 1.00 23.61

ATOM 3817 C ASP B 320 28.202 36.015 25.071 1.00 14.78

ATOM 3818 O ASP B 320 27.982 34.988 24.430 1.00 12.61

ATOM 3820 N ASP B 321 29.360 36.273 25.625 1.00 13.62

ATOM 3821 CA ASP B 321 30.476 35.379 25.512 1.00 14.77

ATOM 3823 CB ASP B 321 31.708 36.105 26.024 1.00 14.54

ATOM 3826 CG ASP B 321 32.949 35.331 25.832 1.00 16.59

ATOM 3827 ODl ASP B 321 32.908 34.081 25.715 1.00 19.71

ATOM 3828 OD2 ASP B 321 33.990 35.978 25.843 1.00 21.50

ATOM 3829 C ASP B 321 30.182 34.183 26.388 1.00 14.50

ATOM 3830 O ASP B 321 30.058 34.316 27.597 1.00 13.85

ATOM 3832 N ALA B 322 30.143 33.009 25.786 1.00 15.29

ATOM 3833 CA ALA B 322 29.815 31.797 26.548 1.00 15.97

ATOM 3835 CB ALA B 322 29.661 30.587 25.576 1.00 16.07

ATOM 3839 C ALA B 322 30.819 31.504 27.635 1.00 16.59

ATOM 3840 O ALA B 322 30.501 30.807 28.592 1.00 18.44

ATOM 3842 N CYS B 323 32.038 32.034 27.532 1.00 17.57

ATOM 3843 CA CYS B 323 33.055 31.812 28.586 1.00 17.41

ATOM 3845 CB CYS B 323 34.425 32.317 28.143 1.00 20.76 ATOM 3848 SG CYS B 323 35.010 31.572 26.572 1.00 25.17

ATOM 3850 C CYS B 323 32.708 32.418 29.936 1.00 17.31

ATOM 3851 O CYS B 323 33.359 32.120 30.954 1.00 16.28

ATOM 3853 N LEU B 324 31.699 33.273 29.949 1.00 15.50

ATOM 3854 CA LEU B 324 31.215 33.900 31.190 1.00 15.38

ATOM 3856 CB LEU B 324 30.765 35.338 30.880 1.00 14.75

ATOM 3859 CG LEU B 324 31.848 36.162 30.199 1.00 13.58

ATOM 3861 CDl LEU B 324 31.359 37.613 30.080 1.00 17.93

ATOM 3865 CD2 LEU B 324 33.169 36.103 30.893 1.00 17.73

ATOM 3869 C LEU B 324 30.122 33.110 31.863 1.00 14.64

ATOM 3870 O LEU B 324 29.583 33.560 32.887 1.00 14.12

ATOM 3872 N TYR B 325 29.843 31.889 31.347 1.00 13.48

ATOM 3873 CA TYR B 325 28.735 31.090 31.792 1.00 12.18

ATOM 3875 CB TYR B 325 27.587 31.075 30.803 1.00 11.75

ATOM 3878 CG TYR B 325 27.072 32.478 30.588 1.00 15.09

ATOM 3879 CDl TYR B 325 26.025 32.977 31.366 1.00 16.43

ATOM 3881 CEl TYR B 325 25.617 34.315 31.258 1.00 16.77

ATOM 3883 CZ TYR B 325 26.209 35.145 30.313 1.00 16.01

ATOM 3884 OH TYR B 325 25.784 36.463 30.164 1.00 19.17

ATOM 3886 CE2 TYR B 325 27.261 34.695 29.522 1.00 13.11

ATOM 3888 CD2 TYR B 325 27.685 33.323 29.658 1.00 13.41

ATOM 3890 C TYR B 325 29.191 29.692 32.041 1.00 13.04

ATOM 3891 O TYR B 325 30.180 29.271 31.489 1.00 13.57

ATOM 3893 N SER B 326 28.472 29.018 32.911 1.00 14.84

ATOM 3894 CA SER B 326 28.678 27.595 33.134 1.00 14.59

ATOM 3896 CB SER B 326 29.301 27.403 34.518 1.00 13.38

ATOM 3899 OG SER B 326 30.623 27.864 34.543 1.00 15 . 84

ATOM 3901 C SER B 326 27.372 26.805 33.055 1.00 15 . 36

ATOM 3902 O SER B 326 26.310 27.298 33.431 1.00 15 . 57

ATOM 3904 N PRO B 327 27.444 25.536 32.645 1.00 17 . 28

ATOM 3905 CA PRO B 327 28.616 24.792 32.217 1.00 17 . 44

ATOM 3907 CB PRO B 327 28.138 23.325 32.225 1.00 17 . 86

ATOM 3910 CG PRO B 327 26.708 23.337 32.376 1.00 18 . 87

ATOM 3913 CD PRO B 327 26.235 24.690 32.705 1.00 17 . 16

ATOM 3916 C PRO B 327 29.214 25.156 30.862 1.00 17 . 12

ATOM 3917 O PRO B 327 30.211 24.568 30.526 1.00 17 . 20

ATOM 3918 N ALA B 328 28.644 26.120 30.130 1.00 15.37

ATOM 3919 CA ALA B 328 29.129 26.508 28.795 1.00 15.63

ATOM 3921 CB ALA B 328 28.489 27.833 28.360 1.00 15.50

ATOM 3925 C ALA B 328 30.648 26.616 28.751 1.00 14.79

ATOM 3926 O ALA B 328 31.274 26.132 27.816 1.00 16.03

ATOM 3928 N SER B 329 31.243 27.276 29.747 1.00 13.30

ATOM 3929 CA SER B 329 32.664 27.571 29.771 1.00 15.00

ATOM 3931 CB SER B 329 32.958 28.714 30.739 1.00 14.72

ATOM 3934 OG SER B 329 32.634 28.347 32.078 1.00 15.86

ATOM 3936 C SER B 329 33.612 26.388 30.092 1.00 19.20

ATOM 3937 O SER B 329 34.799 26.524 29.941 1.00 18.81

ATOM 3939 N ALA B 330 33.098 25.246 30.501 1.00 20.38

ATOM 3940 CA ALA B 330 33.944 24.099 30.847 1.00 21.93

ATOM 3942 CB ALA B 330 33.064 23.110 31.636 1.00 20.68

ATOM 3946 C ALA B 330 34.526 23.478 29.560 1.00 24.51

ATOM 3947 O ALA B 330 33.784 23.012 28.743 1.00 25.77

ATOM 3949 N PRO B 331 35.875 23.447 29.367 1.00 29.32

ATOM 3950 CA PRO B 331 36.401 23.035 28.051 1.00 28.74

ATOM 3952 CB PRO B 331 37.924 23.198 28.208 1.00 30.94

ATOM 3955 CG PRO B 331 38.099 24.102 29.420 1.00 32.15

ATOM 3958 CD PRO B 331 36.977 23.698 30.312 1.00 29.16

ATOM 3961 C PRO B 331 36.072 21.588 27.635 1.00 28.68

ATOM 3962 O PRO B 331 35.938 21.308 26.418 1.00 26.89

ATOM 3963 N GLU B 332 35.951 20.689 28.620 1.00 24.38

ATOM 3964 CA GLU B 332 35.641 19.299 28.312 1.00 25.73 ATOM 3966 CB GLU B 332 36.001 18.383 29.464 1.00 25.63

ATOM 3969 CG GLU B 332 37.471 18.415 29.841 1.00 34.53

ATOM 3972 CD GLU B 332 38.308 17.424 29.050 1.00 47.45

ATOM 3973 OEl GLU B 332 38.434 17.615 27.815 1.00 50.90

ATOM 3974 OE2 GLU B 332 38.837 16.457 29.667 1.00 54.82

ATOM 3975 C GLU B 332 34.162 19.066 27.957 1.00 23.57

ATOM 3976 O GLU B 332 33.804 17.980 27.536 1.00 26.83

ATOM 3978 N VAL B 333 33.325 20.072 28.109 1.00 20.31

ATOM 3979 CA VAL B 333 31.894 19.971 27.793 1.00 19.32

ATOM 3981 CB VAL B 333 31.076 20.804 28.796 1.00 20.15

ATOM 3983 CGl VAL B 333 29.580 20.816 28.485 1.00 21.98

ATOM 3987 CG2 VAL B 333 31.307 20.273 30.203 1.00 19.75

ATOM 3991 C VAL B 333 31.723 20.495 26.370 1.00 18.79

ATOM 3992 O VAL B 333 32.327 21.513 25.996 1.00 19.77

ATOM 3994 N ILE B 334 30.910 19.810 25.582 1.00 15.88

ATOM 3995 CA ILE B 334 30.594 20.265 24.225 1.00 15.23

ATOM 3997 CB ILE B 334 30.129 19.132 23.325 1.00 16.29

ATOM 3999 CGl ILE B 334 31.240 18.077 23.244 1.00 18.35

ATOM 4002 CDl ILE B 334 30.738 16.656 23.005 1.00 29.66

ATOM 4006 CG2 ILE B 334 29.798 19.684 21.892 1.00 13.85

ATOM 4010 C ILE B 334 29.535 21.340 24.351 1.00 14.34

ATOM 4011 O ILE B 334 28.424 21.094 24.794 1.00 15.84

ATOM 4013 N THR B 335 29.914 22.565 24.027 1.00 14.66

ATOM 4014 CA THR B 335 29.027 23.716 24.201 1.00 13.57

ATOM 4016 CB THR B 335 29.822 24.854 24.764 1.00 15.63

ATOM 4018 OGl THR B 335 30.412 24.425 26.001 1.00 12.95

ATOM 4020 CG2 THR B 335 28.952 26.059 25.013 1.00 13.53

ATOM 4024 C THR B 335 28.407 24.148 22.890 1.00 13.30

ATOM 4025 O THR B 335 29. Ill 24.364 21.916 1.00 14.28

ATOM 4027 N VAL B 336 27.088 24.283 22.877 1.00 13.15

ATOM 4028 CA VAL B 336 26.367 24.387 21.633 1.00 13.18

ATOM 4030 CB VAL B 336 25.469 23.201 21.421 1.00 10.68

ATOM 4032 CGl VAL B 336 24.844 23.237 19.992 1.00 9.87

ATOM 4036 CG2 VAL B 336 26.248 21.870 21.699 1.00 13.46

ATOM 4040 C VAL B 336 25.549 25.683 21.537 1.00 13.50

ATOM 4041 O VAL B 336 24.712 25.983 22.398 1.00 13.08

ATOM 4043 N GLY B 337 25.838 26.457 20.505 1.00 13.09

ATOM 4044 CA GLY B 337 25.076 27.686 20.237 1.00 13.43

ATOM 4047 C GLY B 337 23.913 27.353 19.303 1.00 13.22

ATOM 4048 O GLY B 337 23.824 26.250 18.757 1.00 13.91

ATOM 4050 N ALA B 338 23.041 28.323 19.048 1.00 13.14

ATOM 4051 CA ALA B 338 21.790 28.039 18.304 1.00 12.86

ATOM 4053 CB ALA B 338 20.586 28.413 19.127 1.00 14.72

ATOM 4057 C ALA B 338 21.806 28.829 17.025 1.00 14.01

ATOM 4058 O ALA B 338 22.072 30.027 17.054 1.00 13.68

ATOM 4060 N THR B 339 21.504 28.162 15.921 1.00 15.40

ATOM 4061 CA THR B 339 21.297 28.813 14.624 1.00 15.57

ATOM 4063 CB THR B 339 22.312 28.368 13.603 1.00 13.81

ATOM 4065 OGl THR B 339 22.410 26.924 13.600 1.00 15.72

ATOM 4067 CG2 THR B 339 23.671 28.925 13.932 1.00 17.36

ATOM 4071 C THR B 339 19.861 28.502 14.133 1.00 16.23

ATOM 4072 O THR B 339 19.205 27.516 14.551 1.00 14.74

ATOM 4074 N ASN B 340 19.391 29.358 13.235 1.00 17.63

ATOM 4075 CA ASN B 340 18.053 29.249 12.694 1.00 18.18

ATOM 4077 CB ASN B 340 17.396 30.623 12.680 1.00 18.53

ATOM 4080 CG ASN B 340 18.041 31.588 11.745 1.00 21.80

ATOM 4081 ODl ASN B 340 18.808 31.216 10.859 1.00 19.04

ATOM 4082 ND2 ASN B 340 17.766 32.867 11.959 1.00 25.11

ATOM 4085 C ASN B 340 18.052 28.603 11.314 1.00 20.46

ATOM 4086 O ASN B 340 19.081 28.141 10.838 1.00 19.97

ATOM 4088 N ALA B 341 16.883 28.554 10.690 1.00 20.37 ATOM 4089 CA ALA I3 341 16.708 27.950 9.378 1.00 20.96

ATOM 4091 CB ALA I 3 341 15.231 27.991 8.970 1.00 20.11

ATOM 4095 C ALA I 3 341 17.538 28.595 8.312 1.00 21.68

ATOM 4096 O ALA I 3 341 17.784 27.971 7.309 1.00 21.13

ATOM 4098 N GLN I 3 342 17.960 29.838 8.513 1.00 22.38

ATOM 4099 CA GLN I 3 342 18.849 30.487 7.573 1.00 25.37

ATOM 4101 CB GLN I 3 342 18.380 31.922 7.364 1.00 26.97

ATOM 4104 CG GLN I 3 342 17.006 31.981 6.605 1.00 31.45

ATOM 4107 CD GLN I 3 342 15.784 31.655 7.486 1.00 39.59

ATOM 4108 OEl GLN I 3 342 15.650 32.170 8.594 1.00 46.41

ATOM 4109 NE2 GLN I 3 342 14.893 30.790 6.989 1.00 46.40

ATOM 4112 C GLN I 3 342 20.344 30.370 7.965 1.00 25.31

ATOM 4113 O GLN I 3 342 21.216 31.056 7.419 1.00 24.65

ATOM 4115 N ASP I 3 343 20.606 29.444 8.890 1.00 24.78

ATOM 4116 CA ASP I 3 343 21.921 29.187 9.474 1.00 25.42

ATOM 4118 CB ASP I 3 343 22.909 28.609 8.447 1.00 26.88

ATOM 4121 CG ASP I 3 343 22.623 27.154 8.079 1.00 28.59

ATOM 4122 ODl ASP I 3 343 22.202 26.310 8.938 1.00 24.01

ATOM 4123 OD2 ASP I 3 343 22.850 26.844 6.898 1.00 37.07

ATOM 4124 C ASP I 3 343 22.516 30.413 10.126 1.00 23.76

ATOM 4125 O ASP I 3 343 23.731 30.517 10.238 1.00 23.46

ATOM 4127 N GLN I 3 344 21.671 31.331 10.577 1.00 21.97

ATOM 4128 CA GLN I 3 344 22.154 32.514 11.283 1.00 20.73

ATOM 4130 CB GLN I 3 344 21.461 33.759 10.727 1.00 21.10

ATOM 4133 CG GLN I 3 344 21.743 33.925 9.221 1.00 26.30

ATOM 4136 CD GLN I 3 344 23.219 33.706 1.00 32.79

ATOM 4137 OEl GLN I 3 344 24.087 34.415 9.415 1.00 30.48

ATOM 4138 NE2 GLN I 3 344 23.517 32.703 8.019 1.00 30.39

ATOM 4141 C GLN I 3 344 21.940 32.365 12.799 1.00 18.88

ATOM 4142 O GLN I 3 344 21.094 31.585 13.223 1.00 17.17

ATOM 4144 N PRO I 3 345 22.756 33.056 13.605 1.00 16.29

ATOM 4145 CA PRO I 3 345 22.572 32.920 15.046 1.00 18.40

ATOM 4147 CB PRO I 3 345 23.707 33.741 15.671 1.00 18.04

ATOM 4150 CG PRO I 3 345 24.618 34.101 14.539 1.00 21.74

ATOM 4153 CD PRO I 3 345 23.857 33.954 13.250 1.00 19.82

ATOM 4156 C PRO I 3 345 21.185 33.357 15.502 1.00 18.04

ATOM 4157 O PRO I 3 345 20.618 34.331 14.991 1.00 19.53

ATOM 4158 N VAL I 3 346 20.631 32.603 16.428 1.00 15.99

ATOM 4159 CA VAL I 3 346 19.253 32.812 16.857 1.00 16.62

ATOM 4161 CB VAL I 3 346 18.729 31.614 17.576 1.00 15.02

ATOM 4163 CGl VAL I 3 346 17.317 31.902 18.090 1.00 20.57

ATOM 4167 CG2 VAL I 3 346 18.714 30.385 16.660 1.00 15.59

ATOM 4171 C VAL I 3 346 19.139 34.055 17.794 1.00 18.62

ATOM 4172 O VAL I 3 346 19.915 34.206 18.737 1.00 17.67

ATOM 4174 N THR I 3 347 18.214 34.963 17.461 1.00 20.81

ATOM 4175 CA THR I 3 347 17.788 36.052 18.333 1.00 21.37

ATOM 4177 CB THR I 3 347 17.253 37.270 17.490 1.00 22.48

ATOM 4179 OGl THR I 3 347 18.283 37.718 16.596 1.00 25.33

ATOM 4181 CG2 THR I 3 347 16.895 38.415 18.398 1.00 24.91

ATOM 4185 C THR I 3 347 16.641 35.543 19.200 1.00 22.25

ATOM 4186 O THR I 3 347 15.735 34.867 18.723 1.00 21.97

ATOM 4188 N LEU I 3 348 16.691 35.861 20.483 1.00 25.21

ATOM 4189 CA LEU I 3 348 15.728 35.410 21.461 1.00 26.36

ATOM 4191 CB LEU I 3 348 16.347 34.346 22.386 1.00 26.95

ATOM 4194 CG LEU I 3 348 16.755 33.036 21.714 1.00 28.31

ATOM 4196 CDl LEU I 3 348 17.701 32.225 22.604 1.00 31.12

ATOM 4200 CD2 LEU I 3 348 15.502 32.239 21.320 1.00 30.54

ATOM 4204 C LEU I 3 348 15.347 36.659 22.263 1.00 28.26

ATOM 4205 O LEU I 3 348 16.049 37.064 23.188 1.00 27.92

ATOM 4207 N GLY I 3 349 14.262 37.303 21.845 1.00 29.78

ATOM 4208 CA GLY I 3 349 13.897 38.629 22.356 1.00 29.79 ATOM 4211 C GLY I3 349 14.970 39.650 22.056 1.00 28.34

ATOM 4212 O GLY I 3 349 15.372 39.824 20.921 1.00 28.40

ATOM 4214 N THR I 3 350 15.455 40.305 23.100 1.00 27.89

ATOM 4215 CA THR I 3 350 16.512 41.287 22.968 1.00 27.06

ATOM 4217 CB THR I 3 350 16.437 42.368 24.059 1.00 27.24

ATOM 4219 OGl THR I 3 350 16.302 41.738 25.346 1.00 30.04

ATOM 4221 CG2 THR I 3 350 15.260 43.308 23.792 1.00 32.20

ATOM 4225 C THR I 3 350 17.864 40.623 23.102 1.00 24.36

ATOM 4226 O THR I 3 350 18.886 41.277 22.939 1.00 22.36

ATOM 4228 N LEU I 3 351 17.881 39.318 23.368 1.00 22.06

ATOM 4229 CA LEU I 3 351 19.146 38.611 23.480 1.00 18.32

ATOM 4231 CB LEU I 3 351 19.348 38.091 24.921 1.00 19.42

ATOM 4234 CG LEU I 3 351 19.400 39.156 26.060 1.00 21.73

ATOM 4236 CDl LEU I 3 351 19.577 38.539 27.448 1.00 23.59

ATOM 4240 CD2 LEU I 3 351 20.479 40.161 25.781 1.00 25.94

ATOM 4244 C LEU I 3 351 19.227 37.537 22.383 1.00 17.52

ATOM 4245 O LEU I 3 351 18.831 37.775 21.220 1.00 17.04

ATOM 4247 N GLY I 3 352 19.748 36.366 22.706 1.00 15.96

ATOM 4248 CA GLY I 3 352 20.066 35.392 21.673 1.00 15.88

ATOM 4251 C GLY I 3 352 21.170 34.443 22.065 1.00 14.39

ATOM 4252 O GLY I 3 352 21.659 34.450 23.209 1.00 15.36

ATOM 4254 N THR I 3 353 21.539 33.611 21.119 1.00 13.51

ATOM 4255 CA THR I 3 353 22.600 32.638 21.351 1.00 13.30

ATOM 4257 CB THR I 3 353 22.878 31.787 20.137 1.00 13.54

ATOM 4259 OGl THR I 3 353 23.826 30.777 20.480 1.00 14.11

ATOM 4261 CG2 THR I 3 353 23.460 32.639 18.956 1.00 11.61

ATOM 4265 C THR I 3 353 23.862 33.328 21.809 1.00 13.46

ATOM 4266 O THR I 3 353 24.233 34.416 21.327 1.00 13.26

ATOM 4268 N ASN I 3 354 24.507 32.734 22.799 1.00 13.95

ATOM 4269 CA ASN I 3 354 25.863 33.108 23.136 1.00 13.45

ATOM 4271 CB ASN I 3 354 26.286 32.488 24.448 1.00 14.06

ATOM 4274 CG ASN I 3 354 25.739 33.191 25.650 1.00 13.19

ATOM 4275 ODl ASN I 3 354 25.113 34.242 25.560 1.00 13.53

ATOM 4276 ND2 ASN I 3 354 25.977 32.592 26.824 1.00 14.57

ATOM 4279 C ASN I 3 354 26.831 32.691 22.026 1.00 13.77

ATOM 4280 O ASN I 3 354 26.486 31.952 21.116 1.00 13.94

ATOM 4282 N PHE I 3 355 28.071 33.148 22.123 1.00 14.16

ATOM 4283 CA PHE I 3 355 29.058 32.927 21.081 1.00 11.85

ATOM 4285 CB PHE I 3 355 28.925 34.058 20.051 1.00 13.16

ATOM 4288 CG PHE I 3 355 28.735 35.428 20.696 1.00 9.16

ATOM 4289 CDl PHE I 3 355 27.491 36.022 20.736 1.00 15.69

ATOM 4291 CEl PHE I 3 355 27.298 37.220 21.367 1.00 14.51

ATOM 4293 CZ PHE I 3 355 28.350 37.852 21.964 1.00 11.82

ATOM 4295 CE 2 PHE I 3 355 29.573 37.294 21.982 1.00 12.53

ATOM 4297 CD2 PHE I 3 355 29.784 36.052 21.341 1.00 16.86

ATOM 4299 C PHE I 3 355 30.431 32.944 21.746 1.00 12.21

ATOM 4300 O PHE I 3 355 30.558 32.918 22.989 1.00 11.59

ATOM 4302 N GLY I 3 356 31.468 32.969 20.936 1.00 12.19

ATOM 4303 CA GLY I 3 356 32.822 33.049 21.437 1.00 12.85

ATOM 4306 C GLY I 3 356 33.543 31.720 21.512 1.00 14.36

ATOM 4307 O GLY I 3 356 33.060 30.699 21.036 1.00 15.73

ATOM 4309 N ARG I 3 357 34.738 31.736 22.108 1.00 15.39

ATOM 4310 CA ARG I 3 357 35.644 30.615 21.953 1.00 16.15

ATOM 4312 CB ARG I 3 357 37.090 31.002 22.238 1.00 16.02

ATOM 4315 CG ARG I 3 357 37.263 31.623 23.547 1.00 19.39

ATOM 4318 CD ARG I 3 357 38.740 31.618 24.016 1.00 23.64

ATOM 4321 NE ARG I 3 357 38.667 31.933 25.435 1.00 30.05

ATOM 4323 CZ ARG I 3 357 38.639 31.059 26.431 1.00 23.41

ATOM 4324 NHl ARG I 3 357 38.796 29.766 26.222 1.00 30.78

ATOM 4327 NH2 ARG I 3 357 38.530 31.515 27.664 1.00 35.25

ATOM 4330 C ARG I 3 357 35.272 29.401 22.811 1.00 14.84 ATOM 4331 O ARG B 357 35.810 28.356 22.577 1.00 16.04

ATOM 4333 N CYS B 358 34.398 29.549 23.806 1.00 15.95

ATOM 4334 CA CYS B 358 33.872 28.398 24.550 1.00 14.72

ATOM 4336 CB CYS B 358 33.484 28.848 25.962 1.00 15.84

ATOM 4339 SG CYS B 358 34.987 29.471 26.895 1.00 19.90

ATOM 4341 C CYS B 358 32.718 27.681 23.829 1.00 17.68

ATOM 4342 O CYS B 358 32.235 26.668 24.302 1.00 17.09

ATOM 4344 N VAL B 359 32.250 28.215 22.702 1.00 16.69

ATOM 4345 CA VAL B 359 31.234 27.515 21.937 1.00 15.11

ATOM 4347 CB VAL B 359 30.282 28.493 21.153 1.00 14.97

ATOM 4349 CGl VAL B 359 29.339 27.715 20.225 1.00 16.62

ATOM 4353 CG2 VAL B 359 29.466 29.375 22.089 1.00 14.64

ATOM 4357 C VAL B 359 31.994 26.596 20.971 1.00 15.08

ATOM 4358 O VAL B 359 32.881 27.039 20.259 1.00 14.07

ATOM 4360 N ASP B 360 31.620 25.324 20.947 1.00 14.70

ATOM 4361 CA ASP B 360 32.234 24.316 20. Ill 1.00 15.40

ATOM 4363 CB ASP B 360 32.062 22.942 20.793 1.00 15.25

ATOM 4366 CG ASP B 360 32.920 22.825 22.011 1.00 18.36

ATOM 4367 ODl ASP B 360 34.139 22.777 21.821 1.00 18.51

ATOM 4368 OD2 ASP B 360 32.427 22.867 23.148 1.00 20.47

ATOM 4369 C ASP B 360 31.639 24.323 18.705 1.00 15.87

ATOM 4370 O ASP B 360 32.359 24.189 17.704 1.00 16.23

ATOM 4372 N LEU B 361 30.320 24.464 18.637 1.00 15.50

ATOM 4373 CA LEU B 361 29.617 24.497 17.391 1.00 15.35

ATOM 4375 CB LEU B 361 29.564 23.119 16.731 1.00 16.33

ATOM 4378 CG LEU B 361 28.661 22.018 17.273 1.00 17.60

ATOM 4380 CDl LEU B 361 28.848 21.643 18.759 1.00 17.15

ATOM 4384 CD2 LEU B 361 28.908 20.762 16.346 1.00 14.47

ATOM 4388 C LEU B 361 28.228 24.999 17.605 1.00 13.98

ATOM 4389 O LEU B 361 27.777 25.172 18.743 1.00 14.80

ATOM 4391 N PHE B 362 27.548 25.258 16.497 1.00 13.52

ATOM 4392 CA PHE B 362 26.136 25.623 16.550 1.00 12.57

ATOM 4394 CB PHE B 362 25.877 26.889 15.731 1.00 13.14

ATOM 4397 CG PHE B 362 26.537 28.099 16.311 1.00 12.16

ATOM 4398 CDl PHE B 362 25.809 29.006 17.053 1.00 12.48

ATOM 4400 CEl PHE B 362 26.408 30.063 17.650 1.00 12.16

ATOM 4402 CZ PHE B 362 27.802 30.281 17.470 1.00 11.71

ATOM 4404 CE 2 PHE B 362 28.535 29.412 16.750 1.00 14.68

ATOM 4406 CD2 PHE B 362 27.908 28.314 16.161 1.00 14.61

ATOM 4408 C PHE B 362 25.292 24.465 16.048 1.00 13.31

ATOM 4409 O PHE B 362 25.769 23.601 15.328 1.00 15.26

ATOM 4411 N ALA B 363 24.012 24.514 16.370 1.00 14.68

ATOM 4412 CA ALA B 363 23.066 23.547 15.904 1.00 16.41

ATOM 4414 CB ALA B 363 23.095 22.278 16.818 1.00 10.91

ATOM 4418 C ALA B 363 21.667 24.206 15.839 1.00 15.83

ATOM 4419 O ALA B 363 21.453 25.295 16.404 1.00 15.36

ATOM 4421 N PRO B 364 20.734 23.594 15.087 1.00 16.59

ATOM 4422 CA PRO B 364 19.379 24.144 15.003 1.00 16.04

ATOM 4424 CB PRO B 364 18.633 23.052 14.242 1.00 15.78

ATOM 4427 CG PRO B 364 19.654 22.539 13.327 1.00 14.72

ATOM 4430 CD PRO B 364 20.860 22.433 14.196 1.00 16.80

ATOM 4433 C PRO B 364 18.769 24.425 16.350 1.00 17.25

ATOM 4434 O PRO B 364 18.720 23.543 17.203 1.00 17.50

ATOM 4435 N GLY B 365 18.383 25.684 16.573 1.00 15.13

ATOM 4436 CA GLY B 365 17.788 26.102 17.833 1.00 17.93

ATOM 4439 C GLY B 365 16.753 27.219 17.735 1.00 18.01

ATOM 4440 O GLY B 365 16.508 27.949 18.707 1.00 16.73

ATOM 4442 N GLU B 366 16.094 27.319 16.583 1.00 18.78

ATOM 4443 CA GLU B 366 14.938 28.188 16.428 1.00 18.73

ATOM 4445 CB GLU B 366 15.290 29.360 15.527 1.00 21.06

ATOM 4448 CG GLU B 366 14.170 30.369 15.423 1.00 20.47 ATOM 4451 CD GLU B 366 14.580 31.702 14.878 1.00 28.78

ATOM 4452 OEl GLU B 366 15.658 32.210 15.216 1.00 32.86

ATOM 4453 OE 2 GLU B 366 13.803 32.251 14.094 1.00 33.94

ATOM 4454 C GLU B 366 13.801 27.407 15.793 1.00 19.31

ATOM 4455 O GLU B 366 14.044 26.643 14.846 1.00 16.45

ATOM 4457 N ASP B 367 12.586 27.557 16.306 1.00 18.91

ATOM 4458 CA ASP B 367 11.423 26.947 15.678 1.00 19.09

ATOM 4460 CB ASP B 367 11.180 27.547 14.299 1.00 21.48

ATOM 4463 CG ASP B 367 9.895 27.023 13.625 1.00 26.56

ATOM 4464 ODl ASP B 367 8.991 26.497 14.324 1.00 33.14

ATOM 4465 OD2 ASP B 367 9.819 27.144 12.377 1.00 36.96

ATOM 4466 C ASP B 367 11.616 25.441 15.554 1.00 19.61

ATOM 4467 O ASP B 367 11.486 24.844 14.469 1.00 18.25

ATOM 4469 N ILE B 368 11.962 24.832 16.680 1.00 18.31

ATOM 4470 CA ILE B 368 12.306 23.414 16.698 1.00 17.47

ATOM 4472 CB ILE B 368 13.479 23.123 17.659 1.00 16.96

ATOM 4474 CGl ILE B 368 14.735 23.881 17.204 1.00 15.48

ATOM 4477 CDl ILE B 368 15.239 23.630 15.747 1.00 18.36

ATOM 4481 CG2 ILE B 368 13.720 21.612 17.828 1.00 13.56

ATOM 4485 C ILE B 368 11.085 22.689 17.192 1.00 17.94

ATOM 4486 O ILE B 368 10.692 22.831 18.341 1.00 16.39

ATOM 4488 N ILE B 369 10.481 21.881 16.331 1.00 19.66

ATOM 4489 CA ILE B 369 9.251 21.214 16.762 1.00 21.02

ATOM 4491 CB ILE B 369 8.346 20.872 15.561 1.00 22.63

ATOM 4493 CGl ILE B 369 6.861 20.695 16.032 1.00 27.84

ATOM 4496 CDl ILE B 369 6.047 22.049 16.269 1.00 27.28

ATOM 4500 CG2 ILE B 369 8.901 19.702 14.845 1.00 23.24

ATOM 4504 C ILE B 369 9.582 19.990 17.610 1.00 20.33

ATOM 4505 O ILE B 369 10.537 19.256 17.346 1.00 21.17

ATOM 4507 N GLY B 370 8.841 19.817 18.684 1.00 20.75

ATOM 4508 CA GLY B 370 9.002 18.637 19.515 1.00 20.70

ATOM 4511 C GLY B 370 7.859 18.445 20.480 1.00 21.39

ATOM 4512 O GLY B 370 6.966 19.272 20.594 1.00 22.77

ATOM 4514 N ALA B 371 7.913 17.362 21.227 1.00 21.28

ATOM 4515 CA ALA B 371 6.876 17.047 22.194 1.00 22.75

ATOM 4517 CB ALA B 371 7.351 15.926 23.125 1.00 22.69

ATOM 4521 C ALA B 371 6.441 18.211 23.041 1.00 22.16

ATOM 4522 O ALA B 371 7.279 18.879 23.651 1.00 22.27

ATOM 4524 N SER B 372 5.120 18.396 23.146 1.00 20.60

ATOM 4525 CA SER B 372 4.516 19.406 24.009 1.00 22.20

ATOM 4527 CB SER B 372 3.450 20.184 23.255 1.00 23.00

ATOM 4530 OG SER B 372 2.847 21.141 24.117 1.00 24.89

ATOM 4532 C SER B 372 3.840 18.702 25.172 1.00 24.01

ATOM 4533 O SER B 372 2.994 17.824 24.958 1.00 25.44

ATOM 4535 N SER B 373 4.140 19.120 26.386 1.00 24.84

ATOM 4536 CA SER B 373 3.530 18.530 27.550 1.00 27.08

ATOM 4538 CB SER B 373 4.339 18.866 28.792 1.00 27.78

ATOM 4541 OG SER B 373 4.348 20.247 29.024 1.00 26.48

ATOM 4543 C SER B 373 2.089 18.995 27.753 1.00 29.21

ATOM 4544 O SER B 373 1.467 18.675 28.768 1.00 30.43

ATOM 4546 N ASP B 374 1.557 19.761 26.813 1.00 30.44

ATOM 4547 CA ASP B 374 0.124 20.084 26.843 1.00 32.69

ATOM 4549 CB ASP B 374 -0.230 21.028 25.706 1.00 33.07

ATOM 4552 CG ASP B 374 0.277 22.413 25.938 1.00 37.98

ATOM 4553 ODl ASP B 374 0.633 22.734 27.106 1.00 47.15

ATOM 4554 OD2 ASP B 374 0.334 23.185 24.952 1.00 46.97

ATOM 4555 C ASP B 374 -0.719 18.841 26.761 1.00 33.27

ATOM 4556 O ASP B 374 -1.688 18.684 27.504 1.00 35.45

ATOM 4558 N CYS B 375 -0.348 17.942 25.864 1.00 33.77

ATOM 4559 CA CYS B 375 -1.092 16.713 25.724 1.00 34.47

ATOM 4561 CB CYS B 375 -2.351 16.958 24.868 1.00 34.59 ATOM 4564 SG CYS B 375 -2.126 16.611 23.124 1.00 41.57

ATOM 4566 C CYS B 375 -0.179 15.675 25.130 1.00 32.73

ATOM 4567 O CYS B 375 0.813 15.996 24.478 1.00 31.76

ATOM 4569 N SER B 376 -0.519 14.419 25.342 1.00 30.37

ATOM 4570 CA SER B 376 0.404 13.348 25.066 1.00 30.58

ATOM 4572 CB SER B 376 -0.147 12.040 25.616 1.00 31.42

ATOM 4575 OG SER B 376 -1.224 11.636 24.800 1.00 37.25

ATOM 4577 C SER B 376 0.717 13.164 23.596 1.00 28.59

ATOM 4578 O SER B 376 1.616 12.415 23.247 1.00 28.11

ATOM 4580 N THR B 377 -0.009 13.841 22.713 1.00 28.14

ATOM 4581 CA THR B 377 0.292 13.744 21.297 1.00 27.34

ATOM 4583 CB THR B 377 -0.815 13.007 20.571 1.00 28.76

ATOM 4585 OGl THR B 377 -2.037 13.728 20.763 1.00 27.89

ATOM 4587 CG2 THR B 377 -0.915 11.571 21.133 1.00 30.46

ATOM 4591 C THR B 377 0.522 15.110 20.664 1.00 25.78

ATOM 4592 O THR B 377 0.720 15.198 19.471 1.00 25.01

ATOM 4594 N CYS B 378 0.577 16.148 21.490 1.00 23.78

ATOM 4595 CA CYS B 378 0.726 17.498 21.027 1.00 24.71

ATOM 4597 CB CYS B 378 0.179 18.436 22.073 1.00 24.65

ATOM 4600 SG CYS B 378 -1.630 18.412 22.235 1.00 33.23

ATOM 4602 C CYS B 378 2.199 17.832 20.763 1.00 24.42

ATOM 4603 O CYS B 378 3.105 17.215 21.342 1.00 22.76

ATOM 4605 N PHE B 379 2.421 18.840 19.932 1.00 21.02

ATOM 4606 CA PHE B 379 3.759 19.315 19.589 1.00 20.66

ATOM 4608 CB PHE B 379 4.125 18.910 18.171 1.00 21.77

ATOM 4611 CG PHE B 379 4.514 17.460 18.035 1.00 23.69

ATOM 4612 CDl PHE B 379 5.839 17.080 18.017 1.00 24.11

ATOM 4614 CEl PHE B 379 6.199 15.751 17.910 1.00 26.53

ATOM 4616 CZ PHE B 379 5.230 14.786 17.797 1.00 26.77

ATOM 4618 CE 2 PHE B 379 3.891 15.144 17.800 1.00 30.78

ATOM 4620 CD2 PHE B 379 3.539 16.477 17.923 1.00 27.22

ATOM 4622 C PHE B 379 3.798 20.815 19.728 1.00 20.56

ATOM 4623 O PHE B 379 2.756 21.478 19.670 1.00 20.49

ATOM 4625 N VAL B 380 4.994 21.355 19.981 1.00 19.16

ATOM 4626 CA VAL B 380 5.203 22.798 20.145 1.00 19.03

ATOM 4628 CB VAL B 380 5.110 23.236 21.613 1.00 19.76

ATOM 4630 CGl VAL B 380 6.250 22.606 22.434 1.00 21.43

ATOM 4634 CG2 VAL B 380 5.093 24.813 21.760 1.00 16.45

ATOM 4638 C VAL B 380 6.583 23.119 19.576 1.00 19.53

ATOM 4639 O VAL B 380 7.503 22.286 19.677 1.00 18.62

ATOM 4641 N SER B 381 6.714 24.274 18.933 1.00 21.42

ATOM 4642 CA SER B 381 8.033 24.771 18.496 1.00 22.67

ATOM 4644 CB SER B 381 7.989 25.582 17.194 1.00 24.74

ATOM 4647 OG SER B 381 7.662 24.744 16.092 1.00 34.61

ATOM 4649 C SER B 381 8.615 25.621 19.611 1.00 21.99

ATOM 4650 O SER B 381 7.958 26.493 20.179 1.00 22.38

ATOM 4652 N GLN B 382 9.884 25.371 19.907 1.00 20.31

ATOM 4653 CA GLN B 382 10.607 26.111 20.904 1.00 19.45

ATOM 4655 CB GLN B 382 10.807 25.251 22.137 1.00 18.23

ATOM 4658 CG GLN B 382 9.510 25.021 22.929 1.00 20.85

ATOM 4661 CD GLN B 382 9.727 24.467 24.360 1.00 24.15

ATOM 4662 OEl GLN B 382 10.856 24.396 24.857 1.00 30.86

ATOM 4663 NE 2 GLN B 382 8.625 24.080 25.019 1.00 26.38

ATOM 4666 C GLN B 382 11.954 26.538 20.321 1.00 17.64

ATOM 4667 O GLN B 382 12.407 25.984 19.323 1.00 16.73

ATOM 4669 N SER B 383 12.540 27.576 20.907 1.00 16.56

ATOM 4670 CA SER B 383 13.809 28.105 20.440 1.00 15.38

ATOM 4672 CB SER B 383 13.612 29.471 19.741 1.00 17.69

ATOM 4675 OG SER B 383 12.721 29.370 18.616 1.00 16.48

ATOM 4677 C SER B 383 14.759 28.231 21.623 1.00 15.39

ATOM 4678 O SER B 383 14.346 28.525 22.749 1.00 14.53 ATOM 4680 N GLY B 384 16.045 28.026 21.391 1.00 15.01

ATOM 4681 CA GLY B 384 17.015 28.247 22.481 1.00 14.44

ATOM 4684 C GLY B 384 18.246 27.441 22.262 1.00 13.97

ATOM 4685 O GLY B 384 18.298 26.522 21.395 1.00 14.28

ATOM 4687 N THR B 385 19.293 27.812 22.977 1.00 13.25

ATOM 4688 CA THR B 385 20.500 27.027 22.878 1.00 14.51

ATOM 4690 CB THR B 385 21.731 27.749 23.450 1.00 13.06

ATOM 4692 OGl THR B 385 21.463 28.103 24.805 1.00 13.63

ATOM 4694 CG2 THR B 385 22.076 28.960 22.600 1.00 11.69

ATOM 4698 C THR B 385 20.292 25.647 23.574 1.00 14.11

ATOM 4699 O THR B 385 21.050 24.740 23.276 1.00 15.70

ATOM 4701 N SER B 386 19.319 25.489 24.493 1.00 15.31

ATOM 4702 CA SER B 386 18.991 24.118 25.004 1.00 15.42

ATOM 4704 CB SER B 386 17.793 24.127 25.920 1.00 17.71

ATOM 4707 OG SER B 386 18.003 24.948 27.067 1.00 25.51

ATOM 4709 C SER B 386 18.585 23.186 23.846 1.00 14.82

ATOM 4710 O SER B 386 18.951 22.013 23.818 1.00 14.31

ATOM 4712 N GLN B 387 17.728 23.704 22.959 1.00 14.91

ATOM 4713 CA GLN B 387 17.259 22.941 21.788 1.00 14.75

ATOM 4715 CB GLN B 387 16.184 23.683 20.999 1.00 13.83

ATOM 4718 CG GLN B 387 14.772 23.521 21.533 1.00 13.66

ATOM 4721 CD GLN B 387 14.533 24.291 22.781 1.00 16.54

ATOM 4722 OEl GLN B 387 15.211 25.275 23.042 1.00 18.38

ATOM 4723 NE2 GLN B 387 13.622 23.786 23.626 1.00 19.49

ATOM 4726 C GLN B 387 18.433 22.592 20.893 1.00 15.63

ATOM 4727 O GLN B 387 18.561 21.447 20.428 1.00 15.84

ATOM 4729 N ALA B 388 19.301 23.571 20.666 1.00 14.83

ATOM 4730 CA ALA B 388 20.527 23.345 19.909 1.00 14.54

ATOM 4732 CB ALA B 388 21.300 24.645 19.811 1.00 14.70

ATOM 4736 C ALA B 388 21.361 22.254 20.544 1.00 13.76

ATOM 4737 O ALA B 388 21.773 21.296 19.873 1.00 18.18

ATOM 4739 N ALA B 389 21.554 22.348 21.855 1.00 15.18

ATOM 4740 CA ALA B 389 22.352 21.370 22.569 1.00 12.80

ATOM 4742 CB ALA B 389 22.490 21.782 24.023 1.00 12.89

ATOM 4746 C ALA B 389 21.734 19.966 22.443 1.00 13.04

ATOM 4747 O ALA B 389 22.446 18.997 22.348 1.00 14.74

ATOM 4749 N ALA B 390 20.418 19.879 22.431 1.00 13.16

ATOM 4750 CA ALA B 390 19.696 18.592 22.295 1.00 14.21

ATOM 4752 CB ALA B 390 18.163 18.816 22.439 1.00 13.60

ATOM 4756 C ALA B 390 20.000 17.951 20.968 1.00 14.57

ATOM 4757 O ALA B 390 20.102 16.731 20.883 1.00 14.85

ATOM 4759 N HIS B 391 20.125 18.750 19.908 1.00 14.35

ATOM 4760 CA HIS B 391 20.519 18.199 18.617 1.00 15.43

ATOM 4762 CB HIS B 391 20.575 19.307 17.571 1.00 15.24

ATOM 4765 CG HIS B 391 19.237 19.673 17.061 1.00 19.47

ATOM 4766 NDl HIS B 391 18.358 20.460 17.779 1.00 18.55

ATOM 4768 CEl HIS B 391 17.241 20.599 17.075 1.00 20.75

ATOM 4770 NE2 HIS B 391 17.354 19.887 15.958 1.00 12.32

ATOM 4772 CD2 HIS B 391 18.613 19.346 15.902 1.00 13.68

ATOM 4774 C HIS B 391 21.883 17.546 18.675 1.00 15.10

ATOM 4775 O HIS B 391 22.102 16.424 18.192 1.00 15.33

ATOM 4777 N VAL B 392 22.798 18.221 19.355 1.00 14.82

ATOM 4778 CA VAL B 392 24.167 17.735 19.423 1.00 13.56

ATOM 4780 CB VAL B 392 25.138 18.852 19.817 1.00 14.60

ATOM 4782 CGl VAL B 392 26.542 18.295 20.169 1.00 15.65

ATOM 4786 CG2 VAL B 392 25.208 19.883 18.678 1.00 13.78

ATOM 4790 C VAL B 392 24.197 16.525 20.356 1.00 13.43

ATOM 4791 O VAL B 392 24.887 15.598 20.077 1.00 16.72

ATOM 4793 N ALA B 393 23.418 16.523 21.421 1.00 15.76

ATOM 4794 CA ALA B 393 23.303 15.309 22.249 1.00 16.04

ATOM 4796 CB ALA B 393 22.385 15.540 23.441 1.00 17.33 ATOM 4800 C ALA B 393 22.813 14.122 21.418 1.00 16.90

ATOM 4801 O ALA B 393 23.373 13.032 21.501 1.00 16.59

ATOM 4803 N GLY B 394 21.769 14.333 20.611 1.00 17.09

ATOM 4804 CA GLY B 394 21.298 13.328 19.661 1.00 16.65

ATOM 4807 C GLY B 394 22.330 12.857 18.656 1.00 17.37

ATOM 4808 O GLY B 394 22.489 11.657 18.449 1.00 18.09

ATOM 4810 N ILE B 395 23.040 13.787 18.027 1.00 14.37

ATOM 4811 CA ILE B 395 24.110 13.472 17.079 1.00 15.08

ATOM 4813 CB ILE B 395 24.709 14.756 16.432 1.00 14.81

ATOM 4815 CGl ILE B 395 23.652 15.430 15.558 1.00 19.14

ATOM 4818 CDl ILE B 395 24.043 16.800 15.030 1.00 17.06

ATOM 4822 CG2 ILE B 395 25.998 14.412 15.645 1.00 15.01

ATOM 4826 C ILE B 395 25.233 12.688 17.755 1.00 16.58

ATOM 4827 O ILE B 395 25.734 11.691 17.188 1.00 16.92

ATOM 4829 N ALA B 396 25.579 13.071 18.992 1.00 15.94

ATOM 4830 CA ALA B 396 26.639 12.383 19.742 1.00 16.38

ATOM 4832 CB ALA B 396 26.941 13.098 21.069 1.00 15.66

ATOM 4836 C ALA B 396 26.208 10.957 20.024 1.00 17.03

ATOM 4837 O ALA B 396 27.007 10.031 19.911 1.00 18.99

ATOM 4839 N ALA B 397 24.956 10.793 20.413 1.00 17.20

ATOM 4840 CA ALA B 397 24.412 9.477 20.723 1.00 18.30

ATOM 4842 CB ALA B 397 23.007 9.603 21.260 1.00 17.28

ATOM 4846 C ALA B 397 24.470 8.588 19.490 1.00 19.82

ATOM 4847 O ALA B 397 24.840 7.417 19.571 1.00 19.53

ATOM 4849 N MET B 398 24.168 9.167 18.333 1.00 19.94

ATOM 4850 CA MET B 398 24.236 8.428 17.078 1.00 21.16

ATOM 4852 CB MET B 398 23.604 9.263 15.978 1.00 21.56

ATOM 4855 CG MET B 398 22.155 9.561 16.290 1.00 30.90

ATOM 4858 SD MET B 398 21.160 8.288 15.591 1.00 40.95

ATOM 4859 CE MET B 398 21.079 9.027 13.954 1.00 35.61

ATOM 4863 C MET B 398 25.666 8.074 16.705 1.00 20.26

ATOM 4864 O MET B 398 25.971 6.953 16.273 1.00 21.19

ATOM 4866 N MET B 399 26.560 9.032 16.859 1.00 18.36

ATOM 4867 CA MET B 399 27.927 8.807 16.526 1.00 17.82

ATOM 4869 CB MET B 399 28.719 10.106 16.629 1.00 18.09

ATOM 4872 CG MET B 399 28.489 11.089 15.483 1.00 22.35

ATOM 4875 SD MET B 399 29.393 12.585 15.847 1.00 24.05

ATOM 4876 CE MET B 399 29.188 13.522 14.298 1.00 23.79

ATOM 4880 C MET B 399 28.574 7.759 17.401 1.00 17.58

ATOM 4881 O MET B 399 29.379 6.960 16.927 1.00 16.17

ATOM 4883 N LEU B 400 28.220 7.775 18.685 1.00 17.56

ATOM 4884 CA LEU B 400 28.756 6.861 19.663 1.00 17.63

ATOM 4886 CB LEU B 400 28.538 7.393 21.067 1.00 16.67

ATOM 4889 CG LEU B 400 29.372 8.580 21.523 1.00 19.99

ATOM 4891 CDl LEU B 400 28.809 9.182 22.848 1.00 21.81

ATOM 4895 CD2 LEU B 400 30.823 8.161 21.670 1.00 23.77

ATOM 4899 C LEU B 400 28.128 5.463 19.542 1.00 20.89

ATOM 4900 O LEU B 400 28.763 4.484 19.887 1.00 20.50

ATOM 4902 N SER B 401 26.900 5.373 19.037 1.00 22.71

ATOM 4903 CA SER B 401 26.302 4.073 18.743 1.00 23.25

ATOM 4905 CB SER B 401 24.834 4.238 18.428 1.00 24.69

ATOM 4908 OG SER B 401 24.263 4.931 19.514 1.00 33.74

ATOM 4910 C SER B 401 27.038 3.410 17.603 1.00 22.74

ATOM 4911 O SER B 401 27.265 2.202 17.616 1.00 20.11

ATOM 4913 N ALA B 402 27.474 4.225 16.655 1.00 22.91

ATOM 4914 CA ALA B 402 28.191 3.746 15.481 1.00 22.65

ATOM 4916 CB ALA B 402 28.084 4.798 14.342 1.00 23.10

ATOM 4920 C ALA B 402 29.651 3.431 15.793 1.00 22.81

ATOM 4921 O ALA B 402 30.224 2.462 15.263 1.00 24.50

ATOM 4923 N GLU B 403 30.273 4.245 16.640 1.00 19.88

ATOM 4924 CA GLU B 403 31.684 4.104 16.972 1.00 19.26 ATOM 4926 CB GLU B 403 32.524 5.165 16.273 1.00 20.21

ATOM 4929 CG GLU B 403 32.473 5.118 14.732 1.00 20.78

ATOM 4932 CD GLU B 403 33.383 6.171 14.127 1.00 20.39

ATOM 4933 OEl GLU B 403 32.991 7.342 14.088 1.00 28.28

ATOM 4934 OE 2 GLU B 403 34.526 5.849 13.760 1.00 28.88

ATOM 4935 C GLU B 403 31.809 4.258 18.495 1.00 19.94

ATOM 4936 O GLU B 403 32.200 5.308 19.013 1.00 17.96

ATOM 4938 N PRO B 404 31.431 3.215 19.222 1.00 21.15

ATOM 4939 CA PRO B 404 31.332 3.321 20.679 1.00 21.45

ATOM 4941 CB PRO B 404 30.790 1.949 21.083 1.00 21.72

ATOM 4944 CG PRO B 404 30.171 1.405 19.836 1.00 20.81

ATOM 4947 CD PRO B 404 31.030 1.885 18.745 1.00 22.07

ATOM 4950 C PRO B 404 32.629 3.615 21.411 1.00 21.32

ATOM 4951 O PRO B 404 32.577 4.093 22.544 1.00 22.43

ATOM 4952 N GLU B 405 33.766 3.310 20.790 1.00 20.99

ATOM 4953 CA GLU B 405 35.057 3.486 21.421 1.00 23.43

ATOM 4955 CB GLU B 405 36.053 2.453 20.883 1.00 23.44

ATOM 4958 CG GLU B 405 35.648 0.978 21.190 1.00 26.70

ATOM 4961 CD GLU B 405 36.590 -0.085 20.577 1.00 29.51

ATOM 4962 OEl GLU B 405 37.674 0.263 20.052 1.00 36.83

ATOM 4963 OE 2 GLU B 405 36.250 -1.295 20.639 1.00 38.65

ATOM 4964 C GLU B 405 35.600 4.914 21.286 1.00 23.11

ATOM 4965 O GLU B 405 36.684 5.199 21.779 1.00 24.33

ATOM 4967 N LEU B 406 34.855 5.822 20.655 1.00 21.26

ATOM 4968 CA LEU B 406 35.350 7.194 20.481 1.00 19.96

ATOM 4970 CB LEU B 406 34.300 8.091 19.824 1.00 19.86

ATOM 4973 CG LEU B 406 33.972 7.765 18.363 1.00 18.38

ATOM 4975 CDl LEU B 406 32.810 8.630 17.880 1.00 19.26

ATOM 4979 CD2 LEU B 406 35.241 7.946 17.497 1.00 19.03

ATOM 4983 C LEU B 406 35.729 7.798 21.811 1.00 21.94

ATOM 4984 O LEU B 406 34.950 7.735 22.744 1.00 23.70

ATOM 4986 N THR B 407 36.926 8.381 21.879 1.00 22.33

ATOM 4987 CA THR B 407 37.300 9.231 22.995 1.00 22.98

ATOM 4989 CB THR B 407 38.806 9.507 23.015 1.00 21.95

ATOM 4991 OGl THR B 407 39.155 10.215 21.836 1.00 24.72

ATOM 4993 CG2 THR B 407 39.592 8.232 23.021 1.00 25.15

ATOM 4997 C THR B 407 36.550 10.544 22.820 1.00 23.16

ATOM 4998 O THR B 407 36.091 10.869 21.715 1.00 22.81

ATOM 5000 N LEU B 408 36.426 11.329 23.891 1.00 22.98

ATOM 5001 CA LEU B 408 35.828 12.674 23.764 1.00 22.14

ATOM 5003 CB LEU B 408 35.898 13.413 25.097 1.00 23.40

ATOM 5006 CG LEU B 408 35.345 14.829 25.074 1.00 26.29

ATOM 5008 CDl LEU B 408 33.834 14.849 24.687 1.00 27.51

ATOM 5012 CD2 LEU B 408 35.582 15.456 26.448 1.00 25.01

ATOM 5016 C LEU B 408 36.501 13.492 22.650 1.00 21.18

ATOM 5017 O LEU B 408 35.844 14.249 21.900 1.00 21.18

ATOM 5019 N ALA B 409 37.820 13.369 22.525 1.00 20.73

ATOM 5020 CA ALA B 409 38.547 14.187 21.559 1.00 18.66

ATOM 5022 CB ALA B 409 40.077 14.194 21.872 1.00 18.87

ATOM 5026 C ALA B 409 38.225 13.722 20.118 1.00 19.53

ATOM 5027 O ALA B 409 38.077 14.527 19.201 1.00 17.15

ATOM 5029 N GLU B 410 38.059 12.413 19.948 1.00 19.49

ATOM 5030 CA GLU B 410 37.671 11.858 18.659 1.00 19.55

ATOM 5032 CB GLU B 410 37.839 10.348 18.661 1.00 17.70

ATOM 5035 CG GLU B 410 39.286 9.972 18.670 1.00 21.08

ATOM 5038 CD GLU B 410 39.499 8.489 18.896 1.00 25.91

ATOM 5039 OEl GLU B 410 38.575 7.783 19.383 1.00 25.66

ATOM 5040 OE 2 GLU B 410 40.622 8.049 18.613 1.00 28.32

ATOM 5041 C GLU B 410 36.244 12.254 18.313 1.00 19.00

ATOM 5042 O GLU B 410 35.937 12.523 17.169 1.00 20.23

ATOM 5044 N LEU B 411 35.387 12.298 19.314 1.00 19.16 ATOM 5045 CA LEU I3 411 34.012 12.660 19.086 1.00 20.33

ATOM 5047 CB LEU I 3 411 33.174 12.344 20.295 1.00 20.65

ATOM 5050 CG LEU I 3 411 31.710 12.770 20.289 1.00 25.11

ATOM 5052 CDl LEU I 3 411 30.948 12.012 19.233 1.00 23.49

ATOM 5056 CD2 LEU I 3 411 31.154 12.502 21.709 1.00 21.48

ATOM 5060 C LEU I 3 411 33.922 14.131 18.757 1.00 18.64

ATOM 5061 O LEU I 3 411 33.169 14.532 17.887 1.00 18.44

ATOM 5063 N ARG I 3 412 34.676 14.951 19.470 1.00 18.38

ATOM 5064 CA ARG I 3 412 34.661 16.375 19.208 1.00 18.05

ATOM 5066 CB ARG I 3 412 35.496 17.094 20.243 1.00 20.37

ATOM 5069 CG ARG I 3 412 35.413 18.572 20.119 1.00 22.89

ATOM 5072 CD ARG I 3 412 36.406 19.233 21.007 1.00 21.06

ATOM 5075 NE ARG I 3 412 36.133 19.013 22.421 1.00 25.29

ATOM 5077 CZ ARG I 3 412 36.879 18.286 23.250 1.00 32.02

ATOM 5078 NHl ARG I 3 412 37.959 17.639 22.827 1.00 26.77

ATOM 5081 NH2 ARG I 3 412 36.528 18.198 24.534 1.00 32.64

ATOM 5084 C ARG I 3 412 35.190 16.682 17.810 1.00 17.91

ATOM 5085 O ARG I 3 412 34.641 17.499 17.116 1.00 16.45

ATOM 5087 N GLN I 3 413 36.244 15.993 17.390 1.00 18.24

ATOM 5088 CA GLN I 3 413 36.838 16.223 16.068 1.00 19.52

ATOM 5090 CB GLN I 3 413 38.151 15.450 15.957 1.00 19.60

ATOM 5093 CG GLN I 3 413 39.290 16.029 16.846 1.00 18.75

ATOM 5096 CD GLN I 3 413 40.262 16.854 16.105 1.00 19.68

ATOM 5097 OEl GLN I 3 413 40.016 17.227 14.950 1.00 17.78

ATOM 5098 NE 2 GLN I 3 413 41.433 17.112 16.722 1.00 14.93

ATOM 5101 C GLN I 3 413 35.874 15.821 14.952 1.00 18.60

ATOM 5102 O GLN I 3 413 35.856 16.436 13.911 1.00 19.35

ATOM 5104 N ARG I 3 414 35.110 14.759 15.179 1.00 20.27

ATOM 5105 CA ARG I 3 414 34.069 14.331 14.256 1.00 19.30

ATOM 5107 CB ARG I 3 414 33.553 12.943 14.631 1.00 20.52

ATOM 5110 CG ARG I 3 414 34.475 11.847 14.141 1.00 20.47

ATOM 5113 CD ARG I 3 414 34.312 10.611 14.939 1.00 23.85

ATOM 5116 NE ARG I 3 414 35.100 9.539 14.370 1.00 25.56

ATOM 5118 CZ ARG I 3 414 36.415 9.405 14.509 1.00 34.87

ATOM 5119 NHl ARG I 3 414 37.013 8.366 13.929 1.00 37.93

ATOM 5122 NH2 ARG I 3 414 37.141 10.312 15.169 1.00 31.43

ATOM 5125 C ARG I 3 414 32.917 15.324 14.191 1.00 19.42

ATOM 5126 O ARG I 3 414 32.471 15.683 13.101 1.00 20.13

ATOM 5128 N LEU I 3 415 32.476 15.816 15.348 1.00 17.85

ATOM 5129 CA LEU I 3 415 31.419 16.812 15.370 1.00 18.01

ATOM 5131 CB LEU I 3 415 31.099 17.237 16.792 1.00 17.70

ATOM 5134 CG LEU I 3 415 30.328 16.196 17.567 1.00 20.17

ATOM 5136 CDl LEU I 3 415 30.373 16.532 19.063 1.00 13.80

ATOM 5140 CD2 LEU I 3 415 28.895 16.141 17.048 1.00 20.92

ATOM 5144 C LEU I 3 415 31.820 18.030 14.567 1.00 17.48

ATOM 5145 O LEU I 3 415 31.011 18.572 13.825 1.00 19.60

ATOM 5147 N ILE I 3 416 33.082 18.441 14.686 1.00 17.22

ATOM 5148 CA ILE I 3 416 33.598 19.602 13.949 1.00 16.72

ATOM 5150 CB ILE I 3 416 35.006 20.038 14.479 1.00 15.52

ATOM 5152 CGl ILE I 3 416 34.905 20.622 15.919 1.00 18.10

ATOM 5155 CDl ILE I 3 416 36.251 20.762 16.652 1.00 16.74

ATOM 5159 CG2 ILE I 3 416 35.673 20.974 13.523 1.00 17.75

ATOM 5163 C ILE I 3 416 33.701 19.209 12.471 1.00 16.76

ATOM 5164 O ILE I 3 416 33.305 19.952 11.582 1.00 17.60

ATOM 5166 N HIS I 3 417 34.257 18.036 12.202 1.00 18.02

ATOM 5167 CA HIS I 3 417 34.553 17.661 10.822 1.00 19.54

ATOM 5169 CB HIS I 3 417 35.375 16.375 10.769 1.00 21.39

ATOM 5172 CG HIS I 3 417 35.599 15.877 9.372 1.00 24.45

ATOM 5173 NDl HIS I 3 417 36.456 16.490 8.491 1.00 27.35

ATOM 5175 CEl HIS I 3 417 36.406 15.868 7.323 1.00 27.02

ATOM 5177 NE 2 HIS I 3 417 35.552 14.868 7.421 1.00 26.01 ATOM 5179 CD2 HIS B 417 35.024 14.861 8.689 1.00 32.90

ATOM 5181 C HIS B 417 33.281 17.519 9.966 1.00 21.48

ATOM 5182 O HIS B 417 33.238 17.946 8.801 1.00 21.65

ATOM 5184 N PHE B 418 32.257 16.901 10.539 1.00 20.21

ATOM 5185 CA PHE B 418 30.993 16.703 9.841 1.00 21.05

ATOM 5187 CB PHE B 418 30.348 15.419 10.347 1.00 21.62

ATOM 5190 CG PHE B 418 31.174 14.207 10.024 1.00 20.30

ATOM 5191 CDl PHE B 418 31.516 13.939 8.700 1.00 26.27

ATOM 5193 CEl PHE B 418 32.298 12.816 8.367 1.00 27.18

ATOM 5195 CZ PHE B 418 32.774 11.993 9.358 1.00 26.46

ATOM 5197 CE 2 PHE B 418 32.455 12.255 10.696 1.00 23.13

ATOM 5199 CD2 PHE B 418 31.656 13.379 11.017 1.00 27.68

ATOM 5201 C PHE B 418 30.035 17.891 9.884 1.00 20.70

ATOM 5202 O PHE B 418 28.951 17.826 9.325 1.00 19.08

ATOM 5204 N SER B 419 30.449 18.995 10.505 1.00 19.87

ATOM 5205 CA SER B 419 29.609 20.181 10.538 1.00 18.07

ATOM 5207 CB SER B 419 30.091 21.178 11.605 1.00 18.62

ATOM 5210 OG SER B 419 29.657 20.773 12.901 1.00 21.88

ATOM 5212 C SER B 419 29.619 20.875 9.197 1.00 18.20

ATOM 5213 O SER B 419 30.591 20.779 8.459 1.00 20.29

ATOM 5215 N ALA B 420 28.555 21.600 8.921 1.00 18.61

ATOM 5216 CA ALA B 420 28.493 22.589 7.819 1.00 20.19

ATOM 5218 CB ALA B 420 27.026 23.058 7.587 1.00 18.00

ATOM 5222 C ALA B 420 29.380 23.759 8.202 1.00 20.27

ATOM 5223 O ALA B 420 29.325 24.237 9.324 1.00 20.68

ATOM 5225 N LYS B 421 30.230 24.193 7.286 1.00 22.05

ATOM 5226 CA LYS B 421 31.229 25.192 7.625 1.00 24.20

ATOM 5228 CB LYS B 421 32.607 24.653 7.295 1.00 24.63

ATOM 5231 CG LYS B 421 32.830 23.338 7.976 1.00 25.94

ATOM 5234 CD LYS B 421 34.224 23.029 8.252 1.00 29.05

ATOM 5237 CE LYS B 421 34.323 21.684 8.925 1.00 27.68

ATOM 5240 NZ LYS B 421 33.578 20.616 8.194 1.00 25.36

ATOM 5244 C LYS B 421 30.979 26.499 6.902 1.00 24.85

ATOM 5245 O LYS B 421 30.508 26.503 5.773 1.00 24.49

ATOM 5247 N ASP B 422 31.282 27.596 7.590 1.00 25.50

ATOM 5248 CA ASP B 422 31.273 28.923 7.016 1.00 27.96

ATOM 5250 CB ASP B 422 32.358 29.052 5.943 1.00 29.36

ATOM 5253 CG ASP B 422 32.621 30.493 5.576 1.00 37.07

ATOM 5254 ODl ASP B 422 32.945 31.292 6.476 1.00 49.92

ATOM 5255 OD2 ASP B 422 32.465 30.844 4.392 1.00 50.69

ATOM 5256 C ASP B 422 29.933 29.357 6.452 1.00 26.74

ATOM 5257 O ASP B 422 29.871 30.057 5.458 1.00 28.60

ATOM 5259 N VAL B 423 28.874 28.974 7.129 1.00 25.48

ATOM 5260 CA VAL B 423 27.502 29.272 6.735 1.00 25.60

ATOM 5262 CB VAL B 423 26.693 27.977 6.820 1.00 26.37

ATOM 5264 CGl VAL B 423 25.257 28.273 6.827 1.00 33.66

ATOM 5268 CG2 VAL B 423 27.054 27.045 5.649 1.00 23.17

ATOM 5272 C VAL B 423 26.855 30.352 7.637 1.00 24.30

ATOM 5273 O VAL B 423 25.814 30.907 7.320 1.00 21.02

ATOM 5275 N ILE B 424 27.445 30.627 8.792 1.00 24.25

ATOM 5276 CA ILE B 424 26.935 31.702 9.656 1.00 24.58

ATOM 5278 CB ILE B 424 27.281 31.411 11.152 1.00 24.07

ATOM 5280 CGl ILE B 424 26.890 30.003 11.579 1.00 23.80

ATOM 5283 CDl ILE B 424 27.370 29.666 12.966 1.00 24.74

ATOM 5287 CG2 ILE B 424 26.599 32.361 12.073 1.00 25.09

ATOM 5291 C ILE B 424 27.518 33.055 9.189 1.00 24.16

ATOM 5292 O ILE B 424 28.724 33.156 8.967 1.00 25.06

ATOM 5294 N ASN B 425 26.695 34.101 9.051 1.00 25.37

ATOM 5295 CA ASN B 425 27.223 35.463 8.809 1.00 27.02

ATOM 5297 CB ASN B 425 26.152 36.457 8.279 1.00 27.87

ATOM 5300 CG ASN B 425 26.725 37.861 7.959 1.00 27.90 ATOM 5301 ODl ASN B 425 27.872 38.188 8.277 1.00 28.69

ATOM 5302 ND2 ASN B 425 25.917 38.681 7.300 1.00 35.36

ATOM 5305 C ASN B 425 27.742 35.968 10.140 1.00 27.90

ATOM 5306 O ASN B 425 26.975 36.171 11.077 1.00 28.17

ATOM 5308 N GLU B 426 29.038 36.156 10.249 1.00 27.87

ATOM 5309 CA GLU B 426 29.573 36.419 11.579 1.00 29.02

ATOM 5311 CB GLU B 426 31.033 36.061 11.614 1.00 29.30

ATOM 5314 CG GLU B 426 31.297 34.591 11.335 1.00 36.37

ATOM 5317 CD GLU B 426 32.785 34.278 11.381 1.00 40.51

ATOM 5318 OEl GLU B 426 33.586 35.242 11.285 1.00 41.44

ATOM 5319 OE 2 GLU B 426 33.137 33.078 11.508 1.00 40.28

ATOM 5320 C GLU B 426 29.378 37.880 12.019 1.00 28.19

ATOM 5321 O GLU B 426 29.676 38.201 13.161 1.00 27.95

ATOM 5323 N ALA B 427 28.861 38.729 11.118 1.00 27.10

ATOM 5324 CA ALA B 427 28.445 40.133 11.428 1.00 25.54

ATOM 5326 CB ALA B 427 27.791 40.792 10.211 1.00 25.46

ATOM 5330 C ALA B 427 27.479 40.236 12.594 1.00 23.97

ATOM 5331 O ALA B 427 27.412 41.254 13.256 1.00 18.90

ATOM 5333 N TRP B 428 26.720 39.186 12.841 1.00 22.45

ATOM 5334 CA TRP B 428 25.790 39.165 13.936 1.00 23.21

ATOM 5336 CB TRP B 428 25.025 37.849 13.826 1.00 24.45

ATOM 5339 CG TRP B 428 23.862 37.719 14.646 1.00 25.56

ATOM 5340 CDl TRP B 428 22.580 37.984 14.276 1.00 26.18

ATOM 5342 NEl TRP B 428 21.728 37.714 15.317 1.00 30.38

ATOM 5344 CE 2 TRP B 428 22.455 37.236 16.379 1.00 29.35

ATOM 5345 CD2 TRP B 428 23.806 37.217 15.985 1.00 24.74

ATOM 5346 CE 3 TRP B 428 24.763 36.767 16.899 1.00 24.25

ATOM 5348 CZ3 TRP B 428 24.347 36.348 18.155 1.00 23.67

ATOM 5350 CH2 TRP B 428 23.019 36.366 18.520 1.00 24.03

ATOM 5352 CZ2 TRP B 428 22.041 36.809 17.651 1.00 22.98

ATOM 5354 C TRP B 428 26.509 39.244 15.306 1.00 22.41

ATOM 5355 O TRP B 428 25.946 39.738 16.303 1.00 21.48

ATOM 5357 N PHE B 429 27.739 38.713 15.347 1.00 22.04

ATOM 5358 CA PHE B 429 28.541 38.639 16.567 1.00 20.51

ATOM 5360 CB PHE B 429 29.556 37.504 16.469 1.00 19.43

ATOM 5363 CG PHE B 429 28.964 36.153 16.248 1.00 20.54

ATOM 5364 CDl PHE B 429 28.004 35.647 17.098 1.00 19.79

ATOM 5366 CEl PHE B 429 27.487 34.386 16.890 1.00 19.69

ATOM 5368 CZ PHE B 429 27.952 33.622 15.882 1.00 17.38

ATOM 5370 CE 2 PHE B 429 28.949 34.085 15.068 1.00 18.44

ATOM 5372 CD2 PHE B 429 29.466 35.326 15.256 1.00 20.19

ATOM 5374 C PHE B 429 29.329 39.923 16.761 1.00 19.63

ATOM 5375 O PHE B 429 29.756 40.519 15.785 1.00 20.55

ATOM 5377 N PRO B 430 29.609 40.303 18.022 1.00 17.75

ATOM 5378 CA PRO B 430 30.504 41.415 18.255 1.00 17.83

ATOM 5380 CB PRO B 430 30.660 41.436 19.791 1.00 17.73

ATOM 5383 CG PRO B 430 29.479 40.689 20.282 1.00 16.15

ATOM 5386 CD PRO B 430 29.125 39.706 19.283 1.00 17.57

ATOM 5389 C PRO B 430 31.821 41.201 17.529 1.00 18.11

ATOM 5390 O PRO B 430 32.265 40.075 17.321 1.00 17.50

ATOM 5391 N GLU B 431 32.443 42.291 17.128 1.00 19.54

ATOM 5392 CA GLU B 431 33.588 42.221 16.249 1.00 20.79

ATOM 5394 CB GLU B 431 34.130 43.635 15.974 1.00 22.92

ATOM 5397 CG GLU B 431 33.131 44.436 15.175 1.00 25.25

ATOM 5400 CD GLU B 431 33.640 45.776 14.718 1.00 37.87

ATOM 5401 OEl GLU B 431 34.817 46.077 15.001 1.00 42.75

ATOM 5402 OE 2 GLU B 431 32.850 46.504 14.058 1.00 39.85

ATOM 5403 C GLU B 431 34.692 41.341 16.782 1.00 19.90

ATOM 5404 O GLU B 431 35.260 40.569 16.046 1.00 22.94

ATOM 5406 N ASP B 432 35.006 41.449 18.060 1.00 20.59

ATOM 5407 CA ASP B 432 36.139 40.705 18.595 1.00 22.28 ATOM 5409 CB ASP B 432 36.596 41.276 19.923 1.00 25.67

ATOM 5412 CG ASP B 432 37.254 42.635 19.766 1.00 29.40

ATOM 5413 ODl ASP B 432 37.892 42.870 18.714 1.00 37.79

ATOM 5414 OD2 ASP B 432 37.100 43.473 20.670 1.00 44.16

ATOM 5415 C ASP B 432 35.825 39.230 18.749 1.00 22.18

ATOM 5416 O ASP B 432 36.744 38.455 18.925 1.00 22.06

ATOM 5418 N GLN B 433 34.543 38.848 18.670 1.00 20.34

ATOM 5419 CA GLN B 433 34.137 37.445 18.882 1.00 20.51

ATOM 5421 CB GLN B 433 32.822 37.415 19.651 1.00 19.77

ATOM 5424 CG GLN B 433 32.980 38.113 20.997 1.00 18.80

ATOM 5427 CD GLN B 433 33.576 37.226 22.040 1.00 25.39

ATOM 5428 OEl GLN B 433 33.841 36.046 21.800 1.00 24.31

ATOM 5429 NE 2 GLN B 433 33.756 37.765 23.228 1.00 26.34

ATOM 5432 C GLN B 433 34.060 36.668 17.605 1.00 21.52

ATOM 5433 O GLN B 433 33.986 35.427 17.608 1.00 23.07

ATOM 5435 N ARG B 434 34.111 37.374 16.491 1.00 21.36

ATOM 5436 CA ARG B 434 33.991 36.726 15.202 1.00 21.56

ATOM 5438 CB ARG B 434 33.948 37.771 14.110 1.00 23.76

ATOM 5441 CG ARG B 434 32.640 38.520 14.124 1.00 21.89

ATOM 5444 CD ARG B 434 32.703 39.739 13.246 1.00 23.75

ATOM 5447 NE ARG B 434 31.572 40.585 13.536 1.00 24.28

ATOM 5449 CZ ARG B 434 31.391 41.815 13.073 1.00 24.02

ATOM 5450 NHl ARG B 434 32.263 42.369 12.249 1.00 19.40

ATOM 5453 NH2 ARG B 434 30.319 42.482 13.442 1.00 24.74

ATOM 5456 C ARG B 434 35.099 35.705 14.992 1.00 22.23

ATOM 5457 O ARG B 434 34.802 34.557 14.758 1.00 27.93

ATOM 5459 N VAL B 435 36.354 36.097 15.164 1.00 23.17

ATOM 5460 CA VAL B 435 37.485 35.184 15.069 1.00 24.69

ATOM 5462 CB VAL B 435 38.809 35.920 15.265 1.00 24.45

ATOM 5464 CGl VAL B 435 39.950 34.957 15.071 1.00 31.54

ATOM 5468 CG2 VAL B 435 38.960 37.026 14.254 1.00 30.05

ATOM 5472 C VAL B 435 37.458 34.039 16.099 1.00 22.20

ATOM 5473 O VAL B 435 37.937 32.957 15.854 1.00 24.96

ATOM 5475 N LEU B 436 36.894 34.285 17.259 1.00 20.03

ATOM 5476 CA LEU B 436 36.875 33.278 18.302 1.00 18.27

ATOM 5478 CB LEU B 436 36.736 34.006 19.630 1.00 17.83

ATOM 5481 CG LEU B 436 37.863 34.930 20.059 1.00 20.03

ATOM 5483 CDl LEU B 436 37.574 35.599 21.406 1.00 21.95

ATOM 5487 CD2 LEU B 436 39.135 34.149 20.096 1.00 19.97

ATOM 5491 C LEU B 436 35.735 32.264 18.152 1.00 17.69

ATOM 5492 O LEU B 436 35.753 31.171 18.767 1.00 16.08

ATOM 5494 N THR B 437 34.719 32.626 17.372 1.00 15.63

ATOM 5495 CA THR B 437 33.478 31.848 17.326 1.00 15.53

ATOM 5497 CB THR B 437 32.267 32.819 17.217 1.00 15.93

ATOM 5499 OGl THR B 437 32.206 33.599 18.422 1.00 14.43

ATOM 5501 CG2 THR B 437 30.973 32.078 17.051 1.00 16.43

ATOM 5505 C THR B 437 33.510 30.826 16.173 1.00 17.10

ATOM 5506 O THR B 437 33.675 31.196 15.022 1.00 16.80

ATOM 5508 N PRO B 438 33.308 29.538 16.459 1.00 16.81

ATOM 5509 CA PRO B 438 33.413 28.575 15.360 1.00 18.63

ATOM 5511 CB PRO B 438 33.281 27.210 16.043 1.00 18.19

ATOM 5514 CG PRO B 438 33.441 27.506 17.530 1.00 22.80

ATOM 5517 CD PRO B 438 32.938 28.882 17.731 1.00 21.20

ATOM 5520 C PRO B 438 32.265 28.735 14.384 1.00 18.13

ATOM 5521 O PRO B 438 31.121 28.786 14.795 1.00 17.59

ATOM 5522 N ASN B 439 32.562 28.746 13.101 1.00 17.67

ATOM 5523 CA ASN B 439 31.512 28.905 12.122 1.00 17.03

ATOM 5525 CB ASN B 439 31.987 29.806 11.002 1.00 18.38

ATOM 5528 CG ASN B 439 30.856 30.351 10.223 1.00 17.01

ATOM 5529 ODl ASN B 439 29.926 29.630 9.920 1.00 17.34

ATOM 5530 ND2 ASN B 439 30.925 31.619 9.870 1.00 14.88 ATOM 5533 C ASN B 439 31.192 27.514 11.631 1.00 18.73

ATOM 5534 O ASN B 439 31.685 27.071 10.570 1.00 19.33

ATOM 5536 N LEU B 440 30.395 26.832 12.452 1.00 16.42

ATOM 5537 CA LEU B 440 30.039 25.439 12.301 1.00 17.33

ATOM 5539 CB LEU B 440 30.886 24.603 13.238 1.00 17.87

ATOM 5542 CG LEU B 440 32.403 24.604 13.137 1.00 16.86

ATOM 5544 CDl LEU B 440 32.921 23.845 14.367 1.00 11.36

ATOM 5548 CD2 LEU B 440 32.842 23.960 11.832 1.00 14.50

ATOM 5552 C LEU B 440 28.599 25.207 12.713 1.00 17.94

ATOM 5553 O LEU B 440 28.171 25.672 13.791 1.00 18.19

ATOM 5555 N VAL B 441 27.872 24.458 11.877 1.00 16.37

ATOM 5556 CA VAL B 441 26.524 24.037 12.186 1.00 15.34

ATOM 5558 CB VAL B 441 25.456 24.632 11.279 1.00 16.07

ATOM 5560 CGl VAL B 441 24.085 24.094 11.693 1.00 15.74

ATOM 5564 CG2 VAL B 441 25.513 26.176 11.362 1.00 16.03

ATOM 5568 C VAL B 441 26.531 22.521 12.106 1.00 15.02

ATOM 5569 O VAL B 441 26.864 21.948 11.070 1.00 15.18

ATOM 5571 N ALA B 442 26.185 21.910 13.224 1.00 13.20

ATOM 5572 CA ALA B 442 26.249 20.453 13.421 1.00 13.11

ATOM 5574 CB ALA B 442 25.690 20.123 14.768 1.00 12.39

ATOM 5578 C ALA B 442 25.481 19.663 12.359 1.00 14.10

ATOM 5579 O ALA B 442 24.418 20.097 11.881 1.00 13.84

ATOM 5581 N ALA B 443 25.999 18.479 12.034 1.00 15.56

ATOM 5582 CA ALA B 443 25.316 17.539 11.180 1.00 15.60

ATOM 5584 CB ALA B 443 25.666 17.802 9.705 1.00 14.23

ATOM 5588 C ALA B 443 25.751 16.147 11.557 1.00 18.10

ATOM 5589 O ALA B 443 26.875 15.931 12.040 1.00 18.04

ATOM 5591 N LEU B 444 24.872 15.205 11.271 1.00 19.96

ATOM 5592 CA LEU B 444 25.170 13.789 11.344 1.00 20.83

ATOM 5594 CB LEU B 444 23.884 12.990 11.094 1.00 21.19

ATOM 5597 CG LEU B 444 22.962 13.000 12.308 1.00 23.52

ATOM 5599 CDl LEU B 444 21.539 12.667 11.871 1.00 26.99

ATOM 5603 CD2 LEU B 444 23.493 12.021 13.392 1.00 24.13

ATOM 5607 C LEU B 444 26.225 13.383 10.341 1.00 21.33

ATOM 5608 O LEU B 444 26.305 13.968 9.269 1.00 20.52

ATOM 5610 N PRO B 445 27.046 12.369 10.682 1.00 23.81

ATOM 5611 CA PRO B 445 28.051 11.907 9.740 1.00 26.47

ATOM 5613 CB PRO B 445 28.860 10.894 10.547 1.00 25.83

ATOM 5616 CG PRO B 445 27.987 10.442 11.626 1.00 29.47

ATOM 5619 CD PRO B 445 27.055 11.596 11.941 1.00 26.43

ATOM 5622 C PRO B 445 27.371 11.276 8.495 1.00 27.81

ATOM 5623 O PRO B 445 26.295 10.695 8.621 1.00 26.22

ATOM 5624 N PRO B 446 27.957 11.443 7.310 1.00 31.59

ATOM 5625 CA PRO B 446 27.349 10.741 6.191 1.00 35.46

ATOM 5627 CB PRO B 446 28.080 11.289 4.969 1.00 34.34

ATOM 5630 CG PRO B 446 29.357 11.831 5.478 1.00 35.76

ATOM 5633 CD PRO B 446 29.115 12.246 6.903 1.00 31.55

ATOM 5636 C PRO B 446 27.569 9.248 6.310 1.00 39.92

ATOM 5637 O PRO B 446 28.446 8.818 7.035 1.00 38.47

ATOM 5638 N SER B 447 26.742 8.480 5.613 1.00 45.17

ATOM 5639 CA SER B 447 26.961 7.043 5.438 1.00 50.02

ATOM 5641 CB SER B 447 25.769 6.441 4.701 1.00 50.25

ATOM 5644 OG SER B 447 24.588 6.729 5.424 1.00 53.91

ATOM 5646 C SER B 447 28.252 6.736 4.657 1.00 53.09

ATOM 5647 O SER B 447 28.808 5.642 4.797 1.00 54.37

ATOM 5649 N THR B 448 28.712 7.686 3.836 1.00 56.17

ATOM 5650 CA THR B 448 29.993 7.546 3.112 1.00 59.16

ATOM 5652 CB THR B 448 30.233 8.714 2.064 1.00 59.41

ATOM 5654 OGl THR B 448 31.542 8.596 1.477 1.00 63.42

ATOM 5656 CG2 THR B 448 30.090 10.098 2.684 1.00 59.27

ATOM 5660 C THR B 448 31.212 7.341 4.049 1.00 60.86 ATOM 5661 O THR I3 448 32.229 6.792 3.618 1.00 61.85

ATOM 5663 N HIS I 3 449 31.104 7.780 5.310 1.00 62.66

ATOM 5664 CA HIS I 3 449 32.053 7.400 6.391 1.00 63.74

ATOM 5666 CB HIS I 3 449 33.488 7.930 6.148 1.00 64.54

ATOM 5669 CG HIS I 3 449 33.572 9.396 5.834 1.00 66.99

ATOM 5670 NDl HIS I 3 449 34.249 10.290 6.639 1.00 70.88

ATOM 5672 CEl HIS I 3 449 34.185 11.499 6.107 1.00 71.47

ATOM 5674 NE 2 HIS I 3 449 33.481 11.426 4.989 1.00 73.06

ATOM 5676 CD2 HIS I 3 449 33.098 10.119 4.788 1.00 70.30

ATOM 5678 C HIS I 3 449 31.563 7.814 7.786 1.00 63.31

ATOM 5679 O HIS I 3 449 31.151 8.953 8.004 1.00 62.24

ATOM 5681 N GLY I 3 452 38.470 4.250 5.594 1.00 54.33

ATOM 5682 CA GLY I 3 452 39.783 4.232 6.242 1.00 54.43

ATOM 5685 C GLY I 3 452 40.135 5.539 6.942 1.00 54.16

ATOM 5686 O GLY I 3 452 39.299 6.449 7.065 1.00 54.83

ATOM 5688 N TRP I 3 453 41.393 5.630 7.376 1.00 53.20

ATOM 5689 CA TRP I 3 453 41.861 6.703 8.251 1.00 51.78

ATOM 5691 CB TRP I 3 453 43.176 6.290 8.898 1.00 52.90

ATOM 5694 CG TRP I 3 453 43.639 7.247 9.923 1.00 54.73

ATOM 5695 CDl TRP I 3 453 43.299 7.275 11.248 1.00 56.66

ATOM 5697 NEl TRP I 3 453 43.935 8.332 11.872 1.00 57.33

ATOM 5699 CE 2 TRP I 3 453 44.688 9.004 10.943 1.00 56.83

ATOM 5700 CD2 TRP I 3 453 44.526 8.345 9.710 1.00 55.94

ATOM 5701 CE 3 TRP I 3 453 45.192 8.840 8.591 1.00 56.98

ATOM 5703 CZ3 TRP I 3 453 46.002 9.958 8.735 1.00 56.56

ATOM 5705 CH2 TRP I 3 453 46.147 10.584 9.973 1.00 55.17

ATOM 5707 CZ2 TRP I 3 453 45.503 10.126 11.085 1.00 55.44

ATOM 5709 C TRP I 3 453 42.013 8.084 7.586 1.00 49.31

ATOM 5710 O TRP I 3 453 42.405 8.209 6.419 1.00 49.39

ATOM 5712 N GLN I 3 454 41.704 9.118 8.369 1.00 45.54

ATOM 5713 CA GLN I 3 454 41.714 10.500 7.907 1.00 42.04

ATOM 5715 CB GLN I 3 454 40.300 10.960 7.645 1.00 42.45

ATOM 5718 CG GLN I 3 454 40.180 12.453 7.366 1.00 47.91

ATOM 5721 CD GLN I 3 454 38.979 12.777 6.503 1.00 54.71

ATOM 5722 OEl GLN I 3 454 37.970 12.058 6.521 1.00 59.00

ATOM 5723 NE 2 GLN I 3 454 39.086 13.849 5.723 1.00 56.79

ATOM 5726 C GLN I 3 454 42.339 11.388 8.974 1.00 37.12

ATOM 5727 O GLN I 3 454 42.232 11.096 10.148 1.00 35.93

ATOM 5729 N LEU I 3 455 42.998 12.456 8.548 1.00 32.29

ATOM 5730 CA LEU I 3 455 43.631 13.377 9.476 1.00 27.76

ATOM 5732 CB LEU I 3 455 44.874 14.021 8.829 1.00 26.61

ATOM 5735 CG LEU I 3 455 45.654 15.021 9.688 1.00 25.09

ATOM 5737 CDl LEU I 3 455 45.945 14.501 11.076 1.00 18.58

ATOM 5741 CD2 LEU I 3 455 46.950 15.412 8.944 1.00 25.24

ATOM 5745 C LEU I 3 455 42.668 14.458 9.932 1.00 24.91

ATOM 5746 O LEU I 3 455 42.324 15.329 9.166 1.00 26.00

ATOM 5748 N PHE I 3 456 42.301 14.424 11.212 1.00 23.85

ATOM 5749 CA PHE I 3 456 41.373 15.397 11.810 1.00 23.28

ATOM 5751 CB PHE I 3 456 40.430 14.726 12.787 1.00 24.01

ATOM 5754 CG PHE I 3 456 39.425 13.777 12.164 1.00 30.49

ATOM 5755 CDl PHE I 3 456 38.360 14.256 11.436 1.00 33.65

ATOM 5757 CEl PHE I 3 456 37.416 13.376 10.884 1.00 35.64

ATOM 5759 CZ PHE I 3 456 37.531 12.041 11.083 1.00 31.35

ATOM 5761 CE 2 PHE I 3 456 38.592 11.545 11.823 1.00 35.31

ATOM 5763 CD2 PHE I 3 456 39.521 12.413 12.373 1.00 32.73

ATOM 5765 C PHE I 3 456 42.181 16.360 12.638 1.00 19.90

ATOM 5766 O PHE I 3 456 42.939 15.901 13.463 1.00 17.74

ATOM 5768 N CYS I 3 457 41.983 17.662 12.439 1.00 19.60

ATOM 5769 CA CYS I 3 457 42.640 18.711 13.239 1.00 19.21

ATOM 5771 CB CYS I 3 457 43.717 19.464 12.446 1.00 21.90

ATOM 5774 SG CYS I 3 457 45.167 18.513 12.015 1.00 23.75 ATOM 5776 C CYS B 457 41.601 19.705 13.634 1.00 19.41

ATOM 5777 O CYS B 457 40.632 19.895 12.898 1.00 20.56

ATOM 5779 N ARG B 458 41.849 20.378 14.765 1.00 17.46

ATOM 5780 CA ARG B 458 40.979 21.426 15.268 1.00 18.09

ATOM 5782 CB ARG B 458 40.017 20.873 16.336 1.00 18.61

ATOM 5785 CG ARG B 458 40.736 20.456 17.613 1.00 19.59

ATOM 5788 CD ARG B 458 39.815 19.883 18.624 1.00 18.45

ATOM 5791 NE ARG B 458 40.487 19.452 19.834 1.00 23.15

ATOM 5793 CZ ARG B 458 40.334 20.012 21.021 1.00 23.13

ATOM 5794 NHl ARG B 458 39.552 21.078 21.193 1.00 18.12

ATOM 5797 NH2 ARG B 458 40.997 19.519 22.053 1.00 23.15

ATOM 5800 C ARG B 458 41.836 22.542 15.849 1.00 17.25

ATOM 5801 O ARG B 458 42.990 22.316 16.284 1.00 17.75

ATOM 5803 N THR B 459 41.273 23.745 15.823 1.00 17.33

ATOM 5804 CA THR B 459 41.940 24.945 16.279 1.00 17.08

ATOM 5806 CB THR B 459 41.666 26.101 15.346 1.00 17.33

ATOM 5808 OGl THR B 459 42.111 25.766 14.013 1.00 19.60

ATOM 5810 CG2 THR B 459 42.393 27.333 15.810 1.00 16.16

ATOM 5814 C THR B 459 41.416 25.240 17.703 1.00 18.31

ATOM 5815 O THR B 459 40.190 25.286 17.946 1.00 14.09

ATOM 5817 N VAL B 460 42.339 25.379 18.637 1.00 17.24

ATOM 5818 CA VAL B 460 42.000 25.546 20.058 1.00 16.52

ATOM 5820 CB VAL B 460 42.638 24.515 20.913 1.00 15.91

ATOM 5822 CGl VAL B 460 42.324 24.808 22.373 1.00 19.06

ATOM 5826 CG2 VAL B 460 42.166 23.098 20.558 1.00 14.87

ATOM 5830 C VAL B 460 42.556 26.919 20.432 1.00 16.91

ATOM 5831 O VAL B 460 43.788 27.138 20.396 1.00 19.51

ATOM 5833 N TRP B 461 41.673 27.867 20.668 1.00 15.86

ATOM 5834 CA TRP B 461 42.093 29.188 21.128 1.00 16.38

ATOM 5836 CB TRP B 461 41.071 30.236 20.735 1.00 17.45

ATOM 5839 CG TRP B 461 41.123 30.615 19.353 1.00 18.75

ATOM 5840 CDl TRP B 461 40.746 29.862 18.305 1.00 16.45

ATOM 5842 NEl TRP B 461 40.906 30.542 17.152 1.00 18.58

ATOM 5844 CE2 TRP B 461 41.432 31.765 17.439 1.00 16.14

ATOM 5845 CD2 TRP B 461 41.542 31.852 18.834 1.00 18.37

ATOM 5846 CE3 TRP B 461 42.039 33.027 19.404 1.00 17.27

ATOM 5848 CZ3 TRP B 461 42.379 34.059 18.562 1.00 18.33

ATOM 5850 CH2 TRP B 461 42.231 33.938 17.167 1.00 17.10

ATOM 5852 CZ2 TRP B 461 41.735 32.803 16.603 1.00 18.15

ATOM 5854 C TRP B 461 42.190 29.145 22.638 1.00 18.90

ATOM 5855 O TRP B 461 41.323 28.562 23.281 1.00 18.75

ATOM 5857 N SER B 462 43.251 29.718 23.211 1.00 21.05

ATOM 5858 CA SER B 462 43.364 29.855 24.676 1.00 21.95

ATOM 5860 CB SER B 462 44.782 30.266 25.095 1.00 22.56

ATOM 5863 OG SER B 462 45.101 31.552 24.602 1.00 21.44

ATOM 5865 C SER B 462 42.470 30.958 25.165 1.00 22.94

ATOM 5866 O SER B 462 42.041 31.830 24.401 1.00 20.65

ATOM 5868 N ALA B 463 42.277 30.967 26.478 1.00 25.72

ATOM 5869 CA ALA B 463 41.942 32.201 27.155 1.00 25.96

ATOM 5871 CB ALA B 463 41.875 31.978 28.686 1.00 26.61

ATOM 5875 C ALA B 463 42.978 33.261 26.814 1.00 26.83

ATOM 5876 O ALA B 463 44.172 32.987 26.594 1.00 27.13

ATOM 5878 N HIS B 464 42.497 34.482 26.741 1.00 27.50

ATOM 5879 CA HIS B 464 43.321 35.635 26.525 1.00 28.88

ATOM 5881 CB HIS B 464 42.374 36.820 26.435 1.00 29.32

ATOM 5884 CG HIS B 464 43.010 38.083 25.985 1.00 33.35

ATOM 5885 NDl HIS B 464 43.312 39.103 26.853 1.00 34.77

ATOM 5887 CEl HIS B 464 43.839 40.106 26.176 1.00 38.22

ATOM 5889 NE2 HIS B 464 43.890 39.770 24.898 1.00 40.19

ATOM 5891 CD2 HIS B 464 43.367 38.511 24.751 1.00 39.63

ATOM 5893 C HIS B 464 44.272 35.744 27.742 1.00 29.00 ATOM 5894 O HIS B 464 43.837 35.592 28.891 1.00 29.84

ATOM 5896 N SER B 465 45.550 35.989 27.497 1.00 27.23

ATOM 5897 CA SER B 465 46.562 36.040 28.579 1.00 27.46

ATOM 5899 CB SER B 465 47.935 36.248 27.973 1.00 26.38

ATOM 5902 OG SER B 465 48.013 37.573 27.459 1.00 25.64

ATOM 5904 C SER B 465 46.395 37.177 29.596 1.00 28.33

ATOM 5905 O SER B 465 46.998 37.133 30.669 1.00 30.13

ATOM 5907 N GLY B 466 45.674 38.223 29.225 1.00 29.34

ATOM 5908 CA GLY B 466 45.615 39.442 30.034 1.00 30.07

ATOM 5911 C GLY B 466 46.855 40.277 29.823 1.00 30.47

ATOM 5912 O GLY B 466 47.797 39.832 29.170 1.00 30.00

ATOM 5914 N PRO B 467 46.872 41.498 30.392 1.00 30.39

ATOM 5915 CA PRO B 467 47.879 42.476 30.020 1.00 30.73

ATOM 5917 CB PRO B 467 47.192 43.801 30.329 1.00 30.58

ATOM 5920 CG PRO B 467 46.294 43.493 31.510 1.00 29.19

ATOM 5923 CD PRO B 467 45.949 42.016 31.426 1.00 31.58

ATOM 5926 C PRO B 467 49.210 42.386 30.774 1.00 30.55

ATOM 5927 O PRO B 467 50.088 43.183 30.506 1.00 29.98

ATOM 5928 N THR B 468 49.385 41.461 31.706 1.00 32.20

ATOM 5929 CA THR B 468 50.658 41.457 32.423 1.00 34.40

ATOM 5931 CB THR B 468 50.705 40.431 33.529 1.00 34.88

ATOM 5933 OGl THR B 468 50.656 39.130 32.957 1.00 36.97

ATOM 5935 CG2 THR B 468 49.530 40.626 34.473 1.00 33.57

ATOM 5939 C THR B 468 51.840 41.303 31.458 1.00 37.08

ATOM 5940 O THR B 468 51.777 40.578 30.454 1.00 36.35

ATOM 5942 N ARG B 469 52.918 42.023 31.759 1.00 40.27

ATOM 5943 CA ARG B 469 54.043 42.160 30.837 1.00 42.38

ATOM 5945 CB ARG B 469 55.143 43.053 31.445 1.00 43.63

ATOM 5948 CG ARG B 469 54.736 44.520 31.702 1.00 51.13

ATOM 5951 CD ARG B 469 54.407 45.294 30.413 1.00 60.79

ATOM 5954 NE ARG B 469 53.562 46.475 30.640 1.00 65.25

ATOM 5956 CZ ARG B 469 52.251 46.558 30.371 1.00 68.56

ATOM 5957 NHl ARG B 469 51.579 45.524 29.848 1.00 69.29

ATOM 5960 NH2 ARG B 469 51.599 47.696 30.620 1.00 65.03

ATOM 5963 C ARG B 469 54.628 40.809 30.435 1.00 42.39

ATOM 5964 O ARG B 469 54.992 40.607 29.265 1.00 42.59

ATOM 5966 N MET B 470 54.707 39.900 31.410 1.00 42.34

ATOM 5967 CA MET B 470 55.204 38.542 31.206 1.00 43.15

ATOM 5969 CB MET B 470 56.050 38.112 32.419 1.00 44.29

ATOM 5972 CG MET B 470 57.247 38.998 32.707 1.00 49.48

ATOM 5975 SD MET B 470 58.414 38.970 31.337 1.00 59.43

ATOM 5976 CE MET B 470 57.902 40.396 30.359 1.00 57.11

ATOM 5980 C MET B 470 54.048 37.553 31.063 1.00 41.88

ATOM 5981 O MET B 470 54.202 36.358 31.391 1.00 42.02

ATOM 5983 N ALA B 471 52.889 38.039 30.611 1.00 39.06

ATOM 5984 CA ALA B 471 51.701 37.200 30.534 1.00 37.70

ATOM 5986 CB ALA B 471 50.446 38.040 30.225 1.00 36.81

ATOM 5990 C ALA B 471 51.938 36.192 29.433 1.00 35.59

ATOM 5991 O ALA B 471 52.537 36.524 28.401 1.00 36.03

ATOM 5993 N THR B 472 51.502 34.960 29.681 1.00 34.97

ATOM 5994 CA THR B 472 51.469 33.942 28.655 1.00 33.70

ATOM 5996 CB THR B 472 52.610 32.887 28.824 1.00 34.55

ATOM 5998 OGl THR B 472 52.329 32.022 29.929 1.00 37.16

ATOM 6000 CG2 THR B 472 53.984 33.573 29.037 1.00 33.82

ATOM 6004 C THR B 472 50.071 33.291 28.573 1.00 32.35

ATOM 6005 O THR B 472 49.389 33.119 29.582 1.00 31.51

ATOM 6007 N ALA B 473 49.640 32.989 27.347 1.00 30.39

ATOM 6008 CA ALA B 473 48.405 32.236 27.097 1.00 29.44

ATOM 6010 CB ALA B 473 47.585 32.892 25.969 1.00 30.02

ATOM 6014 C ALA B 473 48.823 30.827 26.713 1.00 28.17

ATOM 6015 O ALA B 473 49.845 30.660 26.037 1.00 26.66 ATOM 6017 N ILE I3 474 48.081 29.826 27.182 1.00 26.51

ATOM 6018 CA ILE I 3 474 48.389 28.429 26.872 1.00 27.47

ATOM 6020 CB ILE I 3 474 48.794 27.609 28.109 1.00 27.19

ATOM 6022 CGl ILE I 3 474 50.108 28.144 28.703 1.00 33.24

ATOM 6025 CDl ILE I 3 474 50.784 27.189 29.662 1.00 37.63

ATOM 6029 CG2 ILE I 3 474 49.023 26.159 27.736 1.00 29.79

ATOM 6033 C ILE I 3 474 47.193 27.777 26.204 1.00 26.20

ATOM 6034 O ILE I 3 474 46.104 27.820 26.735 1.00 27.64

ATOM 6036 N ALA I 3 475 47.397 27.223 25.011 1.00 24.50

ATOM 6037 CA ALA I 3 475 46.387 26.418 24.333 1.00 22.28

ATOM 6039 CB ALA I 3 475 46.176 26.895 22.885 1.00 20.81

ATOM 6043 C ALA I 3 475 46.893 25.004 24.371 1.00 22.82

ATOM 6044 O ALA I 3 475 48.019 24.719 23.934 1.00 24.68

ATOM 6046 N ARG I 3 476 46.080 24.119 24.922 1.00 23.13

ATOM 6047 CA ARG I 3 476 46.392 22.714 25.028 1.00 24.36

ATOM 6049 CB ARG I 3 476 46.158 22.259 26.459 1.00 24.97

ATOM 6052 CG ARG I 3 476 46.963 22.991 27.492 1.00 29.94

ATOM 6055 CD ARG I 3 476 46.680 22.405 28.857 1.00 38.16

ATOM 6058 NE ARG I 3 476 47.659 22.917 29.799 1.00 40.26

ATOM 6060 CZ ARG I 3 476 47.627 24.142 30.285 1.00 42.51

ATOM 6061 NHl ARG I 3 476 46.651 24.967 29.938 1.00 43.26

ATOM 6064 NH2 ARG I 3 476 48.577 24.538 31.126 1.00 46.28

ATOM 6067 C ARG I 3 476 45.496 21.801 24.173 1.00 25.42

ATOM 6068 O ARG I 3 476 44.317 22.082 23.951 1.00 26.10

ATOM 6070 N CYS I 3 477 46.040 20.638 23.860 1.00 25.21

ATOM 6071 CA CYS I 3 477 45.306 19.608 23.168 1.00 25.29

ATOM 6073 CB CYS I 3 477 46.191 18.971 22.107 1.00 26.12

ATOM 6076 SG CYS I 3 477 46.815 20.161 20.878 1.00 26.43

ATOM 6078 C CYS I 3 477 44.832 18.565 24.165 1.00 25.57

ATOM 6079 O CYS I 3 477 45.215 18.576 25.321 1.00 24.04

ATOM 6081 N ALA I 3 478 43.970 17.686 23.701 1.00 24.42

ATOM 6082 CA ALA I 3 478 43.493 16.593 24.506 1.00 25.97

ATOM 6084 CB ALA I 3 478 42.270 15.925 23.849 1.00 23.55

ATOM 6088 C ALA I 3 478 44.639 15.603 24.633 1.00 25.92

ATOM 6089 O ALA I 3 478 45.582 15.624 23.835 1.00 24.80

ATOM 6091 N PRO I 3 479 44.564 14.727 25.643 1.00 28.67

ATOM 6092 CA PRO I 3 479 45.628 13.750 25.875 1.00 28.52

ATOM 6094 CB PRO I 3 479 45.058 12.865 26.976 1.00 29.34

ATOM 6097 CG PRO I 3 479 44.090 13.722 27.703 1.00 31.35

ATOM 6100 CD PRO I 3 479 43.491 14.634 26.647 1.00 28.74

ATOM 6103 C PRO I 3 479 45.934 12.913 24.648 1.00 28.93

ATOM 6104 O PRO I 3 479 47.106 12.611 24.400 1.00 30.49

ATOM 6105 N ASP I 3 480 44.905 12.555 23.884 1.00 27.54

ATOM 6106 CA ASP I 3 480 45.097 11.699 22.709 1.00 29.00

ATOM 6108 CB ASP I 3 480 43.948 10.683 22.559 1.00 29.15

ATOM 6111 CG ASP I 3 480 42.554 11.304 22.617 1.00 31.64

ATOM 6112 ODl ASP I 3 480 42.326 12.307 23.338 1.00 34.78

ATOM 6113 OD2 ASP I 3 480 41.661 10.708 21.966 1.00 27.33

ATOM 6114 C ASP I 3 480 45.352 12.428 21.395 1.00 28.47

ATOM 6115 O ASP I 3 480 45.403 11.807 20.333 1.00 29.98

ATOM 6117 N GLU I 3 481 45.525 13.741 21.466 1.00 27.05

ATOM 6118 CA GLU I 3 481 45.845 14.556 20.297 1.00 25.70

ATOM 6120 CB GLU I 3 481 44.985 15.818 20.319 1.00 25.40

ATOM 6123 CG GLU I 3 481 43.508 15.550 20.043 1.00 22.73

ATOM 6126 CD GLU I 3 481 42.647 16.790 20.209 1.00 25.85

ATOM 6127 OEl GLU I 3 481 42.988 17.646 21.058 1.00 23.44

ATOM 6128 OE2 GLU I 3 481 41.639 16.919 19.471 1.00 22.15

ATOM 6129 C GLU I 3 481 47.309 14.984 20.265 1.00 25.96

ATOM 6130 O GLU I 3 481 47.960 15.068 21.311 1.00 26.35

ATOM 6132 N GLU I 3 482 47.800 15.311 19.078 1.00 23.70

ATOM 6133 CA GLU I 3 482 49.106 15.909 18.931 1.00 24.38 ATOM 6135 CB GLU B 482 49.899 15.229 17.820 1.00 25.55

ATOM 6138 CG GLU B 482 49.943 13.713 17.926 1.00 29.70

ATOM 6141 CD GLU B 482 51.049 13.229 18.838 1.00 37.13

ATOM 6142 OEl GLU B 482 52.013 13.993 19.071 1.00 34.11

ATOM 6143 OE2 GLU B 482 50.957 12.075 19.307 1.00 43.94

ATOM 6144 C GLU B 482 48.929 17.380 18.587 1.00 23.53

ATOM 6145 O GLU B 482 48.082 17.766 17.788 1.00 23.35

ATOM 6147 N LEU B 483 49.724 18.208 19.224 1.00 23.27

ATOM 6148 CA LEU B 483 49.871 19.599 18.830 1.00 21.43

ATOM 6150 CB LEU B 483 50.578 20.329 19.977 1.00 21.88

ATOM 6153 CG LEU B 483 50.854 21.814 19.788 1.00 23.10

ATOM 6155 CDl LEU B 483 51.744 22.378 20.906 1.00 26.51

ATOM 6159 CD2 LEU B 483 49.489 22.456 19.725 1.00 18.76

ATOM 6163 C LEU B 483 50.729 19.680 17.577 1.00 22.34

ATOM 6164 O LEU B 483 51.954 19.513 17.661 1.00 23.27

ATOM 6166 N LEU B 484 50.138 19.930 16.401 1.00 20.31

ATOM 6167 CA LEU B 484 50.941 20.041 15.184 1.00 18.73

ATOM 6169 CB LEU B 484 50.213 19.447 13.957 1.00 18.70

ATOM 6172 CG LEU B 484 49.958 17.962 14.086 1.00 20.55

ATOM 6174 CDl LEU B 484 49.694 17.354 12.700 1.00 17.34

ATOM 6178 CD2 LEU B 484 51.064 17.262 14.789 1.00 19.70

ATOM 6182 C LEU B 484 51.441 21.422 14.832 1.00 19.62

ATOM 6183 O LEU B 484 52.385 21.552 14.044 1.00 19.40

ATOM 6185 N SER B 485 50.822 22.450 15.376 1.00 17.61

ATOM 6186 CA SER B 485 51.326 23.792 15.234 1.00 19.54

ATOM 6188 CB SER B 485 50.973 24.386 13.872 1.00 20.43

ATOM 6191 OG SER B 485 49.588 24.681 13.781 1.00 22.36

ATOM 6193 C SER B 485 50.780 24.708 16.321 1.00 17.87

ATOM 6194 O SER B 485 49.862 24.358 17.056 1.00 17.51

ATOM 6196 N CYS B 486 51.299 25.924 16.328 1.00 21.63

ATOM 6197 CA CYS B 486 51.000 26.872 17.377 1.00 21.85

ATOM 6199 CB CYS B 486 51.965 26.589 18.504 1.00 24.16

ATOM 6202 SG CYS B 486 51.986 27.783 19.853 1.00 24.55

ATOM 6204 C CYS B 486 51.162 28.247 16.780 1.00 21.47

ATOM 6205 O CYS B 486 52.193 28.532 16.143 1.00 22.16

ATOM 6207 N SER B 487 50.114 29.063 16.882 1.00 18.64

ATOM 6208 CA SER B 487 50.140 30.425 16.424 1.00 17.46

ATOM 6210 CB SER B 487 49.381 30.652 15.098 1.00 19.10

ATOM 6213 OG SER B 487 47.964 30.434 15.224 1.00 20.43

ATOM 6215 C SER B 487 49.603 31.291 17.555 1.00 19.48

ATOM 6216 O SER B 487 49.392 30.812 18.689 1.00 20.62

ATOM 6218 N SER B 488 49.521 32.574 17.291 1.00 20.85

ATOM 6219 CA SER B 488 49.052 33.537 18.296 1.00 22.38

ATOM 6221 CB SER B 488 50.199 33.969 19.229 1.00 22.95

ATOM 6224 OG SER B 488 51.302 34.497 18.506 1.00 23.01

ATOM 6226 C SER B 488 48.469 34.727 17.590 1.00 23.12

ATOM 6227 O SER B 488 48.608 34.878 16.374 1.00 22.64

ATOM 6229 N PHE B 489 47.799 35.575 18.357 1.00 24.90

ATOM 6230 CA PHE B 489 47.056 36.680 17.806 1.00 25.46

ATOM 6232 CB PHE B 489 45.696 36.197 17.321 1.00 27.36

ATOM 6235 CG PHE B 489 44.791 37.305 16.812 1.00 27.38

ATOM 6236 CDl PHE B 489 44.972 37.847 15.558 1.00 27.33

ATOM 6238 CEl PHE B 489 44.143 38.842 15.087 1.00 33.03

ATOM 6240 CZ PHE B 489 43.107 39.308 15.853 1.00 27.77

ATOM 6242 CE2 PHE B 489 42.905 38.777 17.102 1.00 29.75

ATOM 6244 CD2 PHE B 489 43.755 37.786 17.583 1.00 25.67

ATOM 6246 C PHE B 489 46.847 37.666 18.921 1.00 26.55

ATOM 6247 O PHE B 489 46.518 37.273 20.036 1.00 25.01

ATOM 6249 N SER B 490 47.070 38.929 18.607 1.00 29.54

ATOM 6250 CA SER B 490 46.557 40.041 19.409 1.00 33.26

ATOM 6252 CB SER B 490 47.662 40.695 20.244 1.00 33.83 ATOM 6255 OG SER B 490 48.181 41.855 19.609 1.00 41.18

ATOM 6257 C SER B 490 45.920 41.079 18.509 1.00 34.17

ATOM 6258 O SER B 490 46.377 41.331 17.409 1.00 32.02

ATOM 6260 N ARG B 491 44.870 41.711 19.012 1.00 36.19

ATOM 6261 CA ARG B 491 44.135 42.689 18.218 1.00 37.54

ATOM 6263 CB ARG B 491 42.776 42.983 18.869 1.00 39.02

ATOM 6266 CG ARG B 491 41.924 41.728 18.915 1.00 43.46

ATOM 6269 CD ARG B 491 40.734 41.810 19.854 1.00 49.86

ATOM 6272 NE ARG B 491 40.222 40.468 20.158 1.00 50.06

ATOM 6274 CZ ARG B 491 39.661 39.643 19.268 1.00 50.78

ATOM 6275 NHl ARG B 491 39.504 40.004 17.991 1.00 49.99

ATOM 6278 NH2 ARG B 491 39.239 38.445 19.660 1.00 50.09

ATOM 6281 C ARG B 491 44.973 43.944 18.022 1.00 36.60

ATOM 6282 O ARG B 491 44.866 44.590 16.984 1.00 35.36

ATOM 6284 N SER B 492 45.851 44.245 18.976 1.00 37.01

ATOM 6285 CA SER B 492 46.814 45.356 18.830 1.00 38.21

ATOM 6287 CB SER B 492 47.302 45.821 20.200 1.00 38.59

ATOM 6290 OG SER B 492 47.971 44.780 20.880 1.00 38.43

ATOM 6292 C SER B 492 48.037 45.012 17.962 1.00 39.25

ATOM 6293 O SER B 492 48.633 45.880 17.325 1.00 39.39

ATOM 6295 N GLY B 493 48.400 43.735 17.931 1.00 39.95

ATOM 6296 CA GLY B 493 49.628 43.312 17.299 1.00 40.73

ATOM 6299 C GLY B 493 50.810 43.424 18.241 1.00 40.54

ATOM 6300 O GLY B 493 51.930 43.210 17.818 1.00 41.13

ATOM 6302 N LYS B 494 50.554 43.723 19.520 1.00 39.78

ATOM 6303 CA LYS B 494 51.593 43.832 20.529 1.00 39.01

ATOM 6305 CB LYS B 494 51.256 44.943 21.525 1.00 39.84

ATOM 6308 CG LYS B 494 51.424 46.308 20.900 1.00 42.34

ATOM 6311 CD LYS B 494 50.788 47.365 21.748 1.00 47.63

ATOM 6314 CE LYS B 494 50.957 48.731 21.131 1.00 49.73

ATOM 6317 NZ LYS B 494 50.457 49.761 22.084 1.00 55.20

ATOM 6321 C LYS B 494 51.834 42.503 21.236 1.00 38.10

ATOM 6322 O LYS B 494 51.245 42.202 22.262 1.00 36.67

ATOM 6324 N ARG B 495 52.847 41.806 20.730 1.00 37.21

ATOM 6325 CA ARG B 495 52.933 40.368 20.726 1.00 36.20

ATOM 6327 CB ARG B 495 52.368 39.938 19.364 1.00 37.36

ATOM 6330 CG ARG B 495 51.767 38.601 19.285 1.00 40.90

ATOM 6333 CD ARG B 495 50.824 38.516 18.094 1.00 40.18

ATOM 6336 NE ARG B 495 51.508 38.677 16.810 1.00 41.00

ATOM 6338 CZ ARG B 495 52.164 37.711 16.175 1.00 38.61

ATOM 6339 NHl ARG B 495 52.739 37.956 15.011 1.00 37.34

ATOM 6342 NH2 ARG B 495 52.266 36.498 16.707 1.00 38.91

ATOM 6345 C ARG B 495 54.417 40.007 20.790 1.00 32.82

ATOM 6346 O ARG B 495 55.211 40.655 20.132 1.00 32.40

ATOM 6348 N ARG B 496 54.785 39.009 21.589 1.00 29.64

ATOM 6349 CA ARG B 496 56.131 38.414 21.526 1.00 29.45

ATOM 6351 CB ARG B 496 56.808 38.441 22.902 1.00 29.23

ATOM 6354 CG ARG B 496 57.428 39.806 23.249 1.00 30.04

ATOM 6357 CD ARG B 496 58.272 39.776 24.516 1.00 34.21

ATOM 6360 NE ARG B 496 57.624 39.137 25.668 1.00 43.38

ATOM 6362 CZ ARG B 496 58.001 37.975 26.225 1.00 49.80

ATOM 6363 NHl ARG B 496 59.030 37.270 25.748 1.00 50.65

ATOM 6366 NH2 ARG B 496 57.331 37.499 27.279 1.00 49.62

ATOM 6369 C ARG B 496 56.116 36.988 20.919 1.00 27.73

ATOM 6370 O ARG B 496 57.045 36.197 21.141 1.00 27.60

ATOM 6372 N GLY B 497 55.069 36.702 20.138 1.00 25.97

ATOM 6373 CA GLY B 497 54.906 35.435 19.440 1.00 24.88

ATOM 6376 C GLY B 497 54.522 34.276 20.328 1.00 24.32

ATOM 6377 O GLY B 497 53.903 34.436 21.368 1.00 24.49

ATOM 6379 N GLU B 498 54.926 33.084 19.921 1.00 22.51

ATOM 6380 CA GLU B 498 54.509 31.881 20.588 1.00 22.63 ATOM 6382 CB GLU B 498 53.166 31.390 19.996 1.00 22.69

ATOM 6385 CG GLU B 498 53.251 30.774 18.601 1.00 23.38

ATOM 6388 CD GLU B 498 53.610 31.728 17.470 1.00 26.32

ATOM 6389 OEl GLU B 498 53.066 32.855 17.382 1.00 26.26

ATOM 6390 OE2 GLU B 498 54.440 31.317 16.621 1.00 23.57

ATOM 6391 C GLU B 498 55.543 30.794 20.443 1.00 22.18

ATOM 6392 O GLU B 498 56.393 30.843 19.571 1.00 23.05

ATOM 6394 N ARG B 499 55.437 29.778 21.270 1.00 22.91

ATOM 6395 CA ARG B 499 56.349 28.668 21.198 1.00 25.90

ATOM 6397 CB ARG B 499 57.540 28.904 22.148 1.00 25.49

ATOM 6400 CG ARG B 499 57.142 28.941 23.604 1.00 34.76

ATOM 6403 CD ARG B 499 58.001 29.882 24.474 1.00 48.54

ATOM 6406 NE ARG B 499 59.278 29.310 24.877 1.00 55.16

ATOM 6408 CZ ARG B 499 60.163 29.919 25.678 1.00 60.28

ATOM 6409 NHl ARG B 499 59.928 31.142 26.167 1.00 61.31

ATOM 6412 NH2 ARG B 499 61.307 29.305 25.985 1.00 58.76

ATOM 6415 C ARG B 499 55.604 27.425 21.607 1.00 27.38

ATOM 6416 O ARG B 499 54.654 27.495 22.377 1.00 25.40

ATOM 6418 N MET B 500 56.046 26.288 21.077 1.00 29.53

ATOM 6419 CA MET B 500 55.550 24.990 21.491 1.00 31.87

ATOM 6421 CB MET B 500 55.542 24.044 20.288 1.00 31.90

ATOM 6424 CG MET B 500 54.644 24.556 19.150 1.00 33.82

ATOM 6427 SD MET B 500 54.755 23.652 17.580 1.00 35.97

ATOM 6428 CE MET B 500 56.087 24.559 16.753 1.00 33.82

ATOM 6432 C MET B 500 56.518 24.523 22.542 1.00 33.97

ATOM 6433 O MET B 500 57.712 24.428 22.273 1.00 34.75

ATOM 6435 N GLU B 501 56.023 24.278 23.746 1.00 35.51

ATOM 6436 CA GLU B 501 56.859 23.891 24.875 1.00 38.56

ATOM 6438 CB GLU B 501 56.936 25.032 25.927 1.00 38.68

ATOM 6441 CG GLU B 501 55.747 25.120 26.900 1.00 42.36

ATOM 6444 CD GLU B 501 56.103 25.779 28.226 1.00 42.22

ATOM 6445 OEl GLU B 501 56.727 26.862 28.182 1.00 53.39

ATOM 6446 OE2 GLU B 501 55.760 25.218 29.304 1.00 44.22

ATOM 6447 C GLU B 501 56.252 22.639 25.476 1.00 37.89

ATOM 6448 O GLU B 501 55.031 22.503 25.472 1.00 34.87

ATOM 6450 N ALA B 502 57.089 21.717 25.952 1.00 39.23

ATOM 6451 CA ALA B 502 56.604 20.497 26.602 1.00 42.09

ATOM 6453 CB ALA B 502 57.633 19.378 26.515 1.00 42.17

ATOM 6457 C ALA B 502 56.207 20.761 28.049 1.00 45.52

ATOM 6458 O ALA B 502 56.698 21.691 28.681 1.00 46.82

ATOM 6460 N GLN B 503 55.296 19.937 28.563 1.00 48.11

ATOM 6461 CA GLN B 503 54.625 20.218 29.825 1.00 49.90

ATOM 6463 CB GLN B 503 53.698 21.415 29.646 1.00 50.17

ATOM 6466 CG GLN B 503 53.218 22.011 30.928 1.00 52.54

ATOM 6469 CD GLN B 503 52.831 23.455 30.755 1.00 55.74

ATOM 6470 OEl GLN B 503 53.597 24.252 30.203 1.00 61.35

ATOM 6471 NE2 GLN B 503 51.641 23.811 31.219 1.00 57.75

ATOM 6474 C GLN B 503 53.838 18.997 30.293 1.00 50.58

ATOM 6475 O GLN B 503 52.869 18.586 29.650 1.00 51.84

ATOM 6477 N GLY B 504 54.264 18.396 31.400 1.00 50.70

ATOM 6478 CA GLY B 504 53.716 17.114 31.807 1.00 50.01

ATOM 6481 C GLY B 504 53.887 16.082 30.709 1.00 49.99

ATOM 6482 O GLY B 504 53.002 15.253 30.489 1.00 50.55

ATOM 6484 N GLY B 505 55.026 16.141 30.012 1.00 49.46

ATOM 6485 CA GLY B 505 55.358 15.179 28.940 1.00 48.35

ATOM 6488 C GLY B 505 54.524 15.324 27.673 1.00 47.17

ATOM 6489 O GLY B 505 54.413 14.386 26.859 1.00 48.77

ATOM 6491 N LYS B 506 53.940 16.501 27.498 1.00 44.35

ATOM 6492 CA LYS B 506 53.058 16.762 26.381 1.00 41.06

ATOM 6494 CB LYS B 506 51.636 16.512 26.831 1.00 41.60

ATOM 6497 CG LYS B 506 50.604 16.848 25.829 1.00 40.47 ATOM 6500 CD LYS I3 506 49.310 16.156 26.173 1.00 41.71

ATOM 6503 CE LYS I 3 506 48.221 16.607 25.208 1.00 42.74

ATOM 6506 NZ LYS I 3 506 48.541 16.202 23.808 1.00 37.20

ATOM 6510 C LYS I 3 506 53.220 18.204 25.913 1.00 38.06

ATOM 6511 O LYS I 3 506 53.331 19.110 26.712 1.00 37.73

ATOM 6513 N LEU I 3 507 53.224 18.411 24.606 1.00 34.89

ATOM 6514 CA LEU I 3 507 53.478 19.740 24.061 1.00 32.93

ATOM 6516 CB LEU I 3 507 54.024 19.632 22.645 1.00 33.61

ATOM 6519 CG LEU I 3 507 55.429 19.020 22.591 1.00 37.48

ATOM 6521 CDl LEU I 3 507 55.782 18.620 21.168 1.00 37.56

ATOM 6525 CD2 LEU I 3 507 56.447 20.003 23.171 1.00 36.32

ATOM 6529 C LEU I 3 507 52.223 20.619 24.091 1.00 30.88

ATOM 6530 O LEU I 3 507 51.118 20.183 23.718 1.00 31.59

ATOM 6532 N VAL I 3 508 52.428 21.857 24.530 1.00 27.37

ATOM 6533 CA VAL I 3 508 51.410 22.869 24.604 1.00 26.36

ATOM 6535 CB VAL I 3 508 51.110 23.294 26.084 1.00 26.40

ATOM 6537 CGl VAL I 3 508 52.239 24.099 26.637 1.00 27.23

ATOM 6541 CG2 VAL I 3 508 50.867 22.058 26.968 1.00 27.03

ATOM 6545 C VAL I 3 508 51.879 24.050 23.774 1.00 24.72

ATOM 6546 O VAL I 3 508 53.074 24.177 23.434 1.00 22.41

ATOM 6548 N CYS I 3 509 50.926 24.897 23.409 1.00 23.87

ATOM 6549 CA CYS I 3 509 51.176 26.102 22.641 1.00 21.79

ATOM 6551 CB CYS I 3 509 50.087 26.282 21.575 1.00 19.78

ATOM 6554 SG CYS I 3 509 50.161 27.752 20.649 1.00 22.49

ATOM 6556 C CYS I 3 509 51.137 27.246 23.635 1.00 22.01

ATOM 6557 O CYS I 3 509 50.121 27.462 24.279 1.00 21.86

ATOM 6559 N ARG I 3 510 52.253 27.947 23.788 1.00 22.47

ATOM 6560 CA ARG I 3 510 52.341 29.069 24.697 1.00 24.42

ATOM 6562 CB ARG I 3 510 53.456 28.794 25.697 1.00 26.40

ATOM 6565 CG ARG I 3 510 53.621 29.821 26.826 1.00 33.57

ATOM 6568 CD ARG I 3 510 54.955 29.527 27.525 1.00 45.70

ATOM 6571 NE ARG I 3 510 54.979 29.872 28.951 1.00 55.34

ATOM 6573 CZ ARG I 3 510 56.090 29.909 29.700 1.00 57.63

ATOM 6574 NHl ARG I 3 510 57.287 29.612 29.171 1.00 56.22

ATOM 6577 NH2 ARG I 3 510 56.009 30.246 30.987 1.00 55.70

ATOM 6580 C ARG I 3 510 52.614 30.351 23.944 1.00 23.90

ATOM 6581 O ARG I 3 510 53.529 30.412 23.118 1.00 24.69

ATOM 6583 N ALA I 3 511 51.831 31.385 24.225 1.00 23.86

ATOM 6584 CA ALA I 3 511 52.004 32.675 23.547 1.00 23.72

ATOM 6586 CB ALA I 3 511 50.750 33.114 22.814 1.00 22.99

ATOM 6590 C ALA I 3 511 52.359 33.680 24.577 1.00 24.42

ATOM 6591 O ALA I 3 511 51.922 33.566 25.736 1.00 25.46

ATOM 6593 N HIS I 3 512 53.109 34.673 24.136 1.00 25.35

ATOM 6594 CA HIS I 3 512 53.726 35.664 25.001 1.00 27.02

ATOM 6596 CB HIS I 3 512 55.240 35.620 24.816 1.00 27.59

ATOM 6599 CG HIS I 3 512 55.862 34.362 25.292 1.00 29.32

ATOM 6600 NDl HIS I 3 512 56.103 34.116 26.628 1.00 37.71

ATOM 6602 CEl HIS I 3 512 56.642 32.917 26.759 1.00 41.06

ATOM 6604 NE 2 HIS I 3 512 56.773 32.388 25.555 1.00 44.34

ATOM 6606 CD2 HIS I 3 512 56.289 33.271 24.620 1.00 38.08

ATOM 6608 C HIS I 3 512 53.248 37.056 24.651 1.00 27.22

ATOM 6609 O HIS I 3 512 53.279 37.452 23.503 1.00 27.05

ATOM 6611 N ASN I 3 513 52.843 37.804 25.668 1.00 31.25

ATOM 6612 CA ASN I 3 513 52.401 39.176 25.493 1.00 33.42

ATOM 6614 CB ASN I 3 513 51.554 39.583 26.701 1.00 33.97

ATOM 6617 CG ASN I 3 513 50.888 40.923 26.540 1.00 32.01

ATOM 6618 ODl ASN I 3 513 50.650 41.400 25.422 1.00 30.70

ATOM 6619 ND2 ASN I 3 513 50.579 41.560 27.688 1.00 31.23

ATOM 6622 C ASN I 3 513 53.620 40.071 25.362 1.00 36.44

ATOM 6623 O ASN I 3 513 54.703 39.728 25.842 1.00 35.84

ATOM 6625 N ALA I 3 514 53.445 41.188 24.668 1.00 39.09 ATOM 6626 CA ALA I3 514 54.465 42.212 24.571 1.00 41.65

ATOM 6628 CB ALA I 3 514 54.378 42.917 23.213 1.00 42.63

ATOM 6632 C ALA I 3 514 54.277 43.226 25.689 1.00 44.24

ATOM 6633 O ALA I 3 514 53.181 43.372 26.228 1.00 43.78

ATOM 6635 N PHE I 3 515 55.357 43.932 26.009 1.00 47.03

ATOM 6636 CA PHE I 3 515 55.329 45.076 26.922 1.00 49.16

ATOM 6638 CB PHE I 3 515 56.740 45.685 27.043 1.00 51.57

ATOM 6641 CG PHE I 3 515 56.975 46.443 28.327 1.00 55.58

ATOM 6642 CDl PHE I 3 515 57.560 45.808 29.428 1.00 59.00

ATOM 6644 CEl PHE I 3 515 57.768 46.502 30.623 1.00 58.96

ATOM 6646 CZ PHE I 3 515 57.403 47.850 30.717 1.00 58.98

ATOM 6648 CE 2 PHE I 3 515 56.832 48.495 29.620 1.00 58.41

ATOM 6650 CD2 PHE I 3 515 56.623 47.792 28.432 1.00 58.37

ATOM 6652 C PHE I 3 515 54.352 46.117 26.392 1.00 47.81

ATOM 6653 O PHE I 3 515 54.490 46.604 25.271 1.00 47.21

ATOM 6655 N GLY I 3 516 53.344 46.433 27.188 1.00 47.25

ATOM 6656 CA GLY I 3 516 52.312 47.362 26.765 1.00 47.07

ATOM 6659 C GLY I 3 516 51.201 46.708 25.959 1.00 46.94

ATOM 6660 O GLY I 3 516 50.245 47.381 25.563 1.00 47.64

ATOM 6662 N GLY I 3 517 51.305 45.398 25.715 1.00 45.48

ATOM 6663 CA GLY I 3 517 50.236 44.682 25.031 1.00 43.05

ATOM 6666 C GLY I 3 517 49.081 44.486 25.985 1.00 41.45

ATOM 6667 O GLY I 3 517 49.290 44.332 27.192 1.00 42.72

ATOM 6669 N GLU I 3 518 47.867 44.500 25.450 1.00 38.09

ATOM 6670 CA GLU I 3 518 46.663 44.156 26.206 1.00 37.05

ATOM 6672 CB GLU I 3 518 45.397 44.642 25.487 1.00 37.39

ATOM 6675 CG GLU I 3 518 45.019 43.900 24.190 1.00 43.91

ATOM 6678 CD GLU I 3 518 45.957 44.191 23.020 1.00 53.69

ATOM 6679 OEl GLU I 3 518 46.829 45.086 23.155 1.00 59.72

ATOM 6680 OE 2 GLU I 3 518 45.827 43.526 21.965 1.00 58.14

ATOM 6681 C GLU I 3 518 46.561 42.658 26.515 1.00 34.36

ATOM 6682 O GLU I 3 518 45.773 42.245 27.371 1.00 32.41

ATOM 6684 N GLY I 3 519 47.385 41.851 25.843 1.00 32.40

ATOM 6685 CA GLY I 3 519 47.349 40.413 26.010 1.00 30.85

ATOM 6688 C GLY I 3 519 47.257 39.748 24.651 1.00 28.45

ATOM 6689 O GLY I 3 519 47.049 40.380 23.637 1.00 28.21

ATOM 6691 N VAL I 3 520 47.413 38.444 24.663 1.00 27.63

ATOM 6692 CA VAL I 3 520 47.454 37.672 23.434 1.00 25.72

ATOM 6694 CB VAL I 3 520 48.926 37.353 23.046 1.00 25.73

ATOM 6696 CGl VAL I 3 520 49.610 36.605 24.186 1.00 27.22

ATOM 6700 CG2 VAL I 3 520 49.657 38.602 22.693 1.00 27.51

ATOM 6704 C VAL I 3 520 46.725 36.358 23.621 1.00 24.85

ATOM 6705 O VAL I 3 520 46.524 35.890 24.756 1.00 23.08

ATOM 6707 N TYR I 3 521 46.385 35.754 22.478 1.00 24.59

ATOM 6708 CA TYR I 3 521 45.851 34.413 22.430 1.00 22.99

ATOM 6710 CB TYR I 3 521 44.656 34.347 21.502 1.00 24.70

ATOM 6713 CG TYR I 3 521 43.473 35.176 21.897 1.00 24.93

ATOM 6714 CDl TYR I 3 521 42.573 34.713 22.833 1.00 25.16

ATOM 6716 CEl TYR I 3 521 41.455 35.464 23.190 1.00 26.14

ATOM 6718 CZ TYR I 3 521 41.253 36.666 22.583 1.00 22.99

ATOM 6719 OH TYR I 3 521 40.154 37.405 22.925 1.00 33.21

ATOM 6721 CE 2 TYR I 3 521 42.135 37.140 21.629 1.00 25.32

ATOM 6723 CD2 TYR I 3 521 43.244 36.406 21.306 1.00 24.11

ATOM 6725 C TYR I 3 521 46.891 33.468 21.858 1.00 21.58

ATOM 6726 O TYR I 3 521 47.602 33.828 20.929 1.00 20.74

ATOM 6728 N ALA I 3 522 46.951 32.280 22.442 1.00 20.61

ATOM 6729 CA ALA I 3 522 47.682 31.150 21.905 1.00 21.39

ATOM 6731 CB ALA I 3 522 48.286 30.370 22.985 1.00 20.54

ATOM 6735 C ALA I 3 522 46.665 30.293 21.162 1.00 20.28

ATOM 6736 O ALA I 3 522 45.544 30.102 21.621 1.00 18.05

ATOM 6738 N ILE I 3 523 47.067 29.783 20.000 1.00 20.35 ATOM 6739 CA ILE B 523 46.152 29.133 19.078 1.00 18.01

ATOM 6741 CB ILE B 523 45.875 29.997 17.884 1.00 19.14

ATOM 6743 CGl ILE B 523 45.273 31.325 18.321 1.00 20.01

ATOM 6746 CDl ILE B 523 45.485 32.448 17.406 1.00 18.44

ATOM 6750 CG2 ILE B 523 44.908 29.263 16.927 1.00 15.05

ATOM 6754 C ILE B 523 46.809 27.849 18.635 1.00 19.63

ATOM 6755 O ILE B 523 47.749 27.888 17.820 1.00 19.61

ATOM 6757 N ALA B 524 46.395 26.749 19.248 1.00 17.96

ATOM 6758 CA ALA B 524 46.892 25.431 18.908 1.00 19.79

ATOM 6760 CB ALA B 524 46.860 24.523 20.117 1.00 17.99

ATOM 6764 C ALA B 524 46.115 24.771 17.772 1.00 19.64

ATOM 6765 O ALA B 524 44.877 24.914 17.648 1.00 20.88

ATOM 6767 N ARG B 525 46.848 24.008 16.991 1.00 18.12

ATOM 6768 CA ARG B 525 46.289 23.070 16.070 1.00 17.90

ATOM 6770 CB ARG B 525 46.895 23.263 14.698 1.00 19.68

ATOM 6773 CG ARG B 525 46.105 22.648 13.661 1.00 21.45

ATOM 6776 CD ARG B 525 44.939 23.517 13.209 1.00 21.76

ATOM 6779 NE ARG B 525 44.379 22.867 12.043 1.00 17.60

ATOM 6781 CZ ARG B 525 43.141 22.991 11.580 1.00 20.12

ATOM 6782 NHl ARG B 525 42.254 23.764 12.169 1.00 19.14

ATOM 6785 NH2 ARG B 525 42.784 22.295 10.507 1.00 24.60

ATOM 6788 C ARG B 525 46.497 21.662 16.579 1.00 18.07

ATOM 6789 O ARG B 525 47.627 21.162 16.639 1.00 19.30

ATOM 6791 N CYS B 526 45.402 21.039 17.000 1.00 17.15

ATOM 6792 CA CYS B 526 45.434 19.796 17.729 1.00 18.51

ATOM 6794 CB CYS B 526 44.566 19.904 18.972 1.00 21.45

ATOM 6797 SG CYS B 526 45.151 21.093 20.196 1.00 22.00

ATOM 6799 C CYS B 526 44.839 18.752 16.819 1.00 19.53

ATOM 6800 O CYS B 526 43.731 18.952 16.318 1.00 17.49

ATOM 6802 N CYS B 527 45.537 17.649 16.628 1.00 18.42

ATOM 6803 CA CYS B 527 45.173 16.710 15.555 1.00 20.87

ATOM 6805 CB CYS B 527 46.143 16.836 14.396 1.00 19.48

ATOM 6808 SG CYS B 527 46.274 18.485 13.739 1.00 24.58

ATOM 6810 C CYS B 527 45.199 15.312 16.071 1.00 21.86

ATOM 6811 O CYS B 527 45.929 15.006 17.002 1.00 24.20

ATOM 6813 N LEU B 528 44.392 14.454 15.471 1.00 23.01

ATOM 6814 CA LEU B 528 44.365 13.058 15.857 1.00 22.92

ATOM 6816 CB LEU B 528 42.942 12.520 15.833 1.00 21.61

ATOM 6819 CG LEU B 528 41.974 13.048 16.875 1.00 22.39

ATOM 6821 CDl LEU B 528 40.550 12.604 16.508 1.00 17.53

ATOM 6825 CD2 LEU B 528 42.379 12.534 18.279 1.00 23.76

ATOM 6829 C LEU B 528 45.286 12.325 14.882 1.00 26.09

ATOM 6830 O LEU B 528 44.958 12.160 13.703 1.00 26.74

ATOM 6832 N LEU B 529 46.456 11.935 15.387 1.00 29.44

ATOM 6833 CA LEU B 529 47.533 11.371 14.580 1.00 32.58

ATOM 6835 CB LEU B 529 48.601 12.437 14.273 1.00 33.00

ATOM 6838 CG LEU B 529 49.642 12.140 13.194 1.00 31.83

ATOM 6840 CDl LEU B 529 48.992 11.829 11.831 1.00 30.67

ATOM 6844 CD2 LEU B 529 50.653 13.305 13.081 1.00 32.36

ATOM 6848 C LEU B 529 48.106 10.226 15.399 1.00 36.36

ATOM 6849 O LEU B 529 49.014 10.424 16.205 1.00 37.79

ATOM 6851 N PRO B 530 47.538 9.031 15.238 1.00 39.96

ATOM 6852 CA PRO B 530 48.114 7.854 15.879 1.00 41.93

ATOM 6854 CB PRO B 530 47.002 6.822 15.753 1.00 42.13

ATOM 6857 CG PRO B 530 46.353 7.165 14.458 1.00 42.94

ATOM 6860 CD PRO B 530 46.352 8.683 14.432 1.00 41.29

ATOM 6863 C PRO B 530 49.366 7.369 15.136 1.00 42.09

ATOM 6864 O PRO B 530 49.475 7.499 13.903 1.00 40.66

ATOM 6865 N GLN B 531 50.291 6.811 15.901 1.00 43.63

ATOM 6866 CA GLN B 531 51.567 6.300 15.381 1.00 45.30

ATOM 6868 CB GLN B 531 51.374 5.380 14.154 1.00 45.99 ATOM 6871 CG GLN B 531 50.335 4.253 14.346 1.00 49.74

ATOM 6874 CD GLN B 531 50.613 3.385 15.584 1.00 56.46

ATOM 6875 OEl GLN B 531 50.339 3.787 16.720 1.00 58.55

ATOM 6876 NE 2 GLN B 531 51.157 2.185 15.359 1.00 58.92

ATOM 6879 C GLN B 531 52.546 7.430 15.068 1.00 44.58

ATOM 6880 O GLN B 531 53.660 7.173 14.606 1.00 47.45

ATOM 6882 N ALA B 532 52.149 8.671 15.343 1.00 42.98

ATOM 6883 CA ALA B 532 53.031 9.813 15.158 1.00 41.12

ATOM 6885 CB ALA B 532 52.240 11.092 15.065 1.00 40.54

ATOM 6889 C ALA B 532 54.007 9.898 16.315 1.00 39.61

ATOM 6890 O ALA B 532 53.639 9.698 17.468 1.00 39.61

ATOM 6892 N ASN B 533 55.256 10.189 15.980 1.00 38.15

ATOM 6893 CA ASN B 533 56.255 10.597 16.937 1.00 37.54

ATOM 6895 CB ASN B 533 57.471 9.687 16.830 1.00 37.75

ATOM 6898 CG ASN B 533 57.237 8.322 17.473 1.00 40.47

ATOM 6899 ODl ASN B 533 56.312 8.158 18.274 1.00 36.79

ATOM 6900 ND2 ASN B 533 58.076 7.347 17.136 1.00 47.01

ATOM 6902 C ASN B 533 56.638 12.027 16.585 1.00 35.45

ATOM 6903 O ASN B 533 57.335 12.235 15.594 1.00 35.63

ATOM 6905 N CYS B 534 56.150 12.993 17.365 1.00 34.19

ATOM 6906 CA CYS B 534 56.363 14.412 17.063 1.00 33.10

ATOM 6908 CB CYS B 534 55.049 15.180 16.992 1.00 33.53

ATOM 6911 SG CYS B 534 53.894 14.617 15.740 1.00 30.48

ATOM 6913 C CYS B 534 57.253 15.062 18.092 1.00 33.33

ATOM 6914 O CYS B 534 57.183 14.758 19.274 1.00 31.92

ATOM 6916 N SER B 535 58.072 15.995 17.630 1.00 31.34

ATOM 6917 CA SER B 535 58.986 16.678 18.501 1.00 30.86

ATOM 6919 CB SER B 535 60.362 16.094 18.296 1.00 31.64

ATOM 6922 OG SER B 535 60.690 16.239 16.931 1.00 35.53

ATOM 6924 C SER B 535 59.016 18.129 18.086 1.00 29.55

ATOM 6925 O SER B 535 58.442 18.495 17.058 1.00 28.75

ATOM 6927 N VAL B 536 59.729 18.939 18.858 1.00 26.92

ATOM 6928 CA VAL B 536 59.964 20.342 18.482 1.00 24.27

ATOM 6930 CB VAL B 536 59.357 21.309 19.516 1.00 24.23

ATOM 6932 CGl VAL B 536 59.678 22.788 19.135 1.00 20.25

ATOM 6936 CG2 VAL B 536 57.834 21.064 19.607 1.00 25.78

ATOM 6940 C VAL B 536 61.461 20.590 18.333 1.00 23.34

ATOM 6941 O VAL B 536 62.272 20.104 19.135 1.00 20.66

ATOM 6943 N HIS B 537 61.829 21.315 17.290 1.00 20.96

ATOM 6944 CA HIS B 537 63.213 21.672 17.058 1.00 22.14

ATOM 6946 CB HIS B 537 63.655 21.265 15.664 1.00 23.09

ATOM 6949 CG HIS B 537 63.731 19.785 15.472 1.00 27.48

ATOM 6950 NDl HIS B 537 64.591 19.201 14.569 1.00 33.23

ATOM 6952 CEl HIS B 537 64.450 17.886 14.624 1.00 34.69

ATOM 6954 NE 2 HIS B 537 63.519 17.603 15.516 1.00 28.32

ATOM 6956 CD2 HIS B 537 63.058 18.774 16.064 1.00 28.07

ATOM 6958 C HIS B 537 63.215 23.182 17.153 1.00 22.86

ATOM 6959 O HIS B 537 62.456 23.834 16.413 1.00 21.93

ATOM 6961 N THR B 538 64.066 23.714 18.032 1.00 22.58

ATOM 6962 CA THR B 538 64.143 25.129 18.325 1.00 23.16

ATOM 6964 CB THR B 538 63.819 25.425 19.796 1.00 25.03

ATOM 6966 OGl THR B 538 62.446 25.151 20.042 1.00 26.99

ATOM 6968 CG2 THR B 538 64.090 26.870 20.158 1.00 20.53

ATOM 6972 C THR B 538 65.528 25.667 18.034 1.00 24.69

ATOM 6973 O THR B 538 66.549 24.975 18.236 1.00 22.73

ATOM 6975 N ALA B 539 65.548 26.894 17.517 1.00 24.98

ATOM 6976 CA ALA B 539 66.766 27.651 17.404 1.00 25.50

ATOM 6978 CB ALA B 539 67.208 27.723 16.004 1.00 23.47

ATOM 6982 C ALA B 539 66.534 29.058 17.950 1.00 26.96

ATOM 6983 O ALA B 539 65.500 29.695 17.649 1.00 26.32

ATOM 6985 N PRO B 540 67.515 29.567 18.719 1.00 27.96 ATOM 6986 CA PRO B 540 67.488 30.908 19.271 1.00 28.40

ATOM 6988 CB PRO B 540 68.592 30.878 20.339 1.00 28.24

ATOM 6991 CG PRO B 540 69.593 29.890 19.804 1.00 28.37

ATOM 6994 CD PRO B 540 68.771 28.859 19.054 1.00 28.01

ATOM 6997 C PRO B 540 67.795 31.942 18.189 1.00 29.44

ATOM 6998 O PRO B 540 68.154 31.585 17.061 1.00 29.18

ATOM 6999 N PRO B 541 67.637 33.227 18.515 1.00 31.41

ATOM 7000 CA PRO B 541 67.839 34.243 17.502 1.00 33.44

ATOM 7002 CB PRO B 541 67.729 35.539 18.295 1.00 33.52

ATOM 7005 CG PRO B 541 66.913 35.190 19.463 1.00 32.65

ATOM 7008 CD PRO B 541 67.280 33.809 19.818 1.00 32.18

ATOM 7011 C PRO B 541 69.219 34.127 16.853 1.00 36.75

ATOM 7012 O PRO B 541 70.219 33.988 17.555 1.00 34.74

ATOM 7013 N ALA B 542 69.261 34.151 15.527 1.00 40.63

ATOM 7014 CA ALA B 542 70.530 34.050 14.806 1.00 44.34

ATOM 7016 CB ALA B 542 70.284 33.791 13.350 1.00 43.75

ATOM 7020 C ALA B 542 71.285 35.357 14.978 1.00 47.91

ATOM 7021 O ALA B 542 72.519 35.374 15.164 1.00 49.26

ATOM 7023 N GLU B 543 70.508 36.437 14.896 1.00 51.98

ATOM 7024 CA GLU B 543 70.951 37.816 15.055 1.00 54.88

ATOM 7026 CB GLU B 543 71.856 37.976 16.285 1.00 55.11

ATOM 7029 CG GLU B 543 71.141 37.735 17.619 1.00 57.87

ATOM 7032 CD GLU B 543 70.097 38.803 17.930 1.00 62.30

ATOM 7033 OEl GLU B 543 69.914 39.730 17.101 1.00 65.31

ATOM 7034 OE 2 GLU B 543 69.448 38.711 18.997 1.00 64.33

ATOM 7035 C GLU B 543 71.616 38.366 13.799 1.00 57.18

ATOM 7036 O GLU B 543 72.156 39.479 13.821 1.00 58.49

ATOM 7038 N ALA B 544 71.531 37.622 12.696 1.00 58.77

ATOM 7039 CA ALA B 544 72.272 37.982 11.498 1.00 59.77

ATOM 7041 CB ALA B 544 73.720 37.522 11.639 1.00 60.01

ATOM 7045 C ALA B 544 71.680 37.422 10.205 1.00 60.54

ATOM 7046 O ALA B 544 71.471 36.219 10.080 1.00 60.99

ATOM 7048 N SER B 545 71.396 38.331 9.270 1.00 60.86

ATOM 7049 CA SER B 545 71.370 38.058 7.824 1.00 60.98

ATOM 7051 CB SER B 545 72.713 37.447 7.366 1.00 61.47

ATOM 7054 OG SER B 545 72.710 37.159 5.976 1.00 62.34

ATOM 7056 C SER B 545 70.187 37.241 7.321 1.00 60.53

ATOM 7057 O SER B 545 69.172 37.809 6.903 1.00 60.68

ATOM 7059 N MET B 546 70.319 35.914 7.350 1.00 59.90

ATOM 7060 CA MET B 546 69.348 35.011 6.707 1.00 59.32

ATOM 7062 CB MET B 546 70.030 33.683 6.313 1.00 60.50

ATOM 7065 CG MET B 546 71.251 33.807 5.373 1.00 64.31

ATOM 7068 SD MET B 546 70.881 33.768 3.586 1.00 73.90

ATOM 7069 CE MET B 546 72.536 33.673 2.885 1.00 67.40

ATOM 7073 C MET B 546 68.115 34.708 7.590 1.00 56.77

ATOM 7074 O MET B 546 67.313 33.826 7.253 1.00 56.78

ATOM 7076 N GLY B 547 67.955 35.428 8.705 1.00 52.69

ATOM 7077 CA GLY B 547 66.884 35.124 9.651 1.00 49.29

ATOM 7080 C GLY B 547 67.269 33.940 10.508 1.00 45.84

ATOM 7081 O GLY B 547 68.354 33.407 10.362 1.00 45.19

ATOM 7083 N THR B 548 66.382 33.549 11.419 1.00 41.93

ATOM 7084 CA THR B 548 66.611 32.413 12.305 1.00 38.60

ATOM 7086 CB THR B 548 66.078 32.684 13.732 1.00 38.19

ATOM 7088 OGl THR B 548 66.672 33.877 14.231 1.00 37.27

ATOM 7090 CG2 THR B 548 66.430 31.575 14.694 1.00 36.44

ATOM 7094 C THR B 548 65.918 31.230 11.639 1.00 37.73

ATOM 7095 O THR B 548 64.823 31.356 11.124 1.00 36.46

ATOM 7097 N ARG B 549 66.576 30.082 11.624 1.00 35.98

ATOM 7098 CA ARG B 549 66.105 28.966 10.835 1.00 35.28

ATOM 7100 CB ARG B 549 66.880 28.887 9.512 1.00 35.85

ATOM 7103 CG ARG B 549 66.645 30.056 8.558 1.00 38.41 ATOM 7106 CD ARG I3 549 67.248 29.808 7.187 1.00 39.23

ATOM 7109 NE ARG I 3 549 67.069 30.993 6.341 1.00 46.95

ATOM 7111 CZ ARG I 3 549 66.628 31.011 5.077 1.00 49.53

ATOM 7112 NHl ARG I 3 549 66.338 29.895 4.414 1.00 53.72

ATOM 7115 NH2 ARG I 3 549 66.499 32.180 4.449 1.00 50.20

ATOM 7118 C ARG I 3 549 66.310 27.698 11.621 1.00 32.83

ATOM 7119 O ARG I 3 549 67.260 27.590 12.391 1.00 32.64

ATOM 7121 N VAL I 3 550 65.419 26.738 11.417 1.00 30.30

ATOM 7122 CA VAL I 3 550 65.529 25.422 12.023 1.00 28.76

ATOM 7124 CB VAL I 3 550 64.947 25.394 13.452 1.00 27.22

ATOM 7126 CGl VAL I 3 550 63.406 25.303 13.428 1.00 27.16

ATOM 7130 CG2 VAL I 3 550 65.524 24.250 14.210 1.00 26.78

ATOM 7134 C VAL I 3 550 64.795 24.466 11.120 1.00 29.31

ATOM 7135 O VAL I 3 550 63.815 24.839 10.463 1.00 31.05

ATOM 7137 N HIS I 3 551 65.269 23.238 11.027 1.00 30.87

ATOM 7138 CA HIS I 3 551 64.595 22.296 10.152 1.00 31.20

ATOM 7140 CB HIS I 3 551 65.275 22.255 8.779 1.00 32.56

ATOM 7143 CG HIS I 3 551 66.611 21.616 8.816 1.00 34.32

ATOM 7144 NDl HIS I 3 551 66.831 20.346 8.336 1.00 42.42

ATOM 7146 CEl HIS I 3 551 68.096 20.018 8.545 1.00 43.67

ATOM 7148 NE 2 HIS I 3 551 68.694 21.022 9.163 1.00 45.71

ATOM 7150 CD2 HIS I 3 551 67.782 22.031 9.357 1.00 38.82

ATOM 7152 C HIS I 3 551 64.492 20.931 10.791 1.00 30.90

ATOM 7153 O HIS I 3 551 65.202 20.640 11.742 1.00 30.88

ATOM 7155 N CYS I 3 552 63.552 20.129 10.295 1.00 32.23

ATOM 7156 CA CYS I 3 552 63.378 18.737 10.710 1.00 34.05

ATOM 7158 CB CYS I 3 552 61.971 18.234 10.359 1.00 34.50

ATOM 7161 SG CYS I 3 552 60.648 19.271 11.036 1.00 33.87

ATOM 7163 C CYS I 3 552 64.418 17.916 9.958 1.00 36.28

ATOM 7164 O CYS I 3 552 64.215 17.543 8.795 1.00 35.58

ATOM 7166 N HIS I 3 553 65.536 17.677 10.618 1.00 38.22

ATOM 7167 CA HIS I 3 553 66.720 17.136 9.961 1.00 40.70

ATOM 7169 CB HIS I 3 553 67.989 17.533 10.733 1.00 40.99

ATOM 7172 CG HIS I 3 553 68.097 16.901 12.083 1.00 41.46

ATOM 7173 NDl HIS I 3 553 67.633 17.511 13.228 1.00 44.82

ATOM 7175 CEl HIS I 3 553 67.862 16.727 14.265 1.00 42.10

ATOM 7177 NE 2 HIS I 3 553 68.456 15.629 13.832 1.00 46.23

ATOM 7179 CD2 HIS I 3 553 68.622 15.717 12.472 1.00 43.09

ATOM 7181 C HIS I 3 553 66.696 15.621 9.790 1.00 42.70

ATOM 7182 O HIS I 3 553 67.479 15.088 8.999 1.00 44.61

ATOM 7184 N GLN I 3 554 65.827 14.925 10.518 1.00 43.56

ATOM 7185 CA GLN I 3 554 65.800 13.473 10.454 1.00 44.64

ATOM 7187 CB GLN I 3 554 65.085 12.909 11.679 1.00 44.96

ATOM 7190 CG GLN I 3 554 65.996 12.912 12.923 1.00 50.54

ATOM 7193 CD GLN I 3 554 65.283 13.237 14.232 1.00 55.67

ATOM 7194 OEl GLN I 3 554 64.485 14.176 14.309 1.00 62.11

ATOM 7195 NE 2 GLN I 3 554 65.601 12.487 15.276 1.00 57.23

ATOM 7198 C GLN I 3 554 65.175 12.984 9.152 1.00 45.56

ATOM 7199 O GLN I 3 554 64.233 13.588 8.635 1.00 45.24

ATOM 7201 N GLN I 3 555 65.723 11.902 8.598 1.00 45.75

ATOM 7202 CA GLN I 3 555 65.105 11.254 7.427 1.00 46.32

ATOM 7204 CB GLN I 3 555 65.937 10.058 6.928 1.00 46.28

ATOM 7207 CG GLN I 3 555 66.772 10.378 5.679 1.00 50.00

ATOM 7210 CD GLN I 3 555 67.754 9.265 5.307 1.00 50.60

ATOM 7211 OEl GLN I 3 555 67.437 8.065 5.410 1.00 58.68

ATOM 7212 NE 2 GLN I 3 555 68.956 9.659 4.867 1.00 54.90

ATOM 7215 C GLN I 3 555 63.648 10.836 7.701 1.00 43.49

ATOM 7216 O GLN I 3 555 63.321 10.270 8.753 1.00 42.90

ATOM 7218 N GLY I 3 556 62.775 11.168 6.755 1.00 42.05

ATOM 7219 CA GLY I 3 556 61.343 10.897 6.881 1.00 40.96

ATOM 7222 C GLY I 3 556 60.535 11.708 7.900 1.00 39.89 ATOM 7223 O GLY B 556 59.365 11.405 8.116 1.00 40.21

ATOM 7225 N HIS B 557 61.128 12.709 8.553 1.00 37.73

ATOM 7226 CA HIS B 557 60.326 13.607 9.387 1.00 37.16

ATOM 7228 CB HIS B 557 61.147 14.246 10.521 1.00 37.88

ATOM 7231 CG HIS B 557 61.278 13.355 11.718 1.00 40.02

ATOM 7232 NDl HIS B 557 61.587 12.010 11.613 1.00 45.09

ATOM 7234 CEl HIS B 557 61.624 11.472 12.819 1.00 43.02

ATOM 7236 NE2 HIS B 557 61.349 12.417 13.703 1.00 46.42

ATOM 7238 CD2 HIS B 557 61.134 13.605 13.040 1.00 44.36

ATOM 7240 C HIS B 557 59.638 14.638 8.491 1.00 34.96

ATOM 7241 O HIS B 557 60.200 15.055 7.456 1.00 35.38

ATOM 7243 N VAL B 558 58.390 14.967 8.838 1.00 31.17

ATOM 7244 CA VAL B 558 57.642 16.010 8.151 1.00 28.07

ATOM 7246 CB VAL B 558 56.244 15.513 7.652 1.00 28.10

ATOM 7248 CGl VAL B 558 56.391 14.245 6.819 1.00 27.56

ATOM 7252 CG2 VAL B 558 55.345 15.221 8.828 1.00 28.34

ATOM 7256 C VAL B 558 57.479 17.196 9.091 1.00 25.89

ATOM 7257 O VAL B 558 57.209 17.029 10.277 1.00 23.32

ATOM 7259 N LEU B 559 57.637 18.392 8.542 1.00 23.34

ATOM 7260 CA LEU B 559 57.340 19.611 9.261 1.00 22.66

ATOM 7262 CB LEU B 559 58.087 20.766 8.666 1.00 22.72

ATOM 7265 CG LEU B 559 57.746 22.151 9.199 1.00 21.75

ATOM 7267 CDl LEU B 559 58.340 22.330 10.573 1.00 18.34

ATOM 7271 CD2 LEU B 559 58.245 23.173 8.218 1.00 21.65

ATOM 7275 C LEU B 559 55.830 19.866 9.163 1.00 21.71

ATOM 7276 O LEU B 559 55.230 19.879 8.059 1.00 20.72

ATOM 7278 N THR B 560 55.214 20.041 10.318 1.00 19.49

ATOM 7279 CA THR B 560 53.772 20.246 10.398 1.00 19.18

ATOM 7281 CB THR B 560 53.135 19.254 11.406 1.00 21.35

ATOM 7283 OGl THR B 560 53.621 19.542 12.732 1.00 19.91

ATOM 7285 CG2 THR B 560 53.473 17.797 11.056 1.00 18.11

ATOM 7289 C THR B 560 53.389 21.663 10.861 1.00 19.85

ATOM 7290 O THR B 560 52.208 22.063 10.742 1.00 19.34

ATOM 7292 N GLY B 561 54.369 22.430 11.362 1.00 19.24

ATOM 7293 CA GLY B 561 54.090 23.697 12.003 1.00 19.49

ATOM 7296 C GLY B 561 55.361 24.437 12.317 1.00 20.05

ATOM 7297 O GLY B 561 56.367 23.818 12.762 1.00 18.07

ATOM 7299 N CYS B 562 55.330 25.747 12.052 1.00 22.17

ATOM 7300 CA CYS B 562 56.357 26.686 12.495 1.00 22.84

ATOM 7302 CB CYS B 562 56.915 27.482 11.307 1.00 24.91

ATOM 7305 SG CYS B 562 57.647 26.424 10.057 1.00 27.28

ATOM 7307 C CYS B 562 55.803 27.703 13.504 1.00 22.52

ATOM 7308 O CYS B 562 54.725 28.253 13.292 1.00 22.43

ATOM 7310 N SER B 563 56.561 27.966 14.565 1.00 20.03

ATOM 7311 CA SER B 563 56.293 29.042 15.520 1.00 19.92

ATOM 7313 CB SER B 563 55.884 28.474 16.875 1.00 21.04

ATOM 7316 OG SER B 563 54.704 27.683 16.754 1.00 20.98

ATOM 7318 C SER B 563 57.548 29.879 15.733 1.00 22.06

ATOM 7319 O SER B 563 58.663 29.436 15.466 1.00 20.37

ATOM 7321 N SER B 564 57.368 31.079 16.265 1.00 21.39

ATOM 7322 CA SER B 564 58.483 31.979 16.528 1.00 22.99

ATOM 7324 CB SER B 564 58.766 32.855 15.332 1.00 22.04

ATOM 7327 OG SER B 564 59.948 33.625 15.523 1.00 26.63

ATOM 7329 C SER B 564 58.094 32.832 17.718 1.00 24.67

ATOM 7330 O SER B 564 56.951 33.296 17.793 1.00 26.28

ATOM 7332 N HIS B 565 58.994 32.993 18.672 1.00 24.56

ATOM 7333 CA HIS B 565 58.799 34.021 19.689 1.00 24.85

ATOM 7335 CB HIS B 565 58.397 33.434 21.034 1.00 24.33

ATOM 7338 CG HIS B 565 59.540 32.896 21.820 1.00 27.10

ATOM 7339 NDl HIS B 565 60.193 31.736 21.470 1.00 25.99

ATOM 7341 CEl HIS B 565 61.177 31.511 22.324 1.00 29.49 ATOM 7343 NE 2 HIS I3 565 61.183 32.488 23.217 1.00 29.61

ATOM 7345 CD2 HIS I 3 565 60.177 33.374 22.917 1.00 34.51

ATOM 7347 C HIS I 3 565 60.065 34.872 19.800 1.00 27.65

ATOM 7348 O HIS I 3 565 61.138 34.443 19.407 1.00 24.24

ATOM 7350 N TRP I 3 566 59.916 36.080 20.329 1.00 29.70

ATOM 7351 CA TRP I 3 566 61.053 36.954 20.537 1.00 34.20

ATOM 7353 CB TRP I 3 566 61.121 38.030 19.431 1.00 35.05

ATOM 7356 CG TRP I 3 566 59.820 38.716 19.107 1.00 36.86

ATOM 7357 CDl TRP I 3 566 59.402 39.935 19.579 1.00 38.44

ATOM 7359 NEl TRP I 3 566 58.157 40.237 19.067 1.00 39.48

ATOM 7361 CE 2 TRP I 3 566 57.744 39.213 18.246 1.00 38.11

ATOM 7362 CD2 TRP I 3 566 58.758 38.229 18.255 1.00 38.82

ATOM 7363 CE 3 TRP I 3 566 58.568 37.058 17.500 1.00 38.19

ATOM 7365 CZ3 TRP I 3 566 57.380 36.915 16.769 1.00 37.47

ATOM 7367 CH2 TRP I 3 566 56.394 37.907 16.790 1.00 36.50

ATOM 7369 CZ 2 TRP I 3 566 56.555 39.061 17.521 1.00 37.39

ATOM 7371 C TRP I 3 566 61.006 37.538 21.963 1.00 38.57

ATOM 7372 O TRP I 3 566 59.967 37.510 22.639 1.00 37.29

ATOM 7374 N GLU I 3 567 62.152 38.011 22.435 1.00 43.02

ATOM 7375 CA GLU I 3 567 62.235 38.612 23.760 1.00 46.95

ATOM 7377 CB GLU I 3 567 63.253 37.845 24.619 1.00 47.48

ATOM 7380 CG GLU I 3 567 62.610 36.649 25.348 1.00 49.99

ATOM 7383 CD GLU I 3 567 63.513 35.429 25.493 1.00 56.28

ATOM 7384 OEl GLU I 3 567 63.936 35.133 26.632 1.00 57.84

ATOM 7385 OE 2 GLU I 3 567 63.779 34.742 24.477 1.00 60.75

ATOM 7386 C GLU I 3 567 62.523 40.108 23.662 1.00 50.36

ATOM 7387 O GLU I 3 567 62.491 40.810 24.659 1.00 51.61

ATOM 7389 N VAL I 3 568 62.735 40.591 22.442 1.00 54.58

ATOM 7390 CA VAL I 3 568 63.024 41.995 22.189 1.00 57.92

ATOM 7392 CB VAL I 3 568 63.759 42.195 20.825 1.00 58.32

ATOM 7394 CGl VAL I 3 568 62.837 41.876 19.641 1.00 59.07

ATOM 7398 CG2 VAL I 3 568 64.314 43.617 20.712 1.00 60.67

ATOM 7402 C VAL I 3 568 61.740 42.802 22.189 1.00 60.35

ATOM 7403 O VAL I 3 568 60.654 42.274 21.923 1.00 60.39

ATOM 7405 N GLU I 3 569 61.880 44.089 22.488 1.00 63.71

ATOM 7406 CA GLU I 3 569 60.750 45.012 22.505 1.00 66.03

ATOM 7408 CB GLU I 3 569 61.138 46.348 23.158 1.00 66.74

ATOM 7411 CG GLU I 3 569 61.877 46.239 24.518 1.00 69.38

ATOM 7414 CD GLU I 3 569 61.171 45.345 25.536 1.00 72.81

ATOM 7415 OEl GLU I 3 569 59.942 45.129 25.415 1.00 75.35

ATOM 7416 OE 2 GLU I 3 569 61.856 44.863 26.471 1.00 75.21

ATOM 7417 C GLU I 3 569 60.212 45.245 21.096 1.00 67.24

ATOM 7418 O GLU I 3 569 59.009 45.379 20.918 1.00 67.29

ATOM 7420 N ASP I 3 570 61.098 45.288 20.102 1.00 68.97

ATOM 7421 CA ASP I 3 570 60.672 45.331 18.697 1.00 70.39

ATOM 7423 CB ASP I 3 570 60.153 46.733 18.336 1.00 70.74

ATOM 7426 CG ASP I 3 570 58.961 46.691 17.386 1.00 73.17

ATOM 7427 ODl ASP I 3 570 58.915 45.785 16.521 1.00 76.39

ATOM 7428 OD2 ASP I 3 570 58.067 47.563 17.507 1.00 74.69

ATOM 7429 C ASP I 3 570 61.791 44.909 17.731 1.00 70.85

ATOM 7430 O ASP I 3 570 62.950 44.764 18.136 1.00 71.17

ATOM 7432 N LEU I 3 571 61.433 44.706 16.462 1.00 71.43

ATOM 7433 CA LEU I 3 571 62.395 44.286 15.434 1.00 72.11

ATOM 7435 CB LEU I 3 571 61.680 43.867 14.137 1.00 72.40

ATOM 7438 CG LEU I 3 571 60.721 44.830 13.410 1.00 73.14

ATOM 7440 CDl LEU I 3 571 61.010 46.311 13.678 1.00 73.57

ATOM 7444 CD2 LEU I 3 571 60.715 44.527 11.897 1.00 72.57

ATOM 7448 C LEU I 3 571 63.431 45.367 15.127 1.00 72.21

ATOM 7449 O LEU I 3 571 63.991 45.412 14.030 1.00 72.23

ATOM 7451 N GLN I 3 584 62.379 25.744 1.407 1.00 56.02

ATOM 7452 CA GLN I 3 584 63.337 24.660 1.602 1.00 56.16 ATOM 7454 CB GLN I3 584 64.683 25.211 2.085 1.00 56.39

ATOM 7457 CG GLN I 3 584 65.454 25.921 0.965 1.00 57.67

ATOM 7460 CD GLN I 3 584 66.659 26.706 1.463 1.00 58.25

ATOM 7461 OEl GLN I 3 584 66.838 26.897 2.666 1.00 61.74

ATOM 7462 NE 2 GLN I 3 584 67.496 27.167 0.530 1.00 59.48

ATOM 7465 C GLN I 3 584 62.770 23.639 2.588 1.00 54.32

ATOM 7466 O GLN I 3 584 62.605 23.958 3.764 1.00 54.64

ATOM 7468 N PRO I 3 585 62.454 22.419 2.098 1.00 51.66

ATOM 7469 CA PRO I 3 585 61.749 21.363 2.830 1.00 49.24

ATOM 7471 CB PRO I 3 585 62.171 20.090 2.086 1.00 49.60

ATOM 7474 CG PRO I 3 585 62.301 20.522 0.691 1.00 51.27

ATOM 7477 CD PRO I 3 585 62.773 21.970 0.722 1.00 51.85

ATOM 7480 C PRO I 3 585 62.052 21.210 4.322 1.00 45.42

ATOM 7481 O PRO I 3 585 63.198 21.072 4.742 1.00 44.45

ATOM 7482 N ASN I 3 586 60.984 21.229 5.102 1.00 41.52

ATOM 7483 CA ASN I 3 586 61.043 20.955 6.517 1.00 38.48

ATOM 7485 CB ASN I 3 586 61.600 19.551 6.760 1.00 38.05

ATOM 7488 CG ASN I 3 586 60.677 18.457 6.239 1.00 39.25

ATOM 7489 ODl ASN I 3 586 59.507 18.694 5.927 1.00 39.28

ATOM 7490 ND2 ASN I 3 586 61.197 17.240 6.169 1.00 44.47

ATOM 7493 C ASN I 3 586 61.796 22.012 7.307 1.00 35.80

ATOM 7494 O ASN I 3 586 62.251 21.751 8.415 1.00 35.48

ATOM 7496 N GLN I 3 587 61.857 23.225 6.758 1.00 33.33

ATOM 7497 CA GLN I 3 587 62.532 24.338 7.382 1.00 32.17

ATOM 7499 CB GLN I 3 587 63.608 24.906 6.451 1.00 32.75

ATOM 7502 CG GLN I 3 587 64.567 25.861 7.155 1.00 34.61

ATOM 7505 CD GLN I 3 587 65.786 26.221 6.322 1.00 35.30

ATOM 7506 OEl GLN I 3 587 65.659 26.750 5.218 1.00 42.19

ATOM 7507 NE 2 GLN I 3 587 66.970 25.988 6.874 1.00 38.72

ATOM 7510 C GLN I 3 587 61.551 25.450 7.744 1.00 30.29

ATOM 7511 O GLN I 3 587 60.684 25.816 6.942 1.00 29.16

ATOM 7513 N CYS I 3 588 61.711 25.984 8.956 1.00 28.33

ATOM 7514 CA CYS I 3 588 61.020 27.184 9.394 1.00 26.42

ATOM 7516 CB CYS I 3 588 60.498 27.006 10.831 1.00 26.26

ATOM 7519 SG CYS I 3 588 59.341 25.709 10.959 1.00 24.76

ATOM 7521 C CYS I 3 588 62.015 28.326 9.392 1.00 27.89

ATOM 7522 O CYS I 3 588 63.172 28.149 9.751 1.00 28.85

ATOM 7524 N VAL I 3 589 61.552 29.512 9.041 1.00 29.33

ATOM 7525 CA VAL I 3 589 62.388 30.703 9.042 1.00 30.89

ATOM 7527 CB VAL I 3 589 62.637 31.181 7.610 1.00 32.17

ATOM 7529 CGl VAL I 3 589 63.355 32.533 7.613 1.00 33.61

ATOM 7533 CG2 VAL I 3 589 63.403 30.103 6.833 1.00 31.87

ATOM 7537 C VAL I 3 589 61.691 31.810 9.827 1.00 31.50

ATOM 7538 O VAL I 3 589 60.508 32.092 9.604 1.00 33.60

ATOM 7540 N GLY I 3 590 62.408 32.397 10.772 1.00 30.85

ATOM 7541 CA GLY I 3 590 61.909 33.512 11.520 1.00 31.31

ATOM 7544 C GLY I 3 590 62.770 34.747 11.336 1.00 32.69

ATOM 7545 O GLY I 3 590 63.804 34.721 10.632 1.00 30.87

ATOM 7547 N HIS I 3 591 62.338 35.821 11.999 1.00 33.83

ATOM 7548 CA HIS I 3 591 63.113 37.043 12.113 1.00 35.87

ATOM 7550 CB HIS I 3 591 62.321 38.109 12.880 1.00 36.91

ATOM 7553 CG HIS I 3 591 62.883 39.487 12.739 1.00 41.60

ATOM 7554 NDl HIS I 3 591 63.969 39.930 13.464 1.00 48.58

ATOM 7556 CEl HIS I 3 591 64.249 41.176 13.122 1.00 48.36

ATOM 7558 NE 2 HIS I 3 591 63.386 41.556 12.197 1.00 50.21

ATOM 7560 CD2 HIS I 3 591 62.519 40.519 11.942 1.00 47.54

ATOM 7562 C HIS I 3 591 64.425 36.751 12.840 1.00 35.86

ATOM 7563 O HIS I 3 591 64.472 35.888 13.713 1.00 36.13

ATOM 7565 N ARG I 3 592 65.475 37.504 12.496 1.00 36.07

ATOM 7566 CA ARG I 3 592 66.826 37.266 13.006 1.00 36.33

ATOM 7568 CB ARG I 3 592 67.832 38.194 12.310 1.00 38.05 ATOM 7571 CG ARG I3 592 67.663 39.668 12.701 1.00 42.69

ATOM 7574 CD ARG I 3 592 68.178 40.616 11.621 1.00 50.90

ATOM 7577 NE ARG I 3 592 69.628 40.820 11.675 1.00 54.79

ATOM 7579 CZ ARG I 3 592 70.344 41.386 10.698 1.00 57.37

ATOM 7580 NHl ARG I 3 592 69.755 41.791 9.573 1.00 58.59

ATOM 7583 NH2 ARG I 3 592 71.659 41.527 10.831 1.00 56.33

ATOM 7586 C ARG I 3 592 66.933 37.453 14.499 1.00 35.61

ATOM 7587 O ARG I 3 592 67.789 36.862 15.128 1.00 36.12

ATOM 7589 N GLU I 3 593 66.030 38.254 15.065 1.00 34.37

ATOM 7590 CA GLU I 3 593 66.011 38.527 16.490 1.00 33.51

ATOM 7592 CB GLU I 3 593 65.609 39.982 16.704 1.00 33.65

ATOM 7595 CG GLU I 3 593 66.474 40.967 15.947 1.00 39.34

ATOM 7598 CD GLU I 3 593 66.132 42.395 16.311 1.00 46.59

ATOM 7599 OEl GLU I 3 593 65.534 43.095 15.464 1.00 48.10

ATOM 7600 OE2 GLU I 3 593 66.437 42.792 17.469 1.00 54.07

ATOM 7601 C GLU I 3 593 65.035 37.642 17.228 1.00 30.76

ATOM 7602 O GLU I 3 593 64.845 37.802 18.435 1.00 31.26

ATOM 7604 N ALA I 3 594 64.430 36.693 16.510 1.00 28.22

ATOM 7605 CA ALA I 3 594 63.406 35.804 17.077 1.00 26.81

ATOM 7607 CB ALA I 3 594 62.171 35.838 16.201 1.00 26.82

ATOM 7611 C ALA I 3 594 63.915 34.378 17.129 1.00 25.53

ATOM 7612 O ALA I 3 594 64.730 33.986 16.281 1.00 23.76

ATOM 7614 N SER I 3 595 63.406 33.610 18.089 1.00 21.87

ATOM 7615 CA SER I 3 595 63.602 32.173 18.113 1.00 21.76

ATOM 7617 CB SER I 3 595 63.399 31.619 19.518 1.00 22.39

ATOM 7620 OG SER I 3 595 64.303 32.169 20.445 1.00 27.99

ATOM 7622 C SER I 3 595 62.600 31.511 17.169 1.00 23.73

ATOM 7623 O SER I 3 595 61.515 32.039 16.923 1.00 24.41

ATOM 7625 N ILE I 3 596 62.953 30.351 16.638 1.00 22.63

ATOM 7626 CA ILE I 3 596 62.139 29.701 15.648 1.00 21.28

ATOM 7628 CB ILE I 3 596 62.778 29.788 14.252 1.00 21.63

ATOM 7630 CGl ILE I 3 596 61.806 29.313 13.186 1.00 23.75

ATOM 7633 CDl ILE I 3 596 60.709 30.346 12.879 1.00 21.83

ATOM 7637 CG2 ILE I 3 596 64.028 28.961 14.154 1.00 28.31

ATOM 7641 C ILE I 3 596 61.949 28.283 16.143 1.00 21.31

ATOM 7642 O ILE I 3 596 62.889 27.664 16.691 1.00 19.06

ATOM 7644 N HIS I 3 597 60.728 27.777 15.984 1.00 19.10

ATOM 7645 CA HIS I 3 597 60.356 26.466 16.501 1.00 20.77

ATOM 7647 CB HIS I 3 597 59.426 26.598 17.702 1.00 21.37

ATOM 7650 CG HIS I 3 597 59.863 27.619 18.689 1.00 23.99

ATOM 7651 NDl HIS I 3 597 60.868 27.382 19.602 1.00 23.82

ATOM 7653 CEl HIS I 3 597 61.039 28.455 20.352 1.00 25.41

ATOM 7655 NE2 HIS I 3 597 60.177 29.374 19.962 1.00 20.86

ATOM 7657 CD2 HIS I 3 597 59.428 28.876 18.923 1.00 24.36

ATOM 7659 C HIS I 3 597 59.648 25.696 15.405 1.00 21.37

ATOM 7660 O HIS I 3 597 58.708 26.213 14.813 1.00 22.87

ATOM 7662 N ALA I 3 598 60.083 24.466 15.156 1.00 21.52

ATOM 7663 CA ALA I 3 598 59.490 23.612 14.131 1.00 20.51

ATOM 7665 CB ALA I 3 598 60.535 23.194 13.129 1.00 22.60

ATOM 7669 C ALA I 3 598 58.868 22.399 14.824 1.00 19.57

ATOM 7670 O ALA I 3 598 59.482 21.798 15.708 1.00 20.83

ATOM 7672 N SER I 3 599 57.644 22.058 14.465 1.00 17.63

ATOM 7673 CA SER I 3 599 57.049 20.813 14.882 1.00 17.41

ATOM 7675 CB SER I 3 599 55.525 20.912 15.008 1.00 18.08

ATOM 7678 OG SER I 3 599 54.947 19.593 15.087 1.00 19.22

ATOM 7680 C SER I 3 599 57.372 19.809 13.811 1.00 18.93

ATOM 7681 O SER I 3 599 56.944 19.972 12.665 1.00 18.34

ATOM 7683 N CYS I 3 600 58.089 18.764 14.201 1.00 20.64

ATOM 7684 CA CYS I 3 600 58.590 17.730 13.306 1.00 24.30

ATOM 7686 CB CYS I 3 600 60.107 17.637 13.454 1.00 24.08

ATOM 7689 SG CYS I 3 600 60.923 19.177 13.025 1.00 30.39 ATOM 7691 C CYS B 600 58.005 16.419 13.758 1.00 26.04

ATOM 7692 O CYS B 600 58.206 16.054 14.905 1.00 25.85

ATOM 7694 N CYS B 601 57.316 15.711 12.873 1.00 27.73

ATOM 7695 CA CYS B 601 56.727 14.414 13.213 1.00 28.38

ATOM 7697 CB CYS B 601 55.210 14.450 13.049 1.00 29.10

ATOM 7700 SG CYS B 601 54.392 15.669 14.040 1.00 31.91

ATOM 7702 C CYS B 601 57.219 13.310 12.318 1.00 30.16

ATOM 7703 O CYS B 601 57.351 13.504 11.120 1.00 30.42

ATOM 7705 N HIS B 602 57.462 12.144 12.893 1.00 32.21

ATOM 7706 CA HIS B 602 57.587 10.961 12.091 1.00 34.64

ATOM 7708 CB HIS B 602 58.640 9.992 12.622 1.00 36.98

ATOM 7711 CG HIS B 602 59.084 8.991 11.600 1.00 42.26

ATOM 7712 NDl HIS B 602 59.415 9.350 10.308 1.00 50.51

ATOM 7714 CEl HIS B 602 59.747 8.271 9.623 1.00 48.34

ATOM 7716 NE2 HIS B 602 59.638 7.222 10.422 1.00 51.94

ATOM 7718 CD2 HIS B 602 59.216 7.643 11.662 1.00 48.81

ATOM 7720 C HIS B 602 56.203 10.350 12.055 1.00 35.14

ATOM 7721 O HIS B 602 55.676 9.883 13.064 1.00 33.24

ATOM 7723 N ALA B 603 55.599 10.436 10.878 1.00 37.63

ATOM 7724 CA ALA B 603 54.228 10.007 10.663 1.00 39.27

ATOM 7726 CB ALA B 603 53.268 11.193 10.792 1.00 38.66

ATOM 7730 C ALA B 603 54.243 9.430 9.248 1.00 41.12

ATOM 7731 O ALA B 603 53.990 10.137 8.263 1.00 42.10

ATOM 7733 N PRO B 604 54.598 8.149 9.140 1.00 43.23

ATOM 7734 CA PRO B 604 54.983 7.623 7.839 1.00 43.65

ATOM 7736 CB PRO B 604 55.552 6.229 8.156 1.00 44.26

ATOM 7739 CG PRO B 604 55.640 6.151 9.683 1.00 45.04

ATOM 7742 CD PRO B 604 54.631 7.119 10.196 1.00 43.95

ATOM 7745 C PRO B 604 53.804 7.562 6.870 1.00 43.14

ATOM 7746 O PRO B 604 54.013 7.699 5.662 1.00 43.76

ATOM 7747 N GLY B 605 52.587 7.411 7.388 1.00 41.13

ATOM 7748 CA GLY B 605 51.403 7.524 6.540 1.00 41.40

ATOM 7751 C GLY B 605 51.013 8.944 6.119 1.00 40.84

ATOM 7752 O GLY B 605 49.932 9.147 5.552 1.00 42.03

ATOM 7754 N LEU B 606 51.876 9.929 6.372 1.00 38.58

ATOM 7755 CA LEU B 606 51.484 11.316 6.252 1.00 37.46

ATOM 7757 CB LEU B 606 51.808 12.049 7.553 1.00 37.68

ATOM 7760 CG LEU B 606 50.852 13.164 7.933 1.00 40.49

ATOM 7762 CDl LEU B 606 49.464 12.539 8.215 1.00 42.92

ATOM 7766 CD2 LEU B 606 51.385 13.918 9.126 1.00 38.22

ATOM 7770 C LEU B 606 52.239 11.972 5.117 1.00 35.91

ATOM 7771 O LEU B 606 53.454 11.903 5.078 1.00 35.68

ATOM 7773 N GLU B 607 51.512 12.604 4.203 1.00 35.19

ATOM 7774 CA GLU B 607 52.105 13.484 3.200 1.00 34.78

ATOM 7776 CB GLU B 607 51.599 13.099 1.821 1.00 34.12

ATOM 7779 CG GLU B 607 51.972 14.079 0.706 1.00 38.00

ATOM 7782 CD GLU B 607 51.430 13.670 -0.665 1.00 38.16

ATOM 7783 OEl GLU B 607 50.550 12.775 -0.725 1.00 49.24

ATOM 7784 OE2 GLU B 607 51.874 14.255 -1.679 1.00 38.55

ATOM 7785 C GLU B 607 51.718 14.922 3.553 1.00 32.17

ATOM 7786 O GLU B 607 50.580 15.160 3.957 1.00 32.46

ATOM 7788 N CYS B 608 52.666 15.854 3.456 1.00 29.30

ATOM 7789 CA CYS B 608 52.403 17.287 3.649 1.00 27.97

ATOM 7791 CB CYS B 608 52.983 17.815 4.969 1.00 27.60

ATOM 7794 SG CYS B 608 52.463 16.906 6.423 1.00 30.83

ATOM 7796 C CYS B 608 52.969 18.130 2.522 1.00 26.36

ATOM 7797 O CYS B 608 54.033 17.836 1.983 1.00 27.36

ATOM 7799 N LYS B 609 52.284 19.204 2.191 1.00 25.17

ATOM 7800 CA LYS B 609 52.795 20.182 1.256 1.00 25.89

ATOM 7802 CB LYS B 609 52.107 20.075 -0.118 1.00 26.42

ATOM 7805 CG LYS B 609 52.333 18.719 -0.832 1.00 28.71 ATOM 7808 CD LYS B 609 51.723 18.750 -2.260 1.00 27.25

ATOM 7811 CE LYS B 609 52.206 17.619 -3.090 1.00 25.92

ATOM 7814 NZ LYS B 609 51.373 17.454 -4.316 1.00 29.43

ATOM 7818 C LYS B 609 52.593 21.562 1.852 1.00 25.21

ATOM 7819 O LYS B 609 51.830 21.712 2.771 1.00 25.27

ATOM 7821 N VAL B 610 53.289 22.560 1.317 1.00 25.23

ATOM 7822 CA VAL B 610 53.171 23.928 1.784 1.00 26.04

ATOM 7824 CB VAL B 610 54.523 24.472 2.223 1.00 27.24

ATOM 7826 CGl VAL B 610 54.388 25.904 2.688 1.00 27.01

ATOM 7830 CG2 VAL B 610 55.111 23.577 3.303 1.00 25.03

ATOM 7834 C VAL B 610 52.629 24.806 0.693 1.00 27.51

ATOM 7835 O VAL B 610 53.163 24.842 -0.395 1.00 26.11

ATOM 7837 N LYS B 611 51.570 25.550 1.010 1.00 28.18

ATOM 7838 CA LYS B 611 50.934 26.425 0.069 1.00 29.18

ATOM 7840 CB LYS B 611 49.485 25.979 -0.110 1.00 30.67

ATOM 7843 CG LYS B 611 48.727 26.684 -1.201 1.00 29.54

ATOM 7846 CD LYS B 611 47.334 26.093 -1.348 1.00 30.26

ATOM 7849 CE LYS B 611 46.448 26.976 -2.250 1.00 30.63

ATOM 7852 NZ LYS B 611 45.093 26.388 -2.499 1.00 27.42

ATOM 7856 C LYS B 611 51.034 27.848 0.636 1.00 30.46

ATOM 7857 O LYS B 611 50.747 28.083 1.813 1.00 28.08

ATOM 7859 N GLU B 612 51.483 28.763 -0.208 1.00 32.32

ATOM 7860 CA GLU B 612 51.774 30.140 0.167 1.00 35.16

ATOM 7862 CB GLU B 612 53.191 30.511 -0.233 1.00 35.69

ATOM 7865 CG GLU B 612 54.234 30.142 0.747 1.00 41.09

ATOM 7868 CD GLU B 612 55.569 30.763 0.388 1.00 46.41

ATOM 7869 OEl GLU B 612 55.660 31.392 -0.693 1.00 51.85

ATOM 7870 OE 2 GLU B 612 56.511 30.629 1.191 1.00 50.27

ATOM 7871 C GLU B 612 50.876 31.064 -0.600 1.00 36.47

ATOM 7872 O GLU B 612 50.492 30.767 -1.728 1.00 36.01

ATOM 7874 N HIS B 613 50.545 32.195 0.001 1.00 38.61

ATOM 7875 CA HIS B 613 49.906 33.254 -0.746 1.00 40.72

ATOM 7877 CB HIS B 613 48.401 33.041 -0.825 1.00 40.55

ATOM 7880 CG HIS B 613 47.695 34.094 -1.621 1.00 43.13

ATOM 7881 NDl HIS B 613 46.529 34.696 -1.201 1.00 43.95

ATOM 7883 CEl HIS B 613 46.154 35.590 -2.098 1.00 46.23

ATOM 7885 NE 2 HIS B 613 47.047 35.604 -3.072 1.00 43.38

ATOM 7887 CD2 HIS B 613 48.018 34.676 -2.800 1.00 42.73

ATOM 7889 C HIS B 613 50.208 34.581 -0.102 1.00 42.45

ATOM 7890 O HIS B 613 50.066 34.722 1.109 1.00 42.16

ATOM 7892 N GLY B 614 50.624 35.551 -0.911 1.00 45.04

ATOM 7893 CA GLY B 614 50.913 36.889 -0.404 1.00 47.66

ATOM 7896 C GLY B 614 50.371 37.999 -1.282 1.00 50.20

ATOM 7897 O GLY B 614 50.198 37.816 -2.491 1.00 49.70

ATOM 7899 N ILE B 615 50.113 39.154 -0.663 1.00 53.29

ATOM 7900 CA ILE B 615 49.542 40.325 -1.347 1.00 55.96

ATOM 7902 CB ILE B 615 47.975 40.336 -1.282 1.00 55.55

ATOM 7904 CGl ILE B 615 47.459 39.897 0.090 1.00 55.94

ATOM 7907 CDl ILE B 615 45.945 39.638 0.132 1.00 55.92

ATOM 7911 CG2 ILE B 615 47.381 39.430 -2.346 1.00 56.08

ATOM 7915 C ILE B 615 50.102 41.630 -0.750 1.00 57.62

ATOM 7916 O ILE B 615 50.722 41.605 0.320 1.00 58.10

ATOM 7918 N PRO B 616 49.928 42.769 -1.464 1.00 59.55

ATOM 7919 CA PRO B 616 50.155 44.137 -0.937 1.00 59.73

ATOM 7921 CB PRO B 616 49.267 44.987 -1.848 1.00 60.02

ATOM 7924 CG PRO B 616 49.400 44.301 -3.185 1.00 59.95

ATOM 7927 CD PRO B 616 49.551 42.810 -2.894 1.00 59.58

ATOM 7930 C PRO B 616 49.774 44.360 0.534 1.00 60.98

ATOM 7931 O PRO B 616 49.203 45.404 0.882 1.00 62.52

ATOM 7932 N GLN B 619 46.759 45.836 3.519 1.00 59.36

ATOM 7933 CA GLN B 619 45.968 44.608 3.459 1.00 59.16 ATOM 7935 CB GLN B 619 46.680 43.580 2.584 1.00 59.51

ATOM 7938 CG GLN B 619 46.478 43.815 1.102 1.00 61.41

ATOM 7941 CD GLN B 619 45.064 43.486 0.659 1.00 64.36

ATOM 7942 OEl GLN B 619 44.153 44.306 0.787 1.00 64.94

ATOM 7943 NE2 GLN B 619 44.874 42.278 0.132 1.00 64.67

ATOM 7946 C GLN B 619 45.700 44.030 4.853 1.00 58.05

ATOM 7947 O GLN B 619 46.631 43.684 5.580 1.00 59.21

ATOM 7949 N GLU B 620 44.422 43.920 5.210 1.00 56.27

ATOM 7950 CA GLU B 620 44.009 43.576 6.582 1.00 54.77

ATOM 7952 CB GLU B 620 42.571 44.035 6.819 1.00 54.67

ATOM 7955 CG GLU B 620 42.125 43.916 8.275 1.00 57.90

ATOM 7958 CD GLU B 620 40.892 44.770 8.603 1.00 58.49

ATOM 7959 OEl GLU B 620 40.116 45.103 7.670 1.00 66.06

ATOM 7960 OE 2 GLU B 620 40.703 45.105 9.799 1.00 65.28

ATOM 7961 C GLU B 620 44.110 42.086 6.910 1.00 51.10

ATOM 7962 O GLU B 620 44.260 41.703 8.070 1.00 50.70

ATOM 7964 N GLN B 621 44.011 41.254 5.879 1.00 47.32

ATOM 7965 CA GLN B 621 43.913 39.825 6.063 1.00 43.49

ATOM 7967 CB GLN B 621 42.479 39.482 6.411 1.00 43.62

ATOM 7970 CG GLN B 621 42.119 38.037 6.374 1.00 43.19

ATOM 7973 CD GLN B 621 40.709 37.807 6.849 1.00 41.44

ATOM 7974 OEl GLN B 621 40.338 38.181 7.964 1.00 41.89

ATOM 7975 NE 2 GLN B 621 39.910 37.199 6.005 1.00 36.04

ATOM 7978 C GLN B 621 44.311 39.150 4.772 1.00 41.07

ATOM 7979 O GLN B 621 43.799 39.499 3.715 1.00 39.40

ATOM 7981 N VAL B 622 45.244 38.206 4.863 1.00 37.62

ATOM 7982 CA VAL B 622 45.574 37.362 3.731 1.00 35.15

ATOM 7984 CB VAL B 622 47.036 37.595 3.168 1.00 35.96

ATOM 7986 CGl VAL B 622 47.306 36.690 1.959 1.00 34.83

ATOM 7990 CG2 VAL B 622 48.086 37.401 4.227 1.00 37.41

ATOM 7994 C VAL B 622 45.288 35.925 4.125 1.00 33.27

ATOM 7995 O VAL B 622 45.335 35.550 5.306 1.00 31.27

ATOM 7997 N THR B 623 44.974 35.133 3. Ill 1.00 30.95

ATOM 7998 CA THR B 623 44.277 33.892 3.289 1.00 29.83

ATOM 8000 CB THR B 623 42.792 34.229 3.105 1.00 31.63

ATOM 8002 OGl THR B 623 42.159 34.379 4.397 1.00 30.90

ATOM 8004 CG2 THR B 623 42.077 33.248 2.231 1.00 24.31

ATOM 8008 C THR B 623 44.785 32.858 2.270 1.00 30.04

ATOM 8009 O THR B 623 45.012 33.173 1.104 1.00 30.15

ATOM 8011 N VAL B 624 44.998 31.635 2.731 1.00 28.31

ATOM 8012 CA VAL B 624 45.397 30.547 1.870 1.00 26.95

ATOM 8014 CB VAL B 624 46.937 30.489 1.674 1.00 28.01

ATOM 8016 CGl VAL B 624 47.295 29.592 0.442 1.00 24.90

ATOM 8020 CG2 VAL B 624 47.661 30.042 2.927 1.00 27.12

ATOM 8024 C VAL B 624 44.831 29.251 2.423 1.00 26.88

ATOM 8025 O VAL B 624 44.958 28.973 3.637 1.00 26.95

ATOM 8027 N ALA B 625 44.180 28.496 1.535 1.00 24.89

ATOM 8028 CA ALA B 625 43.480 27.275 1.871 1.00 25.71

ATOM 8030 CB ALA B 625 42.046 27.343 1.356 1.00 26.60

ATOM 8034 C ALA B 625 44.169 26.033 1.317 1.00 26.80

ATOM 8035 O ALA B 625 44.684 26.020 0.177 1.00 25.90

ATOM 8037 N CYS B 626 44.169 24.987 2.129 1.00 25.95

ATOM 8038 CA CYS B 626 44.537 23.670 1.661 1.00 26.55

ATOM 8040 CB CYS B 626 44.576 22.665 2.804 1.00 26.39

ATOM 8043 SG CYS B 626 45.749 23.105 4.071 1.00 30.72

ATOM 8045 C CYS B 626 43.519 23.163 0.653 1.00 26.62

ATOM 8046 O CYS B 626 42.349 23.541 0.660 1.00 24.12

ATOM 8048 N GLU B 627 43.970 22.216 -0.148 1.00 28.08

ATOM 8049 CA GLU B 627 43.130 21.622 -1.156 1.00 29.55

ATOM 8051 CB GLU B 627 43.986 20.921 -2.230 1.00 30.48

ATOM 8054 CG GLU B 627 45.062 21.854 -2.861 1.00 30.20 ATOM 8057 CD GLU B 627 44.494 23.104 -3.511 1.00 31.55

ATOM 8058 OEl GLU B 627 43.273 23.168 -3.778 1.00 39.95

ATOM 8059 OE2 GLU B 627 45.276 24.041 -3.762 1.00 34.28

ATOM 8060 C GLU B 627 42.209 20.666 -0.465 1.00 30.43

ATOM 8061 O GLU B 627 42.523 20.130 0.606 1.00 30.08

ATOM 8063 N GLU B 628 41.057 20.460 -1.087 1.00 31.59

ATOM 8064 CA GLU B 628 40.053 19.564 -0.573 1.00 32.57

ATOM 8066 CB GLU B 628 38.880 19.476 -1.552 1.00 34.01

ATOM 8069 CG GLU B 628 37.601 18.992 -0.940 1.00 40.30

ATOM 8072 CD GLU B 628 36.666 18.433 -1.992 1.00 53.20

ATOM 8073 OEl GLU B 628 36.018 19.234 -2.715 1.00 57.24

ATOM 8074 OE2 GLU B 628 36.596 17.188 -2.105 1.00 60.26

ATOM 8075 C GLU B 628 40.689 18.212 -0.341 1.00 31.09

ATOM 8076 O GLU B 628 41.477 17.729 -1.160 1.00 31.61

ATOM 8078 N GLY B 629 40.387 17.621 0.811 1.00 30.24

ATOM 8079 CA GLY B 629 40.939 16.326 1.199 1.00 29.55

ATOM 8082 C GLY B 629 42.271 16.437 1.932 1.00 28.53

ATOM 8083 O GLY B 629 42.869 15.415 2.302 1.00 29.35

ATOM 8085 N TRP B 630 42.770 17.665 2.075 1.00 27.26

ATOM 8086 CA TRP B 630 43.980 17.926 2.850 1.00 26.32

ATOM 8088 CB TRP B 630 44.957 18.793 2.054 1.00 26.02

ATOM 8091 CG TRP B 630 45.543 18.114 0.874 1.00 27.15

ATOM 8092 CDl TRP B 630 44.933 17.898 -0.332 1.00 27.20

ATOM 8094 NEl TRP B 630 45.791 17.236 -1.186 1.00 29.67

ATOM 8096 CE2 TRP B 630 46.979 17.019 -0.541 1.00 29.12

ATOM 8097 CD2 TRP B 630 46.867 17.579 0.756 1.00 25.57

ATOM 8098 CE3 TRP B 630 47.959 17.486 1.626 1.00 26.86

ATOM 8100 CZ3 TRP B 630 49.101 16.894 1.190 1.00 24.94

ATOM 8102 CH2 TRP B 630 49.192 16.354 -0.124 1.00 27.02

ATOM 8104 CZ2 TRP B 630 48.148 16.424 -0.994 1.00 27.49

ATOM 8106 C TRP B 630 43.585 18.644 4.140 1.00 25.95

ATOM 8107 O TRP B 630 42.624 19.411 4.172 1.00 26.57

ATOM 8109 N THR B 631 44.343 18.411 5.200 1.00 23.50

ATOM 8110 CA THR B 631 44.029 19.004 6.491 1.00 22.17

ATOM 8112 CB THR B 631 43.963 17.935 7.560 1.00 21.42

ATOM 8114 OGl THR B 631 42.893 17.012 7.293 1.00 20.70

ATOM 8116 CG2 THR B 631 43.728 18.589 8.930 1.00 20.16

ATOM 8120 C THR B 631 45.113 20.014 6.852 1.00 20.84

ATOM 8121 O THR B 631 46.296 19.657 6.908 1.00 20.87

ATOM 8123 N LEU B 632 44.730 21.270 7.078 1.00 19.52

ATOM 8124 CA LEU B 632 45.687 22.294 7.507 1.00 18.84

ATOM 8126 CB LEU B 632 45.013 23.674 7.607 1.00 19.86

ATOM 8129 CG LEU B 632 45.784 24.985 7.935 1.00 19.75

ATOM 8131 CDl LEU B 632 44.778 26.116 7.932 1.00 23.22

ATOM 8135 CD2 LEU B 632 46.854 25.309 6.977 1.00 25.39

ATOM 8139 C LEU B 632 46.242 21.887 8.874 1.00 19.48

ATOM 8140 O LEU B 632 45.464 21.692 9.813 1.00 16.02

ATOM 8142 N THR B 633 47.566 21.747 8.964 1.00 17.88

ATOM 8143 CA THR B 633 48.229 21.467 10.245 1.00 18.73

ATOM 8145 CB THR B 633 49.268 20.341 10.118 1.00 19.92

ATOM 8147 OGl THR B 633 50.322 20.744 9.239 1.00 18.60

ATOM 8149 CG2 THR B 633 48.613 18.962 9.629 1.00 17.87

ATOM 8153 C THR B 633 48.908 22.699 10.833 1.00 20.28

ATOM 8154 O THR B 633 49.041 22.811 12.062 1.00 21.92

ATOM 8156 N GLY B 634 49.385 23.594 9.976 1.00 21.30

ATOM 8157 CA GLY B 634 50.065 24.799 10.412 1.00 21.80

ATOM 8160 C GLY B 634 49.755 26.003 9.558 1.00 22.56

ATOM 8161 O GLY B 634 49.546 25.898 8.349 1.00 23.69

ATOM 8163 N CYS B 635 49.732 27.154 10.208 1.00 23.58

ATOM 8164 CA CYS B 635 49.392 28.418 9.583 1.00 24.55

ATOM 8166 CB CYS B 635 47.920 28.732 9.834 1.00 24.75 ATOM 8169 SG CYS B 635 47.431 30.378 9.385 1.00 25.58

ATOM 8171 C CYS B 635 50.271 29.502 10.181 1.00 25.27

ATOM 8172 O CYS B 635 50.355 29.635 11.391 1.00 24.55

ATOM 8174 N SER B 636 50.968 30.234 9.327 1.00 25.99

ATOM 8175 CA SER B 636 51.885 31.273 9.794 1.00 26.14

ATOM 8177 CB SER B 636 53.238 30.675 10.156 1.00 27.19

ATOM 8180 OG SER B 636 53.893 30.180 8.996 1.00 26.13

ATOM 8182 C SER B 636 52.061 32.320 8.723 1.00 28.25

ATOM 8183 O SER B 636 51.683 32.121 7.577 1.00 27.02

ATOM 8185 N ALA B 637 52.620 33.448 9.127 1.00 29.78

ATOM 8186 CA ALA B 637 52.949 34.522 8.219 1.00 31.83

ATOM 8188 CB ALA B 637 52.540 35.845 8.811 1.00 30.13

ATOM 8192 C ALA B 637 54.455 34.488 7.974 1.00 34.06

ATOM 8193 O ALA B 637 55.246 34.341 8.910 1.00 35.54

ATOM 8195 N LEU B 638 54.842 34.611 6.716 1.00 36.15

ATOM 8196 CA LEU B 638 56.256 34.820 6.360 1.00 37.92

ATOM 8198 CB LEU B 638 56.368 35.075 4.851 1.00 38.61

ATOM 8201 CG LEU B 638 57.262 34.183 3.974 1.00 41.25

ATOM 8203 CDl LEU B 638 56.884 34.380 2.496 1.00 43.68

ATOM 8207 CD2 LEU B 638 57.169 32.717 4.352 1.00 40.87

ATOM 8211 C LEU B 638 56.751 36.031 7.162 1.00 39.19

ATOM 8212 O LEU B 638 56.009 36.985 7.327 1.00 39.42

ATOM 8214 N PRO B 639 57.981 35.980 7.704 1.00 39.96

ATOM 8215 CA PRO B 639 58.511 37.130 8.455 1.00 41.01

ATOM 8217 CB PRO B 639 59.689 36.535 9.233 1.00 41.54

ATOM 8220 CG PRO B 639 60.110 35.343 8.453 1.00 41.93

ATOM 8223 CD PRO B 639 58.934 34.859 7.647 1.00 40.69

ATOM 8226 C PRO B 639 58.984 38.267 7.544 1.00 41.21

ATOM 8227 O PRO B 639 58.993 38.100 6.310 1.00 40.75

ATOM 8228 N SER B 642 52.611 44.200 6.921 1.00 58.10

ATOM 8229 CA SER B 642 54.006 43.977 7.283 1.00 58.10

ATOM 8231 CB SER B 642 54.876 45.147 6.814 1.00 58.47

ATOM 8234 OG SER B 642 54.700 45.389 5.424 1.00 59.57

ATOM 8236 C SER B 642 54.139 43.794 8.791 1.00 57.37

ATOM 8237 O SER B 642 55.040 43.080 9.262 1.00 58.24

ATOM 8239 N HIS B 643 53.259 44.462 9.539 1.00 55.46

ATOM 8240 CA HIS B 643 53.085 44.188 10.960 1.00 53.93

ATOM 8242 CB HIS B 643 52.939 45.461 11.773 1.00 54.53

ATOM 8245 CG HIS B 643 52.635 45.188 13.207 1.00 57.17

ATOM 8246 NDl HIS B 643 53.467 44.424 13.999 1.00 61.01

ATOM 8248 CEl HIS B 643 52.942 44.318 15.206 1.00 60.56

ATOM 8250 NE 2 HIS B 643 51.795 44.977 15.222 1.00 61.48

ATOM 8252 CD2 HIS B 643 51.575 45.523 13.981 1.00 59.00

ATOM 8254 C HIS B 643 51.843 43.324 11.178 1.00 51.17

ATOM 8255 O HIS B 643 50.701 43.802 11.081 1.00 51.80

ATOM 8257 N VAL B 644 52.073 42.054 11.490 1.00 47.48

ATOM 8258 CA VAL B 644 50.998 41.105 11.568 1.00 44.11

ATOM 8260 CB VAL B 644 51.397 39.684 11.032 1.00 43.90

ATOM 8262 CGl VAL B 644 51.743 38.728 12.144 1.00 43.28

ATOM 8266 CG2 VAL B 644 52.517 39.783 10.011 1.00 43.94

ATOM 8270 C VAL B 644 50.498 41.074 12.998 1.00 40.94

ATOM 8271 O VAL B 644 51.283 41.109 13.935 1.00 42.16

ATOM 8273 N LEU B 645 49.179 41.054 13.133 1.00 36.98

ATOM 8274 CA LEU B 645 48.484 40.857 14.396 1.00 34.85

ATOM 8276 CB LEU B 645 47.013 41.239 14.247 1.00 35.20

ATOM 8279 CG LEU B 645 46.695 42.731 14.306 1.00 36.97

ATOM 8281 CDl LEU B 645 45.785 43.115 13.140 1.00 36.23

ATOM 8285 CD2 LEU B 645 47.987 43.567 14.319 1.00 34.29

ATOM 8289 C LEU B 645 48.561 39.413 14.825 1.00 32.46

ATOM 8290 O LEU B 645 48.642 39.103 16.005 1.00 31.01

ATOM 8292 N GLY B 646 48.536 38.522 13.853 1.00 30.59 ATOM 8293 CA GLY B 646 48.636 37.110 14.158 1.00 28.53

ATOM 8296 C GLY B 646 48.178 36.298 12.993 1.00 26.23

ATOM 8297 O GLY B 646 47.887 36.814 11.932 1.00 27.08

ATOM 8299 N ALA B 647 48.139 35.000 13.216 1.00 25.44

ATOM 8300 CA ALA B 647 47.737 34.042 12.214 1.00 24.50

ATOM 8302 CB ALA B 647 48.955 33.448 11.560 1.00 23.36

ATOM 8306 C ALA B 647 46.942 32.971 12.911 1.00 24.33

ATOM 8307 O ALA B 647 47.166 32.669 14.077 1.00 25.31

ATOM 8309 N TYR B 648 46.008 32.382 12.190 1.00 24.27

ATOM 8310 CA TYR B 648 45.185 31.313 12.742 1.00 22.50

ATOM 8312 CB TYR B 648 44.114 31.875 13.680 1.00 22.25

ATOM 8315 CG TYR B 648 43.399 33.099 13.159 1.00 24.33

ATOM 8316 CDl TYR B 648 43.847 34.373 13.475 1.00 22.10

ATOM 8318 CEl TYR B 648 43.173 35.473 13.042 1.00 23.77

ATOM 8320 CZ TYR B 648 42.067 35.330 12.267 1.00 19.94

ATOM 8321 OH TYR B 648 41.441 36.441 11.801 1.00 28.08

ATOM 8323 CE 2 TYR B 648 41.608 34.096 11.911 1.00 25.95

ATOM 8325 CD2 TYR B 648 42.264 32.979 12.380 1.00 23.54

ATOM 8327 C TYR B 648 44.551 30.514 11.621 1.00 21.27

ATOM 8328 O TYR B 648 44.263 31.044 10.556 1.00 20.08

ATOM 8330 N ALA B 649 44.403 29.222 11.869 1.00 20.69

ATOM 8331 CA ALA B 649 43.690 28.312 11.014 1.00 20.77

ATOM 8333 CB ALA B 649 44.088 26.874 11.355 1.00 19.65

ATOM 8337 C ALA B 649 42.194 28.467 11.261 1.00 21.75

ATOM 8338 O ALA B 649 41.752 28.497 12.421 1.00 25.01

ATOM 8340 N VAL B 650 41.429 28.597 10.189 1.00 19.38

ATOM 8341 CA VAL B 650 39.973 28.514 10.234 1.00 21.20

ATOM 8343 CB VAL B 650 39.333 29.759 9.648 1.00 20.20

ATOM 8345 CGl VAL B 650 37.841 29.595 9.616 1.00 25.10

ATOM 8349 CG2 VAL B 650 39.742 30.979 10.443 1.00 24.74

ATOM 8353 C VAL B 650 39.618 27.320 9.375 1.00 21.77

ATOM 8354 O VAL B 650 39.723 27.385 8.159 1.00 20.44

ATOM 8356 N ASP B 651 39.231 26.218 10.010 1.00 22.62

ATOM 8357 CA ASP B 651 39.007 24.963 9.306 1.00 22.34

ATOM 8359 CB ASP B 651 37.791 25.033 8.400 1.00 23.00

ATOM 8362 CG ASP B 651 37.465 23.687 7.773 1.00 28.78

ATOM 8363 ODl ASP B 651 37.832 22.636 8.379 1.00 41.71

ATOM 8364 OD2 ASP B 651 36.871 23.683 6.679 1.00 36.81

ATOM 8365 C ASP B 651 40.294 24.630 8.560 1.00 22.45

ATOM 8366 O ASP B 651 41.302 24.452 9.213 1.00 23.64

ATOM 8368 N ASN B 652 40.292 24.619 7.218 1.00 22.90

ATOM 8369 CA ASN B 652 41.501 24.332 6.424 1.00 21.73

ATOM 8371 CB ASN B 652 41.243 23.143 5.503 1.00 22.88

ATOM 8374 CG ASN B 652 41.060 21.861 6.291 1.00 23.68

ATOM 8375 ODl ASN B 652 41.870 21.549 7.178 1.00 25.46

ATOM 8376 ND2 ASN B 652 39.990 21.124 6.003 1.00 25.61

ATOM 8379 C ASN B 652 42.050 25.526 5.656 1.00 22.15

ATOM 8380 O ASN B 652 42.803 25.359 4.700 1.00 22.18

ATOM 8382 N THR B 653 41.735 26.716 6.161 1.00 22.08

ATOM 8383 CA THR B 653 42.198 27.977 5.631 1.00 22.01

ATOM 8385 CB THR B 653 41.031 28.887 5.305 1.00 21.47

ATOM 8387 OGl THR B 653 40.238 28.260 4.295 1.00 27.20

ATOM 8389 CG2 THR B 653 41.505 30.230 4.772 1.00 19.56

ATOM 8393 C THR B 653 43.074 28.672 6.656 1.00 22.04

ATOM 8394 O THR B 653 42.688 28.844 7.825 1.00 22.13

ATOM 8396 N CYS B 654 44.254 29.069 6.224 1.00 20.77

ATOM 8397 CA CYS B 654 45.189 29.792 7.074 1.00 21.91

ATOM 8399 CB CYS B 654 46.646 29.476 6.683 1.00 22.26

ATOM 8402 SG CYS B 654 47.810 30.526 7.370 1.00 23.53

ATOM 8404 C CYS B 654 44.925 31.266 6.900 1.00 22.16

ATOM 8405 O CYS B 654 44.869 31.757 5.779 1.00 21.75 ATOM 8407 N VAL B 655 44.679 31.961 8.005 1.00 22.64

ATOM 8408 CA VAL B 655 44.419 33.394 7.933 1.00 23.60

ATOM 8410 CB VAL B 655 43.099 33.811 8.646 1.00 24.98

ATOM 8412 CGl VAL B 655 42.956 35.358 8.607 1.00 25.10

ATOM 8416 CG2 VAL B 655 41.889 33.124 8.054 1.00 24.82

ATOM 8420 C VAL B 655 45.542 34.145 8.598 1.00 23.89

ATOM 8421 O VAL B 655 45.905 33.861 9.741 1.00 23.94

ATOM 8423 N VAL B 656 46.089 35.127 7.894 1.00 26.07

ATOM 8424 CA VAL B 656 47.074 36.031 8.473 1.00 27.73

ATOM 8426 CB VAL B 656 48.365 36.075 7.634 1.00 28.30

ATOM 8428 CGl VAL B 656 49.213 37.281 8.023 1.00 27.81

ATOM 8432 CG2 VAL B 656 49.160 34.746 7.816 1.00 27.89

ATOM 8436 C VAL B 656 46.459 37.420 8.569 1.00 30.58

ATOM 8437 O VAL B 656 45.896 37.916 7.592 1.00 29.39

ATOM 8439 N ARG B 657 46.571 38.020 9.754 1.00 33.66

ATOM 8440 CA ARG B 657 45.985 39.308 10.034 1.00 35.89

ATOM 8442 CB ARG B 657 45.117 39.225 11.292 1.00 35.83

ATOM 8445 CG ARG B 657 43.802 38.488 11.110 1.00 37.24

ATOM 8448 CD ARG B 657 42.719 39.363 10.461 1.00 41.61

ATOM 8451 NE ARG B 657 42.395 40.473 11.347 1.00 43.08

ATOM 8453 CZ ARG B 657 41.573 40.405 12.392 1.00 44.42

ATOM 8454 NHl ARG B 657 40.931 39.276 12.699 1.00 39.19

ATOM 8457 NH2 ARG B 657 41.391 41.492 13.139 1.00 44.93

ATOM 8460 C ARG B 657 47.094 40.317 10.212 1.00 37.97

ATOM 8461 O ARG B 657 48.045 40.087 10.957 1.00 36.41

ATOM 8463 N SER B 658 46.971 41.437 9.517 1.00 42.22

ATOM 8464 CA SER B 658 47.902 42.546 9.684 1.00 45.93

ATOM 8466 CB SER B 658 48.834 42.613 8.486 1.00 46.24

ATOM 8469 OG SER B 658 48.087 42.916 7.330 1.00 49.26

ATOM 8471 C SER B 658 47.160 43.870 9.850 1.00 48.51

ATOM 8472 O SER B 658 45.935 43.930 9.690 1.00 48.84

ATOM 8474 N ARG B 659 47.917 44.919 10.181 1.00 52.24

ATOM 8475 CA ARG B 659 47.351 46.262 10.396 1.00 54.62

ATOM 8477 CB ARG B 659 48.179 47.048 11.431 1.00 55.31

ATOM 8480 CG ARG B 659 47.339 47.944 12.361 1.00 59.46

ATOM 8483 CD ARG B 659 47.921 47.988 13.778 1.00 66.97

ATOM 8486 NE ARG B 659 46.973 48.501 14.771 1.00 70.83

ATOM 8488 CZ ARG B 659 45.930 47.827 15.268 1.00 73.63

ATOM 8489 NHl ARG B 659 45.651 46.587 14.865 1.00 74.15

ATOM 8492 NH2 ARG B 659 45.142 48.407 16.174 1.00 73.93

ATOM 8495 C ARG B 659 47.256 47.039 9.078 1.00 55.39

ATOM 8496 O ARG B 659 48.259 47.246 8.385 1.00 56.84

ATOM 8498 N ALA B 671 54.934 43.088 0.839 1.00 51.43

ATOM 8499 CA ALA B 671 53.818 42.169 0.665 1.00 51.11

ATOM 8501 CB ALA B 671 53.988 41.374 -0.616 1.00 51.11

ATOM 8505 C ALA B 671 53.735 41.220 1.854 1.00 50.59

ATOM 8506 O ALA B 671 54.754 40.655 2.265 1.00 52.10

ATOM 8508 N VAL B 672 52.535 41.043 2.403 1.00 48.41

ATOM 8509 CA VAL B 672 52.325 40.103 3.511 1.00 46.51

ATOM 8511 CB VAL B 672 51.238 40.609 4.466 1.00 46.81

ATOM 8513 CGl VAL B 672 51.672 41.939 5.074 1.00 48.84

ATOM 8517 CG2 VAL B 672 50.961 39.585 5.561 1.00 47.15

ATOM 8521 C VAL B 672 51.931 38.737 2.950 1.00 44.14

ATOM 8522 O VAL B 672 51.198 38.659 1.960 1.00 43.15

ATOM 8524 N THR B 673 52.399 37.667 3.589 1.00 41.41

ATOM 8525 CA THR B 673 52.240 36.331 3.015 1.00 39.38

ATOM 8527 CB THR B 673 53.525 35.900 2.314 1.00 39.65

ATOM 8529 OGl THR B 673 53.714 36.731 1.163 1.00 42.77

ATOM 8531 CG2 THR B 673 53.456 34.422 1.877 1.00 39.06

ATOM 8535 C THR B 673 51.825 35.249 4.008 1.00 36.39

ATOM 8536 O THR B 673 52.524 34.996 4.975 1.00 36.99 ATOM 8538 N ALA B 674 50.693 34.609 3.716 1.00 33.03

ATOM 8539 CA ALA B 674 50.186 33.484 4.477 1.00 30.54

ATOM 8541 CB ALA B 674 48.650 33.406 4.367 1.00 28.77

ATOM 8545 C ALA B 674 50.807 32.190 3.961 1.00 28.97

ATOM 8546 O ALA B 674 50.941 31.989 2.751 1.00 28.38

ATOM 8548 N VAL B 675 51.159 31.316 4.897 1.00 26.57

ATOM 8549 CA VAL B 675 51.763 30.018 4.600 1.00 25.38

ATOM 8551 CB VAL B 675 53.267 30.006 5.023 1.00 25.94

ATOM 8553 CGl VAL B 675 53.896 28.647 4.736 1.00 25.66

ATOM 8557 CG2 VAL B 675 54.028 31.126 4.324 1.00 27.31

ATOM 8561 C VAL B 675 51.031 28.915 5.351 1.00 23.56

ATOM 8562 O VAL B 675 50.977 28.941 6.574 1.00 24.51

ATOM 8564 N ALA B 676 50.453 27.970 4.617 1.00 20.87

ATOM 8565 CA ALA B 676 49.720 26.831 5.165 1.00 20.74

ATOM 8567 CB ALA B 676 48.361 26.657 4.480 1.00 20.56

ATOM 8571 C ALA B 676 50.523 25.574 4.918 1.00 21.29

ATOM 8572 O ALA B 676 51.033 25.382 3.821 1.00 21.36

ATOM 8574 N ILE B 677 50.634 24.747 5.947 1.00 20.17

ATOM 8575 CA ILE B 677 51.177 23.415 5.834 1.00 20.55

ATOM 8577 CB ILE B 677 52.109 23.086 7.005 1.00 20.74

ATOM 8579 CGl ILE B 677 53.284 24.085 7.005 1.00 23.32

ATOM 8582 CDl ILE B 677 54.209 23.966 8.174 1.00 21.37

ATOM 8586 CG2 ILE B 677 52.581 21.650 6.901 1.00 19.02

ATOM 8590 C ILE B 677 49.967 22.539 5.840 1.00 21.54

ATOM 8591 O ILE B 677 49.173 22.598 6.763 1.00 22.01

ATOM 8593 N CYS B 678 49.818 21.735 4.794 1.00 22.07

ATOM 8594 CA CYS B 678 48.635 20.905 4.590 1.00 22.02

ATOM 8596 CB CYS B 678 47.954 21.310 3.299 1.00 23.41

ATOM 8599 SG CYS B 678 47.573 23.063 3.183 1.00 29.39

ATOM 8601 C CYS B 678 49.073 19.468 4.491 1.00 22.63

ATOM 8602 O CYS B 678 49.999 19.176 3.750 1.00 23.98

ATOM 8604 N CYS B 679 48.403 18.577 5.207 1.00 22.12

ATOM 8605 CA CYS B 679 48.777 17.168 5.248 1.00 25.20

ATOM 8607 CB CYS B 679 49.374 16.813 6.615 1.00 24.84

ATOM 8610 SG CYS B 679 50.802 17.869 7.114 1.00 29.63

ATOM 8612 C CYS B 679 47.590 16.270 4.996 1.00 26.99

ATOM 8613 O CYS B 679 46.442 16.667 5.172 1.00 25.86

ATOM 8615 N ARG B 680 47.874 15.032 4.612 1.00 29.32

ATOM 8616 CA ARG B 680 46.837 14.034 4.518 1.00 31.40

ATOM 8618 CB ARG B 680 46.103 14.146 3.172 1.00 30.41

ATOM 8621 CG ARG B 680 46.874 13.570 2.017 1.00 33.00

ATOM 8624 CD ARG B 680 46.110 13.650 0.698 1.00 33.17

ATOM 8627 NE ARG B 680 47.036 13.482 -0.414 1.00 36.42

ATOM 8629 CZ ARG B 680 46.693 13.487 -1.700 1.00 36.62

ATOM 8630 NHl ARG B 680 45.435 13.647 -2.062 1.00 29.02

ATOM 8633 NH2 ARG B 680 47.633 13.334 -2.620 1.00 38.68

ATOM 8636 C ARG B 680 47.427 12.638 4.732 1.00 33.50

ATOM 8637 O ARG B 680 48.632 12.444 4.689 1.00 33.52

ATOM 8639 N SER B 681 46.543 11.692 5.000 1.00 38.39

ATOM 8640 CA SER B 681 46.854 10.265 5.013 1.00 41.90

ATOM 8642 CB SER B 681 45.584 9.497 5.350 1.00 42.26

ATOM 8645 OG SER B 681 45.850 8.131 5.565 1.00 47.83

ATOM 8647 C SER B 681 47.331 9.852 3.628 1.00 43.67

ATOM 8648 O SER B 681 46.747 10.262 2.626 1.00 44.62

ATOM 8650 N ARG B 682 48.381 9.046 3.564 1.00 45.51

ATOM 8651 CA ARG B 682 49.017 8.711 2.291 1.00 47.73

ATOM 8653 CB ARG B 682 50.529 8.650 2.493 1.00 47.66

ATOM 8656 CG ARG B 682 51.358 8.394 1.255 1.00 51.20

ATOM 8659 CD ARG B 682 52.846 8.320 1.637 1.00 51.70

ATOM 8662 NE ARG B 682 53.528 9.617 1.551 1.00 56.05

ATOM 8664 CZ ARG B 682 54.622 9.953 2.240 1.00 59.30 ATOM 8665 NHl ARG B 682 55.176 9.103 3.113 1.00 61.30

ATOM 8668 NH2 ARG B 682 55.168 11.157 2.066 1.00 57.99

ATOM 8671 C ARG B 682 48.472 7.378 1.800 1.00 47.99

ATOM 8672 O ARG B 682 47.555 6.818 2.418 1.00 49.18

ATOM 8674 CA CA C 1 33.006 24.044 25.670 1.00 60.13

ATOM 8675 Cl NAG D 504 57.410 6.066 17.249 1.00 61.39

ATOM 8678 C2 NAG D 504 57.849 4.851 18.079 1.00 67.64

ATOM 8680 N2 NAG D 504 58.843 5.273 19.063 1.00 70.03

ATOM 8682 C7 NAG D 504 59.122 4.572 20.169 1.00 69.79

ATOM 8683 07 NAG D 504 60.275 4.239 20.459 1.00 67.77

ATOM 8684 C8 NAG D 504 57.968 4.209 21.066 1.00 69.17

ATOM 8688 C3 NAG D 504 58.370 3.647 17.287 1.00 69.10

ATOM 8690 03 NAG D 504 57.896 2.479 17.922 1.00 73.34

ATOM 8692 C4 NAG D 504 57.967 3.629 15.813 1.00 68.84

ATOM 8694 04 NAG D 504 58.863 2.804 15.102 1.00 70.16

ATOM 8696 C5 NAG D 504 57.960 5.055 15.257 1.00 69.60

ATOM 8698 C6 NAG D 504 57.582 5.186 13.789 1.00 71.44

ATOM 8701 06 NAG D 504 57.007 6.460 13.578 1.00 72.09

ATOM 8703 05 NAG D 504 56.957 5.712 15.969 1.00 64.68

ATOM 8704 O HOH W 1 23.713 39.227 29.802 1.00 43.16

ATOM 8707 O HOH W 2 39.092 34.447 46.487 1.00 34.70

ATOM 8710 O HOH W 3 35.185 28.395 12.172 1.00 22.00

ATOM 8713 O HOH W 4 42.872 25.872 46.855 1.00 30.74

ATOM 8716 O HOH W 5 36.850 24.746 37.585 1.00 18.55

ATOM 8719 O HOH W 6 43.792 12.705 5.643 1.00 31.06

ATOM 8722 O HOH W 7 30.412 38.957 44.348 1.00 37.37

ATOM 8725 O HOH W 8 24.348 23.024 64.225 1.00 44.19

ATOM 8728 O HOH W 9 34.141 13.196 49.875 1.00 21.63

ATOM 8731 O HOH W 10 40.255 18.397 10.292 1.00 27.91

ATOM 8734 O HOH W 11 13.392 12.922 37.899 1.00 21.41

ATOM 8737 O HOH W 12 49.629 13.056 -5.046 1.00 44.84

ATOM 8740 O HOH W 13 33.258 30.301 40.846 1.00 20.51

ATOM 8743 O HOH W 14 11.128 22.327 13.705 1.00 15.23

ATOM 8746 O HOH W 15 43.571 36.537 0.622 1.00 38.22

ATOM 8749 O HOH W 16 20.846 26.682 47.671 1.00 24.42

ATOM 8752 O HOH W 17 54.340 12.273 19.574 1.00 35.00

ATOM 8755 O HOH W 18 35.234 11.835 45.400 1.00 37.01

ATOM 8758 O HOH W 19 35.564 26.190 26.907 1.00 30.06

ATOM 8761 O HOH W 20 38.769 23.689 14.322 1.00 14.55

ATOM 8764 O HOH W 21 28.134 37.179 56.279 1.00 24.88

ATOM 8767 O HOH W 22 26.143 41.665 39.125 1.00 20.70

ATOM 8770 O HOH W 23 36.025 8.692 48.894 1.00 26.09

ATOM 8773 O HOH W 24 18.836 22.542 40.860 1.00 20.83

ATOM 8776 O HOH W 25 10.791 28.922 22.921 1.00 25.58

ATOM 8779 O HOH W 26 11.998 32.126 18.518 1.00 56.89

ATOM 8782 O HOH W 27 33.098 6.138 23.868 1.00 34.23

ATOM 8785 O HOH W 28 10.095 22.811 9.731 1.00 34.56

ATOM 8788 O HOH W 29 41.753 18.203 -3.993 1.00 32.07

ATOM 8791 O HOH W 30 38.392 31.900 13.505 1.00 25.39

ATOM 8794 O HOH W 31 28.231 -0.128 16.791 1.00 23.61

ATOM 8797 O HOH W 32 52.889 26.839 11.032 1.00 18.19

ATOM 8800 O HOH W 33 42.676 19.547 44.642 1.00 31.06

ATOM 8803 O HOH W 34 30.750 7.789 27.599 1.00 28.83

ATOM 8806 O HOH W 35 22.045 4.053 8.954 1.00 48.50

ATOM 8809 O HOH W 36 10.044 14.225 35.563 1.00 23.73

ATOM 8812 O HOH W 37 22.875 30.447 63.601 1.00 35.80

ATOM 8815 O HOH W 38 28.298 3.457 31.230 1.00 30.26

ATOM 8818 O HOH W 39 28.453 17.648 13.659 1.00 20.87

ATOM 8821 O HOH W 40 25.796 26.368 29.984 1.00 18.67

ATOM 8824 O HOH W 41 24.825 29.926 60.500 1.00 25.90

ATOM 8827 O HOH W 42 34.666 20.787 24.107 1.00 33.02 ATOM 8830 O HOH W 43 14.347 28.958 12.025 1.00 29.72

ATOM 8833 O HOH W 44 24.177 21.236 9.248 1.00 27.41

ATOM 8836 O HOH W 45 10.478 14.732 40.511 1.00 37.92

ATOM 8839 O HOH W 46 34.823 23.942 17.461 1.00 18.56

ATOM 8842 O HOH W 47 27.217 32.701 44.241 1.00 19.04

ATOM 8845 O HOH W 48 26.870 -3.826 34.297 1.00 26.54

ATOM 8848 O HOH W 49 12.547 19.979 5.441 1.00 33.79

ATOM 8851 O HOH W 50 9.616 15.582 19.973 1.00 22.52

ATOM 8854 O HOH W 51 49.344 27.077 13.260 1.00 24.66

ATOM 8857 O HOH W 52 30.524 35.140 35.198 1.00 22.66

ATOM 8860 O HOH W 53 37.464 9.998 26.196 1.00 38.45

ATOM 8863 O HOH W 54 31.605 39.953 23.824 1.00 32.46

ATOM 8866 O HOH W 55 35.643 32.660 31.998 1.00 27.98

ATOM 8869 O HOH W 56 26.736 24.307 63.842 1.00 27.05

ATOM 8872 O HOH W 57 34.856 32.719 60.157 1.00 22.06

ATOM 8875 O HOH W 58 35.122 34.288 23.454 1.00 19.95

ATOM 8878 O HOH W 59 37.937 17.990 13.014 1.00 23.28

ATOM 8881 O HOH W 60 38.675 28.328 23.710 1.00 28.66

ATOM 8884 O HOH W 61 32.340 15.653 27.600 1.00 24.64

ATOM 8887 O HOH W 62 36.759 26.483 34.686 1.00 39.66

ATOM 8890 O HOH W 63 6.873 20.555 25.964 1.00 23.17

ATOM 8893 O HOH W 64 24.195 12.633 44.166 1.00 24.46

ATOM 8896 O HOH W 65 15.979 13.063 44.763 1.00 39.42

ATOM 8899 O HOH W 66 21.086 26.156 11.410 1.00 19.20

ATOM 8902 O HOH W 67 10.176 21.331 36.580 1.00 27.01

ATOM 8905 O HOH W 68 34.406 30.489 8.481 1.00 36.19

ATOM 8908 O HOH W 69 38.727 28.290 28.990 1.00 36.66

ATOM 8911 O HOH W 70 19.837 33.164 49.714 1.00 43.80

ATOM 8914 O HOH W 71 56.006 19.950 5.260 1.00 29.61

ATOM 8917 O HOH W 72 12.640 18.432 15.541 1.00 20.81

ATOM 8920 O HOH W 73 33.864 42.912 20.035 1.00 26.77

ATOM 8923 O HOH W 74 22.039 29.983 55.713 1.00 25.54

ATOM 8926 O HOH W 75 31.049 14.164 43.870 1.00 22.33

ATOM 8929 O HOH W 76 20.476 37.710 44.956 1.00 54.95

ATOM 8932 O HOH W 77 9.993 6.508 33.830 1.00 27.87

ATOM 8935 O HOH W 78 23.909 4.252 14.243 1.00 56.39

ATOM 8938 O HOH W 79 46.899 11.615 18.026 1.00 25.44

ATOM 8941 O HOH W 80 37.126 38.887 15.338 1.00 28.75

ATOM 8944 O HOH W 81 20.529 19.752 48.357 1.00 26.03

ATOM 8947 O HOH W 82 18.583 15.531 45.846 1.00 34.46

ATOM 8950 O HOH W 83 53.000 33.598 11.999 1.00 38.65

ATOM 8953 O HOH W 84 30.001 34.215 37.837 1.00 27.40

ATOM 8956 O HOH W 85 32.743 31.713 24.452 1.00 20.09

ATOM 8959 O HOH W 86 14.244 19.320 45.572 1.00 34.13

ATOM 8962 O HOH W 87 38.515 25.825 60.817 1.00 29.43

ATOM 8965 O HOH W 88 29.776 18.159 64.609 1.00 30.77

ATOM 8968 O HOH W 89 39.252 16.311 25.180 1.00 34.07

ATOM 8971 O HOH W 90 38.954 24.282 39.674 1.00 35.70

ATOM 8974 O HOH W 91 24.867 13.426 51.564 1.00 26.41

ATOM 8977 O HOH W 92 27.672 42.651 15.631 1.00 24.01

ATOM 8980 O HOH W 93 30.390 22.735 4.767 1.00 24.91

ATOM 8983 O HOH W 94 44.067 29.358 -1.228 1.00 31.61

ATOM 8986 O HOH W 95 8.292 14.232 9.524 1.00 47.16

ATOM 8989 O HOH W 96 12.625 14.078 35.559 1.00 24.97

ATOM 8992 O HOH W 97 12.016 28.220 10.985 1.00 30.83

ATOM 8995 O HOH W 98 57.645 28.629 5.505 1.00 66.98

ATOM 8998 O HOH W 99 18.349 23.010 44.243 1.00 22.97

ATOM 9001 O HOH W 100 36.490 35.439 27.874 1.00 34.57

ATOM 9004 O HOH W 101 39.905 12.569 24.546 1.00 28.31

ATOM 9007 O HOH W 102 14.990 30.346 32.098 1.00 28.59

ATOM 9010 O HOH W 103 64.381 37.208 20.853 1.00 22.54 ATOM 9013 O HOH W 104 20.944 21.623 46.547 1.00 24.57

ATOM 9016 O HOH W 105 38.878 17.024 20.176 1.00 21.47

ATOM 9019 O HOH W 106 23.008 28.494 5.039 1.00 43.79

ATOM 9022 O HOH W 107 37.182 28.668 18.742 1.00 27.90

ATOM 9025 O HOH W 108 14.348 26.788 25.075 1.00 26.81

ATOM 9028 O HOH W 109 52.048 16.800 20.748 1.00 33.65

ATOM 9031 O HOH W 110 16.639 34.330 15.056 1.00 21.53

ATOM 9034 O HOH W 111 12.461 12.614 10.437 1.00 42.35

ATOM 9037 O HOH W 112 40.070 14.411 57.974 1.00 47.85

ATOM 9040 O HOH W 113 28.082 15.698 7.741 1.00 27.90

ATOM 9043 O HOH W 114 11.599 17.107 18.748 1.00 27.21

ATOM 9046 O HOH W 115 39.165 22.041 23.985 1.00 32.98

ATOM 9049 O HOH W 116 38.258 28.042 14.632 1.00 27.92

ATOM 9052 O HOH W 117 24.842 3.056 27.208 1.00 28.78

ATOM 9055 O HOH W 118 27.573 38.818 62.152 1.00 39.88

ATOM 9058 O HOH W 119 39.379 35.825 10.260 1.00 36.30

ATOM 9061 O HOH W 120 17.924 29.265 41.708 1.00 25.93

ATOM 9064 O HOH W 121 16.417 31.263 28.582 1.00 41.37

ATOM 9067 O HOH W 122 39.524 34.842 27.271 1.00 37.68

ATOM 9070 O HOH W 123 39.316 19.960 44.449 1.00 31.36

ATOM 9073 O HOH W 124 47.817 39.044 32.484 1.00 37.85

ATOM 9076 O HOH W 125 43.228 24.030 52.785 1.00 25.92

ATOM 9079 O HOH W 126 59.955 35.515 13.508 1.00 30.65

ATOM 9082 O HOH W 127 35.037 27.888 66.671 1.00 43.50

ATOM 9085 O HOH W 128 36.302 22.995 33.003 1.00 42.30

ATOM 9088 O HOH W 129 39.142 22.181 12.208 1.00 25.63

ATOM 9091 O HOH W 130 44.714 25.837 45.894 1.00 51.50

ATOM 9094 O HOH W 131 33.549 32.352 62.608 1.00 35.43

ATOM 9097 O HOH W 132 33.842 8.429 40.493 1.00 37.57

ATOM 9100 O HOH W 133 16.594 6.231 39.350 1.00 34.73

ATOM 9103 O HOH W 134 22.274 3.976 41.623 1.00 45.59

ATOM 9106 O HOH W 135 50.394 17.474 22.590 1.00 32.96

ATOM 9109 O HOH W 136 15.795 36.774 25.809 1.00 35.87

ATOM 9112 O HOH W 137 20.610 6.900 36.789 1.00 39.69

ATOM 9115 O HOH W 138 57.086 10.735 8.327 1.00 36.34

ATOM 9118 O HOH W 139 56.487 32.040 12.539 1.00 34.49

ATOM 9121 O HOH W 140 34.563 46.083 20.131 1.00 36.83

ATOM 9124 O HOH W 141 22.956 4.780 33.186 1.00 30.06

ATOM 9127 O HOH W 142 37.817 4.987 18.208 1.00 46.21

ATOM 9130 O HOH W 143 64.931 30.181 22.174 1.00 42.51

ATOM 9133 O HOH W 144 10.265 31.037 34.048 1.00 47.90

ATOM 9136 O HOH W 145 39.574 40.010 15.422 1.00 47.92

ATOM 9139 O HOH W 146 39.830 8.961 15.242 1.00 51.33

ATOM 9142 O HOH W 147 35.369 27.055 20.108 1.00 24.39

ATOM 9145 O HOH W 148 27.814 28.529 42.714 1.00 26.63

ATOM 9148 O HOH W 149 59.996 13.684 15.917 1.00 39.47

ATOM 9151 O HOH W 150 32.670 6.477 32.531 1.00 34.80

ATOM 9154 O HOH W 151 42.246 8.784 16.652 1.00 30.86

ATOM 9157 O HOH W 152 42.936 15.986 51.321 1.00 35.68

ATOM 9160 O HOH W 153 30.550 7.780 14.587 1.00 24.35

ATOM 9163 O HOH W 154 27.369 43.798 12.590 1.00 38.15

ATOM 9166 O HOH W 155 38.493 31.402 34.921 1.00 43.79

ATOM 9169 O HOH W 156 48.595 20.062 24.737 1.00 31.55

ATOM 9172 O HOH W 157 17.830 32.340 30.453 1.00 33.12

ATOM 9175 O HOH W 158 52.955 27.432 8.453 1.00 28.80

ATOM 9178 O HOH W 159 43.668 29.122 28.023 1.00 33.87

ATOM 9181 O HOH W 160 37.729 27.973 37.527 1.00 36.83

ATOM 9184 O HOH W 161 51.433 33.530 14.889 1.00 29.85

ATOM 9187 O HOH W 162 14.908 39.638 25.996 1.00 52.69

ATOM 9190 O HOH W 163 23.942 23.933 7.766 1.00 41.78

ATOM 9193 O HOH W 164 46.765 28.367 14.005 1.00 25.11 ATOM 9196 O HOH W 165 39.969 24.048 1.609 1.00 47.69

ATOM 9199 O HOH W 166 41.878 21.054 24.293 1.00 32.10

ATOM 9202 O HOH W 167 58.795 29.616 7.779 1.00 36.99

ATOM 9205 O HOH W 168 33.357 9.910 23.776 1.00 36.68

ATOM 9208 O HOH W 169 18.396 33.742 41.248 1.00 37.63

ATOM 9211 O HOH W 170 17.434 24.315 46.287 1.00 30.17

ATOM 9214 O HOH W 171 52.051 36.371 20.690 1.00 30.89

ATOM 9217 O HOH W 172 43.902 28.415 -3.846 1.00 53.30

ATOM 9220 O HOH W 173 9.737 6.909 37.571 1.00 46.49

ATOM 9223 O HOH W 174 7.695 12.728 35.212 1.00 37.67

ATOM 9226 O HOH W 175 32.167 34.521 63.073 1.00 35.86

ATOM 9229 O HOH W 176 42.114 24.926 54.696 1.00 34.46

ATOM 9232 O HOH W 177 44.523 17.547 -4.030 1.00 36.34

ATOM 9235 O HOH W 178 23.629 2.741 34.786 1.00 42.76

ATOM 9238 O HOH W 179 17.681 35.288 27.063 1.00 37.94

ATOM 9241 O HOH W 180 14.107 28.805 28.165 1.00 36.67

ATOM 9244 O HOH W 181 26.852 38.729 59.331 1.00 27.70

ATOM 9247 O HOH W 182 21.284 29.784 49.517 1.00 37.58

ATOM 9250 O HOH W 183 36.786 28.152 30.738 1.00 35.14

ATOM 9253 O HOH W 184 35.094 32.047 10.476 1.00 43.69

ATOM 9256 O HOH W 185 55.432 14.933 3.066 1.00 40.35

ATOM 9259 O HOH W 186 51.675 28.066 13.262 1.00 29.68

ATOM 9262 O HOH W 187 40.490 31.888 56.621 1.00 30.98

ATOM 9265 O HOH W 188 5.441 22.929 26.283 1.00 45.01

ATOM 9268 O HOH W 189 31.093 34.193 67.149 1.00 51.03

ATOM 9271 O HOH W 190 55.798 10.513 5.967 1.00 47.55

ATOM 9274 O HOH W 191 19.083 36.286 14.297 1.00 34.97

ATOM 9277 O HOH W 192 42.266 8.595 20.516 1.00 35.36

ATOM 9280 O HOH W 193 14.110 15.932 33.907 1.00 28.16

ATOM 9283 O HOH W 194 48.603 42.567 22.846 1.00 38.89

ATOM 9286 O HOH W 195 56.741 31.021 7.938 1.00 46.79

ATOM 9289 O HOH W 196 9.015 21.523 7.759 1.00 43.99

ATOM 9292 O HOH W 197 36.467 24.797 15.521 1.00 21.81

ATOM 9295 O HOH W 198 45.443 5.074 6.696 1.00 48.61

ATOM 9298 O HOH W 199 8.536 6.845 29.302 1.00 37.60

ATOM 9301 O HOH W 200 18.417 34.847 10.000 1.00 33.08

ATOM 9304 O HOH W 201 42.706 11.744 12.449 1.00 28.65

ATOM 9307 O HOH W 202 34.603 10.121 26.192 1.00 35.71

ATOM 9310 O HOH W 203 24.533 30.718 5.024 1.00 37.25

ATOM 9313 O HOH W 204 44.534 41.209 22.240 1.00 36.00

ATOM 9316 O HOH W 205 64.018 34.534 21.627 1.00 29.08

ATOM 9319 O HOH W 206 21.354 30.668 4.833 1.00 50.26

ATOM 9322 O HOH W 207 38.564 11.770 46.374 1.00 39.67

ATOM 9325 O HOH W 208 54.933 34.552 16.142 1.00 38.17

ATOM 9328 O HOH W 209 17.346 8.862 14.267 1.00 37.37

ATOM 9331 O HOH W 210 40.975 22.986 42.265 1.00 34.73

ATOM 9334 O HOH W 211 10.277 6.574 21.237 1.00 55.77

ATOM 9337 O HOH W 212 20.610 2.679 36.832 1.00 43.95

ATOM 9340 O HOH W 213 69.452 30.006 12.821 1.00 44.61

ATOM 9343 O HOH W 214 34.439 32.546 13.532 1.00 29.13

ATOM 9346 O HOH W 215 48.017 35.015 31.641 1.00 48.08

ATOM 9349 O HOH W 216 24.277 36.477 10.997 1.00 38.01

ATOM 9352 O HOH W 217 28.690 30.667 42.204 1.00 42.67

ATOM 9355 O HOH W 218 54.844 38.033 5.531 1.00 42.64

ATOM 9358 O HOH W 219 7.749 13.164 5.747 1.00 41.55

ATOM 9361 O HOH W 220 8.852 25.363 10.761 1.00 49.97

ATOM 9364 O HOH W 221 16.064 14.040 6.774 1.00 41.35

ATOM 9367 O HOH W 222 55.328 18.580 17.328 1.00 39.52

ATOM 9370 O HOH W 223 40.796 33.655 31.988 1.00 50.52

ATOM 9373 O HOH W 224 44.651 32.692 -1.449 1.00 48.01

ATOM 9376 O HOH W 225 22.316 4.067 16.120 1.00 37.24 ATOM 9379 O HOH W 226 34.934 4.299 9.420 1.00 45.99

ATOM 9382 O HOH W 227 53.783 31.115 13.830 1.00 44.34

ATOM 9385 O HOH W 228 18.867 12.304 9.509 1.00 44.89

ATOM 9388 O HOH W 229 41.576 20.016 61.921 1.00 50.55

ATOM 9391 O HOH W 230 37.318 18.652 8.063 1.00 50.84

ATOM 9394 O HOH W 231 35.968 5.843 39.929 1.00 36.79

ATOM 9397 O HOH W 232 38.500 9.643 30.268 1.00 36.42

ATOM 9400 O HOH W 233 5.451 6.382 32.785 1.00 52.35

ATOM 9403 O HOH W 234 48.698 11.780 0.341 1.00 59.48

ATOM 9406 O HOH W 235 35.132 15.792 62.823 1.00 44.32

ATOM 9409 O HOH W 236 41.980 27.415 45.170 1.00 26.86

ATOM 9412 O HOH W 237 39.543 33.836 48.894 1.00 30.81

ATOM 9415 O HOH W 238 23.728 38.099 31.951 1.00 44.47

ATOM 9418 O HOH W 239 35.667 11.633 48.285 1.00 33.56

ATOM 9421 O HOH W 240 34.662 27.004 10.246 1.00 32.50

ATOM 9424 O HOH W 241 28.646 39.335 42.603 1.00 28.12

ATOM 9427 O HOH W 242 37.596 23.004 35.855 1.00 27.04

ATOM 9430 O HOH W 243 51.382 14.720 -4.430 1.00 36.84

ATOM 9433 O HOH W 244 43.115 15.114 5.281 1.00 33.70

ATOM 9436 O HOH W 245 35.776 30.580 12.778 1.00 34.69

ATOM 9439 O HOH W 246 53.162 10.429 20.132 1.00 50.14

ATOM 9442 O HOH W 247 31.015 31.634 40.680 1.00 28.62

ATOM 9445 O HOH W 248 32.275 37.226 41.999 1.00 31.46

ATOM 9448 O HOH W 249 43.665 24.880 48.857 1.00 35.35

ATOM 9451 O HOH W 250 42.131 38.345 1.363 1.00 58.90

ATOM 9454 O HOH W 251 40.373 20.792 9.152 1.00 26.77

ATOM 9457 O HOH W 252 58.180 25.773 5.451 1.00 39.42

ATOM 9460 O HOH W 253 19.676 28.690 4.018 1.00 48.47

ATOM 9463 O HOH W 254 37.699 18.746 10.574 1.00 50.03

ATOM 9466 O HOH W 255 27.863 17.675 63.522 1.00 47.25

ATOM 9469 O HOH W 256 10.680 13.428 38.920 1.00 30.73

ATOM 9472 O HOH W 257 23.713 40.243 27.804 1.00 39.34

ATOM 9475 O HOH W 258 9.436 23.970 31.915 1.00 22.92

ATOM 9478 O HOH W 259 31.039 19.604 5.876 1.00 41.79

ATOM 9481 O HOH W 260 46.859 21.117 0.006 1.00 31.57

ATOM 9484 O HOH W 261 24.980 31.336 38.295 1.00 28.91

ATOM 9487 O HOH W 262 34.875 17.382 65.308 1.00 47.14

ATOM 9490 O HOH W 263 39.050 26.305 12.957 1.00 25.02

ATOM 9493 O HOH W 264 43.352 25.101 26.188 1.00 33.04

ATOM 9496 O HOH W 265 38.994 14.001 28.822 1.00 46.79

ATOM 9499 O HOH W 266 25.722 40.131 18.964 1.00 21.91

ATOM 9502 O HOH W 267 38.862 27.691 20.827 1.00 25.70

ATOM 9505 O HOH W 268 45.871 31.188 28.915 1.00 40.10

ATOM 9508 O HOH W 269 38.693 16.745 59.346 1.00 44.17

ATOM 9511 O HOH W 270 36.295 20.799 31.196 1.00 44.55

ATOM 9514 O HOH W 271 56.775 27.858 32.801 1.00 53.92

ATOM 9517 O HOH W 272 29.410 40.361 24.807 1.00 25.21

ATOM 9520 O HOH W 273 28.987 35.011 50.381 1.00 24.33

ATOM 9523 O HOH W 274 32.714 45.063 10.819 1.00 46.59

ATOM 9526 O HOH W 275 36.403 11.631 43.597 1.00 58.11

ATOM 9529 O HOH W 276 69.902 30.457 15.452 1.00 32.44

ATOM 9532 O HOH W 277 34.897 48.304 12.290 1.00 58.89

ATOM 9535 O HOH W 278 28.075 39.344 30.835 1.00 30.05

ATOM 9538 O HOH W 279 30.451 40.294 28.273 1.00 40.22

ATOM 9541 O HOH W 280 12.488 36.307 19.825 1.00 48.47

ATOM 9544 O HOH W 281 66.161 29.809 0.656 1.00 52.42

ATOM 9547 O HOH W 282 36.097 6.348 10.863 1.00 58.83

ATOM 9550 O HOH W 283 23.473 41.074 12.102 1.00 48.91

ATOM 9553 O HOH W 284 36.011 5.713 25.154 1.00 33.84

ATOM 9556 O HOH W 285 21.032 1.679 17.348 1.00 45.47

ATOM 9559 O HOH W 286 40.020 18.337 6.891 1.00 41.92 ATOM 9562 O HOH W 287 0.882 22.072 21.999 1.00 43.08

ATOM 9565 O HOH W 288 40.074 23.856 61.549 1.00 45.38

ATOM 9568 O HOH W 289 10.793 13.789 11.027 1.00 37.69

ATOM 9571 O HOH W 290 29.947 26.979 3.155 1.00 48.59

ATOM 9574 O HOH W 291 22.747 32.911 55.879 1.00 44.16

ATOM 9577 O HOH W 292 57.364 0.776 20.520 1.00 57.48

ATOM 9580 O HOH W 293 43.713 46.201 10.366 1.00 53.05

ATOM 9583 O HOH W 294 33.545 25.253 27.484 1.00 37.96

ATOM 9586 O HOH W 295 23.471 9.078 9.606 1.00 47.67

ATOM 9589 O HOH W 296 34.017 38.165 26.875 1.00 44.91

ATOM 9592 O HOH W 297 40.237 8.370 11.266 1.00 43.87

ATOM 9595 O HOH W 298 34.102 20.534 5.550 1.00 40.60

ATOM 9598 O HOH W 299 31.764 7.796 25.125 1.00 34.39

ATOM 9601 O HOH W 300 11.789 29.825 40.382 1.00 37.06

ATOM 9604 O HOH W 301 30.233 44.827 11.200 1.00 49.80

ATOM 9607 O HOH W 302 55.069 13.992 21.681 1.00 59.64

ATOM 9610 O HOH W 303 41.717 44.487 12.136 1.00 57.39

ATOM 9613 O HOH W 304 6.965 25.237 13.790 1.00 37.15

ATOM 9616 O HOH W 305 24.424 -4.845 34.943 1.00 30.59

ATOM 9619 O HOH W 306 37.706 20.419 70.354 1.00 56.88

ATOM 9622 O HOH W 307 29.718 1.671 12.779 1.00 34.34

ATOM 9625 O HOH W 308 17.831 3.205 17.264 1.00 50.98

ATOM 9628 O HOH W 309 60.412 34.150 26.772 1.00 56.44

ATOM 9631 O HOH W 310 31.802 3.624 4.729 1.00 59.01

ATOM 9634 O HOH W 311 39.047 25.459 24.473 1.00 59.19

ATOM 9637 O HOH W 312 39.009 26.005 4.703 1.00 41.41

ATOM 9640 O HOH W 313 10.162 28.983 18.424 1.00 43.68

ATOM 9643 O HOH W 314 39.814 5.145 3.412 1.00 58.17

ATOM 9646 O HOH W 315 12.915 16.721 46.528 1.00 53.68

ATOM 9649 O HOH W 316 41.617 26.712 25.289 1.00 41.08

ATOM 9652 O HOH W 317 66.746 36.447 29.443 1.00 53.77

ATOM 9655 O HOH W 318 30.613 35.474 8.019 1.00 42.66

ATOM 9658 O HOH W 319 32.819 16.871 6. Ill 1.00 47.91

ATOM 9661 O HOH W 320 27.743 32.666 38.604 1.00 29.67

ATOM 9664 O HOH W 321 40.010 29.976 14.180 1.00 30.61

ATOM 9667 O HOH W 322 29.210 44.736 15.791 1.00 24.53

ATOM 9670 O HOH W 323 37.994 25.708 21.918 1.00 29.20

ATOM 9673 O HOH W 324 38.189 26.898 16.899 1.00 27.26

ATOM 9676 O HOH W 325 20.950 15.241 49.017 1.00 39.69

ATOM 9679 O HOH W 326 38.406 7.893 36.254 1.00 34.04

Table 2

Table 2 details data collection and refinement statistics for a typical crystal of the present invention. The following definitions are used for the associated data statistics of table 2: (f ) Rfactor = ∑IIi-<Ii>l I/∑IIJ where I₁ is the scaled intensity of the ith measurement, and <Ij> is the mean intensity for that reflection.

(*) R_free = as for Rc_ryst, but for 5.0% of the total reflections chosen at random and omitted from refinement.

Table 2

[0080] The amino acid residues that are of particular interest to the invention for designing compounds that modulate PCSK9 activity are detailed in Table 3, infra.

Table 3

Table 3 lists sets of amino acid residues identified around key surface and active site areas across the three domains of PCSK9 where compounds or polypeptide could interact with and modulate the activity of PCSK9. These sites can be used for designing compounds or polypeptides to interact with PCSK9 using their associated 3-dimensional coordinates from table 1, supra.

Residue Number Region

PRO 75 Region of S127R mutation in Pro domain GLY 76 Region of S127R mutation in Pro domain

THR 77 Region of S127R mutation in Pro domain

TYR 78 Region of S127R mutation in Pro domain

ALA 102 Region of S127R mutation in Pro domain

GLY 106 Region of S127R mutation in Pro domain

TYR 107 Region of S127R mutation in Pro domain

LEU 108 Region of S127R mutation in Pro domain

THR 109 Region of S127R mutation in Pro domain

LYS 1 10 Region of S127R mutation in Pro domain

VAL 124 Region of S 127R mutation in Pro domain

LYS 125 Region of S 127R mutation in Pro domain

M ET 126 Region of S 127R mutation in Pro domain

SER 127 Region of S127R mutation in Pro domain

GLY 128 Region of S 127R mutation in Pro domain

AS P 129 Region of S 127R mutation in Pro domain

LEU 130 Region of S127R mutation in Pro domain

LEU 131 Region of S 127R mutation in Pro domain

ARG 73 Region around S4 Pocket

ASP 146 Region around S4 Pocket

SER 147 Region around S4 Pocket

SER 262 Region around S4 Pocket

GLY 263 Region around S4 Pocket

THR 264 Region around S4 Pocket

TYR 325 Region around S4 Pocket

SER 326 Region around S4 Pocket

PRO 327 Region around S4 Pocket

TRP 72 Region around S3 pocket

SER 148 Region around S3 pocket

THR 260 Region around S3 pocket

VAL 261 Region around S3 pocket

GLY 292 Region around S3 pocket

LEU 185 Region Around S2 pocket

THR 187 Region Around S2 pocket

GLY 227 Region Around S2 pocket

VAL 252 Region Around S2 pocket

LEU 253 Region Around S2 pocket

ASN 254 Region Around S2 pocket

GLN 256 Region Around S2 pocket

GLY 259 Region Around S2 pocket

VAL 149 P4 residue

PHE 150 P3 residue

ALA 151 P2 residue

GLN 152 Pl residue

ASP 186 Region around Sl pocket 152

HIS 226 Region around Sl pocket 152 GLY 257 Region around Sl pocket 152

LYS 258 Region around Sl pocket 152

LEU 287 Region around Sl pocket 152

PRO 288 Region around Sl pocket 152

LEU 289 Region around Sl pocket 152

ALA 290 Region around S 1 pocket 152

GLY 291 Region around Sl pocket 152

THR 313 Region around Sl pocket 152

ALA 314 Region around Sl pocket 152

ALA 315 Region around Sl pocket 152

GLY 316 Region around Sl pocket 152

ASN 317 Region around Sl pocket 152

PHE 318 Region around S 1 pocket 152

THR 353 Region around Sl pocket 152

SER 383 Region around Sl pocket 152

GLY 384 Region around Sl pocket 152

THR 385 Region around Sl pocket 152

SER 386 Region around Sl pocket 152

GLN 387 Region around Sl pocket 152

ALA 388 Region around Sl pocket 152

ALA 389 Region around Sl pocket 152

GLN 190 Region around gain of function mutation D374Y

HIS 193 Region around gain of function mutation D374Y

ALA 220 Region around gain of function mutation D374Y

SER 221 Region around gain of function mutation D374Y

LYS 222 Region around gain of function mutation D374Y

ASP 224 Region around gain of function mutation D374Y

SER 225 Region around gain of function mutation D374Y

THR 228 Region around gain of function mutation D374Y

ALA 371 Region around gain of function mutation D374Y

SER 372 Region around gain of function mutation D374Y

SER 373 Region around gain of function mutation D374Y

ASP 374 Region around gain of function mutation D374Y

CYS 375 Region around gain of function mutation D374Y

SER 376 Region around gain of function mutation D374Y

THR 377 Region around gain of function mutation D374Y

CYS 378 Region around gain of function mutation D374Y

PHE 379 Region around gain of function mutation D374Y

VAL 380 Region around gain of function mutation D374Y gain of function mutation associated with mutation

LEU 41 1 H417Q gain of function mutation associated with mutation

ARG 412 H417Q gain of function mutation associated with mutation

GLN 413 H417Q gain of function mutation associated with mutation

ARG 414 H417Q

LEU 415 gain of function mutation associated with mutation H417Q gain of function mutation associated with mutation ILE 416 H417Q gain of function mutation associated with mutation HIS 417 H417Q gain of function mutation associated with mutation PHE 418 H417Q gain of function mutation associated with mutation SER 419 H417Q gain of function mutation associated with mutation ALA 420 H417Q gain of function mutation associated with mutation LYS 421 H417Q gain of function mutation associated with mutation LEU 440 H417Q gain of function mutation associated with mutation ALA 442 H417Q gain of function mutation associated with mutation ALA 443 H417Q gain of function mutation associated with mutation PRO 445 H417Q gain of function mutation associated with mutation PHE 456 H417Q gain of function mutation associated with mutation ARG 458 H417Q gain of function mutation associated with mutation ASP 651 H417Q

Putative binding region of DRD associated with SER 462 R469W mutation Resistin like domain

Putative binding region of DRD associated with ALA 463 R469W mutation Resistin like domain

Putative binding region of DRD associated with HIS 464 R469W mutation Resistin like domain

Putative binding region of DRD associated with SER 465 R469W mutation Resistin like domain

Putative binding region of DRD associated with GLY 466 R469W mutation Resistin like domain

Putative binding region of DRD associated with PRO 467 R469W mutation Resistin like domain

Putative binding region of DRD associated with THR 468 R469W mutation Resistin like domain

Putative binding region of DRD associated with ARG 469 R469W mutation Resistin like domain

Putative binding region of DRD associated with MET 470 R469 W mutation Resistin like domain

Putative binding region of DRD associated with ALA 471 R469W mutation Resistin like domain

Putative binding region of DRD associated with THR 472 R469W mutation Resistin like domain Putative binding region of DRD associated with HIS 512 R469W mutation Resistin like domain

Putative binding region of DRD associated with ASN 513 R469W mutation Resistin like domain

Putative binding region of DRD associated with ALA 514 R469W mutation Resistin like domain

Putative binding region of DRD associated with PHE 515 R469W mutation Resistin like domain

Putative binding region of DRD associated with GLY 516 R469W mutation Resistin like domain

Putative binding region of DRD associated with GLY 517 R469W mutation Resistin like domain

Putative binding region of DRD associated with GLU 518 R469W mutation Resistin like domain

Putative binding region of DRD associated with GLY 519 R469W mutation Resistin like domain

CYS 457 Region around gain-of-function mutation E482G

ARG 476 Region around gain-of-function mutation E482G

CYS 477 Region around gain-of-function mutation E482G

ALA 478 Region around gain-of-function mutation E482G

PRO 479 Region around gain-of-function mutation E482G

ASP 480 Region around gain-of-function mutation E482G

GLU 481 Region around gain-of-function mutation E482G

GLU 482 Region around gain-of-function mutation E482G

LEU 483 Region around gain-of-function mutation E482G

LEU 484 Region around gain-of-function mutation E482G

SER 485 Region around gain-of-function mutation E482G

ARG 491 Region around gain-of-function mutation E482G

SER 492 Region around gain-of-function mutation E482G

GLY 493 Region around gain-of-function mutation E482G

LYS 506 Region around gain-of-function mutation E482G

LEU 507 Region around gain-of-function mutation E482G

VAL 508 Region around gain-of-function mutation E482G

ALA 514 Region around gain-of-function mutation E482G

PHE 515 Region around gain-of-function mutation E482G

GLY 516 Region around gain-of-function mutation E482G

GLY 517 Region around gain-of-function mutation E482G

GLU 518 Region around gain-of-function mutation E482G

GLY 519 Region around gain-of-function mutation E482G

VAL 520 Region around gain-of-function mutation E482G

ALA 524 Region around gain-of-function mutation E482G

ARG 525 Region around gain-of-function mutation E482G

CYS 526 Region around gain-of-function mutation E482G

CYS 527 Region around gain-of-function mutation E482G

LEU 528 Region around gain-of-function mutation E482G

LEU 529 Region around gain-of-function mutation E482G

PRO 530 Region around gain-of-function mutation E482G

ALA 532 Region around gain-of-function mutation E482G

ASN 533 Region around gain-of-function mutation E482G CYS 534 Region around gain-of-function mutation E482G

SER 535 Region around gain-of-function mutation E482G

CYS 601 Region around gain-of-function mutation E482G

Region around resistin homologue binding region gain of function mutation F515L First lobe of resistin-like

LYS 494 binding

Region around resistin homologue binding region gain of function mutation F515L First lobe of resistin-like

ARG 495 binding

Region around resistin homologue binding region gain of function mutation F515L First lobe of resistin-like

GLU 567 binding

Region around resistin homologue binding region gain of function mutation F515L First lobe of resistin-like

VAL 568 binding

Region around resistin homologue binding region gain of function mutation F515L First lobe of resistin-like

GLU 569 binding

Region around resistin homologue binding region gain of function mutation F515L First lobe of resistin-like

ASP 570 binding

HIS 537 Region around gain of function mutation H553R

PRO 540 Region around gain of function mutation H553R

PRO 541 Region around gain of function mutation H553R

ALA 542 Region around gain of function mutation H553R

GLU 543 Region around gain of function mutation H553R

ALA 544 Region around gain of function mutation H553R

SER 545 Region around gain of function mutation H553R

MET 546 Region around gain of function mutation H553R

GLY 547 Region around gain of function mutation H553R

VAL 550 Region around gain of function mutation H553R

HIS 551 Region around gain of function mutation H553R

CYS 552 Region around gain of function mutation H553R

HIS 553 Region around gain of function mutation H553R

GLN 554 Region around gain of function mutation H553R

GLN 555 Region around gain of function mutation H553R

GLY 556 Region around gain of function mutation H553R

HIS 557 Region around gain of function mutation H553R

VAL 558 Region around gain of function mutation H553R

LEU 559 Region around gain of function mutation H553R

GLU 567 Region around gain of function mutation H553R

VAL 568 Region around gain of function mutation H553R

GLU 569 Region around gain of function mutation H553R

ASP 570 Region around gain of function mutation H553R

LEU 571 Region around gain of function mutation H553R

GLY 572 Region around gain of function mutation H553R

PRO 585 Region around gain of function mutation H553R

ASN 586 Region around gain of function mutation H553R GLN 587 Region around gain of function mutation H553R

HIS 591 Region around gain of function mutation H553R

ARG 592 Region around gain of function mutation H553R

GLU 593 Region around gain of function mutation H553R

ALA 594 Region around gain of function mutation H553R

CYS 600 Region around gain of function mutation H553R

PRO 616 Third lobe of resistin like domain

GLN 619 Third lobe of resistin like domain

GLU 620 Third lobe of resistin like domain

GLN 621 Third lobe of resistin like domain

LEU 638 Third lobe of resistin like domain

PRO 639 Third lobe of resistin like domain

SER 642 Third lobe of resistin like domain

HIS 643 Third lobe of resistin like domain

SER 658 Third lobe of resistin like domain

ARG 659 Third lobe of resistin like domain

ALA 671 Third lobe of resistin like domain

VAL 672 Third lobe of resistin like domain

Claims

We Claim:

1. A composition comprising a polypeptide in crystalline form, wherein the polypeptide is a PCSK9 polypeptide.

2. The composition according to claim 1, wherein the PCSK9 polypeptide is the expression product of a polynucleotide encoded by the amino acid residues of SEQ. ID 1.

3. The composition according to claim 1, further comprising a binding partner suitable for co- crystallization with the PCSK9 polypeptide.

4. The composition according to claim 1, wherein the PCSK9 crystal diffracts to 1.9 Angstroms.

5. The composition according to claim 4, wherein the crystal space group is Pl₁I₁I₁.

6. The composition according to claim 5, wherein the unit cell of the crystal comprises 1 crystallographically independent PCSK9 molecules.

7. The composition according to claim 6, wherein the PCSK9 crystal has unit cell dimensions of a=62.5A, b=70.1A, c=148.6A and alpha=beta=gamma=90.0 degrees.

8. The composition according to claim 1, wherein the polypeptide is characterized by the structure coordinates according to Table 1, or a substantial part thereof.

9. A method for crystallizing a PCSK9 polypeptide, comprising: (A) mixing a solution comprising a PCSK9 polypeptide and an optional binding partner with a crystallization buffer; and (B) crystallizing the mixture of step (A) by drop vapor diffusion to form a crystalline precipitate.

10. The method of claim 9, wherein said crystallization buffer comprises 20% w/v PEG 8000 buffered with 0.1M CAPS, pH of greater than about 8.0.

11. The method of claim 9, wherein crystallization occurs at a temperature ranging from 4 to 20 degrees Celsius.

12. The method of claim 9, wherein the PCSK9 polypeptide is at a final concentration of about lOg/mL.

13. A method of identifying a compound that associates with PCSK9, comprising (A) designing a compound that associates with at least one of the sets of amino acid residues of Table 3, (B) synthesizing said compound, and (C) determining in vitro whether said compound modulates the activity of PCSK9.