BACKGROUND ART The peroxisome proliferator-activated receptors (PPARs) are members of the nuclear hormone receptor subfamily of transcription factors. PPARs form heterodimers with retinoid X receptors (RXRs) and these heterodimers regulate transcription of various genes. PPARs may be involved in diseases such as diabetes, obesity, atherosclerosis and cancer. This, together with the fact that PPAR activity can be modulated by drugs such as thiazolidinediones and fibrates, has instigated a huge research effort into PPARs (Desvergene, B. & Wahli, W. (1999) Endocr. Rev. 20,649- 688). For further reviews on PPARs and their medical significance, see e. g. Berger & Moller (2002) Annu. Rev. Med. 53: 409-435; Kersten, S. et al. (2000) Nature 405: 421- 424; Willson, T. M. et al. (2000) J. Med. Chem. 43: 527-550; Vamecq, J. et al. (1999) Lancet 354: 141-148.

Three PPAR isotypes have been identified: a, ß (also called 8 and NUC1) and y.

PPARa is expressed most in brown adipose tissue and liver, then kidney, heart and skeletal muscle. PPARy (GenBank Accession No. X90563) is mainly expressed in adipose tissue, and to a lesser extent in colon, the immune system and the retina.

Whereas PPARa operates in the catabolism of fatty acids in the liver, PPARy influences the storage of fatty acids in the adipose tissue. With the C/EBP transcription factors, PPARy is part of the adipocyte differentiation program that induces the maturation of pre-adipocytes into fat cells (Rosen, E. D. et al. (1999) Mol. Cell 4,611-617). Most of the PPARy target genes in adipose tissue are directly implicated in lipogenic pathways,

including lipoprotein lipase (LPL), adipocyte fatty acid binding protein (A-FABP or aP2), acyl-CoA synthase and fatty acid transport protein (FATP). Lowell (Cell 99: 239- 242; 1999) reviewed the role of PPARy in adipogenesis.

In adipose tissue, the amounts of sterol response element binding protein 1 (SREBP 1) and PPARy are elevated, probably because of regulation by insulin (Rieusset, J. et al. (1999) Diabetes 48,699-705). PPARy is a direct target gene of SREBP1 (Fajas, L. et al. (1999) Mol. Cell. Biol. 19,5495-5503), which emphasizes the cooperative and additive functions between these two types of receptor. In addition, SREBP1 may be involved in producing an endogenous ligand (probably fatty acid) for PPARy. The overall effect is stimulation of the uptake of glucose and fatty acids, and their subsequent conversion to triglycerides.

Metabolic disorders such as hyperlipidaemia, atherosclerosis, diabetes and obesity rarely occur in isolation, but are usually part of a complex phenotype of metabolic abnormalities called syndrome X. Synthetic agonists for both PPARa (fibrates) and PPARy (thiazolidinediones ; TZDs) are useful in the treatment of the diseases that are part of this syndrome. Synthetic PPARy ligands are used for their potent antidiabetic effects. In the United States, three TZDs, troglitazone (Rezulin), rosiglitazone (Avandia) and pioglitazone (Actos), are approved for use in type II diabetic patients. They bind PPARy with moderate (troglitazone) to high (rosiglitazone) affinity, so it is believed that their hypoglycaemic effect is exerted by activating PPARy.

The X-ray crystal structure of apo-PPARy LBD was reported by Nolte et al.

(1998 ; Nature 395: 137-143) and Uppenberg et al. (1998 ; J. Biol. Chem. 273: 31108- 31112). The structure revealed a total of 12 helices and a small (3-sheet of four strands.

Helix 12 was predicted to cover the predicted LBD (ligand-binding domain) pocket, which could be divided into two interconnected cavities, both of which extend into a wide surface accessible groove parallel to helix 3. Nolte et al. also reported the structure of holo-PPARy LBD in complex with rosiglitazone. This structure identified the amino acid side chains of His323, His449 and Tyr473 as being important residues for receptor- ligand interactions and it was suggested that the binding of ligands to these residues

would be critical for coactivator binding and transcriptional activation of the target gene. The structural basis for PPARy activation by ligands is reviewed by Willson et al.

(2001) Annu. Rev. Bicchem. 70: 341-367. More recent data suggest that the nature of PPARy ligands can influence the receptor binding preferences for different coactivators.

As a consequence different ligands show different physiological effects (Rochi et al.

(2001) Mol. Cell 8: 737-747). This opens up the possibility of developing"selective PPAR modulators"with tissue specific activities (Rangwala & Lazar (2002) Sci STKE Vol. 2002 (121) : PE9), in analogy with the much-studied"selective estrogen receptor modulators" (SERMs) (Shang et al. (2002) Science 295: 2465-2468).

BRIEF DESCRIPTION OF THE DRAWINGS Figure 1 illustrates the crystal structure of the compound lithium 2- [ (2, 4- dichlorobenzoyl) amino]-5-(2-thienylmethoxy) benzoate in complex with the PPARy ligand binding domain.

Figure 2 illustrates the new identified pharmacophore model represented by the compound lithium 2- [ (2, 4-dichlorobenzoyl) amino]-5- (2-thienyhnetlioxy) benzoate in its bioactive conformation.

DISCLOSURE OF THE INVENTION The present invention relates to compounds modulating PPARy by a previously unknown binding mode. Co-crystal structures of PPARy and ligands to PPARy have been determined by X-ray diffraction. The identified binding mode of the compounds reveals a novel pharmacophoric pattern for PPARy ligands with the potential to selectively modulate the binding of coactivators and activate gene transcription. The invention comprises the use of this pharmacophore model and the X-ray structure as design tools for new classes of PPARy modulators. These classes of modulators are predicted to be useful in the treatment of metabolic diseases, e. g. type II diabetes. The amino acid sequence of PPARy is shown below (SEQ ID NO: 1) and the X-ray structure atomic coordinates are provided in, e. g. , Uppenberg et al. (1998) J. Biol. Chem. 273:

31108-31112 ; see also Protein Data Bank (http ://www. rcsb. org/pdb/), code 3prg. Those of skill in the art will understand that a set of structure coordinates for a protein (e. g., PPARy), is a relative set of points that define a shape in three dimensions. Thus, it is possible that an entirely different set of coordinates could define a similar or identical shape. Moreover, slight variations in the individual coordinates will have little effect on overall shape.

Consequently, in a first aspect this invention provides a method for identifying a compound capable of selectively modulating, in particular agonizing, the activity of PPARy, said method comprising: (i) providing test compounds that fit spatially and preferentially into a PPARy ligand binding domain; (ii) screening said test compounds for binding to the PPARy ligand binding domain; and (ii) identifying a test compound that selectively modulates the activity of PPARy ; wherein said compound comprises: (a) a benzoate group wherein the aromatic ring is capable of interacting with the side chains of Ile341 and Cys285 of SEQ ID NO: 1 and the back bone atoms of Gly284 and Cys285 of SEQ ID NO : 1; (b) a carboxylate group bound to the benzoate group of (a), said carboxylate moiety being capable of interacting, by polar interaction, with the backbone amide nitrogen of residue Ser342 of SEQ ID NO: 1; preferably, the carboxylate group is stabilized by an internal hydrogen bond to an amide nitrogen on the ligand; and (c) an aromatic group bound by an amide group to the benzoate group of (a), the said aromatic group being located in a hydrophobic region and being capable of interacting with the side chains of Leu330, Ile326, Arg288, Leu333 and Met329 of SEQ ID NO : 1.

Assays to determine if a compound modulates (e. g. , stimulates or inhibits) the activity of PPARy are well known in the art and are also illustrated in the examples below.

The term"ligand binding domain, "as used herein, refers to a region of PPARy protein, that, as a result of its shape, favorably binds to a ligand (e. g. , a peptide or an

organic molecule). The ligand binding domain includes amino acids Gly284, Cys285, Arg288, Ile326, Met329, Leu330, Leu333, Ile341, and Ser342 of SEQ ID NO: 1, and its shape can be defined by atomic coordinates of these amino acids according to Table II.

The term"coordinates"refers to three-dimensional atomic coordinates derived from mathematical equations related to the experimentally measured intensities obtained upon diffraction of a mono-or polychromatic beam of X-rays by the atoms (scattering centers) of a protein or protein-ligand complex in crystal form. The diffraction data may be used to calculate an electron density map of the repeating unit of the crystal. The electron density maps can be used to establish the positions of the individual atoms within the unit cell of the crystal. Alternatively, computer programs such as XPLOR can be used to establish and refine the positions of individual atoms.

Those of skill in the art understand that a set of structure coordinates determined by X- ray crystallography is not without error. For the purposes of this invention, any set of structure coordinates for a PPARy, that have a root mean square deviation of equivalent protein backbone atoms (N, Ca, C and 0) of less than about 1. 50 A, or alternatively less than about 1. OOA when superimposed, using backbone atoms, on the structure coordinates listed herein shall be considered identical and within the scope of the invention.

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

The term"complex"refers to a protein in covalent or non-covalent association with a ligand, such ligand including, for example, a chemical entity, compound, or inhibitor, candidate drug, and the like. The term"association"refers to a condition of proximity between the ligand and the protein, or their respective portions thereof, in any appropriate physicochemical interaction.

The term"bind"or"binding"refers to non-covalent molecular interactions that include hydrogen bonding, van der Waals interactions, hydrophobic interactions, and electrostatic interactions.

The term"selective modulating"refers to those compounds modulating the activity of PPARy more than the other proteins, such as modulating the activity of PPARy at least 20% (e. g. , 30%, 50%, 80%, or 100%) more than the others.

In a preferred aspect of the invention, the PPARy ligand binding domain is based on a structural model of PPARy bound to the compound lithium 2- [ (2, 4- dichlorobenzoyl) amino]-5- (2-thienylmethoxy) benzoate, and has the pharmacophoric features shown in Table 1. The test compounds can e. g. be provided by structure-based design, or by virtual screening of compound databases using the pharmacophore described above as search pattern.

The structure-based design method is a method for optimizing interactions between a protein, e. g., PPARY, and a compound (e. g. , a test compound, a compound of formula 1) by determining and evaluating the three-dimensional structure of successive sets of protein/compound complexes. The method may incorporate computer-assisted drug design (CADD) techniques, known in the art and examples of which are delineated herein. It may begin by visual inspection of, e. g. , a PPARy ligand binding domain on the computer screen based on the atomic coordinates in Table II or other coordinates which define a similar shape. Selected fragments of a compound may then be positioned in a variety of orientations, or docked, within that binding domain as defined supra.

Docking may be accomplished using computer software, followed by energy minimization and molecular dynamics with standard molecular mechanics force fields.

Instead of proceeding to build a compound in a step-wise fashion one fragment at a time as described above, a compound may be designed as a whole or"de llOVO"using either an empty binding site or optionally including some portion (s) of a known compound (e. g. , a known binding ligand). The virtual screening is computational screening of small molecule databases for compounds that can bind in whole, or in part, to a binding domain (e. g. , a PPARy ligand binding domain). In this screening, the quality of fit of

such compounds to the binding domain may be judged either by shape complementarity or by estimated interaction energy.

Included in the invention are compounds identified by the methods as described above. In a preferred aspect, such a compound has the formula I or is a pharmaceutically acceptable salt or a prodrug form thereof, wherein Ar is a 5-or 6-membered aromatic group or a fused aromatic ring system, e. g. phenyl, imidazole or naphthyl, substituted with a group expanding into the unoccupied part of the ligand binding pocket and making hydrogen bonding interactions with one or more of the side chain of Tyr473, His323 and His449 of SEQ ID NO: 1; in this context the term"unoccupied part of the ligand binding pocket"shall mean the region of the binding pocket that is delimited by the side chains of Phe282, Cys285, His323, Tyr327, Phe363, Met364, Lys367, His449, Leu469 and Tyr473 of SEQ ID NO: 1 ; X is a bond, or a heteroalkyl chain comprising from 1 to 4 carbon atoms and from 1 to 4 heteroatoms, or a formula wherein m is 0, 1, or 2,

nisO, 1, 2, or 3, and Y is a bond, O, S, NH, NHSOa, NHC (O) NH, or CH=CH ; and R is an optionally substituted aryl or heteroaryl group.

Preferred compounds of the formula I include those wherein: The group on Ar expanding into the unoccupied part of the ligand binding pocket is selected from the group consisting of C1-6 alkyl, Ci. 6 alkoxy, Cri-6 alkylthio allyloxy, aryloxy, and arylthio; each of which ends in a carboxylic acid or bioisosteric replacement thereof, wherein the term"bioisosteric replacement"is defined as a substituent making interactions with PPARy that are analogous with a COOH moiety (e. g. , tetrazole, amide).

X is a bond; O-(CH2) n wherein n is an integer 0 to 3, e. g. O, O-CH2, or O-(CH2) 2; O-(CH2) n-Y, wherein n is an integer 0 to 3, and Y is an atom selected from O, N and S, e. g. O-(CH2)2-O, or 0- (CH2) 2-S; 0- (CH2) 2-0- (CH2) 2-NH ; 0- (CH2) 2-0- (CH2) 2-NHS02 ; or 0- (CH2) 2-0- (CH2) 2-NHCONH ; R is selected from the group consisting of, optionally substituted, phenyl, naphthyl, thienyl, pyridinyl, quinoxalinyl, benzoylphenyl, thiazolyl, furyl, imidazolyl, oxazolyl, pyrazinyl, quinolinyl, indolyl, benzofuran, benzothiophenyl (benzothienyl), pyrimidinyl, benzodioxolyl;

R is independently substituted in one or more positions with C1-6-alkyl, Cl 6-alkoxy, C1-6-alkylthio, Cl 6-acyl, cyano, nitro, hydroxy, methylhydroxy, carboxy, fluoromethyl, difluoromethyl, trifluoromethyl, difluorometlioxy, trifluoromethoxy, difluoromethylthio, trifluoromethylthio, halogen, formyl, amino, Cl 6-alkylamino, di (Cl 6-alkyl) amino or Cl 6-acylamino, aryl, aryloxy, arylthio, C1-6-alkylsulphonyl, C2-6-allyloxy, benzyloxy, benzoyl.

In particular, R can be independently substituted in one or more positions with methyl,

ethyl, isopropyl, methoxy, thiometlioxy ethoxy, methylsulfonyl, formyl, acetyl, nitro, cyano, methylhydroxy, methylamino, carboxy, trifluoromethyl, trifluoromethoxy, chloro, fluoro, bromo, iodo, benzyloxy, amino, dimethylamino, acetylamino, phenyl, phenoxy, or benzoyl.

The tenn''C1 6 alkyl"denotes a straight or branched alkyl group having from 1 to 6 carbon atoms. Examples of said C1-6 alkyl include methyl, ethyl, n-propyl, iso- propyl, n-butyl, iso-butyl, sec-butyl, t-butyl and straight-and branched-chain pentyl and hexyl.

The term''C1 6 alkoxy"denotes a straight or branched alkoxy group having from 1 to 6 carbon atoms. Examples of said Cl-6 alkoxy include methoxy, ethoxy, n- propoxy, iso-propoxy, n-butoxy, iso-butoxy, sec-butoxy, t-butoxy and straight-and branched-chain pentoxy and hexoxy.

The term"halogen"shall mean fluorine, chlorine, bromine or iodine.

The term"aryl"denotes aromatic rings (monocyclic or bicyclic) having from 6 to 10 ring carbon atoms. Examples of said aryl include phenyl, indenyl and naphthyl.

The term"heteroaryl"denotes a mono-or bicyclic ring system (only one ring need to be aromatic, and substitution may be in any ring) having from 5 to 10 ring atoms (which are carbon atoms), in which one or more of the carbon ring atoms are other than carbon, such as nitrogen, oxygen and sulfur. Examples of said heteroaryl include pyrrole, thiazole, imidazole, thiophene, furan, isothiazole, thiadiazole, oxazole, isoxazole, oxadiazole, pyridine, pyrazine, pyrimidine, pyridazine, pyrazole, triazole, tetrazole, chroman, isochroman, quinoline, quinoxaline, isoquinoline, phthalazine, quinazolineindole, indole, isoindole, isoindoline, indoline, benzothiophene, benzofuran, 2,3-dihydrobenzofuran, isobenzofuran, benzoxazole, 2,1, 3-benzoxadiazole, benzothiazole, 2,1, 3-benzothiadiazole, 2,1, 3-benzoselenadiazole, benzimidazole, indazole, 2, 3-dihydro-1, 4-benzodioxine, indane, 1,3-benzodioxole, 3, 4-dihydro-2H-1, 4- benzoxazine, 1,5-naphthyridine, and 1,8-naphthyridine.

The term"heteroalkyl chain"denotes a straight or branched, saturated or unsaturated, chain comprising from 1 to 4 carbon atoms and from 1 to 4 heteroatoms selected from the group consisting of O, N, and S. The heteroatom (s) may be placed at any position of the heteroalkyl group.

Depending on the process conditions, the end products of the Formula I are obtained either in neutral or salt form (e. g. , lithium, sodium, potassium salts, hydrochloride, hydrobromide, and the like).

The invention relates to a crystal of a protein-ligand complex comprising a protein-ligand complex of PPARy and a ligand (e. g. , lithium 2- [2, 4- dichlorobenzoyl) amino]-5- (2-thienylmethoxy) benzoate), wherein the crystal effectively diffracts X-rays for the determination of the atomic coordinates of the protein-ligand complex to a resolution of greater (meaning better as used in this context throughout) than 5.0 Angstroms, alternatively greater than 3.0 Angstroms, or alternatively greater than 2.0 Angstroms.

One embodiment is the crystal of described above, wherein the PPARy comprises an amino acid sequence containing amino acids amino acids Gly284, Cys285, Arg288, Ile326, Met329, Leu330, Leu333, Ile341, and Ser342 of SEQ ID NO: 1, or an amino acid sequence that differs from the amino acid sequence by only conservative substitutions, or alternatively, wherein PPARy ligand binding domain comprises the binding site as defined herein.

This invention also features a method of using the protein-ligand crystals described herein for identifying a compound that binds to a PPARy ligand binding domain. The method includes the steps of : (i) using the atomic coordinates according to Table generate a three- dimensional structure comprising a PPARy ligand binding domain; (ii) employing the three-dimensional structure to identify a compound; and (iii) determining whether the compound binds to the PPARy ligand binding domain; wherein the compound comprises: (a) a benzoate group wherein the aromatic ring is capable of interacting with the side chains of Ile341 and Cys285 of SEQ ID NO: 1 and the back bone atoms of Gly284 and Cys285 of SEQ ID NO: 1; (b) a carboxylate group bound to the benzoate group of (a), said carboxylate moiety being capable of interacting with the backbone amide nitrogen of residue Ser342 of SEQ ID NO: 1; and (c) an aromatic group bound by an amide group to the benzoate group of (a), the said aromatic group being located in a hydrophobic region and being

capable of interacting with the side chains of Leu330, Ile326, Arg288, Leu333 and Met329 of SEQ ID NO: 1.

Assays to determine if a compound binds to the PPARy ligand binding domain are well known in the art and are also illustrated in the examples below.

This invention further features a method of using the three-dimensional structure coordinates according to Table II, comprising: (a) determining structure factors from the coordinates; and (b) applying said structure factor information to a set of X-ray diffraction data obtained from a complex of another ligand and PPARy.

In one embodiment, the invention relates to a computer-readable data storage medium comprising a data storage material encoded with computer readable data, which when used by a computer programmed with instructions for using such data, displays a three-dimensional graphical representation of a molecule or molecular complex comprising a ligand binding domain defined by structure coordinates according to Table II, or a homologue of said molecule or molecular complex, wherein said homologue comprises a binding domain that has a root mean square deviation from the backbone atoms of said amino acids of SEQ ID NO : 1 less than about 1. 50A, or alternatively less than about l. 00A.

The computer may comprise a central processing unit, a working memory, for example, random access memory and/or storage memory in the form of one or more disk drives (e. g. , floppy, Zip, Jazzy), tape drives, CD-ROM drives, DVD drives, and the like, a display terminal such as for example, a cathode ray tube type or a liquid crystal type display, and input and output lines for data transmission, including a keyboard and/or mouse controller. The computer may be a stand-alone, or connected to a network and/or shared server. Data storage materials include, for example, hard drives, floppy, Zip and JazzTM type disks, tapes, CDs, and DVDs.

In another embodiment, the invention relates to a computer readable data storage material encoded with computer readable data comprising structure coordinates according to Table IILJ Alternate embodiments of the invention are those crystals described above, and methods of using such crystals or structure coordinates thereof.

Crystals of PPARy protein or protein-ligand complex can be produced or grown by a number of techniques including batch crystallization, vapor diffusion (either by sitting drop or hanging drop), soaking, and by microdialysis. Seeding of the crystals in some instances is required to obtain X-ray quality crystals. Standard micro and/or macro seeding of crystals may therefore be used. Preferably, the crystal effectively diffracts X-rays for the determination of the atomic coordinates of the protein-ligand complex to a resolution greater than 5.0 Angstroms, alternatively greater than 3.0 Angstroms, or alternatively greater than 2.0 Angstroms. Once a crystal is produced, X- ray diffraction data can be collected. The example below used standard cryogenic conditions for such X-ray diffraction data collection though alternative methods may also be used. For example, diffraction data can be collected by using X-rays produced in a conventional source (such as a sealed tube or rotating anode) or using a synchrotron source. Methods of X-ray data collection include, but are not limited to, precession photography, oscillation photography and diffractometer data collection. Data can be processed using packages including, for example, DENZO and SCALPACK (Z.

Otwinowski and W. Minor) and the like.

The three-dimensional structure of the protein or protein-ligand complex constituting the crystal may be determined by conventional means as described herein.

Where appropriate, the structure factors from the three-dimensional structure coordinates of a related protein may be utilized to aid the structure determination of the protein-ligand complex. Structure factors are mathematical expressions derived from three-dimensional structure coordinates of a molecule. These mathematical expressions include, for example, amplitude and phase information. The term"structure factors"is known to those of ordinary skill in the art. Alternatively, the three-dimensional structure of the protein-ligand complex may be determined using molecular replacement analysis.

This analysis utilizes a known three-dimensional structure as a search model to determine the structure of a closely related protein-ligand complex. The measured X- ray diffraction intensities of the crystal are compared with the computed structure factors of the search model to determine the position and orientation of the protein in the protein-ligand complex crystal. Computer programs that can be used in such analyses include, for example, X-PLOR and AmoRe (J. Navaza, Acta Crystallographics ASO, 157-163 (1994)). Once the position and orientation are known, an electron density map may be calculated using the search model to provide X-ray phases. The electron density can be inspected for structural differences and the search model may be modified to conform to the new structure. Using this approach, one may use the structure of the protein-ligand complex or complexes described herein to solve other protein-ligand complex crystal structures, particularly where the ligand is a different compound. Computer programs that can be used in such analyses include, for example, QUANTA and the like.

Upon determination of the three-dimensional structure of a crystal of a protein- ligand complex, a potential compound that binds to the protein (e. g., PPARy) may be evaluated by any of several methods, alone or in combination. Such evaluation may utilize visual inspection of a three-dimensional representation of the active site, based on the X-ray coordinates of a crystal described herein, on a computer screen.

Evaluation, or modeling, may be accomplished through the use of computer modeling techniques (including CADD methods), hardware, and software known to those of ordinary skill in the art. This may additionally involve model building, model docking, or other analysis of protein-ligand interactions using software including, for example, QUANTA or SYBYL, followed by energy minimization and molecular dynamics with standard molecular mechanics forcefields including, for example, CHARMM and AMBER. The three-dimensional structural information of a protein-ligand complex may also be utilized in conjunction with computer modeling to generate computer models of other protein-ligand complexes. Using the structure coordinates described herein, computer models of PPARy-ligand (e. g., lithium 2- [ (2, 4- dichlorobenzoyl) amino]-5-(thienylmethoxy] benzoate), may be created using standard methods and techniques known to those of ordinary skill in the art, including software packages described herein.

Once the three-dimensional structure of a crystal comprising a protein-ligand complex formed between a protein and a standard ligand for that protein is determined, a potential ligand is examined through the use of computer modeling using a docking program such as FLEX X, DOCK, or AUTODOCK (see, Dunbrack et al., Folding & Design, 2: R27-42 (1997) ), to identify potential ligands for the protein. This procedure can include computer fitting of potential ligands to the ligand binding site to ascertain how well the shape and the chemical structure of the potential ligand will complement the binding site. [Bugg et al., Scientific American, December: 92-98 (1993); West et al., TIPS, 16: 67-74 (1995) ]. Computer programs can also be employed to estimate the attraction, repulsion, and steric hindrance of the two binding partners (i. e. , the ligand- binding site and the potential ligand). Generally the tighter the fit, the lower the steric hindrances, and the greater the attractive forces, the more potent the potential drug since these properties are consistent with a tighter binding constant. Furthermore, the more specificity in the design of a potential drug, the more likely that the drug will not interact as well with other proteins. This will minimize potential side-effects due to unwanted interactions with other proteins.

A variety of methods are available to one skilled in the art for evaluating and virtually screening molecules or chemical fragments appropriate for associating with a protein. Such association may be in a variety of forms including, for example, steric interactions, van der Waals interactions, electrostatic interactions, solvation interactions, charge interactions, covalent bonding interactions, non-covalent bonding interactions (e. g. , hydrogen-bonding interactions), entropically or enthalpically favorable interactions, and the like.

Numerous computer programs are available and suitable for rational drug design and the processes of computer modeling, model building, and computationally identifying, selecting and evaluating potential inhibitors in the methods described herein. These include, for example, GRID (available form Oxford University, UK), MCSS (available from Molecular Simulations Inc. , Burlington, MA), AUTODOCK (available from Oxford Molecular Group), FLEX X (available from Tripos, St. Louis.

MO), DOCK (available from University of California, San Francisco), CAVEAT

(available from University of California, Berkeley), HOOK (available from Molecular Simulations Inc. , Burlington, MA), and 3D database systems such as MACCS-3D (available from MDL Information Systems, San Leandro, CA), UNITY (available from Tripos, St. Louis. MO), and CATALYST (available from Molecular Simulations Inc., Burlington, MA). Potential inhibitors may also be computationally designed"de novo" using such software packages as LUDI (available from Biosym Technologies, San Diego, CA), LEGEND (available from Molecular Simulations Inc., Burlington, MA), and LEAPFROG (Tripos Associates, St. Louis, MO). Compound deformation energy and electrostatic repulsion, may be evaluated using programs such as GAUSSIAN 92, AMBER, QUANTA/CHARMM, AND INSIGHT II/DISCOVER. These computer evaluation and modeling techniques may be performed on any suitable hardware including for example, workstations available from Silicon Graphics, Sun Microsystems, and the like. These techniques, methods, hardware and software packages are representative and are not intended to be comprehensive listing. Other modeling techniques known in the art may also be employed in accordance with this invention. See for example, N. C. Cohen, Molecular Modeling in Drug Design, Academic Press (1996) (and references therein), and software identified at internet sites including the CAOS/CAMM Center Cheminformatics Suite at http://www. caos. kun. nl/, and the NIH Molecular Modeling Home Page at http://www. fi. muni. cz/usr/mejzlik/mirrors/molbio. info. nih. gov/modeling/software_list/.

A potential compound that binds to PPARy and modulates PPARy activities is selected by performing rational design with the three-dimensional structure (or structures) determined for the crystal described herein, especially in conjunction with computer modeling and methods described above. The potential compound is then obtained from commercial sources or is synthesized from readily available starting materials using standard synthetic techniques and methodologies known to those of ordinary skill in the art. The potential compound is then assayed to determine its ability to modulate PPARy activities.

The potential compound selected or identified by the aforementioned process may be assayed to determine its ability to modulate (e. g., inhibit or stimulate) PPARy activity. The assay may be in vitro or in vivo. Modulation can be measured by various

methods, including, for example, those methods illustrated in the examples below. The compounds described herein may be used in assays, including radiolabelled, antibody detection and fluorometric, for the isolation, identification, or structural or functional characterization. The assay may be a protein inhibition assay, utilizing a full length or truncated protein, said protein having sequence homology with that of mammalian origin, including for example, human, murine, rat, and the like. The protein is contacted with the potential inhibitor and a measurement of the binding affinity of the potential inhibitor against a standard is determined. Such assays are known to one of ordinary skill in the art. The assay may also be a cell-based assay. The potential compound is contacted with a cell and a measurement of inhibition of a standard marker produced in the cell is determined. Cells may be either isolated from an animal, including a transformed cultured cell, or may be in a living animal. Such assays are also known to one of ordinary skill in the art.

When suitable potential compounds are identified as described above, a supplemental crystal can be produced or grown (using techniques described herein) that comprises a protein-ligand complex formed between a protein (e. g., PPARy) and the potential ligand. Preferably, the crystal effectively diffracts X-rays for the determination of the atomic coordinates of the protein-ligand complex to a resolution greater than 5.0 Angstroms, alternatively greater than 3.0 Angstroms, or alternatively greater than 2.0 Angstroms. The three-dimensional structure of the protein-ligand complex constituting the supplemental crystal may be determined by conventional means such as those described herein.

The potential compound described above is selected by performing rational drug design with the three-dimensional structure (or structures) determined for the supplemental crystal, especially in conjunction with computer modeling described above. The potential compound is then obtained from commercial sources or is synthesized from readily available starting materials using standard synthetic techniques and methodologies known to those of ordinary skill in the art. The potential compound is then assayed to determine its ability to modulate PPARy activities.

For all potential compound (agonist, antagonist) screening or assay methods described herein, further refinements to the structure of the potential compound may generally be necessary and can be made by successive iterations of any/or all of the steps provided by the screening assay method.

Once the potential compound is determined to bind to PPARy protein and to modulate its activities, the compound may be useful in therapeutic or prophylactic treatment of mammals, including man, for conditions where modulation of either PPARa or PPARy activity, or the combination of both PPARa and PPARy activities.

Such conditions could be e. g. diabetes, diabetes mellitus type 2, insulin resistance, impaired glucose tolerance and/or in combinations with dyslipidemias, obesity, atherosclerosis, coronary artery disease, PCOS, gestational diabetes, or inflammation.

The compounds described above are particularly useful for the treatment of type II diabetes, in combination (s) with dyslipidemias, obesity, atherosclerosis and coronary artery disease. For this purpose the compounds can be used alone or in combination (s) with sulfonylureas, metformin, alpha-glycosidase inhibitors, insulin or other anti- diabetic treatments/agents. Reference to treatment is intended to include prophylaxis as well as the alleviation of established symptoms.

For clinical use, the compounds are formulated into pharmaceutical formulations for oral, rectal, parenteral or other mode of administration. Pharmaceutical formulations are usually prepared by mixing the active substance, or a pharmaceutically acceptable salt thereof, with conventional pharmaceutical excipients. The formulations can be further prepared by known methods such as granulation, compression, microencapsulation, spray coating, etc.

The formulations may be prepared by conventional methods in the dosage form of tablets, capsules, granules, powders, syrups, suspensions, suppositories or injections.

Liquid formulations may be prepared by dissolving or suspending the active substance in water or other suitable vehicles. Tablets and granules may be coated in a conventional manner. The typical daily dose of the active substance varies within a wide range and

will depend on various factors such as for example the individual requirement of each patient and the route of administration.

The compounds may also be administered as prodrugs that may be converted to the active ingredient in question after metabolic transformation iii vivo. Conventional procedures for the selection and preparation of suitable prodrug derivatives are described, for example, in"Design of Prodrugs"ed. H. Bundgaard, Elsevier, 1985.

"An effective amount"refers to an amount of a compound which confers a therapeutic effect on the treated subject (eg. , a human, a mammal, a horse, a dog, or a cat). The therapeutic effect may be objective (i. e. , measurable by some test or marker) or subjective (i. e. , subject gives an indication of or feels an effect). The dose level and frequency of dosage of the specific compound will vary depending on a variety of factors including the potency of the specific compound employed, the metabolic stability and length of action of that compound, the patient's age, body weight, general health, sex, diet, mode and time of administration, rate of excretion, drug combination, the severity of the condition to be treated, and the patient undergoing therapy. The daily dosage may, for example, range from about 0. 001 mg to about 100 mg per kilo of body weight, administered singly or multiply in doses, e. g. from about 0.01 mg to about 25 mg each. Normally, such a dosage is given orally but parenteral administration may also be chosen.

The compounds can be prepared by, or in analogy with, standard synthetic methods, and especially according to, or in analogy with, the methods described in the co-pending international patent application derived from Swedish patent application No. 0102384- 5, filed July 3, 2001.

More specifically, the compounds described above can be prepared by, or in analogy with, standard synthetic methods, and especially according to, or in analogy with, the following methods.

Method 1 Compounds of formula (I) in which X is oxygen can be prepared beginning with commercially available 2-amino-5-hydroxybenzoic acid (i) as shown in Scheme 1. The

corresponding methyl ester (ii) is formed by treatment with sulfuric acid and methanol and is subsequently coupled with a benzoyl chloride or a heteroarylcarbonyl chloride (commercially available or prepared from the corresponding carboxylic acid using thionyl chloride or oxalyl chloride) to provide the amide (iii). Reaction of (iii) with an alcohol in the presence of diethyl azodicarboxylate (DEAD) or 1, 1'-azobis (N, N- dimethylformamide) (TMAD; cf. Tetrahedron Lett. 1995, vol. 36: 3789-3792) and triphenylphosphine or polymer supported triphenylphosphine in a solvent such as dichloromethane and/or tetrahydrofuran (Mitsunobu reaction ; see Org. React. 1992, vol.

42: 335-656) gives the adduct (iv). Ester hydrolysis, using 1M lithium hydroxide, affords the target compounds (v) as lithium salts.

Scheme 1 0 O O R-OH OH OH \ H HO) OH H2SO4 ArCOCI II TMAD or DEAD Hua 2 HzN,, PPh3 or -PP ''-° DCMHF (i) (iii) 0 0 OR 1M LiOH / HN THF HN ArO ArO zu Method 2 Other compounds of the present invention can be prepared as shown in Scheme 2. The Mitsunobu reaction can also be performed on the intermediate (ii), i. e. before the amide coupling, to form the adduct (vi). Subsequent amide coupling and ester hydrolysis afford the target compounds (v).

Scheme 2 0 R-OH 0 0 OH TMAD or DEAD0 R ARCOCI R HN I PPh3 or -PPh3 HN base HN DCM/THF (vi) 0 0- 1M LiOH / TUF HAN ArO (v)

Method 3 Compounds of formula (1) in which X = Co and R is an aryl or heteroaryl substituent can be prepared as outlined in Scheme 3. Treatment of the commercially available 2-amino-5-iodobenzoic acid (vii) with trichloromethyl chloroformate in solvents such as dioxane gives the isatoic anhydride (viii) which can be further reacted with methanol and a base such as potassium carbonate to form the methyl ester (ix).

Subsequent coupling with a benzoyl chloride or a heteroarylcarbonyl chloride (commercially available or prepared from the corresponding carboxylic acid using thionyl chloride or oxalyl chloride) provides amide (x). Palladium-catalyzed cross- coupling of (x) with an aryl or heteroaryl boronic acid (Suzuki coupling; see Chem.

Rev. 1995,95, 2457-2483) gives biaryl (xii) or a mixture of (xii) and the bicycle (xi).

Subsequent ester hydrolysis using 1M lithium hydroxide solution affords the target compounds (xiii).

Scheme 3

o o i HOJ ci MEOH I ARCOCI basa H2N Dioxane o H K2CO3 H2N bTaHsj (vii) (viii) (ix) 0 0 O O O 04 (PPh3) aPd HN 2N Na2CO3 (xi) LiOH Li o WR Lion Ar 0 RB (OH) 2 0 dioxane HN DME Me0 water Ar''O (x) H N R (xiii) o 0 (xii) Method 4 Other compounds of the present invention can be prepared as shown in Scheme 4. The intermediate (iii) can be reacted with nitrogen containing heterocycles to form diaryl ethers (xiv) which can be hydrolyzed as described earlier to afford compounds (xv).

Scheme 4 o ° 0 . o. > Cl) ba e HX R > °> Han HN R DMF HN Ar 0 heat Ar O ArO (iii) (iii) (fiv) Method 5 Other compounds of the present invention can be prepared as shown in Scheme 5. Intermediate (iii) can be reacted with benzylic (or aliphatic) bromides to form

compounds (xvi) which can be hydrolyzed as described earlier to afford compounds (xvii).

Scheme 5 0 0 0 Jb bF R-Br > JW R hydrolysis Li ° XO>R JL + R-Br---- JLJ"J ! J HN DMF HN HN ArO heat Ar''O Ar''O (iii) (xvi) (xvii) The chemicals used in the above-described synthetic routes may include, for example, solvents, reagents, catalysts, protecting group and deprotecting group reagents. The methods described above may also additionally include steps, either before or after the steps described specifically herein, to add or remove suitable protecting groups in order to ultimately allow synthesis of the compounds of Formula (I). In addition, various synthetic steps may be performed in an alternate sequence or order to give the desired compounds. Synthetic chemistry transformations and protecting group methodologies (protection and deprotection) useful in synthesizing applicable compounds are known in the art and include, for example, those described in R. Larock, Comprehensive Organic Transformations, VCH Publishers (1989) ; T. W.

Greene and P. G. M. Wuts, Protective Groups in Organic Synthesis, 2 d Ed. , John Wiley and Sons (1991) ; L. Fieser and M. Fieser, Fieser and Fieser's Reagents for Organic Synthesis, John Wiley and Sons (1994); and L. Paquette, ed., Encyclopedia of Reagents for Organic Synthesis, John Wiley and Sons (1995) and subsequent editions thereof.

EXAMPLES EXAMPLE 1: Synthesis of lithium 2- [ (2, 4-dichlorobenzoyl) amino]-5-(2- thienylmethoxy) benzoate Step 1 : Metiçyl 2-amino-5-hydroxybenzoate

To a stirred suspension of 2-amino-5-hydroxybenzoic acid (15 g, 98 mmol) in methanol (100 ml) was added sulfuric acid (95%, 15 ml) at room temperature. The solution was stirred at 90°C for 3.5 hours after which it was allowed to reach room temperature and carefully poured into saturated sodium bicarbonate. Subsequent extraction with chloroform (3 x 300 ml), drying of the organic phase using magnesium sulfate and concentration iii vacuo gave the title compound (15 g, 80%) as a dark solid. mp: 154- 155°C ;'H NMR (DMSO) # 8.66 (s, 1H), 7.09 (d, J= 2.72 Hz 1H), 6. 82-6. 76 (m, 1H), 6.66-6. 60 (m, 1H), 6.07 (br s, 2H), 3.75 (s, 3H) ; 13C NMR (DMSO) 5 167.7, 146.6, 144.8, 123.6, 117.9, 114.4, 108.8, 51,4 ; MS m/z 168 (M+1).

Step 2: Methyl 2- [ (2, 4-dichlorobenzoyl) aminol-5-liydroxybenzoate

To a stirred mixture of methyl 2-amino-5-hydroxybenzoate (10 g, 60 mmol) pyridine (80 ml) and molecular sieves (4A), 2,4-dichlorobenzoyl chloride (7.6 ml, 54 mmol) in pyridine (3 ml) was added slowly at 0°C. The mixture was allowed to reach room temperature and then stirred over night. After addition of chloroform, the mixture was

filtered and the filtrate washed with 1M hydrochloric acid (3 x 150 ml) and brine, dried with magnesium sulfate and concentrated in vacuo. The residue was re-crystallized from chloroform to give the title compound (4 g, 20%) as a gray solid. mp: 181-182°C ; 1H NMR (DMSO) J 10.64 (s, 1H), 9.81 (s, 1H), 7. 92-7. 55 (m, 4H), 7.29 (d, J = 2.73 Hz 1H), 7.08-7. 02 (m, 1H), 3.79 (m, 3H); MS m/z 338 (M-1).

Step 3: Methyl 2-[(2,4-dichlorobenzoyl)amino]-5-(2-thienylmethoxy)benzoate TMAD (183 mg, 1.06 mmol) was added to a suspension of methyl 2- [ (2, 4- dichlorobenzoyl) amino] -5-hydroxybenzoate (240 mg, 0.71 mmol ; prepared in Example XX), polymer bound triphenylphosphine (480 mg, 1.4 mmol) and thiophene-2-methanol (73 p1, 0.78 mmol) in anhydrous THF (3 ml) and DCM (3 ml). The suspension was shaken at room temperature over night and filtered through a plug of Celite. The filtrate was concentrated in vacuo and the residue purified by chromatography on silica gel eluting with CHC13 to give the title compound (130 mg, 42%) as yellow oil. lH NMR (CDC13) a 11.31 (s, 1H), 8.79 (d, J = 9.40 Hz 1H), 7.67-7. 57 (m, 2H), 7.47 (d, J= 1. 98 Hz 1H), 7. 35-7. 30 (m, 2H), 7.27-7. 21 (m, 1H), 7.12-7. 09 (m, 1H), 7.02-6. 97 (m, 1H), 5.23 (s, 1H), 3. 89 (s, 3H) ; 13C NMR (CDC13) a 168.3, 164.1, 153.7, 138.7, 136.9, 135.2, 134.7, 132.3, 130.5, 130.4, 127.6, 127.2, 127.0, 126.6, 122.2, 122.0, 116.6, 166.6, 65.5, 52.7 Step 4 : Lithium 2-[(2, 4-dichlorobenzoyl) amino/-5-(2-thienylmethoxy) benzoate

Lithium hydroxide (1 M solution, 298 pi) was added at room temperature to a stirred solution of methyl 2- [ (2, 4-dichlorobenzoyl) amino]-5- (2-thienylmethoxy) benzoate (130 mg, 0.30 mmol) in THF (2 ml). The mixture was stirred over night and then concentrated in vacuo, re-dissolved in methanol and concentrated again. The residue was washed with diethyl ether to give the title compound (120 mg, 94%) as yellow solid. mp: 165-168°C ; lH NMR (CD30D) a S. 56 (d, J= 8.91 Hz 1H), 7.75 (d, J = 2.97 Hz 1H), 7.66-7. 56 (m, 2H), 7.47-7. 37 (m, 2H), 7.17-7. 13 (m, 1H), 7.08 (dd, J= 9.16, 3.22 Hz 1H), 7.02-6. 97 (m, 1H), 5.27 (s, 2H) ; 13C NMR (CD30D) a 172.5, 164.4, 154.1, 139.6, 136.2, 135.6, 133.6, 132.1, 129.9, 127.4, 126.7, 126.3, 125.9, 125.6, 120.6, 118.0, 116.9, 64.9 ; MS milz 420 (M-1).

EXAMPLE 2: Crystal structure of the PPARy ligand binding domain in complex with lithium 2- [ (2, 4-dichlorobenzoyl) amino]-5- (2-thienylmethoxy) benzoate.

The structure of the PPARy ligand-binding domain in complex with lithium 2- [ (2, 4-dichlorobenzoyl) amino]-5-(2-thienylmethoxy) benzoate (Example 1) was determined by X-ray crystallography. Standard molecular biology techniques were used to produce the ligand binding domain of human PPARy in E. coli bacterial cells. The protein was purified to homogeneity and concentrated to a final concentration of 10 mg/ml. Crystals of PPARy-LBD complexes were grown by the hanging drop diffusion method at 18°C and appeared in 3-5 days. The well solution contained 0.1 M Tris/HCl buffer, pH 7.5, 22% polyethylene glycol 3000 and 0.2 M Ca acetate. Typically 3 1ll of the precipitant was mixed with 3 pi of a solution containing 9 mg/ml PPARy-LBD, 1mM GRIP-1 co-activator peptide (KEKHKILHRLLQDS, SEQ ID NO: 2) and 1mM ligand in the drop. Crystals were mounted in glass capillaries and diffracted to 2.90 A.

All data were collected at room temperature using a Rigaku RU300 rotating anode with Molecular Structure Corp. mirrors and an Raxis4 image plate detector. The data were processed with the programs DENZO and Scalepack. The structures were solved by molecular replacement with coordinates from PDB entry 3prg, using the AMoRe program package. Model building was performed using the O software package, and the models were refined using simulated annealing and restrained B factor refinement included in CNS. The ligand in Example 1 and co-activator peptide were modeled according to the difference electron density maps.

The obtained crystal structure indicated a new binding mode for a PPARy ligand. In contrast to the binding mode previously suggested by Nolte et al. (1998; Nature 395: 137-143), the novel binding mode positions the ligand in a region distant from helix 12 and the residues His323, His449 and Tyr473 of SEQ ID NO: 1. The novel binding mode is characterized by: (a) There is a polar interaction between the carboxylate moiety (designated"negative ionizing feature"in Fig. 2) of the 5-substituted 2-amidobenzoic acid ligand and the backbone amide nitrogen of residue Ser342 of SEQ ID NO: 1 (Fig. 1). The carboxylate group is further stabilized by a hydrogen bond to the amide nitrogen in the ligand.

(b) The aromatic ring of the benzoate group (designated"hydrophobic aromatic feature 1"in Fig. 2) is interacting through the side chains of Ile341 and Cys285 of SEQ ID NO: 1 and the backbone atoms of Gly284 and Cys285 of SEQ ID NO: 1.

(c) An additional aromatic group is linked by an amide to the benzoate group. This aromatic group (designated"hydrophobic aromatic feature 2"in Fig. 2) is located in a hydrophobic region and interacts with the side chains of Leu330, Ile326, Arg288, Leu333 and Met329 of SEQ ID NO: 1.

The interacting features in the pharmacophore, defined by the X-ray structure and extracted from the ligand coordinates using the Catalyst software (Accelrys), are illustrated in Fig. 1 and the coordinates are given in Tables I and II.

TABLE I (coordinates in Angstrom) Feature x y z Tolerance Hydrophobic-9. 478 10.445-0. 636 2 Aromatic 1 Hydrophobic-7.806 17.517 0. 875 2 Aromatic 2 Negative-5.505 11.519 1.151 2 Ionizing

EXAMPLE 3: Ligand binding assay Crude extracts are prepared from E. coli (BL21 (DE3) pLysS, Novagen) producing GST-PPARyLBD fusion protein by freeze thawing in buffer containing 50 mM Tris-HCl pH 7.9, 250 mM KCI, 10% glycerol, 1% Triton X- 100,10 mM DTT, 1mM PMSF, 10 ßg/mL DNase and 10 mM MgCl.

Competitive ligand binding assays are performed on immobilized GST-GST- PPARyLBD fusion protein from crude extracts incubated with glutathione- Sepharose 4B (Amersham Pharmacia Biotech). Following immobilization, the slurry is washed three times in binding buffer containing 50 mM Tris-HCL, pH 7.9, 50 mM KC1, 0.1% Triton-X100, 10 mM DTT, 2 mM EDTA, dispensed in 96-well filter plates (MHVB N45, Millipore) and incubated with a fixed amount tritiated ligand and different concentrations of cold competing ligands.

Equilibrium binding is reached after incubation for 2 hours at room temperature on a plate shaker. The plates are then washed 3 times in binding buffer, dried overnight at room temperature followed by scintillation counting after the addition of 25 ul ofscintillant (Optiscint Hisafe, Wallac) per well.

Each experiment is performed in duplicate and repeated independently at least three times. 3H-BRL49653 (ART-605; American Radiolabeled Chemicals, USA) is used as tracer in PPARy competitive ligand binding experiments at a concentration of 30 nM. The compounds of Formula I exhibit Ki values on PPAR. in the range of 0.3 to 35 uM.

EXAMPLE 4: Cell-based reporter assay The effect of identified compounds on activation of PPARy is determined. Reporter gene assays are performed essentially as described in Bertilsson et al. , 1998 (Proc. Natl. Acad. Sci. U. S. A. 95: 12208-12213), by transient co-transfections of CaCo2/TC cells with a GAL-4-LBD (Ligand Binding Domain) fusion constructs, containing the nucleotide sequence corresponding to human PPARyLBD (i. e. amino acid residues 204-477), together with a 4xUAS-luciferase reporter gene construct, using the FuGENE-6 transfection reagent (Roche) according to the manufacturers recommendations.

After 24 hours, the cells are treated with trypsin, transferred to 96-well microplates and allowed to settle. Induction is performed for 24 hours by applying different concentrations of compounds diluted in DMSO or DMSO alone (vehicle). Subsequently, the cells are lysed and luciferase activity measured, according to standard procedures. The compounds of Formula I exhibit EC50 values on PPARy in the range of 0.3 to 50 pM.

TABLE II Atomic co-ordinates of the crystal structure according to Example 2.

REMARK coordinates PPARgamma-Gripl-bvt762 complex REMARK starting r= 0.2403 freer= 0.3182 REMARK final r= 0.2223 freer= 0.3079 CRYST1 48.954 66.941 123.233 90.00 90.00 90.00 P 21 21 21 ATOM 1 CB ALA A 200 2.796 6.461 34.710 1.00 76.99 A ATOM 2 C ALA A 200 2.711 5.546 37.067 1.00 90.10 A ATOM 3 O ALA A 200 3.885 5.683 37. 438 1.00 95.30 A ATOM 4 N ALA A 200 2.176 7.969 36.579 1.00 81.55 A ATOM 5 CA ALA A 200 2.093 6.560 36.079 1.00 85.63 A ATOM 6 N VAL A 201 1.920 4.546 37.490 1.00 86.34 A ATOM 7 CA VAL A 201 2.388 3.494 38.414 1.00 78.34 A ATOM 8 CB VAL A 201 1.371 2.340 38.545 1.00 77.58 A ATOM 9 CG1 VAL A 201 1.880 1. 321 39.563 1.00 75.28 A ATOM 10 CG2 VAL A 201 0.004 2.883 38.948 1.00 77.33 A ATOM 11 C VAL A 201 3.669 2.901 37.846 1.00 76. 06 A ATOM 12 O VAL A 201 3.632 1.953 37.049 1.00 71.26 A ATOM 13 N HIS A 202 4.798 3.457 38.271 1.00 75.43 A ATOM 14 CA HIS A 202 6.088 3.023 37.763 1.00 75.63 A ATOM 15 CB HIS A 202 7.168 4.089 38.032 1.00 81.98 A ATOM 16 CG HIS A 202 7.689 4.742 36.784 1.00 86.72 A ATOM 17 CD2 HIS A 202 7.681 6.036 36.380 1.00 87.63 A ATOM 18 ND1 HIS A 202 8.260 4.023 35.750 1.00 86.54 A ATOM 19 CE1 HIS A 202 8.574 4.845 34.764 1.00 88.88 A ATOM 20 NE2 HIS A 202 8.233 6. 072 35.120 1.00 90.15 A ATOM 21 C HIS A 202 6.596 1.671 38.218 1.00 68.30 A ATOM 22 O HIS A 202 6.828 1.442 39.406 1.00 70.60 A ATOM 23 N TYR A 203 6.762 0.795 37.231 1.00 58. 01 A ATOM 24 CA TYR A 203 7.287-0. 553 37.391 1.00 53.37 A ATOM 25 CB TYR A 203 6.166-1. 595 37.429 1.00 57.52 A ATOM 26 CG TYR A 203 5.528-1. 837 38.779 1.00 60.71 A ATOM 27 CD1 TYR A 203 4.726-2. 966 38.996 1.00 63.63 A ATOM 28 CE1 TYR A 203 4.118-3. 196 40.232 1.00 67.17 A ATOM 29 CD2 TYR A 203 5.706-0. 945 39.832 1.00 61.80 A ATOM 30 CE2 TYR A 203 5.105-1. 161 41.071 1.00 68.20 A ATOM 31 CZ TYR A 203 4.313-2. 284 41.264 1.00 69.95 A ATOM 32 OH TYR A 203 3.711-2. 478 42.485 1.00 72.37 A ATOM 33 C TYR A 203 8.116-0. 783 36.133 1.00 45.95 A ATOM 34 O TYR A 203 7.659-0. 493 35.033 1.00 44.42 A ATOM 35 N LEU A 204 9.332-1. 284 36.273 1.00 43.69 A ATOM 36 CA LEU A 204 10.123-1. 532 35.081 1.00 44.17 A ATOM 37 CB LEU A 204 11.371-2. 335 35.432 1.00 35.72 A ATOM 38 CG LEU A 204 12.357-2. 483 34.285 1.00 32.88 A ATOM 39 CD1 LEU A 204 13.693-1. 937 34.723 1.00 35.12 A ATOM 40 CD2 LEU A 204 12.459-3. 942 33.862 1.00 34.56 A ATOM 41 C LEU A 204 9.227-2. 322 34.116 1.00 53.19 A ATOM 42 O LEU A 204 8.987-3. 520 34.303 1.00 61.39 A ATOM 43 N ASN A 205 8.711-1. 635 33.100 1.00 58.17 A ATOM 44 CA ASN A 205 7.834-2. 262 32.110 1.00 62.80 A ATOM 45 CB ASN A 205 7.230-1. 193 31.191 1.00 73.55 A ATOM 46 CG ASN A 205 6.484-0. 097 31.954 1.00 78.48 A ATOM 47 OD1 ASN A 205 5.388-0. 325 32.476 1.00 80.20 A ATOM 48 ND2 ASN A 205 7.078 1.100 32.016 1.00 77. 28 A ATOM 49 C ASN A 205 8.589-3. 277 31.248 1.00 61.50 A ATOM 50 O ASN A 205 9.759-3. 084 30.928 1.00 60.41 A ATOM 51 N PRO A 206 7.919-4. 370 30. 846 1.00 63.40 A TABLE II (continued) ATOM 52 CD PRO A 206 6.513-4. 686 31.165 1.00 65.09 A ATOM 53 CA PRO A 206 8.521-5. 425 30.010 1.00 60.25 A ATOM 54 CB PRO A 206 7.493-6. 548 30.088 1.00 60.32 A ATOM 55 CG PRO A 206 6.191-5. 782 30.157 1.00 64.33 A ATOM 56 C PRO A 206 8.755-4. 955 28.569 1.00 57.15 A ATOM 57 O PRO A 206 9.157-5. 730 27.694 1.00 56.30 A ATOM 58 N GLU A 207 8.484-3. 673 28.346 1.00 57.82 A ATOM 59 CA GLU A 207 8.644-3. 029 27.048 1.00 57.62 A ATOM 60 CB GLU A 207 7.290-2. 477 26.569 1.00 66.27 A ATOM 61 CG GLU A 207 6.689-1. 394 27.495 1.00 75.95 A ATOM 62 CD GLU A 207 5.182-1. 554 27.757 1.00 78.33 A ATOM 63 OE1 GLU A 207 4.393-1. 574 26.785 1.00 79.48 A ATOM 64 OE2 GLU A 207 4.790-1. 651 28.945 1.00 75.35 A ATOM 65 C GLU A 207 9.622-1. 885 27.272 1.00 55.14 A ATOM 66 O GLU A 207 9.681-0. 949 26.481 1.00 58.99 A ATOM 67 N SER A 208 10.378-1. 969 28.367 1.00 51.82 A ATOM 68 CA SER A 208 11.356-0. 945 28.733 1.00 44. 64 A ATOM 69 CB SER A 208 11.430-0. 794 30.250 1.00 41.14 A ATOM 70 OG SER A 208 12.434-1. 649 30.778 1.00 41.82 A ATOM 71 C SER A 208 12.745-1. 309 28.224 1.00 40.86 A ATOM 72 O SER A 208 13.540-0. 434 27.885 1.00 37.66 A ATOM 73 N ALA A 209 13.041-2. 603 28.198 1.00 36.04 A ATOM 74 CA ALA A 209 14.340-3. 051 27.726 1.00 36.75 A ATOM 75 CB ALA A 209 14.399-4. 565 27.733 1.00 36.00 A ATOM 76 C ALA A 209 14.547-2. 517 26.315 1.00 44.36 A ATOM 77 0 ALA A 209 15.654-2. 119 25.941 1.00 43.44 A ATOM 78 N ASP A 210 13.465-2. 500 25.538 1.00 50.70 A ATOM 79 CA ASP A 210 13.510-2. 009 24.163 1.00 49.28 A ATOM 80 CB ASP A 210 12.169-2. 275 23.464 1.00 53.39 A ATOM 81 CG ASP A 210 12.149-3. 613 22. 722 1.00 59.36 A ATOM 82 OD1 ASP A 210 13.009-3. 810 21.832 1.00 64.33 A ATOM 83 OD2 ASP A 210 11.278-4. 462 23.020 1.00 61.30 A ATOM 84 C ASP A 210 13.837-0. 517 24.135 1.00 46.33 A ATOM 85 0 ASP A 210 14.632-0. 054 23.308 1.00 41.30 A ATOM 86 N LEU A 211 13.224 0.224 25.053 1.00 40.99 A ATOM 87 CA LEU A 211 13.437 1.660 25.162 1.00 35.08 A ATOM 88 CB LEU A 211 12.511 2.225 26.231 1.00 28.02 A ATOM 89 CG LEU A 211 11.047 1.960 25.916 1.00 25.96 A ATOM 90 CD1 LEU A 211 10.209 2.288 27.123 1.00 26.82 A ATOM 91 CD2 LEU A 211 10.623 2.781 24.719 1.00 29.27 A ATOM 92 C LEU A 211 14.895 2.026 25.476 1.00 35.51 A ATOM 93 O LEU A 211 15.445 2.959 24.884 1.00 35.81 A ATOM 94 N ARG A 212 15.518 1.309 26.406 1.00 30.15 A ATOM 95 CA ARG A 212 16.904 1.593 26.740 1.00 34.58 A ATOM 96 CB ARG A 212 17.316 0.843 27.996 1.00 39.00 A ATOM 97 CG ARG A 212 16.552 1.287 29.225 1.00 47.32 A ATOM 98 CD ARG A 212 17.212 2.476 29.895 1.00 42.01 A ATOM 99 NE ARG A 212 17.279 3.669 29.060 1.00 34.19 A ATOM 100 CZ ARG A 212 18.148 4.645 29.282 1.00 31.41 A ATOM 101 NH1 ARG A 212 18.989 4.521 30.297 1.00 27.06 A ATOM 102 NH2 ARG A 212 18.176 5.734 28.517 1.00 33.51 A ATOM 103 C ARG A 212 17.730 1.136 25. 558 1.00 39.16 A ATOM 104 O ARG A 212 18.864 1.590 25.356 1.00 37.72 A ATOM 105 N ALA A 213 17.137 0.236 24.774 1.00 37.82 A ATOM 106 CA ALA A 213 17.782-0. 291 23. 579 1.00 34.08 A ATOM 107 CB ALA A 213 17.059-1. 536 23. 104 1.00 31.44 A TABLE II (continued) ATOM 108 C ALA A 213 17. 729 0.785 22.507 1.00 29.77 A ATOM 109 0 ALA A 213 18.712 1.037 21.817 1.00 24.91 A ATOM 110 N LEU A 214 16.572 1.428 22.384 1.00 28.52 A ATOM 111 CA LEU A 214 16.381 2.474 21.394 1.00 25.87 A ATOM 112 CB LEU A 214 14.893 2.823 21.268 1.00 20.60 A ATOM 113 CG LEU A 214 14.401 3.303 19.892 1.00 12.77 A ATOM 114 CD1 LEU A 214 12. 955 3.756 19.984 1.00 4.43 A ATOM 115 CD2 LEU A 214 15.263 4.442 19.400 1.00 8.41 A ATOM 116 C LEU A 214 17.175 3.724 21.764 1.00 26.83 A ATOM 117 O LEU A 214 17.727 4.392 20.888 1.00 28.35 A ATOM 118 N ALA A 215 17.237 4.035 23. 058 1.00 24.35 A ATOM 119 CA ALA A 215 17.965 5.216 23.529 1.00 28.93 A ATOM 120 CB ALA A 215 17.712 5.433 25.023 1.00 24.68 A ATOM 121 C ALA A 215 19.474 5.133 23.259 1.00 29.08 A ATOM 122 O ALA A 215 20.142 6.149 23.009 1.00 25.62 A ATOM 123 N LYS A 216 20. 007 3.917 23.307 1.00 28.11 A ATOM 124 CA LYS A 216 21.430 3.706 23.081 1.00 29.26 A ATOM 125 CB LYS A 216 21. 831 2.322 23.574 1.00 37.18 A ATOM 126 CG LYS A 216 23.319 2.068 23.681 1.00 40.03 A ATOM 127 CD LYS A 216 23.532 0.689 24.295 1.00 51.26 A ATOM 128 CE LYS A 216 22.821 0.562 25.655 1.00 51.63 A ATOM 129 NZ LYS A 216 22.495-0. 846 26.034 1.00 45.54 A ATOM 130 C LYS A 216 21.732 3.823 21.606 1.00 31.39 A ATOM 131 O LYS A 216 22.702 4.471 21.213 1.00 32.53 A ATOM 132 N HIS A 217 20.898 3.190 20. 784 1.00 35.31 A ATOM 133 CA HIS A 217 21.109 3.233 19.345 1.00 34.28 A ATOM 134 CB HIS A 217 19.994 2.481 18. 607' 1.00 32.74 A ATOM 135 CG HIS A 217 19.956 2.776 17.144 1.00 33.36 A ATOM 136 CD2 HIS A 217 18.985 3.304 16.364 1.00 34.72 A ATOM 137 ND1 HIS A 217 21.058 2.629 16.333 1.00 35.92 A ATOM 138 CE1 HIS A 217 20.772 3.062 15.119 1.00 35.79 A ATOM 139 NE2 HIS A 217 19.519 3.478 15.112 1.00 33.82 A ATOM 140 C HIS A 217 21.181 4.688 18.870 1.00 31.05 A ATOM 141 O HIS A 217 22.183 5.113 18.287 1.00 28.96 A ATOM 142 N LEU A 218 20.121 5.446 19.137 1.00 25.00 A ATOM 143 CA LEU A 218 20.071 6.855 18.762 1.00 22.16 A ATOM 144 CB LEU A 218 18.795 7.499 19.334 1.00 15.59 A ATOM 145 CG LEU A 218 17.531 6.883 18.715 1.00 17.55 A ATOM 146 CD1 LEU A 218 16.227 7.461 19.288 1.00 9.29 A ATOM 147 CD2 LEU A 218 17.604 7.133 17.222 1.00 18.74 A ATOM 148 C LEU A 218 21.334 7.600 19.243 1.00 27.73 A ATOM 149 O LEU A 218 22.016 8.270 18.445 1.00 17.54 A ATOM 150 N TYR A 219 21.661 7.460 20.532 1.00 29.77 A ATOM 151 CA TYR A 219 22.837 8.123 21.088 1.00 24.74 A ATOM 152 CB TYR A 219 23.045 7.770 22.555 1.00 24.20 A ATOM 153 CG TYR A 219 24.244 8.486 23.151 1.00 32.89 A ATOM 154 CD1 TYR A 219 24.154 9.811 23.554 1.00 39.68 A ATOM 155 CE1 TYR A 219 25.256 10.489 24.065 1.00 36.91 A ATOM 156 CD2 TYR A 219 25.477 7.852 23.279 1.00 34.68 A ATOM 157 CE2 TYR A 219 26.581 8.524 23.787 1.00 33.90 A ATOM 158 CZ TYR A 219 26.461 9.842 24.177 1.00 33.21 A ATOM 159 OH TYR A 219 27.545 10.532 24.676 1.00 43.79 A ATOM 160 C TYR A 219 24.122 7.817 20.335 1.00 23.76 A ATOM 161 O TYR A 219 24.870 8.733 20.022 1.00 25.47 A ATOM 162 N ASP A 220 24.403 6.549 20.043 1.00 22.92 A ATOM 163 CA ASP A 220 25.633 6.248 19.319 1.00 25.29 A TABLE II (continued) ATOM 164 CB ASP A 220 25.862 4.737 19.221 1.00 32.13 A ATOM 165 CG ASP A 220 26.223 4.107 20.566 1.00 39.64 A ATOM 166 OD1 ASP A 220 27.142 4.615 21.254 1.00 38.02 A ATOM 167 OD2 ASP A 220 25.592 3.093 20.935 1.00 40.83 A ATOM 168 C ASP A 220 25.580 6.879 17.935 1.00 19.93 A ATOM 169 O ASP A 220 26.557 7.446 17.461 1.00 21.04 A ATOM 170 N SER A 221 24.415 6.807 17.305 1.00 20.51 A ATOM 171 CA SER A 221 24.215 7.379 15.975 1.00 23.82 A ATOM 172 CB SER A 221 22.802 7.090 15.488 1.00 22.99 A ATOM 173 OG SER A 221 22.408 5.775 15.850 1.00 36.55 A ATOM 174 C SER A 221 24.392 8.883 16.019 1.00 26.29 A ATOM 175 O SER A 221 24.808 9.499 15.040 1.00 23.04 A ATOM 176 N TYR A 222 24.043 9.454 17.168 1.00 25.32 A ATOM 177 CA TYR A 222 24.105 10.889 17.416 1.00 23.74 A ATOM 178 CB TYR A 222 23.262 11.205 18.665 1.00 16.47 A ATOM 179 CG TYR A 222 23.400 12.600 19.238 1.00 6.87 A ATOM 180 CD1 TYR A 222 22.519 13.609 18.909 1.00 11.23 A ATOM 181 CE1 TYR A 222 22.647 14.872 19.462 1.00 5.23 A ATOM 182 CD2 TYR A 222 24.412 12.895 20.134 1.00 7.70 A ATOM 183 CE2 TYR A 222 24.544 14.150 20.686 1.00 5.26 A ATOM 184 CZ TYR A 222 23.668 15.127 20.349 1.00 7.82 A ATOM 185 OH TYR A 222 23.852 16.364 20.904 1.00 21.30 A ATOM 186 C TYR A 222 25.542 11.392 17.569 1.00 29.69 A ATOM 187 O TYR A 222 25.916 12.401 16.969 1.00 30.44 A ATOM 188 N ILE A 223 26.348 10. 689 18.361 1.00 35. 61 A ATOM 189 CA ILE A 223 27.740 11.076 18.583 1.00 36.46 A ATOM 190 CB ILE A 223 28.308 10.343 19.810 1.00 34.41 A ATOM 191 CG2 ILE A 223 28.229 8.858 19.590 1.00 34.96 A ATOM 192 CG1 ILE A 223 29.763 10.749 20.060 1.00 45.68 A ATOM 193 CD1 ILE A 223 29.954 12.155 20.598 1.00 46.85 A ATOM 194 C ILE A 223 28.552 10.713 17.334 1.00 37.76 A ATOM 195 O ILE A 223 29.737 11.027 17.215 1.00 30.45 A ATOM 196 N LYS A 224 27.882 10.058 16.395 1.00 40.48 A ATOM 197 CA LYS A 224 28.503 9.647 15.144 1.00 42.56 A ATOM 198 CB LYS A 224 28.063 8.213 14.799 1.00 47.75 A ATOM 199 CG LYS A 224 28.771 7.597 13.599 1.00 61.51 A ATOM 200 CD LYS A 224 28. 757 6.063 13.637 1.00 71.69 A ATOM 201 CE LYS A 224 29.691 5.479 12.558 1.00 77.69 A ATOM 202 NZ LYS A 224 29.886 3.993 12.638 1.00 74.65 A ATOM 203 C LYS A 224 28.118 10.612 14.015 1.00 34.99 A ATOM 204 O LYS A 224 28.887 10.826 13.073 1.00 30.22 A ATOM 205 N SER A 225 26.931 11.204 14.135 1.00 28.84 A ATOM 206 CA SER A 225 26.405 12.127 13.126 1.00 25.92 A ATOM 207 CB SER A 225 24.877 11.979 13.015 1.00 26. 44 A ATOM 208 OG SER A 225 24.491 10.633 12.807 1.00 21.33 A ATOM 209 C SER A 225 26.747 13.584 13.417 1.00 18.61 A ATOM 210 O SER A 225 26.889 14.387 12.494 1.00 13.38 A ATOM 211 N PHE A 226 26.867 13.914 14.701 1.00 15.18 A ATOM 212 CA PHE A 226 27.193 15.270 15.136 1.00 14.68 A ATOM 213 CB PHE A 226 26.139 15.750 16.112 1.00 7.14 A ATOM 214 CG PHE A 226 24.762 15.699 15.556 1.00 8.31 A ATOM 215 CD1 PHE A 226 24.432 16.444 14.437 1.00 5.39 A ATOM 216 CD2 PHE A 226 23.790 14.919 16. 153 1.00 12.30 A ATOM 217 CE1 PHE A 226 23.149 16.419 13.923 1.00 5.25 A ATOM 218 CE2 PHE A 226 22.505 14.884 15.648 1.00 8.95 A ATOM 219 CZ PHE A 226 22.183 15.637 14. 531 1.00 10.17 A TABLE II (continued) ATOM 220 C PHE A 226 28.585 15.350 15.764 1.00 22.15 A ATOM 221 O PHE A 226 28.833 14.834 16.858 1.00 26.07 A ATOM 222 N PRO A 227 29.505 16.034 15.076 1.00 23.33 A ATOM 223 CD PRO A 227 29.135 17.052 14.071 1.00 29.81 A ATOM 224 CA PRO A 227 30.892 16.209 15.501 1.00 27.27 A ATOM 225 CB PRO A 227 31.438 17.205 14.485 1.00 31.34 A ATOM 226 CG PRO A 227 30.243 18.069 14.194 1.00 32.71 A ATOM 227 C PRO A 227 31.034 16.693 16.930 1.00 32.58 A ATOM 228 0 PRO A 227 31.293 15.890 17.834 1.00 39.62 A ATOM 229 N LEU A 228 30.851 17.998 17.130 1.00 22.18 A ATOM 230 CA LEU A 228 30.978 18.611 18.448 1.00 25.76 A ATOM 231 CB LEU A 228 31.208 20.121 18.311 1.00 29.25 A ATOM 232 CG LEU A 228 32.291 20.839 19.142 1.00 29.24 A ATOM 233 CD1 LEU A 228 32.045 22.328 19.027 1.00 24.87 A ATOM 234 CD2 LEU A 228 32.275 20.436 20.604 1.00 16.35 A ATOM 235 C LEU A 228 29.732 18.409 19.280 1.00 20.58 A ATOM 236 O LEU A 228 28.713 19.007 18.982 1.00 20.02 A ATOM 237 N THR A 229 29.803 17.595 20.328 1.00 16.39 A ATOM 238 CA THR A 229 28.634 17.402 21.166 1.00 18.63 A ATOM 239 CB THR A 229 28.615 16.030 21.770 1.00 20.77 A ATOM 240 OG1 THR A 229 29. 846 15.798 22.462 1.00 24.80 A ATOM 241 CG2 THR A 229 28.416 15.005 20.680 1.00 26.09 A ATOM 242 C THR A 229 28.566 18.427 22.283 1.00 20.14 A ATOM 243 O THR A 229 29.392 19.330 22.370 1.00 13.21 A ATOM 244 N LYS A 230 27.573 18.299 23.148 1.00 18.18 A ATOM 245 CA LYS A 230 27.440 19.263 24.223 1.00 15.05 A ATOM 246 CB Lys230 26.143 19.030 24.978 1.00 3.69 A ATOM 247 CG LYS A 230 25.752 20.132 25.917 1.00 2.00 A ATOM 248 CD LYS A 230 24.259 20.258 25.884 1.00 7.16 A ATOM 249 CE LYS A 230 23.743 21.211 26.919 1.00 5.90 A ATOM 250 NZ LYS A 230 23.855 20.591 28.243 1.00 3.51 A ATOM 251 C LYS A 230 28. 616 19.117 25.147 1.00 18.93 A ATOM 252 0 LYS A 230 29.051 20.078 25.768 1.00 21.51 A ATOM 253 N ALA A 231 29.136 17.898 25.213 1.00 23.32 A ATOM 254 CA ALA A 231 30.272 17.573 26.061 1.00 23.97 A ATOM 255 CB ALA A 231 30.585 16.095 25.927 1.00 18.17 A ATOM 256 C ALA A 231 31.515 18.418 25.731 1.00 28.63 A ATOM 257 O ALA A 231 32.009 19.183 26.571 1.00 29.19 A ATOM 258 N LYS A 232 32.023 18.278 24.513 1.00 25.95 A ATOM 259 CA LYS A 232 33.197 19.037 24.118 1.00 32.98 A ATOM 260 CB LYS A 232 33.666 18.599 22.731 1.00 35.83 A ATOM 261 CG LYS A 232 33.579 17.105 22.490 1.00 46.18 A ATOM 262 CD LYS A 232 33.744 16.787 21.005 1.00 56.50 A ATOM 263 CE LYS A 232 33.423 15.334 20.694 1.00 57. 95 A ATOM 264 NZ LYS A 232 33.595 15.024 19.248 1.00 59.06 A ATOM 265 C LYS A 232 32.845 20.529 24. 109 1.00 35.29 A ATOM 266 O LYS A 232 33.662 21.384 24.447 1.00 39.29 A ATOM 267 N ALA A 233 31.617 20.844 23.724 1.00 33.52 A ATOM 268 CA ALA A 233 31.207 22.233 23.685 1.00 32.75 A ATOM 269 CB ALA A 233 29.789 22.342 23.173 1.00 28.29 A ATOM 270 C ALA A 233 31.307 22.808 25.086 1.00 33.74 A ATOM 271 O ALA A 233 31.807 23.912 25.272 1.00 31. 18 A ATOM 272 N ARG A 234 30. 842 22.044 26.071 1.00 35.52 A ATOM 273 CA ARG A 234 30.855 22.491 27.458 1.00 33.48 A ATOM 274 CB ARG A 234 29.782 21.752 28.270 1.00 29. 34 A ATOM 275 CG ARG A 234 28.464 22. 523 28.402 1.00 31.64 A TABLE II (continued) ATOM 276 CD ARG A 234 28.676 23.806 29.238 1.00 42.29 A ATOM 277 NE ARG A 234 27.458 24.590 29.502 1.00 48.29 A ATOM 278 CZ ARG A 234 26.773 25.288 28.592 1.00 49.87 A ATOM 279 NH1 ARG A 234 27.167 25.319 27.323 1.00 48.10 A ATOM 280 NH2 ARG A 234 25.688 25.967 28.959 1.00 51.51 A ATOM 281 C ARG A 234 32.213 22.363 28.124 1.00 37.16 A ATOM 282 O ARG A 234 32.549 23.163 28. 994 1.00 43.33 A ATOM 283 N ALA A 235 32.997 21.364 27.728 1.00 37.80 A ATOM 284 CA ALA A 235 34.338 21.201 28.302 1.00 39.65 A ATOM 285 CB ALA A 235 35.065 20.028 27.645 1.00 37.03 A ATOM 286 C ALA A 235 35.103 22.491 28.022 1.00 37.42 A ATOM 287 O ALA A 235 35.573 23.169 28.935 1.00 41.70 A ATOM 288 N ILE A 236 35.200 22.808 26.733 1.00 34.29 A ATOM 289 CA ILE A 236 35.872 23.991 26. 201 1.00 28.18 A ATOM 290 CB ILE A 236 35.541 24.117 24.710 1.00 17.54 A ATOM 291 CG2 ILE A 236 36.124 25.375 24.158 1.00 13.90 A ATOM 292 CG1 ILE A 236 36.048 22.886 23.969 1.00 10.93 A ATOM 293 CD1 ILE A 236 35.649 22. 840 22. 532 1.00 12.80 A ATOM 294 C ILE A 236 35.548 25.331 26.895 1.00 31.80 A ATOM 295 O ILE A 236 36.453 26.049 27.330 1.00 31.24 A ATOM 296 N LEU A 237 34.260 25.662 26.975 1.00 35.73 A ATOM 297 CA LEU A 237 33.797 26.904 27.599 1.00 34.27 A ATOM 298 CB LEU A 237 32.288 27.071 27.388 1.00 22.76 A ATOM 299 CG LEU A 237 31.798 27.245 25.951 1.00 11.12 A ATOM 300 CD1 LEU A 237 30.292 27.086 25.918 1.00 10. 69 A ATOM 301 CD2 LEU A 237 32.231 28.605 25.414 1.00 6.04 A ATOM 302 C LEU A 237 34.094 26.951 29.092 1.00 41.64 A ATOM 762 O LEU A 237 33.971 28.005 29.714 1.00 48.06 A ATOM 304 N THR A 238 34.460 25.800 29.657 1.00 48.84 A ATOM 305 CA THR A 238 34.790 25.677 31.075 1.00 50.07 A ATOM 306 CB THR A 238 34.116 24.437 31.704 1.00 50.01 A ATOM 307 OG1 THR A 238 32.717 24.445 31.407 1.00 52.95 A ATOM 308 CG2 THR A 238 34.284 24.445 33.207 1.00 52.58 A ATOM 309 C THR A 238 36.304 25.518 31.198 1.00 51.18 A ATOM 310 O THR A 238 36.821 25.199 32. 266 1.00 52.00 A ATOM 311 N GLY A 239 37.003 25.740 30. 088 1.00 57.06 A ATOM 312 CA GLY A 239 38.449 25.622 30.072 1.00 66. 61 A ATOM 313 C GLY A 239 38.953 24.400 30.810 1.00 73.65 A ATOM 314 O GLY A 239 39.745 24.514 31.742 1.00 76.26 A ATOM 315 N LYS A 240 38.488 23.225 30.403 1.00 84.76 A ATOM 316 CA LYS A 240 38.906 21.981 31.038 1.00 91.14 A ATOM 317 CB LYS A 240 37.714 21.308 31.729 1.00 93.26 A ATOM 318 CG LYS A 240 38.123 20.218 32.708 1.00 97.51 A ATOM 319 CD LYS A 240 36.933 19.487 33.312 1.00 96.52 A ATOM 320 CE LYS A 240 37.404 18.389 34.260 1.00 94.26 A ATOM 321 NZ LYS A 240 36.288 17.541 34.753 1.00 94.80 A ATOM 322 C LYS A 240 39.520 21.032 30.006 1.00 92. 76 A ATOM 323 O LYS A 240 39.473 19.812 30.157 1.00 90.69 A ATOM 324 N THR A 241 40.087 21.611 28.950 1.00 95.75 A ATOM 325 CA THR A 241 40.737 20.852 27.882 1.00 97.72 A ATOM 326 CB THR A 241 39.731 20.416 26.794 1.00 98.97 A ATOM 327 OG1 THR A 241 39.173 21.575 26.163 1.00100. 00 A ATOM 328 CG2 THR A 241 38.611 19.584 27.401 1.00100. 00 A ATOM 329 C THR A 241 41.802 21.738 27.231 1.00100. 00 A ATOM 330 O THR A 241 41.563 22.327 26.174 1.00100. 00 A ATOM 331 N THR A 242 42.970 21.825 27.874 1.00100. 00 A TABLE II (continued) ATOM 332 CA THR A 242 44.099 22.644 27.406 1.00100. 00 A ATOM 333 CB THR A 242 45.450 22.185 28.057 1.00100. 00 A ATOM 334 OG1 THR A 242 45. 423 22. 446 29.468 1.00100. 00 A ATOM 335 CG2 THR A 242 46.639 22.928 27.437 1.00 99.95 A ATOM 336 C THR A 242 44.274 22.661 25.887 1.00100. 00 A ATOM 337 0 THR A 242 44.193 23.721 25.256 1.00100. 00 A ATOM 338 N ASP A 243 44.518 21.488 25.307 1.00 99.54 A ATOM 339 CA ASP A 243 44.716 21.368 23.868 1.00 98.92 A ATOM 340 CB ASP A 243 44.375 19.936 23.405 1.00100. 00 A ATOM 341 CG ASP A 243 43.086 19.394 24.023 1.00100. 00 A ATOM 342 OD1 ASP A 243 43.002 19.309 25.268 1. 00100. 00 A ATOM 343 OD2 ASP A 243 42.160 19.038 23.259 1.00 98.49 A ATOM 344 C ASP A 243 43.928 22.401 23.056 1.00 95.04 A ATOM 345 O ASP A 243 44.452 22.990 22.111 1.00 94.20 A ATOM 346 N LYS A 244 42.681 22.639 23.443 1.00 92.32 A ATOM 347 CA LYS A 244 41.840 23.592 22.732 1.00 91.56 A ATOM 348 CB LYS A 244 40.634 22.859 22.135 1.00 90.75 A ATOM 349 CG LYS A 244 40.950 22.081 20.868 1.00 87.59 A ATOM 350 CD LYS A 244 41.025 23. 004 19.659 1.00 88.52 A ATOM 351 CE LYS A 244 39.646 23.554 19.291 1.00 88.27 A ATOM 352 NZ LYS A 244 38.663 22.473 18.970 1.00 83.95 A ATOM 353 C LYS A 244 41.356 24.791 23.557 1.00 88.97 A ATOM 354 0 LYS A 244 40.548 24.649 24.482 1.00 89.20 A ATOM 355 N SER A 245 41.867 25.969 23.202 1.00 79.21 A ATOM 356 CA SER A 245 41.501 27.227 23.845 1.00 71.46 A ATOM 357 CB SER A 245 42.691 27.781 24.627 1.00 73.58 A ATOM 358 OG SER A 245 43.858 27.810 23.824 1.00 78.37 A ATOM 359 C SER A 245 41.121 28.169 22.699 1.00 64.67 A ATOM 360 0 SER A 245 41.995 28.707 22.020 1.00 68.47 A ATOM 361 N PRO A 246 39.808 28.378 22.474 1.00 54.22 A ATOM 362 CD PRO A 246 38.728 27.910 23.353 1.00 48.95 A ATOM 363 CA PRO A 246 39.255 29.234 21.415 1.00 46.28 A ATOM 364 CB PRO A 246 37.746 29.138 21.638 1.00 44.82 A ATOM 365 CG PRO A 246 37.566 27.882 22.404 1.00 45.26 A ATOM 366 C PRO A 246 39.715 30.677 21.461 1. 00 41.39 A ATOM 367 O PRO A 246 39.909 31.231 22.538 1.00 43.18 A ATOM 368 N PHE A 247 39.888 31.286 20.292 1.00 31.67 A ATOM 369 CA PHE A 247 40.291 32.685 20.230 1.00 29.72 A ATOM 370 CB PHE A 247 40.872 33.019 18.869 1.00 32.28 A ATOM 371 CG PHE A 247 41.235 34.464 18.711 1.00 35.80 A ATOM 372 CD1 PHE A 247 42.516 34.910 19.015 1.00 42.17 A ATOM 373 CD2 PHE A 247 40.296 35.385 18.261 1.00 35.30 A ATOM 374 CE1 PHE A 247 42.865 36.254 18.875 1.00 40.30 A ATOM 375 CE2 PHE A 247 40.631 36.729 18.117 1.00 38.95 A ATOM 376 CZ PHE A 247 41.925 37.163 18.428 1.00 37.12 A ATOM 377 C PHE A 247 39.006 33.464 20.432 1.00 29.21 A ATOM 378 0 PHE A 247 37.974 33.083 19.887 1.00 39.79 A ATOM 379 N VAL A 248 39.049 34. 546 21.203 1.00 25.21 A ATOM 380 CA VAL A 248 37.834 35.318 21.458 1.00 23.85 A ATOM 381 CB VAL A 248 37.787 35.768 22.956 1.00 14.79 A ATOM 382 CG1 VAL A 248 36.416 36.300 23.316 1.00 6. 01 A ATOM 383 CG2 VAL A 248 38.147 34.601 23.859 1.00 2.00 A ATOM 384 C VAL A 248 37.727 36.522 20.500 1.00 26.84 A ATOM 385 0 VAL A 248 38.731 37.174 20.205 1.00 36.18 A ATOM 386 N ILE A 249 36.516 36.790 20.002 1. 00 23.80 A ATOM 387 CA ILE A 249 36.266 37.893 19.060 1.00 17.77 A TABLE II (continued) ATOM 388 CB ILE A 249 35.668 37.381 17.733 1.00 18.47 A ATOM 389 CG2 ILE A 249 35.405 38.538 16.794 1.00 7.60 A ATOM 390 CG1 ILE A 249 36.614 36.372 17.088 1.00 25.11 A ATOM 391 CD1 ILE A 249 35.957 35.514 16.023 1.00 24.00 A ATOM 392 C ILE A 249 35.258 38.871 19.635 1.00 22.22 A ATOM 393 O ILE A 249 34.068 38.601 19.596 1.00 24.80 A ATOM 394 N TYR A 250 35.726 40.011 20.139 1.00 32.50 A ATOM 395 CA TYR A 250 34.841 41.017 20. 726 1.00 33.51 A ATOM 396 CB TYR A 250 35.310 41.374 22.146 1.00 36.60 A ATOM 397 CG TYR A 250 36.783 41.744 22.278 1.00 34.70 A ATOM 398 CD1 TYR A 250 37.189 43.079 22.404 1.00 36.69 A ATOM 399 CE1 TYR A 250 38.556 43.416 22.526 1.00 42.65 A ATOM 400 CD2 TYR A 250 37.774 40.749 22.278 1.00 37.30 A ATOM 401 CE2 TYR A 250 39.133 41.068 22.397 1.00 40.41 A ATOM 402 CZ TYR A 250 39.522 42.402 22.513 1.00 44.80 A ATOM 403 OH TYR A 250 40.875 42.702 22.555 1.00 40.86 A ATOM 404 C TYR A 250 34.678 42.298 19.905 1.00 34.36 A ATOM 405 O TYR A 250 33.604 42.911 19.904 1.00 32.08 A ATOM 406 N ASP A 251 35.729 42.710 19.208 1.00 35.33 A ATOM 407 CA ASP A 251 35.643 43.930 18.409 1.00 39.39 A ATOM 408 CB ASP A 251 36.282 45.094 19.165 1.00 40.74 A ATOM 409 CG ASP A 251 37.637 44.731 19.741 1.00 46.89 A ATOM 410 OD1 ASP A 251 38.026 43.538 19.648 1.00 46.85 A ATOM 411 OD2 ASP A 251 38.311 45.637 20.295 1.00 53.18 A ATOM 412 C ASP A 251 36.251 43.818 17.011 1.00 40.92 A ATOM 413 O ASP A 251 37.012 42.883 16.705 1.00 34.74 A ATOM 414 N MET A 252 35.900 44. 787 16.169 1.00 43.95 A ATOM 415 CA MET A 252 36.371 44.807 14.797 1.00 47.31 A ATOM 416 CB MET A 252 36.119 46.186 14.163 1.00 51.27 A ATOM 417 CG MET A 252 35.184 46.172 12.929 1.00 50.53 A ATOM 418 SD MET A 252 33.543 45.377 13.172 1.00 49.86 A ATOM 419 CE MET A 252 32.364 46.861 13.265 1.00 45.59 A ATOM 420 C MET A 252 37.852 44.451 14.764 1.00 46.82 A ATOM 421 O MET A 252 38.315 43.798 13.826 1.00 47.59 A ATOM 422 N ASN A 253 38.600 44.842 15.795 1.00 44.21 A ATOM 423 CA ASN A 253 40.024 44.512 15.796 1.00 44.11 A ATOM 424 CB ASN A 253 40.800 45.345 16.823 1.00 46.46 A ATOM 425 CG ASN A 253 42.315 45.267 16.605 1.00 52.03 A ATOM 426 OD1 ASN A 253 42.800 45.443 15.481 1.00 52.81 A ATOM 427 ND2 ASN A 253 43.065 45.011 17.675 1.00 55.65 A ATOM 428 C ASN A 253 40.247 43.032 16.067 1.00 40.00 A ATOM 429 O ASN A 253 40.939 42.359 15.306 1.00 38.08 A ATOM 430 N SER A 254 39.664 42.529 17.153 1.00 39.64 A ATOM 431 CA SER A 254 39.807 41.118 17.496 1.00 36.14 A ATOM 432 CB SER A 254 39.053 40.789 18.781 1.00 33.82 A ATOM 433 OG SER A 254 37.670 41.042 18.614 1.00 35.57 A ATOM 434 C SER A 254 39.244 40.287 16.352 1.00 35.96 A ATOM 435 0 SER A 254 39.776 39.220 16.045 1.00 38.47 A ATOM 436 N LEU A 255 38.176 40.773 15.720 1.00 28.44 A ATOM 437 CA LEU A 255 37.581 40.042 14.606 1.00 24.24 A ATOM 438 CB LEU A 255 36.470 40.872 13.948 1.00 24.55 A ATOM 439 CG LEU A 255 35.560 40.205 12.908 1.00 14.36 A ATOM 440 CD1 LEU A 255 36.347 39.896 11.679 1.00 13.83 A ATOM 441 CD2 LEU A 255 34.962 38.946 13.457 1.00 11.25 A ATOM 442 C LEU A 255 38.691 39.734 13.600 1.00 29.81 A ATOM 443 0 LEU A 255 38.818 38.603 13. 132 1.00 27.74 A TABLE II (continued) ATOM 444 N MET A 256 39.509 40.739 13.291 1.00 39.59 A ATOM 445 CA MET A 256 40.620 40.564 12.351 1.00 46.83 A ATOM 446 CB MET A 256 41.243 41.923 11.994 1.00 43.87 A ATOM 447 CG MET A 256 40.346 42.823 11.162 1.00 53.92 A ATOM 448 SD MET A 256 40.888 44.550 11.085 1.00 64.75 A ATOM 449 CE MET A 256 39.411 45.411 11.775 1.00 61.35 A ATOM 450 C MET A 256 41.705 39.644 12.929 1.00 53.01 A ATOM 451 O MET A 256 42.238 38.772 12.235 1.00 53.48 A ATOM 452 N MET A 257 42.028 39.839 14.203 1.00 59.25 A ATOM 453 CA MET A 257 43.059 39.035 14.847 1.00 63.73 A ATOM 454 CB MET A 257 43.215 39.448 16.318 1.00 69.34 A ATOM 455 CG MET A 257 43.175 40.955 16.592 1.00 69.20 A ATOM 456 SD MET A 257 44.500 41.895 15.797 1.00 77.33 A ATOM 457 CE MET A 257 45.946 41.373 16.786 1.00 77.57 A ATOM 458 C MET A 257 42.676 37.555 14.766 1.00 65.79 A ATOM 459 O MET A 257 43.547 36.684 14.644 1.00 65.39 A ATOM 460 N GLY A 258 41.370 37.285 14.833 1.00 64.17 A ATOM 461 CA GLY A 258 40.874 35.920 14.786 1.00 65.10 A ATOM 462 C GLY A 258 40.558 35.464 13.376 1.00 65.09 A ATOM 463 O GLY A 258 40.192 34.312 13.144 1.00 64.39 A ATOM 464 N GLU A 259 40.691 36.379 12.427 1.00 66.40 A ATOM 465 CA GLU A 259 40. 432 36.054 11.038 1.00 70.50 A ATOM 466 CB GLU A 259 39.983 37.299 10.277 1.00 68.02 A ATOM 467 CG GLU A 259 39.505 37.027 8.869 1.00 64.26 A ATOM 468 CD GLU A 259 38.743 38.197 8.294 1.00 65.55 A ATOM 469 OE1 GLU A 259 39.356 39.264 8.087 1.00 69.20 A ATOM 470 OE2 GLU A 259 37.526 38.052 8.058 1.00 60.59 A ATOM 471 C GLU A 259 41.715 35.506 10.436 1.00 75.94 A ATOM 472 O GLU A 259 41.777 35.203 9.249 1.00 80.45 A ATOM 473 N ASP A 260 42.742 35.386 11.269 1.00 78.84 A ATOM 474 CA ASP A 260 44.022 34.864 10.824 1.00 83.70 A ATOM 475 CB ASP A 260 45.118 35.906 11.049 1.00 89.63 A ATOM 476 CG ASP A 260 45.035 37.060 10.066 1.00 94.31 A ATOM 477 OD1 ASP A 260 43.926 37.604 9. 876 1.00 95.13 A ATOM 478 OD2 ASP A 260 46.083 37.427 9.490 1.00 95.14 A ATOM 479 C ASP A 260 44.348 33.578 11.575 1.00 88.09 A ATOM 480 O ASP A 260 45.508 33.183 11.673 1.00 91.12 A ATOM 481 N LYS A 261 43.312 32.928 12.100 1.00 90.47 A ATOM 482 CA LYS A 261 43.471 31.680 12.842 1.00 90.39 A ATOM 483 CB LYS A 261 43.795 32. 000 14.305 1.00 84.67 A ATOM 484 CG LYS A 261 45.008 32.911 14.472 1.00 84.33 A ATOM 485 CD LYS A 261 45. 156 33.434 15.887 1.00 86.59 A ATOM 486 CE LYS A 261 46. 300 34.429 15. 981 1.00 85.77 A ATOM 487 NZ LYS A 261 46.422 35.003 17.344 1.00 86. 80 A ATOM 488 C LYS A 261 42.196 30.821 12.740 1.00 94.58 A ATOM 489 O LYS A 261 41.875 30.057 13.650 1.00 95.29 A ATOM 490 N ILE A 262 41.490 30.953 11.614 1.00 99.71 A ATOM 491 CA ILE A 262 40.238 30.233 11.335 1.00100. 00 A ATOM 492 CB ILE A 262 40.471 28.713 11.081 1. 00100. 00 A ATOM 493 CG2 ILE A 262 39.138 28.015 10.813 1.00 97.88 A ATOM 494 CG1 ILE A 262 41.367 28.514 9.858 1. 00100. 00 A ATOM 495 CD1 ILE A 262 41.571 27.061 9.480 1.00100. 00 A ATOM 496 C ILE A 262 39.186 30.394 12.432 1.00100. 00 A ATOM 497 O ILE A 262 39.131 29.525 13.328 1.00100. 00 A ATOM 498 OXT ILE A 262 38.432 31.393 12.386 1.00100. 00 A ATOM 499 CB SER B 274 36.458 43.126-0. 445 1.00100. 00 B TABLE II (continued) ATOM 500 OG SER B 274 36.048 41.863-0. 950 1.00100. 00 B ATOM 501 C SER B 274 34.135 43.419 0.457 1.00100. 00 B ATOM 502 O SER B 274 32.959 43.767 0.304 1.00100. 00 B ATOM 503 N SER B 274 35.719 45.377 0.298 1.00 97.84 B ATOM 504 CA SER B 274 35.271 44.094-0. 325 1.00100. 00 B ATOM 505 N LYS B 275 34.495 42.452 1.295 1.00 95.47 B ATOM 506 CA LYS B 275 33.519 41.716 2.089 1.00 89.92 B ATOM 507 CB LYS B 275 33.943 40.247 2.140 1.00 89.02 B ATOM 508 CG LYS B 275 34.219 39.680 0.756 1.00 82.41 B ATOM 509 CD LYS B 275 34.734 38.272 0.809 1.00 75.96 B ATOM 510 CE LYS B 275 34.908 37.747-0. 586 1.00 72.03 B ATOM 511 NZ LYS B 275 35.400 36.357-0. 557 1.00 68.59 B ATOM 512 C LYS B 275 33.397 42.301 3.501 1.00 88.25 B ATOM 513 0 LYS B 275 34.263 42.075 4.352 1.00 89.81 B ATOM 514 N GLU B 276 32.319 43.050 3.743 1.00 79.99 B ATOM 515 CA GLU B 276 32.103 43.676 5.047 1.00 70.71 B ATOM 516 CB GLU B 276 31.094 44.825 4.924 1.00 71.44 B ATOM 517 CG GLU B 276 29.744 44.482 4.312 1.00 68.99 B ATOM 518 CD GLU B 276 28.818 45.696 4.282 1.00 73.30 B ATOM 519 OE1 GLU B 276 29.185 46.705 3.640 1.00 76.48 B ATOM 520 OE2 GLU B 276 27.731 45.649 4.902 1.00 71.53 B ATOM 521 C GLU B 276 31.669 42.703 6.148 1.00 64.98 B ATOM 522 O GLU B 276 30.727 41.927 5.971 1.00 63.09 B ATOM 523 N VAL B 277 32.371 42.769 7.282 1.00 56.77 B ATOM 524 CA VAL B 277 32.133 41. 905 8.444 1.00 43.71 B ATOM 525 CB VAL B 277 32.631 42.581 9.745 1.00 33.59 B ATOM 526 CG1 VAL B 277 34.071 43. 026 9.576 1.-00 36.59 B ATOM 527 CG2 VAL B 277 31.762 43.767 10.087 1.00 30.59 B ATOM 528 C VAL B 277 30.679 41.458 8.649 1.00 40.52 B ATOM 529 O VAL B 277 30.410 40.265 8.832 1.00 28.73 B ATOM 530 N ALA B 278 29.746 42.407 8.622 1.00 39.74 B ATOM 531 CA ALA B 278 28.346 42.076 8.796 1.00 29.24 B ATOM 532 CB ALA B 278 27.499 43.261 8.446 1.00 36.77 B ATOM 533 C ALA B 278 28.004 40.898 7.893 1.00 33.54 B ATOM 534 0 ALA B 278 27.445 39.903 8.354 1.00 39.62 B ATOM 535 N ILE B 279 28.363 40.994 6.614 1.00 29.45 B ATOM 536 CA ILE B 279 28.069 39.926 5.651 1.00 26.12 B ATOM 537 CB ILE B 279 28.023 40.475 4.183 1.00 18.23 B ATOM 538 CG2 ILE B 279 28.063 39.327 3.179 1.00 2.00 B ATOM 539 CG1 ILE B 279 26.768 41.332 3.987 1.00 11.73 B ATOM 540 CD1 ILE B 279 26.644 41.916 2.608 1.00 15.15 B ATOM 541 C ILE B 279 29.020 38.733 5.701 1.00 25.53 B ATOM 542 O ILE B 279 28.588 37.587 5.686 1.00 25.76 B ATOM 543 N ARG B 280 30.312 39.007 5.752 1.00 28.53 B ATOM 544 CA ARG B 280 31.323 37.954 5.796 1.00 33.45 B ATOM 545 CB ARG B 280 32.696 38.605 6.007 1.00 37.00 B ATOM 546 CG ARG B 280 33.887 37.923 5.367 1.00 40.67 B ATOM 547 CD ARG B 280 35.084 38.884 5. 368 1.00 51.37 B ATOM 548 NE ARG B 280 35.457 39.304 6.721 1.00 59.78 B ATOM 549 CZ ARG B 280 36.285 40.306 7.007 1.00 61.45 B ATOM 550 NH1 ARG B 280 36. 558 40.601 8.270 1.00 59.53 B ATOM 551 NH2 ARG B 280 36.836 41.021 6.035 1.00 63.41 B ATOM 552 C ARG B 280 31.022 36.968 6.930 1.00 36.26 B ATOM 553 O ARG B 280 31.494 35.832 6.917 1.00 33.66 B ATOM 554 N ILE B 281 30.216 37.418 7.895 1.00 43.14 B ATOM 555 CA ILE B 281 29.843 36.636 9.081 1.00 39.13 B TABLE II (continued) ATOM 556 CB ILE B 281 29.827 37.540 10.324 1.00 38.25 B ATOM 557 CG2 ILE B 281 28.652 37.191 11.222 1.00 37.41 B ATOM 558 CG1 ILE B 281 31.187 37.437 11.028 1.00 39.79 B ATOM 559 CD1 ILE B 281 31.382 38.410 12.180 1.00 39.22 B ATOM 560 C ILE B 281 28.512 35.911 8.971 1.00 41.70 B ATOM 561 O ILE B 281 28.363 34.790 9.461 1.00 41.18 B ATOM 562 N PHE B 282 27.530 36.570 8.370 1.00 46.43 B ATOM 563 CA PHE B 282 26.238 35.942 8.152 1.00 42.78 B ATOM 564 CB PHE B 282 25.300 36.914 7.464 1.00 41.14 B ATOM 565 CG PHE B 282 23.964 36.331 7.144 1.00 42.62 B ATOM 566 CD1 PHE B 282 23.095 35.961 8.160 1.00 45.39 B ATOM 567 CD2 PHE B 282 23.556 36.177 5.821 1.00 40.24 B ATOM 568 CE1 PHE B 282 21.835 35.451 7.863 1.00 48.58 B ATOM 569 CE2 PHE B 282 22.299 35.669 5.514 1.00 39.36 B ATOM 570 CZ PHE B 282 21.437 35.307 6.536 1.00 45.22 B ATOM 571 C PHE B 282 26.552 34.783 7.207 1.00 39.14 B ATOM 572 O PHE B 282 26.001 33.696 7.323 1.00 37.82 B ATOM 573 N GLN B 283 27.456 35.046 6. 268 1.00 43.67 B ATOM 574 CA GLN B 283 27.906 34.051 5.304 1.00 46.63 B ATOM 575 CB GLN B 283 29.095 34.577 4.488 1.00 50.31 B ATOM 576 CG GLN B 283 28.742 35.581 3.409 1.00 62.57 B ATOM 577 CD GLN B 283 27.671 35.064 2.466 1.00 69.79 B ATOM 578 OE1 GLN B 283 27.662 33.884 2.111 1.00 73.38 B ATOM 579 NE2 GLN B 283 26.765 35.949 2.046 1.00 70.34 B ATOM 580 C GLN B 283 28.341 32.786 6.026 1.00 41.28 B ATOM 581 0 GLN B 283 27.702 31.750 5.910 1.00 43.33 B ATOM 582 N GLY B 284 29.439 32.878 6.768 1.00 37.26 B ATOM 583 CA GLY B 284 29.941 31.724 7.488 1.00 35.46 B ATOM 584 C GLY B 284 28.890 31.070 8. 1.00 39.56 B ATOM 585 O GLY B 284 29.058 29.925 8. 809 1.00 36.88 B ATOM 586 N CYS B 285 27.809 31.802 8.623 1.00 39.20 B ATOM 587 CA CYS B 285 26.721 31.286 9.443 1.00 38.82 B ATOM 588 CB CYS B 285 25.812 32.434 9.891 1.00 39.03 B ATOM 589 SG CYS B 285 24.231 31.910 10.593 1.00 48.76 B ATOM 590 C CYS B 285 25.927 30.254 8.646 1.00 33.93 B ATOM 591 O CYS B 285 25.670 29.146 9.121 1.00 24.72 B ATOM 592 N GLN B 286 25.550 30.608 7.420 1.00 35.53 B ATOM 593 CA GLN B 286 24.803 29.668 6.610 1.00 32.25 B ATOM 594 CB GLN B 286 24.121 30.346 5.414 1.00 33.36 B ATOM 595 CG GLN B 286 25. 003 31.001 4.386 1.00 29.31 B ATOM 596 CD GLN B 286 24.186 31.465 3.201 1.00 27.88 B ATOM 597 OE1 GLN B 286 23.160 32.119 3.364 1.00 28.86 B ATOM 598 NE2 GLN B 286 24.634 31.125 2.004 1.00 30.37 B ATOM 599 C GLN B 286 25.644 28.499 6.146 1.00 28.65 B ATOM 600 O GLN B 286 25.136 27.391 6.103 1.00 41.62 B ATOM 601 N PHE B 287 26.912 28.711 5.804 1.00 29.29 B ATOM 602 CA PHE B 287 27.737 27.569 5.384 1.00 38.15 B ATOM 603 CB PHE B 287 29.155 28.008 4.963 1.00 48.40 B ATOM 604 CG PHE B 287 29.248 28.436 3.508 1.00 62.48 B ATOM 605 CD1 PHE B 287 28. 943 27. 533 2.479 1.00 65.34 B ATOM 606 CD2 PHE B 287 29. 574 29.749 3.165 1.00 60.85 B ATOM 607 CE1 PHE B 287 28.954 27. 935 1.134 1.00 60.78 B ATOM 608 CE2 PHE B 287 29. 588 30.157 1.825 1.00 59.56 B ATOM 609 CZ PHE B 287 29.276 29.249 0.810 1.00 58.05 B ATOM 610 C PHE B 287 27.800 26.509 6.491 1.00 34.48 B ATOM 611 O PHE B 287 27.840 25.307 6.220 1.00 34.57 B TABLE II (continued) ATOM 612 N ARG B 288 27.778 26.948 7.744 1.00 35.05 B ATOM 613 CA ARG B 288 27.809 25.993 8.839 1.00 26.91 B ATOM 614 CB ARG B 288 28.136 26.678 10.161 1.00 30.84 B ATOM 615 CG ARG B 288 28.941 25.817 11.108 1.00 30.28 B ATOM 616 CD ARG B 288 28.325 24.462 11.296 1.00 35.26 B ATOM 617 NE ARG B 288 29.063 23.693 12.288 1.00 50.28 B ATOM 618 CZ ARG B 288 28.770 22.444 12.633 1.00 53.81 B ATOM 619 NH1 ARG B 288 27.750 21.813 12.058 1.00 48.78 B ATOM 620 NH2 ARG B 288 29.488 21.837 13.570 1.00 51.94 B ATOM 621 C ARG B 288 26.419 25.394 8.898 1.00 23.54 B ATOM 622 O ARG B 288 26.258 24.242 9.273 1.00 31.12 B ATOM 623 N SER B 289 25.411 26.175 8.526 1.00 20. 08 B ATOM 624 CA SER B 289 24.048 25. 668 8.529 1.00 16.84 B ATOM 625 CB SER B 289 23.057 26. 766 8.136 1.00 14.98 B ATOM 626 OG SER B 289 23.091 27.854 9.045 1.00 20.63 B ATOM 627 C SER B 289 23.900 24.503 7.550 1.00 21.81 B ATOM 628 O SER B 289 23.580 23.382 7.957 1.00 18.91 B ATOM 629 N VAL B 290 24.147 24.767 6.263 1.00 21.49 B ATOM 630 CA VAL B 290 23.991 23.737 5.238 1.00 23.24 B ATOM 631 CB VAL B 290 24.524 24.166 3.822 1.00 22.50 B ATOM 632 CG1 VAL B 290 24.350 25.662 3.637 1.00 19.86 B ATOM 633 CG2 VAL B 290 25.978 23.718 3.606 1.00 28.57 B ATOM 634 C VAL B 290 24.683 22.473 5.658 1.00 22.52 B ATOM 635 O VAL B 290 24.169 21.382 5.447 1.00 32.34 B ATOM 636 N GLU B 291 25. 845 22.609 6.271 1.00 17. 63 B ATOM 637 CA GLU B 291 26.540 21.423 6. 692 1.00 19.54 B ATOM 638 CB GLU B 291 27.871 21.799 7.333 1.00 28.28 B ATOM 639 CG GLU B 291 29.003 20.869 6.945 1.00 38.80 B ATOM 640 CD GLU B 291 30.305 21.256 7.594 1.00 43.75 B ATOM 641 OE1 GLU B 291 30.856 22.321 7.234 1.00 47.40 B ATOM 642 OE2 GLU B 291 30.768 20.496 8.469 1.00 39.64 B ATOM 643 C GLU B 291 25.620 20.730 7.687 1.00 12.99 B ATOM 644 O GLU B 291 25.294 19. 554 7.548 1.00 6.85 B ATOM 645 N ALA B 292 25.164 21.488 8.672 1.00 15.81 B ATOM 646 CA ALA B 292 24.288 20.951 9.693 1.00 16. 19 B ATOM 647 CB ALA B 292 23. 824 22.070 10.596 1.00 6.16 B ATOM 648 C ALA B 292 23.091 20.211 9.087 1.00 17.79 B ATOM 649 O ALA B 292 22.694 19.152 9.581 1.00 21.53 B ATOM 650 N VAL B 293 22.514 20.763 8.021 1.00 13.55 B ATOM 651 CA VAL B 293 21.377 20.114 7.382 1.00 10.77 B ATOM 652 CB VAL B 293 20. 870 20. 908 6.192 1.00 9.72 B ATOM 653 CG1 VAL B 293 19.841 20.097 5.449 1.00 8.13 B ATOM 654 CG2 VAL B 293 20.259 22.203 6.665 1.00 6.40 B ATOM 655 C VAL B 293 21.808 18.739 6.909 1.00 8.31 B ATOM 656 O VAL B 293 21.085 17.764 7.066 1.00 16.32 B ATOM 657 N GLN B 294 22.989 18.663 6.322 1.00 2.00 B ATOM 658 CA GLN B 294 23.503 17.386 5.883 1.00 12.39 B ATOM 659 CB GLN B 294 24.878 17.543 5.242 1.00 11.94 B ATOM 660 CG GLN B 294 24.870 18.048 3.837 1.00 19.90 B ATOM 661 CD GLN B 294 26.260 18.219 3.307 1.00 27.50 B ATOM 662 OE1 GLN B 294 26.951 19. 176 3.650 1.00 34.53 B ATOM 663 NE2 GLN B 294 26.695 17.281 2.476 1.00 32.69 B ATOM 664 C GLN B 294 23.639 16.481 7.100 1.00 17.46 B ATOM 665 O GLN B 294 23.213 15.333 7.080 1.00 29.23 B ATOM 666 N GLU B 295 24.243 16.996 8.163 1.00 19.83 B ATOM 667 CA GLU B 295 24.427 16.199 9.372 1.00 18.55 B TABLE II (continued) ATOM 668 CB GLU B 295 25.193 17.003 10.431 1.00 23.24 B ATOM 669 CG GLU B 295 26.347 17.828 9.852 1.00 35.83 B ATOM 670 CD GLU B 295 27.276 18.423 10. 908 1.00 41.32 B ATOM 671 OE1 GLU B 295 26.778 18.904 11.959 1.00 38.57 B ATOM 672 OE2 GLU B 295 28.509 18.420 10.663 1.00 43.27 B ATOM 673 C GLU B 295 23.070 15.753 9.917 1.00 20.50 B ATOM 674 O GLU B 295 22.911 14.596 10.307 1.00 17.48 B ATOM 675 N ILE B 296 22.093 16.662 9.945 1.00 17.97 B ATOM 676 CA ILE B 296 20.764 16.306 10.427 1.00 13.56 B ATOM 677 CB ILE B 296 19.807 17.529 10.453 1.00 11.39 B ATOM 678 CG2 ILE B 296 18.398 17.097 10.829 1.00 2.27 B ATOM 679 CG1 ILE B 296 20.297 18.548 11.481 1.00 14.20 B ATOM 680 CD1 ILE B 296 19.365 19.743 11.675 1.00 12.42 B ATOM 681 C ILE B 296 20.176 15.215 9.530 1.00 18.03 B ATOM 682 O ILE B 296 19.745 14.169 10.012 1.00 20.35 B ATOM 683 N THR B 297 20.183 15.447 8.225 1.00 13.00 B ATOM 684 CA THR B 297 19.638 14.475 7.293 1.00 9.41 B ATOM 685 CB THR B 297 19.902 14.877 5.842 1.00 4.74 B ATOM 686 OG1 THR B 297 19.309 16.153 5.589 1.00 15.72 B ATOM 687 CG2 THR B 297 19.300 13.860 4.902 1.00 3.43 B ATOM 688 C THR B 297 20.203 13.079 7.486 1.00 6.01 B ATOM 689 0 THR B 297 19.491 12.090 7.357 1.00 11.21 B ATOM 690 N GLU B 298 21.487 12.996 7.798 1.00 11.88 B ATOM 691 CA GLU B 298 22.143 11.708 7.971 1.00 15.80 B ATOM 692 CB GLU B 298 23.659 11.898 7.969 1.00 27.15 B ATOM 693 CG GLU B 298 24.421 10.600 8.099 1.00 46. 12 B ATOM 694 CD GLU B 298 25.923 10. 788 8.128 1.00 55.59 B ATOM 695 OE1 GLU B 298 26.437 11.434 9.074 1.00 52.45 B ATOM 696 OE2 GLU B 298 26.586 10.280 7.197 1.00 65.53 B ATOM 697 C GLU B 298 21.718 10.990 9.238 1.00 17.79 B ATOM 698 0 GLU B 298 21.554 9.773 9.243 1.00 13.61 B ATOM 699 N TYR B 299 21.557 11.756 10.315 1.00 24.43 B ATOM 700 CA TYR B 299 21.147 11.221 11.612 1.00 19.04 B ATOM 701 CB TYR B 299 21.098 12.336 12.661 1.00 14.95 B ATOM 702 CG TYR B 299 20.511 11.908 13.993 1.00 19.53 B ATOM 703 CD1 TYR B 299 21.153 10.967 14.794 1.00 17.79 B ATOM 704 CE1 TYR B 299 20.611 10.586 16.029 1.00 21.02 B ATOM 705 CD2 TYR B 299 19.310 12.456 14.461 1.00 19.20 B ATOM 706 CE2 TYR B 299 18. 761 12.079 15.695 1.00 15.55 B ATOM 707 CZ TYR B 299 19.417 11.147 16.468 1.00 18.22 B ATOM 708 OH TYR B 299 18.885 10.764 17.673 1.00 21.58 B ATOM 709 C TYR B 299 19.769 10.629 11.471 1.00 18.53 B ATOM 710 0 TYR B 299 19.494 9.555 11.976 1.00 21.24 B ATOM 711 N ALA B 300 18.916 11.360 10.762 1.00 18.64 B ATOM 712 CA ALA B 300 17.531 10.986 10.530 1.00 16.85 B ATOM 713 CB ALA B 300 16.885 12.013 9.638 1.00 18.09 B ATOM 714 C ALA B 300 17.353 9.607 9.935 1.00 13.77 B ATOM 715 O ALA B 300 16.570 8.798 10.435 1.00 6.93 B ATOM 716 N LYS B 301 18.076 9.346 8.856 1.00 7.75 B ATOM 717 CA LYS B 301 17.983 8.064 8.189 1.00 13.28 B ATOM 718 CB LYS B 301 18.921 8.042 6.977 1.00 12.46 B ATOM 719 CG LYS B 301 18.325 8.696 5.740 1.00 17. 07 B ATOM 720 CD LYS B 301 19.244 8.602 4.529 1.00 17. 29 B ATOM 721 CE LYS B 301 20.158 9.816 4.455 1.00 23.76 B ATOM 722 NZ LYS B 301 21.251 9.678 3.449 1.00 29.85 B ATOM 723 C LYS B 301 18.296 6.916 9.139 1.00 14.74 B TABLE II (continued) ATOM 724 O LYS B 301 18. 085 5.749 8.817 1.00 19.37 B ATOM 725 N SER B 302 18.776 7.256 10.325 1.00 9.93 B ATOM 726 CA SER B 302 19.133 6.255 11.309 1.00 8.91 B ATOM 727 CB SER B 302 20.373 6.689 12.068 1.00 12.49 B ATOM 728 OG SER B 302 20.521 5.897 13.228 1.00 22.98 B ATOM 729 C SER B 302 18.040 5.961 12.305 1.00 6.18 B ATOM 730 O SER B 302 18.059 4.924 12.955 1.00 10.16 B ATOM 731 N ILE B 762 17.092 6.875 12.440 1.00 8.52 B ATOM 732 CA ILE B 762 16.009 6.669 13.380 1.00 13.16 B ATOM 733 CB ILE B 762 15.119 7.897 13.468 1.00 10.93 B ATOM 734 CG2 ILE B 762 14.077 7.705 14.556 1.00 4.42 B ATOM 735 CG1 ILE B 762 15.981 9.122 13.767 1.00 6.48 B ATOM 736 CD1 ILE B 762 15.200 10.414 13. 828 1.00 6.15 B ATOM 737 C ILE B 762 15.183 5.474 12.942 1.00 17.74 B ATOM 738 O ILE B 762 14.532 5.509 11.903 1.00 23.39 B ATOM 739 N PRO B 304 15.207 4.393 13.739 1.00 18.12 B ATOM 740 CD PRO B 304 15.705 4.377 15.124 1.00 18.42 B ATOM 741 CA PRO B 304 14.467 3.166 13.449 1.00 15.38 B ATOM 742 CB PRO B 304 14.404 2.473 14.799 1.00 13.66 B ATOM 743 CG PRO B 304 15.648 2.917 15.456 1.00 21.17 B ATOM 744 C PRO B 304 13.088 3.533 12.965 1.00 23.36 B ATOM 745 O PRO B 304 12.295 4.069 13.729 1.00 27.39 B ATOM 746 N GLY B 305 12.809 3.270 11.694 1.00 23.93 B ATOM 747 CA GLY B 305 11.499 3.584 11.154 1.00 22.69 B ATOM 748 C GLY B 305 11.497 4.604 10.035 1.00 27.51 B ATOM 749 O GLY B 305 10.939 4.349 8.977 1.00 35.17 B ATOM 750 N PHE B 306 12.132 5.751 10.267 1.00 29.41 B ATOM 751 CA PHE B 306 12.205 6.852 9.300 1.00 23.72 B ATOM 752 CB PHE B 306 13.247 7.868 9.761 1.00 19.06 B ATOM 753 CG PHE B 306 13.332 9.077 8.890 1.00 14.83 B ATOM 754 CD1 PHE B 306 12.392 10.092 8.994 1.00 9.36 B ATOM 755 CD2 PHE B 306 14.341 9.201 7.956 1.00 19.14 B ATOM 756 CE1 PHE B 306 12.460 11.213 8.180 1.00 2.00 B ATOM 757 CE2 PHE B 306 14.415 10.320 7.138 1.00 22.27 B ATOM 758 CZ PHE B 306 13.474 11.324 7.252 1.00 11.40 B ATOM 759 C PHE B 306 12.504 6.478 7.847 1.00 22.40 B ATOM 760 O PHE B 306 11.886 7.012 6.932 1.00 26.22 B ATOM 761 N VAL B 307 13.453 5.579 7.623 1.00 23.42 B ATOM 762 CA VAL B 307 13.788 5.193 6.261 1.00 21.18 B ATOM 763 CB VAL B 307 14.991 4.232 6.215 1.00 13.59 B ATOM 764 CG1 VAL B 307 16.218 4.997 5.796 1.00 11.71 B ATOM 765 CG2 VAL B 307 15.216 3.574 7.583 1.00 11.36 B ATOM 766 C VAL B 307 12.644 4.556 5.489 1.00 24. 32 B ATOM 767 O VAL B 307 12.647 4.570 4.265 1.00 30.81 B ATOM 768 N ASN B 308 11.659 4.010 6.189 1.00 27.87 B ATOM 769 CA ASN B 308 10.535 3.357 5.522 1.00 30.87 B ATOM 770 CB ASN B 308 10.163 2.080 6.280 1.00 39.07 B ATOM 771 CG ASN B 308 11.221 0.993 6.142 1.00 45.34 B ATOM 772 OD1 ASN B 308 11.436 0.455 5.054 1.00 48.47 B ATOM 773 ND2 ASN B 308 11.890 0.671 7.246 1.00 44.06 B ATOM 774 C ASN B 308 9.291 4.224 5.309 1.00 26. 98 B ATOM 775 O ASN B 308 8.383 3.848 4.571 1.00 28.95 B ATOM 776 N LEU B 309 9.245 5.383 5.953 1.00 28.64 B ATOM 777 CA LEU B 309 8. 117 6.287 5.790 1.00 23.42 B ATOM 778 CB LEU B 309 8.322 7.547 6.617 1.00 19.27 B ATOM 779 CG LEU B 309 8.431 7.431 8.124 1.00 16.77 B TABLE II (continued) ATOM 780 CD1 LEU B 309 8.740 8.793 8.684 1.00 19.26 B ATOM 781 CD2 LEU B 309 7.136 6.898 8.695 1.00 20.34 B ATOM 782 C LEU B 309 8.073 6.685 4.326 1.00 25.88 B ATOM 783 0 LEU B 309 9.063 6.534 3. 618 1.00 29.42 B ATOM 784 N ASP B 310 6.935 7.203 3.878 1.00 27.12 B ATOM 785 CA ASP B 310 6.788 7.640 2.499 1.00 26.63 B ATOM 786 CB ASP B 310 5.375 8.158 2.256 1.00 41.05 B ATOM 787 CG ASP B 310 5.297 9.111 1.079 1.00 52.70 B ATOM 788 OD1 ASP B 310 4.303 9.887 1. 013 1.00 55.62 B ATOM 789 OD2 ASP B 310 6.222 9. 082 0.226 1.00 57.66 B ATOM 790 C ASP B 310 7.799 8.737 2.230 1.00 21.19 B ATOM 791 O ASP B 310 7.771 9.799 2.840 1.00 19.44 B ATOM 792 N LEU B 311 8.696 8.454 1.299 1.00 24.05 B ATOM 793 CA LEU B 311 9.759 9.365 0.909 1.00 21.46 B ATOM 794 CB LEU B 311 10.490 8.776-0. 293 1.00 20.24 B ATOM 795 CG LEU B 311 11.618 9.591-0. 902 1.00 23.60 B ATOM 796 CD1 LEU B 311 12.639 8.667-1. 553 1.00 30.92 B ATOM 797 CD2 LEU B 311 11.034 10.548-1. 908 1.00 14.85 B ATOM 798 C LEU B 311 9.256 10.776 0.610 1.00 22.06 B ATOM 799 0 LEU B 311 9.993 11.751 0.750 1.00 18.98 B ATOM 800 N ASN B 312 8.002 10.892 0.194 1.00 18.77 B ATOM 801 CA ASN B 312 7.470 12.206-0. 085 1.00 24.77 B ATOM 802 CB ASN B 312 6.061 12.115-0. 672 1.00 36.61 B ATOM 803 CG ASN B 312 5.631 13.409-1. 365 1.00 50.23 B ATOM 804 OD1 ASN B 312 6.019 13.676-2. 511 1.00 58.55 B ATOM 805 ND2 ASN B 312 4.841 14.225-0. 668 1.00 50.36 B ATOM 806 C ASN B 312 7.419 12.912 1.261 1.00 24.96 B ATOM 807 0 ASN B 312 7.747 14.093 1.354 1.00 27.31 B ATOM 808 N ASP B 313 7.023 12.159 2.296 1.00 23.93 B ATOM 809 CA ASP B 313 6.892 12.657 3.672 1.00 16.45 B ATOM 810 CB ASP B 313 6.004 11.743 4.516 1.00 9.36 B ATOM 811 CG ASP B 313 4.556 11.863 4.163 1.00 12.00 B ATOM 812 OD1 ASP B 313 4.174 12.876 3.554 1.00 14.83 B ATOM 813 OD2 ASP B 313 3.797 10.946 4.508 1.00 17.67 B ATOM 814 C ASP B 313 8.187 12.856 4.429 1.00 15.53 B ATOM 815 O ASP B 313 8.210 13.608 5.398 1.00 18.43 B ATOM 816 N GLN B 314 9.252 12.173 4.027 1.00 11.11 B ATOM 817 CA GLN B 314 10.531 12.349 4.700 1.00 8.76 B ATOM 818 CB GLN B 314 11.573 11.374 4.187 1.00 13.01 B ATOM 819 CG GLN B 314 11.415 9.980 4.663 1.00 20.33 B ATOM 820 CD GLN B 314 12. 307 9.055 3.901 1. 00 26.57 B ATOM 821 OE1 GLN B 314 13.454 9.385 3.603 1.00 34.54 B ATOM 822 NE2 GLN B 314 11.794 7.883 3.579 1.00 30.43 B ATOM 823 C GLN B 314 11.030 13.734 4.411 1.00 6.46 B ATOM 824 O GLN B 314 11.567 14.391 5.287 1.00 12.45 B ATOM 825 N VAL B 315 10.857 14.171 3.172 1.00 2.00 B ATOM 826 CA VAL B 315 11.316 15.487 2.779 1.00 11.68 B ATOM 827 CB VAL B 315 11.123 15.737 1.280 1.00 9.54 B ATOM 828 CG1 VAL B 315 11.437 17.188 0.945 1.00 2.00 B ATOM 829 CG2 VAL B 315 12.031 14.832 0.502 1.00 7.75 B ATOM 830 C VAL B 315 10.626 16.599 3.539 1.00 13.49 B ATOM 831 O VAL B 315 11.221 17.657 3.752 1.00 16.79 B ATOM 832 N THR B 316 9.379 16.366 3.946 1.00 11.86 B ATOM 833 CA THR B 316 8.617 17.372 4.687 1.00 11.97 B ATOM 834 CB THR B 316 7.107 17.102 4. 650 1.00 7. 04 B ATOM 835 OG1 THR B 316 6. 642 17.179 3.300 1.00 10.31 B TABLE II (continued) ATOM 836 CG2 THR B 316 6.372 18.134 5.477 1.00 2.00 B ATOM 837 C THR B 316 9.053 17.418 6.128 1.00 5.36 B ATOM 838 O THR B 316 9.163 18.481 6.713 1.00 7.35 B ATOM 839 N LEU B 317 9.301 16.252 6.697 1.00 6.40 B ATOM 840 CA LEU B 317 9.737 16.181 8.067 1.00 8.53 B ATOM 841 CB LEU B 317 9.848 14.735 8.492 1.00 8.66 B ATOM 842 CG LEU B 317 8.499 14.034 8.506 1.00 4.70 B ATOM 843 CD1 LEU B 317 8.641 12.723 9.217 1.00 4.41 B ATOM 844 CD2 LEU B 317 7.491 14.882 9.220 1.00 2.00 B ATOM 845 C LEU B 317 11.061 16.892 8.242 1.00 14.56 B ATOM 846 O LEU B 317 11.329 17.449 9.307 1.00 17.26 B ATOM 847 N LEU B 318 11.895 16.870 7.205 1.00 13.54 B ATOM 848 CA LEU B 318 13.178 17.572 7.255 1.00 16.34 B ATOM 849 CB LEU B 318 14.190 16.991 6.260 1.00 11.56 B ATOM 850 CG LEU B 318 15.153 15.895 6.725 1.00 11.51 B ATOM 851 CD1 LEU B 318 15.695 16.229 8.091 1.00 17.14 B ATOM 852 CD2 LEU B 318 14.441 14.591 6.781 1.00 15.83 B ATOM 853 C LEU B 318 12.971 19.047 6.934 1.00 19.17 B ATOM 854 O LEU B 318 13.403 19.904 7.685 1.00 24.26 B ATOM 855 N LYS B 319 12.303 19.335 5.820 1.00 21.58 B ATOM 856 CA LYS B 319 12.041 20.715 5.394 1.00 20.08 B ATOM 857 CB LYS B 319 10.923 20.738 4.318 1.00 21.97 B ATOM 858 CG LYS B 319 10.580 22.116 3.717 1.00 28.76 B ATOM 859 CD LYS B 319 10.007 22.047 2.265 1.00 35.77 B ATOM 860 CE LYS B 319 11.070 21.680 1.175 1.00 36.25 B ATOM 861 NZ LYS B 319 10.563 21.558-0. 256 1.00 9.54 B ATOM 862 C LYS B 319 11.658 21.557 6.602 1.00 14.49 B ATOM 863 O LYS B 319 12.108 22.686 6.751 1.00 16.41 B ATOM 864 N TYR B 320 10.847 20.987 7.482 1.00 7.43 B ATOM 865 CA TYR B 320 10.403 21.692 8.674 1.00 13.30 B ATOM 866 CB TYR B 320 8.981 21.266 9.055 1.00 15.20 B ATOM 867 CG TYR B 320 7.909 21.971 8.266 1.00 19.07 B ATOM 868 CD1 TYR B 320 7.521 21.517 7.008 1.00 26.42 B ATOM 869 CE1 TYR B 320 6.598 22.226 6.239 1.00 24.38 B ATOM 870 CD2 TYR B 320 7.339 23.144 8.740 1.00 17.76 B ATOM 871 CE2 TYR B 320 6.422 23.855 7.984 1.00 20.51 B ATOM 872 CZ TYR B 320 6.060 23.395 6.736 1.00 19.39 B ATOM 873 OH TYR B 320 5.195 24.134 5.975 1.00 20.15 B ATOM 874 C TYR B 320 11.317 21.455 9.853 1.00 17.26 B ATOM 875 O TYR B 320 11.584 22.363 10.633 1.00 23.49 B ATOM 876 N GLY B 321 11.797 20.226 9.968 1.00 5.31 B ATOM 877 CA GLY B 321 12.659 19.855 11.070 1.00 6.04 B ATOM 878 C GLY B 321 13.987 20.560 11.313 1.00 11.26 B ATOM 879 O GLY B 321 14.246 21.016 12.421 1.00 11.83 B ATOM 880 N VAL B 322 14.845 20.647 10.304 1.00 10.14 B ATOM 881 CA VAL B 322 16.138 21.275 10.497 1.00 9.38 B ATOM 882 CB VAL B 322 16.807 21.577 9.133 1.00 8.24 B ATOM 883 CG1 VAL B 322 15.782 21.736 8.100 1.00 5.17 B ATOM 884 CG2 VAL B 322 17.650 22.828 9.201 1.00 17.93 B ATOM 885 C VAL B 322 16.162 22.504 11.418 1.00 9.92 B ATOM 886 O VAL B 322 16.724 22.430 12.502 1.00 14.36 B ATOM 887 N HIS B 323 15.542 23.616 11.041 1.00 17.48 B ATOM 888 CA HIS B 323 15.610 24.804 11.905 1.00 24.66 B ATOM 889 CB HIS B 323 14.691 25.906 11.408 1.00 21.63 B ATOM 890 CG HIS B 323 15.210 26.578 10.188 1.00 31.72 B ATOM 891 CD2 HIS B 323 16.134 27.556 10.040 1.00 35.68 B TABLE II (continued) ATOM 892 ND1 HIS B 323 14.882 26.160 8.915 1.00 39. 42 B ATOM 893 CE1 HIS B 323 15.586 26. 851 8.037 1.00 39. 92 B ATOM 894 NE2 HIS B 323 16.354 27.704 8.693 1.00 38. 33 B ATOM 895 C HIS B 323 15.346 24.569 13.371 1.00 23.29 B ATOM 896 0 HIS B 323 16.058 25.090 14.233 1.00 18. 19 B ATOM 897 N GLU B 324 14.316 23.791 13.659 1.00 21.93 B ATOM 898 CA GLU B 324 13.991 23.505 15.034 1.00 16.63 B ATOM 899 CB GLU B 324 12.803 22.548 15.098 1.00 10.54 B ATOM 900 CG GLU B 324 11.685 23.092 15. 929 1.00 18. 51 B ATOM 901 CD GLU B 324 10.346 23.012 15.232 1.00 23.51 B ATOM 902 OE1 GLU B 324 9.718 21.931 15.285 1.00 25.74 B ATOM 903 OE2 GLU B 324 9.924 24.026 14.622 1.00 27.21 B ATOM 904 C GLU B 324 15.215 22.901 15.708 1. 00 14.70 B ATOM 905 O GLU B 324 15.496 23.204 16.859 1.00 20.44 B ATOM 906 N ILE B 325 15. 958 22.073 14.978 1.00 11.34 B ATOM 907 CA ILE B 325 17.134 21.419 15.539 1.00 9.48 B ATOM 908 CB ILE B 325 17.536 20.163 14.751 1.00 9.38 B ATOM 909 CG2 ILE B 325 18.355 19.256 15.643 1.00 2.00 B ATOM 910 CG1 ILE B 325 16.297 19.438 14.217 1.00 12.69 B ATOM 911 CD1 ILE B 325 15.398 18.852 15.268 1.00 20.56 B ATOM 912 C ILE B 325 18.352 22.331 15.584 1.00 15.71 B ATOM 913 O ILE B 325 19.038 22.388 16.609 1.00 15.20 B ATOM 914 N ILE B 326 18.630 23.033 14.481 1.00 11.96 B ATOM 915 CA ILE B 326 19.775 23.928 14.431 1.00 2.00 B ATOM 916 CB ILE B 326 19.721 24.852 13.215 1.00 2.00 B ATOM 917 CG2 ILE B 326 20.807 25.884 13.296 1.00 5.13 B ATOM 918 CG1 ILE B 326 19.924 24.037 11.943 1.00 7.26 B ATOM 919 CD1 ILE B 326 20. 005 24.875 10.703 1.00 6.45 B ATOM 920 C ILE B 326 19.760 24.743 15.696 1.00 5.52 B ATOM 921 O ILE B 326 20.790 24.953 16.309 1.00 17.20 B ATOM 922 N TYR B 327 18.574 25.173 16.104 1.00 14.07 B ATOM 923 CA TYR B 327 18.388 25.953 17.328 1.00 18.69 B ATOM 924 CB TYR B 327 16.930 26.414 17.428 1.00 25.90 B ATOM 925 CG TYR B 327 16.675 27.752 16.788 1. 00 35.74 B ATOM 926 CD1 TYR B 327 17.026 27.995 15.463 1.00 44.44 B ATOM 927 CE1 TYR B 327 16.848 29.256 14.889 1.00 48.49 B ATOM 928 CD2 TYR B 327 16.129 28.799 17.529 1.00 41.99 B ATOM 929 CE2 TYR B 327 15.944 30.062 16.973 1.00 47.91 B ATOM 930 CZ TYR B 327 16.308 30.287 15.655 1.00 51.71 B ATOM 931 OH TYR B 327 16.157 31. 547 15.118 1.00 54.14 B ATOM 932 C TYR B 327 18.773 25.221 18.624 1.00 19.80 B ATOM 933 O TYR B 327 19.384 25.810 19.508 1.00 18.24 B ATOM 934 N THR B 328 18.418 23.946 18.749 1.00 14.88 B ATOM 935 CA THR B 328 18.755 23.219 19.966 1.00 13.93 B ATOM 936 CB THR B 328 17.969 21.928 20.106 1.00 6.07 B ATOM 937 OG1 THR B 328 18.513 20.957 19.221 1.00 18.99 B ATOM 938 CG2 THR B 328 16.534 22.148 19.770 1.00 5.69 B ATOM 939 C THR B 328 20.228 22.852 20.029 1.00 16.11 B ATOM 940 O THR B 328 20.804 22.760 21.113 1.00 21.71 B ATOM 941 N MET B 329 20.829 22.612 18.869 1.00 16.98 B ATOM 942 CA MET B 329 22.239 22.267 18.829 1.00 21.40 B ATOM 943 CB MET B 329 22.640 21.702 17.468 1.00 23.00 B ATOM 944 CG MET B 329 21. 952 20. 406 17.101 1.00 32.09 B ATOM 945 SD MET B 329 23.027 19.322 16.144 1.00 43.99 B ATOM 946 CE MET B 329 23.403 20.311 14.706 1.00 28. 73 B ATOM 947 C MET B 329 23.019 23.534 19.113 1.00 22.74 B TABLE II (continued) ATOM 948 O MET B 329 24.151 23.483 19.593 1.00 27.32 B ATOM 949 N LEU B 330 22.409 24.679 18.818 1.00 17.33 B ATOM 950 CA LEU B 330 23.073 25.941 19.078 1.00 14.81 B ATOM 951 CB LEU B 330 22.381 27.110 18.365 1.00 12.96 B ATOM 952 CG LEU B 330 23.049 27.505 17.047 1.00 10.19 B ATOM 953 CD1 LEU B 330 22.333 28.655 16.414 1.00 11.86 B ATOM 954 CD2 LEU B 330 24.472 27.888 17.309 1.00 10.68 B ATOM 955 C LEU B 330 23.094 26.160 20.577 1.00 14.47 B ATOM 956 O LEU B 330 24.095 26.576 21.113 1.00 17.94 B ATOM 957 N ALA B 331 22.014 25.868 21.279 1.00 10.27 B ATOM 958 CA ALA B 331 22.063 26.063 22.715 1.00 6.10 B ATOM 959 CB ALA B 331 20.782 25.500 23.375 1.00 2.00 B ATOM 960 C ALA B 331 23.327 25.360 23.269 1.00 11. 69 B ATOM 961 O ALA B 331 24.023 25.897 24.139 1.00 10.25 B ATOM 962 N SER B 332 23.635 24.176 22.734 1.00 10.70 B ATOM 963 CA SER B 332 24.782 23.382 23.173 1.00 11.74 B ATOM 964 CB SER B 332 24.928 22.134 22.307 1.00 9.51 B ATOM 965 OG SER B 332 23.833 21.261 22.494 1.00 17.19 B ATOM 966 C SER B 332 26.084 24. 142 23.142 1.00 10.74 B ATOM 967 O SER B 332 26.983 23.880 23.935 1.00 14.92 B ATOM 968 N LEU B 333 26.181 25.096 22.229 1.00 2.00 B ATOM 969 CA LEU B 333 27.398 25.870 22.078 1.00 2.00 B ATOM 970 CB LEU B 333 27.844 25.828 20.615 1.00 6.93 B ATOM 971 CG LEU B 333 27.525 24.592 19.770 1. 00 5. 54 B ATOM 972 CD1 LEU B 333 28.076 24.799 18.394 1.00 2.00 B ATOM 973 CD2 LEU B 333 28.103 23.354 20.378 1.00 8.10 B ATOM 974 C LEU B 333 27.254 27.319 22.522 1. 00 3.88 B ATOM 975 0 LEU B 333 28.058 28. 162 22.148 1.00 14.57 B ATOM 976 N MET B 334 26.239 27.610 23.325 1.00 7.09 B ATOM 977 CA MET B 334 26.009 28.972 23.790 1.00 12.13 B ATOM 978 CB MET B 334 24.643 29.486 23.307 1.00 15.62 B ATOM 979 CG MET B 334 24.602 29.961 21.860 1.00 18.04 B ATOM 980 SD MET B 334 23.022 30.606 21.314 1.00 25.36 B ATOM 981 CE MET B 334 23.266 30.622 19.629 1.00 24.46 B ATOM 982 C MET B 334 26.041 29.131 25.291 1.00 12.04 B ATOM 983 0 MET B 334 26.010 28.163 26. 036 1.00 19.63 B ATOM 984 N ASN B 335 26.118 30.386 25.708 1.00 9.54 B ATOM 985 CA ASN B 335 26.062 30.782 27.102 1.00 12.70 B ATOM 986 CB ASN B 335 27.390 30.566 27.850 1.00 14.82 B ATOM 987 CG ASN B 335 28.541 31.354 27.278 1.00 20.22 B ATOM 988 OD1 ASN B 335 28.360 32.452 26.770 1.00 25.80 B ATOM 989 ND2 ASN B 335 29.751 30.805 27.390 1.00 28.62 B ATOM 990 C ASN B 335 25.682 32.244 27.012 1.00 14.89 B ATOM 991 0 ASN B 335 25.812 32.829 25.945 1.00 19.93 B ATOM 992 N LYS B 336 25.190 32.829 28.099 1.00 15.29 B ATOM 993 CA LYS B 336 24.770 34.225 28.073 1.00 13.00 B ATOM 994 CB LYS B 336 24.431 34.728 29.484 1.00 13.88 B ATOM 995 CG LYS B 336 25.627 34.830 30. 404 1.00 27.39 B ATOM 996 CD LYS B 336 25.293 35.468 31.752 1.00 39.01 B ATOM 997 CE LYS B 336 25.026 36.961 31.614 1.00 48.51 B ATOM 998 NZ LYS B 336 24.888 37.642 32. 936 1.00 55.83 B ATOM 999 C LYS B 336 25.809 35.147 27.441 1.00 16.01 B ATOM 1000 O LYS B 336 25.471 36.266 27.048 1.00 24.88 B ATOM 1001 N ASP B 337 27.055 34. 681 27.320 1.00 11.69 B ATOM 1002 CA ASP B 337 28.136 35.498 26.753 1.00 17.48 B ATOM 1003 CB ASP B 337 29.410 35.394 27.618 1.00 23.01 B TABLE II (continued) ATOM 1004 CG ASP B 337 29.217 35.914 29.048 1.00 26.48 B ATOM 1005 OD1 ASP B 337 28.606 36.989 29.243 1.00 31.70 B ATOM 1006 OD2 ASP B 337 29.699 35.244 29.985 1.00 24.96 B ATOM 1007 C ASP B 337 28.531 35.255 25.287 1.00 21.28 B ATOM 1008 O ASP B 337 29.045 36.163 24.641 1.00 28.52 B ATOM 1009 N GLY B 338 28.319 34.058 24.746 1.00 25.61 B ATOM 1010 CA GLY B 338 28.708 33.843 23.357 1.00 22.07 B ATOM 1011 C GLY B 338 28.410 32.505 22.702 1.00 17.81 B ATOM 1012 O GLY B 338 27.783 31.627 23.295 1.00 15.66 B ATOM 1013 N VAL B 339 28.861 32.372 21.454 1.00 12.38 B ATOM 1014 CA VAL B 339 28.679 31.149 20.677 1.00 13.17 B ATOM 1015 CB VAL B 339 27.823 31.370 19.410 1.00 13.66 B ATOM 1016 CG1 VAL B 339 26.392 31.605 19.776 1.00 15.07 B ATOM 1017 CG2 VAL B 339 28.340 32.554 18.639 1.00 11.61 B ATOM 1018 C VAL B 339 30.027 30.616 20.209 1.00 17.03 B ATOM 1019 O VAL B 339 30.885 31.383 19.763 1.00 19.91 B ATOM 1020 N LEU B 340 30.205 29.302 20.330 1.00 14.27 B ATOM 1021 CA LEU B 340 31.421 28.633 19.903 1.00 14.64 B ATOM 1022 CB LEU B 340 31.554 27.279 20.595 1.00 9.06 B ATOM 1023 CG LEU B 340 32.284 27.136 21.922 1.00 13.86 B ATOM 1024 CD1 LEU B 340 32.082 25.732 22.464 1.00 17.17 B ATOM 1025 CD2 LEU B 340 33.768 27.414 21.719 1.00 14.89 B ATOM 1026 C LEU B 340 31.340 28.410 18.392 1.00 23.41 B ATOM 1027 O LEU B 340 30.642 27.496 17.925 1.00 26.15 B ATOM 1028 N ILE B 341 32.049 29.241 17.629 1.00 23.84 B ATOM 1029 CA ILE B 341 32.066 29.114 16.173 1.00 18.00 B ATOM 1030 CB ILE B 341 32.250 30.477 15.463 1.00 15.73 B ATOM 1031 CG2 ILE B 341 31.324 31.532 16.081 1.00 12.61 B ATOM 1032 CG1 ILE B 341 33.711 30.915 15.556 1.00 9.37 B ATOM 1033 CD1 ILE B 341 33.985 32.223 14.881 1.00 11.80 B ATOM 1034 C ILE B 341 33.201 28.215 15.696 1.00 13.96 B ATOM 1035 O ILE B 341 33.954 27.658 16.484 1.00 13.15 B ATOM 1036 N SER B 342 33.298 28.094 14.382 1.00 11.01 B ATOM 1037 CA SER B 342 34.322 27.310 13.726 1.00 12.04 B ATOM 1038 CB SER B 342 35.518 28.216 13.430 1.00 12.95 B ATOM 1039 OG SER B 342 36.632 27.465 12.988 1.00 24.63 B ATOM 1040 C SER B 342 34.778 26.085 14.495 1.00 10.20 B ATOM 1041 O SER B 342 35. 959 25.933 14.782 1.00 22.42 B ATOM 1042 N GLU B 343 33.854 25. 193 14.811 1.00 14.81 B ATOM 1043 CA GLU B 343 34.210 23.984 15.554 1.00 25.71 B ATOM 1044 CB GLU B 343 35.039 23.054 14.673 1.00 30. 05 B ATOM 1045 CG GLU B 343 34. 292 22.526 13.468 1. 00 48.18 B ATOM 1046 CD GLU B 343 32. 950 21.928 13.837 1.00 55.68 B ATOM 1047 OE1 GLU B 343 31. 967 22.690 13.990 1.00 59.78 B ATOM 1048 OE2 GLU B 343 32.887 20.690 13.985 1.00 59.93 B ATOM 1049 C GLU B 343 34.974 24.267 16.857 1.00 27.70 B ATOM 1050 O GLU B 343 36.131 23.901 16.997 1.00 30.86 B ATOM 1051 N GLY B 344 34.315 24.922 17.806 1.00 34.20 B ATOM 1052 CA GLY B 344 34.938 25.231 19. 078 1.00 29.94 B ATOM 1053 C GLY B 344 36.313 25.850 18.982 1.00 30.71 B ATOM 1054 O GLY B 344 37.134 25.621 19.864 1.00 37.63 B ATOM 1055 N GLN B 345 36.563 26.635 17.934 1.00 28. 16 B ATOM 1056 CA GLN B 345 37.865 27.284 17.735 1.00 28.71 B ATOM 1057 CB GLN B 345 38.410 26.976 16.346 1.00 31. 72 B ATOM 1058 CG GLN B 345 38.866 25.551 16.148 1.00 39.56 B ATOM 1059 CD GLN B 345 39.609 25.383 14.836 1.00 45.10 B TABLE II (continued) ATOM 1060 OEl GLN B 345 40.594 26.089 14.574 1.00 49.55 B ATOM 1061 NE2 GLN B 345 39.145 24.452 13.998 1.00 36.23 B ATOM 1062 C GLN B 345 37.855 28.798 17.920 1.00 26.99 B ATOM 1063 0 GLN B 345 38.894 29.407 18.176 1.00 28.17 B ATOM 1064 N GLY B 346 36.681 29.400 17.772 1.00 21.31 B ATOM 1065 CA GLY B 346 36.553 30.836 17.936 1.00 18.01 B ATOM 1066 C GLY B 346 35.428 31.096 18.908 1.00 14.71 B ATOM 1067 O GLY B 346 34.667 30.188 19.202 1.00 21.17 B ATOM 1068 N PHE B 347 35.317 32.315 19.415 1.00 11.96 B ATOM 1069 CA PHE B 347 34.255 32.633 20.360 1.00 11.87 B ATOM 1070 CB PHE B 347 34.812 32.614 21.788 1.00 7.31 B ATOM 1071 CG PHE B 347 33.757 32.648 22.865 1.00 11.80 B ATOM 1072 CD1 PHE B 347 32.980 31.523 23.134 1.00 11.77 B ATOM 1073 CD2 PHE B 347 33.539 33.805 23.613 1.00 8.82 B ATOM 1074 CE1 PHE B 347 31.994 31.549 24 138 1. 00 9.97 B ATOM 1075 CE2 PHE B 347 32.561 33.846 24.617 1.00 9.21 B ATOM 1076 CZ PHE B 347 31.787 32.719 24.880 1.00 11.92 B ATOM 1077 C PHE B 347 33.688 34.013 20. 013 1.00 15.95 B ATOM 1078 O PHE B 347 34.360 35.032 20.155 1.00 20.73 B ATOM 1079 N MET B 348 32.450 34.048 19.546 1.00 13.24 B ATOM 1080 CA MET B 348 31.852 35.311 19.179 1.00 14.61 B ATOM 1081 CB MET B 348 31.102 35.176 17.863 1.00 25.34 B ATOM 1082 CG MET B 348 31.056 36.443 17.036 1.00 31.96 B ATOM 1083 SD MET B 348 30.523 36.100 15.347 1.00 41.50 B ATOM. 1084 CE MET B 348 31.995 35.279 14.673 1.00 28. 86' : B ATOM 1085 C MET B 348 30.915 35. 765 20.268 1.00 18.05 B ATOM 1086 O MET B 348 29.962 35. 082 20.629 1.00 20.57 B ATOM 1087 N THR B 349 31.225 36.936 20.793 1.00 20.05 B ATOM 1088 CA THR B 349 30.487 37.587 21.857 1.00 17. 56 B ATOM 1089 CB THR B 349 31.201 38.861 22.236 1.00 19.96 B ATOM 1090 OG1 THR B 349 32.431 38.520 22.879 1.00 25.04 B ATOM 1091 CG2 THR B 349 30. 337 39.719 23.133 1. 00 27.26 B ATOM 1092 C THR B 349 29.051 37.957 21. 511 1.00 19.55 B ATOM 1093 O THR B 349 28.800 38.609 20.499 1.00 21.19 B ATOM 1094 N ARG B 350 28.108 37.565 22.364 1.00 18.36 B ATOM 1095 CA ARG B 350 26.727 37.918 22.110 1.00 19.21 B ATOM 1096 CB ARG B 350 25.777 37.461 23. 223 1.00 18.93 B ATOM 1097 CG ARG B 350 24.548 38.388 23. 374 1.00 18.80 B ATOM 1098 CD ARG B 350 23.211 37.707 23. 752 1. 00 21.20 B ATOM 1099 NE ARG B 350 23.158 37.117 25. 092 1.00 19.58 B ATOM 1100 CZ ARG B 350 22.025 36.869 25. 747 1.00 23.88 B ATOM 1101 NH1 ARG B 350 20.853 37.165 25. 202 1.00 15.49 B ATOM 1102 NH2 ARG B 350 22.060 36.308 26. 944 1.00 25.24 B ATOM 1103 C ARG B 350 26.661 39.427 22. 014 1.00 19.97 B ATOM 1104 O ARG B 350 25.758 39.961 21.371 1.00 35.57 B ATOM 1105 N GLU B 351 27.596 40.139 22.633 1.00 21.10 B ATOM 1106 CA GLU B 351 27.516 41.599 22. 541 1.00 22.21 B ATOM 1107 CB GLU B 351 28.292 42.275 23.675 1.00 20.29 B ATOM 1108 CG GLU B 351 27.456 42.511 24.920 1.00 21.20 B ATOM 1109 CD GLU B 351 26.141 43.192 24.608 1.00 23.47 B ATOM 1110 OE1 GLU B 351 26.161 44.231 23. 908 1.00 26.58 B ATOM 1111 OE2 GLU B 351 25.091 42. 689 25.067 1.00 19.39 B ATOM 1112 C GLU B 351 27.979 42.143 21.202 1.00 21.95 B ATOM 1113 O GLU B 351 27.385 43.071 20.660 1.00 27.75 B ATOM 1114 N PHE B 352 29.039 41.564 20. 665 1.00 21.89 B ATOM 1115 CA PHE B 352 29.553 42.022 19. 384 1.00 18.90 B TABLE II (continued) ATOM 1116 CB PHE B 352 30.838 41.288 19.037 1.00 18.12 B ATOM 1117 CG PHE B 352 31.260 41.464 17.626 1.00 19.06 B ATOM 1118 CD1 PHE B 352 31.556 42.724 17.130 1.00 20.38 B ATOM 1119 CD2 PHE B 352 31.395 40.367 16.790 1.00 20.93 B ATOM 1120 CE1 PHE B 352 31.994 42.887 15.799 1.00 22.18 B ATOM 1121 CE2 PHE B 352 31.831 40.520 15.465 1.00 23.59 B ATOM 1122 CZ PHE B 352 32.130 41.782 14.974 1.00 20.17 B ATOM 1123 C PHE B 352 28.510 41.707 18.335 1.00 23.31 B ATOM 1124 O PHE B 352 28.242 42.515 17.454 1.00 28.80 B ATOM 1125 N LEU B 353 27.913 40.524 18.448 1.00 24.29 B ATOM 1126 CA LEU B 353 26.918 40.081 17.490 1.00 17.42 B ATOM 1127 CB LEU B 353 26.410 38.684 17.840 1.00 15.82 B ATOM 1128 CG LEU B 353 27.235 37.466 17.427 1.00 13.37 B ATOM 1129 CD1 LEU B 353 26.516 36.215 17.914 1.00 16.89 B ATOM 1130 CD2 LEU B 353 27.414 37.436 15.910 1.00 2.97 B ATOM 1131 C LEU B 353 25.749 41.017 17.427 1.00 19.54 B ATOM. 1132 O LEU B 353 25.003 41.006 16.455 1.00 32.78 B ATOM 1133 N LYS B 354 25.584 41.823 18.469 1.00 20.54 B ATOM 1134 CA LYS B 354 24.461 42.764 18.542 1.00 21.49 B ATOM 1135 CB LYS B 354 23.926 42.808 19.979 1.00 26.91 B ATOM 1136 CG LYS B 354 22.465 43.179 20.094 1.00 30.67 B ATOM 1137 CD LYS B 354 22.108 43.576 21.531 1.00 36.17 B ATOM 1138 CE LYS B 354 22.327 42.444 22.522 1.00 37.31 B ATOM 1139 NZ LYS B 354 21.968 42.826 23.940 1.00 44.26 B ATOM 1140 C LYS B 354 24.885 44.164 18.091 1.00 21.75 B ATOM 1141 0 LYS B 354 24.072 45.078 18.029 1.00 27.45 B ATOM 1142 N SER B 355 26.167 44.306 17.776 1.00 21.43 B ATOM 1143 CA SER B 355 26.739 45.567 17.327 1.00 23.55 B ATOM 1144 CB SER B 355 28.123 45.752 17. 950 1.00 26.52 B ATOM 1145 OG SER B 355 29.022 44.734 17.542 1.00 33.39 B ATOM 1146 C SER B 355 26.854 45.689 15. 797 1.00 29.76 B ATOM 1147 O SER B 355 27.359 46.695 15.295 1. 00 35.98 B ATOM 1148 N LEU B 356 26.410 44.669 15. 062 1.00 32.66 B ATOM 1149 CA LEU B 356 26.449 44.688 13. 598 1.00 30.52 B ATOM 1150 CB LEU B 356 26.302 43.278 13.030 1.00 33.40 B ATOM 1151 CG LEU B 356 27.367 42.238 13.373 1.00 31.12 B ATOM 1152 CD1 LEU B 356 26.997 40.867 12.795 1.00 35.86 B ATOM 1153 CD2 LEU B 356 28.682 42.700 12.814 1.00 31.14 B ATOM 1154 C LEU B 356 25.300 45.542 13. 065 1.00 38.07 B ATOM 1155 O LEU B 356 24.370 45.882 13. 813 1.00 32.34 B ATOM 1156 N ARG B 357 25.370 45.858 11.768 1.00 49.72 B ATOM 1157 CA ARG B 357 24.377 46. 684 11.045 1.00 59.78 B ATOM 1158 CB ARG B 357 24.592 46.564 9.523 1.00 60.68 B ATOM 1159 CG ARG B 357 26.029 46.753 9.026 1.00 63.08 B ATOM 1160 CD ARG B 357 26.115 46.540 7.506 1.00 66.02 B ATOM 1161 NE ARG B 357 25.080 47.288 6.790 1.00 69.52 B ATOM 1162 CZ ARG B 357 23.968 46.756 6.289 1.00 68.68 B ATOM 1163 NH1 ARG B 357 23.728 45.458 6.409 1.00 67.68 B ATOM 1164 NH2 ARG B 357 23.082 47.532 5.680 1. 00 71.75 B ATOM 1165 C ARG B 357 22.880 46.418 11.335 1.00 65.11 B ATOM 1166 O ARG B 357 22.477 45.304 11.690 1.00 72.47 B ATOM 1167 N LYS B 358 22.077 47.462 11.128 1.00 65.53 B ATOM 1168 CA LYS B 358 20.626 47.479 11.336 1.00 66.46 B ATOM 1169 CB LYS B 358 19.994 48.469 10.350 1.00 70.47 B ATOM 1170 CG LYS B 358 20.669 49.839 10.375 1.00 73.20 B ATOM 1171 CD LYS B 358 20.058 50.827 9.391 1.00 69. 42 B TABLE II (continued) ATOM 1172 CE LYS B 358 20.796 52.162 9.455 1.00 72.56 B ATOM 1173 NZ LYS B 358 20.130 53.230 8.660 1.00 70.70 B ATOM 1174 C LYS B 358 19.844 46.163 11.299 1.00 66.46 B ATOM 1175 O LYS B 358 18.953 45.952 12.134 1.00 72.26 B ATOM 1176 N PRO B 359 20.139 45.273 10.328 1.00 60.45 B ATOM 1177 CD PRO B 359 20.869 45.551 9.073 1.00 53.56 B ATOM 1178 CA PRO B 359 19.421 43.989 10.240 1.00 57.75 B ATOM 1179 CB PRO B 359 19.268 43.800 8.741 1.00 56.27 B ATOM 1180 CG PRO B 359 20.634 44.277 8.248 1. 00 57.19 B ATOM 1181 C PRO B 359 20.140 42.790 10.880 1.00 52.79 B ATOM 1182 O PRO B 359 19.636 42. 167 11.813 1.00 51.77 B ATOM 1183 N PHE B 360 21.318 42.482 10.345 1.00 49.22 B ATOM 1184 CA PHE B 360 22.150 41.364 10.775 1.00 45.80 B ATOM 1185 CB PHE B 360 23.531 41.480 10.111 1.00 50.96 B ATOM 1186 CG PHE B 360 23.490 41.429 8.594 1.00 50.62 B ATOM 1187 CD1 PHE B 360 24.635 41.695 7.847 1.00 49.37 B ATOM 1188 CD2 PHE B 360 22.321 41.081 7.921 1.00 49.40 B ATOM 1189 CE1 PHE B 360 24.620 41. 613 6.465 1.00 49.70 B ATOM 1190 CE2 PHE B 360 22.299 40.995 6.545 1.00 54.73 B ATOM 1191 CZ PHE B 360 23.450 41. 261 5.814 1.00 55.65 B ATOM 1192 C PHE B 360 22.323 41.164 12.274 1.00 42.99 B ATOM 1193 O PHE B 360 21.778 40.222 12.837 1.00 46.11 B ATOM 1194 N GLY B 361 23.089 42.041 12.916 1.00 42.94 B ATOM 1195 CA GLY B 361 23.326 41.919 14.348 1.00 42.23 B ATOM 1196 C GLY B 361 22.093 41.935 15.236 1.00 39.85 B ATOM 1197 O GLY B 361 22.135 42.373 16.391 1.00 36.81 B ATOM 1198 N ASP B 362 20.991 41.430 14.704 1.00 41.20 B ATOM 1199 CA ASP B 362 19.749 41.409 15.440 1.00 39.24 B ATOM 1200 CB ASP B 362 18. 884 42.580 14.980 1.00 40.72 B ATOM 1201 CG ASP B 362 17.938 43.052 16.041 1.00 44.02 B ATOM 1202 OD1 ASP B 362 17.266 44. 070 15.804 1.00 45.09 B ATOM 1203 OD2 ASP B 362 17.867 42.412 17.107 1.00 46.95 B ATOM 1204 C ASP B 362 19.022 40.086 15.218 1.00 41.42 B ATOM 1205 O ASP B 362 17.911 39.897 15.716 1.00 44.51 B ATOM 1206 N PHE B 363 19.642 39.169 14.476 1.00 40.13 B ATOM 1207 CA PHE B 363 19.003 37.882 14.228 1.00 45.64 B ATOM 1208 CB PHE B 363 19.059 37.522 12.719 1.00 56.77 B ATOM 1209 CG PHE B 363 20.302 36. 786 12.276 1.00 65.20 B ATOM 1210 CD1 PHE B 363 21.570 37.340 12.440 1.00 73.33 B ATOM 1211 CD2 PHE B 363 20.193 35.547 11.643 1.00 72.47 B ATOM 1212 CE1 PHE B 363 22.726 36.669 11.973 1.00 78.18 B ATOM 1213 CE2 PHE B 363 21.333 34.865 11.175 1.00 79.74 B ATOM 1214 CZ PHE B 363 22.604 35.430 11.341 1.00 79.09 B ATOM 1215 C PHE B 363 19.529 36.745 15.104 1.00 39.25 B ATOM 1216 O PHE B 363 18.842 35.744 15.303 1.00 37.79 B ATOM 1217 N MET B 364 20.734 36.906 15.647 1.00 37.73 B ATOM 1218 CA MET B 364 21.323 35.896 16.528 1.00 29.57 B ATOM 1219 CB MET B 364 22.850 36. 035 16. 579 1.00 31.00 B ATOM 1220 CG MET B 364 23.608 35.400 15.434 1.00 41.75 B ATOM 1221 SD MET B 364 23.364 33.617 15.346 1.00 53.03 B ATOM 1222 CE MET B 364 24.043 33.104 16.885 1.00 49.81 B ATOM 1223 C MET B 364 20. 784 36.000 17.961 1.00 25.40 B ATOM 1224 O MET B 364 21.009 35.106 18.767 1.00 22.50 B ATOM 1225 N GLU B 365 20.076 37.079 18.283 1.00 21.75 B ATOM 1226 CA GLU B 365 19.554 37.254 19.637 1. 00 18.66 B ATOM 1227 CB GLU B 365 19.146 38.720 19.849 1.00 17.35 B TABLE II (continued) ATOM 1228 CG GLU B 365 19.119 39.199 21.313 1.00 24. 42 B ATOM 1229 CD GLU B 365 20.473 39.084 22.009 1.00 29.67 B ATOM 1230 OE1 GLU B 365 21.509 39.193 21.320 1.00 40.11 B ATOM 1231 OE2 GLU B 365 20.509 38.898 23.245 1.00 26.20 B ATOM 1232 C GLU B 365 18.391 36. 326 20.044 1.00 22.03 B ATOM 1233 O GLU B 365 18.331 35.857 21.178 1.00 29.65 B ATOM 1234 N PRO B 366 17.449 36.048 19.139 1.00 19.73 B ATOM 1235 CD PRO B 366 17.126 36.607 17.819 1.00 23.85 B ATOM 1236 CA PRO B 366 16.379 35.166 19.603 1.00 14.60 B ATOM 1237 CB PRO B 366 15.402 35.151 18.437 1.00 16.38 B ATOM 1238 CG PRO B 366 15.608 36.485 17.799 1.00 21.96 B ATOM 1239 C PRO B 366 16.920 33.789 19.898 1.00 16.37 B ATOM 1240 O PRO B 366 16.285 33.007 20.596 1.00 20.43 B ATOM 1241 N LYS B 367 18.095 33.483 19.363 1.00 17.53 B ATOM 1242 CA LYS B 367 18.681 32.164 19.604 1.00 22. 98 B ATOM 1243 CB LYS B 367 19.707 31.847 18.517 1.00 24.33 B ATOM 1244 CG LYS B 367 19.067 31.765 17.141 1.00 26. 17 B ATOM 1245 CD LYS B 367 20.095 31.695 16.024 1.00 31.12 B ATOM 1246 CE LYS B 367 19.420 31.719 14.654 1.00 34.39 B ATOM 1247 NZ LYS B 367 18.488 32.889 14.490 1.00 27. 86 B ATOM 1248 C LYS B 367 19.304 32.080 21.004 1.00 21.51 B ATOM 1249 O LYS B 367 19.127 31.074 21.706 1.00 19.20 B ATOM 1250 N PHE B 368 20.007 33.148 21.402 1.00 21.50 B ATOM 1251 CA PHE B 368 20.656 33.255 22.715 1.00 11.70 B ATOM 1252 CB PHE B 368 21.483 34.533 22.831 1.00 4.63 B ATOM 1253 CG PHE B 368 22.831 34.448 22.221 1.00 2.47 B ATOM 1254 CD1 PHE B 368 23.765 33.554 22.699 1.00 12.23 B ATOM 1255 CD2 PHE B 368 23.185 35.302 21.195 1.00 5.62 B ATOM 1256 CE1 PHE B 368 25.034 33.514 22.166 1.00 14.47 B ATOM 1257 CE2 PHE B 368 24.450 35.272 20.654 1.00 2.00 B ATOM 1258 CZ PHE B 368 25.376 34.375 21.141 1.00 5.21 B ATOM 1259 C PHE B 368 19.647 33.275 23.840 1.00 10.65 B ATOM 1260 O PHE B 368 19.965 32.869 24.947 1.00 12.23 B ATOM 1261 N GLU B 369 18.448 33.785 23.592 1.00 7.52 B ATOM 1262 CA GLU B 369 17.466 33.781 24.659 1.00 14.86 B ATOM 1263 CB GLU B 369 16.339 34. 776 24.395 1.00 25.48 B ATOM 1264 CG GLU B 369 16.751 36.223 24.616 1.00 45.09 B ATOM 1265 CD GLU B 369 15.588 37.198 24.516 1.00 58.81 B ATOM 1266 OE1 GLU B 369 14.645 37.085 25.331 1.00 63.00 B ATOM 1267 OE2 GLU B 369 15.620 38.079 23.627 1.00 66.66 B ATOM 1268 C GLU B 369 16.936 32.363 24.760 1.00 12.13 B ATOM 1269 O GLU B 369 16.964 31.760 25.823 1.00 22.19 B ATOM 1270 N PHE B 370 16.479 31.803 23.653 1.00 16.70 B ATOM 1271 CA PHE B 370 15.993 30.432 23.708 1.00 21.02 B ATOM 1272 CB PHE B 370 15.628 29.926 22.313 1.00 12.22 B ATOM 1273 CG PHE B 370 15.550 28.449 22.236 1.00 4.83 B ATOM 1274 CD1 PHE B 370 14.497 27.776 22.795 1.00 2.54 B ATOM 1275 CD2 PHE B 370 16.588 27.725 21.684 1.00 10.68 B ATOM 1276 CE1 PHE B 370 14.476 26.402 22.814 1.00 8.12 B ATOM 1277 CE2 PHE B 370 16.578 26.351 21.694 1.00 12.04 B ATOM 1278 CZ PHE B 370 15.516 25.686 22. 264 1.00 8.64 B ATOM 1279 C PHE B 370 17.072 29.517 24. 328 1.00 20.09 B ATOM 1280 0 PHE B 370 16.763 28.540 25.006 1.00 20.20 B ATOM 1281 N ALA B 371 18.334 29. 850 24. 097 1.00 17.51 B ATOM 1282 CA ALA B 371 19.452 29. 072 24.617 1.00 17.79 B ATOM 1283 CB ALA B 371 20.746 29.607 24. 058 1.00 15.76 B TABLE II (continued) ATOM 1284 C ALA B 371 19.543 29.048 26.135 1.00 20.79 B ATOM 1285 0 ALA B 371 19.594 27.978 26.748 1.00 23.10 B ATOM 1286 N VAL B 372 19. 590 30.236 26.732 1.00 23.43 B ATOM 1287 CA VAL B 372 19.712 30.378 28.181 1.00 21.77 B ATOM 1288 CB VAL B 372 19.753 31.870 28.586 1. 00 13.30 B ATOM 1289 CG1 VAL B 372 19.942 31.986 30.077 1.00 17.10 B ATOM 1290 CG2 VAL B 372 20.893 32.571 27.873 1.00 5.39 B ATOM 1291 C VAL B 372 18.579 29.669 28.923 1.00 21.83 B ATOM 1292 O VAL B 372 18.805 28.971 29.907 1.00 23. 16 B ATOM 1293 N LYS B 373 17.357 29.842 28.445 1.00 21.73 B ATOM 1294 CA LYS B 373 16.210 29.191 29.071 1.00 30.63 B ATOM 1295 CB LYS B 373 14.887 29.733 28.482 1.00 33. 64 B ATOM 1296 CG LYS B 373 14.610 31.209 28.799 1.00 43.27 B ATOM 1297 CD LYS B 373 14.604 31.450 30.322 1.00 55.92 B ATOM 1298 CE LYS B 373 14.296 32.902 30.715 1.00 60.32 B ATOM 1299 NZ LYS B 373 13.959 33.010 32.175 1.00 55.38 B ATOM 1300 C LYS B 373 16.286 27.674 28.864 1.00 26.24 B ATOM 1301 O LYS B 373 15.840 26.901 29.720 1.00 23.34 B ATOM 1302 N PHE B 374 16. 868 27.263 27.733 1.00 19.95 B ATOM 1303 CA PHE B 374 16.979 25.853 27.374 1.00 6.12 B ATOM 1304 CB PHE B 374 17.103 25.706 25.864 1.00 2.00 B ATOM 1305 CG PHE B 374 17.044 24.284 25.390 1.00 5.32 B ATOM 1306 CD1 PHE B 374 15.836 23.593 25.365 1. 00 5.86 B ATOM 1307 CD2 PHE B 374 18.199 23.620 24.988 1.00 8.17 B ATOM 1308 CE1 PHE B 374 15.782 22.263 24.947 1.00 6.56 B ATOM 1309 CE2 PHE B 374 18.149 22.288 24.569 1.00 6.44 B ATOM 1310 CZ PHE B 374 16.941 21.612 24.549 1.00 2.00 B ATOM 1311 C PHE B 374 18.145 25.150 28.031 1.00 8.01 B ATOM 1312 0 PHE B 374 18.077 23.958 28.322 1.00 11.24 B ATOM 1313 N ASN B 375 19.229 25.877 28.255 1.00 4.00 B ATOM 1314 CA ASN B 375 20.364 25.259 28.883 1. 00 2.00 B ATOM 1315 CB ASN B 375 21.631 26.009 28.533 1.00 3.15 B ATOM 1316 CG ASN B 375 22.097 25.715 27.130 1.00 11. 60 B ATOM 1317 OD1 ASN B 375 21.812 24.648 26.568 1.00 15.61 B ATOM 1318 ND2 ASN B 375 22.838 26.648 26.558 1.00 7.37 B ATOM 1319 C ASN B 375 20. 185 25.158 30.379 1.00 2.00 B ATOM 1320 O ASN B 375 21.023 24.614 31.068 1.00 12.77 B ATOM 1321 N ALA B 376 19.069 25.664 30.879 1.00 8.50 B ATOM 1322 CA ALA B 376 18.783 25.600 32.300 1.00 8.71 B ATOM 1323 CB ALA B 376 17.858 26.719 32.709 1.00 8.11 B ATOM 1324 C ALA B 376 18.148 24.262 32.612 1.00 11.20 B ATOM 1325 O ALA B 376 18.055 23.871 33.765 1.00 19.88 B ATOM 1326 N LEU B 377 17.681 23.558 31.595 1.00 11.53 B ATOM 1327 CA LEU B 377 17.111 22.252 31.857 1.00 20.07 B ATOM 1328 CB LEU B 377 16.292 21.768 30.674 1.00 20.12 B ATOM 1329 CG LEU B 377 14.967 22.472 30.414 1.00 21.72 B ATOM 1330 CD1 LEU B 377 14.349 21. 806 29.198 1.00 31.73 B ATOM 1331 CD2 LEU B 377 14.020 22.357 31.604 1.00 14.54 B ATOM 1332 C LEU B 377 18.269 21.291 32.103 1.00 26.01 B ATOM 1333 O LEU B 377 18.062 20.131 32.478 1.00 27.07 B ATOM 1334 N GLU B 378 19.490 21.789 31.884 1.00 31.93 B ATOM 1335 CA GLU B 378 20.719 21. 010 32.067 1.00 34.41 B ATOM 1336 CB GLU B 378 20.982 20.788 33.557 1.00 41.67 B ATOM 1337 CG GLU B 378 20.768 22.014 34.397 1.00 50.95 B ATOM 1338 CD GLU B 378 22.052 22.529 34.996 1.00 58.66 B ATOM 1339 OE1 GLU B 378 23.106 22.464 34.305 1.00 55.27 B TABLE II (continued) ATOM 1340 OE2 GLU B 378 21.996 23.010 36.153 1.00 62.50 B ATOM 1341 C GLU B 378 20. 668 19.636 31.392 1.00 28.02 B ATOM 1342 O GLU B 378 21.223 18.674 31.931 1.00 30.84 B ATOM 1343 N LEU B 379 20.004 19.522 30.244 1.00 18.97 B ATOM 1344 CA LEU B 379 19.937 18.230 29.577 1.00 20.31 B ATOM 1345 CB LEU B 379 19.028 18.300 28.345 1.00 24.83 B ATOM 1346 CG LEU B 379 17.503 18.471 28.419 1.00 25.82 B ATOM 1347 CD1 LEU B 379 16.966 18.360 27.017 1.00 27. 05 B ATOM 1348 CD2 LEU B 379 16.843 17.398 29.270 1.00 23.52 B ATOM 1349 C LEU B 379 21.341 17.817 29.145 1.00 20.73 B ATOM 1350 O LEU B 379 22.236 18.653 29.043 1.00 25.94 B ATOM 1351 N ASP B 380 21.537 16.525 28.899 1.00 19.35 B ATOM 1352 CA ASP B 380 22.840 16.028 28. 458 1.00 25.95 B ATOM 1353 CB ASP B 380 23.479 15.110 29.525 1.00 35.61 B ATOM 1354 CG ASP B 380 23.171 13.636 29.312 1.00 38.67 B ATOM 1355 OD1 ASP B 380 22.344 13.077 30.063 1.00 34.33 B ATOM 1356 OD2 ASP B 380 23.769 13.036 28.392 1.00 51.63 B ATOM 1357 C ASP B 380 22.679 15.292 27.130 1.00 25.50 B ATOM 1358 0 ASP B 380 21.568 14.918 26.752 1.00 23.84 B ATOM 1359 N ASP B 381 23.789 15. 076 26.431 1.00 24.58 B ATOM 1360 CA ASP B 381 23.743 14.431 25.127 1.00 23.26 B ATOM 1361 CB ASP B 381 25.154 14.047 24.688 1.00 20.30 B ATOM 1362 CG ASP B 381 25.972 15.255 24.263 1.00 28.65 B ATOM 1363 OD1 ASP B 381 25.700 15. 833 23.182 1.00 26.28 B ATOM 1364 OD2 ASP B 381 26.883 15.637 25.023 1.00 39.41 B ATOM 1365 C ASP B 381 22.792 13.248 24.978 1.00 25.15 B ATOM 1366 O ASP B 381 22.096 13.144 23. 973 1.00 32.97 B ATOM 1367 N SER B 382 22.740 12.361 25.962 1.00 21.26 B ATOM 1368 CA SER B 382 21.837 11.218 25.865 1.00 20.23 B ATOM 1369 CB SER B 382 21.990 10.325 27.099 1.00 21.06 B ATOM 1370 OG SER B 382 23.262 9.707 27.121 1.00 30.11 B ATOM 1371 C SER B 382 20.381 11.666 25.710 1.00 19.71 B ATOM 1372 O SER B 382 19.627 11.092 24.928 1.00 23.16 B ATOM 1373 N ASP B 383 19.996 12.698 26.453 1.00 15.59 B ATOM 1374 CA ASP B 383 18.639 13.220 26.391 1.00 11.13 B ATOM 1375 CB ASP B 383 18.416 14.263 27.487 1.00 14.93 B ATOM 1376 CG ASP B 383 18.560 13.689 28.909 1.00 21.03 B ATOM 1377 OD1 ASP B 383 17.783 12.780 29.327 1.00 16.18 B ATOM 1378 OD2 ASP B 383 19.461 14.175 29.626 1.00 24.26 B ATOM 1379 C ASP B 383 18.337 13.854 25.038 1.00 12.69 B ATOM 1380 O ASP B 383 17.295 13.585 24.445 1.00 15.80 B ATOM 1381 N LEU B 384 19.255 14.697 24.561 1. 00 8.93 B ATOM 1382 CA LEU B 384 19.101 15.385 23.285 1.00 4.93 B ATOM 1383 CB LEU B 384 20.284 16.314 23.030 1.00 2.00 B ATOM 1384 CG LEU B 384 20.532 17.447 24.026 1.00 2.68 B ATOM 1385 CD1 LEU B 384 21.575 18.381 23.463 1.00 2.00 B ATOM 1386 CD2 LEU B 384 19.260 18. 212 24.288 1.00 2.00 B ATOM 1387 C LEU B 384 18.954 14.413 22.130 1.00 9.68 B ATOM 1388 O LEU B 384 18.134 14.624 21.255 1.00 14.99 B ATOM 1389 N ALA B 385 19.743 13.346 22.116 1.00 13.16 B ATOM 1390 CA ALA B 385 19.645 12.360 21.047 1.00 10.99 B ATOM 1391 CB ALAB 385 20.444 11.138 21.397 1.00 8.37 B ATOM 1392 C ALA B 385 18.176 11.986 20.831 1.00 15.65 B ATOM 1393 O ALA B 385 17. 690 12.005 19.705 1.00 19. 05 B ATOM 1394 N ILE B 386 17.471 11.666 21.916 1.00 11.94 B ATOM 1395 CA ILE B 386 16.058 11.305 21.847 1.00 9.14 B TABLE II (continued) ATOM 1396 CB ILE B 386 15.595 10.601 23.119 1.00 7.30 B ATOM 1397 CG2 ILE B 386 14.206 10.049 22.925 1.00 2. 00 B ATOM 1398 CG1 ILE B 386 16.534 9.453 23.445 1.00 11.70 B ATOM 1399 CD1 ILE B 386 16.051 8.612 24.590 1.00 15.61 B ATOM 1400 C ILE B 386 15.143 12.510 21.632 1.00 11.13 B ATOM 1401 O ILE B 386 14.117 12.392 20.973 1.00 6. 25 B ATOM 1402 N PHE B 387 15.482 13.664 22.196 1.00 8.94 B ATOM 1403 CA PHE B 387 14.641 14.841 22.003 1.00 11.84 B ATOM 1404 CB PHE B 387 15.251 16.054 22.700 1.00 2.00 B ATOM 1405 CG PHE B 387 14.470 17.335 22.507 1.00 2.00 B ATOM 1406 CD1 PHE B 387 13.204 17.488 23.054 1.00 2.00 B ATOM 1407 CD2 PHE B 387 15.035 18.419 21.835 1.00 2.00 B ATOM 1408 CE1 PHE B 387 12.525 18.690 22.945 1.00 2.00 B ATOM 1409 CE2 PHE B 387 14.358 19.620 21.726 1.00 2.00 B ATOM 1410 CZ PHE B 387 13.106 19.754 22.283 1.00 4.29 B ATOM 1411 C PHE B 387 14.539 15.102 20.499 1.00 20.16 B ATOM 1412 0 PHE B 387 13.453 15.111 19.911 1.00 25. 66 B ATOM 1413 N ILE B 388 15.697 15.293 19.884 1.00 20.20 B ATOM 1414 CA ILE B 388 15.802 15.558 18.464 1.00 8.11 B ATOM 1415 CB ILE B 388 17.275 15.526 18.057 1.00 2.00 B ATOM 1416 CG2 ILE B 388 17.432 15.171 16.607 1.00 4.38 B ATOM 1417 CG1 ILE B 388 17.880 16.883 18.361 1.00 2.00 B ATOM 1418 CD1 ILE B 388 19.338 16. 942 18.137 1.00 8.08 B ATOM-1419 C ILE B 388 14.967 14. 634 17.588 1.00 10. 58-B ATOM 1420 O ILE B 388 14.180 15.106 16.788 1.00 12.39 ; B ATOM 1421 N ALA B 389 15.120 13.325 17.721 1.00 13.90 B ATOM 1422 CA ALA B 389 14.322 12.436 16.900 1.00 9.23 B ATOM 1423 CB ALA B 389 14.720 10. 997 17.130 1.00 13.12 B ATOM 1424 C ALA B 389 12.850 12.651 17.242 1.00 9.95 B ATOM 1425 O ALA B 389 11.961 12.285 16.478 1.00 12.32 B ATOM 1426 N VAL B 390 12.573 13.243 18.392 1.00 2.00 B ATOM 1427 CA VAL B 390 11. 184 13.483 18.710 1.00 8.95 B ATOM 1428 CB VAL B 390 10.987 13.790 20.194 1.00 11.89 B ATOM 1429 CG1 VAL B 390 9.643 14.425 20.417 1.00 13.27 B ATOM 1430 CG2 VAL B 390 11.069 12.512 20.988 1.00 15.48 B ATOM 1431 C VAL B 390 10.702 14.646 17.844 1.00 8.75 B ATOM 1432 O VAL B 390 9.573 14.649 17.379 1.00 18.92 B ATOM 1433 N ILE B 391 11.572 15.618 17.607 1.00 10.78 B ATOM 1434 CA ILE B 391 11.243 16.786 16.780 1.00 15.83 B ATOM 1435 CB ILE B 391 12.325 17.862 16.882 1.00 13.37 B ATOM 1436 CG2 ILE B 391 12.000 19.021 15.956 1.00 20.83 B ATOM 1437 CG1 ILE B 391 12.437 18.353 18.310 1.00 16. 22 B ATOM 1438 CD1 ILE B 391 13.500 19.407 18.450 1.00 16.19 B ATOM 1439 C ILE B 391 11.105 16.484 15.285 1.00 15.58 B ATOM 1440 O ILE B 391 10.251 17.041 14.590 1.00 13.02 B ATOM 1441 N ILE B 392 11.988 15.635 14.786 1.00 19. 03 B ATOM 1442 CA ILE B 392 11.982 15.274 13.384 1.00 15.82 B ATOM 1443 CB ILE B 392 13.143 14.338 13.082 1.00 15.21 B ATOM 1444 CG2 ILE B 392 13.290 14.154 11.598 1.00 17.75 B ATOM 1445 CG1 ILE B 392 14.426 14.918 13.649 1.00 12.36 B ATOM 1446 CD1 ILE B 392 15.577 13.999 13.511 1.00 20.01 B ATOM 1447 C ILE B 392 10.674 14.570 13.037 1.00 22.51 B ATOM 1448 O ILE B 392 10.031 14.890 12.038 1.00 22.59 B ATOM 1449 N LEU B 393 10.286 13.621 13. 886 1.00 18. 46 B ATOM 1450 CA LEU B 393 9.073 12.844 13.690 1.00 18.12 B ATOM 1451 CB LEU B 393 9.267 11.454 14.287 1.00 19.53 B TABLE II (continued) ATOM 1452 CG LEU B 393 10.216 10.511 13.552 1.00 18.69 B ATOM 1453 CD1 LEU B 393 10.620 9.348 14.445 1.00 19. 41 B ATOM 1454 CD2 LEU B 393 9.520 10.004 12.315 1.00 20.07 B ATOM 1455 C LEU B 393 7.811 13.471 14.281 1.00 22.01 B ATOM 1456 O LEU B 393 7.265 12.953 15.258 1.00 30.91 B ATOM 1457 N SER B 394 7.345 14.573 13.694 1.00 11.66 B ATOM 1458 CA SER B 394 6.130 15.238 14.154 1.00 9.05 B ATOM 1459 CB SER B 394 6.374 16.723 14.359 1.00 18.03 B ATOM 1460 OG SER B 394 7.538 16.941 15.126 1.00 33.76 B ATOM 1461 C SER B 394 5.027 15.080 13.119 1.00 14.85 B ATOM 1462 O SER B 394 5.176 15.508 11.977 1.00 23.56 B ATOM 1463 N GLY B 395 3.916 14.465 13.519 1.00 21.60 B ATOM 1464 CA GLY B 395 2.792 14.285 12.613 1.00 15.36 B ATOM 1465 C GLY B 395 1.952 15.545 12.537 1.00 21. 64 B ATOM 1466 O GLY B 395 0.798 15.487 12.147 1.00 32.25 B ATOM 1467 N ASP B 396 2.538 16.678 12.919 1.00 25.92 B ATOM 1468 CA ASP B 396 1.876 17.984 12.900 1.00 28.15 B ATOM 1469 CB ASP B 396 2.345 18.854 14.065 1.00 37.34 B ATOM 1470 CG ASP B 396 1. 952 18.305 15.409 1.00 53.63 B ATOM 1471 OD1 ASP B 396 2.331 17. 155 15.732 1.00 63.25 B ATOM 1472 OD2 ASP B 396 1.271 19.040 16.158 1.00 58.66 B ATOM 1473 C ASP B 396 2.235 18.743 11.627 1.00 32.37 B ATOM 1474 O ASP B 396 1.475 19.590 11.152 1.00 29.50 B ATOM 1475 N ARG B 397 3.423 18.459 11.103 1.00 30.10 B ATOM 1476 CA ARG B 397 3.907 19.130 9.916 1.00 25.23 B ATOM 1477 CB ARG B 397 5.135 18.400 9.370 1.00 19.46 B ATOM 1478 CG ARG B 397 6.439 18.823 10. 031 1. 00 18.67 B ATOM 1479 CD ARG B 397 6.285 18.857 11.525 1.00 21.06 B ATOM 1480 NE ARG B 397 7.185 19.797 12.183 1.00 21.28 B ATOM 1481 CZ ARG B 397 8.442 19.529 12.490 1.00 28.28 B ATOM 1482 NH1 ARG B 397 8.959 18.347 12.193 1.00 33.95 B ATOM 1483 NH2 ARG B 397 9.168 20.435 13.117 1.00 30.59 B ATOM 1484 C ARG B 397 2.828 19.218 8.861 1.00 27.84 B ATOM 1485 O ARG B 397 2.046 18.286 8.690 1.00 33.01 B ATOM 1486 N PRO B 398 2.723 20.377 8.187 1.00 25.28 B ATOM 1487 CD PRO B 398 3.165 21. 688 8.696 1.00 20.43 B ATOM 1488 CA PRO B 398 1.718 20.551 7.134 1.00 25.05 B ATOM 1489 CB PRO B 398 1.565 22.076 7.049 1.00 23.79 B ATOM 1490 CG PRO B 398 2.855 22. 597 7.548 1.00 12.40 B ATOM 1491 C PRO B 398 2.124 19.924 5.789 1.00 30.25 B ATOM 1492 O PRO B 398 3.262 20.075 5.343 1.00 33.28 B ATOM 1493 N GLY B 399 1.197 19.205 5.158 1.00 33.70 B ATOM 1494 CA GLY B 399 1.481 18.604 3. 863 1.00 32.45 B ATOM 1495 C GLY B 399 1.854 17.139 3. 866 1.00 28.07 B ATOM 1496 O GLY B 399 2.347 16.610 2.868 1.00 30.52 B ATOM 1497 N LEU B 400 1.612 16.473 4.984 1.00 19.59 B ATOM 1498 CA LEU B 400 1.952 15.068 5.091 1.00 20. 82 B ATOM 1499 CB LEU B 400 2.088 14.653 6.563 1.00 19.72 B ATOM 1500 CG LEU B 400 3.005 15.420 7.535 1.00 18.48 B ATOM 1501 CD1 LEU B 400 2.775 14.843 8.911 1.00 26.27 B ATOM 1502 CD2 LEU B 400 4.478 15.327 7.172 1.00 9.00 B ATOM 1503 C LEU B 400 0.844 14.283 4.444 1.00 18.49 B ATOM 1504 O LEU B 400-0.290 14.732 4.432 1.00 24.21 B ATOM 1505 N LEU B 401 1.171 13.120 3.894 1.00 20. 60 B ATOM 1506 CA LEU B 401 0.165 12.276 3.266 1.00 20.86 B ATOM 1507 CB LEU B 401 0.723 11.619 1.999 1.00 31.26 B TABLE II (continued) ATOM 1508 CG LEU B 401 1.148 12.565 0.857 1.00 28.34 B ATOM 1509 CD1 LEU B 401 0. 064 13.591 0.572 1.00 14.12 B ATOM 1510 CD2 LEU B 401 2.431 13.275 1.239 1.00 37.93 B ATOM 1511 C LEU B 401-0.308 11. 244 4.290 1.00 17.25 B ATOM 1512 O LEU B 401-1.389 11.414 4.835 1.00 23.37 B ATOM 1513 N ASN B 402 0.459 10. 189 4.575 1.00 8.52 B ATOM 1514 CA ASN B 402 0.000 9.253 5.611 1.00 25.08 B ATOM 1515 CB ASN B 402 0. 187 7.766 5.221 1.00 25.16 B ATOM 1516 CG ASN B 402 1.610 7.379 4.984 1.00 34.08 B ATOM 1517 OD1 ASN B 402 2.441 8.199 4.606 1.00 47.79 B ATOM 1518 ND2 ASN B 402 1.900 6.101 5.178 1.00 30.11 B ATOM 1519 C ASN B 402 0.662 9.568 6.952 1.00 27.11 B ATOM 1520 O ASN B 402 1.883 9.587 7.072 1.00 28.86 B ATOM 1521 N VAL B 403-0.180 9.817 7.956 1.00 29.85 B ATOM 1522 CA VAL B 403 0.256 10.203 9.289 1.00 26.35 B ATOM 1523 CB VAL B 403-0.722 11.234 9.857 1.00 25.99 B ATOM 1524 CG1 VAL B 403-0.155 11.886 11.099 1.00 31.42 B ATOM 1525 CG2 VAL B 403-1.013 12.271 8.799 1.00 32.50 B ATOM 1526 C VAL B 403 0.455 9.104 10.329 1. 00 26.55 B ATOM 1527 O VAL B 403 1. 369 9.195 11.145 1.00 24.76 B ATOM 1528 N LYS B 404-0.382 8.070 10.316 1.00 26.74 B ATOM 1529 CA LYS B 404-0.245 7.007 11.312 1.00 25.88 B ATOM 1530 CB LYS B 404-1.230 5.871 11.041 1.00 27.74 B ATOM 1531 CG LYS B 404-2.661 6.262 11.374 1.00 44.45 B ATOM 1532 CD LYS B 404-3.669 5.175 10.991 1.00 52.43 B ATOM 1533 CE LYS B 404-5.106 5.662 11.174 1.00 51.36 B ATOM 1534 NZ LYS B 404-6.092 4.668 10.686 1.00 45.88 B ATOM 1535 C LYS B 404 1.151 6.430 11.470 1.00 23.75 B ATOM 1536 O LYS B 404 1.667 6.355 12.578 1.00 30.94 B ATOM 1537 N PRO B 405 1.795 6.031 10.370 1.00 19.45 B ATOM 1538 CD PRO B 405 1.554 6.326 8.950 1.00 23.95 B ATOM 1539 CA PRO B 405 3.132 5.475 10.554 1.00 19.46 B ATOM 1540 CB PRO B 405 3.528 5. 071 9.139 1.00 9.44 B ATOM 1541 CG PRO B 405 2.941 6.156 8.350 1.00 19.35 B ATOM 1542 C PRO B 405 4.100 6.474 11.190 1.00 20.31 B ATOM 1543 0 PRO B 405 5.136 6.078 11.720 1.00 23.23 B ATOM 1544 N ILE B 406 3.765 7.763 11.143 1.00 22.25 B ATOM 1545 CA ILE B 406 4.628 8.780 11.743 1.00 19.95 B ATOM 1546 CB ILE B 406 4.468 10.176 11.077 1.00 17.93 B ATOM 1547 CG2 ILE B 406 5.159 11.243 11.928 1.00 10.10 B ATOM 1548 CG1 ILE B 406 5.064 10.158 9.667 1.00 17.48 B ATOM 1549 CD1 ILE B 406 5.037 11.495 8.974 1.00 21.15 B ATOM 1550 C ILE B 406 4.311 8.908 13.224 1.00 18.62 B ATOM 1551 O ILE B 406 5.214 8.904 14.059 1.00 19.47 B ATOM 1552 N GLU B 407 3. 031 9. 028 13.553 1.00 20.88 B ATOM 1553 CA GLU B 407 2.658 9.132 14.953 1.00 20.64 B ATOM 1554 CB GLU B 407 1.142 9.251 15.125 1.00 32.04 B ATOM 1555 CG GLU B 407 0.458 10.361 14. 349 1.00 41.57 B ATOM 1556 CD GLU B 407-1.066 10.284 14. 470 1.00 55.33 B ATOM 1557 OE1 GLU B 407-1.613 9.155 14.432 1.00 61.82 B ATOM 1558 OE2 GLU B 407-1.722 11.346 14.589 1.00 59.88 B ATOM 1559 C GLU B 407 3.129 7.844 15.610 1.00 16. 84 B ATOM 1560 O GLU B 407 3.689 7.880 16.683 1.00 20. 48 B ATOM 1561 N ASP B 408 2.910 6.709 14.948 1.00 23.14 B ATOM 1562 CA ASP B 408 3.299 5.401 15. 480 1.00 28. 22 B ATOM 1563 CB ASP B 408 3. 030 4.281 14. 455 1.00 42.15 B TABLE II (continued) ATOM 1564 CG ASP B 408 1.556 4.121 14.113 1.00 52.55 B ATOM 1565 OD1 ASP B 408 0.703 4.304 15.007 1.00 55.16 B ATOM 1566 OD2 ASP B 408 1.255 3.790 12.945 1.00 59.10 B ATOM 1567 C ASP B 408 4.762 5.312 15.922 1.00 30.08 B ATOM 1568 O ASP B 408 5.059 4.728 16.964 1.00 30.99 B ATOM 1569 N ILE B 409 5.675 5.866 15.124 1.00 31.35 B ATOM 1570 CA ILE B 409 7.101 5.835 15. 449 1.00 22.26 B ATOM 1571 CB ILE B 409 7.991 6.147 14.228 1.00 17.05 B ATOM 1572 CG2 ILE B 409 9.426 6.314 14.666 1.00 8.72 B ATOM 1573 CG1 ILE B 409 7.900 5.024 13.205 1.00 17.92 B ATOM 1574 CD1 ILE B 409 8.719 5.281 11.968 1.00 16.74 B ATOM 1575 C ILE B 409 7.404 6.865 16.517 1.00 28.34 B ATOM 1576 O ILE B 409 8.244 6.629 17.380 1.00 38.54 B ATOM 1577 N GLN B 410 6.726 8.008 16.452 1.00 23.84 B ATOM 1578 CA GLN B 410 6.933 9.070 17.434 1. 00 23.14 B ATOM 1579 CB GLN B 410 6.192 10.349 17.044 1.00 20.80 B ATOM 1580 CG GLN B 410 5.978 11.263 18.250 1.00 17.87 B ATOM 1581 CD GLN B 410 5.646 12.679 17.878 1.00 22.81 B ATOM 1582 OE1 GLN B 410 4.534 12.972 17. 441 1.00 33.73 B ATOM 1583 NE2 GLN B 410 6.616 13. 576 18.044 1.00 10.60 B ATOM 1584 C GLN B 410 6.502 8.713 18.850 1.00 26.07 B ATOM 1585 O GLN B 410 7.222 8.952 19. 815 1.00 33.48 B ATOM 1586 N ASP B 411 5.304 8.170 18.978 1.00 34.87 B ATOM 1587 CA ASP B 411 4.788 7.815 20.286 1.00 38.75 B ATOM 1588 CB ASP B 411 3.443 7.092 20.144 1.00 49.01 B ATOM 1589 CG ASP B 411 2. 661 7.067 21.437 1.00 61.58 B ATOM 1590 OD1 ASP B 411 2.405 8.161 21.990 1.00 66.56 B ATOM 1591 OD2 ASP B 411 2.305 5.958 21.900 1.00 70.05 B ATOM 1592 C ASP B 411 5.796 6.941 21. 016 1.00 35.80 B ATOM 1593 O ASP B 411 5.964 7.059 22.229 1.00 37.35 B ATOM 1594 N ASN B 412 6.493 6.088 20.277 1.00 30.35 B ATOM 1595 CA ASN B 412 7.471 5.200 20.891 1.00 30.84 B ATOM 1596 CB ASN B 412 7.770 4.048 19.945 1.00 30. 99 B ATOM 1597 CG ASN B 412 8.179 2.811 20.680 1.00 37.77 B ATOM 1598 OD1 ASN B 412 9.316 2.358 20.564 1.00 43.17 B ATOM 1599 ND2 ASN B 412 7.252 2.252 21.463 1.00 41.40 B ATOM 1600 C ASN B 412 8.774 5.900 21. 316 1.00 31.52 B ATOM 1601 O ASN B 412 9.389 5.535 22.326 1.00 29.24 B ATOM 1602 N LEU B 413 9. 199 6. 889 20.532 1. 00 25.85 B ATOM 1603 CA LEU B 413 10. 387 7.659 20.854 1.00 18.06 B ATOM 1604 CB LEU B 413 10. 670 8. 691 19.773 1.00 16.09 B ATOM 1605 CG LEU B 413 11.288 8.274 18.457 1.00 18.40 B ATOM 1606 CD1 LEU B 413 11.383 9.483 17.540 1.00 18.16 B ATOM 1607 CD2 LEU B 413 12.661 7.699 18.736 1.00 21. 77 B ATOM 1608 C LEU B 413 10.051 8.399 22.143 1.00 25.22 B ATOM 1609 O LEU B 413 10.773 8.312 23.137 1.00 30.48 B ATOM 1610 N LEU B 414 8.943 9.135 22.123 1. 00 17.21 B ATOM 1611 CA LEU B 414 8.532 9.879 23.296 1.00 19.08 B ATOM 1612 CB LEU B 414 7.084 10.343 23. 146 1.00 14.57 B ATOM 1613 CG LEU B 414 6.965 11.552 22.212 1.00 10.95 B ATOM 1614 CD1 LEU B 414 5.614 11.583 21.580 1.00 8.00 B ATOM 1615 CD2 LEU B 414 7.221 12.827 22.978 1.00 8.92 B ATOM 1616 C LEU B 414 8.732 9.017 24.532 1. 00 20.71 B ATOM 1617 O LEU B 414 9.533 9.354 25.381 1.00 30.87 B ATOM 1618 N GLN B 415 8.048 7.891 24.632 1.00 22.84 B ATOM 1619 CA GLN B 415 8.255 7.041 25.794 1.00 22.09 B TABLE II (continued) ATOM 1620 CB GLN B 415 7.652 5.654 25.560 1.00 28.02 B ATOM 1621 CG GLN B 415 6.135 5.625 25.475 1.00 34.13 B ATOM 1622 CD GLN B 415 5.622 4.326 24.886 1.00 45.47 B ATOM 1623 OE1 GLN B 415 6.058 3.242 25.279 1.00 47.81 B ATOM 1624 NE2 GLN B 415 4.689 4.425 23.941 1.00 48.89 B ATOM 1625 C GLN B 415 9.761 6.919 26.082 1.00 22.24 B ATOM 1626 O GLN B 415 10.207 7. 240 27.180 1.00 26.26 B ATOM 1627 N ALA B 416 10.548 6.473 25.104 1.00 19.62 B ATOM 1628 CA ALA B 416 11.991 6.337 25.307 1.00 16.57 B ATOM 1629 CB ALA B 416 12.691 6.051 24.003 1.00 13.92 B ATOM 1630 C ALA B 416 12.548 7.611 25.894 1.00 24.55 B ATOM 1631 O ALA B 416 13.506 7.581 26.666 1.00 32.37 B ATOM 1632 N LEU B 417 11.951 8.736 25.512 1.00 28.59 B ATOM 1633 CA LEU B 417 12.386 10.042 26.005 1.00 29.54 B ATOM 1634 CB LEU B 417 11.734 11.177 25.187 1.00 23.21 B ATOM 1635 CG LEU B 417 11.934 12.624 25.674 1.00 19.24 B ATOM 1636 CD1 LEU B 417 13.422 12.982 25.656 1.00 9.77 B ATOM 1637 CD2 LEU B 417 11.129 13. 585 24.804 1.00 13.19 B ATOM 1638 C LEU B 417 12.029 10.190 27.480 1.00 21.99 B ATOM 1639 O LEU B 417 12.840 10.634 28.281 1.00 24.64 B ATOM 1640 N GLU B 418 10.814 9.807 27.838 1.00 19.14 B ATOM 1641 CA GLU B 418 10.393 9.917 29.214 1.00 17.65 B ATOM 1642 CB GLU B 418 8.945 9.482 29.389 1.00 16.72 B ATOM 1643 CG GLU B 418 8.445 9.734 30.782 1.00 27.43 B ATOM 1644 CD GLU B 418 6.963 9.503 30.925 1.00 38.54 B ATOM 1645 OE1 GLU B 418 6. 488 8.413 30.536 1.00 45. 36 B ATOM 1646 OE2'GLU B 418 6.275 10.411 31.434 1.00 36.88 B ATOM 1647 C GLU B 418 11.292 9.050 30.062 1.00 18.37 B ATOM 1648 O GLU B 418 11.973 9.549 30.953 1.00 20.24 B ATOM 1649 N LEU B 419 11.324 7.753 29.785 1.00 20.33 B ATOM 1650 CA LEU B 419 12. 167 6.867 30.576 1.00 21.38 B ATOM 1651 CB LEU B 419 12.225 5.467 29.957 1.00 19.38 B ATOM 1652 CG LEU B 419 12.276 4.293 30.956 1.00 23.36 B ATOM 1653 CD1 LEU B 419 12.271 2.973 30.200 1.00 25.02 B ATOM 1654 CD2 LEU B 419 13.513 4.387 31.821 1.00 27. 33 B ATOM 1655 C LEU B 419 13.581 7.442 30.728 1.00 21.60 B ATOM 1656 O LEU B 419 14.081 7.560 31.843 1.00 26.55 B ATOM 1657 N GLN B 420 14.231 7.815 29. 630 1.00 21.09 B ATOM 1658 CA GLN B 420 15.572 8.371 29.750 1.00 14.63 B ATOM 1659 CB GLN B 420 16.053 8.892 28.398 1.00 14.74 B ATOM 1660 CG GLN B 420 17.548 8.706 28.145 1.00 20.45 B ATOM 1661 CD GLN B 420 18.394 9.717 28.866 1.00 19.79 B ATOM 1662 OE1 GLN B 420 18.368 9.792 30.081 1.00 32.28 B ATOM 1663 NE2 GLN B 420 19.152 10.507 28.118 1.00 18.06 B ATOM 1664 C GLN B 420 15.550 9.503 30.783 1.00 18.64 B ATOM 1665 O GLN B 420 16.289 9.461 31.755 1.00 21.54 B ATOM 1666 N LEU B 421 14.680 10. 492 30.598 1.00 20.96 B ATOM 1667 CA LEU B 421 14.589 11.624 31.525 1.00 21.42 B ATOM 1668 CB LEU B 421 13.559 12.656 31.049 1.00 22.11 B ATOM 1669 CG LEU B 421 13. 776 13.423 29.745 1.00 25.60 B ATOM 1670 CD1 LEU B 421 12.651 14.446 29.565 1.00 22.38 B ATOM 1671 CD2 LEU B 421 15.136 14. 111 29. 772 1.00 23.98 B ATOM 1672 C LEU B 421 14.232 11.261 32.962 1.00 24.73 B ATOM 1673 0 LEU B 421 14.401 12.085 33.861 1.00 35. 05 B ATOM 1674 N LYS B 422 13.706 10.060 33.188 1.00 28. 60 B ATOM 1675 CA LYS B 422 13. 338 9. 649 34.552 1.00 26. 60 B TABLE II (continued) ATOM 1676 CB LYS B 422 12.255 8.560 34.538 1.00 26.13 B ATOM 1677 CG LYS B 422 10.951 8.923 35.227 1.00 32.67 B ATOM 1678 CD LYS B 422 10.213 10.034 34.494 1.00 46.57 B ATOM 1679 CE LYS B 422 8.812 10.253 35.096 1.00 59.16 B ATOM 1680 NZ LYS B 422 8.039 11.404 34.502 1.00 64.63 B ATOM 1681 C LYS B 422 14.577 9.091 35.217 1.00 21.26 B ATOM 1682 O LYS B 422 14.841 9.352 36.384 1.00 23.24 B ATOM 1683 N LEU B 423 15.340 8.317 34.462 1.00 21.42 B ATOM 1684 CA LEU B 423 16.539 7.732 35.004 1.00 19.39 B ATOM 1685 CB LEU B 423 17.066 6.626 34.086 1.00 16.56 B ATOM 1686 CG LEU B 423 16.093 5.543 33.598 1.00 23.90 B ATOM 1687 CD1 LEU B 423 16.895 4.399 32.978 1.00 27.59 B ATOM 1688 CD2 LEU B 423 15.235 5.014 34.745 1.00 32.08 B ATOM 1689 C LEU B 423 17.616 8. 789 35.212 1.00 29.79 B ATOM 1690 O LEU B 423 17.943 9.109 36.360 1.00 33.17 B ATOM 1691 N ASN B 424 18.139 9.351 34.115 1.00 34.28 B ATOM 1692 CA ASN B 424 19.224 10.336 34.189 1.00 35.46 B ATOM 1693 CB ASN B 424 19.838 10.560 32.800 1.00 41.03 B ATOM 1694 CG ASN B 424 21.361 10.672 32.848 1.00 53.17 B ATOM 1695 OD1 ASN B 424 22.068 9.661 32.928 1.00 55.53 B ATOM 1696 ND2 ASN B 424 21.872 11.904 32.816 1.00 55.50 B ATOM 1697 C ASN B 424 18.931 11.700 34.839 1.00 35.52 B ATOM 1698 O ASN B 424 19.816 12.575 34.880 1.00 39.43 B ATOM 1699 N HIS B 425 17.717 11.889 35.357 1.00 36.72 B ATOM 1700 CA HIS B 425 17.364 13.160 36.005 1.00 39.35 B ATOM 1701 CB HIS B 425 16.675 14.123 35.005 1.00 35.16 B ATOM 1702 CG HIS B 425 17.586 14.670 33.953 1.00 25.83 B ATOM 1703 CD2 HIS B 425 17.530 14.602 32.604 1.00 28.44 B ATOM 1704 ND1 HIS B 425 18.730 15.371 34.255 1.00 30.08 B ATOM 1705 CE1 HIS B 425 19.343 15.708 33.135 1.00 25.32 B ATOM 1706 NE2 HIS B 425 18.636 15.253 32.119 1.00 26.70 B ATOM 1707 C HIS B 425 16.452 12.964 37.226 1.00 46.17 B ATOM 1708 O HIS B 425 15.214 13.060 37.129 1.00 51.85 B ATOM 1709 N PRO B 426 17. 046 12.666 38.394 1.00 47.50 B ATOM 1710 CD PRO B 426 18.423 12.218 38.670 1.00 40.64 B ATOM 1711 CA PRO B 426 16.190 12.484 39.571 1.00 48.75 B ATOM 1712 CB PRO B 426 17.101 11.731 40.544 1.00 43.73 B ATOM 1713 CG PRO B 426 18.465 12.216 40.176 1.00 36.97 B ATOM 1714 C PRO B 426 15.703 13.831 40.119 1.00 47.53 B ATOM 1715 O PRO B 426 14.556 13.959 40. 563 1.00 39.60 B ATOM 1716 N GLU B 427 16.580 14.831 40.059 1.00 49.79 B ATOM 1717 CA GLU B 427 16.265 16.160 40. 555 1.00 56.61 B ATOM 1718 CB GLU B 427 17.421 17.122 40.271 1.00 58.78 B ATOM 1719 CG GLU B 427 18.475 17.154 41.390 1.00 68.62 B ATOM 1720 CD GLU B 427 19.498 16.018 41.313 1.00 71.55 B ATOM 1721 OE1 GLU B 427 19.135 14.912 40. 861 1.00 75. 36 B ATOM 1722 OE2 GLU B 427 20.665 16.229 41.719 1.00 68.13 B ATOM 1723 C GLU B 427 14.968 16.705 39.983 1.00 62.24 B ATOM 1724 0 GLU B 427 14.006 16.923 40.721 1. 00 67.64 B ATOM 1725 N SER B 428 14.940 16.921 38.671 1.00 66.97 B ATOM 1726 CA SER B 428 13.744 17.437 38.008 1.00 73.31 B ATOM 1727 CB SER B 428 14.076 17.878 36.578 1.00 77.72 B ATOM 1728 OG SER B 428 12.911 18.306 35.883 1.00 84.00 B ATOM 1729 C SER B 428 12.646 16.374 37.971 1.00 75.79 B ATOM 1730 0 SER B 428 12.604 15.531 37.058 1.00 76.00 B ATOM 1731 N SER B 429 11.761 16.417 38.966 1. 00 76.34 B TABLE II (continued) ATOM 1732 CA SER B 429 10.666 15.455 39.055 1.00 76.89 B ATOM 1733 CB SER B 429 9.710 15.832 40.197 1.00 78.45 B ATOM 1734 OG SER B 429 10.368 15.812 41.455 1.00 76.69 B ATOM 1735 C SER B 429 9.906 15.431 37.739 1.00 74.13 B ATOM 1736 O SER B 429 9.732 14.371 37.124 1.00 76.33 B ATOM 1737 N GLN B 430 9.475 16.611 37.301 1.00 69.21 B ATOM 1738 CA GLN B 430 8.726 16.716 36.060 1.00 62.84 B ATOM 1739 CB GLN B 430 7.353 17.342 36.318 1.00 69.24 B ATOM 1740 CG GLN B 430 6.263 16.531 35.654 1.00 77.59 B ATOM 1741 CD GLN B 430 6.814 15.742 34.467 1.00 79.47 B ATOM 1742 OE1 GLN B 430 7.135 16.312 33.418 1.00 77.68 B ATOM 1743 NE2 GLN B 430 6.956 14.428 34.644 1.00 82.95 B ATOM 1744 C GLN B 430 9.432 17.471 34.937 1.00 50.63 B ATOM 1745 O GLN B 430 9.070 18.612 34.607 1.00 46.47 B ATOM 1746 N LEU B 431 10.425 16.814 34.342 1.00 34.17 B ATOM 1747 CA LEU B 431 11.183 17.404 33.258 1.00 17.81 B ATOM 1748 CB LEU B 431 12.526 16.718 33.122 1.00 8.81 B ATOM 1749 CG LEU B 431 13.748 17.618 33.216 1.00 10.26 B ATOM 1750 CD1 LEU B 431 14.985 16.876 32.682 1.00 2.00 B ATOM 1751 CD2 LEU B 431 13.499 18.878 32.420 1.00 8.98 B ATOM 1752 C LEU B 431 10. 414 17.242 31.966 1.00 22.19 B ATOM 1753 O LEU B 431 9.995 18.222 31.362 1.00 23.04 B ATOM 1754 N PHE B 432 10.232 15.991 31.556 1.00 22.81 B ATOM 1755 CA PHE B 432 9.517 15.637 30.332 1.00 20.08 B ATOM 1756 CB PHE B 432 8.845 14.286 30.504 1.00 22.49 B ATOM 1757 CG PHE B 432 8.045 13.848 29.308 1.00 27.91 B ATOM 1758 CD1 PHE B 432 8.630 13.773 28.054 1.00 31.10 B ATOM 1759 CD2 PHE B 432 6.716 13.461 29.447 1.00 28.68 B ATOM 1760 CE1 PHE B 432 7.905 13.317 26.963 1.00 35.47 B ATOM 1761 CE2 PHE B 432 5.984 13.004 28.362 1.00 30.98 B ATOM 1762 CZ PHE B 432 6.578 12.931 27.121 1.00 36.29 B ATOM 1763 C PHE B 432 8.474 16.637 29.867 1.00 22.17 B ATOM 1764 O PHE B 432 8.274 16.810 28.675 1.00 25.91 B ATOM 1765 N ALA B 433 7.794 17.279 30.807 1.00 26.08 B ATOM 1766 CA ALA B 433 6.774 18.262 30.469 1.00 24.88 B ATOM 1767 CB ALA B 433 5.978 18.612 31.689 1.00 29.98 B ATOM 1768 C ALA B 433 7.424 19.510 29.923 1.00 25.95 B ATOM 1769 O ALA B 433 7.009 20.043 28.899 1.00 27.74 B ATOM 1770 N LYS B 434 8.439 19.982 30.634 1.00 29.62 B ATOM 1771 CA LYS B 434 9.176 21.172 30.229 1.00 31.61 B ATOM 1772 CB LYS B 434 10.299 21.468 31.234 1.00 41.22 B ATOM 1773 CG LYS B 434 9.814 21.961 32.590 1.00 47.30 B ATOM 1774 CD LYS B 434 10.956 21.969 33.603 1.00 59. 90 B ATOM 1775 CE LYS B 434 10.561 22.671 34.907 1.00 64.56 B ATOM 1776 NZ LYS B 434 10.346 24.147 34.705 1.00 65.85 B ATOM 1777 C LYS B 434 9.753 21.019 28.820 1.00 24.85 B ATOM 1778 0 LYS B 434 9.653 21.939 28.013 1.00 20.83 B ATOM 1779 N LEU B 435 10.364 19. 874 28.519 1.00 24.55 B ATOM 1780 CA LEU B 435 10.902 19.670 27.172 1. 00 27.56 B ATOM 1781 CB LEU B 435 11.416 18.235 26.977 1.00 19.21 B ATOM 1782 CG LEU B 435 12.833 17.852 27.389 1.00 15. 46 B ATOM 1783 CD1 LEU B 435 13.122 16.434 26.914 1.00 13.13 B ATOM 1784 CD2 LEU B 435 13.816 18.826 26. 783 1.00 16.84 B ATOM 1785 C LEU B 435 9.789 19.943 26. 149 1.00 35.74 B ATOM 1786 O LEU B 435 9.909 20.839 25.302 1.00 39.67 B ATOM 1787 N LEU B 436 8.705 19.170 26.252 1.00 38.18 B TABLE II (continued) ATOM 1788 CA LEU B 436 7.548 19.288 25.363 1.00 34.93 B ATOM 1789 CB LEU B 436 6.406 18.403 25.858 1.00 34.74 B ATOM 1790 CG LEU B 436 6.791 16.946 26.121 1.00 40.66 B ATOM 1791 CD1 LEU B 436 5.526 16.111 26.293 1.00 41.98 B ATOM 1792 CD2 LEU B 436 7.631 16.408 24.966 1.00 43.28 B ATOM 1793 C LEU B 436 7.052 20.719 25.232 1.00 35.05 B ATOM 1794 O LEU B 436 6.502 21.094 24.196 1.00 35.49 B ATOM 1795 N GLN B 437 7.230 21.512 26. 283 1.00 36.64 B ATOM 1796 CA GLN B 437 6.811 22.906 26.237 1.00 43.50 B ATOM 1797 CB GLN B 437 6.711 23.491 27.653 1.00 50.37 B ATOM 1798 CG GLN B 437 5.297 23.869 28.088 1.00 51.37 B ATOM 1799 CD GLN B 437 4. 700 24.956 27.220 1.00 58.10 B ATOM 1800 OE1 GLN B 437 5.284 26.027 27.070 1.00 65.51 B ATOM 1801 NE2 GLN B 437 3.532 24.687 26.641 1.00 54.76 B ATOM 1802 C GLN B 437 7.830 23.688 25.400 1.00 42.08 B ATOM 1803 O GLN B 437 7.463 24.612 24.661 1.00 44.92 B ATOM 1804 N LYS B 438 9.106 23.317 25.514 1.00 33.37 B ATOM 1805 CA LYS B 438 10.154 23.977 24.743 1.00 27. 25 B ATOM 1806 CB LYS B 438 11.545 23.567 25.235 1.00 26.15 B ATOM 1807 CG LYS B 438 12.017 24.233 26.538 1.00 36.31 B ATOM 1808 CD LYS B 438 12. 558 25.670 26.341 1.00 36.55 B ATOM 1809 CE LYS B 438 11.487 26.760 26.517 1.00 38.16 B ATOM 1810 NZ LYS B 438 10.986 26.889 27.929 1.00 36.79 B ATOM 1811 C LYS B 438 10. 000 23.571 23.284 1.00 22.59 B ATOM 1812 O LYS B 438 10. 35'7 24.328 22.385 1.00 24.75 B ATOM 1813 N MET B 439 9.456 22.380 23.045 1.00 23.14 B ATOM 1814 CA MET B 439 9.290 21.897 21. 676 1.00 21.94 B ATOM 1815 CB MET B 439 8.524 20.569 21.658 1.00 17.04 B ATOM 1816 CG MET B 439 8.785 19.683 20.460 1.00 15.47 B ATOM 1817 SD MET B 439 7.986 18.091 20.692 1.00 25.82 B ATOM 1818 CE MET B 439 9.100 17.350 21.750 1.00 22.86 B ATOM 1819 C MET B 439 8.518 22.957 20.935 1.00 19.72 B ATOM 1820 O MET B 439 9.015 23.558 19.989 1.00 24.39 B ATOM 1821 N THR B 440 7.307 23.206 21.407 1.00 25.96 B ATOM 1822 CA THR B 440 6.421 24.196 20. 818 1.00 29.59 B ATOM 1823 CB THR B 440 5.146 24.311 21.640 1.00 31.22 B ATOM 1824 OG1 THR B 440 4.304 23. 183 21.370 1.00 36.57 B ATOM 1825 CG2 THR B 440 4.427 25.610 21.324 1.00 32.37 B ATOM 1826 C THR B 440 7.045 25.578 20.711 1.00 31.17 B ATOM 1827 O THR B 440 6.919 26.245 19.692 1.00 31.90 B ATOM 1828 N ASP B 441 7.707 26.015 21.771 1.00 32.75 B ATOM 1829 CA ASP B 441 8.323 27.326 21.765 1.00 36.35 B ATOM 1830 CB ASP B 441 9.114 27.549 23.062 1.00 48.81 B ATOM 1831 CG ASP B 441 8.209 27.820 24.267 1.00 59.65 B ATOM 1832 OD1 ASP B 441 8.734 27.893 25.401 1.00 66.37 B ATOM 1833 OD2 ASP B 441 6.978 27.968 24.084 1.00 62.54 B ATOM 1834 C ASP B 441 9.222 27.525 20.551 1.00 30.04 B ATOM 1835 O ASP B 441 9.371 28.647 20.070 1.00 34.65 B ATOM 1836 N LEU B 442 9.817 26.445 20.048 1.00 28.40 B ATOM 1837 CA LEU B 442 10.699 26.540 18. 881 1.00 23.26 B ATOM 1838 CB LEU B 442 11.530 25.258 18.720 1.00 13.90 B ATOM 1839 CG LEU B 442 12.790 25. 059 19.575 1.00 13.79 B ATOM 1840 CD1 LEU B 442 13.226 23.630 19. 471 1.00 12.87 B ATOM 1841 CD2 LEU B 442 13.911 25.964 19. 122 1.00 19.93 B ATOM 1842 C LEU B 442 9.911 26.807 17.595 1.00 26.26 B ATOM 1843 O LEU B 442 10.305 27.652 16.790 1.00 29.42 B TABLE II (continued) ATOM 1844 N ARG B 443 8.802 26.086 17.406 1.00 23.58 B ATOM 1845 CA ARG B 443 7.962 26.260 16.224 1.00 15.21 B ATOM 1846 CB ARG B 443 6.604 25.575 16.392 1.00 16. 62 B ATOM 1847 CG ARG B 443 6.678 24.059 16.496 1.00 23.45 B ATOM 1848 CD ARG B 443 5.437 23.389 15.929 1.00 15.51 B ATOM 1849 NE ARG B 443 5.553 21.939 15.993 1.00 28.94 B ATOM 1850 CZ ARG B 443 4.612 21.091 15.584 1.00 38. 14 B ATOM 1851 NH1 ARG B 443 3.478 21.551 15.077 1.00 42. 17 B ATOM 1852 NH2 ARG B 443 4.803 19. 780 15.684 1.00 42.70 B ATOM 1853 C ARG B 443 7.749 27.735 16.016 1.00 21. 82 B ATOM 1854 O ARG B 443 7.861 28.224 14.896 1.00 29.08 B ATOM 1855 N GLN B 444 7.464 28.443 17.105 1.00 29.18 B ATOM 1856 CA GLN B 444 7.238 29.886 17.066 1.00 36. 51 B ATOM 1857 CB GLN B 444 6.473 30.340 18.321 1.00 46. 25 B ATOM 1858 CG GLN B 444 6.558 31.846 18.623 1.00 57. 65 B ATOM 1859 CD GLN B 444 5.897 32. 720 17.568 1.00 62. 67 B ATOM 1860 OE1 GLN B 444 6.080 33.938 17.556 1.00 61. 26 B ATOM 1861 NE2 GLN B 444 5.120 32.105 16.683 1.00 66.99 B ATOM 1862 C GLN B 444 8.530 30.694 16.925 1.00 30.21 B ATOM 1863 O GLN B 444 8.534 31.759 16.307 1.00 33. 67 B ATOM 1864 N ILE B 445 9.625 30.202 17.488 1.00 20. 06 B ATOM 1865 CA ILE B 445 10.875 30. 938 17.385 1.00 20-56 B ATOM 1866 CB ILE B 445 11.858 30.505 18.463 1.00 19. 85 B ATOM 1867 CG2 ILE B 445 13.201 31.178 18.238 1.00 13.20 B ATOM 1868 CG1 ILE B 445 11.252 30.866 19.824 1.00 27.96 B ATOM 1869 CD1 ILE B 445 12.127 30.601 21.030 1.00 37.25 B ATOM 1870 C ILE B 445 11.498 30. 790 16.013 1.00 17.92 B ATOM 1871 0 ILE B 445 12.340 31.594 15.608 1.00 10.61 B ATOM 1872 N VAL B 446 11.062 29.755 15.304 1.00 20.73 B ATOM 1873 CA VAL B 446 11.522 29.482 13.954 1.00 18.87 B ATOM 1874 CB VAL B 446 11.309 28. 016 13.611 1.00 9.43 B ATOM 1875 CG1 VAL B 446 11.396 27.811 12.123 1.00 5.04 B ATOM 1876 CG2 VAL B 446 12.356 27.186 14.317 1.00 7.95 B ATOM 1877 C VAL B 446 10.693 30.375 13.038 1.00 26.41 B ATOM 1878 0 VAL B 446 11.181 30.895 12.035 1.00 24.04 B ATOM 1879 N THR B 447 9.430 30.554 13.403 1.00 27.28 B ATOM 1880 CA THR B 447 8.544 31.428 12.658 1.00 25.96 B ATOM 1881 CB THR B 447 7.191 31.533 13.316 1.00 23.73 B ATOM 1882 OG1 THR B 447 6.373 30.429 12.913 1.00 26.04 B ATOM 1883 CG2 THR B 447 6.539 32.842 12.937 1.00 22.88 B ATOM 1884 C THR B 447 9.151 32.823 12.640 1.00 37.51 B ATOM 1885 0 THR B 447 9.270 33.429 11.572 1.00 43.95 B ATOM 1886 N GLU B 448 9.518 33.323 13.826 1.00 44.02 B ATOM 1887 CA GLU B 448 10.132 34.652 13.985 1.00 46.69 B ATOM 1888 CB GLU B 448 10.531 34. 896 15. 450 1.00 52.23 B ATOM 1889 CG GLU B 448 9.920 36.144 16.105 1.00 58.14 B ATOM 1890 CD GLU B 448 8.498 35.923 16.645 1.00 61.16 B ATOM 1891 OE1 GLU B 448 8.311 35.017 17.490 1.00 53.23 B ATOM 1892 OE2 GLU B 448 7. 571 36.661 16.237 1.00 62.43 B ATOM 1893 C GLU B 448 11.377 34.805 13. 100 1.00 48.73 B ATOM 1894 O GLU B 448 11.598 35.865 12.513 1.00 49.98 B ATOM 1895 N HIS B 449 12.181 33.744 13.013 1.00 47.56 B ATOM 1896 CA HIS B 449 13.411 33.731 12.204 1.00 48.36 B ATOM 1897 CB HIS B 449 14.204 32.439 12.504 1.00 50.96 B ATOM 1898 CG HIS B 449 15.473 32.284 11.712 1.00 48.86 B ATOM 1899 CD2 HIS B 449 15.872 31.312 10. 854 1.00 46.83 B TABLE II (continued) ATOM 1900 ND1 HIS B 449 16.526 33.171 11.798 1.00 52.27 B ATOM 1901 CE1 HIS B 449 17.517 32.753 11.030 1.00 53.97 B ATOM 1902 NE2 HIS B 449 17.146 31.627 10.447 1.00 51.56 B ATOM 1903 C HIS B 449 13.102 33.829 10.704 1.00 45.59 B ATOM 1904 0 HIS B 449 13.851 34.436 9.941 1.00 42.04 B ATOM 1905 N VAL B 450 11. 997 33.219 10.291 1.00 45.09 B ATOM 1906 CA VAL B 450 11.581 33.233 8.897 1.00 47.23 B ATOM 1907 CB VAL B 450 10. 458 32.194 8.656 1. 00 47.28 B ATOM 1908 CG1 VAL B 450 9.749 32.460 7.342 1.00 44.77 B ATOM 1909 CG2 VAL B 450 11.053 30.803 8.641 1.00 45.27 B ATOM 1910 C VAL B 450 11.088 34.619 8.492 1.00 55.11 B ATOM 1911 O VAL B 450 11.554 35.185 7.498 1.00 50. 63 B ATOM 1912 N GLN B 451 10.147 35.159 9.267 1.00 59.15 B ATOM 1913 CA GLN B 451 9.587 36. 477 8.987 1.00 60.97 B ATOM 1914 CB GLN B 451 8.660 36.917 10.116 1.00 64.39 B ATOM 1915 CG GLN B 451 7.505 35.976 10.380 1.00 76.09 B ATOM 1916 CD GLN B 451 6.583 36.476 11.483 1.00 82.33 B ATOM 1917 OE1 GLN B 451 7.014 36.721 12.612 1.00 85.39 B ATOM 1918 NE2 GLN B 451 5.305 36.625 11.160 1.00 85.93 B ATOM 1919 C GLN B 451 10.693 37.505 8.826 1.00 60.09 B ATOM 1920 O GLN B 451 10.560 38.450 8.050 1.00 62.02 B ATOM 1921 N LEU B 452 11.785 37. 316 9.559 1.00 59.04 B ATOM 1922 CA LEU B 452 12.906 38. 241 9.487 1. 00 65.58 B ATOM 1923 CB LEU B 452 13.876 38.035 10. 664 1.00 73.64 B ATOM 1924 CG LEU B 452 14.812 39.217 11.006 1. 00. 74.68 B ATOM 1925 CD1 LEU B 452 14.071 40.199 11.933 1.00 70.96 B ATOM 1926 CD2 LEU B 452 16.091 38.724 11.684 1.'00 68.44 B ATOM 1927 C LEU B 452 13.667 38.063 8.181 1.00 65.00 B ATOM 1928 0 LEU B 452 13.984 39.042 7.505 1.00 67.14 B ATOM 1929 N LEU B 453 13.959 36.814 7.826 1.00 67.78 B ATOM 1930 CA LEU B 453 14.699 36.513 6.598 1.00 63.82 B ATOM 1931 CB LEU B 453 15.014 35.019 6.529 1.00 52.62 B ATOM 1932 CG LEU B 453 16.286 34.722 5.747 1.00 45.21 B ATOM 1933 CD1 LEU B 453 17.493 35.090 6.601 1.00 39.33 B ATOM 1934 CD2 LEU B 453 16.334 33.254 5.371 1.00 44.38 B ATOM 1935 C LEU B 453 13. 939 36.946 5.333 1.00 67.34 B ATOM 1936 O LEU B 453 14.493 36.930 4.224 1.00 63.91 B ATOM 1937 N GLN B 454 12.669 37.318 5.519 1.00 70.73 B ATOM 1938 CA GLN B 454 11.799 37.799 4.439 1.00 72.46 B ATOM 1939 CB GLN B 454 10. 333 37.431 4.716 1.00 77.30 B ATOM 1940 CG GLN B 454 10.087 35.952 5.047 1.00 83.53 B ATOM 1941 CD GLN B 454 10.251 35.031 3.843 1.00 87.57 B ATOM 1942 OE1 GLN B 454 9.534 35.160 2.850 1.00 89.37 B ATOM 1943 NE2 GLN B 454 11.196 34.095 3.930 1.00 86.83 B ATOM 1944 C GLN B 454 11.951 39.320 4.471 1.00 69.33 B ATOM 1945 O GLN B 454 11. 000 40.068 4.223 1.00 69. 86 B ATOM 1946 N VAL B 455 13.162 39.750 4.814 1.00 62.26 B ATOM 1947 CA VAL B 455 13.526 41. 153 4.922 1.00 53.41 B ATOM 1948 CB VAL B 455 13.610 41.593 6.407 1.00 43.21 B ATOM 1949 CG1 VAL B 455 14.166 43.003 6.524 1.00 37.39 B ATOM 1950 CG2 VAL B 455 12.238 41.523 7.031 1.00 41.33 B ATOM 1951 C VAL B 455 14.891 41. 305 4. 276 1.00 57.83 B ATOM 1952 O VAL B 455 15.038 42.045 3.308 1.00 60.42 B ATOM 1953 N ILE B 456 15.880 40.586 4.808 1.00 62.41 B ATOM 1954 CA ILE B 456 17.246 40.633 4.284 1.00 69.75 B ATOM 1955 CB ILE B 456 18.137 39.553 4.959 1.00 62.89 B TABLE II (continued) ATOM 1956 CG2 ILE B 456 19.402 39.302 4.140 1.00 52.74 B ATOM 1957 CG1 ILE B 456 18.493 40.016 6.375 1.00 63.49 B ATOM 1958 CD1 ILE B 456 19.404 39.077 7.128 1.00 63.54 B ATOM 1959 C ILE B 456 17.324 40.511 2.753 1.00 81.54 B ATOM 1960 O ILE B 456 18.201 41.112 2.124 1.00 87.35 B ATOM 1961 N LYS B 457 16.419 39.743 2.149 1.00 87.18 B ATOM 1962 CA LYS B 457 16.403 39.616 0.691 1.00 84.94 B ATOM 1963 CB LYS B 457 15.561 38.411 0.257 1.00 82.68 B ATOM 1964 CG LYS B 457 16.053 37.067 0.771 1.00 83.29 B ATOM 1965 CD LYS B 457 15.099 35.954 0.366 1.00 83.45 B ATOM 1966 CE LYS B 457 13.680 36.226 0.872 1.00 85.61 B ATOM 1967 NZ LYS B 457 12.716 35.129 0.542 1.00 85.49 B ATOM 1968 C LYS B 457 15.775 40.902 0.141 1.00 87.54 B ATOM 1969 O LYS B 457 16.152 41.388-0. 932 1.00 89.65 B ATOM 1970 N LYS B 458 14.824 41.452 0.900 1.00 87.40 B ATOM 1971 CA LYS B 458 14. 115 42.677 0.525 1.00 84.87 B ATOM 1972 CB LYS B 458 12.632 42.580 0.919 1.00 88.35 B ATOM 1973 CG LYS B 458 11.758 41.740-0. 016 1.00 92.36 B ATOM 1974 CD LYS B 458 11.641 42.373-1. 400 1.00 95.19 B ATOM 1975 CE LYS B 458 10.764 41.543-2. 331 1.00 96.51 B ATOM 1976 NZ LYS B 458 10.776 42.076-3. 728 1.00 94.76 B ATOM 1977 C LYS B 458 14.699 43.946 1.138 1.00 81.74 B ATOM 1978 0 LYS B 458 13.953 44.829 1.553 1.00 83.35 B ATOM 1979 N THR B 459 16.022 44.039 1.198 1.00 80.71 B ATOM 1980 CA THR B 459 16.686 45.220 1.749 1.00 83. 87 B ATOM 1981 CB THR B 459 16.480 45.344 3.296 1. 00 82.73 B ATOM 1982 OG1 THR B 459 15.141 45.777 3.574 1.00 79.48 B ATOM 1983 CG2 THR B 459 17.450 46.361 3.894 1.00 82.49 B ATOM 1984 C THR B 459 18.180 45.172 1.435 1.00 85.41 B ATOM 1985 O THR B 459 18.776 46. 176 1.040 1.00 81.40 B ATOM 1986 N GLU B 460 18.779 43.999 1.607 1.00 88.06 B ATOM 1987 CA GLU B 460 20.200 43.820 1.328 1.00 93.84 B ATOM 1988 CB GLU B 460 20.901 43.117 2.499 1.00 94.28 B ATOM 1989 CG GLU B 460 20.818 43.824 3.850 1.00 95.43 B ATOM 1990 CD GLU B 460 21.725 45.032 3.952 1.00 95.17 B ATOM 1991 OE1 GLU B 460 22.945 44.883 3.725 1.00 96.90 B ATOM 1992 OE2 GLU B 460 21.219 46.128 4.269 1.00 96.04 B ATOM 1993 C GLU B 460 20.375 42.972 0.068 1.00 97.84 B ATOM 1994 O GLU B 460 20.435 41.740 0.147 1.00 96.33 B ATOM 1995 N THR B 461 20.441 43.622-1. 093 1.00100. 00 B ATOM 1996 CA THR B 461 20.629 42. 888-2. 340 1.00100. 00 B ATOM 1997 CB THR B 461 20.082 43.667-3. 564 1. 00100. 00 B ATOM 1998 OG1 THR B 461 18.739 44.098-3. 301 1.00100. 00 B ATOM 1999 CG2 THR B 461 20.054 42.764-4. 794 1.00100. 00 B ATOM 2000 C THR B 461 22.133 42.657-2. 475 1.00 97.97 B ATOM 2001 O THR B 461 22.887 42.937-1. 539 1.00 99.21 B ATOM 2002 N ASP B 462 22.582 42. 169-3. 625 1.00 97.67 B ATOM 2003 CA ASP B 462 24.000 41.873-3. 786 1.00 98.75 B ATOM 2004 CB ASP B 462 24.857 43.135-3. 610 1.00100. 00 B ATOM 2005 CG ASP B 462 24.837 44.034-4. 839 1.00100. 00 B ATOM 2006 OD1 ASP B 462 23.742 44.481-5. 245 1.00100. 00 B ATOM 2007 OD2 ASP B 462 25.922 44.295-5. 403 1.00100. 00 B ATOM 2008 C ASP B 462 24.265 40.882-2. 660 1.00 97.17 B ATOM 2009 O ASP B 462 25.177 41.057-1. 846 1.00 95.23 B ATOM 2010 N MET B 463 23.412 39.858-2. 622 1.00 95.38 B ATOM 2011 CA MET B 463 23.459 38. 786-1. 626 1.00 92.42 B TABLE II (continued) ATOM 2012 CB MET B 463 22.114 38.699-0. 886 1.00 90.24 B ATOM 2013 CG MET B 463 22.137 39.194 0.554 1.00 85.52 B ATOM 2014 SD MET B 463 23.174 38.151 1.595 1.00 80.41 B ATOM 2015 CE MET B 463 22.280 36. 556 1.438 1.00 84.72 B ATOM 2016 C MET B 463 23.750 37.451-2. 311 1.00 89.45 B ATOM 2017 O MET B 463 24.573 37.391-3. 229 1.00 90.32 B ATOM 2018 N SER B 464 23.064 36.395-1. 864 1.00 84.45 B ATOM 2019 CA SER B 464 23.228 35.048-2. 415 1.00 75.18 B ATOM 2020 CB SER B 464 24.685 34.800-2. 805 1.00 79.37 B ATOM 2021 OG SER B 464 25.532 34.921-1. 672 1.00 78.04 B ATOM 2022 C SER B 464 22.833 33.988-1. 399 1.00 66.16 B ATOM 2023 O SER B 464 23.707 33. 365-0. 795 1.00 62.24 B ATOM 2024 N LEU B 465 21.537 33.773-1. 200 1.00 56. 29 B ATOM 2025 CA LEU B 465 21.122 32.760-0. 239 1.00 47.40 B ATOM 2026 CB LEU B 465 19.661 32.975 0.166 1.00 53.08 B ATOM 2027 CG LEU B 465 19.137 32.189 1.377 1.00 53.88 B ATOM 2028 CD1 LEU B 465 17.809 32.763 1.830 1.00 53.82 B ATOM 2029 CD2 LEU B 465 18.971 30.725 1.024 1.00 57.40 B ATOM 2030 C LEU B 465 21.311 31.391-0. 894 1.00 40.71 B ATOM 2031 O LEU B 465 20.745 31.132-1. 957 1.00 40.72 B ATOM 2032 N HIS B 466 22.121 30.536-0. 260 1.00 27.90 B ATOM 2033 CA HIS B 466 22.433 29.189-0. 757 1.00 23.57 B ATOM 2034 CB HIS B 466 23.241 28.418 0. 310 1.00 24.70 B ATOM 2035 CG HIS B 466 23.726 27.061-0. 127 1.00 24.75 B ATOM 2036 CD2 HIS B 466 24.967 26.621-0. 442 1.00 23.35 B ATOM 2037 ND1 HIS B 466 22.895 25.965-0. 243 1.00 26.73 B ATOM 2038 CE1 HIS B 466 23.601 24. 911-0. 609 1.00 19.81 B ATOM 2039 NE2 HIS B 466 24.861 25.281-0. 737 1.00 22.15 B ATOM 2040 C HIS B 466 21.162 28.428-1. 138 1.00 22.55 B ATOM 2041 O HIS B 466 20.209 28.367-0. 369 1.00 22.32 B ATOM 2042 N PRO B 467 21.140 27.833-2. 337 1.00 19.11 B ATOM 2043 CD PRO B 467 22.290 27.646-3. 224 1.00 16.56 B ATOM 2044 CA PRO B 467 20.000 27.075-2. 844 1.00 20.72 B ATOM 2045 CB PRO B 467 20.565 26.413-4. 094 1.00 20.55 B ATOM 2046 CG PRO B 467 21.984 26.309-3. 796 1.00 18.49 B ATOM 2047 C PRO B 467 19.332 26.074-1. 904 1.00 23.76 B ATOM 2048 O PRO B 467 18.149 25.775-2. 064 1.00 29.66 B ATOM 2049 N LEU B 468 20.068 25.550-0. 933 1.00 20.00 B ATOM 2050 CA LEU B 468 19.476 24.593-0. 003 1.00 18.32 B ATOM 2051 CB LEU B 468 20.561 23.850 0.776 1.00 13.78 B ATOM 2052 CG LEU B 468 20.552 22.314 0.774 1.00 13.06 B ATOM 2053 CD1 LEU B 468 21.465 21.806 1.891 1.00 4.90 B ATOM 2054 CD2 LEU B 468 19.148 21.790 0.974 1.00 14.37 B ATOM 2055 C LEU B 468 18.550 25.305 0.985 1.00 25.06 B ATOM 2056 0 LEU B 468 17.432 24.850 1.237 1. 00 28.92 B ATOM 2057 N LEU B 469 19.015 26.419 1.547 1.00 21.65 B ATOM 2058 CA LEU B 469 18.210 27.159 2.503 1.00 16.91 B ATOM 2059 CB LEU B 469 19.065 28.212 3.212 1.00 2.28 B ATOM 2060 CG LEU B 469 20.209 27. 578 4.019 1.00 10.36 B ATOM 2061 CD1 LEU B 469 21.116 28.649 4.618 1.00 2.27 B ATOM 2062 CD2 LEU B 469 19.634 26.691 5.103 1.00 2.00 B ATOM 2063 C LEU B 469 17.018 27.778 1.785 1.00 22.13 B ATOM 2064 O LEU B 469 15.951 27.958 2.370 1.00 28.06 B ATOM 2065 N GLN B 470 17.184 28.082 0. 505 1.00 23.32 B ATOM 2066 CA GLN B 470 16.081 28. 642-0. 259 1.00 28.26 B ATOM 2067 CB GLN B 470 16.537 29. 072-1. 655 1.00 35.96 B TABLE II (continued) ATOM 2068 CG GLN B 470 17.143 30.466-1. 720 1.00 45.66 B ATOM 2069 CD GLN B 470 17.077 31.071-3. 122 1.00 54.88 B ATOM 2070 OE1 GLN B 470 17.729 30.595-4. 058 1.00 55.94 B ATOM 2071 NE2 GLN B 470 16.276 32.124-3. 271 1.00 56.17 B ATOM 2072 C GLN B 470 14.984 27.584-0. 373 1.00 27.30 B ATOM 2073 0 GLN B 470 13.807 27.914-0. 463 1.00 27.19 B ATOM 2074 N GLU B 471 15.376 26.314-0. 361 1.00 23.67 B ATOM 2075 CA GLU B 471 14.420 25.215-0. 449 1.00 24.89 B ATOM 2076 CB GLU B 471 15.117 23.913-0. 853 1.00 20.97 B ATOM 2077 CG GLU B 471 15.441 23.745-2. 304 1.00 18.18 B ATOM 2078 CD GLU B 471 15.840 22.328-2. 617 1.00 18.02 B ATOM 2079 OE1 GLU B 471 16.164 22.049-3. 783 1.00 24.26 B ATOM 2080 OE2 GLU B 471 15.826 21.492-1. 696 1.00 11.24 B ATOM 2081 C GLU B 471 13.722 24.957 0.879 1.00 23.67 B ATOM 2082 O GLU B 471 12.694 24.288 0.930 1.00 30.39 B ATOM 2083 N ILE B 472 14.288 25.464 1.961 1.00 18.70 B ATOM 2084 CA ILE B 472 13.703 25.226 3.270 1.00 33.47 B ATOM 2085 CB ILE B 472 14.766 24.543 4.197 1.00 31.91 B ATOM 2086 CG2 ILE B 472 14.273 24.448 5.639 1.00 25. 10 B ATOM 2087 CG1 ILE B 472 15.062 23.139 3.646 1.00 32.52 B ATOM 2088 CD1 ILE B 472 16.211 22.415 4.297 1.00 29.39 B ATOM 2089 C ILE B 472 13.118 26.500 3.885 1.00 41.74 B ATOM 2090 O ILE B 472 12.949 26.615 5.100 1.00 50.46 B ATOM 2091 N TYR B 473 12.804 27.459 3.024 1.00 40. 36 B ATOM 2092 CA TYR B 473 12.206 28.713 3.452 1.00 37.84 B ATOM 2093 CB TYR B 473 13.198 29.876 3.347 1.00 40.35 B ATOM 2094 CG TYR B 473 14.322 29.875 4.354 1.00 41.05 B ATOM 2095 CD1 TYR B 473 14.083 29.623 5.702 1.00 44.18 B ATOM 2096 CE1 TYR B 473 15.121 29.669 6.641 1.00 46.54 B ATOM 2097 CD2 TYR B 473 15.624 30.171 3.967 1.00 44.55 B ATOM 2098 CE2 TYR B 473 16.668 30.215 4.897 1.00 46.31 B ATOM 2099 CZ TYR B 473 16.409 29.964 6.229 1.00 45.82 B ATOM 2100 OH TYR B 473 17.438 30.003 7.142 1.00 50.36 B ATOM 2101 C TYR B 473 11.040 28.992 2.521 1.00 42.83 B ATOM 2102 O TYR B 473 10.138 29.742 2.866 1.00 46.48 B ATOM 2103 N LYS B 474 11.071 28.384 1.336 1.00 48.34 B ATOM 2104 CA LYS B 474 10.033 28.588 0.337 1.00 53.04 B ATOM 2105 CB LYS B 474 10.026 27.466-0. 699 1.00 54.75 B ATOM 2106 CG LYS B 474 10.987 27.696-1. 858 1.00 64.43 B ATOM 2107 CD LYS B 474 10.933 29.139-2. 386 1.00 65.62 B ATOM 2108 CE LYS B 474 9.544 29.531-2. 880 1.00 66.06 B ATOM 2109 NZ LYS B 474 9.471 30.967-3. 275 1.00 62.88 B ATOM 2110 C LYS B 474 8.658 28.713 0.928 1.00 57.12 B ATOM 2111 O LYS B 474 8.257 29.792 1.350 1.00 60.60 B ATOM 2112 N ASP B 475 7.920 27.618 0.947 1.00 57.16 B ATOM 2113 CA ASP B 475 6.588 27.674 1.498 1.00 65.41 B ATOM 2114 CB ASP B 475 5.616 26.901 0. 604 1.00 69.32 B ATOM 2115 CG ASP B 475 5.571 27.447-0. 816 1.00 71.65 B ATOM 2116 OD1 ASP B 475 5.444 28.680-0. 977 1.00 67.85 B ATOM 2117 OD2 ASP B 475 5.657 26.645-1. 771 1.00 71. 03 B ATOM 2118 C ASP B 475 6.642 27.095 2.899 1.00 71.27 B ATOM 2119 O ASP B 475 6.103 26.024 3.161 1.00 79.70 B ATOM 2120 N LEU B 476 7.302 27.821 3.798 1.00 75.45 B ATOM 2121 CA LEU B 476 7.459 27.390 5.183 1.00 78.74 B ATOM 2122 CB LEU B 476 8.938 27.075 5.450 1.00 77.31 B ATOM 2123 CG LEU B 476 9.393 26.634 6.842 1.00 74.62 B TABLE II (continued) ATOM 2124 CD1 LEU B 476 10.682 25.845 6.730 1.00 75.35 B ATOM 2125 CD2 LEU B 476 9.582 27.844 7.737 1.00 76.52 B ATOM 2126 C LEU B 476 6.944 28.407 6.204 1.00 84.23 B ATOM 2127 O LEU B 476 7.014 29.618 5.988 1.00 84.65 B ATOM 2128 N TYR B 477 6.419 27.893 7.314 1.00 88.13 B ATOM 2129 CA TYR B 477 5.889 28.715 8.398 1.00 85.03 B ATOM 2130 CB TYR B 477 4.367 28.880 8.268 1.00 92.11 B ATOM 2131 CG TYR B 477 3.866 29.210 6.874 1.00 98.10 B ATOM 2132 CD1 TYR B 477 3.731 28.213 5.905 1.00100. 00 B ATOM 2133 CE1 TYR B 477 3.258 28.505 4.623 1.00 99.17 B ATOM 2134 CD2 TYR B 477 3.517 30.516 6.524 1.00 99.28 B ATOM 2135 CE2 TYR B 477 3.045 30.819 5.242 1.00100. 00 B ATOM 2136 CZ TYR B 477 2.918 29. 808 4.299 1.00 99.61 B ATOM 2137 OH TYR B 477 2.456 30.094 3.033 1.00 94.05 B ATOM 2138 C TYR B 477 6.219 28.042 9.733 1.00 80.02 B ATOM 2139 O TYR B 477 5.334 27.368 10.296 1.00 73.83 B ATOM 2140 OXT TYR B 477 7.369 28.174 10.194 1.00 76.80 B ATOM 2141 CB HIS 604 11.206 19.827-2. 523 1.00 69.99 MOLC ATOM 2142 CG HIS 604 10.843 20.473-3. 823 1.00 78.40 MOLC ATOM 2143 CD2 HIS 604 11.527 21.333-4. 615 1.00 78.17 MOLC ATOM 2144 ND1 HIS 604 9.628 20.269-4. 441 1.00 81.66 MOLC ATOM 2145 CE1 HIS 604 9.579 20.974-5. 556 1.00 79.67 MOLC ATOM 2146 NE2 HIS 604 10.720 21.629-5. 684 1.00 80.61 MOLC ATOM 2147 C HIS 604 13.528 19.125-3. 137 1.00 57.27 MOLC ATOM 2148 O HIS 604 13.725 17.935-2. 928 1.00 56.38 MOLC ATOM 2149 N HIS 604 13.072 21.401-2. 130 1.00 67.32 MOLC ATOM 2150 CA HIS 604 12.686 19.961-2. 162 1.00 64.94 MOLC ATOM 2151 N LYS 605 14.040 19.739-4. 195 1.00 54.10 MOLC ATOM 2152 CA LYS 605 14.837 18.993-5. 168 1.00 48.09 MOLC ATOM 2153 CB LYS 605 15.047 19.841-6. 431 1.00 53.26 MOLC ATOM 2154 CG LYS 605 15.567 19.075-7. 636 1.00 58.93 MOLC ATOM 2155 CD LYS 605 15.414 19.886-8. 919 1.00 68.94 MOLC ATOM 2156 CE LYS 605 13.942 20.130-9. 261 1.00 74.12 MOLC ATOM 2157 NZ LYS 605 13.748 20.942-10. 509 1.00 76.25 MOLC ATOM 2158 C LYS 605 16.181 18.521-4. 613 1.00 39.32 MOLC ATOM 2159 O LYS 605 16.631 17.426-4. 938 1.00 42.23 MOLC ATOM 2160 N ILE 606 16.814 19.337-3. 773 1.00 26.84 MOLC ATOM 2161 CA ILE 606 18. 108 18.979-3. 190 1.00 16.55 MOLC ATOM 2162 CB ILE 606 18. 909 20.230-2. 742 1.00 10.87 MOLC ATOM 2163 CG2 ILE 606 20.242 19.809-2. 153 1.00 2.00 MOLC ATOM 2164 CG1 ILE 606 19.140 21.167-3. 929 1.00 8.36 MOLC ATOM 2165 CD1 ILE 606 19.643 22.540-3. 540 1.00 6.20 MOLC ATOM 2166 C ILE 606 17.924 18.063-1. 988 1.00 23.07 MOLC ATOM 2167 O ILE 606 18.611 17.054-1. 868 1.00 28.14 MOLC ATOM 2168 N LEU 607 17.007 18.415-1. 090 1.00 21.19 MOLC ATOM 2169 CA LEU 607 16.755 17.581 0.074 1.00 16.90 MOLC ATOM 2170 CB LEU 607 15.621 18.142 0.922 1.00 8.95 MOLC ATOM 2171 CG LEU 607 15. 880 19.336 1.830 1.00 15.59 MOLC ATOM 2172 CD1 LEU 607 14.600 19.633 2.583 1.00 15.98 MOLC ATOM 2173 CD2 LEU 607 17. 015 19.051 2.803 1.00 7.11 MOLC ATOM 2174 C LEU 607 16.360 16.205-0. 424 1.00 25.01 MOLC ATOM 2175 O LEU 607 16.440 15.226 0.304 1.00 33.31 MOLC ATOM 2176 N HIS 608 15.920 16. 139-1. 675 1.00 29.98 MOLC ATOM 2177 CA HIS 608 15.510 14.881-2. 282 1.00 33.41 MOLC ATOM 2178 CB HIS 608 14.710 15.149-3. 557 1.00 44.84 MOLC ATOM 2179 CG HIS 608 13.265 14.767-3. 461 1.00 54.97 MOLC TABLE II (continued) ATOM 2180 CD2 HIS 608 12.145 15.526-3. 384 1.00 58.38 MOLC ATOM 2181 ND1 HIS 608 12.842 13.456-3. 421 1.00 54.84 MOLC ATOM 2182 CE1 HIS 608 11.524 13.425-3. 323 1.00 59.22 MOLC ATOM 2183 NE2 HIS 608 11.077 14.668-3. 298 1.00 58.86 MOLC ATOM 2184 C HIS 608 16.740 14.066-2. 626 1.00 32.15 MOLC ATOM 2185 O HIS 608 16.722 12.839-2. 568 1.00 37.73 MOLC ATOM 2186 N ARG 609 17.810 14.760-2. 988 1.00 25.30 MOLC ATOM 2187 CA ARG 609 19.046 14.101-3. 355 1.00 24.31 MOLC ATOM 2188 CB ARG 609 19.935 15.073-4. 117 1.00 21.54 MOLC ATOM 2189 CG ARG 609 21.110 14.445-4. 818 1.00 29.67 MOLC ATOM 2190 CD ARG 609 21. 865 15.536-5. 523 1.00 35.70 MOLC ATOM 2191 NE ARG 609 20.961 16.329-6. 346 1.00 38.50 MOLC ATOM 2192 CZ ARG 609 21.234 17.547-6. 797 1.00 45.94 MOLC ATOM 2193 NH1 ARG 609 22.389 18.123-6. 503 1.00 50.97 MOLC ATOM 2194 NH2 ARG 609 20.354 18.192-7. 547 1.00 47.63 MOLC ATOM 2195 C ARG 609 19.747 13.615-2. 103 1.00 30.23 MOLC ATOM 2196 O ARG 609 20.295 12.513-2. 079 1.00 40.62 MOLC ATOM 2197 N LEU 610 19.709 14.434-1. 055 1.00 28.06 MOLC ATOM 2198 CA LEU 610 20.353 14. 098 0.209 1.00 24.98 MOLC ATOM 2199 CB LEU 610 20.355 15.310 1.136 1.00 19.65 MOLC ATOM 2200 CG LEU 610 21.329 16.412 0.731 1.00 17.71 MOLC ATOM 2201 CD1 LEU 610 21.115 17.618 1.582 1.00 24.50 MOLC ATOM 2202 CD2 LEU 610 22.741 15.925 0.885 1.00 17.07 MOLC ATOM 2203 C LEU 610 19.747 12.901 0.922 1.00 26.18 MOLC ATOM 2204 O LEU 610 20.465 12.150 1.569 1.00 35.02 MOLC ATOM 2205 N LEU 611 18.436 12.719 0.816 1.00 24.68 MOLC ATOM 2206 CA LEU 611 17.796 11. 577 1.449 1.00 25.97 MOLC ATOM 2207 CB LEU 611 16.279 11.738 1.467 1.00 23.28 MOLC ATOM 2208 CG LEU 611 15. 778 12.796 2.451 1. 00 31.19 MOLC ATOM 2209 CD1 LEU 611 14.288 12.960 2.324 1.00 34.87 MOLC ATOM 2210 CD2 LEU 611 16.137 12.391 3.866 1.00 39.72 MOLC ATOM 2211 C LEU 611 18.176 10.329 0.678 1.00 36.23 MOLC ATOM 2212 O LEU 611 17.633 9.258 0.920 1.00 40.43 MOLC ATOM 2213 N GLN 612 19.114 10.487-0. 259 1.00 47.01 MOLC ATOM 2214 CA GLN 612 19.632 9.389-1. 081 1.00 51.20 MOLC ATOM 2215 CB GLN 612 18.906 9.348-2. 426 1.00 51.77 MOLC ATOM 2216 CG GLN 612 17.420 9.064-2. 354 1.00 58.26 MOLC ATOM 2217 CD GLN 612 16.742 9.212-3. 710 1.00 65.50 MOLC ATOM 2218 OE1 GLN 612 17.145 8.586-4. 692 1.00 65. 28 MOLC ATOM 2219 NE2 GLN 612 15.707 10.042-3. 768 1.00 68.30 MOLC ATOM 2220 C GLN 612 21.145 9.569-1. 327 1.00 54.09 MOLC ATOM 2221 O GLN 612 21.950 9.078-0. 503 1.00 50.34 MOLC ATOM 2222 OXT GLN 612 21.514 10.216-2. 333 1.00 54.62 MOLC ATOM 2223 CL1 762 501 28.026 27.230 15.860 1.00 2.00 ATOM 2224 CL2 762 501 24.210 23.523 14.409 1.00 2.00 ATOM 2225 N1 762 501 28.117 29.127 13.329 1.00 21.89 ATOM 2226 01 762 501 31.287 28.225 11.261 1.00 39.36 ATOM 2227 Cl 762 501 30.985 31.142 11.840 1.00 26.42 ATOM 2228 C10 762 501 26.161 27.672 13.787 1.00 11.56 ATOM 2229 Cll 762 501 26.672 26.796 14.819 1.00 8.99 ATOM 2230 C12 762 501 26. 060 25.502 15.016 1.00 17.04 ATOM 2231 C13 762 501 24.951 25.086 14. 191 1.00 11.07 ATOM 2232 C14 762 501 24.456 25.954 13.184 1.00 9.95 ATOM 2233 C15 762 501 25.052 27.229 12.984 1.00 8.24 ATOM 2234 C2 762 501 30.238 30.048 12.329 1.00 23.41 ATOM 2235 02 762 501 30.964 27.945 13.477 1.00 27.22 TABLE II (continued) ATOM 2236 03 762 501 25.973 29.950 13.245 1.00 23.61 ATOM 2237 C3 762 501 30.465 32.468 11.822 1.00 33.58 ATOM 2238 C4 762 501 28.898 30.269 12.827 1.00 23.90 ATOM 2239 C5 762 501 29.136 32.696 12.318 1.00 31.81 ATOM 2240 C6 762 501 28.366 31.609 12.814 1.00 27.88 ATOM 2241 C7 762 501 26.732 29.014 13.491 1.00 17.00 ATOM 2242 08 762 501 31.309 33.484 11.294 1.00 43.51 ATOM 2243 C9 762 501 30.865 28.699 12.309 1.00 27.78 ATOM 2244 C22 762 501 32.684 33.617 11.697 1.00 49.66 ATOM 2245 C23 762 501 33.479 34.458 10.733 1.00 55.44 ATOM 2246 C24 762 501 33.596 34.183 9.377 1.00 59.09 ATOM 2247 C25 762 501 34.386 35.114 8.742 1.00 61.91 ATOM 2248 C26 762 501 34.860 36.082 9.616 1.00 59.94 ATOM 2249 S27 762 501 34.341 35.874 11.244 1.00 57.91 END