Crystalline structure of human MAPKAP kinase-2

Abstract

The crystal structure of human MAPKAP kinase-2 is described, including the high-resolution X-ray diffraction structure and atomic structure coordinates obtained therefrom. A method of crystallization of MK-2 involving the use of a crystallization additive and the specific empirical conditions involved in this crystallization method is also described. This method of crystallization allows a resolution of about 3 Angstroms to be achieved. The tertiary structure of this protein as determined by X-ray crystallography to a resolution of 3 Angstroms is shown. Also described are methods by which the atomic structural information obtained from the MK-2 crystals can be used to screen for, identify and/or design new drugs.

Description

FIELD OF THE INVENTION

[0002] The present invention relates to the crystallization of human MAPKAP Kinase-2 (MK-2). More specifically, the invention relates to methods of crystallizing MK-2 and the unique empirical conditions involved in these crystallization methods. The present invention further relates to the crystal structure of human MK-2 itself, including the high-resolution X-ray diffraction structure and data obtained thereof. The MK-2 crystals of the invention and the atomic structural information obtained therefrom are useful for screening for, identifying and/or designing new drugs.

BACKGROUND OF THE INVENTION

[0003] The response of cells to extracellular stimuli is mediated in part by a number of intracellular kinase and phosphatase enzymes. The mitogen-activated protein (MAP) kinases are participants in discrete signaling cascades, or pathways which function to convert extracellular stimuli into intracellular processes. One such mitogen-activated protein kinase (MAPK) pathway is the p38 signaling transduction pathway. The p38 signaling transduction pathway plays an essential role in regulating many cellular processes including inflammation, cell differentiation, cell growth and cell death.

[0004] The p38 MAPK pathway is potentially activated by a wide variety of stresses and cellular insults. These stresses and cellular insults include heat shock, UV radiation, inflammatory cytokines (such as TNF and IL-1), tunicamycin, chemotherapeutic drugs (i.e., cisplatinum), anisomycin, sorbitol/hyperosmolarity, gamma irradiation, sodium arsenite, and ischaemia. (K. Ono, J. Han, Cellular Signalling 12 (2000) 1-13, 2.) Activation of the p38 pathway is involved in (1) production of proinflammatory cytokines such as TNF-α; (2) induction of enzymes such as COX-2, which controls connective tissue remodeling in pathological conditions; (3) expression of an intracellular enzyme such as iNOS, which plays an important role in the regulation of oxidation; (4) induction of adherent proteins such as VCAM-1 and many other inflammatory related molecules. Furthermore, the p38 pathway functions as a regulator in the proliferation and differentiation of cells of the immune system. Id. at 7.

[0005] p38 is an upstream kinase of mitogen-activated protein kinase-activated protein kinase-2 (MAPKAP kinase-2 or MK-2). (Freshney N W et al. J. Cell 1994;78:1039-49.) MK-2 is a protein which appears to be predominantly regulated by p38 in cells. Indeed, MAPKAP kinase-2 was the first substrate of p38α to be identified. For example, in vitro phosphorylation of MK-2 by p38α activates MK-2. The substrates which MAPKAP kinase-2 in turn act upon include heat shock protein 27, lymphocyte-specific protein 1 (LSP1), cAMP response element-binding protein (CREB), ATF1, SRF and tyrosine hydroxylase. The substrate of MAPKAP kinase-2 that has been best characterized is small heat shock protein 27 (hsp27). Supra at 6.

[0006] The role of the p38 pathway in inflammatory-related diseases has been studied in several animal models. SB203580 is a specific inhibitor of p38 in vivo and also has been shown to inhibit activation of MK-2. (Freshney N W et al. J.Cell 1994;78:1039-49; Rouse J, Cohen P, Trigon S, Morange M, Alonso-Llamazares A, Zamanillo D, Hunt T, Nebreda A R. Cell 1994;78:1027-37; Cuenda A, Dorow D S. Biochem J 1998;333:11-5.) Inhibition of p38 by SB203580 can reduce mortality in a murine model of endotoxin-induced shock and inhibit the development of mouse collagen-induced arthritis and rat adjuvant arthritis. (Badger A M, Bradbeer J N, Votta B, Lee J C, Adams J L, Griswold D E. J Pharmacol Exp Ther 1996;279:1453-61.) Another p38 inhibitor that has been utilized in an animal model that is believed to be more potent than SB203580 in its inhibitory effect on p38 is SB220025. A recent animal study has demonstrated that SB220025 caused a significant dose-dependent decrease in vascular density of granulomas in laboratory rats. (Jackson J R, Bolognese B, Hillegrass L, Kassis S, Adams J, Griswold D E, Winkler J D. J Pharmacol Exp Ther 1998;284:687-92.) The results of these animal studies have indicated that p38 or the components of the p38 pathway can be useful therapeutic targets for inflammatory disease.

[0007] Due to its integral role in the p38 signaling pathway, MK-2 has been used as a monitor for the level of activation in the pathway. MK-2 has been measured as a more convenient, albeit indirect, method of assessing p38 activation. However, so far research efforts have focused mainly on inhibiting p38 as a therapeutic strategy. These efforts have centered around two p38 inhibitors, the pyridinylimidazole inhibitor SKF 86002 and the 2,4,5 triaryl imidazole inhibitor SB203580. (John C. Lee et al., Inhibition of p38 MAP kinase as a therapeutic strategy”, Immunopharmacology 47 (2000), 185-201, 192.) Compounds possessing a similar structure have also been investigated as potential p38 inhibitors. Indeed, p38 MAP kinase's role in various disease states has been elucidated through the use of inhibitors. The discovery of information regarding the structural aspects of inhibitor/kinase interaction by techniques including X-ray crystallography and mutagenesis has made it possible to design second generation inhibitors with improved potency, selectivity and reduced undesirable side effects. Id. at 195.

[0008] MAPKAP kinase-2 has also been suggested as a focal point for regulating the inflammatory response. In “MAPKAP kinase 2 is essential for LPS-induced TNF-α biosynthesis” Alexey Kotlyarov et al. introduced a targeted mutation into the mouse MK-2 gene to investigate the function of MK-2 in vivo. Mice that lack MK-2 demonstrated enhanced stress resistance and were able to survive LPS-induced endotoxic shock. This phenomenon was shown to be a result of a reduction of approximately 90% in the production of TNF-α rather than being due to any change in signaling from the TNF receptor itself. The authors concluded that MK-2 regulates the biosynthesis of TNF-α at a post-transcriptional level and as such is an essential component in the inflammatory response. MAPKAP kinase-2 also has the potential advantage of being downstream from p38 in the p38 signaling transduction pathway and may as a focal point be effective in regulating the inflammatory response without affecting as many substrates as an enzyme further upstream in the signaling cascade would, such as p38 MAP kinase. By virtue of its downstream position in the p38 signaling transduction pathway, MAPKAP kinase-2 has the potential to yield inhibitors possessing similar advantages to those possessed by p38 MAP kinase inhibitors, namely, improved potency, selectivity and reduced undesirable side effects.

[0009] It would, therefore, be highly desirable to determine the structure of MK-2 in order to facilitate the identification and development of drugs for the treatment of inflammation, inflammatory diseases and related disorders. The three dimensional structure of MK-2 is expected to accelerate the drug discovery process of developing potent and selective inhibitors of MK-2.

SUMMARY OF THE INVENTION

[0010] The present invention provides the MK-2 reagent that comprises amino acid residues 45-371 of human MK-2 for obtaining crystals of MK-2. The present invention further provides the crystal structure of human MK-2. The crystal structure of MK-2 was solved utilizing crystals of a complex of MK-2 formed from MK-2 grown in the presence of a non-hydrolysable ATP analog (AMP-PNP), a 13-residue inhibitor peptide (SC-83598) and MgCl2. The X-ray crystallographic data were obtained from these crystals and the method of molecular replacement was then employed to determine the MK-2 crystal structure, using the program EPMR. The present invention thus provides a method of growing crystals by combining a solution of MK-2 polypeptide molecules with a precipitant solution containing a crystallization additive and allowing crystals of MK-2 to form using the method of vapor diffusion. Crystals formed with the use of certain crystallization additives enable the measurement of X-ray diffraction data to resolution of 3.0 Angstrom.

[0011] The present invention also provides the crystal structure of MK-2, including the mapping of the details of the ATP binding site. In a further embodiment of the invention methods are provided for screening for, identifying and/or designing new drugs using the crystal structure and data obtained thereof.

BRIEF DESCRIPTION OF THE FIGURES

[0012] FIG. 1 is a ribbon drawing of the MK-2 crystal structure.

[0013] FIG. 2 is a stereo representation of the Cα rendering of the MK-2 complex.

[0014] FIG. 3 is an electron density map of the MK-2 crystal structure.

[0015] FIG. 4 is a sequence listing (SEQ ID No. 1) of the human MK-2 protein.

[0016] FIG. 5 is a sequence listing (SEQ ID No. 2) of the portion of the human MK-2 protein, amino acid numbers 45 to37 1, which were used for obtaining crystals of MK-2 for as discussed in this application.

DETAILED DESCRIPTION OF THE INVENTION

[0017] Crystallization and Structure Determination

[0018] The crystals from which the atomic structure coordinates of the invention are derived can be obtained by conventional means as are well-known in the art of protein crystallography, including batch, liquid bridge, dialysis, and vapor diffusion methods (see, e.g., McPherson, 1982, Preparation and Analysis of Protein Crystals, John Wiley, New York; McPherson, 1990, Eur. J. Biochem. 189:1-23.; Weber, 1991, Adv. Protein Chem. 41:1-36.). It is well known that the processes for obtaining crystals of particular proteins are individual to each protein. In a preferred embodiment, co-crystals are grown by the method of vapor diffusion involving hanging/sitting drops (McPherson, 1982, Preparation and Analysis of Protein Crystals, John Wiley, New York; McPherson, 1990, Eur. J. Biochem. 189:1-23.). In this method, the protein solution is allowed to equilibrate in a closed container with a larger aqueous reservoir having a precipitant concentration optimal for producing crystals. In general, approximately 2-5 μL of substantially pure polypeptide solution is mixed with an equal volume of reservoir solution, giving a precipitant concentration about half that required for crystallization. This solution is suspended as a droplet on a coverslip, which is then sealed on the top of the reservoir. The sealed container is allowed to stand, usually for about 2-6 weeks, until co-crystals grow.

[0019] Following this general procedure the co-crystals were grown by sitting drop vapor diffusion. Specifically, a protein solution was prepared consisting of 1.5-5 mg/mL MK-2(45-371) in 50 mM Tris at a pH of about 8 to 9 and containing around 15-50 mM NaCl, 2 mM DTT and 5% glycerol. This protein solution was mixed in a 1:1 ratio with a reservoir solution containing around 1.6-2.6M ammonium sulfate and 100 mM sodium acetate, the reservoir solution being at a pH of between around 4.2-5.4. Small bipyramidal or prism-shaped crystals appeared in the drops in 1-2 days and grew to as large as 0.4 mm×0.4 mm in about 1 to 3 weeks.

[0020] The process of crystallization was facilitated with the use of certain additives. These additives were selected from those additives that improve crystallization generally. Such additives can be divalent cations, non-volatile organic compounds, amphiphiles, ions, reducing agents, chelators, co-factors, carbohydrates, polyamines, linkers, polymers, solubilizing agents, dissociating agents, charotropes, detergents and salts. Many of the crystallization additives are salts. Examples of suitable crystallization additives are listed in Table 1 below.

TABLE 1
acetone
Anapoe ® C13E8
Anapoe ® X-114,
Cymal ®-1
C-HEGA-8 ™
C12E8
deoxy-BigChap
dichloromethane
dimethyl sulfoxide
1,4-dithio-DL-threitol (DTT)
EDTA sodium salt
ethanol
FOS-Choline ® 9
D(+) glucose
glycine
glycyl-glycyl-glycine
magnesium chloride
methanol
NAD+
n-dodecyl- -D-maltoside
n-hexadecyl- -D-maltoside
n-tetradecyl- -D-maltoside
n-tridecyl- -D-maltoside
1,3-propanediol
sodium fluoride
spermidine
spermidine-tetra-HCl
strontium chloride hexahydrate
tert-butanol
trimethylamine hydrochloride
TRITON X-100
urea
yttrium chloride hexahydrate

[0021] The additives of Table 1 are commercially available as crystallization Additive Screen kits I, II and III and Detergent Screens I, II, and III from Hampton Research Company, San Diego, Calif. Other additives, other additive screen kits and detergent screen kits can be used to identify additives which, when added to the aforementioned crystallization conditions, can facilitate crystallization. These additives can be added at a concentration of from between about 0 mM to about 150 mM. Preferably, the concentration of the additives is between about 3 mM to about 50 mM. More preferably, the concentration is around 5 mM to about 30 mM. Even more preferably, the concentration is between about 10 mM to about 20 mM.

[0022] The crystallization of molecules from solution is a reversible equilibrium process, and the kinetic and thermodynamic parameters are a function of the chemical and physical properties of the solvent system and solute of interest (McPherson, A., In: Preparation and Analysis of Protein Crystals, Wiley Interscience (1982); Weber, P. C., Adv. Protein Chem. 41:1-36 (1991)) 1991). Under supersaturating conditions, the system is driven toward equilibrium where the solute is partitioned between the soluble and solid phase instead of the unfolded and native states. The molecules in the crystalline phase pack in ordered and periodic three dimensional arrays that are energetically dominated by many of the same types of cohesive forces that are important for protein folding, i.e. van der Waals interactions, electrostatic interactions, hydrogen bonds, and covalent bonds (Moore, W. J., In: Physical Chemistry, 4th Ed., Prentice Hall, (1972), pp. 865-898).

[0023] Thus, in many ways protein crystallization can be viewed as a higher level variation of protein folding where whole molecules are packed to maximize cohesive energies instead of individual amino acid residues. Moreover, for both protein crystallization and protein folding, the composition of the solvent can make very important contributions to the extent of partitioning between the soluble (unfolded) and crystalline (native) forms. The cohesive interactions present in protein macromolecules and the role played by solvent in modulating these interactions for both protein folding and protein crystallization are complex and not fully understood at the present time. Without intending to be bound by any theory, it is believed that the crystallization additives participate in modulating these cohesive interactions in a manner that is advantageous to stability in the crystalline state.

[0024] The crystal structure was solved using crystals of MK-2 grown in the presence of a non-hydrolyzable ATP analog (AMP-PNP), a 13-residue inhibitor peptide (SC-83598) (KKKALLRQLGVAA) and MgCl2. The structure of the inhibitor peptide SC-83598 is shown in Structure 1.

[0025] SC-83598 (inhibitor peptide) 1

[0026] The structure of AMP-PNP is shown in Structure 2. 2

[0027] AMP-PNP (adenosine 5′-[β,gamma-imido] triphosphate tetralithium salt hydrate

[0028] The MK-2 crystal structure that was obtained is shown in FIG. 1. The non-hydrolysable ATP analog (AMP-PNP) can be seen bound at the ATP site of MK-2 in the ribbon drawing in FIG. 1. Although residual electron density is visible at the site that is known to bind peptide substrate in protein kinases, the inhibitor peptide (SC83598) has not been modeled in the current structure.

[0029] A stereo representation of the Cox rendering of the MK-2 complex is shown in FIG. 2. The AMP-PNP bound at the ATP site of MK-2 is also visible in this Calpha drawing of the MK-2 complex.

[0030] This complex of MK-2 was formed using enzyme/peptide/Mg2+/AMP-PNP molar ratios of 1:3:5:20, in a manner similar to that used in crystallizing a ternary complex of c-AMP-dependent protein kinase, as described by Zheng et al. in Crystal Structure of the Catalytic Subunit of cAMP-Dependent Protein Kinase Complexed with MgATP and Peptide Inhibitor, Biochemistry, 1993, Vol.32, No. 9, pages 2154-2161. The procedure used to form the ternary complex of c-AMP-dependent protein kinase is described specifically in the second paragraph of the first column of page 2155.

[0031] The dimensions of a unit cell of a crystal are defined by six numbers, the lengths of three unique edges, a, b, and c, and three unique angles α, β, and, γ. The type of unit cell that comprises a crystal is dependent on the value of these variables and the various symmetry elements that are present within the unit cell. The MK-2 crystal has a face-centered cubic lattice having the space group of F4132, and contain a single copy of the ternary complex in the asymmetic unit. The unit cell dimensions are about 254.8 (+/−2) Angstroms along the three edges. The unit cell contains 96 MK-2 molecules.

[0032] Of course, the processes for obtaining crystals of particular proteins are individual to each protein. Also, the presence of ligands can have a profound effect on the crystallization of a given protein. Thus, the processes for crystallizing the MK-2 protein, as with any protein, would change with a concomitant change in the MK-2 protein itself. For example, mutant proteins may crystallize under slightly different crystallization conditions compared to the wild-type protein, or under entirely new crystallization conditions, depending on the nature of the mutation, and its location in the protein. For example, a non-conservative mutation may result in alteration of the hydrophilicity of the mutant, which may in turn make the mutant protein either more soluble or less soluble than the wild-type protein. Typically, if a protein becomes more hydrophilic as a result of a mutation, it will be more soluble than the wild-type protein in an aqueous solution and a higher precipitant concentration will be needed to cause it to crystallize. Conversely, if a protein becomes less hydrophilic as a result of a mutation, it will be less soluble in an aqueous solution and a lower precipitant concentration will be needed to cause it to crystallize. If the mutation happens to be in a region of the protein involved in crystal lattice contacts, crystallization conditions may be affected in more unpredictable ways.

[0033] X-Ray Diffraction

[0034] The diffraction data from X-ray crystallography is generally obtained as follows. When a crystal is placed in an X-ray beam, the incident X-rays interact with the electron cloud of the molecules that make up the crystal, resulting in X-ray scatter. The combination of X-ray scatter with the lattice of the crystal gives rise to nonuniformity of the scatter; areas of high intensity are called diffracted X-rays. The angle at which diffracted beams emerge from the crystal can be computed by treating diffraction as if it were reflection from sets of equivalent, parallel planes of atoms in a crystal (Bragg's Law). The most obvious sets of planes in a crystal lattice are those that are parallel to the faces of the unit cell. These and other sets of planes can be drawn through the lattice points. Each set of planes is identified by three indices, hk1. The h index gives the number of parts into which the a edge of the unit cell is cut, the k index gives the number of parts into which the b edge of the unit cell is cut, and the 1 index gives the number of parts into which the c edge of the unit cell is cut by the set of hk1 planes. Thus, for example, the 235 planes cut the a edge of each unit cell into halves, the b edge of each unit cell into thirds, and the c edge of each unit cell into fifths. Planes that are parallel to the bc face of the unit cell are the 100 planes; planes that are parallel to the ac face of the unit cell are the 010 planes; and planes that are parallel to the ab face of the unit cell are the 001 planes.

[0035] When a detector is placed in the path of the diffracted X-rays, in effect cutting into the sphere of diffraction, a series of spots, or reflections, are recorded to produce a “still” diffraction pattern. Each reflection is the result of X-rays reflecting off one set of parallel planes, and is characterized by an intensity, which is related to the distribution of molecules in the unit cell, and hk1 indices, which correspond to the parallel planes from which the beam producing that spot was reflected. If the crystal is rotated about an axis perpendicular to the X-ray beam, a large number of reflections is recorded on the detector, resulting in a diffraction pattern.

[0036] The unit cell dimensions and space group of a crystal can be determined from its diffraction pattern. First, the spacing of reflections is inversely proportional to the lengths of the edges of the unit cell. Therefore, if a diffraction pattern is recorded when the X-ray beam is perpendicular to a face of the unit cell, two of the unit cell dimensions may be deduced from the spacing of the reflections in the x and y directions of the detector, the crystal-to-detector distance, and the wavelength of the X-rays. Those of skill in the art will appreciate that, in order to obtain all three unit cell dimensions, the crystal must be rotated such that the X-ray beam is perpendicular to another face of the unit cell. Second, the angles of a unit cell can be determined by the angles between lines of spots on the diffraction pattern. Third, the absence of certain reflections and the repetitive nature of the diffraction pattern, which may be evident by visual inspection, indicate the internal symmetry, or space group, of the crystal. Therefore, a crystal may be characterized by its unit cell and space group, as well as by its diffraction pattern.

[0037] Once the dimensions of the unit cell are determined, the likely number of polypeptides in the asymmetric unit can be deduced from the size of the polypeptide, the density of the average protein, and the typical solvent content of a protein crystal, which is usually in the range of 30-70% of the unit cell volume.

[0038] The diffraction pattern is related to the three-dimensional shape of the molecule by a Fourier transform. The process of determining the solution is in essence a re-focusing of the diffracted X-rays to produce a three-dimensional image of the molecule in the crystal. Since re-focusing of X-rays cannot be done with a lens at this time, it is done via mathematical operations.

[0039] The sphere of diffraction has symmetry that depends on the internal symmetry of the crystal, which means that certain orientations of the crystal will produce the same set of reflections. Thus, a crystal with high symmetry has a more repetitive diffraction pattern, and there are fewer unique reflections that need to be recorded in order to have a complete representation of the diffraction. The goal of data collection, a dataset, is a set of consistently measured, indexed intensities for as many reflections as possible. A complete dataset is collected if at least 80%, preferably at least 90%, most preferably at least 95% of unique reflections are recorded. In one embodiment, a complete dataset is collected using one crystal. In another embodiment, a complete dataset is collected using more than one crystal of the same type.

[0040] Sources of X-rays include, but are not limited to, a rotating anode X-ray generator such as a Rigaku RU-200 or a beamline at a synchrotron light source, such as the Advanced Photon Source at Argonne National Laboratory. Suitable detectors for recording diffraction patterns include, but are not limited to, X-ray sensitive film, multiwire area detectors, image plates coated with phosphorus, and CCD cameras. Typically, the detector and the X-ray beam remain stationary, so that, in order to record diffraction from different parts of the crystal's sphere of diffraction, the crystal itself is moved via an automated system of moveable circles called a goniostat.

[0041] One of the biggest problems in data collection, particularly from macromolecular crystals having a high solvent content, is the rapid degradation of the crystal in the X-ray beam. In order to slow the degradation, data is often collected from a crystal at liquid nitrogen temperatures. In order for a crystal to survive the initial exposure to liquid nitrogen, the formation of ice within the crystal must be prevented by the use of a cryoprotectant. Suitable cryoprotectants include, but are not limited to, low molecular weight polyethylene glycols, ethylene glycol, sucrose, glycerol, xylitol, and combinations thereof. Crystals may be soaked in a solution comprising one or more cryoprotectants prior to exposure to liquid nitrogen, or the one or more cryoprotectants may be added to the crystallization solution. Data collection at liquid nitrogen temperatures may allow the collection of an entire dataset from one crystal.

[0042] Initial crystals of the MK-2 complex diffracted typically to about 4-5 Angstoms. This diffraction data was acquired at the Advanced Photon Source at Argonne National Laboratory. However, co-crystals grown in the presence of various additives allowed an improved resolution to be achieved. These additives are selected from those additives that improve crystallization generally. These preferred crystallization additives include deoxy-BigChap, n-hexadecyl-beta-D-maltoside, n-tridecyl-beta-D-maltoside, and Yttrium chloride hexahydrate. These preferred additives both facilitate the formation of crystals and allow an improved resolution to be achieved in X-ray diffraction. These preferred additives can be added at a concentration of from between about 0 mM to about 20 mM. Preferably, the concentration of the additives is between about 10 mM to about 20 mM.

[0043] Thus, preferred conditions for both crystallization and diffraction include concentrations of deoxy-BigChap, n-hexadecyl-beta-D-maltoside, Yttrium chloride hexahydrate or n-tridecyl-beta-D-maltoside between about 0 mM to about 20 mM, more preferably between about 10 mM to about 20 mM. Co-crystals of MK-2, AMP-PNP, magnesium, and SC-83598 grown in the presence of these additives can diffract to a resolution of better than 4-5 Angstroms. Preferably, the co-crystals of MK-2, AMP-PNP, magnesium, and SC-83598 grown in the presence of these additives can diffract to a resolution of better than 3.5 Angstroms. More preferably, the co-crystals of MK-2, AMP-PNP, magnesium, and SC-83598 grown in the presence of these additives can diffract to a resolution of between about 2.5 to about 3.3 Angstroms. This improved diffraction yielded the diffraction data summarized in Table 2.

TABLE 2
Summary of Diffraction Data From MK-2 Crystals
	Data Set	Crystal (1)	Crystal (2)	Crystal (3)
	Resolution (A)	40.0-3.0	40.0-3.3	40.0-3.3
	Rsymm	7.7	8.6	7.6
	Completeness	94.4	97.4	96.6
	Redundancy	6.0	7.1	4.8
	Cell edge (A)	254.0	253.5	253.5

[0044] The three dimensional (x, y, z) coordinates of MK-2 are shown below in Table 3 in the standard Protein Data Bank (PDB) format. (Bernstein F. C., et al. J. Mol. Biol. (1977) 122, 535).

TABLE 3
ATOM	1	CB	GLN	45	102.406	264.041	78.035	1.00	100.00	6
ATOM	2	CG	GLN	45	103.925	264.125	78.221	1.00	100.00	6
ATOM	3	CD	GLN	45	104.542	265.347	77.549	1.00	100.00	6
ATOM	4	OE1	GLN	45	103.923	265.981	76.687	1.00	100.00	8
ATOM	5	NE2	GLN	45	105.769	265.683	77.946	1.00	97.48	7
ATOM	6	C	GLN	45	102.013	263.395	80.451	1.00	99.88	6
ATOM	7	O	GLN	45	102.125	262.501	81.293	1.00	100.00	8
ATOM	8	N	GLN	45	100.218	263.114	78.730	1.00	100.00	7
ATOM	9	CA	GLN	45	101.684	263.066	78.985	1.00	100.00	6
ATOM	10	N	PHE	46	102.123	264.685	80.746	1.00	95.46	7
ATOM	11	CA	PHE	46	102.439	265.167	82.082	1.00	89.46	6
ATOM	12	CB	PHE	46	103.465	266.301	81.948	1.00	87.16	6
ATOM	13	CG	PHE	46	104.122	266.716	83.238	1.00	74.67	6
ATOM	14	CD1	PHE	46	105.202	266.009	83.742	1.00	67.95	6
ATOM	15	CD2	PHE	46	103.722	267.873	83.895	1.00	67.67	6
ATOM	16	CE1	PHE	46	105.872	266.457	84.876	1.00	66.39	6
ATOM	17	CE2	PHE	46	104.391	268.322	85.029	1.00	59.60	6
ATOM	18	CZ	PHE	46	105.464	267.618	85.518	1.00	57.34	6
ATOM	19	C	PHE	46	101.180	265.661	82.790	1.00	86.96	6
ATOM	20	O	PHE	46	100.750	266.802	82.583	1.00	83.75	8
ATOM	21	N	HIS	47	100.547	264.775	83.558	1.00	86.89	7
ATOM	22	CA	HIS	47	99.336	265.152	84.286	1.00	87.76	6
ATOM	23	CB	HIS	47	98.081	264.344	83.878	1.00	90.07	6
ATOM	24	CG	HIS	47	98.312	262.879	83.676	1.00	92.87	6
ATOM	25	CD2	HIS	47	97.520	261.927	83.126	1.00	94.34	6
ATOM	26	ND1	HIS	47	99.474	262.238	84.051	1.00	99.02	7
ATOM	27	CEl	HIS	47	99.389	260.957	83.740	1.00	100.00	6
ATOM	28	NE2	HIS	47	98.213	260.742	83.177	1.00	98.84	7
ATOM	29	C	HIS	47	99.535	265.156	85.791	1.00	78.29	6
ATOM	30	O	HIS	47	99.327	264.152	86.474	1.00	79.69	8
ATOM	31	N	VAL	48	99.998	266.305	86.274	1.00	66.71	7
ATOM	32	CA	VAL	48	100.257	266.532	87.680	1.00	55.57	6
ATOM	33	CB	VAL	48	101.402	267.540	87.896	1.00	55.61	6
ATOM	34	CG1	VAL	48	102.703	266.958	87.434	1.00	63.49	6
ATOM	35	CG2	VAL	48	101.120	268.829	87.152	1.00	52.37	6
ATOM	36	C	VAL	48	99.018	267.134	88.296	1.00	52.63	6
ATOM	37	O	VAL	48	98.098	267.558	87.604	1.00	49.40	8
ATOM	38	N	LYS	49	99.016	267.195	89.613	1.00	47.32	7
ATOM	39	CA	LYS	49	97.903	267.750	90.339	1.00	46.17	6
ATOM	40	CB	LYS	49	97.024	266.633	90.872	1.00	41.03	6
ATOM	41	CG	LYS	49	96.542	265.715	89.795	1.00	38.47	6
ATOM	42	CD	LYS	49	95.346	264.941	90.240	1.00	52.41	6
ATOM	43	CE	LYS	49	94.601	264.454	89.019	1.00	67.61	6
ATOM	44	NZ	LYS	49	94.186	265.601	88.160	1.00	75.30	7
ATOM	45	C	LYS	49	98.475	268.576	91.470	1.00	49.70	6
ATOM	46	O	LYS	49	99.553	268.289	91.971	1.00	53.57	8
ATOM	47	N	SER	50	97.738	269.591	91.885	1.00	51.51	7
ATOM	48	CA	SER	50	98.168	270.475	92.956	1.00	52.26	6
ATOM	49	CB	SER	50	97.079	271.519	93.208	1.00	56.64	6
ATOM	50	OG	SER	50	95.897	270.905	93.693	1.00	70.83	8
ATOM	51	C	SER	50	98.526	269.797	94.272	1.00	50.52	6
ATOM	52	O	SER	50	98.013	268.731	94.606	1.00	52.72	8
ATOM	53	N	GLY	51	99.423	270.430	95.013	1.00	43.31	7
ATOM	54	CA	GLY	51	99.808	269.910	96.306	1.00	46.43	6
ATOM	55	C	GLY	51	98.828	270.392	97.358	1.00	44.12	6
ATOM	56	O	GLY	51	97.862	271.083	97.031	1.00	46.55	8
ATOM	57	N	LEU	52	99.080	270.055	98.620	1.00	46.67	7
ATOM	58	CA	LEU	52	98.184	270.464	99.688	1.00	47.87	6
ATOM	59	CB	LEU	52	98.407	269.615	100.936	1.00	47.72	6
ATOM	60	CG	LEU	52	97.329	269.600	102.026	1.00	48.14	6
ATOM	61	CD1	LEU	52	97.805	270.396	103.182	1.00	46.08	6
ATOM	62	CD2	LEU	52	95.987	270.114	101.531	1.00	50.92	6
ATOM	63	C	LEU	52	98.296	271.952	100.003	1.00	51.25	6
ATOM	64	O	LEU	52	99.373	272.471	100.277	1.00	52.03	8
ATOM	65	N	GLN	53	97.150	272.621	99.937	1.00	52.39	7
ATOM	66	CA	GLN	53	97.028	274.050	100.198	1.00	55.58	6
ATOM	67	CB	GLN	53	96.029	274.673	99.201	1.00	73.54	6
ATOM	68	CG	GLN	53	95.030	273.678	98.466	1.00	86.15	6
ATOM	69	CD	GLN	53	94.026	272.909	99.373	1.00	86.10	6
ATOM	70	OE1	GLN	53	93.195	273.506	100.080	1.00	82.19	8
ATOM	71	NE2	GLN	53	94.075	271.579	99.299	1.00	76.86	7
ATOM	72	C	GLN	53	96.545	274.341	101.612	1.00	50.45	6
ATOM	73	O	GLN	53	95.340	274.300	101.876	1.00	52.43	8
ATOM	74	N	ILE	54	97.456	274.645	102.528	1.00	41.32	7
ATOM	75	CA	ILE	54	97.010	274.931	103.886	1.00	37.32	6
ATOM	76	CB	ILE	54	98.045	274.544	104.948	1.00	35.94	6
ATOM	77	CG2	ILE	54	97.562	274.953	106.326	1.00	40.25	6
ATOM	78	CG1	ILE	54	98.205	273.026	104.951	1.00	38.37	6
ATOM	79	CD1	ILE	54	99.236	272.482	105.925	1.00	40.44	6
ATOM	80	C	ILE	54	96.590	276.378	104.035	1.00	34.42	6
ATOM	81	O	ILE	54	97.386	277.232	104.376	1.00	37.32	8
ATOM	82	N	LYS	55	95.316	276.627	103.765	1.00	35.43	7
ATOM	83	CA	LYS	55	94.714	277.955	103.850	1.00	38.05	6
ATOM	84	CB	LYS	55	93.238	277.872	103.420	1.00	40.98	6
ATOM	85	CG	LYS	55	92.991	277.575	101.941	1.00	47.96	6
ATOM	86	CD	LYS	55	91.513	277.259	101.681	1.00	55.91	6
ATOM	87	CE	LYS	55	91.084	277.555	100.236	1.00	61.30	6
ATOM	88	NZ	LYS	55	91.809	276.754	99.214	1.00	66.90	7
ATOM	89	C	LYS	55	94.786	278.503	105.283	1.00	37.65	6
ATOM	90	O	LYS	55	94.303	277.856	106.219	1.00	34.81	8
ATOM	91	N	LYS	56	95.385	279.683	105.456	1.00	34.35	7
ATOM	92	CA	LYS	56	95.487	280.266	106.789	1.00	31.71	6
ATOM	93	CB	LYS	56	96.803	281.023	107.004	1.00	32.85	6
ATOM	94	CG	LYS	56	98.060	280.388	106.414	1.00	46.33	6
ATOM	95	CD	LYS	56	98.249	278.923	106.766	1.00	46.90	6
ATOM	96	CE	LYS	56	98.461	278.723	108.238	1.00	58.39	6
ATOM	97	NZ	LYS	56	99.749	279.306	108.684	1.00	77.25	7
ATOM	98	C	LYS	56	94.316	281.181	107.149	1.00	31.86	6
ATOM	99	O	LYS	56	94.136	281.501	108.317	1.00	39.82	8
ATOM	100	N	ASN	57	93.501	281.584	106.177	1.00	25.32	7
ATOM	101	CA	ASN	57	92.358	282.462	106.473	1.00	29.61	6
ATOM	102	CB	ASN	57	91.746	282.991	105.191	1.00	30.38	6
ATOM	103	CG	ASN	57	91.062	281.921	104.396	1.00	30.96	6
ATOM	104	OD1	ASN	57	89.852	281.729	104.524	1.00	36.24	8
ATOM	105	ND2	ASN	57	91.821	281.226	103.549	1.00	29.49	7
ATOM	106	C	ASN	57	91.275	281.774	107.317	1.00	30.61	6
ATOM	107	O	ASN	57	91.218	280.547	107.378	1.00	33.98	8
ATOM	108	N	ALA	58	90.404	282.550	107.956	1.00	32.03	7
ATOM	109	CA	ALA	58	89.351	281.955	108.785	1.00	30.01	6
ATOM	110	CB	ALA	58	88.490	283.007	109.431	1.00	26.97	6
ATOM	111	C	ALA	58	88.516	281.086	107.913	1.00	32.48	6
ATOM	112	O	ALA	58	88.212	281.465	106.801	1.00	36.61	8
ATOM	113	N	ILE	59	88.153	279.915	108.410	1.00	35.25	7
ATOM	114	CA	ILE	59	87.345	278.997	107.633	1.00	36.12	6
ATOM	115	CB	ILE	59	87.232	277.658	108.349	1.00	33.16	6
ATOM	116	CG2	ILE	59	86.502	277.850	109.647	1.00	29.32	6
ATOM	117	CG1	ILE	59	86.528	276.639	107.448	1.00	34.35	6
ATOM	118	CD1	ILE	59	86.239	275.315	108.122	1.00	40.00	6
ATOM	119	C	ILE	59	85.957	279.595	107.430	1.00	39.31	6
ATOM	120	O	ILE	59	85.263	279.312	106.450	1.00	43.48	8
ATOM	121	N	ILE	60	85.607	280.486	108.344	1.00	37.34	7
ATOM	122	CA	ILE	60	84.335	281.173	108.349	1.00	34.72	6
ATOM	123	CB	ILE	60	84.182	281.920	109.703	1.00	34.16	6
ATOM	124	CG2	ILE	60	84.411	283.431	109.592	1.00	23.79	6
ATOM	125	CG1	ILE	60	82.860	281.544	110.314	1.00	36.06	6
ATOM	126	CD1	ILE	60	82.728	280.073	110.483	1.00	48.15	6
ATOM	127	C	ILE	60	84.088	282.072	107.139	1.00	41.20	6
ATOM	128	O	ILE	60	82.940	282.341	106.777	1.00	46.55	8
ATOM	129	N	ASP	61	85.165	282.515	106.501	1.00	37.84	7
ATOM	130	CA	ASP	61	85.069	283.376	105.332	1.00	35.17	6
ATOM	131	CB	ASP	61	86.431	284.007	105.010	1.00	32.16	6
ATOM	132	CG	ASP	61	86.998	284.841	106.175	1.00	57.04	6
ATOM	133	OD1	ASP	61	86.321	284.987	107.228	1.00	61.36	8
ATOM	134	OD2	ASP	61	88.139	285.352	106.037	1.00	58.09	8
ATOM	135	C	ASP	61	84.560	282.589	104.125	1.00	42.27	6
ATOM	136	O	ASP	61	83.848	283.135	103.283	1.00	50.87	8
ATOM	137	N	ASP	62	84.875	281.294	104.083	1.00	44.74	7
ATOM	138	CA	ASP	62	84.469	280.406	102.989	1.00	42.04	6
ATOM	139	CB	ASP	62	85.677	279.622	102.482	1.00	41.94	6
ATOM	140	CG	ASP	62	86.821	280.512	102.085	1.00	49.48	6
ATOM	141	OD1	ASP	62	86.573	281.672	101.695	1.00	56.91	8
ATOM	142	OD2	ASP	62	87.977	280.050	102.164	1.00	51.91	8
ATOM	143	C	ASP	62	83.311	279.422	103.181	1.00	43.99	6
ATOM	144	O	ASP	62	82.648	279.080	102.204	1.00	45.86	8
ATOM	145	N	TYR	63	83.063	278.968	104.408	1.00	39.85	7
ATOM	146	CA	TYR	63	81.976	278.017	104.666	1.00	40.47	6
ATOM	147	CB	TYR	63	82.563	276.684	105.131	1.00	35.58	6
ATOM	148	CG	TYR	63	83.251	275.868	104.068	1.00	30.21	6
ATOM	149	CD1	TYR	63	84.588	276.115	103.701	1.00	21.95	6
ATOM	150	CE1	TYR	63	85.199	275.380	102.696	1.00	14.53	6
ATOM	151	CD2	TYR	63	82.558	274.866	103.408	1.00	24.00	6
ATOM	152	CE2	TYR	63	83.153	274.126	102.408	1.00	30.67	6
ATOM	153	CZ	TYR	63	84.466	274.385	102.050	1.00	29.59	6
ATOM	154	OH	TYR	63	85.008	273.656	101.020	1.00	41.33	8
ATOM	155	C	TYR	63	81.024	278.491	105.744	1.00	43.02	6
ATOM	156	O	TYR	63	81.200	279.567	106.308	1.00	57.74	8
ATOM	157	N	LYS	64	80.000	277.692	106.019	1.00	43.49	7
ATOM	158	CA	LYS	64	79.032	278.037	107.055	1.00	45.33	6
ATOM	159	CB	LYS	64	77.632	278.333	106.506	1.00	48.55	6
ATOM	160	CG	LYS	64	76.730	278.937	107.587	1.00	58.11	6
ATOM	161	CD	LYS	64	75.253	279.082	107.204	1.00	68.53	6
ATOM	162	CE	LYS	64	74.421	279.540	108.437	1.00	79.27	6
ATOM	163	NZ	LYS	64	72.924	279.604	108.263	1.00	78.52	7
ATOM	164	C	LYS	64	78.997	276.838	108.002	1.00	48.19	6
ATOM	165	O	LYS	64	78.559	275.741	107.632	1.00	49.68	8
ATOM	166	N	VAL	65	79.532	277.031	109.202	1.00	42.62	7
ATOM	167	CA	VAL	65	79.561	275.965	110.182	1.00	43.03	6
ATOM	168	CB	VAL	65	80.686	276.179	111.189	1.00	45.24	6
ATOM	169	CG1	VAL	65	80.776	274.992	112.150	1.00	47.57	6
ATOM	170	CG2	VAL	65	81.998	276.386	110.449	1.00	43.02	6
ATOM	171	C	VAL	65	78.234	275.875	110.904	1.00	45.71	6
ATOM	172	O	VAL	65	77.753	276.857	111.439	1.00	52.95	8
ATOM	173	N	THR	66	77.629	274.695	110.865	1.00	49.19	7
ATOM	174	CA	THR	66	76.343	274.448	111.512	1.00	51.62	6
ATOM	175	CB	THR	66	75.368	273.706	110.559	1.00	48.24	6
ATOM	176	OG1	THR	66	75.634	272.300	110.576	1.00	55.53	8
ATOM	177	CG2	THR	66	75.547	274.197	109.138	1.00	44.65	6
ATOM	178	C	THR	66	76.569	273.607	112.765	1.00	52.90	6
ATOM	179	O	THR	66	77.543	272.851	112.834	1.00	52.91	8
ATOM	180	N	SER	67	75.661	273.708	113.734	1.00	60.50	7
ATOM	181	CA	SER	67	75.792	272.941	114.980	1.00	69.76	6
ATOM	182	CB	SER	67	75.119	273.666	116.154	1.00	72.74	6
ATOM	183	OG	SER	67	73.716	273.774	115.971	1.00	84.73	8
ATOM	184	C	SER	67	75.284	271.505	114.901	1.00	68.09	6
ATOM	185	O	SER	67	75.117	270.845	115.927	1.00	67.25	8
ATOM	186	N	GLN	68	75.012	271.041	113.685	1.00	69.13	7
ATOM	187	CA	GLN	68	74.526	269.685	113.462	1.00	69.93	6
ATOM	188	CB	GLN	68	73.831	269.575	112.106	1.00	75.31	6
ATOM	189	CG	GLN	68	73.348	268.162	111.786	1.00	85.40	6
ATOM	190	CD	GLN	68	72.759	268.046	110.381	1.00	93.11	6
ATOM	191	OE1	GLN	68	71.723	268.645	110.098	1.00	98.35	8
ATOM	192	NE2	GLN	68	73.365	267.307	109.471	1.00	95.21	7
ATOM	193	C	GLN	68	75.738	268.761	113.480	1.00	66.46	6
ATOM	194	O	GLN	68	76.820	269.117	112.995	1.00	68.83	8
ATOM	195	N	VAL	69	75.549	267.594	114.044	1.00	60.50	7
ATOM	196	CA	VAL	69	76.632	266.614	114.147	1.00	58.43	6
ATOM	197	CB	VAL	69	76.736	266.100	115.580	1.00	53.45	6
ATOM	198	CG1	VAL	69	77.751	264.967	115.731	1.00	57.68	6
ATOM	199	CG2	VAL	69	77.169	267.183	116.569	1.00	52.23	6
ATOM	200	C	VAL	69	76.376	265.442	113.206	1.00	58.19	6
ATOM	201	O	VAL	69	75.232	264.994	113.041	1.00	62.83	8
ATOM	202	N	LEU	70	77.463	264.983	112.617	1.00	59.48	7
ATOM	203	CA	LEU	70	77.439	263.854	111.680	1.00	55.76	6
ATOM	204	CB	LEU	70	78.297	264.148	110.446	1.00	53.10	6
ATOM	205	CG	LEU	70	77.685	265.176	109.489	1.00	48.51	6
ATOM	206	CD1	LEU	70	78.745	265.926	108.674	1.00	50.87	6
ATOM	207	CD2	LEU	70	76.739	264.556	108.457	1.00	50.63	6
ATOM	208	C	LEU	70	78.003	262.588	112.343	1.00	55.32	6
ATOM	209	O	LEU	70	77.786	261.469	111.864	1.00	55.85	8
ATOM	210	N	GLY	71	78.731	262.787	113.438	1.00	50.81	7
ATOM	211	CA	GLY	71	79.348	261.666	114.186	1.00	46.72	6
ATOM	212	C	GLY	71	80.312	262.184	115.266	1.00	47.78	6
ATOM	213	O	GLY	71	80.638	263.378	115.313	1.00	47.24	8
ATOM	214	N	LEU	72	80.750	261.254	116.112	1.00	47.63	7
ATOM	215	CA	LEU	72	81.669	261.566	117.226	1.00	50.20	6
ATOM	216	CB	LEU	72	80.993	261.319	118.579	1.00	49.87	6
ATOM	217	CG	LEU	72	79.689	262.096	118.760	1.00	54.65	6
ATOM	218	CD1	LEU	72	78.458	261.284	118.354	1.00	54.07	6
ATOM	219	CD2	LEU	72	79.443	262.526	120.209	1.00	58.26	6
ATOM	220	C	LEU	72	82.925	260.697	117.193	1.00	50.62	6
ATOM	221	O	LEU	72	82.939	259.650	116.548	1.00	50.74	8
ATOM	222	N	GLY	73	83.971	261.124	117.895	1.00	47.58	7
ATOM	223	CA	GLY	73	85.202	260.362	117.889	1.00	51.22	6
ATOM	224	C	GLY	73	86.359	260.959	118.672	1.00	60.34	6
ATOM	225	O	GLY	73	86.221	261.975	119.365	1.00	58.42	8
ATOM	226	N	ILE	74	87.522	260.326	118.514	1.00	65.56	7
ATOM	227	CA	ILE	74	88.759	260.703	119.199	1.00	66.96	6
ATOM	228	CB	ILE	74	89.969	259.885	118.684	1.00	70.55	6
ATOM	229	CG2	ILE	74	89.881	258.435	119.159	1.00	67.80	6
ATOM	230	CG1	ILE	74	90.060	260.001	117.159	1.00	74.63	6
ATOM	231	CD1	ILE	74	91.332	259.424	116.560	1.00	83.87	6
ATOM	232	C	ILE	74	89.148	262.169	119.154	1.00	66.26	6
ATOM	233	O	ILE	74	90.018	262.598	119.909	1.00	68.57	8
ATOM	234	N	ASN	75	88.566	262.930	118.237	1.00	64.57	7
ATOM	235	CA	ASN	75	88.907	264.342	118.159	1.00	66.27	6
ATOM	236	CB	ASN	75	89.597	264.648	116.838	1.00	66.39	6
ATOM	237	CG	ASN	75	90.846	263.818	116.649	1.00	71.37	6
ATOM	238	OD1	ASN	75	91.866	264.049	117.309	1.00	72.25	8
ATOM	239	ND2	ASN	75	90.759	262.804	115.789	1.00	73.86	7
ATOM	240	C	ASN	75	87.695	265.233	118.384	1.00	66.72	6
ATOM	241	O	ASN	75	87.791	266.466	118.334	1.00	69.85	8
ATOM	242	N	GLY	76	86.567	264.592	118.680	1.00	60.95	7
ATOM	243	CA	GLY	76	85.346	265.319	118.927	1.00	56.44	6
ATOM	244	C	GLY	76	84.287	265.061	117.887	1.00	56.27	6
ATOM	245	O	GLY	76	84.266	264.018	117.238	1.00	55.10	8
ATOM	246	N	LYS	77	83.430	266.057	117.701	1.00	57.39	7
ATOM	247	CA	LYS	77	82.328	265.969	116.750	1.00	54.08	6
ATOM	248	CB	LYS	77	81.200	266.909	117.185	1.00	52.09	6
ATOM	249	CG	LYS	77	80.884	266.889	118.661	1.00	53.19	6
ATOM	250	CD	LYS	77	79.714	267.791	118.960	1.00	57.46	6
ATOM	251	CE	LYS	77	79.555	268.003	120.451	1.00	64.77	6
ATOM	252	NZ	LYS	77	78.465	268.963	120.763	1.00	70.29	7
ATOM	253	C	LYS	77	82.738	266.353	115.335	1.00	50.72	6
ATOM	254	O	LYS	77	83.542	267.257	115.149	1.00	54.53	8
ATOM	255	N	VAL	78	82.258	265.604	114.351	1.00	43.80	7
ATOM	256	CA	VAL	78	82.567	265.898	112.963	1.00	38.13	6
ATOM	257	CB	VAL	78	82.569	264.647	112.058	1.00	34.24	6
ATOM	258	CG1	VAL	78	82.678	265.074	110.625	1.00	40.36	6
ATOM	259	CG2	VAL	78	83.720	263.738	112.380	1.00	29.95	6
ATOM	260	C	VAL	78	81.330	266.711	112.631	1.00	41.66	6
ATOM	261	O	VAL	78	80.220	266.184	112.635	1.00	44.45	8
ATOM	262	N	LEU	79	81.511	267.998	112.379	1.00	40.18	7
ATOM	263	CA	LEU	79	80.391	268.881	112.059	1.00	41.65	6
ATOM	264	CB	LEU	79	80.707	270.262	112.637	1.00	38.15	6
ATOM	265	CG	LEU	79	80.110	270.716	113.976	1.00	31.75	6
ATOM	266	CD1	LEU	79	79.719	269.572	114.881	1.00	27.67	6
ATOM	267	CD2	LEU	79	81.103	271.625	114.637	1.00	30.45	6
ATOM	268	C	LEU	79	79.966	269.029	110.586	1.00	42.10	6
ATOM	269	O	LEU	79	80.795	268.928	109.695	1.00	43.31	8
ATOM	270	N	GLN	80	78.668	269.220	110.326	1.00	45.40	7
ATOM	271	CA	GLN	80	78.214	269.391	108.93	1.00	47.63	6
ATOM	272	CB	GLN	80	76.734	269.129	108.719	1.00	48.74	6
ATOM	273	CG	GLN	80	76.361	269.379	107.269	1.00	54.02	6
ATOM	274	CD	GLN	80	74.945	268.977	106.940	1.00	63.80	6
ATOM	275	OE1	GLN	80	73.990	269.467	107.557	1.00	68.91	8
ATOM	276	NE2	GLN	80	74.792	268.094	105.945	1.00	63.65	7
ATOM	277	C	GLN	80	78.513	270.847	108.645	1.00	47.13	6
ATOM	278	O	GLN	80	78.339	271.694	109.513	1.00	50.46	8
ATOM	279	N	ILE	81	78.816	271.162	107.399	1.00	42.64	7
ATOM	280	CA	ILE	81	79.145	272.524	107.064	1.00	40.48	6
ATOM	281	CB	ILE	81	80.693	272.635	107.273	1.00	38.74	6
ATOM	282	CG2	ILE	81	81.474	272.717	105.983	1.00	31.42	6
ATOM	283	CG1	ILE	81	81.012	273.723	108.273	1.00	48.96	6
ATOM	284	CD1	ILE	81	82.474	273.835	108.567	1.00	55.74	6
ATOM	285	C	ILE	81	78.685	272.844	105.644	1.00	44.62	6
ATOM	286	O	ILE	81	78.404	271.925	104.885	1.00	46.52	8
ATOM	287	N	PHE	82	78.513	274.127	105.306	1.00	44.59	7
ATOM	288	CA	PHE	82	78.077	274.477	103.945	1.00	41.12	6
ATOM	289	CB	PHE	82	76.668	275.054	103.948	1.00	33.54	6
ATOM	290	CG	PHE	82	75.645	274.110	104.450	1.00	32.56	6
ATOM	291	CD1	PHE	82	75.262	274.127	105.783	1.00	34.08	6
ATOM	292	CD2	PHE	82	75.092	273.159	103.606	1.00	37.31	6
ATOM	293	CE1	PHE	82	74.340	273.191	106.275	1.00	38.32	6
ATOM	294	CE2	PHE	82	74.169	272.222	104.090	1.00	38.08	6
ATOM	295	CZ	PHE	82	73.796	272.242	105.427	1.00	34.81	6
ATOM	296	C	PHE	82	78.999	275.448	103.215	1.00	43.16	6
ATOM	297	O	PHE	82	79.437	276.445	103.782	1.00	46.44	8
ATOM	298	N	ASN	83	79.336	275.128	101.972	1.00	41.27	7
ATOM	299	CA	ASN	83	80.200	275.990	101.182	1.00	42.24	6
ATOM	300	CB	ASN	83	80.743	275.208	99.986	1.00	43.94	6
ATOM	301	CG	ASN	83	81.437	276.093	98.952	1.00	41.93	6
ATOM	302	OD1	ASN	83	80.787	276.658	98.081	1.00	41.79	8
ATOM	303	ND2	ASN	83	82.757	276.167	99.012	1.00	35.30	7
ATOM	304	C	ASN	83	79.336	277.153	100.702	1.00	43.66	6
ATOM	305	O	ASN	83	78.489	276.971	99.847	1.00	48.05	8
ATOM	306	N	LYS	84	79.546	278.344	101.249	1.00	42.83	7
ATOM	307	CA	LYS	84	78.770	279.532	100.863	1.00	38.88	6
ATOM	308	CB	LYS	84	79.491	280.783	101.353	1.00	32.85	6
ATOM	309	CG	LYS	84	79.523	280.909	102.865	1.00	27.55	6
ATOM	310	CD	LYS	84	80.393	282.038	103.280	1.00	32.58	6
ATOM	311	CE	LYS	84	80.051	282.486	104.670	1.00	36.92	6
ATOM	312	NZ	LYS	84	81.018	283.559	105.010	1.00	51.72	7
ATOM	313	C	LYS	84	78.513	279.672	99.365	1.00	39.20	6
ATOM	314	O	LYS	84	77.379	279.709	98.908	1.00	42.34	8
ATOM	315	N	ARG	85	79.597	279.713	98.612	1.00	41.62	7
ATOM	316	CA	ARG	85	79.579	279.847	97.162	1.00	44.84	6
ATOM	317	CB	ARG	85	81.011	279.668	96.681	1.00	52.98	6
ATOM	318	CG	ARG	85	81.339	279.950	95.236	1.00	57.19	6
ATOM	319	CD	ARG	85	82.801	279.486	94.986	1.00	72.19	6
ATOM	320	NE	ARG	85	83.740	279.926	96.047	1.00	82.00	7
ATOM	321	CZ	ARG	85	84.383	279.114	96.900	1.00	81.32	6
ATOM	322	NH1	ARG	85	84.219	277.794	96.835	1.00	85.38	7
ATOM	323	NH2	ARG	85	85.151	279.626	97.859	1.00	75.16	7
ATOM	324	C	ARG	85	78.648	278.909	96.383	1.00	46.34	6
ATOM	325	O	ARG	85	77.944	279.363	95.490	1.00	54.59	8
ATOM	326	N	THR	86	78.594	277.628	96.742	1.00	40.87	7
ATOM	327	CA	THR	86	77.737	276.683	96.023	1.00	38.65	6
ATOM	328	CB	THR	86	78.548	275.502	95.500	1.00	35.15	6
ATOM	329	OG1	THR	86	78.997	274.724	96.611	1.00	44.88	8
ATOM	330	CG2	THR	86	79.752	275.966	94.751	1.00	33.53	6
ATOM	331	C	THR	86	76.612	276.078	96.838	1.00	40.46	6
ATOM	332	O	THR	86	75.726	275.428	96.291	1.00	44.60	8
ATOM	333	N	GLN	87	76.680	276.266	98.145	1.00	38.56	7
ATOM	334	CA	GLN	87	75.694	275.747	99.076	1.00	39.20	6
ATOM	335	CB	GLN	87	74.318	276.303	98.773	1.00	32.20	6
ATOM	336	CG	GLN	87	74.199	277.741	99.114	1.00	42.79	6
ATOM	337	CD	GLN	87	74.108	277.971	100.591	1.00	50.66	6
ATOM	338	OE1	GLN	87	73.171	277.493	101.227	1.00	55.20	8
ATOM	339	NE2	GLN	87	75.071	278.713	101.156	1.00	51.42	7
ATOM	340	C	GLN	87	75.653	274.223	99.207	1.00	45.59	6
ATOM	341	O	GLN	87	74.636	273.661	99.630	1.00	49.90	8
ATOM	342	N	GLU	88	76.751	273.555	98.844	1.00	48.14	7
ATOM	343	CA	GLU	88	76.826	272.096	98.942	1.00	52.41	6
ATOM	344	CB	GLU	88	77.826	271.536	97.940	1.00	56.92	6
ATOM	345	CG	GLU	88	77.384	271.716	96.500	1.00	72.33	6
ATOM	346	CD	GLU	88	78.506	271.494	95.495	1.00	78.20	6
ATOM	347	OE1	GLU	88	78.279	270.775	94.491	1.00	78.58	8
ATOM	348	OE2	GLU	88	79.611	272.057	95.702	1.00	80.85	8
ATOM	349	C	GLU	88	77.222	271.707	100.372	1.00	52.55	6
ATOM	350	O	GLU	88	77.835	272.500	101.095	1.00	53.86	8
ATOM	351	N	LYS	89	76.862	270.493	100.779	1.00	49.27	7
ATOM	352	CA	LYS	89	77.174	270.010	102.123	1.00	48.29	6
ATOM	353	CB	LYS	89	76.097	269.036	102.638	1.00	52.03	6
ATOM	354	CG	LYS	89	75.125	268.494	101.564	1.00	72.16	6
ATOM	355	CD	LYS	89	74.065	269.559	101.138	1.00	83.35	6
ATOM	356	CE	LYS	89	73.454	269.295	99.754	1.00	80.24	6
ATOM	357	NZ	LYS	89	74.505	269.274	98.688	1.00	83.18	7
ATOM	358	C	LYS	89	78.544	269.368	102.220	1.00	47.72	6
ATOM	359	O	LYS	89	78.964	268.640	101.326	1.00	54.20	8
ATOM	360	N	PHE	90	79.246	269.660	103.309	1.00	45.18	7
ATOM	361	CA	PHE	90	80.572	269.122	103.554	1.00	41.92	6
ATOM	362	CB	PHE	90	81.586	270.139	103.133	1.00	36.66	6
ATOM	363	CG	PHE	90	81.730	270.257	101.655	1.00	39.45	6
ATOM	364	CD1	PHE	90	82.324	269.244	100.926	1.00	40.56	6
ATOM	365	CD2	PHE	90	81.379	271.422	101.001	1.00	40.83	6
ATOM	366	CE1	PHE	90	82.571	269.402	99.571	1.00	43.06	6
ATOM	367	CE2	PHE	90	81.629	271.582	99.644	1.00	38.17	6
ATOM	368	CZ	PHE	90	82.226	270.580	98.933	1.00	35.41	6
ATOM	369	C	PHE	90	80.755	268.764	105.024	1.00	44.84	6
ATOM	370	O	PHE	90	79.888	269.073	105.831	1.00	51.86	8
ATOM	371	N	ALA	91	81.842	268.072	105.373	1.00	39.95	7
ATOM	372	CA	ALA	91	82.076	267.699	106.771	1.00	31.48	6
ATOM	373	CB	ALA	91	82.148	266.222	106.931	1.00	34.87	6
ATOM	374	C	ALA	91	83.348	268.326	107.261	1.00	33.54	6
ATOM	375	O	ALA	91	84.350	268.344	106.559	1.00	42.48	8
ATOM	376	N	LEU	92	83.293	268.840	108.479	1.00	33.04	7
ATOM	377	CA	LEU	92	84.407	269.498	109.141	1.00	28.82	6
ATOM	378	CB	LEU	92	83.920	270.805	109.723	1.00	23.23	6
ATOM	379	CG	LEU	92	84.962	271.643	110.423	1.00	24.07	6
ATOM	380	CD1	LEU	92	85.909	272.134	109.369	1.00	33.26	6
ATOM	381	CD2	LEU	92	84.338	272.814	111.171	1.00	25.16	6
ATOM	382	C	LEU	92	84.921	268.649	110.289	1.00	40.27	6
ATOM	383	O	LEU	92	84.157	268.182	111.145	1.00	44.45	8
ATOM	384	N	LYS	93	86.235	268.482	110.311	1.00	45.27	7
ATOM	385	CA	LYS	93	86.930	267.707	111.332	1.00	41.65	6
ATOM	386	CB	LYS	93	87.596	266.501	110.675	1.00	37.36	6
ATOM	387	CG	LYS	93	88.303	265.598	111.620	1.00	33.77	6
ATOM	388	CD	LYS	93	88.724	264.365	110.885	1.00	36.49	6
ATOM	389	CE	LYS	93	88.861	263.201	111.850	1.00	42.11	6
ATOM	390	NZ	LYS	93	88.934	261.912	111.132	1.00	38.11	7
ATOM	391	C	LYS	93	87.974	268.654	111.939	1.00	43.64	6
ATOM	392	O	LYS	93	88.759	269.267	111.217	1.00	45.73	8
ATOM	393	N	MET	94	87.951	268.814	113.253	1.00	41.61	7
ATOM	394	CA	MET	94	88.899	269.695	113.905	1.00	47.32	6
ATOM	395	CB	MET	94	88.136	270.627	114.831	1.00	56.18	6
ATOM	396	CG	MET	94	86.914	271.277	114.187	1.00	69.87	6
ATOM	397	SD	MET	94	86.015	272.356	115.325	1.00	81.88	16
ATOM	398	CE	MET	94	87.465	273.270	116.131	1.00	71.12	6
ATOM	399	C	MET	94	89.948	268.945	114.710	1.00	50.04	6
ATOM	400	O	MET	94	89.618	267.997	115.415	1.00	57.12	8
ATOM	401	N	LEU	95	91.213	269.350	114.603	1.00	50.63	7
ATOM	402	CA	LEU	95	92.294	268.688	115.354	1.00	52.04	6
ATOM	403	CB	LEU	95	93.269	267.930	114.446	1.00	46.71	6
ATOM	404	CG	LEU	95	92.911	266.734	113.573	1.00	36.39	6
ATOM	405	CD1	LEU	95	91.531	266.159	113.868	1.00	32.69	6
ATOM	406	CD2	LEU	95	93.007	267.222	112.158	1.00	40.02	6
ATOM	407	C	LEU	95	93.084	269.726	116.132	1.00	56.47	6
ATOM	408	O	LEU	95	92.912	270.919	115.914	1.00	60.28	8
ATOM	409	N	GLN	96	93.986	269.269	116.996	1.00	58.01	7
ATOM	410	CA	GLN	96	94.798	270.177	117.798	1.00	62.01	6
ATOM	411	CB	GLN	96	95.359	269.456	119.037	1.00	71.46	6
ATOM	412	CG	GLN	96	96.483	270.193	119.815	1.00	79.76	6
ATOM	413	CD	GLN	96	95.982	271.072	120.957	1.00	86.55	6
ATOM	414	OE1	GLN	96	95.459	272.170	120.739	1.00	88.23	8
ATOM	415	NE2	GLN	96	96.170	270.600	122.187	1.00	86.54	7
ATOM	416	C	GLN	96	95.927	270.809	117.002	1.00	60.46	6
ATOM	417	O	GLN	96	96.461	271.839	117.400	1.00	70.38	8
ATOM	418	N	ASP	97	96.269	270.222	115.866	1.00	52.27	7
ATOM	419	CA	ASP	97	97.348	270.746	115.024	1.00	50.91	6
ATOM	420	CB	ASP	97	97.085	272.173	114.543	1.00	49.86	6
ATOM	421	CG	ASP	97	98.188	272.699	113.619	1.00	57.50	6
ATOM	422	OD1	ASP	97	98.852	271.899	112.929	1.00	56.02	8
ATOM	423	OD2	ASP	97	98.391	273.929	113.576	1.00	63.44	8
ATOM	424	C	ASP	97	98.709	270.687	115.687	1.00	50.91	6
ATOM	425	O	ASP	97	99.100	271.562	116.452	1.00	48.95	8
ATOM	426	N	CYS	98	99.408	269.609	115.385	1.00	53.53	7
ATOM	427	CA	CYS	98	100.737	269.340	115.892	1.00	53.91	6
ATOM	428	CB	CYS	98	100.677	268.209	116.903	1.00	54.20	6
ATOM	429	SG	CYS	98	99.754	266.827	116.282	1.00	65.92	16
ATOM	430	C	CYS	98	101.411	268.866	114.626	1.00	54.51	6
ATOM	431	O	CYS	98	100.775	268.830	113.570	1.00	56.51	8
ATOM	432	N	PRO	99	102.715	268.567	114.678	1.00	53.03	7
ATOM	433	CD	PRO	99	103.725	268.874	115.698	1.00	50.80	6
ATOM	434	CA	PRO	99	103.345	268.104	113.439	1.00	49.34	6
ATOM	435	CB	PRO	99	104.831	268.222	113.752	1.00	47.85	6
ATOM	436	CG	PRO	99	104.880	268.053	115.234	1.00	54.89	6
ATOM	437	C	PRO	99	102.892	266.698	112.996	1.00	46.94	6
ATOM	438	O	PRO	99	102.973	266.369	111.819	1.00	45.51	8
ATOM	439	N	LYS	100	102.362	265.903	113.924	1.00	46.00	7
ATOM	440	CA	LYS	100	101.891	264.556	113.600	1.00	49.79	6
ATOM	441	CB	LYS	100	101.720	263.722	114.871	1.00	55.32	6
ATOM	442	CG	LYS	100	101.310	262.272	114.621	1.00	65.19	6
ATOM	443	CD	LYS	100	101.091	261.476	115.923	1.00	78.43	6
ATOM	444	CE	LYS	100	99.723	261.755	116.576	1.00	86.39	6
ATOM	445	NZ	LYS	100	99.439	260.970	117.838	1.00	81.26	7
ATOM	446	C	LYS	100	100.553	264.625	112.849	1.00	53.43	6
ATOM	447	O	LYS	100	100.232	263.739	112.064	1.00	53.34	8
ATOM	448	N	ALA	101	99.752	265.655	113.130	1.00	57.24	7
ATOM	449	CA	ALA	101	98.452	265.838	112.476	1.00	53.76	6
ATOM	450	CB	ALA	101	97.602	266.806	113.251	1.00	47.38	6
ATOM	451	C	ALA	101	98.703	266.369	111.067	1.00	55.06	6
ATOM	452	O	ALA	101	98.135	265.870	110.095	1.00	55.05	8
ATOM	453	N	ARG	102	99.578	267.367	110.964	1.00	53.35	7
ATOM	454	CA	ARG	102	99.919	267.963	109.683	1.00	57.33	6
ATOM	455	CB	ARG	102	101.032	268.997	109.864	1.00	57.65	6
ATOM	456	CG	ARG	102	100.601	270.370	110.374	1.00	67.20	6
ATOM	457	CD	ARG	102	101.739	271.098	111.118	1.00	76.53	6
ATOM	458	NE	ARG	102	102.992	271.117	110.354	1.00	90.17	7
ATOM	459	CZ	ARG	102	104.207	270.929	110.873	1.00	92.00	6
ATOM	460	NH1	ARG	102	104.360	270.714	112.175	1.00	88.60	7
ATOM	461	NH2	ARG	102	105.271	270.896	110.074	1.00	90.41	7
ATOM	462	C	ARG	102	100.411	266.850	108.758	1.00	61.79	6
ATOM	463	O	ARG	102	100.158	266.865	107.555	1.00	66.20	8
ATOM	464	N	ARG	103	101.057	265.847	109.345	1.00	62.64	7
ATOM	465	CA	ARG	103	101.589	264.719	108.588	1.00	60.89	6
ATOM	466	CB	ARG	103	102.681	264.033	109.410	1.00	60.83	6
ATOM	467	CG	ARG	103	103.504	263.002	108.657	1.00	66.42	6
ATOM	468	CD	ARG	103	104.803	262.680	109.395	1.00	69.20	6
ATOM	469	NE	ARG	103	104.572	262.408	110.812	1.00	69.35	7
ATOM	470	CZ	ARG	103	105.142	263.076	111.809	1.00	70.13	6
ATOM	471	NH1	ARG	103	105.993	264.064	111.568	1.00	71.72	7
ATOM	472	NH2	ARG	103	104.830	262.779	113.056	1.00	73.81	7
ATOM	473	C	ARG	103	100.531	263.710	108.130	1.00	60.06	6
ATOM	474	O	ARG	103	100.595	263.197	107.008	1.00	60.04	8
ATOM	475	N	GLU	104	99.527	263.475	108.967	1.00	58.04	7
ATOM	476	CA	GLU	104	98.475	262.528	108.620	1.00	56.01	6
ATOM	477	CB	GLU	104	97.767	262.037	109.876	1.00	58.13	6
ATOM	478	CG	GLU	104	98.753	261.438	110.856	1.00	69.69	6
ATOM	479	CD	GLU	104	98.104	260.709	112.005	1.00	76.95	6
ATOM	480	OE1	GLU	104	98.323	259.485	112.113	1.00	82.32	8
ATOM	481	OE2	GLU	104	97.405	261.354	112.813	1.00	81.38	8
ATOM	482	C	GLU	104	97.499	263.026	107.557	1.00	53.22	6
ATOM	483	O	GLU	104	97.165	262.276	106.641	1.00	50.63	8
ATOM	484	N	VAL	105	97.072	264.290	107.646	1.00	51.15	7
ATOM	485	CA	VAL	105	96.140	264.837	106.652	1.00	48.46	6
ATOM	486	CB	VAL	105	95.653	266.280	106.992	1.00	44.02	6
ATOM	487	CG1	VAL	105	95.000	266.310	108.339	1.00	51.39	6
ATOM	488	CG2	VAL	105	96.794	267.267	106.952	1.00	42.57	6
ATOM	489	C	VAL	105	96.852	264.896	105.304	1.00	49.32	6
ATOM	490	O	VAL	105	96.255	264.684	104.246	1.00	48.10	8
ATOM	491	N	GLU	106	98.152	265.153	105.364	1.00	48.27	7
ATOM	492	CA	GLU	106	98.959	265.247	104.172	1.00	45.34	6
ATOM	493	CB	GLU	106	100.345	265.751	104.559	1.00	47.84	6
ATOM	494	CG	GLU	106	100.973	266.701	103.552	1.00	61.82	6
ATOM	495	CD	GLU	106	101.917	265.972	102.601	1.00	78.09	6
ATOM	496	OE1	GLU	106	101.419	265.334	101.636	1.00	80.27	8
ATOM	497	OE2	GLU	106	103.154	266.020	102.835	1.00	78.34	8
ATOM	498	C	GLU	106	98.991	263.895	103.475	1.00	45.77	6
ATOM	499	O	GLU	106	99.230	263.814	102.273	1.00	46.16	8
ATOM	500	N	LEU	107	98.715	262.832	104.228	1.00	44.59	7
ATOM	501	CA	LEU	107	98.709	261.485	103.667	1.00	42.00	6
ATOM	502	CB	LEU	107	98.979	260.433	104.740	1.00	44.06	6
ATOM	503	CG	LEU	107	100.439	260.131	105.103	1.00	39.64	6
ATOM	504	CD1	LEU	107	100.485	259.244	106.312	1.00	36.64	6
ATOM	505	CD2	LEU	107	101.114	259.462	103.938	1.00	37.18	6
ATOM	506	C	LEU	107	97.368	261.260	103.024	1.00	43.35	6
ATOM	507	O	LEU	107	97.299	260.738	101.930	1.00	46.96	8
ATOM	508	N	HIS	108	96.307	261.686	103.710	1.00	45.35	7
ATOM	509	CA	HIS	108	94.920	261.562	103.234	1.00	44.94	6
ATOM	510	CB	HIS	108	93.995	262.190	104.270	1.00	40.43	6
ATOM	511	CG	HIS	108	92.545	261.909	104.054	1.00	39.88	6
ATOM	512	CD2	HIS	108	91.885	261.345	103.014	1.00	38.35	6
ATOM	513	ND1	HIS	108	91.589	262.212	105.000	1.00	40.72	7
ATOM	514	CE1	HIS	108	90.400	261.843	104.553	1.00	41.23	6
ATOM	515	NE2	HIS	108	90.553	261.313	103.352	1.00	35.89	7
ATOM	516	C	HIS	108	94.801	262.302	101.883	1.00	49.84	6
ATOM	517	O	HIS	108	94.172	261.813	100.953	1.00	51.83	8
ATOM	518	N	TRP	109	95.398	263.491	101.805	1.00	51.27	7
ATOM	519	CA	TRP	109	95.400	264.317	100.597	1.00	49.60	6
ATOM	520	CB	TRP	109	95.727	265.774	100.963	1.00	49.30	6
ATOM	521	CG	TRP	109	95.997	266.662	99.760	1.00	48.30	6
ATOM	522	CD2	TRP	109	95.051	267.506	99.112	1.00	50.26	6
ATOM	523	CE2	TRP	109	95.693	268.072	97.993	1.00	55.71	6
ATOM	524	CE3	TRP	109	93.711	267.836	99.364	1.00	51.64	6
ATOM	525	CD1	TRP	109	97.164	266.762	99.034	1.00	46.93	6
ATOM	526	NE1	TRP	109	96.982	267.600	97.969	1.00	52.62	7
ATOM	527	CZ2	TRP	109	95.032	268.955	97.124	1.00	62.74	6
ATOM	528	CZ3	TRP	109	93.056	268.711	98.500	1.00	51.35	6
ATOM	529	CH2	TRP	109	93.715	269.258	97.397	1.00	58.44	6
ATOM	530	C	TRP	109	96.595	263.747	99.860	1.00	52.52	6
ATOM	531	O	TRP	109	97.712	264.189	100.070	1.00	67.99	8
ATOM	532	N	ARG	110	96.391	262.733	99.049	1.00	45.97	7
ATOM	533	CA	ARG	110	97.492	262.107	98.301	1.00	41.85	6
ATOM	534	CB	ARG	110	98.669	261.778	99.220	1.00	35.57	6
ATOM	535	CG	ARG	110	100.009	262.248	98.697	1.00	44.63	6
ATOM	536	CD	ARG	110	101.092	262.412	99.797	1.00	51.06	6
ATOM	537	NE	ARG	110	101.614	261.134	100.285	1.00	54.76	7
ATOM	538	CZ	ARG	110	102.437	260.341	99.604	1.00	54.90	6
ATOM	539	NH1	ARG	110	102.859	260.687	98.401	1.00	56.96	7
ATOM	540	NH2	ARG	110	102.787	259.165	100.101	1.00	54.78	7
ATOM	541	C	ARG	110	96.796	260.840	97.903	1.00	45.91	6
ATOM	542	O	ARG	110	96.825	260.422	96.746	1.00	53.36	8
ATOM	543	N	ALA	111	96.072	260.316	98.886	1.00	40.86	7
ATOM	544	CA	ALA	111	95.297	259.115	98.766	1.00	41.11	6
ATOM	545	CB	ALA	111	95.167	258.469	100.125	1.00	43.86	6
ATOM	546	C	ALA	111	93.931	259.552	98.283	1.00	43.14	6
ATOM	547	O	ALA	111	93.100	258.713	97.978	1.00	49.96	8
ATOM	548	N	SER	112	93.715	260.868	98.210	1.00	49.04	7
ATOM	549	CA	SER	112	92.444	261.467	97.774	1.00	52.26	6
ATOM	550	CB	SER	112	92.385	262.935	98.169	1.00	55.06	6
ATOM	551	OG	SER	112	92.121	263.079	99.555	1.00	65.98	8
ATOM	552	C	SER	112	92.006	261.329	96.329	1.00	52.46	6
ATOM	553	O	SER	112	90.837	261.541	96.032	1.00	49.95	8
ATOM	554	N	GLN	113	92.939	261.016	95.432	1.00	56.12	7
ATOM	555	CA	GLN	113	92.616	260.853	94.018	1.00	59.35	6
ATOM	556	CB	GLN	113	93.806	261.230	93.115	1.00	66.37	6
ATOM	557	CG	GLN	113	94.518	262.528	93.483	1.00	78.46	6
ATOM	558	CD	GLN	113	93.565	263.688	93.749	1.00	85.18	6
ATOM	559	OE1	GLN	113	93.538	264.244	94.855	1.00	84.58	8
ATOM	560	NE2	GLN	113	92.779	264.061	92.737	1.00	87.90	7
ATOM	561	C	GLN	113	92.256	259.390	93.808	1.00	58.14	6
ATOM	562	O	GLN	113	92.648	258.764	92.828	1.00	63.76	8
ATOM	563	N	CYS	114	91.548	258.826	94.767	1.00	56.79	7
ATOM	564	CA	CYS	114	91.147	257.445	94.677	1.00	59.72	6
ATOM	565	CB	CYS	114	91.916	256.602	95.676	1.00	60.66	6
ATOM	566	SG	CYS	114	91.109	255.057	95.975	1.00	71.13	16
ATOM	567	C	CYS	114	89.672	257.404	94.996	1.00	62.75	6
ATOM	568	O	CYS	114	89.265	257.704	96.122	1.00	66.87	8
ATOM	569	N	PRO	115	88.849	257.010	94.013	1.00	62.36	7
ATOM	570	CD	PRO	115	89.294	256.445	92.733	1.00	60.83	6
ATOM	571	CA	PRO	115	87.390	256.914	94.130	1.00	60.74	6
ATOM	572	CB	PRO	115	86.992	256.124	92.880	1.00	58.69	6
ATOM	573	CG	PRO	115	88.255	255.392	92.512	1.00	65.07	6
ATOM	574	C	PRO	115	86.809	256.305	95.408	1.00	59.83	6
ATOM	575	O	PRO	115	85.714	256.692	95.820	1.00	62.08	8
ATOM	576	N	HIS	116	87.527	255.388	96.056	1.00	56.30	7
ATOM	577	CA	HIS	116	86.990	254.793	97.272	1.00	52.90	6
ATOM	578	CB	HIS	116	87.027	253.274	97.210	1.00	51.70	6
ATOM	579	CG	HIS	116	85.999	252.690	96.298	1.00	52.79	6
ATOM	580	CD2	HIS	116	84.745	252.245	96.536	1.00	52.48	6
ATOM	581	ND1	HIS	116	86.213	252.520	94.946	1.00	56.60	7
ATOM	582	CE1	HIS	116	85.135	251.996	94.392	1.00	52.78	6
ATOM	583	NE2	HIS	116	84.231	251.817	95.336	1.00	50.42	7
ATOM	584	C	HIS	116	87.517	255.283	98.599	1.00	53.01	6
ATOM	585	O	HIS	116	87.283	254.648	99.622	1.00	58.06	8
ATOM	586	N	ILE	117	88.204	256.417	98.599	1.00	47.98	7
ATOM	587	CA	ILE	117	88.742	256.975	99.832	1.00	43.43	6
ATOM	588	CB	ILE	117	90.269	257.013	99.811	1.00	42.89	6
ATOM	589	CG2	ILE	117	90.801	257.841	100.963	1.00	44.01	6
ATOM	590	CG1	ILE	117	90.820	255.596	99.926	1.00	44.44	6
ATOM	591	CD1	ILE	117	92.303	255.531	99.826	1.00	45.46	6
ATOM	592	C	ILE	117	88.164	258.378	99.900	1.00	44.72	6
ATOM	593	O	ILE	117	88.309	259.134	98.947	1.00	49.50	8
ATOM	594	N	VAL	118	87.465	258.690	100.999	1.00	43.07	7
ATOM	595	CA	VAL	118	86.835	259.996	101.221	1.00	38.87	6
ATOM	596	CB	VAL	118	86.306	260.121	102.655	1.00	40.23	6
ATOM	597	CG1	VAL	118	87.414	260.478	103.635	1.00	42.59	6
ATOM	598	CG2	VAL	118	85.206	261.133	102.691	1.00	46.81	6
ATOM	599	C	VAL	118	87.764	261.153	100.868	1.00	38.89	6
ATOM	600	O	VAL	118	88.879	261.243	101.379	1.00	39.66	8
ATOM	601	N	ARG	119	87.284	262.050	100.011	1.00	38.95	7
ATOM	602	CA	ARG	119	88.062	263.195	99.558	1.00	37.81	6
ATOM	603	CB	ARG	119	87.553	263.634	98.197	1.00	37.92	6
ATOM	604	CG	ARG	119	87.959	265.039	97.819	1.00	53.56	6
ATOM	605	CD	ARG	119	87.549	265.412	96.402	1.00	65.48	6
ATOM	606	NE	ARG	119	88.604	265.153	95.425	1.00	66.50	7
ATOM	607	CZ	ARG	119	88.571	264.158	94.548	1.00	68.27	6
ATOM	608	NH1	ARG	119	87.533	263.327	94.528	1.00	71.30	7
ATOM	609	NH2	ARG	119	89.567	264.002	93.682	1.00	66.97	7
ATOM	610	C	ARG	119	88.240	264.425	100.414	1.00	38.22	6
ATOM	611	O	ARG	119	87.255	265.030	100.820	1.00	41.60	8
ATOM	612	N	ILE	120	89.502	264.792	100.677	1.00	37.19	7
ATOM	613	CA	ILE	120	89.797	265.980	101.477	1.00	33.79	6
ATOM	614	CB	ILE	120	91.218	266.009	102.067	1.00	35.24	6
ATOM	615	CG2	ILE	120	91.706	267.466	102.234	1.00	29.10	6
ATOM	616	CG1	ILE	120	91.213	265.274	103.410	1.00	37.06	6
ATOM	617	CD1	ILE	120	92.479	265.428	104.262	1.00	35.77	6
ATOM	618	C	ILE	120	89.667	267.057	100.435	1.00	38.15	6
ATOM	619	O	ILE	120	90.312	267.009	99.381	1.00	42.06	8
ATOM	620	N	VAL	121	88.796	268.006	100.727	1.00	39.84	7
ATOM	621	CA	VAL	121	88.521	269.120	99.835	1.00	36.51	6
ATOM	622	CB	VAL	121	87.007	269.164	99.597	1.00	29.88	6
ATOM	623	CG1	VAL	121	86.464	270.529	99.714	1.00	33.08	6
ATOM	624	CG2	VAL	121	86.699	268.542	98.281	1.00	29.00	6
ATOM	625	C	VAL	121	89.091	270.485	100.239	1.00	39.45	6
ATOM	626	O	VAL	121	89.252	271.359	99.394	1.00	40.76	8
ATOM	627	N	ASP	122	89.459	270.640	101.507	1.00	41.18	7
ATOM	628	CA	ASP	122	90.010	271.900	101.995	1.00	40.56	6
ATOM	629	CB	ASP	122	88.876	272.923	102.138	1.00	47.35	6
ATOM	630	CG	ASP	122	88.872	273.973	101.045	1.00	46.11	6
ATOM	631	OD1	ASP	122	89.847	274.058	100.264	1.00	47.72	8
ATOM	632	OD2	ASP	122	87.878	274.721	100.987	1.00	45.35	8
ATOM	633	C	ASP	122	90.632	271.711	103.366	1.00	40.26	6
ATOM	634	O	ASP	122	90.055	271.029	104.205	1.00	46.40	8
ATOM	635	N	VAL	123	91.787	272.324	103.610	1.00	36.94	7
ATOM	636	CA	VAL	123	92.441	272.196	104.913	1.00	34.79	6
ATOM	637	CB	VAL	123	93.750	271.349	104.886	1.00	34.97	6
ATOM	638	CG1	VAL	123	94.197	271.065	106.287	1.00	36.05	6
ATOM	639	CG2	VAL	123	93.585	270.052	104.109	1.00	33.40	6
ATOM	640	C	VAL	123	92.811	273.588	105.418	1.00	37.15	6
ATOM	641	O	VAL	123	93.600	274.309	104.800	1.00	40.68	8
ATOM	642	N	TYR	124	92.247	273.955	106.558	1.00	39.65	7
ATOM	643	CA	TYR	124	92.508	275.251	107.164	1.00	40.57	6
ATOM	644	CB	TYR	124	91.192	275.944	107.534	1.00	39.39	6
ATOM	645	CG	TYR	124	90.394	276.371	106.341	1.00	36.94	6
ATOM	646	CD1	TYR	124	90.547	277.654	105.814	1.00	39.91	6
ATOM	647	CE1	TYR	124	89.921	278.032	104.648	1.00	37.05	6
ATOM	648	CD2	TYR	124	89.574	275.475	105.672	1.00	36.08	6
ATOM	649	CE2	TYR	124	88.944	275.844	104.500	1.00	46.34	6
ATOM	650	CZ	TYR	124	89.126	277.126	103.991	1.00	42.79	6
ATOM	651	OH	TYR	124	88.539	277.482	102.803	1.00	45.73	8
ATOM	652	C	TYR	124	93.339	275.130	108.429	1.00	45.50	6
ATOM	653	O	TYR	124	93.305	274.110	109.135	1.00	46.67	8
ATOM	654	N	GLU	125	94.038	276.218	108.727	1.00	45.98	7
ATOM	655	CA	GLU	125	94.880	276.315	109.896	1.00	45.17	6
ATOM	656	CB	GLU	125	96.346	276.312	109.513	1.00	49.65	6
ATOM	657	CG	GLU	125	97.225	276.399	110.742	1.00	74.22	6
ATOM	658	CD	GLU	125	98.649	275.961	110.497	1.00	86.81	6
ATOM	659	OE1	GLU	125	98.876	274.762	110.157	1.00	87.23	8
ATOM	660	OE2	GLU	125	99.539	276.829	110.671	1.00	95.16	8
ATOM	661	C	GLU	125	94.510	277.631	110.571	1.00	45.43	6
ATOM	662	O	GLU	125	95.118	278.666	110.302	1.00	47.22	8
ATOM	663	N	ASN	126	93.494	277.576	111.430	1.00	43.90	7
ATOM	664	CA	ASN	126	92.997	278.742	112.162	1.00	46.65	6
ATOM	665	CB	ASN	126	91.514	278.966	111.838	1.00	43.85	6
ATOM	666	CG	ASN	126	91.254	279.129	110.359	1.00	46.86	6
ATOM	667	OD1	ASN	126	90.141	278.940	109.905	1.00	48.51	8
ATOM	668	ND2	ASN	126	92.276	279.498	109.606	1.00	46.98	7
ATOM	669	C	ASN	126	93.134	278.675	113.674	1.00	46.10	6
ATOM	670	O	ASN	126	93.118	277.604	114.254	1.00	51.28	8
ATOM	671	N	LEU	127	93.226	279.843	114.298	1.00	46.48	7
ATOM	672	CA	LEU	127	93.352	279.981	115.745	1.00	46.37	6
ATOM	673	CB	LEU	127	93.945	281.334	116.087	1.00	45.87	6
ATOM	674	CG	LEU	127	95.417	281.436	116.400	1.00	49.01	6
ATOM	675	CD1	LEU	127	95.665	282.803	116.954	1.00	51.50	6
ATOM	676	CD2	LEU	127	95.784	280.385	117.418	1.00	53.61	6
ATOM	677	C	LEU	127	92.002	279.938	116.437	1.00	50.25	6
ATOM	678	O	LEU	127	91.115	280.707	116.098	1.00	51.90	8
ATOM	679	N	TYR	128	91.849	279.084	117.438	1.00	57.66	7
ATOM	680	CA	TYR	128	90.581	279.017	118.135	1.00	67.26	6
ATOM	681	CB	TYR	128	90.171	277.571	118.409	1.00	72.99	6
ATOM	682	CG	TYR	128	88.675	277.376	118.601	1.00	80.33	6
ATOM	683	CD1	TYR	128	88.060	276.184	118.213	1.00	85.27	6
ATOM	684	CE1	TYR	128	86.687	275.983	118.402	1.00	91.31	6
ATOM	685	CD2	TYR	128	87.877	278.373	119.185	1.00	80.56	6
ATOM	686	CE2	TYR	128	86.507	278.191	119.382	1.00	84.39	6
ATOM	687	CZ	TYR	128	85.912	276.988	118.989	1.00	92.94	6
ATOM	688	OH	TYR	128	84.554	276.773	119.183	1.00	94.57	8
ATOM	689	C	TYR	128	90.728	279.841	119.429	1.00	72.05	6
ATOM	690	O	TYR	128	90.868	281.074	119.367	1.00	75.92	8
ATOM	691	N	ALA	129	90.718	279.195	120.592	1.00	69.32	7
ATOM	692	CA	ALA	129	90.854	279.946	121.834	1.00	69.96	6
ATOM	693	CB	ALA	129	90.210	279.185	122.974	1.00	71.00	6
ATOM	694	C	ALA	129	92.336	280.143	122.101	1.00	72.34	6
ATOM	695	O	ALA	129	92.862	279.634	123.088	1.00	77.83	8
ATOM	696	N	GLY	130	93.017	280.877	121.223	1.00	70.46	7
ATOM	697	CA	GLY	130	94.449	281.068	121.382	1.00	65.45	6
ATOM	698	C	GLY	130	95.251	279.840	120.953	1.00	62.00	6
ATOM	699	O	GLY	130	96.447	279.941	120.711	1.00	59.82	8
ATOM	700	N	ARG	131	94.596	278.681	120.884	1.00	61.34	7
ATOM	701	CA	ARG	131	95.224	277.426	120.470	1.00	62.10	6
ATOM	702	CB	ARG	131	94.569	276.234	121.188	1.00	72.05	6
ATOM	703	CG	ARG	131	94.807	276.052	122.698	1.00	83.50	6
ATOM	704	CD	ARG	131	94.232	274.670	123.112	1.00	93.50	6
ATOM	705	NE	ARG	131	94.244	274.361	124.550	1.00	98.15	7
ATOM	706	CZ	ARG	131	93.539	273.369	125.107	1.00	99.21	6
ATOM	707	NH1	ARG	131	92.762	272.589	124.363	1.00	94.93	7
ATOM	708	NH2	ARG	131	93.620	273.135	126.411	1.00	98.95	7
ATOM	709	C	ARG	131	95.046	277.200	118.958	1.00	57.49	6
ATOM	710	O	ARG	131	93.940	277.307	118.450	1.00	57.51	8
ATOM	711	N	LYS	132	96.110	276.811	118.264	1.00	51.73	7
ATOM	712	CA	LYS	132	96.050	276.562	116.822	1.00	48.76	6
ATOM	713	CB	LYS	132	97.452	276.483	116.235	1.00	45.36	6
ATOM	714	CG	LYS	132	98.309	277.684	116.375	1.00	52.39	6
ATOM	715	CD	LYS	132	99.696	277.343	115.847	1.00	55.25	6
ATOM	716	CE	LYS	132	99.660	276.845	114.401	1.00	57.49	6
ATOM	717	NZ	LYS	132	101.037	276.596	113.850	1.00	56.75	7
ATOM	718	C	LYS	132	95.359	275.261	116.362	1.00	52.12	6
ATOM	719	O	LYS	132	96.011	274.225	116.266	1.00	55.37	8
ATOM	720	N	CYS	133	94.075	275.302	116.031	1.00	52.86	7
ATOM	721	CA	CYS	133	93.398	274.093	115.571	1.00	55.23	6
ATOM	722	CB	CYS	133	91.911	274.144	115.921	1.00	66.98	6
ATOM	723	SG	CYS	133	91.479	273.424	117.557	1.00	93.79	16
ATOM	724	C	CYS	133	93.580	273.923	114.045	1.00	50.94	6
ATOM	725	O	CYS	133	93.731	274.899	113.318	1.00	45.59	8
ATOM	726	N	LEU	134	93.613	272.676	113.577	1.00	48.19	7
ATOM	727	CA	LEU	134	93.779	272.352	112.149	1.00	43.79	6
ATOM	728	CB	LEU	134	94.890	271.318	111.982	1.00	36.69	6
ATOM	729	CG	LEU	134	95.073	270.665	110.625	1.00	34.12	6
ATOM	730	CD1	LEU	134	96.107	271.405	109.813	1.00	29.08	6
ATOM	731	CD2	LEU	134	95.511	269.247	110.855	1.00	40.95	6
ATOM	732	C	LEU	134	92.473	271.758	111.638	1.00	42.98	6
ATOM	733	O	LEU	134	92.190	270.601	111.918	1.00	43.44	8
ATOM	734	N	LEU	135	91.711	272.534	110.864	1.00	40.09	7
ATOM	735	CA	LEU	135	90.421	272.088	110.317	1.00	35.41	6
ATOM	736	CB	LEU	135	89.432	273.265	110.279	1.00	32.99	6
ATOM	737	CG	LEU	135	89.161	274.032	111.582	1.00	34.85	6
ATOM	738	CD1	LEU	135	90.052	275.216	111.673	1.00	36.09	6
ATOM	739	CD2	LEU	135	87.742	274.511	111.652	1.00	38.95	6
ATOM	740	C	LEU	135	90.486	271.411	108.949	1.00	34.00	6
ATOM	741	O	LEU	135	91.092	271.953	108.028	1.00	33.53	8
ATOM	742	N	ILE	136	89.902	270.210	108.833	1.00	31.34	7
ATOM	743	CA	ILE	136	89.902	269.468	107.561	1.00	30.34	6
ATOM	744	CB	ILE	136	90.757	268.077	107.604	1.00	32.50	6
ATOM	745	CG2	ILE	136	91.589	267.922	108.872	1.00	20.30	6
ATOM	746	CG1	ILE	136	89.865	266.844	107.496	1.00	41.24	6
ATOM	747	CD1	ILE	136	89.726	266.280	106.088	1.00	44.23	6
ATOM	748	C	ILE	136	88.468	269.305	107.007	1.00	28.31	6
ATOM	749	O	ILE	136	87.570	268.814	107.683	1.00	30.67	8
ATOM	750	N	VAL	137	88.247	269.819	105.804	1.00	28.22	7
ATOM	751	CA	VAL	137	86.938	269.747	105.153	1.00	32.67	6
ATOM	752	CB	VAL	137	86.570	271.096	104.463	1.00	31.29	6
ATOM	753	CG1	VAL	137	85.133	271.052	103.943	1.00	32.08	6
ATOM	754	CG2	VAL	137	86.755	272.264	105.429	1.00	32.62	6
ATOM	755	C	VAL	137	86.904	268.646	104.103	1.00	34.59	6
ATOM	756	O	VAL	137	87.710	268.660	103.181	1.00	37.66	8
ATOM	757	N	MET	138	85.943	267.730	104.206	1.00	33.28	7
ATOM	758	CA	MET	138	85.847	266.635	103.238	1.00	35.76	6
ATOM	759	CB	MET	138	86.464	265.370	103.824	1.00	37.44	6
ATOM	760	CG	MET	138	85.736	264.826	105.023	1.00	41.23	6
ATOM	761	SD	MET	138	86.916	264.123	106.117	1.00	39.58	16
ATOM	762	CE	MET	138	86.250	264.575	107.677	1.00	45.86	6
ATOM	763	C	MET	138	84.442	266.331	102.737	1.00	35.00	6
ATOM	764	O	MET	138	83.460	266.769	103.334	1.00	41.33	8
ATOM	765	N	GLU	139	84.347	265.540	101.670	1.00	30.10	7
ATOM	766	CA	GLU	139	83.046	265.193	101.112	1.00	39.75	6
ATOM	767	CB	GLU	139	83.156	264.290	99.874	1.00	42.80	6
ATOM	768	CG	GLU	139	83.858	262.953	100.032	1.00	48.42	6
ATOM	769	CD	GLU	139	83.817	262.138	98.734	1.00	54.91	6
ATOM	770	OE1	GLU	139	84.549	262.471	97.770	1.00	56.45	8
ATOM	771	OE2	GLU	139	83.028	261.176	98.666	1.00	60.18	8
ATOM	772	C	GLU	139	82.105	264.587	102.127	1.00	45.08	6
ATOM	773	O	GLU	139	82.426	263.589	102.761	1.00	47.19	8
ATOM	774	N	CYS	140	80.959	265.233	102.318	1.00	50.05	7
ATOM	775	CA	CYS	140	79.984	264.739	103.271	1.00	52.82	6
ATOM	776	CB	CYS	140	78.900	265.773	103.536	1.00	47.54	6
ATOM	777	SG	CYS	140	77.619	265.125	104.606	1.00	50.11	16
ATOM	778	C	CYS	140	79.337	263.422	102.852	1.00	55.80	6
ATOM	779	O	CYS	140	78.439	263.398	102.011	1.00	60.82	8
ATOM	780	N	LEU	141	79.807	262.328	103.439	1.00	55.40	7
ATOM	781	CA	LEU	141	79.269	261.020	103.133	1.00	57.23	6
ATOM	782	CB	LEU	141	80.332	259.945	103.322	1.00	52.66	6
ATOM	783	CG	LEU	141	81.637	260.014	102.538	1.00	52.11	6
ATOM	784	CD1	LEU	141	82.624	259.085	103.180	1.00	53.91	6
ATOM	785	CD2	LEU	141	81.432	259.646	101.096	1.00	46.92	6
ATOM	786	C	LEU	141	78.141	260.768	104.127	1.00	63.81	6
ATOM	787	O	LEU	141	78.392	260.546	105.311	1.00	63.90	8
ATOM	788	N	ASP	142	76.899	260.897	103.673	1.00	67.57	7
ATOM	789	CA	ASP	142	75.760	260.665	104.547	1.00	71.27	6
ATOM	790	CB	ASP	142	74.977	261.957	104.865	1.00	72.82	6
ATOM	791	CG	ASP	142	74.569	262.750	103.622	1.00	79.35	6
ATOM	792	OD1	ASP	142	74.091	263.896	103.796	1.00	80.77	8
ATOM	793	OD2	ASP	142	74.710	262.249	102.484	1.00	81.62	8
ATOM	794	C	ASP	142	74.884	259.565	103.957	1.00	72.26	6
ATOM	795	O	ASP	142	73.885	259.820	103.298	1.00	75.60	8
ATOM	796	N	GLY	143	75.346	258.333	104.133	1.00	72.50	7
ATOM	797	CA	GLY	143	74.636	257.169	103.648	1.00	70.03	6
ATOM	798	C	GLY	143	74.837	256.015	104.614	1.00	72.94	6
ATOM	799	O	GLY	143	74.685	254.854	104.236	1.00	75.97	8
ATOM	800	N	GLY	144	75.237	256.336	105.846	1.00	71.12	7
ATOM	801	CA	GLY	144	75.438	255.330	106.878	1.00	68.70	6
ATOM	802	C	GLY	144	76.639	254.410	106.747	1.00	68.54	6
ATOM	803	O	GLY	144	77.202	254.253	105.656	1.00	68.34	8
ATOM	804	N	GLU	145	77.021	253.797	107.870	1.00	64.95	7
ATOM	805	CA	GLU	145	78.147	252.866	107.912	1.00	65.01	6
ATOM	806	CB	GLU	145	78.490	252.519	109.355	1.00	66.21	6
ATOM	807	CG	GLU	145	78.773	253.764	110.201	1.00	73.19	6
ATOM	808	CD	GLU	145	79.216	253.440	111.628	1.00	82.81	6
ATOM	809	OE1	GLU	145	79.225	252.218	112.039	1.00	83.16	8
ATOM	810	OE2	GLU	145	79.581	254.391	112.420	1.00	83.36	8
ATOM	811	C	GLU	145	77.748	251.594	107.129	1.00	66.76	6
ATOM	812	O	GLU	145	76.561	251.245	107.038	1.00	68.33	8
ATOM	813	N	LEU	146	78.759	250.940	106.582	1.00	68.74	7
ATOM	814	CA	LEU	146	78.606	249.725	105.743	1.00	66.25	6
ATOM	815	CB	LEU	146	79.902	248.909	105.752	1.00	57.44	6
ATOM	816	CG	LEU	146	79.773	247.563	105.032	1.00	47.88	6
ATOM	817	CD1	LEU	146	79.265	247.693	103.594	1.00	46.14	6
ATOM	818	CD2	LEU	146	81.101	246.807	104.933	1.00	50.82	6
ATOM	819	C	LEU	146	77.465	248.809	106.229	1.00	67.39	6
ATOM	820	O	LEU	146	76.381	248.759	105.631	1.00	67.26	8
ATOM	821	N	PHE	147	77.740	248.090	107.303	1.00	70.22	7
ATOM	822	CA	PHE	147	76.792	247.116	107.885	1.00	72.92	6
ATOM	823	CB	PHE	147	77.421	246.452	109.106	1.00	65.49	6
ATOM	824	CG	PHE	147	78.681	245.679	108.738	1.00	66.56	6
ATOM	825	CD1	PHE	147	79.865	245.888	109.451	1.00	63.92	6
ATOM	826	CD2	PHE	147	78.645	244.768	107.678	1.00	62.65	6
ATOM	827	CE1	PHE	147	81.022	245.185	109.099	1.00	55.36	6
ATOM	828	CE2	PHE	147	79.802	244.066	107.324	1.00	60.25	6
ATOM	829	CZ	PHE	147	80.991	244.275	108.034	1.00	60.76	6
ATOM	830	C	PHE	147	75.479	247.787	108.298	1.00	74.88	6
ATOM	831	O	PHE	147	74.384	247.306	107.965	1.00	76.29	8
ATOM	832	N	SER	148	75.630	248.880	109.016	1.00	83.68	7
ATOM	833	CA	SER	148	74.496	249.666	109.527	1.00	84.38	6
ATOM	834	CB	SER	148	75.004	250.936	110.213	1.00	86.90	6
ATOM	835	OG	SER	148	75.821	250.595	111.322	1.00	93.14	8
ATOM	836	C	SER	148	73.564	250.083	108.385	1.00	83.98	6
ATOM	837	O	SER	148	72.724	250.981	108.543	1.00	86.96	8
ATOM	838	N	ARG	149	73.732	249.418	107.258	1.00	84.50	7
ATOM	839	CA	ARG	149	72.934	249.702	106.056	1.00	88.99	6
ATOM	840	CB	ARG	149	73.710	250.629	105.124	1.00	90.89	6
ATOM	841	CG	ARG	149	72.815	251.332	104.107	1.00	94.32	6
ATOM	842	CD	ARG	149	73.539	252.436	103.340	1.00	99.43	6
ATOM	843	NE	ARG	149	72.701	253.056	102.307	1.00	95.52	7
ATOM	844	CZ	ARG	149	72.814	252.799	100.999	1.00	91.72	6
ATOM	845	NH1	ARG	149	73.729	251.934	100.542	1.00	93.06	7
ATOM	846	NH2	ARG	149	72.048	253.365	100.057	1.00	90.70	7
ATOM	847	C	ARG	149	72.609	248.412	105.294	1.00	88.60	6
ATOM	848	O	ARG	149	71.889	248.432	104.297	1.00	89.68	8
ATOM	849	N	ILE	150	73.186	247.298	105.734	1.00	90.04	7
ATOM	850	CA	ILE	150	72.937	246.012	105.085	1.00	88.63	6
ATOM	851	CB	ILE	150	74.035	244.954	105.439	1.00	87.45	6
ATOM	852	CG2	ILE	150	73.618	243.569	104.969	1.00	84.81	6
ATOM	853	CG1	ILE	150	75.380	245.326	104.793	1.00	83.66	6
ATOM	854	CD1	ILE	150	75.414	245.214	103.273	1.00	71.70	6
ATOM	855	C	ILE	150	71.583	245.566	105.619	1.00	87.90	6
ATOM	856	O	ILE	150	70.727	245.083	104.869	1.00	85.06	8
ATOM	857	N	GLN	151	71.389	245.807	106.914	1.00	87.71	7
ATOM	858	CA	GLN	151	70.155	245.456	107.609	1.00	94.70	6
ATOM	859	CB	GLN	151	70.393	245.437	109.123	1.00	89.92	6
ATOM	860	CG	GLN	151	71.027	246.693	109.681	1.00	92.02	6
ATOM	861	CD	GLN	151	71.391	246.558	111.147	1.00	92.48	6
ATOM	862	OE1	GLN	151	70.539	246.254	111.981	1.00	91.88	8
ATOM	863	NE2	GLN	151	72.663	246.784	111.468	1.00	90.51	7
ATOM	864	C	GLN	151	68.994	246.397	107.261	1.00	97.00	6
ATOM	865	O	GLN	151	67.826	246.067	107.481	1.00	99.89	8
ATOM	866	N	ASP	152	69.319	247.561	106.708	1.00	98.27	7
ATOM	867	CA	ASP	152	68.305	248.537	106.331	1.00	97.52	6
ATOM	868	CB	ASP	152	68.895	249.949	106.341	1.00	100.00	6
ATOM	869	CG	ASP	152	69.240	250.441	107.744	1.00	100.00	6
ATOM	870	OD1	ASP	152	69.085	249.678	108.727	1.00	99.03	8
ATOM	871	OD2	ASP	152	69.667	251.611	107.858	1.00	100.00	8
ATOM	872	C	ASP	152	67.706	248.246	104.959	1.00	100.00	6
ATOM	873	O	ASP	152	66.737	248.895	104.557	1.00	100.00	8
ATOM	874	N	ALA	153	68.276	247.265	104.257	1.00	100.00	7
ATOM	875	CA	ALA	153	67.818	246.870	102.920	1.00	100.00	6
ATOM	876	CB	ALA	153	68.836	245.920	102.268	1.00	100.00	6
ATOM	877	C	ALA	153	66.421	246.245	102.907	1.00	99.95	6
ATOM	878	O	ALA	153	65.495	246.798	102.312	1.00	98.31	8
ATOM	879	N	GLY	154	66.284	245.086	103.545	1.00	100.00	7
ATOM	880	CA	GLY	154	64.999	244.405	103.596	1.00	100.00	6
ATOM	881	C	GLY	154	64.691	243.532	102.388	1.00	100.00	6
ATOM	882	O	GLY	154	64.387	242.340	102.534	1.00	100.00	8
ATOM	883	N	ALA	155	64.737	244.129	101.199	1.00	100.00	7
ATOM	884	CA	ALA	155	64.466	243.405	99.960	1.00	100.00	6
ATOM	885	CB	ALA	155	63.096	243.806	99.401	1.00	97.77	6
ATOM	886	C	ALA	155	65.567	243.673	98.929	1.00	100.00	6
ATOM	887	O	ALA	155	65.898	244.864	98.714	1.00	100.00	8
ATOM	888	OT	ALA	155	66.096	242.688	98.360	1.00	100.00	8
ATOM	889	CB	PHE	158	72.866	241.609	100.293	1.00	100.00	6
ATOM	890	CG	PHE	158	74.263	241.800	100.805	1.00	98.97	6
ATOM	891	CD1	PHE	158	75.327	241.911	99.926	1.00	96.55	6
ATOM	892	CD2	PHE	158	74.513	241.866	102.176	1.00	98.95	6
ATOM	893	CE1	PHE	158	76.619	242.084	100.399	1.00	99.47	6
ATOM	894	CE2	PHE	158	75.803	72.954	243.096	1.00	100.00	6
ATOM	895	CZ	PHE	158	118.737	74.087	244.013	1.00	100.00	6
ATOM	896	C	PHE	158	118.645	74.381	244.373	1.00	99.29	6
ATOM	897	O	PHE	158	117.180	73.737	245.267	1.00	100.00	8
ATOM	898	N	PHE	158	119.440	72.846	246.032	1.00	98.27	7
ATOM	899	CA	PHE	158	119.059	74.441	245.460	1.00	100.00	6
ATOM	900	N	THR	159	120.552	74.237	246.608	1.00	99.84	7
ATOM	901	CA	THR	159	121.436	75.351	246.659	1.00	99.67	6
ATOM	902	CB	THR	159	122.482	74.180	247.927	1.00	98.54	6
ATOM	903	OG1	THR	159	120.669	73.540	248.887	1.00	98.40	8
ATOM	904	CG2	THR	159	121.100	74.853	247.955	1.00	98.27	6
ATOM	905	C	THR	159	119.528	74.875	249.138	1.00	100.00	6
ATOM	906	O	THR	159	118.683	73.475	249.507	1.00	100.00	8
ATOM	907	N	GLU	160	118.210	72.926	248.880	1.00	99.64	7
ATOM	908	CA	GLU	160	117.293	75.797	248.923	1.00	99.65	6
ATOM	909	CB	GLU	160	117.495	72.873	250.470	1.00	98.97	6
ATOM	910	CG	GLU	160	118.905	71.524	250.954	1.00	100.00	6
ATOM	911	CD	GLU	160	118.606	70.497	250.299	1.00	100.00	6
ATOM	912	OE1	GLU	160	119.534	71.472	252.478	1.00	99.95	8
ATOM	913	OE2	GLU	160	118.744	71.050	253.128	1.00	100.00	8
ATOM	914	C	GLU	160	117.767	71.875	253.007	1.00	99.48	6
ATOM	915	O	GLU	160	119.807	237.806	96.720	1.00	98.63	8
ATOM	916	N	ARG	161	77.252	237.544	95.320	1.00	100.00	7
ATOM	917	CA	ARG	161	77.774	238.422	94.268	1.00	99.32	6
ATOM	918	CB	ARG	161	76.840	238.487	93.051	1.00	99.62	6
ATOM	919	CG	ARG	161	76.776	237.243	92.184	1.00	99.61	6
ATOM	920	CD	ARG	161	76.106	237.519	90.821	1.00	100.00	6
ATOM	921	NE	ARG	161	74.793	238.165	90.946	1.00	100.00	7
ATOM	922	CZ	ARG	161	73.665	237.717	90.397	1.00	97.68	6
ATOM	923	NH1	ARG	161	73.664	236.604	89.670	1.00	96.75	7
ATOM	924	NH2	ARG	161	72.528	238.376	90.594	1.00	88.21	7
ATOM	925	C	ARG	161	77.937	239.835	94.790	1.00	99.67	6
ATOM	926	O	ARG	161	78.942	240.491	94.517	1.00	100.00	8
ATOM	927	N	GLU	162	76.923	240.317	95.502	1.00	97.59	7
ATOM	928	CA	GLU	162	76.963	241.660	96.056	1.00	97.16	6
ATOM	929	CB	GLU	162	75.601	242.039	96.626	1.00	97.68	6
ATOM	930	CG	GLU	162	74.510	242.165	95.578	1.00	100.00	6
ATOM	931	CD	GLU	162	73.129	242.417	96.180	1.00	100.00	6
ATOM	932	OE1	GLU	162	73.017	242.543	97.424	1.00	100.00	8
ATOM	933	OE2	GLU	162	72.149	242.481	95.399	1.00	100.00	8
ATOM	934	C	GLU	162	78.037	241.784	97.131	1.00	95.58	6
ATOM	935	O	GLU	162	78.765	242.782	97.181	1.00	97.66	8
ATOM	936	N	ALA	163	78.159	240.753	97.964	1.00	89.28	7
ATOM	937	CA	ALA	163	79.145	240.750	99.031	1.00	85.28	6
ATOM	938	CB	ALA	163	79.094	239.445	99.779	1.00	83.94	6
ATOM	939	C	ALA	163	80.523	240.972	98.435	1.00	85.18	6
ATOM	940	O	ALA	163	81.292	241.798	98.920	1.00	88.15	8
ATOM	941	N	SER	164	80.802	240.270	97.343	1.00	84.25	7
ATOM	942	CA	SER	164	82.082	240.376	96.655	1.00	84.10	6
ATOM	943	CB	SER	164	82.106	239.436	95.446	1.00	82.73	6
ATOM	944	OG	SER	164	83.274	239.620	94.669	1.00	81.87	8
ATOM	945	C	SER	164	82.365	241.808	96.203	1.00	84.15	6
ATOM	946	O	SER	164	83.448	242.342	96.444	1.00	86.16	8
ATOM	947	N	GLU	165	81.377	242.439	95.581	1.00	82.16	7
ATOM	948	CA	GLU	165	81.537	243.807	95.103	1.00	81.81	6
ATOM	949	CB	GLU	165	80.242	244.284	94.442	1.00	85.50	6
ATOM	950	CG	GLU	165	79.761	243.359	93.330	1.00	91.21	6
ATOM	951	CD	GLU	165	78.367	243.695	92.831	1.00	96.12	6
ATOM	952	OE1	GLU	165	77.451	243.893	93.667	1.00	97.13	8
ATOM	953	OE2	GLU	165	78.192	243.749	91.595	1.00	93.84	8
ATOM	954	C	GLU	165	81.968	244.755	96.225	1.00	77.89	6
ATOM	955	O	GLU	165	82.830	245.614	96.028	1.00	75.81	8
ATOM	956	N	ILE	166	81.392	244.571	97.409	1.00	73.64	7
ATOM	957	CA	ILE	166	81.731	245.414	98.546	1.00	70.16	6
ATOM	958	CB	ILE	166	80.845	245.092	99.782	1.00	71.64	6
ATOM	959	CG2	ILE	166	81.350	245.828	101.032	1.00	69.95	6
ATOM	960	CG1	ILE	166	79.392	245.478	99.495	1.00	71.59	6
ATOM	961	CD1	ILE	166	78.467	245.322	100.691	1.00	73.87	6
ATOM	962	C	ILE	166	83.199	245.188	98.871	1.00	67.47	6
ATOM	963	O	ILE	166	83.969	246.134	99.008	1.00	65.49	8
ATOM	964	N	MET	167	83.599	243.927	98.931	1.00	66.41	7
ATOM	965	CA	MET	167	84.983	243.615	99.235	1.00	66.97	6
ATOM	966	CB	MET	167	85.186	242.114	99.409	1.00	64.61	6
ATOM	967	CG	MET	167	84.631	241.592	100.701	1.00	62.83	6
ATOM	968	SD	MET	167	85.047	242.672	102.095	1.00	65.77	16
ATOM	969	CE	MET	167	86.840	242.791	101.993	1.00	55.22	6
ATOM	970	C	MET	167	85.939	244.152	98.192	1.00	67.52	6
ATOM	971	O	MET	167	87.018	244.630	98.532	1.00	69.09	8
ATOM	972	N	LYS	168	85.526	244.121	96.930	1.00	66.31	7
ATOM	973	CA	LYS	168	86.371	244.611	95.854	1.00	67.69	6
ATOM	974	CB	LYS	168	85.726	244.329	94.507	1.00	64.03	6
ATOM	975	CG	LYS	168	86.525	244.820	93.342	1.00	59.62	6
ATOM	976	CD	LYS	168	85.811	244.534	92.055	1.00	62.43	6
ATOM	977	CE	LYS	168	86.667	244.936	90.884	1.00	65.62	6
ATOM	978	NZ	LYS	168	87.995	244.269	90.962	1.00	74.64	7
ATOM	979	C	LYS	168	86.646	246.101	96.005	1.00	72.08	6
ATOM	980	O	LYS	168	87.760	246.558	95.760	1.00	74.89	8
ATOM	981	N	SER	169	85.632	246.845	96.441	1.00	74.39	7
ATOM	982	CA	SER	169	85.749	248.289	96.635	1.00	74.74	6
ATOM	983	CB	SER	169	84.371	248.892	96.887	1.00	76.12	6
ATOM	984	OG	SER	169	83.470	248.522	95.859	1.00	83.04	8
ATOM	985	C	SER	169	86.687	248.606	97.800	1.00	73.95	6
ATOM	986	O	SER	169	87.665	249.335	97.625	1.00	75.56	8
ATOM	987	N	ILE	170	86.393	248.042	98.978	1.00	67.40	7
ATOM	988	CA	ILE	170	87.204	248.250	100.177	1.00	57.14	6
ATOM	989	CB	ILE	170	86.681	247.425	101.361	1.00	54.17	6
ATOM	990	CG2	ILE	170	87.443	247.789	102.636	1.00	51.19	6
ATOM	991	CG1	ILE	170	85.186	247.665	101.561	1.00	54.65	6
ATOM	992	CD1	ILE	170	84.543	246.774	102.627	1.00	53.52	6
ATOM	993	C	ILE	170	88.618	247.778	99.867	1.00	57.07	6
ATOM	994	O	ILE	170	89.590	248.277	100.421	1.00	58.79	8
ATOM	995	N	GLY	171	88.714	246.796	98.978	1.00	55.40	7
ATOM	996	CA	GLY	171	90.002	246.275	98.575	1.00	56.58	6
ATOM	997	C	GLY	171	90.755	247.342	97.810	1.00	58.83	6
ATOM	998	O	GLY	171	91.868	247.700	98.189	1.00	60.19	8
ATOM	999	N	GLU	172	90.120	247.880	96.764	1.00	60.90	7
ATOM	1000	CA	GLU	172	90.696	248.926	95.910	1.00	60.95	6
ATOM	1001	CB	GLU	172	89.673	249.370	94.858	1.00	63.76	6
ATOM	1002	CG	GLU	172	89.439	248.329	93.764	1.00	74.49	6
ATOM	1003	CD	GLU	172	88.244	248.622	92.864	1.00	80.58	6
ATOM	1004	OE1	GLU	172	87.975	247.791	91.968	1.00	81.43	8
ATOM	1005	OE2	GLU	172	87.568	249.661	93.048	1.00	84.08	8
ATOM	1006	C	GLU	172	91.234	250.136	96.683	1.00	56.80	6
ATOM	1007	O	GLU	172	92.255	250.708	96.312	1.00	55.99	8
ATOM	1008	N	ALA	173	90.549	250.519	97.755	1.00	49.99	7
ATOM	1009	CA	ALA	173	90.973	251.647	98.565	1.00	46.26	6
ATOM	1010	CB	ALA	173	89.978	251.877	99.684	1.00	47.73	6
ATOM	1011	C	ALA	173	92.336	251.314	99.147	1.00	50.11	6
ATOM	1012	O	ALA	173	93.246	252.136	99.131	1.00	50.34	8
ATOM	1013	N	ILE	174	92.467	250.083	99.642	1.00	54.38	7
ATOM	1014	CA	ILE	174	93.707	249.592	100.246	1.00	56.54	6
ATOM	1015	CB	ILE	174	93.466	248.261	100.994	1.00	54.70	6
ATOM	1016	CG2	ILE	174	94.729	247.814	101.677	1.00	54.75	6
ATOM	1017	CG1	ILE	174	92.388	248.439	102.060	1.00	55.56	6
ATOM	1018	CD1	ILE	174	92.759	249.439	103.132	1.00	61.81	6
ATOM	1019	C	ILE	174	94.838	249.430	99.220	1.00	55.76	6
ATOM	1020	O	ILE	174	96.004	249.721	99.503	1.00	54.57	8
ATOM	1021	N	GLN	175	94.483	248.972	98.026	1.00	50.89	7
ATOM	1022	CA	GLN	175	95.455	248.781	96.969	1.00	48.91	6
ATOM	1023	CB	GLN	175	94.782	248.129	95.768	1.00	49.16	6
ATOM	1024	CG	GLN	175	95.660	248.026	94.543	1.00	57.32	6
ATOM	1025	CD	GLN	175	95.082	247.080	93.526	1.00	67.72	6
ATOM	1026	OE1	GLN	175	94.009	247.329	92.970	1.00	73.86	8
ATOM	1027	NE2	GLN	175	95.771	245.964	93.296	1.00	70.28	7
ATOM	1028	C	GLN	175	96.109	250.108	96.574	1.00	48.06	6
ATOM	1029	O	GLN	175	97.296	250.160	96.265	1.00	45.44	8
ATOM	1030	N	TYR	176	95.326	251.180	96.590	1.00	49.18	7
ATOM	1031	CA	TYR	176	95.840	252.495	96.233	1.00	46.76	6
ATOM	1032	CB	TYR	176	94.693	253.492	96.022	1.00	47.48	6
ATOM	1033	CG	TYR	176	95.122	254.810	95.409	1.00	47.49	6
ATOM	1034	CD1	TYR	176	94.948	255.049	94.053	1.00	47.65	6
ATOM	1035	CE1	TYR	176	95.365	256.235	93.474	1.00	46.78	6
ATOM	1036	CD2	TYR	176	95.728	255.802	96.179	1.00	47.35	6
ATOM	1037	CE2	TYR	176	96.155	256.989	95.608	1.00	47.39	6
ATOM	1038	CZ	TYR	176	95.970	257.199	94.254	1.00	49.35	6
ATOM	1039	OH	TYR	176	96.403	258.366	93.666	1.00	55.02	8
ATOM	1040	C	TYR	176	96.745	252.951	97.356	1.00	44.79	6
ATOM	1041	O	TYR	176	97.838	253.460	97.130	1.00	42.65	8
ATOM	1042	N	LEU	177	96.298	252.714	98.577	1.00	45.97	7
ATOM	1043	CA	LEU	177	97.072	253.102	99.735	1.00	49.57	6
ATOM	1044	CB	LEU	177	96.256	252.882	101.004	1.00	43.02	6
ATOM	1045	CG	LEU	177	95.211	253.961	101.230	1.00	35.55	6
ATOM	1046	CD1	LEU	177	94.448	253.643	102.471	1.00	41.43	6
ATOM	1047	CD2	LEU	177	95.882	255.295	101.390	1.00	29.71	6
ATOM	1048	C	LEU	177	98.426	252.388	99.798	1.00	52.23	6
ATOM	1049	O	LEU	177	99.449	253.020	100.070	1.00	51.81	8
ATOM	1050	N	HIS	178	98.449	251.093	99.489	1.00	51.55	7
ATOM	1051	CA	HIS	178	99.710	250.369	99.532	1.00	51.08	6
ATOM	1052	CB	HIS	178	99.492	248.857	99.664	1.00	43.74	6
ATOM	1053	CG	HIS	178	98.800	248.456	100.936	1.00	47.07	6
ATOM	1054	CD2	HIS	178	98.460	249.172	102.036	1.00	46.50	6
ATOM	1055	ND1	HIS	178	98.328	247.181	101.158	1.00	48.56	7
ATOM	1056	CE1	HIS	178	97.727	247.129	102.334	1.00	44.08	6
ATOM	1057	NE2	HIS	178	97.792	248.324	102.886	1.00	39.34	7
ATOM	1058	C	HIS	178	100.592	250.728	98.337	1.00	54.56	6
ATOM	1059	O	HIS	178	101.808	250.857	98.477	1.00	60.07	8
ATOM	1060	N	SER	179	99.977	251.005	97.190	1.00	53.28	7
ATOM	1061	CA	SER	179	100.742	251.358	95.999	1.00	48.40	6
ATOM	1062	CB	SER	179	99.839	251.443	94.792	1.00	46.50	6
ATOM	1063	OG	SER	179	98.933	252.510	94.955	1.00	58.97	8
ATOM	1064	C	SER	179	101.491	252.669	96.173	1.00	50.14	6
ATOM	1065	O	SER	179	102.375	252.984	95.383	1.00	55.19	8
ATOM	1066	N	ILE	180	101.088	253.476	97.147	1.00	48.95	7
ATOM	1067	CA	ILE	180	101.776	254.740	97.372	1.00	49.17	6
ATOM	1068	CB	ILE	180	100.885	256.001	97.168	1.00	45.91	6
ATOM	1069	CG2	ILE	180	100.692	256.258	95.696	1.00	49.21	6
ATOM	1070	CG1	ILE	180	99.542	255.878	97.875	1.00	46.39	6
ATOM	1071	CD1	ILE	180	98.718	257.152	97.806	1.00	40.29	6
ATOM	1072	C	ILE	180	102.478	254.744	98.726	1.00	51.29	6
ATOM	1073	O	ILE	180	102.776	255.802	99.285	1.00	51.35	8
ATOM	1074	N	ASN	181	102.737	253.532	99.226	1.00	52.87	7
ATOM	1075	CA	ASN	181	103.412	253.285	100.502	1.00	57.36	6
ATOM	1076	CB	ASN	181	104.861	253.769	100.424	1.00	63.31	6
ATOM	1077	CG	ASN	181	105.620	253.120	99.295	1.00	75.30	6
ATOM	1078	OD1	ASN	181	105.802	251.901	99.276	1.00	83.57	8
ATOM	1079	ND2	ASN	181	106.040	253.924	98.324	1.00	79.92	7
ATOM	1080	C	ASN	181	102.743	253.872	101.735	1.00	57.83	6
ATOM	1081	O	ASN	181	103.406	254.484	102.582	1.00	61.51	8
ATOM	1082	N	ILE	182	101.437	253.654	101.849	1.00	51.41	7
ATOM	1083	CA	ILE	182	100.667	254.159	102.974	1.00	46.59	6
ATOM	1084	CB	ILE	182	99.690	255.300	102.533	1.00	44.22	6
ATOM	1085	CG2	ILE	182	98.816	255.745	103.693	1.00	40.74	6
ATOM	1086	CG1	ILE	182	100.458	256.506	101.992	1.00	40.60	6
ATOM	1087	CD1	ILE	182	99.577	257.562	101.394	1.00	29.78	6
ATOM	1088	C	ILE	182	99.831	253.034	103.551	1.00	48.39	6
ATOM	1089	O	ILE	182	99.079	252.379	102.832	1.00	49.44	8
ATOM	1090	N	ALA	183	100.015	252.764	104.834	1.00	46.67	7
ATOM	1091	CA	ALA	183	99.255	251.719	105.497	1.00	47.68	6
ATOM	1092	CB	ALA	183	100.129	251.001	106.454	1.00	54.24	6
ATOM	1093	C	ALA	183	98.143	252.462	106.240	1.00	49.64	6
ATOM	1094	O	ALA	183	98.410	253.427	106.960	1.00	52.17	8
ATOM	1095	N	HIS	184	96.901	252.036	106.075	1.00	47.11	7
ATOM	1096	CA	HIS	184	95.812	252.724	106.757	1.00	50.78	6
ATOM	1097	CB	HIS	184	94.443	252.293	106.216	1.00	55.29	6
ATOM	1098	CG	HIS	184	93.301	253.092	106.765	1.00	58.16	6
ATOM	1099	CD2	HIS	184	92.997	254.406	106.647	1.00	60.55	6
ATOM	1100	ND1	HIS	184	92.312	252.541	107.553	1.00	61.00	7
ATOM	1101	CE1	HIS	184	91.447	253.478	107.895	1.00	57.28	6
ATOM	1102	NE2	HIS	184	91.839	254.618	107.358	1.00	61.01	7
ATOM	1103	C	HIS	184	95.859	252.567	108.264	1.00	49.24	6
ATOM	1104	O	HIS	184	95.921	253.559	108.978	1.00	51.74	8
ATOM	1105	N	ARG	185	95.806	251.320	108.728	1.00	48.51	7
ATOM	1106	CA	ARG	185	95.841	250.980	110.147	1.00	47.17	6
ATOM	1107	CB	ARG	185	97.055	251.629	110.815	1.00	46.44	6
ATOM	1108	CG	ARG	185	98.341	251.272	110.142	1.00	51.52	6
ATOM	1109	CD	ARG	185	99.449	251.153	111.127	1.00	53.05	6
ATOM	1110	NE	ARG	185	100.278	252.341	111.191	1.00	53.65	7
ATOM	1111	CZ	ARG	185	100.571	252.958	112.326	1.00	60.18	6
ATOM	1112	NH1	ARG	185	100.075	252.487	113.462	1.00	61.35	7
ATOM	1113	NH2	ARG	185	101.414	253.988	112.339	1.00	61.75	7
ATOM	1114	C	ARG	185	94.565	251.273	110.957	1.00	51.20	6
ATOM	1115	O	ARG	185	94.628	251.567	112.155	1.00	56.09	8
ATOM	1116	N	ASP	186	93.404	251.212	110.318	1.00	48.72	7
ATOM	1117	CA	ASP	186	92.172	251.467	111.034	1.00	40.68	6
ATOM	1118	CB	ASP	186	92.085	252.915	111.479	1.00	44.16	6
ATOM	1119	CG	ASP	186	91.420	253.059	112.834	1.00	51.99	6
ATOM	1120	OD1	ASP	186	90.682	254.043	113.061	1.00	53.20	8
ATOM	1121	OD2	ASP	186	91.652	252.178	113.686	1.00	58.97	8
ATOM	1122	C	ASP	186	90.960	251.100	110.226	1.00	41.38	6
ATOM	1123	O	ASP	186	89.914	251.711	110.363	1.00	43.75	8
ATOM	1124	N	VAL	187	91.085	250.064	109.411	1.00	39.20	7
ATOM	1125	CA	VAL	187	89.976	249.623	108.583	1.00	39.69	6
ATOM	1126	CB	VAL	187	90.487	248.745	107.433	1.00	36.87	6
ATOM	1127	CG1	VAL	187	89.342	248.258	106.588	1.00	32.54	6
ATOM	1128	CG2	VAL	187	91.477	249.519	106.592	1.00	30.39	6
ATOM	1129	C	VAL	187	88.881	248.899	109.377	1.00	43.45	6
ATOM	1130	O	VAL	187	88.689	247.695	109.229	1.00	45.72	8
ATOM	1131	N	LYS	188	88.183	249.646	110.232	1.00	47.30	7
ATOM	1132	CA	LYS	188	87.100	249.107	111.057	1.00	51.33	6
ATOM	1133	CB	LYS	188	86.867	249.957	112.307	1.00	49.13	6
ATOM	1134	CG	LYS	188	88.086	250.443	113.038	1.00	55.63	6
ATOM	1135	CD	LYS	188	87.711	251.686	113.831	1.00	58.48	6
ATOM	1136	CE	LYS	188	88.841	252.183	114.711	1.00	57.13	6
ATOM	1137	NZ	LYS	188	88.737	253.666	114.966	1.00	58.82	7
ATOM	1138	C	LYS	188	85.830	249.244	110.237	1.00	56.93	6
ATOM	1139	O	LYS	188	85.808	249.931	109.210	1.00	58.62	8
ATOM	1140	N	PRO	189	84.750	248.585	110.674	1.00	61.62	7
ATOM	1141	CD	PRO	189	84.717	247.481	111.647	1.00	65.55	6
ATOM	1142	CA	PRO	189	83.481	248.678	109.949	1.00	62.65	6
ATOM	1143	CB	PRO	189	82.573	247.754	110.751	1.00	62.24	6
ATOM	1144	CG	PRO	189	83.513	246.685	111.188	1.00	67.01	6
ATOM	1145	C	PRO	189	82.998	250.116	110.031	1.00	62.95	6
ATOM	1146	O	PRO	189	82.466	250.665	109.072	1.00	65.70	8
ATOM	1147	N	GLU	190	83.270	250.740	111.171	1.00	65.71	7
ATOM	1148	CA	GLU	190	82.876	252.123	111.421	1.00	67.33	6
ATOM	1149	CB	GLU	190	83.208	252.521	112.873	1.00	71.23	6
ATOM	1150	CG	GLU	190	82.547	251.611	113.955	1.00	84.17	6
ATOM	1151	CD	GLU	190	83.380	250.358	114.350	1.00	88.04	6
ATOM	1152	OE1	GLU	190	84.187	250.431	115.310	1.00	86.76	8
ATOM	1153	OE2	GLU	190	83.207	249.288	113.727	1.00	87.85	8
ATOM	1154	C	GLU	190	83.471	253.127	110.422	1.00	64.28	6
ATOM	1155	O	GLU	190	82.783	254.047	109.982	1.00	66.82	8
ATOM	1156	N	ASN	191	84.715	252.906	110.003	1.00	56.39	7
ATOM	1157	CA	ASN	191	85.357	253.812	109.060	1.00	45.18	6
ATOM	1158	CB	ASN	191	86.867	253.793	109.221	1.00	42.98	6
ATOM	1159	CG	ASN	191	87.309	254.354	110.536	1.00	49.63	6
ATOM	1160	OD1	ASN	191	86.626	255.187	111.123	1.00	60.26	8
ATOM	1161	ND2	ASN	191	88.460	253.908	111.012	1.00	51.71	7
ATOM	1162	C	ASN	191	85.005	253.616	107.611	1.00	44.46	6
ATOM	1163	O	ASN	191	85.763	254.043	106.737	1.00	41.99	8
ATOM	1164	N	LEU	192	83.888	252.942	107.349	1.00	41.14	7
ATOM	1165	CA	LEU	192	83.453	252.708	105.969	1.00	48.59	6
ATOM	1166	CB	LEU	192	83.408	251.218	105.646	1.00	48.59	6
ATOM	1167	CG	LEU	192	84.743	250.479	105.724	1.00	49.22	6
ATOM	1168	CD1	LEU	192	84.472	249.000	105.613	1.00	52.37	6
ATOM	1169	CD2	LEU	192	85.695	250.933	104.632	1.00	40.17	6
ATOM	1170	C	LEU	192	82.075	253.349	105.800	1.00	49.36	6
ATOM	1171	O	LEU	192	81.088	252.868	106.354	1.00	55.53	8
ATOM	1172	N	LEU	193	82.016	254.458	105.066	1.00	46.44	7
ATOM	1173	CA	LEU	193	80.760	255.152	104.855	1.00	40.87	6
ATOM	1174	CB	LEU	193	80.890	256.568	105.363	1.00	36.02	6
ATOM	1175	CG	LEU	193	81.582	256.608	106.719	1.00	33.27	6
ATOM	1176	CD1	LEU	193	82.047	257.996	107.073	1.00	41.39	6
ATOM	1177	CD2	LEU	193	80.631	256.094	107.738	1.00	39.25	6
ATOM	1178	C	LEU	193	80.336	255.178	103.412	1.00	47.34	6
ATOM	1179	O	LEU	193	81.156	255.270	102.506	1.00	48.69	8
ATOM	1180	N	TYR	194	79.032	255.073	103.211	1.00	52.17	7
ATOM	1181	CA	TYR	194	78.436	255.080	101.884	1.00	57.65	6
ATOM	1182	CB	TYR	194	77.139	254.266	101.929	1.00	60.06	6
ATOM	1183	CG	TYR	194	77.275	252.840	101.431	1.00	59.19	6
ATOM	1184	CD1	TYR	194	77.639	252.588	100.113	1.00	56.00	6
ATOM	1185	CE1	TYR	194	77.733	251.308	99.626	1.00	56.23	6
ATOM	1186	CD2	TYR	194	77.006	251.752	102.259	1.00	55.91	6
ATOM	1187	CE2	TYR	194	77.096	250.454	101.777	1.00	58.61	6
ATOM	1188	CZ	TYR	194	77.462	250.241	100.451	1.00	62.12	6
ATOM	1189	OH	TYR	194	77.553	248.968	99.922	1.00	67.45	8
ATOM	1190	C	TYR	194	78.163	256.546	101.550	1.00	60.39	6
ATOM	1191	O	TYR	194	77.766	257.310	102.435	1.00	62.81	8
ATOM	1192	N	THR	195	78.377	256.959	100.303	1.00	60.44	7
ATOM	1193	CA	THR	195	78.134	258.361	99.954	1.00	63.96	6
ATOM	1194	CB	THR	195	78.442	258.669	98.481	1.00	58.05	6
ATOM	1195	OG1	THR	195	77.790	257.713	97.647	1.00	59.81	8
ATOM	1196	CG2	THR	195	79.926	258.649	98.216	1.00	55.74	6
ATOM	1197	C	THR	195	76.720	258.846	100.266	1.00	71.40	6
ATOM	1198	O	THR	195	76.510	259.594	101.221	1.00	76.25	8
ATOM	1199	N	SER	196	75.756	258.403	99.468	1.00	74.19	7
ATOM	1200	CA	SER	196	74.363	258.782	99.639	1.00	75.97	6
ATOM	1201	CB	SER	196	73.807	259.245	98.300	1.00	78.14	6
ATOM	1202	OG	SER	196	74.475	258.593	97.234	1.00	80.44	8
ATOM	1203	C	SER	196	73.545	257.627	100.186	1.00	79.13	6
ATOM	1204	O	SER	196	74.105	256.592	100.543	1.00	80.00	8
ATOM	1205	N	ALA	197	72.228	257.820	100.288	1.00	83.31	7
ATOM	1206	CA	ALA	197	71.320	256.784	100.802	1.00	84.85	6
ATOM	1207	CB	ALA	197	70.150	257.417	101.561	1.00	75.89	6
ATOM	1208	C	ALA	197	70.806	255.890	99.676	1.00	86.03	6
ATOM	1209	O	ALA	197	70.322	254.788	99.922	1.00	85.29	8
ATOM	1210	N	ARG	198	70.966	256.368	98.445	1.00	89.96	7
ATOM	1211	CA	ARG	198	70.542	255.667	97.230	1.00	95.64	6
ATOM	1212	CB	ARG	198	70.782	256.584	96.016	1.00	98.85	6
ATOM	1213	CG	ARG	198	72.208	257.104	95.879	1.00	100.00	6
ATOM	1214	CD	ARG	198	72.355	258.073	94.709	1.00	100.00	6
ATOM	1215	NE	ARG	198	72.564	257.391	93.432	1.00	100.00	7
ATOM	1216	CZ	ARG	198	72.521	257.987	92.241	1.00	100.00	6
ATOM	1217	NH1	ARG	198	72.269	259.291	92.144	1.00	100.00	7
ATOM	1218	NH2	ARG	198	72.745	257.275	91.142	1.00	100.00	7
ATOM	1219	C	ARG	198	71.222	254.298	97.024	1.00	96.37	6
ATOM	1220	O	ARG	198	72.057	253.891	97.831	1.00	96.91	8
ATOM	1221	N	PRO	199	70.839	253.554	95.963	1.00	96.90	7
ATOM	1222	CD	PRO	199	69.736	253.830	95.020	1.00	96.34	6
ATOM	1223	CA	PRO	199	71.434	252.237	95.685	1.00	96.10	6
ATOM	1224	CB	PRO	199	70.446	251.629	94.694	1.00	96.27	6
ATOM	1225	CG	PRO	199	69.994	252.831	93.913	1.00	96.20	6
ATOM	1226	C	PRO	199	72.841	252.319	95.076	1.00	94.70	6
ATOM	1227	O	PRO	199	73.753	251.601	95.487	1.00	94.16	8
ATOM	1228	N	ASN	200	73.006	253.202	94.096	1.00	92.92	7
ATOM	1229	CA	ASN	200	74.283	253.393	93.421	1.00	91.48	6
ATOM	1230	CB	ASN	200	74.101	254.336	92.220	1.00	97.04	6
ATOM	1231	CG	ASN	200	75.391	254.558	91.440	1.00	100.00	6
ATOM	1232	OD1	ASN	200	76.085	255.561	91.632	1.00	100.00	8
ATOM	1233	ND2	ASN	200	75.718	253.617	90.556	1.00	100.00	7
ATOM	1234	C	ASN	200	75.329	253.957	94.383	1.00	87.10	6
ATOM	1235	O	ASN	200	76.527	253.908	94.104	1.00	85.57	8
ATOM	1236	N	ALA	201	74.867	254.484	95.516	1.00	82.18	7
ATOM	1237	CA	ALA	201	75.748	255.060	96.532	1.00	78.87	6
ATOM	1238	CB	ALA	201	75.003	255.212	97.842	1.00	79.82	6
ATOM	1239	C	ALA	201	76.989	254.214	96.745	1.00	74.77	6
ATOM	1240	O	ALA	201	76.894	253.056	97.142	1.00	76.13	8
ATOM	1241	N	ILE	202	78.150	254.783	96.447	1.00	69.27	7
ATOM	1242	CA	ILE	202	79.392	254.053	96.615	1.00	67.80	6
ATOM	1243	CB	ILE	202	80.327	254.323	95.452	1.00	67.42	6
ATOM	1244	CG2	ILE	202	80.728	255.767	95.422	1.00	56.12	6
ATOM	1245	CG1	ILE	202	81.502	253.340	95.510	1.00	79.53	6
ATOM	1246	CD1	ILE	202	81.087	251.827	95.400	1.00	74.54	6
ATOM	1247	C	ILE	202	80.092	254.286	97.965	1.00	65.15	6
ATOM	1248	O	ILE	202	80.070	255.390	98.498	1.00	66.53	8
ATOM	1249	N	LEU	203	80.666	253.230	98.545	1.00	61.06	7
ATOM	1250	CA	LEU	203	81.339	253.381	99.829	1.00	56.16	6
ATOM	1251	CB	LEU	203	81.108	252.186	100.772	1.00	58.37	6
ATOM	1252	CG	LEU	203	81.307	250.698	100.456	1.00	56.67	6
ATOM	1253	CD1	LEU	203	82.537	250.450	99.606	1.00	61.89	6
ATOM	1254	CD2	LEU	203	81.390	249.932	101.774	1.00	49.61	6
ATOM	1255	C	LEU	203	82.807	253.716	99.767	1.00	51.96	6
ATOM	1256	O	LEU	203	83.535	253.263	98.882	1.00	49.35	8
ATOM	1257	N	LYS	204	83.234	254.509	100.740	1.00	45.12	7
ATOM	1258	CA	LYS	204	84.611	254.922	100.819	1.00	43.06	6
ATOM	1259	CB	LYS	204	84.790	256.344	100.284	1.00	42.02	6
ATOM	1260	CG	LYS	204	83.511	257.097	99.994	1.00	45.94	6
ATOM	1261	CD	LYS	204	83.421	257.543	98.535	1.00	44.24	6
ATOM	1262	CE	LYS	204	84.528	258.498	98.155	1.00	41.72	6
ATOM	1263	NZ	LYS	204	84.277	259.032	96.814	1.00	39.77	7
ATOM	1264	C	LYS	204	85.142	254.815	102.228	1.00	42.06	6
ATOM	1265	O	LYS	204	84.409	254.988	103.200	1.00	40.61	8
ATOM	1266	N	LEU	205	86.422	254.472	102.313	1.00	38.25	7
ATOM	1267	CA	LEU	205	87.121	254.317	103.569	1.00	40.08	6
ATOM	1268	CB	LEU	205	88.347	253.440	103.345	1.00	42.57	6
ATOM	1269	CG	LEU	205	89.348	253.319	104.490	1.00	39.94	6
ATOM	1270	CD1	LEU	205	88.971	252.120	105.338	1.00	38.09	6
ATOM	1271	CD2	LEU	205	90.755	253.190	103.915	1.00	39.78	6
ATOM	1272	C	LEU	205	87.562	255.681	104.064	1.00	40.59	6
ATOM	1273	O	LEU	205	88.048	256.502	103.281	1.00	44.38	8
ATOM	1274	N	THR	206	87.438	255.905	105.370	1.00	39.00	7
ATOM	1275	CA	THR	206	87.830	257.180	105.959	1.00	38.13	6
ATOM	1276	CB	THR	206	86.589	257.967	106.448	1.00	35.42	6
ATOM	1277	OG1	THR	206	86.148	257.423	107.695	1.00	42.69	8
ATOM	1278	CG2	THR	206	85.452	257.867	105.465	1.00	37.41	6
ATOM	1279	C	THR	206	88.750	257.006	107.170	1.00	37.92	6
ATOM	1280	O	THR	206	89.062	255.897	107.572	1.00	45.69	8
ATOM	1281	N	ASP	207	89.181	258.130	107.725	1.00	36.48	7
ATOM	1282	CA	ASP	207	90.046	258.193	108.891	1.00	35.51	6
ATOM	1283	CB	ASP	207	89.394	257.479	110.065	1.00	38.57	6
ATOM	1284	CG	ASP	207	89.933	257.955	111.402	1.00	47.47	6
ATOM	1285	OD1	ASP	207	90.957	258.676	111.442	1.00	46.47	8
ATOM	1286	OD2	ASP	207	89.322	257.619	112.424	1.00	43.26	8
ATOM	1287	C	ASP	207	91.508	257.800	108.799	1.00	36.22	6
ATOM	1288	O	ASP	207	91.910	256.715	109.203	1.00	43.91	8
ATOM	1289	N	PHE	208	92.326	258.761	108.420	1.00	33.81	7
ATOM	1290	CA	PHE	208	93.747	258.525	108.294	1.00	29.95	6
ATOM	1291	CB	PHE	208	94.287	259.273	107.066	1.00	28.44	6
ATOM	1292	CG	PHE	208	93.917	258.626	105.768	1.00	28.85	6
ATOM	1293	CD1	PHE	208	92.582	258.410	105.434	1.00	27.89	6
ATOM	1294	CD2	PHE	208	94.904	258.169	104.909	1.00	33.81	6
ATOM	1295	CE1	PHE	208	92.239	257.745	104.260	1.00	38.94	6
ATOM	1296	CE2	PHE	208	94.575	257.496	103.721	1.00	38.70	6
ATOM	1297	CZ	PHE	208	93.243	257.281	103.397	1.00	41.48	6
ATOM	1298	C	PHE	208	94.444	258.926	109.586	1.00	29.60	6
ATOM	1299	O	PHE	208	95.592	259.408	109.588	1.00	30.80	8
ATOM	1300	N	GLY	209	93.753	258.666	110.691	1.00	29.35	7
ATOM	1301	CA	GLY	209	94.285	259.017	111.991	1.00	35.84	6
ATOM	1302	C	GLY	209	95.396	258.094	112.433	1.00	40.83	6
ATOM	1303	O	GLY	209	96.220	258.457	113.258	1.00	39.24	8
ATOM	1304	N	PHE	210	95.420	256.886	111.893	1.00	44.71	7
ATOM	1305	CA	PHE	210	96.457	255.954	112.268	1.00	49.18	6
ATOM	1306	CB	PHE	210	95.828	254.681	112.816	1.00	56.40	6
ATOM	1307	CG	PHE	210	95.223	254.854	114.177	1.00	60.12	6
ATOM	1308	CD1	PHE	210	95.637	255.893	115.005	1.00	61.16	6
ATOM	1309	CD2	PHE	210	94.230	254.003	114.622	1.00	55.90	6
ATOM	1310	CE1	PHE	210	95.064	256.079	116.247	1.00	60.53	6
ATOM	1311	CE2	PHE	210	93.660	254.187	115.857	1.00	58.70	6
ATOM	1312	CZ	PHE	210	94.077	255.226	116.670	1.00	58.39	6
ATOM	1313	C	PHE	210	97.422	255.642	111.138	1.00	50.47	6
ATOM	1314	O	PHE	210	98.411	254.951	111.349	1.00	50.23	8
ATOM	1315	N	ALA	211	97.140	256.194	109.958	1.00	51.05	7
ATOM	1316	CA	ALA	211	97.946	256.009	108.751	1.00	48.01	6
ATOM	1317	CB	ALA	211	97.361	256.800	107.609	1.00	47.95	6
ATOM	1318	C	ALA	211	99.385	256.403	108.918	1.00	50.58	6
ATOM	1319	O	ALA	211	99.687	257.390	109.586	1.00	50.34	8
ATOM	1320	N	LYS	212	100.265	255.627	108.291	1.00	53.63	7
ATOM	1321	CA	LYS	212	101.696	255.883	108.351	1.00	56.44	6
ATOM	1322	CB	LYS	212	102.353	255.148	109.539	1.00	63.40	6
ATOM	1323	CG	LYS	212	103.008	253.788	109.258	1.00	76.41	6
ATOM	1324	CD	LYS	212	104.079	253.462	110.333	1.00	82.06	6
ATOM	1325	CE	LYS	212	105.002	252.277	109.953	1.00	89.38	6
ATOM	1326	NZ	LYS	212	104.397	250.897	110.073	1.00	87.51	7
ATOM	1327	C	LYS	212	102.329	255.514	107.014	1.00	55.76	6
ATOM	1328	O	LYS	212	101.830	254.641	106.307	1.00	50.44	8
ATOM	1329	N	GLU	213	103.371	256.255	106.644	1.00	58.32	7
ATOM	1330	CA	GLU	213	104.100	256.047	105.398	1.00	67.18	6
ATOM	1331	CB	GLU	213	104.936	257.283	105.040	1.00	71.89	6
ATOM	1332	CG	GLU	213	104.204	258.611	105.074	1.00	86.72	6
ATOM	1333	CD	GLU	213	104.291	259.336	106.422	1.00	95.76	6
ATOM	1334	OE1	GLU	213	104.964	260.393	106.477	1.00	97.93	8
ATOM	1335	OE2	GLU	213	103.668	258.879	107.415	1.00	98.12	8
ATOM	1336	C	GLU	213	105.055	254.878	105.573	1.00	71.80	6
ATOM	1337	O	GLU	213	106.019	254.980	106.331	1.00	73.99	8
ATOM	1338	N	THR	214	104.798	253.781	104.867	1.00	75.36	7
ATOM	1339	CA	THR	214	105.640	252.593	104.948	1.00	77.86	6
ATOM	1340	CB	THR	214	104.870	251.329	104.538	1.00	76.30	6
ATOM	1341	OG1	THR	214	104.327	251.499	103.226	1.00	75.42	8
ATOM	1342	CG2	THR	214	103.743	251.070	105.498	1.00	79.20	6
ATOM	1343	C	THR	214	106.885	252.739	104.080	1.00	82.25	6
ATOM	1344	O	THR	214	107.031	252.089	103.042	1.00	83.65	8
ATOM	1345	N	THR	215	107.787	253.609	104.516	1.00	85.50	7
ATOM	1346	CA	THR	215	109.018	253.846	103.790	1.00	87.69	6
ATOM	1347	CB	THR	215	108.849	254.980	102.781	1.00	83.73	6
ATOM	1348	OG1	THR	215	110.033	255.083	101.989	1.00	86.26	8
ATOM	1349	CG2	THR	215	108.592	256.295	103.485	1.00	80.18	6
ATOM	1350	C	THR	215	110.163	254.165	104.747	1.00	92.77	6
ATOM	1351	O	THR	215	109.901	254.745	105.823	1.00	94.28	8
ATOM	1352	OT	THR	215	111.313	253.796	104.421	1.00	100.00	8
ATOM	1353	CB	PRO	227	89.937	244.648	120.244	1.00	83.11	6
ATOM	1354	CG	PRO	227	89.564	243.764	121.414	1.00	84.17	6
ATOM	1355	C	PRO	227	88.626	243.453	118.471	1.00	89.53	6
ATOM	1356	O	PRO	227	89.667	242.869	118.169	1.00	93.85	8
ATOM	1357	N	PRO	227	87.543	244.487	120.434	1.00	84.11	7
ATOM	1358	CD	PRO	227	88.101	244.125	121.750	1.00	81.36	6
ATOM	1359	CA	PRO	227	88.640	244.631	119.447	1.00	86.67	6
ATOM	1360	N	TYR	228	87.439	243.123	117.973	1.00	88.50	7
ATOM	1361	CA	TYR	228	87.257	242.020	117.034	1.00	87.60	6
ATOM	1362	CB	TYR	228	85.784	241.966	116.618	1.00	90.26	6
ATOM	1363	CG	TYR	228	84.819	241.893	117.784	1.00	98.08	6
ATOM	1364	CD1	TYR	228	85.216	241.341	119.010	1.00	100.00	6
ATOM	1365	CE1	TYR	228	84.322	241.211	120.085	1.00	100.00	6
ATOM	1366	CD2	TYR	228	83.497	242.322	117.659	1.00	99.01	6
ATOM	1367	CE2	TYR	228	82.586	242.191	118.732	1.00	100.00	6
ATOM	1368	CZ	TYR	228	83.011	241.630	119.943	1.00	100.00	6
ATOM	1369	OH	TYR	228	82.137	241.463	121.002	1.00	98.67	8
ATOM	1370	C	TYR	228	88.123	242.178	115.790	1.00	88.14	6
ATOM	1371	O	TYR	228	88.837	241.264	115.385	1.00	88.87	8
ATOM	1372	N	TYR	229	88.102	243.401	115.270	1.00	89.24	7
ATOM	1373	CA	TYR	229	88.814	243.854	114.077	1.00	85.42	6
ATOM	1374	CB	TYR	229	88.275	245.240	113.703	1.00	87.28	6
ATOM	1375	CG	TYR	229	86.817	245.341	114.070	1.00	94.81	6
ATOM	1376	CD1	TYR	229	85.864	244.543	113.423	1.00	96.81	6
ATOM	1377	CE1	TYR	229	84.555	244.425	113.909	1.00	95.27	6
ATOM	1378	CD2	TYR	229	86.413	246.048	115.204	1.00	97.64	6
ATOM	1379	CE2	TYR	229	85.100	245.934	115.696	1.00	99.46	6
ATOM	1380	CZ	TYR	229	84.186	245.114	115.046	1.00	95.00	6
ATOM	1381	OH	TYR	229	82.930	244.936	115.568	1.00	92.96	8
ATOM	1382	C	TYR	229	90.329	243.873	114.142	1.00	84.18	6
ATOM	1383	O	TYR	229	90.979	243.629	113.132	1.00	87.46	8
ATOM	1384	N	VAL	230	90.892	244.152	115.316	1.00	79.67	7
ATOM	1385	CA	VAL	230	92.345	244.199	115.483	1.00	74.92	6
ATOM	1386	CB	VAL	230	92.727	244.637	116.919	1.00	71.07	6
ATOM	1387	CG1	VAL	230	94.220	244.579	117.120	1.00	73.09	6
ATOM	1388	CG2	VAL	230	92.255	246.047	117.169	1.00	67.91	6
ATOM	1389	C	VAL	230	93.039	242.881	115.116	1.00	76.44	6
ATOM	1390	O	VAL	230	92.495	241.801	115.334	1.00	77.17	8
ATOM	1391	N	ALA	231	94.206	242.990	114.483	1.00	77.28	7
ATOM	1392	CA	ALA	231	94.989	241.830	114.069	1.00	76.81	6
ATOM	1393	CB	ALA	231	95.826	242.176	112.869	1.00	76.00	6
ATOM	1394	C	ALA	231	95.888	241.369	115.211	1.00	81.07	6
ATOM	1395	O	ALA	231	96.348	242.182	116.015	1.00	82.90	8
ATOM	1396	N	PRO	232	96.173	240.058	115.282	1.00	82.37	7
ATOM	1397	CD	PRO	232	95.707	239.014	114.359	1.00	81.62	6
ATOM	1398	CA	PRO	232	97.021	239.471	116.326	1.00	82.35	6
ATOM	1399	CB	PRO	232	97.041	237.986	115.958	1.00	81.66	6
ATOM	1400	CG	PRO	232	96.789	237.991	114.494	1.00	83.50	6
ATOM	1401	C	PRO	232	98.431	240.057	116.470	1.00	82.38	6
ATOM	1402	O	PRO	232	98.884	240.291	117.592	1.00	82.76	8
ATOM	1403	N	GLU	233	99.125	240.303	115.360	1.00	80.47	7
ATOM	1404	CA	GLU	233	100.471	240.863	115.455	1.00	82.16	6
ATOM	1405	CB	GLU	233	101.102	241.075	114.073	1.00	77.29	6
ATOM	1406	CG	GLU	233	100.446	242.129	113.197	1.00	68.78	6
ATOM	1407	CD	GLU	233	99.520	241.540	112.147	1.00	68.98	6
ATOM	1408	OE1	GLU	233	99.340	242.181	111.089	1.00	68.64	8
ATOM	1409	OE2	GLU	233	98.970	240.443	112.372	1.00	61.80	8
ATOM	1410	C	GLU	233	100.438	242.182	116.221	1.00	88.51	6
ATOM	1411	O	GLU	233	101.390	242.520	116.930	1.00	91.95	8
ATOM	1412	N	VAL	234	99.302	242.878	116.121	1.00	92.16	7
ATOM	1413	CA	VAL	234	99.079	244.167	116.781	1.00	92.42	6
ATOM	1414	CB	VAL	234	98.095	245.040	115.963	1.00	90.31	6
ATOM	1415	CG1	VAL	234	98.124	246.490	116.444	1.00	88.48	6
ATOM	1416	CG2	VAL	234	98.433	244.958	114.483	1.00	85.57	6
ATOM	1417	C	VAL	234	98.570	244.003	118.225	1.00	95.05	6
ATOM	1418	O	VAL	234	98.058	244.948	118.834	1.00	93.29	8
ATOM	1419	N	LEU	235	98.727	242.797	118.766	1.00	97.73	7
ATOM	1420	CA	LEU	235	98.300	242.495	120.129	1.00	99.51	6
ATOM	1421	CB	LEU	235	97.271	241.351	120.155	1.00	98.60	6
ATOM	1422	CG	LEU	235	95.825	241.652	119.732	1.00	95.25	6
ATOM	1423	CD1	LEU	235	95.007	240.377	119.769	1.00	94.91	6
ATOM	1424	CD2	LEU	235	95.203	242.686	120.645	1.00	91.60	6
ATOM	1425	C	LEU	235	99.489	242.171	121.040	1.00	100.00	6
ATOM	1426	O	LEU	235	99.302	241.684	122.159	1.00	100.00	8
ATOM	1427	N	GLY	236	100.708	242.413	120.554	1.00	99.29	7
ATOM	1428	CA	GLY	236	101.880	242.161	121.380	1.00	100.00	6
ATOM	1429	C	GLY	236	103.014	241.279	120.870	1.00	100.00	6
ATOM	1430	O	GLY	236	104.180	241.605	121.111	1.00	98.58	8
ATOM	1431	N	PRO	237	102.724	240.153	120.187	1.00	100.00	7
ATOM	1432	CD	PRO	237	101.389	239.630	119.835	1.00	100.00	6
ATOM	1433	CA	PRO	237	103.777	239.263	119.676	1.00	100.00	6
ATOM	1434	CB	PRO	237	102.999	238.332	118.745	1.00	100.00	6
ATOM	1435	CG	PRO	237	101.688	238.196	119.468	1.00	99.91	6
ATOM	1436	C	PRO	237	104.944	239.977	118.968	1.00	100.00	6
ATOM	1437	O	PRO	237	105.808	240.568	119.632	1.00	97.78	8
ATOM	1438	N	GLU	238	104.959	239.933	117.634	1.00	100.00	7
ATOM	1439	CA	GLU	238	106.018	240.576	116.853	1.00	100.00	6
ATOM	1440	CB	GLU	238	105.996	240.099	115.391	1.00	100.00	6
ATOM	1441	CG	GLU	238	105.447	238.690	115.165	1.00	100.00	6
ATOM	1442	CD	GLU	238	104.071	238.694	114.502	1.00	100.00	6
ATOM	1443	OE1	GLU	238	103.963	239.203	113.359	1.00	100.00	8
ATOM	1444	OE2	GLU	238	103.103	238.190	115.122	1.00	100.00	8
ATOM	1445	C	GLU	238	105.858	242.099	116.902	1.00	100.00	6
ATOM	1446	O	GLU	238	106.282	242.738	117.865	1.00	100.00	8
ATOM	1447	N	LYS	239	105.201	242.659	115.886	1.00	99.84	7
ATOM	1448	CA	LYS	239	104.971	244.098	115.790	1.00	100.00	6
ATOM	1449	CB	LYS	239	106.252	244.795	115.323	1.00	100.00	6
ATOM	1450	CG	LYS	239	106.650	246.005	116.158	1.00	100.00	6
ATOM	1451	CD	LYS	239	107.284	245.587	117.478	1.00	100.00	6
ATOM	1452	CE	LYS	239	108.548	244.762	117.253	1.00	100.00	6
ATOM	1453	NZ	LYS	239	109.077	244.229	118.539	1.00	100.00	7
ATOM	1454	C	LYS	239	103.845	244.365	114.783	1.00	100.00	6
ATOM	1455	O	LYS	239	102.912	243.567	114.665	1.00	100.00	8
ATOM	1456	N	TYR	240	103.907	245.513	114.103	1.00	100.00	7
ATOM	1457	CA	TYR	240	102.906	245.908	113.100	1.00	100.00	6
ATOM	1458	CB	TYR	240	101.645	246.516	113.752	1.00	100.00	6
ATOM	1459	CG	TYR	240	101.786	246.991	115.194	1.00	100.00	6
ATOM	1460	CD1	TYR	240	101.896	248.351	115.496	1.00	100.00	6
ATOM	1461	CE1	TYR	240	101.963	248.794	116.815	1.00	98.88	6
ATOM	1462	CD2	TYR	240	101.752	246.082	116.260	1.00	100.00	6
ATOM	1463	CE2	TYR	240	101.821	246.513	117.579	1.00	99.97	6
ATOM	1464	CZ	TYR	240	101.925	247.869	117.850	1.00	100.00	6
ATOM	1465	OH	TYR	240	101.996	248.302	119.156	1.00	100.00	8
ATOM	1466	C	TYR	240	103.520	246.883	112.081	1.00	100.00	6
ATOM	1467	O	TYR	240	104.577	247.474	112.353	1.00	100.00	8
ATOM	1468	N	ASP	241	102.895	247.020	110.902	1.00	100.00	7
ATOM	1469	CA	ASP	241	103.410	247.930	109.860	1.00	96.18	6
ATOM	1470	CB	ASP	241	104.752	247.422	109.269	1.00	100.00	6
ATOM	1471	CG	ASP	241	104.802	245.893	109.083	1.00	100.00	6
ATOM	1472	OD1	ASP	241	103.789	245.282	108.675	1.00	100.00	8
ATOM	1473	OD2	ASP	241	105.876	245.305	109.344	1.00	98.96	8
ATOM	1474	C	ASP	241	102.489	248.363	108.717	1.00	89.13	6
ATOM	1475	O	ASP	241	102.251	249.550	108.548	1.00	86.16	8
ATOM	1476	N	LYS	242	102.004	247.408	107.926	1.00	84.52	7
ATOM	1477	CA	LYS	242	101.120	247.690	106.789	1.00	81.66	6
ATOM	1478	CB	LYS	242	101.941	248.159	105.576	1.00	90.30	6
ATOM	1479	CG	LYS	242	102.807	247.066	104.915	1.00	99.46	6
ATOM	1480	CD	LYS	242	103.963	246.576	105.823	1.00	100.00	6
ATOM	1481	CE	LYS	242	104.456	245.158	105.462	1.00	100.00	6
ATOM	1482	NZ	LYS	242	105.261	245.082	104.200	1.00	99.42	7
ATOM	1483	C	LYS	242	100.359	246.444	106.371	1.00	75.64	6
ATOM	1484	O	LYS	242	99.879	246.341	105.242	1.00	66.08	8
ATOM	1485	N	SER	243	100.344	245.465	107.264	1.00	76.83	7
ATOM	1486	CA	SER	243	99.664	244.202	107.029	1.00	73.99	6
ATOM	1487	CB	SER	243	100.586	243.052	107.435	1.00	71.49	6
ATOM	1488	OG	SER	243	99.870	241.835	107.473	1.00	73.89	8
ATOM	1489	C	SER	243	98.340	244.130	107.801	1.00	72.34	6
ATOM	1490	O	SER	243	97.505	243.254	107.539	1.00	70.04	8
ATOM	1491	N	CYS	244	98.163	245.056	108.749	1.00	67.68	7
ATOM	1492	CA	CYS	244	96.958	245.120	109.566	1.00	61.25	6
ATOM	1493	CB	CYS	244	96.976	246.348	110.462	1.00	56.73	6
ATOM	1494	SG	CYS	244	98.539	246.728	111.218	1.00	73.70	16
ATOM	1495	C	CYS	244	95.768	245.253	108.645	1.00	60.20	6
ATOM	1496	O	CYS	244	94.699	244.708	108.917	1.00	64.77	8
ATOM	1497	N	ASP	245	95.966	245.991	107.556	1.00	54.68	7
ATOM	1498	CA	ASP	245	94.928	246.229	106.565	1.00	48.62	6
ATOM	1499	CB	ASP	245	95.462	247.137	105.449	1.00	45.94	6
ATOM	1500	CG	ASP	245	95.797	248.541	105.950	1.00	46.85	6
ATOM	1501	OD1	ASP	245	95.365	248.885	107.074	1.00	54.27	8
ATOM	1502	OD2	ASP	245	96.489	249.299	105.240	1.00	35.11	8
ATOM	1503	C	ASP	245	94.336	244.950	106.005	1.00	48.94	6
ATOM	1504	O	ASP	245	93.111	244.806	105.961	1.00	46.25	8
ATOM	1505	N	MET	246	95.201	243.994	105.666	1.00	50.39	7
ATOM	1506	CA	MET	246	94.755	242.718	105.115	1.00	51.29	6
ATOM	1507	CB	MET	246	95.926	241.912	104.572	1.00	47.87	6
ATOM	1508	CG	MET	246	96.678	242.633	103.479	1.00	52.16	6
ATOM	1509	SD	MET	246	95.621	243.393	102.238	1.00	49.79	16
ATOM	1510	CE	MET	246	94.887	241.958	101.484	1.00	52.46	6
ATOM	1511	C	MET	246	93.945	241.891	106.099	1.00	53.01	6
ATOM	1512	O	MET	246	93.013	241.191	105.694	1.00	53.41	8
ATOM	1513	N	TRP	247	94.305	241.950	107.381	1.00	54.63	7
ATOM	1514	CA	TRP	247	93.574	241.198	108.396	1.00	55.52	6
ATOM	1515	CB	TRP	247	94.240	241.318	109.774	1.00	56.45	6
ATOM	1516	CG	TRP	247	93.399	240.736	110.914	1.00	65.11	6
ATOM	1517	CD2	TRP	247	93.396	239.377	111.381	1.00	68.69	6
ATOM	1518	CE2	TRP	247	92.471	239.302	112.449	1.00	67.69	6
ATOM	1519	CE3	TRP	247	94.090	238.216	111.006	1.00	67.51	6
ATOM	1520	CD1	TRP	247	92.498	241.405	111.701	1.00	66.10	6
ATOM	1521	NE1	TRP	247	91.941	240.553	112.623	1.00	64.36	7
ATOM	1522	CZ2	TRP	247	92.223	238.110	113.144	1.00	66.74	6
ATOM	1523	CZ3	TRP	247	93.843	237.034	111.701	1.00	64.67	6
ATOM	1524	CH2	TRP	247	92.916	236.992	112.756	1.00	64.64	6
ATOM	1525	C	TRP	247	92.186	241.821	108.447	1.00	55.47	6
ATOM	1526	O	TRP	247	91.175	241.138	108.300	1.00	52.14	8
ATOM	1527	N	SER	248	92.165	243.142	108.578	1.00	59.79	7
ATOM	1528	CA	SER	248	90.926	243.893	108.647	1.00	63.08	6
ATOM	1529	CB	SER	248	91.217	245.390	108.646	1.00	65.65	6
ATOM	1530	OG	SER	248	91.911	245.763	109.829	1.00	70.45	8
ATOM	1531	C	SER	248	89.960	243.515	107.538	1.00	64.15	6
ATOM	1532	O	SER	248	88.764	243.336	107.789	1.00	63.30	8
ATOM	1533	N	LEU	249	90.486	243.343	106.326	1.00	65.08	7
ATOM	1534	CA	LEU	249	89.650	242.972	105.190	1.00	66.77	6
ATOM	1535	CB	LEU	249	90.477	242.853	103.909	1.00	67.67	6
ATOM	1536	CG	LEU	249	90.932	244.142	103.226	1.00	67.64	6
ATOM	1537	CD1	LEU	249	91.941	243.850	102.104	1.00	62.51	6
ATOM	1538	CD2	LEU	249	89.704	244.858	102.699	1.00	65.06	6
ATOM	1539	C	LEU	249	89.003	241.634	105.490	1.00	67.59	6
ATOM	1540	O	LEU	249	87.794	241.488	105.335	1.00	69.42	8
ATOM	1541	N	GLY	250	89.815	240.687	105.969	1.00	66.68	7
ATOM	1542	CA	GLY	250	89.341	239.346	106.299	1.00	64.64	6
ATOM	1543	C	GLY	250	88.247	239.308	107.353	1.00	62.65	6
ATOM	1544	O	GLY	250	87.255	238.589	107.211	1.00	62.59	8
ATOM	1545	N	VAL	251	88.446	240.069	108.425	1.00	58.91	7
ATOM	1546	CA	VAL	251	87.471	240.163	109.498	1.00	54.13	6
ATOM	1547	CB	VAL	251	87.979	241.105	110.567	1.00	44.55	6
ATOM	1548	CG1	VAL	251	86.941	241.308	111.631	1.00	43.98	6
ATOM	1549	CG2	VAL	251	89.252	240.578	111.133	1.00	40.69	6
ATOM	1550	C	VAL	251	86.176	240.744	108.928	1.00	59.21	6
ATOM	1551	O	VAL	251	85.081	240.252	109.200	1.00	61.29	8
ATOM	1552	N	ILE	252	86.327	241.776	108.104	1.00	60.74	7
ATOM	1553	CA	ILE	252	85.201	242.450	107.474	1.00	60.79	6
ATOM	1554	CB	ILE	252	85.667	243.794	106.824	1.00	58.77	6
ATOM	1555	CG2	ILE	252	84.658	244.304	105.790	1.00	55.58	6
ATOM	1556	CG1	ILE	252	85.879	244.835	107.925	1.00	52.79	6
ATOM	1557	CD1	ILE	252	86.468	246.110	107.438	1.00	59.93	6
ATOM	1558	C	ILE	252	84.460	241.555	106.479	1.00	60.31	6
ATOM	1559	O	ILE	252	83.232	241.599	106.404	1.00	56.21	8
ATOM	1560	N	MET	253	85.203	240.714	105.762	1.00	61.63	7
ATOM	1561	CA	MET	253	84.610	239.810	104.783	1.00	65.41	6
ATOM	1562	CB	MET	253	85.695	239.152	103.920	1.00	63.78	6
ATOM	1563	CG	MET	253	85.148	238.512	102.652	1.00	65.10	6
ATOM	1564	SD	MET	253	86.307	237.496	101.749	1.00	70.31	16
ATOM	1565	CE	MET	253	87.046	238.636	100.685	1.00	64.35	6
ATOM	1566	C	MET	253	83.766	238.735	105.495	1.00	71.22	6
ATOM	1567	O	MET	253	82.744	238.287	104.962	1.00	74.37	8
ATOM	1568	N	TYR	254	84.189	238.322	106.694	1.00	69.39	7
ATOM	1569	CA	TYR	254	83.454	237.310	107.453	1.00	65.81	6
ATOM	1570	CB	TYR	254	84.239	236.895	108.699	1.00	65.59	6
ATOM	1571	CG	TYR	254	83.631	235.726	109.453	1.00	67.43	6
ATOM	1572	CD1	TYR	254	82.676	235.933	110.442	1.00	67.39	6
ATOM	1573	CE1	TYR	254	82.097	234.867	111.127	1.00	69.25	6
ATOM	1574	CD2	TYR	254	84.002	234.410	109.166	1.00	67.21	6
ATOM	1575	CE2	TYR	254	83.429	233.334	109.845	1.00	67.52	6
ATOM	1576	CZ	TYR	254	82.472	233.568	110.827	1.00	70.44	6
ATOM	1577	OH	TYR	254	81.872	232.515	111.497	1.00	64.64	8
ATOM	1578	C	TYR	254	82.088	237.884	107.862	1.00	66.99	6
ATOM	1579	O	TYR	254	81.046	237.300	107.563	1.00	68.68	8
ATOM	1580	N	ILE	255	82.105	239.057	108.497	1.00	65.08	7
ATOM	1581	CA	ILE	255	80.887	239.727	108.946	1.00	57.40	6
ATOM	1582	CB	ILE	255	81.188	241.111	109.593	1.00	53.71	6
ATOM	1583	CG2	ILE	255	79.903	241.789	110.057	1.00	43.44	6
ATOM	1584	CG1	ILE	255	82.125	240.948	110.791	1.00	49.82	6
ATOM	1585	CD1	ILE	255	82.466	242.259	111.489	1.00	47.02	6
ATOM	1586	C	ILE	255	79.912	239.912	107.793	1.00	59.61	6
ATOM	1587	O	ILE	255	78.710	239.947	108.003	1.00	63.64	8
ATOM	1588	N	LEU	256	80.413	240.008	106.572	1.00	61.50	7
ATOM	1589	CA	LEU	256	79.506	240.184	105.450	1.00	71.57	6
ATOM	1590	CB	LEU	256	80.230	240.729	104.218	1.00	72.29	6
ATOM	1591	CG	LEU	256	80.267	242.243	104.010	1.00	70.71	6
ATOM	1592	CD1	LEU	256	80.689	242.533	102.563	1.00	69.15	6
ATOM	1593	CD2	LEU	256	78.910	242.844	104.308	1.00	61.55	6
ATOM	1594	C	LEU	256	78.741	238.924	105.061	1.00	76.51	6
ATOM	1595	O	LEU	256	77.509	238.948	104.965	1.00	81.67	8
ATOM	1596	N	LEU	257	79.468	237.829	104.857	1.00	76.11	7
ATOM	1597	CA	LEU	257	78.866	236.558	104.469	1.00	75.77	6
ATOM	1598	CB	LEU	257	79.948	235.588	103.999	1.00	74.28	6
ATOM	1599	CG	LEU	257	80.569	235.770	102.612	1.00	76.18	6
ATOM	1600	CD1	LEU	257	79.530	235.506	101.539	1.00	80.60	6
ATOM	1601	CD2	LEU	257	81.157	237.150	102.452	1.00	77.69	6
ATOM	1602	C	LEU	257	77.979	235.866	105.498	1.00	79.47	6
ATOM	1603	O	LEU	257	77.199	234.991	105.132	1.00	82.30	8
ATOM	1604	N	CYS	258	78.073	236.257	106.768	1.00	81.87	7
ATOM	1605	CA	CYS	258	77.254	235.634	107.808	1.00	84.11	6
ATOM	1606	CB	CYS	258	78.116	234.728	108.680	1.00	81.73	6
ATOM	1607	SG	CYS	258	79.297	235.619	109.695	1.00	78.97	16
ATOM	1608	C	CYS	258	76.486	236.612	108.699	1.00	87.63	6
ATOM	1609	O	CYS	258	75.325	236.364	109.026	1.00	93.56	8
ATOM	1610	N	GLY	259	77.148	237.681	109.144	1.00	88.18	7
ATOM	1611	CA	GLY	259	76.487	238.669	109.985	1.00	85.25	6
ATOM	1612	C	GLY	259	77.014	238.800	111.402	1.00	84.92	6
ATOM	1613	O	GLY	259	76.386	239.446	112.239	1.00	84.46	8
ATOM	1614	N	TYR	260	78.166	238.196	111.674	1.00	87.33	7
ATOM	1615	CA	TYR	260	78.784	238.244	113.003	1.00	90.48	6
ATOM	1616	CB	TYR	260	78.187	237.163	113.910	1.00	92.90	6
ATOM	1617	CG	TYR	260	78.151	235.784	113.283	1.00	94.92	6
ATOM	1618	CD1	TYR	260	77.125	235.429	112.409	1.00	93.88	6
ATOM	1619	CE1	TYR	260	77.082	234.181	111.826	1.00	94.27	6
ATOM	1620	CD2	TYR	260	79.143	234.839	113.558	1.00	93.73	6
ATOM	1621	CE2	TYR	260	79.109	233.584	112.976	1.00	93.88	6
ATOM	1622	CZ	TYR	260	78.072	233.264	112.111	1.00	95.62	6
ATOM	1623	OH	TYR	260	78.011	232.024	111.526	1.00	100.00	8
ATOM	1624	C	TYR	260	80.292	238.046	112.890	1.00	91.76	6
ATOM	1625	O	TYR	260	80.762	237.263	112.074	1.00	94.22	8
ATOM	1626	N	PRO	261	81.068	238.729	113.736	1.00	92.32	7
ATOM	1627	CD	PRO	261	80.602	239.652	114.780	1.00	94.11	6
ATOM	1628	CA	PRO	261	82.534	238.636	113.733	1.00	95.28	6
ATOM	1629	CB	PRO	261	82.930	239.496	114.934	1.00	95.01	6
ATOM	1630	CG	PRO	261	81.826	240.495	115.014	1.00	97.25	6
ATOM	1631	C	PRO	261	83.059	237.214	113.903	1.00	96.16	6
ATOM	1632	O	PRO	261	82.473	236.424	114.638	1.00	98.72	8
ATOM	1633	N	PRO	262	84.160	236.865	113.205	1.00	95.84	7
ATOM	1634	CD	PRO	262	84.965	237.679	112.278	1.00	97.74	6
ATOM	1635	CA	PRO	262	84.724	235.520	113.330	1.00	94.34	6
ATOM	1636	CB	PRO	262	85.857	235.526	112.298	1.00	93.04	6
ATOM	1637	CG	PRO	262	86.285	236.942	112.266	1.00	93.98	6
ATOM	1638	C	PRO	262	85.228	235.341	114.763	1.00	94.02	6
ATOM	1639	O	PRO	262	85.263	234.231	115.283	1.00	98.20	8
ATOM	1640	N	PHE	263	85.600	236.452	115.391	1.00	90.37	7
ATOM	1641	CA	PHE	263	86.091	236.463	116.760	1.00	90.96	6
ATOM	1642	CB	PHE	263	87.547	236.919	116.828	1.00	87.79	6
ATOM	1643	CG	PHE	263	88.481	236.099	115.984	1.00	88.65	6
ATOM	1644	CD1	PHE	263	89.037	234.925	116.479	1.00	87.25	6
ATOM	1645	CD2	PHE	263	88.798	236.494	114.683	1.00	88.06	6
ATOM	1646	CE1	PHE	263	89.893	234.156	115.690	1.00	85.42	6
ATOM	1647	CE2	PHE	263	89.653	235.731	113.890	1.00	84.34	6
ATOM	1648	CZ	PHE	263	90.199	234.561	114.396	1.00	83.14	6
ATOM	1649	C	PHE	263	85.207	237.514	117.395	1.00	95.73	6
ATOM	1650	O	PHE	263	84.999	238.574	116.800	1.00	98.83	8
ATOM	1651	N	TYR	264	84.662	237.214	118.573	1.00	99.85	7
ATOM	1652	CA	TYR	264	83.781	238.149	119.288	1.00	100.00	6
ATOM	1653	CB	TYR	264	82.338	238.028	118.771	1.00	98.26	6
ATOM	1654	CG	TYR	264	81.836	236.608	118.589	1.00	96.85	6
ATOM	1655	CD1	TYR	264	82.506	235.521	119.159	1.00	93.27	6
ATOM	1656	CE1	TYR	264	82.067	234.224	118.967	1.00	95.74	6
ATOM	1657	CD2	TYR	264	80.702	236.353	117.820	1.00	96.01	6
ATOM	1658	CE2	TYR	264	80.251	235.059	117.620	1.00	99.17	6
ATOM	1659	CZ	TYR	264	80.938	233.997	118.194	1.00	100.00	6
ATOM	1660	OH	TYR	264	80.503	232.708	117.977	1.00	100.00	8
ATOM	1661	C	TYR	264	83.838	238.034	120.821	1.00	100.00	6
ATOM	1662	O	TYR	264	84.925	238.168	121.404	1.00	100.00	8
ATOM	1663	N	SER	265	82.674	237.846	121.460	1.00	100.00	7
ATOM	1664	CA	SER	265	82.544	237.713	122.922	1.00	100.00	6
ATOM	1665	CB	SER	265	83.525	236.653	123.461	1.00	100.00	6
ATOM	1666	OG	SER	265	83.478	236.552	124.877	1.00	100.00	8
ATOM	1667	C	SER	265	82.675	239.017	123.728	1.00	100.00	6
ATOM	1668	O	SER	265	83.354	239.963	123.310	1.00	100.00	8
ATOM	1669	N	ASN	266	82.013	239.054	124.887	1.00	100.00	7
ATOM	1670	CA	ASN	266	82.045	240.230	125.765	1.00	100.00	6
ATOM	1671	CB	ASN	266	80.951	240.161	126.866	1.00	100.00	6
ATOM	1672	CG	ASN	266	80.983	238.859	127.692	1.00	100.00	6
ATOM	1673	OD1	ASN	266	80.179	237.944	127.465	1.00	100.00	8
ATOM	1674	ND2	ASN	266	81.874	238.801	128.687	1.00	100.00	7
ATOM	1675	C	ASN	266	83.434	240.451	126.368	1.00	100.00	6
ATOM	1676	O	ASN	266	83.803	241.582	126.706	1.00	99.50	8
ATOM	1677	N	HIS	267	84.200	239.361	126.468	1.00	100.00	7
ATOM	1678	CA	HIS	267	85.558	239.382	127.016	1.00	100.00	6
ATOM	1679	CB	HIS	267	85.548	239.702	128.517	1.00	99.65	6
ATOM	1680	CG	HIS	267	86.670	240.596	128.947	1.00	100.00	6
ATOM	1681	CD2	HIS	267	87.569	241.309	128.225	1.00	100.00	6
ATOM	1682	ND1	HIS	267	86.946	240.861	130.271	1.00	100.00	7
ATOM	1683	CE1	HIS	267	87.965	241.700	130.348	1.00	100.00	6
ATOM	1684	NE2	HIS	267	88.361	241.986	129.121	1.00	100.00	7
ATOM	1685	C	HIS	267	86.284	238.057	126.779	1.00	100.00	6
ATOM	1686	O	HIS	267	85.609	237.001	126.781	1.00	99.13	8
ATOM	1687	OT	HIS	267	87.522	238.099	126.591	1.00	100.00	8
ATOM	1688	CB	ALA	275	87.847	237.517	122.968	1.00	71.75	6
ATOM	1689	C	ALA	275	90.121	236.696	122.240	1.00	77.78	6
ATOM	1690	O	ALA	275	90.486	236.200	121.171	1.00	74.24	8
ATOM	1691	N	ALA	275	88.962	235.648	124.194	1.00	72.73	7
ATOM	1692	CA	ALA	275	88.778	236.298	122.860	1.00	76.10	6
ATOM	1693	N	ALA	276	90.863	237.571	122.921	1.00	80.81	7
ATOM	1694	CA	ALA	276	92.163	238.023	122.426	1.00	84.26	6
ATOM	1695	CB	ALA	276	92.769	239.068	123.370	1.00	79.85	6
ATOM	1696	C	ALA	276	93.089	236.815	122.283	1.00	89.16	6
ATOM	1697	O	ALA	276	94.123	236.885	121.607	1.00	92.66	8
ATOM	1698	N	ALA	277	92.708	235.717	122.943	1.00	92.55	7
ATOM	1699	CA	ALA	277	93.462	234.462	122.917	1.00	91.98	6
ATOM	1700	CB	ALA	277	93.171	233.632	124.179	1.00	86.98	6
ATOM	1701	C	ALA	277	93.016	233.710	121.661	1.00	89.40	6
ATOM	1702	O	ALA	277	93.836	233.378	120.796	1.00	87.90	8
ATOM	1703	N	ALA	278	91.700	233.525	121.538	1.00	84.60	7
ATOM	1704	CA	ALA	278	91.109	232.831	120.401	1.00	81.23	6
ATOM	1705	CB	ALA	278	89.592	232.818	120.519	1.00	80.32	6
ATOM	1706	C	ALA	278	91.547	233.496	119.102	1.00	81.59	6
ATOM	1707	O	ALA	278	91.612	232.847	118.062	1.00	81.48	8
ATOM	1708	N	ILE	279	91.851	234.791	119.172	1.00	81.36	7
ATOM	1709	CA	ILE	279	92.293	235.536	118.004	1.00	80.80	6
ATOM	1710	CB	ILE	279	92.277	237.069	118.233	1.00	81.66	6
ATOM	1711	CG2	ILE	279	93.338	237.759	117.375	1.00	78.92	6
ATOM	1712	CG1	ILE	279	90.898	237.638	117.895	1.00	84.39	6
ATOM	1713	CD1	ILE	279	90.782	239.156	118.077	1.00	81.98	6
ATOM	1714	C	ILE	279	93.707	235.111	117.680	1.00	80.72	6
ATOM	1715	O	ILE	279	93.976	234.681	116.565	1.00	82.68	8
ATOM	1716	N	ARG	280	94.605	235.202	118.657	1.00	81.91	7
ATOM	1717	CA	ARG	280	95.994	234.817	118.422	1.00	86.81	6
ATOM	1718	CB	ARG	280	96.904	235.269	119.564	1.00	87.27	6
ATOM	1719	CG	ARG	280	97.051	236.786	119.620	1.00	91.90	6
ATOM	1720	CD	ARG	280	98.335	237.223	120.307	1.00	96.88	6
ATOM	1721	NE	ARG	280	98.447	236.689	121.665	1.00	100.00	7
ATOM	1722	CZ	ARG	280	99.076	237.298	122.668	1.00	100.00	6
ATOM	1723	NH1	ARG	280	99.658	238.480	122.475	1.00	100.00	7
ATOM	1724	NH2	ARG	280	99.128	236.718	123.866	1.00	99.94	7
ATOM	1725	C	ARG	280	96.197	233.346	118.072	1.00	87.87	6
ATOM	1726	O	ARG	280	97.208	232.975	117.470	1.00	87.49	8
ATOM	1727	N	MET	281	95.219	232.518	118.418	1.00	88.64	7
ATOM	1728	CA	MET	281	95.294	231.091	118.125	1.00	89.59	6
ATOM	1729	CB	MET	281	94.341	230.299	119.024	1.00	88.02	6
ATOM	1730	CG	MET	281	94.790	230.135	120.466	1.00	85.68	6
ATOM	1731	SD	MET	281	96.047	228.875	120.668	1.00	81.12	16
ATOM	1732	CE	MET	281	95.053	227.403	120.638	1.00	82.63	6
ATOM	1733	C	MET	281	94.855	230.912	116.678	1.00	90.40	6
ATOM	1734	O	MET	281	95.266	229.963	116.011	1.00	94.24	8
ATOM	1735	N	GLY	282	94.051	231.860	116.196	1.00	88.92	7
ATOM	1736	CA	GLY	282	93.523	231.796	114.845	1.00	85.88	6
ATOM	1737	C	GLY	282	92.422	230.760	114.886	1.00	86.15	6
ATOM	1738	O	GLY	282	92.349	229.871	114.032	1.00	85.30	8
ATOM	1739	N	GLN	283	91.581	230.872	115.915	1.00	84.85	7
ATOM	1740	CA	GLN	283	90.482	229.945	116.151	1.00	83.57	6
ATOM	1741	CB	GLN	283	90.465	229.552	117.630	1.00	84.62	6
ATOM	1742	CG	GLN	283	89.545	228.389	117.962	1.00	87.92	6
ATOM	1743	CD	GLN	283	89.383	228.185	119.457	1.00	89.75	6
ATOM	1744	OE1	GLN	283	90.294	228.477	120.249	1.00	83.71	8
ATOM	1745	NE2	GLN	283	88.218	227.678	119.855	1.00	88.55	7
ATOM	1746	C	GLN	283	89.114	230.478	115.737	1.00	83.15	6
ATOM	1747	O	GLN	283	88.310	230.886	116.579	1.00	83.14	8
ATOM	1748	N	TYR	284	88.852	230.469	114.435	1.00	84.76	7
ATOM	1749	CA	TYR	284	87.576	230.949	113.903	1.00	84.23	6
ATOM	1750	CB	TYR	284	87.782	232.158	112.965	1.00	77.45	6
ATOM	1751	CG	TYR	284	88.813	231.955	111.875	1.00	64.97	6
ATOM	1752	CD1	TYR	284	88.435	231.520	110.615	1.00	64.14	6
ATOM	1753	CE1	TYR	284	89.377	231.309	109.608	1.00	71.84	6
ATOM	1754	CD2	TYR	284	90.167	232.186	112.114	1.00	66.79	6
ATOM	1755	CE2	TYR	284	91.126	231.984	111.121	1.00	70.67	6
ATOM	1756	CZ	TYR	284	90.723	231.540	109.866	1.00	75.84	6
ATOM	1757	OH	TYR	284	91.653	231.302	108.873	1.00	74.32	8
ATOM	1758	C	TYR	284	86.864	229.814	113.178	1.00	85.85	6
ATOM	1759	O	TYR	284	87.469	229.090	112.383	1.00	87.41	8
ATOM	1760	N	GLU	285	85.583	229.641	113.471	1.00	85.92	7
ATOM	1761	CA	GLU	285	84.816	228.582	112.832	1.00	88.53	6
ATOM	1762	CB	GLU	285	83.998	227.815	113.882	1.00	91.78	6
ATOM	1763	CG	GLU	285	84.808	227.351	115.102	1.00	97.83	6
ATOM	1764	CD	GLU	285	86.105	226.625	114.733	1.00	100.00	6
ATOM	1765	OE1	GLU	285	87.197	227.168	115.020	1.00	100.00	8
ATOM	1766	OE2	GLU	285	86.036	225.511	114.164	1.00	100.00	8
ATOM	1767	C	GLU	285	83.889	229.132	111.763	1.00	86.91	6
ATOM	1768	O	GLU	285	83.602	230.323	111.751	1.00	88.23	8
ATOM	1769	N	PHE	286	83.455	228.264	110.851	1.00	86.96	7
ATOM	1770	CA	PHE	286	82.546	228.641	109.764	1.00	90.35	6
ATOM	1771	CB	PHE	286	83.085	228.171	108.395	1.00	87.31	6
ATOM	1772	CG	PHE	286	84.132	229.068	107.783	1.00	81.90	6
ATOM	1773	CD1	PHE	286	84.140	230.441	108.022	1.00	84.48	6
ATOM	1774	CD2	PHE	286	85.111	228.531	106.953	1.00	79.50	6
ATOM	1775	CE1	PHE	286	85.110	231.267	107.447	1.00	81.25	6
ATOM	1776	CE2	PHE	286	86.086	229.342	106.371	1.00	80.35	6
ATOM	1777	CZ	PHE	286	86.088	230.714	106.618	1.00	81.62	6
ATOM	1778	C	PHE	286	81.195	227.949	110.024	1.00	93.74	6
ATOM	1779	O	PHE	286	80.821	227.020	109.300	1.00	97.91	8
ATOM	1780	N	PRO	287	80.424	228.417	111.028	1.00	96.58	7
ATOM	1781	CD	PRO	287	80.646	229.619	111.848	1.00	96.93	6
ATOM	1782	CA	PRO	287	79.124	227.817	111.359	1.00	98.72	6
ATOM	1783	CB	PRO	287	78.481	228.879	112.248	1.00	96.06	6
ATOM	1784	CG	PRO	287	79.650	229.426	112.971	1.00	96.25	6
ATOM	1785	C	PRO	287	78.246	227.488	110.157	1.00	100.00	6
ATOM	1786	O	PRO	287	77.943	228.365	109.353	1.00	100.00	8
ATOM	1787	N	ASN	288	77.837	226.219	110.063	1.00	100.00	7
ATOM	1788	CA	ASN	288	76.988	225.726	108.972	1.00	99.97	6
ATOM	1789	CB	ASN	288	76.934	224.192	108.978	1.00	100.00	6
ATOM	1790	CG	ASN	288	78.240	223.554	108.494	1.00	100.00	6
ATOM	1791	OD1	ASN	288	78.594	222.442	108.907	1.00	100.00	8
ATOM	1792	ND2	ASN	288	78.953	224.251	107.604	1.00	100.00	7
ATOM	1793	C	ASN	288	75.572	226.313	108.887	1.00	99.86	6
ATOM	1794	O	ASN	288	75.004	226.395	107.797	1.00	98.15	8
ATOM	1795	N	PRO	289	74.964	226.695	110.030	1.00	100.00	7
ATOM	1796	CD	PRO	289	75.342	226.519	111.443	1.00	99.94	6
ATOM	1797	CA	PRO	289	73.616	227.266	109.932	1.00	99.25	6
ATOM	1798	CB	PRO	289	73.237	227.506	111.393	1.00	99.05	6
ATOM	1799	CG	PRO	289	74.571	227.618	112.093	1.00	100.00	6
ATOM	1800	C	PRO	289	73.581	228.562	109.121	1.00	98.81	6
ATOM	1801	O	PRO	289	72.509	229.030	108.748	1.00	99.96	8
ATOM	1802	N	GLU	290	74.756	229.131	108.849	1.00	98.86	7
ATOM	1803	CA	GLU	290	74.868	230.372	108.078	1.00	98.50	6
ATOM	1804	CB	GLU	290	75.124	231.577	109.003	1.00	100.00	6
ATOM	1805	CG	GLU	290	73.878	232.222	109.634	1.00	100.00	6
ATOM	1806	CD	GLU	290	73.688	231.868	111.103	1.00	100.00	6
ATOM	1807	OE1	GLU	290	74.690	231.820	111.852	1.00	100.00	8
ATOM	1808	OE2	GLU	290	72.528	231.652	111.511	1.00	98.65	8
ATOM	1809	C	GLU	290	75.972	230.322	107.019	1.00	95.42	6
ATOM	1810	O	GLU	290	75.966	231.112	106.085	1.00	93.17	8
ATOM	1811	N	TRP	291	76.892	229.372	107.154	1.00	97.25	7
ATOM	1812	CA	TRP	291	78.010	229.213	106.221	1.00	98.31	6
ATOM	1813	CB	TRP	291	79.327	229.167	106.991	1.00	99.73	6
ATOM	1814	CG	TRP	291	79.835	230.505	107.415	1.00	99.76	6
ATOM	1815	CD2	TRP	291	80.652	231.389	106.640	1.00	97.41	6
ATOM	1816	CE2	TRP	291	80.930	232.507	107.444	1.00	94.32	6
ATOM	1817	CE3	TRP	291	81.185	231.333	105.348	1.00	98.04	6
ATOM	1818	CD1	TRP	291	79.648	231.111	108.618	1.00	97.37	6
ATOM	1819	NE1	TRP	291	80.304	232.313	108.644	1.00	96.11	7
ATOM	1820	CZ2	TRP	291	81.709	233.566	106.999	1.00	96.95	6
ATOM	1821	CZ3	TRP	291	81.960	232.383	104.907	1.00	98.79	6
ATOM	1822	CH2	TRP	291	82.218	233.486	105.733	1.00	99.72	6
ATOM	1823	C	TRP	291	77.965	228.001	105.304	1.00	99.56	6
ATOM	1824	O	TRP	291	78.707	227.946	104.319	1.00	99.23	8
ATOM	1825	N	SER	292	77.129	227.023	105.649	1.00	100.00	7
ATOM	1826	CA	SER	292	76.979	225.792	104.867	1.00	100.00	6
ATOM	1827	CB	SER	292	75.840	224.940	105.429	1.00	97.10	6
ATOM	1828	OG	SER	292	74.624	225.670	105.452	1.00	97.55	8
ATOM	1829	C	SER	292	76.741	226.058	103.382	1.00	99.29	6
ATOM	1830	O	SER	292	77.561	225.684	102.543	1.00	100.00	8
ATOM	1831	N	GLU	293	75.638	226.736	103.076	1.00	95.37	7
ATOM	1832	CA	GLU	293	75.272	227.067	101.704	1.00	94.55	6
ATOM	1833	CB	GLU	293	73.899	227.758	101.680	1.00	99.13	6
ATOM	1834	CG	GLU	293	73.865	229.208	102.223	1.00	100.00	6
ATOM	1835	CD	GLU	293	74.064	229.316	103.739	1.00	100.00	6
ATOM	1836	OE1	GLU	293	75.219	229.168	104.208	1.00	100.00	8
ATOM	1837	OE2	GLU	293	73.065	229.570	104.456	1.00	100.00	8
ATOM	1838	C	GLU	293	76.312	227.930	100.972	1.00	92.35	6
ATOM	1839	O	GLU	293	76.289	228.022	99.743	1.00	89.41	8
ATOM	1840	N	VAL	294	77.213	228.554	101.730	1.00	91.83	7
ATOM	1841	CA	VAL	294	78.267	229.412	101.167	1.00	91.69	6
ATOM	1842	CB	VAL	294	78.742	230.473	102.209	1.00	94.30	6
ATOM	1843	CG1	VAL	294	79.813	231.395	101.611	1.00	93.85	6
ATOM	1844	CG2	VAL	294	77.557	231.294	102.691	1.00	96.91	6
ATOM	1845	C	VAL	294	79.480	228.621	100.664	1.00	87.73	6
ATOM	1846	O	VAL	294	79.968	227.714	101.344	1.00	86.99	8
ATOM	1847	N	SER	295	79.994	229.027	99.505	1.00	83.60	7
ATOM	1848	CA	SER	295	81.151	228.399	98.857	1.00	85.59	6
ATOM	1849	CB	SER	295	81.595	229.275	97.679	1.00	87.62	6
ATOM	1850	OG	SER	295	82.783	228.784	97.077	1.00	90.76	8
ATOM	1851	C	SER	295	82.380	228.046	99.721	1.00	84.88	6
ATOM	1852	O	SER	295	82.494	228.458	100.875	1.00	82.15	8
ATOM	1853	N	GLU	296	83.282	227.254	99.143	1.00	86.09	7
ATOM	1854	CA	GLU	296	84.507	226.828	99.817	1.00	88.44	6
ATOM	1855	CB	GLU	296	84.747	225.331	99.619	1.00	91.27	6
ATOM	1856	CG	GLU	296	84.934	224.532	100.914	1.00	95.23	6
ATOM	1857	CD	GLU	296	86.173	224.933	101.707	1.00	98.21	6
ATOM	1858	OE1	GLU	296	87.239	225.177	101.099	1.00	97.65	8
ATOM	1859	OE2	GLU	296	86.079	224.990	102.953	1.00	100.00
ATOM	1860	C	GLU	296	85.682	227.611	99.245	1.00	88.98	6
ATOM	1861	O	GLU	296	86.727	227.749	99.890	1.00	89.20	8
ATOM	1862	N	GLU	297	85.503	228.100	98.017	1.00	89.53	7
ATOM	1863	CA	GLU	297	86.521	228.883	97.314	1.00	87.42	6
ATOM	1864	CB	GLU	297	86.072	229.171	95.881	1.00	86.30	6
ATOM	1865	CG	GLU	297	86.965	230.157	95.143	1.00	88.87	6
ATOM	1866	CD	GLU	297	86.231	230.954	94.071	1.00	91.65	6
ATOM	1867	OE1	GLU	297	86.914	231.502	93.180	1.00	92.26	8
ATOM	1868	OE2	GLU	297	84.982	231.050	94.123	1.00	90.45	8
ATOM	1869	C	GLU	297	86.691	230.202	98.053	1.00	85.34	6
ATOM	1870	O	GLU	297	87.804	230.693	98.224	1.00	84.25	8
ATOM	1871	N	VAL	298	85.562	230.749	98.494	1.00	84.38	7
ATOM	1872	CA	VAL	298	85.502	232.008	99.227	1.00	86.45	6
ATOM	1873	CB	VAL	298	84.037	232.461	99.406	1.00	89.83	6
ATOM	1874	CG1	VAL	298	83.976	233.919	99.859	1.00	93.97	6
ATOM	1875	CG2	VAL	298	83.260	232.254	98.122	1.00	92.45	6
ATOM	1876	C	VAL	298	86.114	231.862	100.621	1.00	86.34	6
ATOM	1877	O	VAL	298	86.588	232.835	101.209	1.00	86.25	8
ATOM	1878	N	LYS	299	86.074	230.643	101.149	1.00	87.55	7
ATOM	1879	CA	LYS	299	86.614	230.350	102.469	1.00	85.81	6
ATOM	1880	CB	LYS	299	86.085	229.002	102.982	1.00	85.19	6
ATOM	1881	CG	LYS	299	84.563	228.983	103.128	1.00	87.80	6
ATOM	1882	CD	LYS	299	84.018	227.695	103.729	1.00	93.61	6
ATOM	1883	CE	LYS	299	82.493	227.766	103.861	1.00	97.09	6
ATOM	1884	NZ	LYS	299	81.884	226.597	104.563	1.00	98.33	7
ATOM	1885	C	LYS	299	88.133	230.390	102.471	1.00	84.77	6
ATOM	1886	O	LYS	299	88.728	230.782	103.472	1.00	84.87	8
ATOM	1887	N	MET	300	88.754	230.019	101.349	1.00	83.67	7
ATOM	1888	CA	MET	300	90.220	230.025	101.239	1.00	83.82	6
ATOM	1889	CB	MET	300	90.673	229.485	99.875	1.00	91.34	6
ATOM	1890	CG	MET	300	92.173	229.730	99.528	1.00	98.50	6
ATOM	1891	SD	MET	300	92.674	231.467	99.102	1.00	100.00	16
ATOM	1892	CE	MET	300	93.082	231.332	97.329	1.00	93.54	6
ATOM	1893	C	MET	300	90.748	231.443	101.413	1.00	78.22	6
ATOM	1894	O	MET	300	91.868	231.656	101.892	1.00	79.06	8
ATOM	1895	N	LEU	301	89.921	232.398	101.000	1.00	71.14	7
ATOM	1896	CA	LEU	301	90.221	233.821	101.069	1.00	63.05	6
ATOM	1897	CB	LEU	301	89.171	234.566	100.269	1.00	59.75	6
ATOM	1898	CG	LEU	301	89.650	235.763	99.485	1.00	61.24	6
ATOM	1899	CD1	LEU	301	91.117	235.598	99.091	1.00	59.15	6
ATOM	1900	CD2	LEU	301	88.731	235.904	98.277	1.00	63.03	6
ATOM	1901	C	LEU	301	90.211	234.320	102.502	1.00	61.02	6
ATOM	1902	O	LEU	301	91.184	234.904	102.980	1.00	57.69	8
ATOM	1903	N	ILE	302	89.104	234.075	103.190	1.00	58.87	7
ATOM	1904	CA	ILE	302	88.971	234.496	104.569	1.00	61.17	6
ATOM	1905	CB	ILE	302	87.608	234.110	105.122	1.00	58.05	6
ATOM	1906	CG2	ILE	302	87.491	234.540	106.570	1.00	51.39	6
ATOM	1907	CG1	ILE	302	86.519	234.776	104.282	1.00	62.26	6
ATOM	1908	CD1	ILE	302	85.168	234.091	104.351	1.00	67.55	6
ATOM	1909	C	ILE	302	90.071	233.855	105.406	1.00	66.49
ATOM	1910	O	ILE	302	90.503	234.419	106.404	1.00	69.43	8
ATOM	1911	N	ARG	303	90.544	232.694	104.958	1.00	71.10	7
ATOM	1912	CA	ARG	303	91.597	231.957	105.643	1.00	69.40	6
ATOM	1913	CB	ARG	303	91.552	230.485	105.243	1.00	71.07	6
ATOM	1914	CG	ARG	303	90.412	229.716	105.894	1.00	75.29	6
ATOM	1915	CD	ARG	303	90.375	228.250	105.454	1.00	76.49	6
ATOM	1916	NE	ARG	303	89.275	227.523	106.088	1.00	77.93	7
ATOM	1917	CZ	ARG	303	88.691	226.440	105.587	1.00	77.15	6
ATOM	1918	NH1	ARG	303	89.092	225.929	104.433	1.00	78.05	7
ATOM	1919	NH2	ARG	303	87.690	225.873	106.240	1.00	80.74	7
ATOM	1920	C	ARG	303	92.979	232.543	105.393	1.00	69.41	6
ATOM	1921	O	ARG	303	93.776	232.673	106.326	1.00	67.01	8
ATOM	1922	N	ASN	304	93.262	232.899	104.143	1.00	71.15	7
ATOM	1923	CA	ASN	304	94.565	233.478	103.797	1.00	76.89	6
ATOM	1924	CB	ASN	304	94.780	233.516	102.279	1.00	77.87	6
ATOM	1925	CG	ASN	304	95.230	232.177	101.713	1.00	80.94	6
ATOM	1926	OD1	ASN	304	95.138	231.950	100.505	1.00	83.74	8
ATOM	1927	ND2	ASN	304	95.740	231.293	102.575	1.00	76.87	7
ATOM	1928	C	ASN	304	94.712	234.885	104.378	1.00	76.89	6
ATOM	1929	O	ASN	304	95.826	235.334	104.696	1.00	77.32	8
ATOM	1930	N	LEU	305	93.577	235.572	104.504	1.00	72.94	7
ATOM	1931	CA	LEU	305	93.539	236.925	105.044	1.00	65.51	6
ATOM	1932	CB	LEU	305	92.222	237.606	104.665	1.00	61.03	6
ATOM	1933	CG	LEU	305	92.084	238.318	103.321	1.00	58.86	6
ATOM	1934	CD1	LEU	305	92.633	237.498	102.173	1.00	59.31	6
ATOM	1935	CD2	LEU	305	90.623	238.619	103.100	1.00	61.97	6
ATOM	1936	C	LEU	305	93.656	236.841	106.559	1.00	62.51	6
ATOM	1937	O	LEU	305	94.436	237.574	107.173	1.00	55.05	8
ATOM	1938	N	LEU	306	92.894	235.910	107.139	1.00	61.43	7
ATOM	1939	CA	LEU	306	92.871	235.681	108.582	1.00	60.96	6
ATOM	1940	CB	LEU	306	91.522	235.117	109.019	1.00	50.96	6
ATOM	1941	CG	LEU	306	90.481	236.052	109.610	1.00	49.81	6
ATOM	1942	CD1	LEU	306	90.914	237.500	109.493	1.00	47.89	6
ATOM	1943	CD2	LEU	306	89.158	235.798	108.915	1.00	41.87	6
ATOM	1944	C	LEU	306	93.985	234.791	109.128	1.00	64.54	6
ATOM	1945	O	LEU	306	93.730	233.916	109.960	1.00	67.76	8
ATOM	1946	N	LYS	307	95.204	234.999	108.634	1.00	65.30	7
ATOM	1947	CA	LYS	307	96.369	234.237	109.068	1.00	64.60	6
ATOM	1948	CB	LYS	307	97.432	234.239	107.967	1.00	65.63	6
ATOM	1949	CG	LYS	307	97.119	233.323	106.792	1.00	63.42	6
ATOM	1950	CD	LYS	307	97.448	231.877	107.143	1.00	67.43	6
ATOM	1951	CE	LYS	307	97.116	230.900	106.025	1.00	65.67	6
ATOM	1952	NZ	LYS	307	97.505	229.531	106.450	1.00	65.81	7
ATOM	1953	C	LYS	307	96.884	234.962	110.314	1.00	63.50	6
ATOM	1954	O	LYS	307	96.854	236.182	110.368	1.00	64.53	8
ATOM	1955	N	THR	308	97.330	234.228	111.324	1.00	63.07	7
ATOM	1956	CA	THR	308	97.818	234.890	112.525	1.00	62.57	6
ATOM	1957	CB	THR	308	97.850	233.944	113.769	1.00	67.53	6
ATOM	1958	OG1	THR	308	99.080	233.203	113.799	1.00	70.53	8
ATOM	1959	CG2	THR	308	96.652	232.984	113.764	1.00	61.84	6
ATOM	1960	C	THR	308	99.186	235.517	112.331	1.00	60.55	6
ATOM	1961	O	THR	308	99.553	236.452	113.040	1.00	58.58	8
ATOM	1962	N	ALA	309	99.955	234.987	111.388	1.00	63.03	7
ATOM	1963	CA	ALA	309	101.289	235.534	111.140	1.00	68.60	6
ATOM	1964	CB	ALA	309	102.236	234.452	110.577	1.00	57.95	6
ATOM	1965	C	ALA	309	101.236	236.742	110.204	1.00	69.72	6
ATOM	1966	O	ALA	309	100.473	236.747	109.223	1.00	73.60	8
ATOM	1967	N	ALA	310	101.984	237.789	110.556	1.00	65.13	7
ATOM	1968	CA	ALA	310	102.028	238.995	109.742	1.00	60.27	6
ATOM	1969	CB	ALA	310	103.065	239.957	110.291	1.00	63.72	6
ATOM	1970	C	ALA	310	102.406	238.504	108.338	1.00	58.37	6
ATOM	1971	O	ALA	310	101.584	238.576	107.422	1.00	56.83	8
ATOM	1972	N	ALA	311	103.599	237.907	108.198	1.00	55.01	7
ATOM	1973	CA	ALA	311	104.070	237.375	106.908	1.00	51.77	6
ATOM	1974	CB	ALA	311	105.453	236.778	107.069	1.00	28.89	6
ATOM	1975	C	ALA	311	103.056	236.271	106.564	1.00	56.29	6
ATOM	1976	O	ALA	311	102.069	236.104	107.287	1.00	61.54	8
ATOM	1977	N	ALA	312	103.230	235.542	105.469	1.00	58.24	7
ATOM	1978	CA	ALA	312	102.261	234.473	105.136	1.00	62.72	6
ATOM	1979	CB	ALA	312	102.285	233.375	106.227	1.00	61.28	6
ATOM	1980	C	ALA	312	100.801	234.892	104.864	1.00	62.04	6
ATOM	1981	O	ALA	312	100.050	234.151	104.220	1.00	57.84	8
ATOM	1982	N	ARG	313	100.396	236.049	105.387	1.00	62.33	7
ATOM	1983	CA	ARG	313	99.043	236.557	105.201	1.00	58.23	6
ATOM	1984	CB	ARG	313	98.718	237.610	106.266	1.00	52.76	6
ATOM	1985	CG	ARG	313	97.249	237.978	106.338	1.00	44.89	6
ATOM	1986	CD	ARG	313	96.978	239.079	107.360	1.00	43.94	6
ATOM	1987	NE	ARG	313	96.960	238.630	108.748	1.00	34.75	7
ATOM	1988	CZ	ARG	313	97.746	239.124	109.702	1.00	39.40	6
ATOM	1989	NH1	ARG	313	98.613	240.088	109.439	1.00	37.30	7
ATOM	1990	NH2	ARG	313	97.705	238.619	110.921	1.00	42.01	7
ATOM	1991	C	ARG	313	99.004	237.185	103.821	1.00	60.40	6
ATOM	1992	O	ARG	313	99.933	237.909	103.437	1.00	63.00	8
ATOM	1993	N	MET	314	97.946	236.875	103.072	1.00	60.87	7
ATOM	1994	CA	MET	314	97.742	237.388	101.712	1.00	59.63	6
ATOM	1995	CB	MET	314	96.308	237.061	101.262	1.00	54.24	6
ATOM	1996	CG	MET	314	95.992	237.476	99.839	1.00	56.69	6
ATOM	1997	SD	MET	314	94.404	236.858	99.263	1.00	65.96	16
ATOM	1998	CE	MET	314	94.890	235.270	98.573	1.00	71.51	6
ATOM	1999	C	MET	314	98.015	238.897	101.550	1.00	61.09	6
ATOM	2000	O	MET	314	97.755	239.685	102.472	1.00	63.27	8
ATOM	2001	N	THR	315	98.572	239.284	100.397	1.00	58.39	7
ATOM	2002	CA	THR	315	98.878	240.692	100.107	1.00	55.90	6
ATOM	2003	CB	THR	315	100.172	240.853	99.249	1.00	57.21	6
ATOM	2004	OG1	THR	315	99.922	240.486	97.881	1.00	57.00	8
ATOM	2005	CG2	THR	315	101.308	240.008	99.813	1.00	52.24	6
ATOM	2006	C	THR	315	97.693	241.337	99.361	1.00	56.00	6
ATOM	2007	O	THR	315	96.795	240.626	98.898	1.00	56.57	8
ATOM	2008	N	ILE	316	97.673	242.670	99.257	1.00	56.10	7
ATOM	2009	CA	ILE	316	96.572	243.361	98.559	1.00	52.69	6
ATOM	2010	CB	ILE	316	96.618	244.922	98.735	1.00	46.51	6
ATOM	2011	CG2	ILE	316	97.711	245.545	97.882	1.00	42.44	6
ATOM	2012	CG1	ILE	316	95.304	245.542	98.271	1.00	32.71	6
ATOM	2013	CD1	ILE	316	94.130	245.091	99.068	1.00	36.32	6
ATOM	2014	C	ILE	316	96.559	243.056	97.068	1.00	52.94	6
ATOM	2015	O	ILE	316	95.498	242.975	96.448	1.00	53.27	8
ATOM	2016	N	THR	317	97.751	242.867	96.515	1.00	51.84	7
ATOM	2017	CA	THR	317	97.913	242.575	95.101	1.00	53.59	6
ATOM	2018	CB	THR	317	99.381	242.692	94.709	1.00	54.78	6
ATOM	2019	OG1	THR	317	100.054	243.558	95.646	1.00	53.23	8
ATOM	2020	CG2	THR	317	99.503	243.240	93.290	1.00	48.84	6
ATOM	2021	C	THR	317	97.401	241.182	94.777	1.00	55.92	6
ATOM	2022	O	THR	317	96.935	240.922	93.671	1.00	54.42	8
ATOM	2023	N	GLU	318	97.497	240.294	95.761	1.00	61.74	7
ATOM	2024	CA	GLU	318	97.048	238.920	95.613	1.00	66.53	6
ATOM	2025	CB	GLU	318	97.812	237.995	96.575	1.00	67.74	6
ATOM	2026	CG	GLU	318	99.322	237.900	96.298	1.00	66.05	6
ATOM	2027	CD	GLU	318	100.045	236.885	97.187	1.00	71.37	6
ATOM	2028	OE1	GLU	318	99.979	236.998	98.438	1.00	66.66	8
ATOM	2029	OE2	GLU	318	100.700	235.981	96.622	1.00	72.71	8
ATOM	2030	C	GLU	318	95.544	238.861	95.881	1.00	68.15	6
ATOM	2031	O	GLU	318	94.828	238.049	95.290	1.00	69.31	8
ATOM	2032	N	PHE	319	95.068	239.743	96.759	1.00	68.68	7
ATOM	2033	CA	PHE	319	93.653	239.794	97.102	1.00	68.65	6
ATOM	2034	CB	PHE	319	93.405	240.792	98.249	1.00	62.07	6
ATOM	2035	CG	PHE	319	91.947	240.908	98.661	1.00	59.39	6
ATOM	2036	CD1	PHE	319	91.063	241.715	97.949	1.00	55.67	6
ATOM	2037	CD2	PHE	319	91.457	240.199	99.752	1.00	54.87	6
ATOM	2038	CE1	PHE	319	89.730	241.808	98.316	1.00	49.32	6
ATOM	2039	CE2	PHE	319	90.122	240.294	100.118	1.00	51.67	6
ATOM	2040	CZ	PHE	319	89.261	241.099	99.396	1.00	46.18	6
ATOM	2041	C	PHE	319	92.878	240.236	95.873	1.00	71.46	6
ATOM	2042	O	PHE	319	91.898	239.609	95.486	1.00	72.12	8
ATOM	2043	N	MET	320	93.359	241.306	95.251	1.00	74.50	7
ATOM	2044	CA	MET	320	92.736	241.868	94.067	1.00	76.81	6
ATOM	2045	CB	MET	320	93.363	243.229	93.756	1.00	78.28	6
ATOM	2046	CG	MET	320	92.338	244.342	93.529	1.00	80.53	6
ATOM	2047	SD	MET	320	91.087	244.456	94.831	1.00	77.61	16
ATOM	2048	CE	MET	320	92.080	244.892	96.188	1.00	80.25	6
ATOM	2049	C	MET	320	92.757	240.970	92.840	1.00	78.75	6
ATOM	2050	O	MET	320	91.973	241.174	91.915	1.00	80.84	8
ATOM	2051	N	ASN	321	93.650	239.983	92.828	1.00	80.16	7
ATOM	2052	CA	ASN	321	93.754	239.061	91.700	1.00	79.55	6
ATOM	2053	CB	ASN	321	95.211	238.780	91.373	1.00	79.09	6
ATOM	2054	CG	ASN	321	95.758	239.743	90.364	1.00	81.54	6
ATOM	2055	OD1	ASN	321	95.105	240.041	89.367	1.00	85.07	8
ATOM	2056	ND2	ASN	321	96.961	240.241	90.608	1.00	84.63	7
ATOM	2057	C	ASN	321	92.990	237.753	91.873	1.00	81.16	6
ATOM	2058	O	ASN	321	92.842	236.985	90.922	1.00	82.37	8
ATOM	2059	N	HIS	322	92.525	237.488	93.088	1.00	83.32	7
ATOM	2060	CA	HIS	322	91.776	236.269	93.359	1.00	86.48	6
ATOM	2061	CB	HIS	322	91.506	236.131	94.861	1.00	87.65	6
ATOM	2062	CG	HIS	322	90.691	234.931	95.230	1.00	87.78	6
ATOM	2063	CD2	HIS	322	90.948	233.905	96.074	1.00	90.78	6
ATOM	2064	ND1	HIS	322	89.430	234.698	94.724	1.00	88.02	7
ATOM	2065	CE1	HIS	322	88.947	233.583	95.238	1.00	89.57	6
ATOM	2066	NE2	HIS	322	89.849	233.082	96.062	1.00	92.43	7
ATOM	2067	C	HIS	322	90.466	236.366	92.576	1.00	87.09	6
ATOM	2068	O	HIS	322	89.874	237.447	92.471	1.00	86.22	8
ATOM	2069	N	PRO	323	90.016	235.244	91.986	1.00	87.32	7
ATOM	2070	CD	PRO	323	90.742	233.967	91.885	1.00	83.40	6
ATOM	2071	CA	PRO	323	88.780	235.185	91.200	1.00	86.59	6
ATOM	2072	CB	PRO	323	88.692	233.711	90.838	1.00	84.41	6
ATOM	2073	CG	PRO	323	90.129	233.361	90.654	1.00	82.75	6
ATOM	2074	C	PRO	323	87.507	235.701	91.875	1.00	86.16	6
ATOM	2075	O	PRO	323	86.775	236.482	91.272	1.00	85.38	8
ATOM	2076	N	TRP	324	87.252	235.295	93.119	1.00	86.13	7
ATOM	2077	CA	TRP	324	86.053	235.743	93.832	1.00	85.95	6
ATOM	2078	CB	TRP	324	86.062	235.281	95.294	1.00	82.18	6
ATOM	2079	CG	TRP	324	84.729	235.477	95.975	1.00	80.10	6
ATOM	2080	CD2	TRP	324	84.411	236.424	97.002	1.00	83.28	6
ATOM	2081	CE2	TRP	324	83.051	236.228	97.345	1.00	82.38	6
ATOM	2082	CE3	TRP	324	85.137	237.422	97.667	1.00	86.77	6
ATOM	2083	CD1	TRP	324	83.583	234.774	95.739	1.00	80.05	6
ATOM	2084	NE1	TRP	324	82.573	235.215	96.557	1.00	78.64	7
ATOM	2085	CZ2	TRP	324	82.402	236.993	98.327	1.00	82.54	6
ATOM	2086	CZ3	TRP	324	84.487	238.189	98.648	1.00	84.53	6
ATOM	2087	CH2	TRP	324	83.136	237.966	98.964	1.00	82.88	6
ATOM	2088	C	TRP	324	85.878	237.259	93.783	1.00	87.44	6
ATOM	2089	O	TRP	324	84.758	237.751	93.627	1.00	85.83	8
ATOM	2090	N	ILE	325	86.993	237.982	93.912	1.00	87.47	7
ATOM	2091	CA	ILE	325	87.000	239.445	93.888	1.00	83.93	6
ATOM	2092	CB	ILE	325	88.282	240.016	94.568	1.00	75.44	6
ATOM	2093	CG2	ILE	325	88.310	241.524	94.472	1.00	71.00	6
ATOM	2094	CG1	ILE	325	88.373	239.566	96.029	1.00	65.12	6
ATOM	2095	CD1	ILE	325	87.279	240.088	96.893	1.00	59.73	6
ATOM	2096	C	ILE	325	86.937	239.938	92.443	1.00	88.32	6
ATOM	2097	O	ILE	325	85.976	240.599	92.041	1.00	93.04	8
ATOM	2098	N	MET	326	87.960	239.592	91.670	1.00	88.36	7
ATOM	2099	CA	MET	326	88.058	239.979	90.271	1.00	92.38	6
ATOM	2100	CB	MET	326	89.508	239.830	89.823	1.00	93.38	6
ATOM	2101	CG	MET	326	89.740	240.014	88.340	1.00	96.92	6
ATOM	2102	SD	MET	326	91.466	239.719	87.936	1.00	100.00	16
ATOM	2103	CE	MET	326	91.967	241.392	87.385	1.00	100.00	6
ATOM	2104	C	MET	326	87.155	239.131	89.380	1.00	95.92	6
ATOM	2105	O	MET	326	87.380	237.929	89.240	1.00	99.69	8
ATOM	2106	N	GLN	327	86.148	239.752	88.765	1.00	97.73	7
ATOM	2107	CA	GLN	327	85.228	239.017	87.887	1.00	99.65	6
ATOM	2108	CB	GLN	327	84.477	237.924	88.675	1.00	96.03	6
ATOM	2109	CG	GLN	327	83.977	238.325	90.068	1.00	95.50	6
ATOM	2110	CD	GLN	327	82.881	239.376	90.050	1.00	95.94	6
ATOM	2111	OE1	GLN	327	81.737	239.089	89.694	1.00	93.98	8
ATOM	2112	NE2	GLN	327	83.225	240.601	90.448	1.00	91.15	7
ATOM	2113	C	GLN	327	84.216	239.837	87.070	1.00	100.00	6
ATOM	2114	O	GLN	327	83.933	239.498	85.907	1.00	100.00	8
ATOM	2115	N	ALA	328	83.695	240.910	87.680	1.00	100.00	7
ATOM	2116	CA	ALA	328	82.699	241.816	87.077	1.00	100.00	6
ATOM	2117	CB	ALA	328	82.999	242.097	85.595	1.00	100.00	6
ATOM	2118	C	ALA	328	81.316	241.170	87.241	1.00	100.00	6
ATOM	2119	O	ALA	328	80.362	241.821	87.661	1.00	98.40	8
ATOM	2120	N	ALA	329	81.251	239.869	86.954	1.00	100.00	7
ATOM	2121	CA	ALA	329	80.034	239.062	87.049	1.00	100.00	6
ATOM	2122	CB	ALA	329	78.997	239.528	86.015	1.00	100.00	6
ATOM	2123	C	ALA	329	80.422	237.598	86.791	1.00	100.00	6
ATOM	2124	O	ALA	329	80.806	237.247	85.667	1.00	100.00	8
ATOM	2125	N	ALA	330	80.356	236.764	87.836	1.00	100.00	7
ATOM	2126	CA	ALA	330	80.697	235.332	87.738	1.00	100.00	6
ATOM	2127	CB	ALA	330	82.150	235.149	87.265	1.00	100.00	6
ATOM	2128	C	ALA	330	80.483	234.581	89.055	1.00	98.79	6
ATOM	2129	O	ALA	330	80.353	233.354	89.065	1.00	95.99	8
ATOM	2130	N	ALA	331	80.494	235.322	90.163	1.00	99.07	7
ATOM	2131	CA	ALA	331	80.303	234.749	91.493	1.00	97.00	6
ATOM	2132	CB	ALA	331	80.692	235.766	92.566	1.00	93.98	6
ATOM	2133	C	ALA	331	78.854	234.329	91.675	1.00	96.04	6
ATOM	2134	O	ALA	331	77.952	234.942	91.111	1.00	96.34	8
ATOM	2135	N	ALA	332	78.633	233.281	92.459	1.00	95.51	7
ATOM	2136	CA	ALA	332	77.282	232.788	92.711	1.00	95.51	6
ATOM	2137	CB	ALA	332	77.336	231.537	93.590	1.00	93.26	6
ATOM	2138	C	ALA	332	76.439	233.860	93.394	1.00	95.31	6
ATOM	2139	O	ALA	332	76.960	234.669	94.152	1.00	100.00	8
ATOM	2140	N	ALA	333	75.146	233.895	93.090	1.00	94.01	7
ATOM	2141	CA	ALA	333	74.252	234.875	93.699	1.00	91.18	6
ATOM	2142	CB	ALA	333	73.240	235.360	92.690	1.00	89.00	6
ATOM	2143	C	ALA	333	73.552	234.221	94.900	1.00	91.02	6
ATOM	2144	O	ALA	333	72.571	234.753	95.427	1.00	84.80	8
ATOM	2145	N	ALA	334	74.112	233.084	95.331	1.00	94.02	7
ATOM	2146	CA	ALA	334	73.635	232.269	96.453	1.00	95.02	6
ATOM	2147	CB	ALA	334	74.770	231.379	96.974	1.00	90.08	6
ATOM	2148	C	ALA	334	72.994	233.042	97.602	1.00	96.31	6
ATOM	2149	O	ALA	334	73.604	233.236	98.656	1.00	95.05	8
ATOM	2150	N	ALA	335	71.725	233.394	97.392	1.00	97.89	7
ATOM	2151	CA	ALA	335	70.886	234.140	98.329	1.00	98.67	6
ATOM	2152	CB	ALA	335	69.426	233.725	98.167	1.00	95.01	6
ATOM	2153	C	ALA	335	71.280	234.096	99.800	1.00	99.36	6
ATOM	2154	O	ALA	335	71.326	233.033	100.424	1.00	99.14	8
ATOM	2155	N	ALA	336	71.576	235.281	100.324	1.00	100.00	7
ATOM	2156	CA	ALA	336	71.972	235.487	101.711	1.00	99.16	6
ATOM	2157	CB	ALA	336	73.497	235.496	101.833	1.00	95.56	6
ATOM	2158	C	ALA	336	71.384	236.838	102.154	1.00	100.00	6
ATOM	2159	O	ALA	336	71.726	237.356	103.220	1.00	100.00	8
ATOM	2160	N	ALA	337	70.486	237.387	101.324	1.00	100.00	6
ATOM	2161	CA	ALA	337	69.815	238.672	101.573	1.00	100.00	6
ATOM	2162	CB	ALA	337	68.731	238.927	100.516	1.00	100.00	6
ATOM	2163	C	ALA	337	69.225	238.738	102.970	1.00	100.00	6
ATOM	2164	O	ALA	337	69.547	239.639	103.743	1.00	99.70	8
ATOM	2165	N	ALA	338	68.357	237.780	103.283	1.00	100.00	7
ATOM	2166	CA	ALA	338	67.725	237.719	104.593	1.00	100.00	6
ATOM	2167	CB	ALA	338	66.491	236.815	104.538	1.00	97.78	6
ATOM	2168	C	ALA	338	68.757	237.183	105.613	1.00	100.00	6
ATOM	2169	O	ALA	338	68.666	237.476	106.808	1.00	100.00	8
ATOM	2170	N	ALA	339	69.760	236.444	105.118	1.00	100.00	7
ATOM	2171	CA	ALA	339	70.818	235.859	105.952	1.00	97.64	6
ATOM	2172	CB	ALA	339	71.768	235.026	105.099	1.00	92.80	6
ATOM	2173	C	ALA	339	71.601	236.886	106.762	1.00	96.62	6
ATOM	2174	O	ALA	339	71.297	237.116	107.934	1.00	94.32	8
ATOM	2175	N	ALA	340	72.601	237.505	106.136	1.00	97.27	7
ATOM	2176	CA	ALA	340	73.422	238.507	106.814	1.00	97.97	6
ATOM	2177	CB	ALA	340	74.502	239.049	105.873	1.00	92.72	6
ATOM	2178	C	ALA	340	72.579	239.652	107.376	1.00	97.43	6
ATOM	2179	O	ALA	340	72.806	240.094	108.500	1.00	95.64	8
ATOM	2180	N	ALA	341	71.575	240.083	106.615	1.00	97.30	7
ATOM	2181	CA	ALA	341	70.702	241.172	107.034	1.00	97.50	6
ATOM	2182	CB	ALA	341	69.729	241.525	105.933	1.00	96.32	6
ATOM	2183	C	ALA	341	69.951	240.870	108.319	1.00	100.00	6
ATOM	2184	O	ALA	341	70.023	241.647	109.274	1.00	100.00	8
ATOM	2185	N	ALA	342	69.232	239.750	108.348	1.00	100.00	7
ATOM	2186	CA	ALA	342	68.477	239.381	109.544	1.00	100.00	6
ATOM	2187	CB	ALA	342	67.555	238.199	109.266	1.00	100.00	6
ATOM	2188	C	ALA	342	69.417	239.066	110.701	1.00	99.76	6
ATOM	2189	O	ALA	342	69.171	239.485	111.831	1.00	99.57	8
ATOM	2190	N	ALA	343	70.513	238.369	110.404	1.00	98.98	7
ATOM	2191	CA	ALA	343	71.494	238.003	111.424	1.00	98.76	6
ATOM	2192	CB	ALA	343	72.595	237.124	110.816	1.00	94.09	6
ATOM	2193	C	ALA	343	72.098	239.265	112.033	1.00	98.91	6
ATOM	2194	O	ALA	343	72.278	239.361	113.254	1.00	96.27	8
ATOM	2195	N	ALA	344	72.350	240.252	111.173	1.00	99.66	7
ATOM	2196	CA	ALA	344	72.928	241.521	111.601	1.00	100.00	6
ATOM	2197	CB	ALA	344	73.314	242.383	110.391	1.00	98.13	6
ATOM	2198	C	ALA	344	71.964	242.262	112.514	1.00	98.63	6
ATOM	2199	O	ALA	344	72.365	243.165	113.249	1.00	99.84	8
ATOM	2200	N	ALA	345	70.696	241.866	112.478	1.00	97.69	7
ATOM	2201	CA	ALA	345	69.681	242.497	113.312	1.00	100.00	6
ATOM	2202	CB	ALA	345	68.315	242.474	112.605	1.00	96.25	6
ATOM	2203	C	ALA	345	69.596	241.795	114.674	1.00	100.00	6
ATOM	2204	O	ALA	345	69.655	242.445	115.725	1.00	98.58	8
ATOM	2205	N	ALA	346	69.530	240.462	114.623	1.00	100.00	7
ATOM	2206	CA	ALA	346	69.435	239.584	115.792	1.00	100.00	6
ATOM	2207	CB	ALA	346	70.153	238.270	115.523	1.00	100.00	6
ATOM	2208	C	ALA	346	69.883	240.165	117.123	1.00	99.45	6
ATOM	2209	O	ALA	346	69.069	240.324	118.033	1.00	100.00	8
ATOM	2210	N	ALA	347	71.166	240.496	117.236	1.00	99.03	7
ATOM	2211	CA	ALA	347	71.689	241.061	118.478	1.00	100.00	6
ATOM	2212	CB	ALA	347	71.898	239.963	119.520	1.00	99.73	6
ATOM	2213	C	ALA	347	72.978	241.848	118.278	1.00	100.00	6
ATOM	2214	O	ALA	347	73.959	241.337	117.729	1.00	100.00	8
ATOM	2215	N	ALA	348	72.954	243.096	118.737	1.00	100.00	7
ATOM	2216	CA	ALA	348	74.087	244.013	118.645	1.00	100.00	6
ATOM	2217	CB	ALA	348	74.381	244.373	117.180	1.00	100.00	6
ATOM	2218	C	ALA	348	73.737	245.283	119.431	1.00	100.00	6
ATOM	2219	O	ALA	348	72.850	246.053	119.040	1.00	99.90	8
ATOM	2220	N	ALA	349	74.443	245.457	120.533	1.00	100.00	7
ATOM	2221	CA	ALA	349	74.238	246.595	121.447	1.00	100.00	6
ATOM	2222	CB	ALA	349	75.383	246.674	122.455	1.00	100.00	6
ATOM	2223	C	ALA	349	74.172	247.921	120.677	1.00	100.00	6
ATOM	2224	O	ALA	349	73.527	248.885	121.113	1.00	100.00	8
ATOM	2225	N	ALA	350	74.845	247.951	119.544	1.00	99.04	7
ATOM	2226	CA	ALA	350	74.882	249.149	118.692	1.00	100.00	6
ATOM	2227	C	ALA	350	73.465	249.495	118.219	1.00	100.00	6
ATOM	2228	O	ALA	350	72.940	248.886	117.276	1.00	100.00	8
ATOM	2229	CB	ALA	350	75.775	248.902	117.475	1.00	100.00	6
ATOM	2230	N	ALA	351	72.884	250.468	118.902	1.00	100.00	7
ATOM	2231	CA	ALA	351	71.524	250.954	118.606	1.00	100.00	6
ATOM	2232	CB	ALA	351	70.519	250.326	119.573	1.00	98.63	6
ATOM	2233	C	ALA	351	71.472	252.478	118.744	1.00	100.00	6
ATOM	2234	O	ALA	351	71.050	253.128	117.767	1.00	100.00	8
ATOM	2235	OT	ALA	351	71.875	253.007	119.807	1.00	98.22	8
ATOM	2236	P3	ANP	100	87.742	257.555	114.645	1.00	42.42	15
ATOM	2237	O1G	ANP	1001	87.10	257.082	115.999	1.00	54.42	8
ATOM	2238	O2G	ANP	1001	87.349	256.642	113.476	1.00	23.41	8
ATOM	2239	O3G	ANP	1001	89.289	257.514	114.872	1.00	37.25	8
ATOM	2240	P2	ANP	1001	87.963	260.430	114.225	1.00	68.82	15
ATOM	2241	O1B	ANP	1001	87.627	261.465	115.351	1.00	59.81	8
ATOM	2242	O2B	ANP	1001	89.496	260.281	114.015	1.00	69.69	8
ATOM	2243	N3B	ANP	1001	87.264	259.008	114.382	1.00	53.72	7
ATOM	2244	P1	ANP	1001	86.413	260.097	112.093	1.00	52.56	15
ATOM	2245	O1A	ANP	1001	86.439	260.381	110.627	1.00	59.00	8
ATOM	2246	O2A	ANP	1001	86.900	258.693	111.952	1.00	53.10	8
ATOM	2247	O3A	ANP	1001	87.279	261.039	112.972	1.00	53.02	8
ATOM	2248	O5′	ANP	1001	84.992	260.144	112.683	1.00	49.93	8
ATOM	2249	C5′	ANP	1001	84.097	259.019	112.514	1.00	49.91	6
ATOM	2250	C4′	ANP	1001	82.627	259.436	112.572	1.00	41.87	6
ATOM	2251	O4′	ANP	1001	82.464	260.819	112.270	1.00	38.43	8
ATOM	2252	C3′	ANP	1001	81.812	258.632	111.534	1.00	50.98	6
ATOM	2253	O3′	ANP	1001	81.126	257.509	112.115	1.00	59.84	8
ATOM	2254	C2′	ANP	1001	80.815	259.637	110.975	1.00	50.96	6
ATOM	2255	O2′	ANP	1001	79.583	259.607	111.738	1.00	59.86	8
ATOM	2256	C1′	ANP	1001	81.593	260.934	111.143	1.00	49.40	6
ATOM	2257	N9	ANP	1001	82.268	261.368	109.931	1.00	45.89	7
ATOM	2258	C8	ANP	1001	83.614	261.549	109.862	1.00	49.56	6
ATOM	2259	N7	ANP	1001	83.939	262.006	108.632	1.00	47.99	7
ATOM	2260	C5	ANP	1001	82.788	262.114	107.889	1.00	42.44	6
ATOM	2261	C6	ANP	1001	82.433	262.508	106.593	1.00	42.99	6
ATOM	2262	N6	ANP	1001	83.400	262.938	105.676	1.00	36.10	7
ATOM	2263	N1	ANP	1001	81.137	262.471	106.213	1.00	41.43	7
ATOM	2264	C2	ANP	1001	80.158	262.075	107.018	1.00	42.75	6
ATOM	2265	N3	ANP	1001	80.331	261.673	108.272	1.00	42.93	7
ATOM	2266	C4	ANP	1001	81.657	261.692	108.718	1.00	42.82	6

[0045] Once a dataset such as the one in Table 2 is collected, the information is used to determine the three-dimensional structure of the molecule in the crystal. However, in the absence alone of a suitable molecular model, this cannot be done from a single measurement of reflection intensities because certain information, known as phase information, is lost between the three-dimensional shape of the molecule and its Fourier transform, the diffraction pattern. This phase information must be acquired by methods described below in order to perform a Fourier transform on the diffraction pattern to obtain the three-dimensional structure of the molecule in the crystal. It is the determination of phase information that in effect refocuses X-rays to produce the image of the molecule.

[0046] One method of obtaining phase information is by isomorphous replacement, in which heavy-atom derivative crystals are used. In this method, the positions of heavy atoms bound to the molecules in the heavy-atom derivative crystal are determined, and this information is then used to obtain the phase information necessary to elucidate the three-dimensional structure of a native crystal. (Blundel et al., 1976, Protein Crystallography, Academic Press).

[0047] Another method of obtaining phase information is by molecular replacement, which is a method of calculating initial phases for a new crystal of a polypeptide or polypeptide co-complex whose structure coordinates are unknown by orienting and positioning a related polypeptide whose structure coordinates are known within the unit cell of the new crystal so as to best account for the observed diffraction pattern of the new crystal. To enable this, the related molecule must have a similar three dimensional structure. Briefly, the principle behind the method of molecular replacement is as follows. A suitable search model, whose three-dimensional structure is similar to that of the unknown target, is identified first. The search model is then rotated and translated within the unit cell of the unknown. For each position of the model, a set of structure factors of the model is computed. These calculated structure factors are then compared with the measured intensities of the unknown and expressed as correlation coefficients. The solution with the highest correlation coefficient is selected as the true solution. These concepts are discussed at length in the book “The Molecular Replacement Method edited by Rossmann (1972, Int. Sci. Rev. Ser. No 13, Gordon & Breach, New York).

[0048] A third method of phase determination is multi-wavelength anomalous dispersion or MAD. In this method, X-ray diffraction data are collected at several different wavelengths from a single crystal containing at least one heavy atom with absorption edges near the energy of incoming X-ray radiation. The resonance between X-rays and electron orbitals leads to differences in X-ray scattering that permits the locations of the heavy atoms to be identified, which in turn provides phase information for a crystal of a polypeptide. A detailed discussion of MAD analysis can be found in Hendrickson, 1985, Trans. Am. Crystallogr. Assoc., 21:11; Hendrickson et al., 1990, EMBO J. 9:1665; and Hendrickson, 1991, Science 4:91.

[0049] A fourth method of determining phase information is single wavelength anomalous w dispersion or SAD. In this technique, X-ray diffraction data are collected at a single wavelength from a single native or heavy-atom derivative crystal, and phase information is extracted using anomalous scattering information from atoms such as sulfur or chlorine in the native crystal or from the heavy atoms in the heavy-atom derivative crystal. A detailed discussion of SAD analysis can be found in Brodersen et al., 2000, Acta Cryst., D56:431-441.

[0050] A fifth method of determining phase information is single isomorphous replacement with anomalous scattering or SIRAS. This technique combines isomorphous replacement and anomalous scattering techniques to provide phase information for a crystal of a polypeptide. X-ray diffraction data are collected at a single wavelength, usually from a single heavy-atom derivative crystal. Phase information obtained only from the location of the heavy atoms in a single heavy-atom derivative crystal leads to an ambiguity in the phase angle, which is resolved using anomalous scattering from the heavy atoms. Phase information is therefore extracted from both the location of the heavy atoms and from anomalous scattering of the heavy atoms. A detailed discussion of SIRAS analysis can be found in North, 1965, Acta Cryst. 18:212-216; Matthews, 1966, Acta Cryst. 20:82-86.

[0051] The MK-2 structure was determined using the method of molecular replacement. Initially, a homology model of MK-2 was constructed using the crystal structures of calcium calmodulin-dependent protein kinase (36% identical at the level of amino acid sequence, 1A06), phosphorylase kinase (30%, 2PHK) and cyclic AMP-dependent protein kinase (29%, 1ATP). This resulted in a model that consisted of residues 64-327 for the minimal kinase domain of MK-2. Residues 64-142 were assigned to be part of the N-terminal lobe of MK-2 and residues 143-327 were designated as the C-terminal domain.

[0052] The homology model was then used as the search model for molecular replacement using several program suites including X-PLOR, AMORE and EPMR. In order to arrive at a consistent solution, molecular replacement calculations were repeated by varying several of the parameters including: resolution of the data, Patterson vector length, B-factor of the model, the number of molecules per asymmetric unit and space group (F432 or F4132). The high symmetry of the crystal lattice (face-centered cubic lattice) and the relatively high solvent content of the crystals (72%) presented significant technical challenges to the molecular replacement calculations. Of the three program suites used, only program EPMR (Kissinger C R, Gehlhaar D R and Fogel D B Acta Crystallogr (1999) D55, 484-491) was successful in arriving at a consistent and reasonable solution to the three rotation and three translation variables. Better results were obtained with a poly-alanine template of the homology model where all the non-glycine amino acids were truncated back to alanine.

[0053] For the successful molecular replacement calculation replacement calculation using EPMR, diffraction data in the resojution range 15-4 angstroms was used. The top solution had a correlation coefficient of 0.522 and an R-factor of 54.2%. The peak height of the top solution was 14.2 sigma where sigma is the root mean square fluctuation in the correlation function between Fobs and Fcalc. The rotation and translation parameters for the top solution are listed below for the two domains of MK-2.

Domain	Alpha	Beta	Gamma	X	Y	Z
N-term	187.60	153.98	96.51	88.88	251.12	108.02
C-term	172.99	151.99	81.30	88.17	250.39	108.21

[0054] The N- and C-terminal domains of MK-2 homology were rotated approximately 11 degrees relative to those in the homology model.

[0055] Once phase information is obtained, it is combined with the diffraction data to produce an electron density map, an image of the electron clouds that surround the molecules in the unit cell. The higher the resolution of the data, the more distinguishable are the features of the electron density map, e.g., amino acid side chains and the positions of carbonyl oxygen atoms in the peptide backbones, because atoms that are closer together are resolvable. A model of the macromolecule is then built into the electron density map with the aid of a computer, using as a guide all available information, such as the polypeptide sequence and the established rules of molecular structure and stereochemistry. Interpreting the electron density map is a process of finding the chemically realistic conformation that fits the map precisely.

[0056] After a model is generated, the structure is refined. Refinement is the process of minimizing the function Φ, which is the difference between observed and calculated intensity values (measured by an R-factor), and which is a function of the position, temperature factor, and occupancy of each non-hydrogen atom in the model. This usually involves alternate cycles of real space refinement, i.e., calculation of electron density maps and model building, and reciprocal space refinement, i.e., computational attempts to improve the agreement between the original intensity data and intensity data generated from each successive model. Refinement ends when the function Φ converges on a minimum wherein the model fits the electron density map and is stereochemically and conformationally reasonable. During refinement, ordered solvent molecules are added to the structure. The transformed coordinates of the MK-2 homology model were used as the initial model for crystallographic refinement. A number of different crystallographic refinement protocols were evaluated. The best result was obtained with a dynamic torsion angle refinement procedure where the model was assigned an initial temperature of 2500 Kelvin. The R-factor and the Rfree at the end of refinement were 24.7% and 30.7% respectively.

[0057] With the best solution from the molecular replacement calculations, an initial model of MK-2 was constructed using the homology model. This model was then subjected to several rounds of crystallographic refinement. An electron density map was then calculated. Well-defined electron density was visible for AMP-PNP at the ATP site of MK-2 as shown in FIG. 3.

[0058] Well-connected electron density was also observed for the glycine flap region (residues 71-76), presumably due to strong interactions with AMP-PNP. In addition, electron density was present for several of the missing amino acid residues in some of the loops that were excluded from the homology model.

[0059] In an iterative fashion as described before, the MK-2 model was gradually improved by including more atoms into the structure. The N-terminus was extended all the way to residue 45, the fist amino acid residue of MK-2 construct that was used for crystallization. Similarly, the C-terminus was extended to residue 351. This includes part of the auto-inhibitory domain of MK-2. The R-factor and Rfree at the end of final refinement were 24.7% and 30.7% (8.0-3.0 A resolution) respectively. The following amino acids have been excluded from the current model since they could not be clearly located in the electron density: 156-157, 216-226, 268-274 and 352-371. In addition, the following residues have been modeled as alanine since their side chains could not be identified unambiguously: Arg 153, Asp 155, Lys 197, Met 275, Lys 276, Ile 277, Arg 278, Glu 309, Pro 310, Thr 311, Gln 312, Ser 328, Thr 329, Lys 330, Val 331, Pro 332, Gly 333, Thr 334, Pro 335, Leu 336, His 337, Thr 338, Ser 339, Arg 340, Val 341, Leu 342, Lys 343, Glu 344, Asp 345, Lys 346, Glu 347, Arg 348, Trp 349, Glu 350 and Asp 351.

[0060] The ATP-analogue, AMP-PNP, binds in a narrow pocket at the ATP site of MK-2. The ATP binding site is defined by amino acid residues (within a radius of 8.0 A around AMP-PNP): 69-80, 90-95, 104, 108, 118-119, 136-147, 184-195, 204-210, and 224-226. Specifically, amino acid residues 69-80 are: Val 69, Leu 70, Gly 71, Leu 72, Gly 73, Ile 74, Asn 75, Gly 76, Lys 77, Val 78, Leu 79, and Gln 80. Amino acid residues 90-95 are: Phe 90, Ala 91, Leu 92, Lys 93, Met 94, and Leu 95. Amino acid residues 104 and 108 are Glu 104 and His 108 and amino acid residues 118-119 are Val 118 and Arg 119. The segment 136-147 contains the following amino acids: Ile 136, Val 137, Met 138, Glu 138, Cys 140, Leu 141, Asp 142, Gly 143, Gly 144, Glu 145, Leu 146, and Phe 147. The peptide segment 184-195 consists of the amino acids: His 184, Arg 185, Asp 186, Val 187, Lys 188, Pro 189, Glu 190, Asn 191, Leu 192, Leu 193, Tyr 194, and Thr 195. Amino acid residues 204-210 are: Lys 204, Leu 205, Thr 206, Asp 207, Phe 208, Gly 209, and Phe 210.

[0061] The adenine ring of AMP-PNP forms hydrogen bonding interactions with the peptide backbone of residues Glu 139 and Leu 141. In addition, the bicyclic ring of adenine forms close contacts with residues Ala 91, Met 138, Cys 140, Val 118, Leu 70, and Val 78. The ribose sugar of AMP-PNP interacts with residues, Gly 71, Leu 72, Glu 145, and Leu 193. The triphosphate moiety is surrounded by amino acid residues, Leu 72, Gly 73, Ile 74, Asn 75, Val 78, Asp 207, Lys 93, Lys 188, Asn 191, Glu 190, and Thr 206. The auto-inhibitory domain of MK-2 folds back on the protein and approaches the binding sites for ATP and the peptide substrate. As a result, the ATP binding site is constricted even further.

[0062] The atomic structure coordinates and machine readable media of the invention have a variety of uses. The present invention encompasses the structure coordinates and other information, e.g., amino acid sequence, connectivity tables, vector-based representations, temperature factors, etc., used to generate the three-dimensional structures of the polypeptides for use in the software programs described below and other software programs. For example, the coordinates listed in Table 3 are useful for solving the three-dimensional crystal or solution structures of other proteins to high resolution. MK-2 can be crystallized in a diffraction lattice of other homologous proteins.

[0063] Additionally, the invention encompasses machine readable media embedded with the three-dimensional structures of the models described herein, or with portions thereof. As used herein, “machine readable medium” refers to any medium that can be read and accessed directly by a computer or scanner. Such media include, but are not limited to: magnetic storage media, such as floppy discs, hard disc storage medium and magnetic tape; optical storage media such as optical discs or CD-ROM; electrical storage media such as RAM or ROM; and hybrids of these categories such as magnetic/optical storage media. Such media further include paper on which is recorded a representation of the atomic structure coordinates, e.g., Cartesian coordinates, that can be read by a scanning device and converted into a three-dimensional structure with an Optical Character Recognition (OCR).

[0064] A variety of data storage structures are available to a skilled artisan for creating a computer readable medium having recorded thereon the atomic structure coordinates of the invention or portions thereof and/or X-ray diffraction data. The choice of the data storage structure will generally be based on the means chosen to access the stored information. In addition, a variety of data processor programs and formats can be used to store the sequence and X-ray data information on a computer readable medium. Such formats include, but are not limited to, Protein Data Bank (“PDB”) format (Research Collaboratory for Structural Bioinformatics; http://www.rcsb.org/pdb/docs/format/pdbguide2.2/guide2.2_frame.html); Cambridge Crystallographic Data Centre format (http://www.ccdc.cam.ac.uk/support/csd_doc/volume3/z323.html); Structure-data (“SD”) file format (MDL Information Systems, Inc.; Dalby et al., 1992, J. Chem. Inf. Comp. Sci. 32:244-255), and line-notation, e.g., as used in SMILES (Weininger, 1988, J. Chem. Inf. Comp. Sci. 28:31-36). Methods of converting between various formats read by different computer software will be readily apparent to those of skill in the art, e.g., BABEL (v. 1.06, Walters & Stahl, © 1992, 1993, 1994; http://www.brunel.ac.uk/departments/chem/babel.htm.) All format representations of the polypeptide coordinates described herein, or portions thereof, are contemplated by the present invention. By providing computer readable medium having stored thereon the atomic coordinates of the invention, one of skill in the art can routinely access the atomic coordinates of the invention, or portions thereof, and related information for use in modeling and design programs, described in detail below.

[0065] While Cartesian coordinates are important and convenient representations of the three-dimensional structure of a polypeptide, those of skill in the art will readily recognize that other representations of the structure are also useful. Therefore, the three-dimensional structure of a polypeptide, as discussed herein, includes not only the Cartesian coordinate representation, but also all alternative representations of the three-dimensional distribution of atoms. For example, atomic coordinates may be represented as a Z-matrix, wherein a first atom of the protein is chosen, a second atom is placed at a defined distance from the first atom, a third atom is placed at a defined distance from the second atom so that it makes a defined angle with the first atom. Each subsequent atom is placed at a defined distance from a previously placed atom with a specified angle with respect to the third atom, and at a specified torsion angle with respect to a fourth atom. Atomic coordinates may also be represented as a Patterson function, wherein all interatomic vectors are drawn and are then placed with their tails at the origin. This representation is particularly useful for locating heavy atoms in a unit cell. In addition, atomic coordinates may be represented as a series of vectors having magnitude and direction and drawn from a chosen origin to each atom in the polypeptide structure. Furthermore, the positions of atoms in a three-dimensional structure may be represented as fractions of the unit cell (fractional coordinates), or in spherical polar coordinates.

[0066] Additional information, such as thermal parameters, which measure the motion of each atom in the structure, chain identifiers, which identify the particular chain of a multi-chain protein or protein co-complex in which an atom is located, and connectivity information, which indicates to which atoms a particular atom is bonded, is also useful for representing a three-dimensional molecular structure.

[0067] Uses of the Atomic Structure Coordinates: Drug Design

[0068] Structural information, often in the form of atomic structure coordinates, may also be used in a variety of molecular modeling and computer-based screening applications to, for example, design variants that have altered biological properties or to computationally design, screen for and/or identify compounds that bind to the MK-2 protein or to fragments of the MK-2 protein. Such compounds may be used as lead compounds in pharmaceutical efforts to identify compounds that may be useful as drugs in the treatment of inflammatory diseases or inflammation.

[0069] Thus, in a further aspect of the invention, the data from the crystal structure of MK-2 is used to evaluate compounds for their utility as drugs. These methods comprise designing and synthesizing candidate compounds using the atomic coordinates of the three dimensional structure of such co-crystals and screening for its utility in various pharmaceutical applications. Examples of such pharmaceutical applications include the treatment of inflammation, inflammatory disease states, and related conditions.

[0070] In one embodiment, the co-crystals and structure coordinates obtained therefrom are useful for identifying and/or designing compounds that inhibit MK-2 as an approach towards developing new therapeutic agents for inflammation and inflammatory disease states. For example, a high resolution X-ray structure will often show the locations of ordered solvent molecules around the protein, and in particular at or near putative binding sites on the protein. This information can then be used to design molecules that bind at these sites, which then could be synthesized and tested for binding in biological assays. (Travis, 1993, Science 262:1374)

[0071] In another embodiment, the structures are probed with a plurality of molecules to determine their ability to bind to the MK-2 protein at various sites. Such compounds can be used as targets or leads in medicinal chemistry efforts to identify, for example, inhibitors of potential therapeutic importance in the treatment of inflammation, inflammatory disease states or other disorders.

[0072] In specific embodiments described herein, the high resolution X-ray structures of the MK-2 co-complex show details of the interactions between MK-2 and AMP-PNP. This information can be used to design molecules that bind to the sites of interaction, thereby blocking co-complex formation.

[0073] In yet another embodiment, the structures can be used to computationally screen small molecule databases for chemical entities or compounds that can bind in whole, or in part, to MK-2. In this screening, the quality of fit of such entities or compounds to the binding site may be judged either by shape complementarity or by estimated interaction energy. (Meng et al., 1992, J. Comp. Chem. 13:505-524).

[0074] The design of compounds that bind to MK-2 according to this invention generally involves consideration of two factors. First, the compound must be capable of physically and structurally associating with MK-2. This association can be covalent or non-covalent. For example, covalent interactions may be important for designing suicide or irreversible inhibitors of a protein. Non-covalent molecular interactions important in the association of MK-2 include hydrogen bonding, ionic and other polar interactions, interactions as well as van der Waals interactions. Second, the compound must be able to assume a conformation that allows it to associate with the MK-2 protein. Although certain portions of the compound will not directly participate in this association with the protein, those portions may still influence the overall conformation of the molecule. This, in turn, may have a significant impact on potency. Such conformational requirements include the overall three-dimensional structure and orientation of the chemical group or compound in relation to all or a portion of the binding site, or the spacing between functional groups of a compound comprising several chemical groups that directly interact with the protein.

[0075] The potential inhibitory or binding effect of a chemical compound on MK-2 may be analyzed prior to its actual synthesis and testing by the use of computer modeling techniques. If the theoretical structure of the given compound suggests insufficient interaction and association between it and the protein, synthesis and testing of the compound is unnecessary. However, if computer modeling indicates a strong interaction, the molecule may then be synthesized and tested for its ability to bind to the protein and inhibit its activity. In this manner, synthesis of ineffective compounds may be avoided.

[0076] An inhibitory or other binding compound of MK-2 may be computationally evaluated and designed by means of a series of steps in which chemical groups or fragments are screened and selected for their ability to associate with the individual binding pockets or interface surfaces of each of the proteins. One skilled in the art may use one of several methods to screen chemical groups or fragments for their ability to associate with MK-2. This process may begin by visual inspection of, for example, the protein/protein interfaces or the various binding sites of MK-2 on the computer screen based on the MK-2, AMP-PNP, magnesium, and SC-83598 co-complex coordinates. Selected fragments or chemical groups may then be positioned in a variety of orientations, or docked, at an individual surface of MK-2 that participates in a protein/protein interface in the co-complex or in other binding sites of MK-2. Docking may be accomplished using software such as QUANTA and SYBYL, followed by energy minimization and molecular dynamics with standard molecular mechanics forcefields, such as CHARMM and AMBER.

[0077] Specialized computer programs may also assist in the process of selecting fragments or chemical groups. These include:

[0078] 1. GRID (Goodford, 1985, J. Med. Chem. 28:849-857). GRID is available from Oxford University, Oxford, UK;

[0079] 2. MCSS (Miranker & Karplus, 1991, Proteins: Structure, Function and Genetics 11:29-34). MCSS is available from Molecular Simulations, Burlington, Mass.;

[0080] 3. AUTODOCK (Goodsell & Olsen, 1990, Proteins: Structure, Function, and Genetics 8:195-202). AUTODOCK is available from Scripps Research Institute, La Jolla, Calif.;

[0081] 4. DOCK (Kuntz et al., 1982, J. Mol. Biol. 161:269-288). DOCK is available from University of California, San Francisco, Calif.;

[0082] 5. FlexE (Clausen H, Buning C, Rarey M and Lengauer T) J. Mol. Biol. (2001) 308, 377-395. FlexE is available from Tripos, St. Louis, Mo.;

[0083] 6. Glide, Glide is available from Schrodinger, Portland, Oreg.;

[0084] 7. Gold, Jones et al. J. Mol. Biol. 245, 43-53, 1995;

[0085] 8. QXP, McMartin C, Bohacek RS. J Comput Aided Mol Des 1997 11:333-44;

[0086] 9. ICM. (http://www.molsoft.com). Available from Molsoft, San Diego, Calif.; and

[0087] 10. FlexX. [Sybl, Tripos, St. Louis, Mo.].

[0088] Once suitable chemical groups or fragments have been selected, they can be assembled into a single compound or inhibitor. Assembly may proceed by visual inspection of the relationship of the fragments to each other in the three-dimensional image displayed on a computer screen in relation to the structure coordinates of MK-2. This would be followed by manual model building using software such as QUANTA or SYBYL.

[0089] Useful programs to aid one of skill in the art in connecting the individual chemical groups or fragments include:

[0090] 1. CAVEAT (Bartlett et al., 1989, ‘CAVEAT: A Program to Facilitate the Structure-Derived Design of Biologically Active Molecules’. In Molecular Recognition in Chemical and Biological Problems', Special Pub., Royal Chem. Soc. 78:182-196). CAVEAT is available from the University of California, Berkeley, Calif.;

[0091] 2. 3D Database systems such as MACCS-3D (MDL Information Systems, San Leandro, Calif.). This area is reviewed in Martin, 1992, J. Med. Chem. 35:2145-2154); and

[0092] 3. HOOK (available from Molecular Simulations, Burlington, Mass.).

[0093] Instead of proceeding to build an inhibitor of MK-2 in a step-wise fashion one fragment or chemical group at a time, as described above, MK-2-binding compounds or inhibitors may be designed as a whole or ‘de novo’ using either an empty binding site or the surface of a protein that participates in protein/protein interactions in a co-complex, or optionally including some portion(s) of a known inhibitor(s). These methods include:

[0094] 1. LUDI (Bohm, 1992, J. Comp. Aid. Molec. Design 6:61-78). LUDI is available from Molecular Simulations, Inc., San Diego, Calif.;

[0095] 2. LEGEND (Nishibata & Itai, 1991, Tetrahedron 47:8985). LEGEND is available from Molecular Simulations, Burlington, Mass.; and

[0096] 3. LeapFrog (available from Tripos, Inc., St. Louis, Mo.).

[0097] Other molecular modeling techniques may also be employed in accordance with this invention. See, e.g., Cohen et al., 1990, J. Med. Chem. 33:883-894. See also, Navia & Murcko, 1992, Current Opinions in Structural Biology 2:202-210.

[0098] Once a compound has been designed or selected by the above methods, the efficiency with which that compound may bind to MK-2 may be tested and optimized by computational evaluation. An effective inhibitor of MK-2 must preferably demonstrate a relatively small difference in energy between its bound and free states (i.e., it must have a small deformation energy of binding). Thus, the most efficient inhibitors should preferably be designed with a deformation energy of binding of not greater than about 10 kcal/mol, preferably, not greater than 7 kcal/mol. Inhibitors may interact with the protein in more than one conformation that is similar in overall binding energy. In those cases, the deformation energy of binding is taken to be the difference between the energy of the free compound and the average energy of the conformations observed when the inhibitor binds to the protein.

[0099] A compound selected or designed for binding to or inhibiting MK-2 may be further computationally optimized so that in its bound state it would preferably lack repulsive electrostatic interaction with the target protein. Such non-complementary electrostatic interactions include repulsive charge-charge, dipole-dipole and charge-dipole interactions. Specifically, the sum of all electrostatic interactions between the inhibitor and the protein when the inhibitor is bound to it preferably make a neutral or favorable contribution to the enthalpy of binding.

[0100] Specific computer software is available in the art to evaluate compound deformation energy and electrostatic interaction. Examples of programs designed for such uses include: Gaussian 92, revision C (Frisch, Gaussian, Inc., Pittsburgh, Pa. ©p1992); AMBER, version 4.0 (Kollman, University of California at San Francisco, ©1994); QUANTA/CHARMM (Molecular Simulations, Inc., Burlington, Mass., ©1994); and Insight II/Discover (Biosym Technologies Inc., San Diego, Calif., ©1994). These programs may be implemented, for instance, using a computer workstation, as are well-known in the art. Other hardware systems and software packages will be known to those skilled in the art.

[0101] The computer-assisted methods for designing an inhibitor of MK-2 activity can be de novo or based on a candidate compound. An example of a computer-assisted method for designing an inhibitor of MK-2 activity de novo would thus involve the steps of: (1) supplying a computer modeling application with a set of structure coordinates of a molecule or molecular complex comprising at least a portion of an MK-2 or MK-2-like ATP binding site, the ATP binding site comprising the 69-80, 90-95, 104, 108, 118-119, 136-147, 184-195, 204-210, and 224-226 amino acid sequence; (2) computationally building a chemical entity represented by a set of structure coordinates; and (3) determining whether the chemical entity is an inhibitor expected to bind to or interfere with the molecule or molecular complex, wherein binding to or interfering with the molecule or molecular complex is indicative of potential inhibition of MK-2 activity.

[0102] An example of a computer-assisted method for designing an inhibitor of MK-2 activity based on a candidate compound would involve the steps of (1) supplying a computer modeling application with a set of structure coordinates of a molecule or molecular complex comprising at least a portion of an MK-2 or MK-2-like ATP binding site, the ATP binding site comprising the 69-80, 90-95, 104, 108, 118-119, 136-147, 184-195,204-210, and224-226 amino acid sequence; (2) supplying the computer modeling application with a set of structure coordinates of a chemical entity; (3) evaluating the potential binding interactions between the chemical entity and ATP binding site of the molecule or molecular complex; (4) structurally modifying the chemical entity to yield a set of structure coordinates for a modified chemical entity; and (5) determining whether the modified chemical entity is an inhibitor.

[0103] Once an inhibitor or MK-2 binding compound has been optimally selected or designed, as described above, substitutions may then be made in some of its atoms or chemical groups in order to improve or modify its binding properties. Generally, initial substitutions are conservative, i.e., the replacement group will have approximately the same size, shape, hydrophobicity and charge as the original group. One of skill in the art will understand that substitutions known in the art to alter conformation should be avoided. Such altered chemical compounds may then be analyzed for efficiency of binding to MK-2 by the same computer methods described in detail above.

[0104] An example of such a computer-assisted method for identifying an inhibitor of MK-2 activity would thus involve (1) supplying a computer modeling application with a set of structure coordinates of a molecule or molecular complex comprising at least a portion of an MK-2 or MK-2-like compound, (2) supplying the computer modeling application with a set of structure coordinates of a chemical entity; and (3) determining whether the chemical entity is an inhibitor expected to bind to or interfere with the molecule or molecular complex.

[0105] The structure coordinates of the MK-2 co-complex, or of MK-2 alone, or of portions thereof, are particularly useful to solve the structure of other co-complexes of MK-2, of mutants, of the MK-2 co-complex further complexed to another molecule, or of the crystalline form of any other protein or protein co-complex with significant amino acid sequence homology to any functional domain of MK-2.

[0106] One method that may be employed for this purpose is molecular replacement. In this method, the unknown co-crystal structure, whether it is another MK-2 co-complex, a mutant, a MK-2 co-complex that is further complexed to another molecule, or the crystal of some other protein or protein co-complex with significant amino acid sequence homology to any functional domain of one of the proteins in the co-complex crystal, may be determined using phase information from the present MK-2 co-complex structure coordinates. This method will provide an accurate three-dimensional structure for the unknown protein or protein co-complex in the new crystal more quickly and efficiently than attempting to determine such information ab initio.

[0107] If an unknown crystal form has the same space group as and similar cell dimensions to the known co-complex crystal form, then the phases derived from the known crystal form can be directly applied to the unknown crystal form, and in turn, an electron density map for the unknown crystal form can be calculated. Difference electron density maps can then be used to examine the differences between the unknown crystal form and the known crystal form. A difference electron density map is a subtraction of one electron density map, e.g., that derived from the known crystal form, from another electron density map, e.g., that derived from the unknown crystal form. Therefore, all similar features of the two electron density maps are eliminated in the subtraction and only the differences between the two structures remain. However, if the space groups and/or cell dimensions of the two crystal forms are different, then this approach will not work and molecular replacement must be used in order to derive phases for the unknown crystal form.

[0108] The techniques of X-ray diffraction can be employed in the study of the co-complexes of MK-2. This information may thus be used to optimize known inhibitors of MK-2 and more importantly, to design and synthesize novel classes of inhibitors of MK-2.

[0109] Subsets of the atomic structure coordinates can also be used in any of the above methods. Particularly useful subsets of the coordinates include, but are not limited to, coordinates of single domains, coordinates of residues lining an active site, coordinates of residues that participate in important protein-protein contacts at an interface, and Cα coordinates. For example, the coordinates of one domain of a protein that contains the active site may be used to design inhibitors that bind to that site, even though the protein is fully described by a larger set of atomic coordinates. Therefore, as described in detail for the specific embodiments, below, a set of atomic coordinates that define the entire polypeptide chain, although useful for many applications, do not necessarily need to be used for the methods described herein.

[0110] Uses of Subsets of Atomic Coordinates in Specific Embodiments

[0111] The structure coordinates of the present invention, and subsets thereof, are useful for designing or screening for compounds that bind to the MK-2 protein. The high resolution X-ray structure of the co-complexes of the present invention show details of the interactions between MK-2 and AMP-PNP. This information can be used to design and/or screen for compounds that act as inhibitors of MK-2, thereby inhibiting the biosynthesis of TNF-α at a post-transcriptional level.

[0112] Those of skill in the art will recognize that the complete set of MK-2 co-complex structure coordinates will be useful in the methods of the present invention. Those of skill in the art will further recognize that the coordinates of the MK-2 co-complex will be useful separate from the coordinates of the MK-2 protein. In addition, those of skill in the art will recognize that subsets of the structure coordinates of the MK-2 protein, such as the coordinates of a single domain or interface or binding pocket, will be useful in the methods of the invention, as discussed in more detail below.

[0113] Using the techniques for solving the structure of MK-2 described above, it has been determined that the ATP-analogue binds in a narrow pocket at the ATP site of MK-2. The ATP binding site is defined by amino acid residues (within a radius of 8.0A around AMP-PNP/Mg2+): 69-80, 90-95, 104, 108, 118-119, 136-147, 184-195, 204-210, and 224-226. Thus, the MK-2 coordinates, or a subset of the MK-2 coordinates at the ATP site of MK-2, are useful for designing and/or screening for compounds that disrupt the binding at the ATP site of MK-2. Such a compound could potentially be useful in disrupting the binding of ATP, ATP analogues, or other unrelated ligands to MK-2. A subset of MK-2 coordinates useful for this embodiment of the invention include those of amino acid residues 69-80, 90-95, 104, 108, 118-119, 136-147, 184-195, 204-210, and 224-226.

[0114] The adenine ring of AMP-PNP forms hydrogen bonding interactions with the peptide backbone of residues Glu 139 and Leu 141. In addition, the bicyclic ring of adenine forms close contacts with residues, Ala 91, Met 138, Cys 140, Val 118, Leu 70, and Val 78. The ribose sugar of AMP-PNP interacts with residues, Gly 71, Leu 72, Glu 145, and Leu 193. The triphosphate moiety is surrounded by amino acid residues, Leu 72, Gly 73, Ile 74, Asn 75, Val 78, Asp 207, Lys 93, Lys 188, Asn 191, Glu 190 and Thr 206. To the extent that these physical interactions assist in the formation or stabilization of the MK-2 co-complex, the MK-2 coordinates, or a subset of the MK-2 coordinates at these sites of MK-2, are useful for designing and/or screening for compounds that disrupt the stabilization and consequently possibly the formation of co-complexes of MK-2 and ATP analogues. A subset of MK-2 coordinates useful for this embodiment of the invention as it relates to the hydrogen bonding interactions with the adenine ring of AMP-PNP include those of amino acid residues Glu 139 and Leu 141. A subset of MK-2 coordinates useful for this embodiment of the invention as it relates to the contacts formed by the bicyclic ring of adenine include those of Ala 91, Met 138, Cys 140, Val 118, Leu 70, and Val 78. A subset of MK-2 coordinates useful for this embodiment of the invention as it relates to interactions with the ribose sugar of AMP-PNP include those of amino acid residues Gly 71, Leu 72, Glu 145, and Leu 193. A subset of MK-2coordinates useful for this embodiment of the invention as it relates to interactions with the triphosphate moiety include those of Leu 72, Gly 73, Ile 74, Asn 75, Val 78, Asp 207, Lys 93, Lys 188, Asn 191, Glu 190 and Thr 206.

[0115] The following examples illustrate the invention, but are not to be taken as limiting the various aspects of the invention so illustrated.

EXAMPLES

Example 1

[0116] Generation of MK-2 Protein

[0117] The specific MK-2 sequence (listed in FIG. 4) was used as a fusion protein with glutathiones transferase (GST) for expression in E-coli.

Example 2

[0118] Protein Purification

[0119] Human MK-2 (45-371) was expressed as a GST fusion protein in E. coli BL21(LysS) cells. 500 g E. coli cell paste was suspended into 2L PBS and sonnicated using a microfluidizer under 10,000 psi pressure. The lysate was centrifuged twice at 11,300×g and the supernatant was collected each time. The supernatant was bound with 100 ml 50% PBS washed glutathione resin for 45 min at 4-8° C. The resin was washed with 10 column volumes of PBS with 1% Triton X-100, then 20 column volumes of PBS. To cleave the GST-tag, the resin was then mixed with 2500 Units of thrombin protease for 4 hours at room temperature. PMSF, DTT and glycerol were then added. The eluate was buffer exchanged against 40× its volume of dialysis buffer (50 mM Tris, pH 8.8, 2mM DTT, 5% glycerol). The dialyzed material was run over a MonoQ column using a 0-25 mM NaCl gradient over 20 column volumes (buffer A: 50 mM Tris, pH 8.8, 2 mM DTT, 5% glycerol; buffer B: same as buffer A except with 1 M NaCl). The most pure MK-2 (>98%) eluted at the front peak of ˜15 mM NaCl. This material was concentrated to 1-15 mg/mL in a Centricon protein concentrator or (MWCO=10 kD) and used in crystallization experiments.

Example 3

[0120] Crystallization of MK-2

[0121] Crystals of MK-2(45-371) were grown by the sitting drop method of vapor diffusion at room temperature. A protein solution consisting of 1.5-15 mg/mL MK-2(45-371) in 50 mM Tris, pH 8.5-8.8, or 50 mM MES pH 6-6.3, 15 mM NaCl, 2 mM DTT, and 5% glycerol was mixed in a 1:1 ratio with a reservoir solution containing 1.6-2.6M ammonium sulfate and 100 mM sodium acetate, pH 4.2-5.4, or citrate pH 3.8-6.2. Small bipyramidal or prism-shaped crystals appeared in the drops in 1-2 days and grew to as large as 0.4 mm×0.4 mm over 1-3 weeks. The crystal structure was solved using crystals of MK-2 grown in the presence of a non-hydrolysable ATP analog (AMP-PNP), a 13-mer inhibitor peptide (SC-83598) and MgCl2. This ternary complex was formed using enzyme/peptide/Mg2+/AMP-PNP molar ratios of 1:3:5:20, in a manner similar to that used in crystallizing a ternary complex of c-AMP-dependent protein kinase, as described by Zheng et al. in Crystal Structure of the Catalytic Subunit of cAMP-Dependent Protein Kinase Complexed with MgATP and Peptide Inhibitor, Biochemistry, 1993, Vol.32, No. 9, pages 2154-2161, 2155. Initial crystals of the MK-2 complex diffracted typically to 4-5 Angstroms at the Advanced Photon Source at Argonne National Laboratory. Crystallization additive screen kits from Hampton Research were employed to identify additives which, when added to the aforementioned crystallization conditions, improved the diffraction of the resulting crystals to 3.0 Angstroms.

Example 4

[0122] MK-2 Structure Determination

[0123] Square-bipyramidal crystals of MK-2 were obtained as described in Example 2. These crystals belong to the space group F4132 (Space group No. 210) with face-centered cubic lattice and contain a single copy of the ternary complex in the asymmetric unit. The unit cell parameters are about 254.8 Angstroms along the three edges. The presence of additive improved the diffraction resolution to 3.0 Angstroms. Complete diffraction data has been obtained from several crystals of the putative ternary complex using synchrotron X-rays of Beamline 17ID at the Advanced Photon Source of the Argonne National Lab in Darian, Ill. The crystals were flash frozen in liquid nitrogen. A summary of the data set from individual crystals appears in Table 2, reproduced below.

TABLE 2
Summary of Diffraction Data From MK-2 Crystals
	Data Set	Crystal (1)	Crystal (2)	Crystal (3)
	Resolution (A)	40.0 − 3.0	40.0 − 3.3	40.0 − 3.3
	Rsymm	7.7	8.6	7.6
	Completeness	94.4	97.4	96.6
	Redundancy	6.0	7.1	4.8
	Cell edge (A)	254.0	253.5	253.5

[0124] Merging of diffraction data from different crystals results in a complete data set (99.8% complete with an overall R merge of 5.6%).

[0125] A homology model of MK-2 was constructed using the structures of cyclic-AMP dependent protein kinase (1ATP), the calmodulin-dependent protein kinase (1Ao6) and the phosphorylase kinase (2PHK). This resulted in a model of MK-2 that comprised of residues of 64-327 for the minimal kinase domain. The homology model was used as a search model for molecular replacement using the program EPMR. Better results were obtained with a poly-alanine template of the homology model where all the non-glycine amino acids were truncated back to alanine. Residues 64-142 were assigned to be part of the N-terminal lobe of MK-2 and residues 143-327 were designated as the C-terminal domain. Diffraction data in the resolution range 15-4.0 A were used for the molecular replacement calculations. The top solution had a correlation coefficient of 0.522 and an R-factor of 54.2%. The peak height of the top solution was 14.2 sigma where sigma is the root mean square fluctuation in the correlation function between Fobs and Fcalc. The rotation and translation parameters for the top solution are listed below for the two domains of MK-2.

Domain	Alpha	Beta	Gamma	X	Y	Z
N-term	187.60	153.98	96.51	88.88	251.12	108.02
C-term	172.99	151.99	81.30	88.17	250.39	108.21

[0126] The N- and C-terminal domains of MK-2 homology were rotated approximately 11 degrees relative to those in the homology model. The transformed coordinates of the MK-2 homology model were used as the initial model for crystallographic refinement. A number of different crystallographic refinement protocols were evaluated. The best result was obtained with a dynamic torsion and refinement procedure where the model was assigned an initial temperature of 2500 Kelvin. The R-factor and the R-free at the end of refinement were 24.7% and 30.7% respectively. An overall structure of MK-2 with the ligand, AMP-PNP, is shown in FIG. 1.

[0127] An electron density map was calculated at this stage. Well-defined electron density is visible for AMP-PNP and Mg2+ at the ATP site of MK-2 as shown in FIG. 3. In addition, electron density is visible for missing amino acids in some of the loop regions that were excluded from the initial model.

[0128] The ATP-analogue binds in a narrow pocket at the ATP site of MK-2. The ATP binding site is defined by amino acid residues (within a radius of 8.0A around AMP-PNP/Mg2+): 69-80, 90-95, 104, 108, 118-119, 136-147, 184-195, 204-210, and 224-226 Well-connected electron density is observed for the glycine flap region (71-76), presumable due to strong interactions with AMP-PNP. The adenine ring of AMP-PNP forms hydrogen bonding interactions with the peptide backbone of residues Glu 139 and Leu 141. In addition, the bicyclic ring of adenine forms close contacts with residues, Ala 91, Met 138, Cys 140, Val 118, Leu 70, and Val 78. The ribose sugar of AMP-PNP interacts with residues, Gly 71, Leu 72, Glu 145, and Leu 193. The triphosphate moiety is surrounded by amino acid residues, Leu 72, Gly 73, Ile 74, Asn 75, Val 78, Asp 207, Lys 93, Lys 188, Asn 191, Glu 190 and Thr 206. The auto-inhibitory domain of MK-2 folds back on the protein and approaches the binding sites for ATP and the peptide substrate. As a result, the ATP binding site is constricted even further.

Claims

1. Crystalline MK-2.

2. The crystalline MK-2 of claim 1 wherein said MK-2 is human MK-2.

3. The crystalline MK-2 of claim 1 wherein said MK-2 is crystallized with a crystallization additive selected from the group consisting of cobaltous chloride hexahydrate, magnesium chloride, strontium chloride hexahydrate, yttrium chloride hexahydrate, ethanol, methanol, trimethylamine hydrochloride, urea, EDTA sodium salt, NAD+, D(+) flucose, spermidine, spermidine-tetra-HCl, glycine, glycyl-glycyl-glycine, dimethyl sulfoxide, sodium fluoride, tert-butanol, 1,3-propanediol, n-propanol, acetone, dichloromethane, 1,4-dithio-DL-threitol, C12E8, n-dodecyl-D-maltoside, TRITON X-100, deoxy-BigChap, Anapoe® X-114, Anapoe® C13E8, C-HEGA-8™, n-hexadecyl-D-maltoside, n-tetradecyl-D maltoside, n-tridecyl-D maltoside, FOS-Choline® 9, and Cymal® −1.

4. The crystalline MK-2 of claim 1 wherein said MK-2 is crystallized with a crystallization additive selected from the group consisting of deoxy-BigChap, n-hexadecyl-beta-D-maltoside, Yttrium chloride hexahydrate, and n-tridecyl-beta-D-maltoside.

5. The crystalline MK-2 of claim 1 wherein said MK-2 is crystallized with deoxy-BigChap.

6. The crystalline MK-2 of claim 1 wherein said MK-2 is crystallized with n-hexadecyl-beta-D-maltoside.

7. The crystalline MK-2 of claim 1 wherein said MK-2 is crystallized with Yttrium chloride hexahydrate.

8. The crystalline MK-2 of claim 1 wherein said MK-2 is crystallized with n-tridecyl-b eta-D-maltoside.

9. A human MK-2 construct comprising SEQ ID No. 1.

10. A human MK-2 construct comprising SEQ ID No. 1 and conservative substitutions thereof.

11. A crystalline composition comprising MK-2 in association with an additional species in a co-complex.

12. The crystalline composition of claim 11 wherein the additional species comprises an ATP analogue.

13. The crystalline composition of claim 12 wherein said ATP analogue is AMP-PNP.

14. A composition which comprises MK-2 polypeptide molecules arranged in a crystalline manner in a space group F4132, so as to form a unit cell of dimensions a=b=c= about 252 to about 256 angstroms, which effectively diffracts X-rays for determination of atomic coordinates of the MK-2 polypeptide to a resolution of better than 3.5 angstroms.

15. A composition which comprises MK-2 polypeptide molecules arranged in a crystalline manner in a space group F4132, so as to form a unit cell of dimensions a=b=c= about 254.8 angstroms, which effectively diffracts X-rays for determination of atomic coordinates of the MK-2 polypeptide to a resolution of between about 2.5 to about 3.3 angstroms.

16. A model of the structure of MK-2 comprising a data set embodying the structure of the crystalline MK-2 of claim 1.

17. The model of claim 16 wherein said data set was determined by crystallographic analysis of MK-2.

18. The model of claim 16 wherein said data set embodies the entire structure of MK-2.

19. The model of claim 16 wherein said data set embodies a portion of the structure of MK-2.

20. The model of claim 19 wherein said portion is the ATP binding site of MK-2.

21. The model of claim 16 wherein said MK-2 exists in a co-complex with an ATP analogue.

22. The model of claim 21 wherein said ATP analogue is AMP-PNP.

23. A computer readable medium having stored thereon the model of claim 16.

24. A method of identifying a species which is an inhibitor of MK-2 activity comprising: (a) providing the model of claim 16;(b) studying the interaction of candidate species with such model; and (c) selecting a species which is predicted to act as said inhibitor.

25. A species identified in accordance with the method of claim 24.

26. A method of growing crystals comprising: (a) providing a solution of MK-2 polypeptide molecules; (b) providing a precipitant solution comprising about 1.6 to about 2.6M ammonium sulfate, about 80-120 mM sodium acetate and about 2-50 mM of a crystallization additive; and (c) combining the solution of MK-2 polypeptide molecules with the precipitant solution and allowing crystals of protein MK-2 to form.

27. The method of claim 26 wherein the crystals of protein MK-2 are formed in the presence of Mg2+, an ATP analogue and an inhibitor.

28. The method of claim 27 wherein the ATP analogue is AMP-PNP.

29. The method of claim 27 wherein the inhibitor is SC-83598.

30. The method of claim 26 wherein the crystallization additives are selected from the group consisting of cobaltous chloride hexahydrate, magnesium chloride, strontium chloride hexahydrate, yttrium chloride hexahydrate, ethanol, methanol, trimethylamine hydrochloride, urea, EDTA sodium salt, NAD+, D(+) flucose, spermidine, spermidine-tetra-HCl, glycine, glycyl-glycyl-glycine, dimethyl sulfoxide, sodium fluoride, tert-butanol, 1,3-propanediol, n-propanol, acetone, dichloromethane, 1,4-dithio-DL-threitol, C12E8, n-dodecyl-D-maltoside, TRITON X-100, deoxy-BigChap, Anapoe® X-114, Anapoe® C13E8, C-HEGA-8™, n-hexadecyl-D-maltoside, n-tetradecyl-D maltoside, n-tridecyl-D maltoside, FOS-Choline® 9, and Cymal −1.

31. The method of claim 26 wherein the crystallization additive comprises deoxy-BigChap, n-hexadecyl-beta-D-maltoside, Yttrium chloride hexahydrate, and n-tridecyl-beta-D-maltoside.

32. The method of claim 30 wherein the crystallization additives are present in a concentration of between about 10 to about 20 mM.

33. A method of crystallizing MK-2 wherein X-rays taken of the resulting crystal can be diffracted to a resolution of 3.5 angstroms or better.

34. The method of claim 26 wherein the X-rays taken of the resulting crystal can be diffracted to a resolution of between about 2.5 to about 3.3 angstroms.

35. A method of solving a crystal structure, the method comprising using the structure coordinates of the crystal of claim 1, or portions thereof, to solve a crystal form of a mutant, homologue, or co-complex of MK-2.

36. A method for determining the three-dimensional structure of the crystallized MK-2 protein comprising the data set of claim 16, having space group F4132, and a resolution of about 3.0 angstroms, the method comprising: (a) crystallizing the MK-2 protein from a solution containing a crystallization additive; and (b) analyzing a crystal to determine the three-dimensional structure.

37. The method of claim 36 wherein the crystallization additive is selected from the group consisting of cobaltous chloride hexahydrate, magnesium chloride, strontium chloride hexahydrate, yttrium chloride hexahydrate, ethanol, methanol, trimethylamine hydrochloride, urea, EDTA sodium salt, NAD+, D(+) flucose, spermidine, spermidine-tetra-HCl, glycine, glycyl-glycyl-glycine, dimethyl sulfoxide, sodium fluoride, tert-butanol, 1,3-propanediol, n-propanol, acetone, dichloromethane, 1,4-dithio-DL-threitol, C12E8, n-dodecyl-D-maltoside, TRITON X-100, deoxy-BigChap, Anapoe® X-114, Anapoe® C13E8, C-HEGA-8™, n-hexadecyl-D-maltoside, n-tetradecyl-D maltoside, n-tridecyl-D maltoside, FOS-Choline® 9, and Cymal −1.

38. The method of claim 29 wherein the crystallization additive is selected from the group consisting of deoxy-BigChap, n-hexadecyl-beta-D-maltoside, Yttrium chloride hexahydrate, and n-tridecyl-beta-D-maltoside.

39. A method of identifying inhibitors of MK-2 by rational drug design comprising: (a) designing a potential inhibitor that will bond with one or more amino acids in the ATP binding sequence selected from the group consisting of amino acid residues 69-80,90-95, 104, 108, 118-119, 136-147, 184-195, 204-210, and 224-226 based upon the crystal structure co-ordinates of crystalline of MK-2 of claim 1;(b) synthesizing the inhibitor; and (c) determining whether the potential inhibitor inhibits the activity of MK-2.

40. The method of claim 39 wherein said inhibitor is designed to interact with one or more amino acids in the sequence selected from the group consisting of Gly 7 1, Leu 72, Gly 73, Ile 74, Asn 75, and Gly 76.

41. The method of claim 39 wherein said inhibitor is designed to interact with one or more amino acids selected from the group consisting of Glu 139 and Leu 141.

42. The method of claim 39 wherein said inhibitor is designed to interact with one or more amino acids in the sequence selected from the group consisting of Ala 91, Met 138, Cys 140, Val 118, Leu 70, and Val 78.

43. The method of claim 39 wherein said inhibitor is designed to interact with one or more amino acids in the sequence selected from the group consisting of Gly 71, Leu 72, Glu 145, and Leu 193.

44. The method of claim 39 wherein said inhibitor is designed to interact with one or more amino acids in the sequence selected from the group consisting of Leu 72, Gly 73, Ile 74, Asn 75, Val 78, Asp 207, Lys 93, Lys 188, Asn 191, Glu 190 and Thr 206.

45. A computer-assisted method for identifying an inhibitor of MK-2 activity comprising: (a) supplying a computer modeling application with a set of structure coordinates of a molecule or molecular complex comprising at least a portion of an MK-2 or MK-2-like ATP binding site, the ATP binding site comprising amino acids 69-80, 90-95, 104, 108, 118-119, 136-147, 184-195,204-210,and224-226; (b) supplying the computer modeling application with a set of structure coordinates of a chemical entity; and (c) determining whether the chemical entity is an inhibitor expected to bind to or interfere with the molecule or molecular complex.

46. A computer-assisted method for designing an inhibitor of MK-2 activity comprising: (a) supplying a computer modeling application with a set of structure coordinates of a molecule or molecular complex comprising at least a portion of an MK-2 or MK-2-like ATP binding site, the ATP binding site comprising amino acids 69-80, 90-95, 104, 108, 118-119, 136-147, 184-195,204-210,and 224-226; (b) supplying the computer modeling application with a set of structure coordinates of a chemical entity; and (c) evaluating the potential binding interactions between the chemical entity and ATP binding site of the molecule or molecular complex; (d) structurally modifying the chemical entity to yield a set of structure coordinates for a modified chemical entity; and (e) determining whether the modified chemical entity is an inhibitor.

47. A computer-assisted method for designing an inhibitor of MK-2 activity de novo comprising: (a) supplying a computer modeling application with a set of structure coordinates of a molecule or molecular complex comprising at least a portion of an MK-2 or MK-2-like ATP binding site, the ATP binding site comprising amino acids 69-80, 90-95, 104, 108, 118-119, 136-147, 184-195,204-210, and 224-226; (b) computationally building a chemical entity represented by a set of structure coordinates; and (c) determining whether the chemical entity is an inhibitor expected to bind to or interfere with the molecule or molecular complex, wherein binding to or interfering with the molecule or molecular complex is indicative of potential inhibition of MK-2 activity.