Abstract:
3 α-hydroxysteroid dehydrogenase (3a-HSD) plays a central role in the metabolism and action of steroid hormones and neurosteroids (steroids synthesized in the central nervous system). The high resolution structure of human type III 3a-HSD crystallized in complex with cofactor NADP is determined by X-ray diffraction. Furthermore the active site is determined. The structure coordinates of the enzyme may be used to design and select novel classes of modulators to human type III 3a-HSD.

Description:
FIELD OF THE INVENTION  
       [0001]     The present invention relates to a method to identify modulators for human 3α-hydroxysteroid dehydrogenase (3a-HSD) by using compounds with certain structural, physical and spatial characteristics that allow for the interaction of said compounds with specific residues of the active site of the enzyme. This interaction between the compounds of the invention and the active site inhibits or potentiates the activity of 3a-HSD and these compounds are useful for treating disease in which a deficiency of allopregnanolone, an endogenous neuroactive substrate and the product of the 3a-HSD, is indicated, such as major unipolar depression, premenstrual dysphoric disorder (PMDD, PMS) and other affective disorders. This invention relates also to a novel crystalline structure of type-3 human 3a-HSD, the identification of the detailed catalytic site for the human form of this enzyme and methods enabling the design and selection of inhibitors and potentiators of said active site.  
       BACKGROUND OF THE INVENTION  
       [0002]     Human 3a-HSD s play central roles in the metabolism and action of steroid hormones and neurosteroids (steroids synthesized in the central nervous system). The 3a-HSD is a member of the aldo-keto reductase (AKR) superfamily. In general, the function of mammalian 3a-HSD s is to convert (reduce) 5α- and 5α,3-ketosteroids into 5α,3α- and 5α,3α-tetrahydrosteroids, respectively, and to further oxidize these 3α-reduced tertrahydrosteroids back to their parent 3-keto steroidal precursors. The steroids that are target substrates of the 3a-HSDs are androgens and progestins. For example, in the prostate the potent androgen 5α-dihidrotestosterone will be converted by the 3a-HSD into the weak androgen 3α-androstanediol. By contrast, in the central nervous system, 3a-HSD can regulate the occupancy of the g-aminobutyric acid (GABA) A  receptor by converting 5α-dihydroprogesterone into 3α-hydroxy-5a-pregnan-20-one (allopregnanolone), a potent allosteric effector of the GABA A  receptor (K d =10 −9  M) (Majewski, M. D. et al. (1986) Science 232, 1004-1007; Majewski, M. D. (1992) Prog. Neurobiol. 38, 379-395; Lambert, J. J. et al., Trends Pharmacol. Sci. 16, 295-303). In the presence of GABA, allopregnanolone will potentiate GABA A -mediated chloride conductance. As a result 3a-HSD is responsible for the production of anxiolytic steroids, and decreased activity in this pathway has been implicated in the symptoms of pre-menstrual syndrome (Morrow, A. L. et al. (1998) Nature (London) 395, 652-653). Thus 3a-HSD isoforms regulate the occupancy of both a nuclear receptor (androgen receptor) and a membrane-bound chloride-ion gated channel (GABA A  receptor) and may have profound effects on receptor function. For these reasons the 3α-HSD is considered a molecular switch turning on and off the function of steroid hormones in the prostate and of neurosteroids in the CNS.  
         [0003]     Four human 3a-HSD isoforms have been cloned, sequenced and characterized: type-1 3α-HSD (AKR1C4), type-2 3α(17β)-HSD (AKR1C3), type-3 3α-HSD (AKR1C2), and 20α(3α)-HSD (AKR1C1), sharing at least 84% amino acid and sequence identity. Of these isoforms only type-2 and type-3 are expressed in the brain with type-3 being the predominant form present in the CNS. Types-2 and -3 3α-HSDs share almost 90% nucleotide sequence identity and 88% amino acid homology. Their putative substrate binding pockets and catalytic domains are highly conserved (as are among the other members of the AKR superfamily). The type-3 isoform is believed to be the major form responsible for the oxidation (turning off) of the anxiolytic GABA A  receptor-active neurosteroid allopregnanolone in the brain.  
         [0004]     All 3a-HSD s are NAD(P)(H) dependent oxido-reductases implying that NAD + , NADH, NADP +  and NADPH are the cofactors. The oxidative function requires the presence of NAD +  or NADP + , while NADPH is being utilized for the reduction of 3-ketosteroids. Known inhibitors of the 3a-HSD are the class of the non-steroidal anti-inflamatory drugs (NSAIDs) (Penning et al., PNAS (1983) 80, 4504-4508) and the selective serotonin reuptake inhibitors (SSRIs) that were reported to potentiate and inhibit at the same time the 3a-HSD (Griffin and Mellon, PNAS (1999) 96, 13512-13517.  
       SUMMARY OF THE INVENTION  
       [0005]     In one aspect the invention comprises the crystalline structure of human type III 3a-HSD and to determine its structure coordinates.  
         [0006]     The structure coordinates of a human type III 3a-HSD crystal are used to reveal the atomic details of the active site or the cofactor binding site of the enzyme and to solve the structure of a different human type III 3a-HSD crystal, or a crystal of a mutant, homologue or co-complex, of human type III 3a-HSD.  
         [0007]     It is also an object of this invention to use the structure coordinates and atomic details of human type III 3a-HSD, or its mutants or homologues or co-complexes, to provide potentiators or inhibitors of human type III 3a-HSD.  
         [0008]     In still a further aspect, the invention provides a method of screening compounds for their ability to modulate the human type III 3a-HSD. 
     
    
     DETAILED DESCRIPTION  
       [0009]     Table 1 lists the atomic structure coordinates of human type III 3a-HSD as derived by X-ray diffreaction from a crystal of human type III 3a-HSD 3a-HSD complexed to the NADP cofactor [Theoretical total number of refl. in resol. range: 56988 (100.0%); number of unobserved reflections (no entry or IFI=0): 1562 (2.7%); number of reflections rejected: 0 (0.0%); total number of reflections used: 55426 (97.3%); number of reflections in working set: 49806 (87.4%); number of reflections in test set: 5620 (9.9%)]. The following abbreviations are used in Table 1. “Atom type” refers to the element whose coordinates are measured. The first letter in the column defines the element. “X, Y, Z” crystographically defines the atomic position of the element measured. “B” is a thermal factor that measures movement of the atom around its atomic center.  
         [0000]     Abreviations:  
         [0000]    
       
          Å=Ångstrom  
          TIP=represents in the listings of molecule of e.g. active site a water molecule 
 
 Definitions: 
 
       
     
         [0012]     The following terms are also used herein:  
         [0013]     The term “co-complex” means human type III 3a-HSD or homologue of human type III 3a-HSD in covalent or non-covalent association with a chemical entity or compound.  
         [0014]     The term “associating with” refers to a condition of proximity between a chemical entity or compound, or portions thereof, and a human type III 3a-HSD molecule or portions thereof. The association may be non-covalent—wherein the juxtaposition is energetically favored by hydrogen bonding or van der Waals or electrostatic interactions—or it may be covalent. The term “active site” or “active site moiety” refers to any or all of the following sites in human type III 3a-HSD: the substrate binding site; and the site where the reduction of the substrate occurs. The active site is characterized by at least amino acid residues TYR 24, ALA 25, ALA 52, VAL 54, TYR 55, LYS 84, TRP 86, HIS 117, ILE 129, ASN 167, GLN 190, TYR 216, HIS 222, GLU 224, PRO 226, TRP 227, LEU 306, LEU 308, ILE 310, PHE 311, TIP 1, TIP 33, TIP 131, TIP 225, TIP 235 using the sequence and numbering according to SEQ ID NO: 1 and Table 1 (for the TIP (=water) molecules).  
         [0015]     The term “cofactor” binding site refers to any or all of the following sites in the human type III 3a-HSD: the cofactor binding site (cofactor e.g. NADP). The cofactor binding site (here NADP) is characterized by at least amino acid residues GLY 22, THR 23, TYR 24, ASP 50, TYR 55, LYS 84, HIS 117, SER 166, ASN 167, GLN 190, TYR 216, SER 217, ALA 218, LEU 219, GLY 220, SER 221, HIS 222, LEU 236, ALA 253, LEU 268, ALA 269, LYS 270, SER 271, TYR 272, ASN 273, ARG 276, GLN 279, ASN 280, LEU 306, TIP 17, TIP 27, TIP 53, TIP 93, TIP 122, TIP 207, TIP 219, TIP 224 using the sequence and numbering according to SEQ ID NO: 1 and Table 1 (for the TIP (=water) molecules).  
         [0016]     The term “structure coordinates” refers to mathematical coordinates derived from mathematical equations related to the patterns obtained on diffraction of a monochromatic beam of X-rays by the atoms (scattering centers) of a human type III 3a-HSD molecule in crystal form. The diffraction data are used to calculate an electron density map of the repeating unit of the crystal. The electron density maps are used to establish the positions of the individual atoms within the unit cell of the crystal.  
         [0017]     Those of skilled in the art understand that a set of structure coordinates determined by X-ray crystallography is not without standard error. For the purpose of this invention, any set of structure coordinates for human type III 3a-HSD or human type III 3a-HSD variants that have a root mean square deviation of protein backbone atoms (N, α-C, C and O) of less than 0.75 Å when superimposed—using backbone atoms—on the structure coordinates listed in Table 1 shall be considered identical.  
         [0018]     The term “variant” refers to a polynucleotide or polypeptide that differs from a reference polynucleotide or polypeptide, but retains the essential properties thereof. A typical variant of a polynucleotide differs in nucleotide sequence from the reference polynucleotide. Changes in the nucleotide sequence of the variant may or may not alter the amino acid sequence of a polypeptide encoded by the reference polynucleotide. Nucleotide changes may result in amino acid substitutions, additions, deletions, fusions and truncations in the polypeptide encoded by the reference sequence, as discussed below. A typical variant of a polypeptide differs in amino acid sequence from the reference polypeptide. Generally, alterations are limited so that the sequences of the reference polypeptide and the variant are closely similar overall and, in many regions, identical. A variant and reference polypeptide may differ in amino acid sequence by one or more substitutions, insertions, deletions in any combination. A substituted or inserted amino acid residue may or may not be one encoded by the genetic code. Typical conservative substitutions include Gly, Ala; Val, Ile, Leu; Asp, Glu; Asn, Gin, Ser, Thr; Lys, Arg; and Phe and Tyr. A variant of a polynucleotide or polypeptide may be naturally occurring such as an allele, or it may be a variant that is not known to occur naturally. Non-naturally occurring variants of polynucleotides and polypeptides may be made by mutagenesis techniques or by direct synthesis. Also included as variants are polypeptides having one or more post-translational modifications, for instance glycosylation, phosphorylation, methylation, ADIP ribosylation and the like. Embodiments include methylation of the N-terminal amino acid, phosphorylations of serines and threonines and modification of C-terminal glycines. The term “unit cell” refers to a basic 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 “space group” refers to the arrangement of symmetry elements of a crystal. The term “molecular replacement” refers to a method that involves generating a-preliminary model of a variant of human type III 3a-HSD crystal whose structure coordinates are unknown, by orienting and positioning a molecule whose structure coordinates are known (e.g., human type III 3a-HSD coordinates from Table 1) within the unit cell of the unknown crystal so as best to account for the observed diffraction pattern of the unknown crystal. Phases can then be calculated from this model and combined with the observed amplitudes to give an approximate Fourier synthesis of the structure whose coordinates are unknown. This, in turn, can be subject to any of the several forms of refinement to provide a final, accurate structure of the unknown crystal. Lattman, E., “Use of the Rotation and Translation Functions”, in Methods in Enzymology, 115, pp. 55-77 (1985); M. G. Rossmann, ed., “The Molecular Replacement Method”, Int. Sci. Rev. Ser., No. 13, Gordon &amp; Breach, New York, (1972). Using the structure coordinates of human type III 3a-HSD provided by this invention, molecular replacement may be used to determine the structure coordinates of a crystalline variant, e.g co-complexed with a specific inhibitor, or homologue of human type III 3a-HSD or of a different crystal form of human type III 3a-HSD.  
       DETAILED DESCRIPTION OF THE INVENTION  
       [0019]     In order that the invention described herein may be more fully understood, the following detailed description is set forth.  
         [0020]     The present invention relates to crystalline human type III 3a-HSD, the structure of human type III 3a-HSD 3a-HSD as determined by. X-ray crystallography, the use of that structure to solve the structure of human type III 3a-HSD homologues and of other crystal forms of human type III 3a-HSD, co-complexes of human type III 3a-HSD, and the use of the human type III 3a-HSD structure and that of its homologues, and co-complexes to design and to select modulators of human type III 3a-HSD.  
         [0000]     A. The Structure of Human type III 3a-HSD in Complex with NADP.  
         [0021]     The present invention provides, for the first time, crystals of human type III 3a-HSD grown in the presence of NADP from solutions of polyethylene glycol. The crystals have rhombohedral space group symmetry and reached 0.5×0.5×0.2 mm. The unit cell of said crystals is of the following dimensions: a=b=c=108.5+/−1 Å, α=β=γ−85.1°+/−1°. The structure coordinates of human type III 3a-HSD 3a-HSD, as determined by X-ray crystallography of crystalline human type III 3a-HSD, is listed in Table 1.  
         [0022]     Crystal packing reveals that human type III 3a-HSD crystallizes in a single dimmer (data in Table 1 are for the dimer).  
         [0023]     The enzyme core is formed by a α/β barrel with a cylindrical core of eight parallel β-strands surrounded by eight α-helices which run anti-parallel to the β-sheet. This barrel is formed by repeating the β/α unit eight times with two deviations: First, an additional helix exists between β-strand 7 and helix 8 of the barrel; and a second helix exists between helix 8 and the C-terminal region. At the N-terminus, two additional, anti-parallel β-strands, which are connected by a tight hairpin-loop, form the bottom seal of the barrel.  
         [0024]     Our understanding of the structure of human type III 3a-HSD has enabled the identification of the active and cofactor binding sites of the enzyme. The active site moiety is characterized by at least amino acid residues TYR 24, ALA 25, ALA 52, VAL 54, TYR 55, LYS 84, TRP 86, HIS 117, ILE 129, ASN 167, GLN 190, TYR 216, HIS 222, GLU 224, PRO 226, TRP 227, LEU 306, LEU 308, ILE 310, PHE 311, TIP 1, TIP 33, TIP 131, TIP 225, TIP 235 using the sequence and numbering according to SEQ ID NO:1. The cofactor binding site (here NADP) is characterized by at least amino acid residues GLY 22, THR 23, TYR 24, ASP 50, TYR 55, LYS 84, HIS 117, SER 166, ASN 167, GLN 190, TYR 216, SER 217, ALA 218, LEU 219, GLY 220, SER 221, HIS 222, LEU 236, ALA 253, LEU 268, ALA 269, LYS 270, SER 271, TYR 272, ASN 273, ARG 276, GLN 279, ASN 280, LEU 306, TIP 17, TIP 27, TIP 53, TIP 93, TIP 122, TIP 207, TIP 219, TIP 224 using the sequence and numbering according to SEQ ID NO:1 and Table 1 (for the TIP (=water) molecules).  
         [0000]     B. Uses of the Structure Coordinates of Human Type III 3a-HSD  
         [0025]     For the first time, the present invention permits the use of molecular design techniques to design, select and synthesize chemical entities and compounds, including inhibitory compounds, capable of binding to the active site or accessory binding site of human type III 3a-HSD, in whole or in part.  
         [0026]     One approach enabled by this invention, is to use the structure coordinates of human type III 3a-HSD to design compounds that bind to the enzyme and alter the physical properties of the compounds in different ways, e.g., solubility. For example, this invention enables the design of compounds that act as competitive inhibitors of the human type III 3a-HSD enzyme by binding to, all or a portion of, the active site of human type III 3a-HSD. A second design approach is to probe a human type III 3a-HSD crystal with molecules composed of a variety of different chemical entities to determine optimal sites for interaction between candidate human type III 3a-HSD inhibitors and the enzyme. For example, high resolution X-ray diffraction data collected from crystals saturated with solvent allows the determination of where each type of solvent molecule sticks. Small molecules that bind tightly to those sites can then be designed and synthesized and tested for their human type III 3a-HSD inhibitor activity. Travis, J., Science, 262, p.1374 (1993).  
         [0027]     This invention also enables the development of compounds that can isomerize to short-lived reaction intermediates in the chemical reaction of a substrate or other compound that binds to human type III 3a-HSD, with human type III 3a-HSD. Thus, the time-dependent analysis of structural changes in human type III 3a-HSD 3a-HSD during its interaction with other molecules is enabled. The reaction intermediates of human type III 3a-HSD can also be deduced from the reaction product in co-complex with human type III 3a-HSD. Such information is useful to design improved analogues of known human type III 3a-HSD potentiators or inhibitors or to design novel classes of potentiators or inhibitors based on the reaction intermediates of the human type III 3a-HSD 3a-HSD enzyme and human type III 3a-HSD-ligand co-complex. This provides a novel route for designing human type III 3a-HSD 3α-HSD inhibitors with both high specificity and stability.  
         [0028]     Another approach made possible and enabled by this invention, is to screen computationally small molecule data bases for chemical entities or compounds that can bind in whole, or in part, to the human type III 3a-HSD enzyme. In this screening, the quality of fit of such entities or compounds to the binding site may be judged either by shape complementarity or by estimated interaction energy (Meng, E. C. et al., J. Comp. Chem., 13, pp. 505-524 (1992)).  
         [0029]     Because human type III 3a-HSD may crystallize in more than one crystal form, the structure coordinates of human type III 3a-HSD, or portions thereof, as provided by this invention are particularly useful to solve the structure of those other crystal forms of human type III 3a-HSD. They may also be used to solve the structure of human type III 3a-HSD co-complexes, or of the crystalline form of any other protein with significant amino acid sequence homology to any functional domain of human type III 3a-HSD.  
         [0030]     One method that may be employed for this purpose is molecular replacement. In this method, the unknown crystal structure, whether it is another crystal form of human type III 3a-HSD, human type III 3a-HSD co-complex, or the crystal of some other protein with significant amino acid sequence homology to any functional domain of human type III 3a-HSD, may be determined using the human type III 3a-HSD structure coordinates of this invention as provided in Table 1. This method will provide an accurate structural form for the unknown crystal more quickly and efficiently than attempting to determine such information ab initio.  
         [0031]     In addition, in accordance with this invention, human type III 3a-HSD may be crystallized in co-complex with known human type III 3a-HSD inhibitors, as e.g. NSAIDs and SSRIs. The crystal structures of a series of such complexes may then be solved by molecular replacement and compared with that of wild-type human type III 3a-HSD. Potential sites for modification within the binding site of the enzyme may thus be identified. This information provides an additional tool for determining the most efficient binding interactions, for example, increased hydrophobic interactions, between human type III 3a-HSD and a chemical entity or compound.  
         [0032]     All of the complexes referred to above may be studied using well-known X-ray diffraction techniques and may be refined versus 1-3 Å resolution X-ray data to an R value of about 0.20 or less using computer software, such as X-PLOR (Yale University, .COPYRGT.1992, distributed by Molecular Simulations, Inc.). See, e.g., Blundel &amp; Johnson, supra; Methods in Enzymology, vol. 114 &amp; 115, H. W. Wyckoff et al., eds., Academic Press (1985). This information may thus be used to optimize known classes of human type III 3a-HSD potentiators and inhibitors, and more importantly, to design and synthesize novel classes of human type III 3a-HSD potentiators and inhibitors.  
         [0033]     The design of compounds that bind to human type III 3a-HSD according to this invention generally involves consideration of two factors. First, the compound must be capable of physically and structurally associating with human type III 3a-HSD. Non-covalent molecular interactions important in the association of human type III 3a-HSD with its substrate include hydrogen bonding, van der Waals and hydrophobic interactions.  
         [0034]     Second, the compound must be able to assume a conformation that allows it to associate with human type III 3a-HSD. Although certain portions of the compound will not directly participate in this association with human type III 3a-HSD, those portions may still influence the overall conformation of the molecule. This, in turn, may have a significant impact on potency. Such conformational requirements include the overall three-dimensional structure and orientation of the chemical entity or compound in relation to all or a portion of the binding site, e.g., active site or accessory binding site of human type III 3a-HSD, or the spacing between functional groups of a compound comprising several chemical entities that directly interact with human type III 3a-HSD.  
         [0035]     The potential inhibitory or binding effect of a chemical compound on human type III 3a-HSD may be analyzed prior to its actual synthesis and testing by the use of computer modelling techniques. If the theoretical structure of the given compound suggests insufficient interaction and association between it and human type III 3a-HSD, synthesis and testing of the compound is obviated. However, if computer modeling indicates a strong interaction, the molecule may then be synthesized and tested for its ability to activate or inhibit the human type-3 by testing it in two functional assays—a spectrophotometric and a modified radiometrc assay as described by L. Griffin and S. Mellon in Proc. Natl. Acad. Sci. USA, 1999, 96 (23), 13512-13517, and by T. Penning et al. In Biochem. J., 2000, 351, 67-77. In this manner, synthesis of inoperative compounds may be avoided.  
         [0036]     An inhibitory or other binding compound of human type III 3a-HSD may be computationally evaluated and designed by means of a series of steps in which chemical entities or fragments are screened and selected for their ability to associate with the individual binding pockets or other areas of human type III 3a-HSD.  
         [0037]     One skilled in the art may use one of several methods to screen chemical entities or fragments for their ability to associate with human type III 3a-HSD and more particularly with the individual binding pockets of the human type III 3a-HSD active site. This process may begin by visual inspection of, for example, the active site on the computer screen based on the human type III 3a-HSD coordinates in Table 1. Selected fragments or chemical entities may then be positioned in a variety of orientations, or docked, within an individual binding pocket of human type III 3a-HSD. Docking may be accomplished using software such as Quanta and Sybyl, followed by energy minimization and molecular dynamics with standard molecular mechanics forcefields, such as CHARMM and AMBER.  
         [0038]     Specialized computer programs may also assist in the process of selecting fragments or chemical entities. These include: 
    1. GRID (Goodford, P. J., “A Computational Procedure for Determining Energetically Favorable Binding Sites on Biologically Important Macromolecules”, J. Med. Chem., 28, 849-857 (1985)). GRID is available from Oxford University, Oxford, UK.     2. MCSS (Miranker, A. and M. Karplus, “Functionality Maps of Binding Sites: A Multiple Copy Simultaneous Search Method.” Proteins: Structure. Function and Genetics, 11, 29-34 (1991)). MCSS is available from Molecular Simulations, Burlington, Mass.     3. AUTODOCK (Goodsell, D. S. and A. J. Olsen, “Automated Docking of Substrates to Proteins by Simulated Annealing”, Proteins: Structure. Function, and Genetics, 8, 195-202 (1990)). AUTODOCK is available from Scripps Research Institute, La Jolla, Calif.     4. DOCK (Kuntz, I. D. et al., “A Geometric Approach to Macromolecule-Ligand Interactions”, J. Mol. Biol., 161, 269-288 (1982)). DOCK is available from University of California, San Francisco, Calif.     5. GOLD (Jones G et al., “Development and Validation of a Gentic Algorithm for Flexible Docking”, J. Mol. Biol. 267, 727-748 (1997))    
 
         [0044]     Once suitable chemical entities or fragments have been selected, they can be assembled into a single compound or inhibitor. Assembly may be proceed by visual inspection of the relationship of the fragments to each other on the three-dimensional image displayed on a computer screen in relation to the structure coordinates of human type III 3a-HSD. This would be followed by manual model building using software such as Quanta or Sybyl. Useful programs to aid one of skill in the art in connecting the individual chemical entities or fragments include: 
    1. CAVEAT (Bartlett, P. A. et al, “CAVEAT: A Program to Facilitate the Structure-Derived Design of Biologically Active Molecules”. In “Molecular Recognition in Chemical and Biological Problems”, Special Pub., Royal Chem. Soc., 78, pp. 182-196 (1989)). CAVEAT is available from the University of California, Berkeley, Calif.     2. 3D Database systems such as MACCS-3D (MDL Information Systems, San Leandro, Calif.). This area is reviewed in Martin, Y. C., “3D Database Searching in Drug Design”, J. Med. Chem., 35, pp. 2145-2154 (1992)).     3. HOOK (available from Molecular Simulations, Burlington, Mass.).    
 
         [0048]     Instead of proceeding to build an human type III 3a-HSD potentiator or inhibitor in a step-wise fashion one fragment or chemical entity at a time as described above, human type III 3a-HSD binding compounds may be designed as a whole or “de novo” using either an empty active site or optionally including some portion(s) of a known inhibitor(s). These methods include: 
    1. LUDI (Bohm, H.-J., “The Computer Program LUDI: A New Method for the De Novo Design of Enzyme Inhibitors”, J. Comp. Aid. Molec. Design, 6, pp. 61-78 (1992)). LUDI is available from Biosym Technologies, San Diego, Calif.     2. LEGEND (Nishibata, Y. and A. Itai, Tetrahedron, 47, p. 8985 (1991)). LEGEND is available from Molecular Simulations, Burlington, Mass.     3. LeapFrog (available from Tripos Associates, St. Louis, Mo.).    
 
         [0052]     Other molecular modelling techniques may also be employed in accordance with this invention. See, e.g., Cohen, N. C. et al., “Molecular Modeling Software and Methods for Medicinal Chemistry”, J. Med. Chem., 33, pp. 883-894 (1990). See also, Navia, M. A. and M. A. Murcko, “The Use of Structural Information in Drug Design”, Current Opinions in Structural Biology, 2, pp. 202-210 (1992).  
         [0053]     Once a compound has been designed or selected by the above methods, the efficiency with which that compound may bind to human type III 3a-HSD may be tested and optimized by computational evaluation. For example, a compound that has been designed or selected to function as an human type III 3a-HSD inhibitor must also preferably traverse a volume not overlapping that occupied by the active site when it is bound to the native substrate. An effective human type III 3a-HSD inhibitor must preferably demonstrate a relatively small difference in energy between its bound and free states (i.e., a small deformation energy of binding). Thus, the most efficient human type III 3a-HSD inhibitors should preferably be designed with a deformation energy of binding of not greater than about 10 kcal/mole, preferably, not greater than 7 kcavmole. Human type III 3a-HSD inhibitors may interact with the enzyme in more than one conformation that is similar in overall binding energy. In those cases, the deformation energy of binding is taken to be the difference between the energy of the free compound and the average energy of the conformations observed when the inhibitor binds to the enzyme.  
         [0054]     A compound designed or selected as binding to human type III 3a-HSD may be further computationally optimized so that in its bound state it would preferably lack repulsive electrostatic interaction with the target enzyme. Such non-complementary (e.g., electrostatic) interactions include repulsive charge-charge, dipole-dipole and charge-dipole interactions. Specifically, the sum of all electrostatic interactions between the inhibitor and the enzyme when the inhibitor is bound to human type III 3a-HSD, preferably make a neutral or favorable contribution to the enthalpy of binding.  
         [0055]     Specific computer software is available in the art to evaluate compound deformation energy and electrostatic interaction. Examples of programs designed for such uses include: Gaussian 92, revision C [M. J. Frisch, Gaussian, Inc., Pittsburgh, Pa. .COPYRGT.1992]; AMBER, version 4.0 [P. A. Kollman, University of California at San Francisco, .COPYRGT. 1994]; QUANTA/CHARMM [Molecular Simulations, Inc., Burlington, Mass. .COPYRGT.1994]; and Insight II/Discover (Biosysm Technologies Inc., San Diego, Calif. .COPYRGT.1994). These programs may be implemented, for instance, using a Silicon Graphics workstation, IRIS 4D/35 or IBM RISC/6000 workstation model 550. Other hardware systems and software packages will be known to those skilled in the art. Once an human type III 3a-HSD-binding compound has been optimally selected or designed, as described above, substitutions may then be made in some of its atoms or side groups in order to improve or modify its binding properties. Generally, initial substitutions are conservative, i.e., the replacement group will have approximately the same size, shape, hydrophobicity and charge as the original group. It should, of course, be understood that components known in the art to alter conformation should be avoided. Such substituted chemical compounds may then be analyzed for efficiency of fit to human type III 3a-HSD by the same computer methods described in detail, above.  
         [0056]     The following Examples illustrate the present invention, without in any way limiting the scope thereof.  
       EXAMPLE 1  
     Structure Determination of Human type III 3a-HSD Complexed with NADP with X-Ray  
       [0057]     Cloning: Full length type III 3a-HSD cDNA is amplified by RT-PCR from human fetal brain total RNA (Clontech). Both first strand cDNA synthesis and PCR are performed in a single tube using gene-specifc primers with the SuperScript One-Step RT-PCR (GibcoBRL, Life Technologies) kit emplyoing an RT/Platinum Taq polymerase mix. The following reaction components are mixed in a single PCR tube according to the vendor&#39;s instructions: 2× Reaction Mix 25 μl, 1 μg template RNA, 0.4 μM final concentration of each gene-specific primer (sense and anti-sense), 1 μl RT/Platinum Taq polymerase mix, and nuclease-free water up to 50 μl final reaction volume.  
         [0058]     The sense gene-specific primers are of the following sequences:  
         [0059]     For the His-tagged construct:  
                                     (SEQ ID NO: 3)                5′ - ATACATATGCACCACCACCACCACCACCTCGAGGTTCTGTTCCAG                   GGTCCGGATTCGAAATACCAGTGTGTG          
 
         [0060]     For the non-tagged construct:  
                               5′ - TTTCATATGGATTCGAAATACCAGTGTGTG   (SEQ ID NO: 4)              
 
         [0061]     The same anti-sense gene-specific primer with the following sequence is used for the full length amplification of both cDNAs:  
                               5′ - AGAGCGGCCGCTGTTAATATTCATCAGAAA   (SEQ ID NO: 5)              
 
         [0062]     The RT-PCR is performed on a GeneAmp PCR System 9700 (PE Appliad Biosystems). First strand cDNA synthesis is achieved with one cycle at 45° C. for 30 min, followed by RT denaturation at 94° C. for 2 min. PCR is conducted with 40 cycles of: denaturation at 94° C. for 15 sec, primer annealling at 55° C. for 30sec, and primer extension at 68° C. for 2 min, followed by a single cycle of final extension at 72° C. for 10 min.  
         [0063]     The PCR product is digested with NdeI and NotI, purified by agarose gel electrophoresis, and ligated into the NdeI/NotI sites of pET26b(+) (Novagen) using standard ligation conditions with T4 DNA ligase (Promega). Both constructs are sequenced (see Appendix).  
         [0000]     Expression  
         [0064]     The plasmids are transformed into BL21 (DE3) and BL21 (DE3)pLysS  E. coli  cells (Novagen). Small scale (10 ml) cultures are grown to check expression levels and solubility. It is found that both 3a-HSD constructs lead to high levels of inclusion bodies even at 25° C. BL21 (DE3) gives better expression levels than BL21 (DE3)pLysS. For production scale, 4 liter shake flask cultures are grown: TBII medium, 37° C., induced with 1 mM IPTG for 4 h.  
         [0065]     The usual pellet mass is 30 to 40 g. Due to the fact, that refolding is the method of choice to produce soluble protein, the non-tagged construct is used for the next steps.  
         [0000]     Refolding and Purification  
         [0066]      E. coli  wet cell pellets are suspended to 15% w/v in lysis buffer (50 mM Tris, 5 mM DTT, 5 mM EDTA, 5 mM Benzamidine-HCl; pH 8.0) using a Heidolph DIAX 600 homogenizer. Cells are lysed by passage twice through a Manton-Gaulin homogenizer (set at 1200 bar). The cell lysate is spun for 30 min at 16,000g and the supernatant removed. The resulting inclusion body pellets are resuspended in lysis buffer (to approx. 5% w/v) using the Heidolph homogenizer and re-centrifuged. This process is repeated until the resulting supernatant is clear. A final wash using Milli-Q water (containing 5 mM DTT) as solvent is carried out, a sample of the water suspension diluted 10-fold with guanidine buffer (6M guanidine-HCl, 50 mM Tris and 50 mM DTT; pH 8.0.) and analysed using an analytical RP-HPLC system (Thermo Separation Products), fitted with an Orpegen C8 analytical column (HD-gel-RP-7s-300, 150 mm×4 mm). The resulting inclusion body pellet is then solubilized to 14 mg/ml using guanidine buffer and centrifuged.  
         [0067]     The guanidine supernatant is diluted with guanidine buffer to a protein concentration of 200 μg/ml and subsequently dialysed at 4° C. vs 3×10 volumes of 50 mM Tris pH 8.5, containing 5 mM DTT and 1 mM EDTA. The rententate is centrifuged (30 min at 16,000g) and loaded onto a Q-Sepharose HP anion-exchange column at a flow rate of 8 ml/min, equilibrated with 50 mM Tris pH 8.5 containing 5 mM DTT. After washing the column with 5 column vol (250 ml) of buffer, a linear salt gradient of 0-1 M NaCl in the same buffer is used to elute the bound proteins from the column. The unbound is collected and concentrated using a 10,000 Da cut-off ultrafiltration membrane to approximately 10 mg/ml and loaded onto a gel-filtration column. The column (Superdex 75, XK26/60) is pre-equilibrated with 50 mM Tris pH 8.0 containing 150 mM NaCl and 5 mM DTT. 12 ml of concentrated protein solution is loaded and eluted at a flow-rate of 3 ml/min. The 3a-HSD peak elutes at ˜190 ml, well separated from a small quantity of aggregated material MS: 36736.4 Da (M+H) + . (ESI-MS).  
         [0068]     Binding of natural ligands is a prerequisite for functionality. One method to detect ligand binding by NMR takes advantage of the increased transverse relaxation rates of the ligand protons when the ligand is bound. Increased line widths in the presence of protein thus indicates binding. Binding experiments of NADP to 3a-HSD are done and check by NMR. In the presence of 3a-HSD, the NADP peaks are broadened so much that they are hardly visible in the spectrum. This proves binding of NADP to 3a-HSD.  
         [0069]     Similarly, binding of the presumed natural substrate, allopregnanolone, is proven by observing line broadening of allopregnanolone resonances. Since allopregnanolone is poorly soluble in water, 2% DMSO-d 6  and 5% ethanol are added as co-solvents. Even then, the maximum achievable concentration of allo-pregnanolone is only about 20 μM. This is sufficient, however, to see the two upfield shifted methyl resonances of allopregnanolone broadening in the presence of 3a-HSD. Based on the NMR analysis, 3a-HSD appears well-folded and functional in respect to cofactor- and ligand-binding.  
         [0070]     Crystallization: 3a-HSD in 50 mM Tris pH 8.0, 150 mM NaCl and 5 mM DTT, is concentrated to 20 mg/ml. For NADP-complexed 3a-HSD, solid NADP-sodium salt is added. Standard crystallization screening using the hanging drop method at 20° C. is used. Commercial screens from Hampton Research and Emerald BioStructures Inc. are used. The following crystallization conditions are found to give promising results: 
    200 mM Ammonium acetate, 100 mM Sodium citrate, pH 5.6, 30% PEG 4000     200 mM Ammonium sulfate, 100 mM MES, pH 6.0, 30% PEG monomethylether 5000    
 
         [0073]     Other conditions which are found to give crystals: 
    200 mM Ammonium sulfate, 100 mM MES, pH 6.0, 30% PEG monomethylether 5000, 5%     1,2-Propandiol; 200 mM Ammonium sulfate, 100 mM MES, pH 6.0, 30% PEG     monomethylether 5000, 5% Ethanol; 200 mM Ammonium sulfate, 100 mM MES, pH 6.0, 30%     PEG monomethylether 5000, 5% 1-Propanol. Thus, in general, the following conditions may laed to crystals:     50-200 mM ammonium sulfate or ammonium acetate, 25-200 mM MES, pH 6.0 or 25-200 mM sodium citrate, 20-30% PEG monomethylether 2000 or 5000 or 20-30% PEG 2000, 4000, 6000, 8000; 0-10% additives as for example glycerin, 1,2-propandiol, ethylene glycol, and 0-20 mM DTT.    
 
         [0079]     The NADP-complexed protein gives much nicer crystals than the apo-protein and crystallization conditions are optimized for the cofactor-3α-HSD complex. Finally, large prisms can be grown which reached 0.5×0.5×0.2 mm. Optimal growth conditions are 25% PEG monomethylether 5000, 5% Glycerol, 100 mM MES, pH 6.0, 200 mM ammoniumsulfate in the precence of 5 mM DTT. Optimal crystal size is reached after 1-2 weeks. A large crystal (3a-HSD in complex with NADP) is mounted in a capillary and diffraction data is collected using a 30 cm MAR imaging plate detector. Those of skill in the art will appreciate that the aforesaid crystallization conditions can be varied. Such variations may be used alone or in combination, and include final protein/inhibitor complex concentrations between 5 mg/ml and 35 mg/ml; all combinations of 3α-HSD/inhibitor to precipitant ratios; citrate concentrations between 1 mM and 200 mM; DTT concentrations between 0 mM and 20 mM; and any concentration of β-mercaptoethanol; pH ranges between 5.5 and 9.5; PEG concentrations between 10% and 25% (gms/100 ml); PEG weights between 2000 and 20000; HEPES concentrations between 5 and 395 mM; and any concentration or type of detergent; any temperature between −5° C. and 100° C.; and crystallization of 3α-HSD co-complexes by batch, liquid bridge, or dialysis method using these conditions or variations thereof.  
         [0080]     Structure determination with X-ray: A single crystal of the human type III 3a-HSD complexed with the cofactor NADP is mounted into a glass capillary and X-ray diffraction data is collected at room temperature with a MAR imaging plate system (150 μm pixel size) mounted on a Enraf-Nonius FR591 rotation anode generator equipped with a Cu target, a 0.3 mm×3.0 mm fine focus and Osmic mirrors. Images are collected with 1.0° oscillation each, using an exposure time of 600sec per frame and a crystal-to-detector distance of 120 mm. Raw diffraction data are processed and scaled with the HKL program suite version 1.96.6 (Otwinowski, Z and Minor, W. Processing of X-ray Diffraction Data Collected in Oscillation Mode. Methods in Enzymology 1996; 276. C. W. Carter, Jr. and R. M. Sweet, Eds., Academic Press).  
         [0081]     The structure is determined by molecular replacement, using the crystal structure of rat type III 3a-HSD (available at the PDB under accession number 1AFS) as search model Molecular replacement is performed with CNX 2000 (Brünger, AT et al. Crystallography &amp; NMR System: A new software suite for macromolecular structure determination. Acta Cryst.1998; D54: 905-921.), using data between 15 and 4 Å; the “Fastdirect” option is used. At this stage, inspection of the σ A -weighted Fo-Fc electron density map with the program O version 7.0 (Jones, T A et al. Improved Methods for Building Protein Models in Electron Density Maps and the Location of Errors in these Models. Acta Crystallogr. 1991; A47: 110-19) reveals strong density for most of the side chains and all backbone atoms. The model of 3αHSD is built and adjusted to fit the density where necessary. The structure is refined by a number of cycles of torsion angle dynamics and energy minimization, interspersed by model rebuilding steps. For refinement, the “refine.inp” script pf CNX 2000 is used, with the following (non-default) option: Bulk solvent correction (based on the mask method). Cross-validation is used throughout refinement using a test set comprising 5% of the reflections. Water molecules are identified with the CNX script water_pick.inp, and selected based on difference peak height (greater than 3.0σ), hydrogen-bonding and distance criteria. The quality of the final refined model is assessed with the programs CNX 2000. The mean figure of merit for the crystal structure is up to 2 Å resolution (Table 1).  
       EXAMPLE 2  
     The Use of Molecular Replacement to Solve an Unknown Type III 3a-HSD Crystal Structure  
       [0082]     The method of molecular replacement is used to determine the structure coordinates of crystals of human type III 3a-HSD in complex with a ligand (see below Example 4: e.g. 2-acetylbenzofuran) and NADP (as cofactor) in comparison with crystals of human type III 3a-HSD in complex with NADP (as prepared in Example 1). Crystals of human type III 3a-HSD in complex with e.g. 2-acetylbenzofuran are grown under conditions identical to those for crystals of human type III 3a-HSD in complex with the cofactor NADP.  
         [0083]     X-ray diffraction data up to 2.0 Å resolution is collected on the 3a-HSD/NADP-2-acetylbenzofuran co-complex. A difference electron density map that combines diffraction data of the 2 results is used to locate structure changes that has occurred. Negative features (electron density) are found in the map wherever localized atoms in the ligand complex are removed or shifted by switching to the new ligand. Positive features are found when localized atoms are introduced into the structure, and indicated the new positions of shifted atoms.  
         [0084]     These shifts, plus the new atoms referred to above, are modeled, and the resulting structure is refined against the X-ray data to determine a final picture of the co-complex of NSAIDs with 3a-HSD. The human type III 3a-HSD structure coordinates known for the first time by virtue of this invention may be used to solve the unknown structure of any homologue or co-complex of 3a-HSD using the above-described method. This method may also be used to determine the binding or orientation of a ligand or chemical entity in the active binding site of 3a-HSD. With this approach, we find that the structure of crystals, e.g. in the active site, of human type III 3a-HSD complexed with potential modulators, e.g. inhibitors may be different than the structure of human type III 3a-HSD complexed with NADP alone, e.g. as described in Table 1.  
       EXAMPLE 3  
     In Silico Gold Docking: Simulation of binding of Allopregnolone or Other Compounds to Human Type III 3a-HSD  
       [0085]     We simulate the binding mode of ligands to the active site of HSD using the X-ray structure of HSD. As a ligand molecule we select allopregnanolone of which we build a molecular model and to which we apply molecular mechanics minimization with the Sybyl (version 6.7.2) molecular modeling program. The model of HSD is obtained by assignment of Sybyl atom types to the atoms of chain A of HSD and co-cystallised NAP. To all 2263 atoms we add in total 2626 missing hydrogen atoms whereby polar amino acids Glu (in total 23), Asp (in total 18), Arg (in total 15), Lys (in total 26) as well as NADP (1) are regarded to be in their ionized state. The GOLD docking program is used to carry out 20 independent runs of docking the ligand model to the HSD model. The radius of the sphere defining the binding site is set to 15A, and the coordinates of the center of the sphere are such that 1029 atoms (including hydrogen atoms) of the following 90 residues NAP 1, GLY 22, THR 23, TYR 24, ALA 25, PRO 26, ALA 27, GLU 28, VAL 29, PRO 30, LYS 31, ALA 34, ASP 50, SER 51, ALA 52, HIS 53, VAL 54, TYR 55, ASN 56, ASN 57, GLU 58, GLU 59, GLN 60, VAL 61, TYR 81, THR 82, SER 83, LYS 84, LEU 85, TRP 86, SER 87, ASN 88, SER 89, HIS 90, ALA 98, ARG 101, SER 102, ASN 105, TYR 114, LEU 115, ILE 116, HIS 117, PHE 118, PRO 119, VAL 120, SER 121, VAL 122, LYS 123, PRO 124, GLY 125, GLU 126, GLU 127, VAL 128, ILE 129, PRO 130, LYS 131, ILE 137, LEU 138, PHE 139, SER 166, ASN 167, GLN 190, VAL 191, GLU 192, TYR 216, SER 217, SER 221, HIS 222, ARG 223, GLU 224, GLU 225, PRO 226, TRP 227, VAL 228, ASP 229, LEU 268, LYS 270, TYR 272, ARG 304, TYR 305, LEU 306, THR 307, LEU 308, ASP 309, ILE 310, PHE 311, ALA 312, TYR 317, PRO 318, and PHE 319 define the binding cavity in the GOLD program. Each of the 20 GOLD runs with our models of HSD and allopregnanolone results in a scored model of the molecule allopregnanolone docked to HSD. The GOLD score or Fitness of the models ranges from 26.94 to 42.54. All residues with atoms within 4A of docked allopregnanolone are depicted, namely NAP 1, TYR 24, ALA 27, VAL 54, TYR 55, TRP 86, HIS 117, PHE 118, VAL 128, ILE 129, ASN 167, HIS 222, TRP 227, LEU 306, LEU 308 and PHE 311. Atom pair distances smaller than 0.9A (Sum of van der Waals radii of atom pair) are found between allopregnanolone (A) and the following 12 atoms of HSD: 
    /A/TYR — 24/HH=1.967 Å    /A/VAL — 541HG22=2.131 Å    /A/VAL — 54/HB=1.986 Å    /A/TRP — 86/CZ3=2.504 Å    /A/TRP — 86/CH2=2.460 Å    /A/HIS — 117/NE2=2.427 Å    /A/HIS — 117/NE2=1.799 Å (Hydrogen Bond)     /A/VAL — 128/CG2=2.779 Å    /A/VAL — 128/HG22=2.281 Å    /A/TRP — 227/CZ2=2.576 Å    /A/TRP — 227/HZ2=2.088 Å    /A/LEU — 308/HD22=2.152 Å   
 
         [0098]     In particular, it is seen that the 3-hydroxy group of allopregnanolone makes favorable strong electrostatic contacts with HIS 113, TYR 55 and the carboxamido group of NADP. Examples of regions in the binding site unoccupied by the docked ligand allopregnanolone can be seen within 4.5A of allopregnanolone and at more than 3A of HSD. Appropriate substitutions of allopregnanolone or molecules which share the modelled binding mode of allopregnanolone may occupy these regions and confer additional affinity to HSD. Similar Docking Procedures can be performed with other compounds, e.g. with compounds of a virtual library (available for example using MoSELECT (Gillet et al. J. of Molecular Graphics &amp; Modelling (2002) 20(6), 491-498) or with compounds obtained by the methods described herein.  
       EXAMPLE 4  
     NMR Screening  
       [0099]     NMR spectroscopy can be used to discover and design inhibitors of 3a-HSD type III. This is due to the well-known ability of NMR to detect interactions between ligands and a target protein, even if the interactions are only weak and have affinities in the millimolar range (Diercks, T.; Coles, M.; Kessler, H. Applications of NMR in drug discovery.  Curr. Opin. Chem. Biol.  2001, 5, 285-291; Hajduk, P. J.; Meadows, R. P.; Fesik, S. W. NMR-based screening in drug discovery.  Q. Rev. Biophys.  1999, 32, 211-240; Pellecchia, M.; Sem, D. S.; Wuthrich, K. NMR in drug discovery.  Nature Reviews Drug Discovery  2002, 1, 211-219). For this purpose, a solution of 3a-HSD is added to a mixture of compounds, and NMR properties of the compounds, such as their relaxation rates, are measured and compared in the presence and absence of 3a-HSD. An increase in relaxation rates reveals binding affinity between 3a-HSD and said compound. This effect can be enhanced by about a factor of 15 if side chains of 3a-HSD are spin-labeled with paramagnetic centers such as TEMPO (2,2,6,6-Tetramethylpiperidin-N-oxyl) or PROXYL (2,2,5,5-Tetramethylpyrrolidine-N-oxyl) (Jahnke, W.; Ruedisser, S.; Zurini, M. Spin Label Enhanced NMR Screening.  J. Am. Chem. Soc.  2001, 123, 3149-3150; Jahnke, W. Spin labels as a tool to identify and characterize protein—ligand interactions by NMR spectroscopy.  ChemBioChem  2002, 3, 167-173).  
         [0100]     About 200 compounds from an in-house NMR compound library (or library available from ACD Database, MDL Information Systems, Inc) containing a diverse set of small fragments of potential drugs are screened for interactions with 3a-HSD. Several fragments are identified which exhibited affinities to 3a-HSD with dissociation constants below 2 mM, more preferrentially 1 mM, even more preferrentially 0.5 mM. E.g. 2-acetylbenzofuran is found by this method and had a K i OX  of about 132.5 μM (see Example 5).  
         [0101]     Although 2-acetylbenzofuran binds to 3a-HSD only weakly, it is a progressible compound, i.e. it is a very small, soluble and “drug-like” compound that is amenable to chemical modification so that its potency can be improved. There are several ways to achieve this by NMR. One possibility is to select compounds by substructure or similarity search, and test them by NMR. Another possibility is to identify by NMR screening another compound that binds in the vicinity to 2-acetylbenzofuran, and to chemically link both compounds to yield a high-affinity ligand (Shuker, S. B.; Hajduk, P. J.; Meadows, R. P.; Fesik, S. W. Discovering high-affinity ligands for proteins: SAR by NMR.  Science  1996, 274, 1531-1534; Jahnke, W.; Florsheimer, A.; Blommers, M.; Paris, C. G.; Heim, J.; Nalin, C. M.; Perez, L. B. Second-site NMR screening and linker design.  Current Topics in Medicinal Chemistry  2002, 2, 1337-1348 (in press)). Given the availability of the coordinates from the crystal structure of 3a-HSD, however, the best way is to combine the results from NMR screening with in-silico GOLD docking, as described in example 3. NMR screening hits such as 2-acetylbenzofuran serve as input for GOLD docking experiments and guide the selection of compounds that are docked in silico. Since the docking itself, and the scoring of the results is not fully reliable, docking results need experimental validation by NMR. NMR and docking thus form an iterative cycle which leads to drastically improved compound potencies.  
         [0102]     In spite of its low affinity, the dissociation rate of 2-acetylbenzofuran is so slow that severe line broadening is observed by NMR, and more tightly binding compounds cannot be detected by conventional ligand-observe NMR screening (Diercks, T.; Coles, M.; Kessler, H. Applications of NMR in drug discovery.  Curr. Opin. Chem. Biol.  2001, 5, 285-291). We therefore had to develop an improved NMR screening method called NMR reporter screening. This method uses 2-acetylbenzofuran as “reporter ligand” and measures the ability of any test compound to displace the reporter ligand. By this technique, higher-affinity compounds can be detected by NMR screening that could previously not be detected (W. Jahnke, P. Floersheim, C. Ostermeier, X. Zhang, R. Hemmig, K. Hurth, D. Uzunov “NMR Reporter Screening for the Detection of High-Affinity Ligands”  Angew. Chemie , in press). The combination of NMR reporter screening and GOLD docking lead us to identify sub-micromolar inhibitors within short time with very little chemistry efforts.  
       EXAMPLE 5  
     Functional In Vitro Assay  
       [0103]     Materials: Steroid standards (&gt;98% purity) were purchased from Sigma Chemical Co.  3 H-allopregnanolone (64 Ci/mmol, [9, 11, 12- 3 H(N)]-allopregnanolone, herein after referred to as  3 H-ALLO) was purchased from New England Nuclear.  3 H-5α-dihydroprogesterone ( 3 H-5α-DHP) was synthesized in our lab using an enzymatic conversion of  3 H-ALLO to  3 H-5α-DHP by the 3a-HSD (see Enzymatic reactions). The oxidation product  3 H-5α-DHP was isolated and purified by semi-preparative HPLC and confirmed by GC/MS. All solvents were of analytical grade (Merck) and were used without further purification.  
         [0104]     Enzymatic reactions (oxidation of  3 H-ALLO to  3 H-5α-DHP and reduction of  3 H-5α-DHP to  3 H-ALLO): All enzymatic reactions were performed using pure recombinant type-3 human 3a-HSD expressed in  E. coli  and refolded and purified from bacterial inclusion bodies.  3 H-5a-DHP reduction was conducted in 100 μl reaction systems containing 100 mM sodium phosphate (pH 7.4), 4 μg of recombinant enzyme, 2 mM NADPH and 2.5 μM  3 H-5α-DHP (40 000 cpm) in 4% acetonitrile. Similarly,  3 H-ALLO oxidation was conducted in 100 μl reaction systems containing 100 mM sodium phosphate (pH 7.4), 4 μg of recombinant enzyme, 2 mM NADP +  and 2.5 μM  3 H-ALLO (40 000 cpm) in 4% acetonitrile. Reactions were initiated by the addition of the respective substrate and were incubated at 37° C. for 25 min. The selected reaction conditions afforded a rate of product accumulation within the linear range of the enzymatic conversion. Following the incubation, the reactions were quenched with 400 μl of ice-cold ethyl acetate. The resulting organic extracts were evaporated to dryness under a gentle stream of nitrogen and redissolved in hexane and injected into the HPLC for analysis. Negative control reactions omitting cofactor (NADPH or NADP + ) or enzyme were carried out in order to exclude any non-enzymatic conversion. In all instances the control reactions resulted in no detectable product formation.  
         [0105]     HPLC separation: Chromatographic separation of  3 H-ALLO and  3 H-5α-DHP was done on an Agilent 1100 series HPLC system (Agilent Technologies) equipped with a vacuum degasser, an autosampler, a quaternary pump and a compartment with a 5 μm normal phase LiChrosorb Diol column 125×4.6 mm (Merck). Chromatographic separation was achieved by isocratic elution with hexane/2-propanol (95:5, v/v). The flow rate was held constant at 1 ml/min. Sample injection volume is 1 ml. Column efflux is directly introduced into the Radioflow scintillation detector (Packard, 500 TR Series).  
         [0106]     Candidate-inhibitors for type III human 3a-HSD obtained by methods described above, e.g. Examples 1 to 5 are tested in the functional assay and its K i OX  determined (K i OX  is the dissociation constant of the inhibitor for the oxidation of  3 H-ALLO to  3 H-5α-DHP: K i =IC50/(1+[S]K m ), whereas IC50 is the concentration of the inhibitor required to achieve a half-maximal degree of inhibition. IC50 values are determined graphically by plotting inhibitor concentrations versus rate of conversion of substrate to product. [S] is the concentration of the substrate (i.e.  3 H-ALLO plus non-radiolabelled ALLO) in the sample and K m  is the Michaelis-Menten constant which is 4.9 μM for the oxidation of ALLO by the type-3 human 3a-HSD. E.g. 2-acetylbenzofuran has a K i OX  of about 132 μM.  
       EXAMPLE 6  
     Method to Find an Inhibitor of the Human Type III 3a-HSD Using the Rational Drug Design, the NMR Screening Methods, the In Silico Gold Docking, the Molecular Replacement and the In Vitro Functional Assay as Described Herein  
       [0107]     Improved inhibitors of human type III 3a-HSD can be found in combining any of the methods, e.g. as described before, e.g. by using rational drug design techniques as described above in the description, the NMR screening method or NMR reporter screening as e.g. described in example 4, in silico Gold Docking, as e.g. described in example 3, Molecular Replacement, e.g. as described in Example 2 and an in vitro functional assay, e.g. as described in Example 5, in order to validate candidates obtained by any in silico/X-ray method described above. One of the preferred combinations for finding inhibitors to human type III 3a-HSD comprises the following methods: 
    1.) obtaining first inhibitory candidates by using NMR screening and/or NMR reporter screening; and    
 
         [0109]     2.) co-crystallize the positive molecules (potential inhibitor) with the NADP/human type III 3a HSD complex and determine the difference of the three-dimensional structure of the active site of the Inhibitor-NADP-3a_HSD complex with the NADP-3a_HSD complex (as described in Table 1).  
                                                                                     TABLE 1                           Atom   Resi-   Num-                           Atom   Type   due   ber   X   Y   Z   OCC   B                                1   CB   SER   3   29.684   51.64   91.533   1   53.36       2   OG   SER   3   29.417   51.09   92.819   1   55.34       3   C   SER   3   29.46   49.403   90.45   1   47.9       4   O   SER   3   28.974   48.588   91.232   1   48.75       5   N   SER   3   27.49   50.911   90.626   1   52.53       6   CA   SER   3   28.97   50.849   90.429   1   50.93       7   N   LYS   4   30.414   49.08   89.582   1   43.74       8   CA   LYS   4   30.966   47.73   89.541   1   38.13       9   CB   LYS   4   30.745   47.095   88.163   1   38.91       10   CG   LYS   4   29.324   46.569   87.945   1   40.17       11   CD   LYS   4   29.191   45.868   86.602   1   41.95       12   CE   LYS   4   27.86   45.138   86.479   1   43.75       13   NZ   LYS   4   26.694   46.036   86.66   1   44.35       14   C   LYS   4   32.456   47.757   89.881   1   34.56       15   O   LYS   4   33.145   48.739   89.612   1   33.21       16   N   TYR   5   32.943   46.681   90.491   1   29.37       17   CA   TYR   5   34.346   46.58   90.884   1   26.52       18   CB   TYR   5   34.592   47.403   92.151   1   24.65       19   CG   TYR   5   33.549   47.202   93.228   1   25.8       20   CD1   TYR   5   33.731   46.272   94.256   1   24.69       21   CE1   TYR   5   32.756   46.091   95.248   1   27.04       22   CD2   TYR   5   32.367   47.945   93.211   1   24.77       23   CE2   TYR   5   31.391   47.773   94.184   1   26.99       24   CZ   TYR   5   31.592   46.845   95.201   1   27.76       25   OH   TYR   5   30.626   46.679   96.17   1   29.56       26   C   TYR   5   34.695   45.112   91.108   1   24.56       27   O   TYR   5   33.812   44.299   91.378   1   25.07       28   N   GLN   6   35.975   44.775   90.99   1   22.99       29   CA   GLN   6   36.412   43.393   91.142   1   23.88       30   CB   GLN   6   37.799   43.189   90.518   1   25.49       31   CG   GLN   6   37.861   43.549   89.035   1   29.27       32   CD   GLN   6   39.184   43.18   88.366   1   30.43       33   OE1   GLN   6   39.488   43.678   87.276   1   30.76       34   NE2   GLN   6   39.967   42.295   89.003   1   24.78       35   C   GLN   6   36.425   42.911   92.586   1   22.92       36   O   GLN   6   37.017   43.544   93.466   1   19.91       37   N   CYS   7   35.765   41.772   92.8   1   22.7       38   CA   CYS   7   35.646   41.126   94.106   1   23.76       39   CB   CYS   7   34.227   41.255   94.655   1   26.64       40   SG   CYS   7   33.651   42.899   94.969   1   32.59       41   C   CYS   7   35.906   39.637   93.971   1   25.06       42   O   CYS   7   35.891   39.089   92.868   1   24.42       43   N   VAL   8   36.144   38.99   95.108   1   23.76       44   CA   VAL   8   36.326   37.546   95.155   1   23.21       45   CB   VAL   8   37.743   37.12   95.601   1   24.81       46   CG1   VAL   8   38.736   37.422   94.498   1   28.43       47   CG2   VAL   8   38.138   37.83   96.901   1   23.25       48   C   VAL   8   35.312   37.022   96.163   1   22.77       49   O   VAL   8   34.985   37.706   97.137   1   21.39       50   N   LYS   9   34.799   35.821   95.923   1   22.09       51   CA   LYS   9   33.826   35.233   96.835   1   22.21       52   CB   LYS   9   32.967   34.197   96.1   1   22.05       53   CG   LYS   9   31.756   33.734   96.904   1   23.4       54   CD   LYS   9   30.88   32.796   96.084   1   25.76       55   CE   LYS   9   29.619   32.417   96.841   1   27.37       56   NZ   LYS   9   28.71   31.573   96.02   1   30.87       57   C   LYS   9   34.542   34.561   98.009   1   21.14       58   O   LYS   9   35.465   33.777   97.809   1   20.76       59   N   LEU   10   34.115   34.881   99.228   1   20.25       60   CA   LEU   10   34.693   34.303   100.441   1   20.25       61   CB   LEU   10   34.502   35.271   101.613   1   20.7       62   CG   LEU   10   35.566   36.326   101.924   1   24.07       63   CD1   LEU   10   36.404   36.635   100.726   1   23.86       64   CD2   LEU   10   34.896   37.572   102.491   1   21.11       65   C   LEU   10   34.022   32.963   100.751   1   20.4       66   O   LEU   10   32.942   32.677   100.228   1   21.07       67   N   ASN   11   34.641   32.146   101.604   1   19.41       68   CA   ASN   11   34.065   30.838   101.913   1   19.95       69   CB   ASN   11   35.099   29.916   102.589   1   20.22       70   CG   ASN   11   35.601   30.448   103.931   1   20.22       71   OD1   ASN   11   34.838   30.99   104.723   1   22.84       72   ND2   ASN   11   36.892   30.269   104.191   1   17.3       73   C   ASN   11   32.768   30.888   102.724   1   20.53       74   O   ASN   11   32.155   29.85   102.983   1   21.53       75   N   ASP   12   32.335   32.084   103.12   1   19.89       76   CA   ASP   12   31.072   32.204   103.858   1   19.81       77   CB   ASP   12   31.238   33.04   105.14   1   19.46       78   CG   ASP   12   31.491   34.522   104.862   1   20.54       79   OD1   ASP   12   31.606   34.92   103.688   1   18.88       80   OD2   ASP   12   31.58   35.297   105.836   1   23.31       81   C   ASP   12   29.979   32.819   102.989   1   20.88       82   O   ASP   12   28.908   33.182   103.486   1   19.57       83   N   GLY   13   30.258   32.947   101.693   1   21.36       84   CA   GLY   13   29.272   33.502   100.782   1   20.73       85   C   GLY   13   29.366   34.996   100.522   1   21.91       86   O   GLY   13   28.736   35.487   99.587   1   22.03       87   N   HIS   14   30.114   35.729   101.346   1   19.06       88   CA   HIS   14   30.261   37.162   101.134   1   19.56       89   CB   HIS   14   30.579   37.878   102.454   1   20.87       90   CG   HIS   14   29.413   37.943   103.39   1   23.26       91   CD2   HIS   14   28.218   38.569   103.279   1   23.14       92   ND1   HIS   14   29.379   37.266   104.591   1   24.98       93   CE1   HIS   14   28.214   37.47   105.178   1   23.12       94   NE2   HIS   14   27.49   38.257   104.403   1   25.76       95   C   HIS   14   31.341   37.459   100.091   1   19.18       96   O   HIS   14   32.131   36.58   99.73   1   19.71       97   N   PHE   15   31.363   38.696   99.609   1   18.44       98   CA   PHE   15   32.322   39.115   98.596   1   20.05       99   CB   PHE   15   31.588   39.59   97.34   1   20.76       100   CG   PHE   15   30.994   38.472   96.529   1   22.15       101   CD1   PHE   15   29.79   37.879   96.903   1   23.83       102   CD2   PHE   15   31.648   38.005   95.395   1   21.78       103   CE1   PHE   15   29.244   36.834   96.151   1   23.21       104   CE2   PHE   15   31.113   36.961   94.637   1   22.5       105   CZ   PHE   15   29.91   36.378   95.016   1   22.08       106   C   PHE   15   33.236   40.219   99.103   1   19.31       107   O   PHE   15   32.795   41.145   99.77   1   20.45       108   N   MET   16   34.513   40.108   98.77   1   17.56       109   CA   MET   16   35.505   41.084   99.197   1   18.31       110   CB   MET   16   36.553   40.375   100.063   1   16.53       111   CG   MET   16   37.762   41.217   100.464   1   19.92       112   SD   MET   16   39.091   40.217   101.224   1   23.07       113   CE   MET   16   38.55   40.145   102.873   1   20.88       114   C   MET   16   36.193   41.74   97.998   1   17.1       115   O   MET   16   36.657   41.043   97.097   1   17.96       116   N   PRO   17   38.257   43.088   97.969   1   17.41       117   CD   PRO   17   35.566   44.018   98.887   1   16.2       118   CA   PRO   17   36.913   43.814   96.864   1   17.6       119   CB   PRO   17   36.69   45.286   97.232   1   17.75       120   CG   PRO   17   35.361   45.249   98.013   1   16.66       121   C   PRO   17   38.399   43.417   96.906   1   19.01       122   O   PRO   17   38.993   43.38   97.984   1   18.82       123   N   VAL   18   38.996   43.121   95.754   1   18.52       124   CA   VAL   18   40.388   42.664   95.709   1   19.91       125   CB   VAL   18   40.702   41.981   94.349   1   21.31       126   CG1   VAL   18   39.786   40.79   94.151   1   21.12       127   CG2   VAL   18   40.527   42.983   93.206   1   20.92       128   C   VAL   18   41.482   43.692   95.989   1   19.98       129   O   VAL   18   42.636   43.328   96.212   1   20.88       130   N   LEU   19   41.133   44.97   95.946   1   19.6       131   CA   LEU   19   42.101   46.024   96.227   1   21.48       132   CB   LEU   19   42.226   46.994   95.041   1   21.81       133   CG   LEU   19   43.07   48.259   95.308   1   22.44       134   CD1   LEU   19   44.508   47.876   95.554   1   21.46       135   CD2   LEU   19   42.977   49.207   94.122   1   23.75       136   C   LEU   19   41.59   46.769   97.449   1   20.8       137   O   LEU   19   40.466   47.272   97.449   1   21.52       138   N   GLY   20   42.406   46.812   98.499   1   20.99       139   CA   GLY   20   42.003   47.487   99.718   1   20.32       140   C   GLY   20   42.889   48.67   100.076   1   20.56       141   O   GLY   20   44.073   48.7   99.744   1   20.63       142   N   PHE   21   42.304   49.644   100.759   1   19.53       143   CA   PHE   21   43.021   50.842   101.173   1   21.46       144   CB   PHE   21   42.103   52.061   101.04   1   22.25       145   CG   PHE   21   42.789   53.364   101.343   1   23.59       146   CD1   PHE   21   43.777   53.859   100.494   1   23.09       147   CD2   PHE   21   42.482   54.07   102.502   1   24.76       148   CE1   PHE   21   44.458   55.047   100.799   1   25.75       149   CE2   PHE   21   43.149   55.25   102.822   1   25.54       150   CZ   PHE   21   44.143   55.741   101.967   1   24.8       151   C   PHE   21   43.508   50.717   102.625   1   21.08       152   O   PHE   21   42.707   50.506   103.531   1   21.23       153   N   GLY   22   44.818   50.847   102.835   1   21.87       154   CA   GLY   22   45.375   50.748   104.178   1   22.01       155   C   GLY   22   45.302   52.092   104.88   1   24.14       156   O   GLY   22   45.555   53.117   104.253   1   22.23       157   N   THR   23   44.972   52.107   106.172   1   22.37       158   CA   THR   23   44.843   53.379   106.886   1   24.15       159   CB   THR   23   43.435   53.534   107.476   1   23.82       160   OG1   THR   23   43.215   52.515   108.462   1   22.83       161   CG2   THR   23   42.388   53.408   106.382   1   23.53       162   C   THR   23   45.84   53.643   108.014   1   25.4       163   O   THR   23   45.764   54.678   108.677   1   26.47       164   N   TYR   24   46.763   52.721   108.25   1   25.3       165   CA   TYR   24   47.74   52.934   109.308   1   28.67       166   CB   TYR   24   48.488   51.643   109.649   1   29.42       167   CG   TYR   24   49.586   51.88   110.671   1   31.62       168   CD1   TYR   24   49.275   52.095   112.013   1   33.37       169   CE1   TYR   24   50.268   52.404   112.948   1   33.58       170   CD2   TYR   24   50.927   51.975   110.281   1   32.74       171   CE2   TYR   24   51.931   52.286   111.206   1   33.21       172   CZ   TYR   24   51.59   52.5   112.536   1   35.01       173   OH   TYR   24   52.562   52.829   113.454   1   36.55       174   C   TYR   24   48.779   53.977   108.904   1   29.73       175   O   TYR   24   49.238   53.996   107.764   1   29.54       176   N   ALA   25   49.154   54.831   109.849   1   30.5       177   CA   ALA   25   50.178   55.842   109.606   1   33.31       178   CB   ALA   25   49.536   57.146   109.119   1   32.46       179   C   ALA   25   50.934   56.078   110.913   1   35.53       180   O   ALA   25   50.366   55.919   111.993   1   34.49       181   N   PRO   26   52.231   56.434   110.83   1   38.01       182   CD   PRO   26   53.02   56.593   109.594   1   39.29       183   CA   PRO   26   53.059   56.694   112.016   1   39.8       184   CB   PRO   26   54.336   57.279   111.422   1   40.12       185   CG   PRO   26   54.448   56.563   110.113   1   40.44       186   C   PRO   26   52.369   57.677   112.957   1   42.01       187   O   PRO   26   51.652   58.576   112.513   1   41.02       188   N   ALA   27   52.598   57.509   114.255   1   45.58       189   CA   ALA   27   51.988   58.376   115.262   1   48.46       190   CB   ALA   27   52.436   57.946   116.66   1   49.56       191   C   ALA   27   52.302   59.856   115.043   1   49.84       192   O   ALA   27   51.566   60.726   115.509   1   50.69       193   N   GLU   28   53.392   60.136   114.337   1   50.59       194   CA   GLU   28   53.792   61.509   114.06   1   52.06       195   CB   GLU   28   55.211   61.531   113.489   1   54.9       196   CG   GLU   28   55.375   60.676   112.24   1   59.71       197   CD   GLU   28   56.81   60.597   111.755   1   62.27       198   OE1   GLU   28   57.347   61.635   111.299   1   64.37       199   OE2   GLU   28   57.401   59.493   111.832   1   63.33       200   C   GLU   28   52.836   62.196   113.086   1   51.24       201   O   GLU   28   52.762   63.424   113.044   1   52.06       202   N   VAL   29   52.106   61.406   112.302   1   49.06       203   CA   VAL   29   51.158   61.953   111.331   1   46.23       204   CB   VAL   29   50.911   60.963   110.168   1   44.91       205   CG1   VAL   29   50.031   61.611   109.112   1   44.36       206   CG2   VAL   29   52.231   60.519   109.564   1   44.23       207   C   VAL   29   49.812   62.268   111.989   1   46.13       208   O   VAL   29   49.256   61.444   112.71   1   45.55       209   N   PRO   30   49.273   63.475   111.747   1   45.99       210   CD   PRO   30   49.877   64.564   110.958   1   46.31       211   CA   PRO   30   47.987   63.895   112.318   1   46.18       212   CB   PRO   30   47.788   65.294   111.735   1   45.8       213   CG   PRO   30   49.191   65.784   111.527   1   46.49       214   C   PRO   30   46.845   62.953   111.916   1   46.96       215   O   PRO   30   46.754   62.536   110.759   1   45.97       216   N   LYS   31   45.974   62.637   112.87   1   46.63       217   CA   LYS   31   44.844   61.753   112.609   1   48.02       218   CB   LYS   31   44.114   61.41   113.915   1   48.47       219   CG   LYS   31   44.941   60.604   114.911   1   49.59       220   CD   LYS   31   45.462   59.309   114.3   1   50.1       221   CE   LYS   31   46.34   58.554   115.287   1   50.23       222   NZ   LYS   31   47.041   57.403   114.652   1   52.26       223   C   LYS   31   43.86   62.375   111.622   1   47.6       224   O   LYS   31   42.999   61.685   111.074   1   48.62       225   N   SER   32   43.992   63.677   111.394   1   47.2       226   CA   SER   32   43.109   64.382   110.469   1   45.71       227   CB   SER   32   43.283   65.9   110.621   1   46.43       228   OG   SER   32   44.594   66.315   110.261   1   48.27       229   C   SER   32   43.376   63.977   109.022   1   44.36       230   O   SER   32   42.477   64.017   108.183   1   44.55       231   N   LYS   33   44.615   63.597   108.729   1   43.24       232   CA   LYS   33   44.973   63.183   107.38   1   42.33       233   CB   LYS   33   46.494   63.097   107.227   1   45.32       234   CG   LYS   33   47.195   64.447   107.134   1   49.02       235   CD   LYS   33   48.667   64.267   106.781   1   52.78       236   CE   LYS   33   49.383   65.604   106.637   1   55.15       237   NZ   LYS   33   50.83   65.425   106.309   1   56.11       238   C   LYS   33   44.335   61.836   107.03   1   39.84       239   O   LYS   33   44.162   61.517   105.858   1   38.33       240   N   ALA   34   43.992   61.049   108.049   1   37.92       241   CA   ALA   34   43.362   59.754   107.815   1   36.35       242   CB   ALA   34   43.311   58.938   109.1   1   36.8       243   C   ALA   34   41.955   60.004   107.288   1   34.73       244   O   ALA   34   41.474   59.295   106.404   1   34.44       245   N   LEU   35   41.299   61.024   107.828   1   33.55       246   CA   LEU   35   39.953   61.369   107.393   1   33.63       247   CB   LEU   35   39.387   62.602   108.258   1   33.49       248   CG   LEU   35   38.068   63.145   107.816   1   33.7       249   CD1   LEU   35   36.942   62.127   107.752   1   34.9       250   CD2   LEU   35   37.728   64.246   108.801   1   35.32       251   C   LEU   35   39.954   61.788   105.928   1   33.83       252   O   LEU   35   39.104   61.353   105.147   1   32.52       253   N   GLU   36   40.914   62.627   105.553   1   34.41       254   CA   GLU   36   41.01   63.102   104.175   1   34.68       255   CB   GLU   36   42.034   64.231   104.081   1   38.75       256   CG   GLU   36   41.765   65.357   105.062   1   47.25       257   CD   GLU   36   42.812   66.459   104.996   1   51.7       258   OE1   GLU   36   44.023   66.142   105.073   1   54.07       259   OE2   GLU   36   42.419   67.642   104.878   1   54.43       260   C   GLU   36   41.405   61.981   103.23   1   32.2       261   O   GLU   36   40.844   61.856   102.146   1   32.14       262   N   ALA   37   42.367   61.166   103.655   1   29.99       263   CA   ALA   37   42.849   60.063   102.839   1   28.84       264   CB   ALA   37   44.001   59.354   103.539   1   27.75       265   C   ALA   37   41.747   59.066   102.487   1   28.07       266   O   ALA   37   41.636   58.653   101.334   1   28.97       267   N   VAL   38   40.936   58.674   103.467   1   26.41       268   CA   VAL   38   39.863   57.728   103.196   1   26.44       269   CB   VAL   38   39.164   57.27   104.497   1   25.3       270   CG1   VAL   38   37.989   56.356   104.167   1   24.07       271   CG2   VAL   38   40.157   56.522   105.376   1   26.35       272   C   VAL   38   38.834   58.301   102.227   1   27.14       273   O   VAL   38   38.334   57.588   101.359   1   26       274   N   LYS   39   38.523   59.587   102.362   1   28.93       275   CA   LYS   39   37.56   60.217   101.461   1   30.2       276   CB   LYS   39   37.327   61.675   101.852   1   32.14       277   CG   LYS   39   36.432   61.861   103.054   1   34.97       278   CD   LYS   39   36.169   63.343   103.281   1   40.49       279   CE   LYS   39   35.184   63.567   104.412   1   43.92       280   NZ   LYS   39   34.842   65.012   104.574   1   46.69       281   C   LYS   39   38.06   60.156   100.025   1   28.98       282   O   LYS   39   37.306   59.804   99.124   1   30.66       283   N   LEU   40   39.331   60.492   99.826   1   29.51       284   CA   LEU   40   39.945   60.475   98.496   1   30.36       285   CB   LEU   40   41.368   61.049   98.564   1   31.84       286   CG   LEU   40   41.514   62.554   98.853   1   35.77       287   CD1   LEU   40   42.989   62.908   99.07   1   35.52       288   CD2   LEU   40   40.936   63.362   97.685   1   36.06       289   C   LEU   40   39.989   59.06   97.918   1   29.76       290   O   LEU   40   39.742   58.86   96.729   1   28.44       291   N   ALA   41   40.306   58.082   98.768   1   28.87       292   CA   ALA   41   40.378   56.685   98.338   1   26.84       293   CB   ALA   41   40.854   55.794   99.492   1   25.05       294   C   ALA   41   39.016   56.223   97.84   1   25.75       295   O   ALA   41   38.914   55.526   96.829   1   26.2       296   N   ILE   42   37.961   56.602   98.55   1   25.35       297   CA   ILE   42   36.629   56.221   98.118   1   27.2       298   CB   ILE   42   35.57   56.58   99.187   1   26.66       299   CG2   ILE   42   34.159   56.397   98.628   1   27.75       300   CG1   ILE   42   35.754   55.661   100.406   1   26.13       301   CD1   ILE   42   34.852   55.998   101.595   1   25.97       302   C   ILE   42   36.306   56.904   96.787   1   28.89       303   O   ILE   42   35.74   56.287   95.892   1   28.44       304   N   GLU   43   36.677   58.174   96.653   1   31.16       305   CA   GLU   43   36.435   58.907   95.407   1   32.94       306   CB   GLU   43   36.827   60.374   95.577   1   35.59       307   CG   GLU   43   35.907   61.14   96.502   1   42.17       308   CD   GLU   43   36.38   62.561   96.745   1   45.48       309   OE1   GLU   43   36.856   63.201   95.781   1   47.75       310   OE2   GLU   43   36.262   63.044   97.892   1   46.68       311   C   GLU   43   37.225   58.307   94.246   1   30.98       312   O   GLU   43   36.749   58.292   93.115   1   32.76       313   N   ALA   44   38.428   57.816   94.532   1   29.59       314   CA   ALA   44   39.284   57.224   93.504   1   28.25       315   CB   ALA   44   40.728   57.115   94.014   1   28.17       316   C   ALA   44   38.798   55.857   93.028   1   27.79       317   O   ALA   44   39.182   55.406   91.949   1   26.16       318   N   GLY   45   37.97   55.187   93.828   1   27.07       319   CA   GLY   45   37.474   53.88   93.421   1   26.05       320   C   GLY   45   37.757   52.729   94.375   1   26.58       321   O   GLY   45   37.528   51.57   94.027   1   26.47       322   N   PHE   46   38.269   53.031   95.565   1   24.63       323   CA   PHE   46   38.539   51.989   96.56   1   25.36       324   CB   PHE   46   39.503   52.495   97.638   1   23.2       325   CG   PHE   46   40.949   52.423   97.253   1   23.59       326   CD1   PHE   46   41.712   51.302   97.571   1   22.81       327   CD2   PHE   46   41.566   53.496   98.611   1   23.75       328   CE1   PHE   46   43.069   51.248   97.267   1   22.04       329   CE2   PHE   46   42.926   53.453   96.298   1   23.33       330   CZ   PHE   46   43.681   52.325   96.629   1   24.41       331   C   PHE   46   37.208   51.638   97.222   1   24.15       332   O   PHE   46   36.455   52.532   97.628   1   25.33       333   N   HIS   47   36.91   50.345   97.321   1   22.85       334   CA   HIS   47   35.667   49.882   97.952   1   22.14       335   CB   HIS   47   34.85   49.062   96.952   1   21.04       336   CG   HIS   47   34.209   49.888   95.882   1   23.38       337   CD2   HIS   47   34.66   50.28   94.668   1   23.45       338   ND1   HIS   47   32.97   50.471   96.036   1   24.56       339   CE1   HIS   47   32.685   51.189   94.964   1   24.39       340   NE2   HIS   47   33.696   51.091   94.119   1   24.67       341   C   HIS   47   35.946   49.027   99.189   1   22.75       342   O   HIS   47   35.022   48.521   99.83   1   23.25       343   N   HIS   48   37.224   48.875   99.514   1   20.59       344   CA   HIS   48   37.675   48.065   100.645   1   20.27       345   CB   HIS   48   38.399   46.83   100.081   1   20.69       346   CG   HIS   48   39.029   45.939   101.111   1   22.81       347   CD2   HIS   48   39.289   46.13   102.426   1   21.12       348   ND1   HIS   48   39.532   44.692   100.798   1   22.45       349   CE1   HIS   48   40.077   44.157   101.876   1   23.25       350   NE2   HIS   48   39.944   45.009   102.877   1   23.18       351   C   HIS   48   38.603   48.949   101.489   1   21.79       352   O   HIS   48   39.575   49.507   100.976   1   20.72       353   N   ILE   49   38.27   49.09   102.774   1   19.58       354   CA   ILE   49   39.036   49.92   103.706   1   19.68       355   CB   ILE   49   38.183   51.11   104.212   1   20.44       356   CG2   ILE   49   39.011   52   105.148   1   21       357   CG1   ILE   49   37.68   51.919   103.005   1   24.53       358   CD1   ILE   49   36.588   52.902   103.333   1   30.47       359   C   ILE   49   39.464   49.069   104.896   1   20.16       360   O   ILE   49   38.639   48.422   105.533   1   19.37       361   N   ASP   50   40.752   49.102   105.199   1   18.44       362   CA   ASP   50   41.313   48.303   106.271   1   18.73       363   CB   ASP   50   42.475   47.462   105.728   1   17.47       364   CG   ASP   50   43.06   46.52   106.784   1   19.24       365   OD1   ASP   50   42.554   45.389   106.907   1   16.55       366   OD2   ASP   50   44.008   46.922   107.486   1   17.4       367   C   ASP   50   41.81   49.131   107.448   1   19.63       368   O   ASP   50   42.648   50.021   107.28   1   19.78       369   N   SER   51   41.277   48.861   108.636   1   18.56       370   CA   SER   51   41.745   49.567   109.819   1   19.98       371   CB   SER   51   40.838   50.746   110.162   1   18.97       372   OG   SER   51   41.521   51.606   111.062   1   23.18       373   C   SER   51   41.846   48.609   111.008   1   18.6       374   O   SER   51   41.919   47.393   110.829   1   20.07       375   N   ALA   52   41.838   49.159   112.216   1   18.69       376   CA   ALA   52   41.971   48.344   113.414   1   17.84       377   CB   ALA   52   43.332   47.638   113.41   1   14.77       378   C   ALA   52   41.878   49.243   114.632   1   19.96       379   O   ALA   52   42.15   50.447   114.557   1   18.84       380   N   HIS   53   41.502   48.657   115.763   1   19.14       381   CA   HIS   53   41.409   49.419   116.992   1   20.34       382   CB   HIS   53   40.997   48.499   118.145   1   20.52       383   CG   HIS   53   41.041   49.165   119.486   1   23.94       384   CD2   HIS   53   41.803   48.92   120.579   1   23.25       385   ND1   HIS   53   40.255   50.255   119.8   1   23.72       386   CE1   HIS   53   40.534   50.654   121.03   1   25       387   NE2   HIS   53   41.469   49.861   121.524   1   24.2       388   C   HIS   53   42.755   50.095   117.312   1   20.43       389   O   HIS   53   42.802   51.293   117.611   1   18.98       390   N   VAL   54   43.847   49.339   117.223   1   21.34       391   CA   VAL   54   45.174   49.877   117.545   1   23.8       392   CB   VAL   54   46.292   48.809   117.566   1   26.89       393   CG1   VAL   54   46.201   48.001   118.817   1   30.04       394   CG2   VAL   54   46.239   47.948   116.315   1   25.21       395   C   VAL   54   45.704   50.985   116.665   1   24.26       396   O   VAL   54   46.69   51.62   117.028   1   23.77       397   N   TYR   55   45.088   51.213   115.51   1   22.57       398   CA   TYR   55   45.559   52.283   114.632   1   23.31       399   CB   TYR   55   45.026   52.103   113.211   1   20.13       400   CG   TYR   55   45.522   50.852   112.51   1   20.5       401   CD1   TYR   55   46.531   50.058   113.068   1   19.22       402   CE1   TYR   55   46.958   48.886   112.438   1   19.39       403   CD2   TYR   55   44.957   50.447   111.296   1   19.69       404   CE2   TYR   55   45.369   49.288   110.659   1   18.6       405   CZ   TYR   55   46.368   48.508   111.238   1   20.53       406   OH   TYR   55   46.742   47.334   110.629   1   20.19       407   C   TYR   55   45.096   53.624   115.185   1   24.66       408   O   TYR   55   45.559   54.683   114.756   1   25.17       409   N   ASN   56   44.171   53.562   116.137   1   25.36       410   CA   ASN   56   43.639   54.754   116.787   1   27.21       411   CB   ASN   56   44.723   55.399   117.649   1   31.46       412   CG   ASN   56   44.148   56.263   118.749   1   37.58       413   OD1   ASN   56   44.81   57.173   119.248   1   42.85       414   ND2   ASN   56   42.912   55.976   119.145   1   39.28       415   C   ASN   56   43.105   55.786   115.796   1   28.09       416   O   ASN   56   43.309   56.991   115.974   1   27.95       417   N   ASN   57   42.419   55.322   114.754   1   25.17       418   CA   ASN   57   41.873   56.237   113.756   1   24.82       419   CB   ASN   57   42.783   56.263   112.513   1   25.32       420   CG   ASN   57   42.839   54.916   111.793   1   24.64       421   OD1   ASN   57   42.006   54.035   112.03   1   26.13       422   ND2   ASN   57   43.804   54.763   110.894   1   25.4       423   C   ASN   57   40.447   55.888   113.326   1   24.2       424   O   ASN   57   39.912   56.502   112.406   1   23.01       425   N   GLU   58   39.819   54.921   113.996   1   23.33       426   CA   GLU   58   38.474   54.511   113.6   1   23.19       427   CB   GLU   58   38.028   53.276   114.4   1   25.16       428   CG   GLU   58   38.761   52.004   113.921   1   23.69       429   CD   GLU   58   38.196   50.71   114.49   1   23.95       430   OE1   GLU   58   38.121   50.579   115.731   1   22.25       431   OE2   GLU   58   37.843   49.816   113.691   1   23.43       432   C   GLU   58   37.431   55.616   113.658   1   25.46       433   O   GLU   58   36.455   55.599   112.908   1   23.44       434   N   GLU   59   37.639   56.585   114.539   1   26.95       435   CA   GLU   59   36.723   57.703   114.64   1   28.91       436   CB   GLU   59   37.121   58.573   115.829   1   33.46       437   CG   GLU   59   36.187   59.716   116.111   1   40.91       438   CD   GLU   59   36.522   60.395   117.425   1   45.45       439   OE1   GLU   59   37.593   61.038   117.513   1   47.49       440   OE2   GLU   59   35.715   60.264   118.371   1   48.25       441   C   GLU   59   36.805   58.507   113.328   1   28.63       442   O   GLU   59   35.782   58.854   112.742   1   27.41       443   N   GLN   60   38.022   58.78   112.866   1   27.82       444   CA   GLN   60   38.206   59.534   111.627   1   28.77       445   CB   GLN   60   39.669   59.966   111.455   1   30.05       446   CG   GLN   60   40.163   61.032   112.434   1   31.29       447   CD   GLN   60   40.225   60.531   113.862   1   35.92       448   OE1   GLN   60   40.558   59.37   114.109   1   34.47       449   NE2   GLN   60   39.923   61.41   114.815   1   36.75       450   C   GLN   60   37.782   58.714   110.41   1   27.57       451   O   GLN   60   37.099   59.221   109.514   1   27.1       452   N   VAL   61   38.184   57.446   110.377   1   25.88       453   CA   VAL   61   37.847   56.563   109.258   1   24.99       454   CB   VAL   61   38.497   55.155   109.432   1   24.7       455   CG1   VAL   61   37.992   54.204   108.344   1   26.3       456   CG2   VAL   61   40.009   56.276   109.353   1   22.58       457   C   VAL   61   36.334   56.43   109.14   1   24.41       458   O   VAL   61   35.781   56.514   108.044   1   24.23       459   N   GLY   62   35.662   56.25   110.276   1   24.84       460   CA   GLY   62   34.216   56.134   110.272   1   24.97       461   C   GLY   62   33.536   57.385   109.731   1   28.11       462   O   GLY   62   32.566   57.307   108.968   1   27.32       463   N   LEU   63   34.041   58.546   110.132   1   29.01       464   CA   LEU   63   33.484   59.813   109.685   1   30.07       465   CB   LEU   63   34.182   60.968   110.408   1   32.74       466   CG   LEU   63   33.581   62.367   110.247   1   36.32       467   CD1   LEU   63   32.132   62.385   110.715   1   36.66       468   CD2   LEU   63   34.412   63.346   111.059   1   38.02       469   C   LEU   63   33.657   59.956   108.165   1   29.27       470   O   LEU   63   32.764   60.444   107.477   1   28.89       471   N   ALA   64   34.801   59.521   107.643   1   27.8       472   CA   ALA   64   35.041   59.616   106.209   1   28.67       473   CB   ALA   64   36.453   59.141   105.872   1   27.84       474   C   ALA   64   34.004   58.786   105.459   1   28.56       475   O   ALA   64   33.386   59.254   104.497   1   28.44       476   N   ILE   65   33.803   57.556   105.917   1   27.46       477   CA   ILE   65   32.842   56.647   105.304   1   27.58       478   CB   ILE   65   32.883   55.244   105.993   1   26.41       479   CG2   ILE   65   31.763   54.352   105.462   1   25.23       480   CG1   ILE   65   34.243   54.593   105.743   1   26.7       481   CD1   ILE   65   34.441   53.259   106.467   1   29.76       482   C   ILE   65   31.415   57.191   105.357   1   27.92       483   O   ILE   65   30.727   57.228   104.335   1   27       484   N   ARG   66   30.969   57.613   106.537   1   28.78       485   CA   ARG   66   29.612   58.128   106.673   1   31.41       486   CB   ARG   66   29.281   58.413   108.143   1   33.31       487   CG   ARG   66   29.385   57.194   109.053   1   37.74       488   CD   ARG   66   28.628   57.401   110.361   1   40.54       489   NE   ARG   66   28.971   58.657   111.032   1   45.75       490   CZ   ARG   66   30.147   58.912   111.596   1   46.01       491   NH1   ARG   66   31.103   57.998   111.574   1   49.47       492   NH2   ARG   66   30.366   60.078   112.183   1   47.04       493   C   ARG   66   29.389   59.39   105.836   1   31.9       494   O   ARG   66   28.287   59.619   105.33   1   31.91       495   N   SER   67   30.428   60.204   105.673   1   32.21       496   CA   SER   67   30.266   61.424   104.893   1   34.84       497   CB   SER   67   31.432   62.394   105.146   1   34.39       498   OG   SER   67   32.65   61.892   104.634   1   42.99       499   C   SER   67   30.126   61.103   103.4   1   34.73       500   O   SER   67   29.411   61.795   102.676   1   34.04       501   N   LYS   68   30.784   60.04   102.942   1   34.45       502   CA   LYS   68   30.695   59.654   101.54   1   33.99       503   CB   LYS   68   31.876   58.766   101.159   1   35.63       504   CG   LYS   68   33.135   59.563   100.891   1   38.42       505   CD   LYS   68   32.923   60.445   99.667   1   41.52       506   CE   LYS   68   34.016   61.477   99.507   1   43.47       507   NZ   LYS   68   33.729   62.366   98.343   1   44.99       508   C   LYS   68   29.373   58.953   101.248   1   34.95       509   O   LYS   68   28.914   58.913   100.104   1   33.66       510   N   ILE   69   28.763   58.395   102.287   1   34.96       511   CA   ILE   69   27.473   57.742   102.141   1   34.58       512   CB   ILE   69   27.222   56.725   103.272   1   33.98       513   CG2   ILE   69   25.756   56.314   103.298   1   34.62       514   CG1   ILE   69   28.106   55.49   103.064   1   34.34       515   CD1   ILE   69   28.041   54.493   104.205   1   32.78       516   C   ILE   69   26.395   58.824   102.195   1   35.62       517   O   ILE   69   25.425   58.79   101.431   1   36.68       518   N   ALA   70   26.583   59.79   103.089   1   34.93       519   CA   ALA   70   25.637   60.887   103.272   1   36.65       520   CB   ALA   70   26.019   61.701   104.511   1   35.13       521   C   ALA   70   25.522   61.812   102.063   1   38.48       522   O   ALA   70   24.447   62.345   101.791   1   40.31       523   N   ASP   71   26.617   62.02   101.337   1   39.74       524   CA   ASP   71   26.553   62.897   100.175   1   40.68       525   CB   ASP   71   27.894   63.602   99.923   1   40.7       526   CG   ASP   71   28.996   62.649   99.521   1   42.25       527   OD1   ASP   71   28.7   61.584   98.939   1   44.06       528   OD2   ASP   71   30.175   62.977   99.771   1   43.7       529   C   ASP   71   26.119   62.143   98.923   1   41.09       530   O   ASP   71   26.115   62.696   97.823   1   41.94       531   N   GLY   72   25.762   60.875   99.097   1   40.42       532   CA   GLY   72   25.307   60.074   97.976   1   39.8       533   C   GLY   72   26.374   59.531   97.04   1   40.31       534   O   GLY   72   26.058   59.056   95.95   1   40.6       535   N   SER   73   27.636   59.588   97.444   1   38.43       536   CA   SER   73   28.703   59.079   96.593   1   37.64       537   CB   SER   73   30.058   59.606   97.063   1   37.67       538   OG   SER   73   30.126   61.008   96.915   1   39.98       539   C   SER   73   28.745   57.554   96.556   1   37.46       540   O   SER   73   29.1   56.959   95.538   1   37.38       541   N   VAL   74   28.382   56.916   97.662   1   35.43       542   CA   VAL   74   28.408   55.463   97.716   1   33.58       543   CB   VAL   74   29.848   54.969   98.062   1   33.69       544   CG1   VAL   74   30.203   55.347   99.49   1   32.42       545   CG2   VAL   74   29.965   53.479   97.845   1   35.96       546   C   VAL   74   27.408   54.952   98.748   1   32.69       547   O   VAL   74   26.995   55.693   99.638   1   32.42       548   N   LYS   75   26.998   53.695   98.61   1   31.87       549   CA   LYS   75   26.064   53.097   99.556   1   32.26       550   CB   LYS   75   25.018   52.269   98.812   1   35.55       551   CG   LYS   75   24.183   53.097   97.852   1   40.86       552   CD   LYS   75   22.981   52.332   97.316   1   44.16       553   CE   LYS   75   23.38   51.169   96.417   1   47.87       554   NZ   LYS   75   23.802   49.949   97.176   1   51.63       555   C   LYS   75   26.846   52.212   100.527   1   29.61       556   O   LYS   75   27.936   51.753   100.204   1   27.7       557   N   ARG   76   26.291   51.974   101.711   1   28.81       558   CA   ARG   76   26.972   51.145   102.701   1   28.53       559   CB   ARG   76   26.093   50.949   103.937   1   28.03       560   CG   ARG   76   26.729   50.063   105.02   1   26       561   CD   ARG   76   27.977   50.705   105.629   1   25.59       562   NE   ARG   76   28.65   49.818   106.583   1   25       563   CZ   ARG   76   29.549   48.896   106.245   1   26.42       564   NH1   ARG   76   29.886   48.744   104.972   1   24.23       565   NH2   ARG   76   30.112   48.12   107.175   1   23.44       566   C   ARG   76   27.342   49.781   102.126   1   27.32       567   O   ARG   76   28.436   49.28   102.366   1   27.95       568   N   GLU   77   26.424   49.193   101.367   1   27.83       569   CA   GLU   77   26.635   47.879   100.756   1   29.8       570   CB   GLU   77   25.378   47.433   99.998   1   33.42       571   CG   GLU   77   24.055   47.598   100.746   1   40.95       572   CD   GLU   77   23.716   49.056   101.045   1   43.36       573   OE1   GLU   77   23.841   49.9   100.134   1   45.86       574   OE2   GLU   77   23.315   49.35   102.188   1   47.53       575   C   GLU   77   27.824   47.856   99.785   1   28.52       576   O   GLU   77   28.323   48.783   99.424   1   27.64       577   N   ASP   78   28.276   49.027   99.345   1   26.62       578   CA   ASP   78   29.396   49.061   98.409   1   26.46       579   CB   ASP   78   29.087   49.988   97.235   1   28.06       580   CG   ASP   78   28.002   49.419   96.333   1   30.89       581   OD1   ASP   78   28.169   48.278   95.853   1   32.5       582   OD2   ASP   78   26.987   50.101   96.121   1   32.99       583   C   ASP   78   30.712   49.427   99.055   1   25.52       584   O   ASP   78   31.692   49.732   98.376   1   26.85       585   N   ILE   79   30.72   49.39   100.38   1   23.95       586   CA   ILE   79   31.92   49.657   101.152   1   23.73       587   CB   ILE   79   31.737   50.864   102.115   1   26.37       588   CG2   ILE   79   32.917   50.952   103.084   1   25.91       589   CG1   ILE   79   31.643   52.171   101.317   1   26.85       590   CD1   ILE   79   32.86   52.453   100.463   1   30.23       591   C   ILE   79   32.173   48.398   101.977   1   22.09       592   O   ILE   79   31.264   47.876   102.626   1   23.32       593   N   PHE   80   33.398   47.898   101.92   1   21.12       594   CA   PHE   80   33.797   46.715   102.679   1   21.03       595   CB   PHE   80   34.446   45.678   101.75   1   19.03       596   CG   PHE   80   34.744   44.357   102.414   1   17.82       597   CD1   PHE   80   35.864   44.205   103.236   1   20.27       598   CD2   PHE   80   33.904   43.259   102.211   1   18.83       599   CE1   PHE   80   36.147   42.969   103.851   1   20.09       600   CE2   PHE   80   34.172   42.016   102.816   1   17.91       601   CZ   PHE   80   35.293   41.871   103.632   1   18.48       602   C   PHE   80   34.802   47.243   103.705   1   20.8       603   O   PHE   80   35.921   47.617   103.356   1   20.58       604   N   TYR   81   34.374   47.298   104.964   1   19.98       605   CA   TYR   81   35.21   47.807   106.048   1   20.09       606   CB   TYR   81   34.448   48.848   106.882   1   19.18       607   CG   TYR   81   35.278   49.371   108.03   1   19.57       608   CD1   TYR   81   36.36   50.217   107.796   1   20.5       609   CE1   TYR   81   37.203   50.613   108.828   1   21.7       610   CD2   TYR   81   35.051   48.938   109.337   1   19.42       611   CE2   TYR   81   35.894   49.322   110.379   1   19.3       612   CZ   TYR   81   36.968   50.156   110.12   1   21.87       613   OH   TYR   81   37.84   50.522   111.125   1   21.28       614   C   TYR   81   35.692   46.695   106.978   1   18.98       615   O   TYR   81   34.902   45.891   107.471   1   17.3       616   N   THR   82   36.997   46.671   107.217   1   18.4       617   CA   THR   82   37.618   45.666   108.081   1   18.46       618   CB   THR   82   38.817   44.994   107.369   1   18.41       619   OG1   THR   82   38.356   44.311   106.198   1   19.05       620   CG2   THR   82   39.527   44.007   108.304   1   18.15       621   C   THR   82   38.177   48.291   109.358   1   18.18       622   O   THR   82   38.807   47.345   109.306   1   17.43       623   N   SER   83   37.921   45.665   110.5   1   17.08       624   CA   SER   83   38.508   46.128   111.746   1   17.19       625   CB   SER   83   37.472   46.685   112.718   1   18.59       626   OG   SER   83   38.145   47.278   113.832   1   20.29       627   C   SER   83   39.184   44.9   112.354   1   17.14       628   O   SER   83   38.992   43.782   111.879   1   17.04       629   N   LYS   84   39.968   45.109   113.403   1   16.23       630   CA   LYS   84   40.686   44.011   114.024   1   16.39       631   CB   LYS   84   42.152   44.007   113.567   1   15.34       632   CG   LYS   84   42.357   44.222   112.061   1   16.74       633   CD   LYS   84   43.826   44.043   111.632   1   16.82       634   CE   LYS   84   44.049   44.374   110.145   1   16.85       635   NZ   LYS   84   44.124   45.858   109.915   1   16.41       636   C   LYS   84   40.642   44.065   115.544   1   16.86       637   O   LYS   84   40.701   45.142   116.154   1   15.47       638   N   LEU   85   40.542   42.882   116.14   1   15.88       639   CA   LEU   85   40.52   42.713   117.591   1   15.47       640   CB   LEU   85   39.926   41.342   117.927   1   13.95       641   CG   LEU   85   39.971   40.905   119.392   1   15.62       642   CD1   LEU   85   38.884   41.636   120.165   1   13.92       643   CD2   LEU   85   39.764   39.395   119.477   1   15.4       644   C   LEU   85   41.96   42.775   118.118   1   16.61       645   O   LEU   85   42.792   41.953   117.733   1   16.73       646   N   TRP   86   42.268   43.73   118.995   1   15.09       647   CA   TRP   86   43.631   43.81   119.515   1   17.26       648   CB   TRP   86   43.965   45.195   120.094   1   17.06       649   CG   TRP   86   45.414   45.287   120.479   1   19.24       650   CD2   TRP   86   46.54   44.941   119.658   1   22.26       651   CE2   TRP   86   47.7   45.097   120.449   1   23.01       652   CE3   TRP   86   48.677   44.512   118.33   1   22.33       653   CD1   TRP   86   45.925   45.637   121.697   1   22.03       654   NE1   TRP   86   47.296   45.523   121.687   1   22.49       655   CZ2   TRP   86   48.986   44.84   119.958   1   24.56       656   CZ3   TRP   86   47.952   44.255   117.836   1   24.7       657   CH2   TRP   86   48.095   44.419   118.654   1   25.47       658   C   TRP   86   43.846   42.739   120.581   1   18.13       659   O   TRP   86   42.893   42.234   121.18   1   16.98       660   N   SER   87   45.113   42.408   120.807   1   17.74       661   CA   SER   87   45.525   41.359   121.742   1   17.82       662   CB   SER   87   47.019   41.107   121.557   1   18.06       663   OG   SER   87   47.272   40.662   120.229   1   18.53       664   C   SER   87   45.215   41.516   123.222   1   17.94       665   O   SER   87   45.416   40.575   123.988   1   17.93       666   N   ASN   88   44.744   42.691   123.637   1   17.38       667   CA   ASN   88   44.392   42.886   125.034   1   17.57       668   CB   ASN   88   44.656   44.335   125.473   1   16.77       669   CG   ASN   88   43.895   45.366   124.645   1   18.03       670   OD1   ASN   88   43.328   45.064   123.596   1   19.23       671   ND2   ASN   88   43.903   46.604   125.118   1   16.61       672   C   ASN   88   42.927   42.504   125.264   1   18.4       673   O   ASN   88   42.417   42.621   126.374   1   17.59       674   N   SER   89   42.262   42.025   124.212   1   18.17       675   CA   SER   89   40.865   41.617   124.322   1   17.2       676   CB   SER   89   39.959   42.628   123.605   1   17.98       677   OG   SER   89   39.98   43.887   124.274   1   20.02       678   C   SER   89   40.623   40.205   123.775   1   18.15       679   O   SER   89   39.572   39.924   123.207   1   18.42       680   N   HIS   90   41.597   39.311   123.961   1   17.09       681   CA   HIS   90   41.464   37.926   123.506   1   17       682   CB   HIS   90   42.844   37.249   123.41   1   16.29       683   CG   HIS   90   43.6   37.577   122.155   1   17.98       684   CD2   HIS   90   43.281   38.355   121.092   1   18.58       685   ND1   HIS   90   44.858   37.073   121.897   1   16.64       686   CE1   HIS   90   45.282   37.527   120.731   1   17.97       687   NE2   HIS   90   44.346   38.308   120.219   1   17.4       688   C   HIS   90   40.565   37.064   124.403   1   17.65       689   O   HIS   90   40.002   36.063   123.947   1   16.1       690   N   ARG   91   40.45   37.417   125.683   1   17.7       691   CA   ARG   91   39.606   36.611   126.573   1   18.28       692   CB   ARG   91   39.629   37.173   127.993   1   17.65       693   CG   ARG   91   41.002   37.069   128.64   1   17.56       694   CD   ARG   91   40.984   37.566   130.079   1   18.35       695   NE   ARG   91   42.319   37.549   130.67   1   19.75       696   CZ   ARG   91   42.586   37.926   131.914   1   22.75       697   NH1   ARG   91   41.602   38.354   132.709   1   20.62       698   NH2   ARG   91   43.832   37.882   132.364   1   20.67       699   C   ARG   91   38.2   36.625   125.983   1   16.86       700   O   ARG   91   37.715   37.669   125.57   1   17.21       701   N   PRO   92   37.528   35.462   125.937   1   19.49       702   CD   PRO   92   37.924   34.203   126.592   1   18.57       703   CA   PRO   92   36.177   35.334   125.37   1   18.62       704   CB   PRO   92   35.735   33.947   125.834   1   20.65       705   CG   PRO   92   37.025   33.202   125.912   1   24.15       706   C   PRO   92   35.153   36.4   125.748   1   19.04       707   O   PRO   92   34.416   36.896   124.889   1   16.63       708   N   GLU   93   35.098   36.743   127.032   1   17.82       709   CA   GLU   93   34.128   37.733   127.508   1   18.94       710   CB   GLU   93   33.979   37.639   129.034   1   19.61       711   CG   GLU   93   35.209   38.107   129.818   1   21.01       712   CD   GLU   93   36.133   36.963   130.236   1   25.88       713   OE1   GLU   93   36.331   36.003   129.462   1   24.23       714   OE2   GLU   93   36.682   37.035   131.348   1   28.77       715   C   GLU   93   34.491   39.172   127.126   1   17.69       716   O   GLU   93   33.717   40.09   127.382   1   15.74       717   N   LEU   94   35.665   39.365   126.523   1   17.28       718   CA   LEU   94   36.098   40.698   126.112   1   17.92       719   CB   LEU   94   37.549   40.943   126.547   1   17.98       720   CG   LEU   94   37.873   40.883   128.051   1   19.7       721   CD1   LEU   94   39.362   41.156   128.265   1   20.48       722   CD2   LEU   94   37.047   41.92   128.792   1   21.4       723   C   LEU   94   35.996   40.959   124.614   1   17.5       724   O   LEU   94   36.132   42.102   124.176   1   17.02       725   N   VAL   95   35.75   39.911   123.832   1   16.76       726   CA   VAL   95   35.688   40.054   122.378   1   16.55       727   CB   VAL   95   35.65   38.663   121.664   1   17.34       728   CG1   VAL   95   35.582   38.847   120.134   1   15.37       729   CG2   VAL   95   36.901   37.849   122.05   1   16.26       730   C   VAL   95   34.524   40.911   121.881   1   16.68       731   O   VAL   95   34.737   41.832   121.085   1   15.22       732   N   ARG   96   33.303   40.63   122.326   1   14.23       733   CA   ARG   96   32.187   41.434   121.848   1   17.06       734   CB   ARG   96   30.839   40.829   122.268   1   18.39       735   CG   ARG   96   29.679   41.649   121.738   1   21.14       736   CD   ARG   96   28.351   40.922   121.808   1   22.25       737   NE   ARG   96   27.264   41.861   121.562   1   23.91       738   CZ   ARG   96   26.017   41.514   121.249   1   23.83       739   NH1   ARG   96   25.684   40.236   121.135   1   22.82       740   NH2   ARG   96   25.104   42.453   121.05   1   23.05       741   C   ARG   96   32.283   42.9   122.292   1   17.26       742   O   ARG   96   31.963   43.809   121.523   1   17.44       743   N   PRO   97   32.703   43.149   123.548   1   16.36       744   CD   PRO   97   32.777   42.22   124.692   1   16.82       745   CA   PRO   97   32.816   44.539   123.997   1   15.62       746   CB   PRO   97   33.264   44.395   125.452   1   16.84       747   CG   PRO   97   32.551   43.144   125.879   1   18.16       748   C   PRO   97   33.837   45.318   123.142   1   16.16       749   O   PRO   97   33.645   46.499   122.875   1   13.69       750   N   ALA   98   34.919   44.66   122.716   1   14.1       751   CA   ALA   98   35.927   45.329   121.88   1   16.12       752   CB   ALA   98   37.178   44.431   121.709   1   15.85       753   C   ALA   98   35.345   45.684   120.507   1   16.76       754   O   ALA   98   35.65   46.743   119.948   1   17.68       755   N   LEU   99   34.525   44.792   119.956   1   15.77       756   CA   LEU   99   33.913   45.055   118.66   1   17.8       757   CB   LEU   99   33.219   43.794   118.114   1   16.25       758   CG   LEU   99   32.394   43.934   116.815   1   18.18       759   CD1   LEU   99   33.206   44.632   115.715   1   16.77       760   CD2   LEU   99   31.969   42.54   116.352   1   19.62       761   C   LEU   99   32.908   46.208   118.812   1   18.26       762   O   LEU   99   32.893   47.139   118.003   1   16.49       763   N   GLU   100   32.088   46.157   119.861   1   17.72       764   CA   GLU   100   31.108   47.218   120.113   1   18.21       765   CB   GLU   100   30.275   46.89   121.354   1   20.01       766   CG   GLU   100   29.413   45.656   121.131   1   25.55       767   CD   GLU   100   28.605   45.256   122.347   1   29.61       768   OE1   GLU   100   29.11   45.388   123.484   1   33.34       769   OE2   GLU   100   27.475   44.778   122.157   1   32.17       770   C   GLU   100   31.778   48.58   120.279   1   18.89       771   O   GLU   100   31.232   49.599   119.86   1   19.15       772   N   ARG   101   32.959   48.596   120.888   1   18.88       773   CA   ARG   101   33.696   49.838   121.08   1   19.61       774   CB   ARG   101   34.917   49.606   121.965   1   20.04       775   CG   ARG   101   35.718   50.871   122.224   1   22.92       776   CD   ARG   101   36.952   50.596   123.061   1   22.13       777   NE   ARG   101   37.562   51.834   123.54   1   20.45       778   CZ   ARG   101   38.721   51.893   124.19   1   23.07       779   NH1   ARG   101   39.403   50.781   124.434   1   21.59       780   NH2   ARG   101   39.191   53.06   124.617   1   22.84       781   C   ARG   101   34.14   50.395   119.725   1   20.18       782   O   ARG   101   34.029   51.597   119.478   1   19.44       783   N   SER   102   34.654   49.525   118.854   1   19.39       784   CA   SER   102   35.066   49.952   117.521   1   18.23       785   CB   SER   102   35.684   48.787   116.733   1   18.96       786   OG   SER   102   37.08   48.656   116.98   1   19.01       787   C   SER   102   33.821   50.469   116.787   1   18.98       788   O   SER   102   33.85   51.536   116.182   1   18.92       789   N   LEU   103   32.729   49.713   116.848   1   19.27       790   CA   LEU   103   31.492   50.124   116.185   1   21.56       791   CB   LEU   103   30.397   49.056   116.363   1   21.46       792   CG   LEU   103   30.63   47.777   115.554   1   20.28       793   CD1   LEU   103   29.546   46.75   115.841   1   22.01       794   CD2   LEU   103   30.661   48.131   114.071   1   21.19       795   C   LEU   103   30.986   51.479   116.678   1   22.36       796   O   LEU   103   30.456   52.27   115.897   1   23.53       797   N   LYS   104   31.143   51.751   117.966   1   23.04       798   CA   LYS   104   30.694   53.023   118.52   1   24.98       799   CB   LYS   104   30.738   52.986   120.049   1   29.66       800   CG   LYS   104   30.214   54.246   120.706   1   34.22       801   CD   LYS   104   29.922   54.011   122.17   1   40.01       802   CE   LYS   104   29.267   55.238   122.803   1   43.84       803   NZ   LYS   104   28.94   55.015   124.255   1   47.11       804   C   LYS   104   31.558   54.165   117.998   1   25.4       805   O   LYS   104   31.047   55.241   117.696   1   24.95       806   N   ASN   105   32.864   53.93   117.887   1   25.13       807   CA   ASN   105   33.774   54.946   117.37   1   24.96       808   CB   ASN   105   35.235   54.511   117.539   1   25.12       809   CG   ASN   105   35.729   54.683   118.961   1   28.69       810   OD1   ASN   105   35.288   55.581   119.669   1   28.82       811   ND2   ASN   105   36.657   53.831   119.379   1   27.74       812   C   ASN   105   33.501   55.228   115.896   1   25.76       813   O   ASN   105   33.613   56.367   115.438   1   24.28       814   N   LEU   106   33.142   54.179   115.162   1   23.88       815   CA   LEU   106   32.843   54.282   113.736   1   25.15       816   CB   LEU   106   32.941   52.905   113.086   1   22.08       817   CG   LEU   106   34.331   52.29   112.934   1   22.12       818   CD1   LEU   106   34.233   50.762   112.937   1   21.11       819   CD2   LEU   106   34.958   52.797   111.64   1   21.78       820   C   LEU   106   31.453   54.829   113.452   1   25.59       821   O   LEU   106   31.217   55.437   112.407   1   25.31       822   N   GLN   107   30.539   54.608   114.39   1   26.92       823   CA   GLN   107   29.149   55.011   114.232   1   29.28       824   CB   GLN   107   29.033   56.505   113.922   1   32.87       825   CG   GLN   107   29.232   57.377   115.148   1   40.8       826   CD   GLN   107   28.179   57.107   116.208   1   46.03       827   OE1   GLN   107   26.99   57.377   116.005   1   50.08       828   NE2   GLN   107   28.606   56.559   117.346   1   48.27       829   C   GLN   107   28.531   54.183   113.111   1   28.78       830   O   GLN   107   27.671   54.658   112.375   1   26.96       831   N   LEU   108   29   52.943   112.975   1   26.63       832   CA   LEU   108   28.461   52.025   111.978   1   25.41       833   CB   LEU   108   29.575   51.426   111.112   1   26.3       834   CG   LEU   108   30.287   52.412   110.175   1   28.35       835   CD1   LEU   108   31.452   51.723   109.498   1   28.35       836   CD2   LEU   108   29.301   52.944   109.154   1   29.34       837   C   LEU   108   27.744   50.914   112.728   1   24.32       838   O   LEU   108   28.076   50.619   113.875   1   23.03       839   N   ASP   109   26.767   50.294   112.081   1   24.81       840   CA   ASP   109   26.005   49.218   112.709   1   27.01       841   CB   ASP   109   24.634   49.087   112.04   1   31.65       842   CG   ASP   109   23.81   50.363   112.14   1   36.75       843   OD1   ASP   109   23.676   50.904   113.26   1   39.05       844   OD2   ASP   109   23.292   50.817   111.1   1   41.28       845   C   ASP   109   26.731   47.867   112.67   1   25.66       846   O   ASP   109   26.429   46.969   113.454   1   24.54       847   N   TYR   110   27.691   47.719   111.763   1   23.81       848   CA   TYR   110   28.428   46.465   111.669   1   22.04       849   CB   TYR   110   27.544   45.378   111.026   1   23.87       850   CG   TYR   110   27.186   45.676   109.576   1   25.91       851   CD1   TYR   110   25.993   46.333   109.234   1   28.25       852   CE1   TYR   110   25.709   46.666   107.888   1   29.75       853   CD2   TYR   110   28.077   45.356   108.552   1   25.45       854   CE2   TYR   110   27.812   45.678   107.23   1   27.56       855   CZ   TYR   110   26.631   46.334   106.901   1   29.12       856   OH   TYR   110   26.414   46.661   105.585   1   31.81       857   C   TYR   110   29.684   46.65   110.833   1   22.34       858   O   TYR   110   29.802   47.633   110.096   1   21.73       859   N   VAL   111   30.634   45.723   110.967   1   19.67       860   CA   VAL   111   31.84   45.773   110.149   1   19.49       861   CB   VAL   111   33.166   45.587   110.963   1   20.04       862   CG1   VAL   111   33.339   46.742   111.957   1   18       863   CG2   VAL   111   33.173   44.23   111.681   1   16.54       864   C   VAL   111   31.688   44.613   109.176   1   19.37       865   O   VAL   111   31.033   43.62   109.483   1   19.55       866   N   ASP   112   32.27   44.741   107.99   1   17.64       867   CA   ASP   112   32.175   43.672   107.013   1   17.89       868   CB   ASP   112   32.5   44.229   105.629   1   16.76       869   CG   ASP   112   31.501   45.28   105.202   1   17.24       870   OD1   ASP   112   30.485   44.906   104.592   1   18.14       871   OD2   ASP   112   31.711   46.469   105.507   1   17.83       872   C   ASP   112   33.103   42.522   107.357   1   17.41       873   O   ASP   112   32.824   41.372   107.019   1   19.21       874   N   LEU   113   34.192   42.838   108.043   1   17.31       875   CA   LEU   113   35.172   41.832   108.423   1   17.56       876   CB   LEU   113   36.258   41.717   107.344   1   17.25       877   CG   LEU   113   37.397   40.707   107.527   1   17.91       878   CD1   LEU   113   36.846   39.286   107.672   1   16.18       879   CD2   LEU   113   38.336   40.788   106.317   1   13.46       880   C   LEU   113   35.826   42.178   109.746   1   17.46       881   O   LEU   113   36.238   43.321   109.97   1   17.2       882   N   TYR   114   35.924   41.182   110.623   1   16.2       883   CA   TYR   114   36.56   41.378   111.921   1   16.4       884   CB   TYR   114   35.544   41.235   113.056   1   16.09       885   CG   TYR   114   36.015   41.87   114.342   1   16.96       886   CD1   TYR   114   36.565   43.158   114.339   1   16.89       887   CE1   TYR   114   36.935   43.792   115.519   1   16.7       888   CD2   TYR   114   35.853   41.227   115.562   1   15.54       889   CE2   TYR   114   36.219   41.854   116.757   1   16.92       890   CZ   TYR   114   36.753   43.131   116.73   1   17.55       891   OH   TYR   114   37.094   43.762   117.905   1   17.16       892   C   TYR   114   37.627   40.314   112.042   1   15.59       893   O   TYR   114   37.346   39.131   111.875   1   15.09       894   N   LEU   115   38.845   40.741   112.343   1   16.26       895   CA   LEU   115   39.974   39.83   112.433   1   18.24       896   CB   LEU   115   41.055   40.247   111.431   1   16.82       897   CG   LEU   115   40.689   40.523   109.969   1   17.32       898   CD1   LEU   115   41.931   41.003   109.231   1   16.49       899   CD2   LEU   115   40.124   39.261   109.327   1   13.58       900   C   LEU   115   40.663   39.777   113.772   1   17.71       901   O   LEU   115   40.703   40.772   114.494   1   17.3       902   N   ILE   116   41.21   38.611   114.102   1   16.66       903   CA   ILE   116   42.032   38.533   115.297   1   17.19       904   CB   ILE   116   42.314   37.079   115.72   1   19.47       905   CG2   ILE   116   43.477   37.042   116.72   1   17.88       906   CG1   ILE   116   41.037   36.456   116.295   1   19.53       907   CD1   ILE   116   41.17   34.985   116.718   1   20.36       908   C   ILE   116   43.308   39.146   114.686   1   16.44       909   O   ILE   116   43.847   38.633   113.696   1   16.7       910   N   HIS   117   43.787   40.233   115.272   1   16.1       911   CA   HIS   117   44.952   40.963   114.763   1   17.06       912   CB   HIS   117   45.02   42.32   115.469   1   17.25       913   CG   HIS   117   45.752   43.379   114.7   1   18.13       914   CD2   HIS   117   46.722   43.296   113.757   1   19.98       915   ND1   HIS   117   45.517   44.726   114.886   1   19.09       916   CE1   HIS   117   46.311   45.426   114.094   1   19.36       917   NE2   HIS   117   47.053   44.583   113.399   1   19.51       918   C   HIS   117   46.319   40.275   114.863   1   19.74       919   O   HIS   117   47.11   40.305   113.913   1   16.67       920   N   PHE   118   46.584   39.658   116.011   1   18.7       921   CA   PHE   118   47.857   38.999   116.275   1   19.93       922   CB   PHE   118   48.848   40   116.869   1   18.32       923   CG   PHE   118   50.284   39.587   116.726   1   21.12       924   CD1   PHE   118   50.87   39.518   115.462   1   22.69       925   CD2   PHE   118   51.04   39.227   117.837   1   20.64       926   CE1   PHE   118   52.195   39.09   115.299   1   23.73       927   CE2   PHE   118   52.375   38.794   117.692   1   21.43       928   CZ   PHE   118   52.948   38.725   116.424   1   22.01       929   C   PHE   118   47.56   37.895   117.283   1   18.66       930   O   PHE   118   46.855   38.118   118.25   1   19.59       931   N   PRO   119   48.108   36.692   117.063   1   19.24       932   CD   PRO   119   49.001   36.354   115.938   1   18.33       933   CA   PRO   119   47.895   35.531   117.938   1   19.19       934   CB   PRO   119   48.368   34.359   117.075   1   18.53       935   CG   PRO   119   49.486   34.963   116.282   1   18       936   C   PRO   119   48.513   35.527   119.329   1   17.99       937   O   PRO   119   48.215   34.637   120.115   1   21.68       938   N   VAL   120   49.355   36.504   119.646   1   18.15       939   CA   VAL   120   49.945   36.562   120.988   1   18.91       940   CB   VAL   120   51.391   37.115   120.937   1   19.49       941   CG1   VAL   120   51.929   37.309   122.356   1   17.66       942   CG2   VAL   120   52.288   36.135   120.162   1   18.69       943   C   VAL   120   49.065   37.48   121.857   1   18.14       944   O   VAL   120   48.751   38.592   121.456   1   17.51       945   N   SER   121   48.678   37.021   123.043   1   17.59       946   CA   SER   121   47.817   37.822   123.916   1   17.32       947   CB   SER   121   46.881   36.905   124.71   1   15.31       948   OG   SER   121   46.364   35.884   123.876   1   18.77       949   C   SER   121   48.586   38.679   124.902   1   16.53       950   O   SER   121   49.671   38.289   125.339   1   18.72       951   N   VAL   122   48.046   39.85   125.246   1   16.49       952   CA   VAL   122   48.696   40.698   126.253   1   17.36       953   CB   VAL   122   49.271   42.039   125.671   1   18.28       954   CG1   VAL   122   50.271   41.728   124.564   1   20.07       955   CG2   VAL   122   48.179   42.954   125.157   1   15.48       956   C   VAL   122   47.673   40.971   127.359   1   18.29       957   O   VAL   122   46.476   40.699   127.196   1   16.66       958   N   LYS   123   48.142   41.474   128.492   1   18.31       959   CA   LYS   123   47.27   41.747   129.635   1   20.99       960   CB   LYS   123   48.106   42.344   130.785   1   24.66       961   CG   LYS   123   47.307   42.812   131.988   1   32.3       962   CD   LYS   123   48.235   43.421   133.051   1   38.57       963   CE   LYS   123   47.469   43.943   134.271   1   42.41       964   NZ   LYS   123   46.502   45.024   133.898   1   46.41       965   C   LYS   123   46.101   42.683   129.314   1   19.29       966   O   LYS   123   46.277   43.694   128.65   1   20.06       967   N   PRO   124   44.882   42.339   129.768   1   20.15       968   CD   PRO   124   44.467   41.12   130.489   1   19.25       969   CA   PRO   124   43.731   43.208   129.495   1   20.69       970   CB   PRO   124   42.565   42.476   130.17   1   21.24       971   CG   PRO   124   42.995   41.04   130.159   1   21.45       972   C   PRO   124   43.962   44.587   130.117   1   22.18       973   O   PRO   124   44.658   44.711   131.13   1   21.98       974   N   GLY   125   43.369   45.614   129.519   1   23.23       975   CA   GLY   125   43.537   46.961   130.033   1   25.26       976   C   GLY   125   43.556   47.962   128.893   1   26.59       977   O   GLY   125   43.563   47.567   127.729   1   26.11       978   N   GLU   126   43.584   49.254   129.21   1   27.64       979   CA   GLU   126   43.579   50.267   128.16   1   29.99       980   CB   GLU   126   43.293   51.658   128.746   1   31.39       981   CG   GLU   126   43.076   52.729   127.676   1   34.06       982   CD   GLU   126   41.855   52.452   126.794   1   35.58       983   OE1   GLU   126   41.789   53.014   125.681   1   37.56       984   OE2   GLU   126   40.959   51.689   127.217   1   36.34       985   C   GLU   126   44.868   50.306   127.336   1   29.78       986   O   GLU   126   44.819   50.591   126.141   1   30.29       987   N   GLU   127   46.01   50.002   127.955   1   28.44       988   CA   GLU   127   47.289   50.03   127.235   1   30.75       989   CB   GLU   127   48.465   49.912   128.204   1   33.73       990   CG   GLU   127   48.672   51.126   129.078   1   42.95       991   CD   GLU   127   49.823   50.947   130.051   1   47.41       992   OE1   GLU   127   49.723   50.076   130.949   1   49.7       993   OE2   GLU   127   50.831   51.681   129.919   1   51.13       994   C   GLU   127   47.392   48.915   126.208   1   28.97       995   O   GLU   127   47.241   47.742   126.544   1   27.85       996   N   VAL   128   47.674   49.27   124.96   1   26.71       997   CA   VAL   128   47.767   48.247   123.928   1   26.17       998   CB   VAL   128   47.54   48.85   122.522   1   26.28       999   CG1   VAL   128   46.132   49.421   122.462   1   27.24       1000   CG2   VAL   128   48.563   49.931   122.207   1   26.18       1001   C   VAL   128   49.07   47.448   123.985   1   25.98       1002   O   VAL   128   49.126   46.314   123.508   1   25.13       1003   N   ILE   129   50.11   48.026   124.578   1   23.42       1004   CA   ILE   129   51.378   47.318   124.728   1   24.86       1005   CB   ILE   129   52.487   47.88   123.817   1   28       1006   CG2   ILE   129   53.739   47.041   123.974   1   27.42       1007   CG1   ILE   129   52.034   47.895   122.353   1   29.89       1008   CD1   ILE   129   51.761   46.543   121.76   1   31.44       1009   C   ILE   129   51.827   47.492   126.172   1   24.28       1010   O   ILE   129   52.717   48.289   126.464   1   24.94       1011   N   PRO   130   51.207   46.749   127.102   1   22.67       1012   CD   PRO   130   50.149   45.736   126.905   1   21.84       1013   CA   PRO   130   51.579   46.866   128.513   1   22.3       1014   CB   PRO   130   50.444   46.137   129.231   1   20.51       1015   CG   PRO   130   50.08   45.046   128.265   1   19.52       1016   C   PRO   130   52.945   46.244   128.768   1   22.31       1017   O   PRO   130   53.245   45.177   128.241   1   19.83       1018   N   LYS   131   53.766   46.928   129.562   1   22.4       1019   CA   LYS   131   55.114   46.469   129.88   1   25.57       1020   CB   LYS   131   56.155   47.367   129.196   1   28.25       1021   CG   LYS   131   56.134   47.33   127.676   1   31.78       1022   CD   LYS   131   57.074   48.379   127.09   1   37.23       1023   CE   LYS   131   56.971   48.45   125.575   1   39.52       1024   NZ   LYS   131   57.799   49.567   125.021   1   44.65       1025   C   LYS   131   55.377   46.465   131.383   1   25.7       1026   O   LYS   131   54.735   47.201   132.137   1   22.82       1027   N   ASP   132   56.317   45.631   131.819   1   26.15       1028   CA   ASP   132   56.652   45.567   133.235   1   29.24       1029   CB   ASP   132   57.032   44.142   133.66   1   28.46       1030   CG   ASP   132   58.196   43.568   132.853   1   29.04       1031   OD1   ASP   132   59.076   44.338   132.417   1   29.33       1032   OD2   ASP   132   58.222   42.335   132.671   1   28.3       1033   C   ASP   132   57.802   46.516   133.557   1   30.65       1034   O   ASP   132   58.279   47.257   132.694   1   29.64       1035   N   GLU   133   58.237   46.473   134.809   1   34.55       1036   CA   GLU   133   59.313   47.323   135.303   1   38.41       1037   CB   GLU   133   59.566   47.015   136.784   1   41.71       1038   CG   GLU   133   59.922   45.552   137.058   1   48.53       1039   CD   GLU   133   60.018   45.225   138.548   1   53.12       1040   OE1   GLU   133   60.742   45.944   139.28   1   56.07       1041   OE2   GLU   133   59.379   44.238   138.989   1   54.63       1042   C   GLU   133   60.605   47.163   134.512   1   39.06       1043   O   GLU   133   61.351   48.123   134.33   1   40.02       1044   N   ASN   134   60.856   45.952   134.026   1   38.55       1045   CA   ASN   134   62.072   45.672   133.273   1   37.71       1046   CB   ASN   134   62.454   44.204   133.445   1   37.78       1047   CG   ASN   134   62.665   43.834   134.891   1   37.39       1048   OD1   ASN   134   62.221   42.781   135.35   1   39.84       1049   ND2   ASN   134   63.346   44.703   135.625   1   39.06       1050   C   ASN   134   61.935   45.996   131.802   1   36.69       1051   O   ASN   134   62.848   45.742   131.022   1   38.22       1052   N   GLY   135   60.796   46.562   131.42   1   35.14       1053   CA   GLY   135   60.581   46.896   130.024   1   32.83       1054   C   GLY   135   60.104   45.722   129.18   1   31.48       1055   O   GLY   135   60.066   45.818   127.96   1   31.99       1056   N   LYS   136   59.742   44.612   129.816   1   29.85       1057   CA   LYS   136   59.267   43.441   129.076   1   29.54       1058   CB   LYS   136   59.692   42.158   129.789   1   32.26       1059   CG   LYS   136   61.175   42.088   130.14   1   36.49       1060   CD   LYS   136   62.056   42.186   128.905   1   38.71       1061   CE   LYS   136   63.539   42.114   129.266   1   40.88       1062   NZ   LYS   136   64.392   42.228   128.048   1   44.11       1063   C   LYS   136   57.742   43.467   128.947   1   29.07       1064   O   LYS   136   57.034   43.889   129.862   1   26.85       1065   N   ILE   137   57.228   43.004   127.816   1   27.92       1066   CA   ILE   137   55.788   43.008   127.618   1   27.14       1067   CB   ILE   137   55.447   42.61   126.171   1   29.57       1068   CG2   ILE   137   53.945   42.462   125.995   1   27.1       1069   CG1   ILE   137   55.97   43.696   125.223   1   31.39       1070   CD1   ILE   137   55.665   43.437   123.778   1   35.74       1071   C   ILE   137   55.06   42.097   128.605   1   24.95       1072   O   ILE   137   55.551   41.026   128.955   1   24.12       1073   N   LEU   138   53.902   42.551   129.079   1   22.65       1074   CA   LEU   138   53.083   41.771   130.003   1   21.66       1075   CB   LEU   138   52.241   42.693   130.894   1   21.35       1076   CG   LEU   139   52.985   43.488   131.982   1   23.73       1077   CD1   LEU   138   52.012   44.465   132.654   1   23.73       1078   CD2   LEU   138   53.584   42.532   133.014   1   20.64       1079   C   LEU   138   52.156   40.879   129.187   1   21.5       1080   O   LEU   138   51.053   41.284   128.823   1   20.11       1081   N   PHE   139   52.608   39.669   128.89   1   19.99       1082   CA   PHE   139   51.811   38.727   128.113   1   21.48       1083   CB   PHE   139   52.693   37.577   127.629   1   21.3       1084   CG   PHE   139   53.817   38.005   126.737   1   23.78       1085   CD1   PHE   139   55.137   37.933   127.173   1   22.62       1086   CD2   PHE   139   53.555   38.441   125.44   1   22.45       1087   CE1   PHE   139   56.185   38.284   126.322   1   24.11       1088   CE2   PHE   139   54.589   38.796   124.582   1   23.09       1089   CZ   PHE   139   55.909   38.717   125.019   1   23.08       1090   C   PHE   139   50.672   38.133   128.94   1   21.65       1091   O   PHE   139   50.707   38.157   130.167   1   22.63       1092   N   ASP   140   49.668   37.592   128.258   1   20.57       1093   CA   ASP   140   48.542   36.941   128.923   1   20.45       1094   CB   ASP   140   47.237   37.733   128.711   1   20.67       1095   CG   ASP   140   46.088   37.25   129.614   1   23.36       1096   OD1   ASP   140   46.366   36.708   130.692   1   23.17       1097   OD2   ASP   140   44.903   37.43   129.256   1   23.79       1098   C   ASP   140   48.457   35.576   128.24   1   20.96       1099   O   ASP   140   49.043   35.382   127.174   1   22.89       1100   N   THR   141   47.761   34.633   128.862   1   18.57       1101   CA   THR   141   47.607   33.305   128.291   1   18.74       1102   CB   THR   141   48.14   32.235   129.248   1   20.47       1103   OG1   THR   141   49.555   32.405   129.374   1   21.87       1104   CG2   THR   141   47.827   30.829   128.731   1   15.71       1105   C   THR   141   46.127   33.082   128.033   1   18.17       1106   O   THR   141   45.315   33.138   128.949   1   17.06       1107   N   VAL   142   45.781   32.842   126.775   1   18.08       1108   CA   VAL   142   44.393   32.641   126.38   1   18.65       1109   CB   VAL   142   43.789   33.949   125.8   1   19.5       1110   CG1   VAL   142   42.308   33.755   125.49   1   18.74       1111   CG2   VAL   142   43.993   35.099   126.772   1   20.06       1112   C   VAL   142   44.322   31.588   125.291   1   18.64       1113   O   VAL   142   45.118   31.614   124.355   1   16.35       1114   N   ASP   143   43.373   30.672   125.43   1   18.87       1115   CA   ASP   143   43.129   29.624   124.448   1   19.44       1116   CB   ASP   143   42.149   28.608   125.044   1   20.43       1117   CG   ASP   143   41.763   27.512   124.064   1   22.27       1118   OD1   ASP   143   42.212   27.556   122.905   1   19.67       1119   OD2   ASP   143   41.007   26.614   124.474   1   22.89       1120   C   ASP   143   42.488   30.326   123.234   1   18.39       1121   O   ASP   143   41.353   30.799   123.317   1   16.12       1122   N   LEU   144   43.211   30.41   122.119   1   18.24       1123   CA   LEU   144   42.673   31.07   120.929   1   18.62       1124   CB   LEU   144   43.73   31.161   119.817   1   21.51       1125   CG   LEU   144   44.895   32.131   120.073   1   24.41       1126   CD1   LEU   144   45.867   32.132   118.906   1   23.81       1127   CD2   LEU   144   44.332   33.524   120.285   1   25.19       1128   C   LEU   144   41.421   30.395   120.394   1   18.64       1129   O   LEU   144   40.64   31.017   119.674   1   17.42       1130   N   CYS   145   41.221   29.117   120.706   1   18.25       1131   CA   CYS   145   39.994   28.458   120.237   1   19.32       1132   CB   CYS   145   40.044   26.945   120.5   1   19.66       1133   SG   CYS   145   41.139   26.087   119.368   1   25.77       1134   C   CYS   145   38.795   29.091   120.943   1   19.56       1135   O   CYS   145   37.71   29.184   120.362   1   19.58       1136   N   ALA   146   38.991   29.541   122.185   1   18.68       1137   CA   ALA   146   37.906   30.192   122.939   1   18.93       1138   CB   ALA   146   38.276   30.292   124.428   1   19.44       1139   C   ALA   146   37.645   31.59   122.353   1   17.77       1140   O   ALA   146   36.505   32.05   122.28   1   18.91       1141   N   THR   147   38.716   32.262   121.939   1   17.75       1142   CA   THR   147   38.603   33.575   121.316   1   17.1       1143   CB   THR   147   39.995   34.145   120.941   1   19.35       1144   OG1   THR   147   40.825   34.171   122.107   1   17.02       1145   CG2   THR   147   39.873   35.567   120.38   1   18.51       1146   C   THR   147   37.796   33.402   120.023   1   17.22       1147   O   THR   147   36.89   34.184   119.743   1   15.66       1148   N   TRP   148   38.131   32.373   119.242   1   16.44       1149   CA   TRP   148   37.429   32.129   117.98   1   16.96       1150   CB   TRP   148   38.051   30.956   117.207   1   15.95       1151   CG   TRP   148   37.484   30.862   115.818   1   17.93       1152   CD2   TRP   148   37.688   31.799   114.751   1   17.54       1153   CE2   TRP   148   36.892   31.372   113.658   1   18.38       1154   CE3   TRP   148   38.46   32.961   114.614   1   17.37       1155   CD1   TRP   148   36.599   29.926   115.342   1   17.42       1156   NE1   TRP   148   36.239   30.23   114.046   1   18.41       1157   CZ2   TRP   148   36.851   32.071   112.438   1   17.82       1158   CZ3   TRP   148   38.415   33.661   113.391   1   18.03       1159   CH2   TRP   148   37.617   33.21   112.329   1   16.09       1160   C   TRP   148   35.937   31.884   118.2   1   17.16       1161   O   TRP   148   35.1   32.384   117.447   1   16.61       1162   N   GLU   149   35.597   31.114   119.229   1   17.78       1163   CA   GLU   149   34.191   30.865   119.528   1   19.7       1164   CB   GLU   149   34.064   29.939   120.748   1   22.43       1165   CG   GLU   149   34.121   28.467   120.381   1   27.26       1166   CD   GLU   149   34.365   27.553   121.579   1   33.05       1167   OE1   GLU   149   33.912   27.883   122.694   1   35.61       1168   OE2   GLU   149   34.998   26.498   121.391   1   33.21       1169   C   GLU   149   33.444   32.174   119.774   1   18.35       1170   O   GLU   149   32.312   32.35   119.333   1   17.6       1171   N   ALA   150   34.083   33.092   120.488   1   18.08       1172   CA   ALA   150   33.477   34.391   120.768   1   18.24       1173   CB   ALA   150   34.336   35.176   121.771   1   16.07       1174   C   ALA   150   33.331   35.183   119.456   1   17.9       1175   O   ALA   150   32.357   35.906   119.28   1   16.93       1176   N   MET   151   34.3   35.047   118.545   1   16.76       1177   CA   MET   151   34.241   35.728   117.244   1   16.67       1178   CB   MET   151   35.519   35.466   116.431   1   18.01       1179   CG   MET   151   36.805   36.086   117.001   1   20.11       1180   SD   MET   151   36.915   37.856   116.729   1   24.45       1181   CE   MET   151   37.436   37.875   114.95   1   23.58       1182   C   MET   151   33.041   35.209   116.448   1   17.22       1183   O   MET   151   32.336   35.986   115.8   1   18.3       1184   N   GLU   152   32.817   33.897   116.486   1   15.7       1185   CA   GLU   152   31.693   33.289   115.761   1   17.57       1186   CB   GLU   152   31.704   31.768   115.928   1   18.48       1187   CG   GLU   152   32.923   31.092   115.302   1   17.62       1188   CD   GLU   152   32.923   29.577   115.515   1   20.58       1189   OE1   GLU   152   32.559   29.154   116.627   1   18.71       1190   OE2   GLU   152   33.294   28.832   114.585   1   18.38       1191   C   GLU   152   30.369   33.859   116.259   1   18.9       1192   O   GLU   152   29.448   34.104   115.473   1   17.35       1193   N   LYS   153   30.276   34.067   117.569   1   18.75       1194   CA   LYS   153   29.068   34.641   118.157   1   19.9       1195   CB   LYS   153   29.146   34.588   119.681   1   22.18       1196   CG   LYS   153   28.977   33.186   120.229   1   25.13       1197   CD   LYS   153   29.123   33.157   121.732   1   30.14       1198   CE   LYS   153   28.915   31.753   122.274   1   33.98       1199   NZ   LYS   153   29.057   31.725   123.755   1   36.09       1200   C   LYS   153   28.837   36.084   117.696   1   20.24       1201   O   LYS   153   27.688   36.541   117.608   1   19.49       1202   N   CYS   154   29.916   36.809   117.407   1   19.47       1203   CA   CYS   154   29.765   38.183   116.92   1   20.4       1204   CB   CYS   154   31.104   38.926   116.933   1   22.16       1205   SG   CYS   154   31.681   39.373   118.591   1   22.96       1206   C   CYS   154   29.195   38.154   115.502   1   19.84       1207   O   CYS   154   28.421   39.033   115.138   1   18.69       1208   N   LYS   155   29.588   37.159   114.706   1   19.14       1209   CA   LYS   155   29.055   37.022   113.351   1   20.04       1210   CB   LYS   155   29.812   35.937   112.576   1   19.99       1211   CG   LYS   155   29.231   35.627   111.197   1   21.91       1212   CD   LYS   155   30.122   34.669   110.424   1   22.3       1213   CE   LYS   155   29.422   34.106   109.196   1   24.2       1214   NZ   LYS   155   28.968   35.161   108.261   1   24.25       1215   C   LYS   155   27.563   36.653   113.447   1   21.9       1216   O   LYS   155   26.723   37.229   112.752   1   22.03       1217   N   ASP   156   27.231   35.694   114.303   1   22.09       1218   CA   ASP   156   25.83   35.307   114.45   1   23.73       1219   CB   ASP   156   25.69   34.124   115.401   1   24.59       1220   CG   ASP   156   26.094   32.82   114.754   1   27.27       1221   OD1   ASP   156   26.001   32.729   113.513   1   27.59       1222   OD2   ASP   156   26.487   31.895   115.482   1   27.25       1223   C   ASP   156   24.959   36.457   114.941   1   23.15       1224   O   ASP   156   23.79   36.549   114.581   1   23.39       1225   N   ALA   157   25.534   37.326   115.766   1   21.56       1226   CA   ALA   157   24.809   38.474   116.293   1   22.11       1227   CB   ALA   157   25.534   39.031   117.512   1   23.07       1228   C   ALA   157   24.658   39.566   115.227   1   22.43       1229   O   ALA   157   23.962   40.559   115.442   1   23.8       1230   N   GLY   158   25.322   39.388   114.091   1   21.85       1231   CA   GLY   158   25.234   40.365   113.016   1   21.14       1232   C   GLY   158   26.175   41.553   113.135   1   22.19       1233   O   GLY   158   26.092   42.466   112.322   1   22.57       1234   N   LEU   159   27.073   41.552   114.121   1   20.77       1235   CA   LEU   159   28.002   42.675   114.307   1   20.11       1236   CB   LEU   159   28.557   42.678   115.736   1   21.83       1237   CG   LEU   159   27.519   42.778   116.859   1   25.56       1238   CD1   LEU   159   28.177   42.514   118.221   1   27.21       1239   CD2   LEU   159   26.88   44.15   116.823   1   26.46       1240   C   LEU   159   29.169   42.65   113.311   1   19.47       1241   O   LEU   159   29.758   43.688   113.006   1   18.75       1242   N   ALA   160   29.511   41.458   112.838   1   17.69       1243   CA   ALA   160   30.577   41.272   111.854   1   19.37       1244   CB   ALA   160   31.801   40.615   112.502   1   18.51       1245   C   ALA   160   29.986   40.348   110.797   1   19.78       1246   O   ALA   160   29.504   39.269   111.131   1   21.12       1247   N   LYS   161   30   40.769   109.534   1   18.95       1248   CA   LYS   161   29.451   39.946   108.454   1   19.09       1249   CB   LYS   161   29.339   40.769   107.164   1   20.12       1250   CG   LYS   161   28.32   41.893   107.236   1   24.07       1251   CD   LYS   161   26.908   41.356   107.425   1   27.39       1252   CE   LYS   161   25.872   42.478   107.298   1   33.77       1253   NZ   LYS   161   24.462   41.972   107.365   1   35.4       1254   C   LYS   161   30.316   38.716   108.219   1   17.87       1255   O   LYS   161   29.796   37.625   107.976   1   17.04       1256   N   SER   162   31.633   38.902   108.295   1   16.04       1257   CA   SER   162   32.609   37.815   108.119   1   16.14       1258   CB   SER   162   33.281   37.907   106.742   1   15.8       1259   OG   SER   162   32.334   37.755   105.688   1   16.86       1260   C   SER   162   33.69   37.943   109.197   1   17.65       1261   O   SER   162   33.892   39.019   109.765   1   17.35       1262   N   ILE   163   34.379   36.846   109.489   1   16.91       1263   CA   ILE   163   35.438   36.874   110.484   1   16.36       1264   CB   ILE   163   34.99   36.216   111.834   1   16.11       1265   CG2   ILE   163   33.944   37.095   112.523   1   15.46       1266   CG1   ILE   163   34.428   34.811   111.58   1   15.57       1267   CD1   ILE   163   34.054   34.06   112.868   1   18.24       1268   C   ILE   163   36.647   36.139   109.926   1   16.61       1269   O   ILE   163   36.504   35.203   109.148   1   15.65       1270   N   GLY   164   37.839   36.576   110.316   1   15.81       1271   CA   GLY   164   39.042   35.931   109.825   1   16.03       1272   C   GLY   164   40.187   36.153   110.784   1   17.05       1273   O   GLY   164   39.973   36.541   111.938   1   13.78       1274   N   VAL   165   41.407   35.918   110.317   1   16.41       1275   CA   VAL   165   42.562   36.093   111.183   1   16.57       1276   CB   VAL   165   43.152   34.73   111.6   1   15.92       1277   CG1   VAL   165   42.113   33.949   112.409   1   17.39       1278   CG2   VAL   165   43.571   33.923   110.346   1   16.45       1279   C   VAL   165   43.642   36.901   110.471   1   17.39       1280   O   VAL   165   43.553   37.185   109.273   1   18.21       1281   N   SER   166   44.667   37.269   111.223   1   17.77       1282   CA   SER   166   45.773   38.023   110.679   1   17.79       1283   CB   SER   166   45.571   39.517   110.937   1   17.65       1284   OG   SER   166   46.616   40.274   110.34   1   19.57       1285   C   SER   166   47.026   37.53   111.374   1   18.06       1286   O   SER   166   46.995   37.211   112.559   1   18.54       1287   N   ASN   167   48.125   37.448   110.633   1   17.64       1288   CA   ASN   167   49.387   36.999   111.202   1   19.25       1289   CB   ASN   167   49.867   38.006   112.256   1   19.41       1290   CG   ASN   167   50.185   39.348   111.641   1   20.11       1291   OD1   ASN   167   50.968   39.409   110.695   1   21.27       1292   ND2   ASN   167   49.578   40.422   112.153   1   17.29       1293   C   ASN   167   49.372   35.589   111.784   1   19.5       1294   O   ASN   167   50.066   35.296   112.76   1   20.27       1295   N   PHE   168   48.578   34.714   111.181   1   18.79       1296   CA   PHE   168   48.525   33.33   111.615   1   18.69       1297   CB   PHE   168   47.102   32.766   111.518   1   19.54       1298   CG   PHE   168   46.287   32.928   112.777   1   17.92       1299   CD1   PHE   168   46.274   34.131   113.473   1   17.75       1300   CD2   PHE   168   45.506   31.877   113.243   1   17.13       1301   CE1   PHE   168   45.486   34.287   114.624   1   17.96       1302   CE2   PHE   168   44.718   32.02   114.384   1   18.1       1303   CZ   PHE   168   44.711   33.229   115.072   1   17.59       1304   C   PHE   168   49.434   32.513   110.707   1   20.98       1305   O   PHE   168   49.583   32.82   109.519   1   18.73       1306   N   ASN   169   50.053   31.481   111.275   1   20.45       1307   CA   ASN   169   50.909   30.6   110.5   1   22.66       1308   CB   ASN   169   52.233   30.316   111.23   1   20.98       1309   CG   ASN   169   52.028   29.731   112.617   1   23.01       1310   OD1   ASN   169   50.971   29.177   112.921   1   23.96       1311   ND2   ASN   169   53.051   29.837   113.463   1   21.34       1312   C   ASN   169   50.13   29.31   110.276   1   22.19       1313   O   ASN   169   48.97   29.195   110.685   1   20.94       1314   N   HIS   170   50.773   28.355   109.613   1   22.88       1315   CA   HIS   170   50.187   27.053   109.294   1   24.29       1316   CB   HIS   170   51.263   26.184   108.618   1   28.3       1317   CG   HIS   170   50.883   24.745   108.455   1   31.8       1318   CD2   HIS   170   51.495   23.61   108.869   1   34.28       1319   ND1   HIS   170   49.749   24.344   107.784   1   35.5       1320   CE1   HIS   170   49.675   23.024   107.793   1   34.89       1321   NE2   HIS   170   50.723   22.555   108.446   1   36.77       1322   C   HIS   170   49.616   26.333   110.52   1   23.9       1323   O   HIS   170   48.469   25.882   110.511   1   21.22       1324   N   ARG   171   50.427   26.232   111.567   1   24.03       1325   CA   ARG   171   50.033   25.567   112.806   1   24.73       1326   CB   ARG   171   51.224   25.576   113.779   1   28.13       1327   CG   ARG   171   50.912   25.161   115.213   1   36.51       1328   CD   ARG   171   52.165   25.229   116.091   1   41.26       1329   NE   ARG   171   51.874   25.777   117.415   1   47.16       1330   CZ   ARG   171   51.533   27.042   117.639   1   48.77       1331   NH1   ARG   171   51.443   27.89   116.625   1   53.05       1332   NH2   ARG   171   51.276   27.462   118.871   1   50.54       1333   C   ARG   171   48.8   26.215   113.456   1   23.52       1334   O   ARG   171   47.85   25.527   113.821   1   22.84       1335   N   LEU   172   48.811   27.536   113.594   1   21.13       1336   CA   LEU   172   47.685   28.236   114.207   1   21.39       1337   CB   LEU   172   48.047   29.705   114.426   1   20.14       1338   CG   LEU   172   49.114   29.918   115.512   1   22.06       1339   CD1   LEU   172   49.559   31.366   115.531   1   21.5       1340   CD2   LEU   172   48.543   29.512   116.877   1   24.46       1341   C   LEU   172   46.405   28.117   113.368   1   21.98       1342   O   LEU   172   45.292   27.999   113.9   1   20.69       1343   N   LEU   173   46.561   28.15   112.052   1   21.14       1344   CA   LEU   173   45.413   28.014   111.176   1   23.89       1345   CB   LEU   173   45.843   28.24   109.723   1   25.01       1346   CG   LEU   173   45.296   29.426   108.917   1   29.42       1347   CD1   LEU   173   44.975   30.622   109.772   1   30.46       1348   CD2   LEU   173   46.322   29.768   107.856   1   29.01       1349   C   LEU   173   44.822   26.608   111.362   1   23.96       1350   O   LEU   173   43.61   26.444   111.482   1   23.79       1351   N   GLU   174   45.689   25.601   111.405   1   24.75       1352   CA   GLU   174   45.247   24.224   111.576   1   26.43       1353   CB   GLU   174   46.449   23.282   111.549   1   29.69       1354   CG   GLU   174   46.127   21.906   111.02   1   40.76       1355   CD   GLU   174   46.01   21.876   109.506   1   44.29       1356   OE1   GLU   174   47.062   21.767   108.832   1   47.58       1357   OE2   GLU   174   44.87   21.976   108.995   1   45.18       1358   C   GLU   174   44.491   24.067   112.899   1   25.16       1359   O   GLU   174   43.476   23.374   112.966   1   23.12       1360   N   MET   175   44.993   24.717   113.946   1   24.01       1361   CA   MET   175   44.364   24.663   115.26   1   25.32       1362   CB   MET   175   45.1   25.591   116.233   1   26.63       1363   CG   MET   175   44.524   25.62   117.633   1   30.63       1364   SD   MET   175   45.217   26.949   118.657   1   34.03       1365   CE   MET   175   46.64   26.091   119.374   1   39.82       1366   C   MET   175   42.886   25.086   115.167   1   24.83       1367   O   MET   175   42   24.436   115.733   1   22.66       1368   N   ILE   176   42.627   26.176   114.45   1   21.34       1369   CA   ILE   176   41.26   26.675   114.281   1   22.39       1370   CB   ILE   176   41.236   28.101   113.643   1   21.64       1371   CG2   ILE   176   39.787   28.566   113.442   1   22.69       1372   CG1   ILE   176   41.976   29.096   114.53   1   22.22       1373   CD1   ILE   176   41.449   29.174   115.944   1   25.11       1374   C   ILE   176   40.427   25.749   113.396   1   22.36       1375   O   ILE   176   39.304   25.383   113.75   1   19.6       1376   N   LEU   177   40.979   25.376   112.245   1   22.2       1377   CA   LEU   177   40.271   24.513   111.313   1   25.16       1378   CB   LEU   177   41.096   24.301   110.038   1   25.81       1379   CG   LEU   177   41.358   25.551   109.191   1   27.74       1380   CD1   LEU   177   42.259   25.198   108.013   1   26.85       1381   CD2   LEU   177   40.03   26.125   108.704   1   28.04       1382   C   LEU   177   39.892   23.16   111.894   1   26.29       1383   O   LEU   177   38.852   22.607   111.543   1   26.05       1384   N   ASN   178   40.726   22.627   112.779   1   25.93       1385   CA   ASN   178   40.455   21.328   113.385   1   29.26       1386   CB   ASN   178   41.757   20.537   113.549   1   31.42       1387   CG   ASN   178   42.41   20.222   112.22   1   33.25       1388   OD1   ASN   178   41.756   19.752   111.298   1   37.3       1389   ND2   ASN   178   43.706   20.476   112.119   1   37.97       1390   C   ASN   178   39.751   21.441   114.732   1   29.32       1391   O   ASN   178   39.544   20.445   115.417   1   29.78       1392   N   LYS   179   39.377   22.658   115.103   1   27.59       1393   CA   LYS   179   38.697   22.881   116.368   1   27.88       1394   CB   LYS   179   38.444   24.366   116.571   1   27.48       1395   CG   LYS   179   37.618   24.689   117.79   1   28.61       1396   CD   LYS   179   37.127   26.12   117.718   1   30.71       1397   CE   LYS   179   36.13   26.396   118.795   1   32.98       1398   NZ   LYS   179   34.946   25.52   118.666   1   31.58       1399   C   LYS   179   37.365   22.139   116.409   1   27.87       1400   O   LYS   179   36.573   22.204   115.474   1   26.45       1401   N   PRO   180   37.107   21.411   117.499   1   28.33       1402   CD   PRO   180   37.971   21.14   118.66   1   28.78       1403   CA   PRO   180   35.84   20.683   117.597   1   28.01       1404   CB   PRO   180   36.029   19.827   118.851   1   29.62       1405   CG   PRO   180   36.981   20.63   119.676   1   31.19       1406   C   PRO   180   34.671   21.667   117.717   1   26.76       1407   O   PRO   180   34.764   22.676   118.424   1   24.04       1408   N   GLY   181   33.588   21.385   117.002   1   24       1409   CA   GLY   181   32.426   22.253   117.059   1   24.33       1410   C   GLY   181   32.545   23.52   116.232   1   24.58       1411   O   GLY   181   31.699   24.407   116.34   1   23.81       1412   N   LEU   182   33.584   23.6   115.401   1   23.25       1413   CA   LEU   182   33.817   24.766   114.547   1   23.59       1414   CB   LEU   182   34.961   24.488   113.565   1   24.45       1415   CG   LEU   182   35.326   25.629   112.611   1   23.77       1416   CD1   LEU   182   35.98   26.754   113.405   1   23.78       1417   CD2   LEU   182   36.281   25.128   111.524   1   25.03       1418   C   LEU   182   32.571   25.132   113.75   1   24.35       1419   O   LEU   182   31.982   24.288   113.08   1   22.97       1420   N   LYS   183   32.17   25.393   113.811   1   23.3       1421   CA   LYS   183   30.997   28.818   113.063   1   24.46       1422   CB   LYS   183   30.119   27.703   113.942   1   25.98       1423   CG   LYS   183   28.748   27.971   113.374   1   32.36       1424   CD   LYS   183   27.84   28.643   114.406   1   35.98       1425   CE   LYS   183   26.432   28.846   113.847   1   37.3       1426   NZ   LYS   183   25.525   29.477   114.843   1   36.68       1427   C   LYS   183   31.385   27.569   111.789   1   24.49       1428   O   LYS   183   30.812   27.337   110.727   1   23.6       1429   N   TYR   184   32.362   28.464   111.894   1   21.68       1430   CA   TYR   184   32.796   29.251   110.745   1   21.19       1431   CB   TYR   184   32.35   30.71   110.902   1   20.85       1432   CG   TYR   184   30.863   30.894   111.11   1   21.79       1433   CD1   TYR   184   29.956   30.495   110.137   1   21.73       1434   CE1   TYR   184   28.591   30.68   110.306   1   24.81       1435   CD2   TYR   184   30.363   31.49   112.275   1   21.6       1436   CE2   TYR   184   28.986   31.685   112.452   1   22.27       1437   CZ   TYR   184   28.112   31.276   111.461   1   24.98       1438   OH   TYR   184   26.753   31.457   111.604   1   27.58       1439   C   TYR   184   34.304   29.236   110.619   1   22.22       1440   O   TYR   184   35.011   29.551   111.581   1   20.83       1441   N   LYS   185   34.839   28.864   109.466   1   20.22       1442   CA   LYS   185   36.285   28.939   109.415   1   24.29       1443   CB   LYS   185   36.874   27.868   108.492   1   28.55       1444   CG   LYS   185   36.238   27.715   107.162   1   31.16       1445   CD   LYS   185   36.773   26.439   106.534   1   33.15       1446   CE   LYS   185   36.692   26.5   105.036   1   34.09       1447   NZ   LYS   185   37.438   25.381   104.39   1   36       1448   C   LYS   185   36.698   30.347   109.003   1   22.03       1449   O   LYS   185   35.871   31.138   108.553   1   20.79       1450   N   PRO   186   37.972   30.702   109.206   1   21.24       1451   CD   PRO   186   39.062   29.974   109.88   1   20.76       1452   CA   PRO   186   38.387   32.054   108.815   1   20.4       1453   CB   PRO   186   39.864   32.083   109.193   1   21.52       1454   CG   PRO   186   39.954   31.103   110.335   1   23.92       1455   C   PRO   186   38.189   32.27   107.314   1   18.7       1456   O   PRO   186   38.472   31.376   106.522   1   15.86       1457   N   VAL   187   37.702   33.446   106.92   1   18.54       1458   CA   VAL   187   37.517   33.706   105.497   1   18.05       1459   CB   VAL   187   36.461   34.824   105.196   1   17.24       1460   CG1   VAL   187   35.097   34.444   105.764   1   17.86       1461   CG2   VAL   187   36.924   36.161   105.764   1   14.04       1462   C   VAL   187   38.847   34.134   104.891   1   18.78       1463   O   VAL   187   39.049   34.005   103.679   1   19.13       1464   N   CYS   188   39.756   34.641   105.725   1   17.42       1465   CA   CYS   188   41.055   35.1   105.227   1   17.53       1466   CB   CYS   188   40.941   36.539   104.703   1   15.97       1467   SG   CYS   188   40.627   37.798   106.032   1   21.11       1468   C   CYS   188   42.142   35.095   106.29   1   17.11       1469   O   CYS   188   41.878   34.943   107.476   1   17.34       1470   N   ASN   189   43.373   35.273   105.832   1   16.95       1471   CA   ASN   189   44.522   35.377   106.715   1   17.15       1472   CB   ASN   189   45.385   34.108   106.681   1   14.74       1473   CG   ASN   189   46.527   34.16   107.677   1   16.7       1474   OD1   ASN   189   46.525   34.987   108.587   1   18.43       1475   ND2   ASN   189   47.516   33.28   107.508   1   17.17       1476   C   ASN   189   45.289   36.56   106.142   1   17.14       1477   O   ASN   189   45.848   36.464   105.052   1   16.91       1478   N   GLN   190   45.279   37.682   106.859   1   17.05       1479   CA   GLN   190   45.98   38.885   106.409   1   17.47       1480   CB   GLN   190   45.261   40.152   106.897   1   16.49       1481   CG   GLN   190   45.905   41.437   106.373   1   18.11       1482   CD   GLN   190   45.299   42.705   106.951   1   17.19       1483   OE1   GLN   190   46.012   43.546   107.504   1   17.23       1484   NE2   GLN   190   43.985   42.861   106.806   1   17.87       1485   C   GLN   190   47.411   38.838   106.948   1   18.81       1486   O   GLN   190   47.631   38.895   108.158   1   17.72       1487   N   VAL   191   48.377   38.709   106.038   1   18.5       1488   CA   VAL   191   49.784   38.618   106.414   1   18.2       1489   CB   VAL   191   50.301   37.16   106.312   1   19.63       1490   CG1   VAL   191   49.566   36.259   107.306   1   17.52       1491   CG2   VAL   191   50.105   36.634   104.888   1   16.96       1492   C   VAL   191   50.671   39.47   105.514   1   20.88       1493   O   VAL   191   50.231   39.973   104.483   1   19.09       1494   N   GLU   192   51.93   39.629   105.908   1   19.94       1495   CA   GLU   192   52.872   40.398   105.1   1   20.74       1496   CB   GLU   192   54.2   40.567   105.843   1   22.62       1497   CG   GLU   192   55.229   41.419   105.094   1   23.94       1498   CD   GLU   192   56.525   41.599   105.873   1   27.59       1499   OE1   GLU   192   56.49   41.569   107.129   1   25.12       1500   OE2   GLU   192   57.577   41.792   105.226   1   26.79       1501   C   GLU   192   53.118   39.609   103.814   1   19.96       1502   O   GLU   192   53.343   38.403   103.866   1   18.25       1503   N   CYS   193   53.086   40.281   102.666   1   20.13       1504   CA   CYS   193   53.326   39.593   101.406   1   21.76       1505   CB   CYS   193   52.079   38.819   100.987   1   19.37       1506   SG   CYS   193   52.408   37.619   99.683   1   23.32       1507   C   CYS   193   53.736   40.568   100.31   1   21.4       1508   O   CYS   193   53.053   41.557   100.055   1   21.27       1509   N   HIS   194   54.865   40.279   99.671   1   23.08       1510   CA   HIS   194   55.399   41.124   98.609   1   24.27       1511   CB   HIS   194   56.004   42.402   99.206   1   23.92       1512   CG   HIS   194   56.972   42.143   100.321   1   25.35       1513   CD2   HIS   194   58.256   41.72   100.303   1   23.07       1514   ND1   HIS   194   56.621   42.246   101.652   1   27.77       1515   CE1   HIS   194   57.648   41.892   102.404   1   24.38       1516   NE2   HIS   194   58.653   41.567   101.611   1   27.71       1517   C   HIS   194   56.464   40.321   97.864   1   24.71       1518   O   HIS   194   56.789   39.198   98.254   1   24.63       1519   N   PRO   195   57.021   40.882   96.773   1   26.31       1520   CD   PRO   195   56.625   42.142   96.115   1   26.37       1521   CA   PRO   195   58.048   40.183   95.989   1   25.75       1522   CB   PRO   195   58.438   41.22   94.937   1   25.95       1523   CG   PRO   195   57.132   41.94   94.692   1   28.17       1524   C   PRO   195   59.263   39.645   96.762   1   26.5       1525   O   PRO   195   59.886   38.667   96.336   1   27.97       1526   N   TYR   196   59.617   40.274   97.88   1   26.19       1527   CA   TYR   196   60.76   39.791   98.658   1   28.47       1528   CB   TYR   196   61.483   40.944   99.348   1   30.42       1529   CG   TYR   196   62.294   41.826   98.416   1   32.54       1530   CD1   TYR   196   62.64   41.401   97.131   1   33.58       1531   CE1   TYR   196   63.42   42.205   96.292   1   34.32       1532   CD2   TYR   196   62.744   43.076   98.84   1   33.82       1533   CE2   TYR   196   63.517   43.884   98.017   1   35.16       1534   CZ   TYR   196   63.851   43.441   96.743   1   35.05       1535   OH   TYR   196   64.612   44.254   95.939   1   35.28       1536   C   TYR   196   60.361   38.749   99.697   1   29.4       1537   O   TYR   196   61.217   38.175   100.374   1   29.07       1538   N   PHE   197   59.059   38.507   99.816   1   28.6       1539   CA   PHE   197   58.539   37.518   100.756   1   28.65       1540   CB   PHE   197   58.412   38.154   102.143   1   29.99       1541   CG   PHE   197   58.385   37.157   103.267   1   34.19       1542   CD1   PHE   197   59.536   36.462   103.626   1   35.26       1543   CD2   PHE   197   57.205   36.897   103.954   1   34.95       1544   CE1   PHE   197   59.513   35.519   104.651   1   36.46       1545   CE2   PHE   197   57.169   35.955   104.983   1   35.86       1546   CZ   PHE   197   58.326   35.263   105.332   1   36.97       1547   C   PHE   197   57.164   37.14   100.203   1   27.15       1548   O   PHE   197   56.142   37.528   100.765   1   25.95       1549   N   ASN   198   57.152   36.376   99.108   1   26.53       1550   CA   ASN   198   55.91   36.01   98.437   1   25.85       1551   CB   ASN   198   56.187   35.616   96.97   1   26.42       1552   CG   ASN   198   56.943   34.315   96.831   1   26.28       1553   OD1   ASN   198   56.717   33.361   97.57   1   27.54       1554   ND2   ASN   198   57.836   34.262   95.85   1   28.12       1555   C   ASN   198   54.992   34.982   99.097   1   24.9       1556   O   ASN   198   53.934   34.674   98.559   1   23.53       1557   N   GLN   199   55.393   34.443   100.244   1   24.33       1558   CA   GLN   199   54.543   33.513   100.991   1   25.12       1559   CB   GLN   199   53.378   34.302   101.612   1   23.81       1560   CG   GLN   199   53.817   35.412   102.578   1   23.35       1561   CD   GLN   199   53.912   34.925   104.018   1   23.03       1562   OE1   GLN   199   54.128   33.744   104.256   1   23.69       1563   NE2   GLN   199   53.759   35.839   104.981   1   21.88       1564   C   GLN   199   53.969   32.347   100.195   1   26.39       1565   O   GLN   199   52.883   31.851   100.51   1   25.84       1566   N   ARG   200   54.693   31.89   99.18   1   26.76       1567   CA   ARG   200   54.211   30.797   98.339   1   26.95       1568   CB   ARG   200   55.335   30.346   97.39   1   31.47       1569   CG   ARG   200   54.882   29.526   96.184   1   38.93       1570   CD   ARG   200   55.38   28.086   96.268   1   44.51       1571   NE   ARG   200   54.485   27.254   97.075   1   48.92       1572   CZ   ARG   200   54.768   26.022   97.494   1   49.45       1573   NH1   ARG   200   55.935   25.465   97.188   1   51.27       1574   NH2   ARG   200   53.879   25.346   98.21   1   47.89       1575   C   ARG   200   53.658   29.598   99.12   1   25.86       1576   O   ARG   200   52.563   29.112   98.823   1   23.36       1577   N   LYS   201   54.393   29.117   100.121   1   23.87       1578   CA   LYS   201   53.913   27.959   100.884   1   25.87       1579   CB   LYS   201   54.977   27.474   101.876   1   29.05       1580   CG   LYS   201   56.172   26.75   101.257   1   36.51       1581   CD   LYS   201   57.085   26.212   102.358   1   40.48       1582   CE   LYS   201   58.328   25.532   101.8   1   44.89       1583   NZ   LYS   201   58.001   24.347   100.958   1   47.66       1584   C   LYS   201   52.61   28.227   101.648   1   23.98       1585   O   LYS   201   51.687   27.411   101.622   1   23.69       1586   N   LEU   202   52.551   29.358   102.34   1   22.85       1587   CA   LEU   202   51.362   29.717   103.097   1   23.18       1588   CB   LEU   202   51.636   30.954   103.956   1   20.86       1589   CG   LEU   202   50.474   31.425   104.855   1   22.77       1590   CD1   LEU   202   50.004   30.272   105.741   1   21.21       1591   CD2   LEU   202   50.918   32.606   105.717   1   22.29       1592   C   LEU   202   50.186   29.975   102.15   1   21.97       1593   O   LEU   202   49.043   29.602   102.439   1   22.71       1594   N   LEU   203   50.466   30.608   101.012   1   21.34       1595   CA   LEU   203   49.415   30.893   100.035   1   20.14       1596   CB   LEU   203   49.969   31.739   98.873   1   19.23       1597   CG   LEU   203   49.06   32.017   97.659   1   19.8       1598   CD1   LEU   203   47.774   32.712   98.087   1   18.79       1599   CD2   LEU   203   49.826   32.891   96.657   1   17.97       1600   C   LEU   203   48.785   29.607   99.515   1   20.34       1601   O   LEU   203   47.556   29.501   99.451   1   21.16       1602   N   ASP   204   49.602   28.62   99.149   1   21.43       1603   CA   ASP   204   49.046   27.353   98.658   1   21.76       1604   CB   ASP   204   50.147   26.4   98.163   1   24.09       1605   CG   ASP   204   50.626   26.742   96.753   1   27.58       1606   OD1   ASP   204   49.828   27.309   95.975   1   27.53       1607   OD2   ASP   204   51.785   26.431   98.416   1   28.62       1608   C   ASP   204   48.242   26.661   99.746   1   21.55       1609   O   ASP   204   47.205   26.059   99.464   1   21.62       1610   N   PHE   205   48.718   26.733   100.987   1   21       1611   CA   PHE   205   47.979   26.105   102.074   1   21.06       1612   CB   PHE   205   48.706   26.247   103.41   1   22.19       1613   CG   PHE   205   47.909   25.714   104.577   1   24.78       1614   CD1   PHE   205   47.711   24.347   104.733   1   25.01       1615   CD2   PHE   205   47.303   26.582   105.478   1   24.02       1616   CE1   PHE   205   48.913   23.846   105.771   1   27.56       1617   CE2   PHE   205   46.505   26.091   106.517   1   26.08       1618   CZ   PHE   205   46.311   24.722   106.661   1   25.41       1619   C   PHE   205   46.6   26.764   102.185   1   19.7       1620   O   PHE   205   45.582   26.077   102.26   1   19.85       1621   N   CYS   206   46.568   28.092   102.207   1   18.87       1622   CA   CYS   206   45.295   28.801   102.301   1   21.52       1623   CB   CYS   206   45.524   30.318   102.374   1   21.11       1624   SG   CYS   208   46.169   30.88   103.968   1   23.47       1625   C   CYS   206   44.35   28.46   101.147   1   20.35       1626   O   CYS   206   43.146   28.246   101.355   1   21.75       1627   N   LYS   207   44.879   28.415   99.93   1   20.83       1628   CA   LYS   207   44.049   28.079   98.771   1   21.69       1629   CB   LYS   207   44.87   28.139   97.481   1   22.56       1630   CG   LYS   207   45.175   29.545   97.019   1   23.24       1631   CD   LYS   207   46.032   29.545   95.777   1   25.16       1632   CE   LYS   207   46.236   30.963   95.275   1   27.78       1633   NZ   LYS   207   47.12   31.017   94.087   1   31.64       1634   C   LYS   207   43.441   26.693   98.905   1   21.5       1635   O   LYS   207   42.29   26.484   98.526   1   20.72       1636   N   SER   208   44.217   25.747   99.433   1   22.01       1637   CA   SER   208   43.725   24.385   99.597   1   23.65       1638   CB   SER   208   44.854   23.454   100.062   1   23.05       1639   OG   SER   208   45.144   23.632   101.437   1   24.76       1640   C   SER   208   42.559   24.339   100.59   1   22.4       1641   O   SER   208   41.764   23.407   100.563   1   23.6       1642   N   LYS   209   42.446   25.348   101.449   1   22.91       1643   CA   LYS   209   41.357   25.391   102.442   1   24.13       1644   CB   LYS   209   41.932   25.673   103.837   1   25.7       1645   CG   LYS   209   42.998   24.683   104.294   1   28.43       1648   CD   LYS   209   42.431   23.266   104.387   1   31.36       1647   CE   LYS   209   43.501   22.265   104.799   1   33.97       1648   NZ   LYS   209   42.959   20.882   104.989   1   36.69       1649   C   LYS   209   40.321   26.465   102.104   1   23.79       1650   O   LYS   209   39.426   26.744   102.899   1   23.5       1651   N   ASP   210   40.448   27.043   100.911   1   23.78       1652   CA   ASP   210   39.579   28.119   100.432   1   23.96       1653   CB   ASP   210   38.115   27.677   100.257   1   26.36       1654   CG   ASP   210   37.301   28.697   99.448   1   29.34       1655   OD1   ASP   210   36.07   28.818   99.644   1   30.37       1656   OD2   ASP   210   37.911   29.385   98.597   1   28.41       1657   C   ASP   210   39.611   29.325   101.365   1   23.52       1658   O   ASP   210   38.579   29.943   101.643   1   23.64       1659   N   ILE   211   40.802   29.641   101.857   1   20.71       1660   CA   ILE   211   41.008   30.798   102.716   1   19.71       1661   CB   ILE   211   41.887   30.443   103.936   1   20.89       1662   CG2   ILE   211   42.266   31.718   104.699   1   18.01       1663   CG1   ILE   211   41.145   29.441   104.835   1   20.41       1664   CD1   ILE   211   41.958   28.975   106.045   1   21.68       1665   C   ILE   211   41.75   31.809   101.847   1   21.09       1666   O   ILE   211   42.75   31.465   101.217   1   19       1667   N   VAL   212   41.251   33.04   101.792   1   20.06       1668   CA   VAL   212   41.882   34.076   100.977   1   21.03       1669   CB   VAL   212   40.867   35.191   100.604   1   22.91       1670   CG1   VAL   212   41.592   36.368   99.972   1   22.76       1671   CG2   VAL   212   39.806   34.639   99.644   1   22.98       1672   C   VAL   212   43.046   34.725   101.712   1   21.05       1673   O   VAL   212   42.932   35.058   102.889   1   20.92       1674   N   LEU   213   44.171   34.9   101.025   1   20.26       1675   CA   LEU   213   45.32   35.546   101.645   1   20.09       1676   CB   LEU   213   46.633   34.929   101.13   1   20.99       1677   CG   LEU   213   47.907   35.315   101.904   1   21.62       1678   CD1   LEU   213   48.979   34.25   101.737   1   25.02       1579   CD2   LEU   213   48.407   35.657   101.421   1   24.82       1680   C   LEU   213   45.245   37.033   101.307   1   20.03       1681   O   LEU   213   45.068   37.407   100.149   1   22.02       1682   N   VAL   214   45.339   37.883   102.323   1   20.42       1683   CA   VAL   214   45.287   39.326   102.119   1   17.7       1684   CB   VAL   214   44.221   39.99   103.026   1   18.15       1685   CG1   VAL   214   44.234   41.504   102.834   1   15.93       1686   CG2   VAI.   214   42.834   39.416   102.69   1   17.11       1687   C   VAL   214   46.675   39.85   102.459   1   19.11       1688   O   VAL   214   47.179   39.646   103.57   1   17.5       1689   N   ALA   215   47.29   40.526   101.495   1   17.91       1690   CA   ALA   215   48.643   41.03   101.659   1   19.16       1691   CB   ALA   215   49.387   40.953   100.312   1   18.93       1692   C   ALA   215   48.773   42.426   102.203   1   19.94       1693   O   ALA   215   48.172   43.361   101.672   1   20.38       1694   N   TYR   216   49.556   42.572   103.269   1   19.96       1695   CA   TYR   216   49.815   43.899   103.795   1   20.9       1696   CB   TYR   216   49.424   44.028   105.277   1   19.49       1697   CG   TYR   216   50.232   43.251   106.286   1   18.59       1698   CD1   TYR   216   51.564   43.577   106.551   1   17.27       1699   CE1   TYR   216   52.262   42.984   107.618   1   20.63       1700   CD2   TYR   216   49.613   42.293   107.096   1   19.09       1701   CE2   TYR   216   50.295   41.689   108.164   1   19.94       1702   CZ   TYR   216   51.615   42.047   108.423   1   20.81       1703   OH   TYR   216   52.26   41.511   109.518   1   20.35       1704   C   TYR   216   51.3   44.174   103.546   1   20.4       1705   O   TYR   216   52.064   43.251   103.249   1   20.03       1706   N   SER   217   51.69   45.441   103.632   1   22.14       1707   CA   SER   217   53.06   45.857   103.352   1   24.39       1708   CB   SER   217   54.022   45.31   104.411   1   26.95       1709   OG   SER   217   53.768   45.944   105.663   1   30.12       1710   C   SER   217   53.454   45.373   101.958   1   24.21       1711   O   SER   217   54.61   45.034   101.702   1   25.59       1712   N   ALA   218   52.476   45.361   101.053   1   24.73       1713   CA   ALA   218   52.685   44.903   99.676   1   24.91       1714   CB   ALA   218   51.339   44.762   98.965   1   25.44       1715   C   ALA   218   53.597   45.83   98.88   1   25.61       1716   O   ALA   218   54.077   45.459   97.808   1   27.04       1717   N   LEU   219   53.822   47.031   99.405   1   26.13       1718   CA   LEU   219   54.694   48.013   98.768   1   27.81       1719   CB   LEU   219   53.979   49.364   98.652   1   25.58       1720   CG   LEU   219   52.701   49.368   97.802   1   26.17       1721   CD1   LEU   219   52.123   50.779   97.73   1   25.96       1722   CD2   LEU   219   53.013   48.848   96.406   1   25.65       1723   C   LEU   219   56.011   48.191   99.53   1   28.63       1724   O   LEU   219   56.749   49.148   99.287   1   29.16       1725   N   GLY   220   56.302   47.281   100.459   1   29.75       1726   CA   GLY   220   57.547   47.374   101.207   1   30.62       1727   C   GLY   220   57.427   47.906   102.624   1   31.28       1728   O   GLY   220   58.443   48.092   103.303   1   29.88       1729   N   SER   221   56.187   45.166   103.046   1   29.92       1730   CA   SER   221   55.846   48.667   104.383   1   32.01       1731   CB   SER   221   56.544   47.841   105.474   1   31.88       1732   OG   SER   221   57.806   48.401   105.804   1   31.34       1733   C   SER   221   56.161   50.138   104.61   1   33.56       1734   O   SER   221   56.877   50.762   103.832   1   32.52       1735   N   HIS   222   55.61   50.675   105.694   1   35.54       1736   CA   HIS   222   55.82   52.065   106.073   1   37.26       1737   CB   HIS   222   54.874   52.434   107.215   1   38.35       1738   CG   HIS   222   54.804   51.4   108.297   1   40.7       1739   CD2   HIS   222   55.685   51.064   109.27   1   40.28       1740   ND1   HIS   222   53.726   50.552   108.448   1   42.24       1741   CE1   HIS   222   53.944   49.742   109.469   1   41.92       1742   NE2   HIS   222   55.126   50.032   109.985   1   42.06       1743   C   HIS   222   57.262   52.323   106.513   1   38.38       1744   O   HIS   222   57.695   53.471   106.587   1   39.38       1745   N   ARG   223   58   51.254   106.805   1   39.44       1746   CA   ARG   223   59.388   51.368   107.243   1   40.59       1747   CB   ARG   223   60.265   51.922   106.112   1   40.47       1748   CG   ARG   223   60.263   51.072   104.84   1   40.92       1749   CD   ARG   223   61.224   51.637   103.806   1   40.98       1750   NE   ARG   223   62.611   51.502   104.244   1   40.62       1751   CZ   ARG   223   63.344   50.401   104.096   1   41.19       1752   NH1   ARG   223   62.828   49.329   103.509   1   39.72       1753   NH2   ARG   223   64.593   50.362   104.551   1   40.52       1754   C   ARG   223   59.529   52.255   108.477   1   41.44       1755   O   ARG   223   60.501   52.995   108.604   1   42.07       1756   N   GLU   224   58.563   52.178   109.388   1   42.47       1757   CA   GLU   224   58.599   52.982   110.609   1   44.5       1758   CB   GLU   224   57.18   53.191   111.146   1   45.56       1759   CG   GLU   224   57.075   54.202   112.277   1   47.34       1760   CD   GLU   224   55.732   54.142   112.987   1   49.12       1761   OE1   GLU   224   54.743   53.719   112.357   1   50.19       1762   OE2   GLU   224   55.658   54.524   114.172   1   49.07       1763   C   GLU   224   59.443   52.312   111.695   1   44.7       1764   O   GLU   224   59.279   51.127   111.978   1   42.69       1765   N   GLU   225   60.35   53.075   112.296   1   46.25       1766   CA   GLU   225   61.194   52.558   113.368   1   47.31       1767   CB   GLU   225   62.481   53.371   113.466   1   49.21       1768   CG   GLU   225   63.417   53.203   112.286   1   53.19       1769   CD   GLU   225   64.614   54.13   112.369   1   55.54       1770   OE1   GLU   225   64.472   55.323   112.018   1   56.97       1771   OE2   GLU   225   65.691   53.668   112.799   1   56.42       1772   C   GLU   225   60.416   52.68   114.673   1   46.84       1773   O   GLU   225   59.602   53.587   114.825   1   45.7       1774   N   PRO   226   60.659   51.765   115.629   1   47.12       1775   CD   PRO   226   60.318   52.004   117.037   1   48.37       1776   CA   PRO   226   61.613   50.653   115.53   1   47.43       1777   CB   PRO   226   62.056   50.435   116.981   1   40.28       1778   CG   PRO   226   61.623   51.685   117.707   1   49.15       1779   C   PRO   226   60.983   49.385   114.967   1   46.53       1780   O   PRO   226   61.581   48.315   115.036   1   47.34       1781   N   TRP   227   59.779   49.504   114.42   1   45.2       1782   CA   TRP   227   59.074   48.347   113.875   1   44.16       1783   CB   TRP   227   57.657   48.744   113.468   1   46.38       1784   CG   TRP   227   56.908   49.418   114.561   1   48.83       1785   CD2   TRP   227   56.443   48.819   115.776   1   49.79       1786   CE2   TRP   227   55.815   49.836   116.528   1   50.43       1787   CE3   TRP   227   56.495   47.52   116.302   1   50.77       1788   CD1   TRP   227   56.555   50.734   114.622   1   49.43       1789   NE1   TRP   227   55.899   50.994   115.8   1   50.06       1790   CZ2   TRP   227   55.243   49.597   117.784   1   51.29       1791   CZ3   TRP   227   55.925   47.281   117.553   1   51.95       1792   CH2   TRP   227   55.307   48.318   118.278   1   51.69       1793   C   TRP   227   59.78   47.705   112.686   1   42.72       1794   O   TRP   227   59.835   48.48   112.577   1   41.39       1795   N   VAL   228   60.311   48.532   111.794   1   40.57       1796   CA   VAL   228   61.006   48.029   110.619   1   40.35       1797   CB   VAL   228   60.378   48.583   109.323   1   39.03       1798   CG1   VAL   228   61.076   47.991   108.105   1   37.37       1799   CG2   VAL   228   58.894   48.274   109.295   1   37.04       1800   C   VAL   228   62.475   48.425   110.653   1   41.11       1801   O   VAL   228   62.807   49.579   110.918   1   41.12       1802   N   ASP   229   63.344   47.46   110.375   1   42.45       1803   CA   ASP   229   64.783   47.686   110.366   1   44.15       1804   CB   ASP   229   65.518   46.342   110.326   1   44.85       1805   CG   ASP   229   67.017   46.501   110.153   1   46.51       1806   OD1   ASP   229   67.565   47.529   110.597   1   48.44       1807   OD2   ASP   229   67.651   45.591   109.588   1   46.66       1808   C   ASP   229   65.206   48.552   109.182   1   44.5       1809   O   ASP   229   65.016   48.171   108.026   1   43.42       1810   N   PRO   230   65.783   49.735   109.463   1   45.57       1811   CD   PRO   230   65.977   50.287   110.814   1   46.21       1812   CA   PRO   230   65.245   50.69   108.447   1   45.92       1813   CB   PRO   230   66.863   51.809   109.281   1   46.03       1814   CG   PRO   230   66.057   51.775   110.535   1   47.39       1815   C   PRO   230   67.241   50.088   107.461   1   45.87       1816   O   PRO   230   67.399   50.586   106.349   1   46.92       1817   N   ASN   231   67.912   49.019   107.87   1   45.84       1818   CA   ASN   231   68.878   48.371   106.999   1   46.56       1819   CB   ASN   231   69.892   47.581   107.821   1   49.47       1820   CG   ASN   231   70.792   48.478   108.642   1   52.53       1821   OD1   ASN   231   71.419   49.395   108.106   1   53.82       1822   ND2   ASN   231   70.864   48.22   109.948   1   53.65       1823   C   ASN   231   68.229   47.448   105.98   1   45.65       1824   O   ASN   231   68.899   46.96   105.072   1   45.76       1825   N   SER   232   66.932   47.196   106.133   1   43.44       1826   CA   SER   232   66.228   45.324   105.196   1   42.14       1827   CB   SER   232   64.802   48.046   105.686   1   41.81       1828   OG   SER   232   64.045   47.238   105.793   1   40.94       1829   C   SER   232   66.188   48.976   103.815   1   40.57       1830   O   SER   232   66.055   48.196   103.691   1   39.09       1831   N   PRO   233   66.308   48.168   102.756   1   39.8       1832   CD   PRO   233   66.411   44.698   102.748   1   39.27       1833   CA   PRO   233   66.283   45.707   101.393   1   39.82       1834   CB   PRO   233   66.588   45.48   100.531   1   39.77       1835   CG   PRO   233   65.995   44.35   101.336   1   40.75       1836   C   PRO   233   64.95   47.361   101.041   1   39.89       1837   O   PRO   233   63.902   46.978   101.56   1   39.22       1838   N   VAL   234   65.003   48.36   100.167   1   38.87       1839   CA   VAL   234   63.806   49.065   99.736   1   38.86       1840   CB   VAL   234   64.137   50.51   99.331   1   40.06       1841   CG1   VAL   234   62.857   51.279   99.03   1   39.32       1842   CG2   VAL   234   64.914   51.185   100.451   1   40.19       1843   C   VAL   234   63.189   48.332   98.551   1   38.15       1844   O   VAL   234   63.743   48.328   97.448   1   37.93       1845   N   LEU   235   62.037   47.712   98.787   1   36.78       1846   CA   LEU   235   61.35   46.95   97.748   1   36.19       1847   CB   LEU   235   59.983   46.465   98.253   1   34.15       1848   CG   LEU   235   59.17   45.628   97.254   1   33.96       1849   CD1   LEU   235   59.821   44.265   97.082   1   32.16       1850   CD2   LEU   235   57.733   45.471   97.75   1   32.57       1851   C   LEU   235   61.147   47.71   96.442   1   35.2       1852   O   LEU   235   61.53   47.226   95.384   1   35.48       1853   N   LEU   236   60.55   48.895   96.521   1   35.43       1854   CA   LEU   236   60.259   49.681   95.328   1   37.25       1855   CB   LEU   236   59.364   50.868   95.691   1   37.23       1856   CG   LEU   236   57.987   50.481   96.25   1   38.48       1857   CD1   LEU   236   57.144   51.728   96.456   1   38.3       1858   CD2   LEU   236   57.295   49.523   95.288   1   37.67       1859   C   LEU   236   61.475   50.167   94.542   1   39.23       1860   O   LEU   236   61.335   50.8   93.49   1   39.02       1861   N   GLU   237   62.666   49.867   95.046   1   39.37       1862   CA   GLU   237   63.891   50.263   94.369   1   40.97       1863   CB   GLU   237   64.886   50.854   95.372   1   42.53       1864   CG   GLU   237   64.709   52.347   95.595   1   45.84       1865   CD   GLU   237   65.614   52.888   96.685   1   49.27       1866   OE1   GLU   237   66.772   52.434   96.778   1   50.58       1867   OE2   GLU   237   65.172   53.778   97.445   1   51.15       1868   C   GLU   237   64.513   49.078   93.649   1   40.7       1869   O   GLU   237   65.563   49.203   93.023   1   40.04       1870   N   ASP   238   63.857   47.926   93.728   1   39.55       1871   CA   ASP   238   64.368   46.726   93.077   1   39.87       1872   CB   ASP   238   63.452   45.541   93.379   1   38.76       1873   CG   ASP   238   63.947   44.256   92.771   1   38.72       1874   OD1   ASP   238   63.671   44.016   91.576   1   38.63       1875   OD2   ASP   238   64.622   43.481   93.483   1   39.32       1876   C   ASP   238   64.49   46.943   91.566   1   39.9       1877   O   ASP   238   63.568   47.451   90.929   1   39.8       1878   N   PRO   239   65.64   46.562   90.977   1   39.5       1879   CD   PRO   239   66.812   45.988   91.662   1   40.04       1880   CA   PRO   239   65.906   46.712   89.541   1   39.48       1881   CB   PRO   239   67.265   46.034   89.366   1   40.14       1882   CG   PRO   239   67.931   46.275   90.676   1   41.52       1883   C   PRO   239   64.853   46.086   88.636   1   38.81       1884   O   PRO   239   64.346   46.736   87.718   1   38.72       1885   N   VAL   240   64.537   44.82   88.893   1   37.76       1886   CA   VAL   240   63.554   44.094   88.098   1   36.76       1887   CB   VAL   240   63.412   42.645   88.603   1   36.48       1888   CG1   VAL   240   62.382   41.888   87.766   1   37.11       1889   CG2   VAL   240   64.759   41.949   88.527   1   35.46       1890   C   VAL   240   62.196   44.791   88.107   1   36.79       1891   O   VAL   240   61.568   44.961   87.057   1   35.48       1892   N   LEU   241   61.757   45.207   89.291   1   36.18       1893   CA   LEU   241   60.484   45.903   89.436   1   36.29       1894   CB   LEU   241   60.203   46.186   90.92   1   35.86       1895   CG   LEU   241   59.057   45.418   91.589   1   36.72       1896   CD1   LEU   241   59.078   43.946   91.193   1   36.56       1897   CD2   LEU   241   59.166   45.581   93.098   1   36.14       1898   C   LEU   241   60.488   47.211   88.652   1   36.13       1899   O   LEU   241   59.503   47.56   88.008   1   35.34       1900   N   CYS   242   61.596   47.94   88.708   1   37.21       1901   CA   CYS   242   61.683   49.206   87.988   1   38.27       1902   CB   CYS   242   62.909   49.998   88.457   1   39.33       1903   SG   CYS   242   62.797   50.558   90.196   1   44.22       1904   C   CYS   242   61.732   48.981   86.472   1   37.44       1905   O   CYS   242   61.162   49.757   85.704   1   37.1       1906   N   ALA   243   62.398   47.91   86.054   1   37.04       1907   CA   ALA   243   62.516   47.577   84.641   1   37.85       1908   CB   ALA   243   63.483   46.406   84.457   1   38.26       1909   C   ALA   243   61.153   47.227   84.051   1   38.69       1910   O   ALA   243   60.783   47.714   82.98   1   38.51       1911   N   LEU   244   60.409   46.371   84.751   1   37.63       1912   CA   LEU   244   59.084   45.964   84.295   1   36.83       1913   CB   LEU   244   58.525   44.86   85.2   1   36.85       1914   CG   LEU   244   59.199   43.488   85.065   1   37.84       1915   CD1   LEU   244   58.739   42.554   86.183   1   38.32       1916   CD2   LEU   244   58.864   42.898   83.71   1   38.61       1917   C   LEU   244   58.143   47.161   84.281   1   36.98       1918   O   LEU   244   57.247   47.241   83.444   1   36.39       1919   N   ALA   245   58.355   48.094   85.206   1   36.97       1920   CA   ALA   245   57.525   49.291   85.282   1   38.57       1921   CB   ALA   245   57.863   50.082   86.541   1   36.81       1922   C   ALA   245   57.717   50.172   84.046   1   40.02       1923   O   ALA   245   56.749   50.659   83.466   1   40.15       1924   N   LYS   246   58.97   50.379   83.655   1   42.4       1925   CA   LYS   246   59.276   51.202   82.49   1   44.83       1926   CB   LYS   246   60.788   51.396   82.368   1   47.34       1927   CG   LYS   246   61.387   52.148   83.545   1   50.83       1928   CD   LYS   246   62.881   52.372   83.384   1   53.82       1929   CE   LYS   246   63.469   53.041   84.623   1   54.6       1930   NZ   LYS   246   64.949   53.184   84.523   1   56.72       1931   C   LYS   246   58.722   50.564   81.223   1   44.53       1932   O   LYS   246   58.207   51.25   80.345   1   45.4       1933   N   LYS   247   58.826   49.244   81.145   1   45.11       1934   CA   LYS   247   58.33   48.497   80.001   1   45.55       1935   CB   LYS   247   58.658   47.015   80.183   1   46.31       1936   CG   LYS   247   58.091   46.099   79.119   1   49       1937   CD   LYS   247   58.414   44.643   79.445   1   51.05       1938   CE   LYS   247   57.768   43.677   78.461   1   52.33       1939   NZ   LYS   247   58.061   42.251   78.803   1   52.42       1940   C   LYS   247   56.821   48.686   79.835   1   45.9       1941   O   LYS   247   56.328   48.847   78.718   1   45.84       1942   N   HIS   248   56.094   48.669   80.948   1   44.47       1943   CA   HIS   248   54.642   48.835   80.931   1   43.29       1944   CB   HIS   248   54.006   48.026   82.067   1   42.91       1945   CG   HIS   248   53.815   46.578   81.749   1   42.56       1946   CD2   HIS   248   54.581   45.495   82.022   1   42.78       1947   ND1   HIS   248   52.716   46.106   81.062   1   42.35       1948   CE1   HIS   248   52.812   44.795   80.929   1   43.28       1949   NE2   HIS   248   53.935   44.399   81.502   1   43.23       1950   C   HIS   248   54.236   50.295   81.072   1   41.93       1951   O   HIS   248   53.05   50.613   81.078   1   41.29       1952   N   LYS   249   55.226   51.175   81.183   1   42.25       1953   CA   LYS   249   54.969   52.599   81.339   1   43.15       1954   CB   LYS   249   54.24   53.152   80.108   1   47.39       1955   CG   LYS   249   55.026   54.211   79.341   1   50.86       1956   CD   LYS   249   56.278   53.632   78.696   1   54.03       1957   CE   LYS   249   55.933   52.775   77.482   1   57.3       1958   NZ   LYS   249   55.299   53.585   76.396   1   58.33       1959   C   LYS   249   54.134   52.85   82.597   1   42.46       1960   O   LYS   249   53.218   53.675   82.607   1   41.54       1961   N   ARG   250   54.452   52.119   83.659   1   40.73       1962   CA   ARG   250   53.751   52.268   84.928   1   38.52       1963   CB   ARG   250   53.04   50.962   85.3   1   37.53       1964   CG   ARG   250   52.011   50.489   84.281   1   37.01       1965   CD   ARG   250   50.801   51.413   84.237   1   35.26       1966   NE   ARG   250   49.873   51.028   83.178   1   34.52       1967   CZ   ARG   250   48.673   51.571   82.998   1   34.48       1968   NH1   ARG   250   48.243   52.528   83.81   1   34.48       1969   NH2   ARG   250   47.905   51.159   82.001   1   34.14       1970   C   ARG   250   54.777   52.619   86   1   38.11       1971   O   ARG   250   55.777   53.28   85.719   1   37.87       1972   N   THR   251   54.529   52.171   87.226   1   36.4       1973   CA   THR   251   55.443   52.432   88.33   1   34.98       1974   CB   THR   251   54.832   53.42   89.338   1   35.26       1975   OG1   THR   251   53.65   52.844   89.905   1   34.94       1976   CG2   THR   251   54.465   54.739   88.654   1   34.78       1977   C   THR   251   55.742   51.122   89.057   1   34.17       1978   O   THR   251   55.002   50.144   88.921   1   34.37       1979   N   PRO   252   56.841   51.08   89.827   1   33.46       1980   CD   PRO   252   57.871   52.123   89.995   1   33.42       1981   CA   PRO   252   57.204   49.868   90.566   1   31.79       1982   CB   PRO   252   58.446   50.296   91.345   1   33.43       1983   CG   PRO   252   59.063   51.318   90.453   1   34.85       1984   C   PRO   252   56.073   49.418   91.494   1   29.43       1985   O   PRO   252   55.82   48.226   91.638   1   28.84       1986   N   ALA   253   55.405   50.379   92.124   1   28.12       1987   CA   ALA   253   54.305   50.069   93.036   1   28.73       1988   CB   ALA   253   53.743   51.347   93.65   1   26.03       1989   C   ALA   253   53.2   49.321   92.301   1   28.76       1990   O   ALA   253   52.707   48.299   92.785   1   27.92       1991   N   LEU   254   52.807   49.828   91.133   1   27.76       1992   CA   LEU   254   51.754   49.182   90.357   1   27.06       1993   CB   LEU   254   51.413   50.018   89.122   1   27.29       1994   CG   LEU   254   50.529   51.229   89.432   1   28.73       1995   CD1   LEU   254   50.36   52.099   88.181   1   28.92       1996   CD2   LEU   254   49.169   50.742   89.919   1   27.78       1997   C   LEU   254   52.131   47.764   89.958   1   25.42       1998   O   LEU   254   51.29   46.863   89.964   1   25.92       1999   N   ILE   255   53.399   47.559   89.618   1   24.15       2000   CA   ILE   255   53.857   46.227   89.244   1   24.33       2001   CB   ILE   255   55.351   46.241   88.806   1   26.07       2002   CG2   ILE   255   55.826   44.812   88.551   1   22.96       2003   CG1   ILE   255   55.542   47.128   87.557   1   26.67       2004   CD1   ILE   255   54.781   46.648   86.311   1   28.41       2005   C   ILE   255   53.703   45.284   90.454   1   24.72       2006   O   ILE   255   53.214   44.159   90.321   1   23.96       2007   N   ALA   256   54.117   45.756   91.63   1   23.68       2008   CA   ALA   256   54.049   44.953   92.852   1   25.5       2009   CB   ALA   256   54.716   45.696   94.01   1   24.12       2010   C   ALA   256   52.616   44.596   93.217   1   24.66       2011   O   ALA   256   52.348   43.494   93.689   1   24.59       2012   N   LEU   257   51.699   45.533   93.004   1   25.64       2013   CA   LEU   257   50.286   45.3   93.299   1   24.19       2014   CB   LEU   257   49.517   46.628   93.248   1   24.73       2015   CG   LEU   257   49.19   47.386   94.531   1   27.37       2016   CD1   LEU   257   50.18   47.092   95.627   1   28.38       2017   CD2   LEU   257   49.133   48.867   94.212   1   26.24       2018   C   LEU   257   49.678   44.312   92.303   1   24.13       2019   O   LEU   257   48.98   43.375   92.7   1   23.36       2020   N   ARG   258   49.948   44.516   91.013   1   21.76       2021   CA   ARG   258   49.396   43.638   89.976   1   21.32       2022   CB   ARG   258   49.793   44.131   88.579   1   20.62       2023   CG   ARG   258   49.115   43.356   87.444   1   21.27       2024   CD   ARG   258   47.62   43.63   87.383   1   19.89       2025   NE   ARG   258   46.898   42.562   85.687   1   21.41       2026   CZ   ARG   258   45.602   42.602   86.396   1   20.8       2027   NH1   ARG   258   44.881   43.664   86.733   1   21.02       2028   NH2   ARG   258   45.025   41.571   85.789   1   21.49       2029   C   ARG   258   49.856   42.2   90.156   1   20.44       2030   O   ARG   258   49.112   41.254   89.907   1   19.9       2031   N   TYR   259   51.105   42.048   90.575   1   20.01       2032   CA   TYR   259   51.675   40.736   90.823   1   22.19       2033   CB   TYR   259   53.06   40.913   91.447   1   21.54       2034   CG   TYR   259   53.676   39.663   92.022   1   22.47       2035   CD1   TYR   259   54.087   38.617   91.197   1   21.09       2036   CE1   TYR   259   54.673   37.468   91.731   1   24.15       2037   CD2   TYR   259   53.864   39.535   93.4   1   21.46       2038   CE2   TYR   259   54.448   38.392   93.944   1   23.27       2039   CZ   TYR   259   54.851   37.365   93.111   1   24.07       2040   OH   TYR   259   55.433   36.23   93.646   1   25.03       2041   C   TYR   259   50.768   39.944   91.773   1   22.3       2042   O   TYR   259   50.43   38.785   91.503   1   24.44       2043   N   GLN   260   50.364   40.572   92.873   1   21.31       2044   CA   GLN   260   49.517   39.891   93.859   1   21.5       2045   CB   GLN   260   49.363   40.755   95.123   1   20.4       2046   CG   GLN   260   50.692   41.128   95.788   1   20.56       2047   CD   GLN   260   51.391   39.942   96.438   1   23.73       2048   OE1   GLN   260   50.998   38.787   96.242   1   22.78       2049   NE2   GLN   260   52.446   40.219   97.206   1   22.67       2050   C   GLN   260   48.149   39.536   93.298   1   21.05       2051   O   GLN   260   47.642   38.43   93.526   1   20.53       2052   N   LEU   261   47.539   40.46   92.562   1   20.98       2053   CA   LEU   261   46.221   40.174   91.994   1   22.92       2054   CB   LEU   261   45.687   41.388   91.234   1   23.96       2055   CG   LEU   261   45.351   42.607   92.089   1   25.12       2056   CD1   LEU   261   44.726   43.66   91.186   1   26.75       2057   CD2   LEU   261   44.383   42.231   93.212   1   23.31       2058   C   LEU   261   46.219   38.961   91.065   1   23.12       2059   O   LEU   261   45.28   38.167   91.08   1   23.7       2060   N   GLN   262   47.267   38.802   90.264   1   22.38       2061   CA   GLN   262   47.297   37.675   89.34   1   22.84       2062   CB   GLN   262   48.264   37.959   68.187   1   22.63       2063   CG   GLN   262   47.873   39.221   87.462   1   23.55       2064   CD   GLN   262   48.477   39.386   86.07   1   24.5       2065   OE1   GLN   262   48.43   40.484   85.518   1   24.63       2066   NE2   GLN   262   49.02   38.308   85.492   1   22.08       2067   C   GLN   262   47.595   36.331   89.984   1   23.25       2068   O   GLN   262   47.433   35.284   89.35   1   23.72       2069   N   ARG   263   48.035   36.342   91.238   1   22.12       2070   CA   ARG   263   48.283   35.077   91.918   1   23.73       2071   CB   ARG   263   49.647   35.093   92.639   1   25.01       2072   CG   ARG   263   49.89   36.244   93.574   1   26.67       2073   CD   ARG   263   51.395   36.514   93.732   1   27.18       2074   NE   ARG   263   52.15   35.356   94.211   1   25.96       2075   CZ   ARG   263   52.567   35.183   95.462   1   25.36       2076   NH1   ARG   263   52.309   36.096   96.391   1   25.36       2077   NH2   ARG   263   53.249   34.089   95.783   1   24.76       2078   C   ARG   263   47.137   34.751   92.879   1   23.22       2079   O   ARG   263   47.246   33.846   93.702   1   24.73       2080   N   GLY   264   46.034   35.492   92.756   1   23.03       2081   CA   GLY   264   44.859   35.25   93.578   1   21.99       2082   C   GLY   264   44.865   35.854   94.967   1   22.05       2083   O   GLY   264   44.065   35.465   95.817   1   21.8       2084   N   VAL   265   45.761   36.807   95.196   1   20.76       2085   CA   VAL   265   45.886   37.458   96.493   1   20.75       2086   CB   VAL   265   47.395   37.712   96.809   1   20.54       2087   CG1   VAL   265   47.546   38.622   98.01   1   19.37       2088   CG2   VAL   265   48.112   36.382   97.065   1   20.48       2089   C   VAL   265   45.11   38.786   96.526   1   21.62       2090   O   VAL   265   45.072   39.508   95.534   1   22.39       2091   N   VAL   266   44.45   39.074   97.647   1   21.11       2092   CA   VAL   266   43.745   40.343   97.807   1   20.94       2093   CB   VAL   266   42.58   40.236   98.807   1   20.65       2094   CG1   VAL   266   42.082   41.633   99.176   1   19.84       2095   CG2   VAL   266   41.441   39.423   98.178   1   19.17       2096   C   VAL   266   44.851   41.241   98.359   1   21.24       2097   O   VAL   266   45.578   40.847   99.273   1   21.37       2098   N   VAL   267   44.992   42.443   97.814   1   20.32       2099   CA   VAL   267   46.092   43.295   98.236   1   19.96       2100   CB   VAL   267   47.071   43.491   97.019   1   22.82       2101   CG1   VAL   267   46.396   44.342   95.928   1   21.52       2102   CG2   VAL   267   48.377   44.121   97.47   1   21.72       2103   C   VAL   267   45.701   44.641   98.631   1   19.92       2104   O   VAL   267   44.755   45.291   98.383   1   21.24       2105   N   LEU   268   46.425   45.045   99.87   1   20.4       2106   CA   LEU   268   46.171   46.332   100.506   1   21.21       2107   CB   LEU   268   46.276   46.209   102.033   1   21.71       2108   CG   LEU   268   45.316   45.226   102.716   1   22.01       2109   CD1   LEU   268   45.492   45.28   104.237   1   21.04       2110   CD2   LEU   268   43.893   45.586   102.349   1   19.01       2111   C   LEU   268   47.24   47.306   100.006   1   21.6       2112   O   LEU   268   48.311   46.893   99.569   1   22.1       2113   N   ALA   269   46.927   48.592   100.054   1   22.37       2114   CA   ALA   269   47.859   49.636   99.654   1   23.5       2115   CB   ALA   269   47.747   49.941   98.154   1   24.65       2116   C   ALA   269   47.5   50.866   100.46   1   21.63       2117   O   ALA   269   46.365   51.336   100.432   1   20.76       2118   N   LYS   270   48.473   51.371   101.201   1   22.49       2119   CA   LYS   270   48.259   52.555   102.006   1   23.31       2120   CB   LYS   270   48.854   52.366   103.403   1   24.43       2121   CG   LYS   270   48.799   53.615   104.287   1   25.8       2122   CD   LYS   270   49.942   54.593   103.998   1   27.08       2123   CE   LYS   270   49.876   55.81   104.909   1   28.38       2124   NZ   LYS   270   51.044   56.73   104.709   1   29.11       2125   C   LYS   270   48.941   53.744   101.355   1   23.74       2126   O   LYS   270   50.076   53.637   100.899   1   23.72       2127   N   SER   271   48.237   54.867   101.316   1   24.86       2128   CA   SER   271   48.783   56.115   100.802   1   26.56       2129   CB   SER   271   48.802   56.15   99.278   1   27.2       2130   OG   SER   271   49.375   57.377   98.845   1   27.96       2131   C   SER   271   47.951   57.284   101.3   1   26.81       2132   O   SER   271   46.723   57.232   101.287   1   26.35       2133   N   TYR   272   48.62   58.336   101.758   1   27.32       2134   CA   TYR   272   47.909   59.52   102.214   1   29.84       2135   CB   TYR   272   48.415   59.954   103.588   1   30.58       2136   CG   TYR   272   47.739   59.233   104.735   1   33.04       2137   CD1   TYR   272   47.133   57.99   104.546   1   32.63       2138   CE1   TYR   272   46.53   57.315   105.605   1   34.22       2139   CD2   TYR   272   47.726   59.785   106.018   1   32.82       2140   CE2   TYR   272   47.128   59.121   107.086   1   33.95       2141   CZ   TYR   272   46.532   57.887   106.875   1   35.22       2142   OH   TYR   272   45.938   57.227   107.928   1   35.13       2143   C   TYR   272   48.111   60.642   101.203   1   31.07       2144   O   TYR   272   47.744   61.784   101.458   1   31.91       2145   N   ASN   273   48.685   60.301   100.052   1   31.74       2146   CA   ASN   273   48.943   61.273   98.99   1   32.79       2147   CB   ASN   273   50.365   61.082   98.46   1   33.57       2148   CG   ASN   273   50.713   62.062   97.356   1   36.73       2149   OD1   ASN   273   50.345   61.869   95.194   1   36.9       2150   ND2   ASN   273   51.419   63.129   97.718   1   34.92       2151   C   ASN   273   47.932   61.11   97.855   1   33.61       2152   O   ASN   273   47.805   60.029   97.288   1   32.66       2153   N   GLU   274   47.224   62.184   97.519   1   34.9       2154   CA   GLU   274   46.21   62.137   96.468   1   37.68       2155   CB   GLU   274   45.654   63.534   96.204   1   40.27       2156   CG   GLU   274   44.286   63.518   95.55   1   45.62       2157   CD   GLU   274   43.744   64.91   95.286   1   49.14       2158   OE1   GLU   274   43.877   65.781   96.175   1   51.78       2159   OE2   GLU   274   43.172   65.122   94.197   1   51.55       2160   C   GLU   274   46.689   61.532   95.15   1   37.73       2161   O   GLU   274   46.005   60.693   94.565   1   38.29       2162   N   GLN   275   47.856   61.964   94.684   1   37.55       2163   CA   GLN   275   48.418   61.466   93.433   1   38.35       2164   CB   GLN   275   49.774   62.134   93.156   1   41.05       2165   CG   GLN   275   50.53   61.549   91.96   1   47.47       2166   CD   GLN   275   52.015   61.897   91.974   1   50.47       2167   OE1   GLN   275   52.72   61.617   92.946   1   54.12       2168   NE2   GLN   275   52.495   62.5   90.893   1   51.74       2169   C   GLN   275   48.605   59.952   93.465   1   36.21       2170   O   GLN   275   48.182   59.239   92.557   1   36.07       2171   N   ARG   276   49.245   59.461   94.519   1   34.21       2172   CA   ARG   276   49.496   58.035   94.63   1   32.82       2173   CB   ARG   276   50.544   57.779   95.713   1   32.52       2174   CG   ARG   276   51.914   58.352   95.336   1   31.92       2175   CD   ARG   276   53.003   57.977   96.328   1   32.43       2176   NE   ARG   276   53.012   58.823   97.515   1   36.32       2177   CZ   ARG   276   53.549   60.039   97.565   1   39.2       2178   NH1   ARG   276   54.127   60.555   96.484   1   37.68       2179   NH2   ARG   276   53.517   60.734   98.699   1   38.21       2180   C   ARG   276   48.221   57.217   94.869   1   32.1       2181   O   ARG   276   48.105   56.093   94.379   1   31.08       2182   N   ILE   277   47.266   57.78   95.603   1   29.08       2183   CA   ILE   277   46.007   57.094   95.846   1   30.23       2184   CB   ILE   277   45.068   57.946   96.733   1   29.19       2185   CG2   ILE   277   43.645   57.385   96.686   1   28.24       2186   CG1   ILE   277   45.606   57.979   98.165   1   28.81       2187   CD1   ILE   277   44.878   58.939   99.09   1   30.07       2188   C   ILE   277   45.32   56.823   94.502   1   31.49       2189   O   ILE   277   44.871   55.705   94.229   1   29.95       2190   N   ARG   278   45.254   57.854   93.663   1   32.62       2191   CA   ARG   278   44.637   57.745   92.343   1   33.3       2192   CB   ARG   278   44.586   59.124   91.677   1   37.93       2193   CG   ARG   278   43.538   60.072   92.247   1   42.19       2194   CD   ARG   278   42.168   59.771   91.662   1   48.23       2195   NE   ARG   278   41.132   60.665   92.182   1   53.2       2196   CZ   ARG   276   39.866   60.662   91.77   1   54.66       2197   NH1   ARG   278   39.477   59.812   90.829   1   56.28       2198   NH2   ARG   278   38.989   61.501   92.305   1   56.34       2199   C   ARG   278   45.426   56.783   91.464   1   32.02       2200   O   ARG   278   44.855   56.039   90.673   1   33.73       2201   N   GLN   279   46.744   56.795   91.613   1   30.29       2202   CA   GLN   279   47.609   55.93   90.824   1   30.03       2203   CB   GLN   279   49.07   56.324   91.04   1   31.01       2204   CG   GLN   279   50.064   55.42   90.322   1   34.41       2205   CD   GLN   279   51.495   55.658   90.766   1   36.75       2206   OE1   GLN   279   51.999   56.78   90.694   1   39.52       2207   NE2   GLN   279   52.16   54.601   91.227   1   35.02       2208   C   GLN   279   47.446   54.438   91.133   1   29.57       2209   O   GLN   279   47.482   53.603   90.226   1   28.68       2210   N   ASN   280   47.276   54.099   92.41   1   27.58       2211   CA   ASN   280   47.141   52.702   92.8   1   26.53       2212   CB   ASN   280   47.177   52.569   94.331   1   27.16       2213   CG   ASN   280   48.537   52.944   94.918   1   29.46       2214   OD1   ASN   280   49.559   52.914   94.224   1   30.7       2215   ND2   ASN   280   48.556   53.287   96.201   1   28.8       2216   C   ASN   280   45.918   51.978   92.23   1   25.59       2217   O   ASN   280   45.976   50.768   92.005   1   25.49       2218   N   VAL   281   44.825   52.696   91.984   1   25.25       2219   CA   VAL   281   43.644   52.05   91.424   1   28.01       2220   CB   VAL   281   42.366   52.943   91.522   1   29.55       2221   CG1   VAL   281   42.003   53.182   92.978   1   31.31       2222   CG2   VAL   281   42.584   54.256   90.81   1   29.72       2223   C   VAL   281   43.861   51.663   89.963   1   26.71       2224   O   VAL   281   43.069   50.922   89.394   1   26.49       2225   N   GLN   282   44.939   52.152   89.361   1   27.5       2226   CA   GLN   282   45.228   51.832   87.964   1   28.61       2227   CB   GLN   282   46.247   52.818   87.395   1   30.28       2228   CG   GLN   282   45.711   54.232   87.279   1   34.49       2229   CD   GLN   282   46.75   55.214   86.773   1   39.88       2230   OE1   GLN   282   46.492   56.414   86.692   1   43.4       2231   NE2   GLN   282   47.935   54.708   86.431   1   41.09       2232   C   GLN   282   45.744   50.409   87.808   1   28.72       2233   O   GLN   282   46.041   49.97   86.698   1   29       2234   N   VAL   283   45.846   49.69   88.923   1   26.48       2235   CA   VAL   283   46.311   48.314   88.898   1   24.82       2236   CB   VAL   283   46.386   47.727   90.337   1   24.36       2237   CG1   VAL   283   44.992   47.641   90.93   1   22.65       2238   CG2   VAL   283   47.064   46.355   90.312   1   24.34       2239   C   VAL   283   45.371   47.453   88.037   1   24.17       2240   O   VAL   283   45.757   46.392   87.553   1   24.72       2241   N   PHE   284   44.145   47.92   87.835   1   23.25       2242   CA   PHE   284   43.182   47.177   87.024   1   23.62       2243   CB   PHE   284   41.757   47.473   87.5   1   23.6       2244   CG   PHE   284   41.496   47.06   88.923   1   24.18       2245   CD1   PHE   284   41.483   45.711   89.282   1   22.53       2246   CD2   PHE   284   41.273   48.024   89.909   1   22.51       2247   CE1   PHE   284   41.251   45.329   90.607   1   23.77       2248   CE2   PHE   284   41.043   47.654   91.23   1   22.18       2249   CZ   PHE   284   41.031   46.303   91.584   1   22.16       2250   C   PHE   284   43.283   47.504   85.531   1   25.17       2251   O   PHE   284   42.581   46.905   84.705   1   24.92       2252   N   GLU   285   44.163   48.439   85.184   1   27.11       2253   CA   GLU   285   44.312   48.874   83.798   1   29.76       2254   CB   GLU   285   44.623   50.367   83.757   1   32.45       2255   CG   GLU   285   43.413   51.25   83.992   1   39.53       2256   CD   GLU   285   43.792   52.711   84.138   1   45.17       2257   OE1   GLU   285   44.736   53.159   83.441   1   48.18       2258   OE2   GLU   285   43.138   53.414   84.943   1   49.47       2259   C   GLU   285   45.328   48.131   82.948   1   29.29       2260   O   GLU   285   45.457   48.412   81.758   1   29.9       2261   N   PHE   286   46.052   47.189   83.535   1   27.1       2262   CA   PHE   286   47.017   46.435   82.755   1   26.36       2263   CB   PHE   286   48.375   47.143   82.727   1   26.81       2264   CG   PHE   286   49.09   47.159   84.056   1   27.15       2265   CD1   PHE   286   48.684   48.014   85.078   1   27.28       2266   CD2   PHE   286   50.161   46.304   84.284   1   27.07       2267   CE1   PHE   286   49.338   48.015   86.317   1   27.05       2268   CE2   PHE   286   50.82   46.295   85.515   1   28.67       2269   CZ   PHE   286   50.407   47.151   86.531   1   26.96       2270   C   PHE   286   47.173   45.03   83.315   1   27.5       2271   O   PHE   286   46.636   44.713   84.379   1   27.55       2272   N   GLN   287   47.911   44.191   82.593   1   25.8       2273   CA   GLN   287   48.135   42.815   83.008   1   26.97       2274   CB   GLN   287   47.224   41.873   82.215   1   26.77       2275   CG   GLN   287   45.742   42.192   82.333   1   29.69       2276   CD   GLN   287   44.893   41.246   81.52   1   30.19       2277   OE1   GLN   287   44.981   40.029   81.682   1   32.01       2278   NE2   GLN   287   44.066   41.795   80.637   1   31.32       2279   C   GLN   287   49.588   42.423   82.783   1   27.79       2280   O   GLN   287   50.289   43.044   81.982   1   28.2       2281   N   LEU   288   50.039   41.393   83.494   1   27.7       2282   CA   LEU   288   51.411   40.9   83.363   1   27.07       2283   CB   LEU   288   52.063   40.785   84.743   1   27.06       2284   CG   LEU   288   52.234   42.062   85.571   1   28.71       2285   CD1   LEU   288   52.724   41.709   86.985   1   28.37       2286   CD2   LEU   288   53.226   42.991   84.885   1   28.27       2287   C   LEU   288   51.388   39.526   82.689   1   27.12       2288   O   LEU   288   50.478   38.735   82.928   1   24.97       2289   N   THR   289   52.387   39.244   81.853   1   26.53       2290   CA   THR   289   52.455   37.957   81.158   1   27.17       2291   CB   THR   289   53.336   38.047   79.897   1   27.63       2292   OG1   THR   289   54.682   38.364   80.278   1   26.9       2293   CG2   THR   289   52.812   39.136   78.959   1   25.8       2294   C   THR   289   53.038   36.883   82.077   1   27.96       2295   O   THR   289   53.555   37.197   83.147   1   27.68       2296   N   SER   290   52.951   35.622   81.662   1   28.4       2297   CA   SER   290   53.469   34.528   82.47   1   30.6       2298   CB   SER   290   53.229   33.179   81.778   1   30.42       2299   OG   SER   290   53.976   33.073   80.576   1   31.38       2300   C   SER   290   54.963   34.725   82.732   1   32.77       2301   O   SER   290   55.459   34.428   83.823   1   30.89       2302   N   GLU   291   55.679   35.242   81.735   1   33.92       2303   CA   GLU   291   57.117   35.472   81.871   1   34.91       2304   CB   GLU   291   57.731   35.831   80.516   1   39.23       2305   CG   GLU   291   57.841   34.657   79.563   1   45.97       2306   CD   GLU   291   58.255   35.077   78.161   1   50.17       2307   OE1   GLU   291   59.283   35.783   78.024   1   51.85       2308   OE2   GLU   291   57.553   34.692   77.197   1   52.8       2309   C   GLU   291   57.436   36.569   82.874   1   33.19       2310   O   GLU   291   58.407   36.473   83.625   1   31.81       2311   N   GLU   292   56.631   37.621   82.883   1   31.47       2312   CA   GLU   292   56.864   38.703   83.825   1   31.8       2313   CB   GLU   292   56.025   39.923   83.444   1   31.61       2314   CG   GLU   292   56.276   40.389   82.013   1   33.47       2315   CD   GLU   292   55.423   41.572   81.617   1   32.37       2316   OE1   GLU   292   54.201   41.539   81.864   1   31.84       2317   OE2   GLU   292   55.972   42.534   81.043   1   36.21       2318   C   GLU   292   56.523   38.221   85.245   1   31.56       2319   O   GLU   292   57.179   38.61   86.209   1   32.01       2320   N   MET   293   55.504   37.375   85.37   1   30.5       2321   CA   MET   293   55.13   36.846   86.675   1   29.87       2322   CB   MET   293   53.841   36.015   86.579   1   28.77       2323   CG   MET   293   52.554   36.849   86.431   1   26.63       2324   SD   MET   293   52.246   37.9   87.874   1   26.45       2325   CE   MET   293   51.638   36.608   89.044   1   25.3       2326   C   MET   293   56.273   35.981   87.206   1   32.23       2327   O   MET   293   56.614   36.05   88.389   1   31.14       2328   N   LYS   294   56.863   35.164   86.332   1   32.57       2329   CA   LYS   294   57.974   34.299   86.733   1   35.38       2330   CB   LYS   294   58.431   33.41   85.57   1   39.68       2331   CG   LYS   294   57.96   31.965   85.65   1   45.54       2332   CD   LYS   294   56.448   31.852   85.514   1   49.88       2333   CE   LYS   294   55.999   30.391   85.456   1   52.47       2334   NZ   LYS   294   56.305   29.635   86.714   1   54.82       2335   C   LYS   294   59.159   35.127   87.207   1   34.03       2336   O   LYS   294   59.832   34.768   88.172   1   33.36       2337   N   ALA   295   59.409   36.236   86.52   1   32.69       2338   CA   ALA   295   60.509   37.114   86.876   1   33.18       2339   CB   ALA   295   60.597   38.286   85.898   1   33.31       2340   C   ALA   295   60.326   37.637   88.292   1   33.5       2341   O   ALA   295   61.28   37.688   89.069   1   32.63       2342   N   ILE   296   59.099   38.027   88.628   1   31.97       2343   CA   ILE   296   58.828   38.561   89.956   1   31.01       2344   CB   ILE   296   57.451   39.252   90   1   29.14       2345   CG2   ILE   296   57.227   39.865   91.379   1   27.21       2346   CG1   ILE   296   57.406   40.352   88.931   1   28.02       2347   CD1   ILE   296   56.034   40.958   88.686   1   25.89       2348   C   ILE   296   58.932   37.483   91.033   1   31.54       2349   O   ILE   296   59.401   37.759   92.139   1   31.57       2350   N   ASP   297   58.517   36.261   90.705   1   31.84       2351   CA   ASP   297   58.613   35.149   91.652   1   33.86       2352   CB   ASP   297   58.059   33.85   91.061   1   34.57       2353   CG   ASP   297   56.55   33.81   91.032   1   36.81       2354   OD1   ASP   297   55.902   34.511   91.839   1   39.31       2355   OD2   ASP   297   56.008   33.049   90.206   1   38.82       2356   C   ASP   297   60.068   34.895   92.025   1   34.35       2357   O   ASP   297   60.363   34.396   93.111   1   34.05       2358   N   GLY   298   60.976   35.229   91.114   1   34.64       2359   CA   GLY   298   62.39   35.009   91.366   1   34.61       2360   C   GLY   298   63.035   36.004   92.312   1   35.12       2361   O   GLY   298   64.189   35.829   92.697   1   35.46       2362   N   LEU   299   62.3   37.045   92.691   1   34.08       2363   CA   LEU   299   62.829   38.062   93.591   1   34.15       2364   CB   LEU   299   62.093   39.387   93.386   1   33.2       2365   CG   LEU   299   62.196   40.02   92.004   1   33.51       2366   CD1   LEU   299   61.387   41.306   91.968   1   32.39       2367   CD2   LEU   299   63.658   40.295   91.679   1   34.46       2368   C   LEU   299   62.73   37.663   95.06   1   34.53       2369   O   LEU   299   63.289   38.33   95.931   1   34.06       2370   N   ASN   300   62.02   36.577   95.335   1   34.76       2371   CA   ASN   300   61.847   36.127   96.705   1   36.44       2372   CB   ASN   300   61.079   34.812   96.737   1   35.58       2373   CG   ASN   300   60.647   34.433   98.135   1   36.05       2374   OD1   ASN   300   60.01   35.222   98.836   1   36.46       2375   ND2   ASN   300   60.982   33.221   98.547   1   37.41       2376   C   ASN   300   63.187   35.959   97.411   1   38.47       2377   O   ASN   300   64.067   35.248   96.931   1   38.65       2378   N   ARG   301   63.339   36.614   98.554   1   39.52       2379   CA   ARG   301   64.586   36.526   99.298   1   41.71       2380   CB   ARG   301   65.442   37.765   99.016   1   43.08       2381   CG   ARG   301   64.727   39.072   99.283   1   46.16       2382   CD   ARG   301   65.672   40.256   99.172   1   49.91       2383   NE   ARG   301   66.08   40.526   97.798   1   52.67       2384   CZ   ARG   301   66.937   41.484   97.45   1   54.39       2385   NH1   ARG   301   67.483   42.268   98.376   1   54.14       2386   NH2   ARG   301   67.244   41.662   96.171   1   54.23       2387   C   ARG   301   64.342   36.386   100.798   1   42.2       2388   O   ARG   301   65.248   36.593   101.605   1   41.63       2389   N   ASN   302   63.111   36.036   101.157   1   41.8       2390   CA   ASN   302   62.72   35.858   102.549   1   42.57       2391   CB   ASN   302   63.375   34.604   103.129   1   48.14       2392   CG   ASN   302   62.704   33.328   102.656   1   49.75       2393   OD1   ASN   302   62.655   33.037   101.458   1   51.99       2394   ND2   ASN   302   62.179   32.559   103.601   1   53.11       2395   C   ASN   302   63.029   37.052   103.441   1   40.58       2396   O   ASN   302   63.645   36.909   104.493   1   40.69       2397   N   VAL   303   62.599   38.23   103.012   1   38.42       2398   CA   VAL   303   62.807   39.445   103.78   1   36.2       2399   CB   VAL   303   63.283   40.61   102.887   1   36.8       2400   CG1   VAL   303   63.207   41.927   103.652   1   37.98       2401   CG2   VAL   303   64.711   40.359   102.434   1   38.8       2402   C   VAL   303   61.49   39.845   104.439   1   34.67       2403   O   VAL   303   60.564   40.315   103.77   1   33.77       2404   N   ARG   304   61.416   39.655   105.751   1   31.64       2405   CA   ARG   304   60.223   40.003   106.513   1   30.43       2406   CB   ARG   304   59.967   38.938   107.596   1   30.41       2407   CG   ARG   304   58.654   39.11   108.348   1   29.74       2408   CD   ARG   304   58.533   38.137   109.519   1   28.02       2409   NE   ARG   304   58.301   36.74   109.147   1   25.39       2410   CZ   ARG   304   57.155   36.254   108.684   1   27.16       2411   NH1   ARG   304   56.109   37.05   108.514   1   28.29       2412   NH2   ARG   304   57.047   34.958   108.417   1   25.72       2413   C   ARG   304   60.473   41.365   107.151   1   29.91       2414   O   ARG   304   61.386   41.51   107.967   1   29.76       2415   N   TYR   305   59.689   42.369   106.764   1   28.58       2416   CA   TYR   305   59.842   43.712   107.326   1   29.92       2417   CB   TYR   305   59.175   44.759   106.43   1   30.86       2418   CG   TYR   305   59.829   44.92   105.075   1   32.58       2419   CD1   TYR   305   61.124   45.423   104.958   1   33.72       2420   CE1   TYR   305   61.73   45.566   103.708   1   34.63       2421   CD2   TYR   305   59.153   44.563   103.911   1   32.87       2422   CE2   TYR   305   59.749   44.7   102.657   1   35.12       2423   CZ   TYR   305   61.036   45.199   102.564   1   35.52       2424   OH   TYR   305   61.624   45.304   101.327   1   37.64       2425   C   TYR   305   59.266   43.849   108.735   1   30.66       2426   O   TYR   305   59.838   44.542   109.576   1   30.76       2427   N   LEU   306   58.128   43.205   108.988   1   29.79       2428   CA   LEU   306   57.491   43.28   110.298   1   29.5       2429   CB   LEU   306   56.014   43.638   110.145   1   32.3       2430   CG   LEU   306   55.756   45.115   109.854   1   35.29       2431   CD1   LEU   306   54.351   45.289   109.342   1   39.03       2432   CD2   LEU   306   55.975   45.929   111.126   1   37       2433   C   LEU   306   57.625   41.984   111.072   1   29.03       2434   O   LEU   306   56.808   41.078   110.935   1   25.39       2435   N   THR   307   58.665   41.905   111.893   1   29.26       2436   CA   THR   307   58.907   40.713   112.688   1   30.49       2437   CB   THR   307   60.402   40.537   112.984   1   31.61       2438   OG1   THR   307   60.868   41.676   113.714   1   33.59       2439   CG2   THR   307   61.194   40.402   111.689   1   33.13       2440   C   THR   307   58.172   40.776   114.017   1   29.79       2441   O   THR   307   57.867   39.737   114.598   1   29.68       2442   N   LEU   308   57.9   41.989   114.492   1   28.32       2443   CA   LEU   308   57.207   42.176   115.767   1   30.8       2444   CB   LEU   308   55.725   41.79   115.623   1   31.6       2445   CG   LEU   308   54.873   42.714   114.74   1   34.08       2446   CD1   LEU   308   53.54   42.067   114.422   1   35.47       2447   CD2   LEU   308   54.662   44.035   115.458   1   34.47       2448   C   LEU   308   57.87   41.314   116.844   1   30.56       2449   O   LEU   308   57.192   40.717   117.684   1   27.97       2450   N   ASP   309   59.198   41.256   116.813   1   30.42       2451   CA   ASP   309   59.955   40.453   117.769   1   32.55       2452   CB   ASP   309   61.439   40.467   117.41   1   36.27       2453   CG   ASP   309   61.919   41.832   117.016   1   39.6       2454   OD1   ASP   309   61.657   42.797   117.765   1   42.38       2455   OD2   ASP   309   62.555   41.943   115.948   1   44.74       2456   C   ASP   309   59.789   40.827   119.239   1   31.54       2457   O   ASP   309   60.25   40.096   120.109   1   31.57       2458   N   ILE   310   59.152   41.96   119.525   1   31.29       2459   CA   ILE   310   58.935   42.336   120.915   1   31.99       2460   CB   ILE   310   58.413   43.782   121.057   1   33.71       2461   CG2   ILE   310   59.488   44.76   120.617   1   36.9       2462   CG1   ILE   310   57.134   43.961   120.245   1   35.24       2463   CD1   ILE   310   56.419   45.26   120.535   1   38.78       2464   C   ILE   310   57.901   41.378   121.514   1   30.39       2465   O   ILE   310   57.754   41.304   122.729   1   30.07       2466   N   PHE   311   57.2   40.647   120.645   1   27.74       2467   CA   PHE   311   56.185   39.686   121.066   1   25.41       2468   CB   PHE   311   54.937   39.79   120.169   1   26.66       2469   CG   PHE   311   54.149   41.063   120.354   1   29.51       2470   CD1   PHE   311   53.505   41.339   121.556   1   31.8       2471   CD2   PHE   311   54.066   41.996   119.327   1   31.54       2472   CE1   PHE   311   52.79   42.532   121.735   1   32.67       2473   CE2   PHE   311   53.354   43.189   119.498   1   33.98       2474   CZ   PHE   311   52.717   43.455   120.703   1   31.44       2475   C   PHE   311   56.718   38.25   121.026   1   24.05       2476   O   PHE   311   55.969   37.315   121.262   1   22.96       2477   N   ALA   312   58.005   38.076   120.715   1   22.35       2478   CA   ALA   312   58.616   36.743   120.651   1   22.48       2479   CB   ALA   312   60.019   36.827   120.035   1   24.12       2480   C   ALA   312   58.706   36.108   122.038   1   21.84       2481   O   ALA   312   58.876   36.807   123.035   1   21.95       2482   N   GLY   313   58.584   34.784   122.101   1   21.93       2483   CA   GLY   313   58.662   34.1   123.385   1   21.35       2484   C   GLY   313   57.513   33.138   123.608   1   22.17       2485   O   GLY   313   57.735   31.956   123.844   1   21.77       2486   N   PRO   314   56.263   33.627   123.562   1   21.99       2487   CD   PRO   314   55.906   35.057   123.499   1   22.26       2488   CA   PRO   314   55.068   32.798   123.753   1   21.99       2489   CB   PRO   314   53.923   33.812   123.648   1   23.79       2490   CG   PRO   314   54.544   35.078   124.16   1   21.52       2491   C   PRO   314   54.959   31.725   122.669   1   22.73       2492   O   PRO   314   55.431   31.905   121.546   1   20.06       2493   N   PRO   315   54.332   30.589   122.994   1   23.89       2494   CD   PRO   315   53.725   30.2   124.278   1   23.5       2495   CA   PRO   315   54.195   29.528   121.995   1   24.17       2496   CB   PRO   315   53.477   28.409   122.762   1   25.56       2497   CG   PRO   315   52.733   29.146   123.844   1   26.38       2498   C   PRO   315   53.434   29.99   120.75   1   23.75       2499   O   PRO   315   53.656   29.467   119.66   1   21.44       2500   N   ASN   316   52.564   30.988   120.891   1   22.99       2501   CA   ASN   316   51.823   31.448   119.719   1   23.53       2502   CB   ASN   316   50.456   32.017   120.114   1   24.15       2503   CG   ASN   316   49.496   30.953   120.616   1   26.61       2504   OD1   ASN   316   49.741   29.752   120.475   1   25.81       2505   ND2   ASN   316   48.379   31.395   121.191   1   27.23       2506   C   ASN   316   52.554   32.466   118.829   1   22.97       2507   O   ASN   316   51.985   32.899   117.828   1   22.03       2508   N   TYR   317   53.777   32.877   119.185   1   22.46       2509   CA   TYR   317   54.514   33.809   118.322   1   21.8       2510   CB   TYR   317   55.935   34.053   118.833   1   22.35       2511   CG   TYR   317   56.73   34.969   117.926   1   23.24       2512   CD1   TYR   317   56.404   36.325   117.813   1   22.38       2513   CE1   TYR   317   57.108   37.169   116.945   1   22.18       2514   CD2   TYR   317   57.784   34.476   117.151   1   22.97       2515   CE2   TYR   317   58.491   35.314   116.28   1   22.18       2516   CZ   TYR   317   58.148   36.648   116.182   1   23.21       2517   OH   TYR   317   58.846   37.451   115.314   1   24.39       2518   C   TYR   317   54.534   33.067   116.976   1   22.49       2519   O   TYR   317   55.036   31.946   116.878   1   22.27       2520   N   PRO   318   53.981   33.688   115.924   1   22.42       2521   CD   PRO   318   53.57   35.098   115.948   1   21.67       2522   CA   PRO   318   53.87   33.138   114.567   1   23.78       2523   CB   PRO   318   52.764   33.986   113.926   1   23.9       2524   CG   PRO   318   52.502   35.136   114.898   1   24.92       2525   C   PRO   318   55.035   33.025   113.605   1   24.17       2526   O   PRO   318   55.026   32.133   112.753   1   24.57       2527   N   PHE   319   56.017   33.908   113.723   1   24.31       2528   CA   PHE   319   57.105   33.929   112.764   1   27.99       2529   CB   PHE   319   57.528   35.386   112.531   1   25.41       2530   CG   PHE   319   56.36   36.332   112.331   1   24.36       2531   CD1   PHE   319   55.244   35.949   111.584   1   24.42       2532   CD2   PHE   319   56.387   37.606   112.874   1   25.1       2533   CE1   PHE   319   54.167   36.833   111.38   1   22.49       2534   CE2   PHE   319   55.326   38.496   112.679   1   26.18       2535   CZ   PHE   319   54.218   38.107   111.932   1   23.79       2536   C   PHE   319   58.312   33.053   113.042   1   30.78       2537   O   PHE   319   59.367   33.255   112.454   1   34.17       2538   N   SER   320   58.15   32.069   113.912   1   32.82       2539   CA   SER   320   59.237   31.156   114.228   1   35.99       2540   CB   SER   320   59.107   30.649   115.664   1   35.8       2541   OG   SER   320   59.553   31.627   116.577   1   39.46       2542   C   SER   320   59.25   29.968   113.273   1   36.75       2543   O   SER   320   60.308   29.547   112.814   1   37.09       2544   N   ASP   321   58.07   29.433   112.972   1   36.63       2545   CA   ASP   321   57.969   28.286   112.081   1   37.7       2546   CB   ASP   321   56.557   27.699   112.12   1   37.98       2547   CG   ASP   321   56.151   27.257   113.504   1   39.08       2548   OD1   ASP   321   57.04   27.127   114.371   1   41.4       2549   OD2   ASP   321   54.944   27.03   113.719   1   37.81       2550   C   ASP   321   58.318   28.641   110.641   1   38.03       2551   O   ASP   321   58.362   29.814   110.274   1   36.77       2552   N   GLU   322   58.566   27.62   109.829   1   38.02       2553   CA   GLU   322   58.9   27.839   108.429   1   40.14       2554   CB   GLU   322   59.163   26.509   107.728   1   43.27       2555   CG   GLU   322   59.509   26.666   106.259   1   49.62       2556   CD   GLU   322   59.682   25.334   105.562   1   53.4       2557   OE1   GLU   322   58.738   24.509   105.602   1   55.39       2558   OE2   GLU   322   60.76   25.112   104.966   1   56.35       2559   C   GLU   322   57.772   28.586   107.723   1   38.44       2560   O   GLU   322   58.02   29.42   106.857   1   38.44       2561   N   TYR   323   56.532   28.273   108.084   1   35.34       2562   CA   TYR   323   55.373   28.951   107.507   1   34.25       2563   CB   TYR   323   55.209   28.587   106.02   1   34.15       2564   CG   TYR   323   54.545   27.256   105.747   1   34.6       2565   CD1   TYR   323   53.197   27.191   105.389   1   35.02       2566   CE1   TYR   323   52.568   25.97   105.156   1   36.34       2567   CD2   TYR   323   55.254   26.063   105.866   1   36.3       2568   CE2   TYR   323   54.637   24.834   105.64   1   38.59       2569   CZ   TYR   323   53.293   24.797   105.286   1   39.03       2570   OH   TYR   323   52.681   23.586   105.079   1   40.66       2571   C   TYR   323   54.126   28.568   108.304   1   33.55       2572   O   TYR   323   53.076   29.211   108.12   1   32.2       2573   OXT   TYR   323   54.225   27.623   109.114   1   33.11       2574   TYR   A       2575   CB   SER   3   23.11   40.285   92.904   1   51.49       2576   OG   SER   3   23.122   40.992   91.671   1   52.76       2577   C   SER   3   25.24   41.36   93.638   1   46.66       2578   O   SER   3   25.53   42.299   92.899   1   47.86       2579   N   SER   3   23.054   42.379   94.244   1   50.69       2580   CA   SER   3   23.787   41.092   94.021   1   49.5       2581   N   LYS   4   26.154   40.54   94.149   1   42.8       2582   CA   LYS   4   27.568   40.693   93.824   1   37.17       2583   CB   LYS   4   28.391   40.953   95.092   1   39.55       2584   CG   LYS   4   28.317   42.395   95.597   1   41.23       2585   CD   LYS   4   29.222   42.614   96.796   1   43.05       2586   CE   LYS   4   29.335   44.087   97.159   1   44.48       2587   NZ   LYS   4   28.017   44.716   97.433   1   46.38       2588   C   LYS   4   28.084   39.452   93.099   1   33.85       2589   O   LYS   4   27.602   38.349   93.333   1   32.85       2590   N   TYR   5   29.054   39.64   92.206   1   29.33       2591   CA   TYR   5   29.628   38.536   91.442   1   26.37       2592   CB   TYR   5   28.686   38.139   90.295   1   24.54       2593   CG   TYR   5   28.12   39.312   89.526   1   24.48       2594   CD1   TYR   5   28.732   39.775   88.355   1   24.71       2595   CE1   TYR   5   28.218   40.871   87.656   1   25.46       2596   CD2   TYR   5   26.98   39.974   89.981   1   23.74       2597   CE2   TYR   5   26.456   41.068   89.292   1   25.68       2598   CZ   TYR   5   27.077   41.512   88.133   1   27.64       2599   OH   TYR   5   26.558   42.591   87.449   1   27.65       2600   C   TYR   5   30.99   38.956   90.908   1   25.38       2601   O   TYR   5   31.26   40.149   90.754   1   24.54       2602   N   GLN   6   31.85   37.983   90.623   1   23.54       2603   CA   GLN   6   33.191   38.284   90.14   1   23.98       2604   CB   GLN   6   34.113   37.066   90.316   1   24.98       2605   CG   GLN   6   34.23   36.605   91.762   1   29.43       2606   CD   GLN   6   35.292   35.541   91.992   1   30.13       2607   OE1   GLN   6   35.286   34.875   93.035   1   33.67       2608   NE2   GLN   6   36.214   35.379   91.033   1   23.36       2609   C   GLN   6   33.223   38.751   88.689   1   23.14       2610   O   GLN   6   32.671   38.097   87.804   1   21.74       2611   N   CYS   7   33.881   39.889   88.478   1   22.96       2612   CA   CYS   7   34.047   40.52   87.162   1   25.27       2613   CB   CYS   7   33.195   41.784   87.036   1   27.29       2614   SG   CYS   7   31.453   41.58   87.206   1   33.83       2615   C   CYS   7   35.48   40.981   86.989   1   24.65       2616   O   CYS   7   36.238   41.08   87.958   1   24.06       2617   N   VAL   8   35.839   41.277   85.745   1   24.96       2618   CA   VAL   8   37.156   41.81   85.423   1   23.89       2619   CB   VAL   8   37.998   40.855   84.539   1   25.46       2620   CG1   VAL   8   38.426   39.652   85.36   1   29.75       2621   CG2   VAL   8   37.203   40.418   83.303   1   24.53       2622   C   VAL   8   36.913   43.096   84.649   1   24.28       2623   O   VAL   8   35.929   43.208   83.915   1   22.61       2624   N   LYS   9   37.799   44.071   84.821   1   22.76       2625   CA   LYS   9   37.661   45.341   84.12   1   24.08       2626   CB   LYS   9   38.384   46.451   84.885   1   22.1       2627   CG   LYS   9   38.062   47.846   84.377   1   24.27       2628   CD   LYS   9   38.73   48.914   85.236   1   28.1       2629   CE   LYS   9   38.286   50.312   84.831   1   29.63       2630   NZ   LYS   9   38.878   51.354   85.715   1   33.48       2631   C   LYS   9   38.237   45.241   82.705   1   23.39       2632   O   LYS   9   39.359   44.767   82.517   1   26.48       2633   N   LEU   10   37.462   45.676   81.717   1   23.77       2634   CA   LEU   10   37.883   45.646   80.313   1   23.05       2635   CB   LEU   10   36.649   45.544   79.405   1   22.2       2636   CG   LEU   10   38.108   44.165   78.997   1   25.16       2637   CD1   LEU   10   36.524   43.11   79.969   1   25.8       2638   CD2   LEU   10   34.586   44.232   78.843   1   23.3       2639   C   LEU   10   38.682   46.904   79.99   1   24.13       2640   O   LEU   10   38.622   47.885   80.735   1   21.46       2641   N   ASN   11   39.423   46.889   78.882   1   23.72       2642   CA   ASN   11   40.231   48.055   78.532   1   24.5       2643   CB   ASN   11   41.281   47.716   77.452   1   23.61       2644   CG   ASN   11   40.668   47.251   76.143   1   23.15       2645   OD1   ASN   11   39.653   47.777   75.692   1   26.36       2646   ND2   ASN   11   41.302   46.27   75.514   1   24.55       2647   C   ASN   11   39.422   49.283   78.117   1   23.94       2648   O   ASN   11   40.001   50.326   77.844   1   24.73       2649   N   ASP   12   38.093   46.172   78.076   1   23.89       2650   CA   ASP   12   37.265   50.336   77.73   1   23.72       2851   CB   ASP   12   36.27   50.01   76.603   1   22.85       2652   CG   ASP   12   35.165   49.063   77.039   1   22.92       2653   OD1   ASP   12   35.21   48.55   78.176   1   23.93       2654   OD2   ASP   12   34.243   48.82   76.228   1   25.82       2655   C   ASP   12   36.511   50.836   78.958   1   24.19       2656   O   ASP   12   35.613   51.672   78.854   1   24.59       2657   N   GLY   13   36.864   50.303   80.124   1   24.62       2658   CA   GLY   13   36.209   50.734   81.346   1   23.34       2659   C   GLY   13   35.017   49.907   81.796   1   25.14       2660   O   GLY   13   34.554   50.066   82.933   1   25.24       2661   N   HIS   14   34.505   49.029   80.932   1   21.75       2662   CA   HIS   14   33.358   48.213   81.325   1   21.95       2663   CB   HIS   14   32.501   47.825   80.102   1   23.02       2664   CG   HIS   14   31.706   48.964   79.54   1   24.58       2665   CD2   HIS   14   30.676   49.674   80.061   1   25.5       2666   ND1   HIS   14   31.975   49.528   78.311   1   27.89       2667   CE1   HIS   14   31.145   50.535   78.097   1   26       2668   NE2   HIS   14   30.347   50.646   79.145   1   27.75       2669   C   HIS   14   33.818   46.972   82.07   1   21.49       2670   O   HIS   14   35.009   46.653   82.071   1   21.38       2671   N   PHE   15   32.875   46.285   82.713   1   21.42       2672   CA   PHE   15   33.188   45.091   83.481   1   21.62       2673   CB   PHE   15   32.81   45.284   84.954   1   23.2       2674   CG   PHE   15   33.742   46.194   85.705   1   23.74       2675   CD1   PHE   15   33.649   47.581   85.576   1   25.06       2676   CD2   PHE   15   34.726   45.655   86.536   1   23.38       2677   CE1   PHE   15   34.529   48.428   86.269   1   24.03       2678   CE2   PHE   15   35.611   46.482   87.232   1   23.84       2679   CZ   PHE   15   35.511   47.877   87.099   1   25.29       2680   C   PHE   15   32.491   43.858   82.931   1   20.99       2681   O   PHE   15   31.321   43.902   82.571   1   23.17       2682   N   MET   16   33.217   42.751   82.88   1   18.67       2683   CA   MET   16   32.675   41.511   82.359   1   19.2       2684   CB   MET   16   33.5   41.083   81.135   1   20.21       2685   CG   MET   16   33.149   39.711   80.564   1   21.12       2686   SD   MET   16   34.37   39.145   79.317   1   26.36       2687   CE   MET   16   33.778   39.965   77.887   1   23.05       2688   C   MET   16   32.716   40.408   83.413   1   18.36       2689   O   MET   16   33.756   40.19   84.038   1   18.24       2690   N   PRO   17   31.581   39.72   83.638   1   17.86       2691   CD   PRO   17   30.237   40.048   83.11   1   17.68       2692   CA   PRO   17   31.52   38.625   84.624   1   18.07       2693   CB   PRO   17   30.054   38.194   84.577   1   17.06       2694   CG   PRO   17   29.31   39.5   84.196   1   17.51       2695   C   PRO   17   32.474   37.532   84.117   1   19.83       2696   O   PRO   17   32.456   37.21   82.931   1   20.42       2697   N   VAL   18   33.292   36.966   85.001   1   20.07       2698   CA   VAL   18   34.288   35.969   84.597   1   20.44       2699   CB   VAL   18   35.369   35.783   85.686   1   21.53       2700   CG1   VAL   18   36.081   37.108   85.935   1   23.77       2701   CG2   VAL   18   34.738   35.272   86.979   1   22.46       2702   C   VAL   18   33.789   34.587   84.199   1   20.34       2703   O   VAL   18   34.549   33.798   83.632   1   19.6       2704   N   LEU   19   32.537   34.277   84.523   1   19.12       2705   CA   LEU   19   31.954   32.989   84.169   1   20.34       2706   CB   LEU   19   31.479   32.223   85.417   1   20.44       2707   CG   LEU   19   30.669   30.939   85.143   1   20.87       2708   CD1   LEU   19   31.551   29.909   84.464   1   22.15       2709   CD2   LEU   19   30.118   30.378   86.442   1   22.51       2710   C   LEU   19   30.77   33.291   83.26   1   19.76       2711   O   LEU   19   29.862   34.036   83.629   1   19.31       2712   N   GLY   20   30.796   32.73   82.061   1   18.97       2713   CA   GLY   20   29.718   32.965   81.119   1   19.62       2714   C   GLY   20   28.978   31.702   80.727   1   20.48       2715   O   GLY   20   29.547   30.609   80.731   1   19.33       2716   N   PHE   21   27.705   31.861   80.383   1   20.13       2717   CA   PHE   21   26.856   30.741   79.99   1   21.82       2718   CB   PHE   21   25.444   30.939   80.566   1   20.86       2719   CG   PHE   21   24.515   29.787   80.303   1   22.06       2720   CD1   PHE   21   24.73   28.554   80.912   1   22.01       2721   CD2   PHE   21   23.455   29.919   79.411   1   23.33       2722   CE1   PHE   21   23.902   27.462   80.634   1   21.96       2723   CE2   PHE   21   22.617   28.835   79.122   1   24.29       2724   CZ   PHE   21   22.845   27.608   79.736   1   23.8       2725   C   PHE   21   26.781   30.636   78.466   1   21.4       2726   O   PHE   21   26.399   31.595   77.789   1   20.17       2727   N   GLY   22   27.153   29.474   77.932   1   21.02       2728   CA   GLY   22   27.099   29.268   76.496   1   22.2       2729   C   GLY   22   25.72   28.796   76.071   1   22.97       2730   O   GLY   22   25.119   27.968   76.754   1   22.67       2731   N   THR   23   25.216   29.293   74.944   1   23.62       2732   CA   THR   23   23.871   28.924   74.502   1   24.19       2733   CB   THR   23   22.993   30.172   74.335   1   22.21       2734   OG1   THR   23   23.536   31.009   73.302   1   21.01       2735   CG2   THR   23   22.948   30.959   75.642   1   22.76       2736   C   THR   23   23.771   28.114   73.207   1   26.42       2737   O   THR   23   22.666   27.767   72.778   1   27.73       2738   N   TYR   24   24.9   27.81   72.58   1   26.09       2739   CA   TYR   24   24.849   27.03   71.348   1   29.15       2740   CB   TYR   24   26.19   27.049   70.614   1   29.87       2741   CG   TYR   24   26.169   26.159   69.379   1   33.24       2742   CD1   TYR   24   25.503   26.561   68.217   1   34.26       2743   CE1   TYR   24   25.405   25.712   67.108   1   35.36       2744   CD2   TYR   24   26.741   24.886   69.401   1   32.89       2745   CE2   TYR   24   26.648   24.031   68.299   1   34.4       2746   CZ   TYR   24   25.975   24.453   67.158   1   35.12       2747   OH   TYR   24   25.859   23.611   66.075   1   36.53       2748   C   TYR   24   24.486   25.579   71.614   1   28.8       2749   O   TYR   24   24.953   24.983   72.582   1   29.48       2750   N   ALA   25   23.665   25.009   70.742   1   29.91       2751   CA   ALA   25   23.28   23.606   70.856   1   32.21       2752   CB   ALA   25   22.016   23.46   71.694   1   30.83       2753   C   ALA   25   23.045   23.062   69.445   1   34.07       2754   O   ALA   25   22.658   23.812   68.551   1   31.89       2755   N   PRO   26   23.294   21.752   69.226   1   36.72       2756   CD   PRO   26   23.816   20.788   70.211   1   37.06       2757   CA   PRO   26   23.105   21.108   67.919   1   39.09       2758   CB   PRO   26   23.298   19.63   68.233   1   39.11       2759   CG   PRO   26   24.31   19.66   69.327   1   39.34       2760   C   PRO   26   21.712   21.394   67.374   1   41.24       2761   O   PRO   26   20.754   21.5   68.142   1   40.63       2762   N   ALA   27   21.604   21.506   66.054   1   44.55       2763   CA   ALA   27   20.326   21.795   65.403   1   47.37       2764   CB   ALA   27   20.514   21.845   63.885   1   48.56       2765   C   ALA   27   19.234   20.792   65.76   1   48.57       2766   O   ALA   27   18.048   21.097   65.654   1   49.96       2767   N   GLU   28   19.638   19.6   66.184   1   49.36       2768   CA   GLU   28   18.686   18.56   66.555   1   50.9       2769   CB   GLU   28   19.413   17.225   66.717   1   53.65       2770   CG   GLU   28   20.564   17.283   67.712   1   58.93       2771   CD   GLU   28   21.368   15.996   67.776   1   61.61       2772   OE1   GLU   28   20.822   14.966   68.233   1   64.23       2773   OE2   GLU   28   22.549   16.018   67.365   1   63.26       2774   C   GLU   28   17.95   18.9   67.847   1   49.9       2775   O   GLU   28   16.866   18.378   68.105   1   50.83       2776   N   VAL   29   18.54   19.77   68.662   1   47.83       2777   CA   VAL   29   17.928   20.168   69.93   1   44.9       2778   CB   VAL   29   18.994   20.656   70.941   1   44.63       2779   CG1   VAL   29   18.346   20.945   72.287   1   43.33       2780   CG2   VAL   29   20.095   19.619   71.084   1   43.27       2781   C   VAL   29   16.914   21.295   69.727   1   44.17       2782   O   VAL   29   17.207   22.292   69.073   1   43.92       2783   N   PRO   30   15.704   21.148   70.292   1   43.3       2784   CD   PRO   30   15.223   19.984   71.056   1   43.06       2785   CA   PRO   30   14.647   22.16   70.17   1   43.44       2786   CB   PRO   30   13.507   21.57   71.002   1   42.61       2787   CG   PRO   30   13.728   20.1   70.898   1   42.89       2788   C   PRO   30   15.091   23.528   70.707   1   42.98       2789   O   PRO   30   15.723   23.614   71.762   1   40.95       2790   N   LYS   31   14.748   24.59   69.986   1   43.38       2791   CA   LYS   31   15.111   25.941   70.402   1   44.42       2792   CB   LYS   31   14.745   26.956   69.309   1   45.21       2793   CG   LYS   31   15.524   26.795   68.008   1   46.67       2794   CD   LYS   31   17.029   26.847   68.241   1   47.63       2795   CE   LYS   31   17.794   26.603   66.949   1   48.38       2796   NZ   LYS   31   19.256   26.429   67.172   1   50.44       2797   C   LYS   31   14.421   26.326   71.71   1   44.37       2798   O   LYS   31   14.805   27.295   72.358   1   45.04       2799   N   SER   32   13.404   25.56   72.097   1   43.67       2800   CA   SER   32   12.667   25.833   73.325   1   42.65       2801   CB   SER   32   11.387   24.991   73.373   1   42.69       2802   OG   SER   32   11.674   23.606   73.413   1   41.36       2803   C   SER   32   13.52   25.551   74.563   1   42.86       2804   O   SER   32   13.341   26.173   75.615   1   43.23       2805   N   LYS   33   14.449   24.61   74.442   1   41.51       2806   CA   LYS   33   15.317   24.271   75.559   1   40.07       2807   CB   LYS   33   16.071   22.971   75.276   1   43.25       2808   CG   LYS   33   15.219   21.716   75.38   1   47.42       2809   CD   LYS   33   16.087   20.468   75.296   1   52.09       2810   CE   LYS   33   15.265   19.196   75.452   1   54.57       2811   NZ   LYS   33   16.114   17.974   75.331   1   56.46       2812   C   LYS   33   16.309   25.399   75.845   1   37.74       2813   O   LYS   33   16.826   25.507   76.957   1   36.52       2814   N   ALA   34   16.575   26.235   74.846   1   34.59       2815   CA   ALA   34   17.49   27.356   75.035   1   34.06       2816   CB   ALA   34   17.826   28.005   73.697   1   34.5       2817   C   ALA   34   16.814   28.368   75.964   1   33.31       2818   O   ALA   34   17.457   28.969   76.828   1   31.23       2819   N   LEU   35   15.509   28.546   75.789   1   32.19       2820   CA   LEU   35   14.761   29.475   76.624   1   31.46       2821   CB   LEU   35   13.312   29.576   76.142   1   32.96       2822   CG   LEU   35   12.317   30.341   77.022   1   33.43       2823   CD1   LEU   35   12.749   31.78   77.22   1   34.56       2824   CD2   LEU   35   10.959   30.294   76.348   1   37.14       2825   C   LEU   35   14.794   29.021   78.081   1   31.43       2826   O   LEU   35   15.036   29.817   78.988   1   29.27       2827   N   GLU   36   14.556   27.735   78.305   1   31.35       2828   CA   GLU   36   14.561   27.195   79.661   1   33.31       2829   CB   GLU   36   14.043   25.76   79.649   1   37.09       2830   CG   GLU   36   12.7   25.633   78.965   1   45.94       2831   CD   GLU   36   12.192   24.203   78.925   1   50.64       2832   OE1   GLU   36   12.944   23.315   78.456   1   53.15       2833   OE2   GLU   36   11.036   23.974   79.353   1   53.3       2834   C   GLU   36   15.953   27.224   80.274   1   31.27       2835   O   GLU   36   16.12   27.582   81.445   1   30.65       2836   N   ALA   37   16.951   26.851   79.479   1   28.97       2837   CA   ALA   37   18.333   26.825   79.954   1   27.45       2838   CB   ALA   37   19.259   26.281   78.852   1   26.57       2839   C   ALA   37   18.822   28.2   80.427   1   26.24       2840   O   ALA   37   19.428   28.31   81.49   1   25.18       2841   N   VAL   38   18.564   29.245   79.645   1   25.53       2842   CA   VAL   38   19.007   30.574   80.041   1   25.16       2843   CB   VAL   38   18.754   31.612   78.921   1   26.09       2844   CG1   VAL   38   19.134   33.008   79.396   1   24.8       2845   CG2   VAL   38   19.585   31.252   77.696   1   24.23       2846   C   VAL   38   18.324   31.016   81.342   1   25.72       2847   O   VAL   38   18.959   31.624   82.201   1   23.17       2848   N   LYS   39   17.039   30.704   81.499   1   25.85       2849   CA   LYS   39   16.336   31.083   82.72   1   26.89       2850   CB   LYS   39   14.87   30.668   82.651   1   28.97       2851   CG   LYS   39   14.01   31.552   81.768   1   31.93       2852   CD   LYS   39   12.548   31.133   81.871   1   38.8       2853   CE   LYS   39   11.646   32.084   81.103   1   42.32       2854   NZ   LYS   39   10.197   31.748   81.265   1   46.18       2855   C   LYS   39   16.985   30.432   83.941   1   26.88       2856   O   LYS   39   17.199   31.085   84.965   1   26.39       2857   N   LEU   40   17.294   29.144   83.827   1   26.1       2858   CA   LEU   40   17.921   28.403   84.915   1   26.99       2859   CB   LEU   40   17.991   26.907   84.562   1   29.26       2860   CG   LEU   40   16.664   26.138   84.492   1   30.91       2861   CD1   LEU   40   16.894   24.739   83.936   1   33.02       2862   CD2   LEU   40   16.036   25.063   85.885   1   32       2863   C   LEU   40   19.323   28.93   85.219   1   26.7       2864   O   LEU   40   19.715   29.03   86.377   1   26.63       2865   N   ALA   41   20.083   29.255   84.175   1   25.67       2866   CA   ALA   41   21.435   29.786   84.35   1   24.31       2867   CB   ALA   41   22.101   29.997   82.98   1   24.12       2868   C   ALA   41   21.385   31.106   85.126   1   23.7       2869   O   ALA   41   22.207   31.347   86.009   1   23.75       2870   N   ILE   42   20.424   31.965   84.798   1   23.4       2871   CA   ILE   42   20.304   33.23   85.504   1   24.4       2872   CB   ILE   42   19.26   34.157   84.83   1   23.89       2873   CG2   ILE   42   18.979   35.361   85.713   1   23.17       2874   CG1   ILE   42   19.801   34.624   83.47   1   24.07       2875   CD1   ILE   42   18.826   35.454   82.645   1   24.15       2876   C   ILE   42   19.926   32.963   86.964   1   26.63       2877   O   ILE   42   20.459   33.596   87.875   1   25.63       2878   N   GLU   43   19.023   32.014   87.191   1   27.75       2879   CA   GLU   43   18.619   31.67   88.557   1   29.96       2880   CB   GLU   43   17.464   30.666   88.529   1   32.5       2881   CG   GLU   43   16.163   31.253   88.02   1   39.88       2882   CD   GLU   43   15.071   30.212   87.883   1   44.77       2883   OE1   GLU   43   14.978   29.336   88.772   1   48.08       2884   OE2   GLU   43   14.299   30.275   86.898   1   46.33       2885   C   GLU   43   19.784   31.078   89.353   1   29.45       2886   O   GLU   43   19.901   31.314   90.552   1   29.01       2887   N   ALA   44   20.642   30.316   88.678   1   27.71       2888   CA   ALA   44   21.784   29.679   89.318   1   26.97       2889   CB   ALA   44   22.332   28.57   88.417   1   25.65       2890   C   ALA   44   22.9   30.665   89.674   1   27.05       2891   O   ALA   44   23.745   30.369   90.519   1   26.75       2892   N   GLY   45   22.915   31.831   89.033   1   25.47       2893   CA   GLY   45   23.957   32.8   89.346   1   26.2       2894   C   GLY   45   24.823   33.257   88.179   1   24.8       2895   O   GLY   45   25.822   33.941   88.383   1   24.11       2896   N   PHE   46   24.463   32.865   86.96   1   22.81       2897   CA   PHE   46   25.206   33.299   85.774   1   23.85       2898   CB   PHE   46   24.873   32.41   84.577   1   21.71       2899   CG   PHE   46   25.639   31.126   84.536   1   21.41       2900   CD1   PHE   46   26.841   31.046   83.844   1   21.32       2901   CD2   PHE   46   25.149   29.986   85.159   1   20.85       2902   CE1   PHE   46   27.553   29.838   83.764   1   22.22       2903   CE2   PHE   46   25.853   28.771   85.085   1   22.8       2904   CZ   PHE   46   27.054   28.701   84.387   1   21.79       2905   C   PHE   46   24.772   34.728   85.449   1   23.48       2906   O   PHE   46   23.58   35.016   85.402   1   24.97       2907   N   HIS   47   25.738   35.617   85.224   1   22.89       2908   CA   HIS   47   25.435   37.01   84.899   1   21.75       2909   CB   HIS   47   26.064   37.937   85.94   1   20.72       2910   CG   HIS   47   25.362   37.921   87.259   1   22.19       2911   CD2   HIS   47   25.554   37.162   88.364   1   23.04       2912   ND1   HIS   47   24.289   38.74   87.538   1   24.37       2913   CE1   HIS   47   23.851   38.487   88.758   1   23.52       2914   NE2   HIS   47   24.6   37.533   89.28   1   22.33       2915   C   HIS   47   25.971   37.379   83.514   1   22.95       2916   O   HIS   47   25.86   38.524   83.082   1   23.41       2917   N   HIS   48   26.547   36.394   82.834   1   21.99       2918   CA   HIS   48   27.142   36.575   81.509   1   21.77       2919   CB   HIS   48   28.669   36.428   81.644   1   21.18       2920   CG   HIS   48   29.429   36.499   80.351   1   21.68       2921   CD2   HIS   48   29.025   36.382   79.064   1   21.78       2922   ND1   HIS   48   30.802   36.624   80.309   1   22.13       2923   CE1   HIS   48   31.21   36.572   79.053   1   23.16       2924   NE2   HIS   48   30.15   36.423   78.278   1   22.2       2925   C   HIS   48   26.53   35.507   80.593   1   21.54       2926   O   HIS   48   26.568   34.317   80.9   1   20.56       2927   N   ILE   49   25.934   35.95   79.488   1   20.27       2928   CA   ILE   49   25.29   35.048   78.53   1   20.69       2929   CB   ILE   49   23.758   35.303   78.48   1   22.42       2930   CG2   ILE   49   23.084   34.324   77.507   1   22.61       2931   CG1   ILE   49   23.177   35.155   79.894   1   23.66       2932   CD1   ILE   49   21.782   35.697   80.036   1   31       2933   C   ILE   49   25.898   35.272   77.145   1   20.39       2934   O   ILE   49   25.953   36.399   76.651   1   20.55       2935   N   ASP   50   26.329   34.186   76.518   1   18.83       2936   CA   ASP   50   26.974   34.263   75.22   1   19.92       2937   CB   ASP   50   28.332   33.549   75.283   1   19.2       2938   CG   ASP   50   29.119   33.669   73.984   1   20.93       2939   OD1   ASP   50   29.888   34.643   73.832   1   17.84       2940   OD2   ASP   50   28.959   32.79   73.105   1   21.3       2941   C   ASP   50   26.142   33.658   74.099   1   19.88       2942   O   ASP   50   25.757   32.491   74.165   1   19.89       2943   N   SER   51   25.846   34.449   73.075   1   19.81       2944   CA   SER   51   25.107   33.915   71.94   1   20.16       2945   CB   SER   51   23.614   34.207   72.041   1   21.03       2946   OG   SER   51   22.906   33.362   71.124   1   24.72       2947   C   SER   51   25.655   34.488   70.636   1   21.26       2948   O   SER   51   26.767   35.009   70.598   1   21.14       2949   N   ALA   52   24.865   34.4   69.573   1   20.99       2950   CA   ALA   52   25.298   34.872   68.273   1   22.57       2951   CB   ALA   52   26.491   34.036   67.792   1   20.12       2952   C   ALA   52   24.156   34.734   67.286   1   22.63       2953   O   ALA   52   23.255   33.919   67.48   1   24.12       2954   N   HIS   53   24.197   35.527   66.227   1   22.43       2955   CA   HIS   53   23.164   35.461   65.206   1   24.21       2956   CB   HIS   53   23.492   36.441   64.07   1   24.8       2957   CG   HIS   53   22.581   36.325   62.892   1   27.19       2958   CD2   HIS   53   22.826   35.955   61.613   1   28.16       2959   ND1   HIS   53   21.226   36.552   62.974   1   28.2       2960   CE1   HIS   53   20.672   36.322   61.796   1   29.25       2961   NE2   HIS   53   21.623   35.958   60.953   1   30.19       2962   C   HIS   53   23.067   34.031   64.661   1   24.84       2963   O   HIS   53   21.979   33.469   64.598   1   24.37       2964   N   VAL   54   24.206   33.432   64.305   1   25.97       2965   CA   VAL   54   24.209   32.079   63.733   1   27.38       2966   CB   VAL   54   25.607   31.625   63.235   1   29.06       2967   CG1   VAL   54   25.938   32.303   61.941   1   31.84       2968   CG2   VAL   54   26.663   31.884   64.292   1   28.59       2969   C   VAL   54   23.713   30.95   64.601   1   27.43       2970   O   VAL   54   23.506   29.85   64.099   1   26.2       2971   N   TYR   55   23.545   31.187   65.897   1   25.66       2972   CA   TYR   55   23.063   30.116   66.767   1   24.57       2973   CB   TYR   55   23.375   30.412   68.242   1   23.08       2974   CG   TYR   55   24.858   30.477   68.572   1   20.87       2975   CD1   TYR   55   25.825   30.083   67.644   1   20.85       2976   CE1   TYR   55   27.19   30.168   67.934   1   19.98       2977   CD2   TYR   55   25.292   30.953   69.81   1   22.02       2978   CE2   TYR   55   26.652   31.041   70.114   1   20.05       2979   CZ   TYR   55   27.592   30.651   69.168   1   20.66       2980   OH   TYR   55   28.928   30.786   69.449   1   20.36       2981   C   TYR   55   21.56   29.975   66.578   1   25.61       2982   O   TYR   55   20.949   29.005   67.023   1   26.05       2983   N   ASN   56   20.971   30.964   65.919   1   26.33       2984   CA   ASN   56   19.543   30.97   65.65   1   28.12       2985   CB   ASN   56   19.199   29.875   64.64   1   32.95       2986   CG   ASN   56   17.921   30.166   63.883   1   38.01       2987   OD1   ASN   56   17.27   29.255   63.371   1   43.36       2988   ND2   ASN   56   17.558   31.444   63.796   1   40.52       2989   C   ASN   56   18.69   30.78   66.904   1   27.75       2990   O   ASN   56   17.686   30.067   66.879   1   27.99       2991   N   ASN   57   19.078   31.421   68.001   1   26.13       2992   CA   ASN   57   18.322   31.298   69.239   1   25.98       2993   CB   ASN   57   19.011   30.296   70.185   1   25.2       2994   CG   ASN   57   20.402   30.755   70.617   1   26.97       2995   OD1   ASN   57   20.771   31.917   70.432   1   27.15       2996   ND2   ASN   57   21.175   29.845   71.206   1   26.44       2997   C   ASN   57   18.141   32.625   69.977   1   25.42       2998   O   ASN   57   17.644   32.638   71.099   1   25.94       2999   N   GLU   58   18.526   33.735   69.357   1   25.6       3000   CA   GLU   58   18.432   35.027   70.031   1   26.34       3001   CB   GLU   58   19.104   36.121   69.183   1   25.7       3002   CG   GLU   58   20.645   36.006   69.244   1   25.77       3003   CD   GLU   58   21.387   37.199   68.658   1   25.84       3004   OE1   GLU   58   21.144   37.541   67.478   1   24.8       3005   OE2   GLU   58   22.231   37.78   69.377   1   24.97       3006   C   GLU   58   17.017   35.414   70.437   1   27.34       3007   O   GLU   58   16.815   36.135   71.418   1   25.53       3008   N   GLU   59   16.034   34.917   69.698   1   27.98       3009   CA   GLU   59   14.651   35.199   70.025   1   30       3010   CB   GLU   59   13.744   34.652   68.93   1   34.43       3011   CG   GLU   59   12.286   34.967   69.106   1   41.73       3012   CD   GLU   59   11.488   34.592   67.875   1   46.56       3013   OE1   GLU   59   11.354   33.38   67.597   1   49.54       3014   OE2   GLU   59   11.013   35.512   57.175   1   49.46       3015   C   GLU   59   14.328   34.539   71.371   1   29.4       3016   O   GLU   59   13.74   35.167   72.255   1   28.42       3017   N   GLN   60   14.731   33.279   71.535   1   27.4       3018   CA   GLN   60   14.48   32.552   72.782   1   27.54       3019   CB   GLN   60   14.765   31.052   72.619   1   29.68       3020   CG   GLN   60   13.806   30.284   71.714   1   30.38       3021   CD   GLN   60   13.884   30.716   70.269   1   32.32       3022   OE1   GLN   60   14.957   31.036   69.756   1   33.54       3023   NE2   GLN   60   12.744   30.71   69.593   1   36.39       3024   C   GLN   60   15.345   33.085   73.925   1   26.83       3025   O   GLN   60   14.865   33.246   75.047   1   26.42       3026   N   VAL   61   16.621   33.341   73.641   1   25.34       3027   CA   VAL   61   17.533   33.863   74.655   1   25.63       3028   CB   VAL   61   18.982   33.995   74.093   1   26.32       3029   CG1   VAL   61   19.892   34.682   75.117   1   26.57       3030   CG2   VAL   61   19.536   32.609   73.774   1   27.75       3031   C   VAL   61   17.024   35.22   75.15   1   25.49       3032   O   VAL   61   16.978   35.471   76.359   1   24.8       3033   N   GLY   62   16.612   36.076   74.215   1   24.34       3034   CA   GLY   62   16.105   37.388   74.583   1   25.51       3035   C   GLY   62   14.885   37.29   75.484   1   26.43       3036   O   GLY   62   14.747   38.033   76.459   1   26.03       3037   N   LEU   63   13.991   36.364   75.156   1   25.93       3038   CA   LEU   63   12.779   36.171   75.941   1   28.5       3039   CB   LEU   63   11.874   35.149   75.251   1   30.77       3040   CG   LEU   63   10.448   34.996   75.777   1   34.72       3041   CD1   LEU   63   9.702   36.324   75.714   1   36.85       3042   CD2   LEU   63   9.734   33.955   74.932   1   36.99       3043   C   LEU   63   13.122   35.707   77.365   1   28.11       3044   O   LEU   63   12.504   36.139   78.344   1   26.23       3045   N   ALA   64   14.108   34.826   77.48   1   26.08       3046   CA   ALA   64   14.516   34.347   78.795   1   26.61       3047   CB   ALA   64   15.625   33.303   78.66   1   25.41       3048   C   ALA   64   15.003   35.522   79.645   1   26.26       3049   O   ALA   64   14.605   35.674   80.804   1   26.32       3050   N   ILE   65   15.861   36.353   79.06   1   25.07       3051   CA   ILE   65   16.417   37.511   79.757   1   26       3052   CB   ILE   65   17.457   38.248   78.869   1   25.98       3053   CG2   ILE   65   17.907   39.549   79.542   1   25.07       3054   CG1   ILE   65   18.66   37.332   78.619   1   25.28       3055   CD1   ILE   65   19.699   37.916   77.673   1   27.03       3056   C   ILE   65   15.326   38.497   80.177   1   26.74       3057   O   ILE   65   15.264   38.902   81.34   1   25.91       3058   N   ARG   66   14.467   38.883   79.237   1   25.35       3059   CA   ARG   66   13.406   39.828   79.561   1   28.96       3060   CB   ARG   66   12.628   40.222   78.305   1   31.16       3061   CG   ARG   66   13.486   40.877   77.24   1   36.86       3062   CD   ARG   66   12.646   41.655   76.242   1   42.52       3063   NE   ARG   66   11.525   40.876   75.708   1   48.22       3064   CZ   ARG   66   11.651   39.833   74.89   1   48.95       3065   NH1   ARG   66   12.85   39.43   74.5   1   49.65       3066   NH2   ARG   66   10.574   39.195   74.459   1   50.89       3067   C   ARG   66   12.441   39.299   80.621   1   29.09       3068   O   ARG   66   11.915   40.07   81.427   1   29.74       3069   N   SER   67   12.205   37.991   80.632   1   29.24       3070   CA   SER   67   11.297   37.425   81.617   1   32.23       3071   CB   SER   67   10.886   35.993   81.229   1   33.45       3072   OG   SER   67   11.973   35.095   81.312   1   41.58       3073   C   SER   67   11.925   37.45   83.014   1   32.16       3074   O   SER   67   11.221   37.622   84.01   1   32.1       3075   N   LYS   68   13.246   37.298   83.093   1   31.73       3076   CA   LYS   68   13.925   37.32   84.39   1   32.39       3077   CB   LYS   68   15.296   36.65   84.288   1   33.23       3078   CG   LYS   68   15.212   35.135   84.342   1   34.93       3079   CD   LYS   68   14.706   34.702   85.715   1.   39.94       3080   CE   LYS   68   14.278   33.253   85.734   1   42.89       3081   NZ   LYS   68   13.7   32.885   87.06   1   44.66       3082   C   LYS   68   14.056   38.746   84.918   1   32.83       3083   O   LYS   68   14.207   38.971   86.123   1   33.07       3084   N   ILE   69   14.003   39.711   84.009   1   31.55       3085   CA   ILE   69   14.062   41.111   84.4   1   32.25       3086   CB   ILE   69   14.544   42.002   83.232   1   30.9       3087   CG2   ILE   69   14.284   43.473   83.544   1   31.96       3088   CG1   ILE   69   16.038   41.781   82.995   1   29.61       3089   CD1   ILE   69   16.572   42.501   81.767   1   29.55       3090   C   ILE   69   12.649   41.538   84.811   1   32.64       3091   O   ILE   69   12.468   42.244   85.798   1   32.2       3092   N   ALA   70   11.656   41.083   84.051   1   33.39       3093   CA   ALA   70   10.258   41.41   84.312   1   35.22       3094   CB   ALA   70   9.386   40.918   83.162   1   34.73       3095   C   ALA   70   9.727   40.868   85.636   1   35.94       3096   O   ALA   70   8.885   41.51   86.266   1   37.17       3097   N   ASP   71   10.199   39.7   86.066   1   36.84       3098   CA   ASP   71   9.72   39.146   87.331   1   38.75       3099   CB   ASP   71   9.743   37.609   87.316   1   39.54       3100   CG   ASP   71   11.142   37.039   87.228   1   39.41       3101   OD1   ASP   71   12.106   37.693   87.669   1   38.74       3102   OD2   ASP   71   11.269   35.908   86.732   1   42.5       3103   C   ASP   71   10.519   39.665   88.519   1   39.01       3104   O   ASP   71   10.317   39.219   89.646   1   40.23       3105   N   GLY   72   11.43   40.599   88.257   1   38.37       3106   CA   GLY   72   12.226   41.182   89.322   1   37.76       3107   C   GLY   72   13.392   40.361   89.837   1   38.24       3108   O   GLY   72   13.955   40.675   90.883   1   39.38       3109   N   SER   73   13.771   39.311   89.12   1   36.99       3110   CA   SER   73   14.889   38.484   89.562   1   35.71       3111   CB   SER   73   14.876   37.139   88.837   1   35.76       3112   OG   SER   73   13.717   36.4   89.17   1   36.17       3113   C   SER   73   16.238   39.163   89.343   1   35.38       3114   O   SER   73   17.175   38.969   90.119   1   35.74       3115   N   VAL   74   16.342   39.962   88.288   1   33.87       3116   CA   VAL   74   17.598   40.636   87.994   1   32.72       3117   CB   VAL   74   18.538   39.679   87.192   1   32.82       3118   CG1   VAL   74   17.979   39.444   85.793   1   31.76       3119   CG2   VAL   74   19.946   40.242   87.131   1   34.65       3120   C   VAL   74   17.344   41.921   87.206   1   31.94       3121   O   VAL   74   16.289   42.09   86.597   1   31.01       3122   N   LYS   75   18.299   42.842   87.242   1   31.16       3123   CA   LYS   75   18.164   44.086   86.502   1   31.69       3124   CB   LYS   75   18.64   45.262   87.353   1   34.89       3125   CG   LYS   75   17.841   45.429   88.632   1   39.76       3126   CD   LYS   75   18.138   46.744   89.34   1   43.3       3127   CE   LYS   75   19.556   46.802   89.894   1   47.44       3128   NZ   LYS   75   20.595   47.115   88.867   1   49.67       3129   C   LYS   75   19.006   43.981   85.234   1   30.56       3130   O   LYS   75   19.945   43.187   85.179   1   28.43       3131   N   ARG   76   18.674   44.777   84.222   1   29.43       3132   CA   ARG   76   19.417   44.746   82.963   1   28.54       3133   CB   ARG   76   18.876   45.805   81.994   1   28.18       3134   CG   ARG   76   19.622   45.855   80.654   1   26.45       3135   CD   ARG   76   19.436   44.573   79.844   1   24.99       3136   NE   ARG   76   20.237   44.585   78.616   1   23.98       3137   CZ   ARG   76   21.497   44.164   78.535   1   24.93       3138   NH1   ARG   76   22.109   43.688   79.612   1   23.32       3139   NH2   ARG   76   22.148   44.218   77.376   1   22.71       3140   C   ARG   76   20.914   44.969   83.182   1   28.68       3141   O   ARG   76   21.749   44.296   82.574   1   28.29       3142   N   GLU   77   21.24   45.906   84.066   1   28.14       3143   CA   GLU   77   22.626   46.248   84.372   1   29.48       3144   CB   GLU   77   22.685   47.418   85.363   1   32.67       3145   CG   GLU   77   21.785   45.611   85.034   1   39.88       3146   CD   GLU   77   20.296   45.272   85.075   1   41.83       3147   OE1   GLU   77   19.857   47.607   86.031   1   44.85       3148   OE2   GLU   77   19.564   45.679   84.152   1   46.46       3149   C   GLU   77   23.404   45.071   84.961   1   27.25       3150   O   GLU   77   24.636   45.081   84.968   1   26.62       3151   N   ASP   78   22.701   44.064   85.468   1   25.71       3152   CA   ASP   78   23.39   42.917   86.05   1   26.07       3153   CB   ASP   78   22.765   42.542   87.391   1   27.02       3154   CG   ASP   78   23.043   43.589   88.462   1   30.21       3155   OD1   ASP   78   24.232   43.88   88.705   1   31.27       3156   OD2   ASP   78   22.083   44.12   89.042   1   31.19       3157   C   ASP   78   23.451   41.703   85.134   1   25.57       3158   O   ASP   78   23.765   40.591   85.562   1   25.87       3159   N   ILE   79   23.139   41.933   83.867   1   25.22       3160   CA   ILE   79   23.199   40.893   82.854   1   23.78       3161   CB   ILE   79   21.824   40.652   82.19   1   25.49       3162   CG2   ILE   79   21.984   39.762   80.955   1   25.78       3163   CG1   ILE   79   20.87   39.991   83.182   1   25.94       3164   CD1   ILE   79   21.372   38.659   83.719   1   28.17       3165   C   ILE   79   24.169   41.408   81.798   1   23.9       3166   O   ILE   79   24.05   42.551   81.35   1   24.38       3167   N   PHE   80   25.143   40.577   81.435   1   20.22       3168   CA   PHE   80   26.129   40.927   80.415   1   20.04       3169   CB   PHE   80   27.55   40.696   80.951   1   19.06       3170   CG   PHE   80   28.644   41.179   80.027   1   19.61       3171   CD1   PHE   80   29.024   40.429   78.911   1   20.29       3172   CD2   PHE   80   29.301   42.38   80.28   1   17.72       3173   CE1   PHE   80   30.051   40.869   78.055   1   17.94       3174   CE2   PHE   80   30.324   42.829   79.442   1   18.63       3175   CZ   PHE   80   30.703   42.07   78.323   1   16.39       3176   C   PHE   80   25.817   39.977   79.253   1   20.87       3177   O   PHE   80   26.037   38.77   79.347   1   20.12       3178   N   TYR   81   25.273   40.532   78.176   1   19.86       3179   CA   TYR   81   24.885   39.751   77.013   1   20.51       3180   CB   TYR   81   23.43   40.053   76.605   1   19.99       3181   CG   TYR   81   23.024   39.287   75.365   1   21.37       3182   CD1   TYR   81   22.825   37.913   75.419   1   21.54       3183   CE1   TYR   81   22.57   37.17   74.274   1   23.14       3184   CD2   TYR   81   22.948   39.915   74.123   1   22.65       3185   CE2   TYR   81   22.692   39.181   72.957   1   21.42       3186   CZ   TYR   81   22.507   37.805   73.047   1   24.06       3187   OH   TYR   81   22.271   37.046   71.922   1   23.23       3188   C   TYR   81   25.795   40.015   75.826   1   20       3189   O   TYR   81   26.017   41.166   75.442   1   20.71       3190   N   THR   82   26.309   38.934   75.248   1   18.88       3191   CA   THR   82   27.203   39.009   74.095   1   19.62       3192   CB   THR   82   28.491   38.176   74.333   1   19.73       3193   OG1   THR   82   29.211   38.708   75.45   1   20.09       3194   CG2   THR   82   29.388   38.19   73.084   1   19.44       3195   C   THR   82   26.562   38.452   72.827   1   19.88       3196   O   THR   82   25.927   37.4   72.86   1   18.43       3197   N   SER   83   26.7   39.169   71.716   1   20.07       3198   CA   SER   83   26.222   38.648   70.442   1   19.78       3199   CB   SER   83   25.044   39.442   69.887   1   22.09       3200   OG   SER   83   24.518   38.772   68.739   1   23.46       3201   C   SER   83   27.416   38.75   69.484   1   19.72       3202   O   SER   83   28.433   39.372   69.803   1   19.32       3203   N   LYS   84   27.283   38.158   68.306   1   19.04       3204   CA   LYS   84   28.367   38.162   67.349   1   19.87       3205   CB   LYS   84   29.11   36.815   67.388   1   18.7       3206   CG   LYS   84   29.415   36.276   68.799   1   20.05       3207   CD   LYS   84   30.287   35.01   68.769   1   19.48       3208   CE   LYS   84   30.471   34.415   70.169   1   18.76       3209   NZ   LYS   84   29.297   33.602   70.612   1   17.06       3210   C   LYS   84   27.89   38.433   65.929   1   18.83       3211   O   LYS   84   26.804   38.005   65.516   1   18.7       3212   N   LEU   85   28.724   39.16   65.194   1   19.54       3213   CA   LEU   85   28.465   39.516   63.803   1   20.7       3214   CB   LEU   85   29.305   40.738   63.439   1   18.63       3215   CG   LEU   85   29.321   41.146   61.962   1   20.07       3216   CD1   LEU   85   28.016   41.856   61.651   1   18.73       3217   CD2   LEU   85   30.512   42.058   61.679   1   17.83       3218   C   LEU   85   28.884   38.337   62.913   1   21.17       3219   O   LEU   85   30.053   37.95   62.918   1   20.5       3220   N   TRP   86   27.948   37.761   62.164   1   21.27       3221   CA   TRP   86   28.311   36.637   61.301   1   21.06       3222   CB   TRP   86   27.092   35.801   60.879   1   21.67       3223   CG   TRP   86   27.521   34.565   60.127   1   23.15       3224   CD2   TRP   86   28.514   33.619   60.546   1   24.43       3225   CE2   TRP   86   28.648   32.664   59.512   1   25.79       3226   CE3   TRP   86   29.304   33.485   61.701   1   24.11       3227   CD1   TRP   86   27.1   34.157   58.891   1   23.02       3228   NE1   TRP   86   27.777   33.018   58.513   1   24.76       3229   CZ2   TRP   86   29.545   31.587   59.592   1   25.02       3230   CZ3   TRP   86   30.195   32.416   61.783   1   25.95       3231   CH2   TRP   86   30.308   31.479   60.731   1   26.23       3232   C   TRP   86   29.047   37.138   60.065   1   21.57       3233   O   TRP   86   28.927   38.299   59.682   1   22.04       3234   N   SER   87   29.803   36.241   59.447   1   21.45       3235   CA   SER   87   30.638   36.538   58.291   1   22.88       3236   CB   SER   87   31.524   35.33   58.017   1   22.58       3237   OG   SER   87   32.38   35.105   59.131   1   24.59       3238   C   SER   87   29.984   36.99   56.994   1   23.13       3239   O   SER   87   30.692   37.401   56.072   1   23.03       3240   N   ASN   88   28.658   36.916   56.909   1   22.33       3241   CA   ASN   88   27.968   37.351   55.7   1   23.47       3242   CB   ASN   88   26.704   36.502   55.453   1   22.73       3243   CG   ASN   88   25.702   36.57   56.601   1   25.84       3244   OD1   ASN   88   26.029   36.995   57.706   1   25.61       3245   ND2   ASN   88   24.476   36.123   56.339   1   24.6       3246   C   ASN   88   27.616   38.832   55.824   1   24.56       3247   O   ASN   88   26.995   39.41   54.93   1   24.77       3248   N   SER   89   28.035   39.452   56.927   1   23.6       3249   CA   SER   89   27.768   40.872   57.144   1   23.68       3250   CB   SER   89   26.697   41.069   58.229   1   24.02       3251   OG   SER   89   25.433   40.577   57.794   1   25.33       3252   C   SER   89   29.019   41.665   57.508   1   22.6       3253   O   SER   89   28.953   42.624   58.285   1   23.13       3254   N   HIS   90   30.155   41.28   56.925   1   22.35       3255   CA   HIS   90   31.434   41.96   57.177   1   22.48       3256   CB   HIS   90   32.625   41.071   56.789   1   21.12       3257   CG   HIS   90   32.979   40.031   57.809   1   21.81       3258   CD2   HIS   90   32.449   39.746   59.022   1   20.99       3259   ND1   HIS   90   34.03   39.154   57.634   1   20.97       3260   CE1   HIS   90   34.135   38.377   58.697   1   20.74       3261   NE2   HIS   90   33.189   38.716   59.556   1   21.43       3262   C   HIS   90   31.586   43.286   56.431   1   23.09       3263   O   HIS   90   32.378   44.146   56.843   1   23.05       3264   N   ARG   91   30.875   43.45   55.321   1   24.36       3265   CA   ARG   91   30.989   44.701   54.574   1   24.7       3266   CB   ARG   91   30.134   44.651   53.309   1   25.26       3267   CG   ARG   91   30.635   43.625   52.294   1   27.18       3268   CD   ARG   91   29.807   43.649   51.017   1   27.88       3269   NE   ARG   91   30.241   42.614   50.083   1   30.92       3270   CZ   ARG   91   29.71   42.427   48.879   1   31.94       3271   NH1   ARG   91   28.724   43.213   48.456   1   32.98       3272   NH2   ARG   91   30.155   41.442   48.107   1   33.31       3273   C   ARG   91   30.536   45.811   55.519   1   24.43       3274   O   ARG   91   29.53   45.678   56.207   1   25.45       3275   N   PRO   92   31.281   46.925   55.565   1   25.75       3276   CD   PRO   92   32.393   47.259   54.661   1   25.11       3277   CA   PRO   92   30.972   48.062   56.439   1   26.83       3278   CB   PRO   92   31.869   49.173   55.893   1   27.11       3279   CG   PRO   92   33.043   48.415   55.379   1   28.11       3280   C   PRO   92   29.516   48.499   56.533   1   26.91       3281   O   PRO   92   29.014   48.719   57.634   1   28.31       3282   N   GLU   93   28.84   48.615   55.393   1   26.36       3283   CA   GLU   93   27.453   49.061   55.369   1   27.12       3284   CB   GLU   93   27.058   49.479   53.943   1   30.41       3285   CG   GLU   93   26.975   48.317   52.955   1   31.77       3286   CD   GLU   93   28.232   48.126   52.125   1   34.21       3287   OE1   GLU   93   29.355   48.302   52.657   1   33.1       3288   OE2   GLU   93   28.091   47.782   50.929   1   38.91       3289   C   GLU   93   26.464   48.012   55.886   1   26.86       3290   O   GLU   93   25.286   48.307   56.07   1   26.1       3291   N   LEU   94   26.941   46.794   56.134   1   25.53       3292   CA   LEU   94   26.063   45.727   56.613   1   24.95       3293   CB   LEU   94   26.336   44.432   55.835   1   24.97       3294   CG   LEU   94   26.132   44.44   54.315   1   26.65       3295   CD1   LEU   94   26.463   43.055   53.724   1   26.84       3296   CD2   LEU   94   24.688   44.813   54.008   1   25.62       3297   C   LEU   94   26.211   45.444   58.112   1   25.43       3298   O   LEU   94   25.394   44.729   58.698   1   25.96       3299   N   VAL   95   27.252   45.999   58.725   1   25.39       3300   CA   VAL   95   27.503   45.78   60.146   1   26.12       3301   CB   VAL   95   28.835   46.43   60.569   1   26.07       3302   CG1   VAL   95   29.067   46.242   62.075   1   23.48       3303   CG2   VAL   95   29.971   45.804   59.772   1   21.76       3304   C   VAL   95   26.384   46.258   61.075   1   27.44       3305   O   VAL   95   25.841   45.466   61.852   1   27.01       3306   N   ARG   96   26.03   47.539   61.007   1   27.47       3307   CA   ARG   96   24.972   48.044   61.874   1   27.84       3308   CB   ARG   96   24.822   49.561   61.722   1   29.5       3309   CG   ARG   96   23.652   50.109   62.515   1   33.27       3310   CD   ARG   96   23.873   51.547   62.916   1   37.19       3311   NE   ARG   96   22.726   52.068   63.657   1   40.47       3312   CZ   ARG   96   22.694   53.273   64.214   1   41.33       3313   NH1   ARG   96   23.747   54.074   64.113   1   41.57       3314   NH2   ARG   96   21.614   53.677   64.868   1   41.86       3315   C   ARG   96   23.626   47.34   61.633   1   27.49       3316   O   ARG   96   22.909   47.019   62.577   1   26.29       3317   N   PRO   97   23.251   47.114   60.363   1   28.66       3318   CD   PRO   97   23.763   47.712   59.116   1   27.81       3319   CA   PRO   97   21.974   46.434   60.126   1   27.05       3320   CB   PRO   97   21.888   46.403   58.603   1   27.89       3321   CG   PRO   97   22.546   47.675   58.22   1   28.33       3322   C   PRO   97   21.958   45.026   60.751   1   27.06       3323   O   PRO   97   20.917   44.556   61.212   1   25.73       3324   N   ALA   98   23.109   44.352   60.765   1   25.7       3325   CA   ALA   98   23.187   43.012   61.359   1   24.62       3326   CB   ALA   98   24.565   42.388   61.11   1   23.84       3327   C   ALA   98   22.94   43.122   62.864   1   24.52       3328   O   ALA   98   22.212   42.315   63.441   1   23.17       3329   N   LEU   99   23.558   44.115   63.496   1   23.39       3330   CA   LEU   99   23.383   44.315   64.927   1   25.24       3331   CB   LEU   99   24.316   45.418   65.447   1   24.65       3332   CG   LEU   99   24.163   45.779   66.946   1   25.76       3333   CD1   LEU   99   24.147   44.511   67.801   1   25.23       3334   CD2   LEU   99   25.305   46.686   67.364   1   25.67       3335   C   LEU   99   21.936   44.672   65.254   1   25.15       3336   O   LEU   99   21.352   44.146   66.209   1   24.56       3337   N   GLU   100   21.351   45.569   64.463   1   26.05       3338   CA   GLU   100   19.967   45.976   64.702   1   27.38       3339   CB   GLU   100   19.564   47.109   63.75   1   28.96       3340   CG   GLU   100   20.558   48.256   63.757   1   34.26       3341   CD   GLU   100   19.999   49.52   63.15   1   36.84       3342   OE1   GLU   100   19.211   49.412   62.187   1   39.85       3343   OE2   GLU   100   20.361   50.614   63.632   1   39.16       3344   C   GLU   100   19.018   44.803   64.54   1   26.48       3345   O   GLU   100   17.98   44.734   65.205   1   25.47       3346   N   ARG   101   19.374   43.868   63.666   1   25.02       3347   CA   ARG   101   18.526   42.706   63.459   1   26.35       3348   CB   ARG   101   18.981   41.941   62.219   1   30.67       3349   CG   ARG   101   18.08   40.784   61.865   1   37.33       3350   CD   ARG   101   18.547   40.148   60.582   1   43.46       3351   NE   ARG   101   17.75   38.974   60.251   1   49.79       3352   CZ   ARG   101   18.031   38.147   59.249   1   52.3       3353   NH1   ARG   101   19.092   38.372   58.484   1   52.79       3354   NH2   ARG   101   17.258   37.093   59.019   1   53.09       3355   C   ARG   101   18.553   41.802   64.696   1   24.03       3356   O   ARG   101   17.521   41.265   65.11   1   23.87       3357   N   SER   102   19.73   41.626   65.289   1   22.85       3358   CA   SER   102   19.822   40.812   66.496   1   24.12       3359   CB   SER   102   21.285   40.612   65.917   1   24.62       3360   OG   SER   102   21.924   39.627   66.121   1   25.5       3361   C   SER   102   19.043   41.493   67.631   1   22.73       3362   O   SER   102   18.311   40.835   68.371   1   24.7       3363   N   LEU   103   19.187   42.808   67.759   1   24.11       3364   CA   LEU   103   18.491   43.547   68.82   1   25.06       3365   CB   LEU   103   18.878   45.032   68.779   1   24.73       3366   CG   LEU   103   20.332   45.368   69.153   1   27.33       3367   CD1   LEU   103   20.622   46.852   68.923   1   28.57       3368   CD2   LEU   103   20.578   45.003   70.622   1   27.99       3369   C   LEU   103   16.981   43.375   68.679   1   26.5       3370   O   LEU   103   16.268   43.275   69.676   1   26.41       3371   N   LYS   104   16.492   43.327   67.443   1   27.65       3372   CA   LYS   104   15.064   43.139   67.228   1   29.21       3373   CB   LYS   104   14.711   43.375   65.76   1   32.36       3374   CG   LYS   104   13.231   43.248   65.477   1   38.44       3375   CD   LYS   104   12.852   43.925   64.174   1   42.49       3376   CE   LYS   104   11.339   44.104   64.091   1   44.61       3377   NZ   LYS   104   10.914   44.934   62.926   1   46.67       3378   C   LYS   104   14.624   41.738   67.668   1   28.63       3379   O   LYS   104   13.585   41.577   68.306   1   26.48       3380   N   ASN   105   15.411   40.721   67.33   1   28.38       3381   CA   ASN   105   15.071   39.363   67.731   1   27.47       3382   CB   ASN   105   16.046   38.356   67.112   1   27.39       3383   CG   ASN   105   15.873   38.243   65.613   1   31.53       3384   OD1   ASN   105   14.807   38.553   65.086   1   33.79       3385   ND2   ASN   105   16.907   37.792   64.922   1   32.72       3386   C   ASN   105   15.11   39.26   69.247   1   26.84       3387   O   ASN   105   14.266   38.61   69.859   1   25.99       3388   N   LEU   106   16.091   39.923   69.847   1   25.55       3389   CA   LEU   106   16.252   39.909   71.293   1   26.49       3390   CB   LEU   106   17.669   40.36   71.668   1   25.12       3391   CG   LEU   106   18.821   39.41   71.332   1   24.02       3392   CD1   LEU   106   20.099   40.203   71.186   1   25.04       3393   CD2   LEU   106   18.945   38.34   72.411   1   25.07       3394   C   LEU   106   15.256   40.81   72.013   1   27.75       3395   O   LEU   106   14.825   40.497   73.117   1   27.21       3396   N   GLN   107   14.891   41.919   71.375   1   28.43       3397   CA   GLN   107   14.003   42.898   71.983   1   30.44       3398   CB   GLN   107   12.7   42.25   72.471   1   31.92       3399   CG   GLN   107   11.698   41.979   71.352   1   35.44       3400   CD   GLN   107   11.285   43.253   70.627   1   38.8       3401   OE1   GLN   107   10.734   44.172   71.237   1   41.91       3402   NE2   GLN   107   11.552   43.317   69.324   1   37.34       3403   C   GLN   107   14.742   43.572   73.144   1   30.8       3404   O   GLN   107   14.18   43.805   74.218   I   30.82       3405   N   LEU   108   16.022   43.858   72.921   1   29.8       3406   CA   LEU   108   16.856   44.55   73.905   1   29.54       3407   CB   LEU   108   18.066   43.691   74.291   1   29.47       3408   CG   LEU   108   17.754   42.432   75.11   1   29.63       3409   CD1   LEU   108   19.025   41.629   75.352   1   29.41       3410   CD2   LEU   108   17.13   42.844   76.437   1   30.16       3411   C   LEU   108   17.312   45.839   73.222   1   29.64       3412   O   LEU   108   17.398   45.885   71.999   1   29.62       3413   N   ASP   109   17.589   46.885   73.998   1   29.32       3414   CA   ASP   109   18.014   48.161   73.428   1   29.12       3415   CB   ASP   109   17.732   49.305   74.408   1   32.9       3416   CG   ASP   109   16.255   49.429   74.75   1   37.9       3417   OD1   ASP   109   15.428   49.475   73.816   1   39.21       3418   OD2   ASP   109   15.926   49.478   75.953   1   41.44       3419   C   ASP   109   19.49   48.169   73.045   1   28.37       3420   O   ASP   109   19.927   48.987   72.236   1   27.72       3421   N   TYR   110   20.265   47.259   73.62   1   26.92       3422   CA   TYR   110   21.687   47.196   73.301   1   25.32       3423   CB   TYR   110   22.431   48.35   73.987   1   26.74       3424   CG   TYR   110   22.411   48.272   75.504   1   27.83       3425   CD1   TYR   110   21.44   48.943   76.258   1   28.23       3426   CE1   TYR   110   21.391   48.816   77.656   1   28.46       3427   CD2   TYR   110   23.337   47.475   76.182   1   27.8       3428   CE2   TYR   110   23.301   47.335   77.563   1   26.49       3429   CZ   TYR   110   22.326   48.006   78.297   1   29.94       3430   OH   TYR   110   22.297   47.835   79.66   1   30.12       3431   C   TYR   110   22.282   45.877   73.775   1   23.75       3432   O   TYR   110   21.685   45.192   74.594   1   23.32       3433   N   VAL   111   23.442   45.51   73.235   1   22.2       3434   CA   VAL   111   24.125   44.305   73.7   1   22.01       3435   CB   VAL   111   24.64   43.378   72.542   1   20.41       3436   CG1   VAL   111   23.464   42.815   71.749   1   19.23       3437   CG2   VAL   111   25.606   44.148   71.635   1   19.31       3438   C   VAL   111   25.326   44.825   74.479   1   19.32       3439   O   VAL   111   25.824   45.905   74.199   1   20.9       3440   N   ASP   112   25.79   44.061   75.456   1   19.53       3441   CA   ASP   112   26.937   44.491   76.249   1   18.48       3442   CB   ASP   112   26.95   43.71   77.552   1   18.38       3443   CG   ASP   112   25.745   44.016   78.397   1   20.85       3444   OD1   ASP   112   25.82   44.966   79.21   1   21.85       3445   OD2   ASP   112   24.72   43.326   78.221   1   20.3       3446   C   ASP   112   28.238   44.291   75.496   1   18.23       3447   O   ASP   112   29.216   45.005   75.721   1   18.75       3448   N   LEU   113   28.239   43.317   74.594   1   16.99       3449   CA   LEU   113   29.423   43   73.821   1   17.76       3450   CB   LEU   113   30.253   41.934   74.559   1   15.82       3451   CG   LEU   113   31.566   41.46   73.91   1   16.22       3452   CD1   LEU   113   32.526   42.629   73.681   1   16.89       3453   CD2   LEU   113   32.209   40.421   74.821   1   16.54       3454   C   LEU   113   29.051   42.492   72.436   1   18.74       3455   O   LEU   113   28.177   41.63   72.289   1   17.72       3456   N   TYR   114   29.711   43.041   71.421   1   18.92       3457   CA   TYR   114   29.462   42.611   70.05   1   20.62       3458   CB   TYR   114   28.854   43.742   69.229   1   19.99       3459   CG   TYR   114   28.154   43.246   67.987   1   21.84       3460   CD1   TYR   114   27.269   42.158   68.049   1   20.26       3461   CE1   TYR   114   26.561   41.737   66.916   1   22.06       3462   CD2   TYR   114   28.319   43.897   66.765   1   20.03       3463   CE2   TYR   114   27.617   43.489   65.636   1   21.15       3464   CZ   TYR   114   26.74   42.412   65.713   1   22.5       3465   OH   TYR   114   26.021   42.015   64.593   1   22.68       3466   C   TYR   114   30.805   42.202   69.471   1   19.94       3467   O   TYR   114   31.77   42.959   69.521   1   21.19       3468   N   LEU   115   30.858   40.999   68.915   1   20.18       3469   CA   LEU   115   32.105   40.478   68.379   1   20.44       3470   CB   LEU   115   32.491   39.194   69.114   1   18.82       3471   CG   LEU   115   32.475   39.126   70.637   1   19.55       3472   CD1   LEU   115   32.736   37.68   71.064   1   18.69       3473   CD2   LEU   115   33.516   40.075   71.204   1   17.11       3474   C   LEU   115   32.098   40.11   66.909   1   19.78       3475   O   LEU   115   31.073   39.705   66.368   1   21.56       3476   N   ILE   116   33.252   40.243   66.266   1   20.57       3477   CA   ILE   116   33.353   39.772   64.893   1   20.53       3478   CB   ILE   116   34.621   40.29   64.189   1   21.9       3479   CG2   ILE   116   34.868   39.468   62.9   1   21.88       3480   CG1   ILE   116   34.472   41.786   63.901   1   19.88       3481   CD1   ILE   116   35.662   42.422   63.206   1   22.71       3482   C   ILE   116   33.507   38.278   65.216   1   21.23       3483   O   ILE   116   34.426   37.886   65.936   1   20.2       3484   N   HIS   117   32.606   37.45   64.695   1   19.53       3485   CA   HIS   117   32.593   36.016   64.985   1   19.41       3486   CB   HIS   117   31.252   35.442   64.523   1   19.59       3487   CG   HIS   117   30.849   34.175   65.216   1   20.13       3488   CD2   HIS   117   31.579   33.221   65.84   1   20.21       3489   ND1   HIS   117   29.533   33.771   65.305   1   20.28       3490   CE1   HIS   117   29.469   32.625   65.96   1   20.28       3491   NE2   HIS   117   30.698   32.269   66.295   1   21.74       3492   C   HIS   117   33.724   35.17   64.404   1   20.54       3493   O   HIS   117   34.267   34.301   65.083   1   19.37       3494   N   PHE   118   34.067   35.432   63.148   1   20.26       3495   CA   PHE   118   35.109   34.687   62.446   1   21.96       3496   CB   PHE   118   34.508   33.45   61.787   1   21.65       3497   CG   PHE   118   35.52   32.395   61.462   1   24.14       3498   CD1   PHE   118   36.152   31.698   62.488   1   24.63       3499   CD2   PHE   118   35.865   32.112   60.141   1   25.78       3500   CE1   PHE   118   37.12   30.727   62.219   1   27.54       3501   CE2   PHE   118   36.841   31.137   59.85   1   26.58       3502   CZ   PHE   118   37.467   30.444   60.897   1   25.92       3503   C   PHE   118   35.677   35.631   61.386   1   22.61       3504   O   PHE   118   34.928   36.305   60.692   1   24.23       3505   N   PRO   119   37.011   35.684   61.248   1   23.82       3506   CD   PRO   119   37.979   34.889   62.026   1   23.73       3507   CA   PRO   119   37.695   36.56   60.292   1   23.42       3508   CB   PRO   119   39.131   36.565   60.81   1   22.99       3509   CG   PRO   119   39.292   35.183   61.332   1   24.47       3510   C   PRO   119   37.591   36.272   58.795   1   24.19       3511   O   PRO   119   38.026   37.084   57.981   1   26.01       3512   N   VAL   120   37.007   35.143   58.42   1   23.47       3513   CA   VAL   120   36.849   34.837   57.003   1   24.24       3514   CB   VAL   120   36.983   33.308   56.749   1   23.87       3515   CG1   VAL   120   36.682   32.989   55.294   1   26.43       3516   CG2   VAL   120   38.408   32.843   57.094   1   24.56       3517   C   VAL   120   35.463   35.34   56.57   1   23.37       3518   O   VAL   120   34.455   35.016   57.198   1   23.97       3519   N   SER   121   35.413   36.137   55.504   1   22.7       3520   CA   SER   121   34.143   36.695   55.028   1   23.83       3521   CB   SER   121   34.341   38.121   54.497   1   22.24       3522   OG   SER   121   35.203   38.894   55.312   1   25.56       3523   C   SER   121   33.482   35.885   53.911   1   24.3       3524   O   SER   121   34.176   35.29   53.091   1   24.53       3525   N   VAL   122   32.146   35.874   53.887   1   24.39       3526   CA   VAL   122   31.39   35.192   52.828   1   24.58       3527   CB   VAL   122   30.561   33.974   53.344   1   24.37       3528   CG1   VAL   122   31.495   32.91   53.92   1   22.74       3529   CG2   VAL   122   29.538   34.417   54.396   1   22.77       3530   C   VAL   122   30.432   36.211   52.195   1   27.4       3531   O   VAL   122   30.149   37.267   52.774   1   26.69       3532   N   LYS   123   29.943   35.893   51.002   1   27.42       3533   CA   LYS   123   29.036   36.773   50.267   1   29.52       3534   CB   LYS   123   28.565   36.072   48.983   1   31.01       3535   CG   LYS   123   28.977   36.762   47.688   1   39.6       3536   CD   LYS   123   30.491   36.807   47.503   1   42.6       3537   CE   LYS   123   30.862   37.461   46.18   1   46.09       3538   NZ   LYS   123   32.336   37.593   46.027   1   49.64       3539   C   LYS   123   27.801   37.219   51.052   1   29.16       3540   O   LYS   123   27.203   36.432   51.787   1   28.49       3541   N   PRO   124   27.4   38.492   50.893   1   29.8       3542   CD   PRO   124   28.141   39.529   50.148   1   30.33       3543   CA   PRO   124   26.225   39.07   51.568   1   30.53       3544   CB   PRO   124   26.174   40.495   51.012   1   30.7       3545   CG   PRO   124   27.608   40.814   50.757   1   30.68       3546   C   PRO   124   24.962   38.282   51.21   1   31.57       3547   O   PRO   124   24.876   37.725   50.119   1   31.86       3548   N   GLY   125   23.994   38.243   52.123   1   31.67       3549   CA   GLY   125   22.762   37.524   51.866   1   33.76       3550   C   GLY   125   22.178   36.898   53.122   1   36.86       3551   O   GLY   125   22.792   36.939   54.189   1   36.34       3552   N   GLU   126   20.992   36.311   53.002   1   39.29       3553   CA   GLU   126   20.342   35.689   54.147   1   42.9       3554   CB   GLU   126   18.865   35.434   53.838   1   46.46       3555   CG   GLU   126   18.069   36.709   53.588   1   51.73       3556   CD   GLU   126   16.646   36.453   53.109   1   55.45       3557   OE1   GLU   126   15.876   35.77   53.828   1   56.9       3558   OE2   GLU   126   16.294   36.944   52.008   1   58.09       3559   C   GLU   126   21.026   34.386   54.563   1   43.66       3560   O   GLU   126   21.092   34.065   55.755   1   44.91       3561   N   GLU   127   21.553   33.649   53.589   1   41.2       3562   CA   GLU   127   22.223   32.383   53.87   1   40.87       3563   CB   GLU   127   22.576   31.683   52.557   1   43.76       3564   CG   GLU   127   21.403   31.584   51.595   1   50.52       3565   CD   GLU   127   21.76   30.874   50.307   1   55.07       3566   OE1   GLU   127   22.779   31.253   49.677   1   57.17       3567   OE2   GLU   127   21.017   29.938   49.917   1   57.54       3568   C   GLU   127   23.485   32.565   54.718   1   38.27       3569   O   GLU   127   24.328   33.41   54.414   1   36.76       3570   N   VAL   128   23.611   31.769   55.779   1   35.57       3571   CA   VAL   128   24.773   31.854   56.661   1   34.51       3572   CB   VAL   128   24.544   31.089   57.991   1   35.34       3573   CG1   VAL   128   23.59   31.872   58.878   1   38.12       3574   CG2   VAL   128   23.973   29.716   57.714   1   38.24       3575   C   VAL   128   26.017   31.308   55.974   1   32.57       3576   O   VAL   128   27.115   31.817   56.17   1   30.06       3577   N   ILE   129   25.85   30.259   55.18   1   30.33       3578   CA   ILE   129   26.978   29.707   54.447   1   30.03       3579   CB   ILE   129   27.35   28.303   54.949   1   30.67       3580   CG2   ILE   129   28.459   27.72   54.081   1   32.7       3581   CG1   ILE   129   27.824   28.388   56.405   1   33.2       3582   CD1   ILE   129   28.245   27.063   57.002   1   33.76       3583   C   ILE   129   26.568   29.659   52.976   1   28.26       3584   O   ILE   129   26.003   28.673   52.511   1   27.38       3585   N   PRO   130   26.835   30.744   52.233   1   26.68       3586   CD   PRO   130   27.563   31.935   52.693   1   26.56       3587   CA   PRO   130   26.504   30.868   50.807   1   27.04       3588   CB   PRO   130   26.872   32.319   50.475   1   25.79       3589   CG   PRO   130   27.009   32.992   51.787   1   28.71       3590   C   PRO   130   27.329   29.9   49.958   1   25.77       3591   O   PRO   130   28.552   29.854   50.088   1   24.5       3592   N   LYS   131   26.656   29.146   49.093   1   24.91       3593   CA   LYS   131   27.315   28.189   48.196   1   24.79       3594   CB   LYS   131   27.078   26.756   48.675   1   26.39       3595   CG   LYS   131   27.803   26.384   49.944   1   27.51       3596   CD   LYS   131   27.34   25.031   50.427   1   33.12       3597   CE   LYS   131   28.06   24.629   51.698   1   35.52       3598   NZ   LYS   131   27.73   23.226   52.05   1   39.05       3599   C   LYS   131   26.75   28.321   46.783   1   24.19       3600   O   LYS   131   25.568   28.616   46.623   1   23.34       3601   N   ASP   132   27.581   28.108   45.759   1   22.71       3602   CA   ASP   132   27.082   28.177   44.387   1   22.22       3603   CB   ASP   132   28.198   28.52   43.383   1   20.55       3604   CG   ASP   132   29.319   27.49   43.344   1   23.23       3605   OD1   ASP   132   29.135   26.342   43.795   1   21.29       3606   OD2   ASP   132   30.396   27.85   42.827   1   23.89       3607   C   ASP   132   26.437   26.831   44.045   1   23.21       3608   O   ASP   132   26.338   25.954   44.907   1   22.1       3609   N   GLU   133   25.992   26.67   42.8   1   22.41       3610   CA   GLU   133   25.321   25.44   42.376   1   23.86       3611   CB   GLU   133   24.8   25.588   40.952   1   25.55       3612   CG   GLU   133   25.876   25.7   39.897   1   28.56       3613   CD   GLU   133   25.286   25.997   38.535   1   31.04       3614   OE1   GLU   133   24.264   25.368   38.192   1   35.64       3615   OE2   GLU   133   25.839   26.842   37.806   1   32.06       3616   C   GLU   133   26.191   24.193   42.462   1   25.26       3617   O   GLU   133   25.685   23.065   42.418   1   24.92       3618   N   ASN   134   27.5   24.391   42.582   1   23.78       3619   CA   ASN   134   28.422   23.26   42.671   1   24.13       3620   CB   ASN   134   29.594   23.475   41.708   1   22.21       3521   CG   ASN   134   29.167   23.344   40.258   1   23.78       3622   OD1   ASN   134   29.56   24.137   39.396   1   28.06       3623   ND2   ASN   134   28.352   22.337   39.98   1   20.35       3624   C   ASN   134   28.921   22.987   44.086   1   23.51       3625   O   ASN   134   29.891   22.255   44.282   1   22.18       3826   N   GLY   135   28.252   23.58   45.072   1   24.03       3627   CA   GLY   135   28.63   23.349   46.458   1   22.56       3628   C   GLY   135   29.825   24.133   46.96   1   23.83       3629   O   GLY   135   30.278   23.916   48.08   1   25.17       3630   N   LYS   136   30.345   25.047   46.153   1   22.25       3631   CA   LYS   136   31.493   25.823   46.592   1   22.88       3632   CB   LYS   136   32.27   26.385   45.399   1   22.99       3633   CG   LYS   136   32.843   25.345   44.44   1   24.46       3634   CD   LYS   136   33.627   26.015   43.311   1   24.1       3635   CE   LYS   136   34.916   26.65   43.817   1   25.34       3636   NZ   LYS   136   35.74   27.192   42.702   1   25.24       3637   C   LYS   136   31.062   26.99   47.478   1   23.81       3638   O   LYS   136   30.102   27.697   47.164   1   23.75       3639   N   ILE   137   31.774   27.179   48.586   1   22.95       3640   CA   ILE   137   31.497   28.284   49.495   1   23.81       3641   CB   ILE   137   32.44   28.287   50.719   1   26.23       3642   CG2   ILE   137   32.107   29.467   51.61   1   25.71       3643   CG1   ILE   137   32.35   26.97   51.49   1   28.54       3644   CD1   ILE   137   31.002   26.691   52.061   1   31.96       3645   C   ILE   137   31.809   29.564   48.732   1   23.61       3646   O   ILE   137   32.849   29.656   48.081   1   23.18       3647   N   LEU   138   30.921   30.547   48.812   1   22.95       3648   CA   LEU   138   31.145   31.826   48.143   1   23.74       3649   CB   LEU   138   29.815   32.423   47.677   1   23.47       3650   CG   LEU   138   29.035   31.61   46.628   1   25.27       3651   CD1   LEU   138   27.66   32.23   46.394   1   26.57       3652   CD2   LEU   138   29.836   31.573   45.335   1   25.69       3653   C   LEU   138   31.841   32.81   49.085   1   25.22       3654   O   LEU   138   31.192   33.526   49.86   1   23.71       3655   N   PHE   139   33.164   32.833   49.019   1   24.91       3656   CA   PHE   139   33.958   33.721   49.851   1   27.07       3657   CB   PHE   139   35.418   33.265   49.87   1   27.38       3658   CG   PHE   139   35.617   31.92   50.487   1   29.34       3659   CD1   PHE   139   36   30.834   49.711   1   29.28       3660   CD2   PHE   139   35.398   31.732   51.85   1   28.38       3661   CE1   PHE   139   36.161   29.575   50.283   1   30.53       3662   CE2   PHE   139   35.556   30.486   52.428   1   29.29       3663   CZ   PHE   139   35.939   29.398   51.646   1   29.9       3664   C   PHE   139   33.884   35.148   49.329   1   29.06       3665   O   PHE   139   33.672   35.376   48.137   1   27.67       3666   N   ASP   140   34.069   36.105   50.229   1   28.6       3667   CA   ASP   140   34.029   37.514   49.866   1   31.58       3668   CB   ASP   140   32.805   38.176   50.517   1   32.21       3669   CG   ASP   140   32.5   39.559   49.945   1   34.68       3670   OD1   ASP   140   32.879   39.833   48.789   1   36.23       3671   OD2   ASP   140   31.863   40.369   50.647   1   34.31       3672   C   ASP   140   35.329   38.139   50.361   1   32.82       3673   O   ASP   140   35.928   37.654   51.32   1   33.86       3674   N   THR   141   35.784   39.189   49.689   1   32.76       3675   CA   THR   141   37.013   39.86   50.087   1   33.56       3676   CB   THR   141   37.913   40.165   48.878   1   35.84       3677   OG1   THR   141   38.103   38.967   48.119   1   39.77       3678   CG2   THR   141   39.274   40.671   49.343   1   36.93       3679   C   THR   141   36.632   41.167   50.755   1   32.53       3680   O   THR   141   36.155   42.101   50.103   1   31.95       3681   N   VAL   142   36.817   41.216   52.067   1   30.52       3682   CA   VAL   142   36.49   42.41   52.82   1   27.86       3683   CB   VAL   142   35.262   42.188   53.735   1   27.77       3684   CG1   VAL   142   34.888   43.496   54.418   1   27.54       3685   CG2   VAL   142   34.082   41.656   52.923   1   26.68       3686   C   VAL   142   37.672   42.797   53.688   1   28.24       3687   O   VAL   142   38.298   41.951   54.323   1   27.91       3688   N   ASP   143   37.984   44.087   53.703   1   28.13       3689   CA   ASP   143   39.077   44.607   54.515   1   27.9       3690   CB   ASP   143   39.408   46.026   54.056   1   29.39       3691   CG   ASP   143   40.48   46.687   54.903   1   33.95       3692   OD1   ASP   143   40.951   46.073   55.887   1   33.81       3693   OD2   ASP   143   40.859   47.835   54.586   1   36.21       3694   C   ASP   143   38.536   44.623   55.945   1   26.94       3695   O   ASP   143   37.636   45.402   56.249   1   27.48       3696   N   LEU   144   39.07   43.768   56.817   1   26.33       3697   CA   LEU   144   38.581   43.706   58.195   1   26.54       3698   CB   LEU   144   39.242   42.554   58.967   1   26.97       3699   CG   LEU   144   38.81   41.135   58.56   1   29.11       3700   CD1   LEU   144   39.538   40.083   59.394   1   28.71       3701   CD2   LEU   144   37.308   41.002   58.733   1   27.25       3702   C   LEU   144   38.775   45.018   58.945   1   26.94       3703   O   LEU   144   38.077   45.287   59.921   1   27.91       3704   N   CYS   145   39.72   45.843   58.507   1   27.33       3705   CA   CYS   145   39.901   47.119   59.177   1   27.7       3706   CB   CYS   145   41.174   47.826   58.692   1   28.73       3707   SG   CYS   145   42.692   47.121   59.402   1   35.09       3708   C   CYS   145   38.667   47.99   58.945   1   26.94       3709   O   CYS   145   38.303   48.781   59.819   1   27.42       3710   N   ALA   146   38.017   47.834   57.788   1   26.6       3711   CA   ALA   146   36.804   48.599   57.47   1   25.31       3712   CB   ALA   146   36.475   48.493   55.96   1   24.37       3713   C   ALA   146   35.64   48.056   58.307   1   25.77       3714   O   ALA   146   34.75   48.806   58.733   1   25.16       3715   N   THR   147   35.64   46.743   58.526   1   24.18       3716   CA   THR   147   34.606   46.114   59.343   1   24.57       3717   CB   THR   147   34.794   44.579   59.399   1   23.82       3718   OG1   THR   147   34.774   44.053   58.065   1   25.31       3719   CG2   THR   147   33.669   43.927   60.205   1   23.43       3720   C   THR   147   34.749   46.678   60.756   1   23.55       3721   O   THR   147   33.767   47.071   61.38   1   25.57       3722   N   TRP   148   35.986   46.742   61.245   1   24.23       3723   CA   TRP   148   36.225   47.25   62.591   1   23.36       3724   CB   TRP   148   37.705   47.142   62.962   1   23.54       3725   CG   TRP   148   37.935   47.433   64.424   1   23.04       3726   CD2   TRP   148   37.494   46.631   65.531   1   22.47       3727   CE2   TRP   148   37.819   47.333   66.717   1   23.42       3728   CE3   TRP   148   36.851   45.387   65.636   1   23.18       3729   CD1   TRP   148   38.503   48.559   64.969   1   24.5       3730   NE1   TRP   148   38.433   48.506   66.348   1   23.64       3731   CZ2   TRP   148   37.521   46.833   67.993   1   23.27       3732   CZ3   TRP   148   36.553   44.889   66.911   1   23.7       3733   CH2   TRP   148   36.89   45.615   68.069   1   20.81       3734   C   TRP   148   35.749   48.694   62.756   1   25.54       3735   O   TRP   148   35.168   49.045   63.786   1   25.46       3736   N   GLU   149   35.998   49.533   61.752   1   26       3737   CA   GLU   149   35.56   50.919   61.817   1   26.33       3738   CB   GLU   149   35.969   51.665   60.544   1   28.95       3739   CG   GLU   149   37.373   52.251   60.629   1   34.18       3740   CD   GLU   149   37.939   52.684   59.289   1   37.43       3741   OE1   GLU   149   37.156   53.113   58.417   1   40.48       3742   OE2   GLU   149   39.175   52.603   59.122   1   39.38       3743   C   GLU   149   34.053   50.97   62.009   1   26.02       3744   O   GLU   149   33.544   51.756   62.816   1   27.1       3745   N   ALA   150   33.332   50.121   61.283   1   24.34       3746   CA   ALA   150   31.879   50.07   61.396   1   24.88       3747   CB   ALA   150   31.299   49.131   60.309   1   24.29       3748   C   ALA   150   31.473   49.598   62.801   1   25.38       3749   O   ALA   150   30.468   50.049   63.347   1   27.18       3750   N   MET   151   32.256   48.692   63.384   1   24.41       3751   CA   MET   151   31.977   48.193   64.732   1   24.44       3752   CB   MET   151   32.961   47.072   65.107   1   25.95       3753   CG   MET   151   32.815   45.755   64.328   1   25.68       3754   SD   MET   151   31.418   44.786   64.877   1   28.58       3755   CE   MET   151   32.086   44.047   66.384   1   26.24       3756   C   MET   151   32.131   49.347   65.737   1   24.56       3757   O   MET   151   31.332   49.488   66.66   1   24.19       3758   N   GLU   152   33.181   50.153   65.565   1   24.73       3759   CA   GLU   152   33.42   51.298   66.447   1   26.03       3760   CB   GLU   152   34.698   52.042   66.032   1   24.12       3761   CG   GLU   152   35.957   51.207   66.192   1   24.68       3762   CD   GLU   152   37.206   51.936   65.738   1   26.19       3763   OE1   GLU   152   37.132   52.656   64.721   1   28.65       3764   OE2   GLU   152   38.264   51.781   66.383   1   27.08       3765   C   GLU   152   32.228   52.255   66.422   1   26.42       3766   O   GLU   152   31.834   52.813   67.457   1   26.39       3767   N   LYS   153   31.644   52.436   65.241   1   27.2       3768   CA   LYS   153   30.493   53.322   65.109   1   26.81       3769   CB   LYS   153   30.157   53.553   63.633   1   29.05       3770   CG   LYS   153   31.166   54.436   62.922   1   30.91       3771   CD   LYS   153   30.82   54.608   61.451   1   34.68       3772   CE   LYS   153   31.836   55.496   60.749   1   38.13       3773   NZ   LYS   153   31.508   55.656   59.306   1   40.81       3774   C   LYS   153   29.285   52.771   65.843   1   26.46       3775   O   LYS   153   28.449   53.541   66.32   1   27.56       3776   N   CYS   154   29.176   51.443   65.937   1   25.25       3777   CA   CYS   154   28.055   50.85   66.664   1   25.09       3778   CB   CYS   154   27.961   49.342   66.401   1   27       3779   SG   CYS   154   27.428   48.921   64.727   1   30.45       3780   C   CYS   154   28.218   51.112   68.159   1   24.11       3781   O   CYS   154   27.233   51.294   68.873   1   24.83       3782   N   LYS   155   29.459   51.123   68.637   1   25.55       3783   CA   LYS   155   29.712   51.406   70.047   1   25.51       3784   CB   LYS   155   31.176   51.138   70.403   1   25.73       3785   CG   LYS   155   31.558   51.53   71.826   1   26.92       3786   CD   LYS   155   32.978   51.09   72.153   1   27.35       3787   CE   LYS   155   33.507   51.759   73.421   1   26.92       3788   NZ   LYS   155   32.652   51.476   74.608   1   29.16       3789   C   LYS   155   29.368   52.878   70.301   1   27.65       3790   O   LYS   155   28.662   53.199   71.257   1   27.97       3791   N   ASP   156   29.856   53.773   69.448   1   28.02       3792   CA   ASP   156   29.55   55.192   69.62   1   28.95       3793   CB   ASP   156   30.254   56.034   68.556   1   30.46       3794   CG   ASP   156   31.73   56.195   68.839   1   31.41       3795   OD1   ASP   156   32.116   56.124   70.024   1   34.3       3796   OD2   ASP   156   32.506   56.408   67.894   1   35       3797   C   ASP   156   28.054   55.468   69.579   1   28.87       3798   O   ASP   156   27.569   56.36   70.273   1   29.89       3799   N   ALA   157   27.322   54.698   68.776   1   27.44       3800   CA   ALA   157   25.878   54.874   68.652   1   27.79       3801   CB   ALA   157   25.371   54.178   67.384   1   28.15       3802   C   ALA   157   25.159   54.318   69.875   1   28.12       3803   O   ALA   157   23.952   54.493   70.029   1   29.4       3804   N   GLY   158   25.907   53.632   70.736   1   26.76       3805   CA   GLY   158   25.32   53.064   71.934   1   26.83       3806   C   GLY   158   24.639   51.713   71.758   1   26.48       3807   O   GLY   158   24.021   51.221   72.7   1   26.46       3808   N   LEU   159   24.751   51.102   70.578   1   24.65       3809   CA   LEU   159   24.11   49.804   70.324   1   24.26       3810   CB   LEU   159   23.961   49.568   68.813   1   24.47       3811   CG   LEU   159   23.131   50.604   68.044   1   26.75       3812   CD1   LEU   159   23.265   50.386   66.538   1   28.57       3813   CD2   LEU   159   21.683   50.501   68.475   1   27.65       3814   C   LEU   159   24.886   48.637   70.957   1   23.19       3815   O   LEU   159   24.311   47.6   71.281   1   22.64       3816   N   ALA   160   26.189   48.824   71.116   1   22.81       3817   CA   ALA   160   27.065   47.827   71.716   1   23.53       3818   CB   ALA   160   27.972   47.197   70.653   1   20.98       3819   C   ALA   160   27.897   48.587   72.738   1   24.49       3820   O   ALA   160   28.546   49.573   72.394   1   25.77       3821   N   LYS   161   27.874   48.15   73.994   1   23.46       3822   CA   LYS   161   28.641   48.84   75.031   1   23.07       3823   CB   LYS   161   28.213   48.339   76.414   1   25.71       3824   CG   LYS   161   26.784   48.701   76.804   1   27.04       3825   CD   LYS   161   26.609   50.209   76.937   1   32.62       3826   CE   LYS   161   25.24   50.561   77.52   1   36.11       3827   NZ   LYS   161   25.07   52.027   77.77   1   38.63       3828   C   LYS   161   30.139   48.63   74.826   1   22.81       3829   O   LYS   161   30.946   49.544   75.02   1   21.97       3830   N   SER   162   30.51   47.413   74.433   1   20.99       3831   CA   SER   162   31.908   47.065   74.173   1   20.14       3832   CB   SER   162   32.482   46.209   75.314   1   20.7       3833   OG   SER   162   32.534   46.928   76.547   1   20.56       3834   C   SER   162   31.964   46.249   72.876   1   20.23       3835   O   SER   162   30.967   45.65   72.471   1   20.14       3836   N   ILE   163   33.122   46.23   72.228   1   19.07       3837   CA   ILE   163   33.286   45.473   70.997   1   19.95       3838   CB   ILE   163   33.313   46.399   69.746   1   18.17       3839   CG2   ILE   163   31.924   46.98   69.504   1   18.41       3840   CG1   ILE   163   34.344   47.514   69.929   1   22.18       3841   CD1   ILE   163   34.512   48.422   68.692   1   21.93       3842   C   ILE   163   34.575   44.668   71.085   1   19.93       3843   O   ILE   163   35.538   45.082   71.733   1   19.82       3844   N   GLY   164   34.581   43.496   70.462   1   19.44       3845   CA   GLY   164   35.766   42.66   70.506   1   18.53       3846   C   GLY   164   35.798   41.737   69.308   1   19.86       3847   O   GLY   164   35.051   41.931   68.351   1   18.58       3848   N   VAL   165   36.649   40.722   69.365   1   20.23       3849   CA   VAL   165   36.767   39.782   68.267   1   20.23       3850   CB   VAL   165   38.089   40.001   67.491   1   20.54       3851   CG1   VAL   165   38.11   41.402   66.883   1   19.71       3852   CG2   VAL   165   39.283   39.813   68.427   1   19.59       3853   C   VAL   165   36.728   38.352   68.775   1   21.06       3854   O   VAL   165   36.782   38.094   69.981   1   20.22       3855   N   SER   166   36.62   37.419   67.838   1   20.87       3856   CA   SER   166   36.584   36.013   68.174   1   20.65       3857   CB   SER   166   35.138   35.52   68.225   1   21.36       3858   OG   SER   166   35.07   34.163   68.626   1   22.02       3859   C   SER   166   37.351   35.273   67.09   1   22.23       3860   O   SER   166   37.302   35.652   65.922   1   21.99       3861   N   ASN   167   38.075   34.233   67.482   1   20.96       3862   CA   ASN   167   38.841   33.435   66.542   1   22.06       3863   CB   ASN   167   37.893   32.728   65.569   1   22.09       3864   CG   ASN   167   37.015   31.708   66.264   1   21.04       3865   OD1   ASN   167   37.518   30.823   66.95   1   23.3       3866   ND2   ASN   167   35.7   31.829   66.099   1   18.81       3867   C   ASN   167   39.902   34.217   65.774   1   23.1       3868   O   ASN   167   40.18   33.922   64.613   1   23.82       3869   N   PHE   168   40.493   35.214   66.421   1   23.08       3870   CA   PHE   168   41.555   35.99   65.794   1   24.03       3871   CB   PHE   168   41.473   37.47   66.192   1   22.46       3872   CG   PHE   168   40.657   38.319   65.247   1   22.17       3873   CD1   PHE   168   39.416   37.888   64.79   1   21.07       3874   CD2   PHE   168   41.126   39.568   64.835   1   21.91       3875   CE1   PHE   168   38.648   38.688   63.932   1   20.2       3876   CE2   PHE   168   40.373   40.374   63.982   1   20.38       3877   CZ   PHE   168   39.131   39.929   63.531   1   21.38       3878   C   PHE   168   42.886   35.428   66.259   1   24.86       3879   O   PHE   168   42.995   34.912   67.372   1   25.03       3880   N   ASN   169   43.898   35.513   65.4   1   24.63       3881   CA   ASN   169   45.225   35.045   65.77   1   24.45       3882   CB   ASN   169   45.829   34.148   64.673   1   24.35       3883   CG   ASN   169   45.875   34.831   63.313   1   25.59       3884   OD1   ASN   169   45.86   36.064   63.219   1   26.35       3885   ND2   ASN   169   45.953   34.029   62.252   1   25.28       3886   C   ASN   169   45.079   36.283   65.986   1   24.06       3887   O   ASN   169   45.585   37.406   65.891   1   23.88       3888   N   HIS   170   47.355   36.066   66.287   1   26.3       3889   CA   HIS   170   48.32   37.137   66.533   1   28.53       3890   CB   HIS   170   49.71   36.504   66.738   1   32.78       3891   CG   HIS   170   50.839   37.486   66.77   1   36.15       3892   CD2   HIS   170   51.968   37.569   66.027   1   37.07       3893   ND1   HIS   170   50.888   38.538   67.66   1   39.45       3894   CE1   HIS   170   51.998   39.229   67.461   1   38.47       3895   NE2   HIS   170   52.671   38.662   66.476   1   39.51       3896   C   HIS   170   48.363   38.167   65.403   1   29.3       3897   O   HIS   170   48.24   39.375   65.635   1   29.28       3898   N   ARG   171   48.536   37.681   64.179   1   29.9       3899   CA   ARG   171   48.61   38.542   63.001   1   30.1       3900   CB   ARG   171   48.852   37.671   61.761   1   33.25       3901   CG   ARG   171   48.681   38.377   60.422   1   39.56       3902   CD   ARG   171   48.92   37.41   59.258   1   43.94       3903   NE   ARG   171   47.972   37.627   58.165   1   49.18       3904   CZ   ARG   171   46.67   37.368   58.247   1   51.35       3905   NH1   ARG   171   45.164   36.878   59.371   1   55.28       3906   NH2   ARG   171   45.868   37.608   57.216   1   52.41       3907   C   ARG   171   47.359   39.408   62.814   1   28.39       3908   O   ARG   171   47.463   40.612   62.588   1   29.64       3909   N   LEU   172   46.178   38.803   62.914   1   26.33       3910   CA   LEU   172   44.938   39.557   62.741   1   25.38       3911   CB   LEU   172   43.747   38.603   62.663   1   24.79       3912   CG   LEU   172   43.709   37.762   61.383   1   26.34       3913   CD1   LEU   172   42.624   36.711   61.48   1   25.89       3914   CD2   LEU   172   43.47   38.669   60.191   1   28.91       3915   C   LEU   172   44.717   40.582   63.849   1   25.71       3916   O   LEU   172   44.188   41.669   63.606   1   25.08       3917   N   LEU   173   45.115   40.232   65.066   1   26.74       3918   CA   LEU   173   44.969   41.138   66.198   1   27.55       3919   CB   LEU   173   45.348   40.409   67.495   1   29.17       3920   CG   LEU   173   44.306   40.19   68.604   1   31.02       3921   CD1   LEU   173   42.906   40.038   68.069   1   32.02       3922   CD2   LEU   173   44.72   38.965   69.392   1   30.16       3923   C   LEU   173   45.889   42.337   65.956   1   29.71       3924   O   LEU   173   45.485   43.49   66.117   1   28.42       3925   N   GLU   174   47.124   42.058   65.545   1   31.33       3926   CA   GLU   174   48.094   43.113   65.27   1   33.6       3927   CB   GLU   174   49.42   42.503   64.813   1   37.04       3928   CG   GLU   174   50.62   43.353   65.18   1   45.07       3929   CD   GLU   174   50.99   43.222   66.642   1   47.57       3930   OE1   GLU   174   51.704   42.248   66.974   1   49.93       3931   OE2   GLU   174   50.56   44.079   67.455   1   50.39       3932   C   GLU   174   47.567   44.066   64.192   1   32.62       3933   O   GLU   174   47.746   45.289   64.28   1   32.33       3934   N   MET   175   48.918   43.5   63.178   1   31.67       3935   CA   MET   175   46.35   44.291   62.089   1   32.26       3936   CB   MET   175   48.595   43.379   61.114   1   34.26       3937   CG   MET   175   44.954   44.113   59.946   1   38.06       3938   SD   MET   175   43.842   43.057   58.977   1   44.03       3939   CE   MET   175   44.985   42.348   57.82   1   42.23       3940   C   MET   175   45.4   48.356   62.645   1   31.22       3941   O   MET   175   45.469   46.525   62.259   1   31.12       3942   N   ILE   176   44.518   44.948   63.556   1   29.2       3943   CA   ILE   176   43.56   45.873   64.169   1   29.44       3944   CB   ILE   176   42.487   45.126   65.013   1   29.2       3945   CG2   ILE   176   41.531   46.13   65.656   1   26.57       3946   CG1   ILE   176   41.711   44.145   64.13   1   29.65       3947   CD1   ILE   176   41.039   44.797   62.933   1   32.17       3948   C   ILE   176   44.25   46.874   65.091   1   29.17       3949   O   ILE   176   43.992   48.069   65.013   1   29.18       3950   N   LEU   177   48.121   46.38   65.968   1   29.28       3951   CA   LEU   177   45.818   47.246   66.909   1   30.31       3952   CB   LEU   177   46.686   46.411   67.853   1   29.49       3953   CG   LEU   177   45.926   46.469   68.798   1   29.49       3954   CD1   LEU   177   46.925   44.666   69.627   1   29.17       3955   CD2   LEU   177   44.999   46.283   69.707   1   29.94       3956   C   LEU   177   46.678   48.318   66.241   1   32.67       3957   O   LEU   177   46.811   49.426   66.762   1   32.4       3958   N   ASN   178   47.258   47.993   65.09   1   33.5       3959   CA   ASN   178   48.109   48.946   64.387   1   34.66       3960   CB   ASN   178   49.302   48.227   63.754   1   35.62       3961   CG   ASN   178   50.198   47.572   64.788   1   39.47       3962   OD1   ASN   178   50.574   48.196   65.781   1   41.76       3963   ND2   ASN   178   50.546   46.311   64.563   1   39.83       3964   C   ASN   178   47.353   49.727   63.32   1   34.67       3965   O   ASN   178   47.949   50.492   62.563   1   35.38       3966   N   LYS   179   46.043   49.537   63.264   1   33.89       3967   CA   LYS   179   45.226   50.237   62.293   1   34.68       3968   CB   LYS   179   43.771   49.784   62.406   1   33.92       3969   CG   LYS   179   42.814   50.569   61.545   1   35.62       3970   CD   LYS   179   41.389   50.295   61.965   1   36.18       3971   CE   LYS   179   40.447   51.217   61.248   1   39.1       3972   NZ   LYS   179   40.762   52.641   61.55   1   38.7       3973   C   LYS   179   45.299   51.746   62.505   1   35.14       3974   O   LYS   179   45.16   52.239   63.623   1   35.3       3975   N   PRO   180   45.529   52.505   61.427   1   35.67       3976   CD   PRO   180   45.81   52.083   60.04   1   35.36       3977   CA   PRO   180   45.601   53.962   61.57   1   33.66       3978   CB   PRO   180   46.109   54.415   60.2   1   34.48       3979   CG   PRO   180   45.559   53.355   59.265   1   36.41       3980   C   PRO   180   44.23   54.539   61.922   1   32.96       3981   O   PRO   180   43.209   54.124   61.37   1   34.61       3982   N   GLY   181   44.207   55.485   62.855   1   32.23       3983   CA   GLY   181   42.949   56.091   63.252   1   32.13       3984   C   GLY   181   42.122   55.246   64.209   1   31.18       3985   O   GLY   181   40.968   55.571   64.479   1   32.43       3986   N   LEU   182   42.711   54.168   64.724   1   30.98       3987   CA   LEU   182   42.024   53.267   65.654   1   30.49       3988   CB   LEU   182   43.005   52.225   66.209   1   30.27       3989   CG   LEU   182   42.43   51.214   67.214   1   28.84       3990   CD1   LEU   182   41.506   50.263   66.485   1   28.21       3991   CD2   LEU   182   43.555   50.434   67.877   1   28.47       3992   C   LEU   182   41.404   54.028   66.818   1   30.66       3993   O   LEU   182   42.079   54.801   67.495   1   30.34       3994   N   LYS   183   40.119   53.807   67.059   1   30.58       3995   CA   LYS   183   39.45   54.491   68.151   1   30.53       3996   CB   LYS   183   38.082   54.983   67.688   1   31.75       3997   CG   LYS   183   37.414   55.943   68.649   1   36.09       3998   CD   LYS   183   36.183   56.587   68.024   1   38.57       3999   CE   LYS   183   35.55   57.61   68.967   1   39.87       4000   NZ   LYS   183   34.336   58.238   68.365   1   40.74       4001   C   LYS   183   39.306   53.584   69.376   1   30.95       4002   O   LYS   183   39.57   54.005   70.501   1   30.93       4003   N   TYR   184   38.904   52.336   69.16   1   29.62       4004   CA   TYR   184   38.717   51.395   70.264   1   28.68       4005   CB   TYR   184   37.223   51.122   70.467   1   28.02       4006   CG   TYR   184   36.38   52.35   70.696   1   28.43       4007   CD1   TYR   184   36.605   53.166   71.804   1   28.38       4008   CE1   TYR   184   35.809   54.279   72.051   1   30.14       4009   CD2   TYR   184   35.333   52.681   69.832   1   27.4       4010   CE2   TYR   184   34.528   53.802   70.072   1   28.51       4011   CZ   TYR   184   34.774   54.592   71.184   1   29.78       4012   OH   TYR   184   33.988   55.698   71.441   1   31.05       4013   C   TYR   184   39.392   50.074   69.962   1   28.58       4014   O   TYR   184   39.149   49.482   68.912   1   28.67       4015   N   LYS   185   40.248   49.584   70.845   1   26.76       4016   CA   LYS   185   40.812   48.299   70.508   1   29.06       4017   CB   LYS   185   42.232   48.14   71.053   1   31.4       4018   CG   LYS   185   42.447   48.535   72.458   1   33.76       4019   CD   LYS   185   43.942   48.577   72.706   1   34.8       4020   CE   LYS   185   44.251   49.368   74.171   1   36.57       4021   NZ   LYS   185   46.708   48.162   74.404   1   35.78       4022   C   LYS   185   39.873   47.213   71.011   1   26.11       4023   O   LYS   185   38.944   47.494   71.761   1   26.29       4024   N   PRO   186   40.051   45.973   70.542   1   24.89       4025   CD   PRO   186   40.938   45.496   69.463   1   25.78       4026   CA   PRO   186   39.158   44.904   71.009   1   24.29       4027   CB   PRO   186   39.651   43.679   70.241   1   23.54       4028   CG   PRO   186   40.209   44.261   68.978   1   26.3       4029   C   PRO   186   39.279   44.715   72.525   1   22.36       4030   O   PRO   186   40.38   44.766   73.067   1   22.48       4031   N   VAL   187   35.161   44.503   73.213   1   21.95       4032   CA   VAL   187   38.242   44.31   74.658   1   20.67       4033   CB   VAL   187   36.91   44.662   75.404   1   21.13       4034   CG1   VAL   187   36.523   46.125   75.154   1   20.89       4035   CG2   VAL   187   35.786   43.718   74.977   1   17.82       4036   C   VAL   187   38.575   42.847   74.943   1   21.82       4037   O   VAL   187   39.071   42.514   76.02   1   20.83       4038   N   CYS   188   38.312   41.971   73.975   1   20.74       4039   CA   CYS   188   38.584   40.55   74.167   1   20.17       4040   CB   CYS   188   37.429   39.887   74.933   1   20.49       4041   SG   CYS   188   35.87   39.834   73.928   1   23.03       4042   C   CYS   188   38.744   39.792   72.856   1   20.41       4043   O   CYS   188   38.411   40.284   71.772   1   21.33       4044   N   ASN   189   39.255   38.574   72.983   1   20.08       4045   CA   ASN   189   39.401   37.666   71.856   1   18.81       4046   CB   ASN   189   40.875   37.51   71.45   1   20.01       4047   CG   ASN   189   41.048   36.651   70.213   1   20.57       4048   OD1   ASN   189   40.092   36.411   69.482   1   18.3       4049   ND2   ASN   189   42.279   36.189   69.966   1   21.29       4050   C   ASN   189   38.835   36.351   72.38   1   19.18       4051   O   ASN   189   39.42   35.721   73.272   1   20.26       4052   N   GLN   190   37.679   35.95   71.853   1   18.43       4053   CA   GLN   190   37.053   34.705   72.29   1   17.94       4054   CB   GLN   190   35.526   34.805   72.222   1   17.13       4055   CG   GLN   190   34.827   33.558   72.778   1   18.21       4056   CD   GLN   190   33.318   33.569   72.608   1   20.51       4057   OE1   GLN   190   32.737   32.648   72.015   1   21.14       4058   NE2   GLN   190   32.67   34.598   73.137   1   19.04       4059   C   GLN   190   37.549   33.574   71.394   1   19.36       4060   O   GLN   190   37.243   33.537   70.201   1   19.38       4061   N   VAL   191   38.317   32.657   71.976   1   20.07       4062   CA   VAL   191   38.893   31.537   71.236   1   20.61       4063   CB   VAL   191   40.406   31.763   70.963   1   21.77       4064   CG1   VAL   191   40.61   32.976   70.066   1   20.92       4065   CG2   VAL   191   41.148   31.96   72.283   1   22.75       4066   C   VAL   191   38.764   30.219   71.99   1   22.39       4067   O   VAL   191   38.426   30.191   73.171   1   20.27       4068   N   GLU   192   39.037   29.119   71.296   1   22.19       4069   CA   GLU   192   38.985   27.808   71.921   1   22.65       4070   CB   GLU   192   39.198   26.705   70.879   1   23.46       4071   CG   GLU   192   39.096   25.296   71.45   1   23.93       4072   CD   GLU   192   39.269   24.213   70.392   1   27.4       4073   OE1   GLU   192   38.971   24.478   69.205   1   26.23       4074   OE2   GLU   192   39.692   23.095   70.759   1   28.5       4075   C   GLU   192   40.116   27.751   72.943   1   21.32       4076   O   GLU   192   41.24   28.144   72.642   1   21.7       4077   N   CYS   193   39.827   27.26   74.145   1   21.5       4078   CA   CYS   193   40.866   27.178   75.172   1   22.88       4079   CB   CYS   193   41.114   28.56   75.781   1   22.37       4080   SG   CYS   193   42.63   28.647   76.765   1   23.81       4081   C   CYS   193   40.486   26.175   76.258   1   23.67       4082   O   CYS   193   39.407   26.256   76.842   1   23.76       4083   N   HIS   194   41.382   25.227   76.518   1   23.84       4084   CA   HIS   194   41.154   24.183   77.514   1   23.63       4085   CB   HIS   194   40.15   23.161   76.986   1   24.05       4086   CG   HIS   194   40.487   22.638   75.622   1   26.96       4087   CD2   HIS   194   41.398   21.722   75.222   1   25.41       4088   ND1   HIS   194   39.897   23.119   74.471   1   27.77       4089   CE1   HIS   194   40.434   22.523   73.42   1   26.58       4090   NE2   HIS   194   41.349   21.671   73.849   1   28.41       4091   C   HIS   194   42.499   23.513   77.806   1   24.5       4092   O   HIS   194   43.505   23.832   77.166   1   23.35       4093   N   PRO   195   42.539   22.581   78.775   1   25.61       4094   CD   PRO   195   41.455   22.199   79.699   1   25.15       4095   CA   PRO   195   43.788   21.896   79.131   1   25.96       4096   CB   PRO   195   43.337   20.907   80.204   1   25.74       4097   CG   PRO   195   42.227   21.645   80.88   1   26.84       4098   C   PRO   195   44.558   21.219   77.984   1   26.11       4099   O   PRO   195   45.774   21.046   78.076   1   26.88       4100   N   TYR   196   43.866   20.824   76.919   1   26.9       4101   CA   TYR   196   44.554   20.189   75.799   1   28.74       4102   CB   TYR   196   43.668   19.137   75.132   1   29.05       4103   CG   TYR   196   43.501   17.855   75.931   1   32.1       4104   CD1   TYR   196   44.364   17.538   76.99   1   31.26       4105   CE1   TYR   196   44.219   16.349   77.707   1   32.71       4106   CD2   TYR   196   42.491   16.947   75.61   1   31.29       4107   CE2   TYR   196   42.337   15.759   76.315   1   34.06       4108   CZ   TYR   196   43.203   15.466   77.361   1   33.36       4109   OH   TYR   196   43.044   14.296   78.056   1   32.95       4110   C   TYR   196   45.021   21.198   74.755   1   29.92       4111   O   TYR   196   45.707   20.84   73.786   1   30.07       4112   N   PHE   197   44.651   22.457   74.957   1   27.87       4113   CA   PHE   197   45.037   23.534   74.052   1   28.15       4114   CB   PHE   197   44.062   23.578   72.873   1   29.53       4115   CG   PHE   197   44.614   24.257   71.654   1   32.44       4116   CD1   PHE   197   45.608   23.647   70.894   1   35.41       4117   CD2   PHE   197   44.156   25.514   71.276   1   34.16       4118   CE1   PHE   197   46.142   24.28   69.772   1   36.3       4119   CE2   PHE   197   44.681   26.162   70.156   1   35.95       4120   CZ   PHE   197   45.677   25.543   69.402   1   37.51       4121   C   PHE   197   44.936   24.806   74.897   1   27.74       4122   O   PHE   197   44.017   25.605   74.716   1   26.07       4123   N   ASN   198   45.894   24.994   75.806   1   27.1       4124   CA   ASN   198   45.853   26.127   76.729   1   27.05       4125   CB   ASN   198   46.695   25.824   77.982   1   27.21       4126   CG   ASN   198   48.183   25.776   77.706   1   26.26       4127   OD1   ASN   198   48.71   26.569   76.933   1   28.28       4128   ND2   ASN   198   48.873   24.857   78.368   1   26.2       4129   C   ASN   198   46.175   27.516   76.192   1   25.79       4130   O   ASN   198   46.119   28.483   76.94   1   24.41       4131   N   GLN   199   46.501   27.615   74.906   1   24.83       4132   CA   GLN   199   46.762   28.912   74.267   1   26.02       4133   CB   GLN   199   45.43   29.658   74.1   1   25.23       4134   CG   GLN   199   44.393   28.922   73.261   1   25.22       4135   CD   GLN   199   44.459   29.298   71.789   1   25.4       4136   OE1   GLN   199   45.507   29.709   71.29   1   25.86       4137   NE2   GLN   199   43.337   29.151   71.087   1   22.14       4138   C   GLN   199   47.742   29.827   74.99   1   26.7       4139   O   GLN   199   47.62   31.046   74.898   1   26.57       4140   N   ARG   200   48.711   29.252   75.694   1   28.09       4141   CA   ARG   200   49.685   30.044   76.448   1   28.58       4142   CB   ARG   200   50.799   29.127   76.969   1   32.25       4143   CG   ARG   200   51.638   29.701   78.105   1   37.74       4144   CD   ARG   200   53.07   29.962   77.65   1   44.51       4145   NE   ARG   200   53.199   31.263   76.995   1   48.39       4146   CZ   ARG   200   54.276   31.669   76.326   1   49.74       4147   NH1   ARG   200   55.329   30.869   76.212   1   51.15       4148   NH2   ARG   200   54.301   32.881   75.781   1   49.06       4149   C   ARG   200   50.286   31.22   75.664   1   28.41       4150   O   ARG   200   50.319   32.345   76.165   1   26.45       4151   N   LYS   201   50.748   30.978   74.436   1   26.72       4152   CA   LYS   201   51.342   32.061   73.649   1   28.31       4153   CB   LYS   201   51.937   31.532   72.34   1   30.68       4154   CG   LYS   201   53.237   30.755   72.486   1   37.8       4155   CD   LYS   201   53.801   30.401   71.105   1   41.9       4156   CE   LYS   201   55.059   29.54   71.184   1   45.86       4157   NZ   LYS   201   56.18   30.229   71.887   1   49.34       4158   C   LYS   201   50.361   33.188   73.329   1   26.58       4159   O   LYS   201   50.688   34.363   73.487   1   26.98       4160   N   LEU   202   49.163   32.828   72.871   1   25.85       4161   CA   LEU   202   48.147   33.823   72.53   1   23.91       4162   CB   LEU   202   46.952   33.153   71.846   1   23.65       4163   CG   LEU   202   45.819   34.079   71.381   1   23.7       4164   CD1   LEU   202   46.368   35.186   70.498   1   25.46       4165   CD2   LEU   202   44.773   33.273   70.623   1   24.46       4166   C   LEU   202   47.688   34.557   73.786   1   23.51       4167   O   LEU   202   47.484   35.773   73.763   1   23.97       4168   N   LEU   203   47.538   33.822   74.885   1   21.67       4169   CA   LEU   203   47.126   34.434   76.149   1   22.3       4170   CB   LEU   203   46.95   33.355   77.234   1   20.74       4171   CG   LEU   203   46.642   33.809   78.676   1   23.3       4172   CD1   LEU   203   45.375   34.669   78.715   1   19.67       4173   CD2   LEU   203   46.471   32.56   79.568   1   20.64       4174   C   LEU   203   48.128   35.5   76.602   1   22.71       4175   O   LEU   203   47.733   36.609   76.969   1   23.72       4176   N   ASP   204   49.425   35.187   76.577   1   23.56       4177   CA   ASP   204   50.419   36.192   76.987   1   24.12       4178   CB   ASP   204   51.842   35.608   77.013   1   26.09       4179   CG   ASP   204   52.115   34.791   78.266   1   27.99       4180   OD1   ASP   204   51.489   35.077   79.306   1   28.64       4181   OD2   ASP   204   52.963   33.875   78.217   1   29.69       4182   C   ASP   204   50.387   37.398   76.059   1   23.51       4183   O   ASP   204   50.542   38.534   76.503   1   23.91       4184   N   PHE   205   50.187   37.158   74.765   1   24.98       4185   CA   PHE   205   50.121   38.274   73.833   1   23.38       4186   CB   PHE   205   49.938   37.798   72.391   1   24.99       4187   CG   PHE   205   49.765   38.929   71.412   1   26.81       4188   CD1   PHE   205   50.83   39.768   71.098   1   26.99       4189   CD2   PHE   205   48.526   39.196   70.856   1   26.55       4190   CE1   PHE   205   50.66   40.864   70.246   1   26.8       4191   CE2   PHE   205   48.346   40.292   70.003   1   30.13       4192   CZ   PHE   205   49.42   41.124   69.702   1   27.73       4193   C   PHE   205   48.949   39.181   74.203   1   22.42       4194   O   PHE   205   49.099   40.398   74.291   1   22.75       4195   N   CYS   206   47.778   38.59   74.413   1   22.27       4196   CA   CYS   206   46.602   39.375   74.774   1   23.67       4197   CB   CYS   206   45.366   38.472   74.882   1   24.33       4198   SG   CYS   206   44.75   37.884   73.267   1   27.76       4199   C   CYS   206   46.808   40.156   76.07   1   22.4       4200   O   CYS   206   46.44   41.326   76.156   1   22.26       4201   N   LYS   207   47.391   39.513   77.077   1   24.23       4202   CA   LYS   207   47.652   40.19   78.346   1   24.63       4203   CB   LYS   207   48.292   39.22   79.342   1   25.13       4204   CG   LYS   207   47.317   38.231   79.935   1   25.83       4205   CD   LYS   207   48.005   37.272   80.885   1   27.27       4206   CE   LYS   207   46.982   36.367   81.564   1   27.36       4207   NZ   LYS   207   47.631   35.354   82.45   1   29.94       4208   C   LYS   207   48.568   41.397   78.161   1   24.44       4209   O   LYS   207   48.386   42.438   78.803   1   25.58       4210   N   SER   208   49.561   41.264   77.286   1   25.32       4211   CA   SER   208   50.494   42.367   77.056   1   25.46       4212   CB   SER   208   51.665   41.91   76.174   1   26.22       4213   OG   SER   208   51.275   41.759   74.818   1   28.33       4214   C   SER   208   49.78   43.562   76.416   1   26.12       4215   O   SER   208   50.264   44.688   76.494   1   26.43       4216   N   LYS   209   48.617   43.325   75.811   1   25.6       4217   CA   LYS   209   47.859   44.407   75.177   1   26.57       4218   CB   LYS   209   47.482   44.016   73.745   1   28.83       4219   CG   LYS   209   48.671   43.646   72.86   1   30.87       4220   CD   LYS   209   49.64   44.82   72.704   1   32.82       4221   CE   LYS   209   50.844   44.434   71.84   1   35.79       4222   NZ   LYS   209   51.782   45.579   71.616   1   36.64       4223   C   LYS   209   46.581   44.74   75.958   1   27.27       4224   O   LYS   209   45.757   45.53   75.506   1   27.83       4225   N   ASP   210   46.444   44.143   77.14   1   26.43       4226   CA   ASP   210   45.277   44.319   78.004   1   27.2       4227   CB   ASP   210   45.101   45.768   78.49   1   28.75       4228   CG   ASP   210   44.099   45.864   79.648   1   31.15       4229   OD1   ASP   210   43.425   46.907   79.819   1   31.49       4230   OD2   ASP   210   43.995   44.873   80.404   1   32.66       4231   C   ASP   210   44.001   43.877   77.295   1   25.84       4232   O   ASP   210   42.953   44.528   77.381   1   26.31       4233   N   ILE   211   44.109   42.772   76.571   1   23.64       4234   CA   ILE   211   42.969   42.195   75.879   1   22.21       4235   CB   ILE   211   43.326   41.807   74.424   1   23       4236   CG2   ILE   211   42.18   41   73.797   1   20.67       4237   CG1   ILE   211   43.627   43.078   73.615   1   22.51       4238   CD1   ILE   211   44.053   42.802   72.17   1   24.95       4239   C   ILE   211   42.637   40.932   76.67   1   21.64       4240   O   ILE   211   43.522   40.135   76.956   1   22.47       4241   N   VAL   212   41.373   49.763   77.04   1   22.74       4242   CA   VAL   212   40.951   39.596   77.809   1   22.77       4243   CB   VAL   212   39.656   39.9   78.613   1   23.55       4244   CG1   VAL   212   39.101   38.62   79.216   1   22.95       4245   CG2   VAL   212   39.964   40.923   79.722   1   24.04       4246   C   VAL   212   40.688   38.412   76.895   1   22.87       4247   O   VAL   212   40.044   38.555   75.862   1   22.07       4248   N   LEU   213   41.203   37.244   77.262   1   21.5       4249   CA   LEU   213   40.958   36.055   76.464   1   22.56       4250   CB   LEU   213   42.175   35.113   76.506   1   22.1       4251   CG   LEU   213   42.166   33.952   75.493   1   23.39       4252   CD1   LEU   213   43.584   33.488   75.184   1   27.12       4253   CD2   LEU   213   41.346   32.807   76.037   1   26.06       4254   C   LEU   213   39.722   35.371   77.059   1   21.64       4255   O   LEU   213   39.646   35.161   78.27   1   22.01       4256   N   VAL   214   38.745   35.062   76.211   1   20.01       4257   CA   VAL   214   37.53   34.384   76.65   1   19.73       4258   CB   VAL   214   36.257   35.133   76.175   1   19.98       4259   CG1   VAL   214   35.003   34.365   76.593   1   15.45       4260   CG2   VAL   214   36.244   36.555   76.771   1   18.52       4261   C   VAL   214   37.576   32.99   76.031   1   21.65       4262   O   VAL   214   37.674   32.84   74.805   1   20.55       4263   N   ALA   215   37.505   31.975   76.882   1   19.93       4264   CA   ALA   215   37.591   30.594   76.434   1   20.81       4265   CB   ALA   215   38.322   29.756   77.495   1   20.96       4266   C   ALA   215   36.288   29.913   76.103   1   21.6       4267   O   ALA   215   35.368   29.899   76.917   1   21.53       4268   N   TYR   216   36.202   29.353   74.899   1   20.94       4269   CA   TYR   216   35.021   28.588   74.551   1   22.1       4270   CB   TYR   216   34.348   29.11   73.275   1   21.22       4271   CG   TYR   216   35.088   28.944   71.968   1   20.46       4272   CD1   TYR   216   35.3   27.679   71.415   1   20.84       4273   CE1   TYR   216   35.814   27.538   70.121   1   21.78       4274   CD2   TYR   216   35.43   30.065   71.209   1   19.29       4275   CE2   TYR   216   35.948   29.941   69.92   1   20.31       4276   CZ   TYR   216   36.127   28.67   69.379   1   20.19       4277   OH   TYR   216   36.569   28.535   68.084   1   22.59       4278   C   TYR   216   35.478   27.135   74.43   1   21.99       4279   O   TYR   216   36.676   26.87   74.339   1   21.2       4280   N   SER   217   34.524   26.208   74.468   1   23.35       4281   CA   SER   217   34.807   24.78   74.417   1   24.92       4282   CB   SER   217   35.403   24.39   73.055   1   25.83       4283   OG   SER   217   34.417   24.514   72.047   1   28.98       4284   C   SER   217   35.769   24.433   75.552   1   24.94       4285   O   SER   217   36.615   23.545   75.426   1   24.4       4286   N   ALA   218   35.615   25.139   76.673   1   24.95       4287   CA   ALA   218   36.461   24.939   77.851   1   24.36       4288   CB   ALA   218   36.197   26.051   78.875   1   25.49       4289   C   ALA   218   36.256   23.577   78.507   1   23.35       4290   O   ALA   218   37.063   23.16   79.345   1   22.95       4291   N   LEU   219   35.169   22.903   78.14   1   24.1       4292   CA   LEU   219   34.856   21.579   78.669   1   25.84       4293   CB   LEU   219   33.414   21.536   79.188   1   24.72       4294   CG   LEU   219   33.095   22.494   80.342   1   25.83       4295   CD1   LEU   219   31.646   22.321   80.784   1   24.61       4296   CD2   LEU   219   34.037   22.215   81.501   1   24.76       4297   C   LEU   219   35.055   20.482   77.618   1   26.63       4298   O   LEU   219   34.61   19.352   77.808   1   28.68       4299   N   GLY   220   35.714   20.813   76.51   1   28.28       4300   CA   GLY   220   35.949   19.815   75.472   1   29.4       4301   C   GLY   220   35.057   19.901   74.242   1   30.96       4302   O   GLY   220   35.138   19.046   73.353   1   30.61       4303   N   SER   221   34.202   20.925   74.21   1   30.65       4304   CA   SER   221   33.268   21.204   73.113   1   32.44       4305   CB   SER   221   33.985   21.168   71.754   1   32.4       4306   OG   SER   221   33.932   19.867   71.178   1   30.8       4307   C   SER   221   32.055   20.28   73.05   1   33.25       4308   O   SER   221   32.005   19.234   73.696   1   31.91       4309   N   HIS   222   31.075   20.69   72.256   1   34.38       4310   CA   HIS   222   29.857   19.919   72.067   1   35.94       4311   CB   HIS   222   28.831   20.751   71.299   1   37.09       4312   CG   HIS   222   29.407   21.482   70.124   1   40.16       4313   CD2   HIS   222   29.799   21.046   68.903   1   40.46       4314   ND1   HIS   222   29.652   22.839   70.14   1   42.05       4315   CE1   HIS   222   30.167   23.208   68.98   1   42.17       4316   NE2   HIS   222   30.266   22.137   68.21   1   42.81       4317   C   HIS   222   30.125   18.62   71.302   1   36.26       4318   O   HIS   222   29.291   17.717   71.302   1   34.82       4319   N   ARG   223   31.285   18.535   70.654   1   36.75       4320   CA   ARG   223   31.653   17.355   69.878   1   38.59       4321   CB   ARG   223   31.851   16.146   70.801   1   38.31       4322   CG   ARG   223   32.922   16.338   71.873   1   35.17       4323   CD   ARG   223   33.11   15.061   72.681   1   39.11       4324   NE   ARG   223   33.691   13.994   71.87   1   38.42       4325   CZ   ARG   223   34.993   13.854   71.636   1   39       4326   NH1   ARG   223   35.864   14.706   72.16   1   37.07       4327   NH2   ARG   223   35.422   12.868   70.856   1   39.45       4328   C   ARG   223   30.608   17.02   68.814   1   39.36       4329   O   ARG   223   30.332   15.852   68.555   1   39.26       4330   N   GLU   224   30.034   18.047   68.192   1   41.08       4331   CA   GLU   224   29.026   17.844   67.153   1   43.24       4332   CB   GLU   224   28.105   19.063   67.062   1   43.95       4333   CG   GLU   224   26.878   18.864   66.186   1   46.73       4334   CD   GLU   224   26.177   20.17   65.865   1   48.29       4335   OE1   GLU   224   26.301   21.121   66.662   1   49.58       4338   OE2   GLU   224   25.493   20.247   64.823   1   48.86       4337   C   GLU   224   29.67   17.609   65.786   1   43.52       4338   O   GLU   224   30.557   18.354   65.368   1   41.39       4339   N   GLU   225   29.224   16.568   65.095   1   45.73       4340   CA   GLU   225   29.742   16.261   63.765   1   47.78       4341   CB   GLU   225   29.553   14.78   63.455   1   49.4       4342   CG   GLU   225   30.413   13.853   64.289   1   53.17       4343   CD   GLU   225   30.094   12.389   64.034   1   56.08       4344   OE1   GLU   225   29.093   11.888   64.59   1   57.71       4345   OE2   GLU   225   30.835   11.744   63.263   1   56.97       4346   C   GLU   225   28.967   17.097   62.751   1   47.44       4347   O   GLU   225   27.796   17.405   62.97   1   47.38       4348   N   PRO   226   29.609   17.477   61.633   1   47.69       4349   CD   PRO   226   28.882   17.89   60.426   1   49.01       4350   CA   PRO   226   31.001   17.16   61.29   1   48.17       4351   CB   PRO   226   30.99   17.121   59.755   1   48.21       4352   CG   PRO   226   29.532   17.022   59.388   1   49.35       4353   C   PRO   226   31.987   18.208   61.797   1   47.52       4354   O   PRO   226   33.153   18.202   61.406   1   48.77       4355   N   TRP   227   31.523   19.106   62.658   1   46.39       4356   CA   TRP   227   32.376   20.167   63.185   1   45.73       4357   CB   TRP   227   31.542   21.137   64.022   1   47.52       4358   CG   TRP   227   30.346   21.651   63.292   1   50.07       4359   CD2   TRP   227   30.345   22.544   62.171   1   51.14       4360   CE2   TRP   227   28.997   22.727   61.785   1   51.86       4361   CE3   TRP   227   31.352   23.205   61.452   1   52.61       4362   CD1   TRP   227   29.04   21.34   63.535   1   50.49       4363   NE1   TRP   227   28.223   21.982   62.635   1   51.12       4364   CZ2   TRP   227   28.628   23.547   60.71   1   52.18       4365   CZ3   TRP   227   30.984   24.022   60.381   1   53.15       4366   CH2   TRP   227   29.632   24.183   60.023   1   52.77       4367   C   TRP   227   33.543   19.654   64.016   1   44.43       4368   O   TRP   227   34.661   20.156   63.903   1   44.61       4369   N   VAL   228   33.283   18.658   64.853   1   42.93       4370   CA   VAL   228   34.326   18.096   65.701   1   42.13       4371   CB   VAL   228   33.928   18.156   67.188   1   40.82       4372   CG1   VAL   228   35.066   17.634   68.051   1   39.45       4373   CG2   VAL   228   33.566   19.585   67.568   1   39.2       4374   C   VAL   228   34.596   16.644   65.333   1   42.87       4375   O   VAL   228   33.667   15.851   65.169   1   42.96       4376   N   ASP   229   35.874   16.304   65.21   1   43.32       4377   CA   ASP   229   36.285   14.95   64.862   1   44.79       4378   CB   ASP   229   37.772   14.942   64.407   1   46.03       4379   CG   ASP   229   38.312   13.54   64.255   1   48.28       4380   OD1   ASP   229   37.528   12.655   63.854   1   48.6       4381   OD2   ASP   229   39.525   13.328   64.462   1   48.83       4382   C   ASP   229   36.022   13.975   66.007   1   45.19       4383   O   ASP   229   36.572   14.121   67.098   1   45       4384   N   PRO   230   35.167   12.966   65.771   1   45.41       4385   CD   PRO   230   34.403   12.769   64.528   1   46.46       4386   CA   PRO   230   34.806   11.945   66.763   1   45.67       4387   CB   PRO   230   33.873   11.019   65.983   1   46.29       4385   CG   PRO   230   33.225   11.948   65.011   1   48.91       4389   C   PRO   230   36.01   11.2   67.331   1   45.59       4390   O   PRO   230   35.941   10.641   68.42   1   46.07       4391   N   ASN   231   37.112   11.194   66.588   1   46.41       4392   CA   ASN   231   38.315   10.516   67.046   1   46.32       4393   CB   ASN   231   39.207   10.148   65.864   1   49.03       4394   CG   ASN   231   38.583   9.087   64.984   1   51.81       4395   OD1   ASN   231   38.192   8.02   65.466   1   53.21       4396   ND2   ASN   231   38.486   9.37   63.687   1   52.71       4397   C   ASN   231   39.114   11.34   68.038   1   45.28       4398   O   ASN   231   40.059   10.835   68.641   1   45.04       4399   N   SER   232   38.747   12.607   68.207   1   43.34       4400   CA   SER   232   39.458   13.469   69.148   1   41.47       4401   CB   SER   232   38.972   14.919   69.023   1   41.41       4402   OG   SER   232   37.593   15.03   69.313   1   41.99       4403   C   SER   232   39.245   12.963   70.572   1   39.62       4404   O   SER   232   38.17   12.473   70.916   1   39.11       4405   N   PRO   233   40.276   13.07   71.421   1   38.66       4406   CD   PRO   233   41.599   13.665   71.175   1   38.21       4407   CA   PRO   233   40.162   12.608   72.807   1   38.68       4408   CB   PRO   233   41.58   12.789   73.349   1   38.53       4409   CG   PRO   233   42.087   13.95   72.578   1   37.92       4410   C   PRO   233   39.125   13.389   73.607   1   38.62       4411   O   PRO   233   38.873   14.56   73.329   1   38.88       4412   N   VAL   234   38.517   12.727   74.588   1   38.53       4413   CA   VAL   234   37.51   13.356   75.438   1   37.9       4414   CB   VAL   234   36.514   12.319   75.969   1   36.89       4415   CG1   VAL   234   35.402   13.013   76.727   1   38.46       4416   CG2   VAL   234   35.947   11.515   74.81   1   37.82       4417   C   VAL   234   38.206   14.042   76.608   1   37.12       4418   O   VAL   234   38.758   13.384   77.496   1   37.26       4419   N   LEU   235   38.178   15.37   76.602   1   35.97       4420   CA   LEU   235   38.834   16.149   77.647   1   35.14       4421   CB   LEU   235   38.55   17.647   77.462   1   33.23       4422   CG   LEU   235   39.205   18.573   78.5   1   32.46       4423   CD1   LEU   235   40.711   18.608   78.271   1   31.27       4424   CD2   LEU   235   38.618   19.978   78.409   1   30.84       4425   C   LEU   235   38.442   15.746   79.065   1   34.8       4426   O   LEU   235   39.307   15.472   79.896   1   34.25       4427   N   LEU   236   37.141   15.708   79.336   1   34.93       4428   CA   LEU   236   36.66   15.387   80.675   1   36.72       4429   CB   LEU   236   35.161   15.67   80.775   1   36.23       4430   CG   LEU   236   34.77   17.14   80.555   1   36.7       4431   CD1   LEU   236   33.282   17.316   80.789   1   37.25       4432   CD2   LEU   236   35.564   18.03   81.5   1   35.72       4433   C   LEU   236   36.96   13.976   81.168   1   38.46       4434   O   LEU   236   36.637   13.633   82.302   1   38.15       4435   N   GLU   237   37.583   13.165   80.32   1   39.4       4436   CA   GLU   237   37.937   11.809   80.694   1   40.78       4437   CB   GLU   237   37.581   10.838   79.563   1   42.68       4438   CG   GLU   237   36.157   10.326   79.641   1   46.16       4439   CD   GLU   237   35.772   9.474   78.45   1   49.85       4440   OE1   GLU   237   36.627   8.699   77.971   1   51.65       4441   OE2   GLU   237   34.608   9.569   78   1   51.49       4442   C   GLU   237   39.416   11.708   81.029   1   40.47       4443   O   GLU   237   39.905   10.638   81.375   1   40.93       4444   N   ASP   238   40.127   12.828   80.938   1   39.51       4445   CA   ASP   238   41.557   12.847   81.228   1   39.33       4446   CB   ASP   238   42.115   14.25   80.998   1   38.13       4447   CG   ASP   238   43.6   14.328   81.238   1   37.88       4448   OD1   ASP   238   44.011   14.46   82.41   1   38.54       4449   OD2   ASP   238   44.362   14.247   80.252   1   36.73       4450   C   ASP   238   41.826   12.393   82.662   1   39.27       4451   O   ASP   238   41.178   12.857   83.599   1   39.59       4452   N   PRO   239   42.787   11.469   82.847   1   39.96       4453   CD   PRO   239   43.592   10.835   81.787   1   40.09       4454   CA   PRO   239   43.158   10.928   84.164   1   39.09       4455   CB   PRO   239   44.359   10.037   83.845   1   38.92       4456   CG   PRO   239   44.079   9.576   82.469   1   40.57       4457   C   PRO   239   43.507   11.986   85.212   1   37.19       4458   O   PRO   239   42.994   11.955   86.327   1   37.68       4459   N   VAL   240   44.391   12.906   84.848   1   35.63       4460   CA   VAL   240   44.82   13.961   85.756   1   35.06       4461   CB   VAL   240   45.886   14.858   85.086   1   35.09       4462   CG1   VAL   240   46.315   15.971   86.029   1   34.64       4463   CG2   VAL   240   47.095   14.013   84.704   1   35.8       4464   C   VAL   240   43.636   14.811   86.223   1   35.64       4465   O   VAL   240   43.499   15.11   87.413   1   34.56       4466   N   LEU   241   42.777   15.191   85.282   1   35.51       4467   CA   LEU   241   41.603   15.989   85.604   1   35.92       4468   CB   LEU   241   40.846   16.347   84.319   1   36.74       4469   CG   LEU   241   40.853   17.811   83.862   1   37.91       4470   CD1   LEU   241   42.237   18.414   83.992   1   36.91       4471   CD2   LEL   241   40.363   17.886   82.425   1   36.48       4472   C   LEU   241   40.683   15.228   86.562   1   36.07       4473   O   LEU   241   40.156   15.801   87.518   1   34.97       4474   N   CYS   242   40.487   13.938   86.314   1   35.99       4475   CA   CYS   242   39.626   13.143   87.184   1   37.64       4476   CB   CYS   242   39.331   11.786   86.537   1   39.44       4477   SG   CYS   242   38.353   11.916   85.015   1   44.32       4478   C   CYS   242   40.251   12.951   88.568   1   37.12       4479   O   CYS   242   39.55   12.941   89.58   1   36.63       4480   N   ALA   243   41.573   12.812   88.607   1   36.6       4481   CA   ALA   243   42.286   12.63   89.867   1   37.02       4482   CB   ALA   243   43.757   12.314   89.593   1   37.21       4483   C   ALA   243   42.176   13.88   90.745   1   37.53       4484   O   ALA   243   41.897   13.791   91.941   1   36.53       4485   N   LEU   244   42.41   15.044   90.144   1   36.64       4486   CA   LEU   244   42.325   16.303   90.871   1   36.27       4487   CB   LEU   244   42.803   17.464   89.987   1   36.4       4488   CG   LEU   244   44.314   17.511   89.719   1   38.28       4489   CD1   LEU   244   44.63   18.636   88.627   1   37.5       4490   CD2   LEU   244   45.047   17.85   91.011   1   37.55       4491   C   LEU   244   40.893   16.551   91.336   1   35.84       4492   O   LEU   244   40.669   17.146   92.39   1   36.28       4493   N   ALA   245   39.926   16.084   90.555   1   35.74       4494   CA   ALA   245   38.52   16.254   90.9   1   36.61       4495   CB   ALA   245   37.634   15.803   89.739   1   35.59       4496   C   ALA   245   38.177   15.46   92.159   1   38.55       4497   O   ALA   245   37.514   15.971   93.061   1   37.18       4498   N   LYS   246   38.632   14.211   92.217   1   40.29       4499   CA   LYS   246   38.362   13.359   93.371   1   43.09       4500   CB   LYS   246   38.861   11.937   93.107   1   45.15       4501   CG   LYS   246   38.141   11.261   91.955   1   49.25       4502   CD   LYS   246   38.62   9.839   91.731   1   53.16       4503   CE   LYS   246   37.943   9.22   90.513   1   54.46       4504   NZ   LYS   246   38.453   7.848   90.227   1   57.81       4505   C   LYS   246   39.018   13.92   94.621   1   42.96       4506   O   LYS   246   38.445   13.883   95.707   1   44.05       4507   N   LYS   247   40.221   14.449   94.454   1   43.54       4508   CA   LYS   247   40.961   15.034   95.558   1   44.02       4509   CB   LYS   247   42.34   15.473   95.068   1   44.95       4510   CG   LYS   247   43.174   16.234   96.085   1   46.66       4511   CD   LYS   247   44.482   16.698   95.456   1   49.62       4512   CE   LYS   247   45.305   17.555   96.404   1   50.51       4513   NZ   LYS   247   46.576   18.026   95.768   1   50.78       4514   C   LYS   247   40.213   16.227   96.154   1   44.6       4515   O   LYS   247   40.183   16.399   97.371   1   44.73       4516   N   HIS   248   39.612   17.049   95.295   1   43.6       4517   CA   HIS   248   38.869   18.228   95.737   1   42.89       4518   CB   HIS   248   38.99   19.35   94.701   1   41.76       4519   CG   HIS   248   40.25   20.15   94.814   1   42.45       4520   CD2   HIS   248   41.434   20.048   94.165   1   42.31       4521   ND1   HIS   248   40.382   21.21   95.686   1   43.23       4522   CE1   HIS   248   41.592   21.728   95.568   1   43.61       4523   NE2   HIS   248   42.251   21.041   94.651   1   42.69       4524   C   HIS   248   37.396   17.913   95.954   1   43.32       4525   O   HIS   248   36.618   18.79   96.328   1   44.16       4526   N   LYS   249   37.017   16.661   95.72   1   43.16       4527   CA   LYS   249   35.63   16.238   95.867   1   43.35       4528   CB   LYS   249   35.169   16.403   97.317   1   46.59       4529   CG   LYS   249   34.79   15.096   98   1   50.78       4530   CD   LYS   249   35.993   14.175   98.176   1   53.98       4531   CE   LYS   249   36.915   14.663   99.287   1   56.73       4532   NZ   LYS   249   36.235   14.646   100.616   1   57.33       4533   C   LYS   249   34.725   17.049   94.938   1   42.13       4534   O   LYS   249   33.62   17.456   95.31   1   40.33       4535   N   ARG   250   35.21   17.292   93.724   1   39.33       4536   CA   ARG   250   34.452   18.044   92.732   1   37.2       4537   CB   ARG   250   35.188   19.338   92.368   1   36.51       4538   CG   ARG   250   35.427   20.276   93.536   1   36.98       4539   CD   ARG   250   34.129   20.896   94.037   1   35.57       4540   NE   ARG   250   34.357   21.705   95.23   1   35.89       4541   CZ   ARG   250   33.432   22.453   95.825   1   35.97       4542   NH1   ARG   250   32.196   22.509   95.341   1   36.21       4543   NH2   ARG   250   33.744   23.145   96.913   1   36.22       4544   C   ARG   250   34.298   17.174   91.491   1   36.43       4545   O   ARG   250   34.225   15.951   91.591   1   36.4       4546   N   THR   251   34.257   17.807   90.325   1   34.14       4547   CA   THR   251   34.115   17.081   89.068   1   33.98       4548   CB   THR   251   32.737   17.319   88.439   1   34.97       4549   OG1   THR   251   32.598   18.71   88.119   1   34.88       4550   CG2   THR   251   31.628   16.903   89.403   1   35.34       4551   C   THR   251   35.179   17.565   88.088   1   32.67       4552   O   THR   251   35.74   18.651   88.257   1   31.81       4553   N   PRO   252   35.486   16.758   87.059   1   31.54       4554   CD   PRO   252   34.979   15.399   86.796   1   31.98       4555   CA   PRO   252   36.493   17.143   86.065   1   30.44       4556   CB   PRO   252   36.431   16   85.054   1   31.24       4557   CG   PRO   252   36.054   14.827   85.901   1   33.24       4558   C   PRO   252   36.154   18.498   85.427   1   28.68       4559   O   PRO   252   37.037   19.32   85.187   1   29.75       4560   N   ALA   253   34.872   18.72   85.156   1   26.29       4561   CA   ALA   253   34.429   19.968   84.547   1   26.55       4562   CB   ALA   253   32.92   19.943   84.324   1   24.73       4563   C   ALA   253   34.805   21.156   85.421   1   25.8       4564   O   ALA   253   35.347   22.145   84.93   1   24.51       4565   N   LEU   254   34.515   21.059   86.716   1   24.42       4566   CA   LEU   254   34.835   22.149   87.634   1   25.34       4567   CB   LEU   254   34.308   21.849   89.041   1   24.94       4568   CG   LEU   254   32.8   22.087   89.177   1   27.46       4569   CD1   LEU   254   32.312   21.595   90.536   1   28.96       4570   CD2   LEU   254   32.509   23.582   89.014   1   27.74       4571   C   LEU   254   36.326   22.437   87.68   1   24.52       4572   O   LEU   254   36.739   23.599   87.744   1   25.76       4573   N   ILE   255   37.137   21.389   87.64   1   22.9       4574   CA   ILE   255   38.589   21.561   87.657   1   23.61       4575   CB   ILE   255   39.321   20.179   87.677   1   24.63       4576   CG2   ILE   255   40.825   20.381   87.567   1   23.07       4577   CG1   ILE   255   38.952   19.388   88.947   1   25.8       4578   CD1   ILE   255   39.35   20.05   90.26   1   26.32       4579   C   ILE   255   39.022   22.339   86.396   1   23.34       4580   O   ILE   255   39.815   23.278   86.482   1   24.06       4581   N   ALA   256   38.492   21.946   85.238   1   22.84       4582   CA   ALA   256   38.823   22.589   83.966   1   23.88       4583   CB   ALA   256   38.142   21.857   82.814   1   23.31       4584   C   ALA   256   38.421   24.061   83.957   1   24.82       4585   O   ALA   256   39.137   24.899   83.418   1   25.84       4586   N   LEU   257   37.272   24.37   84.546   1   23.88       4587   CA   LEU   257   36.801   25.751   84.619   1   25.05       4588   CB   LEU   257   35.34   25.787   85.086   1   25.76       4589   CG   LEU   257   34.202   25.919   84.071   1   28.76       4590   CD1   LEU   257   34.585   25.369   82.716   1   28.9       4591   CD2   LEU   257   32.972   25.22   84.633   1   26.81       4592   C   LEU   257   37.661   26.583   85.572   1   23.75       4593   O   LEU   257   38.07   27.692   85.231   1   21.65       4594   N   ARG   258   37.939   26.043   86.758   1   23.02       4595   CA   ARG   258   38.741   26.761   87.758   1   21.98       4596   CB   ARG   258   38.861   25.939   89.046   1   20.7       4597   CG   ARG   258   39.553   26.693   90.182   1   20.23       4598   CD   ARG   258   38.684   27.855   90.707   1   19.44       4599   NE   ARG   258   39.496   28.867   91.388   1   19.08       4600   CZ   ARG   258   39.007   29.941   92.005   1   21.06       4601   NH1   ARG   258   37.69   30.155   92.045   1   18.42       4602   NH2   ARG   258   39.836   30.819   92.565   1   19.9       4603   C   ARG   258   40.133   27.078   87.227   1   21.91       4604   O   ARG   258   40.692   28.129   87.511   1   20.77       4605   N   TYR   259   40.687   26.144   86.463   1   22.99       4606   CA   TYR   259   42.001   26.311   85.862   1   22.35       4607   CB   TYR   259   42.273   25.126   84.929   1   22.8       4608   CG   TYR   259   43.46   25.281   84.012   1   24.23       4609   CD1   TYR   259   44.762   25.283   84.513   1   25.11       4610   CE1   TYR   259   45.859   25.403   83.658   1   26.19       4611   CD2   TYR   259   43.28   25.406   82.628   1   24.17       4612   CE2   TYR   259   44.368   25.527   81.769   1   25.4       4613   CZ   TYR   259   48.655   25.524   82.291   1   26.22       4614   OH   TYR   259   48.739   25.638   81.443   1   26.66       4615   C   TYR   259   42.047   27.627   85.075   1   21.54       4616   O   TYR   259   42.972   28.439   85.231   1   22.01       4617   N   GLN   260   41.046   27.847   84.231   1   20.08       4618   CA   GLN   260   41.017   29.064   83.424   1   20.29       4619   CB   GLN   260   39.872   29.011   82.405   1   19.38       4620   CG   GLN   260   39.926   27.795   81.474   1   22.3       4621   CD   GLN   260   41.077   27.86   80.478   1   22.95       4622   OE1   GLN   260   41.954   28.715   80.584   1   20.97       4623   NE2   GLN   260   41.075   26.949   79.507   1   22.46       4624   C   GLN   260   40.902   30.321   84.275   1   20.48       4625   O   GLN   260   41.575   31.318   84.014   1   20.19       4626   N   LEU   261   40.052   30.284   85.293   1   21.23       4627   CA   LEU   261   39.891   31.462   86.139   1   21.95       4628   CB   LEU   261   38.813   31.221   87.198   1   23.21       4629   CG   LEU   261   37.385   31.083   86.68   1   24.7       4630   CD1   LEU   261   36.445   30.976   87.878   1   24.38       4631   CD2   LEU   261   37.014   32.299   85.816   1   22.85       4632   C   LEU   261   41.177   31.889   86.826   1   21.33       4633   O   LEU   261   41.441   33.088   86.951   1   20.72       4634   N   GLN   262   41.986   30.926   87.265   1   21.12       4635   CA   GLN   262   43.217   31.279   87.964   1   22.21       4636   CB   GLN   262   43.696   30.12   88.848   1   22.11       4637   CG   GLN   262   42.623   29.722   89.843   1   24.36       4638   CD   GLN   262   43.101   28.888   91.017   1   22.45       4639   OE1   GLN   262   42.28   28.295   91.715   1   23.73       4640   NE2   GLN   262   44.411   28.852   91.257   1   22.82       4641   C   GLN   262   44.332   31.765   87.057   1   23.42       4642   O   GLN   262   45.327   32.315   87.535   1   23.79       4643   N   ARG   263   44.171   31.586   85.751   1   22.96       4644   CA   ARG   263   45.189   32.073   84.832   1   23.93       4645   CB   ARG   263   45.546   31.001   83.788   1   24.5       4646   CG   ARG   263   44.395   30.424   82.993   1   27.24       4647   CD   ARG   263   44.751   29.015   82.474   1   28.26       4648   NE   ARG   263   45.962   28.986   81.636   1   26.17       4649   CZ   ARG   263   45.957   28.917   80.305   1   25.85       4650   NH1   ARG   263   44.808   28.869   79.637   1   23.72       4651   NH2   ARG   263   47.101   28.886   79.638   1   24.17       4652   C   ARG   263   44.742   33.385   84.177   1   24.66       4653   O   ARG   263   45.36   33.86   83.227   1   25.78       4654   N   GLY   264   43.668   33.972   84.704   1   23.32       4655   CA   GLY   264   43.184   35.243   84.189   1   22.73       4656   C   GLY   264   42.282   35.172   82.972   1   22.41       4657   O   GLY   264   42.029   36.179   82.321   1   24.09       4658   N   VAL   265   41.781   33.985   82.675   1   22.3       4659   CA   VAL   265   40.904   33.792   81.53   1   22.02       4660   CB   VAL   265   41.228   32.417   80.856   1   21.01       4661   CG1   VAL   265   40.17   32.057   79.812   1   21.44       4662   CG2   VAL   265   42.612   32.467   80.209   1   20.75       4663   C   VAL   265   39.416   33.841   81.924   1   23.05       4664   O   VAL   265   39.044   33.357   82.986   1   24.84       4665   N   VAL   266   38.586   34.464   81.087   1   21.47       4666   CA   VAL   266   37.146   34.498   81.319   1   21.63       4667   CB   VAL   266   36.485   35.715   80.667   1   20.91       4668   CG1   VAL   266   34.968   35.544   80.667   1   18.86       4669   CG2   VAL   266   36.87   36.98   81.434   1   21.5       4670   C   VAL   266   36.679   33.212   80.636   1   22.82       4671   O   VAL   266   37.06   32.935   79.497   1   23.26       4672   N   VAL   267   35.856   32.426   81.315   1   20.87       4673   CA   VAL   267   35.459   31.154   80.755   1   21.74       4674   CB   VAL   267   36.025   30.014   81.664   1   23.39       4675   CG1   VAL   267   35.306   30.023   83.015   1   23.09       4676   CG2   VAL   267   35.9   28.659   80.98   1   23.79       4677   C   VAL   267   33.964   30.957   80.514   1   22.13       4678   O   VAL   267   33.121   31.389   81.307   1   21.27       4679   N   LEU   268   33.643   30.318   79.393   1   20.93       4680   CA   LEU   268   32.255   30.03   79.06   1   21.22       4681   CB   LEU   268   31.996   30.256   77.566   1   21.41       4682   CG   LEU   268   32.265   31.668   77.024   1   21.51       4683   CD1   LEU   268   31.888   31.743   75.53   1   20.35       4684   CD2   LEU   268   31.445   32.673   77.819   1   20.39       4685   C   LEU   268   32.001   28.573   79.394   1   21.7       4686   O   LEU   268   32.934   27.774   79.432   1   20.74       4687   N   ALA   269   30.74   28.241   79.649   1   22.55       4688   CA   ALA   269   30.338   26.871   79.939   1   22.53       4689   CB   ALA   269   30.433   26.565   81.44   1   22.36       4690   C   ALA   269   28.902   26.732   79.473   1   23.29       4691   O   ALA   269   28.016   27.485   79.893   1   22.71       4692   N   LYS   270   28.679   25.775   78.587   1   22.56       4693   CA   LYS   270   27.349   25.532   78.068   1   23.54       4694   CB   LYS   270   27.391   25.342   76.545   1   23.09       4695   CG   LYS   270   26.045   24.951   75.918   1   25.51       4696   CD   LYS   270   25.744   23.451   76.047   1   26.34       4697   CE   LYS   270   24.414   23.091   75.398   1   28.99       4698   NZ   LYS   270   24.153   21.613   75.422   1   28.53       4699   C   LYS   270   26.77   24.28   78.698   1   24.6       4700   O   LYS   270   27.462   23.273   78.831   1   24.26       4701   N   SER   271   25.505   24.357   79.091   1   25.36       4702   CA   SER   271   24.791   23.208   79.638   1   26.27       4703   CB   SER   271   25.179   22.926   81.088   1   26.63       4704   OG   SER   271   24.477   21.781   81.555   1   27.01       4705   C   SER   271   23.302   23.46   79.583   1   26.36       4706   O   SER   271   22.839   24.545   79.93   1   27.11       4707   N   TYR   272   22.548   22.461   79.137   1   27.1       4708   CA   TYR   272   21.1   22.587   79.081   1   29.21       4709   CB   TYR   272   20.571   22.186   77.701   1   29.79       4710   CG   TYR   272   20.606   23.3   76.677   1   30.47       4711   CD1   TYR   272   21.471   24.384   76.824   1   31       4712   CE1   TYR   272   21.521   25.398   75.871   1   30.76       4713   CD2   TYR   272   19.79   23.258   75.545   1   31.83       4714   CE2   TYR   272   19.835   24.265   74.587   1   31.65       4715   CZ   TYR   272   20.7   25.329   74.755   1   31.6       4716   OH   TYR   272   20.743   26.324   73.807   1   33.62       4717   C   TYR   272   20.481   21.711   80.157   1   30.11       4718   O   TYR   272   19.267   21.529   80.194   1   30.36       4719   N   ASN   273   21.326   21.184   81.039   1   31.22       4720   CA   ASN   273   20.878   20.32   82.135   1   32.4       4721   CB   ASN   273   21.786   19.092   82.217   1   32.56       4722   CG   ASN   273   21.39   18.143   83.331   1   35.28       4723   OD1   ASN   273   21.717   18.363   84.497   1   33.94       4724   ND2   ASN   273   20.665   17.083   82.975   1   37.04       4725   C   ASN   273   20.898   21.078   83.463   1   33.03       4726   O   ASN   273   21.938   21.594   83.869   1   32.74       4727   N   GLU   274   19.757   21.128   84.146   1   33.81       4728   CA   GLU   274   19.646   21.854   85.411   1   36.55       4729   CB   GLU   274   18.267   21.626   86.035   1   38.89       4730   CG   GLU   274   17.872   22.716   87.021   1   45.92       4731   CD   GLU   274   16.504   22.491   87.644   1   48.46       4732   OE1   GLU   274   15.567   22.111   86.908   1   51.69       4733   OE2   GLU   274   16.366   22.712   88.865   1   49.91       4734   C   GLU   274   20.725   21.51   86.437   1   36.28       4735   O   GLU   274   21.33   22.402   87.034   1   36.03       4736   N   GLN   275   20.958   20.219   86.639   1   36.36       4737   CA   GLN   275   21.962   19.76   87.591   1   36.95       4738   CB   GLN   275   22.025   18.226   87.591   1   40.69       4739   CG   GLN   275   23.169   17.644   88.423   1   47.46       4740   CD   GLN   275   23.491   16.198   88.054   1   51.47       4741   OE1   GLN   275   23.782   15.888   86.891   1   55.24       4742   NE2   GLN   275   23.451   15.309   89.042   1   52.45       4743   C   GLN   275   23.343   20.318   87.27   1   34.5       4744   O   GLN   275   24.019   20.873   88.139   1   34.08       4745   N   ARG   276   23.763   20.168   86.021   1   32.2       4746   CA   ARG   276   25.076   20.643   85.617   1   31.19       4747   CB   ARG   276   25.45   20.041   84.257   1   31.11       4748   CG   ARG   276   25.631   18.521   84.334   1   30.48       4749   CD   ARG   276   26.147   17.922   83.037   1   32.58       4750   NE   ARG   276   25.103   17.716   82.041   1   35.04       4751   CZ   ARG   276   24.264   16.685   82.034   1   37.39       4752   NH1   ARG   276   24.349   15.756   82.978   1   37.43       4753   NH2   ARG   276   23.346   16.58   81.079   1   37.84       4754   C   ARG   276   25.186   22.168   85.608   1   30.03       4755   O   ARG   276   26.242   22.717   85.931   1   29.73       4756   N   ILE   277   24.1   22.852   85.259   1   28.62       4757   CA   ILE   277   24.101   24.31   85.252   1   28.09       4758   CB   ILE   277   22.73   24.869   84.8   1   27       4759   CG2   ILE   277   22.629   26.353   85.148   1   25.34       4760   CG1   ILE   277   22.549   24.643   83.296   1   26.24       4761   CD1   ILE   277   21.149   24.952   82.779   1   25.36       4762   C   ILE   277   24.405   24.808   86.666   1   29.89       4763   O   ILE   277   25.254   25.679   86.867   1   28.89       4764   N   ARG   278   23.706   24.238   87.642   1   30.34       4765   CA   ARG   278   23.886   24.596   89.047   1   32.08       4766   CB   ARG   278   22.845   23.879   89.909   1   35.91       4767   CG   ARG   278   21.436   24.441   89.8   1   42.12       4768   CD   ARG   278   21.277   25.672   90.68   1   48.14       4769   NE   ARG   278   19.927   26.232   90.608   1   52.74       4770   CZ   ARG   278   19.504   27.255   91.345   1   54.64       4771   NH1   ARG   278   20.327   27.83   92.217   1   56.37       4772   NH2   ARG   278   18.265   27.706   91.206   1   55.07       4773   C   ARG   278   25.282   24.223   89.528   1   30.73       4774   O   ARG   278   25.881   24.934   90.328   1   30.53       4775   N   GLN   279   25.795   23.103   89.03   1   29.46       4776   CA   GLN   279   27.118   22.633   89.405   1   28.96       4777   CB   GLN   279   27.341   21.219   88.871   1   30.93       4778   CG   GLN   279   28.733   20.665   89.13   1   33.53       4779   CD   GLN   279   29.001   19.399   88.345   1   35.97       4780   OE1   GLN   279   28.259   18.42   88.452   1   39.87       4781   NE2   GLN   279   30.06   19.412   87.543   1   32.87       4782   C   GLN   279   28.251   23.532   88.916   1   28.17       4783   O   GLN   279   29.224   23.752   89.636   1   27.5       4784   N   ASN   280   28.132   24.051   87.697   1   27.84       4785   CA   ASN   280   29.193   24.892   87.132   1   27.28       4786   CB   ASN   280   28.913   25.183   85.648   1   26.48       4787   CG   ASN   280   29.011   23.93   84.781   1   28.56       4788   OD1   ASN   280   29.645   22.947   85.168   1   26.68       4789   ND2   ASN   280   28.395   23.965   83.597   1   27.83       4790   C   ASN   280   29.467   26.191   87.89   1   26.15       4791   O   ASN   280   30.605   26.664   87.909   1   26.27       4792   N   VAL   281   28.448   26.765   88.526   1   27.49       4793   CA   VAL   281   28.661   27.999   89.282   1   27.67       4794   CB   VAL   281   27.321   28.695   89.67   1   28.69       4795   CG1   VAL   281   26.57   29.113   88.422   1   29.15       4796   CG2   VAL   281   26.466   27.758   90.51   1   30.98       4797   C   VAL   281   29.47   27.746   90.553   1   26.86       4798   O   VAL   281   29.916   28.683   91.202   1   27.07       4799   N   GLN   282   29.659   26.482   90.912   1   27.07       4800   CA   GLN   282   30.432   26.158   92.107   1   27.85       4801   CB   GLN   282   30.16   24.717   92.537   1   30.9       4802   CG   GLN   282   28.74   24.495   93.019   1   35.25       4803   CD   GLN   282   28.467   23.049   93.373   1   40.44       4804   OE1   GLN   282   27.341   22.689   93.715   1   44.4       4805   NE2   GLN   282   29.497   22.208   93.288   1   42.64       4806   C   GLN   282   31.935   26.361   91.881   1   28.17       4807   O   GLN   282   32.753   26.136   92.781   1   27.57       4808   N   VAL   283   32.296   26.799   90.679   1   24.86       4809   CA   VAL   283   33.693   27.037   90.358   1   23.9       4810   CB   VAL   283   33.851   27.492   88.883   1   22.86       4811   CG1   VAL   283   33.185   28.846   88.68   1   23.2       4812   CG2   VAL   283   35.324   27.549   88.513   1   24.13       4813   C   VAL   283   34.264   28.103   91.299   1   23.81       4814   O   VAL   283   35.47   28.18   91.504   1   23.23       4815   N   PHE   284   33.391   28.917   91.887   1   22.44       4816   CA   PHE   284   33.847   29.963   92.801   1   24.08       4817   CB   PHE   284   32.863   31.136   92.781   1   24.64       4818   CG   PHE   284   32.73   31.791   91.435   1   22.68       4819   CD1   PHE   284   33.793   32.5   90.883   1   23.3       4820   CD2   PHE   284   31.546   31.692   90.718   1   22.4       4821   CE1   PHE   284   33.677   33.102   89.628   1   24.58       4822   CE2   PHE   284   31.419   32.288   89.464   1   23.13       4823   CZ   PHE   284   32.487   32.995   88.92   1   21.07       4824   C   PHE   284   33.999   29.467   94.242   1   25.51       4825   O   PHE   284   34.422   30.22   95.122   1   25.17       4826   N   GLU   285   33.667   28.203   94.476   1   25.57       4827   CA   GLU   285   33.724   27.642   95.823   1   29.39       4828   CB   GLU   285   32.573   26.653   96.015   1   31.89       4829   CG   GLU   285   31.234   27.321   96.252   1   39.46       4830   CD   GLU   285   30.09   26.33   96.255   1   44.77       4831   OE1   GLU   285   30.288   25.186   96.737   1   47.95       4832   OE2   GLU   285   28.987   26.7   95.787   1   49.57       4833   C   GLU   285   35.027   26.983   96.246   1   28.31       4834   O   GLU   285   35.16   26.561   97.394   1   27.4       4835   N   PHE   286   35.989   26.889   95.338   1   25.7       4836   CA   PHE   286   37.254   26.277   95.696   1   25.13       4837   CB   PHE   286   37.214   24.758   95.464   1   25.68       4838   CG   PHE   286   37.153   24.358   94.015   1   25.61       4839   CD1   PHE   286   35.969   24.47   93.29   1   24.99       4840   CD2   PHE   286   38.29   23.876   93.369   1   26.91       4841   CE1   PHE   286   35.917   24.111   91.943   1   25.93       4842   CE2   PHE   286   38.248   23.515   92.02   1   27.1       4843   CZ   PHE   286   37.06   23.634   91.308   1   26.05       4844   C   PHE   286   38.384   26.903   94.897   1   26.27       4845   O   PHE   286   38.144   27.707   93.994   1   24.93       4846   N   GLN   287   39.615   26.533   95.238   1   25.23       4847   CA   GLN   287   40.791   27.061   94.563   1   27.17       4848   CB   GLN   287   41.435   28.157   95.412   1   27.41       4849   CG   GLN   287   40.492   29.293   95.778   1   27.78       4850   CD   GLN   287   41.174   30.349   96.61   1   29.71       4851   OE1   GLN   287   42.214   30.877   96.22   1   30.3       4852   NE2   GLN   287   40.597   30.666   97.766   1   30.43       4853   C   GLN   287   41.802   25.953   94.322   1   26.22       4854   O   GLN   287   41.761   24.925   94.99   1   26.9       4855   N   LEU   288   42.703   26.169   93.364   1   25.77       4856   CA   LEU   288   43.747   25.191   93.036   1   24.94       4857   CB   LEU   288   43.761   24.916   91.523   1   26.15       4858   CG   LEU   288   42.495   24.293   90.905   1   27.46       4859   CD1   LEU   288   42.624   24.269   89.378   1   27.78       4860   CD2   LEU   288   42.286   22.889   91.447   1   27.31       4861   C   LEU   288   45.104   25.744   93.469   1   23.73       4862   O   LEU   288   45.341   26.942   93.374   1   22.56       4863   N   THR   289   45.987   24.875   93.954   1   24.64       4864   CA   THR   289   47.319   25.304   94.383   1   25.36       4865   CB   THR   289   47.948   24.281   95.341   1   25.61       4866   OG1   THR   289   48.143   23.04   94.649   1   25.09       4867   CG2   THR   289   47.024   24.055   96.546   1   22.71       4868   C   THR   289   48.244   25.472   93.177   1   26.62       4869   O   THR   289   47.901   25.064   92.064   1   25.36       4870   N   SER   290   49.414   26.071   93.398   1   26.88       4871   CA   SER   290   50.364   26.267   92.311   1   29.96       4872   CB   SER   290   51.62   26.999   92.811   1   29.73       4873   OG   SER   290   52.346   26.212   93.745   1   32.26       4874   C   SER   290   50.751   24.918   91.69   1   30.98       4875   O   SER   290   50.92   24.818   90.476   1   31.76       4876   N   GLU   291   50.871   23.884   92.52   1   32.52       4877   CA   GLU   291   51.237   22.554   92.037   1   33.88       4878   CB   GLU   291   51.547   21.619   93.212   1   38.55       4879   CG   GLU   291   52.874   21.907   93.889   1   45.94       4880   CD   GLU   291   53.057   21.129   95.176   1   50.9       4881   OE1   GLU   291   52.907   19.884   95.147   1   54.99       4882   OE2   GLU   291   53.354   21.764   96.216   1   53.85       4883   C   GLU   291   50.156   21.932   91.17   1   33.08       4884   O   GLU   291   50.446   21.261   90.174   1   31.43       4885   N   GLU   292   48.903   22.145   91.543   1   30.81       4886   CA   GLU   292   47.812   21.589   90.76   1   30.36       4887   CB   GLU   292   46.506   21.669   91.553   1   30.62       4888   CG   GLU   292   46.6   20.987   92.913   1   31.48       4889   CD   GLU   292   45.324   21.103   93.725   1   31.8       4890   OE1   GLU   292   44.779   22.219   93.816   1   31.91       4891   OE2   GLU   292   44.874   20.084   94.283   1   32.52       4892   C   GLU   292   47.703   22.341   89.43   1   29.31       4893   O   GLU   292   47.383   21.748   88.401   1   29.71       4894   N   MET   293   47.98   23.641   89.451   1   28.6       4895   CA   MET   293   47.929   24.44   88.231   1   29.31       4896   CB   MET   293   48.135   25.927   88.545   1   28.13       4897   CG   MET   293   46.909   26.626   89.168   1   24.99       4898   SD   MET   293   45.459   26.71   88.062   1   24.87       4899   CE   MET   293   46.03   27.955   86.905   1   21.91       4900   C   MET   293   49.023   23.952   87.274   1   31.81       4901   O   MET   293   48.787   23.823   86.068   1   30.75       4902   N   LYS   294   50.21   23.674   87.812   1   32.56       4903   CA   LYS   294   51.323   23.185   86.995   1   35.27       4904   CB   LYS   294   52.593   23.014   87.837   1   38.67       4905   CG   LYS   294   53.627   24.11   87.651   1   44.7       4906   CD   LYS   294   53.13   25.447   88.174   1   49.7       4907   CE   LYS   294   54.232   26.508   88.12   1   52.73       4908   NZ   LYS   294   54.689   26.815   86.725   1   54.6       4909   C   LYS   294   50.978   21.852   85.356   1   33.58       4910   O   LYS   294   51.315   21.604   85.201   1   33.97       4911   N   ALA   295   50.308   20.993   87.116   1   32.23       4812   CA   ALA   295   49.921   19.686   86.62   1   31.87       4913   CB   ALA   295   49.215   18.892   87.716   1   31.59       4914   C   ALA   295   49.004   19.833   85.411   1   32.06       4915   O   ALA   295   49.146   19.111   84.424   1   31.65       4916   N   ILE   296   48.067   20.773   85.485   1   30.84       4917   CA   ILE   296   47.132   20.974   84.386   1   29.42       4918   CB   ILE   296   45.933   21.843   84.826   1   28.15       4919   CG2   ILE   296   44.935   21.981   83.675   1   26.2       4920   CG1   ILE   296   45.245   21.179   86.019   1   26.62       4921   CD1   ILE   296   44.21   22.059   86.722   1   27.4       4922   C   ILE   296   47.816   21.58   83.163   1   30.13       4923   O   ILE   296   47.461   21.245   82.033   1   30.65       4924   N   ASP   297   48.79   22.461   83.387   1   29.89       4925   CA   ASP   297   49.539   23.063   82.291   1   32.57       4926   CB   ASP   297   50.595   24.05   82.798   1   34.19       4927   CG   ASP   297   50.013   25.38   83.218   1   36.04       4928   OD1   ASP   297   48.93   25.756   82.727   1   37.57       4929   OD2   ASP   297   50.664   26.062   84.034   1   37.05       4930   C   ASP   297   50.271   21.981   81.502   1   33.26       4931   O   ASP   297   50.524   22.146   80.315   1   33.27       4932   N   GLY   298   50.62   20.886   82.172   1   33.01       4933   CA   GLY   298   51.332   19.805   81.511   1   34.38       4934   C   GLY   298   50.487   18.934   80.599   1   35.29       4935   O   GLY   298   51.021   18.081   79.886   1   36.21       4936   N   LEU   299   49.175   19.145   80.603   1   34.6       4937   CA   LEU   299   48.275   18.354   79.767   1   34.47       4938   CB   LEU   299   46.869   18.333   80.371   1   34.16       4939   CG   LEU   299   46.734   17.714   81.765   1   35.32       4940   CD1   LEU   299   45.289   17.803   82.229   1   32.85       4941   CD2   LEU   299   47.193   16.259   81.721   1   35.04       4942   C   LEU   299   48.188   18.874   78.338   1   34.82       4943   O   LEU   299   47.619   18.218   77.466   1   34.16       4944   N   ASN   300   48.751   20.051   78.099   1   34.57       4945   CA   ASN   300   48.708   20.644   76.772   1   36.54       4946   CB   ASN   300   49.519   21.939   76.744   1   35.32       4947   CG   ASN   300   49.295   22.73   75.471   1   36.34       4948   OD1   ASN   300   48.154   23.019   75.103   1   34.17       4949   ND2   ASN   300   50.381   23.094   74.796   1   35.9       4950   C   ASN   300   49.232   19.686   75.708   1   38.58       4951   O   ASN   300   50.356   19.193   75.799   1   38.3       4952   N   ARG   301   48.418   19.431   74.692   1   40.03       4953   CA   ARG   301   48.818   18.522   73.628   1   42.19       4954   CB   ARG   301   48.187   17.146   73.864   1   43.22       4955   CG   ARG   301   46.685   17.187   74.009   1   45.6       4956   CD   ARG   301   46.086   15.795   74.05   1   48.02       4957   NE   ARG   301   46.388   15.087   75.288   1   51.11       4958   CZ   ARG   301   46.014   13.835   75.54   1   52.67       4959   NH1   ARG   301   45.323   13.148   74.636   1   53.22       4960   NH2   ARG   301   46.327   13.272   76.697   1   52.78       4961   C   ARG   301   48.428   19.053   72.255   1   42.63       4962   O   ARG   301   48.392   18.306   71.278   1   42.73       4963   N   ASN   302   48.137   20.347   72.194   1   42.33       4964   CA   ASN   302   47.755   21.001   70.949   1   43.77       4965   CB   ASN   302   48.964   21.121   70.019   1   46.96       4966   CG   ASN   302   49.916   22.223   70.447   1   50.49       4967   OD1   ASN   302   50.467   22.193   71.547   1   52.26       4968   ND2   ASN   302   50.112   23.208   69.574   1   52.86       4969   C   ASN   302   46.614   20.321   70.211   1   41.81       4970   O   ASN   302   46.722   20.03   69.023   1   42.49       4971   N   VAL   303   45.523   20.069   70.922   1   40.06       4972   CA   VAL   303   44.349   19.447   70.327   1   38.45       4973   CB   VAL   303   43.776   18.329   71.229   1   38.96       4974   CG1   VAL   303   42.399   17.904   70.734   1   38.55       4975   CG2   VAL   303   44.716   17.133   71.229   1   39.24       4976   C   VAL   303   43.271   20.511   70.123   1   37.41       4977   O   VAL   303   42.66   20.987   71.085   1   36.9       4978   N   ARG   304   43.046   20.879   68.867   1   35.2       4979   CA   ARG   304   42.042   21.878   68.524   1   32.11       4980   CB   ARG   304   42.571   22.781   67.4   1   32.3       4981   CG   ARG   304   41.675   23.962   67.063   1   30.26       4982   CD   ARG   304   42.164   24.706   65.825   1   28.43       4983   NE   ARG   304   43.37   25.511   66.014   1   26.71       4984   CZ   ARG   304   43.421   26.658   66.688   1   28.86       4985   NH1   ARG   304   42.325   27.151   67.262   1   27.75       4986   NH2   ARG   304   44.563   27.331   66.759   1   26.89       4987   C   ARG   304   40.795   21.128   68.067   1   31.89       4988   O   ARG   304   40.83   20.406   67.073   1   31.75       4989   N   TYR   305   39.701   21.275   68.806   1   29.48       4990   CA   TYR   305   38.454   20.597   68.455   1   30.06       4991   CB   TYR   305   37.511   20.533   69.661   1   29.82       4992   CG   TYR   305   38.005   19.656   70.789   1   32.23       4993   CD1   TYR   305   38.144   18.275   70.623   1   32.6       4994   CE1   TYR   305   38.617   17.469   71.66   1   34.66       4995   CD2   TYR   305   38.349   20.209   72.021   1   32.53       4996   CE2   TYR   305   38.821   19.416   73.063   1   33.64       4997   CZ   TYR   305   38.954   18.05   72.877   1   34.42       4998   OH   TYR   305   39.43   17.272   73.905   1   36.03       4999   C   TYR   305   37.716   21.261   67.294   1   29.99       5000   O   TYR   305   37.137   20.577   66.453   1   29.95       5001   N   LEU   306   37.721   22.59   67.26   1   29.06       5002   CA   LEU   306   37.039   23.324   66.198   1   29.57       5003   CB   LEU   306   36.143   24.412   66.794   1   31.17       5004   CG   LEU   306   34.832   23.902   67.379   1   35.1       5005   CD1   LEU   306   34.23   24.953   68.278   1   36.46       5006   CD2   LEU   306   33.872   23.544   66.246   1   35.02       5007   C   LEU   306   38.018   23.955   65.225   1   28.82       5008   O   LEU   306   38.512   25.056   65.458   1   28.22       5009   N   THR   307   38.294   23.248   64.134   1   28.38       5010   CA   THR   307   39.219   23.737   63.122   1   29.36       5011   CB   THR   307   39.927   22.568   62.409   1   31.79       5012   OG1   THR   307   38.942   21.752   61.763   1   33.76       5013   CG2   THR   307   40.713   21.722   63.409   1   33.07       5014   C   THR   307   38.488   24.56   62.068   1   29.69       5015   O   THR   307   39.082   25.423   61.421   1   30.12       5016   N   LEU   308   37.2   24.286   61.889   1   30.15       5017   CA   LEU   308   36.406   25.01   60.9   1   31.95       5018   CB   LEU   308   36.16   26.452   61.374   1   33.81       5019   CG   LEU   308   35.248   26.604   62.606   1   35.34       5020   CD1   LEU   308   35.35   28.004   63.175   1   36.3       5021   CD2   LEU   308   33.816   26.282   62.205   1   35.3       5022   C   LEU   308   37.143   25.035   59.562   1   31.91       5023   O   LEU   308   37.14   26.052   58.868   1   30.16       5024   N   ASP   309   37.759   23.91   59.205   1   33.18       5025   CA   ASP   309   38.537   23.804   57.971   1   34.02       5026   CB   ASP   309   39.256   22.455   57.915   1   37.49       5027   CG   ASP   309   38.383   21.323   58.372   1   40       5028   OD1   ASP   309   37.235   21.222   57.889   1   42.35       5029   OD2   ASP   309   38.845   20.528   59.218   1   46.49       5030   C   ASP   309   37.75   24.022   56.685   1   34.37       5031   O   ASP   309   38.343   24.13   55.618   1   33.61       5032   N   ILE   310   36.424   24.09   56.773   1   33.33       5033   CA   ILE   310   35.634   24.335   55.576   1   33.67       5034   CB   ILE   310   34.132   24.112   55.812   1   35.32       5035   CG2   ILE   310   33.863   22.644   56.1   1   36.47       5036   CG1   ILE   310   33.648   24.997   56.96   1   37.09       5037   CD1   ILE   310   32.143   25.055   57.086   1   39.69       5038   C   ILE   310   35.852   25.788   55.148   1   33.45       5039   O   ILE   310   35.505   26.174   54.031   1   32.28       5040   N   PHE   311   36.429   26.59   56.044   1   30.63       5041   CA   PHE   311   36.714   27.988   55.754   1   28.67       5042   CB   PHE   311   36.357   28.869   56.954   1   31.17       5043   CG   PHE   311   34.881   28.975   57.205   1   32.87       5044   CD1   PHE   311   34.05   29.586   56.274   1   33.44       5045   CD2   PHE   311   34.317   28.442   58.361   1   34.61       5046   CE1   PHE   311   32.669   29.667   56.485   1   34.53       5047   CE2   PHE   311   32.937   28.515   58.586   1   35.78       5048   CZ   PHE   311   32.111   29.131   57.643   1   35.21       5049   C   PHE   311   38.178   28.186   55.397   1   28.06       5050   O   PHE   311   38.64   29.309   55.246   1   28.42       5051   N   ALA   312   38.903   27.085   55.264   1   29.48       5052   CA   ALA   312   40.314   27.14   54.914   1   30.76       5053   CB   ALA   312   40.959   25.781   55.143   1   31.54       5054   C   ALA   312   40.429   27.539   53.446   1   30.85       5055   O   ALA   312   39.536   27.259   52.644   1   30.36       5056   N   GLY   313   41.529   28.194   53.101   1   31.63       5057   CA   GLY   313   41.727   28.627   51.729   1   31.95       5058   C   GLY   313   42.057   30.1   51.706   1   31.33       5059   O   GLY   313   43.196   30.469   51.426   1   31.62       5060   N   PRO   314   41.077   30.974   51.999   1   30.84       5061   CD   PRO   314   39.679   30.671   52.344   1   31.01       5062   CA   PRO   314   41.305   32.421   52.008   1   31.17       5063   CB   PRO   314   39.965   32.982   52.474   1   29.75       5064   CG   PRO   314   38.993   31.966   52.028   1   29.65       5065   C   PRO   314   42.432   32.769   52.98   1   31.38       5066   O   PRO   314   42.672   32.055   53.953   1   30.86       5067   N   PRO   315   43.124   33.885   52.739   1   31.94       5068   CD   PRO   315   42.93   34.835   51.63   1   32.54       5069   CA   PRO   315   44.226   34.307   53.602   1   31.85       5070   CB   PRO   315   44.798   35.506   52.854   1   32.13       5071   CG   PRO   315   43.587   36.073   52.171   1   34.34       5072   C   PRO   315   43.864   34.626   55.059   1   31.91       5073   O   PRO   315   44.717   34.528   55.938   1   31.53       5074   N   ASN   316   42.614   34.989   55.332   1   30.71       5075   CA   ASN   316   42.233   35.312   56.706   1   29.74       5076   CB   ASN   316   41.022   36.243   56.723   1   31.09       5077   CG   ASN   316   41.393   37.672   56.399   1   31.99       5078   OD1   ASN   316   42.564   38.034   56.441   1   32.66       5079   ND2   ASN   316   40.395   38.497   56.086   1   34.21       5080   C   ASN   316   41.957   34.11   57.601   1   29.62       5081   O   ASN   316   41.608   34.281   58.769   1   29.58       5082   N   TYR   317   42.1   32.9   57.066   1   27.38       5083   CA   TYR   317   41.873   31.704   57.875   1   27.4       5084   CB   TYR   317   42.12   30.438   57.051   1   26.75       5085   CG   TYR   317   41.891   29.164   57.836   1   27.13       5086   CD1   TYR   317   40.608   28.797   58.25   1   24.51       5087   CE1   TYR   317   40.4   27.65   59.012   1   28.82       5088   CD2   TYR   317   42.961   28.35   58.204   1   26.21       5089   CE2   TYR   317   42.766   27.206   58.966   1   26.26       5090   CZ   TYR   317   41.489   26.863   59.365   1   26.86       5091   OH   TYR   317   41.294   25.735   60.111   1   27.26       5092   C   TYR   317   42.88   31.813   59.031   1   27.77       5093   O   TYR   317   44.087   31.855   58.81   1   28.39       5094   N   PRO   318   42.388   31.843   60.279   1   27.63       5095   CD   PRO   318   40.989   31.528   60.603   1   27.38       5096   CA   PRO   318   43.178   31.97   61.51   1   28.3       5097   CB   PRO   318   42.143   32.403   62.553   1   26.85       5098   CG   PRO   318   40.796   32.286   61.879   1   29.32       5099   C   PRO   318   44.027   30.842   62.082   1   27.97       5100   O   PRO   318   45.028   31.113   62.744   1   28.92       5101   N   PHE   319   43.641   29.598   61.843   1   28.42       5102   CA   PHE   319   44.342   28.487   62.463   1   30.82       5103   CB   PHE   319   43.32   27.395   62.797   1   28.73       5104   CG   PHE   319   42.063   27.923   63.457   1   27.08       5105   CD1   PHE   319   42.128   28.942   64.415   1   25.83       5106   CD2   PHE   319   40.823   27.395   63.13   1   26.76       5107   CE1   PHE   319   40.967   29.426   65.038   1   25.52       5108   CE2   PHE   319   39.658   27.865   63.743   1   27.67       5109   CZ   PHE   319   39.732   28.881   64.698   1   26.45       5110   C   PHE   319   45.54   27.901   61.732   1   33.58       5111   O   PHE   319   45.967   26.788   62.032   1   34.36       5112   N   SER   320   46.093   28.657   60.793   1   34.56       5113   CA   SER   320   47.256   28.202   60.051   1   37.51       5114   CB   SER   320   47.259   28.797   58.642   1   37.72       5115   OG   SER   320   46.36   28.1   57.807   1   40.24       5116   C   SER   320   48.541   28.59   60.766   1   37.79       5117   O   SER   320   49.473   27.796   60.851   1   38.27       5118   N   ASP   321   48.588   29.812   61.283   1   38.88       5119   CA   ASP   321   49.777   30.293   61.976   1   39.93       5120   CB   ASP   321   49.672   31.796   62.227   1   40.64       5121   CG   ASP   321   49.532   32.588   60.946   1   41.88       5122   OD1   ASP   321   49.799   32.027   59.863   1   44.55       5123   OD2   ASP   321   49.165   33.777   61.016   1   42.35       5124   C   ASP   321   50.001   29.572   63.298   1   40.65       5125   O   ASP   321   49.101   28.9   63.805   1   40.61       5126   N   GLU   322   51.205   29.709   63.848   1   40.39       5127   CA   GLU   322   51.53   29.073   65.116   1   41.97       5128   CB   GLU   322   52.98   29.355   65.502   1   44.61       5129   CG   GLU   322   53.38   28.734   66.829   1   50.18       5130   CD   GLU   322   54.791   29.095   67.243   1   53.4       5131   OE1   GLU   322   55.099   30.304   67.33   1   56.08       5132   OE2   GLU   322   55.589   28.166   67.483   1   56.29       5133   C   GLU   322   50.593   29.577   66.213   1   40.5       5134   O   GLU   322   50.201   28.817   67.09   1   40.87       5135   N   TYR   323   50.245   30.859   66.162   1   39.54       5136   CA   TYR   323   49.331   31.443   67.135   1   38.14       5137   CB   TYR   323   49.979   31.505   68.527   1   37.34       5138   CG   TYR   323   50.918   32.665   68.752   1   37.74       5139   CD1   TYR   323   50.5   33.802   69.44   1   37.26       5140   CE1   TYR   323   51.357   34.888   69.632   1   38.97       5141   CD2   TYR   323   52.223   32.634   68.258   1   39.61       5142   CE2   TYR   323   53.087   33.712   68.442   1   41.09       5143   CZ   TYR   323   52.647   34.837   69.13   1   41.71       5144   OH   TYR   323   53.502   35.906   69.302   1   44.4       5145   C   TYR   323   48.924   32.833   66.657   1   37.95       5146   O   TYR   323   47.966   33.404   67.224   1   37.2       5147   OXT   TYR   323   49.574   33.327   65.708   1   37.14       5148       5149   AP   NAP   1   52.419   49.694   102.271   1   25.98       5150   AO1   NAP   1   53.278   48.524   101.978   1   24.03       5151   AO2   NAP   1   51.09   49.77   101.716   1   25.27       5152   AO5*   NAP   1   53.318   50.97   101.846   1   29.25       5153   AC5*   NAP   1   52.909   52.29   102.189   1   30.23       5154   AC4*   NAP   1   54.039   53.219   101.868   1   31.8       5155   AO4*   NAP   1   54.201   53.232   100.438   1   31.27       5156   AC3*   NAP   1   53.762   54.613   102.308   1   32.3       5157   AO3*   NAP   1   54.958   55.28   102.766   1   35.28       5158   AC2*   NAP   1   53.241   55.281   101.067   1   32.59       5159   AO2*   NAP   1   53.547   56.682   100.997   1   30.26       5160   AC1*   NAP   1   53.986   54.564   99.946   1   31.68       5161   AN9   NAP   1   53.225   54.45   98.65   1   33.36       5162   AC8   NAP   1   51.869   54.208   98.446   1   32.69       5163   AN7   NAP   1   51.537   54.195   97.183   1   33.6       5164   AC5   NAP   1   52.709   54.423   96.504   1   33.07       5165   AC6   NAP   1   53.008   54.54   95.114   1   33       5166   AN6   NAP   1   52.071   54.44   94.174   1   31.6       5167   AN1   NAP   1   54.308   54.77   94.756   1   32.37       5168   AC2   NAP   1   55.276   54.886   95.702   1   32.87       5169   AN3   NAP   1   55.073   54.811   97.031   1   32.45       5170   AC4   NAP   1   53.756   54.576   97.372   1   33.11       5171   O3   NAP   1   52.428   49.962   103.878   1   28.24       5172   NP   NAP   1   51.74   49.352   105.191   1   25.93       5173   NO1   NAP   1   51.185   50.499   105.907   1   29.68       5174   NO2   NAP   1   52.866   48.563   105.843   1   27.83       5175   NO5*   NAP   1   50.679   48.252   104.748   1   24.61       5176   NC5*   NAP   1   49.41   48.673   104.185   1   22.4       5177   NC4*   NAP   1   48.232   48.457   105.153   1   21.8       5178   NO4*   NAP   1   48.282   47.111   105.609   1   22.69       5179   NC3*   NAP   1   48.329   49.251   106.458   1   21.8       5180   NO3*   NAP   1   47.991   50.629   106.38   1   19.92       5181   NC2*   NAP   1   47.396   48.489   107.334   1   22.04       5182   NO2*   NAP   1   46.026   48.804   107.052   1   20.53       5183   NC1*   NAP   1   47.735   47.016   106.914   1   22.46       5184   NN1   NAP   1   48.727   46.402   107.841   1   23.71       5185   NC2   NAP   1   48.212   45.362   108.609   1   22.55       5186   NC3   NAP   1   49.096   44.691   109.529   1   23.34       5187   NC7   NAP   1   48.639   43.554   110.331   1   23.95       5188   NO7   NAP   1   49.358   43.043   111.198   1   23.51       5189   NN7   NAP   1   47.421   43.016   110.121   1   21.98       5190   NC4   NAP   1   50.447   45.146   109.629   1   24.05       5191   NC5   NAP   1   50.944   46.129   108.834   1   25.29       5192   NC6   NAP   1   50.107   46.751   107.934   1   24.49       5193   AP2*   NAP   1   52.398   57.76   100.976   1   33.17       5194   AOP1   NAP   1   51.433   57.516   102.079   1   30.43       5195   AOP2   NAP   1   53.228   58.97   101.146   1   35.2       5196   AOP3   NAP   1   51.84   57.625   99.618   1   31.14       5197       5198   AP   NAP   1   31.491   23.321   76.234   1   26.92       5199   AO1   NAP   1   32.959   23.112   76.092   1   23.4       5200   AO2   NAP   1   31.023   24.344   77.147   1   28.39       5201   AO5*   NAP   1   30.891   21.867   76.578   1   27.18       5202   AC5*   NAP   1   29.483   21.663   76.586   1   30.27       5203   AC4*   NAP   1   29.226   20.199   76.739   1   31.97       5204   AO4*   NAP   1   29.66   19.821   78.06   1   30.87       5205   AC3*   NAP   1   27.783   19.857   76.621   1   31.72       5206   AO3*   NAP   1   27.59   18.576   75.977   1   34.57       5207   AC2*   NAP   1   27.318   19.788   78.042   1   31.52       5208   AO2*   NAP   1   26.267   18.844   78.253   1   31.04       5209   AC1*   NAP   1   28.551   19.293   78.793   1   31.36       5210   AN9   NAP   1   28.676   19.783   80.211   1   31.18       5211   AC8   NAP   1   28.366   21.032   80.732   1   31.01       5212   AN7   NAP   1   28.585   21.116   82.02   1   32.83       5213   AC5   NAP   1   29.061   19.882   82.38   1   31.98       5214   AC6   NAP   1   29.459   19.338   83.632   1   32.42       5215   AN6   NAP   1   29.398   20.04   84.756   1   31.38       5216   AN1   NAP   1   29.904   18.042   83.662   1   31.81       5217   AC2   NAP   1   29.958   17.318   82.516   1   31.07       5218   AN3   NAP   1   29.59   17.76   81.296   1   30.66       5219   AC4   NAP   1   29.139   19.053   81.298   1   31.27       5220   O3   NAP   1   30.829   23.475   74.756   1   26.84       5221   NP   NAP   1   30.744   24.558   73.599   1   26.56       5222   NO1   NAP   1   29.325   24.632   73.216   1   30.95       5223   NO2   NAP   1   31.715   24.056   72.551   1   28.97       5224   NO5*   NAP   1   31.381   25.925   74.121   1   24.33       5225   NC5*   NAP   1   30.623   26.74   75.053   1   24.07       5226   NC4*   NAP   1   30.044   28.012   74.415   1   21.96       5227   NO4*   NAP   1   31.116   28.688   73.763   1   21.63       5228   NC3*   NAP   1   29.051   27.781   73.281   1   21.44       5229   NO3*   NAP   1   27.731   27.385   73.666   1   20.81       5230   NC2*   NAP   1   29.091   29.1   72.586   1   21.74       5231   NO2*   NAP   1   28.314   30.09   73.265   1   20.71       5232   NC1*   NAP   1   30.618   29.432   72.663   1   21.5       5233   NN1   NAP   1   31.326   29.023   71.419   1   24.29       5234   NC2   NAP   1   31.797   30.089   70.659   1   22.71       5235   NC3   NAP   1   32.496   29.798   69.439   1   24.24       5236   NC7   NAP   1   33.068   30.865   68.614   1   24.12       5237   NO7   NAP   1   33.584   30.618   67.517   1   24.87       5238   NN7   NAP   1   33.082   32.142   69.046   1   20.78       5239   NC4   NAP   1   32.651   28.43   69.054   1   23.18       5240   NC5   NAP   1   32.232   27.4   69.831   1   25.36       5241   NC6   NAP   1   31.575   27.679   71.012   1   24.89       5242   AP2*   NAP   1   24.846   19.298   78.758   1   31.12       5243   AOP1   NAP   1   24.346   20.449   77.935   1   29.71       5244   AOP2   NAP   1   24.129   18.035   78.559   1   33.02       5245   AOP3   NAP   1   25.095   19.605   80.174   1   30.62       5246       5247   OH2   TIP   1   45.001   40.378   118.313   1   15.26       5248   OH2   TIP   2   32.516   38.304   123.853   1   14.81       5249   OH2   TIP   3   32.919   34.403   108.28   1   15.52       5250   OH2   TIP   4   41.837   41.292   105.623   1   18.99       5251   OH2   TIP   5   30.917   36.384   75.698   1   20.4       5252   OH2   TIP   6   30.328   45.984   78.024   1   20.83       5253   OH2   TIP   7   33.466   41.619   90.824   1   19.67       5254   OH2   TIP   8   37.501   44.346   125.316   1   20.26       5255   OH2   TIP   9   37.393   32.625   101.943   1   18.16       5256   OH2   TIP   10   40.909   45.982   122.694   1   18.11       5257   OH2   TIP   11   44.528   38.79   126.817   1   23.06       5258   OH2   TIP   12   53.521   36.063   107.923   1   19.33       5259   OH2   TIP   13   55.414   39.924   108.941   1   18.8       5260   OH2   TIP   14   24.457   39.716   64.921   1   23.35       5261   OH2   TIP   15   32.145   36.847   61.428   1   18.79       5262   OH2   TIP   16   41.349   44.99   127.363   1   19.2       5263   OH2   TIP   18   31.821   40.243   104.727   1   19.6       5264   OH2   TIP   19   40.383   45.522   119.941   1   17.85       5265   OH2   TIP   20   41.038   43.926   105.074   1   21.25       5266   OH2   TIP   21   52.798   38.523   108.612   1   21.6       5267   OH2   TIP   22   24.578   34.991   52.277   1   27.2       5268   OH2   TIP   23   43.566   46.144   116.665   1   18.79       5269   OH2   TIP   24   38.407   48.16   96.072   1   21.13       5270   OH2   TIP   25   27.004   35.105   64.406   1   19.85       5271   OH2   TIP   26   35.011   48.336   73.361   1   19.97       5272   OH2   TIP   27   32.296   48.154   124.555   1   21.12       5273   OH2   TIP   28   25.256   38.826   62.122   1   20.05       5274   OH2   TIP   29   39.109   24.774   80.543   1   21.81       5275   OH2   TIP   30   42.063   39.776   126.839   1   22.87       5276   OH2   TIP   31   46.745   46.451   128.813   1   23.39       5277   OH2   TIP   32   50.371   47.093   101.553   1   25.02       5278   OH2   TIP   34   40.126   44.155   77.856   1   23.06       5279   OH2   TIP   35   42.375   29.781   68.382   1   25.35       5280   OH2   TIP   36   38.086   47.952   120.461   1   22.59       5281   OH2   TIP   37   24.488   38.637   59.36   1   25.22       5282   OH2   TIP   38   33.449   37.051   74.61   1   20.61       5283   OH2   TIP   39   31.1   36.961   121.752   1   22.46       5284   OH2   TIP   40   22.204   25.909   36.991   1   23.75       5285   OH2   TIP   41   39.567   26.563   67.439   1   22.52       5286   OH2   TIP   42   41.986   22.37   117.586   1   25.15       5287   OH2   TIP   43   39.491   29.267   68.378   1   22.32       5288   OH2   TIP   44   32.736   26.776   117.39   1   21.24       5289   OH2   TIP   45   52.291   33.953   109.25   1   24.65       5290   OH2   TIP   46   28.534   35.148   85.678   1   21.99       5291   OH2   TIP   47   38.513   51.843   118.035   1   29.58       5292   OH2   TIP   48   58.9   36.787   94.782   1   26.72       5293   OH2   TIP   49   45.997   29.479   122.242   1   25.6       5294   OH2   TIP   50   37.564   23.032   108.863   1   31.22       5295   OH2   TIP   51   53.34   43.038   96.412   1   25.97       5296   OH2   TIP   52   38.245   46.005   93.947   1   26.92       5297   OH2   TIP   53   33.17   26.364   77.101   1   23.27       5298   OH2   TIP   54   30.792   35.957   87.521   1   25.27       5299   OH2   TIP   55   34.833   27.951   47.706   1   26.42       5300   OH2   TIP   56   28.786   46.17   103.396   1   23.32       5301   OH2   TIP   57   44.266   34.136   98.337   1   26.71       5302   OH2   TIP   58   53.209   26.911   111.536   1   27.08       5303   OH2   TIP   59   38.28   46.235   117.616   1   20.29       5304   OH2   TIP   60   45.846   29.481   68.533   1   25.82       5305   OH2   TIP   61   39.477   24.73   123.6   1   24.13       5306   OH2   TIP   62   43.143   32.069   67.027   1   28.39       5307   OH2   TIP   63   33.587   31.372   107.145   1   25.01       5308   OH2   TIP   64   44.207   34.772   130.949   1   27.02       5309   OH2   TIP   65   55.271   33.285   106.717   1   26.54       5310   OH2   TIP   66   51.566   52.972   106.675   1   34.06       5311   OH2   TIP   67   40.855   48.113   126.206   1   39.94       5312   OH2   TIP   68   39.093   47.851   123.163   1   26.75       5313   OH2   TIP   69   54.844   31.2   103.265   1   28.75       5314   OH2   TIP   70   19.433   36.954   65.541   1   30.63       5315   OH2   TIP   71   41.513   46.621   82.033   1   29.13       5316   OH2   TIP   72   39.688   35.104   85.306   1   32.16       5317   OH2   TIP   73   42.495   49.189   124.242   1   22.77       5318   OH2   TIP   74   27.176   49.553   59.439   1   29.39       5319   OH2   TIP   75   32.193   21.851   46.155   1   34.18       5320   OH2   TIP   76   31.155   26.326   40.579   1   33.16       5321   OH2   TIP   77   53.856   31.665   108.599   1   28.69       5322   OH2   TIP   78   45.803   31.563   67.006   1   30.59       5323   OH2   TIP   79   37.812   46.835   90.383   1   32.74       5324   OH2   TIP   80   34.283   25.635   49.031   1   30.24       5325   OH2   TIP   81   48.808   44.792   79.805   1   28.33       5326   OH2   TIP   82   47.473   28.776   92.601   1   29.5       5327   OH2   TIP   83   38.546   38.877   131.989   1   27.52       5328   OH2   TIP   84   40.089   25.09   97.779   1   24.84       5329   OH2   TIP   85   30.793   29.787   118.751   1   29.98       5330   OH2   TIP   86   47.286   55.22   112.543   1   31.6       5331   OH2   TIP   87   42.753   37.02   79.784   1   39.13       5332   OH2   TIP   88   35.057   16.558   77.386   1   31.6       5333   OH2   TIP   89   53.713   38.681   131.57   1   33.22       5334   OH2   TIP   90   29.118   41.306   54.163   1   32       5335   OH2   TIP   91   12.943   37.742   72.249   1   30.26       5336   OH2   TIP   92   51.078   31.946   123.26   1   27.8       5337   OH2   TIP   93   27.2   23.212   73.011   1   34.31       5338   OH2   TIP   94   22.033   35.651   87.698   1   32.6       5339   OH2   TIP   95   20.237   42.493   89.338   1   36.3       5340   OH2   TIP   96   60.838   48.524   101.659   1   30.33       5341   OH2   TIP   97   51.931   24.631   101.105   1   35.53       5342   OH2   TIP   98   28.693   34.432   88.763   1   39.11       5343   OH2   TIP   99   23.52   28.524   54.874   1   38.75       5344   OH2   TIP   100   24.19   45.506   81.007   1   28.77       5345   OH2   TIP   101   56.073   53.112   92.754   1   34.65       5346   OH2   TIP   102   48.516   30.266   71.62   1   34.65       5347   OH2   TIP   103   23.686   42.794   57.713   1   32.93       5348   OH2   TIP   104   31.063   35.267   91.149   1   31.56       5349   OH2   TIP   105   27.649   34.013   105.836   1   30.01       5350   OH2   TIP   106   34.803   30.893   97.929   1   37.48       5351   OH2   TIP   107   34.287   53.842   96.009   1   34.32       5352   OH2   TIP   108   35.036   22.425   62.625   1   35.66       5353   OH2   TIP   109   37.983   18.029   65.397   1   32.91       5354   OH2   TIP   110   47.128   33.366   123.654   1   35.1       5355   OH2   TIP   111   36.675   21.183   113.083   1   30.61       5356   OH2   TIP   112   29.181   34.831   124.926   1   45.05       5357   OH2   TIP   113   23.584   22.96   38.857   1   36.5       5358   OH2   TIP   114   16.564   46.517   84.468   1   36.53       5359   OH2   TIP   115   27.043   49.684   108.942   1   32.55       5360   OH2   TIP   116   33.094   58.091   113.339   1   28.91       5361   OH2   TIP   117   49.645   33.751   80.775   1   34.36       5362   OH2   TIP   118   30.066   42.223   103.534   1   27.54       5363   OH2   TIP   119   35.876   16.599   74.461   1   32.92       5364   OH2   TIP   120   26.7   38.417   110.27   1   27.97       5365   OH2   TIP   121   59.389   50.34   99.207   1   31.84       5366   OH2   TIP   122   32.506   16.893   84.875   1   32.8       5367   OH2   TIP   123   28.477   49.93   119.857   1   33.02       5368   OH2   TIP   124   28.226   46.593   79.868   1   31.4       5369   OH2   TIP   125   47.312   22.624   79.641   1   32.14       5370   OH2   TIP   126   43.274   38.481   93.349   1   36.38       5371   OH2   TIP   127   24.394   39.895   54.703   1   31.22       5372   OH2   TIP   128   62.576   44.383   109.622   1   38.29       5373   OH2   TIP   129   39.313   53.697   63.477   1   35.69       5374   OH2   TIP   130   56.034   30.407   114.992   1   35.51       5375   OH2   TIP   131   58.55   44.64   114.05   1   33.72       5376   OH2   TIP   132   26.613   36.991   107.639   1   33.13       5377   OH2   TIP   133   28.155   52.064   73.725   1   40.93       5378   OH2   TIP   134   26.29   22.128   38.289   1   35.09       5379   OH2   TIP   135   41.992   44.005   85.943   1   38.29       5380   OH2   TIP   136   23.79   53.196   102.275   1   35.55       5381   OH2   TIP   137   38.259   49.291   73.759   1   33.97       5382   OH2   TIP   138   31.186   39.8   53.512   1   28.3       5383   OH2   TIP   139   49.832   29.79   94.84   1   37.52       5384   OH2   TIP   140   51.065   28.329   72.978   1   46.98       5385   OH2   TIP   141   46.66   53.496   98.395   1   31.75       5386   OH2   TIP   142   46.597   30.116   64.655   1   32.73       5387   OH2   TIP   143   25.375   27.537   35.355   1   33.43       5388   OH2   TIP   144   21.898   26.93   69.113   1   38.87       5389   OH2   TIP   145   52.835   55.056   106.028   1   36.26       5390   OH2   TIP   146   37.772   32.55   96.88   1   38.37       5391   OH2   TIP   147   55.816   31.008   110.284   1   35.26       5392   OH2   TIP   148   42.571   41.266   84.444   1   39.27       5393   OH2   TIP   149   57.062   30.146   101.179   1   34.53       5394   OH2   TIP   150   19.557   23.851   68.74   1   38.35       5395   OH2   TIP   151   53.208   33.684   91.837   1   35.29       5396   OH2   TIP   152   26.885   25.98   82.305   1   28.44       5397   OH2   TIP   153   60.656   41.047   133.574   1   43.29       5398   OH2   TIP   154   50.192   35.856   83.36   1   30.89       5399   OH2   TIP   155   46.431   31.285   59.935   1   38.03       5400   OH2   TIP   156   58.677   32.63   120.469   1   39.94       5401   OH2   TIP   157   26.809   34.112   97.918   1   41.53       5402   OH2   TIP   158   33.884   52.712   77.023   1   35.19       5403   OH2   TIP   159   38.057   49.152   93.115   1   41.66       5404   OH2   TIP   160   45.468   33.014   90.44   1   46.45       5405   OH2   TIP   161   11.785   42.754   80.598   1   37.64       5406   OH2   TIP   162   24.311   36.374   91.676   1   43.49       5407   OH2   TIP   163   42.904   31.446   93.489   1   37.26       5408   OH2   TIP   164   19.008   46.343   76.831   1   32.64       5409   OH2   TIP   165   26.792   37.766   121.303   1   45.31       5410   OH2   TIP   166   49.187   35.043   63.624   1   31.95       5411   OH2   TIP   167   36.331   32.254   93.605   1   44.09       5412   OH2   TIP   168   35.186   26.215   102.521   1   43.2       5413   OH2   TIP   169   48.889   58.577   112.794   1   49.41       5414   OH2   TIP   170   52.692   49.72   130.355   1   41.72       5415   OH2   TIP   171   50.466   50.762   125.316   1   39.53       5416   OH2   TIP   172   39.495   33.029   94.392   1   34.89       5417   OH2   TIP   173   41.34   52.958   115.729   1   31.01       5418   OH2   TIP   174   34.57   29.202   41.202   1   45.68       5419   OH2   TIP   175   46.718   51.893   65.788   1   41.59       5420   OH2   TIP   176   28.069   32.273   93.383   1   41.61       5421   OH2   TIP   177   32.318   58.463   117.063   1   43.39       5422   OH2   TIP   178   44.4   43.106   133.577   1   43.84       5423   OH2   TIP   179   46.226   56.794   110.966   1   41.8       5424   OH2   TIP   180   40.422   60.788   94.759   1   37.26       5425   OH2   TIP   181   48.451   28.607   83.392   1   32.96       5426   OH2   TIP   182   24.358   56.785   99.593   1   44.73       5427   OH2   TIP   183   41.25   41.877   55.915   1   42.35       5428   OH2   TIP   184   45.973   35.217   86.966   1   42.98       5429   OH2   TIP   185   24.234   20.35   90.823   1   41.63       5430   OH2   TIP   186   20.05   26.911   71.116   1   44.24       5431   OH2   TIP   187   25.517   47.644   116.084   1   40.22       5432   OH2   TIP   188   38.148   55.74   125.016   1   50.57       5433   OH2   TIP   189   17.415   19.187   83.179   1   51.35       5434   OH2   TIP   190   40.72   36.135   53.695   1   41.2       5435   OH2   TIP   191   58.834   41.888   125.21   1   39.88       5436   OH2   TIP   192   29.41   29.727   93.858   1   48.74       5437   OH2   TIP   193   49.842   27.949   80.741   1   35.45       5438   OH2   TIP   194   37.814   39.274   54.566   1   39.68       5439   OH2   TIP   195   20.41   33.596   67.244   1   47.88       5440   OH2   TIP   196   56.399   38.41   78.303   1   47.48       5441   OH2   TIP   197   18.546   44.981   60.403   1   43.73       5442   OH2   TIP   198   23.994   49.638   108.354   1   49.51       5443   OH2   TIP   199   22.908   22.771   41.59   1   48.79       5444   OH2   TIP   200   51.09   17.174   84.254   1   51.21       5445   OH2   TIP   201   21.801   39.4   59.941   1   38.04       5446   OH2   TIP   202   59.191   44.537   116.947   1   46.96       5447   OH2   TIP   203   53.282   35.753   73.561   1   46.48       5448   OH2   TIP   204   41.701   43.375   82.55   1   42.46       5449   OH2   TIP   205   30.079   46.916   125.452   1   44.25       5450   OH2   TIP   206   52.385   19.609   89.868   1   41.23       5451   OH2   TIP   207   26.106   20.765   73.523   1   40.03       5452   OH2   TIP   208   47.982   60.086   89.854   1   35.91       5453   OH2   TIP   209   45.575   38.685   84.376   1   41.02       5454   OH2   TIP   210   50.34   34.715   124.626   1   42.79       5455   OH2   TIP   211   38.796   34.422   92.168   1   45.42       5456   OH2   TIP   212   57.681   33.9   101.661   1   43.35       5457   OH2   TIP   213   54.846   32.481   93.809   1   39.9       5458   OH2   TIP   214   18.125   49.991   70.464   1   46.3       5459   OH2   TIP   215   21.97   39.651   62.727   1   33.34       5460   OH2   TIP   216   28.842   43.327   125.062   1   45.51       5461   OH2   TIP   217   16.7   46.812   66.283   1   44.74       5462   OH2   TIP   218   30.326   44.411   91.916   1   36.28       5463   OH2   TIP   220   38.045   36.433   53.954   1   37.35       5464   OH2   TIP   221   27.518   52.423   95.841   1   36.13       5465   OH2   TIP   222   45.658   34.782   133.488   1   37.65       5466   OH2   TIP   223   40.129   53.923   117.587   1   38.41       5467   OH2   TIP   226   41.548   42.117   133.921   1   33.86       5468   OH2   TIP   227   14.866   46.35   70.169   1   47.73       5469   OH2   TIP   228   31.95   29.491   106.796   1   45.5       5470   OH2   TIP   229   21.037   21.047   41.409   1   47.05       5471   OH2   TIP   230   28.445   51.038   61.644   1   40.98       5472   OH2   TIP   231   43.854   34.88   90.224   1   49.28       5473   OH2   TIP   232   28.047   27.942   34.429   1   38.25       5474   OH2   TIP   233   12.984   24.147   67.59   1   47.73       5475   OH2   TIP   234   55.247   63.389   98.594   1   51.45       5476   OH2   TIP   235   60.396   46.828   118.097   1   43.58       5477   OH2   TIP   236   29.373   23.257   113.788   1   49.82       5478   OH2   TIP   237   51.361   59.242   106.004   1   44.98       5479   OH2   TIP   238   28.732   34.199   91.896   1   40.79       5480   OH2   TIP   239   47.85   15.242   77.784   1   47.04       5481   OH2   TIP   240   35.188   24.83   51.425   1   37.83       5482   OH2   TIP   241   53.575   29.228   116.275   1   50.9       5483   OH2   TIP   242   47.746   22.817   114.979   1   36.7       5484   OH2   TIP   243   47.14   30.391   90.416   1   51.56       5485   OH2   TIP   244   7.671   43.941   85.116   1   41.02       5486   OH2   TIP   245   31.61   30.446   99.001   1   38.13       5487   OH2   TIP   246   34.582   30.877   124.231   1   38.93       5488   OH2   TIP   247   49.066   21.06   96.132   1   42.69       5489   OH2   TIP   248   49.506   41.872   61.108   1   42.5       5490   OH2   TIP   249   32.245   34.942   125.464   1   39.7       5491   OH2   TIP   250   39.287   56.63   116.779   1   46.55       5492   OH2   TIP   251   47.334   21.723   101.703   1   49.53       5493   OH2   TIP   252   14.215   43.763   87.46   1   41.94       5494   OH2   TIP   253   52.694   63.517   94.843   1   46.38       5495   OH2   TIP   254   57.488   29.835   125.415   1   44.6       5496   OH2   TIP   255   47.278   48.74   79.314   1   47.95       5497   OH2   TIP   256   27.087   51.852   116.357   1   47.55       5498   OH2   TIP   257   41.014   51.312   87.598   1   40.75       5499   OH2   TIP   258   48.855   64.637   94.988   1   46.51       5500   OH2   TIP   259   34.326   51.133   57.401   1   49.68       5501   OH2   TIP   260   38.502   38.24   91.604   1   37.64       5502   OH2   TIP   261   24.129   45.02   113.403   1   48.05       5503   OH2   TIP   262   35.286   54.125   63.327   1   45.56       5504   OH2   TIP   253   30.663   27.704   120.762   1   45.17       5505   OH2   TIP   264   35.871   54.187   124.066   1   50.41       5506   OH2   TIP   265   21.159   41.64   58.64   1   41.93       5507   OH2   TIP   266   19.788   36.679   50.156   1   51.04       5508   OH2   TIP   267   40.486   59.384   116.678   1   55.91       5509   OH2   TIP   268   57.2   30.639   89.246   1   50.27       5510   OH2   TIP   269   40.547   51.106   73.462   1   54.93       5511   OH2   TIP   270   34.237   52.021   91.663   1   44.61       5512   OH2   TIP   271   25.491   31.111   92.578   1   50.81       5513   OH2   TIP   272   39.613   40.278   90.384   1   42.78       5514   OH2   TIP   273   34.485   12.602   83.204   1   45.2       5515   OH2   TIP   274   35.981   24.594   99.268   1   56.4       5516   OH2   TIP   275   29.035   64.519   103.226   1   47.65       5517   OH2   TIP   276   51.698   23.931   95.739   1   55.55       5518   OH2   TIP   277   33.44   19.305   115.417   1   57.07       5519   OH2   TIP   278   56.627   51.75   100.165   1   51.89       5520   OH2   TIP   279   43.5   49.937   132.076   1   47.67       5521   OH2   TIP   280   60.676   35.007   83.418   1   52.33       5522   OH2   TIP   281   14.648   51.474   77.578   1   59.77       5523   OH2   TIP   283   30.345   47.707   82.813   1   36.04       5524   OH2   TIP   284   36.004   46.202   52.162   1   41.13       5525   OH2   TIP   285   32.03   29.957   42.962   1   44.61       5526   OH2   TIP   286   48.798   35.044   85.737   1   47.24       5527   OH2   TIP   287   32.321   33.202   127.513   1   43.68       5528   OH2   TIP   288   22.068   39.15   56.277   1   50.31       5529   OH2   TIP   289   21.987   24.918   66.146   1   47.47       5530   OH2   TIP   290   15.872   33.363   67.16   1   51.12       5531   OH2   TIP   291   26.09   55.172   95.12   1   52.07       5532   OH2   TIP   292   27.583   56.238   65.392   1   49.45       5533   OH2   TIP   293   34.26   23.299   47.224   1   49.03       5534   OH2   TIP   294   57.408   31.747   105.896   1   46.8       5535   OH2   TIP   295   59.962   39.089   123.57   1   44.87       5536   OH2   TIP   296   65.976   39.468   95.276   1   44.84       5537   OH2   TIP   297   48.396   28.207   68.765   1   46.48       5538   OH2   TIP   298   42.283   19.509   65.087   1   46.86       5539   OH2   TIP   299   59.227   33.147   109.151   1   51.7       5540   OH2   TIP   300   29.15   30.207   106.468   1   50.01       5541   OH2   TIP   301   46.663   66.616   95.455   1   54.65       5542   OH2   TIP   302   26.271   35.337   122.528   1   48.4       5543   OH2   TIP   303   18.858   27.274   88.356   1   48.53       5544   OH2   TIP   304   51.926   65.647   96.319   1   53.14       5545   OH2   TIP   305   20.25   51.904   72.655   1   56.14       5546   OH2   TIP   306   34.709   22.106   59.241   1   47.81       5547   OH2   TIP   307   40.433   17.704   66.527   1   52.34       5548   OH2   TIP   308   32.003   18.215   77.58   1   52.34       5549   OH2   TIP   309   23.422   28.55   92.607   1   43.14       5550   OH2   TIP   310   47.257   20.159   98.331   1   50.52       5551   OH2   TIP   311   24.448   42.609   110.078   1   49.23       5552   OH2   TIP   312   33.517   30.6   45.341   1   51.64       5553   OH2   TIP   313   42.127   21.444   98.747   1   54.04       5554   OH2   TIP   314   18.919   43.54   58.143   1   51.11       5555   OH2   TIP   315   23.164   43.23   115.621   1   47.26       5556   OH2   TIP   316   16.176   45.107   61.852   1   53.28       5557   OH2   TIP   317   27.877   27.144   109.844   1   50.1       5558   OH2   TIP   318   67.95   50.314   103.16   1   52.74       5559   OH2   TIP   319   31.95   21.574   113.159   1   41.29       5560   OH2   TIP   320   26.046   58.454   106.489   1   47.06       5561       5562   OH2   TIP   321   31.82   45.915   98.812   1   39.55       5563   OH2   TIP   322   41.201   12.29   77.413   1   43.87       5564   OH2   TIP   323   27.105   33.922   95.152   1   48.88       5565   OH2   TIP   324   44.9   20.824   97.326   1   46.5       5566   OH2   TIP   325   45.613   40.37   134.348   1   43.36       5567   OH2   TIP   326   30.431   42.419   100.809   1   41.71       5568   OH2   TIP   327   21.97   36.04   58.009   1   49.22       5569   OH2   TIP   328   26.728   41.92   84.56   1   45.66       5570   OH2   TIP   329   44.324   37.558   86.373   1   48.13       5571   OH2   TIP   330   13.618   27.035   82.769   1   46.71       5572   OH2   TIP   331   28.796   43.32   84.297   1   51.64       5573   OH2   TIP   332   36.988   64.849   99.594   1   51.26       5574   OH2   TIP   333   39.844   50.346   81.834   1   51.93       5575   OH2   TIP   334   42.475   38.953   83.449   1   49.18       5576   OH2   TIP   335   27.186   48.853   80.722   1   43.66       5577   OH2   TIP   336   11.416   39.187   68.638   1   49.42       5578   OH2   TIP   337   22.473   55.81   101.424   1   49.76       5579   OH2   TIP   338   32.198   34.546   45.862   1   48.14       5580   OH2   TIP   339   34.936   51.874   84.774   1   48.39       5581   OH2   TIP   340   38.076   38.607   88.497   1   43.68       5582   OH2   TIP   341   30.584   45.209   101.344   1   44.22       5583   OH2   TIP   342   37.067   49.443   90.254   1   54.48                  
 
         [0110]