Method to identify modulators for human 3alpha-hydroxysteroid dehydrogenase

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

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

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.

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.

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

In one aspect the invention comprises the crystalline structure of human type III 3a-HSD and to determine its structure coordinates.

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.

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.

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

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.

Abreviations:

• Å=Ångstrom
• TIP=represents in the listings of molecule of e.g. active site a water molecule Definitions:

The following terms are also used herein:

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.

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).

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).

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.

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.

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 & 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

In order that the invention described herein may be more fully understood, the following detailed description is set forth.

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.

A. The Structure of Human type III 3a-HSD in Complex with NADP.

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.

Crystal packing reveals that human type III 3a-HSD crystallizes in a single dimmer (data in Table 1 are for the dimer).

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.

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).

B. Uses of the Structure Coordinates of Human Type III 3a-HSD

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.

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).

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.

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)).

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.

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.

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.

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 & Johnson, supra; Methods in Enzymology, vol. 114 & 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.

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.

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.

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.

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.

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.

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))

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.).

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.).

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).

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.

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.

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.

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

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'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.

The sense gene-specific primers are of the following sequences:

For the His-tagged construct:

(SEQ ID NO: 3)
5′ - ATACATATGCACCACCACCACCACCACCTCGAGGTTCTGTTCCAG
GGTCCGGATTCGAAATACCAGTGTGTG

For the non-tagged construct:

5′ - TTTCATATGGATTCGAAATACCAGTGTGTG (SEQ ID NO: 4)

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)

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.

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).

Expression

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.

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.

Refolding and Purification

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.

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).

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.

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-d₆ 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.

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

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.

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.

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).

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 & 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

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.

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.

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

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

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 & Modelling (2002) 20(6), 491-498) or with compounds obtained by the methods described herein.

EXAMPLE 4

NMR Screening

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).

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).

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.

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

Materials: Steroid standards (>98% purity) were purchased from Sigma Chemical Co. ³H-allopregnanolone (64 Ci/mmol, [9, 11, 12-³H(N)]-allopregnanolone, herein after referred to as ³H-ALLO) was purchased from New England Nuclear. ³H-5α-dihydroprogesterone (³H-5α-DHP) was synthesized in our lab using an enzymatic conversion of ³H-ALLO to ³H-5α-DHP by the 3a-HSD (see Enzymatic reactions). The oxidation product ³H-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.

Enzymatic reactions (oxidation of ³H-ALLO to ³H-5α-DHP and reduction of ³H-5α-DHP to ³H-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. ³H-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 ³H-5α-DHP (40 000 cpm) in 4% acetonitrile. Similarly, ³H-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 ³H-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.

HPLC separation: Chromatographic separation of ³H-ALLO and ³H-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).

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 ³H-ALLO to ³H-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. ³H-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

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

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

Claims

1. A method for identifying an inhibitor to the human type III 3a-HSD enzyme, comprising the steps of a) designing or selecting computationally a potential inhibitor by using the atomic coordinates of the human type III 3a-HSD enzyme or co-complexes, e.g. as described in Table 1; and/or b) obtaining a potential inhibitor by performing a NMR screen with the human type 1113a-HSD and candidate compounds, e.g. from a library of compounds; and/or c) obtaining a potential inhibitor by performing a NMR reporter screen with the human type III 3a-HSD, a first inhibitor candidate to human type III 3a-HSD with a dissociation constant smaller than 2 mM which is either already known or found by a method according to step a) or b) and further a second candidate compound, e.g. from a library of compounds; and/or d) determining the activity of the potential inhibitor from step a), b) or c) at the human type III 3a-HSD enzyme.

2. The method of claim 1, comprising a further step d), said step comprises the step of docking said potential inhibitor to the three-dimensional structure of human type III 3a-HSD enzyme or co-complexes, as described in Table 1, and employing the obtained three-dimensional structure relation to design or select further inhibitors.

3. The method of claim 1, comprising a further step e), said step comprises the step of crystallizing the in step a), b) or c) obtained potential inhibitor with human type III 3a-HSD enzyme or co-complexes, e.g. as described in Table 1, determining the X-ray structure, comparing the three-dimensional structure of the so obtained new co-complex with the formerly known structures of human type III 3a-HSD enzyme and employing the obtained three-dimensional structure difference to design or select further potential inhibitors.

4. The method according to claim 1, wherein said potential inhibitor Is designed de novo.

5. The method according to claim 1, wherein said potential inhibitor is designed from a known inhibitor.

6. The method according to claim 1, wherein said potential inhibitor is a competitive inhibitor of human type III 3a-HSD.

7. The method according to claim 1, wherein said step of employing a three-dimensional structure to design or select said compound comprises the steps of: a) identifying chemical entities or fragments capable of associating with said enzyme; and b) assembling the identified chemical entities or fragments into a single molecule to provide the structure of said potential inhibitor.

8. The method according to claim, wherein said first inhibitor candidate in step c) is 2-acetylbenzofuran.

9. A crystalline complex of human type III 3a-HSD and NADP exhibiting essentially the atomic coordinates listed in Table 1.

10. A process for the production of a crystalline complex according to claim 9, comprising the step of growing the crystalline complex in 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, or 8000; 0-10% additives, and 0-20 mM DTT.