Beta-secretase crystals and methods for preparing and using the same

Abstract

The present invention relates to the expression, purification and crystallization of glycosylated β-secretase protein and a complex thereof. The crystals of the invention are useful, inter alia, for determining the three-dimensional structure of β-secretase and of other, related proteins.

Description

FIELD OF THE INVENTION

[0002] This invention relates to crystalline β-secretase (BACE), the three-dimensional structure of BACE, methods for preparing the crystal and the use of the crystal to solve the structure of BACE homologues, mutants, other BACE crystal forms and similar molecules of unknown structure, and the use of BACE crystals to design inhibitors against BACE.

BACKGROUND OF THE INVENTION

[0003] Alzheimer's disease (AD) is a neurodegenerative disease characterized by neuronal loss due to the extracellular accumulation of amyloid plaques and intracellular accumulation of neurofibrillary tangles in the brain (reviewed by Selkoe, D. J. (1999) Nature 399: A23-31). Two major components of amyloid plaques are small peptide fragments Aβ140 and Aβ42, which are generated from cleavage of the membrane-anchored amyloid precursor protein (APP) by the proteolytic activity of β- and γ- secretases. APP is a type I integral membrane protein containing the Aβ segment, which begins at D672 in the longest isoform and spans the boundary of the exocytoplasmic region (28 amino acids) and the transmembrane domain (12-14 amino acids). The γ-secretase activity cleaves APP within the transmembrane domain to produce the carboxy-terminal end of Aβ polypeptide. The β-secretase activity (aspartic protease activity), identified in a protein that is known as “mamapsin 2”, “human β-site APP-cleaving enzyme” or “BACE”, and “Asp 2”, cleaves APP on the extracellular side of the membrane to produce the amino-terminal end of Aβ. (Vassar, R. et al., (1999) Science 286,735, Sinha, S. et al., (1999) Nature 402,537, Yan, R. et al., (1999) Nature 402,522, Hussain, I. et al., (1999) Mol. Cell Neurosci. 14, 419 and Lin, X. (2000) et al., Proc. Natl. Acad. Sci. USA 97, 1456. Another enzyme, known as α-secretase, cleaves APP at a position within the Aβ sequence to produce a soluble APPα (Esch et al., (1990) Science 248: 1122-1124).

[0004] During the course of AD, Aβ polypeptide accumulates extracellularly in the brain, and forms large, insoluble amyloid fibrils that elicit both cytotoxic and inflammatory responses. Thus, BACE and γ-secretase proteases are targets for potential inhibitor drugs against AD. Since it was discovered that the β-secretase activity is the rate-limiting step in AP production in vivo (Sinha and Lieberburg, (1999) Proc. Natl. Acad. Sci. USA 96: 11049), BACE has become a prime target for the development of inhibitors to treat AD.

[0005] The BACE gene encodes a 501 residue polypeptide having (from N- to C- terminus) an N-terminal signal sequence of 21 amino acids, a pro-protein domain of 22 to 45 residues, which is proteolytically removed by furin to generate a mature β-secretase (Creemers, J. W., et al. (2001) J Biol. Chem. 276: 4211-4217; Bennet, B. D., et al. (2000) J Biol Chem. 275: 37712-37717), a protease (catalytic) domain and a connecting strand, an integral membrane (transmembrane) domain of about 17 amino acids, and a short cytosolic C-terminal tail of 24 amino acids (Vassar et al., supra). Sequence analyses indicate that BACE belongs to a subfamily of membrane-bound and soluble proteases and contains a classic consensus active site motif found in aspartyl proteases (D T/S G T/S) at positions 93 to 96 and 289 to 292. The entire BACE sequence displays only mild homology with known aspartyl proteases (approximately 30% identity and 37% similarity with members of the mammalian pepsin family), with the highest homology found in the central portion of the extracellular domain.

[0006] Accurate information regarding the structure of natural β-secretase is helpful in the design and identification of inhibitors and the enzymatic characterization of the enzyme. A crystal form of a β-secretase, expressed in bacteria, is described in Hong et al., (2000) Science 290:150-153, however this BACE polypeptide is unglycosylated and requires application of extensive refolding methodologies to provide an active enzyme. According to the method of Hong, et al., it was also necessary to form a complex between the polypeptide and an inhibitor 1

[0007] (OM99-2) before crystallization. Typically, refolded polypeptides do not assume the 5 exact three dimensional structure of the native, soluble polypeptide. Thus, there is a need for β-secretase crystals which have similar structure and activity to that of native β-secretase and which can be produced without difficult refolding steps. There is also a need for β-secretase crystals which are uncomplexed and which possess an active site in open configuration to which inhibitors may be easily bound (e.g., by crystal/inhibitor soaking methods).

SUMMARY OF THE INVENTION

[0008] The present invention provides a crystal comprising a polypeptide selected from: (a) a glycosylated, human β-secretase polypeptide characterized by structural coordinates comprising a root mean square deviation of conserved residue backbone atoms of less than about 1.5 Å (e.g., less than about 1.0 Å, less than about 0.5 Å or less than about 0.1 Å) when superimposed on backbone atoms described by structural coordinates of Table 2; (b) a glycosylated, human β-secretase polypeptide complexed with 2

[0009] (OM-99-2) characterized by structural coordinates comprising a root mean square deviation of conserved residue backbone atoms of less than about 1.5 Å (e.g., less than about 1.0 Å, less than about 0.5 Å or less than about 0.1 Å) when superimposed on backbone atoms described by structural coordinates of Table 3; and (c) a glycosylated, human β-secretase polypeptide which comprises a pyramidal structure.

[0010] Preferably, the crystal comprises a polypeptide selected from a glycosylated, human β-secretase polypeptide comprising the amino acid sequence set forth in SEQ ID NO: 1; a glycosylated, human β-secretase polypeptide comprising the amino acid sequence set forth in SEQ ID NO: 5 complexed with OM-99-2; and a glycosylated, human β-secretase polypeptide comprising the amino acid sequence set forth in SEQ ID NO: 4 which crystal is characterized by a pyramidal structure.

[0011] More preferably, the crystal comprises a polypeptide selected from a glycosylated, human β-secretase polypeptide comprising the amino acid sequence set forth in SEQ ID NO: 1 characterized by structural coordinates of Table 2; and a glycosylated, human β-secretase polypeptide comprising the amino acid sequence set forth in SEQ ID NO: 5 complexed with OM-99-2 characterized by structural coordinates of Table 3.

[0012] In preferred embodiments, the crystals of the present invention are able to proteolytically cleave a peptide comprising the amino acid sequence KSEVNLDAEFRK (SEQ ID NO: 3). Preferably, the crystal comprises a β-secretase polypeptide comprising an active site in an open configuration. Preferably, the crystal effectively diffracts x-rays for determination of structural coordinates of the polypeptide to a resolution greater than about 5 Å.

[0013] Also provided by the present invention is a computer for producing a three-dimensional representation of BACE characterized by the structural coordinates of Table 2 or BACE complexed with OM-99-2 characterized by the structural coordinates of Table 3 or a three-dimensional representation of a homologue of said BACE or said BACE complexed with OM-99-2 wherein the homologue has a root mean square deviation from the backbone atoms of Table 2 or 3 of less than about 1.5 A, preferably less than about 1 Å, more preferably less than about 0.5 Å, and even more preferably, less than about 0.1 Å wherein said computer comprises a machine-readable data storage medium comprising a data storage material encoded with machine-readable data, wherein said data comprises the structure coordinates of Table 2 or 3; a working memory for storing instructions for processing said machine-readable data; a central-processing unit coupled to said working memory and to said machine-readable data storage medium for processing said machine readable data into said three-dimensional representation; and a display unit coupled to said central-processing unit for displaying said three-dimensional representation.

[0014] In preferred embodiments of the invention the computer display unit is displaying the three dimensional representation of the polypeptide.

[0015] The invention further relates to the three-dimensional structure of BACE and its structure coordinates, e.g., as determined by x-ray crystallography, the use of the structure to solve the structure of BACE homologues, mutants and complexes thereof, and the use of such BACE structures to design inhibitors against BACE.

[0016] The invention also provides a method for determining at least a portion of the three-dimensional structure of molecules or molecular complexes which contain at least some structurally similar features to a BACE polypeptide complex.

[0017] The present invention also provides methods for obtaining crystals of BACE, preferably, of sufficient quality to determine the three dimensional structure of the polypeptide by x-ray diffraction methods.

[0018] Information derived from BACE crystals may be used to model the tertiary structure of related proteins and/or protein complexes. Accordingly, another aspect of the present invention is to provide starting material for the structure determination of other members of the BACE family of proteins. The knowledge of the structure of the BACE family of proteins provides a tool for investigating the mechanism of action of BACE protein. Knowledge of the protein structure allows for the design and synthesis of small molecules which inhibit the functional activities of the BACE protein. One preferred method is structure-based drug design.

[0019] Another aspect of this invention is the use of the structure coordinates and atomic details of BACE or mutants or homologues or co-complexes thereof to design, evaluate computationally, synthesize and use inhibitors of BACE that prevent or treat the undesirable physical and pharmacological properties of Alzheimer's disease. These inhibitors may be used in the treatment of Alzheimer's disease.

[0020] Still another aspect of the present invention comprises a method for selecting a potential ligand or inhibitor by performing structure-based drug design with a three-dimensional structure determined for the crystal, preferably in conjunction with computer modeling. The potential ligand or inhibitor is then contacted with the BACE polypeptide and the binding thereof is detected. If the ligand is a potential inhibitor of BACE activity, the candidate drug may then be contacted with a cell that expresses BACE and the inhibition of its activity can be measured.

[0021] In another embodiment of the invention, a method for obtaining structural information concerning a polypeptide of unknown structure by using the structure coordinates set forth in Table 2 is provided. Such a method comprises the steps of: generating x-ray diffraction data from said crystallized molecule, and applying crystallographic phases derived from at least a portion of the structure coordinates set forth in Table 2 to said x-ray diffraction pattern to generate a three-dimensional electron density map of at least a portion of the molecule.

DETAILED DESCRIPTION OF THE INVENTION

[0022] The present invention includes a crystalline composition including BACE and BACE complexed with OM-99-2. The BACE crystals of the invention, preferably, comprise post-translational modifications (e.g., glycosylation) which are similar to that of native BACE and, furthermore, the crystals are, preferably, formed in the absence of protein refolding steps. Each of these factors enhances the capacity of the crystals of the invention to assume a three-dimensional structure which is similar to that of the native enzyme. The BACE crystals of the invention, preferably, are catalytically active and comprise an active site which is free and available for inhibitor or substrate binding (e.g., by soaking the crystal with the substrate or with the inhibitor). Preferably, the BACE crystals comprise a soluble BACE polypeptide which lacks the transmembrane domain and C-terminal tail of native BACE. The invention also includes novel methods for preparing and for using the crystalline compositions.

[0023] In accordance with the present invention, there may be employed conventional molecular biology, microbiology, and recombinant DNA techniques within the skill of the art. Such techniques are explained fully in the literature. See, e.g., Sambrook, Fritsch & Maniatis, Molecular Cloning: A Laboratory Manual, Second Edition (1989) Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y. (herein “Sambrook et al., 1989”); DNA Cloning: A Practical Approach, Volumes I and II (D. N. Glover ed. 1985); Oligonucleotide Synthesis (M. J. Gait ed. 1984); Nucleic Acid Hybridization [B. D. Hames & S. J. Higgins eds. (1985)]; Transcription And Translation [B. D. Hames & S. J. Higgins, eds. (1984)]; Animal Cell Culture [R. I. Freshney, ed. (1986)]; Immobilized Cells And Enzymes [IRL Press, (1986)]; B. Perbal, A Practical Guide To Molecular Cloning (1984); F. M. Ausubel et al. (eds.), Current Protocols in Molecular Biology, John Wiley & Sons, Inc. (1996) (herein “Ausubel et al., 1996”).

[0024] A β-secretase polypeptide or BACE used in this invention is any form of BACE from any species, preferably from an animal, more preferably from a mammal (e.g., mouse, rat, rabbit, dog) and most preferably from a human. Preferably, BACE is a glycosylated protein which is structurally and functionally similar to naturally-occurring human BACE and which has an active site with an open configuration. More preferably, BACE crystals comprise a BACE polypeptide which is a glycosylated, soluble fragment of mature, human BACE which lacks the carboxy-terminal tail and transmembrane domain as well as the amino-terminal propeptide and which includes the amino acid sequence set forth in SEQ ID NO: 1, 4 or 5. The scope of the present invention also includes crystals comprising an immature form of BACE, from which the mature form can be made, which comprises an amino-terminal propeptide. The amino acid sequence of an immature BACE polypeptide (proBACE) is set forth in SEQ ID NO: 2. The scope of the present invention also includes crystals comprising BACE polypeptide as disclosed by Vassar et al., (1999) Science, 286: 735-741-Genbank Accession No. AF190725; Murphy et al., (2001) Neuroreport, 12(3):631-634; Capell et al., (2000) J. Biol. Chem., 275(40):30849-30854 and Haniu et al., (2000) J. Biol. Chem., 275(28):21099-21106. The published sequences also include polypeptides that differ from the BACE protein by having amino acid deletions, substitutions, and additions. BACE used in this invention, preferably, contains catalytic (proteolytic) properties that are comparable to those that have been reported for synthetic peptides derived from the β-amyloid precursor protein (APP) peptide sequence. Examples of APP peptides which may be cleaved by BACE of the present invention are disclosed, for example, in Lin et al., (2000) Proc. Nat. Acad. Sci., 97(4):1456-1460 and Turner et al., (2001) Biochemistry, 40(34):10,001-10,006. The bilobal protein, typically, is lightly glycosylated with glycan attachment accounting for approximately 4 kD of the protein's molecular weight.

[0025] Another aspect of the present invention is an uncrystallized mature, soluble fragment of BACE (e.g., SEQ ID NO: 1, 4 or 5) which is the proteolytic cleavage product from a BACE autoprocessing step of, for example, proBACE (e.g., SEQ ID NO: 2) which occurs most efficiently at pH 4.0. When forming the mature, human BACE crystals of the invention, preferably, proBACE is cleaved, to yield mature BACE, by autoprocessing which occurs at the crystallization step.

[0026] In addition to BACE polypeptides described in the art, various mutant forms, homologues and variants of BACE can be employed. The terms “mutant” and “mutation” mean any detectable change in genetic material, e.g., DNA, or any process, mechanism, or result of such a change. This includes gene mutations, in which the structure (e.g., DNA sequence) of a gene is altered, any gene or DNA arising from any mutation process, and any expression product (e.g., protein) expressed by a modified gene or DNA sequence. The term “variant” may also be used to indicate a modified or altered gene, DNA sequence, polypeptide or enzyme, etc., i.e., any kind of mutant. Sequence- and function-conservative variants of BACE polypeptides are contemplated for use in the present invention. “Sequence-conservative variants” of BACE are those in which a change of one or more nucleotides in a given codon position results in no alteration in the amino acid encoded at that position. “Function-conservative variants” of BACE are those in which a given amino acid residue in a BACE polypeptide has been changed without altering the overall conformation and function of the polypeptide, including, but not limited to, replacement of an amino acid with one having similar properties (such as, for example, polarity, hydrogen bonding potential, acidic, basic, hydrophobic, aromatic, and the like).

[0027] Protein or polypeptide homology, or sequence identity, is determined by optimizing residue matches, if necessary, by introducing gaps as required. See, e.g., Needleham, et al. J. Mol. Biol. 48:443-453 (1970); Sankoff et al., “Time Warps, String Edits, and Macromolecules: The Theory and Practice of Sequence Comparison”, Ch. 1, Addison-Wesley, Reading, Mass. (1983); and software packages from IntelliGenetics, Mountain View, Calif. and the University of Wisconsin Genetics Computer Group (GCG), Madison, Wis. This changes when considering conservative substitutions as matches. Conservative substitutions typically include substitutions within the following groups: glycine, alanine; valine, isoleucine, leucine; aspartic acid, glutamic acid; asparagine, glutamine; serine, threonine; lysine, arginine; and phenylalanine, tyrosine. Homologous amino acid sequences are intended to include natural variations of the BACE amino acid sequence. Typical homologous BACE polypeptides used in this invention will have from 50-100% homology (if gaps can be introduced), to 60-100% homology (if conservative substitutions are included), e.g., with BACE comprising the amino acid sequence of SEQ ID NO: 1 or 2. Homology measures are preferably at least about 70%, generally at least 76%, more generally at least 81%, often at least 85%, more often at least 88%, typically at least 90%, more typically at least 92%, usually at least 94%, more usually at least 95%, preferably at least 96%, and more preferably at least 97%, and in particularly preferred embodiments, at least 98% or more. The degree of homology will vary with the length and number of BACE polypeptides compared.

[0028] The terms “express” and “expression” mean allowing or causing the information in a gene or DNA sequence to become manifest, e.g., producing a protein by activating the cellular functions involved in transcription and, optionally, translation of a corresponding gene or DNA sequence. A DNA sequence can be expressed using in vitro translation systems (e.g., rabbit reticulocyte lysate-based systems) or in or by a cell to form an “expression product” such as a mRNA or a protein. The expression product, e.g. the resulting protein, may also be referred to as “expressed”.

[0029] An insect cell used in this invention is any cell derived from an organism of the class Insecta. Preferably, the insect is Spodoptera fruigiperda (Sf9 or Sf21) or Trichoplusia ni (High 5). Examples of insect expression systems that can be used with the present invention, for example to produce BACE polypeptide, include Bac-To-Bac (Invitrogen Corporation, Carlsbad, Calif.) or Gateway (Invitrogen Corporation, Carlsbad, Calif.).

[0030] A BACE polypeptide can be produced by any conventional method, including synthetic methods, such as solid phase, liquid phase and combination solid/liquid phase polypeptide syntheses; recombinant DNA methods, including cDNA cloning, optionally combined with site-directed mutagenesis; and/or purification of the natural products, optionally combined with enzymatic or chemical cleavage methods to produce fragments of naturally-occurring BACE.

[0031] It may also be desirable to add amino acids at the amino- or carboxy-terminus of a BACE polypeptide, e.g., to prepare a fusion protein. In one embodiment, the addition is a polyhistidine tag of 5-20 amino acids, preferably 6 amino acids, in length. Preferably, a histidine tag for aiding in purification of a BACE polypeptide is located at the carboxy-terminus. In another embodiment, a myc tag is added to the carboxy-terminus of BACE. The myc tag may be used for detection or immunopurification of BACE. The myc tag and the polyhistidine tag may both be located at the carboxy -terminus or amino-terminus in a doubly-tagged BACE.

[0032] The term “enzymatically active” means a protein is catalytically active and, preferably, can hydrolyze a peptide bond of a suitable substrate. Preferably, the term relates to the ability of human BACE to cleave β-amyloid precursor protein or a fragment thereof (e.g., SEQ ID NO: 3); catalytic activity of BACE is discussed above.

[0033] The term “active site”, when referring to a BACE polypeptide, describes the area of the polypeptide responsible for peptide recognition and/or peptide bond hydrolysis. For example, the active site for BACE which is used to produce the crystals whose coordinates are set forth in Table 2 includes amino acids Asp72 and Asp268. An active site in an “open configuration” means that the active site is accessible to interaction with a suitable substrate and/or inhibitor. The term “trans-cleavage processing” refers to the ability of one BACE molecule to enzymatically remove the propeptide of another BACE molecule. In general, trans-cleavage processing occurs most efficiently at about pH 4 wherein amino-terminal amino acids are cleaved.

[0034] One aspect of the present invention relates to a method of purifying BACE polypeptides and obtaining BACE crystals. Preferably, a BACE polypeptide is produced in a system which produces BACE polypeptide with an active site in open configuration. Preferably, the polypeptide is produced in a system which produces glycosylated BACE; however, the present invention contemplates crystals comprising BACE which has been modified (e.g., post-translationally modified) in any manner which produces an open active site configuration (e.g., phosphorylation, sulfonation, PEGylation). Although BACE may be produced, for example, in mammalian cells (e.g., CHO cells, NIH3T3 cells), it is preferable to produce the protein recombinantly in an insect cell expression system (e.g., an insect cell/baculovirus-based system). Initial purification may be accomplished by nickel chelate chromatography, as previously described in: Ausubel et al. supra. The BACE preparation may be subjected to anion exchange chromatography for further purification. It may also be desirable to subject the BACE preparation to standard size exclusion gel filtration. The protein preparation may be further concentrated using standard techniques. Finally, the preparation is preferably subjected to ultracentrifugation, which produces a monodisperse preparation of BACE. The BACE in the resulting supernatant is useful for crystallization purposes.

[0035] A BACE preparation preferably contains a protein stabilizing agent, a salt, a buffering agent and, optionally, a reducing agent or oxygen scavenger. Examples of suitable reducing agents are dithiothreitol (DTT), dithioerythritol (DET) and β-mercaptoethanol (BME). If desired, the reducing agent is present in the buffered solution at a concentration of about 10 mM. Preferably, the reducing agent is BME. The pH of the buffering agent may range from about 4.5 to about 8 (e.g., 5, 6, 7), preferably between about pH 7 and about 8 (e.g., 7.2, 7.4, 7.5, 7.6, 7.8).

[0036] Salt concentration appears to be important for the solubility of BACE. Salt may be provided in a concentration of more than about 300 mM (e.g., 500 mM). Various salts are routinely used in the art in similar methods, including sodium chloride and imidazole.

[0037] A “precipitant” is a compound that decreases the solubility of a polypeptide in a concentrated solution. Alternatively, the term “precipitant” can be used to refer to a change in physical or chemical parameters which decreases polypeptide solubility, including temperature, pH and salt concentrations. Precipitants induce crystallization by forming an energetically unfavorable precipitant-depleted layer around the polypeptide molecules. To minimize the relative amount of this depletion layer, the polypeptides form associations and, ultimately, crystals. This process is explained in Weber, Advances in Protein Chemistry 41:1-36 (1991) which is incorporated by reference. In addition to precipitants, other materials are sometimes added to the polypeptide crystallization solution. These include buffers, such as Hepes, to adjust the pH of the solution (and hence surface charge on the peptide) and salts, such as sodium chloride, lithium chloride and sodium citrate, to reduce the solubility of the polypeptide. Various precipitants are known in the art and include the following: ammonium sulfate, ethanol, 3-ethyl-2,4 pentanediol; and many of the polyglycols, such as polyethylene glycol. A suitable precipitant for crystallization of BACE polypeptide complex is polyethylene glycol (PEG), preferably PEG with a molecular weight of 6000 Da, which combines some of the characteristics of the salts and other organic precipitants.

[0038] “Monodisperse” and “predominantly uniform molecular species”, in reference to BACE, are used interchangeably to indicate that the mean radius of particles comprising the BACE varies by less than about 30%, preferably less than about 15%, as determined by, e.g., conventional dynamic light scattering methods. A monodisperse BACE in solution preferably exists in a monomeric form, however, oligomers (e.g., dimers, trimers, tetramers, etc.) may also exist. Such mixtures of BACE have subunits of a molecular weight of about 55 kDa.

[0039] Crystallization may be accomplished by using any of the known methods in the art (Giege, et al., (1994) Acta Crystallogr. D50: 339-350; McPherson, (1990) Eur. J. Biochem. 189: 1-23). Such techniques include microbatch, hanging drop, seeding and dialysis. Preferably, hanging-drop vapor diffusion (McPherson, (1976) J. Biol. Chem. 251: 6300 -6303) or microbatch methods (Chayen (1997) Structure 5: 1269-1274) are used. In each of these methods, it is important to promote continued crystal growth after nucleation by maintaining a supersaturated solution. In the microbatch method, polypeptide is mixed with precipitants to achieve supersaturation, the vessel is sealed and set aside until crystals appear. In the dialysis method, polypeptide is retained in a sealed dialysis membrane which is placed into a solution containing precipitant. Equilibration across the membrane increases the precipitant concentration thereby causing the polypeptide to reach supersaturation levels. It is desirable to use a BACE protein preparation having a concentration of at least about 1 mg/mL and preferably about 10 mg/mL to about 20 mg/mL. Crystallization may be best achieved in a precipitant solution containing polyethylene glycol 1000-20,000 (PEG; average molecular weight ranging from about 1000 to about 20,000 Da), preferably about 5000 to about 7000 Da, more preferably about 6000 Da, with concentrations ranging from about 10% to about 30% (w/v). It may also be desirable to include a protein stabilizing agent. If glycerol is chosen as the protein stabilizing agent, it is preferably provided at a concentration ranging from about 0.5% to about 20%. A suitable salt, such as sodium chloride, lithium chloride or sodium citrate may also be desirable in the precipitant solution, preferably in a concentration ranging from about 1 mM to about 1000 mM. The precipitant is preferably buffered to a pH of from about 3.0 to about 5.0, preferably about 4.0. Specific buffers useful in the precipitant solution may vary and are well-known in the art (Scopes, Protein Purification: Principles and Practice, Third ed., (1994) Springer-Verlag, New York). Examples of useful buffers include, but are not limited to, Hepes, Tris, MES and acetate. Crystals routinely grow at a wide range of temperatures. It is, however, preferred that crystals form at temperatures between about 2° C. and about 26° C., and more preferably at about 2° C. to about 8° C., most preferably at about 4° C.

[0040] The crystals of the present invention have a wide range of uses. For example, high quality crystals are suitable for x-ray or neutron diffraction analysis to determine the three dimensional structure of BACE and in particular to assist in the identification of the protein's active and effector sites. Knowledge of these sites and solvent accessible residues allow structure-based design and construction of agonists and antagonists for BACE.

[0041] In addition, crystallization itself can be used as a purification method. In some instances, a polypeptide or protein crystallizes from a heterogeneous mixture into crystals. Isolation of such crystals by filtration and/or centrifugation, followed by redissolving the polypeptide affords a purified solution suitable for use in growing high-quality crystals which are preferred for diffraction analysis.

[0042] Once a crystal of the present invention is grown, x-ray diffraction data can be collected. One method for determining structure with x-ray diffraction data includes use of synchrotron radiation, under standard cryogenic condition; however, alternative methods may also be used. For example, crystals can be characterized by using x-rays produced by a conventional source, such as a sealed tube or a rotating anode. Methods of characterization include, but are not limited to, precession photography, oscillation photography and diffractometer data collection.

[0043] The crystallizable compositions provided by this invention may be amenable to x- ray crystallography for providing the three-dimensional structure of a BACE polypeptide. The present invention includes crystals which effectively diffract x-rays for the determination of the atomic coordinates of BACE to a resolution of greater than about 5.0 Ångströms (e.g., about 4.5 Å, about 4.0 Å, about 3 Å, about 2.5 Å, about 2 Å, about 1 Å, about 0.5 Å, about 0.1 Å), preferably greater than about 4.0 Ångströms (e.g., about 3 Å, about 2.5 Å, about 2 Å, about 1 Å, about 0.5 Å, about 0.1 Å), more preferably greater than about 2.8 Ångströms (e.g., about 2.5 Å, about 2 Å, about 1 Å, about 0.5 Å, about 0.1 Å) and most preferably greater than about 2.0 Ångströms (e.g., about 1.5 Å, about 1.0 Å, about 0.5 Å, about 0.1 Å).

[0044] The present invention includes BACE crystals whose three-dimensional structure is described by the structure coordinates set forth in Table 2 or 3. The scope of the present invention also includes crystals which possess structural coordinates which are similar to those set forth in Table 2 or 3; preferably, the crystals or the soluble polypeptides which are used to form the crystals exhibit BACE catalytic activity (see above) and, preferably, the crystals include glycosylated BACE. Most preferably, the crystals include a polypeptide which includes the amino acid sequence of SEQ ID NO: 1 or 5. Structural similarity between crystals is discussed in detail below.

[0045] The term “structure coordinates” refers to Cartesian coordinates derived from mathematical equations related to the patterns obtained on diffraction of a beam of x-rays by the atoms (scattering centers) of a molecule. The diffraction data are used to calculate electron density maps and to establish the positions of the individual atoms of the molecule.

[0046] Those of skill in the art will understand that a set of structure coordinates for an enzyme or an enzyme-complex or a portion thereof, is a relative set of points that define a shape in three dimensions. Thus, it is possible that an entirely different set of coordinates could define a similar or identical shape. Moreover, slight variations in the individual coordinates will have little effect on overall shape.

[0047] The present invention includes crystals exhibiting structural coordinates which are similar to those set forth in Table 2 or 3 but for crystallographic permutations of the structure coordinates, fractionalization of the structure coordinates, additions, subtractions, rotations or translations to sets of the structure coordinates or any combinations of the above.

[0048] Alternatively, modifications in the crystal structure due to mutations, additions, substitutions, and/or deletions of amino acids, or other changes in any of the components that make up the crystal may also account for variations in structure coordinates. If such variations are within an acceptable standard error as compared to the coordinates of Table 2 or 3, the resulting three-dimensional shape is considered to be the same and, accordingly, the modified crystal is considered to be within the scope of the present invention.

[0049] Various computational analyses may be necessary to determine whether a crystal is sufficiently similar to the crystals whose structural coordinates are set forth in Table 2 or 3 as to be considered the same. Such analyses may be carried out in current software applications, such as the Molecular Similarity application of QUANTA (Molecular Simulations Inc., San Diego, Calif.) version 4. 1, and as described in the accompanying User's Guide.

[0050] The Molecular Similarity application permits comparisons between different structures, different conformations of the same structure, and different parts of the same structure. In general, the procedure used in Molecular Similarity to compare structures is divided into four steps: 1) input the structures to be compared; 2) define the atom equivalences in these structures; 3) perform a fitting operation; and 4) analyze the results.

[0051] Each structure is identified by a name. One structure is identified as the target (i.e., the fixed structure); all remaining structures are working structures (i.e., moving structures). Since atom equivalency within QUANTA is defined by user input, for the purpose of this invention we will define equivalent atoms as protein backbone atoms (N, Cα, C and O) for all conserved residues between the two structures being compared.

[0052] When a rigid fitting method is used, the working structure is translated and rotated to obtain an optimum fit with the target structure. The fitting operation uses a least squares fitting algorithm that computes the optimum translation and rotation to be applied to the moving structure, such that the root mean square difference of the fit over the specified pairs of equivalent atom is an absolute minimum. This number, given in Angstroms, is reported by QUANTA.

[0053] The term “root mean square deviation” (RMSD) is a commonly known term in the art which, in general, means the square root of the arithmetic mean of the squares of the deviations from the mean distance of corresponding atoms. It is a way to express the deviation or variation from a trend or object.

[0054] For the purpose of this invention, any set of structure coordinates of a molecule that has a RMSD of conserved residue backbone atoms (N, Cα, C, O) of less than about 1.5 Å when superimposed—using backbone atoms—on the relevant structure coordinates of Table 2 or 3 are considered identical and are within the scope of the present invention. Preferably the crystal is a catalytically active human, glycosylated BACE crystal (e.g., SEQ ID NO: 1 or 5). Preferably, the root mean square deviation is less than about 1.0 Å, even more preferably, the root mean square deviation is less than about 0.5 Å and most preferably, the root mean square deviation is less than about 0.1 Å.

[0055] The term “least squares” refers to a method based on the principle that the best estimate of a value is that in which the sum of the squares of the deviations of observed values is a minimum.

[0056] In accordance with the present invention, the structure coordinates of the BACE polypeptide and portions thereof may be stored in a machine-readable storage medium. Such data may be used for a variety of purposes, such as drug discovery and x-ray crystallographic analysis of a protein crystal (e.g., for producing a three-dimensional representation of BACE). Accordingly, one aspect of this invention provides a machine-readable data storage medium comprising a data storage material encoded with the structure coordinates set forth in Table 2 or 3. The machine-readable data storage medium may also include any set of structure coordinates of a molecule that has a root mean square deviation of conserved residue backbone atoms (N, Cα, C, O) of less than about 1.5 Å, preferably, less than about 1.0 Å, more preferably less than about 0.5 Å and even more preferably less than about 0.1 Å when superimposed—using backbone atoms—on the relevant structure coordinates of Table 2 or 3.

[0057] A computer system, useful in reading the machine readable data storage medium, includes a computer comprising a central processing unit (“CPU”) and a memory storage device and is also within the scope of the present invention. In general, the computer system may be any computer with an operating system such as MS-DOS, PC-DOS, Windows, OS/2, Unix, Unix variant or MacOS. Particularly preferred computer systems are the Silicon Graphics Octane workstation or Compaq AlphaServer DS20. Other hardware systems and software packages will be known to those skilled in the art.

[0058] Input hardware coupled to the computer system by input line, may be implemented in a variety of ways. Machine-readable data of this invention may be input via the use of a modem or modems connected by a telephone line or a dedicated data line. Alternatively or additionally, the input hardware may comprise CD-ROM drives or disk drives. A keyboard may also be used as an input device.

[0059] Output hardware, coupled to the computer system by output lines, may similarly be implemented by conventional devices. By way of example, output hardware may include a display terminal (e.g., a cathode ray tube (CRT)) for displaying a graphical representation of the three dimensional structure of BACE or a portion thereof using a program such as INSIGHT (Molecular Simulations Inc., San Diego, Calif.) or QUANTA as described herein. Output hardware might also include a printer, so that hard copy output may be produced, or a disk drive, to store system output for later use. In preferred embodiments, the computer possesses a display which is displaying a three dimensional representation of BACE or a fragment or homologue thereof.

[0060] In operation, the central processing unit (CPU) coordinates the use of the various input and output devices, coordinates data accesses from mass storage and accesses to and from working memory, and determines the sequence of data processing steps. A number of programs may be used to process the machine-readable data of this invention. Such programs are discussed in reference to the computational methods of drug discovery as described herein. Specific references to components of the computer system are included as appropriate throughout the following description of the data storage medium.

[0061] A magnetic data storage medium can be encoded with a machine-readable data by a computer system as described above. Storage medium may be, for example, a conventional floppy diskette or hard disk, having a suitable substrate, which may be conventional, and a suitable coating, which may be conventional, on one or both sides, containing magnetic domains whose polarity or orientation can be altered magnetically. The magnetic domains of the coating of medium may be polarized or oriented so as to encode, in a manner which may be conventional, machine readable data, such as that described herein, for execution by a system as described herein. Storage medium may also have an opening for receiving the spindle of a disk drive or other data storage device. Alternatively, an optically-readable data storage medium can be encoded with such machine-readable data, or a set of instructions. Medium can be a conventional compact disk read only memory (CD-ROM) or a rewritable medium such as a magneto-optical disk which is optically readable and magneto-optically writable.

[0062] In general, in the case of CD-ROM, as is well known, disk coating is reflective and is impressed with a plurality of pits to encode the machine-readable data. The arrangement of the pits is read by reflecting laser light off the surface of the coating. A protective coating, which preferably is substantially transparent, is provided on top of the coating.

[0063] In general, in the case of a magneto-optical disk, as is well known, disk coating has no pits, but has a plurality of magnetic domains whose polarity or orientation can be changed magnetically when heated above a certain temperature, as by a laser. The orientation of the domains can be read by measuring the polarization of laser light reflected from the coating. The arrangement of the domains encodes the data as described above.

[0064] The present invention permits the use of structure-based drug design techniques to design, select, and synthesize chemical entities, including inhibitory compounds that are capable of binding to a BACE polypeptide. Also, de novo and iterative drug design methods can be used to develop drugs from the structure of the BACE crystals of this invention.

[0065] One particularly useful drug design technique enabled by this invention is structure-based drug design. Structure-based drug design is a method for optimizing associations between a protein and a compound by determining and evaluating the three-dimensional structures of successive sets of protein/compound complexes.

[0066] Those skilled in the art will appreciate that association of natural ligands or substrates with the binding pockets of their corresponding receptors or enzymes is the basis of many biological mechanisms of action. The term “binding pocket”, as used herein, may refer to any region of a molecule or molecular complex, that, as a result of its shape, favorably associates with another chemical entity or compound. Similarly, drugs may exert their biological effects through association with the binding pockets of receptors and enzymes. Such association may occur with all or any part of the binding pockets. An understanding of such associations will help lead to the design of drugs having more favorable associations with the target enzyme, and thus, improved biological effects. Therefore, this information is valuable in designing potential enzyme inhibitors, such as inhibitors of BACE.

[0067] In iterative structure-based drug design, crystals of a series of protein/compound complexes are obtained and then the three-dimensional structure of each complex is solved. Such an approach provides insight into the association between the proteins and compounds of each complex. This is accomplished by selecting compounds with inhibitory activity, obtaining crystals of a new polypeptide, solving the three-dimensional structure of the polypeptide, and comparing the associations between the new protein and previously solved protein. By observing how changes in the compound affected the protein/compound associations, these associations may be optimized.

[0068] In some cases, iterative structure-based drug design is carried out by forming successive protein-compound complexes and then crystallizing each new complex. Alternatively, a pre-formed protein crystal is soaked in the presence of an inhibitor, thereby forming a protein/compound complex and obviating the need to crystallize each individual protein/compound complex. Advantageously, BACE crystals provided by this invention may be soaked in the presence of a compound or compounds, such as BACE inhibitors, substrates or other ligands to provide novel BACE/compound crystal complexes. As used herein, the term “soaked” may refer to a process in which the crystal is transferred to a solution containing the compound of interest.

[0069] The structure coordinates set forth in Table 2 or 3 can also be used to aid in obtaining structural information about another crystallized molecule or molecular complex. This may be achieved by any of a number of well-known techniques, including molecular replacement.

[0070] The structure coordinates set forth in Table 2 or 3 can also be used for determining at least a portion of the three-dimensional structure of molecules or molecular complexes which contain at least some structurally similar features to BACE. In particular, structural information about another crystallized molecule or molecular complex may be obtained by well-known techniques, including molecular replacement.

[0071] Therefore, another aspect of this invention provides a method of utilizing molecular replacement to obtain structural information about a crystallized molecule or molecular complex, whose structure is unknown, comprising the steps of generating an x-ray diffraction pattern from said crystallized molecule or molecular complex and applying crystallographic phases derived from at least a portion of the structure coordinates set forth in Table 2 or 3 to the x-ray diffraction pattern to generate a three-dimensional electron density map of the molecule or molecular complex whose structure is unknown.

[0072] Once the structure coordinates of a protein crystal have been determined, they are useful in solving the structures of other crystals. In addition, the structure of BACE homologues may be determined from the structural coordinates of the present invention. For example, polypeptides may be crystallized and their structure elucidated by, for example, difference Fourier techniques and molecular replacement.

[0073] By using molecular replacement, all or part of the structure coordinates of the BACE polypeptide provided by this invention (and set forth in Table 2 or 3) can be used to determine the previously unknown structure of a crystallized molecule or molecular complex more quickly and efficiently than attempting to determine such information ab initio.

[0074] Molecular replacement provides an accurate estimation of the phases for an unknown structure. Phases are a factor in equations used to solve crystal structures that cannot be measured experimentally. Obtaining accurate values for the phases, by methods other than molecular replacement, is a time-consuming process. However, when the crystal structure of a protein containing a homologous portion has been solved, the phases from the known structure may provide a satisfactory estimate of the phases for the unknown structure.

[0075] Thus, this method involves generating a preliminary model of a molecule or molecular complex whose structure coordinates are unknown, by orienting and positioning the relevant portion of the BACE crystal according to Table 2 or 3 within the unit cell of the crystal of the unknown molecule or molecular complex so as best to account for the observed x-ray diffraction pattern amplitudes to generate an election density map of the structure whose coordinates are unknown. This, in turn, can be subjected to any well-known model building and structure refinement techniques to provide a final, accurate structure of the unknown crystallized molecule or molecular complex (Lattman, “Use of the Rotation and Translation Functions”, in Meth. Enzymol., 115: 55-77 (1985); Rossman, ed., “The Molecular Replacement Method”, Int. Sci. Rev. Ser., No. 13, Gordon & Breach, New York (1972)).

[0076] Phase information from the structure coordinates of the present invention may be used to elucidate the structure of other crystals. For example, the structure of BACE in complex with other atoms or molecules may be elucidated. Such complexes include, for example, those containing atoms soaked into or cocrystallized within the crystal lattice. Other structures which can be elucidated using the phase information of the present invention include for example other proteases or homologues or mutants thereof having sufficient three-dimensional structure similarity to BACE complex as to be solved using molecular replacement. Examples of such proteins include, but are not limited to, cathepsin D, renin and pepsin. Also, these protein molecules in a complex with a small molecule substrate(s), inhibitor(s), transition state analog(s), product(s) or analog(s) of any of these may also be solved using the phase information of the present invention. Other complexes whose structure can be elucidated from the phase information of the present invention include a BACE complexed with an inhibitor. Complexes containing a combination of the above molecules may also be solved using the phase information of the present invention.

[0077] The structure of any portion of any crystallized molecule or molecular complex that is sufficiently homologous to any portion of the BACE protein can be solved by this method. The difference Fourier method simply calculates an electron density map using phases calculated from the structure coordinates and observed diffraction amplitudes from a crystal of an unknown structure. This method is often used to solve structures of protein/ligand complexes where the ligand is small and does not affect the crystal form significantly.

[0078] In a preferred embodiment, the method of molecular replacement is utilized to obtain structural information about a molecule wherein the molecule comprises a BACE polypeptide complex. The structure coordinates of BACE provided by this invention are particularly useful in solving the structure of other crystal forms of BACE polypeptide complexes. This approach enables the determination of the optimal sites for interaction between chemical entities, including interaction of candidate inhibitors with BACE.

[0079] BACE crystals may be studied using well-known x-ray diffraction techniques and may be refined versus x-ray data to 3 Å resolution or better to an Rfree value of about 0.40 or less using computer software such as X-PLOR (Yale University, 1992, distributed by Molecular Simulations, Inc.; see e.g., Blundell & Johnson, supra; Meth, Enzymol., vol. 114 & 115, H. W. Wyckoff et al., eds., Academic Press (1985)). This information may be used to optimize known BACE inhibitors and to design new BACE inhibitors.

EXAMPLES

[0080] The following examples are provided to describe the present invention in greater detail and should not be construed to limit the scope of the invention.

[0081] The following Examples describe methods for producing recombinant β-secretase crystals suitable for structure based drug design. Enzymatically active, human β-secretase was produced in insect cells by recombinant means, using recombinant vectors and baculoviruses containing cDNA encoding the 55KDa β-secretase protein. The β-secretase constructs incorporated a Myc-tag and a six-histidine tag at the C-terminus. Expressed β-secretase was purified to homogeneity using a combination of purification steps, including anion exchange chromatography, nickel chelate chromatography and gel filtration chromatography. The resulting monodisperse, enzymatically active β-secretase preparation was suitable for crystallization. X-ray diffraction quality crystals were grown using a hanging-drop vapor diffusion method. The β-secretase solution (1 μl; 10-20 mg/ml protein) in 20 mM Hepes, pH 7.5, 150 mM NaCl was mixed with an equal volume of precipitant, placed on the underside of a siliconized glass coverslip, and sealed in close proximity to 1 ml of the precipitant solution. The precipitant solution contained polyethyleneglycol 6000 with concentrations ranging from 6 to 30% (w/v). The precipitant solution also contained 200 mM to 1000 mM lithium chloride in a 0.1 M sodium citrate buffer between pH 3.8 and 4.6. After incubation at 4° C for 10 to 30 days, small rectangular rod crystals formed. Crystals grew to terminal size within one month with dimensions up to 0.03×0.03×0.2 mm. After transfer of the crystals to cryoprotectant which contains 20% glycerol higher than the crystallization medium, the crystals can be frozen directly in liquid propane for storage prior to diffraction data collection or frozen in a gaseous nitrogen stream immediately before diffraction data collection.

Example 1

[0082] Cloning of Human β-Secretase

[0083] Human β-secretase cDNA clone with C-terminal Myc-tag and 6×His-tag was inserted into a pcDNA4 vector and two PCR primers, sBACE1mutF(5′-ctcgagtctagagggcccttcgaacaaaaactc-3′) and sBACE1mutR (5′-ggttgactcatctgtctgtggaatgttgtagcc-3'), were used to delete the transmembrane domain and C-terminal tail of β-secretase. The sBACE/yc/6×His (myc-tag and 6-histidine-tag at the C-terminus) insert was then excised from the pcDNA4 vector using restriction enzymes HindIII and PmeI. The insert was blunt ended with Klenow enzyme and subcloned into the Stul site of pFASTBACI (A) vector provided in Bac-to-Bac Baculovirus Expression System (GIBCO/BRL, Rockville, Md., USA). The amino acid sequence of the polypeptide encoded by the insert is set forth in SEQ ID NO: 2.

Example 2

[0084] Production of Recombinant Baculoviruses

[0085] Recombinant baculovirus was produced as described in the Bac-to-Bac expression manual (Gibco BRL, Rockville, Md., USA; SF900-II) following the protocol for transposition, isolation of recombinant bacmid DNA, transfection of Sf9 cells with recombinant bacmid DNA and harvesting/storage of recombinant baculovirus. Recombinant virus was then plaque purified according to the manual and amplified by the infection of suspension cultures using a multiplicity of infection of 0.05.

Example 3

[0086] Expression and Recovery of Baculovirus Recombinant Pro-β-Secretase (proBACE).

[0087] Spodoptera frugiperda (Sf9 and Sf21) and Tridchoplusia ni (High Five™; Invitrogen, Carlsbad, Calif., USA) cells were grown in suspension at 27° C. in serum free media (SF900-II; Gibco BRL, Rockville, Md,. USA). Multiplicity of infection (MOI), cell type and time course of expression were all studied to obtain optimal protein expression yields of secreted soluble β-secretase. Sf9 cells infected with a MOI of 5 and incubated for 72 hours were determined to be optimal for protein secretion into the growth media and resulted in expression yields of approximately 4 mg/L.

Example 4:

[0088] Purification of SF-9 derived pro-o-Secretase (proBACE)

[0089] Thirty shake flasks (1.0 liters/flask) of conditioned media Sf-9 cells were collected by centrifugation at 1000 g for 15 minutes. The combined supernatant was concentrated using a Pellicon Laboratory System (Millipore Corporation, Bedford, Mass., USA) with four 30K molecular weight cutoff membrane cassettes; P2C030C05 Pellicon 2- cassette) to 4 L. An equal volume of 50 mM Hepes, pH 8.0 was added to the retentate, which was concentrated to 4 L. This procedure was repeated 4 times. The final retentate (pH 8.0, conductivity=2.8 mS/cm) was applied to a 400 ml Q-sepharose Fast Flow anion exchange column (Millipore Corporation, Bedford, Mass.; XK 50/30) pre-equilibrated with Buffer A (20 mM Hepes, pH 8.0) at 50 ml /min. The column was washed with 10 column volumes (CV) of Buffer A, and the protein was eluted with a sodium chloride gradient (0-300 mM). Sodium chloride and imidazole (Sigma Chemical Company, St. Louis, Mo.) were added to the combined eluate fractions at final concentrations of 500 mM and 20 mM, respectively. The resulting solution was applied to a 30 ml Ni-NTA Superflow (Qiagen Corporation, Valencia, Calif.) column (Millipore Corporation; XK 26/30) at 5 ml/min. The column was washed with 10 CV of Buffer B (20 mM Hepes, 20 mM imidazole, 500 mM sodium chloride) and the protein was eluted with 3 CV of Buffer C (20 mM Hepes, pH 8.0, 250 mM imidazole, 500 mM sodium chloride). The eluate fractions containing proBACE were pooled and concentrated to 2 ml, and injected to a Superdex 200 gel filtration column (Millipore Corporation; HighLoad, 26/60). Buffer D (20 mM Hepes, pH 7.5, 150 mM sodium chloride) was applied to the column at 4 ml/min. Fractions containing proBACE were combined based on SDS-PAGE analysis. The pooled fractions were concentrated to 20 mg/ml. The highly purified β-secretase was monodisperse.

TABLE 1
The recovery of proBACE in the purification steps
Step	Volume	Total protein	Recovery
Conditioned media	285 L
Pellicon concentrate	8.5 L	5.1	g
Q-sepharose (400
ml)
load	8.5 L	5.1	g
Ft/wash	12 L	2.5	g
eluant	2.5 L	1.9	g
Ni-NTA (30 ml)
load	2.5 L	1.9	g
eluant	0.27 L	33	mg
Superdex 200
load	2.0 ml	33	mg
eluant	25 ml	26	mg	0.9 mg/L media

Example 5

[0090] Enzymatic Activity of SF-9 Derived β-Secretase

[0091] To assess the functionality of β-secretase purified from Sf-9 cells, an HPLC assay was developed using a peptide substrate derived from the sequence of “Swedish” amyloid protein peptide (Dreyer et al., (1994) Eur J. Biochem 224: 265-271). In these assays, ProBACE (SEQ ID NO: 2) and mature BACE (SEQ ID NO: 1) were tested. The substrate, Biotin-KSEVNL*DAEFRK-Fluorescein (SEQ ID NO: 3) (* indicates cleavage site), was determined to be a suitable substrate for β-secretase, having a specificity constant (kcat/Km) of 1500 ±100 M−1s−1. The activity of S59 derived ,I-secretase with this substrate sequence is consistent with β-secretase derived from other expression systems (see e.g., Lin et. al., (2000) PNAS USA 97:1456), which confirms that 59-derived β-secretase is enzymatically active. The enzymatic activity of the proBACE and the mature BACE, with this substrate, were determined to be equivalent.

Example 6

[0092] Crystallization of SF-9 derived β-Secretase

[0093] ProBACE (SEQ ID NO: 2) in 20 mM Hepes, pH 7.5, 150 mM NaCl was concentrated by centrifugal filtration to 0.18 to 0.36 mM (10-20 mg / ml) followed by ultra-centrifugation prior to crystallization. Vapor diffusion crystallization experiments were conducted using the hanging drop method. Crystals were grown from a droplet containing 1 μl of protein and 1 μl of the reservoir solution which contained 0.1 M sodium citrate (Fluka BioChemika, Germany), pH 4.0, 10-30 % polyethylene glycol 6000 (Fluka BioChemika, Germany), and 0.2-1.0 M lithium chloride (Fluka BioChemika, Germany). At pH 4.0, the proBACE was autoprocessed, within the droplet, to yield mature BACE (SEQ ID NO: 1). During the autoprocessing step, the carboxy -terminal myc and His tags are cleaved from the polypeptide. Crystallization plates were incubated at 4° C., which grew rectangular rods (0.02×0.2 mm) over 10-30 days.

Mature BACE
ETDEEPEEPG  RRGSFVEMVD  NLRGKSGQGY  YVEMTVGSPP  QTLNILVDTG (SEQ ID NO: 1)
SSNFAVGAAP  HPFLHRYYQR  QLSSTYRDLR  KGVYVPYTQG  KWEGELGTDL
VSIPHGPNVT  VRANIAAITE  SDKFFINGSN  WEGILGLAYA  EIARPDDSLE
PFFDSLVKQT  HVPNLFSLQL  CGAGFPLNQS  EVLASVGGSM  IIGGIDHSLY
TGSLWYTPIR  REWYYEVIIV  RVEINGQDLK  MDCKEYNYDK  SIVDSGTTNL
RLPKKVFEAA  VKSIKAASST  EKFPDGFWLG  EQLVCWQAGT  TPWNIFPVIS
LYLMGEVTNQ  SFRITILPQQ  YLRPVEDVAT  SQDDCYKFAI  SQSSTGTVMG
AVIMEGFYVV  FDRARKRIGF  AVSACHVHDE  FRTAAVEGPF  VTLDMEDCGY
NIPQTDESTL  E
ProBACE
TQHGIRLPLR SGLGGAPLGL RLPRETDEEP EEPGRRGSFV EMVDNLRGKS (SEQ ID NO: 2)
GQGYYVEMTV GSPPQTLNIL VDTGSSNFAV GAAPHPFLHR YYQRQLSSTY
RDLRKGVYVP YTQGKWEGEL GTDLVSIPHG PNVTVRANIA AITESDKFFI
NGSNWEGILG LAYAEIARPD DSLEPFFDSL VKQTHVPNLF SLQLCGAGFP
LNQSEVLASV GGSMIIGGID HSLYTGSLWY TPIRREWYYE VIIVRVEING
QDLKMDCKEY NYDKSIVDSG TTNLRLPKKV FEAAVKSIKA ASSTEKFPDG
FWLGEQLVCW QAGTTPWNIF PVISLYLMGE VTNQSFRITI LPQQYLRPVE
DVATSQDDCY KFAISQSSTG TVMGAVIMEG FYVVFDRARK RIGFAVSACH
VHDEFRTAAV EGPFVTLDME DCGYNIPQTD ESTLE

Example 7

[0094] Crystallographic Analysis of β-Secretase and Model Building and Refinement

[0095] Crystals were removed from the crystallization droplet by adding 20% glycerol, which permitted freezing under both cold nitrogen stream and liquid propane. Diffraction data of the β-secretase crystal was determined from a Rigaku R-Axis IV image plate detector mounted on a Rigaku RU-HR rotating anode generator Cu radiation 1.54 Å operating at 100 mA and 50 kV.

[0096] Data Collection Statistics:

Resolution                       40-3.4 Å
No. of collected reflections     103348
No. of unique reflections (F >= 0) 18402
R-sym                            0.082
Percent of theoretical (I/s >= 1) 99%
Unit Cell                        a = 74 Å, b = 130 Å,
                                 c = 134 Å, α = β = γ = 90°
Space Group                      P212121
Asymmetric unit                  2 molecules

[0097] The underlying structure of the β-secretase crystals was solved using molecular replacement as implemented in CNX (MSI Inc.). The molecular replacement protocol as described in the CNX manual was followed with minor modifications. The search model consisted of molecule A from the β-secretase structure deposited in the PDB (pdb code 1FKN). Analysis of the molecular replacement solution shows two molecules in the asymmetric unit. The active site of both molecules is open and not blocked by crystal contacts.

TABLE 2
Structural coordinates for BACE.
Res.	Atom	#	X	Y	Z	B	C
GLU	CB	41	−8.1	−77.9	86.1	17	A
GLU	CG	41	−8.7	−79.2	85.5	26	A
GLU	CD	41	−10.0	−79.6	86.3	32	A
GLU	OE1	41	−10.9	−78.8	86.6	29	A
GLU	OE2	41	−10.2	−80.9	86.5	32	A
GLU	C	41	−7.5	−77.3	83.8	9	A
GLU	O	41	−7.1	−78.2	83.0	7	A
GLU	N	41	−6.8	−75.9	85.8	1	A
GLU	CA	41	−7.0	−77.3	85.3	10	A
MET	N	42	−8.3	−76.3	83.4	10	A
MET	CA	42	−8.8	−76.2	82.0	7	A
MET	CB	42	−10.3	−75.9	82.0	6	A
MET	CG	42	−11.2	−77.1	82.2	4	A
MET	SD	42	−12.9	−76.8	82.3	1	A
MET	CE	42	−13.2	−76.7	84.0	1	A
MET	C	42	−8.0	−75.1	81.3	6	A
MET	O	42	−7.9	−75.0	80.1	6	A
VAL	N	43	−7.6	−74.1	82.2	2	A
VAL	CA	43	−6.8	−73.0	81.7	2	A
VAL	CB	43	−6.0	−72.5	82.9	1	A
VAL	CG1	43	−5.1	−71.3	82.4	1	A
VAL	CG2	43	−7.0	−72.0	83.9	1	A
VAL	C	43	−5.8	−73.4	80.6	2	A
VAL	O	43	−5.2	−74.5	80.7	5	A
ASP	N	44	−5.5	−72.5	79.7	4	A
ASP	CA	44	−4.6	−72.8	78.6	6	A
ASP	CB	44	−3.2	−73.1	79.2	13	A
ASP	CG	44	−2.3	−71.9	79.2	22	A
ASP	OD1	44	−2.4	−71.1	80.1	28	A
ASP	OD2	44	−1.5	−71.8	78.2	24	A
ASP	C	44	−5.0	−73.9	77.7	7	A
ASP	O	44	−4.2	−74.4	77.0	14	A
ASN	N	45	−6.3	−74.4	77.8	5	A
ASN	CA	45	−6.6	−75.5	76.9	7	A
ASN	CB	45	−7.8	−76.3	77.5	5	A
ASN	CG	45	−9.1	−75.5	77.6	1	A
ASN	OD1	45	−9.1	−74.3	77.4	1	A
ASN	ND2	45	−10.2	−76.1	77.8	1	A
ASN	C	45	−6.9	−75.2	75.5	7	A
ASN	O	45	−7.1	−76.1	74.6	7	A
LEU	N	46	−6.9	−73.9	75.1	4	A
LEU	CA	46	−7.1	−73.4	73.7	3	A
LEU	CB	46	−8.0	−72.2	73.7	3	A
LEU	CG	46	−9.4	−72.4	74.3	10	A
LEU	CD1	46	−10.3	−71.2	73.9	9	A
LEU	CD2	46	−10.0	−73.7	74.0	11	A
LEU	C	46	−5.8	−73.0	73.1	4	A
LEU	O	46	−4.9	−72.6	73.8	6	A
ARG	N	47	−5.7	−73.2	71.8	5	A
ARG	CA	47	−4.5	−72.9	71.0	8	A
ARG	CB	47	−3.6	−74.1	70.7	11	A
ARG	CG	47	−2.7	−74.4	71.8	18	A
ARG	CD	47	−1.7	−75.5	71.3	30	A
ARC	NE	47	−2.3	−76.6	70.6	38	A
ARG	CZ	47	−1.7	−77.6	70.1	42	A
ARG	NH1	47	−0.4	−77.8	70.2	43	A
ARG	NH2	47	−2.4	−78.6	69.5	44	A
ARG	C	47	−5.0	−72.3	69.7	7	A
ARG	O	47	−6.2	−72.6	69.3	5	A
GLY	N	48	−4.2	−71.6	68.9	8	A
GLY	CA	48	−4.6	−71.1	67.6	16	A
GLY	C	48	−3.8	−69.9	67.1	19	A
GLY	O	48	−3.5	−68.9	67.9	20	A
LYS	N	49	−3.3	−70.0	65.9	20	A
LYS	CA	49	−2.5	−69.0	65.3	21	A
LYS	CB	49	−1.6	−69.5	64.2	22	A
LYS	CG	49	−2.3	−70.6	63.3	26	A
LYS	CD	49	−1.3	−71.3	62.3	28	A
LYS	CE	49	−1.2	−70.5	61.0	32	A
LYS	NZ	49	−2.4	−70.8	60.1	30	A
LYS	C	49	−3.3	−67.8	64.8	21	A
LYS	O	49	−4.1	−67.9	63.9	24	A
SER	N	50	−3.0	−66.6	65.3	23	A
SER	CA	50	−3.6	−65.4	65.0	26	A
SER	CB	50	−2.7	−64.6	64.0	31	A
SER	OG	50	−3.2	−63.3	63.7	38	A
SER	C	50	−5.1	−65.4	64.3	26	A
SER	O	50	−6.1	−65.6	65.0	31	A
GLY	N	51	−5.1	−65.0	63.1	24	A
GLY	CA	51	−6.4	−65.0	62.4	19	A
GLY	C	51	−7.0	−66.3	61.9	19	A
GLY	O	51	−7.8	−66.4	61.0	21	A
GLN	N	52	−6.5	−67.4	62.5	19	A
GLN	CA	52	−6.9	−68.7	62.2	18	A
GLN	CB	52	−5.7	−69.7	62.2	16	A
GLN	CG	52	−5.2	−70.1	60.7	15	A
GLN	CD	52	−4.5	−69.0	60.0	20	A
GLN	OE1	52	−4.1	−69.2	58.9	21	A
GLN	NE2	52	−4.4	−67.8	60.6	21	A
GLN	C	52	−7.9	−69.3	63.2	18	A
GLN	O	52	−8.7	−70.2	62.8	17	A
GLY	N	53	−8.0	−68.7	64.3	18	A
GLY	CA	53	−9.0	−69.1	65.3	15	A
GLY	C	53	−8.5	−70.0	66.4	11	A
GLY	O	53	−7.4	−70.6	66.4	9	A
TYR	N	54	−9.4	−70.2	67.4	11	A
TYR	CA	54	−9.0	−70.9	68.6	8	A
TYR	CB	54	−9.5	−70.2	69.9	6	A
TYR	CG	54	−8.9	−68.8	70.0	2	A
TYR	CD1	54	−9.6	−67.8	69.4	4	A
TYR	CE1	54	−9.0	−66.5	69.5	6	A
TYR	CD2	54	−7.8	−68.6	70.7	3	A
TYR	CE2	54	−7.3	−67.3	70.8	5	A
TYR	CZ	54	−7.9	−66.3	70.2	6	A
TYR	OH	54	−7.4	−65.0	70.3	9	A
TYR	C	54	−9.7	−72.3	68.6	8	A
TYR	O	54	−10.8	−72.5	68.1	7	A
TYR	N	55	−8.9	−73.3	69.1	7	A
TYR	CA	55	−9.3	−74.7	69.1	5	A
TYR	CB	55	−8.7	−75.5	68.0	4	A
TYR	CG	55	−7.2	−75.5	67.9	5	A
TYR	CD1	55	−6.5	−76.4	68.7	9	A
TYR	CE1	55	−5.1	−76.5	68.7	4	A
TYR	CD2	55	−6.5	−74.7	67.1	4	A
TYR	CE2	55	−5.1	−74.7	67.0	1	A
TYR	CZ	55	−4.4	−75.6	67.8	1	A
TYR	OH	55	−3.0	−75.7	67.7	1	A
TYR	C	55	−9.0	−75.3	70.5	6	A
TYR	O	55	−8.0	−75.0	71.1	7	A
VAL	N	56	−9.8	−76.3	70.9	5	A
VAL	CA	56	−9.6	−77.0	72.2	6	A
VAL	CB	56	−10.8	−76.8	73.1	1	A
VAL	CG1	56	−12.1	−77.4	72.5	1	A
VAL	CG2	56	−10.5	−77.5	74.4	2	A
VAL	C	56	−9.5	−78.5	71.8	10	A
VAL	O	56	−10.3	−78.9	70.9	13	A
GLU	N	57	−8.7	−79.2	72.4	11	A
GLU	CA	57	−8.5	−80.6	72.1	9	A
GLU	CB	57	−7.2	−81.2	72.7	12	A
GLU	CG	57	−7.0	−82.6	72.5	15	A
GLU	CD	57	−5.6	−83.0	72.9	22	A
GLU	OE1	57	−4.6	−82.7	72.1	27	A
GLU	OE2	57	−5.3	−83.7	73.9	23	A
GLU	C	57	−9.7	−81.5	72.5	9	A
GLU	O	57	−10.2	−81.3	73.6	11	A
MET	N	58	−10.2	−82.3	71.6	6	A
MET	CA	58	−11.3	−83.2	71.9	7	A
MET	CB	58	−12.6	−82.7	71.2	2	A
MET	CG	58	−13.2	−81.4	71.8	6	A
MET	SD	58	−14.6	−80.8	70.8	4	A
MET	CE	58	−16.0	−81.4	71.8	2	A
MET	C	58	−11.1	−84.6	71.3	9	A
MET	O	58	−10.2	−84.8	70.5	13	A
THR	N	59	−11.9	−85.6	71.8	14	A
THR	CA	59	−11.8	−87.0	71.4	15	A
THR	CB	59	−11.1	−87.9	72.4	17	A
THR	OG1	59	−12.0	−88.1	73.5	18	A
THR	CG2	59	−9.8	−87.3	72.9	21	A
THR	C	59	−13.1	−87.5	71.0	15	A
THR	O	59	−14.1	−87.4	71.8	14	A
VAL	N	60	−13.3	−88.2	69.8	15	A
VAL	CA	60	−14.5	−88.7	69.4	14	A
VAL	CB	60	−15.1	−88.1	68.1	12	A
VAL	CG1	60	−15.2	−86.6	68.4	12	A
VAL	CG2	60	−14.1	−88.3	67.0	12	A
VAL	C	60	−14.4	−90.2	69.1	14	A
VAL	O	60	−13.2	−90.7	68.9	14	A
GLY	N	61	−15.5	−91.0	69.1	16	A
GLY	CA	61	−15.5	−92.4	68.9	19	A
GLY	C	61	−14.7	−93.3	69.8	20	A
GLY	O	61	−13.9	−92.8	70.7	24	A
SER	N	62	−14.9	−94.6	69.7	19	A
SER	CA	62	−14.2	−95.5	70.6	18	A
SER	CB	62	−15.2	−96.3	71.4	15	A
SER	OG	62	−15.9	−95.4	72.3	19	A
SER	C	62	−13.4	−96.6	69.8	20	A
SER	O	62	−14.0	−97.2	68.9	24	A
PRO	N	63	−12.1	−96.7	70.0	18	A
PRO	CD	63	−11.2	−97.6	69.2	16	A
PRO	CA	63	−11.3	−96.0	71.0	18	A
PRO	CB	63	−9.9	−96.7	70.9	19	A
PRO	CG	63	−9.9	−97.0	69.4	18	A
PRO	C	63	−11.2	−94.5	70.6	19	A
PRO	O	63	−11.4	−94.1	69.5	20	A
PRO	N	64	−10.8	−93.7	71.6	20	A
PRO	CD	64	−10.5	−94.0	73.0	19	A
PRO	CA	64	−10.6	−92.2	71.4	19	A
PRO	CB	64	−10.2	−91.7	72.8	19	A
PRO	CG	64	−10.8	−92.8	73.7	19	A
PRO	C	64	−9.7	−91.7	70.3	19	A
PRO	O	64	−8.5	−92.0	70.3	21	A
GLN	N	65	−10.3	−90.9	69.4	18	A
GLN	CA	65	−9.6	−90.2	68.3	18	A
GLN	CB	65	−10.4	−90.3	67.0	18	A
GLN	CG	65	−10.4	−91.6	66.4	17	A
GLN	CD	65	−10.8	−91.6	64.9	19	A
GLN	OE1	65	−10.2	−90.9	64.1	18	A
GLN	NE2	65	−11.9	−92.3	64.6	22	A
GLN	C	65	−9.4	−88.7	68.7	18	A
GLN	O	65	−10.3	−88.0	68.8	18	A
THR	N	66	−8.1	−88.4	68.9	16	A
THR	CA	66	−7.8	−87.0	69.2	13	A
THR	CB	66	−6.3	−86.9	69.8	13	A
THR	OG1	66	−6.2	−87.8	70.9	13	A
THR	CG2	66	−6.0	−85.5	70.2	11	A
THR	C	66	−7.9	−86.1	68.0	11	A
THR	O	66	−7.5	−86.4	66.9	11	A
LEU	N	67	−8.6	−84.9	68.2	11	A
LEU	CA	67	−8.8	−83.9	67.2	10	A
LEU	CB	67	−10.1	−84.2	66.4	13	A
LEU	CG	67	−10.1	−85.4	65.4	15	A
LEU	CD1	67	−11.5	−85.7	65.0	15	A
LEU	CD2	67	−9.2	−85.0	64.2	14	A
LEU	C	67	−8.9	−82.5	67.8	10	A
LEU	O	67	−9.5	−82.3	68.8	7	A
ASN	N	68	−8.4	−81.5	67.0	9	A
ASN	CA	68	−8.5	−80.2	67.5	9	A
ASN	CB	68	−7.2	−79.4	67.0	8	A
ASN	CG	68	−6.0	−79.8	67.9	6	A
ASN	OD1	68	−4.9	−79.4	67.6	11	A
ASN	ND2	68	−6.2	−80.5	69.0	10	A
ASN	C	68	−9.7	−79.5	66.9	7	A
ASN	O	68	−9.8	−79.3	65.7	8	A
ILE	N	69	−10.6	−79.1	67.7	6	A
ILE	CA	69	−11.9	−78.4	67.3	7	A
ILE	CB	69	−13.1	−79.0	68.0	7	A
ILE	CG2	69	−14.3	−78.5	67.4	13	A
ILE	CG1	69	−13.0	−80.5	67.8	13	A
ILE	CD1	69	−12.9	−81.0	66.3	14	A
ILE	C	69	−11.9	−76.9	67.5	10	A
ILE	O	69	−11.6	−76.4	68.6	14	A
LEU	N	70	−12.4	−76.2	66.5	8	A
LEU	CA	70	−12.5	−74.7	66.5	6	A
LEU	CB	70	−12.8	−74.3	65.1	6	A
LEU	CG	70	−12.8	−72.8	64.7	4	A
LEU	CD1	70	−11.4	−72.4	64.2	3	A
LEU	CD2	70	−13.9	−72.5	63.7	2	A
LEU	C	70	−13.6	−74.3	67.4	5	A
LEU	O	70	−14.7	−74.8	67.3	7	A
VAL	N	71	−13.3	−73.4	68.4	1	A
VAL	CA	71	−14.3	−73.0	69.3	2	A
VAL	CB	71	−13.7	−72.5	70.6	4	A
VAL	CG1	71	−14.8	−72.2	71.6	5	A
VAL	CG2	71	−12.7	−73.5	71.1	5	A
VAL	C	71	−15.0	−71.8	68.6	2	A
VAL	O	71	−14.4	−70.7	68.4	6	A
ASP	N	72	−16.2	−72.0	68.2	1	A
ASP	CA	72	−17.0	−71.0	67.4	1	A
ASP	CB	72	−17.2	−71.5	66.0	4	A
ASP	CG	72	−18.1	−70.6	65.1	9	A
ASP	OD1	72	−18.3	−69.4	65.5	13	A
ASP	OD2	72	−18.6	−71.1	64.1	7	A
ASP	C	72	−18.4	−70.8	68.0	1	A
ASP	O	72	−19.3	−71.6	68.0	1	A
THR	N	73	−18.6	−69.6	68.6	1	A
THR	CA	73	−19.8	−69.3	69.2	2	A
THR	CB	73	−19.6	−68.3	70.4	3	A
THR	OG1	73	−18.8	−67.2	70.0	6	A
THR	CG2	73	−18.9	−68.9	71.6	2	A
THR	C	73	−20.8	−68.6	68.2	1	A
THR	O	73	−21.7	−67.9	68.6	1	A
GLY	N	74	−20.5	−68.9	66.9	1	A
GLY	CA	74	−21.3	−68.3	65.9	3	A
GLY	C	74	−22.1	−69.3	65.1	1	A
GLY	O	74	−22.7	−69.0	64.0	1	A
SER	N	75	−22.1	−70.5	65.5	2	A
SER	CA	75	−22.8	−71.6	64.8	1	A
SER	CB	75	−21.9	−72.2	63.7	1	A
SER	OG	75	−20.9	−73.0	64.3	5	A
SER	C	75	−23.2	−72.7	65.8	1	A
SER	O	75	−22.8	−72.6	67.0	1	A
SER	N	76	−24.0	−73.7	65.4	2	A
SER	CA	76	−24.4	−74.7	66.4	5	A
SER	CB	76	−25.8	−74.4	66.8	5	A
SER	OG	76	−25.9	−73.4	67.7	6	A
SER	C	76	−24.2	−76.1	65.9	4	A
SER	O	76	−24.9	−77.0	66.3	5	A
ASN	N	77	−23.2	−76.3	65.1	5	A
ASN	CA	77	−23.0	−77.7	64.6	6	A
ASN	CB	77	−23.1	−77.8	63.1	8	A
ASN	CG	77	−24.5	−77.6	62.6	7	A
ASN	OD1	77	−25.0	−76.4	62.6	8	A
ASN	ND2	77	−25.2	−78.6	62.2	6	A
ASN	C	77	−21.6	−78.1	65.1	5	A
ASN	O	77	−20.7	−77.3	65.1	3	A
PHE	N	78	−21.5	−79.4	65.5	6	A
PHE	CA	78	−20.3	−80.0	65.9	6	A
PHE	CB	78	−20.5	−80.9	67.1	6	A
PHE	CG	78	−19.2	−81.6	67.5	8	A
PHE	CD1	78	−19.3	−82.7	68.3	6	A
PHE	CD2	78	−18.0	−81.2	67.1	10	A
PHE	CE1	78	−18.2	−83.5	68.7	4	A
PHE	CE2	78	−16.8	−81.9	67.5	5	A
PHE	CZ	78	−16.9	−83.0	68.3	3	A
PHE	C	78	−19.9	−80.8	64.7	7	A
PHE	O	78	−20.6	−81.8	64.4	6	A
ALA	N	79	−18.9	−80.4	63.9	7	A
ALA	CA	79	−18.5	−81.1	62.7	8	A
ALA	CB	79	−19.0	−80.4	61.5	7	A
ALA	C	79	−17.0	−81.3	62.7	12	A
ALA	O	79	−16.3	−80.6	63.4	11	A
VAL	N	80	−16.6	−82.3	61.9	13	A
VAL	CA	80	−15.1	−82.6	61.8	13	A
VAL	CB	80	−14.7	−83.6	62.9	16	A
VAL	CG1	80	−15.1	−83.1	64.3	15	A
VAL	CG2	80	−15.3	−85.0	62.7	16	A
VAL	C	80	−14.8	−83.2	60.5	13	A
VAL	O	80	−15.7	−83.7	59.8	9	A
GLY	N	81	−13.5	−83.1	60.1	12	A
GLY	CA	81	−13.1	−83.7	58.8	16	A
GLY	C	81	−13.3	−85.2	58.9	20	A
GLY	O	81	−12.8	−85.8	59.9	21	A
ALA	N	82	−13.8	−85.8	57.9	22	A
ALA	CA	82	−14.0	−87.3	57.9	20	A
ALA	CB	82	−15.5	−87.6	58.0	20	A
ALA	C	82	−13.4	−88.0	56.7	21	A
ALA	O	82	−14.0	−89.0	56.2	23	A
ALA	N	83	−12.4	−87.4	56.1	20	A
ALA	CA	83	−11.7	−88.0	54.9	19	A
ALA	CB	83	−12.7	−88.1	53.8	18	A
ALA	C	83	−10.6	−87.1	54.5	21	A
ALA	O	83	−10.8	−85.9	54.4	23	A
PRO	N	84	−9.4	−87.7	54.2	21	A
PRO	CD	84	−9.3	−89.0	53.7	20	A
PRO	CA	84	−8.2	−86.9	53.8	23	A
PRO	CB	84	−7.4	−87.9	53.1	20	A
PRO	CG	84	−8.4	−88.9	52.5	23	A
PRO	C	84	−8.5	−85.7	52.9	25	A
PRO	O	84	−9.2	−85.7	52.0	27	A
HIS	N	85	−7.8	−84.6	53.3	25	A
HIS	CA	85	−8.0	−83.3	52.6	25	A
HIS	CB	85	−9.0	−82.4	53.3	25	A
HIS	CG	85	−9.1	−81.0	52.7	25	A
HIS	CD2	85	−10.1	−80.4	52.2	27	A
HIS	ND1	85	−8.0	−80.2	52.6	25	A
HIS	CE1	85	−8.4	−79.0	52.1	25	A
HIS	NE2	85	−9.7	−79.1	51.8	28	A
HIS	C	85	−6.6	−82.6	52.6	25	A
HIS	O	85	−5.9	−82.7	53.6	26	A
PRO	N	86	−6.2	−82.1	51.4	25	A
PRO	CD	86	−7.1	−81.9	50.2	25	A
PRO	CA	86	−4.9	−81.4	51.2	27	A
PRO	CB	86	−5.2	−80.4	50.1	27	A
PRO	CG	86	−6.1	−81.3	49.2	27	A
PRO	C	86	−4.3	−80.7	52.4	29	A
PRO	O	86	−3.1	−80.6	52.5	29	A
PHE	N	87	−5.2	−80.2	53.3	26	A
PHE	CA	87	−4.7	−79.4	54.5	24	A
PHE	CB	87	−5.5	−78.1	54.6	25	A
PHE	CG	87	−5.2	−77.2	53.5	24	A
PHE	CD1	87	−5.9	−76.0	53.3	28	A
PHE	CD2	87	−4.2	−77.5	52.5	27	A
PHE	CE1	87	−5.7	−75.1	52.3	31	A
PHE	CE2	87	−3.9	−76.6	51.5	29	A
PHE	CZ	87	−4.7	−75.4	51.3	32	A
PHE	C	87	−4.8	−80.2	55.8	20	A
PHE	O	87	−3.9	−80.1	56.6	17	A
LEU	N	88	−5.8	−81.0	55.9	16	A
LEU	CA	88	−6.0	−81.9	57.1	18	A
LEU	CB	88	−7.3	−82.7	57.0	17	A
LEU	CG	88	−8.6	−81.9	57.2	18	A
LEU	CD1	88	−9.8	−82.9	57.2	19	A
LEU	CD2	88	−8.6	−81.1	58.5	19	A
LEU	C	88	−4.9	−82.8	57.4	21	A
LEU	O	88	−4.5	−83.7	56.6	21	A
HIS	N	89	−4.3	−82.6	58.6	21	A
HIS	CA	89	−3.2	−83.4	59.1	22	A
HIS	CB	89	−2.5	−82.8	60.3	27	A
HIS	CG	89	−1.7	−81.5	60.0	35	A
HIS	CD2	89	−1.6	−80.3	60.6	36	A
HIS	ND1	89	−0.8	−81.5	58.9	39	A
HIS	CE1	89	−0.2	−80.3	58.9	39	A
HIS	NE2	89	−0.7	−79.6	59.9	40	A
HIS	C	89	−3.7	−84.8	59.4	20	A
HIS	O	89	−3.0	−85.8	59.3	22	A
ARG	N	90	−4.9	−84.8	59.9	16	A
ARG	CA	90	−5.6	−86.1	60.3	13	A
ARG	CB	90	−5.2	−86.4	61.7	14	A
ARG	CG	90	−5.4	−85.4	62.8	18	A
ARG	CD	90	−5.2	−85.9	64.2	20	A
ARG	NE	90	−5.1	−84.9	65.2	23	A
ARG	CZ	90	−4.9	−85.1	66.5	22	A
ARG	NH1	90	−4.6	−86.4	66.9	16	A
ARG	NH2	90	−4.9	−84.1	67.4	20	A
ARG	C	90	−7.1	−85.9	60.2	12	A
ARG	O	90	−7.6	−84.8	59.9	15	A
TYR	N	91	−7.9	−86.9	60.4	11	A
TYR	CA	91	−9.3	−86.8	60.3	13	A
TYR	CB	91	−9.8	−86.9	58.9	18	A
TYR	CG	91	−9.5	−88.1	58.1	24	A
TYR	CD1	91	−10.4	−89.2	58.2	24	A
TYR	CE2	91	−10.1	−90.4	57.5	27	A
TYR	CD2	91	−8.4	−88.3	57.3	23	A
TYR	CE2	91	−8.1	−89.5	56.6	24	A
TYR	CZ	91	−9.0	−90.5	56.7	28	A
TYR	OH	91	−8.8	−91.7	56.0	32	A
TYR	C	91	−10.0	−87.9	61.2	13	A
TYR	O	91	−9.4	−88.7	61.8	14	A
TYR	N	92	−11.4	−87.8	61.1	15	A
TYR	CA	92	−12.2	−88.7	61.9	15	A
TYR	CB	92	−13.5	−88.0	62.3	10	A
TYR	CG	92	−14.5	−88.9	63.0	6	A
TYR	CD1	92	−14.2	−89.8	64.0	6	A
TYR	CE1	92	−15.2	−90.5	64.6	6	A
TYR	CD2	92	−15.9	−88.7	62.7	3	A
TYR	CE2	92	−16.9	−89.4	63.4	6	A
TYR	CZ	92	−16.5	−90.3	64.3	4	A
TYR	OH	92	−17.5	−91.0	65.0	1	A
TYR	C	92	−12.5	−90.0	61.2	17	A
TYR	O	92	−13.3	−90.0	60.2	21	A
GLN	N	93	−12.0	−91.1	61.7	18	A
GLN	CA	93	−12.2	−92.4	61.0	18	A
GLN	CB	93	−11.0	−93.3	61.2	19	A
GLN	CG	93	−9.8	−92.8	60.4	21	A
GLN	CD	93	−8.5	−93.6	60.7	22	A
GLN	OE1	93	−8.1	−93.8	61.9	23	A
GLN	NE2	93	−7.9	−94.2	59.6	22	A
GLN	C	93	−13.4	−93.1	61.7	16	A
GLN	O	93	−13.3	−93.6	62.8	12	A
ARG	N	94	−14.6	−93.0	61.1	16	A
ARG	CA	94	−15.8	−93.6	61.6	20	A
ARG	CB	94	−17.0	−93.2	60.7	21	A
ARG	CG	94	−17.3	−91.7	60.8	22	A
ARG	CD	94	−18.4	−91.4	59.8	18	A
ARG	NE	94	−17.9	−91.0	58.5	24	A
ARG	CZ	94	−18.7	−90.7	57.4	26	A
ARG	NH1	94	−20.0	−90.7	57.6	24	A
ARG	NH2	94	−18.1	−90.4	56.2	29	A
ARG	C	94	−15.7	−95.1	61.7	19	A
ARG	O	94	−16.0	−95.7	62.7	16	A
GLN	N	95	−15.3	−95.7	60.6	22	A
GLN	CA	95	−15.1	−97.2	60.5	23	A
GLN	CB	95	−14.5	−97.6	59.2	27	A
GLN	CG	95	−15.3	−97.2	58.0	31	A
GLN	CD	95	−14.6	−97.8	56.7	36	A
GLN	OE1	95	−14.6	−99.0	56.5	35	A
GLN	NE2	95	−14.1	−96.9	55.9	37	A
GLN	C	95	−14.4	−97.8	61.7	24	A
GLN	O	95	−14.6	−98.9	62.1	24	A
LEU	N	96	−13.4	−97.0	62.3	21	A
LEU	CA	96	−12.6	−97.5	63.4	19	A
LEU	CB	96	−11.3	−96.9	63.3	18	A
LEU	CG	96	−10.3	−97.5	62.3	15	A
LEU	CD1	96	−9.1	−96.6	62.0	16	A
LEU	CD2	96	−9.8	−98.9	62.9	15	A
LEU	C	96	−13.3	−97.3	64.8	19	A
LEU	O	96	−12.7	−97.6	65.8	20	A
SER	N	97	−14.5	−96.8	64.8	21	A
SER	CA	97	−15.2	−96.5	66.1	22	A
SER	CB	97	−15.8	−95.1	66.2	27	A
SER	OG	97	−16.6	−95.0	67.3	27	A
SER	C	97	−16.3	−97.5	66.3	22	A
SER	O	97	−17.0	−97.9	65.4	22	A
SER	N	98	−16.4	−98.0	67.5	23	A
SER	CA	98	−17.4	−99.0	67.9	24	A
SER	CB	98	−17.0	−99.9	69.0	24	A
SER	OG	98	−16.6	−99.1	70.1	26	A
SER	C	98	−18.7	−98.3	68.2	24	A
SER	O	98	−19.8	−98.8	67.9	24	A
THR	N	99	−18.6	−97.2	68.9	22	A
THR	CA	99	−19.7	−96.4	69.4	19	A
THR	CB	99	−19.4	−95.6	70.6	17	A
THR	OG1	99	−18.2	−94.8	70.3	16	A
THR	CG2	99	−19.1	−96.5	71.8	19	A
THR	C	99	−20.3	−95.4	68.4	19	A
THR	O	99	−21.1	−94.6	68.7	21	A
TYR	N	100	−19.9	−95.6	67.1	17	A
TYR	CA	100	−20.4	−94.7	66.0	17	A
TYR	CB	100	−19.5	−94.8	64.8	17	A
TYR	CG	100	−20.0	−93.9	63.6	18	A
TYR	CD1	100	−19.9	−92.6	63.6	20	A
TYR	CE1	100	−20.3	−91.8	62.5	21	A
TYR	CD2	100	−20.5	−94.6	62.5	19	A
TYR	CE2	100	−21.0	−93.8	61.4	21	A
TYR	CZ	100	−20.8	−92.4	61.4	23	A
TYR	OH	100	−21.2	−91.7	60.3	22	A
TYR	C	100	−21.8	−95.1	65.6	17	A
TYR	O	100	−22.3	−96.2	65.8	18	A
ARG	N	101	−22.5	−94.1	65.1	16	A
ARG	CA	101	−23.9	−94.3	64.6	18	A
ARG	CB	101	−24.9	−93.9	65.7	14	A
ARG	CG	101	−25.3	−95.0	66.6	15	A
ARG	CD	101	−26.5	−94.6	67.5	21	A
ARG	NE	101	−27.0	−95.6	68.4	26	A
ARG	CZ	101	−26.2	−96.2	69.3	29	A
ARG	NH1	101	−25.0	−95.9	69.4	28	A
ARG	NH2	101	−26.8	−97.2	70.1	29	A
ARG	C	101	−24.0	−93.5	63.3	20	A
ARG	O	101	−23.1	−92.7	63.0	21	A
ASP	N	102	−25.1	−93.6	62.6	19	A
ASP	CA	102	−25.3	−92.9	61.4	20	A
ASP	CB	102	−24.7	−93.7	60.3	17	A
ASP	CG	102	−25.1	−93.2	58.9	18	A
ASP	OD1	102	−24.9	−92.1	58.5	19	A
ASP	OD2	102	−25.6	−94.1	58.1	18	A
ASP	C	102	−26.8	−92.6	61.2	21	A
ASP	O	102	−27.5	−93.5	60.9	25	A
LEU	N	103	−27.2	−91.4	61.4	18	A
LEU	CA	103	−28.6	−91.0	61.2	17	A
LEU	CB	103	−29.0	−89.7	61.9	16	A
LEU	CG	103	−28.2	−89.4	63.2	13	A
LEU	CD1	103	−27.2	−88.3	62.9	10	A
LEU	CD2	103	−29.2	−88.9	64.3	11	A
LEU	C	103	−29.1	−91.0	59.8	18	A
LEU	O	103	−30.2	−90.4	59.5	19	A
ARG	N	104	−28.3	−91.5	58.9	18	A
ARG	CA	104	−28.6	−91.6	57.4	21	A
ARG	CB	104	−29.6	−92.7	57.1	24	A
ARG	CG	104	−28.9	−94.1	57.1	28	A
ARG	CD	104	−29.9	−95.3	57.1	31	A
ARG	NE	104	−31.1	−95.1	56.2	35	A
ARG	CZ	104	−32.3	−94.8	56.7	35	A
ARG	NH1	104	−32.5	−94.6	58.0	37	A
ARG	NH2	104	−33.3	−94.6	55.8	32	A
ARG	C	104	−29.3	−90.3	57.0	21	A
ARG	O	104	−30.4	−90.3	56.5	24	A
LYS	N	105	−28.6	−89.2	57.2	21	A
LYS	CA	105	−29.1	−87.8	56.8	22	A
LYS	CB	105	−30.0	−87.3	57.8	20	A
LYS	CG	105	−30.7	−85.9	57.5	23	A
LYS	CD	105	−31.8	−85.5	58.4	26	A
LYS	CE	105	−31.3	−85.3	59.9	21	A
LYS	NZ	105	−32.3	−84.6	60.8	15	A
LYS	C	105	−27.9	−86.9	56.6	23	A
LYS	O	105	−27.2	−86.6	57.5	25	A
GLY	N	106	−27.8	−86.3	55.4	23	A
GLY	CA	106	−26.7	−85.4	55.1	22	A
GLY	C	106	−27.0	−84.0	55.6	21	A
GLY	O	106	−28.1	−83.7	56.1	20	A
VAL	N	107	−26.0	−83.1	55.5	21	A
VAL	CA	107	−26.1	−81.8	56.0	18	A
VAL	CB	107	−25.9	−81.7	57.5	11	A
VAL	CG1	107	−24.4	−81.9	57.8	10	A
VAL	CG2	107	−26.3	−80.3	58.0	7	A
VAL	C	107	−25.2	−80.8	55.2	19	A
VAL	O	107	−24.0	−81.2	54.9	16	A
TYR	N	108	−25.6	−79.6	54.9	20	A
TYR	CA	108	−24.9	−78.6	54.2	20	A
TYR	CB	108	−25.5	−78.3	52.9	21	A
TYR	CG	108	−25.1	−76.9	52.4	23	A
TYR	CD1	108	−23.8	−76.5	52.3	24	A
TYR	CE1	108	−23.5	−75.2	51.8	26	A
TYR	CD2	108	−26.1	−76.0	52.0	22	A
TYR	CE2	108	−25.8	−74.7	51.5	23	A
TYR	CZ	108	−24.5	−74.3	51.4	24	A
TYR	OH	108	−24.1	−73.1	51.0	23	A
TYR	C	108	−24.8	−77.4	55.1	21	A
TYR	O	108	−25.9	−76.8	55.4	21	A
VAL	N	109	−23.7	−77.0	55.6	18	A
VAL	CA	109	−23.6	−75.8	56.4	19	A
VAL	CB	109	−23.0	−76.2	57.8	19	A
VAL	CG1	109	−22.8	−74.9	58.7	15	A
VAL	CG2	109	−24.0	−77.1	58.5	19	A
VAL	C	109	−22.6	−74.7	55.8	21	A
VAL	O	109	−21.4	−74.9	55.8	23	A
PRO	N	110	−23.2	−73.6	55.4	23	A
PRO	CD	110	−24.7	−73.4	55.1	22	A
PRO	CA	110	−22.4	−72.5	54.8	24	A
PRO	CB	110	−23.4	−72.0	53.7	23	A
PRO	CG	110	−24.7	−72.0	54.4	23	A
PRO	C	110	−22.1	−71.5	55.9	24	A
PRO	O	110	−22.7	−71.4	56.9	21	A
TYR	N	111	−21.1	−70.6	55.6	25	A
TYR	CA	111	−20.7	−69.6	56.5	24	A
TYR	CB	111	−19.4	−70.0	57.3	20	A
TYR	CG	111	−19.6	−71.3	58.1	14	A
TYR	CD1	111	−20.1	−71.2	59.4	14	A
TYR	CE1	111	−20.2	−72.3	60.2	17	A
TYR	CD2	111	−19.3	−72.5	57.6	15	A
TYR	CE2	111	−19.4	−73.7	58.4	15	A
TYR	CZ	111	−19.9	−73.6	59.7	14	A
TYR	OH	111	−19.9	−74.7	60.5	14	A
TYR	C	111	−20.4	−68.3	55.7	24	A
TYR	O	111	−20.4	−68.3	54.4	21	A
THR	N	112	−20.0	−67.2	56.4	24	A
THR	CA	112	−19.6	−66.0	55.7	25	A
THR	CB	112	−19.1	−64.9	56.8	26	A
THR	OG1	112	−20.3	−64.3	57.4	28	A
THR	CG2	112	−18.3	−63.8	56.1	24	A
THR	C	112	−18.5	−66.3	54.8	25	A
THR	O	112	−18.6	−66.0	53.6	28	A
GLN	N	113	−17.5	−67.0	55.3	24	A
GLN	CA	113	−16.4	−67.4	54.6	26	A
GLN	CB	113	−15.1	−66.7	55.1	27	A
GLN	CG	113	−14.9	−65.2	54.7	33	A
GLN	CD	113	−14.6	−65.0	53.2	35	A
GLN	OE1	113	−13.7	−65.7	52.7	33	A
GLN	NE2	113	−15.4	−64.2	52.5	33	A
GLN	C	113	−16.3	−68.9	54.9	26	A
GLN	O	113	−15.8	−69.3	56.0	29	A
GLY	N	114	−16.7	−69.8	54.0	27	A
GLY	CA	114	−16.7	−71.2	54.2	23	A
GLY	C	114	−18.0	−71.9	54.0	23	A
GLY	O	114	−19.1	−71.4	54.1	18	A
LYS	N	115	−17.8	−73.2	53.7	24	A
LYS	CA	115	−19.0	−74.1	53.5	26	A
LYS	CB	115	−19.8	−73.7	52.2	27	A
LYS	CG	115	−18.9	−73.8	50.9	32	A
LYS	CD	115	−19.8	−73.8	49.7	33	A
LYS	CE	115	−20.7	−72.6	49.5	35	A
LYS	NZ	115	−21.5	−72.8	48.2	35	A
LYS	C	115	−18.5	−75.6	53.4	23	A
LYS	O	115	−17.5	−75.9	52.8	22	A
TRP	N	116	−19.3	−76.5	54.0	21	A
TRP	CA	116	−19.0	−77.9	53.9	17	A
TRP	CB	116	−18.1	−78.3	55.1	16	A
TRP	CG	116	−18.6	−77.9	56.4	15	A
TRP	CD2	116	−19.6	−78.4	57.2	14	A
TRP	CE2	116	−19.7	−77.7	58.4	14	A
TRP	CE3	116	−20.6	−79.4	57.0	11	A
TRP	CD1	116	−18.0	−76.9	57.2	15	A
TRP	NE1	116	−18.6	−76.8	58.4	16	A
TRP	CZ2	116	−20.6	−78.0	59.4	10	A
TRP	CZ3	116	−21.5	−79.7	58.0	9	A
TRP	CH2	116	−21.5	−79.0	59.2	7	A
TRP	C	116	−20.3	−78.7	54.0	17	A
TRP	O	116	−21.3	−78.3	54.5	16	A
GLU	N	117	−20.2	−79.9	53.3	17	A
GLU	CA	117	−21.4	−80.8	53.2	18	A
GLU	CB	117	−21.7	−81.1	51.7	23	A
GLU	CG	117	−21.9	−82.6	51.3	31	A
GLU	CD	117	−23.3	−83.1	51.7	39	A
GLU	OE1	117	−24.3	−82.5	51.3	42	A
GLU	OE2	117	−23.3	−84.2	52.3	43	A
GLU	C	117	−20.9	−82.1	53.9	17	A
GLU	O	117	−19.8	−82.6	53.6	12	A
GLY	N	118	−21.7	−82.7	54.7	16	A
GLY	CA	118	−21.3	−83.9	55.4	18	A
GLY	C	118	−22.4	−85.0	55.7	19	A
GLY	O	118	−23.5	−84.8	55.3	20	A
GLU	N	119	−22.0	−86.0	56.5	21	A
GLU	CA	119	−23.0	−87.1	56.8	22	A
GLU	CB	119	−22.4	−88.4	56.3	27	A
GLU	CG	119	−22.3	−88.4	54.7	34	A
GLU	CD	119	−21.5	−89.6	54.2	36	A
GLU	OE1	119	−21.4	−89.7	52.9	36	A
GLU	OE2	119	−20.9	−90.4	55.0	35	A
GLU	C	119	−23.2	−87.1	58.3	19	A
GLU	O	119	−22.3	−87.4	59.1	19	A
LEU	N	120	−24.5	−86.9	58.7	15	A
LEU	CA	120	−24.9	−86.9	60.1	16	A
LEU	CB	120	−26.3	−86.3	60.3	14	A
LEU	CG	120	−26.4	−84.8	60.0	19	A
LEU	CD1	120	−27.9	−84.4	60.1	19	A
LEU	CD2	120	−25.6	−84.0	61.0	19	A
LEU	C	120	−24.9	−88.2	60.8	17	A
LEU	O	120	−25.4	−89.2	60.3	20	A
GLY	N	121	−24.2	−88.3	62.0	18	A
GLY	CA	121	−24.1	−89.5	62.8	18	A
GLY	C	121	−24.1	−89.1	64.2	20	A
GLY	O	121	−24.4	−87.9	64.6	23	A
THR	N	122	−23.7	−90.0	65.1	20	A
THR	CA	122	−23.5	−89.7	66.5	20	A
THR	CB	122	−24.8	−90.0	67.3	18	A
THR	OG1	122	−24.8	−91.4	67.6	15	A
THR	CG2	122	−26.0	−89.5	66.6	15	A
THR	C	122	−22.3	−90.5	67.1	20	A
THR	O	122	−21.8	−91.3	66.4	20	A
ASP	N	123	−21.9	−90.2	68.3	20	A
ASP	CA	123	−20.8	−90.9	68.9	17	A
ASP	CB	123	−19.6	−90.7	68.0	12	A
ASP	CG	123	−18.7	−92.0	68.1	11	A
ASP	OD1	123	−18.4	−92.4	69.2	11	A
ASP	OD2	123	−18.3	−92.5	67.0	15	A
ASP	C	123	−20.5	−90.3	70.3	17	A
ASP	O	123	−21.1	−89.3	70.8	16	A
LEU	N	124	−19.5	−90.9	71.0	16	A
LEU	CA	124	−19.1	−90.4	72.3	16	A
LEU	CB	124	−18.6	−91.6	73.1	18	A
LEU	CG	124	−19.5	−92.7	73.4	19	A
LEU	CD1	124	−18.9	−93.8	74.2	18	A
LEU	CD2	124	−20.7	−92.2	74.1	21	A
LEU	C	124	−18.0	−89.3	72.2	16	A
LEU	O	124	−17.0	−89.5	71.5	17	A
VAL	N	125	−18.3	−88.2	72.8	12	A
VAL	CA	125	−17.4	−87.1	72.8	11	A
VAL	CB	125	−18.0	−85.9	72.2	12	A
VAL	CG1	125	−17.0	−84.7	72.2	13	A
VAL	CG2	125	−18.5	−86.1	70.8	12	A
VAL	C	125	−16.8	−86.8	74.1	10	A
VAL	O	125	−17.4	−87.0	75.1	5	A
SER	N	126	−15.5	−86.4	74.1	11	A
SER	CA	126	−14.8	−86.0	75.3	12	A
SER	CB	126	−13.9	−87.2	75.8	14	A
SER	OG	126	−14.6	−88.1	76.6	12	A
SER	C	126	−13.9	−84.8	75.1	12	A
SER	O	126	−13.5	−84.5	74.0	12	A
ILE	N	127	−13.6	−84.2	76.2	12	A
ILE	CA	127	−12.8	−83.0	76.2	13	A
ILE	CB	127	−13.6	−81.7	76.6	9	A
ILE	CG2	127	−12.6	−80.5	76.8	12	A
ILE	CG1	127	−14.6	−81.4	75.5	10	A
ILE	CD1	127	−15.5	−80.2	75.8	12	A
ILE	C	127	−11.7	−83.2	77.3	12	A
ILE	O	127	−11.9	−83.0	78.4	15	A
PRO	N	128	−10.5	−83.7	76.8	11	A
PRO	CD	128	−10.2	−83.9	75.4	11	A
PRO	CA	128	−9.3	−84.0	77.6	10	A
PRO	CB	128	−8.2	−84.1	76.6	13	A
PRO	CG	128	−8.9	−84.7	75.4	10	A
PRO	C	128	−9.1	−83.0	78.7	10	A
PRO	O	128	−9.0	−83.3	79.9	11	A
HIS	N	129	−8.9	−81.7	78.3	8	A
HIS	CA	129	−8.6	−80.7	79.3	7	A
HIS	CB	129	−7.6	−79.7	78.8	7	A
HIS	CG	129	−6.3	−80.5	78.3	8	A
HIS	CD2	129	−5.7	−80.5	77.2	9	A
HIS	ND1	129	−5.7	−81.4	79.2	7	A
HIS	CE1	129	−4.6	−81.9	78.5	11	A
HIS	NE2	129	−4.6	−81.3	77.3	6	A
HIS	C	129	−9.9	−79.9	79.6	6	A
HIS	O	129	−10.0	−78.7	79.5	6	A
GLY	N	130	−10.9	−80.6	80.0	5	A
GLY	CA	130	−12.2	−80.0	80.4	5	A
GLY	C	130	−12.7	−80.9	81.4	6	A
GLY	O	130	−12.0	−81.7	82.1	5	A
PRO	N	131	−14.1	−80.9	81.7	8	A
PRO	CD	131	−15.1	−80.0	81.1	6	A
PRO	CA	131	−14.7	−81.7	82.7	12	A
PRO	CB	131	−16.1	−81.2	82.8	12	A
PRO	CG	131	−16.3	−80.7	81.4	8	A
PRO	C	131	−14.5	−83.2	82.4	16	A
PRO	O	131	−14.7	−83.6	81.3	15	A
ASN	N	132	−14.2	−84.0	83.4	20	A
ASN	CA	132	−14.0	−85.4	83.3	24	A
ASN	CB	132	−13.4	−86.1	84.5	28	A
ASN	CG	132	−12.9	−87.5	84.3	32	A
ASN	OD1	132	−12.3	−88.1	85.2	34	A
ASN	ND2	132	−13.3	−88.1	83.2	34	A
ASN	C	132	−15.3	−86.1	82.9	24	A
ASN	O	132	−15.9	−86.8	83.8	25	A
VAL	N	133	−15.8	−86.0	81.7	22	A
VAL	CA	133	−17.0	−86.6	81.3	19	A
VAL	CB	133	−18.2	−85.7	81.5	16	A
VAL	CG1	133	−18.4	−85.3	82.9	13	A
VAL	CG2	133	−18.1	−84.4	80.6	11	A
VAL	C	133	−17.0	−87.0	79.8	19	A
VAL	O	133	−16.1	−86.6	79.1	17	A
THR	N	134	−18.0	−87.8	79.4	20	A
THR	CA	134	−18.2	−88.3	78.0	20	A
THR	CB	134	−17.6	−89.7	77.8	21	A
THR	OG1	134	−16.2	−89.7	77.9	18	A
THR	CG2	134	−18.1	−90.3	76.5	17	A
THR	C	134	−19.7	−88.2	77.8	18	A
THR	O	134	−20.5	−88.8	78.5	14	A
VAL	N	135	−20.0	−87.6	76.6	18	A
VAL	CA	135	−21.4	−87.5	76.2	18	A
VAL	CB	135	−22.0	−86.1	76.2	16	A
VAL	CG1	135	−21.9	−85.5	77.7	19	A
VAL	CG2	135	−21.1	−85.2	75.3	18	A
VAL	C	135	−21.6	−88.1	74.8	17	A
VAL	O	135	−20.6	−88.1	74.0	19	A
ARG	N	136	−22.8	−88.5	74.5	14	A
ARG	CA	136	−23.1	−88.9	73.1	13	A
ARG	CB	136	−24.1	−90.0	73.1	15	A
ARG	CG	136	−24.5	−90.5	71.7	19	A
ARG	CD	136	−25.2	−91.8	71.7	21	A
ARG	NE	136	−24.4	−92.9	72.2	25	A
ARG	CZ	136	−23.5	−93.5	71.5	25	A
ARG	NH1	136	−23.2	−93.1	70.2	19	A
ARG	NH2	136	−22.8	−94.6	72.0	23	A
ARG	C	136	−23.7	−87.7	72.5	12	A
ARG	O	136	−24.7	−87.2	72.9	12	A
ALA	N	137	−23.0	−87.2	71.4	11	A
ALA	CA	137	−23.5	−86.0	70.8	11	A
ALA	CB	137	−22.6	−84.8	71.0	11	A
ALA	C	137	−23.6	−86.2	69.3	13	A
ALA	O	137	−23.2	−87.2	68.8	13	A
ASN	N	138	−24.2	−85.2	68.6	13	A
ASN	CA	138	−24.4	−85.3	67.2	13	A
ASN	CB	138	−25.5	−84.4	66.7	13	A
ASN	CG	138	−26.9	−84.9	67.2	15	A
ASN	OD1	138	−27.2	−86.1	67.1	13	A
ASN	ND2	138	−27.7	−84.0	67.6	14	A
ASN	C	138	−23.1	−84.8	66.5	12	A
ASN	O	138	−22.5	−83.8	67.0	14	A
ILE	N	139	−22.6	−85.5	65.5	11	A
ILE	CA	139	−21.4	−85.2	64.9	13	A
ILE	CB	139	−20.2	−86.1	65.3	12	A
ILE	CG2	139	−18.9	−85.5	64.7	12	A
ILE	CG1	139	−20.1	−86.2	66.8	11	A
ILE	CD1	139	−18.9	−86.9	67.3	14	A
ILE	C	139	−21.5	−85.3	63.4	15	A
ILE	O	139	−21.8	−86.3	62.8	16	A
ALA	N	140	−21.4	−84.1	62.7	17	A
ALA	CA	140	−21.5	−84.1	61.3	14	A
ALA	CB	140	−21.9	−82.7	60.8	12	A
ALA	C	140	−20.1	−84.5	60.7	15	A
ALA	O	140	−19.1	−83.8	60.9	15	A
ALA	N	141	−20.1	−85.6	60.0	15	A
ALA	CA	141	−18.9	−86.1	59.4	15	A
ALA	CB	141	−19.0	−87.6	59.2	15	A
ALA	C	141	−18.7	−85.4	58.1	14	A
ALA	O	141	−19.4	−85.7	57.1	11	A
ILE	N	142	−17.8	−84.4	58.0	14	A
ILE	CA	142	−17.6	−83.6	56.8	14	A
ILE	CB	142	−16.7	−82.4	57.2	15	A
ILE	CG2	142	−16.3	−81.7	55.9	15	A
ILE	CG1	142	−17.5	−81.4	58.0	12	A
ILE	CD1	142	−16.8	−80.1	58.4	12	A
ILE	C	142	−16.9	−84.5	55.7	13	A
ILE	O	142	−15.8	−84.9	55.8	9	A
THR	N	143	−17.7	−84.6	54.7	14	A
THR	CA	143	−17.3	−85.4	53.5	16	A
THR	CB	143	−18.4	−86.3	53.0	20	A
THR	OG1	143	−19.6	−85.5	52.9	19	A
THR	CG2	143	−18.7	−87.5	53.9	18	A
THR	C	143	−16.8	−84.6	52.4	15	A
THR	O	143	−16.0	−85.0	51.6	13	A
GLU	N	144	−17.3	−83.4	52.3	18	A
GLU	CA	144	−16.9	−82.4	51.3	25	A
GLU	CB	144	−18.0	−82.4	50.2	29	A
GLU	CG	144	−17.6	−81.6	48.9	34	A
GLU	CD	144	−18.6	−81.9	47.8	40	A
GLU	OE1	144	−18.6	−83.0	47.3	40	A
GLU	OE2	144	−19.3	−80.9	47.4	41	A
GLU	C	144	−16.7	−81.1	51.9	28	A
GLU	O	144	−17.5	−80.6	52.8	29	A
SER	N	145	−15.6	−80.4	51.5	30	A
SER	CA	145	−15.3	−79.1	52.1	28	A
SER	CB	145	−14.3	−79.3	53.2	28	A
SER	OG	145	−13.4	−80.4	52.9	26	A
SER	C	145	−14.7	−78.1	51.1	29	A
SER	O	145	−14.1	−78.5	50.1	29	A
ASP	N	146	−15.0	−76.8	51.3	27	A
ASP	CA	146	−14.6	−75.8	50.4	26	A
ASP	CB	146	−15.5	−75.7	49.2	24	A
ASP	CG	146	−15.2	−74.6	48.3	25	A
ASP	OD1	146	−14.1	−74.5	47.9	26	A
ASP	OD2	146	−16.2	−73.8	47.9	27	A
ASP	C	146	−14.5	−74.4	51.1	26	A
ASP	O	146	−15.5	−73.9	51.6	25	A
LYS	N	147	−13.3	−73.8	51.2	24	A
LYS	CA	147	−13.1	−72.5	51.8	23	A
LYS	CB	147	−14.0	−71.5	51.2	26	A
LYS	CG	147	−13.9	−71.2	49.7	22	A
LYS	CD	147	−12.7	−70.3	49.4	25	A
LYS	CE	147	−12.7	−69.9	48.0	24	A
LYS	NZ	147	−11.5	−69.2	47.6	27	A
LYS	C	147	−13.3	−72.6	53.3	22	A
LYS	O	147	−13.5	−71.6	54.0	18	A
PHE	N	148	−13.2	−73.8	53.9	21	A
PHE	CA	148	−13.4	−74.0	55.3	22	A
PHE	CB	148	−14.3	−75.2	55.6	17	A
PHE	CG	148	−14.8	−75.3	57.0	14	A
PHE	CD1	148	−15.8	−74.4	57.5	16	A
PHE	CD2	148	−14.3	−76.3	57.8	15	A
PHE	CE1	148	−16.3	−74.6	58.8	16	A
PHE	CE2	148	−14.8	−76.5	59.1	14	A
PHE	CZ	148	−15.8	−75.6	59.6	12	A
PHE	C	148	−12.0	−74.3	56.0	23	A
PHE	O	148	−11.4	−73.3	56.6	25	A
PHE	N	149	−11.6	−75.5	55.9	21	A
PHE	CA	149	−10.3	−75.9	56.4	18	A
PHE	CB	149	−10.0	−77.4	56.1	16	A
PHE	CG	149	−11.0	−78.3	56.7	16	A
PHE	CD1	149	−11.5	−79.3	56.0	12	A
PHE	CD2	149	−11.5	−78.1	58.0	15	A
PHE	CE1	149	−12.5	−80.2	56.5	15	A
PHE	CE2	149	−12.4	−79.0	58.6	13	A
PHE	CZ	149	−12.9	−80.0	57.8	12	A
PHE	C	149	−9.1	−75.0	55.9	17	A
PHE	O	149	−9.0	−75.0	54.7	19	A
ILE	N	150	−8.4	−74.4	56.8	16	A
ILE	CA	150	−7.3	−73.5	56.4	14	A
ILE	CB	150	−7.2	−72.3	57.4	9	A
ILE	CG2	150	−6.1	−71.3	56.9	9	A
ILE	CG1	150	−8.6	−71.7	57.4	6	A
ILE	CD1	150	−8.7	−70.5	58.4	6	A
ILE	C	150	−6.0	−74.2	56.3	18	A
ILE	O	150	−5.7	−75.1	57.2	19	A
ASN	N	151	−5.1	−73.9	55.4	23	A
ASN	CA	151	−3.8	−74.5	55.3	26	A
ASN	CB	151	−3.0	−74.1	54.1	28	A
ASN	CG	151	−1.8	−75.0	53.8	34	A
ASN	OD1	151	−1.1	−74.9	52.7	36	A
ASN	ND2	151	−1.6	−76.0	54.7	33	A
ASN	C	151	−2.9	−74.3	56.5	26	A
ASN	O	151	−2.5	−73.2	56.8	25	A
GLY	N	152	−2.7	−75.4	57.3	26	A
GLY	CA	152	−1.9	−75.3	58.5	28	A
GLY	C	152	−2.6	−74.6	59.7	29	A
GLY	O	152	−1.9	−74.0	60.5	28	A
SER	N	153	−3.9	−74.6	59.7	28	A
SER	CA	153	−4.7	−73.9	60.8	27	A
SER	CB	153	−6.1	−73.9	60.5	28	A
SER	OG	153	−6.7	−75.2	60.5	27	A
SER	C	153	−4.5	−74.7	62.1	23	A
SER	O	153	−4.5	−74.2	63.2	22	A
ASN	N	154	−4.3	−76.0	61.9	21	A
ASN	CA	154	−4.1	−77.0	62.9	18	A
ASN	CB	154	−3.1	−76.5	64.0	20	A
ASN	CG	154	−2.4	−77.6	64.7	23	A
ASN	OD1	154	−1.9	−78.6	64.1	23	A
ASN	ND2	154	−2.3	−77.5	66.0	26	A
ASN	C	154	−5.3	−77.5	63.6	15	A
ASN	O	154	−5.3	−78.2	64.6	15	A
TRP	N	155	−6.5	−77.1	63.1	13	A
TRP	CA	155	−7.7	−77.6	63.6	12	A
TRP	CB	155	−8.6	−76.5	64.2	12	A
TRP	CG	155	−8.9	−75.3	63.3	11	A
TRP	CD2	155	−9.9	−75.2	62.3	13	A
TRP	CE2	155	−9.8	−73.9	61.8	15	A
TRP	CE3	155	−10.9	−76.1	61.8	12	A
TRP	CD1	155	−8.2	−74.1	63.3	12	A
TRP	NE1	155	−8.8	−73.3	62.4	14	A
TRP	CZ2	155	−10.7	−73.4	60.8	15	A
TRP	CZ3	155	−11.7	−75.6	60.8	13	A
TRP	CH2	155	−11.6	−74.3	60.3	15	A
TRP	C	155	−8.4	−78.4	62.5	13	A
TRP	O	155	−8.3	−78.0	61.4	15	A
GLU	N	156	−9.1	−79.5	62.9	15	A
GLU	CA	156	−9.7	−80.3	61.9	15	A
GLU	CB	156	−9.1	−81.8	61.9	19	A
GLU	CG	156	−7.6	−81.8	61.8	26	A
GLU	CD	156	−6.9	−81.7	63.2	30	A
GLU	OE1	156	−5.7	−81.6	63.3	32	A
GLU	OE2	156	−7.7	−81.7	64.2	35	A
GLU	C	156	−11.2	−80.4	62.1	13	A
GLU	O	156	−11.9	−81.3	61.5	13	A
GLY	N	157	−11.8	−79.5	62.9	12	A
GLY	CA	157	−13.2	−79.6	63.1	10	A
GLY	C	157	−13.7	−78.3	63.8	9	A
GLY	O	157	−12.9	−77.4	64.1	9	A
ILE	N	158	−15.0	−78.2	63.9	8	A
ILE	CA	158	−15.6	−77.0	64.5	7	A
ILE	CB	158	−16.3	−76.1	63.4	7	A
ILE	CG2	158	−17.3	−76.9	62.7	8	A
ILE	CG1	158	−16.9	−74.9	64.0	11	A
ILE	CD1	158	−17.6	−74.0	63.0	16	A
ILE	C	158	−16.7	−77.4	65.5	8	A
ILE	O	158	−17.4	−78.3	65.4	7	A
LEU	N	159	−16.7	−76.6	66.6	7	A
LEU	CA	159	−17.7	−76.8	67.7	5	A
LEU	CB	159	−16.9	−77.1	69.1	1	A
LEU	CG	159	−17.7	−77.2	70.4	1	A
LEU	CD1	159	−18.4	−78.6	70.4	1	A
LEU	CD2	159	−16.8	−77.2	71.5	1	A
LEU	C	159	−18.6	−75.6	67.9	7	A
LEU	O	159	−18.2	−74.6	68.6	5	A
GLY	N	160	−19.8	−75.7	67.3	6	A
GLY	CA	160	−20.7	−74.6	67.5	9	A
GLY	C	160	−21.3	−74.5	68.9	9	A
GLY	O	160	−22.2	−75.4	69.2	12	A
LEU	N	161	−21.0	−73.5	69.7	8	A
LEU	CA	161	−21.5	−73.4	71.0	6	A
LEU	CB	161	−20.4	−72.8	71.9	3	A
LEU	CG	161	−19.2	−73.8	72.1	3	A
LEU	CD1	161	−18.1	−73.1	72.8	3	A
LEU	CD2	161	−19.6	−75.0	72.9	3	A
LEU	C	161	−22.7	−72.6	71.1	6	A
LEU	O	161	−23.2	−72.3	72.2	7	A
ALA	N	162	−23.3	−72.2	69.9	5	A
ALA	CA	162	−24.5	−71.4	69.9	6	A
ALA	CB	162	−24.7	−70.8	68.5	4	A
ALA	C	162	−25.7	−72.2	70.3	4	A
ALA	O	162	−25.5	−73.3	70.8	4	A
TYR	N	163	−26.9	−71.7	70.0	4	A
TYR	CA	163	−28.1	−72.4	70.3	5	A
TYR	CB	163	−29.1	−71.4	70.8	7	A
TYR	CG	163	−28.8	−70.7	72.1	7	A
TYR	CD1	163	−27.9	−69.6	72.1	10	A
TYR	CE1	163	−27.6	−69.0	73.3	11	A
TYR	CD2	163	−29.4	−71.1	73.3	8	A
TYR	CE2	163	−29.1	−70.4	74.5	10	A
TYR	CZ	163	−28.2	−69.4	74.5	8	A
TYR	OH	163	−27.9	−68.7	75.7	5	A
TYR	C	163	−28.6	−73.2	69.1	6	A
TYR	O	163	−28.3	−72.9	68.0	1	A
ALA	N	164	−29.5	−74.1	69.4	8	A
ALA	CA	164	−30.1	−75.0	68.3	8	A
ALA	CB	164	−30.9	−76.1	69.0	7	A
ALA	C	164	−30.9	−74.3	67.3	6	A
ALA	O	164	−30.9	−74.7	66.1	3	A
GLU	N	165	−31.5	−73.2	67.7	8	A
GLU	CA	165	−32.3	−72.4	66.8	9	A
GLU	CB	165	−32.7	−71.0	67.4	13	A
GLU	CG	165	−33.3	−70.0	66.5	18	A
GLU	CD	165	−34.8	−70.1	66.5	25	A
GLU	OE1	165	−35.4	−69.7	67.6	28	A
GLU	OE2	165	−35.5	−70.5	65.5	28	A
GLU	C	165	−31.6	−72.1	65.4	6	A
GLU	O	165	−32.3	−72.0	64.4	5	A
ILE	N	166	−30.3	−72.1	65.3	5	A
ILE	CA	166	−29.6	−71.8	64.1	5	A
ILE	CB	166	−28.7	−70.6	64.1	4	A
ILE	CG2	166	−29.4	−69.4	64.6	6	A
ILE	CG1	166	−27.5	−71.0	65.0	3	A
ILE	CD1	166	−26.4	−69.9	65.1	1	A
ILE	C	166	−28.8	−73.0	63.6	10	A
ILE	O	166	−28.0	−72.9	62.7	11	A
ALA	N	167	−29.1	−74.2	64.2	12	A
ALA	CA	167	−28.4	−75.4	63.8	15	A
ALA	CB	167	−28.4	−76.4	65.0	15	A
ALA	C	167	−29.0	−76.0	62.6	16	A
ALA	O	167	−30.2	−76.1	62.4	16	A
ARG	N	168	−28.1	−76.4	61.6	14	A
ARG	CA	168	−28.5	−77.1	60.4	12	A
ARG	CB	168	−27.4	−76.8	59.3	14	A
ARG	CG	168	−27.3	−75.4	59.0	16	A
ARG	CD	168	−28.2	−75.0	57.9	20	A
ARG	NE	168	−28.0	−73.6	57.4	30	A
ARG	CZ	168	−28.4	−73.1	56.2	36	A
ARG	NH1	168	−29.0	−74.0	55.4	35	A
ARG	NH2	168	−28.1	−71.9	55.9	33	A
ARG	C	168	−28.6	−78.6	60.7	10	A
ARG	O	168	−27.8	−79.1	61.5	8	A
PRO	N	169	−29.5	−79.3	60.1	9	A
PRO	CD	169	−29.6	−80.8	60.4	11	A
PRO	CA	169	−30.6	−79.0	59.1	9	A
PRO	CB	169	−31.1	−80.3	58.7	9	A
PRO	CG	169	−30.0	−81.3	59.0	12	A
PRO	C	169	−31.6	−78.1	59.8	10	A
PRO	O	169	−32.1	−77.2	59.2	15	A
ASP	N	170	−32.1	−78.5	61.0	10	A
ASP	CA	170	−33.1	−77.8	61.7	14	A
ASP	CB	170	−34.5	−78.4	61.4	19	A
ASP	CG	170	−34.6	−79.8	61.8	26	A
ASP	OD1	170	−34.3	−80.7	61.0	27	A
ASP	OD2	170	−35.1	−80.0	63.0	29	A
ASP	C	170	−32.8	−77.8	63.2	14	A
ASP	O	170	−32.0	−78.5	63.6	11	A
ASP	N	171	−33.6	−77.0	63.9	13	A
ASP	CA	171	−33.5	−76.8	65.3	13	A
ASP	CB	171	−34.4	−75.7	65.8	16	A
ASP	CG	171	−35.9	−76.0	65.6	16	A
ASP	OD1	171	−36.1	−77.1	65.0	14	A
ASP	OD2	171	−36.7	−75.2	65.9	16	A
ASP	C	171	−33.7	−78.1	66.1	14	A
ASP	O	171	−34.1	−78.0	67.3	16	A
SER	N	172	−33.6	−79.2	65.5	12	A
SER	CA	172	−33.8	−80.5	66.2	13	A
SER	CB	172	−34.8	−81.4	65.5	12	A
SER	OG	172	−34.1	−82.0	64.4	16	A
SER	C	172	−32.5	−81.2	66.5	14	A
SER	O	172	−32.4	−82.2	67.3	20	A
LEU	N	173	−31.4	−80.8	65.8	12	A
LEU	CA	173	−30.1	−81.4	65.9	10	A
LEU	CB	173	−29.3	−81.1	64.7	6	A
LEU	CG	173	−28.0	−82.0	64.5	2	A
LEU	CD1	173	−28.4	−83.5	64.5	1	A
LEU	CD2	173	−27.4	−81.6	63.1	2	A
LEU	C	173	−29.4	−80.8	67.2	11	A
LEU	O	173	−28.6	−79.9	67.0	9	A
GLU	N	174	−29.8	−81.3	68.3	13	A
GLU	CA	174	−29.3	−80.8	69.6	14	A
GLU	CB	174	−29.7	−81.8	70.7	16	A
GLU	CG	174	−29.2	−81.5	72.1	21	A
GLU	CD	174	−29.7	−82.4	73.2	25	A
GLU	OE1	174	−30.9	−82.3	73.6	20	A
GLU	OE2	174	−28.9	−83.3	73.6	27	A
GLU	C	174	−27.8	−80.7	69.6	14	A
GLU	O	174	−27.0	−81.6	69.5	16	A
PRO	N	175	−27.3	−79.4	69.8	12	A
PRO	CD	175	−28.3	−78.3	69.8	11	A
PRO	CA	175	−25.9	−78.9	69.8	10	A
PRO	CB	175	−26.1	−77.4	70.0	12	A
PRO	CG	175	−27.4	−77.1	69.3	9	A
PRO	C	175	−25.1	−79.5	70.9	10	A
PRO	O	175	−25.6	−79.7	72.1	12	A
PHE	N	176	−23.8	−79.8	70.6	5	A
PHE	CA	176	−22.9	−80.4	71.6	2	A
PHE	CB	176	−21.4	−80.0	71.3	4	A
PHE	CG	176	−20.5	−80.6	72.3	3	A
PHE	CD1	176	−20.1	−81.9	72.2	3	A
PHE	CD2	176	−20.0	−79.9	73.4	4	A
PHE	CE1	176	−19.3	−82.5	73.2	6	A
PHE	CE2	176	−19.2	−80.4	74.3	6	A
PHE	CZ	176	−18.8	−81.7	74.2	7	A
PHE	C	176	−23.1	−80.0	73.1	3	A
PHE	O	176	−23.4	−80.8	73.9	1	A
PHE	N	177	−23.0	−78.7	73.4	4	A
PHE	CA	177	−23.2	−78.2	74.7	5	A
PHE	CB	177	−23.1	−76.6	74.8	1	A
PHE	CG	177	−22.5	−76.1	76.1	1	A
PHE	CD1	177	−21.2	−76.3	76.4	2	A
PHE	CD2	177	−23.3	−75.5	77.0	1	A
PHE	CE1	177	−20.6	−75.9	77.5	2	A
PHE	CE2	177	−22.8	−75.0	78.2	2	A
PHE	CZ	177	−21.4	−75.2	78.5	3	A
PHE	C	177	−24.5	−78.6	75.3	7	A
PHE	O	177	−24.6	−79.1	76.4	7	A
ASP	N	178	−25.6	−78.4	74.5	8	A
ASP	CA	178	−26.9	−78.8	75.0	12	A
ASP	CB	178	−27.9	−78.5	73.8	11	A
ASP	CG	178	−28.6	−77.2	74.0	21	A
ASP	OD1	178	−29.2	−76.9	75.1	24	A
ASP	OD2	178	−28.6	−76.4	73.0	21	A
ASP	C	178	−26.9	−80.2	75.4	12	A
ASP	O	178	−27.5	−80.5	76.4	13	A
SER	N	179	−26.3	−81.1	74.6	11	A
SER	CA	179	−26.2	−82.5	75.0	9	A
SER	CB	179	−25.6	−83.3	73.9	9	A
SER	OG	179	−26.4	−83.3	72.7	1	A
SER	C	179	−25.4	−82.6	76.3	8	A
SER	O	179	−25.8	−83.2	77.2	8	A
LEU	N	180	−24.2	−82.0	76.3	8	A
LEU	CA	180	−23.4	−82.1	77.5	8	A
LEU	CB	180	−22.1	−81.2	77.4	7	A
LEU	CG	180	−21.2	−81.3	78.6	8	A
LEU	CD1	180	−20.5	−82.6	78.6	6	A
LEU	CD2	180	−20.3	−80.1	78.6	7	A
LEU	C	180	−24.1	−81.7	78.8	8	A
LEU	O	180	−23.9	−82.4	79.8	11	A
VAL	N	181	−24.9	−80.7	78.8	8	A
VAL	CA	181	−25.5	−80.3	80.0	9	A
VAL	CB	181	−26.2	−78.9	79.9	10	A
VAL	CG1	181	−27.1	−78.6	81.1	8	A
VAL	CG2	181	−25.1	−77.8	80.0	8	A
VAL	C	181	−26.6	−81.2	80.4	10	A
VAL	O	181	−26.8	−81.5	81.6	9	A
LYS	N	182	−27.4	−81.7	79.5	6	A
LYS	CA	182	−28.5	−82.6	79.8	5	A
LYS	CB	182	−29.4	−82.8	78.5	5	A
LYS	CG	182	−29.9	−81.5	78.0	4	A
LYS	CD	182	−30.8	−81.7	76.7	10	A
LYS	CE	182	−32.2	−82.1	77.1	10	A
LYS	NZ	182	−33.0	−81.0	77.7	7	A
LYS	C	182	−27.9	−84.0	80.2	4	A
LYS	O	182	−28.6	−84.7	81.0	5	A
GLN	N	183	−26.8	−84.4	79.8	2	A
GLN	CA	183	−26.2	−85.7	80.1	4	A
GLN	CB	183	−25.5	−86.2	78.9	3	A
GLN	CG	183	−26.4	−86.8	77.8	7	A
GLN	CD	183	−25.7	−87.0	76.5	13	A
GLN	OE1	183	−24.6	−87.7	76.5	15	A
GLN	NE2	183	−26.3	−86.5	75.4	13	A
GLN	C	183	−25.3	−85.7	81.3	8	A
GLN	O	183	−24.9	−86.8	81.8	13	A
THR	N	184	−24.9	−84.5	81.9	8	A
THR	CA	184	−24.0	−84.5	83.0	7	A
THR	CB	184	−22.5	−84.2	82.6	5	A
THR	OG1	184	−22.4	−82.9	82.1	4	A
THR	CG2	184	−22.0	−85.2	81.6	4	A
THR	C	184	−24.4	−83.4	84.0	8	A
THR	O	184	−25.4	−82.7	83.8	8	A
HIS	N	185	−23.6	−83.2	85.1	10	A
HIS	CA	185	−23.9	−82.2	86.0	12	A
HIS	CB	185	−23.7	−82.7	87.4	20	A
HIS	CG	185	−24.7	−83.7	87.9	28	A
HIS	CD2	185	−25.8	−83.6	88.7	29	A
HIS	ND1	185	−24.6	−85.0	87.5	31	A
HIS	CE1	185	−25.6	−85.7	88.0	31	A
HIS	NE2	185	−26.3	−84.9	88.7	32	A
HIS	C	185	−23.1	−80.9	85.8	10	A
HIS	O	185	−23.2	−80.0	86.6	10	A
VAL	N	186	−22.5	−80.8	84.6	6	A
VAL	CA	186	−21.7	−79.6	84.3	3	A
VAL	CB	186	−21.1	−79.8	82.9	3	A
VAL	CG1	186	−20.3	−78.5	82.5	1	A
VAL	CG2	186	−20.1	−80.9	82.9	1	A
VAL	C	186	−22.7	−78.5	84.2	3	A
VAL	O	186	−23.7	−78.5	83.5	5	A
PRO	N	187	−22.4	−77.4	85.0	3	A
PRO	CD	187	−21.4	−77.4	86.0	8	A
PRO	CA	187	−23.2	−76.2	85.0	4	A
PRO	CB	187	−22.4	−75.2	85.8	9	A
PRO	CG	187	−21.8	−76.1	86.8	8	A
PRO	C	187	−23.5	−75.8	83.6	1	A
PRO	O	187	−22.8	−76.0	82.7	1	A
ASN	N	188	−24.7	−75.1	83.4	1	A
ASN	CA	188	−25.0	−74.7	82.1	1	A
ASN	CB	188	−26.5	−74.5	81.9	6	A
ASN	CG	188	−27.0	−74.2	80.5	5	A
ASN	OD1	188	−26.2	−74.3	79.5	7	A
ASN	ND2	188	−28.2	−73.8	80.3	8	A
ASN	C	188	−24.4	−73.3	81.7	1	A
ASN	O	188	−25.1	−72.4	81.5	1	A
LEU	N	189	−23.1	−73.3	81.5	1	A
LEU	CA	189	−22.4	−72.1	81.1	1	A
LEU	CB	189	−22.6	−71.0	82.1	3	A
LEU	CG	189	−21.9	−71.2	83.4	6	A
LEU	CD1	189	−20.7	−70.2	83.4	4	A
LEU	CD2	189	−22.8	−70.8	84.6	7	A
LEU	C	189	−20.9	−72.3	80.9	1	A
LEU	O	189	−20.3	−73.1	81.6	1	A
PHE	N	190	−20.3	−71.5	80.0	1	A
PHE	CA	190	−18.9	−71.6	79.8	1	A
PHE	CB	190	−18.6	−72.4	78.5	3	A
PHE	CG	190	−19.1	−71.7	77.2	2	A
PHE	CD1	190	−20.4	−71.9	76.8	5	A
PHE	CD2	190	−18.2	−71.0	76.5	2	A
PHE	CE1	190	−20.8	−71.3	75.6	1	A
PHE	CE2	190	−18.6	−70.3	75.3	3	A
PHE	CZ	190	−19.9	−70.5	74.9	3	A
PHE	C	190	−18.3	−70.2	79.6	1	A
PHE	O	190	−19.0	−69.3	79.2	1	A
SER	N	191	−17.0	−70.0	79.8	3	A
SER	CA	191	−16.4	−68.7	79.7	4	A
SER	CB	191	−16.0	−68.2	81.1	6	A
SER	OG	191	−15.0	−69.0	81.7	13	A
SER	C	191	−15.1	−68.9	78.8	3	A
SER	O	191	−14.4	−69.9	78.9	2	A
LEU	N	192	−14.8	−67.9	78.0	1	A
LEU	CA	192	−13.6	−68.0	77.1	1	A
LEU	CB	192	−14.1	−67.9	75.7	1	A
LEU	CG	192	−14.7	−69.1	75.0	1	A
LEU	CD1	192	−15.3	−68.7	73.7	1	A
LEU	CD2	192	−13.6	−70.1	74.7	2	A
LEU	C	192	−12.7	−66.8	77.4	1	A
LEU	O	192	−13.2	−65.7	77.6	1	A
GLN	N	193	−11.4	−67.0	77.4	1	A
GLN	CA	193	−10.5	−66.0	77.6	1	A
GLN	CB	193	−9.6	−66.2	78.8	1	A
GLN	CG	193	−8.6	−65.0	79.0	1	A
GLN	CD	193	−7.4	−65.4	79.8	1	A
GLN	OE1	193	−6.7	−66.4	79.4	2	A
GLN	NE2	193	−7.1	−64.7	80.9	1	A
GLN	C	193	−9.6	−66.1	76.4	1	A
GLN	O	193	−8.6	−66.8	76.5	1	A
LEU	N	194	−9.9	−65.4	75.3	3	A
LEU	CA	194	−9.0	−65.5	74.1	3	A
LEU	CB	194	−9.9	−65.3	72.9	2	A
LEU	CG	194	−11.0	−66.2	72.7	1	A
LEU	CD1	194	−11.9	−65.9	71.6	1	A
LEU	CD2	194	−10.5	−67.6	72.6	1	A
LEU	C	194	−7.9	−64.5	74.3	5	A
LEU	O	194	−8.2	−63.3	74.5	9	A
CYS	N	195	−6.7	−64.9	74.1	5	A
CYS	CA	195	−5.6	−64.0	74.2	9	A
CYS	C	195	−4.9	−63.9	72.9	12	A
CYS	O	195	−4.5	−64.8	72.3	14	A
CYS	CB	195	−4.5	−64.5	75.2	10	A
CYS	SG	195	−5.2	−65.0	76.8	16	A
GLY	N	196	−4.8	−62.7	72.3	16	A
GLY	CA	196	−4.2	−62.5	71.1	17	A
GLY	C	196	−2.7	−62.6	71.2	18	A
GLY	O	196	−2.2	−62.9	72.4	17	A
ALA	N	197	−1.9	−62.4	70.2	19	A
ALA	CA	197	−0.5	−62.5	70.3	21	A
ALA	CB	197	0.1	−62.9	68.9	20	A
ALA	C	197	0.2	−61.2	70.8	23	A
ALA	O	197	0.6	−61.1	71.9	24	A
GLY	N	198	0.2	−60.2	69.9	27	A
GLY	CA	198	0.8	−58.9	70.3	31	A
GLY	C	198	2.2	−58.9	69.6	32	A
GLY	O	198	2.8	−57.9	69.2	38	A
PHE	N	199	2.7	−60.2	69.5	33	A
PHE	CA	199	4.0	−60.4	68.8	37	A
PHE	CB	199	5.0	−61.0	69.8	35	A
PHE	CG	199	4.6	−60.9	71.3	36	A
PHE	CD1	199	4.4	−59.7	71.9	33	A
PHE	CD2	199	4.4	−62.1	72.0	33	A
PHE	CE1	199	4.0	−59.7	73.3	30	A
PHE	CE2	199	4.1	−62.1	73.3	32	A
PHE	CZ	199	3.9	−60.9	74.0	30	A
PHE	C	199	3.7	−61.4	67.7	38	A
PHE	O	199	2.8	−62.2	67.8	38	A
PRO	N	200	4.6	−61.5	66.7	40	A
PRO	CD	200	5.7	−60.6	66.3	41	A
PRO	CA	200	4.3	−62.4	65.6	39	A
PRO	CB	200	5.3	−62.0	64.5	42	A
PRO	CG	200	6.5	−61.4	65.3	41	A
PRO	C	200	4.4	−63.9	65.9	38	A
PRO	O	200	5.2	−64.3	66.8	36	A
LEU	N	201	3.6	−64.7	65.3	37	A
LEU	CA	201	3.6	−66.2	65.4	34	A
LEU	CB	201	2.6	−66.6	66.5	30	A
LEU	CG	201	2.8	−66.3	67.9	33	A
LEU	CD1	201	1.9	−67.2	68.8	29	A
LEU	CD2	201	4.3	−66.6	68.3	28	A
LEU	C	201	3.1	−66.8	64.1	34	A
LEU	O	201	1.9	−66.9	63.8	31	A
ASN	N	202	4.1	−67.2	63.3	34	A
ASN	CA	202	3.8	−67.9	62.0	36	A
ASN	CB	202	5.1	−68.2	61.2	35	A
ASN	CG	202	5.9	−69.4	61.9	37	A
ASN	OD1	202	6.4	−69.3	63.0	36	A
ASN	ND2	202	6.1	−70.5	61.1	32	A
ASN	C	202	3.0	−69.2	62.2	37	A
ASN	O	202	2.2	−69.3	63.2	39	A
GLN	N	203	3.1	−70.1	61.3	38	A
GLN	CA	203	2.4	−71.4	61.5	38	A
GLN	CB	203	2.4	−72.2	60.2	38	A
GLN	CG	203	1.5	−73.5	60.2	39	A
GLN	CD	203	2.2	−74.7	60.7	40	A
GLN	OE1	203	2.2	−75.0	61.9	39	A
GLN	NE2	203	2.8	−75.4	59.7	40	A
GLN	C	203	3.0	−72.3	62.6	39	A
GLN	O	203	2.2	−72.8	63.4	38	A
SER	N	204	4.3	−72.4	62.6	39	A
SER	CA	204	5.0	−73.2	63.7	41	A
SER	CB	204	6.4	−73.5	63.1	41	A
SER	OG	204	7.0	−74.5	64.0	40	A
SER	C	204	5.1	−72.5	65.1	43	A
SER	O	204	6.0	−72.8	65.9	44	A
GLU	N	205	4.1	−71.7	65.4	43	A
GLU	CA	205	4.0	−71.0	66.7	41	A
GLU	CB	205	4.3	−69.5	66.5	37	A
GLU	CG	205	5.7	−69.1	66.2	36	A
GLU	CD	205	6.7	−69.4	67.3	40	A
GLU	OE1	205	6.9	−70.5	67.8	37	A
GLU	OE2	205	7.3	−68.4	67.8	37	A
GLU	C	205	2.7	−71.2	67.4	41	A
GLU	O	205	2.2	−70.4	68.2	39	A
VAL	N	206	2.1	−72.4	67.1	40	A
VAL	CA	206	0.8	−72.8	67.7	38	A
VAL	CB	206	−0.3	−72.9	66.6	34	A
VAL	CG1	206	−1.7	−72.6	67.2	30	A
VAL	CG2	206	0.0	−72.1	65.4	33	A
VAL	C	206	0.8	−74.1	68.5	38	A
VAL	O	206	0.5	−74.2	69.7	35	A
LEU	N	207	1.3	−75.1	67.8	39	A
LEU	CA	207	1.4	−76.5	68.3	39	A
LEU	CB	207	2.0	−77.4	67.3	36	A
LEU	CG	207	1.3	−77.6	65.9	34	A
LEU	CD1	207	1.6	−76.5	64.9	27	A
LEU	CD2	207	1.8	−79.0	65.3	32	A
LEU	C	207	2.3	−76.5	69.6	41	A
LEU	O	207	2.1	−77.3	70.5	40	A
ALA	N	208	3.4	−75.7	69.5	43	A
ALA	CA	208	4.3	−75.6	70.6	43	A
ALA	CB	208	5.7	−75.3	70.1	41	A
ALA	C	208	3.9	−74.7	71.7	44	A
ALA	O	208	4.6	−74.5	72.8	44	A
SER	N	209	2.8	−73.9	71.5	44	A
SER	CA	209	2.3	−73.0	72.5	42	A
SER	CB	209	2.7	−71.5	72.0	41	A
SER	OG	209	4.0	−71.2	72.2	35	A
SER	C	209	0.8	−73.0	72.9	41	A
SER	O	209	0.2	−74.1	72.9	43	A
VAL	N	210	0.3	−71.8	73.3	41	A
VAL	CA	210	−1.1	−71.7	73.7	35	A
VAL	CB	210	−1.2	−72.0	75.3	32	A
VAL	CG1	210	−2.6	−71.8	75.7	29	A
VAL	CG2	210	−0.8	−73.4	75.5	26	A
VAL	C	210	−1.6	−70.2	73.4	34	A
VAL	O	210	−0.9	−69.2	73.7	35	A
GLY	N	211	−2.8	−70.1	72.9	28	A
GLY	CA	211	−3.5	−68.9	72.6	17	A
GLY	C	211	−4.4	−68.4	73.7	13	A
GLY	O	211	−4.8	−67.2	73.8	12	A
GLY	N	212	−4.9	−69.3	74.5	11	A
GLY	CA	212	−5.9	−68.9	75.6	9	A
GLY	C	212	−6.6	−70.0	76.2	7	A
GLY	O	212	−6.2	−71.2	76.1	8	A
SER	N	213	−7.7	−69.7	77.0	4	A
SER	CA	213	−8.4	−70.8	77.7	2	A
SER	CB	213	−8.0	−70.8	79.1	1	A
SER	OG	213	−7.6	−69.6	79.7	1	A
SER	C	213	−10.0	−70.7	77.6	1	A
SER	O	213	−10.6	−69.7	77.6	3	A
MET	N	214	−10.6	−71.9	77.6	1	A
MET	CA	214	−12.0	−72.0	77.6	1	A
MET	CB	214	−12.5	−72.8	76.3	1	A
MET	CG	214	−14.0	−73.3	76.5	1	A
MET	SD	214	−14.7	−74.0	75.0	1	A
MET	CE	214	−14.3	−75.7	75.3	1	A
MET	C	214	−12.4	−72.9	78.8	2	A
MET	O	214	−12.3	−74.1	78.8	2	A
ILE	N	215	−13.0	−72.2	79.8	2	A
ILE	CA	215	−13.5	−72.8	81.0	1	A
ILE	CB	215	−13.5	−71.8	82.2	1	A
ILE	CG2	215	−14.0	−72.5	83.4	3	A
ILE	CG1	215	−12.1	−71.3	82.3	1	A
ILE	CD1	215	−11.0	−72.3	82.3	1	A
ILE	C	215	−14.9	−73.4	80.9	1	A
ILE	O	215	−15.8	−72.6	80.7	1	A
ILE	N	216	−15.0	−74.7	80.9	1	A
ILE	CA	216	−16.3	−75.4	80.8	4	A
ILE	CB	216	−16.2	−76.8	80.2	6	A
ILE	CG2	216	−17.6	−77.4	80.1	4	A
ILE	CG1	216	−15.5	−76.7	78.8	9	A
ILE	CD1	216	−16.2	−75.9	77.8	16	A
ILE	C	216	−17.0	−75.5	82.1	3	A
ILE	O	216	−16.5	−76.1	83.1	1	A
GLY	N	217	−18.2	−74.9	82.3	5	A
GLY	CA	217	−19.0	−75.1	83.5	3	A
GLY	C	217	−18.7	−74.1	84.6	1	A
GLY	O	217	−18.9	−74.5	85.8	3	A
GLY	N	218	−18.4	−72.9	84.3	1	A
GLY	CA	218	−18.1	−71.9	85.4	3	A
GLY	C	218	−17.1	−70.9	85.1	3	A
GLY	O	218	−16.5	−70.8	84.0	2	A
ILE	N	219	−16.9	−70.0	86.1	5	A
ILE	CA	219	−15.9	−68.9	86.0	6	A
ILE	CB	219	−16.6	−67.6	86.4	2	A
ILE	CG2	219	−15.8	−66.4	85.9	5	A
ILE	CG1	219	−18.0	−67.6	85.9	1	A
ILE	CD1	219	−18.8	−66.5	86.5	1	A
ILE	C	219	−14.6	−69.1	86.7	6	A
ILE	O	219	−14.6	−69.7	87.8	12	A
ASP	N	220	−13.5	−68.6	86.2	7	A
ASP	CA	220	−12.2	−68.7	86.8	8	A
ASP	CB	220	−11.2	−69.4	86.0	3	A
ASP	CG	220	−9.9	−69.6	86.6	1	A
ASP	OD1	220	−9.5	−70.8	86.9	1	A
ASP	OD2	220	−9.2	−68.6	86.9	1	A
ASP	C	220	−11.7	−67.3	87.2	11	A
ASP	O	220	−11.1	−66.6	86.3	8	A
HIS	N	221	−11.9	−66.9	88.4	16	A
HIS	CA	221	−11.5	−65.6	88.9	18	A
HIS	CB	221	−11.9	−65.5	90.4	26	A
HIS	CG	221	−13.3	−65.4	90.6	37	A
HIS	CD2	221	−14.3	−66.3	90.6	35	A
HIS	ND1	221	−14.0	−64.2	91.0	39	A
HIS	CE1	221	−15.3	−64.5	91.2	38	A
HIS	NE2	221	−15.5	−65.7	90.9	37	A
HIS	C	221	−10.1	−65.2	88.6	14	A
HIS	O	221	−9.7	−64.0	88.7	13	A
SER	N	222	−9.3	−66.2	88.2	10	A
SER	CA	222	−7.9	−65.9	87.9	8	A
SER	CB	222	−7.0	−67.1	88.3	9	A
SER	OG	222	−6.9	−68.0	87.3	8	A
SER	C	222	−7.6	−65.5	86.5	6	A
SER	O	222	−6.4	−65.6	86.0	3	A
LEU	N	223	−8.6	−65.2	85.8	7	A
LEU	CA	223	−8.5	−64.9	84.4	4	A
LEU	CB	223	−9.3	−65.8	83.5	1	A
LEU	CG	223	−8.9	−67.3	83.6	1	A
LEU	CD1	223	−9.9	−68.2	83.0	1	A
LEU	CD2	223	−7.6	−67.5	82.8	1	A
LEU	C	223	−8.9	−63.4	84.1	2	A
LEU	O	223	−8.7	−62.9	83.0	1	A
TYR	N	224	−9.5	−62.8	85.1	1	A
TYR	CA	224	−9.9	−61.4	84.9	1	A
TYR	CB	224	−11.4	−61.3	84.6	1	A
TYR	CG	224	−12.4	−61.7	85.6	1	A
TYR	CD1	224	−12.6	−63.0	86.0	1	A
TYR	CE1	224	−13.6	−63.3	87.0	1	A
TYR	CD2	224	−13.2	−60.7	86.2	1	A
TYR	CE2	224	−14.2	−61.0	87.1	1	A
TYR	CZ	224	−14.3	−62.3	87.5	1	A
TYR	OH	224	−15.3	−62.7	88.4	3	A
TYR	C	224	−9.7	−60.5	86.1	1	A
TYR	O	224	−9.7	−60.9	87.3	1	A
THR	N	225	−9.5	−59.2	85.8	1	A
THR	CA	225	−9.2	−58.2	86.9	3	A
THR	CB	225	−7.9	−57.4	86.6	2	A
THR	OG1	225	−8.0	−56.8	85.3	2	A
THR	CG2	225	−6.7	−58.3	86.7	4	A
THR	C	225	−10.4	−57.2	86.8	5	A
THR	O	225	−10.9	−56.9	85.7	8	A
GLY	N	226	−10.8	−56.7	87.9	5	A
GLY	CA	226	−12.0	−55.8	87.9	2	A
GLY	C	226	−13.3	−56.6	88.1	1	A
GLY	O	226	−13.2	−57.7	88.7	1	A
SER	N	227	−14.4	−56.0	87.8	1	A
SER	CA	227	−15.7	−56.6	88.0	1	A
SER	CB	227	−16.7	−55.6	88.6	1	A
SER	OG	227	−16.2	−55.0	89.8	4	A
SER	C	227	−16.2	−57.2	86.7	1	A
SER	O	227	−15.7	−57.0	85.6	1	A
LEU	N	228	−17.4	−57.9	86.8	2	A
LEU	CA	228	−18.0	−58.5	85.7	1	A
LEU	CB	228	−18.3	−60.0	85.9	1	A
LEU	CG	228	−17.2	−61.1	85.7	1	A
LEU	CD1	228	−17.7	−62.5	86.1	1	A
LEU	CD2	228	−16.9	−61.0	84.2	1	A
LEU	C	228	−19.4	−57.9	85.4	1	A
LEU	O	228	−20.2	−57.9	86.3	1	A
TRP	N	229	−19.5	−57.2	84.3	1	A
TRP	CA	229	−20.8	−56.6	83.9	1	A
TRP	CB	229	−20.5	−55.2	83.4	2	A
TRP	CG	229	−20.0	−54.2	84.4	1	A
TRP	CD2	229	−20.8	−53.2	85.0	2	A
TRP	CE2	229	−19.9	−52.5	85.9	1	A
TRP	CE3	229	−22.1	−52.8	85.0	2	A
TRP	CD1	229	−18.8	−54.1	84.9	1	A
TRP	NE1	229	−18.7	−53.1	85.8	1	A
TRP	CZ2	229	−20.3	−51.4	86.7	3	A
TRP	CZ3	229	−22.5	−51.7	85.7	1	A
TRP	CH2	229	−21.6	−51.0	86.6	2	A
TRP	C	229	−21.5	−57.4	82.9	1	A
TRP	O	229	−20.9	−57.7	81.9	1	A
TYR	N	230	−22.8	−57.7	83.2	1	A
TYR	CA	230	−23.5	−58.5	82.3	2	A
TYR	CB	230	−24.3	−59.6	83.1	1	A
TYR	CG	230	−23.5	−60.6	83.8	1	A
TYR	CD1	230	−23.0	−60.3	85.1	1	A
TYR	CE1	230	−22.2	−61.2	85.8	1	A
TYR	CD2	230	−23.1	−61.8	83.2	1	A
TYR	CE2	230	−22.3	−62.7	83.9	1	A
TYR	CZ	230	−21.8	−62.3	85.2	1	A
TYR	OH	230	−21.0	−63.2	85.8	1	A
TYR	C	230	−24.5	−57.8	81.4	3	A
TYR	O	230	−24.9	−56.7	81.7	4	A
THR	N	231	−24.7	−58.4	80.2	3	A
THR	CA	231	−25.6	−57.8	79.2	1	A
THR	CB	231	−24.9	−57.3	78.0	1	A
THR	OG1	231	−25.8	−56.9	77.0	1	A
THR	CG2	231	−24.0	−58.5	77.4	1	A
THR	C	231	−26.6	−58.9	78.8	3	A
THR	O	231	−26.2	−60.1	78.6	3	A
PRO	N	232	−27.9	−58.6	78.7	3	A
PRO	CD	232	−28.4	−57.3	78.9	3	A
PRO	CA	232	−28.9	−59.6	78.3	4	A
PRO	CB	232	−30.2	−58.7	78.3	3	A
PRO	CG	232	−29.8	−57.6	79.2	3	A
PRO	C	232	−28.7	−60.3	77.0	7	A
PRO	O	232	−28.3	−59.6	76.1	13	A
ILE	N	233	−29.0	−61.6	76.9	6	A
ILE	CA	233	−28.9	−62.3	75.7	3	A
ILE	CB	233	−28.7	−63.8	75.8	1	A
ILE	CG2	233	−28.7	−64.5	74.5	1	A
ILE	CG1	233	−27.3	−64.1	76.5	3	A
ILE	CD1	233	−26.9	−65.6	76.4	1	A
ILE	C	233	−30.2	−62.1	75.1	2	A
ILE	O	233	−31.2	−62.6	75.6	3	A
ARG	N	234	−30.3	−61.3	74.0	2	A
ARG	CA	234	−31.6	−61.0	73.4	1	A
ARG	CB	234	−31.3	−60.3	72.1	1	A
ARG	CG	234	−32.0	−58.9	72.1	1	A
ARG	CD	234	−32.4	−58.5	70.7	4	A
ARG	NE	234	−33.6	−57.8	70.7	6	A
ARG	CZ	234	−34.3	−57.5	69.6	5	A
ARG	NH1	234	−33.9	−57.9	68.4	2	A
ARG	NH2	234	−35.4	−56.8	69.8	9	A
ARG	C	234	−32.4	−62.2	73.1	1	A
ARG	O	234	−33.4	−62.5	73.8	3	A
ARG	N	235	−32.1	−63.0	72.0	1	A
ARG	CA	235	−32.9	−64.2	71.7	1	A
ARG	CB	235	−33.5	−64.0	70.3	4	A
ARG	CG	235	−34.7	−64.9	70.0	10	A
ARG	CD	235	−34.7	−65.5	68.7	10	A
ARG	NE	235	−34.5	−64.5	67.6	11	A
ARG	CZ	235	−34.4	−64.9	66.3	10	A
ARG	NH1	235	−34.5	−66.2	65.9	9	A
ARG	NH2	235	−34.3	−63.9	65.4	10	A
ARG	C	235	−31.9	−65.3	71.6	1	A
ARG	O	235	−30.8	−65.2	71.1	3	A
GLU	N	236	−32.3	−66.5	72.2	2	A
GLU	CA	236	−31.4	−67.6	72.2	3	A
GLU	CB	236	−31.8	−68.6	73.3	7	A
GLU	CG	236	−31.7	−68.0	74.7	13	A
GLU	CD	236	−31.9	−69.1	75.8	15	A
GLU	OE1	236	−33.0	−69.7	75.8	15	A
GLU	OE2	236	−30.9	−69.3	76.6	16	A
GLU	C	236	−31.2	−68.3	70.9	1	A
GLU	O	236	−31.6	−69.4	70.8	3	A
TRP	N	237	−30.5	−67.7	69.9	1	A
TRP	CA	237	−30.2	−68.3	68.7	1	A
TRP	CB	237	−31.0	−67.7	67.5	1	A
TRP	CG	237	−30.9	−66.2	67.3	3	A
TRP	CD2	237	−31.1	−65.5	66.1	1	A
TRP	CE2	237	−31.1	−64.2	66.4	1	A
TRP	CE3	237	−31.2	−65.9	64.8	1	A
TRP	CD1	237	−30.8	−65.3	68.3	5	A
TRP	NE1	237	−30.9	−64.0	67.7	1	A
TRP	CZ2	237	−31.2	−63.2	65.4	1	A
TRP	CZ3	237	−31.3	−65.0	63.8	2	A
TRP	CH2	237	−31.3	−63.6	64.1	3	A
TRP	C	237	−28.7	−68.1	68.5	1	A
TRP	O	237	−27.9	−69.0	68.8	2	A
TYR	N	238	−28.3	−66.9	68.1	2	A
TYR	CA	238	−26.9	−66.6	68.0	2	A
TYR	CB	238	−26.6	−65.5	67.0	2	A
TYR	CG	238	−26.5	−65.9	65.5	1	A
TYR	CD1	238	−25.4	−66.6	65.0	3	A
TYR	CE1	238	−25.3	−66.9	63.7	5	A
TYR	CD2	238	−27.5	−65.6	64.7	3	A
TYR	CE2	238	−27.5	−65.9	63.3	8	A
TYR	CZ	238	−26.3	−66.5	62.8	6	A
TYR	OH	238	−26.2	−66.8	61.5	10	A
TYR	C	238	−26.8	−66.0	69.4	3	A
TYR	O	238	−27.8	−65.7	70.0	6	A
TYR	N	239	−25.6	−65.7	69.9	3	A
TYR	CA	239	−25.5	−65.1	71.2	3	A
TYR	CB	239	−24.2	−65.3	71.9	2	A
TYR	CG	239	−24.0	−66.7	72.4	1	A
TYR	CD1	239	−23.3	−67.7	71.7	1	A
TYR	CE1	239	−23.2	−69.0	72.1	1	A
TYR	CD2	239	−24.5	−67.1	73.6	1	A
TYR	CE2	239	−24.4	−68.4	74.1	1	A
TYR	CZ	239	−23.7	−69.3	73.4	1	A
TYR	OH	239	−23.6	−70.6	73.8	2	A
TYR	C	239	−25.7	−63.6	71.0	3	A
TYR	O	239	−24.8	−62.8	71.1	1	A
GLU	N	240	−26.9	−63.2	70.6	3	A
GLU	CA	240	−27.2	−61.8	70.3	4	A
GLU	CB	240	−28.6	−61.7	69.6	2	A
GLU	CG	240	−29.1	−60.3	69.4	2	A
GLU	CD	240	−30.3	−60.1	68.5	1	A
GLU	OE1	240	−31.2	−61.0	68.6	1	A
GLU	OE2	240	−30.3	−59.2	67.6	4	A
GLU	C	240	−27.2	−60.9	71.5	3	A
GLU	O	240	−27.6	−61.3	72.6	1	A
VAL	N	241	−26.7	−59.7	71.3	1	A
VAL	CA	241	−26.6	−58.7	72.3	1	A
VAL	CB	241	−25.2	−58.5	72.8	1	A
VAL	CG1	241	−24.7	−59.7	73.5	1	A
VAL	CG2	241	−24.3	−58.1	71.6	1	A
VAL	C	241	−27.1	−57.4	71.6	1	A
VAL	O	241	−27.3	−57.4	70.4	1	A
ILE	N	242	−27.3	−56.3	72.4	1	A
ILE	CA	242	−27.8	−55.1	71.9	1	A
ILE	CB	242	−29.1	−54.7	72.4	1	A
ILE	CG2	242	−29.4	−53.2	72.2	1	A
ILE	CG1	242	−30.2	−55.6	71.8	1	A
ILE	CD1	242	−31.4	−55.6	72.6	1	A
ILE	C	242	−26.8	−53.9	72.2	1	A
ILE	O	242	−26.6	−53.7	73.4	4	A
ILE	N	243	−26.2	−53.3	71.2	1	A
ILE	CA	243	−25.3	−52.2	71.5	1	A
ILE	CB	243	−24.2	−52.1	70.3	1	A
ILE	CG2	243	−23.5	−50.8	70.4	1	A
ILE	CG1	243	−23.3	−53.2	70.4	1	A
ILE	CD1	243	−22.2	−53.2	69.4	1	A
ILE	C	243	−26.1	−50.9	71.6	1	A
ILE	O	243	−27.0	−50.7	70.7	1	A
VAL	N	244	−25.9	−50.1	72.6	1	A
VAL	CA	244	−26.7	−48.9	72.7	1	A
VAL	CB	244	−27.3	−48.8	74.1	1	A
VAL	CG1	244	−28.3	−49.8	74.4	1	A
VAL	CG2	244	−26.2	−48.8	75.2	1	A
VAL	C	244	−25.9	−47.6	72.4	1	A
VAL	O	244	−26.5	−46.5	72.5	1	A
ARG	N	245	−24.6	−47.7	72.2	1	A
ARG	CA	245	−23.8	−46.5	71.9	1	A
ARG	CB	245	−23.8	−45.7	73.2	1	A
ARG	CG	245	−23.0	−44.4	73.1	1	A
ARG	CD	245	−22.7	−43.9	74.6	1	A
ARG	NE	245	−22.1	−42.6	74.7	1	A
ARG	CZ	245	−22.8	−41.5	74.5	5	A
ARG	NH1	245	−24.1	−41.5	74.2	6	A
ARG	NH2	245	−22.2	−40.3	74.6	1	A
ARG	C	245	−22.4	−46.9	71.5	1	A
ARG	O	245	−22.0	−48.0	71.8	1	A
VAL	N	246	−21.8	−46.0	70.7	2	A
VAL	CA	246	−20.4	−46.3	70.3	1	A
VAL	CB	246	−20.4	−46.8	68.9	1	A
VAL	CG1	246	−19.0	−46.9	68.4	1	A
VAL	CG2	246	−21.0	−48.2	68.8	1	A
VAL	C	246	−19.6	−44.9	70.3	1	A
VAL	O	246	−20.2	−43.9	69.8	1	A
GLU	N	247	−18.4	−45.0	70.8	1	A
GLU	CA	247	−17.6	−43.7	70.8	1	A
GLU	CB	247	−17.5	−43.2	72.3	2	A
GLU	CG	247	−18.6	−43.5	73.2	2	A
GLU	CD	247	−18.3	−42.9	74.6	3	A
GLU	OE1	247	−17.1	−42.9	75.0	1	A
GLU	OE2	247	−19.3	−42.4	75.3	3	A
GLU	C	247	−16.2	−44.0	70.3	1	A
GLU	O	247	−15.7	−45.1	70.5	1	A
ILE	N	248	−15.6	−43.1	69.7	1	A
ILE	CA	248	−14.2	−43.2	69.2	1	A
ILE	CB	248	−14.1	−42.9	67.7	1	A
ILE	CG2	248	−12.7	−43.2	67.3	1	A
ILE	CG1	248	−15.1	−43.8	66.9	1	A
ILE	CD1	248	−14.9	−45.2	67.1	1	A
ILE	C	248	−13.4	−42.2	70.0	1	A
ILE	O	248	−13.5	−41.0	69.7	1	A
ASN	N	249	−12.7	−42.6	71.0	1	A
ASN	CA	249	−11.9	−41.7	71.8	1	A
ASN	CB	249	−10.9	−40.9	71.0	1	A
ASN	CG	249	−9.5	−41.4	71.3	1	A
ASN	OD1	249	−9.3	−42.5	71.7	1	A
ASN	ND2	249	−8.5	−40.5	71.0	1	A
ASN	C	249	−12.9	−40.8	72.5	1	A
ASN	O	249	−12.7	−39.6	72.5	1	A
GLY	N	250	−13.9	−41.3	73.1	1	A
GLY	CA	250	−14.9	−40.5	73.8	1	A
GLY	C	250	−15.9	−39.8	73.0	2	A
GLY	O	250	−17.0	−39.4	73.5	4	A
GLN	N	251	−15.6	−39.6	71.7	1	A
GLN	CA	251	−16.6	−38.9	70.9	1	A
GLN	CB	251	−15.8	−38.3	69.7	4	A
GLN	CG	251	−16.6	−37.3	68.9	1	A
GLN	CD	251	−15.6	−36.1	68.6	2	A
GLN	OE1	251	−15.8	−35.5	67.5	6	A
GLN	NE2	251	−14.7	−35.8	69.5	3	A
GLN	C	251	−17.7	−39.9	70.4	1	A
GLN	O	251	−17.4	−40.9	69.7	1	A
ASP	N	252	−18.9	−39.5	70.7	1	A
ASP	CA	252	−20.1	−40.3	70.4	1	A
ASP	CB	252	−21.3	−39.7	71.1	1	A
ASP	CG	252	−22.6	−40.4	70.7	1	A
ASP	OD1	252	−22.5	−41.5	70.1	1	A
ASP	OD2	252	−23.7	−39.8	70.9	1	A
ASP	C	252	−20.3	−40.2	68.9	1	A
ASP	O	252	−20.5	−39.2	68.4	3	A
LEU	N	253	−20.2	−41.4	68.3	1	A
LEU	CA	253	−20.4	−41.6	66.8	1	A
LEU	CB	253	−20.5	−43.0	66.5	1	A
LEU	CG	253	−19.7	−43.6	65.3	1	A
LEU	CD1	253	−18.3	−43.1	65.3	1	A
LEU	CD2	253	−19.8	−45.1	65.3	1	A
LEU	C	253	−21.7	−40.9	66.4	1	A
LEU	O	253	−21.9	−40.5	65.3	2	A
LYS	N	254	−22.6	−40.7	67.4	4	A
LYS	CA	254	−23.9	−40.1	67.3	5	A
LYS	CB	254	−23.6	−38.6	67.1	3	A
LYS	CG	254	−24.7	−37.7	67.7	8	A
LYS	CD	254	−24.5	−36.2	67.3	15	A
LYS	CE	254	−25.6	−35.3	67.8	16	A
LYS	NZ	254	−25.2	−33.8	67.6	16	A
LYS	C	254	−24.7	−40.6	66.2	6	A
LYS	O	254	−25.0	−39.9	65.2	10	A
MET	N	255	−25.0	−41.9	66.3	4	A
MET	CA	255	−25.9	−42.6	65.3	2	A
MET	CB	255	−25.1	−43.7	64.6	1	A
MET	CG	255	−24.5	−43.4	63.3	1	A
MET	SD	255	−23.2	−44.6	62.8	3	A
MET	CE	255	−24.2	−45.7	61.9	3	A
MET	C	255	−27.1	−43.1	66.0	1	A
MET	O	255	−27.2	−43.1	67.2	3	A
ASP	N	256	−28.1	−43.5	65.2	1	A
ASP	CA	256	−29.4	−44.0	65.9	1	A
ASP	CB	256	−30.4	−44.0	64.8	1	A
ASP	CG	256	−31.6	−44.8	65.2	1	A
ASP	OD1	256	−31.5	−46.0	65.2	1	A
ASP	OD2	256	−32.7	−44.2	65.5	5	A
ASP	C	256	−29.2	−45.3	66.5	1	A
ASP	O	256	−28.7	−46.2	65.8	1	A
CYS	N	257	−29.5	−45.5	67.8	1	A
CYS	CA	257	−29.4	−46.7	68.5	1	A
CYS	CB	257	−30.5	−46.8	69.6	1	A
CYS	SG	257	−30.3	−48.2	71.0	1	A
CYS	C	257	−29.4	−47.9	67.6	3	A
CYS	O	257	−28.5	−48.8	67.6	6	A
LYS	N	258	−30.5	−48.0	66.8	2	A
LYS	CA	258	−30.7	−49.1	65.8	1	A
LYS	CB	258	−32.0	−48.9	65.1	1	A
LYS	CG	258	−33.2	−48.9	66.0	4	A
LYS	CD	258	−34.5	−49.4	65.2	9	A
LYS	CE	258	−35.8	−49.2	66.0	13	A
LYS	NZ	258	−36.2	−47.8	66.3	13	A
LYS	C	258	−29.6	−49.4	64.7	1	A
LYS	O	258	−29.6	−50.5	64.3	1	A
GLU	N	259	−28.8	−48.4	64.3	1	A
GLU	CA	259	−27.8	−48.7	63.3	1	A
GLU	CB	259	−27.2	−47.4	62.8	1	A
GLU	CG	259	−28.0	−46.7	61.7	1	A
GLU	CD	259	−28.3	−47.6	60.5	7	A
GLU	OE1	259	−27.5	−48.5	60.3	5	A
GLU	OE2	259	−29.3	−47.3	59.8	7	A
GLU	C	259	−26.7	−49.6	63.7	1	A
GLU	O	259	−26.2	−50.4	62.9	1	A
TYR	N	260	−26.3	−49.5	65.0	1	A
TYR	CA	260	−25.2	−50.4	65.5	1	A
TYR	CB	260	−24.8	−49.9	66.9	1	A
TYR	CG	260	−24.4	−48.4	67.0	1	A
TYR	CD1	260	−24.8	−47.8	68.2	1	A
TYR	CE1	260	−24.5	−46.4	68.3	1	A
TYR	CD2	260	−23.7	−47.8	66.1	1	A
TYR	CE2	260	−23.3	−46.4	66.2	1	A
TYR	CZ	260	−23.7	−45.8	67.4	1	A
TYR	OH	260	−23.5	−44.4	67.6	1	A
TYR	C	260	−25.7	−51.8	65.6	1	A
TYR	O	260	−24.8	−52.7	65.6	1	A
ASN	N	261	−27.0	−52.0	65.7	1	A
ASN	CA	261	−27.5	−53.4	65.8	1	A
ASN	CB	261	−28.4	−53.5	67.1	1	A
ASN	CG	261	−27.7	−53.0	68.3	1	A
ASN	OD1	261	−26.6	−53.5	68.7	1	A
ASN	ND2	261	−28.3	−52.0	69.0	1	A
ASN	C	261	−28.4	−53.8	64.6	1	A
ASN	O	261	−29.3	−54.6	64.8	1	A
TYR	N	262	−28.1	−53.2	63.5	7	A
TYR	CA	262	−28.9	−53.4	62.3	7	A
TYR	CB	262	−28.4	−52.5	61.1	6	A
TYR	CG	262	−29.2	−52.8	59.9	8	A
TYR	CD1	262	−30.5	−53.0	59.8	8	A
TYR	CE1	262	−31.2	−53.3	58.7	7	A
TYR	CD2	262	−28.5	−53.0	58.7	12	A
TYR	CE2	262	−29.1	−53.3	57.5	11	A
TYR	CZ	262	−30.5	−53.4	57.5	10	A
TYR	OH	262	−31.1	−53.8	56.4	12	A
TYR	C	262	−28.9	−54.8	61.8	7	A
TYR	O	262	−27.9	−55.3	61.1	4	A
ASP	N	263	−30.0	−55.5	62.0	8	A
ASP	CA	263	−30.2	−56.9	61.7	6	A
ASP	CB	263	−29.2	−57.4	60.6	8	A
ASP	CG	263	−29.6	−58.8	60.1	15	A
ASP	OD1	263	−30.8	−59.2	60.2	17	A
ASP	OD2	263	−28.7	−59.6	59.7	19	A
ASP	C	263	−29.9	−57.6	63.1	5	A
ASP	O	263	−30.8	−58.0	63.8	5	A
LYS	N	264	−28.6	−57.6	63.4	5	A
LYS	CA	264	−28.3	−58.3	64.7	4	A
LYS	CB	264	−28.4	−59.8	64.6	2	A
LYS	CG	264	−27.5	−60.4	63.5	1	A
LYS	CD	264	−27.6	−61.9	63.6	1	A
LYS	CE	264	−26.7	−62.5	62.4	4	A
LYS	NZ	264	−27.4	−62.3	61.1	7	A
LYS	C	264	−26.9	−57.9	65.2	1	A
LYS	O	264	−26.0	−57.4	64.4	1	A
SER	N	265	−26.6	−58.2	66.5	1	A
SER	CA	265	−25.4	−57.9	67.1	1	A
SER	CB	265	−25.4	−56.7	68.0	1	A
SER	OG	265	−25.4	−55.5	67.3	6	A
SER	C	265	−25.1	−59.2	67.9	1	A
SER	O	265	−25.9	−59.6	68.7	1	A
ILE	N	266	−23.9	−59.8	67.6	1	A
ILE	CA	266	−23.6	−61.1	68.2	1	A
ILE	CB	266	−23.8	−62.2	67.2	1	A
ILE	CG2	266	−25.2	−62.2	66.7	1	A
ILE	CG1	266	−22.9	−62.0	66.0	2	A
ILE	CD1	266	−23.0	−63.1	64.9	1	A
ILE	C	266	−22.1	−61.1	68.7	1	A
ILE	O	266	−21.3	−60.4	68.3	1	A
VAL	N	267	−21.9	−62.1	69.7	2	A
VAL	CA	267	−20.5	−62.3	70.2	1	A
VAL	CB	267	−20.5	−62.3	71.7	1	A
VAL	CG1	267	−19.1	−62.5	72.2	4	A
VAL	CG2	267	−21.1	−61.1	72.3	2	A
VAL	C	267	−20.1	−63.6	69.6	2	A
VAL	O	267	−20.5	−64.6	70.1	4	A
ASP	N	268	−19.3	−63.5	68.5	2	A
ASP	CA	268	−18.9	−64.7	67.8	1	A
ASP	CB	268	−19.4	−64.6	66.3	2	A
ASP	CG	268	−18.8	−65.6	65.4	4	A
ASP	OD1	268	−18.9	−66.8	65.5	4	A
ASP	OD2	268	−18.1	−65.1	64.4	4	A
ASP	C	268	−17.4	−64.9	67.8	1	A
ASP	O	268	−16.7	−64.1	67.2	1	A
SER	N	269	−16.9	−66.0	68.4	1	A
SER	CA	269	−15.5	−66.2	68.5	1	A
SER	CB	269	−15.1	−67.1	69.7	1	A
SER	OG	269	−15.6	−68.4	69.5	1	A
SER	C	269	−14.9	−66.9	67.3	1	A
SER	O	269	−13.7	−67.1	67.1	1	A
GLY	N	270	−15.8	−67.1	66.3	1	A
GLY	CA	270	−15.4	−67.7	65.1	3	A
GLY	C	270	−14.8	−66.8	64.1	3	A
GLY	O	270	−14.1	−67.1	63.2	3	A
THR	N	271	−15.1	−65.5	64.2	4	A
THR	CA	271	−14.6	−64.4	63.3	7	A
THR	CB	271	−15.8	−63.4	62.9	11	A
THR	OG1	271	−17.0	−64.2	62.6	14	A
THR	CG2	271	−15.4	−62.7	61.7	17	A
THR	C	271	−13.5	−63.7	64.0	6	A
THR	O	271	−13.5	−63.4	65.2	5	A
THR	N	272	−12.5	−63.3	63.1	3	A
THR	CA	272	−11.4	−62.5	63.6	1	A
THR	CB	272	−10.2	−62.6	62.6	1	A
THR	OG1	272	−9.9	−63.9	62.3	1	A
THR	CG2	272	−9.0	−61.9	63.1	1	A
THR	C	272	−11.7	−61.1	63.9	1	A
THR	O	272	−11.6	−60.7	65.1	2	A
ASN	N	273	−11.9	−60.3	62.9	1	A
ASN	CA	273	−12.2	−58.9	63.0	1	A
ASN	CB	273	−12.4	−58.3	61.6	1	A
ASN	CG	273	−11.1	−58.5	60.8	2	A
ASN	OD1	273	−10.2	−59.2	61.1	1	A
ASN	ND2	273	−11.1	−57.8	59.6	1	A
ASN	C	273	−13.5	−58.5	63.7	1	A
ASN	O	273	−14.3	−59.3	64.1	6	A
LEU	N	274	−13.6	−57.2	64.0	1	A
LEU	CA	274	−14.8	−56.6	64.7	1	A
LEU	CB	274	−14.5	−55.4	65.5	1	A
LEU	CG	274	−15.6	−54.6	66.2	1	A
LEU	CD1	274	−15.2	−53.2	66.3	1	A
LEU	CD2	274	−16.9	−54.8	65.6	1	A
LEU	C	274	−15.5	−56.2	63.4	1	A
LEU	O	274	−15.0	−55.4	62.6	4	A
ARG	N	275	−16.7	−56.7	63.2	1	A
ARG	CA	275	−17.5	−56.4	62.0	1	A
ARG	CB	275	−18.0	−57.6	61.3	1	A
ARG	CG	275	−16.9	−58.4	60.5	1	A
ARG	CD	275	−17.3	−59.8	60.2	8	A
ARG	NE	275	−18.5	−60.0	59.4	16	A
ARG	CZ	275	−18.6	−59.6	58.2	17	A
ARG	NH1	275	−19.8	−59.8	57.5	19	A
ARG	NH2	275	−17.6	−59.1	57.5	20	A
ARG	C	275	−18.6	−55.4	62.3	1	A
ARG	O	275	−19.4	−55.6	63.2	2	A
LEU	N	276	−18.7	−54.3	61.6	1	A
LEU	CA	276	−19.7	−53.3	61.8	1	A
LEU	CB	276	−19.0	−52.0	62.1	1	A
LEU	CG	276	−18.1	−51.9	63.4	1	A
LEU	CD1	276	−17.6	−50.5	63.5	1	A
LEU	CD2	276	−18.9	−52.2	64.6	1	A
LEU	C	276	−20.5	−53.1	60.6	1	A
LEU	O	276	−20.1	−53.2	59.5	3	A
PRO	N	277	−21.8	−52.8	60.8	3	A
PRO	CD	277	−22.6	−53.0	62.0	4	A
PRO	CA	277	−22.7	−52.6	59.6	6	A
PRO	CB	277	−24.0	−52.2	60.3	5	A
PRO	CG	277	−24.0	−53.1	61.5	1	A
PRO	C	277	−22.2	−51.5	58.7	8	A
PRO	O	277	−21.6	−50.6	59.1	10	A
LYS	N	278	−22.4	−51.7	57.4	11	A
LYS	CA	278	−21.9	−50.8	56.4	13	A
LYS	CB	278	−22.5	−51.2	55.0	18	A
LYS	CG	278	−21.9	−50.5	53.9	22	A
LYS	CD	278	−20.4	−50.6	53.9	23	A
LYS	CE	278	−19.7	−49.7	52.9	26	A
LYS	NZ	278	−18.2	−49.6	53.0	21	A
LYS	C	278	−22.1	−49.4	56.7	10	A
LYS	O	278	−21.4	−48.5	56.1	13	A
LYS	N	279	−23.0	−49.0	57.5	11	A
LYS	CA	279	−23.2	−47.6	57.8	12	A
LYS	CB	279	−24.7	−47.4	58.3	18	A
LYS	CG	279	−25.7	−47.7	57.2	25	A
LYS	CD	279	−26.6	−48.9	57.6	34	A
LYS	CE	279	−27.9	−49.0	56.7	38	A
LYS	NZ	279	−28.9	−50.0	57.3	38	A
LYS	C	279	−22.3	−47.2	59.0	8	A
LYS	O	279	−21.7	−46.1	59.0	4	A
VAL	N	280	−22.2	−48.1	60.0	7	A
VAL	CA	280	−21.4	−47.9	61.2	3	A
VAL	CB	280	−21.8	−48.9	62.2	1	A
VAL	CG1	280	−21.0	−48.6	63.5	2	A
VAL	CG2	280	−23.2	−48.7	62.6	1	A
VAL	C	280	−19.9	−48.0	60.9	3	A
VAL	O	280	−19.1	−47.4	61.6	3	A
PHE	N	281	−19.5	−48.7	59.9	2	A
PHE	CA	281	−18.1	−48.9	59.5	1	A
PHE	CB	281	−17.9	−50.0	58.6	1	A
PHE	CG	281	−16.5	−50.1	58.0	1	A
PHE	CD1	281	−15.5	−50.7	58.8	5	A
PHE	CD2	281	−16.2	−49.7	56.8	1	A
PHE	CE1	281	−14.3	−50.9	58.3	3	A
PHE	CE2	281	−14.9	−49.8	56.3	4	A
PHE	CZ	281	−13.9	−50.4	57.1	5	A
PHE	C	281	−17.6	−47.6	58.9	1	A
PHE	O	281	−16.4	−47.2	59.2	1	A
GLU	N	282	−18.4	−47.0	58.1	1	A
GLU	CA	282	−18.0	−45.7	57.4	5	A
GLU	CB	282	−19.1	−45.3	56.4	9	A
GLU	CG	282	−19.5	−46.4	55.4	15	A
GLU	CD	282	−18.8	−46.2	54.1	19	A
GLU	OE1	282	−19.3	−45.3	53.3	23	A
GLU	OE2	282	−17.9	−47.0	53.7	21	A
GLU	C	282	−17.7	−44.6	58.4	7	A
GLU	O	282	−16.8	−43.8	58.2	11	A
ALA	N	283	−18.6	−44.5	59.4	8	A
ALA	CA	283	−18.5	−43.5	60.4	6	A
ALA	CB	283	−19.9	−43.3	61.1	7	A
ALA	C	283	−17.4	−43.7	61.4	3	A
ALA	O	283	−16.8	−42.8	61.9	7	A
ALA	N	284	−17.2	−45.0	61.8	1	A
ALA	CA	284	−16.2	−45.3	62.7	1	A
ALA	CB	284	−16.4	−46.7	63.2	1	A
ALA	C	284	−14.8	−45.1	62.1	1	A
ALA	O	284	−13.9	−44.5	62.7	1	A
VAL	N	285	−14.6	−45.6	60.9	1	A
VAL	CA	285	−13.4	−45.5	60.3	1	A
VAL	CB	285	−13.3	−46.2	58.9	1	A
VAL	CG1	285	−12.1	−45.8	58.1	1	A
VAL	CG2	285	−13.4	−47.7	59.1	2	A
VAL	C	285	−13.1	−44.0	60.0	1	A
VAL	O	285	−12.0	−43.5	60.1	1	A
LYS	N	286	−14.2	−43.3	59.7	2	A
LYS	CA	286	−14.0	−41.9	59.4	3	A
LYS	CB	286	−15.4	−41.3	59.1	3	A
LYS	CG	286	−15.4	−39.8	58.5	15	A
LYS	CD	286	−14.2	−39.7	57.5	26	A
LYS	CE	286	−14.2	−40.7	56.3	27	A
LYS	NZ	286	−12.9	−40.8	55.6	21	A
LYS	C	286	−13.4	−41.2	60.6	1	A
LYS	O	286	−12.5	−40.3	60.5	1	A
SER	N	287	−13.9	−41.6	61.8	1	A
SER	CA	287	−13.4	−41.0	63.0	1	A
SER	CB	287	−14.4	−41.3	64.1	1	A
SER	OG	287	−13.9	−40.9	65.4	1	A
SER	C	287	−12.0	−41.5	63.4	1	A
SER	O	287	−11.2	−40.8	63.9	1	A
ILE	N	288	−11.8	−42.8	63.2	1	A
ILE	CA	288	−10.5	−43.4	63.5	1	A
ILE	CB	288	−10.6	−45.0	63.4	1	A
ILE	CG2	288	−9.2	−45.6	63.7	1	A
ILE	CG1	288	−11.7	−45.5	64.3	1	A
ILE	CD1	288	−11.9	−47.0	64.1	1	A
ILE	C	288	−9.5	−42.8	62.7	1	A
ILE	O	288	−8.4	−42.5	63.1	1	A
LYS	N	289	−9.8	−42.7	61.4	3	A
LYS	CA	289	−8.9	−42.2	60.4	3	A
LYS	CB	289	−9.6	−42.1	59.0	1	A
LYS	CG	289	−8.6	−42.0	57.8	5	A
LYS	CD	289	−9.3	−42.2	56.5	1	A
LYS	CE	289	−10.0	−43.5	56.3	2	A
LYS	NZ	289	−10.6	−43.8	55.0	2	A
LYS	C	289	−8.5	−40.8	60.9	4	A
LYS	O	289	−7.3	−40.4	60.9	7	A
ALA	N	290	−9.5	−40.0	61.3	5	A
ALA	CA	290	−9.3	−38.7	61.8	2	A
ALA	CB	290	−10.6	−38.0	62.1	1	A
ALA	C	290	−8.4	−38.6	63.1	3	A
ALA	O	290	−7.4	−37.8	63.1	4	A
ALA	N	291	−8.7	−39.4	64.0	2	A
ALA	CA	291	−8.0	−39.5	65.3	1	A
ALA	CB	291	−8.6	−40.4	66.3	1	A
ALA	C	291	−6.5	−39.8	65.1	1	A
ALA	O	291	−5.7	−39.7	66.0	1	A
SER	N	292	−6.1	−40.3	63.9	1	A
SER	CA	292	−4.8	−40.8	63.7	1	A
SER	CB	292	−4.7	−42.2	63.5	1	A
SER	OG	292	−5.9	−42.6	62.7	1	A
SER	C	292	−4.1	−40.0	62.5	4	A
SER	O	292	−3.4	−40.6	61.8	7	A
SER	N	293	−4.4	−38.7	62.4	5	A
SER	CA	293	−3.9	−37.9	61.3	6	A
SER	CB	293	−4.6	−36.6	61.3	6	A
SER	OG	293	−6.0	−36.7	61.3	10	A
SER	C	293	−2.4	−37.7	61.3	7	A
SER	O	293	−1.8	−37.6	60.2	7	A
THR	N	294	−1.8	−37.6	62.5	8	A
THR	CA	294	−0.4	−37.4	62.6	7	A
THR	CB	294	0.1	−37.9	64.0	9	A
THR	OG1	294	−0.8	−37.5	65.0	10	A
THR	CG2	294	1.5	−37.2	64.3	8	A
THR	C	294	0.3	−38.2	61.5	6	A
THR	O	294	1.2	−37.7	60.8	9	A
GLU	N	295	−0.1	−39.5	61.4	6	A
GLU	CA	295	0.5	−40.3	60.3	7	A
GLU	CB	295	1.0	−41.6	61.0	9	A
GLU	CG	295	2.3	−41.5	61.8	9	A
GLU	CD	295	2.8	−42.7	62.4	6	A
GLU	OE1	295	2.8	−43.8	61.8	8	A
GLU	OE2	295	3.1	−42.7	63.6	12	A
GLU	C	295	−0.5	−40.6	59.3	9	A
GLU	O	295	−1.7	−40.4	59.5	11	A
LYS	N	296	0.0	−41.1	58.1	12	A
LYS	CA	296	−0.9	−41.4	57.0	11	A
LYS	CB	296	−0.7	−40.4	55.8	15	A
LYS	CG	296	−1.5	−39.1	55.9	19	A
LYS	CD	296	−3.0	−39.3	55.4	22	A
LYS	CE	296	−3.7	−38.0	55.2	21	A
LYS	NZ	296	−3.9	−37.2	56.4	16	A
LYS	C	296	−0.7	−42.8	56.5	10	A
LYS	O	296	0.5	−43.2	56.6	11	A
PHE	N	297	−1.7	−43.5	56.1	8	A
PHE	CA	297	−1.5	−44.9	55.7	10	A
PHE	CB	297	−2.2	−45.9	56.7	10	A
PHE	CG	297	−2.2	−45.4	58.1	10	A
PHE	CD1	297	−3.1	−44.4	58.5	14	A
PHE	CD2	297	−1.4	−45.9	59.1	10	A
PHE	CE1	297	−3.2	−43.9	59.8	12	A
PHE	CE2	297	−1.5	−45.5	60.4	13	A
PHE	CZ	297	−2.4	−44.5	60.8	10	A
PHE	C	297	−2.2	−45.0	54.3	12	A
PHE	O	297	−3.1	−44.3	54.0	13	A
PRO	N	298	−1.7	−46.0	53.5	12	A
PRO	CD	298	−0.6	−46.9	53.7	8	A
PRO	CA	298	−2.3	−46.2	52.2	15	A
PRO	CB	298	−1.5	−47.4	51.6	11	A
PRO	CG	298	−0.9	−48.1	52.8	11	A
PRO	C	298	−3.8	−46.5	52.3	19	A
PRO	O	298	−4.2	−47.2	53.3	18	A
ASP	N	299	−4.6	−46.1	51.3	25	A
ASP	CA	299	−6.1	−46.2	51.3	28	A
ASP	CB	299	−6.6	−45.7	50.0	31	A
ASP	CG	299	−8.1	−45.4	50.1	35	A
ASP	OD1	299	−8.5	−44.5	50.9	36	A
ASP	OD2	299	−8.9	−46.1	49.4	37	A
ASP	C	299	−6.5	−47.7	51.5	26	A
ASP	O	299	−7.6	−47.9	52.1	20	A
GLY	N	300	−5.7	−48.7	51.1	21	A
GLY	CA	300	−6.1	−50.0	51.3	16	A
GLY	C	300	−6.0	−50.5	52.7	13	A
GLY	O	300	−6.6	−51.5	53.1	12	A
PHE	N	301	−5.2	−49.8	53.5	10	A
PHE	CA	301	−5.0	−50.1	54.9	6	A
PHE	CB	301	−4.1	−49.0	55.6	1	A
PHE	CG	301	−4.1	−49.2	57.1	1	A
PHE	CD1	301	−3.6	−50.4	57.6	1	A
PHE	CD2	301	−4.5	−48.2	57.9	1	A
PHE	CE1	301	−3.6	−50.5	59.0	1	A
PHE	CE2	301	−4.5	−48.3	59.3	1	A
PHE	CZ	301	−4.0	−49.5	59.9	1	A
PHE	C	301	−6.3	−50.2	55.6	6	A
PHE	O	301	−6.6	−51.2	56.1	9	A
TRP	N	302	−7.1	−49.1	55.5	3	A
TRP	CA	302	−8.4	−49.0	56.2	3	A
TRP	CB	302	−8.9	−47.6	56.2	4	A
TRP	CG	302	−8.1	−46.6	56.9	1	A
TRP	CD2	302	−7.9	−46.6	58.3	1	A
TRP	CE2	302	−7.0	−45.5	58.6	1	A
TRP	CE3	302	−8.3	−47.3	59.4	3	A
TRP	CD1	302	−7.4	−45.6	56.4	1	A
TRP	NE1	302	−6.8	−44.9	57.4	1	A
TRP	CZ2	302	−6.6	−45.1	59.9	1	A
TRP	CZ3	302	−7.9	−47.0	60.7	1	A
TRP	CH2	302	−7.1	−45.9	60.9	1	A
TRP	C	302	−9.4	−50.0	55.6	5	A
TRP	O	302	−10.5	−50.1	56.1	7	A
LEU	N	303	−9.0	−50.8	54.6	9	A
LEU	CA	303	−9.9	−51.8	54.1	10	A
LEU	CB	303	−10.1	−51.6	52.6	9	A
LEU	CG	303	−10.7	−50.3	52.1	11	A
LEU	CD1	303	−11.0	−50.4	50.6	15	A
LEU	CD2	303	−12.0	−50.0	52.9	11	A
LEU	C	303	−9.4	−53.3	54.2	9	A
LEU	O	303	−9.9	−54.2	53.6	10	A
GLY	N	304	−8.4	−53.5	55.1	10	A
GLY	CA	304	−7.9	−54.8	55.3	12	A
GLY	C	304	−7.1	−55.4	54.2	13	A
GLY	O	304	−6.8	−56.6	54.2	13	A
GLU	N	305	−6.9	−54.6	53.1	14	A
GLU	CA	305	−6.2	−55.0	51.9	13	A
GLU	CB	305	−6.8	−54.3	50.7	16	A
GLU	CG	305	−8.1	−54.9	50.2	19	A
GLU	CD	305	−8.8	−54.0	49.2	23	A
GLU	OE1	305	−9.8	−54.4	48.5	29	A
GLU	OE2	305	−8.3	−52.8	49.0	23	A
GLU	C	305	−4.7	−54.9	52.0	11	A
GLU	O	305	−4.0	−55.5	51.2	14	A
GLN	N	306	−4.2	−54.1	52.9	8	A
GLN	CA	306	−2.8	−53.9	53.0	10	A
GLN	CB	306	−2.3	−53.0	51.9	11	A
GLN	CG	306	−2.9	−51.6	51.9	20	A
GLN	CD	306	−2.7	−50.9	50.5	27	A
GLN	OE1	306	−3.1	−49.7	50.4	22	A
GLN	NE2	306	−2.2	−51.6	49.5	27	A
GLN	C	306	−2.3	−53.5	54.3	8	A
GLN	O	306	−2.8	−52.5	54.9	9	A
LEU	N	307	−1.3	−54.2	54.9	6	A
LEU	CA	307	−0.8	−53.9	56.2	3	A
LEU	CB	307	−0.2	−55.1	56.8	1	A
LEU	CG	307	0.6	−56.1	55.9	2	A
LEU	CD1	307	1.5	−55.3	54.9	9	A
LEU	CD2	307	1.4	−57.0	56.7	2	A
LEU	C	307	0.1	−52.7	56.4	3	A
LEU	O	307	0.8	−52.3	55.5	3	A
VAL	N	308	0.1	−52.1	57.6	3	A
VAL	CA	308	1.0	−51.0	58.0	3	A
VAL	CB	308	0.1	−50.0	58.8	1	A
VAL	CG1	308	1.1	−49.1	59.5	2	A
VAL	CG2	308	−0.7	−49.2	57.9	8	A
VAL	C	308	2.1	−51.5	58.8	3	A
VAL	O	308	1.9	−52.1	59.8	3	A
CYS	N	309	3.3	−51.1	58.5	3	A
CYS	CA	309	4.5	−51.5	59.3	3	A
CYS	C	309	5.2	−50.4	60.0	3	A
CYS	O	309	5.2	−49.2	59.5	2	A
CYS	CB	309	5.5	−52.3	58.5	5	A
CYS	SG	309	4.9	−53.7	57.6	4	A
TRP	N	310	5.9	−50.6	61.1	2	A
TRP	CA	310	6.7	−49.7	61.8	1	A
TRP	CB	310	5.9	−49.2	63.1	1	A
TRP	CG	310	4.9	−48.1	62.8	1	A
TRP	CD2	310	3.5	−48.2	62.8	1	A
TRP	CE2	310	3.0	−46.9	62.6	1	A
TRP	CE3	310	2.6	−49.3	63.0	1	A
TRP	CD1	310	5.2	−46.8	62.6	1	A
TRP	NE1	310	4.1	−46.1	62.4	1	A
TRP	CZ2	310	1.6	−46.7	62.5	1	A
TRP	CZ3	310	1.3	−49.0	63.0	1	A
TRP	CH2	310	0.8	−47.7	62.7	1	A
TRP	C	310	7.9	−50.4	62.2	3	A
TRP	O	310	7.9	−51.7	62.2	4	A
GLN	N	311	8.9	−49.7	62.7	3	A
GLN	CA	311	10.2	−50.3	63.1	6	A
GLN	CB	311	11.2	−49.2	63.3	13	A
GLN	CG	311	11.1	−48.1	62.2	26	A
GLN	CD	311	9.7	−47.4	62.1	29	A
GLN	OE1	311	9.3	−46.7	62.9	31	A
GLN	NE2	311	9.0	−47.7	61.0	29	A
GLN	C	311	9.9	−51.0	64.5	3	A
GLN	O	311	9.4	−50.4	65.4	6	A
ALA	N	312	10.3	−52.2	64.5	1	A
ALA	CA	312	10.1	−53.0	65.8	4	A
ALA	CB	312	11.2	−54.1	65.8	7	A
ALA	C	312	10.1	−52.2	67.0	2	A
ALA	O	312	11.0	−51.4	67.3	3	A
GLY	N	313	9.2	−52.5	67.9	5	A
GLY	CA	313	9.1	−51.8	69.2	5	A
GLY	C	313	8.9	−50.3	69.2	6	A
GLY	O	313	9.4	−49.6	70.0	4	A
THR	N	314	8.1	−49.8	68.2	7	A
THR	CA	314	7.9	−48.4	68.1	5	A
THR	CB	314	8.9	−47.7	67.1	2	A
THR	OG1	314	8.4	−47.8	65.7	1	A
THR	CG2	314	10.3	−48.3	67.2	3	A
THR	C	314	6.5	−48.0	67.6	3	A
THR	O	314	6.2	−46.9	67.3	3	A
THR	N	315	5.6	−49.0	67.6	2	A
THR	CA	315	4.2	−48.8	67.1	1	A
THR	CB	315	3.4	−50.0	67.2	1	A
THR	OG1	315	4.1	−51.1	66.6	4	A
THR	CG2	315	2.1	−49.8	66.4	2	A
THR	C	315	3.6	−47.7	68.0	1	A
THR	O	315	3.4	−48.0	69.2	1	A
PRO	N	316	3.2	−46.6	67.4	1	A
PRO	CD	316	3.3	−46.4	66.0	2	A
PRO	CA	316	2.6	−45.4	68.1	1	A
PRO	CB	316	2.7	−44.3	67.0	1	A
PRO	CG	316	2.4	−45.1	65.8	2	A
PRO	C	316	1.1	−45.7	68.5	3	A
PRO	O	316	0.2	−45.0	68.0	4	A
TRP	N	317	0.9	−46.6	69.4	1	A
TRP	CA	317	−0.5	−46.9	69.8	1	A
TRP	CB	317	−0.5	−47.9	71.0	1	A
TRP	CG	317	0.3	−49.1	70.7	1	A
TRP	CD2	317	0.0	−50.1	69.8	1	A
TRP	CE2	317	1.1	−51.0	69.8	1	A
TRP	CE3	317	−1.1	−50.4	69.0	1	A
TRP	CD1	317	1.6	−49.4	71.2	1	A
TRP	NE1	317	2.0	−50.5	70.7	1	A
TRP	CZ2	317	1.1	−52.2	69.1	1	A
TRP	CZ3	317	−1.1	−51.6	68.3	1	A
TRP	CH2	317	0.0	−52.4	68.3	1	A
TRP	C	317	−1.1	−45.6	70.3	1	A
TRP	O	317	−2.3	−45.4	70.1	1	A
ASN	N	318	−0.3	−44.7	70.9	4	A
ASN	CA	318	−0.9	−43.5	71.4	5	A
ASN	CB	318	0.3	−42.6	72.1	9	A
ASN	CG	318	0.8	−41.6	71.2	12	A
ASN	OD1	318	0.1	−40.6	70.8	18	A
ASN	ND2	318	2.1	−41.7	70.8	18	A
ASN	C	318	−1.7	−42.7	70.4	4	A
ASN	O	318	−2.7	−42.2	70.7	6	A
ILE	N	319	−1.2	−42.6	69.1	2	A
ILE	CA	319	−2.0	−41.8	68.2	1	A
ILE	CB	319	−1.3	−41.7	66.8	1	A
ILE	CG2	319	0.1	−41.2	67.1	1	A
ILE	CG1	319	−1.2	−43.0	66.1	7	A
ILE	CD1	319	−0.6	−42.9	64.7	11	A
ILE	C	319	−3.4	−42.5	67.9	1	A
ILE	O	319	−4.4	−41.7	67.8	1	A
PHE	N	320	−3.5	−43.8	67.8	1	A
PHE	CA	320	−4.7	−44.5	67.5	1	A
PHE	CB	320	−4.4	−46.0	67.2	1	A
PHE	CG	320	−3.8	−46.2	65.9	1	A
PHE	CD1	320	−4.6	−46.3	64.8	1	A
PHE	CD2	320	−2.4	−46.3	65.8	1	A
PHE	CE1	320	−4.0	−46.5	63.5	1	A
PHE	CE2	320	−1.9	−46.5	64.5	1	A
PHE	CZ	320	−2.7	−46.6	63.4	1	A
PHE	C	320	−5.7	−44.4	68.8	1	A
PHE	O	320	−5.2	−44.5	69.9	1	A
PRO	N	321	−7.0	−44.2	68.5	1	A
PRO	CD	321	−7.6	−44.1	67.2	1	A
PRO	CA	321	−8.0	−44.0	69.5	1	A
PRO	CB	321	−9.0	−43.2	68.8	1	A
PRO	CG	321	−9.1	−43.9	67.5	1	A
PRO	C	321	−8.6	−45.3	70.1	1	A
PRO	O	321	−8.5	−46.3	69.4	1	A
VAL	N	322	−9.1	−45.3	71.3	1	A
VAL	CA	322	−9.7	−46.5	71.8	1	A
VAL	CB	322	−9.8	−46.5	73.4	1	A
VAL	CG1	322	−8.4	−46.4	73.9	2	A
VAL	CG2	322	−10.6	−45.3	73.9	3	A
VAL	C	322	−11.2	−46.5	71.3	1	A
VAL	O	322	−11.7	−45.4	71.1	1	A
ILE	N	323	−11.7	−47.6	71.2	1	A
ILE	CA	323	−13.1	−47.8	70.7	1	A
ILE	CB	323	−13.2	−48.8	69.5	1	A
ILE	CG2	323	−14.6	−48.9	69.0	1	A
ILE	CG1	323	−12.3	−48.3	68.4	1	A
ILE	CD1	323	−12.2	−49.3	67.3	1	A
ILE	C	323	−13.9	−48.3	71.9	1	A
ILE	O	323	−13.6	−49.3	72.5	3	A
SER	N	324	−15.0	−47.6	72.2	1	A
SER	CA	324	−15.9	−48.1	73.2	1	A
SER	CB	324	−16.1	−47.0	74.3	1	A
SER	OG	324	−14.9	−46.7	75.0	1	A
SER	C	324	−17.2	−48.5	72.7	1	A
SER	O	324	−17.8	−47.8	71.9	1	A
LEU	N	325	−17.7	−49.6	73.2	1	A
LEU	CA	325	−19.0	−50.1	72.8	1	A
LEU	CB	325	−18.9	−51.5	72.2	1	A
LEU	CG	325	−18.0	−51.6	70.9	1	A
LEU	CD1	325	−18.1	−53.1	70.5	1	A
LEU	CD2	325	−18.5	−50.7	69.9	1	A
LEU	C	325	−19.9	−50.2	74.1	1	A
LEU	O	325	−19.4	−50.8	75.0	1	A
TYR	N	326	−21.0	−49.6	74.1	1	A
TYR	CA	326	−21.9	−49.6	75.2	1	A
TYR	CB	326	−22.7	−48.3	75.4	1	A
TYR	CG	326	−21.8	−47.2	76.0	1	A
TYR	CD1	326	−20.6	−46.9	75.4	3	A
TYR	CE1	326	−19.8	−45.8	75.9	4	A
TYR	CD2	326	−22.2	−46.4	77.0	4	A
TYR	CE2	326	−21.5	−45.3	77.5	2	A
TYR	CZ	326	−20.3	−45.0	76.9	3	A
TYR	OH	326	−19.5	−43.9	77.4	5	A
TYR	C	326	−23.0	−50.7	75.0	1	A
TYR	O	326	−23.7	−50.7	74.0	1	A
LEU	N	327	−23.0	−51.7	75.9	1	A
LEU	CA	327	−24.0	−52.8	75.9	1	A
LEU	CB	327	−23.3	−54.1	76.2	1	A
LEU	CG	327	−22.0	−54.3	75.4	1	A
LEU	CD1	327	−21.2	−55.4	76.0	1	A
LEU	CD2	327	−22.3	−54.6	74.0	2	A
LEU	C	327	−25.1	−52.6	76.8	1	A
LEU	O	327	−24.9	−52.1	78.0	1	A
MET	N	328	−26.4	−52.9	76.4	1	A
MET	CA	328	−27.5	−52.8	77.3	2	A
MET	CB	328	−28.8	−53.3	76.5	3	A
MET	CG	328	−30.0	−53.5	77.3	1	A
MET	SD	328	−31.2	−54.4	76.4	1	A
MET	CE	328	−32.5	−53.2	76.1	3	A
MET	C	328	−27.3	−53.5	78.6	3	A
MET	O	328	−27.1	−54.7	78.6	4	A
GLY	N	329	−27.5	−52.7	79.7	4	A
GLY	CA	329	−27.3	−53.3	81.0	4	A
GLY	C	329	−28.4	−54.3	81.4	5	A
GLY	O	329	−29.4	−54.4	80.7	2	A
GLU	N	330	−28.2	−54.9	82.5	6	A
GLU	CA	330	−29.2	−55.9	83.1	7	A
GLU	CB	330	−28.5	−57.0	83.8	11	A
GLU	CG	330	−28.3	−58.3	83.0	20	A
GLU	CD	330	−29.7	−58.9	82.7	26	A
GLU	OE1	330	−29.6	−60.0	82.1	30	A
GLU	OE2	330	−30.7	−58.3	83.0	31	A
GLU	C	330	−30.2	−55.2	83.9	5	A
GLU	O	330	−31.2	−55.9	84.4	4	A
VAL	N	331	−30.1	−53.9	84.2	6	A
VAL	CA	331	−31.1	−53.2	85.0	5	A
VAL	CB	331	−30.4	−52.3	86.0	1	A
VAL	CG1	331	−31.3	−52.0	87.1	1	A
VAL	CG2	331	−29.1	−53.0	86.5	2	A
VAL	C	331	−31.9	−52.3	84.1	7	A
VAL	O	331	−31.5	−52.1	82.9	5	A
THR	N	332	−33.0	−51.8	84.5	11	A
THR	CA	332	−33.8	−50.9	83.7	13	A
THR	CB	332	−35.2	−50.8	84.2	16	A
THR	OG1	332	−35.7	−52.2	84.5	21	A
THR	CG2	332	−36.1	−50.2	83.1	15	A
THR	C	332	−33.2	−49.5	83.6	12	A
THR	O	332	−32.9	−48.9	84.6	14	A
ASN	N	333	−33.0	−49.0	82.4	8	A
ASN	CA	333	−32.4	−47.7	82.2	6	A
ASN	CB	333	−33.2	−46.6	83.0	7	A
ASN	CG	333	−34.5	−46.3	82.4	9	A
ASN	OD1	333	−34.8	−46.5	81.2	12	A
ASN	ND2	333	−35.4	−45.9	83.2	10	A
ASN	C	333	−30.9	−47.7	82.6	3	A
ASN	O	333	−30.5	−46.7	83.2	7	A
GLN	N	334	−30.2	−48.7	82.3	7	A
GLN	CA	334	−28.8	−48.8	82.7	8	A
GLN	CB	334	−28.7	−49.3	84.2	13	A
GLN	CG	334	−27.3	−49.9	84.6	17	A
GLN	CD	334	−27.1	−49.8	86.1	24	A
GLN	OE1	334	−26.3	−50.6	86.6	23	A
GLN	NE2	334	−27.9	−49.0	86.8	21	A
GLN	C	334	−27.9	−49.7	81.8	8	A
GLN	O	334	−28.4	−50.7	81.4	8	A
SER	N	335	−26.7	−49.2	81.5	7	A
SER	CA	335	−25.8	−49.9	80.6	1	A
SER	CB	335	−25.9	−49.3	79.2	1	A
SER	OG	335	−25.5	−48.0	79.2	1	A
SER	C	335	−24.4	−49.7	81.1	1	A
SER	O	335	−24.2	−49.0	82.1	1	A
PHE	N	336	−23.5	−50.4	80.5	1	A
PHE	CA	336	−22.1	−50.4	80.9	1	A
PHE	CB	336	−21.7	−51.6	81.7	1	A
PHE	CG	336	−21.8	−52.9	81.0	1	A
PHE	CD1	336	−20.7	−53.3	80.2	1	A
PHE	CD2	336	−22.9	−53.7	81.1	1	A
PHE	CE1	336	−20.8	−54.5	79.5	1	A
PHE	CE2	336	−22.9	−54.9	80.4	1	A
PHE	CZ	336	−21.9	−55.3	79.6	1	A
PHE	C	336	−21.4	−50.4	79.5	1	A
PHE	O	336	−22.0	−50.7	78.5	1	A
ARG	N	337	−20.1	−50.1	79.6	1	A
ARG	CA	337	−19.3	−50.0	78.3	1	A
ARG	CB	337	−19.0	−48.6	78.0	1	A
ARG	CG	337	−17.9	−48.0	78.9	3	A
ARG	CD	337	−17.7	−46.6	78.7	2	A
ARG	NE	337	−16.6	−46.1	79.4	1	A
ARG	CZ	337	−16.4	−44.8	79.9	1	A
ARG	NH1	337	−17.4	−44.0	79.7	3	A
ARG	NH2	337	−15.4	−44.5	80.6	6	A
ARG	C	337	−18.1	−50.8	78.5	1	A
ARG	O	337	−17.5	−51.0	79.6	1	A
ILE	N	338	−17.6	−51.3	77.3	1	A
ILE	CA	338	−16.3	−52.0	77.3	2	A
ILE	CB	338	−16.6	−53.5	76.8	1	A
ILE	CG2	338	−17.3	−54.2	77.8	1	A
ILE	CG1	338	−17.3	−53.5	75.5	1	A
ILE	CD1	338	−17.5	−54.9	74.9	1	A
ILE	C	338	−15.4	−51.3	76.3	3	A
ILE	O	338	−15.9	−50.8	75.3	4	A
THR	N	339	−14.2	−51.1	76.7	2	A
THR	CA	339	−13.3	−50.3	75.8	1	A
THR	CB	339	−12.7	−49.1	76.5	1	A
THR	OG1	339	−13.8	−48.4	77.1	1	A
THR	CG2	339	−12.0	−48.2	75.6	1	A
THR	C	339	−12.1	−51.2	75.4	1	A
THR	O	339	−11.5	−51.9	76.1	1	A
ILE	N	340	−11.8	−51.2	74.1	1	A
ILE	CA	340	−10.7	−51.9	73.5	1	A
ILE	CB	340	−11.2	−52.8	72.3	1	A
ILE	CG2	340	−12.4	−53.6	72.8	1	A
ILE	CG1	340	−11.6	−51.9	71.2	1	A
ILE	CD1	340	−12.1	−52.7	70.0	1	A
ILE	C	340	−9.7	−50.9	72.9	1	A
ILE	O	340	−10.1	−49.8	72.5	1	A
LEU	N	341	−8.4	−51.3	72.9	1	A
LEU	CA	341	−7.4	−50.4	72.5	1	A
LEU	CB	341	−6.2	−50.6	73.4	1	A
LEU	CG	341	−6.5	−50.8	74.9	3	A
LEU	CD1	341	−5.3	−51.3	75.7	1	A
LEU	CD2	341	−7.1	−49.5	75.4	2	A
LEU	C	341	−7.0	−50.8	71.1	1	A
LEU	O	341	−7.4	−51.8	70.5	1	A
PRO	N	342	−6.1	−49.9	70.4	1	A
PRO	CD	342	−5.3	−48.8	71.0	1	A
PRO	CA	342	−5.7	−50.2	69.1	1	A
PRO	CB	342	−4.7	−49.0	68.8	1	A
PRO	CG	342	−4.1	−48.8	70.1	2	A
PRO	C	342	−5.0	−51.5	69.0	1	A
PRO	O	342	−5.1	−52.3	68.0	3	A
GLN	N	343	−4.3	−51.9	70.1	1	A
GLN	CA	343	−3.6	−53.1	70.2	1	A
GLN	CB	343	−3.1	−53.3	71.6	1	A
GLN	CG	343	−1.8	−52.6	72.0	1	A
GLN	CD	343	−2.0	−51.2	72.5	1	A
GLN	OE1	343	−3.1	−50.6	72.5	3	A
GLN	NE2	343	−0.9	−50.5	72.9	4	A
GLN	C	343	−4.5	−54.3	69.8	1	A
GLN	O	343	−4.0	−55.3	69.4	1	A
GLN	N	344	−5.8	−54.1	70.0	1	A
GLN	CA	344	−6.8	−55.1	69.6	3	A
GLN	CB	344	−8.0	−55.0	70.6	3	A
GLN	CG	344	−7.8	−55.9	71.8	6	A
GLN	CD	344	−7.4	−55.0	73.0	7	A
GLN	OE1	344	−7.1	−55.6	74.1	9	A
GLN	NE2	344	−7.4	−53.7	72.9	7	A
GLN	C	344	−7.3	−55.0	68.2	2	A
GLN	O	344	−7.5	−56.1	67.6	2	A
TYR	N	345	−7.6	−53.8	67.7	2	A
TYR	CA	345	−8.1	−53.7	66.3	1	A
TYR	CB	345	−9.1	−52.6	66.2	1	A
TYR	CG	345	−8.7	−51.2	66.4	1	A
TYR	CD1	345	−8.1	−50.4	65.4	1	A
TYR	CE1	345	−7.8	−49.1	65.7	1	A
TYR	CD2	345	−8.8	−50.6	67.7	1	A
TYR	CE2	345	−8.5	−49.3	67.9	1	A
TYR	CZ	345	−8.0	−48.5	66.9	1	A
TYR	OH	345	−7.7	−47.2	67.1	1	A
TYR	C	345	−7.0	−53.7	65.3	3	A
TYR	O	345	−7.2	−53.5	64.1	5	A
LEU	N	346	−5.7	−53.8	65.7	1	A
LEU	CA	346	−4.6	−53.8	64.8	1	A
LEU	CB	346	−3.6	−52.7	65.1	1	A
LEU	CG	346	−4.2	−51.3	64.8	1	A
LEU	CD1	346	−3.1	−50.3	64.9	1	A
LEU	CD2	346	−4.8	−51.3	63.5	1	A
LEU	C	346	−4.0	−55.2	65.0	1	A
LEU	O	346	−3.3	−55.4	66.1	5	A
ARG	N	347	−4.2	−56.1	64.1	1	A
ARG	CA	347	−3.7	−57.5	64.3	1	A
ARG	CB	347	−4.7	−58.4	63.6	3	A
ARG	CG	347	−4.4	−59.9	63.8	8	A
ARG	CD	347	−5.6	−60.7	63.5	7	A
ARG	NE	347	−6.1	−60.5	62.1	11	A
ARG	CZ	347	−5.4	−60.9	61.0	16	A
ARG	NH1	347	−4.2	−61.5	61.1	17	A
ARG	NH2	347	−5.9	−60.6	59.8	20	A
ARG	C	347	−2.3	−57.6	63.7	3	A
ARG	O	347	−2.1	−57.3	62.5	7	A
PRO	N	348	−1.4	−58.1	64.5	5	A
PRO	CD	348	−1.6	−58.5	65.9	8	A
PRO	CA	348	0.0	−58.4	64.1	5	A
PRO	CB	348	0.6	−58.9	65.4	2	A
PRO	CG	348	−0.2	−58.3	66.4	5	A
PRO	C	348	0.1	−59.4	63.0	8	A
PRO	O	348	0.0	−60.6	63.3	10	A
VAL	N	349	0.2	−59.0	61.7	13	A
VAL	CA	349	0.3	−59.9	60.6	18	A
VAL	CB	349	−0.3	−59.4	59.3	20	A
VAL	CG1	349	−1.7	−59.8	59.2	26	A
VAL	CG2	349	−0.2	−57.9	59.3	25	A
VAL	C	349	1.8	−60.2	60.4	21	A
VAL	O	349	2.5	−59.3	59.9	23	A
GLU	N	350	2.2	−61.3	60.8	25	A
GLU	CA	350	3.6	−61.7	60.7	27	A
GLU	CB	350	3.8	−63.2	60.7	23	A
GLU	CG	350	5.0	−63.7	59.9	24	A
GLU	CD	350	6.2	−62.8	60.2	23	A
GLU	OE1	350	7.0	−62.6	59.2	21	A
GLU	OE2	350	6.4	−62.3	61.3	20	A
GLU	C	350	4.1	−61.2	59.3	30	A
GLU	O	350	3.6	−61.5	58.3	30	A
ASP	N	351	5.1	−60.3	59.4	31	A
ASP	CA	351	5.8	−59.7	58.3	33	A
ASP	CB	351	7.2	−59.3	58.6	34	A
ASP	CG	351	7.9	−58.7	57.3	39	A
ASP	OD1	351	7.6	−57.6	56.9	41	A
ASP	OD2	351	8.8	−59.4	56.8	38	A
ASP	C	351	5.7	−60.6	57.0	32	A
ASP	O	351	5.7	−61.8	57.2	34	A
VAL	N	352	5.8	−60.0	55.8	31	A
VAL	CA	352	5.8	−60.7	54.6	33	A
VAL	CB	352	6.2	−59.9	53.4	31	A
VAL	CG1	352	6.2	−60.7	52.1	27	A
VAL	CG2	352	5.4	−58.6	53.2	27	A
VAL	C	352	6.6	−62.0	54.7	35	A
VAL	O	352	6.1	−63.1	54.7	34	A
ALA	N	353	7.9	−61.8	55.0	37	A
ALA	CA	353	8.8	−63.0	55.2	35	A
ALA	CB	353	9.7	−63.1	54.0	35	A
ALA	C	353	9.7	−62.9	56.5	36	A
ALA	O	353	10.9	−63.1	56.4	36	A
THR	N	354	9.0	−62.5	57.6	35	A
THR	CA	354	9.7	−62.3	58.9	35	A
THR	CB	354	10.3	−63.7	59.4	35	A
THR	OG1	354	9.5	−64.8	58.9	30	A
THR	CG2	354	10.3	−63.7	61.0	27	A
THR	C	354	10.8	−61.3	58.7	34	A
THR	O	354	11.9	−61.6	58.3	33	A
SER	N	355	10.5	−60.0	59.0	32	A
SER	CA	355	11.4	−58.9	59.0	30	A
SER	CB	355	11.1	−57.9	57.9	24	A
SER	OG	355	10.1	−57.0	58.4	16	A
SER	C	355	11.6	−58.2	60.3	30	A
SER	O	355	10.9	−58.6	61.3	28	A
GLN	N	356	12.5	−57.3	60.4	31	A
GLN	CA	356	12.8	−56.5	61.6	30	A
GLN	CB	356	14.2	−55.9	61.5	34	A
GLN	CG	356	15.3	−56.9	61.3	41	A
GLN	CD	356	16.5	−56.6	62.2	45	A
GLN	OE1	356	16.9	−55.5	62.4	45	A
GLN	NE2	356	17.1	−57.7	62.8	44	A
GLN	C	356	11.8	−55.3	61.7	26	A
GLN	O	356	12.2	−54.2	61.9	26	A
ASP	N	357	10.5	−55.6	61.5	24	A
ASP	CA	357	9.5	−54.6	61.6	20	A
ASP	CB	357	9.1	−54.0	60.2	21	A
ASP	CG	357	10.1	−53.0	59.8	17	A
ASP	OD1	357	11.3	−53.3	59.9	19	A
ASP	OD2	357	9.7	−51.9	59.4	14	A
ASP	C	357	8.2	−55.3	62.1	16	A
ASP	O	357	7.9	−56.4	61.9	18	A
ASP	N	358	7.4	−54.4	62.8	13	A
ASP	CA	358	6.2	−54.9	63.3	12	A
ASP	CB	358	5.9	−54.2	64.7	10	A
ASP	CG	358	7.0	−54.6	65.7	8	A
ASP	OD1	358	7.0	−54.0	66.7	10	A
ASP	OD2	358	7.7	−55.6	65.4	6	A
ASP	C	358	5.2	−54.4	62.3	11	A
ASP	O	358	5.2	−53.2	61.9	7	A
CYS	N	359	4.3	−55.3	61.8	12	A
CYS	CA	359	3.3	−55.0	60.8	12	A
CYS	C	359	1.9	−55.4	61.3	9	A
CYS	O	359	1.8	−56.3	62.0	10	A
CYS	CB	359	3.6	−55.7	59.5	14	A
CYS	SG	359	5.2	−55.3	58.7	14	A
TYR	N	360	0.9	−54.6	60.9	5	A
TYR	CA	360	−0.4	−54.9	61.3	3	A
TYR	CB	360	−0.8	−54.0	62.5	4	A
TYR	CG	360	0.2	−53.9	63.6	1	A
TYR	CD1	360	1.4	−53.1	63.4	1	A
TYR	CE1	360	2.3	−53.1	64.4	1	A
TYR	CD2	360	0.0	−54.6	64.8	1	A
TYR	CE2	360	1.0	−54.5	65.8	1	A
TYR	CZ	360	2.1	−53.7	65.6	1	A
TYR	OH	360	3.0	−53.7	66.6	3	A
TYR	C	360	−1.5	−54.7	60.3	2	A
TYR	O	360	−1.4	−53.9	59.4	5	A
LYS	N	361	−2.5	−55.5	60.4	1	A
LYS	CA	361	−3.7	−55.4	59.5	3	A
LYS	CB	361	−4.1	−56.8	59.0	5	A
LYS	CG	361	−3.4	−57.1	57.7	11	A
LYS	CD	361	−4.0	−58.3	56.9	21	A
LYS	CE	361	−3.2	−58.6	55.6	25	A
LYS	NZ	361	−3.6	−59.8	54.9	26	A
LYS	C	361	−4.8	−54.8	60.3	2	A
LYS	O	361	−5.1	−55.1	61.5	2	A
PHE	N	362	−5.5	−53.8	59.7	1	A
PHE	CA	362	−6.6	−53.2	60.4	1	A
PHE	CB	362	−7.1	−52.0	59.6	2	A
PHE	CG	362	−8.2	−51.2	60.2	1	A
PHE	CD1	362	−7.9	−50.5	61.4	1	A
PHE	CD2	362	−9.4	−51.1	59.7	1	A
PHE	CE1	362	−8.8	−49.7	62.0	1	A
PHE	CE2	362	−10.4	−50.3	60.3	1	A
PHE	CZ	362	−10.1	−49.6	61.4	1	A
PHE	C	362	−7.7	−54.3	60.6	2	A
PHE	O	362	−8.2	−54.8	59.6	1	A
ALA	N	363	−8.0	−54.6	61.8	1	A
ALA	CA	363	−8.9	−55.7	62.1	1	A
ALA	CB	363	−8.5	−56.5	63.3	3	A
ALA	C	363	−10.4	−55.3	62.2	1	A
ALA	O	363	−11.2	−56.1	62.6	1	A
ILE	N	364	−10.7	−54.1	61.8	1	A
ILE	CA	364	−12.1	−53.6	61.8	1	A
ILE	CB	364	−12.3	−52.3	62.5	1	A
ILE	CG2	364	−13.8	−51.9	62.5	1	A
ILE	CG1	364	−11.8	−52.3	63.9	1	A
ILE	CD1	364	−11.9	−51.0	64.6	1	A
ILE	C	364	−12.6	−53.6	60.4	2	A
ILE	O	364	−12.0	−52.9	59.6	1	A
SER	N	365	−13.6	−54.4	60.0	1	A
SER	CA	365	−14.1	−54.4	58.7	1	A
SER	CB	365	−13.6	−55.7	58.0	1	A
SER	OG	365	−14.2	−56.8	58.5	1	A
SER	C	365	−15.6	−54.3	58.6	1	A
SER	O	365	−16.3	−54.6	59.6	1	A
GLN	N	366	−16.1	−53.9	57.5	1	A
GLN	CA	366	−17.5	−53.8	57.2	3	A
GLN	CB	366	−17.8	−52.9	56.0	7	A
GLN	CG	366	−16.9	−53.3	54.8	20	A
GLN	CD	366	−17.1	−52.3	53.7	28	A
GLN	OE1	366	−18.2	−52.1	53.2	28	A
GLN	NE2	366	−16.0	−51.6	53.3	25	A
GLN	C	366	−18.3	−55.1	57.1	1	A
GLN	O	366	−17.7	−56.1	56.5	1	A
SER	N	367	−19.5	−55.1	57.5	2	A
SER	CA	367	−20.4	−56.3	57.4	1	A
SER	CB	367	−20.6	−56.8	58.8	5	A
SER	OG	367	−21.8	−57.7	58.8	3	A
SER	C	367	−21.7	−56.0	56.8	1	A
SER	O	367	−22.2	−54.9	56.9	4	A
SER	N	368	−22.3	−57.0	56.2	4	A
SER	CA	368	−23.6	−56.8	55.6	5	A
SER	CB	368	−23.6	−57.4	54.2	2	A
SER	OG	368	−23.4	−58.8	54.2	8	A
SER	C	368	−24.7	−57.6	56.4	5	A
SER	O	368	−25.8	−57.5	56.1	1	A
THR	N	369	−24.2	−58.2	57.5	6	A
THR	CA	369	−25.1	−59.0	58.4	6	A
THR	CB	369	−24.6	−60.4	58.4	4	A
THR	OG1	369	−23.2	−60.5	58.6	3	A
THR	CG2	369	−24.9	−61.1	57.0	5	A
THR	C	369	−25.1	−58.4	59.8	5	A
THR	O	369	−25.4	−59.2	60.8	3	A
GLY	N	370	−24.9	−57.1	60.0	4	A
GLY	CA	370	−25.0	−56.6	61.3	8	A
GLY	C	370	−23.7	−56.5	62.1	9	A
GLY	O	370	−22.6	−56.6	61.4	10	A
THR	N	371	−23.7	−56.3	63.4	6	A
THR	CA	371	−22.5	−56.2	64.2	1	A
THR	CB	371	−22.6	−55.2	65.3	1	A
THR	OG1	371	−22.6	−53.9	64.9	1	A
THR	CG2	371	−21.5	−55.4	66.3	1	A
THR	C	371	−22.0	−57.5	64.7	1	A
THR	O	371	−22.8	−58.3	65.2	1	A
VAL	N	372	−20.8	−57.8	64.5	1	A
VAL	CA	372	−20.2	−59.1	65.0	1	A
VAL	CB	372	−19.7	−59.9	63.8	1	A
VAL	CG1	372	−19.1	−61.2	64.3	1	A
VAL	CG2	372	−20.9	−60.3	62.9	1	A
VAL	C	372	−19.0	−58.8	65.9	1	A
VAL	O	372	−18.0	−58.2	65.5	1	A
MET	N	373	−19.1	−59.2	67.2	1	A
MET	CA	373	−18.0	−59.0	68.1	1	A
MET	CB	373	−18.6	−58.8	69.5	1	A
MET	CG	373	−19.0	−57.4	69.8	2	A
MET	SD	373	−20.4	−57.1	71.0	1	A
MET	CE	373	−19.5	−57.0	72.5	5	A
MET	C	373	−17.1	−60.1	68.0	1	A
MET	O	373	−17.1	−61.0	68.9	3	A
GLY	N	374	−16.2	−60.1	67.0	1	A
GLY	CA	374	−15.2	−61.1	66.8	1	A
GLY	C	374	−14.1	−61.2	67.8	1	A
GLY	O	374	−14.2	−60.6	68.9	6	A
ALA	N	375	−13.1	−61.9	67.5	2	A
ALA	CA	375	−11.9	−62.1	68.3	1	A
ALA	CB	375	−11.0	−63.1	67.8	1	A
ALA	C	375	−11.2	−60.9	68.7	1	A
ALA	O	375	−10.5	−60.9	69.7	1	A
VAL	N	376	−11.3	−59.8	68.0	1	A
VAL	CA	376	−10.5	−58.6	68.4	2	A
VAL	CB	376	−10.5	−57.5	67.3	1	A
VAL	CG1	376	−10.2	−58.1	66.0	1	A
VAL	CG2	376	−11.7	−56.6	67.3	1	A
VAL	C	376	−11.2	−58.0	69.6	3	A
VAL	O	376	−10.6	−57.6	70.6	5	A
ILE	N	377	−12.5	−58.0	69.7	3	A
ILE	CA	377	−13.3	−57.5	70.8	3	A
ILE	CB	377	−14.8	−57.3	70.5	5	A
ILE	CG2	377	−15.6	−57.1	71.8	6	A
ILE	CG1	377	−15.0	−56.2	69.5	3	A
ILE	CD1	377	−14.5	−54.9	69.9	4	A
ILE	C	377	−13.1	−58.5	72.0	2	A
ILE	O	377	−13.0	−58.1	73.1	4	A
MET	N	378	−13.1	−59.8	71.6	1	A
MET	CA	378	−12.9	−60.8	72.7	1	A
MET	CB	378	−13.3	−62.1	72.2	1	A
MET	CG	378	−14.8	−62.2	71.9	1	A
MET	SD	378	−15.3	−63.9	71.4	1	A
MET	CE	378	−16.2	−64.4	72.9	2	A
MET	C	378	−11.5	−60.8	73.2	4	A
MET	O	378	−11.3	−61.0	74.4	10	A
GLU	N	379	−10.5	−60.7	72.3	3	A
GLU	CA	379	−9.1	−60.7	72.7	3	A
GLU	CB	379	−8.2	−60.5	71.6	5	A
GLU	CG	379	−7.9	−61.7	70.7	12	A
GLU	CD	379	−6.8	−61.4	69.6	20	A
GLU	OE1	379	−6.6	−62.3	68.8	20	A
GLU	OE2	379	−6.2	−60.4	69.7	22	A
GLU	C	379	−8.8	−59.6	73.8	1	A
GLU	O	379	−7.8	−59.6	74.3	3	A
GLY	N	380	−9.8	−58.8	74.0	1	A
GLY	CA	380	−9.7	−57.8	75.0	1	A
GLY	C	380	−10.2	−58.1	76.4	1	A
GLY	O	380	−9.7	−57.7	77.4	1	A
PHE	N	381	−11.3	−58.9	76.5	1	A
PHE	CA	381	−11.9	−59.2	77.8	1	A
PHE	CB	381	−13.2	−58.5	77.9	3	A
PHE	CG	381	−13.2	−57.2	77.2	1	A
PHE	CD1	381	−13.4	−57.1	75.9	1	A
PHE	CD2	381	−12.8	−56.0	77.9	2	A
PHE	CE1	381	−13.4	−55.9	75.2	1	A
PHE	CE2	381	−12.8	−54.8	77.3	1	A
PHE	CZ	381	−13.0	−54.7	75.9	1	A
PHE	C	381	−12.1	−60.7	78.0	1	A
PHE	O	381	−11.9	−61.6	77.2	1	A
TYR	N	382	−12.6	−61.0	79.2	1	A
TYR	CA	382	−12.9	−62.3	79.7	1	A
TYR	CB	382	−12.6	−62.5	81.1	1	A
TYR	CG	382	−12.9	−63.8	81.7	1	A
TYR	CD1	382	−12.3	−65.0	81.2	1	A
TYR	CE1	382	−12.6	−66.2	81.7	1	A
TYR	CD2	382	−13.8	−64.0	82.8	1	A
TYR	CE2	382	−14.1	−65.3	83.3	1	A
TYR	CZ	382	−13.4	−66.4	82.8	1	A
TYR	OH	382	−13.7	−67.6	83.3	1	A
TYR	C	382	−14.4	−62.3	79.4	1	A
TYR	O	382	−15.1	−61.5	79.9	2	A
VAL	N	383	−14.8	−63.2	78.5	1	A
VAL	CA	383	−16.2	−63.3	78.2	1	A
VAL	CB	383	−16.4	−63.3	76.7	1	A
VAL	CG1	383	−17.9	−63.3	76.3	1	A
VAL	CG2	383	−15.7	−62.2	76.0	1	A
VAL	C	383	−16.9	−64.5	78.8	1	A
VAL	O	383	−16.4	−65.6	78.8	1	A
VAL	N	384	−18.0	−64.2	79.5	2	A
VAL	CA	384	−18.8	−65.3	80.2	1	A
VAL	CB	384	−19.1	−64.9	81.6	1	A
VAL	CG1	384	−20.0	−65.9	82.2	1	A
VAL	CG2	384	−17.8	−65.0	82.4	1	A
VAL	C	384	−20.1	−65.5	79.5	1	A
VAL	O	384	−20.9	−64.6	79.4	1	A
PHE	N	385	−20.4	−66.7	79.0	1	A
PHE	CA	385	−21.6	−67.1	78.4	1	A
PHE	CB	385	−21.3	−68.0	77.2	1	A
PHE	CG	385	−20.5	−67.2	76.1	1	A
PHE	CD1	385	−21.2	−66.7	75.0	2	A
PHE	CD2	385	−19.2	−67.0	76.2	1	A
PHE	CE1	385	−20.5	−66.0	74.0	4	A
PHE	CE2	385	−18.5	−66.3	75.3	3	A
PHE	CZ	385	−19.1	−65.8	74.2	2	A
PHE	C	385	−22.5	−67.8	79.4	1	A
PHE	O	385	−22.5	−69.0	79.4	3	A
ASP	N	386	−23.2	−67.0	80.2	1	A
ASP	CA	386	−24.1	−67.5	81.2	1	A
ASP	CB	386	−24.4	−66.4	82.2	3	A
ASP	CG	386	−24.7	−67.0	83.6	3	A
ASP	OD1	386	−24.8	−68.2	83.8	5	A
ASP	OD2	386	−24.9	−66.2	84.5	4	A
ASP	C	386	−25.4	−68.0	80.5	1	A
ASP	O	386	−26.4	−67.4	80.8	1	A
ARG	N	387	−25.3	−69.0	79.7	2	A
ARG	CA	387	−26.5	−69.5	79.0	3	A
ARG	CB	387	−26.2	−70.8	78.4	1	A
ARG	CG	387	−25.3	−70.7	77.1	1	A
ARG	CD	387	−24.4	−71.9	76.9	1	A
ARG	NE	387	−25.2	−73.1	76.7	3	A
ARG	CZ	387	−25.9	−73.4	75.6	3	A
ARG	NH1	387	−25.9	−72.6	74.6	1	A
ARG	NH2	387	−26.5	−74.6	75.6	1	A
ARG	C	387	−27.6	−69.6	80.0	3	A
ARG	O	387	−28.7	−69.1	79.8	5	A
ALA	N	388	−27.4	−70.4	81.1	4	A
ALA	CA	388	−28.4	−70.6	82.1	7	A
ALA	CB	388	−27.7	−71.2	83.4	10	A
ALA	C	388	−29.2	−69.4	82.5	8	A
ALA	O	388	−30.4	−69.4	82.3	10	A
ARG	N	389	−28.5	−68.3	82.9	8	A
ARG	CA	389	−29.2	−67.1	83.3	8	A
ARG	CB	389	−28.4	−66.4	84.4	10	A
ARG	CG	389	−28.2	−67.2	85.7	15	A
ARG	CD	389	−27.8	−66.3	86.8	16	A
ARG	NE	389	−28.8	−65.3	87.2	18	A
ARG	CZ	389	−28.6	−64.4	88.2	22	A
ARG	NH1	389	−27.5	−64.4	88.9	23	A
ARG	NH2	389	−29.6	−63.5	88.4	21	A
ARG	C	389	−29.5	−66.2	82.1	8	A
ARG	O	389	−30.0	−65.1	82.3	9	A
LYS	N	390	−29.2	−66.7	80.9	9	A
LYS	CA	390	−29.6	−66.0	79.7	6	A
LYS	CB	390	−31.1	−65.8	79.6	7	A
LYS	CG	390	−31.7	−65.5	78.3	19	A
LYS	CD	390	−33.2	−65.4	78.4	25	A
LYS	CE	390	−33.8	−65.0	77.0	30	A
LYS	NZ	390	−35.3	−64.9	77.1	31	A
LYS	C	390	−28.9	−64.6	79.6	3	A
LYS	O	390	−29.6	−63.6	79.6	5	A
ARG	N	391	−27.6	−64.5	79.7	2	A
ARG	CA	391	−26.9	−63.3	79.7	1	A
ARG	CB	391	−27.0	−62.6	81.0	2	A
ARG	CG	391	−26.5	−63.4	82.2	6	A
ARG	CD	391	−26.4	−62.7	83.5	7	A
ARG	NE	391	−25.8	−63.6	84.5	1	A
ARG	CZ	391	−25.6	−63.2	85.8	1	A
ARG	NH1	391	−25.9	−62.0	86.2	2	A
ARG	NH2	391	−25.0	−64.1	86.6	2	A
ARG	C	391	−25.4	−63.4	79.4	1	A
ARG	O	391	−24.9	−64.5	79.5	4	A
ILE	N	392	−24.7	−62.3	79.0	1	A
ILE	CA	392	−23.3	−62.4	78.7	1	A
ILE	CB	392	−23.0	−62.2	77.3	1	A
ILE	CG2	392	−21.6	−61.9	77.0	1	A
ILE	CG1	392	−23.6	−63.3	76.5	1	A
ILE	CD1	392	−23.4	−63.2	75.0	1	A
ILE	C	392	−22.6	−61.4	79.6	1	A
ILE	O	392	−23.0	−60.3	79.7	1	A
GLY	N	393	−21.4	−61.8	80.1	2	A
GLY	CA	393	−20.6	−60.9	80.9	1	A
GLY	C	393	−19.2	−60.7	80.4	1	A
GLY	O	393	−18.6	−61.6	79.9	1	A
PHE	N	394	−18.8	−59.5	80.5	2	A
PHE	CA	394	−17.4	−59.1	80.1	3	A
PHE	CB	394	−17.5	−58.0	79.0	1	A
PHE	CG	394	−18.2	−58.4	77.8	1	A
PHE	CD1	394	−19.6	−58.6	77.8	1	A
PHE	CD2	394	−17.6	−58.4	76.5	1	A
PHE	CE1	394	−20.3	−58.9	76.6	1	A
PHE	CE2	394	−18.3	−58.6	75.4	1	A
PHE	CZ	394	−19.6	−58.8	75.4	1	A
PHE	C	394	−16.7	−58.4	81.3	5	A
PHE	O	394	−17.2	−57.6	82.0	3	A
ALA	N	395	−15.4	−58.8	81.4	4	A
ALA	CA	395	−14.5	−58.2	82.4	4	A
ALA	CB	395	−14.4	−59.2	83.6	8	A
ALA	C	395	−13.2	−58.1	81.7	1	A
ALA	O	395	−12.9	−58.8	80.8	1	A
VAL	N	396	−12.3	−57.2	82.3	2	A
VAL	CA	396	−11.0	−57.0	81.7	3	A
VAL	CB	396	−10.2	−55.8	82.3	2	A
VAL	CG1	396	−9.1	−55.5	81.5	1	A
VAL	CG2	396	−11.2	−54.7	82.4	3	A
VAL	C	396	−10.1	−58.2	81.7	3	A
VAL	O	396	−9.7	−58.7	82.8	1	A
SER	N	397	−9.8	−58.7	80.5	4	A
SER	CA	397	−8.9	−59.9	80.3	8	A
SER	CB	397	−8.8	−60.2	78.8	12	A
SER	OG	397	−8.0	−61.4	78.6	15	A
SER	C	397	−7.5	−59.7	80.9	9	A
SER	O	397	−6.8	−58.8	80.4	9	A
ALA	N	398	−7.2	−60.5	81.8	9	A
ALA	CA	398	−5.9	−60.5	82.5	9	A
ALA	CB	398	−5.8	−61.4	83.7	14	A
ALA	C	398	−4.7	−60.8	81.5	11	A
ALA	O	398	−3.6	−60.8	81.9	12	A
CYS	N	399	−5.1	−61.2	80.3	9	A
CYS	CA	399	−4.1	−61.5	79.3	7	A
CYS	C	399	−4.2	−60.7	78.1	5	A
CYS	O	399	−3.7	−61.1	77.0	11	A
CYS	CB	399	−4.2	−63.0	78.9	8	A
CYS	SG	399	−5.7	−63.3	77.9	19	A
HIS	N	400	−4.7	−59.5	78.2	5	A
HIS	CA	400	−4.9	−58.7	77.0	6	A
HIS	CB	400	−6.1	−57.8	77.0	7	A
HIS	CG	400	−6.0	−56.5	77.7	1	A
HIS	CD2	400	−5.8	−55.2	77.2	2	A
HIS	ND1	400	−6.0	−56.3	79.1	1	A
HIS	CE1	400	−5.9	−55.0	79.4	1	A
HIS	NE2	400	−5.7	−54.4	78.2	1	A
HIS	C	400	−3.7	−57.8	76.8	6	A
HIS	O	400	−3.0	−57.3	77.7	8	A
VAL	N	401	−3.4	−57.5	75.5	6	A
VAL	CA	401	−2.2	−56.7	75.2	7	A
VAL	CB	401	−1.8	−56.8	73.7	6	A
VAL	CG1	401	−0.6	−56.0	73.4	6	A
VAL	CG2	401	−1.6	−58.3	73.3	10	A
VAL	C	401	−2.6	−55.2	75.4	6	A
VAL	O	401	−3.8	−54.8	75.1	5	A
HIS	N	402	−1.7	−54.5	76.0	7	A
HIS	CA	402	−2.0	−53.0	76.3	7	A
HIS	CB	402	−2.8	−52.9	77.5	6	A
HIS	CG	402	−2.1	−53.3	78.8	4	A
HIS	CD2	402	−1.8	−52.7	79.9	5	A
HIS	ND1	402	−1.7	−54.6	79.0	5	A
HIS	CE1	402	−1.1	−54.7	80.2	8	A
HIS	NE2	402	−1.2	−53.5	80.7	4	A
HIS	C	402	−0.6	−52.4	76.6	7	A
HIS	O	402	0.3	−53.0	77.1	10	A
ASP	N	403	−0.5	−51.1	76.2	6	A
ASP	CA	403	0.7	−50.5	76.4	7	A
ASP	CB	403	0.9	−49.3	75.5	9	A
ASP	CG	403	−0.2	−48.3	75.7	9	A
ASP	OD1	403	−0.4	−47.8	76.8	13	A
ASP	OD2	403	−0.9	−47.9	74.7	8	A
ASP	C	403	0.8	−50.0	77.9	9	A
ASP	O	403	−0.1	−50.2	78.7	9	A
GLU	N	404	1.9	−49.3	78.2	12	A
GLU	CA	404	2.2	−48.8	79.5	9	A
GLU	CB	404	3.5	−48.1	79.5	7	A
GLU	CG	404	3.7	−47.0	80.6	7	A
GLU	CD	404	5.0	−46.3	80.6	9	A
GLU	OE1	404	5.5	−45.9	79.5	12	A
GLU	OE2	404	5.7	−46.1	81.6	12	A
GLU	C	404	1.1	−47.8	80.0	8	A
GLU	O	404	0.8	−47.8	81.2	8	A
PHE	N	405	0.6	−47.0	79.1	6	A
PHE	CA	405	−0.4	−45.9	79.4	4	A
PHE	CB	405	−0.2	−44.7	78.5	3	A
PHE	CG	405	1.2	−44.2	78.4	2	A
PHE	CD1	405	2.1	−44.8	77.5	1	A
PHE	CD2	405	1.6	−43.3	79.3	5	A
PHE	CE1	405	3.4	−44.4	77.5	2	A
PHE	CE2	405	3.0	−42.8	79.3	2	A
PHE	CZ	405	3.8	−43.4	78.4	4	A
PHE	C	405	−1.8	−46.3	79.5	5	A
PHE	O	405	−2.5	−46.1	80.5	9	A
ARG	N	406	−2.4	−46.9	78.4	4	A
ARG	CA	406	−3.8	−47.2	78.4	2	A
ARG	CB	406	−4.4	−46.8	77.1	4	A
ARG	CG	406	−4.4	−45.4	76.8	8	A
ARG	CD	406	−5.1	−45.0	75.5	6	A
ARG	NE	406	−4.6	−45.7	74.4	1	A
ARG	CZ	406	−4.7	−45.2	73.2	2	A
ARG	NH1	406	−5.3	−44.1	73.0	3	A
ARG	NH2	406	−4.2	−45.9	72.1	2	A
ARG	C	406	−4.0	−48.7	78.6	2	A
ARG	O	406	−3.1	−49.5	78.7	5	A
THR	N	407	−5.3	−49.1	78.8	1	A
THR	CA	407	−5.6	−50.4	79.0	2	A
THR	CB	407	−5.5	−50.8	80.5	4	A
THR	OG1	407	−5.8	−52.1	80.7	4	A
THR	CG2	407	−6.3	−49.9	81.4	6	A
THR	C	407	−7.1	−50.7	78.6	1	A
THR	O	407	−7.9	−49.8	78.8	2	A
ALA	N	408	−7.4	−51.9	78.2	1	A
ALA	CA	408	−8.7	−52.3	77.8	1	A
ALA	CB	408	−8.8	−53.7	77.5	1	A
ALA	C	408	−9.5	−52.0	79.1	1	A
ALA	O	408	−8.9	−51.9	80.2	6	A
ALA	N	409	−10.8	−52.0	79.1	1	A
ALA	CA	409	−11.5	−51.7	80.3	2	A
ALA	CB	409	−11.3	−50.3	80.8	4	A
ALA	C	409	−13.0	−52.0	80.2	3	A
ALA	O	409	−13.6	−51.9	79.1	5	A
VAL	N	410	−13.7	−52.2	81.3	1	A
VAL	CA	410	−15.1	−52.5	81.4	1	A
VAL	CB	410	−15.4	−53.9	81.8	1	A
VAL	CG1	410	−16.8	−54.2	81.8	1	A
VAL	CG2	410	−14.7	−54.8	80.9	1	A
VAL	C	410	−15.6	−51.6	82.5	1	A
VAL	O	410	−15.2	−51.7	83.7	1	A
GLU	N	411	−16.6	−50.7	82.2	1	A
GLU	CA	411	−17.1	−49.7	83.1	3	A
GLU	CB	411	−16.3	−48.4	83.0	5	A
GLU	CG	411	−14.9	−48.5	83.3	5	A
GLU	CD	411	−14.1	−47.3	82.9	6	A
GLU	OE1	411	−13.2	−46.9	83.6	13	A
GLU	OE2	411	−14.5	−46.7	81.8	7	A
GLU	C	411	−18.6	−49.5	83.1	4	A
GLU	O	411	−19.2	−49.4	82.0	2	A
GLY	N	412	−19.2	−49.2	84.3	5	A
GLY	CA	412	−20.6	−48.9	84.4	5	A
GLY	C	412	−20.9	−48.2	85.7	4	A
GLY	O	412	−20.0	−48.0	86.5	5	A
PRO	N	413	−22.1	−47.8	85.9	1	A
PRO	CD	413	−22.6	−47.4	87.3	1	A
PRO	CA	413	−23.3	−47.9	85.0	2	A
PRO	CB	413	−24.4	−48.2	85.9	1	A
PRO	CG	413	−24.1	−47.3	87.1	1	A
PRO	C	413	−23.5	−46.6	84.3	4	A
PRO	O	413	−23.0	−45.6	84.7	9	A
PHE	N	414	−24.2	−46.7	83.2	6	A
PHE	CA	414	−24.5	−45.5	82.4	8	A
PHE	CB	414	−23.7	−45.5	81.1	10	A
PHE	CG	414	−22.2	−45.5	81.2	9	A
PHE	CD1	414	−21.6	−46.8	81.2	13	A
PHE	CD2	414	−21.5	−44.4	81.5	10	A
PHE	CE1	414	−20.2	−46.9	81.4	12	A
PHE	CE2	414	−20.1	−44.5	81.8	11	A
PHE	CZ	414	−19.5	−45.7	81.7	12	A
PHE	C	414	−26.0	−45.3	82.1	10	A
PHE	O	414	−26.6	−46.2	81.6	11	A
VAL	N	415	−26.5	−44.2	82.5	11	A
VAL	CA	415	−28.0	−44.0	82.3	10	A
VAL	CB	415	−28.4	−42.6	82.8	10	A
VAL	CG1	415	−30.0	−42.7	83.0	8	A
VAL	CG2	415	−27.8	−42.4	84.2	16	A
VAL	C	415	−28.2	−43.9	80.8	10	A
VAL	O	415	−27.6	−43.2	80.0	9	A
THR	N	416	−29.1	−44.8	80.3	11	A
THR	CA	416	−29.5	−44.9	78.9	12	A
THR	CB	416	−28.7	−45.9	78.2	8	A
THR	OG1	416	−27.3	−45.7	78.5	8	A
THR	CG2	416	−28.8	−45.7	76.7	8	A
THR	C	416	−31.0	−45.3	78.9	14	A
THR	O	416	−31.3	−46.3	79.5	16	A
LEU	N	417	−31.8	−44.5	78.3	12	A
LEU	CA	417	−33.2	−44.7	78.2	12	A
LEU	CB	417	−33.9	−43.4	78.4	10	A
LEU	CG	417	−33.5	−42.5	79.5	8	A
LEU	CD1	417	−33.8	−41.1	79.2	5	A
LEU	CD2	417	−34.2	−43.0	80.8	6	A
LEU	C	417	−33.6	−45.4	77.0	12	A
LEU	O	417	−33.0	−45.2	75.9	11	A
ASP	N	418	−34.7	−46.2	77.0	15	A
ASP	CA	418	−35.2	−46.9	75.8	20	A
ASP	CB	418	−35.8	−45.9	74.9	26	A
ASP	CG	418	−36.9	−45.1	75.5	33	A
ASP	OD1	418	−37.1	−43.9	75.0	35	A
ASP	OD2	418	−37.6	−45.6	76.5	40	A
ASP	C	418	−34.1	−47.7	75.1	20	A
ASP	O	418	−33.9	−47.5	73.9	21	A
MET	N	419	−33.4	−48.6	75.8	17	A
MET	CA	419	−32.3	−49.3	75.1	13	A
MET	CB	419	−31.5	−50.0	76.2	10	A
MET	CG	419	−30.8	−49.0	77.1	10	A
MET	SD	419	−29.7	−49.7	78.3	13	A
MET	CE	419	−30.9	−50.0	79.6	13	A
MET	C	419	−32.8	−50.3	74.1	13	A
MET	O	419	−32.1	−50.6	73.1	15	A
GLU	N	420	−34.0	−50.9	74.3	15	A
GLU	CA	420	−34.5	−51.9	73.4	21	A
GLU	CB	420	−35.2	−53.0	74.2	25	A
GLU	CG	420	−35.2	−54.4	73.5	30	A
GLU	CD	420	−35.0	−55.5	74.5	31	A
GLU	OE1	420	−35.6	−55.5	75.6	27	A
GLU	OE2	420	−34.3	−56.5	74.1	31	A
GLU	C	420	−35.4	−51.3	72.3	22	A
GLU	O	420	−35.3	−50.1	72.0	22	A
GLU	OXT	420	−36.2	−52.0	71.8	27	A
GLU	CB	41	52.5	26.9	44.1	21	B
GLU	CG	41	51.9	25.7	44.9	26	B
GLU	CD	41	50.8	26.1	45.8	30	B
GLU	OE1	41	49.9	27.0	45.4	32	B
GLU	OE2	41	50.7	25.6	47.0	33	B
GLU	C	41	52.8	25.4	42.2	12	B
GLU	O	41	53.2	24.3	42.4	9	B
GLU	N	41	53.7	27.8	42.1	8	B
GLU	CA	41	53.4	26.6	43.0	13	B
MET	N	42	51.8	25.7	41.3	10	B
MET	CA	42	51.2	24.7	40.4	7	B
MET	CB	42	49.7	25.0	40.3	3	B
MET	CG	42	48.9	24.5	41.6	11	B
MET	SD	42	47.1	24.9	41.6	15	B
MET	CE	42	47.1	26.3	42.6	8	B
MET	C	42	51.8	24.9	39.0	6	B
MET	O	42	51.8	23.9	38.2	10	B
VAL	N	43	52.3	26.1	38.7	4	B
VAL	CA	43	52.9	26.4	37.5	2	B
VAL	CB	43	53.8	27.6	37.6	1	B
VAL	CG1	43	54.5	27.9	36.3	1	B
VAL	CG2	43	52.9	28.8	38.0	1	B
VAL	C	43	53.8	25.2	37.0	2	B
VAL	O	43	54.4	24.5	37.8	3	B
ASP	N	44	53.8	25.0	35.7	3	B
ASP	CA	44	54.6	23.9	35.1	6	B
ASP	CB	44	56.1	24.0	35.6	10	B
ASP	CG	44	56.9	24.7	34.5	21	B
ASP	OD1	44	56.9	26.0	34.4	29	B
ASP	OD2	44	57.6	24.0	33.8	26	B
ASP	C	44	54.2	22.5	35.6	7	B
ASP	O	44	54.9	21.5	35.4	10	B
ASN	N	45	53.0	22.4	36.1	5	B
ASN	CA	45	52.6	21.0	36.6	4	B
ASN	CB	45	51.6	21.1	37.7	4	B
ASN	CG	45	50.3	21.7	37.3	1	B
ASN	OD1	45	50.2	22.3	36.2	1	B
ASN	ND2	45	49.3	21.5	38.1	1	B
ASN	C	45	52.1	20.1	35.5	4	B
ASN	O	45	51.9	18.9	35.7	2	B
LEU	N	46	52.0	20.6	34.2	4	B
LEU	CA	46	51.6	19.8	33.1	4	B
LEU	CB	46	50.6	20.5	32.2	1	B
LEU	CG	46	49.4	21.0	32.9	2	B
LEU	CD1	46	48.4	21.4	31.9	7	B
LEU	CD2	46	48.8	20.0	33.8	8	B
LEU	C	46	52.8	19.4	32.2	5	B
LEU	O	46	53.8	20.2	32.2	1	B
ARG	N	47	52.7	18.3	31.6	4	B
ARG	CA	47	53.8	17.8	30.7	8	B
ARG	CB	47	54.7	16.8	31.4	14	B
ARG	CG	47	55.8	17.4	32.2	17	B
ARG	CD	47	56.8	16.3	32.6	25	B
ARG	NE	47	56.2	15.1	33.1	35	B
ARG	CZ	47	56.8	14.0	33.6	39	B
ARG	NH1	47	58.1	14.0	33.6	37	B
ARG	NH2	47	56.1	13.0	34.0	40	B
ARG	C	47	53.1	17.1	29.5	7	B
ARG	O	47	51.9	16.7	29.7	8	B
GLY	N	48	53.8	16.9	28.4	11	B
GLY	CA	48	53.2	16.2	27.3	12	B
GLY	C	48	53.8	16.4	26.0	15	B
GLY	O	48	54.1	17.6	25.6	19	B
LYS	N	49	54.2	15.3	25.3	16	B
LYS	CA	49	54.8	15.5	24.0	20	B
LYS	CB	49	55.6	14.2	23.6	21	B
LYS	CG	49	54.9	12.9	24.0	24	B
LYS	CD	49	55.8	11.7	23.9	28	B
LYS	CE	49	55.6	11.0	22.5	32	B
LYS	NZ	49	54.4	10.2	22.3	31	B
LYS	C	49	53.9	15.8	22.8	22	B
LYS	O	49	52.9	15.1	22.5	21	B
SER	N	50	54.1	16.9	22.2	24	B
SER	CA	50	53.4	17.4	21.0	26	B
SER	CB	50	54.1	17.1	19.8	28	B
SER	OG	50	53.5	17.7	18.6	34	B
SER	C	50	51.9	17.0	20.9	28	B
SER	O	50	51.0	17.5	21.6	33	B
GLY	N	51	51.6	16.2	19.9	24	B
GLY	CA	51	50.3	15.8	19.6	19	B
GLY	C	51	49.8	14.7	20.5	18	B
GLY	O	51	48.9	13.9	20.1	21	B
GLN	N	52	50.4	14.5	21.6	16	B
GLN	CA	52	50.1	13.4	22.5	14	B
GLN	CB	52	51.3	12.8	23.1	15	B
GLN	CG	52	51.6	11.4	22.5	17	B
GLN	CD	52	52.2	11.4	21.1	15	B
GLN	OE1	52	52.5	10.3	20.5	17	B
GLN	NE2	52	52.3	12.6	20.5	20	B
GLN	C	52	49.2	13.9	23.6	13	B
GLN	O	52	48.5	13.1	24.3	18	B
GLY	N	53	49.2	15.2	23.9	13	B
GLY	CA	53	48.3	15.7	24.9	11	B
GLY	C	53	49.0	16.1	26.2	9	B
GLY	O	53	50.2	15.7	26.5	10	B
TYR	N	54	48.3	16.9	27.1	8	B
TYR	CA	54	48.9	17.3	28.3	8	B
TYR	CB	54	48.6	18.8	28.6	7	B
TYR	CG	54	49.0	19.7	27.5	4	B
TYR	CD1	54	48.2	19.8	26.4	6	B
TYR	CE1	54	48.7	20.6	25.3	6	B
TYR	CD2	54	50.2	20.3	27.6	5	B
TYR	CE2	54	50.7	21.1	26.5	5	B
TYR	CZ	54	49.9	21.3	25.4	3	B
TYR	OH	54	50.3	22.1	24.4	3	B
TYR	C	54	48.4	16.5	29.5	8	B
TYR	O	54	47.2	16.0	29.5	13	B
TYR	N	55	49.3	16.3	30.5	6	B
TYR	CA	55	48.9	15.5	31.7	6	B
TYR	CB	55	49.4	14.1	31.5	9	B
TYR	CG	55	50.9	13.9	31.4	8	B
TYR	CD1	55	51.8	14.0	32.4	11	B
TYR	CE1	55	53.2	13.8	32.3	8	B
TYR	CD2	55	51.5	13.7	30.1	7	B
TYR	CE2	55	52.8	13.5	29.9	6	B
TYR	CZ	55	53.7	13.6	31.0	6	B
TYR	OH	55	55.0	13.5	30.8	10	B
TYR	C	55	49.5	16.1	32.9	5	B
TYR	O	55	50.5	16.8	32.9	4	B
VAL	N	56	48.8	16.0	34.0	3	B
VAL	CA	56	49.2	16.5	35.3	5	B
VAL	CB	56	48.1	17.4	35.9	1	B
VAL	CG1	56	46.8	16.7	36.1	1	B
VAL	CG2	56	48.6	18.0	37.2	2	B
VAL	C	56	49.3	15.3	36.3	9	B
VAL	O	56	48.6	14.3	36.2	11	B
GLU	N	57	50.3	15.3	37.1	12	B
GLU	CA	57	50.5	14.2	38.0	14	B
GLU	CB	57	51.9	14.3	38.7	16	B
GLU	CG	57	52.3	13.3	39.7	26	B
GLU	CD	57	53.8	13.2	40.0	29	B
GLU	OE1	57	54.5	12.7	39.2	33	B
GLU	OE2	57	54.1	13.6	41.1	32	B
GLU	C	57	49.5	14.1	39.1	13	B
GLU	O	57	49.1	15.1	39.7	14	B
MET	N	58	49.0	12.9	39.3	11	B
MET	CA	58	47.9	12.6	40.3	9	B
MET	CB	58	46.6	12.5	39.7	9	B
MET	CG	58	46.0	13.8	39.0	1	B
MET	SD	58	44.4	13.4	38.2	1	B
MET	CE	58	43.2	13.9	39.4	1	B
MET	C	58	48.2	11.3	41.1	8	B
MET	O	58	49.0	10.5	40.7	6	B
THR	N	59	47.5	11.2	42.3	10	B
THR	CA	59	47.7	10.0	43.1	11	B
THR	CB	59	48.5	10.2	44.3	14	B
THR	OG1	59	47.8	11.1	45.2	18	B
THR	CG2	59	49.8	10.9	44.0	17	B
THR	C	59	46.3	9.4	43.5	10	B
THR	O	59	45.5	10.2	44.0	11	B
VAL	N	60	46.1	8.1	43.3	12	B
VAL	CA	60	44.8	7.5	43.7	10	B
VAL	CB	60	44.1	6.9	42.5	9	B
VAL	CG1	60	43.9	8.0	41.4	7	B
VAL	CG2	60	44.9	5.8	41.9	7	B
VAL	C	60	45.1	6.4	44.7	9	B
VAL	O	60	46.2	5.8	44.8	7	B
GLY	N	61	44.0	6.0	45.4	8	B
GLY	CA	61	44.1	4.9	46.4	11	B
GLY	C	61	45.1	5.1	47.5	13	B
GLY	O	61	45.9	6.0	47.5	16	B
SER	N	62	44.9	4.2	48.6	11	B
SER	CA	62	45.8	4.3	49.7	12	B
SER	CB	62	45.0	4.6	51.0	12	B
SER	OG	62	44.3	5.9	50.9	13	B
SER	C	62	46.5	3.0	50.0	13	B
SER	O	62	45.9	1.9	50.1	15	B
PRO	N	63	47.9	3.0	50.1	13	B
PRO	CD	63	48.7	1.8	50.2	12	B
PRO	CA	63	48.8	4.2	50.0	14	B
PRO	CB	63	50.1	3.6	50.3	13	B
PRO	CG	63	50.0	2.2	49.7	14	B
PRO	C	63	48.7	4.8	48.5	15	B
PRO	O	63	48.3	4.1	47.6	19	B
PRO	N	64	49.2	6.1	48.4	12	B
PRO	CD	64	49.7	6.9	49.5	12	B
PRO	CA	64	49.2	6.8	47.1	9	B
PRO	CB	64	49.8	8.1	47.5	9	B
PRO	CG	64	49.4	8.3	48.9	14	B
PRO	C	64	49.9	6.2	45.9	8	B
PRO	O	64	51.1	5.9	46.0	6	B
GLN	N	65	49.2	6.0	44.8	8	B
GLN	CA	65	49.7	5.5	43.6	7	B
GLN	CB	65	48.8	4.4	42.9	6	B
GLN	CG	65	48.7	3.1	43.7	9	B
GLN	CD	65	48.1	2.0	42.8	11	B
GLN	OE1	65	48.6	1.8	41.7	13	B
GLN	NE2	65	47.1	1.4	43.3	10	B
GLN	C	65	49.9	6.6	42.6	10	B
GLN	O	65	48.9	7.2	42.1	10	B
THR	N	66	51.1	7.0	42.2	9	B
THR	CA	66	51.4	8.1	41.3	7	B
THR	CB	66	52.8	8.4	41.4	6	B
THR	OG1	66	53.2	8.8	42.7	8	B
THR	CG2	66	53.1	9.6	40.4	12	B
THR	C	66	51.0	7.7	39.9	7	B
THR	O	66	51.3	6.6	39.5	10	B
LEU	N	67	50.3	8.5	39.2	7	B
LEU	CA	67	49.8	8.3	37.8	5	B
LEU	CB	67	48.5	7.6	37.8	1	B
LEU	CG	67	48.5	6.1	38.1	3	B
LEU	CD1	67	47.0	5.7	38.2	6	B
LEU	CD2	67	49.1	5.3	36.9	4	B
LEU	C	67	49.7	9.6	37.0	6	B
LEU	O	67	49.3	10.6	37.6	6	B
ASN	N	68	50.1	9.6	35.8	9	B
ASN	CA	68	50.0	10.8	34.9	9	B
ASN	CB	68	51.1	10.8	33.9	9	B
ASN	CG	68	52.4	11.2	34.5	6	B
ASN	OD1	68	53.5	11.1	33.9	2	B
ASN	ND2	68	52.4	11.7	35.7	10	B
ASN	C	68	48.6	10.8	34.2	9	B
ASN	O	68	48.4	9.9	33.3	9	B
ILE	N	69	47.8	11.8	34.5	8	B
ILE	CA	69	46.5	11.9	33.9	9	B
ILE	CB	69	45.4	12.1	34.9	7	B
ILE	CG2	69	44.0	12.1	34.3	8	B
ILE	CG1	69	45.5	11.1	36.0	5	B
ILE	CD1	69	45.4	9.6	35.5	6	B
ILE	C	69	46.3	13.0	32.8	10	B
ILE	O	69	46.8	14.1	33.0	11	B
LEU	N	70	45.7	12.6	31.7	9	B
LEU	CA	70	45.5	13.5	30.6	7	B
LEU	CB	70	44.9	12.7	29.4	5	B
LEU	CG	70	44.8	13.3	28.0	5	B
LEU	CD1	70	46.1	13.1	27.2	5	B
LEU	CD2	70	43.6	12.8	27.3	3	B
LEU	C	70	44.5	14.6	30.9	7	B
LEU	O	70	43.3	14.3	31.3	7	B
VAL	N	71	44.8	15.9	30.8	3	B
VAL	CA	71	43.9	16.9	31.1	1	B
VAL	CB	71	44.6	18.2	31.4	1	B
VAL	CG1	71	43.7	19.2	31.9	4	B
VAL	CG2	71	45.7	18.0	32.3	1	B
VAL	C	71	43.0	17.1	29.8	1	B
VAL	O	71	43.5	17.6	28.8	4	B
ASP	N	72	41.8	16.7	29.9	1	B
ASP	CA	72	40.9	16.7	28.8	1	B
ASP	CB	72	40.5	15.3	28.3	3	B
ASP	CG	72	39.5	15.2	27.2	4	B
ASP	OD1	72	39.3	16.2	26.5	6	B
ASP	OD2	72	38.8	14.2	27.1	3	B
ASP	C	72	39.6	17.5	29.1	1	B
ASP	O	72	38.7	16.9	29.8	4	B
THR	N	73	39.4	18.7	28.6	1	B
THR	CA	73	38.2	19.4	28.8	1	B
THR	CB	73	38.5	20.9	28.7	1	B
THR	OG1	73	39.1	21.2	27.5	1	B
THR	CG2	73	39.4	21.4	29.8	1	B
THR	C	73	37.1	19.1	27.8	1	B
THR	O	73	36.1	19.8	27.6	2	B
GLY	N	74	37.2	17.9	27.2	1	B
GLY	CA	74	36.2	17.4	26.3	1	B
GLY	C	74	35.4	16.2	26.7	1	B
GLY	O	74	34.7	15.6	25.9	1	B
SER	N	75	35.6	15.8	27.9	1	B
SER	CA	75	34.8	14.7	28.5	1	B
SER	CB	75	35.6	13.4	28.2	4	B
SER	OG	75	36.8	13.3	29.0	4	B
SER	C	75	34.6	14.9	30.0	1	B
SER	O	75	35.2	15.8	30.5	1	B
SER	N	76	33.9	14.0	30.6	1	B
SER	CA	76	33.7	14.1	32.0	1	B
SER	CB	76	32.3	14.7	32.3	1	B
SER	OG	76	32.3	16.1	32.0	3	B
SER	C	76	33.9	12.9	32.8	1	B
SER	O	76	33.3	12.7	33.9	2	B
ASN	N	77	34.8	12.0	32.4	1	B
ASN	CA	77	35.1	10.8	33.2	2	B
ASN	CB	77	34.8	9.6	32.4	5	B
ASN	CG	77	33.3	9.4	32.1	5	B
ASN	OD1	77	32.8	10.1	31.2	8	B
ASN	ND2	77	32.7	8.5	32.8	5	B
ASN	C	77	36.5	10.9	33.6	5	B
ASN	O	77	37.4	11.3	32.9	4	B
PHE	N	78	36.7	10.4	34.8	5	B
PHE	CA	78	38.1	10.3	35.4	3	B
PHE	CB	78	38.1	10.8	36.9	1	B
PHE	CG	78	39.4	10.6	37.5	2	B
PHE	CD1	78	39.5	10.5	38.9	3	B
PHE	CD2	78	40.6	10.4	36.8	3	B
PHE	CE1	78	40.7	10.4	39.6	2	B
PHE	CE2	78	41.8	10.3	37.4	3	B
PHE	CZ	78	41.9	10.2	38.8	2	B
PHE	C	78	38.3	8.8	35.3	5	B
PHE	O	78	37.6	8.0	36.0	7	B
ALA	N	79	39.2	8.4	34.4	6	B
ALA	CA	79	39.5	7.0	34.2	6	B
ALA	CB	79	38.8	6.5	32.9	3	B
ALA	C	79	41.0	6.8	34.1	7	B
ALA	O	79	41.7	7.7	33.9	7	B
VAL	N	80	41.4	5.6	34.4	7	B
VAL	CA	80	42.8	5.2	34.4	9	B
VAL	CB	80	43.5	5.5	35.8	10	B
VAL	CG1	80	43.2	6.9	36.3	12	B
VAL	CG2	80	43.0	4.5	36.8	11	B
VAL	C	80	43.0	3.8	34.0	8	B
VAL	O	80	42.1	3.0	34.2	7	B
GLY	N	81	44.2	3.4	33.6	8	B
GLY	CA	81	44.5	2.0	33.2	10	B
GLY	C	81	44.5	1.2	34.5	12	B
GLY	O	81	45.1	1.6	35.5	14	B
ALA	N	82	43.8	0.1	34.5	15	B
ALA	CA	82	43.8	−0.8	35.6	17	B
ALA	CB	82	42.4	−0.8	36.2	16	B
ALA	C	82	44.2	−2.2	35.4	20	B
ALA	O	82	43.8	−3.2	36.0	24	B
ALA	N	83	45.2	−2.4	34.5	21	B
ALA	CA	83	45.7	−3.7	34.1	20	B
ALA	CB	83	44.6	−4.7	33.7	21	B
ALA	C	83	46.7	−3.6	33.0	22	B
ALA	O	83	46.5	−2.9	32.0	21	B
PRO	N	84	47.9	−4.2	33.1	23	B
PRO	CD	84	48.0	−5.5	33.9	24	B
PRO	CA	84	49.0	−4.2	32.1	23	B
PRO	CB	84	49.8	−5.4	32.4	27	B
PRO	CG	84	48.8	−6.4	33.0	24	B
PRO	C	84	48.5	−4.1	30.7	22	B
PRO	O	84	47.6	−4.8	30.2	17	B
HIS	N	85	49.1	−3.2	29.9	22	B
HIS	CA	85	48.8	−3.0	28.5	21	B
HIS	CB	85	47.8	−1.8	28.4	20	B
HIS	CG	85	47.6	−1.4	27.0	22	B
HIS	CD2	85	46.4	−1.4	26.2	22	B
HIS	ND1	85	48.6	−1.0	26.1	22	B
HIS	CE1	85	48.0	−0.7	24.9	22	B
HIS	NE2	85	46.7	−1.0	25.0	21	B
HIS	C	85	50.1	−2.6	27.8	21	B
HIS	O	85	51.0	−1.9	28.3	19	B
PRO	N	86	50.3	−3.2	26.6	20	B
PRO	CD	86	49.3	−4.1	25.9	19	B
PRO	CA	86	51.5	−3.1	25.8	19	B
PRO	CB	86	51.0	−3.4	24.4	18	B
PRO	CG	86	50.1	−4.5	24.7	19	B
PRO	C	86	52.2	−1.7	25.9	20	B
PRO	O	86	53.4	−1.6	25.7	22	B
PHE	N	87	51.4	−0.7	26.1	20	B
PHE	CA	87	52.0	0.7	26.1	20	B
PHE	CB	87	51.2	1.6	25.3	18	B
PHE	CG	87	51.2	1.3	23.8	23	B
PHE	CD1	87	50.4	1.9	22.9	25	B
PHE	CD2	87	52.1	0.3	23.3	25	B
PHE	CE1	87	50.5	1.6	21.5	24	B
PHE	CE2	87	52.2	0.0	22.0	28	B
PHE	CZ	87	51.4	0.6	21.1	25	B
PHE	C	87	52.1	1.3	27.6	21	B
PHE	O	87	53.1	2.0	27.9	24	B
LEU	N	88	51.2	0.9	28.4	20	B
LEU	CA	88	51.2	1.4	29.8	19	B
LEU	CB	88	50.0	0.9	30.5	24	B
LEU	CG	88	48.6	1.6	30.2	22	B
LEU	CD1	88	47.5	1.1	31.1	24	B
LEU	CD2	88	48.8	3.1	30.4	21	B
LEU	C	88	52.5	1.0	30.6	19	B
LEU	O	88	52.8	−0.2	30.8	16	B
HIS	N	89	53.2	2.0	31.0	19	B
HIS	CA	89	54.4	1.8	31.8	21	B
HIS	CB	89	55.2	3.1	31.9	24	B
HIS	CG	89	55.8	3.6	30.7	32	B
HIS	CD2	89	55.9	4.8	30.1	33	B
HIS	ND1	89	56.6	2.7	29.9	36	B
HIS	CE1	89	57.1	3.4	28.9	36	B
HIS	NE2	89	56.6	4.7	28.9	36	B
HIS	C	89	54.0	1.3	33.2	19	B
HIS	O	89	54.8	0.6	33.8	19	B
ARG	N	90	52.9	1.8	33.7	18	B
ARG	CA	90	52.3	1.4	35.0	18	B
ARG	CB	90	52.9	2.3	36.1	16	B
ARG	CG	90	52.7	3.8	35.9	18	B
ARG	CD	90	53.2	4.5	37.1	26	B
ARG	NE	90	53.3	6.0	36.9	27	B
ARG	CZ	90	53.7	6.8	37.8	27	B
ARG	NH1	90	54.1	6.4	39.0	29	B
ARG	NH2	90	53.8	8.1	37.6	26	B
ARG	C	90	50.8	1.5	34.9	18	B
ARG	O	90	50.3	2.0	34.0	16	B
TYR	N	91	50.2	1.0	36.0	17	B
TYR	CA	91	48.7	1.1	36.1	16	B
TYR	CB	91	48.0	−0.1	35.3	15	B
TYR	CG	91	48.3	−1.4	35.9	19	B
TYR	CD1	91	47.6	−1.9	36.9	22	B
TYR	CE1	91	47.8	−3.2	37.4	27	B
TYR	CD2	91	49.3	−2.2	35.3	22	B
TYR	CE2	91	49.6	−3.5	35.8	26	B
TYR	CZ	91	48.8	−4.0	36.9	28	B
TYR	OH	91	49.0	−5.3	37.4	28	B
TYR	C	91	48.2	1.2	37.5	12	B
TYR	O	91	48.9	1.2	38.5	13	B
TYR	N	92	46.8	1.3	37.6	10	B
TYR	CA	92	46.2	1.4	38.9	7	B
TYR	CB	92	44.9	2.3	38.8	6	B
TYR	CG	92	44.0	2.4	40.0	6	B
TYR	CD1	92	44.5	2.5	41.3	7	B
TYR	CE1	92	43.7	2.7	42.4	5	B
TYR	CD2	92	42.6	2.4	39.8	5	B
TYR	CE2	92	41.8	2.5	40.9	5	B
TYR	CZ	92	42.3	2.6	42.2	4	B
TYR	OH	92	41.5	2.8	43.3	5	B
TYR	C	92	45.9	0.1	39.6	8	B
TYR	O	92	45.0	−0.7	39.1	8	B
GLN	N	93	46.6	−0.2	40.6	8	B
GLN	CA	93	46.3	−1.5	41.3	9	B
GLN	CB	93	47.6	−2.0	42.0	15	B
GLN	CG	93	48.7	−2.4	40.9	17	B
GLN	CD	93	50.0	−2.7	41.6	20	B
GLN	OE1	93	50.6	−1.9	42.3	23	B
GLN	NE2	93	50.5	−3.9	41.3	22	B
GLN	C	93	45.3	−1.3	42.4	11	B
GLN	O	93	45.6	−0.7	43.4	12	B
ARG	N	94	44.1	−1.7	42.1	12	B
ARG	CA	94	43.0	−1.6	43.1	14	B
ARG	CB	94	41.6	−2.0	42.4	11	B
ARG	CG	94	41.2	−1.0	41.3	6	B
ARG	CD	94	40.0	−1.5	40.6	10	B
ARG	NE	94	40.3	−2.4	39.4	7	B
ARG	CZ	94	39.4	−2.9	38.7	11	B
ARG	NH1	94	38.1	−2.8	38.9	14	B
ARG	NH2	94	39.8	−3.7	37.6	9	B
ARG	C	94	43.2	−2.4	44.3	14	B
ARG	O	94	43.1	−2.0	45.5	11	B
GLN	N	95	43.5	−3.7	44.1	15	B
GLN	CA	95	43.7	−4.6	45.2	15	B
GLN	CB	95	44.2	−6.0	44.7	19	B
GLN	CG	95	43.3	−6.7	43.8	24	B
GLN	CD	95	43.8	−8.1	43.4	31	B
GLN	OE1	95	43.8	−9.0	44.2	33	B
GLN	NE2	95	44.1	−8.2	42.1	33	B
GLN	C	95	44.7	−4.1	46.3	15	B
GLN	O	95	44.6	−4.5	47.5	15	B
LEU	N	96	45.6	−3.2	45.9	13	B
LEU	CA	96	46.6	−2.6	46.8	14	B
LEU	CB	96	47.9	−2.4	46.1	12	B
LEU	CG	96	48.7	−3.6	45.9	10	B
LEU	CD1	96	49.8	−3.4	44.9	5	B
LEU	CD2	96	49.4	−4.0	47.3	14	B
LEU	C	96	46.1	−1.4	47.5	13	B
LEU	O	96	46.8	−0.8	48.3	16	B
SER	N	97	44.9	−1.0	47.3	15	B
SER	CA	97	44.3	0.2	48.0	17	B
SER	CB	97	43.6	1.1	47.0	16	B
SER	OG	97	43.0	2.2	47.6	20	B
SER	C	97	43.3	−0.2	49.1	19	B
SER	O	97	42.5	−1.1	48.9	23	B
SER	N	98	43.4	0.5	50.2	17	B
SER	CA	98	42.5	0.3	51.3	14	B
SER	CB	98	43.2	0.6	52.6	17	B
SER	OG	98	43.7	1.9	52.6	20	B
SER	C	98	41.2	1.1	51.1	12	B
SER	O	98	40.1	0.6	51.5	14	B
THR	N	99	41.3	2.3	50.6	8	B
THR	CA	99	40.2	3.2	50.4	5	B
THR	CB	99	40.6	4.6	50.5	1	B
THR	OG1	99	41.7	4.8	49.5	1	B
THR	CG2	99	41.1	5.0	51.9	7	B
THR	C	99	39.5	3.0	49.1	7	B
THR	O	99	38.7	3.8	48.8	11	B
TYR	N	100	39.7	1.9	48.4	7	B
TYR	CA	100	39.0	1.6	47.2	3	B
TYR	CB	100	39.7	0.5	46.4	6	B
TYR	CG	100	39.1	0.1	45.1	7	B
TYR	CD1	100	39.1	0.9	44.0	9	B
TYR	CE1	100	38.5	0.5	42.8	13	B
TYR	CD2	100	38.5	−1.2	45.0	6	B
TYR	CE2	100	37.9	−1.6	43.8	12	B
TYR	CZ	100	37.9	−0.7	42.7	13	B
TYR	OH	100	37.3	−1.1	41.5	16	B
TYR	C	100	37.6	1.1	47.4	2	B
TYR	O	100	37.2	0.6	48.5	2	B
ARG	N	101	36.7	1.3	46.4	1	B
ARG	CA	101	35.4	0.9	46.5	3	B
ARG	CB	101	34.4	2.0	47.0	5	B
ARG	CG	101	34.3	2.1	48.5	9	B
ARG	CD	101	33.1	3.1	48.8	12	B
ARG	NE	101	32.9	3.2	50.3	6	B
ARG	CZ	101	33.8	3.5	51.2	4	B
ARG	NH1	101	35.0	3.7	50.8	5	B
ARG	NH2	101	33.4	3.6	52.4	6	B
ARG	C	101	35.0	0.4	45.1	5	B
ARG	O	101	35.8	0.6	44.2	7	B
ASP	N	102	33.8	−0.2	45.0	2	B
ASP	CA	102	33.5	−0.7	43.6	2	B
ASP	CB	102	34.0	−2.2	43.5	1	B
ASP	CG	102	33.3	−3.0	42.4	4	B
ASP	OD1	102	33.4	−2.6	41.3	8	B
ASP	OD2	102	32.8	−4.1	42.8	8	B
ASP	C	102	31.9	−0.7	43.5	4	B
ASP	O	102	31.2	−1.5	44.1	8	B
LEU	N	103	31.4	0.3	42.7	3	B
LEU	CA	103	30.0	0.4	42.5	2	B
LEU	CB	103	29.7	1.8	41.9	1	B
LEU	CG	103	30.5	3.0	42.3	1	B
LEU	CD1	103	31.4	3.4	41.2	1	B
LEU	CD2	103	29.6	4.1	42.7	1	B
LEU	C	103	29.4	−0.7	41.7	4	B
LEU	O	103	28.2	−0.5	41.2	4	B
ARG	N	104	30.1	−1.8	41.5	6	B
ARG	CA	104	29.6	−2.9	40.7	9	B
ARG	CB	104	28.7	−3.8	41.6	13	B
ARG	CG	104	29.5	−4.7	42.6	17	B
ARG	CD	104	28.5	−5.3	43.6	27	B
ARG	NE	104	27.2	−5.8	43.1	32	B
ARG	CZ	104	26.1	−5.2	43.3	34	B
ARG	NH1	104	26.0	−4.1	44.0	30	B
ARG	NH2	104	25.0	−5.8	42.8	36	B
ARG	C	104	28.8	−2.5	39.5	9	B
ARG	O	104	27.6	−2.8	39.4	10	B
LYS	N	105	29.4	−1.7	38.6	10	B
LYS	CA	105	28.8	−1.2	37.4	10	B
LYS	CB	105	27.9	0.0	37.7	11	B
LYS	CG	105	27.1	0.6	36.5	14	B
LYS	CD	105	26.1	1.7	36.9	21	B
LYS	CE	105	26.7	2.9	37.6	27	B
LYS	NZ	105	25.8	4.1	37.8	27	B
LYS	C	105	29.8	−0.8	36.4	7	B
LYS	O	105	30.7	0.0	36.6	2	B
GLY	N	106	29.7	−1.4	35.2	6	B
GLY	CA	106	30.7	−1.2	34.1	8	B
GLY	C	106	30.4	0.1	33.4	6	B
GLY	O	106	29.4	0.7	33.6	7	B
VAL	N	107	31.4	0.5	32.5	4	B
VAL	CA	107	31.2	1.7	31.7	3	B
VAL	CB	107	31.6	2.9	32.5	1	B
VAL	CG1	107	33.1	2.9	32.7	1	B
VAL	CG2	107	31.1	4.2	31.8	4	B
VAL	C	107	31.9	1.6	30.4	4	B
VAL	O	107	33.0	1.0	30.4	1	B
TYR	N	108	31.4	2.1	29.4	8	B
TYR	CA	108	32.0	2.2	28.0	11	B
TYR	CB	108	31.2	1.3	27.0	15	B
TYR	CG	108	31.3	1.7	25.6	14	B
TYR	CD1	108	32.6	1.8	25.0	16	B
TYR	CE1	108	32.8	2.2	23.7	13	B
TYR	CD2	108	30.3	2.0	24.8	16	B
TYR	CE2	108	30.4	2.4	23.5	19	B
TYR	CZ	108	31.7	2.5	22.9	15	B
TYR	OH	108	31.9	2.9	21.6	15	B
TYR	C	108	32.0	3.6	27.6	11	B
TYR	O	108	31.0	4.2	27.4	11	B
VAL	N	109	33.2	4.1	27.4	11	B
VAL	CA	109	33.3	5.5	26.9	10	B
VAL	CB	109	34.1	6.4	28.0	7	B
VAL	CG1	109	34.3	7.7	27.4	4	B
VAL	CG2	109	33.2	6.4	29.2	4	B
VAL	C	109	34.1	5.6	25.6	12	B
VAL	O	109	35.3	5.4	25.5	11	B
PRO	N	110	33.4	6.0	24.5	13	B
PRO	CD	110	31.9	6.0	24.4	14	B
PRO	CA	110	34.0	6.2	23.2	13	B
PRO	CB	110	32.9	5.7	22.3	10	B
PRO	CG	110	31.7	6.3	22.9	9	B
PRO	C	110	34.4	7.6	23.0	14	B
PRO	O	110	33.9	8.5	23.6	12	B
TYR	N	111	35.3	7.8	22.0	15	B
TYR	CA	111	35.7	9.2	21.6	13	B
TYR	CB	111	37.1	9.4	22.3	12	B
TYR	CG	111	37.1	9.3	23.8	8	B
TYR	CD1	111	36.8	10.4	24.6	10	B
TYR	CE1	111	36.9	10.4	26.0	13	B
TYR	CD2	111	37.5	8.2	24.4	11	B
TYR	CE2	111	37.5	8.1	25.8	13	B
TYR	CZ	111	37.2	9.2	26.6	12	B
TYR	OH	111	37.3	9.1	28.0	9	B
TYR	C	111	35.9	9.2	20.1	15	B
TYR	O	111	35.6	8.2	19.4	14	B
THR	N	112	36.2	10.4	19.6	17	B
THR	CA	112	36.4	10.6	18.2	18	B
THR	CB	112	37.0	12.1	17.9	16	B
THR	OG1	112	35.9	13.0	18.0	15	B
THR	CG2	112	37.6	12.1	16.5	15	B
THR	C	112	37.4	9.6	17.7	18	B
THR	O	112	37.2	8.9	16.8	14	B
GLN	N	113	38.5	9.6	18.5	21	B
GLN	CA	113	39.6	8.7	18.2	23	B
GLN	CB	113	40.9	9.4	17.8	29	B
GLN	CG	113	40.9	10.0	16.3	33	B
GLN	CD	113	41.0	8.9	15.3	34	B
GLN	OE1	113	41.9	8.1	15.3	33	B
GLN	NE2	113	40.1	9.0	14.3	35	B
GLN	C	113	39.9	8.0	19.6	19	B
GLN	O	113	40.5	8.6	20.5	18	B
GLY	N	114	39.3	6.8	19.7	18	B
GLY	CA	114	39.5	6.1	21.0	19	B
GLY	C	114	38.3	5.5	21.7	18	B
GLY	O	114	37.2	6.0	21.4	17	B
LYS	N	115	38.5	4.5	22.5	18	B
LYS	CA	115	37.4	3.9	23.3	20	B
LYS	CB	115	36.4	3.2	22.3	22	B
LYS	CG	115	37.1	2.1	21.4	30	B
LYS	CD	115	36.1	1.1	20.9	33	B
LYS	CE	115	35.0	1.7	19.9	35	B
LYS	NZ	115	34.1	0.7	19.4	35	B
LYS	C	115	37.9	2.9	24.3	18	B
LYS	O	115	38.9	2.2	24.1	17	B
TRP	N	116	37.3	2.9	25.4	15	B
TRP	CA	116	37.6	2.0	26.5	13	B
TRP	CB	116	38.7	2.6	27.4	11	B
TRP	CG	116	38.4	4.0	27.9	9	B
TRP	CD2	116	37.5	4.3	28.9	6	B
TRP	CE2	116	37.6	5.7	29.1	6	B
TRP	CE3	116	36.6	3.6	29.7	2	B
TRP	CD1	116	39.0	5.1	27.5	7	B
TRP	NE1	116	38.5	6.2	28.2	4	B
TRP	CZ2	116	36.8	6.4	30.0	1	B
TRP	CZ3	116	35.9	4.3	30.7	1	B
TRP	CH2	116	36.0	5.7	30.8	1	B
TRP	C	116	36.4	1.6	27.3	13	B
TRP	O	116	35.5	2.4	27.5	13	B
GLU	N	117	36.5	0.4	27.9	15	B
GLU	CA	117	35.5	−0.2	28.7	13	B
GLU	CB	117	35.0	−1.5	28.1	16	B
GLU	CG	117	34.8	−2.7	29.0	28	B
GLU	CD	117	33.6	−2.7	29.9	37	B
GLU	OE1	117	32.5	−2.6	29.3	42	B
GLU	OE2	117	33.7	−2.9	31.1	41	B
GLU	C	117	36.1	−0.5	30.1	12	B
GLU	O	117	37.2	−1.0	30.1	13	B
GLY	N	118	35.4	−0.1	31.2	11	B
GLY	CA	118	36.0	−0.3	32.5	12	B
GLY	C	118	35.1	−0.7	33.6	15	B
GLY	O	118	33.9	−0.9	33.4	15	B
GLU	N	119	35.6	−0.7	34.8	16	B
GLU	CA	119	34.8	−1.0	36.0	18	B
GLU	CB	119	35.3	−2.3	36.7	21	B
GLU	CG	119	35.3	−3.5	35.7	28	B
GLU	CD	119	36.1	−4.7	36.2	30	B
GLU	OE1	119	36.1	−5.8	35.5	28	B
GLU	OE2	119	36.8	−4.6	37.3	33	B
GLU	C	119	34.7	0.2	37.0	15	B
GLU	O	119	35.7	0.6	37.5	15	B
LEU	N	120	33.5	0.7	37.2	15	B
LEU	CA	120	33.3	1.8	38.1	14	B
LEU	CB	120	31.9	2.4	37.9	9	B
LEU	CG	120	31.6	3.1	36.6	8	B
LEU	CD1	120	30.1	3.5	36.5	7	B
LEU	CD2	120	32.5	4.3	36.4	9	B
LEU	C	120	33.5	1.6	39.6	15	B
LEU	O	120	33.0	0.6	40.1	17	B
GLY	N	121	34.3	2.4	40.2	13	B
GLY	CA	121	34.5	2.3	41.6	12	B
GLY	C	121	34.8	3.7	42.1	12	B
GLY	O	121	34.4	4.7	41.5	13	B
THR	N	122	35.4	3.9	43.3	11	B
THR	CA	122	35.7	5.2	43.9	11	B
THR	CB	122	34.5	5.7	44.8	9	B
THR	OG1	122	34.5	5.1	46.1	10	B
THR	CG2	122	33.2	5.5	44.2	6	B
THR	C	122	37.0	5.0	44.7	12	B
THR	O	122	37.5	3.9	44.9	14	B
ASP	N	123	37.5	6.2	45.1	12	B
ASP	CA	123	38.7	6.2	45.9	9	B
ASP	CB	123	39.8	5.5	45.1	11	B
ASP	CG	123	40.8	4.8	46.0	11	B
ASP	OD1	123	41.3	5.4	47.0	16	B
ASP	OD2	123	41.1	3.6	45.7	10	B
ASP	C	123	39.2	7.6	46.2	8	B
ASP	O	123	38.5	8.6	45.8	9	B
LEU	N	124	40.2	7.7	47.0	6	B
LEU	CA	124	40.8	9.0	47.3	6	B
LEU	CB	124	41.5	9.0	48.7	9	B
LEU	CG	124	40.6	8.6	49.9	9	B
LEU	CD1	124	41.5	8.5	51.2	10	B
LEU	CD2	124	39.5	9.5	50.0	10	B
LEU	C	124	41.7	9.5	46.3	4	B
LEU	O	124	42.7	8.8	45.9	1	B
VAL	N	125	41.5	10.7	45.8	4	B
VAL	CA	125	42.4	11.3	44.8	8	B
VAL	CB	125	41.5	11.6	43.5	11	B
VAL	CG1	125	42.4	12.3	42.5	8	B
VAL	CG2	125	40.9	10.4	42.9	7	B
VAL	C	125	43.1	12.5	45.3	10	B
VAL	O	125	42.6	13.3	46.1	8	B
SER	N	126	44.3	12.7	44.7	11	B
SER	CA	126	45.1	13.9	45.1	13	B
SER	CB	126	46.1	13.5	46.2	11	B
SER	OG	126	45.6	13.7	47.5	13	B
SER	C	126	45.9	14.4	43.9	14	B
SER	O	126	46.1	13.7	42.9	12	B
ILE	N	127	46.2	15.7	44.0	15	B
ILE	CA	127	47.0	16.3	42.9	14	B
ILE	CB	127	46.2	17.4	42.2	15	B
ILE	CG2	127	47.1	18.2	41.2	10	B
ILE	CG1	127	45.0	16.8	41.5	15	B
ILE	CD1	127	44.1	17.8	40.8	16	B
ILE	C	127	48.2	16.9	43.6	14	B
ILE	O	127	48.2	18.0	44.1	14	B
PRO	N	128	49.4	16.2	43.5	11	B
PRO	CD	128	49.5	14.9	42.8	11	B
PRO	CA	128	50.7	16.6	44.1	8	B
PRO	CB	128	51.7	15.7	43.4	7	B
PRO	CG	128	50.9	14.4	43.3	9	B
PRO	C	128	51.0	18.1	43.9	7	B
PRO	O	128	51.2	18.8	44.9	6	B
HIS	N	129	51.0	18.5	42.7	6	B
HIS	CA	129	51.3	19.9	42.4	4	B
HIS	CB	129	52.2	20.0	41.2	4	B
HIS	CG	129	53.5	19.2	41.3	4	B
HIS	CD2	129	54.0	18.2	40.5	4	B
HIS	ND1	129	54.3	19.2	42.4	3	B
HIS	CE1	129	55.3	18.4	42.3	6	B
HIS	NE2	129	55.1	17.7	41.2	10	B
HIS	C	129	50.0	20.7	42.1	3	B
HIS	O	129	49.9	21.3	41.1	1	B
GLY	N	130	49.1	20.6	43.1	1	B
GLY	CA	130	47.9	21.3	43.0	1	B
GLY	C	130	47.5	21.7	44.4	1	B
GLY	O	130	48.4	21.7	45.2	1	B
PRO	N	131	46.3	22.0	44.7	5	B
PRO	CD	131	45.1	22.1	43.8	8	B
PRO	CA	131	45.9	22.4	46.0	10	B
PRO	CB	131	44.4	22.7	45.9	10	B
PRO	CG	131	44.0	22.0	44.7	6	B
PRO	C	131	46.1	21.2	47.0	11	B
PRO	O	131	45.8	20.0	46.7	12	B
ASN	N	132	46.6	21.5	48.2	15	B
ASN	CA	132	46.9	20.5	49.2	21	B
ASN	CB	132	47.7	21.1	50.4	29	B
ASN	CG	132	48.2	20.1	51.3	34	B
ASN	OD1	132	48.9	20.4	52.3	38	B
ASN	ND2	132	47.7	18.8	51.2	37	B
ASN	C	132	45.6	19.9	49.7	21	B
ASN	O	132	45.2	20.2	50.9	25	B
VAL	N	133	44.9	19.0	48.9	18	B
VAL	CA	133	43.7	18.4	49.3	17	B
VAL	CB	133	42.4	19.1	48.9	16	B
VAL	CG1	133	42.4	20.5	49.5	16	B
VAL	CG2	133	42.4	19.2	47.4	16	B
VAL	C	133	43.6	17.0	48.8	15	B
VAL	O	133	44.3	16.6	47.9	14	B
THR	N	134	42.6	16.2	49.3	13	B
THR	CA	134	42.3	14.9	48.9	10	B
THR	CB	134	42.9	13.8	49.9	9	B
THR	OG1	134	44.3	13.8	49.7	9	B
THR	CG2	134	42.3	12.4	49.6	8	B
THR	C	134	40.8	14.7	48.9	11	B
THR	O	134	40.1	15.1	49.9	10	B
VAL	N	135	40.2	14.2	47.8	9	B
VAL	CA	135	38.8	14.0	47.7	8	B
VAL	CB	135	38.1	15.0	46.6	10	B
VAL	CG1	135	38.3	16.4	47.0	15	B
VAL	CG2	135	38.8	14.7	45.3	7	B
VAL	C	135	38.5	12.6	47.3	8	B
VAL	O	135	39.3	11.9	46.7	11	B
ARG	N	136	37.2	12.2	47.5	6	B
ARG	CA	136	36.8	10.8	47.1	4	B
ARG	CB	136	35.9	10.2	48.2	7	B
ARG	CG	136	35.4	8.8	47.7	8	B
ARG	CD	136	34.7	8.1	48.9	12	B
ARG	NE	136	35.7	7.7	50.0	14	B
ARG	CZ	136	36.6	6.8	49.9	15	B
ARG	NH1	136	36.7	6.1	48.8	12	B
ARG	NH2	136	37.4	6.5	50.9	16	B
ARG	C	136	36.1	11.1	45.9	5	B
ARG	O	136	35.1	11.8	45.9	7	B
ALA	N	137	36.6	10.5	44.8	4	B
ALA	CA	137	35.9	10.8	43.5	5	B
ALA	CB	137	36.8	11.6	42.6	6	B
ALA	C	137	35.6	9.5	42.8	3	B
ALA	O	137	36.0	8.4	43.2	1	B
ASN	N	138	34.9	9.5	41.7	5	B
ASN	CA	138	34.5	8.3	40.9	6	B
ASN	CB	138	33.3	8.6	40.1	7	B
ASN	CG	138	32.1	8.7	40.9	10	B
ASN	OD1	138	31.8	8.0	41.9	10	B
ASN	ND2	138	31.3	9.7	40.6	15	B
ASN	C	138	35.7	8.1	40.0	7	B
ASN	O	138	36.3	9.0	39.4	10	B
ILE	N	139	36.1	6.8	39.9	6	B
ILE	CA	139	37.2	6.4	39.1	3	B
ILE	CB	139	38.5	6.2	39.9	2	B
ILE	CG2	139	39.7	6.0	38.9	1	B
ILE	CG1	139	38.8	7.3	40.9	5	B
ILE	CD1	139	40.1	7.1	41.6	8	B
ILE	C	139	36.9	5.2	38.3	3	B
ILE	O	139	36.7	4.1	38.8	4	B
ALA	N	140	36.9	5.3	37.0	5	B
ALA	CA	140	36.6	4.2	36.1	7	B
ALA	CB	140	36.1	4.7	34.8	9	B
ALA	C	140	37.9	3.5	35.9	7	B
ALA	O	140	38.8	4.0	35.3	5	B
ALA	N	141	37.9	2.2	36.4	10	B
ALA	CA	141	39.1	1.4	36.3	7	B
ALA	CB	141	39.1	0.3	37.3	7	B
ALA	C	141	39.0	0.8	34.9	9	B
ALA	O	141	38.2	−0.1	34.6	8	B
ILE	N	142	39.8	1.3	33.9	8	B
ILE	CA	142	39.9	0.8	32.6	7	B
ILE	CB	142	40.7	1.7	31.7	4	B
ILE	CG2	142	40.8	1.1	30.3	6	B
ILE	CG1	142	39.9	3.0	31.5	6	B
ILE	CD1	142	40.6	4.0	30.6	4	B
ILE	C	142	40.4	−0.6	32.5	10	B
ILE	O	142	41.6	−0.9	32.7	14	B
THR	N	143	39.5	−1.6	32.1	13	B
THR	CA	143	39.9	−3.0	32.0	16	B
THR	CB	143	38.7	−3.9	32.6	20	B
THR	OG1	143	37.5	−3.4	32.0	20	B
THR	CG2	143	38.7	−3.8	34.1	22	B
THR	C	143	40.2	−3.4	30.6	17	B
THR	O	143	40.9	−4.3	30.3	18	B
GLU	N	144	39.6	−2.7	29.6	21	B
GLU	CA	144	39.8	−3.0	28.2	25	B
GLU	CB	144	38.6	−3.7	27.7	31	B
GLU	CG	144	38.7	−4.3	26.3	35	B
GLU	CD	144	37.6	−5.3	25.9	42	B
GLU	OE1	144	37.6	−6.4	26.6	41	B
GLU	OE2	144	36.8	−5.1	25.0	44	B
GLU	C	144	39.9	−1.7	27.5	25	B
GLU	O	144	39.2	−0.7	27.8	26	B
SER	N	145	40.9	−1.6	26.6	26	B
SER	CA	145	41.2	−0.4	25.9	28	B
SER	CB	145	42.4	0.3	26.6	31	B
SER	OG	145	43.3	−0.6	27.2	33	B
SER	C	145	41.5	−0.6	24.4	27	B
SER	O	145	42.1	−1.7	24.0	28	B
ASP	N	146	41.2	0.3	23.6	23	B
ASP	CA	146	41.5	0.2	22.1	21	B
ASP	CB	146	40.4	−0.6	21.5	22	B
ASP	CG	146	40.5	−0.7	20.0	19	B
ASP	OD1	146	41.6	−1.0	19.5	19	B
ASP	OD2	146	39.5	−0.4	19.3	19	B
ASP	C	146	41.5	1.6	21.4	19	B
ASP	O	146	40.6	2.3	21.4	17	B
LYS	N	147	42.7	1.9	20.9	15	B
LYS	CA	147	42.9	3.2	20.2	12	B
LYS	CB	147	41.8	3.4	19.1	14	B
LYS	CG	147	41.8	2.4	18.1	19	B
LYS	CD	147	42.8	2.6	17.0	19	B
LYS	CE	147	42.6	1.7	15.8	19	B
LYS	NZ	147	43.7	1.8	14.8	18	B
LYS	C	147	42.9	4.4	21.1	14	B
LYS	O	147	42.7	5.5	20.7	12	B
PHE	N	148	43.1	4.1	22.4	15	B
PHE	CA	148	43.1	5.1	23.5	15	B
PHE	CB	148	42.3	4.7	24.7	11	B
PHE	CG	148	42.0	5.8	25.7	5	B
PHE	CD1	148	41.1	6.7	25.4	3	B
PHE	CD2	148	42.7	5.8	26.9	2	B
PHE	CE1	148	40.8	7.7	26.4	2	B
PHE	CE2	148	42.4	6.7	27.9	1	B
PHE	CZ	148	41.4	7.7	27.6	1	B
PHE	C	148	44.6	5.4	23.9	15	B
PHE	O	148	45.2	6.4	23.5	15	B
PHE	N	149	45.1	4.6	24.8	15	B
PHE	CA	149	46.5	4.7	25.2	14	B
PHE	CB	149	46.8	3.6	26.2	13	B
PHE	CG	149	45.9	3.5	27.4	11	B
PHE	CD1	149	45.4	2.3	27.9	8	B
PHE	CD2	149	45.7	4.7	28.1	11	B
PHE	CE1	149	44.7	2.2	29.0	10	B
PHE	CE2	149	44.9	4.6	29.3	11	B
PHE	CZ	149	44.4	3.4	29.7	14	B
PHE	C	149	47.5	4.7	24.1	15	B
PHE	O	149	47.5	3.8	23.3	17	B
ILE	N	150	48.3	5.8	24.0	15	B
ILE	CA	150	49.2	5.9	22.9	15	B
ILE	CB	150	49.4	7.4	22.5	12	B
ILE	CG2	150	50.3	7.5	21.4	13	B
ILE	CG1	150	48.0	8.0	22.2	11	B
ILE	CD1	150	48.0	9.4	21.9	8	B
ILE	C	150	50.6	5.4	23.3	19	B
ILE	O	150	51.0	5.5	24.4	20	B
ASN	N	151	51.3	4.8	22.3	23	B
ASN	CA	151	52.7	4.2	22.6	24	B
ASN	CB	151	53.2	3.5	21.5	25	B
ASN	CG	151	54.4	2.6	21.9	31	B
ASN	OD1	151	55.0	1.8	21.0	35	B
ASN	ND2	151	54.8	2.7	23.1	31	B
ASN	C	151	53.6	5.3	23.1	24	B
ASN	O	151	54.0	6.2	22.3	19	B
GLY	N	152	54.0	5.2	24.3	24	B
GLY	CA	152	55.0	6.2	24.9	26	B
GLY	C	152	54.4	7.6	25.1	25	B
GLY	O	152	55.2	8.6	25.0	25	B
SER	N	153	53.1	7.7	25.3	23	B
SER	CA	153	52.5	9.0	25.5	21	B
SER	CB	153	50.9	8.9	25.5	25	B
SER	OG	153	50.5	8.1	26.6	30	B
SER	C	153	52.9	9.5	26.9	19	B
SER	O	153	53.0	10.7	27.1	17	B
ASN	N	154	53.1	8.6	27.8	17	B
ASN	CA	154	53.5	8.8	29.1	16	B
ASN	CB	154	54.6	9.9	29.2	19	B
ASN	CG	154	55.5	9.7	30.5	24	B
ASN	OD1	154	55.9	8.6	30.8	24	B
ASN	ND2	154	55.7	10.9	31.2	26	B
ASN	C	154	52.4	9.2	30.1	11	B
ASN	O	154	52.6	9.6	31.2	11	B
TRP	N	155	51.2	9.0	29.6	9	B
TRP	CA	155	50.0	9.2	30.5	7	B
TRP	CB	155	49.1	10.4	30.1	6	B
TRP	CG	155	48.7	10.4	28.6	5	B
TRP	CD2	155	47.5	9.8	28.1	4	B
TRP	CE2	155	47.5	10.1	26.7	2	B
TRP	CE3	155	46.6	8.9	28.6	8	B
TRP	CD1	155	49.3	11.1	27.6	6	B
TRP	NE1	155	48.5	11.0	26.5	2	B
TRP	CZ2	155	46.5	9.7	25.9	2	B
TRP	CZ3	155	45.6	8.5	27.8	8	B
TRP	CH2	155	45.5	8.9	26.4	8	B
TRP	C	155	49.3	7.9	30.6	7	B
TRP	O	155	49.2	7.2	29.6	11	B
GLU	N	156	48.8	7.6	31.8	6	B
GLU	CA	156	48.0	6.3	31.9	6	B
GLU	CB	156	48.7	5.5	33.0	10	B
GLU	CG	156	50.2	5.3	32.8	20	B
GLU	CD	156	51.0	6.4	33.4	26	B
GLU	OE1	156	52.3	6.4	33.2	28	B
GLU	OE2	156	50.5	7.3	34.0	29	B
GLU	C	156	46.6	6.5	32.3	6	B
GLU	O	156	45.9	5.6	32.8	10	B
GLY	N	157	46.1	7.7	32.1	3	B
GLY	CA	157	44.7	8.0	32.5	1	B
GLY	C	157	44.2	9.3	31.9	3	B
GLY	O	157	44.9	10.0	31.2	1	B
ILE	N	158	42.9	9.5	32.1	5	B
ILE	CA	158	42.3	10.8	31.6	4	B
ILE	CB	158	41.4	10.4	30.3	1	B
ILE	CG2	158	40.4	9.5	30.7	2	B
ILE	CG1	158	40.8	11.7	29.8	5	B
ILE	CD1	158	39.9	11.4	28.6	7	B
ILE	C	158	41.4	11.4	32.6	4	B
ILE	O	158	40.7	10.8	33.4	4	B
LEU	N	159	41.4	12.8	32.7	5	B
LEU	CA	159	40.7	13.6	33.6	4	B
LEU	CB	159	41.6	14.4	34.5	4	B
LEU	CG	159	41.0	15.4	35.6	1	B
LEU	CD1	159	40.4	14.6	36.7	1	B
LEU	CD2	159	42.0	16.3	36.1	1	B
LEU	C	159	39.7	14.5	32.9	3	B
LEU	O	159	40.1	15.6	32.5	1	B
GLY	N	160	38.4	14.1	32.8	3	B
GLY	CA	160	37.5	14.9	32.1	4	B
GLY	C	160	37.0	16.0	33.0	3	B
GLY	O	160	36.3	15.8	34.0	7	B
LEU	N	161	37.4	17.3	32.6	1	B
LEU	CA	161	37.0	18.4	33.4	1	B
LEU	CB	161	38.2	19.4	33.3	1	B
LEU	CG	161	39.5	18.9	34.0	1	B
LEU	CD1	161	40.6	19.9	33.7	1	B
LEU	CD2	161	39.2	18.9	35.5	1	B
LEU	C	161	35.7	19.1	32.9	1	B
LEU	O	161	35.4	20.1	33.4	1	B
ALA	N	162	35.1	18.4	32.0	3	B
ALA	CA	162	33.8	19.0	31.5	1	B
ALA	CB	162	33.4	18.2	30.2	3	B
ALA	C	162	32.7	18.8	32.5	1	B
ALA	O	162	33.0	18.6	33.7	1	B
TYR	N	163	31.5	19.0	32.1	1	B
TYR	CA	163	30.4	18.9	33.1	2	B
TYR	CB	163	29.3	19.9	32.7	4	B
TYR	CG	163	29.8	21.3	32.9	1	B
TYR	CD1	163	30.6	21.9	31.9	1	B
TYR	CE1	163	31.0	23.3	32.0	1	B
TYR	CD2	163	29.4	22.1	33.9	1	B
TYR	CE2	163	29.8	23.4	34.1	3	B
TYR	CZ	163	30.6	24.0	33.1	2	B
TYR	OH	163	30.9	25.3	33.3	4	B
TYR	C	163	29.7	17.5	33.0	3	B
TYR	O	163	29.9	16.7	32.1	4	B
ALA	N	164	29.0	17.1	34.1	6	B
ALA	CA	164	28.3	15.8	34.2	5	B
ALA	CB	164	27.6	15.7	35.5	8	B
ALA	C	164	27.4	15.5	33.1	3	B
ALA	O	164	27.2	14.3	32.8	4	B
GLU	N	165	26.7	16.5	32.5	5	B
GLU	CA	165	25.7	16.3	31.5	6	B
GLU	CB	165	25.4	17.6	30.9	9	B
GLU	CG	165	24.5	17.5	29.6	15	B
GLU	CD	165	23.0	17.6	29.9	20	B
GLU	OE1	165	22.6	18.7	30.3	28	B
GLU	OE2	165	22.3	16.6	29.7	17	B
GLU	C	165	26.2	15.3	30.4	4	B
GLU	O	165	25.4	14.6	29.8	3	B
ILE	N	166	27.5	15.2	30.1	1	B
ILE	CA	166	28.0	14.3	29.1	1	B
ILE	CB	166	28.9	15.0	28.1	1	B
ILE	CG2	166	28.1	16.2	27.4	2	B
ILE	CG1	166	30.2	15.5	28.8	1	B
ILE	CD1	166	31.2	16.1	27.8	1	B
ILE	C	166	28.8	13.2	29.7	3	B
ILE	O	166	29.5	12.5	28.9	5	B
ALA	N	167	28.7	13.0	31.0	3	B
ALA	CA	167	29.5	11.9	31.6	5	B
ALA	CB	167	29.7	12.2	33.0	7	B
ALA	C	167	28.8	10.6	31.4	6	B
ALA	O	167	27.6	10.5	31.6	7	B
ARG	N	168	29.6	9.5	31.1	5	B
ARG	CA	168	29.0	8.2	30.9	3	B
ARG	CB	168	29.9	7.4	30.0	7	B
ARG	CG	168	30.0	8.0	28.6	11	B
ARG	CD	168	28.8	7.4	27.7	15	B
ARG	NE	168	28.9	7.9	26.3	17	B
ARG	CZ	168	28.3	7.2	25.3	23	B
ARG	NH1	168	27.7	6.1	25.5	22	B
ARG	NH2	168	28.4	7.7	24.1	22	B
ARG	C	168	29.1	7.5	32.3	2	B
ARG	O	168	30.0	7.8	33.1	1	B
PRO	N	169	28.1	6.6	32.7	1	B
PRO	CD	169	28.2	6.0	34.0	6	B
PRO	CA	169	27.0	6.1	31.9	1	B
PRO	CB	169	26.5	5.0	32.8	3	B
PRO	CG	169	27.7	4.6	33.7	6	B
PRO	C	169	25.9	7.2	31.8	3	B
PRO	O	169	25.3	7.3	30.8	7	B
ASP	N	170	25.7	7.9	32.9	4	B
ASP	CA	170	24.7	9.0	32.9	5	B
ASP	CB	170	23.3	8.5	33.3	6	B
ASP	CG	170	23.3	8.0	34.8	8	B
ASP	OD1	170	23.6	6.8	35.0	9	B
ASP	OD2	170	23.1	8.8	35.7	14	B
ASP	C	170	25.1	10.2	33.7	5	B
ASP	O	170	26.1	10.1	34.4	1	B
ASP	N	171	24.4	11.3	33.6	8	B
ASP	CA	171	24.7	12.5	34.3	11	B
ASP	CB	171	23.8	13.6	33.9	13	B
ASP	CG	171	22.3	13.3	34.2	15	B
ASP	OD1	171	22.0	12.3	34.8	14	B
ASP	OD2	171	21.5	14.2	33.9	17	B
ASP	C	171	24.6	12.4	35.8	12	B
ASP	O	171	24.5	13.4	36.5	13	B
SER	N	172	24.8	11.2	36.4	11	B
SER	CA	172	24.8	11.1	37.8	8	B
SER	CB	172	23.8	9.9	38.2	6	B
SER	OG	172	24.3	8.7	38.0	7	B
SER	C	172	26.2	10.7	38.3	7	B
SER	O	172	26.4	10.7	39.6	11	B
LEU	N	173	27.1	10.4	37.4	4	B
LEU	CA	173	28.4	10.1	37.9	2	B
LEU	CB	173	29.1	9.2	36.8	1	B
LEU	CG	173	30.3	8.4	37.2	1	B
LEU	CD1	173	30.1	7.6	38.4	1	B
LEU	CD2	173	30.8	7.5	36.0	1	B
LEU	C	173	29.2	11.4	38.0	4	B
LEU	O	173	30.0	11.8	37.1	2	B
GLU	N	174	29.0	12.0	39.2	5	B
GLU	CA	174	29.7	13.3	39.5	6	B
GLU	CB	174	29.5	13.6	41.0	8	B
GLU	CG	174	30.2	14.8	41.5	10	B
GLU	CD	174	29.9	15.1	42.9	10	B
GLU	OE1	174	28.7	15.6	43.2	15	B
GLU	OE2	174	30.7	14.9	43.8	10	B
GLU	C	174	31.2	13.3	39.2	5	B
GLU	O	174	32.0	12.6	39.8	8	B
PRO	N	175	31.5	14.2	38.2	3	B
PRO	CD	175	30.5	14.9	37.4	3	B
PRO	CA	175	32.9	14.4	37.6	4	B
PRO	CB	175	32.6	15.5	36.6	3	B
PRO	CG	175	31.2	15.2	36.2	3	B
PRO	C	175	33.9	14.9	38.7	2	B
PRO	O	175	33.6	15.7	39.6	4	B
PHE	N	176	35.2	14.5	38.5	3	B
PHE	CA	176	36.2	14.8	39.5	1	B
PHE	CB	176	37.6	14.7	38.8	1	B
PHE	CG	176	38.7	15.1	39.8	1	B
PHE	CD1	176	39.2	14.2	40.7	5	B
PHE	CD2	176	39.2	16.3	39.7	1	B
PHE	CE1	176	40.2	14.5	41.6	2	B
PHE	CE2	176	40.2	16.7	40.6	2	B
PHE	CZ	176	40.7	15.8	41.5	2	B
PHE	C	176	36.1	16.2	40.0	1	B
PHE	O	176	36.0	16.4	41.2	4	B
PHE	N	177	36.2	17.2	39.1	2	B
PHE	CA	177	36.2	18.6	39.6	3	B
PHE	CB	177	36.2	19.6	38.4	1	B
PHE	CG	177	36.8	20.9	38.7	5	B
PHE	CD1	177	38.2	20.9	38.8	5	B
PHE	CD2	177	36.1	22.0	38.8	3	B
PHE	CE1	177	38.9	22.1	39.1	6	B
PHE	CE2	177	36.8	23.2	39.1	2	B
PHE	CZ	177	38.1	23.3	39.2	4	B
PHE	C	177	35.0	18.9	40.5	5	B
PHE	O	177	35.1	19.4	41.6	1	B
ASP	N	178	33.8	18.5	40.0	7	B
ASP	CA	178	32.5	18.7	40.7	10	B
ASP	CB	178	31.4	18.0	40.0	11	B
ASP	CG	178	30.6	18.9	39.1	16	B
ASP	OD1	178	30.2	20.0	39.6	19	B
ASP	OD2	178	30.4	18.6	37.9	16	B
ASP	C	178	32.7	18.1	42.1	11	B
ASP	O	178	32.3	18.8	43.1	13	B
SER	N	179	33.3	17.0	42.3	9	B
SER	CA	179	33.5	16.4	43.6	7	B
SER	CB	179	34.1	15.0	43.5	4	B
SER	OG	179	33.1	14.1	42.9	7	B
SER	C	179	34.5	17.3	44.3	5	B
SER	O	179	34.3	17.7	45.4	10	B
LEU	N	180	35.6	17.6	43.7	3	B
LEU	CA	180	36.6	18.5	44.3	1	B
LEU	CB	180	37.7	18.9	43.4	1	B
LEU	CG	180	38.8	19.7	44.1	1	B
LEU	CD1	180	39.6	18.8	45.0	1	B
LEU	CD2	180	39.7	20.4	43.1	1	B
LEU	C	180	36.0	19.8	44.9	2	B
LEU	O	180	36.4	20.1	46.1	2	B
VAL	N	181	35.2	20.4	44.2	3	B
VAL	CA	181	34.6	21.7	44.7	4	B
VAL	CB	181	33.9	22.5	43.6	2	B
VAL	CG1	181	33.1	23.6	44.3	7	B
VAL	CG2	181	34.9	23.1	42.7	5	B
VAL	C	181	33.7	21.5	45.9	4	B
VAL	O	181	33.7	22.2	46.9	5	B
LYS	N	182	32.8	20.5	45.8	5	B
LYS	CA	182	31.9	20.2	46.8	3	B
LYS	CB	182	30.8	19.2	46.4	1	B
LYS	CG	182	30.2	19.6	45.1	1	B
LYS	CD	182	29.2	18.5	44.6	3	B
LYS	CE	182	27.8	18.6	45.3	9	B
LYS	NZ	182	27.0	19.8	44.8	12	B
LYS	C	182	32.5	19.7	48.1	2	B
LYS	O	182	32.0	19.9	49.2	1	B
GLN	N	183	33.7	19.1	48.0	1	B
GLN	CA	183	34.4	18.6	49.1	3	B
GLN	CB	183	35.0	17.2	48.8	3	B
GLN	CG	183	34.0	16.1	48.7	9	B
GLN	CD	183	34.6	14.9	48.0	9	B
GLN	OE1	183	35.7	14.4	48.3	10	B
GLN	NE2	183	33.9	14.4	47.0	10	B
GLN	C	183	35.5	19.4	49.8	5	B
GLN	O	183	36.1	19.1	50.8	4	B
THR	N	184	35.9	20.5	49.1	7	B
THR	CA	184	36.9	21.4	49.6	8	B
THR	CB	184	38.3	21.2	49.0	8	B
THR	OG1	184	38.2	21.5	47.6	5	B
THR	CG2	184	38.7	19.7	49.1	7	B
THR	C	184	36.5	22.9	49.4	11	B
THR	O	184	35.4	23.2	48.9	13	B
HIS	N	185	37.4	23.8	49.8	10	B
HIS	CA	185	37.1	25.2	49.6	13	B
HIS	CB	185	37.6	26.0	50.8	16	B
HIS	CG	185	36.8	25.8	52.0	21	B
HIS	CD2	185	35.8	26.5	52.5	23	B
HIS	ND1	185	36.9	24.7	52.8	26	B
HIS	CE1	185	36.0	24.8	53.8	25	B
HIS	NE2	185	35.3	25.9	53.6	27	B
HIS	C	185	37.8	25.8	48.3	10	B
HIS	O	185	37.8	27.0	48.0	12	B
VAL	N	186	38.3	24.8	47.5	8	B
VAL	CA	186	38.9	25.2	46.2	6	B
VAL	CB	186	39.4	24.0	45.4	7	B
VAL	CG1	186	40.0	24.4	44.1	5	B
VAL	CG2	186	40.5	23.2	46.2	7	B
VAL	C	186	37.9	25.9	45.4	3	B
VAL	O	186	36.8	25.4	45.1	3	B
PRO	N	187	38.2	27.2	45.0	1	B
PRO	CD	187	39.3	28.0	45.4	2	B
PRO	CA	187	37.3	28.0	44.2	1	B
PRO	CB	187	38.1	29.1	43.7	3	B
PRO	CG	187	38.9	29.4	45.0	6	B
PRO	C	187	36.8	27.1	43.0	1	B
PRO	O	187	37.4	26.2	42.6	1	B
ASN	N	188	35.6	27.4	42.5	1	B
ASN	CA	188	35.0	26.7	41.4	1	B
ASN	CB	188	33.5	26.7	41.4	1	B
ASN	CG	188	32.9	25.8	40.4	1	B
ASN	OD1	188	33.5	24.9	39.8	1	B
ASN	ND2	188	31.6	26.0	40.1	1	B
ASN	C	188	35.5	27.1	40.0	1	B
ASN	O	188	34.7	27.6	39.2	1	B
LEU	N	189	36.8	26.9	39.7	1	B
LEU	CA	189	37.3	27.3	38.4	1	B
LEU	CB	189	37.1	28.8	38.2	1	B
LEU	CG	189	38.0	29.7	39.0	1	B
LEU	CD1	189	39.2	30.2	38.1	2	B
LEU	CD2	189	37.3	30.9	39.6	2	B
LEU	C	189	38.8	26.9	38.3	1	B
LEU	O	189	39.5	26.9	39.2	3	B
PHE	N	190	39.2	26.7	37.0	1	B
PHE	CA	190	40.6	26.3	36.8	1	B
PHE	CB	190	40.8	24.8	36.6	1	B
PHE	CG	190	40.1	24.2	35.4	1	B
PHE	CD1	190	38.8	23.8	35.4	1	B
PHE	CD2	190	40.8	24.1	34.2	1	B
PHE	CE1	190	38.1	23.3	34.3	1	B
PHE	CE2	190	40.2	23.6	33.1	1	B
PHE	CZ	190	38.8	23.2	33.1	1	B
PHE	C	190	41.0	27.0	35.5	1	B
PHE	O	190	40.2	27.3	34.6	2	B
SER	N	191	42.3	27.2	35.3	2	B
SER	CA	191	42.9	27.9	34.2	2	B
SER	CB	191	43.4	29.3	34.5	3	B
SER	OG	191	44.5	29.2	35.3	9	B
SER	C	191	44.0	27.0	33.6	1	B
SER	O	191	44.8	26.4	34.4	1	B
LEU	N	192	44.1	26.9	32.3	1	B
LEU	CA	192	45.2	26.2	31.6	1	B
LEU	CB	192	44.5	25.0	30.8	1	B
LEU	CG	192	44.0	23.8	31.4	1	B
LEU	CD1	192	43.1	23.0	30.4	1	B
LEU	CD2	192	45.1	22.9	32.0	1	B
LEU	C	192	46.0	27.0	30.7	1	B
LEU	O	192	45.5	27.9	30.0	1	B
GLN	N	193	47.3	26.8	30.8	1	B
GLN	CA	193	48.2	27.5	29.9	1	B
GLN	CB	193	49.2	28.4	30.7	1	B
GLN	CG	193	50.1	29.1	29.8	2	B
GLN	CD	193	51.5	29.4	30.4	4	B
GLN	OE1	193	52.2	28.5	30.8	3	B
GLN	NE2	193	51.9	30.7	30.5	6	B
GLN	C	193	49.0	26.4	29.2	1	B
GLN	O	193	50.0	26.0	29.7	2	B
LEU	N	194	48.5	26.0	28.0	1	B
LEU	CA	194	49.2	25.0	27.3	1	B
LEU	CB	194	48.2	24.2	26.5	1	B
LEU	CG	194	47.1	23.5	27.3	1	B
LEU	CD1	194	46.0	22.9	26.5	1	B
LEU	CD2	194	47.7	22.6	28.3	1	B
LEU	C	194	50.2	25.6	26.4	3	B
LEU	O	194	49.9	26.6	25.7	4	B
CYS	N	195	51.5	25.2	26.5	1	B
CYS	CA	195	52.5	25.8	25.7	3	B
CYS	C	195	53.0	24.7	24.7	7	B
CYS	O	195	53.4	23.6	25.1	8	B
CYS	CB	195	53.7	26.2	26.5	5	B
CYS	SG	195	53.2	27.2	28.0	3	B
GLY	N	196	52.9	25.0	23.4	11	B
GLY	CA	196	53.4	24.1	22.4	12	B
GLY	C	196	54.9	24.1	22.4	14	B
GLY	O	196	55.5	24.8	23.2	10	B
ALA	N	197	55.5	23.3	21.5	16	B
ALA	CA	197	56.9	23.2	21.5	20	B
ALA	CB	197	57.3	21.9	20.9	16	B
ALA	C	197	57.6	24.4	20.7	23	B
ALA	O	197	58.2	25.3	21.3	24	B
GLY	N	198	57.4	24.3	19.4	28	B
GLY	CA	198	58.0	25.3	18.5	31	B
GLY	C	198	59.3	24.7	17.9	32	B
GLY	O	198	59.7	25.0	16.8	32	B
PHE	N	199	59.9	23.8	18.7	34	B
PHE	CA	199	61.1	23.1	18.4	38	B
PHE	CB	199	62.3	23.5	19.3	37	B
PHE	CG	199	62.0	24.7	20.2	36	B
PHE	CD1	199	61.8	25.9	19.6	33	B
PHE	CD2	199	62.0	24.5	21.6	33	B
PHE	CE1	199	61.6	27.0	20.4	34	B
PHE	CE2	199	61.8	25.6	22.4	34	B
PHE	CZ	199	61.6	26.9	21.8	36	B
PHE	C	199	60.7	21.6	18.6	39	B
PHE	O	199	59.8	21.2	19.3	41	B
PRO	N	200	61.4	20.7	17.9	40	B
PRO	CD	200	62.5	20.9	16.8	41	B
PRO	CA	200	61.1	19.3	18.0	40	B
PRO	CB	200	61.9	18.6	16.9	40	B
PRO	CG	200	63.1	19.5	16.7	42	B
PRO	C	200	61.4	18.6	19.4	41	B
PRO	O	200	62.3	19.0	20.1	42	B
LEU	N	201	60.5	17.7	19.7	40	B
LEU	CA	201	60.6	16.9	21.0	34	B
LEU	CB	201	59.8	17.6	22.1	31	B
LEU	CG	201	60.2	18.9	22.7	29	B
LEU	CD1	201	59.5	19.1	24.0	29	B
LEU	CD2	201	61.7	18.9	22.9	25	B
LEU	C	201	60.1	15.5	20.8	34	B
LEU	O	201	58.9	15.3	20.8	32	B
ASN	N	202	61.0	14.5	20.5	33	B
ASN	CA	202	60.6	13.1	20.3	35	B
ASN	CB	202	61.8	12.3	20.0	35	B
ASN	CG	202	62.7	12.0	21.2	40	B
ASN	OD1	202	63.3	13.0	21.7	40	B
ASN	ND2	202	62.9	10.8	21.6	37	B
ASN	C	202	59.9	12.6	21.6	34	B
ASN	O	202	59.3	13.4	22.3	33	B
GLN	N	203	59.9	11.3	21.8	35	B
GLN	CA	203	59.3	10.7	23.0	36	B
GLN	CB	203	59.2	9.2	22.8	34	B
GLN	CG	203	58.4	8.5	24.0	35	B
GLN	CD	203	59.3	8.1	25.2	40	B
GLN	OE1	203	59.5	8.8	26.1	39	B
GLN	NE2	203	59.8	6.8	25.1	38	B
GLN	C	203	60.1	11.0	24.3	36	B
GLN	O	203	59.5	11.4	25.3	38	B
SER	N	204	61.4	10.9	24.2	38	B
SER	CA	204	62.3	11.2	25.3	38	B
SER	CB	204	63.7	10.5	25.1	38	B
SER	OG	204	64.5	10.5	26.3	40	B
SER	C	204	62.5	12.7	25.6	40	B
SER	O	204	63.5	13.1	26.2	39	B
GLU	N	205	61.5	13.5	25.3	41	B
GLU	CA	205	61.6	15.0	25.5	41	B
GLU	CB	205	61.7	15.7	24.2	38	B
GLU	CG	205	63.1	15.6	23.5	42	B
GLU	CD	205	64.2	16.3	24.3	44	B
GLU	OE1	205	64.5	15.9	25.4	44	B
GLU	OE2	205	64.8	17.3	23.7	47	B
GLU	C	205	60.3	15.5	26.3	41	B
GLU	O	205	59.9	16.6	26.2	39	B
VAL	N	206	59.8	14.6	27.2	40	B
VAL	CA	206	58.6	14.9	28.0	37	B
VAL	CB	206	57.4	14.0	27.6	33	B
VAL	CG1	206	56.1	14.7	27.9	32	B
VAL	CG2	206	57.5	13.5	26.2	33	B
VAL	C	206	58.9	14.7	29.5	38	B
VAL	O	206	58.7	15.7	30.3	37	B
LEU	N	207	59.3	13.5	29.8	39	B
LEU	CA	207	59.6	13.1	31.2	38	B
LEU	CB	207	60.1	11.7	31.3	34	B
LEU	CG	207	59.2	10.5	30.7	31	B
LEU	CD1	207	59.4	10.4	29.2	28	B
LEU	CD2	207	59.8	9.2	31.3	27	B
LEU	C	207	60.7	14.0	31.9	38	B
LEU	O	207	60.6	14.3	33.1	36	B
ALA	N	208	61.6	14.5	31.0	40	B
ALA	CA	208	62.7	15.3	31.5	40	B
ALA	CB	208	64.0	15.0	30.7	37	B
ALA	C	208	62.4	16.8	31.4	40	B
ALA	O	208	63.1	17.7	31.9	39	B
SER	N	209	61.2	17.1	30.9	42	B
SER	CA	209	60.7	18.5	30.7	41	B
SER	CB	209	60.9	18.9	29.3	40	B
SER	OG	209	62.3	19.2	28.9	42	B
SER	C	209	59.3	18.9	31.2	40	B
SER	O	209	58.8	18.3	32.2	37	B
VAL	N	210	58.8	19.9	30.6	40	B
VAL	CA	210	57.5	20.4	30.9	36	B
VAL	CB	210	57.5	21.5	32.1	33	B
VAL	CG1	210	56.2	22.1	32.4	32	B
VAL	CG2	210	58.1	20.8	33.3	30	B
VAL	C	210	56.8	21.1	29.7	34	B
VAL	O	210	57.5	21.9	28.9	38	B
GLY	N	211	55.5	20.9	29.5	28	B
GLY	CA	211	54.8	21.4	28.3	15	B
GLY	C	211	53.9	22.6	28.7	11	B
GLY	O	211	53.5	23.4	27.9	10	B
GLY	N	212	53.6	22.8	30.0	5	B
GLY	CA	212	52.8	23.9	30.4	4	B
GLY	C	212	52.2	23.8	31.8	2	B
GLY	O	212	52.7	23.0	32.6	5	B
SER	N	213	51.2	24.6	32.2	1	B
SER	CA	213	50.6	24.6	33.5	1	B
SER	CB	213	51.2	25.7	34.4	1	B
SER	OG	213	51.5	26.8	33.6	1	B
SER	C	213	49.1	24.6	33.6	1	B
SER	O	213	48.4	25.3	32.8	1	B
MET	N	214	48.5	23.9	34.6	1	B
MET	CA	214	47.1	23.9	34.9	1	B
MET	CB	214	46.5	22.5	34.9	1	B
MET	CG	214	45.2	22.4	35.5	1	B
MET	SD	214	44.3	20.8	35.4	1	B
MET	CE	214	44.8	20.0	36.8	1	B
MET	C	214	46.9	24.4	36.3	1	B
MET	O	214	47.2	23.7	37.3	1	B
ILE	N	215	46.4	25.7	36.5	2	B
ILE	CA	215	46.2	26.3	37.8	3	B
ILE	CB	215	46.3	27.8	37.7	1	B
ILE	CG2	215	46.0	28.4	39.0	1	B
ILE	CG1	215	47.6	28.2	37.2	1	B
ILE	CD1	215	48.8	27.5	37.8	1	B
ILE	C	215	44.8	25.9	38.3	7	B
ILE	O	215	43.8	26.3	37.8	10	B
ILE	N	216	44.8	25.1	39.4	7	B
ILE	CA	216	43.5	24.7	40.0	3	B
ILE	CB	216	43.6	23.4	40.8	6	B
ILE	CG2	216	42.3	23.0	41.4	5	B
ILE	CG1	216	44.2	22.3	39.9	7	B
ILE	CD1	216	43.3	22.0	38.7	12	B
ILE	C	216	43.0	25.7	41.1	3	B
ILE	O	216	43.7	26.0	42.0	4	B
GLY	N	217	41.8	26.2	40.8	3	B
GLY	CA	217	41.2	27.2	41.7	1	B
GLY	C	217	41.5	28.7	41.6	1	B
GLY	O	217	41.5	29.4	42.6	1	B
GLY	N	218	41.7	29.1	40.4	1	B
GLY	CA	218	42.0	30.6	40.2	4	B
GLY	C	218	43.0	30.9	39.1	5	B
GLY	O	218	43.4	30.1	38.4	3	B
ILE	N	219	43.2	32.2	39.0	5	B
ILE	CA	219	44.1	32.7	37.9	3	B
ILE	CB	219	43.4	33.9	37.3	1	B
ILE	CG2	219	44.0	34.1	35.9	3	B
ILE	CG1	219	41.9	33.6	37.1	1	B
ILE	CD1	219	41.1	34.8	36.7	1	B
ILE	C	219	45.5	33.1	38.4	3	B
ILE	O	219	45.6	33.6	39.5	4	B
ASP	N	220	46.5	33.0	37.5	6	B
ASP	CA	220	47.8	33.3	37.8	7	B
ASP	CB	220	48.8	32.1	37.8	8	B
ASP	CG	220	50.2	32.5	38.1	9	B
ASP	OD1	220	50.7	32.0	39.1	9	B
ASP	OD2	220	50.8	33.2	37.4	16	B
ASP	C	220	48.3	34.4	36.9	8	B
ASP	O	220	48.8	34.1	35.8	9	B
HIS	N	221	48.2	35.7	37.3	10	B
HIS	CA	221	48.5	36.8	36.4	12	B
HIS	CB	221	48.4	38.1	37.2	15	B
HIS	CG	221	47.0	38.4	37.5	23	B
HIS	CD2	221	46.1	37.9	38.4	26	B
HIS	ND1	221	46.3	39.5	36.9	23	B
HIS	CE1	221	45.1	39.5	37.4	25	B
HIS	NE2	221	44.9	38.6	38.2	28	B
HIS	C	221	49.9	36.7	35.8	11	B
HIS	O	221	50.2	37.5	34.9	14	B
SER	N	222	50.8	35.8	36.2	8	B
SER	CA	222	52.1	35.7	35.7	6	B
SER	CB	222	53.1	35.3	36.7	7	B
SER	OG	222	53.1	33.9	37.0	17	B
SER	C	222	52.2	34.7	34.5	3	B
SER	O	222	53.2	34.3	34.1	3	B
LEU	N	223	51.0	34.4	33.9	4	B
LEU	CA	223	50.9	33.5	32.8	5	B
LEU	CB	223	50.1	32.3	33.2	4	B
LEU	CG	223	50.7	31.4	34.3	1	B
LEU	CD1	223	49.6	30.5	34.9	5	B
LEU	CD2	223	51.8	30.6	33.8	1	B
LEU	C	223	50.4	34.2	31.6	6	B
LEU	O	223	50.4	33.6	30.5	8	B
TYR	N	224	49.9	35.4	31.7	3	B
TYR	CA	224	49.4	36.1	30.6	4	B
TYR	CB	224	47.9	35.9	30.5	6	B
TYR	CG	224	47.0	36.6	31.5	5	B
TYR	CD1	224	47.0	36.2	32.8	4	B
TYR	CE1	224	46.2	36.8	33.8	4	B
TYR	CD2	224	46.2	37.7	31.2	2	B
TYR	CE2	224	45.4	38.3	32.1	5	B
TYR	CZ	224	45.4	37.8	33.4	8	B
TYR	OH	224	44.5	38.4	34.4	8	B
TYR	C	224	49.7	37.6	30.5	4	B
TYR	O	224	49.8	38.2	31.5	2	B
THR	N	225	49.8	38.1	29.3	4	B
THR	CA	225	50.1	39.5	29.1	5	B
THR	CB	225	51.3	39.7	28.1	5	B
THR	OG1	225	51.0	39.0	26.9	9	B
THR	CG2	225	52.5	39.2	28.8	1	B
THR	C	225	48.8	40.1	28.4	6	B
THR	O	225	48.2	39.4	27.6	8	B
GLY	N	226	48.5	41.3	28.8	6	B
GLY	CA	226	47.3	42.0	28.2	8	B
GLY	C	226	46.1	41.8	29.1	5	B
GLY	O	226	46.3	41.5	30.3	2	B
SER	N	227	44.9	41.9	28.6	5	B
SER	CA	227	43.7	41.7	29.4	5	B
SER	CB	227	42.7	42.9	29.0	5	B
SER	OG	227	43.4	44.1	29.2	8	B
SER	C	227	43.0	40.4	29.1	3	B
SER	O	227	43.4	39.6	28.3	3	B
LEU	N	228	42.0	40.1	29.9	1	B
LEU	CA	228	41.2	38.9	29.8	1	B
LEU	CB	228	41.1	38.2	31.2	1	B
LEU	CG	228	42.2	37.3	31.7	1	B
LEU	CD1	228	41.9	36.8	33.1	1	B
LEU	CD2	228	42.4	36.2	30.8	1	B
LEU	C	228	39.8	39.2	29.3	1	B
LEU	O	228	39.1	39.8	30.0	1	B
TRP	N	229	39.5	38.6	28.1	1	B
TRP	CA	229	38.2	38.8	27.6	1	B
TRP	CB	229	38.2	39.2	26.1	1	B
TRP	CG	229	38.8	40.6	25.9	1	B
TRP	CD2	229	38.0	41.7	25.5	1	B
TRP	CE2	229	39.0	42.8	25.4	1	B
TRP	CE3	229	36.7	42.0	25.3	1	B
TRP	CD1	229	40.1	40.9	25.9	2	B
TRP	NE1	229	40.2	42.3	25.6	1	B
TRP	CZ2	229	38.6	44.1	25.0	1	B
TRP	CZ3	229	36.3	43.3	25.0	3	B
TRP	CH2	229	37.3	44.3	24.9	1	B
TRP	C	229	37.4	37.5	27.7	1	B
TRP	O	229	37.8	36.5	27.3	1	B
TYR	N	230	36.2	37.6	28.3	1	B
TYR	CA	230	35.4	36.5	28.5	1	B
TYR	CB	230	34.7	36.5	29.9	1	B
TYR	CG	230	35.7	36.5	31.0	1	B
TYR	CD1	230	36.4	37.6	31.5	1	B
TYR	CE1	230	37.3	37.6	32.5	1	B
TYR	CD2	230	36.1	35.3	31.6	1	B
TYR	CE2	230	37.1	35.2	32.6	2	B
TYR	CZ	230	37.7	36.4	33.0	1	B
TYR	OH	230	38.6	36.3	34.0	1	B
TYR	C	230	34.3	36.2	27.5	4	B
TYR	O	230	33.8	37.2	26.9	5	B
THR	N	231	33.9	35.0	27.3	3	B
THR	CA	231	32.9	34.6	26.4	2	B
THR	CB	231	33.4	33.9	25.2	1	B
THR	OG1	231	32.4	33.4	24.3	1	B
THR	CG2	231	34.2	32.6	25.6	1	B
THR	C	231	32.0	33.6	27.2	3	B
THR	O	231	32.4	32.8	27.9	1	B
PRO	N	232	30.6	33.8	27.0	2	B
PRO	CD	232	30.0	34.8	26.2	2	B
PRO	CA	232	29.6	33.0	27.7	2	B
PRO	CB	232	28.3	33.6	27.1	1	B
PRO	CG	232	28.7	35.0	26.8	1	B
PRO	C	232	29.7	31.5	27.5	2	B
PRO	O	232	30.0	31.1	26.3	1	B
ILE	N	233	29.5	30.7	28.5	2	B
ILE	CA	233	29.5	29.3	28.3	1	B
ILE	CB	233	29.8	28.5	29.6	1	B
ILE	CG2	233	29.7	27.0	29.3	1	B
ILE	CG1	233	31.3	28.7	30.0	1	B
ILE	CD1	233	31.8	27.8	31.1	1	B
ILE	C	233	28.1	29.0	28.0	1	B
ILE	O	233	27.2	29.1	28.8	1	B
ARG	N	234	27.8	28.6	26.7	1	B
ARG	CA	234	26.5	28.3	26.3	1	B
ARG	CB	234	26.5	27.7	24.9	1	B
ARG	CG	234	25.8	28.6	23.9	1	B
ARG	CD	234	25.2	27.8	22.8	1	B
ARG	NE	234	23.9	28.3	22.4	1	B
ARG	CZ	234	23.1	27.7	21.6	2	B
ARG	NH1	234	23.3	26.5	21.1	1	B
ARG	NH2	234	21.9	28.3	21.3	9	B
ARG	C	234	25.7	27.4	27.2	1	B
ARG	O	234	24.8	27.9	27.9	2	B
ARG	N	235	25.9	26.1	27.1	1	B
ARG	CA	235	25.2	25.2	27.9	1	B
ARG	CB	235	24.4	24.2	27.0	3	B
ARG	CG	235	23.2	23.5	27.8	4	B
ARG	CD	235	23.1	22.1	27.5	1	B
ARG	NE	235	23.0	21.8	26.0	1	B
ARG	CZ	235	23.0	20.6	25.5	2	B
ARG	NH1	235	23.0	19.5	26.4	1	B
ARG	NH2	235	22.9	20.4	24.2	2	B
ARG	C	235	26.3	24.4	28.7	1	B
ARG	O	235	27.3	24.0	28.1	1	B
GLU	N	236	26.0	24.2	30.0	1	B
GLU	CA	236	27.0	23.5	30.8	2	B
GLU	CB	236	26.8	23.7	32.3	3	B
GLU	CG	236	27.0	25.2	32.7	12	B
GLU	CD	236	27.0	25.4	34.2	13	B
GLU	OE1	236	26.0	25.1	34.8	18	B
GLU	OE2	236	28.1	25.8	34.7	13	B
GLU	C	236	27.1	22.0	30.5	3	B
GLU	O	236	26.7	21.2	31.4	9	B
TRP	N	237	27.6	21.6	29.4	1	B
TRP	CA	237	27.8	20.2	29.1	1	B
TRP	CB	237	26.8	19.6	28.0	1	B
TRP	CG	237	26.7	20.4	26.8	1	B
TRP	CD2	237	26.4	19.8	25.5	1	B
TRP	CE2	237	26.3	20.9	24.6	1	B
TRP	CE3	237	26.1	18.5	25.1	1	B
TRP	CD1	237	26.8	21.7	26.6	4	B
TRP	NE1	237	26.6	22.0	25.2	1	B
TRP	CZ2	237	26.0	20.7	23.2	2	B
TRP	CZ3	237	25.8	18.3	23.7	1	B
TRP	CH2	237	25.7	19.4	22.8	1	B
TRP	C	237	29.2	20.1	28.6	1	B
TRP	O	237	30.1	19.6	29.4	1	B
TYR	N	238	29.5	20.4	27.4	1	B
TYR	CA	238	30.8	20.5	26.9	1	B
TYR	CB	238	30.9	20.3	25.4	1	B
TYR	CG	238	30.8	18.9	24.9	1	B
TYR	CD1	238	31.9	18.0	25.0	2	B
TYR	CE1	238	31.9	16.7	24.4	3	B
TYR	CD2	238	29.7	18.4	24.2	1	B
TYR	CE2	238	29.6	17.2	23.6	1	B
TYR	CZ	238	30.7	16.3	23.7	3	B
TYR	OH	238	30.7	15.1	23.1	4	B
TYR	C	238	31.1	21.9	27.2	1	B
TYR	O	238	30.1	22.6	27.5	1	B
TYR	N	239	32.3	22.4	27.2	1	B
TYR	CA	239	32.5	23.9	27.4	1	B
TYR	CB	239	33.9	24.2	27.8	1	B
TYR	CG	239	34.2	23.7	29.2	1	B
TYR	CD1	239	34.9	22.5	29.5	1	B
TYR	CE1	239	35.2	22.1	30.7	1	B
TYR	CD2	239	33.9	24.5	30.3	2	B
TYR	CE2	239	34.2	24.1	31.6	1	B
TYR	CZ	239	34.8	22.9	31.8	1	B
TYR	OH	239	35.1	22.5	33.1	1	B
TYR	C	239	32.1	24.6	26.1	1	B
TYR	O	239	33.0	25.1	25.5	1	B
GLU	N	240	30.9	24.6	25.8	1	B
GLU	CA	240	30.4	25.2	24.5	1	B
GLU	CB	240	29.0	24.7	24.2	1	B
GLU	CG	240	28.4	25.5	23.0	1	B
GLU	CD	240	27.0	24.9	22.5	1	B
GLU	OE1	240	26.2	24.6	23.4	1	B
GLU	OE2	240	26.9	24.8	21.3	1	B
GLU	C	240	30.5	26.7	24.5	1	B
GLU	O	240	30.3	27.3	25.5	1	B
VAL	N	241	30.9	27.2	23.3	1	B
VAL	CA	241	31.0	28.6	23.1	1	B
VAL	CB	241	32.5	29.1	23.1	1	B
VAL	CG1	241	33.2	28.9	24.4	1	B
VAL	CG2	241	33.2	28.3	22.0	1	B
VAL	C	241	30.4	28.9	21.8	1	B
VAL	O	241	30.1	28.0	21.1	1	B
ILE	N	242	30.2	30.2	21.4	1	B
ILE	CA	242	29.6	30.6	20.1	1	B
ILE	CB	242	28.3	31.3	20.4	1	B
ILE	CG2	242	27.9	32.0	19.1	1	B
ILE	CG1	242	27.2	30.4	20.9	1	B
ILE	CD1	242	26.1	31.1	21.5	1	B
ILE	C	242	30.6	31.5	19.3	1	B
ILE	O	242	30.9	32.5	19.8	1	B
ILE	N	243	31.0	31.0	18.2	2	B
ILE	CA	243	31.8	31.8	17.3	1	B
ILE	CB	243	32.7	30.9	16.4	1	B
ILE	CG2	243	33.4	31.7	15.3	1	B
ILE	CG1	243	33.8	30.2	17.3	1	B
ILE	CD1	243	34.7	29.3	16.5	1	B
ILE	C	243	30.9	32.7	16.4	1	B
ILE	O	243	30.0	32.2	15.9	1	B
VAL	N	244	31.2	34.0	16.4	1	B
VAL	CA	244	30.3	34.9	15.6	1	B
VAL	CB	244	29.9	36.1	16.4	1	B
VAL	CG1	244	29.0	35.7	17.5	2	B
VAL	CG2	244	31.1	36.8	16.9	1	B
VAL	C	244	31.0	35.4	14.3	1	B
VAL	O	244	30.3	36.1	13.6	3	B
ARG	N	245	32.2	35.0	14.1	1	B
ARG	CA	245	32.9	35.5	12.9	1	B
ARG	CB	245	33.1	37.0	13.0	1	B
ARG	CG	245	33.7	37.7	11.8	1	B
ARG	CD	245	34.2	39.1	12.2	2	B
ARG	NE	245	34.7	39.9	11.1	1	B
ARG	CZ	245	33.9	40.5	10.2	1	B
ARG	NH1	245	32.6	40.2	10.2	1	B
ARG	NH2	245	34.4	41.3	9.3	2	B
ARG	C	245	34.3	34.8	12.7	1	B
ARG	O	245	34.9	34.4	13.7	1	B
VAL	N	246	34.8	34.7	11.5	1	B
VAL	CA	246	36.1	34.1	11.2	1	B
VAL	CB	246	35.9	32.7	10.8	1	B
VAL	CG1	246	37.3	32.1	10.4	1	B
VAL	CG2	246	35.4	31.9	12.0	1	B
VAL	C	246	36.7	34.9	10.1	1	B
VAL	O	246	36.1	35.1	9.1	1	B
GLU	N	247	38.0	35.3	10.2	1	B
GLU	CA	247	38.7	36.0	9.2	1	B
GLU	CB	247	39.0	37.4	9.6	1	B
GLU	CG	247	38.0	38.1	10.5	2	B
GLU	CD	247	38.4	39.5	10.8	4	B
GLU	OE1	247	39.7	39.8	11.0	6	B
GLU	OE2	247	37.6	40.4	11.0	2	B
GLU	C	247	40.1	35.3	8.9	1	B
GLU	O	247	40.7	34.7	9.8	1	B
ILE	N	248	40.5	35.3	7.7	1	B
ILE	CA	248	41.8	34.8	7.3	1	B
ILE	CB	248	41.8	33.7	6.2	1	B
ILE	CG2	248	43.1	33.1	6.0	1	B
ILE	CG1	248	40.8	32.7	6.5	1	B
ILE	CD1	248	41.1	31.9	7.8	1	B
ILE	C	248	42.6	36.0	6.9	1	B
ILE	O	248	42.4	36.5	5.7	1	B
ASN	N	249	43.5	36.5	7.7	3	B
ASN	CA	249	44.3	37.6	7.4	1	B
ASN	CB	249	45.2	37.4	6.2	1	B
ASN	CG	249	46.7	37.2	6.5	1	B
ASN	OD1	249	47.0	36.9	7.6	1	B
ASN	ND2	249	47.5	37.5	5.5	1	B
ASN	C	249	43.4	38.8	7.2	1	B
ASN	O	249	43.5	39.5	6.2	1	B
GLY	N	250	42.5	39.0	8.1	1	B
GLY	CA	250	41.6	40.1	8.1	1	B
GLY	C	250	40.4	39.9	7.1	1	B
GLY	O	250	39.4	40.7	7.2	3	B
GLN	N	251	40.5	39.0	6.2	2	B
GLN	CA	251	39.4	38.8	5.3	3	B
GLN	CB	251	40.0	38.1	4.0	7	B
GLN	CG	251	39.1	38.2	2.8	7	B
GLN	CD	251	39.9	38.6	1.5	11	B
GLN	OE1	251	39.6	38.2	0.4	12	B
GLN	NE2	251	40.9	39.4	1.7	13	B
GLN	C	251	38.3	37.9	5.9	1	B
GLN	O	251	38.5	36.8	6.2	1	B
ASP	N	252	37.1	38.5	6.0	1	B
ASP	CA	252	36.0	37.8	6.5	1	B
ASP	CB	252	34.8	38.8	6.7	1	B
ASP	CG	252	33.5	38.1	7.0	1	B
ASP	OD1	252	33.6	37.0	7.6	1	B
ASP	OD2	252	32.5	38.7	6.8	1	B
ASP	C	252	35.6	36.7	5.6	1	B
ASP	O	252	35.2	36.9	4.5	1	B
LEU	N	253	35.7	35.4	6.2	1	B
LEU	CA	253	35.3	34.2	5.5	1	B
LEU	CB	253	35.3	33.0	6.4	3	B
LEU	CG	253	35.9	31.7	6.0	1	B
LEU	CD1	253	37.3	32.0	5.5	1	B
LEU	CD2	253	36.0	30.8	7.2	1	B
LEU	C	253	33.9	34.4	4.9	4	B
LEU	O	253	33.5	33.7	3.9	7	B
LYS	N	254	33.2	35.4	5.4	4	B
LYS	CA	254	31.8	35.7	5.0	6	B
LYS	CB	254	31.9	36.4	3.7	9	B
LYS	CG	254	30.8	37.5	3.4	12	B
LYS	CD	254	30.9	38.0	2.0	14	B
LYS	CE	254	29.9	39.1	1.7	19	B
LYS	NZ	254	30.1	39.8	0.4	18	B
LYS	C	254	30.9	34.5	4.9	7	B
LYS	O	254	30.4	34.2	3.8	11	B
MET	N	255	30.7	33.8	6.0	6	B
MET	CA	255	29.8	32.7	6.0	4	B
MET	CB	255	30.5	31.4	6.5	4	B
MET	CG	255	30.9	30.5	5.3	1	B
MET	SD	255	32.1	29.3	5.7	2	B
MET	CE	255	31.2	28.0	6.3	4	B
MET	C	255	28.7	33.0	7.0	2	B
MET	O	255	28.8	34.0	7.8	1	B
ASP	N	256	27.6	32.3	7.0	1	B
ASP	CA	256	26.5	32.6	8.0	1	B
ASP	CB	256	25.3	31.8	7.5	6	B
ASP	CG	256	24.2	31.7	8.5	9	B
ASP	OD1	256	24.4	30.9	9.5	11	B
ASP	OD2	256	23.2	32.3	8.4	13	B
ASP	C	256	26.9	32.2	9.4	1	B
ASP	O	256	27.3	31.1	9.7	1	B
CYS	N	257	26.7	33.2	10.3	1	B
CYS	CA	257	27.0	33.0	11.7	1	B
CYS	CB	257	26.1	33.9	12.6	1	B
CYS	SG	257	26.3	34.0	14.5	7	B
CYS	C	257	26.9	31.5	12.1	1	B
CYS	O	257	27.9	31.0	12.7	1	B
LYS	N	258	25.8	30.9	11.8	1	B
LYS	CA	258	25.6	29.5	12.2	1	B
LYS	CB	258	24.1	29.1	11.8	5	B
LYS	CG	258	23.0	29.9	12.5	9	B
LYS	CD	258	21.7	29.1	12.6	16	B
LYS	CE	258	20.6	29.9	13.1	19	B
LYS	NZ	258	20.1	30.9	12.1	24	B
LYS	C	258	26.5	28.4	11.7	2	B
LYS	O	258	26.7	27.4	12.3	4	B
GLU	N	259	27.1	28.6	10.5	1	B
GLU	CA	259	28.0	27.5	10.0	1	B
GLU	CB	259	28.5	27.9	8.6	5	B
GLU	CG	259	27.5	27.4	7.5	4	B
GLU	CD	259	27.2	26.0	7.5	8	B
GLU	OE1	259	28.0	25.2	8.1	7	B
GLU	OE2	259	26.1	25.6	7.0	11	B
GLU	C	259	29.3	27.2	10.9	1	B
GLU	O	259	29.7	26.1	11.0	1	B
TYR	N	260	29.8	28.3	11.5	1	B
TYR	CA	260	31.0	28.1	12.3	1	B
TYR	CB	260	31.6	29.5	12.7	1	B
TYR	CG	260	31.9	30.4	11.6	1	B
TYR	CD1	260	31.6	31.8	11.8	1	B
TYR	CE1	260	31.8	32.7	10.8	1	B
TYR	CD2	260	32.4	30.0	10.3	1	B
TYR	CE2	260	32.6	31.0	9.3	1	B
TYR	CZ	260	32.4	32.3	9.6	1	B
TYR	OH	260	32.6	33.2	8.6	5	B
TYR	C	260	30.7	27.3	13.5	1	B
TYR	O	260	31.5	26.7	14.2	1	B
ASN	N	261	29.4	27.4	13.9	1	B
ASN	CA	261	28.9	26.7	15.2	1	B
ASN	CB	261	28.3	27.7	16.1	1	B
ASN	CG	261	29.1	28.9	16.4	1	B
ASN	OD1	261	30.2	28.8	16.9	1	B
ASN	ND2	261	28.6	30.1	16.1	1	B
ASN	C	261	28.0	25.6	14.9	2	B
ASN	O	261	27.1	25.3	15.8	1	B
TYR	N	262	28.0	25.0	13.7	8	B
TYR	CA	262	27.2	24.0	13.3	10	B
TYR	CB	262	27.4	23.6	11.8	13	B
TYR	CG	262	26.6	22.4	11.4	22	B
TYR	CD1	262	25.2	22.4	11.8	25	B
TYR	CE1	262	24.5	21.3	11.4	30	B
TYR	CD2	262	27.2	21.3	10.7	26	B
TYR	CE2	262	26.4	20.2	10.4	24	B
TYR	CZ	262	25.0	20.2	10.7	30	B
TYR	OH	262	24.2	19.2	10.4	30	B
TYR	C	262	27.2	22.7	14.1	10	B
TYR	O	262	28.2	21.9	14.0	9	B
ASP	N	263	26.2	22.6	15.0	8	B
ASP	CA	263	26.1	21.5	16.0	8	B
ASP	CB	263	26.9	20.2	15.6	16	B
ASP	CG	263	26.6	19.0	16.4	20	B
ASP	OD1	263	25.5	18.9	16.9	25	B
ASP	OD2	263	27.5	18.2	16.6	23	B
ASP	C	263	26.6	22.1	17.2	4	B
ASP	O	263	25.8	22.4	18.1	2	B
LYS	N	264	27.9	22.3	17.3	3	B
LYS	CA	264	28.4	22.9	18.5	3	B
LYS	CB	264	28.4	21.9	19.7	5	B
LYS	CG	264	29.2	20.7	19.4	9	B
LYS	CD	264	29.3	19.8	20.6	9	B
LYS	CE	264	30.0	18.5	20.3	11	B
LYS	NZ	264	29.1	17.6	19.5	11	B
LYS	C	264	29.9	23.4	18.3	2	B
LYS	O	264	30.6	23.1	17.4	2	B
SER	N	265	30.3	24.3	19.3	1	B
SER	CA	265	31.6	24.9	19.3	1	B
SER	CB	265	31.6	26.3	18.9	3	B
SER	OG	265	31.4	26.5	17.5	3	B
SER	C	265	32.1	24.7	20.7	1	B
SER	O	265	31.4	25.2	21.7	2	B
ILE	N	266	33.2	24.1	20.9	1	B
ILE	CA	266	33.7	23.8	22.2	1	B
ILE	CB	266	33.5	22.3	22.6	2	B
ILE	CG2	266	32.0	22.0	22.5	5	B
ILE	CG1	266	34.3	21.4	21.6	1	B
ILE	CD1	266	34.0	19.9	21.7	1	B
ILE	C	266	35.2	24.0	22.4	1	B
ILE	O	266	36.0	24.0	21.4	6	B
VAL	N	267	35.7	24.2	23.6	1	B
VAL	CA	267	37.1	24.4	23.9	1	B
VAL	CB	267	37.3	25.6	24.9	1	B
VAL	CG1	267	38.7	25.8	25.1	1	B
VAL	CG2	267	36.7	26.8	24.3	1	B
VAL	C	267	37.5	23.1	24.5	2	B
VAL	O	267	37.3	22.9	25.7	4	B
ASP	N	268	38.1	22.2	23.8	3	B
ASP	CA	268	38.6	20.9	24.2	1	B
ASP	CB	268	37.9	19.9	23.3	1	B
ASP	CG	268	38.5	18.5	23.4	1	B
ASP	OD1	268	38.4	17.9	24.5	1	B
ASP	OD2	268	39.0	18.0	22.4	4	B
ASP	C	268	40.1	20.7	24.2	1	B
ASP	O	268	40.7	20.6	23.1	1	B
SER	N	269	40.7	20.6	25.3	1	B
SER	CA	269	42.2	20.5	25.4	1	B
SER	CB	269	42.7	20.9	26.7	2	B
SER	OG	269	42.4	19.9	27.7	5	B
SER	C	269	42.6	19.0	25.1	1	B
SER	O	269	43.8	18.7	25.0	2	B
GLY	N	270	41.6	18.2	24.8	1	B
GLY	CA	270	41.9	16.8	24.6	1	B
GLY	C	270	42.3	16.5	23.1	2	B
GLY	O	270	42.9	15.5	22.8	5	B
THR	N	271	41.9	17.4	22.2	4	B
THR	CA	271	42.2	17.3	20.8	8	B
THR	CB	271	41.0	17.7	19.9	10	B
THR	OG1	271	39.8	17.1	20.5	12	B
THR	CG2	271	41.2	17.1	18.5	18	B
THR	C	271	43.4	18.2	20.4	6	B
THR	O	271	43.5	19.3	20.9	10	B
THR	N	272	44.2	17.7	19.5	4	B
THR	CA	272	45.3	18.5	19.0	1	B
THR	CB	272	46.4	17.6	18.3	3	B
THR	OG1	272	46.7	16.6	19.2	5	B
THR	CG2	272	47.6	18.4	17.9	5	B
THR	C	272	45.0	19.7	18.1	1	B
THR	O	272	45.2	20.8	18.4	1	B
ASN	N	273	44.5	19.3	16.9	3	B
ASN	CA	273	44.1	20.2	15.8	1	B
ASN	CB	273	43.8	19.4	14.6	1	B
ASN	CG	273	44.9	18.7	14.1	1	B
ASN	OD1	273	45.9	18.5	14.7	1	B
ASN	ND2	273	44.8	18.2	12.8	1	B
ASN	C	273	43.0	21.2	16.1	1	B
ASN	O	273	42.3	21.0	17.1	1	B
LEU	N	274	42.8	22.2	15.3	1	B
LEU	CA	274	41.7	23.1	15.4	1	B
LEU	CB	274	42.0	24.5	14.9	3	B
LEU	CG	274	40.9	25.6	14.8	1	B
LEU	CD1	274	41.2	26.5	13.7	1	B
LEU	CD2	274	39.5	25.1	14.7	1	B
LEU	C	274	40.8	22.4	14.4	1	B
LEU	O	274	41.1	22.2	13.3	1	B
ARG	N	275	39.6	22.0	14.9	1	B
ARG	CA	275	38.7	21.3	14.0	1	B
ARG	CB	275	38.2	20.0	14.7	1	B
ARG	CG	275	39.2	18.9	14.7	1	B
ARG	CD	275	38.9	17.8	15.7	6	B
ARG	NE	275	37.6	17.1	15.5	15	B
ARG	CZ	275	37.3	16.3	14.5	23	B
ARG	NH1	275	36.0	15.8	14.4	22	B
ARG	NH2	275	38.2	16.1	13.5	26	B
ARG	C	275	37.5	22.2	13.5	1	B
ARG	O	275	36.9	22.9	14.4	2	B
LEU	N	276	37.3	22.3	12.2	1	B
LEU	CA	276	36.3	23.1	11.7	1	B
LEU	CB	276	36.9	24.1	10.7	1	B
LEU	CG	276	37.9	25.2	11.3	1	B
LEU	CD1	276	38.3	26.1	10.2	1	B
LEU	CD2	276	37.2	25.9	12.4	4	B
LEU	C	276	35.2	22.3	10.9	3	B
LEU	O	276	35.5	21.3	10.3	2	B
PRO	N	277	34.0	22.7	11.0	5	B
PRO	CD	277	33.4	23.7	11.9	6	B
PRO	CA	277	32.9	22.0	10.3	8	B
PRO	CB	277	31.7	22.9	10.5	9	B
PRO	CG	277	31.9	23.3	11.9	4	B
PRO	C	277	33.3	21.9	8.8	9	B
PRO	O	277	33.8	22.8	8.2	6	B
LYS	N	278	32.9	20.7	8.2	12	B
LYS	CA	278	33.2	20.4	6.9	14	B
LYS	CB	278	32.4	19.1	6.4	15	B
LYS	CG	278	32.8	18.6	5.1	22	B
LYS	CD	278	34.4	18.5	5.0	27	B
LYS	CE	278	34.9	18.2	3.6	29	B
LYS	NZ	278	36.4	18.2	3.4	26	B
LYS	C	278	33.0	21.5	5.9	13	B
LYS	O	278	33.6	21.6	4.8	11	B
LYS	N	279	32.1	22.5	6.2	14	B
LYS	CA	279	31.8	23.6	5.3	15	B
LYS	CB	279	30.4	24.1	5.5	21	B
LYS	CG	279	29.3	23.1	5.3	27	B
LYS	CD	279	28.5	22.9	6.6	29	B
LYS	CE	279	27.2	22.2	6.4	29	B
LYS	NZ	279	26.4	22.1	7.6	29	B
LYS	C	279	32.8	24.7	5.5	12	B
LYS	O	279	33.3	25.3	4.6	14	B
VAL	N	280	33.1	24.9	6.8	8	B
VAL	CA	280	34.1	26.0	7.2	4	B
VAL	CB	280	33.9	26.3	8.7	3	B
VAL	CG1	280	34.8	27.4	9.2	3	B
VAL	CG2	280	32.4	26.7	9.0	1	B
VAL	C	280	35.5	25.6	6.9	3	B
VAL	O	280	36.3	26.5	6.8	4	B
PHE	N	281	35.8	24.3	6.9	2	B
PHE	CA	281	37.2	23.9	6.6	1	B
PHE	CB	281	37.3	22.4	6.9	1	B
PHE	CG	281	38.7	21.9	6.5	1	B
PHE	CD1	281	39.8	22.1	7.3	1	B
PHE	CD2	281	38.8	21.1	5.4	1	B
PHE	CE1	281	41.0	21.5	7.0	1	B
PHE	CE2	281	40.0	20.6	5.1	1	B
PHE	CZ	281	41.1	20.8	5.9	1	B
PHE	C	281	37.6	24.2	5.2	1	B
PHE	O	281	38.7	24.5	4.9	1	B
GLU	N	282	36.6	23.9	4.3	3	B
GLU	CA	282	36.8	24.1	2.9	5	B
GLU	CB	282	35.6	23.6	2.1	12	B
GLU	CG	282	35.2	22.2	2.4	18	B
GLU	CD	282	35.6	21.1	1.4	25	B
GLU	OE1	282	35.0	21.1	0.3	29	B
GLU	OE2	282	36.6	20.4	1.7	27	B
GLU	C	282	37.1	25.5	2.5	4	B
GLU	O	282	37.9	25.8	1.6	5	B
ALA	N	283	36.4	26.4	3.1	4	B
ALA	CA	283	36.5	27.9	2.9	4	B
ALA	CB	283	35.3	28.6	3.3	7	B
ALA	C	283	37.7	28.5	3.5	2	B
ALA	O	283	38.3	29.4	3.0	1	B
ALA	N	284	38.1	28.0	4.7	1	B
ALA	CA	284	39.2	28.5	5.5	1	B
ALA	CB	284	39.2	28.0	6.9	1	B
ALA	C	284	40.5	28.0	4.7	1	B
ALA	O	284	41.4	28.8	4.5	6	B
VAL	N	285	40.6	26.7	4.4	1	B
VAL	CA	285	41.7	26.2	3.7	2	B
VAL	CB	285	41.7	24.7	3.5	1	B
VAL	CG1	285	42.8	24.2	2.6	1	B
VAL	CG2	285	41.8	24.0	4.9	1	B
VAL	C	285	41.9	26.9	2.4	1	B
VAL	O	285	42.9	27.2	1.9	1	B
LYS	N	286	40.7	27.2	1.7	2	B
LYS	CA	286	40.7	27.8	0.4	3	B
LYS	CB	286	39.3	28.0	−0.1	8	B
LYS	CG	286	39.2	28.4	−1.5	13	B
LYS	CD	286	40.1	27.6	−2.4	21	B
LYS	CE	286	40.0	26.1	−2.3	23	B
LYS	NZ	286	41.2	25.3	−2.8	17	B
LYS	C	286	41.4	29.1	0.5	1	B
LYS	O	286	42.2	29.5	−0.3	1	B
SER	N	287	41.2	29.8	1.6	2	B
SER	CA	287	41.7	31.1	1.8	1	B
SER	CB	287	40.9	31.9	2.9	1	B
SER	OG	287	41.5	33.1	3.2	1	B
SER	C	287	43.2	31.0	2.3	1	B
SER	O	287	44.0	31.8	1.9	1	B
ILE	N	288	43.4	30.1	3.2	1	B
ILE	CA	288	44.8	29.9	3.7	1	B
ILE	CB	288	44.9	28.9	4.8	1	B
ILE	CG2	288	46.3	28.7	5.3	1	B
ILE	CG1	288	43.9	29.3	5.9	1	B
ILE	CD1	288	43.8	28.3	7.0	1	B
ILE	C	288	45.7	29.5	2.6	1	B
ILE	O	288	46.8	30.0	2.4	1	B
LYS	N	289	45.2	28.6	1.7	2	B
LYS	CA	289	46.0	28.1	0.6	4	B
LYS	CB	289	45.1	27.1	−0.2	3	B
LYS	CG	289	45.9	26.1	−1.0	6	B
LYS	CD	289	45.1	25.0	−1.7	4	B
LYS	CE	289	44.5	24.1	−0.6	5	B
LYS	NZ	289	43.7	22.9	−1.1	5	B
LYS	C	289	46.3	29.3	−0.3	5	B
LYS	O	289	47.4	29.5	−0.8	8	B
ALA	N	290	45.3	30.2	−0.5	3	B
ALA	CA	290	45.5	31.4	−1.3	1	B
ALA	CB	290	44.2	32.1	−1.4	2	B
ALA	C	290	46.5	32.3	−0.7	1	B
ALA	O	290	47.4	32.8	−1.4	1	B
ALA	N	291	46.4	32.6	0.6	1	B
ALA	CA	291	47.3	33.5	1.2	1	B
ALA	CB	291	46.8	33.8	2.7	3	B
ALA	C	291	48.7	33.1	1.2	1	B
ALA	O	291	49.6	33.9	1.5	1	B
SER	N	292	49.0	31.8	0.9	1	B
SER	CA	292	50.3	31.3	0.9	1	B
SER	CB	292	50.5	30.2	1.9	1	B
SER	OG	292	49.3	29.5	2.0	4	B
SER	C	292	50.8	30.8	−0.5	1	B
SER	O	292	51.5	29.8	−0.5	1	B
SER	N	293	50.4	31.5	−1.5	4	B
SER	CA	293	50.7	31.1	−2.9	4	B
SER	CB	293	49.9	31.9	−3.9	3	B
SER	OG	293	48.5	32.0	−3.6	3	B
SER	C	293	52.1	31.1	−3.3	4	B
SER	O	293	52.6	30.3	−4.1	5	B
THR	N	294	52.9	32.1	−2.7	4	B
THR	CA	294	54.3	32.2	−3.0	4	B
THR	CB	294	55.0	33.0	−1.9	3	B
THR	OG1	294	54.2	34.0	−1.4	3	B
THR	CG2	294	56.3	33.6	−2.4	1	B
THR	C	294	54.9	30.8	−3.1	6	B
THR	O	294	55.6	30.5	−4.0	4	B
GLU	N	295	54.6	30.0	−2.1	7	B
GLU	CA	295	55.1	28.6	−2.1	14	B
GLU	CB	295	55.8	28.3	−0.8	13	B
GLU	CG	295	57.1	29.0	−0.6	16	B
GLU	CD	295	57.8	28.7	0.7	18	B
GLU	OE1	295	57.8	27.6	1.2	18	B
GLU	OE2	295	58.3	29.7	1.3	16	B
GLU	C	295	54.0	27.6	−2.4	17	B
GLU	O	295	52.8	28.0	−2.3	21	B
LYS	N	296	54.3	26.4	−2.8	20	B
LYS	CA	296	53.3	25.4	−3.1	21	B
LYS	CB	296	53.4	25.1	−4.6	28	B
LYS	CG	296	52.5	25.9	−5.5	34	B
LYS	CD	296	51.0	25.5	−5.4	36	B
LYS	CE	296	50.1	26.1	−6.5	38	B
LYS	NZ	296	50.0	27.6	−6.4	40	B
LYS	C	296	53.7	24.2	−2.2	18	B
LYS	O	296	54.9	23.9	−2.0	20	B
PHE	N	297	52.7	23.5	−1.8	13	B
PHE	CA	297	52.9	22.3	−1.0	9	B
PHE	CB	297	52.4	22.5	0.5	7	B
PHE	CG	297	52.5	23.9	0.9	9	B
PHE	CD1	297	51.6	24.9	0.5	14	B
PHE	CD2	297	53.4	24.3	1.9	9	B
PHE	CE1	297	51.6	26.2	0.9	10	B
PHE	CE2	297	53.5	25.7	2.3	5	B
PHE	CZ	297	52.6	26.6	1.8	6	B
PHE	C	297	52.1	21.1	−1.6	11	B
PHE	O	297	51.1	21.4	−2.3	19	B
PRO	N	298	52.5	19.9	−1.3	8	B
PRO	CD	298	53.7	19.4	−0.7	4	B
PRO	CA	298	51.7	18.7	−1.9	11	B
PRO	CB	298	52.5	17.5	−1.4	5	B
PRO	CG	298	53.3	18.1	−0.2	3	B
PRO	C	298	50.3	18.7	−1.4	17	B
PRO	O	298	50.0	19.1	−0.3	17	B
ASP	N	299	49.3	18.3	−2.2	27	B
ASP	CA	299	47.9	18.2	−1.9	32	B
ASP	CB	299	47.1	17.5	−3.1	39	B
ASP	CG	299	45.6	17.9	−3.0	39	B
ASP	OD1	299	45.3	19.0	−3.2	42	B
ASP	OD2	299	44.8	16.9	−2.8	38	B
ASP	C	299	47.6	17.6	−0.6	30	B
ASP	O	299	46.6	18.0	0.1	27	B
GLY	N	300	48.4	16.6	−0.2	23	B
GLY	CA	300	48.2	15.9	1.1	17	B
GLY	C	300	48.5	16.8	2.3	13	B
GLY	O	300	48.0	16.6	3.4	13	B
PHE	N	301	49.3	17.8	2.0	9	B
PHE	CA	301	49.7	18.7	3.1	6	B
PHE	CB	301	50.5	19.9	2.6	5	B
PHE	CG	301	50.8	21.0	3.6	1	B
PHE	CD1	301	51.4	20.7	4.8	3	B
PHE	CD2	301	50.4	22.3	3.3	1	B
PHE	CE1	301	51.6	21.7	5.8	1	B
PHE	CE2	301	50.6	23.3	4.3	4	B
PHE	CZ	301	51.2	23.0	5.5	1	B
PHE	C	301	48.5	19.3	3.8	4	B
PHE	O	301	48.3	19.1	5.0	6	B
TRP	N	302	47.6	19.9	3.0	3	B
TRP	CA	302	46.4	20.6	3.5	5	B
TRP	CB	302	45.8	21.4	2.4	5	B
TRP	CG	302	46.6	22.6	2.0	4	B
TRP	CD2	302	47.0	23.7	2.7	2	B
TRP	CE2	302	47.8	24.5	1.9	4	B
TRP	CE3	302	46.8	24.1	4.1	3	B
TRP	CD1	302	47.2	22.7	0.7	4	B
TRP	NE1	302	47.9	23.9	0.7	2	B
TRP	CZ2	302	48.4	25.8	2.3	3	B
TRP	CZ3	302	47.3	25.3	4.5	1	B
TRP	CH2	302	48.1	26.1	3.6	3	B
TRP	C	302	45.4	19.6	4.1	6	B
TRP	O	302	44.3	20.0	4.5	6	B
LEU	N	303	45.8	18.3	4.1	5	B
LEU	CA	303	44.8	17.3	4.6	3	B
LEU	CB	303	44.4	16.2	3.6	1	B
LEU	CG	303	43.7	16.7	2.4	2	B
LEU	CD1	303	43.2	15.5	1.7	9	B
LEU	CD2	303	42.5	17.6	2.8	4	B
LEU	C	303	45.4	16.5	5.8	5	B
LEU	O	303	44.9	15.4	6.2	4	B
GLY	N	304	46.5	17.0	6.4	10	B
GLY	CA	304	47.2	16.4	7.5	11	B
GLY	C	304	47.8	15.0	7.2	10	B
GLY	O	304	48.3	14.3	8.1	11	B
GLU	N	305	47.9	14.7	5.9	10	B
GLU	CA	305	48.4	13.4	5.5	10	B
GLU	CB	305	47.7	12.9	4.2	15	B
GLU	CG	305	46.3	12.3	4.6	18	B
GLU	CD	305	45.4	12.1	3.3	27	B
GLU	OE1	305	44.4	11.4	3.5	26	B
GLU	OE2	305	45.8	12.6	2.2	27	B
GLU	C	305	49.9	13.5	5.2	11	B
GLU	O	305	50.5	12.4	5.1	14	B
GLN	N	306	50.5	14.7	5.0	10	B
GLN	CA	306	51.9	14.7	4.7	11	B
GLN	CB	306	52.2	14.4	3.3	14	B
GLN	CG	306	51.5	15.2	2.3	23	B
GLN	CD	306	51.4	14.6	0.9	26	B
GLN	OE1	306	50.9	15.2	−0.1	25	B
GLN	NE2	306	51.9	13.4	0.8	23	B
GLN	C	306	52.5	16.1	5.1	9	B
GLN	O	306	52.0	17.1	4.7	9	B
LEU	N	307	53.6	16.0	5.9	9	B
LEU	CA	307	54.2	17.3	6.4	6	B
LEU	CB	307	55.1	16.9	7.6	6	B
LEU	CG	307	55.7	15.6	7.7	6	B
LEU	CD1	307	56.4	15.2	6.4	8	B
LEU	CD2	307	56.7	15.6	8.9	12	B
LEU	C	307	55.1	18.0	5.4	4	B
LEU	O	307	55.7	17.5	4.4	2	B
VAL	N	308	55.2	19.3	5.7	2	B
VAL	CA	308	56.0	20.3	4.9	4	B
VAL	CB	308	55.2	21.6	4.6	6	B
VAL	CG1	308	56.2	22.7	4.3	6	B
VAL	CG2	308	54.2	21.4	3.6	7	B
VAL	C	308	57.3	20.6	5.6	4	B
VAL	O	308	57.2	21.0	6.8	8	B
CYS	N	309	58.4	20.5	5.0	4	B
CYS	CA	309	59.7	20.8	5.6	4	B
CYS	C	309	60.4	22.0	5.0	3	B
CYS	O	309	60.2	22.3	3.8	2	B
CYS	CB	309	60.7	19.6	5.6	4	B
CYS	SG	309	60.0	18.1	6.3	9	B
TRP	N	310	61.2	22.6	5.8	1	B
TRP	CA	310	62.0	23.8	5.4	1	B
TRP	CB	310	61.4	25.1	5.9	1	B
TRP	CG	310	60.3	25.6	5.0	3	B
TRP	CD2	310	58.9	25.7	5.2	2	B
TRP	CE2	310	58.3	26.3	4.1	3	B
TRP	CE3	310	58.1	25.2	6.3	1	B
TRP	CD1	310	60.5	26.2	3.7	5	B
TRP	NE1	310	59.3	26.6	3.2	5	B
TRP	CZ2	310	56.9	26.4	4.0	2	B
TRP	CZ3	310	56.8	25.4	6.2	1	B
TRP	CH2	310	56.2	26.0	5.1	1	B
TRP	C	310	63.4	23.6	6.1	3	B
TRP	O	310	63.5	22.9	7.1	3	B
GLN	N	311	64.4	24.3	5.6	5	B
GLN	CA	311	65.7	24.3	6.2	8	B
GLN	CB	311	66.7	25.0	5.2	14	B
GLN	CG	311	66.4	24.8	3.7	24	B
GLN	CD	311	65.0	25.2	3.3	28	B
GLN	OE1	311	64.6	26.4	3.2	30	B
GLN	NE2	311	64.1	24.2	2.9	28	B
GLN	C	311	65.7	24.9	7.6	5	B
GLN	O	311	65.2	26.1	7.7	5	B
ALA	N	312	66.1	24.2	8.6	4	B
ALA	CA	312	66.1	24.7	9.9	1	B
ALA	CB	312	67.3	24.1	10.7	6	B
ALA	C	312	66.3	26.2	10.1	1	B
ALA	O	312	67.1	26.8	9.4	1	B
GLY	N	313	65.4	26.8	10.9	3	B
GLY	CA	313	65.5	28.2	11.1	7	B
GLY	C	313	65.2	29.1	9.9	6	B
GLY	O	313	65.7	30.2	9.8	4	B
THR	N	314	64.3	28.7	9.0	5	B
THR	CA	314	63.9	29.5	7.9	5	B
THR	CB	314	64.8	29.1	6.6	5	B
THR	OG1	314	64.2	27.9	6.0	6	B
THR	CG2	314	66.2	28.7	7.0	6	B
THR	C	314	62.5	29.4	7.5	2	B
THR	O	314	62.1	29.8	6.4	6	B
THR	N	315	61.7	28.8	8.4	2	B
THR	CA	315	60.2	28.7	8.1	2	B
THR	CB	315	59.5	28.0	9.3	2	B
THR	OG1	315	60.3	26.9	9.7	1	B
THR	CG2	315	58.2	27.6	8.8	1	B
THR	C	315	59.6	30.0	7.9	2	B
THR	O	315	59.6	30.9	8.8	4	B
PRO	N	316	59.1	30.3	6.7	1	B
PRO	CD	316	59.0	29.3	5.6	2	B
PRO	CA	316	58.5	31.6	6.2	1	B
PRO	CB	316	58.4	31.4	4.7	2	B
PRO	CG	316	58.0	29.9	4.6	1	B
PRO	C	316	57.1	31.8	6.9	2	B
PRO	O	316	56.1	31.9	6.2	4	B
TRP	N	317	57.1	32.0	8.2	2	B
TRP	CA	317	55.8	32.3	8.8	2	B
TRP	CB	317	56.0	32.6	10.3	1	B
TRP	CG	317	56.9	31.6	11.0	1	B
TRP	CD2	317	56.5	30.3	11.4	1	B
TRP	CE2	317	57.6	29.7	12.0	1	B
TRP	CE3	317	55.3	29.6	11.3	2	B
TRP	CD1	317	58.2	31.8	11.4	1	B
TRP	NE1	317	58.6	30.6	11.9	1	B
TRP	CZ2	317	57.6	28.4	12.4	1	B
TRP	CZ3	317	55.3	28.3	11.7	1	B
TRP	CH2	317	56.4	27.7	12.3	1	B
TRP	C	317	55.1	33.4	8.1	1	B
TRP	O	317	53.9	33.4	7.9	4	B
ASN	N	318	55.9	34.4	7.7	4	B
ASN	CA	318	55.4	35.6	7.1	6	B
ASN	CB	318	56.5	36.6	6.7	10	B
ASN	CG	318	56.8	36.5	5.2	8	B
ASN	OD1	318	56.1	36.9	4.3	10	B
ASN	ND2	318	58.0	36.0	4.9	14	B
ASN	C	318	54.4	35.3	6.0	3	B
ASN	O	318	53.3	35.9	5.9	3	B
ILE	N	319	54.6	34.3	5.1	1	B
ILE	CA	319	53.7	34.1	4.1	1	B
ILE	CB	319	54.3	33.0	3.0	1	B
ILE	CG2	319	55.6	33.5	2.6	1	B
ILE	CG1	319	54.3	31.7	3.6	4	B
ILE	CD1	319	54.7	30.6	2.7	9	B
ILE	C	319	52.4	33.6	4.6	1	B
ILE	O	319	51.3	34.0	4.1	4	B
PHE	N	320	52.4	32.7	5.5	1	B
PHE	CA	320	51.1	32.1	6.1	1	B
PHE	CB	320	51.5	31.0	7.1	1	B
PHE	CG	320	51.9	29.7	6.4	1	B
PHE	CD1	320	51.0	28.8	5.9	1	B
PHE	CD2	320	53.3	29.5	6.2	1	B
PHE	CE1	320	51.4	27.7	5.3	1	B
PHE	CE2	320	53.7	28.4	5.6	1	B
PHE	CZ	320	52.8	27.4	5.1	1	B
PHE	C	320	50.3	33.2	6.8	1	B
PHE	O	320	50.9	34.1	7.5	4	B
PRO	N	321	49.0	33.2	6.7	1	B
PRO	CD	321	48.2	32.2	6.0	1	B
PRO	CA	321	48.1	34.2	7.3	1	B
PRO	CB	321	46.9	34.1	6.4	1	B
PRO	CG	321	46.8	32.7	6.2	1	B
PRO	C	321	47.7	33.9	8.8	1	B
PRO	O	321	47.8	32.7	9.2	1	B
VAL	N	322	47.3	34.9	9.5	1	B
VAL	CA	322	46.8	34.7	10.9	2	B
VAL	CB	322	47.0	35.9	11.8	3	B
VAL	CG1	322	48.5	36.2	11.9	6	B
VAL	CG2	322	46.2	37.0	11.3	4	B
VAL	C	322	45.4	34.3	10.8	2	B
VAL	O	322	44.7	34.8	9.9	1	B
ILE	N	323	44.9	33.5	11.7	1	B
ILE	CA	323	43.5	33.1	11.7	1	B
ILE	CB	323	43.3	31.6	11.8	1	B
ILE	CG2	323	41.9	31.2	11.8	1	B
ILE	CG1	323	44.1	31.0	10.7	1	B
ILE	CD1	323	44.1	29.5	10.8	1	B
ILE	C	323	42.8	33.8	12.9	1	B
ILE	O	323	43.3	33.7	14.0	1	B
SER	N	324	41.7	34.5	12.7	1	B
SER	CA	324	41.0	35.2	13.8	1	B
SER	CB	324	40.9	36.6	13.6	1	B
SER	OG	324	42.2	37.3	13.6	1	B
SER	C	324	39.7	34.6	14.0	1	B
SER	O	324	39.0	34.3	13.0	1	B
LEU	N	325	39.3	34.3	15.3	1	B
LEU	CA	325	38.0	33.7	15.6	1	B
LEU	CB	325	38.2	32.4	16.3	1	B
LEU	CG	325	38.9	31.3	15.6	1	B
LEU	CD1	325	38.9	30.0	16.4	1	B
LEU	CD2	325	38.2	31.0	14.3	1	B
LEU	C	325	37.4	34.7	16.6	1	B
LEU	O	325	38.0	35.1	17.6	1	B
TYR	N	326	36.2	35.2	16.2	1	B
TYR	CA	326	35.4	36.1	17.1	1	B
TYR	CB	326	34.7	37.1	16.2	3	B
TYR	CG	326	35.5	38.2	15.5	1	B
TYR	CD1	326	36.6	37.9	14.8	1	B
TYR	CE1	326	37.4	38.9	14.1	2	B
TYR	CD2	326	35.1	39.5	15.5	1	B
TYR	CE2	326	35.8	40.5	14.9	4	B
TYR	CZ	326	37.0	40.2	14.2	1	B
TYR	OH	326	37.7	41.1	13.5	1	B
TYR	C	326	34.4	35.4	17.9	1	B
TYR	O	326	33.6	34.6	17.4	1	B
LEU	N	327	34.6	35.5	19.2	1	B
LEU	CA	327	33.7	34.9	20.2	1	B
LEU	CB	327	34.5	34.3	21.3	1	B
LEU	CG	327	35.7	33.4	20.9	1	B
LEU	CD1	327	36.6	33.2	22.1	1	B
LEU	CD2	327	35.2	32.1	20.3	1	B
LEU	C	327	32.6	35.8	20.8	1	B
LEU	O	327	33.0	37.0	21.0	2	B
MET	N	328	31.4	35.4	20.9	1	B
MET	CA	328	30.3	36.2	21.5	1	B
MET	CB	328	29.1	35.3	21.7	1	B
MET	CG	328	28.0	36.0	22.4	1	B
MET	SD	328	26.7	34.7	22.8	1	B
MET	CE	328	25.4	35.3	21.9	1	B
MET	C	328	30.8	36.8	22.8	1	B
MET	O	328	31.1	36.1	23.7	1	B
GLY	N	329	30.7	38.1	22.9	1	B
GLY	CA	329	31.1	38.8	24.1	6	B
GLY	C	329	30.1	38.6	25.3	7	B
GLY	O	329	29.1	38.1	25.1	9	B
GLU	N	330	30.5	39.1	26.4	6	B
GLU	CA	330	29.7	39.0	27.6	7	B
GLU	CB	330	30.5	38.9	28.9	13	B
GLU	CG	330	30.7	37.5	29.4	19	B
GLU	CD	330	29.4	36.9	29.9	27	B
GLU	OE1	330	29.4	35.8	30.4	30	B
GLU	OE2	330	28.3	37.5	29.7	29	B
GLU	C	330	28.7	40.2	27.7	6	B
GLU	O	330	27.9	40.2	28.6	9	B
VAL	N	331	28.8	41.2	26.8	5	B
VAL	CA	331	27.9	42.3	26.9	3	B
VAL	CB	331	28.6	43.6	26.7	1	B
VAL	CG1	331	27.8	44.8	27.2	3	B
VAL	CG2	331	30.0	43.5	27.3	4	B
VAL	C	331	26.9	42.1	25.7	5	B
VAL	O	331	27.1	41.3	24.9	5	B
THR	N	332	25.8	42.9	25.7	6	B
THR	CA	332	24.9	42.8	24.7	7	B
THR	CB	332	23.5	43.3	25.1	11	B
THR	OG1	332	23.1	42.8	26.4	11	B
THR	CG2	332	22.4	42.9	24.1	11	B
THR	C	332	25.4	43.5	23.4	4	B
THR	O	332	25.8	44.7	23.5	1	B
ASN	N	333	25.3	42.9	22.3	6	B
ASN	CA	333	25.8	43.4	21.0	7	B
ASN	CB	333	25.1	44.8	20.7	8	B
ASN	CG	333	23.6	44.5	20.4	9	B
ASN	OD1	333	23.2	43.5	19.8	9	B
ASN	ND2	333	22.8	45.5	20.6	5	B
ASN	C	333	27.3	43.7	21.1	6	B
ASN	O	333	27.7	44.8	20.6	9	B
GLN	N	334	28.1	42.8	21.6	7	B
GLN	CA	334	29.5	43.0	21.7	6	B
GLN	CB	334	29.8	43.8	23.0	13	B
GLN	CG	334	31.2	43.8	23.5	20	B
GLN	CD	334	31.6	45.0	24.3	27	B
GLN	OE1	334	32.6	44.9	25.2	29	B
GLN	NE2	334	31.0	46.1	24.1	23	B
GLN	C	334	30.3	41.7	21.8	5	B
GLN	O	334	29.9	40.7	22.4	2	B
SER	N	335	31.4	41.7	21.0	4	B
SER	CA	335	32.3	40.5	21.0	1	B
SER	CB	335	32.0	39.7	19.7	1	B
SER	OG	335	32.3	40.5	18.6	1	B
SER	C	335	33.7	40.9	21.0	1	B
SER	O	335	34.0	42.1	20.9	1	B
PHE	N	336	34.6	40.0	21.0	1	B
PHE	CA	336	36.0	40.2	21.0	1	B
PHE	CB	336	36.6	40.1	22.4	1	B
PHE	CG	336	36.5	38.7	23.0	1	B
PHE	CD1	336	37.5	37.8	22.7	4	B
PHE	CD2	336	35.5	38.4	23.8	1	B
PHE	CE1	336	37.4	36.5	23.3	2	B
PHE	CE2	336	35.4	37.1	24.4	1	B
PHE	CZ	336	36.4	36.2	24.1	1	B
PHE	C	336	36.6	39.1	20.1	1	B
PHE	O	336	35.9	38.1	19.8	1	B
ARG	N	337	37.8	39.2	19.7	1	B
ARG	CA	337	38.4	38.2	18.9	1	B
ARG	CB	337	38.6	38.8	17.5	1	B
ARG	CG	337	39.7	39.8	17.4	1	B
ARG	CD	337	39.8	40.5	16.1	1	B
ARG	NE	337	41.0	41.3	16.0	1	B
ARG	CZ	337	41.1	42.4	15.3	1	B
ARG	NH1	337	40.0	42.8	14.6	1	B
ARG	NH2	337	42.2	43.1	15.3	1	B
ARG	C	337	39.7	37.8	19.4	1	B
ARG	O	337	40.4	38.5	20.2	2	B
ILE	N	338	40.1	36.6	19.0	1	B
ILE	CA	338	41.4	36.0	19.4	1	B
ILE	CB	338	41.2	34.8	20.3	1	B
ILE	CG2	338	40.6	35.2	21.6	1	B
ILE	CG1	338	40.3	33.8	19.6	1	B
ILE	CD1	338	40.2	32.5	20.4	1	B
ILE	C	338	42.1	35.7	18.1	1	B
ILE	O	338	41.4	35.2	17.2	1	B
THR	N	339	43.4	36.0	18.0	2	B
THR	CA	339	44.1	35.7	16.8	1	B
THR	CB	339	44.7	37.0	16.2	1	B
THR	OG1	339	43.7	37.9	16.0	1	B
THR	CG2	339	45.3	36.7	14.8	1	B
THR	C	339	45.3	34.7	17.1	1	B
THR	O	339	46.0	34.9	18.0	3	B
ILE	N	340	45.4	33.7	16.2	1	B
ILE	CA	340	46.5	32.7	16.3	1	B
ILE	CB	340	45.9	31.3	16.4	1	B
ILE	CG2	340	44.9	31.2	17.5	2	B
ILE	CG1	340	45.3	30.9	15.1	1	B
ILE	CD1	340	44.7	29.5	15.1	2	B
ILE	C	340	47.3	32.8	15.1	1	B
ILE	O	340	46.8	33.2	14.0	1	B
LEU	N	341	48.6	32.5	15.2	2	B
LEU	CA	341	49.6	32.6	14.1	1	B
LEU	CB	341	50.9	33.2	14.7	1	B
LEU	CG	341	50.7	34.2	15.8	1	B
LEU	CD1	341	52.0	34.5	16.4	3	B
LEU	CD2	341	50.1	35.5	15.1	5	B
LEU	C	341	49.8	31.3	13.5	1	B
LEU	O	341	49.4	30.2	14.1	1	B
PRO	N	342	50.5	31.2	12.3	1	B
PRO	CD	342	51.3	32.3	11.7	1	B
PRO	CA	342	50.8	30.0	11.7	1	B
PRO	CB	342	51.6	30.4	10.5	2	B
PRO	CG	342	52.3	31.5	11.0	1	B
PRO	C	342	51.5	29.1	12.6	1	B
PRO	O	342	51.4	27.9	12.6	1	B
GLN	N	343	52.4	29.7	13.4	1	B
GLN	CA	343	53.2	29.0	14.4	1	B
GLN	CB	343	53.9	30.0	15.4	1	B
GLN	CG	343	55.1	30.6	14.8	1	B
GLN	CD	343	54.9	31.9	14.0	2	B
GLN	OE1	343	53.8	32.3	13.7	5	B
GLN	NE2	343	56.0	32.5	13.6	1	B
GLN	C	343	52.3	28.0	15.2	3	B
GLN	O	343	52.8	27.0	15.7	2	B
GLN	N	344	51.0	28.4	15.3	3	B
GLN	CA	344	50.1	27.5	16.1	3	B
GLN	CB	344	49.0	28.4	16.7	2	B
GLN	CG	344	49.4	28.9	18.1	4	B
GLN	CD	344	49.9	30.3	18.1	9	B
GLN	OE1	344	50.4	30.7	19.1	18	B
GLN	NE2	344	49.8	30.9	17.0	10	B
GLN	C	344	49.4	26.5	15.2	1	B
GLN	O	344	49.2	25.3	15.7	1	B
TYR	N	345	49.0	26.8	14.0	2	B
TYR	CA	345	48.3	25.8	13.2	1	B
TYR	CB	345	47.2	26.4	12.4	2	B
TYR	CG	345	47.6	27.4	11.3	3	B
TYR	CD1	345	47.9	27.1	10.0	6	B
TYR	CE1	345	48.1	28.1	9.1	4	B
TYR	CD2	345	47.5	28.8	11.6	1	B
TYR	CE2	345	47.7	29.8	10.7	1	B
TYR	CZ	345	48.1	29.4	9.4	1	B
TYR	OH	345	48.2	30.3	8.4	5	B
TYR	C	345	49.3	24.9	12.4	1	B
TYR	O	345	48.8	24.1	11.6	3	B
LEU	N	346	50.5	25.1	12.6	2	B
LEU	CA	346	51.5	24.3	11.9	3	B
LEU	CB	346	52.5	25.2	11.1	1	B
LEU	CG	346	51.8	25.8	9.9	1	B
LEU	CD1	346	52.8	26.4	8.9	1	B
LEU	CD2	346	51.0	24.8	9.1	1	B
LEU	C	346	52.3	23.6	13.1	5	B
LEU	O	346	53.1	24.3	13.8	6	B
ARG	N	347	52.0	22.4	13.3	4	B
ARG	CA	347	52.6	21.6	14.4	3	B
ARG	CB	347	51.6	20.6	14.9	5	B
ARG	CG	347	52.1	19.9	16.1	9	B
ARG	CD	347	50.9	19.1	16.8	14	B
ARG	NE	347	50.3	18.2	15.8	13	B
ARG	CZ	347	50.8	17.1	15.4	14	B
ARG	NH1	347	52.0	16.8	15.8	10	B
ARG	NH2	347	50.2	16.3	14.5	20	B
ARG	C	347	53.9	21.0	14.0	5	B
ARG	O	347	54.0	20.2	13.0	10	B
PRO	N	348	55.0	21.3	14.7	4	B
PRO	CD	348	55.0	22.2	15.9	4	B
PRO	CA	348	56.4	20.7	14.5	2	B
PRO	CB	348	57.2	21.4	15.6	3	B
PRO	CG	348	56.4	22.6	15.9	6	B
PRO	C	348	56.4	19.2	14.6	4	B
PRO	O	348	56.5	18.7	15.7	8	B
VAL	N	349	56.3	18.5	13.5	9	B
VAL	CA	349	56.3	17.0	13.6	15	B
VAL	CB	349	55.6	16.4	12.5	15	B
VAL	CG1	349	54.1	16.0	13.0	21	B
VAL	CG2	349	55.5	17.2	11.3	21	B
VAL	C	349	57.8	16.6	13.5	18	B
VAL	O	349	58.3	16.7	12.4	21	B
GLU	N	350	58.3	16.2	14.6	23	B
GLU	CA	350	59.7	15.8	14.6	25	B
GLU	CB	350	60.0	14.9	15.8	22	B
GLU	CG	350	61.2	13.9	15.6	25	B
GLU	CD	350	62.3	14.6	14.9	24	B
GLU	OE1	350	63.0	13.9	14.1	19	B
GLU	OE2	350	62.6	15.8	15.1	26	B
GLU	C	350	60.1	15.0	13.4	28	B
GLU	O	350	59.5	14.0	13.1	28	B
ASP	N	351	61.0	15.6	12.6	30	B
ASP	CA	351	61.4	15.0	11.3	30	B
ASP	CB	351	62.9	15.4	11.0	31	B
ASP	CG	351	63.4	14.7	9.7	36	B
ASP	OD1	351	62.9	15.1	8.6	34	B
ASP	OD2	351	64.2	13.8	9.8	34	B
ASP	C	351	61.3	13.5	11.3	30	B
ASP	O	351	61.4	12.8	12.4	28	B
VAL	N	352	61.1	12.9	10.1	29	B
VAL	CA	352	61.0	11.4	10.0	30	B
VAL	CB	352	61.3	11.0	8.5	26	B
VAL	CG1	352	61.1	9.5	8.4	22	B
VAL	CG2	352	60.3	11.7	7.6	22	B
VAL	C	352	62.0	10.8	11.0	33	B
VAL	O	352	61.6	10.1	11.9	35	B
ALA	N	353	63.3	11.0	10.8	35	B
ALA	CA	353	64.3	10.4	11.7	35	B
ALA	CB	353	65.1	9.3	11.0	34	B
ALA	C	353	65.3	11.4	12.3	33	B
ALA	O	353	66.5	11.2	12.3	30	B
THR	N	354	64.8	12.6	12.7	32	B
THR	CA	354	65.6	13.7	13.3	31	B
THR	CB	354	66.3	13.2	14.6	28	B
THR	OG1	354	65.5	12.3	15.3	24	B
THR	CG2	354	66.6	14.5	15.5	20	B
THR	C	354	66.6	14.1	12.2	32	B
THR	O	354	67.7	13.5	12.1	33	B
SER	N	355	66.2	15.2	11.4	29	B
SER	CA	355	67.1	15.7	10.4	27	B
SER	CB	355	66.5	15.5	9.0	27	B
SER	OG	355	65.5	16.4	8.7	25	B
SER	C	355	67.4	17.2	10.6	25	B
SER	O	355	66.8	17.8	11.5	19	B
GLN	N	356	68.2	17.7	9.8	26	B
GLN	CA	356	68.6	19.2	9.8	25	B
GLN	CB	356	69.9	19.4	9.1	24	B
GLN	CG	356	71.0	18.6	9.6	33	B
GLN	CD	356	72.3	19.4	9.8	34	B
GLN	OE1	356	72.6	20.2	8.9	31	B
GLN	NE2	356	73.1	19.2	10.9	34	B
GLN	C	356	67.5	20.0	9.1	22	B
GLN	O	356	67.9	20.9	8.3	22	B
ASP	N	357	66.2	19.7	9.4	18	B
ASP	CA	357	65.1	20.4	8.8	13	B
ASP	CB	357	64.6	19.7	7.5	14	B
ASP	CG	357	65.5	20.0	6.3	18	B
ASP	OD1	357	66.7	19.8	6.5	22	B
ASP	OD2	357	64.9	20.4	5.3	17	B
ASP	C	357	64.0	20.6	9.8	10	B
ASP	O	357	63.8	19.7	10.6	12	B
ASP	N	358	63.2	21.7	9.6	8	B
ASP	CA	358	62.1	21.9	10.5	8	B
ASP	CB	358	62.0	23.4	10.8	10	B
ASP	CG	358	63.2	23.9	11.6	13	B
ASP	OD1	358	63.4	25.1	11.6	13	B
ASP	OD2	358	63.9	23.1	12.1	13	B
ASP	C	358	60.9	21.4	9.6	7	B
ASP	O	358	60.8	21.8	8.5	9	B
CYS	N	359	60.1	20.5	10.2	10	B
CYS	CA	359	59.0	20.0	9.4	10	B
CYS	C	359	57.7	20.2	10.2	8	B
CYS	O	359	57.7	20.1	11.4	13	B
CYS	CB	359	59.2	18.5	9.2	10	B
CYS	SG	359	60.6	18.0	8.2	14	B
TYR	N	360	56.6	20.4	9.5	4	B
TYR	CA	360	55.4	20.7	10.2	1	B
TYR	CB	360	55.1	22.2	10.2	1	B
TYR	CG	360	56.2	23.0	10.6	1	B
TYR	CD1	360	57.3	23.3	9.7	1	B
TYR	CE1	360	58.3	24.1	10.2	1	B
TYR	CD2	360	56.2	23.6	11.9	1	B
TYR	CE2	360	57.3	24.3	12.3	1	B
TYR	CZ	360	58.3	24.6	11.4	2	B
TYR	OH	360	59.4	25.4	11.8	5	B
TYR	C	360	54.2	20.0	9.5	2	B
TYR	O	360	54.1	19.8	8.3	1	B
LYS	N	361	53.2	19.7	10.4	1	B
LYS	CA	361	51.9	19.1	9.9	3	B
LYS	CB	361	51.5	17.9	10.7	5	B
LYS	CG	361	52.1	16.6	10.1	14	B
LYS	CD	361	51.4	15.3	10.7	22	B
LYS	CE	361	52.1	14.1	10.1	26	B
LYS	NZ	361	51.7	12.8	10.7	25	B
LYS	C	361	50.9	20.2	10.0	1	B
LYS	O	361	50.8	20.9	11.0	1	B
PHE	N	362	50.0	20.3	9.0	2	B
PHE	CA	362	49.0	21.3	9.1	2	B
PHE	CB	362	48.3	21.4	7.7	2	B
PHE	CG	362	47.3	22.5	7.6	1	B
PHE	CD1	362	47.6	23.8	7.7	2	B
PHE	CD2	362	45.9	22.1	7.4	1	B
PHE	CE1	362	46.7	24.8	7.6	1	B
PHE	CE2	362	45.0	23.1	7.3	1	B
PHE	CZ	362	45.4	24.5	7.4	2	B
PHE	C	362	48.0	20.9	10.2	1	B
PHE	O	362	47.4	19.8	10.1	1	B
ALA	N	363	47.9	21.6	11.2	1	B
ALA	CA	363	47.1	21.3	12.4	1	B
ALA	CB	363	47.7	21.8	13.6	1	B
ALA	C	363	45.6	21.7	12.3	2	B
ALA	O	363	44.9	21.6	13.3	1	B
ILE	N	364	45.1	22.1	11.1	3	B
ILE	CA	364	43.7	22.5	11.0	1	B
ILE	CB	364	43.5	23.9	10.3	1	B
ILE	CG2	364	42.1	24.2	10.2	1	B
ILE	CG1	364	44.2	25.0	11.1	1	B
ILE	CD1	364	44.1	26.3	10.4	1	B
ILE	C	364	43.1	21.4	10.2	2	B
ILE	O	364	43.5	21.2	9.0	5	B
SER	N	365	42.1	20.7	10.8	1	B
SER	CA	365	41.5	19.6	10.0	2	B
SER	CB	365	42.0	18.3	10.5	2	B
SER	OG	365	41.5	18.0	11.8	1	B
SER	C	365	40.0	19.7	10.1	1	B
SER	O	365	39.4	20.3	11.0	1	B
GLN	N	366	39.3	19.1	9.2	3	B
GLN	CA	366	37.8	19.1	9.1	3	B
GLN	CB	366	37.4	18.6	7.7	1	B
GLN	CG	366	38.1	17.4	7.2	8	B
GLN	CD	366	37.7	17.1	5.8	10	B
GLN	OE1	366	36.5	16.8	5.5	13	B
GLN	NE2	366	38.6	17.1	4.8	11	B
GLN	C	366	37.2	18.2	10.2	1	B
GLN	O	366	37.7	17.2	10.6	1	B
SER	N	367	36.0	18.6	10.6	3	B
SER	CA	367	35.2	17.9	11.6	8	B
SER	CB	367	35.2	18.7	12.9	9	B
SER	OG	367	34.2	18.2	13.7	16	B
SER	C	367	33.8	17.7	11.2	11	B
SER	O	367	33.2	18.5	10.4	11	B
SER	N	368	33.2	16.6	11.6	14	B
SER	CA	368	31.8	16.3	11.3	13	B
SER	CB	368	31.7	14.8	11.0	13	B
SER	OG	368	32.1	14.0	12.1	21	B
SER	C	368	30.9	16.5	12.6	10	B
SER	O	368	29.7	16.4	12.5	12	B
THR	N	369	31.6	17.0	13.6	7	B
THR	CA	369	30.9	17.3	14.9	7	B
THR	CB	369	31.4	16.4	16.0	10	B
THR	OG1	369	32.8	16.4	16.1	11	B
THR	CG2	369	30.9	14.9	15.8	9	B
THR	C	369	30.9	18.8	15.3	6	B
THR	O	369	30.8	19.1	16.5	1	B
GLY	N	370	31.0	19.7	14.4	5	B
GLY	CA	370	31.1	21.1	14.7	6	B
GLY	C	370	32.5	21.7	14.9	6	B
GLY	O	370	33.5	21.0	14.5	7	B
THR	N	371	32.7	22.8	15.5	2	B
THR	CA	371	34.0	23.4	15.8	1	B
THR	CB	371	33.9	24.9	15.7	1	B
THR	OG1	371	33.8	25.4	14.4	1	B
THR	CG2	371	35.1	25.5	16.3	1	B
THR	C	371	34.6	23.0	17.1	1	B
THR	O	371	33.9	23.1	18.1	1	B
VAL	N	372	35.8	22.6	17.1	2	B
VAL	CA	372	36.5	22.2	18.3	1	B
VAL	CB	372	36.9	20.7	18.2	1	B
VAL	CG1	372	37.7	20.4	19.4	1	B
VAL	CG2	372	35.6	19.9	18.1	1	B
VAL	C	372	37.8	23.0	18.4	1	B
VAL	O	372	38.7	23.0	17.6	1	B
MET	N	373	37.9	23.8	19.5	1	B
MET	CA	373	39.0	24.6	19.8	1	B
MET	CB	373	38.6	25.9	20.5	1	B
MET	CG	373	38.2	27.0	19.6	1	B
MET	SD	373	36.9	28.1	20.3	2	B
MET	CE	373	37.9	29.4	20.9	9	B
MET	C	373	40.1	23.8	20.5	1	B
MET	O	373	40.2	23.9	21.7	1	B
GLY	N	374	40.8	23.0	19.8	1	B
GLY	CA	374	41.8	22.1	20.3	1	B
GLY	C	374	43.1	22.8	20.8	1	B
GLY	O	374	43.2	24.1	21.0	2	B
ALA	N	375	44.1	22.0	21.1	1	B
ALA	CA	375	45.4	22.6	21.6	1	B
ALA	CB	375	46.3	21.5	21.9	1	B
ALA	C	375	46.1	23.6	20.7	1	B
ALA	O	375	46.9	24.3	21.2	5	B
VAL	N	376	45.8	23.7	19.4	1	B
VAL	CA	376	46.5	24.7	18.6	1	B
VAL	CB	376	46.3	24.5	17.1	1	B
VAL	CG1	376	46.4	23.0	16.8	1	B
VAL	CG2	376	45.1	25.1	16.6	3	B
VAL	C	376	45.9	26.0	19.0	1	B
VAL	O	376	46.7	27.0	19.1	1	B
ILE	N	377	44.6	26.1	19.2	1	B
ILE	CA	377	44.0	27.4	19.5	2	B
ILE	CB	377	42.4	27.3	19.4	2	B
ILE	CG2	377	41.8	28.6	20.1	1	B
ILE	CG1	377	42.0	27.2	18.0	4	B
ILE	CD1	377	42.5	28.3	17.1	6	B
ILE	C	377	44.4	27.7	21.0	3	B
ILE	O	377	44.6	28.9	21.3	3	B
MET	N	378	44.5	26.7	21.8	3	B
MET	CA	378	44.8	26.9	23.2	4	B
MET	CB	378	44.4	25.7	24.0	1	B
MET	CG	378	42.9	25.5	24.2	2	B
MET	SD	378	42.5	24.2	25.3	1	B
MET	CE	378	41.9	25.0	26.6	4	B
MET	C	378	46.3	27.2	23.4	6	B
MET	O	378	46.7	28.0	24.2	8	B
GLU	N	379	47.2	26.5	22.6	8	B
GLU	CA	379	48.6	26.7	22.7	8	B
GLU	CB	379	49.4	25.9	21.7	10	B
GLU	CG	379	49.6	24.4	22.1	17	B
GLU	CD	379	50.5	23.7	21.1	24	B
GLU	OE1	379	50.7	22.5	21.3	27	B
GLU	OE2	379	51.0	24.4	20.2	25	B
GLU	C	379	48.9	28.2	22.5	7	B
GLU	O	379	50.1	28.7	22.6	11	B
GLY	N	380	47.9	29.0	22.1	5	B
GLY	CA	380	48.1	30.4	21.8	2	B
GLY	C	380	47.8	31.3	23.0	1	B
GLY	O	380	48.5	32.3	23.2	1	B
PHE	N	381	46.8	30.9	23.8	1	B
PHE	CA	381	46.4	31.8	24.8	1	B
PHE	CB	381	45.1	32.4	24.5	1	B
PHE	CG	381	44.9	32.7	23.1	4	B
PHE	CD1	381	44.5	31.7	22.2	2	B
PHE	CD2	381	45.2	33.9	22.5	2	B
PHE	CE1	381	44.4	31.9	20.9	4	B
PHE	CE2	381	45.1	34.1	21.2	1	B
PHE	CZ	381	44.7	33.1	20.3	5	B
PHE	C	381	46.3	31.2	26.2	1	B
PHE	O	381	46.5	30.0	26.4	4	B
TYR	N	382	46.0	32.0	27.2	1	B
TYR	CA	382	45.8	31.5	28.5	1	B
TYR	CB	382	46.3	32.6	29.5	1	B
TYR	CG	382	46.2	32.2	31.0	1	B
TYR	CD1	382	46.8	31.1	31.5	1	B
TYR	CE1	382	46.7	30.8	32.9	1	B
TYR	CD2	382	45.4	33.0	31.9	1	B
TYR	CE2	382	45.4	32.7	33.2	1	B
TYR	CZ	382	46.0	31.6	33.7	1	B
TYR	OH	382	45.9	31.2	35.0	1	B
TYR	C	382	44.3	31.4	28.6	1	B
TYR	O	382	43.6	32.4	28.4	6	B
VAL	N	383	43.8	30.2	28.9	1	B
VAL	CA	383	42.4	30.0	28.9	1	B
VAL	CB	383	42.0	28.7	28.1	1	B
VAL	CG1	383	40.5	28.6	28.1	4	B
VAL	CG2	383	42.6	28.9	26.7	1	B
VAL	C	383	41.9	29.8	30.3	1	B
VAL	O	383	42.5	29.1	31.1	1	B
VAL	N	384	40.9	30.5	30.7	1	B
VAL	CA	384	40.3	30.5	32.0	1	B
VAL	CB	384	40.2	31.8	32.7	1	B
VAL	CG1	384	39.3	31.8	33.9	1	B
VAL	CG2	384	41.5	32.4	33.0	1	B
VAL	C	384	38.9	29.8	32.0	1	B
VAL	O	384	38.0	30.4	31.3	3	B
PHE	N	385	38.7	28.7	32.7	1	B
PHE	CA	385	37.4	28.1	32.8	1	B
PHE	CB	385	37.6	26.6	32.7	1	B
PHE	CG	385	38.2	26.1	31.4	1	B
PHE	CD1	385	37.4	25.6	30.4	2	B
PHE	CD2	385	39.5	26.3	31.1	2	B
PHE	CE1	385	37.9	25.2	29.1	1	B
PHE	CE2	385	40.0	26.0	29.8	1	B
PHE	CZ	385	39.2	25.4	28.9	1	B
PHE	C	385	36.7	28.5	34.0	2	B
PHE	O	385	36.7	27.8	35.0	1	B
ASP	N	386	36.1	29.6	34.0	2	B
ASP	CA	386	35.4	30.2	35.1	1	B
ASP	CB	386	35.1	31.7	34.9	3	B
ASP	CG	386	35.0	32.5	36.1	2	B
ASP	OD1	386	35.0	31.8	37.2	4	B
ASP	OD2	386	34.9	33.7	36.0	5	B
ASP	C	386	34.0	29.5	35.2	1	B
ASP	O	386	33.0	30.1	35.0	2	B
ARG	N	387	34.1	28.2	35.6	2	B
ARG	CA	387	32.8	27.4	35.7	2	B
ARG	CB	387	33.1	26.1	36.3	1	B
ARG	CG	387	33.8	25.1	35.4	1	B
ARG	CD	387	34.7	24.2	36.1	2	B
ARG	NE	387	34.1	23.3	37.0	2	B
ARG	CZ	387	33.3	22.3	36.7	2	B
ARG	NH1	387	33.0	22.1	35.5	3	B
ARG	NH2	387	32.7	21.6	37.7	5	B
ARG	C	387	31.8	28.2	36.6	2	B
ARG	O	387	30.7	28.4	36.2	2	B
ALA	N	388	32.3	28.6	37.7	1	B
ALA	CA	388	31.4	29.4	38.7	4	B
ALA	CB	388	32.3	30.0	39.7	5	B
ALA	C	388	30.6	30.4	38.0	4	B
ALA	O	388	29.4	30.4	38.0	6	B
ARG	N	389	31.3	31.4	37.3	5	B
ARG	CA	389	30.5	32.4	36.7	5	B
ARG	CB	389	31.4	33.7	36.6	7	B
ARG	CG	389	31.8	34.2	38.0	12	B
ARG	CD	389	32.3	35.7	38.0	11	B
ARG	NE	389	31.3	36.6	37.5	16	B
ARG	CZ	389	31.5	37.9	37.3	20	B
ARG	NH1	389	32.7	38.4	37.6	24	B
ARG	NH2	389	30.5	38.7	36.9	21	B
ARG	C	389	30.0	32.1	35.3	4	B
ARG	O	389	29.4	32.9	34.6	2	B
LYS	N	390	30.1	30.8	34.9	5	B
LYS	CA	390	29.6	30.3	33.7	6	B
LYS	CB	390	28.1	30.4	33.7	9	B
LYS	CG	390	27.3	29.6	32.7	15	B
LYS	CD	390	25.8	29.8	32.9	22	B
LYS	CE	390	25.0	28.9	31.9	26	B
LYS	NZ	390	23.5	29.2	32.0	27	B
LYS	C	390	30.1	31.0	32.5	4	B
LYS	O	390	29.4	31.6	31.7	4	B
ARG	N	391	31.5	31.0	32.3	3	B
ARG	CA	391	32.1	31.7	31.2	3	B
ARG	CB	391	32.0	33.2	31.4	6	B
ARG	CG	391	32.8	33.6	32.7	8	B
ARG	CD	391	32.9	35.1	33.0	7	B
ARG	NE	391	33.8	35.4	34.2	4	B
ARG	CZ	391	34.1	36.6	34.6	1	B
ARG	NH1	391	33.8	37.7	34.0	5	B
ARG	NH2	391	34.9	36.7	35.7	1	B
ARG	C	391	33.5	31.3	30.9	1	B
ARG	O	391	34.1	30.7	31.8	1	B
ILE	N	392	34.1	31.7	29.8	2	B
ILE	CA	392	35.4	31.3	29.5	1	B
ILE	CB	392	35.5	30.3	28.4	1	B
ILE	CG2	392	36.9	30.1	27.8	1	B
ILE	CG1	392	35.0	28.9	28.9	1	B
ILE	CD1	392	35.0	27.8	27.9	1	B
ILE	C	392	36.2	32.5	29.1	2	B
ILE	O	392	35.7	33.4	28.3	1	B
GLY	N	393	37.4	32.7	29.6	1	B
GLY	CA	393	38.3	33.8	29.2	1	B
GLY	C	393	39.6	33.4	28.6	1	B
GLY	O	393	40.2	32.5	28.9	1	B
PHE	N	394	39.9	34.2	27.6	3	B
PHE	CA	394	41.2	34.1	26.8	4	B
PHE	CB	394	40.9	33.9	25.3	1	B
PHE	CG	394	40.1	32.7	25.0	1	B
PHE	CD1	394	38.7	32.6	25.4	1	B
PHE	CD2	394	40.5	31.7	24.2	1	B
PHE	CE1	394	37.9	31.6	25.0	1	B
PHE	CE2	394	39.7	30.6	23.8	1	B
PHE	CZ	394	38.4	30.6	24.2	1	B
PHE	C	394	42.0	35.4	26.9	3	B
PHE	O	394	41.5	36.5	26.8	1	B
ALA	N	395	43.3	35.2	27.1	3	B
ALA	CA	395	44.3	36.3	27.2	1	B
ALA	CB	395	44.6	36.6	28.6	2	B
ALA	C	395	45.5	35.7	26.5	1	B
ALA	O	395	45.7	34.5	26.5	1	B
VAL	N	396	46.4	36.6	26.0	2	B
VAL	CA	396	47.6	36.2	25.3	2	B
VAL	CB	396	48.3	37.4	24.6	1	B
VAL	CG1	396	49.4	36.8	23.7	1	B
VAL	CG2	396	47.4	38.2	23.9	1	B
VAL	C	396	48.5	35.4	26.2	5	B
VAL	O	396	49.1	35.9	27.2	2	B
SER	N	397	48.8	34.2	25.8	7	B
SER	CA	397	49.6	33.3	26.5	10	B
SER	CB	397	49.6	31.9	25.9	14	B
SER	OG	397	50.4	31.0	26.6	21	B
SER	C	397	51.1	33.7	26.5	11	B
SER	O	397	51.7	33.9	25.4	17	B
ALA	N	398	51.6	34.0	27.7	8	B
ALA	CA	398	53.0	34.4	27.8	10	B
ALA	CB	398	53.2	34.8	29.3	11	B
ALA	C	398	54.0	33.4	27.4	11	B
ALA	O	398	55.2	33.7	27.4	12	B
CYS	N	399	53.5	32.2	27.0	8	B
CYS	CA	399	54.4	31.2	26.5	8	B
CYS	C	399	54.1	30.7	25.2	6	B
CYS	O	399	54.4	29.6	24.8	7	B
CYS	CB	399	54.4	30.0	27.5	9	B
CYS	SG	399	52.8	29.1	27.3	11	B
HIS	N	400	53.5	31.6	24.3	5	B
HIS	CA	400	53.2	31.1	23.0	9	B
HIS	CB	400	51.9	31.7	22.5	7	B
HIS	CG	400	52.0	33.0	21.8	4	B
HIS	CD2	400	52.1	33.3	20.5	2	B
HIS	ND1	400	52.1	34.2	22.5	6	B
HIS	CE1	400	52.2	35.2	21.6	7	B
HIS	NE2	400	52.2	34.7	20.4	6	B
HIS	C	400	54.3	31.4	22.0	12	B
HIS	O	400	55.0	32.4	22.1	15	B
VAL	N	401	54.4	30.5	21.0	13	B
VAL	CA	401	55.4	30.7	20.0	11	B
VAL	CB	401	55.6	29.4	19.2	8	B
VAL	CG1	401	56.7	29.6	18.2	10	B
VAL	CG2	401	55.9	28.3	20.1	6	B
VAL	C	401	54.9	31.8	19.1	13	B
VAL	O	401	53.7	31.9	18.8	13	B
HIS	N	402	55.9	32.7	18.7	12	B
HIS	CA	402	55.6	33.8	17.8	10	B
HIS	CB	402	54.9	34.9	18.5	8	B
HIS	CG	402	55.7	35.6	19.5	9	B
HIS	CD2	402	56.2	36.9	19.6	11	B
HIS	ND1	402	56.3	34.9	20.6	12	B
HIS	CE1	402	57.0	35.8	21.3	11	B
HIS	NE2	402	57.0	37.0	20.7	12	B
HIS	C	402	56.9	34.3	17.2	9	B
HIS	O	402	57.9	34.3	17.9	13	B
ASP	N	403	56.9	34.8	16.0	9	B
ASP	CA	403	58.1	35.3	15.4	7	B
ASP	CB	403	58.0	35.2	13.9	8	B
ASP	CG	403	56.9	36.1	13.3	9	B
ASP	OD1	403	56.9	37.3	13.7	9	B
ASP	OD2	403	56.1	35.5	12.6	12	B
ASP	C	403	58.3	36.7	15.9	8	B
ASP	O	403	57.5	37.2	16.7	7	B
GLU	N	404	59.4	37.3	15.4	8	B
GLU	CA	404	59.8	38.7	15.7	8	B
GLU	CB	404	61.1	39.0	15.0	6	B
GLU	CG	404	61.3	40.5	14.8	16	B
GLU	CD	404	62.6	40.8	14.0	19	B
GLU	OE1	404	62.8	40.2	12.9	20	B
GLU	OE2	404	63.3	41.7	14.4	23	B
GLU	C	404	58.7	39.7	15.4	7	B
GLU	O	404	58.5	40.7	16.1	8	B
PHE	N	405	58.0	39.5	14.2	6	B
PHE	CA	405	57.0	40.5	13.8	3	B
PHE	CB	405	57.0	40.5	12.2	3	B
PHE	CG	405	58.3	40.6	11.6	6	B
PHE	CD1	405	59.1	39.5	11.4	4	B
PHE	CD2	405	58.8	41.9	11.3	9	B
PHE	CE1	405	60.4	39.7	10.9	6	B
PHE	CE2	405	60.1	42.1	10.8	8	B
PHE	CZ	405	60.9	41.0	10.6	8	B
PHE	C	405	55.6	40.4	14.3	3	B
PHE	O	405	55.1	41.3	14.8	6	B
ARG	N	406	55.0	39.2	14.1	2	B
ARG	CA	406	53.6	39.0	14.6	3	B
ARG	CB	406	52.8	38.3	13.6	6	B
ARG	CG	406	52.7	39.0	12.2	11	B
ARG	CD	406	51.8	38.2	11.3	9	B
ARG	NE	406	52.2	36.9	11.1	7	B
ARG	CZ	406	52.0	36.1	10.0	4	B
ARG	NH1	406	51.3	36.7	9.0	3	B
ARG	NH2	406	52.3	34.9	10.0	5	B
ARG	C	406	53.5	38.4	16.0	4	B
ARG	O	406	54.5	37.9	16.5	8	B
THR	N	407	52.3	38.3	16.5	3	B
THR	CA	407	52.1	37.7	17.8	2	B
THR	CB	407	52.5	38.7	18.9	4	B
THR	OG1	407	52.2	38.1	20.2	4	B
THR	CG2	407	51.6	40.0	18.8	5	B
THR	C	407	50.6	37.4	18.0	1	B
THR	O	407	49.7	38.0	17.4	1	B
ALA	N	408	50.4	36.3	18.7	1	B
ALA	CA	408	49.0	35.9	19.0	1	B
ALA	CB	408	49.1	34.7	20.0	1	B
ALA	C	408	48.4	37.1	19.7	1	B
ALA	O	408	49.2	38.0	20.1	3	B
ALA	N	409	47.1	37.2	19.8	1	B
ALA	CA	409	46.5	38.3	20.4	2	B
ALA	CB	409	46.7	39.5	19.5	6	B
ALA	C	409	45.0	38.2	20.7	2	B
ALA	O	409	44.3	37.4	20.1	4	B
VAL	N	410	44.6	39.0	21.7	1	B
VAL	CA	410	43.2	39.0	22.1	1	B
VAL	CB	410	43.1	38.4	23.5	1	B
VAL	CG1	410	41.6	38.4	23.9	5	B
VAL	CG2	410	43.7	37.1	23.6	3	B
VAL	C	410	42.7	40.4	22.1	2	B
VAL	O	410	43.2	41.3	22.8	6	B
GLU	N	411	41.7	40.7	21.3	1	B
GLU	CA	411	41.2	42.1	21.2	2	B
GLU	CB	411	41.8	42.7	19.9	7	B
GLU	CG	411	43.4	42.9	20.0	12	B
GLU	CD	411	43.9	43.2	18.7	12	B
GLU	OE1	411	45.0	44.0	18.6	10	B
GLU	OE2	411	43.4	42.8	17.6	16	B
GLU	C	411	39.7	42.3	21.1	3	B
GLU	O	411	39.0	41.5	20.6	4	B
GLY	N	412	39.3	43.5	21.6	1	B
GLY	CA	412	37.9	43.8	21.6	1	B
GLY	C	412	37.7	45.3	21.9	1	B
GLY	O	412	38.6	45.9	22.2	1	B
PRO	N	413	36.4	45.8	21.9	1	B
PRO	CD	413	36.1	47.1	22.5	1	B
PRO	CA	413	35.2	45.0	21.7	2	B
PRO	CB	413	34.2	45.6	22.6	1	B
PRO	CG	413	34.6	47.1	22.5	1	B
PRO	C	413	34.8	45.2	20.2	4	B
PRO	O	413	35.2	46.2	19.6	7	B
PHE	N	414	34.0	44.4	19.7	3	B
PHE	CA	414	33.5	44.5	18.3	3	B
PHE	CB	414	34.1	43.4	17.4	5	B
PHE	CG	414	35.6	43.4	17.4	5	B
PHE	CD1	414	36.3	42.6	18.2	11	B
PHE	CD2	414	36.2	44.3	16.6	9	B
PHE	CE1	414	37.7	42.6	18.3	13	B
PHE	CE2	414	37.6	44.4	16.6	13	B
PHE	CZ	414	38.4	43.5	17.5	13	B
PHE	C	414	32.0	44.5	18.2	6	B
PHE	O	414	31.4	43.5	18.8	10	B
VAL	N	415	31.4	45.5	17.6	6	B
VAL	CA	415	30.0	45.5	17.5	8	B
VAL	CB	415	29.4	46.8	16.9	6	B
VAL	CG1	415	28.0	47.0	17.2	7	B
VAL	CG2	415	30.2	48.0	17.3	9	B
VAL	C	415	29.5	44.3	16.6	7	B
VAL	O	415	30.0	44.2	15.5	7	B
THR	N	416	28.6	43.5	17.2	8	B
THR	CA	416	28.1	42.4	16.4	7	B
THR	CB	416	28.9	41.1	16.7	1	B
THR	OG1	416	30.3	41.4	16.6	1	B
THR	CG2	416	28.5	40.1	15.6	2	B
THR	C	416	26.7	42.2	17.0	10	B
THR	O	416	26.5	42.1	18.2	13	B
LEU	N	417	25.7	42.2	16.1	9	B
LEU	CA	417	24.3	42.1	16.4	8	B
LEU	CB	417	23.5	43.1	15.5	6	B
LEU	CG	417	24.0	44.5	15.5	8	B
LEU	CD1	417	23.5	45.2	14.2	5	B
LEU	CD2	417	23.5	45.3	16.7	8	B
LEU	C	417	23.8	40.7	16.3	8	B
LEU	O	417	24.3	40.0	15.4	6	B
ASP	N	418	22.8	40.4	17.1	13	B
ASP	CA	418	22.2	39.0	17.0	17	B
ASP	CB	418	21.4	38.9	15.7	21	B
ASP	CG	418	20.3	40.0	15.6	27	B
ASP	OD1	418	20.0	40.3	14.4	25	B
ASP	OD2	418	19.8	40.5	16.6	27	B
ASP	C	418	23.2	37.9	17.0	17	B
ASP	O	418	23.2	37.0	16.1	19	B
MET	N	419	24.1	37.9	18.0	16	B
MET	CA	419	25.1	36.9	18.1	14	B
MET	CB	419	26.1	37.2	19.2	9	B
MET	CG	419	26.9	38.5	18.8	10	B
MET	SD	419	28.1	38.9	20.0	5	B
MET	CE	419	27.2	39.9	21.1	14	B
MET	C	419	24.6	35.4	18.4	15	B
MET	O	419	25.2	34.5	17.9	17	B
GLU	N	420	23.5	35.3	19.1	19	B
GLU	CA	420	23.0	34.0	19.4	21	B
GLU	CB	420	22.4	34.0	20.8	24	B
GLU	CG	420	22.4	32.6	21.5	26	B
GLU	CD	420	22.8	32.7	23.0	27	B
GLU	OE1	420	22.4	33.7	23.7	27	B
GLU	OE2	420	23.6	31.8	23.5	23	B
GLU	C	420	21.9	33.6	18.4	22	B
GLU	O	420	21.9	34.1	17.3	22	B
GLU	OXT	420	21.0	32.8	18.8	21	B
The structural coordinates for the above-described BACE crystal are set forth below.
“Res.” refers to the amino acid whose atomic coordinates have been determined.
“Atom” refers to the atom, of the corresponding residue, whose coordinates have been determined.
“#” refers to the amino acid number of the corresponding residue.
“X”, “Y” and Z” refer to the crystallographically determined atomic position determined for each atom.
“B” refers to a thermal factor that measures movement of the atom around its atomic center.
“C” refers to the molecule to which the corresponding residue belongs.

Example 8

[0098] Crystallization of SF-9 Derived β-Secretase (Pyramidal).

[0099] ProBACE (SEQ ID NO:2) in 20 mM Hepes, pH 7.5, 150 mM NaCl was concentrated by centrifugal filtration to 0.18 to 0.36 mM (10-20 mg / ml) followed by ultra-centrifuigation prior to crystallization. Vapor diffusion crystallization experiments were conducted using the hanging drop method. Crystals were grown from a droplet containing 1 μl of protein and 1 μl of the reservoir solution (0.1 M sodium citrate (Fluka BioChemika, Germany), pH 4.0, 10-30 % polyethylene glycol 6000 (Fluka BioChemika, Germany), and 0.2-1.0 M lithium chloride (Fluka BioChemika, Germany). At pH 4.0, the proBACE was autoprocessed to BACE (SEQ ID NO: 4) within the droplet. Crystallization plates were incubated at 4° C., which grew pyramidal crystals (0.05×0.05×0.05 mm) over 40-120 days (based on mass spectral and immunoblot data of redissolved crystals consistent with BACE SEQ ID NO: 4)

BACE
SEQ ID NO: 4
(Residues 27-429 of SEQ ID NO: 2)
Molecular weight 47.8 KDa
ALTERNATIVE PROCESSING (CAT DOMAIN, 403 AA)
DEEPEEPGRR GSFVEMVDNL RGKSGQGYYV EMTVGSPPQT
LNILVDTGSS NFAVGAAPHP FLHRYYQRQL SSTYRDLRKG
VYVPYTQGKW EGELGTDLVS IPHGPNVTVR ANIAAITESD
KFFINGSNWE GILGLAYAEI ARPDDSLEPF FDSLVKQTHV
PNLFSLQLCG AGFPLNQSEV LASVGGSMII GGIDHSLYTG
SLWYTPIRRE WYYEVIIVRV EINGQDLKMD CKEYNYDKSI
VDSGTTNLRL PKKVFEAAVK SIKAASSTEK FPDGFWLGEQ
LVCWQAGTTP WNIFPVISLY LMGEVTNQSF RITILPQQYL
RPVEDVATSQ DDCYKFAISQ SSTGTVMGAV IMEGFYVVFD
RARKRIGFAV SACHVHDEFR TAAVEGPFVT LDMEDCGYNI
PQT

Example 9

[0100] BACE/OM-99-2 Crystalline Complex

[0101] Auto processing step. ProBACE (SEQ ID NO:2) in 100 mM sodium acetate, pH 4.0, was concentrated by centrifugal filtration to 0.09 to 0.18 mM (5-10 mg / ml). The concentrate was incubated at 22° C. for 18 hours. The resulting mixture was mostly BACE (SEQ ID NO: 5) as analyzed by N-terminal, mass spectral and immunoblot analysis.

[0102] Alternatively, ProBACE may be autoprocessed as follows. ProBACE was concentrated to 10 mg/ml, mixed with 1 volume of 100 mM NaOAc, pH 4.0, and was dialyzed against the same buffer with mild stirring for 9 -16 h at room temperature. At the end of the reaction, the mixture was adjusted to pH 8.0 by adding 0.7 volume of 1 M Hepes buffer, pH 8.0, and the solution was immediately applied to Superdex 200 (High Load, 26/60, Amersham Pharmacia, Piscataway, N.J.), equilibrated in 20 mM Hepes, pH 7.5, 150 mM NaCl. The fractions containing BACE of >95% purity were concentrated, flash-frozen in liquid N2, and stored at −80° C.

BACE
SEQ ID NO: 5
(Residues 22-429 OF SEQ ID NO: 2)
LPRETDEEPE EPGRRGSFVE MVDNLRGKSG QGYYVEMTVG
SPPQTLNILV DTGSSNFAVG AAPHPFLHRY YQRQLSSTYR
DLRKGVYVPY TQGKWEGELG TDLVSIPHGP NVTVRANIAA
ITESDKFFIN GSNWEGILGL AYAEIARPDD SLEPFFDSLV
KQTHVPNLFS LQLCGAGFPL NQSEVLASVG GSMIIGGIDH
SLYTGSLWYT PIRREWYYEV IIVRVEINGQ DLKMDCKEYN
YDKSIVDSGT TNLRLPKKVF EAAVKSIKAA SSTEKFPDGF
WLGEQLVCWQ AGTTPWNIFP VISLYLMGEV TNQSFRITIL
PQQYLRPVED VATSQDDCYK FAISQSSTGT VMGAVIMEGF
YVVFDRARKR IGFAVSACHV HDEFRTAAVE GPFVTLDMED
CGYNIPQT

[0103] Processing. The processed BACE (SEQ ID NO: 5) was complexed with OM-99-2 (Hong, et al., (2000) Science 290: 150-153; Bachem Bioscience Inc.; King of Prussia, Pa.), an inhibitor of BACE at a 1:5 molar ratio.

[0104] It should be noted that OM-99-2 is a transition state mimetic that is also characterized by the structure EVN{(2R,4S,5S)-5-amino-4-hydroxy-2,7-dimethyl-octsnoyl}AEF. The chemical structure of OM-99-2 is shown below: 3

[0105] The complex was then incubated on ice for 5 minutes in 20 mM Hepes, pH 7.5, 150 mM NaCl was concentrated by centrifugal filtration to 0.18 to 0.36 mM (10-20 mg /ml) followed by ultra-centrifugation prior to crystallization. Vapor diffusion crystallization experiments were conducted using the hanging drop method. Crystals were grown from a droplet containing 1 μl of protein and 1 μl of the reservoir solution (0.1 M TRIS (Fluka BioChemika, Germany), pH 8.0, 10-30 % polyethylene glycol 3000 (Fluka BioChemika, Germany), and 0.1-1.0 M calcium acetate (Fluka BioChemika, Germany). Crystallization plates were incubated at 4° C., which grew rectangular rods (0.04×0.4 mm) over 3-5 days.

[0106] Crystals were removed from the crystallization droplet by addition of 20% glycerol, which permitted freezing under both cold nitrogen stream and liquid propane. Diffraction data of β-secretase crystal was determined from a Rigaku R-Axis IV image plate detector mounted on a Rigaku RU-HR rotating anode generator Cu radiation 1.54 Å operating at 100 mA and 50 kV.

[0107] Data Collection Statistics:

Resolution                       50.0-2.25 Å
No. of collected reflections     227292
No. of unique reflections (F >= 0) 44920
R-sym                            6.7%
Percent of theoretical (I/s >= 1) 97.1%
Unit Cell                        a = 54.96 Å, b = 99.42 Å,
                                 c = 94.83 Å, α = 90.0
                                 β = 107.0 γ = 90.0°
Space Group                      P212121
Asymmetric unit                  2 molecules

[0108]

TABLE 3
Structural coordinates for BACE/OM-99-2 Complex.
Res.	At.	Ch.	#	X	Y	Z	B
SER	CB	A	38	−3.8	−38.4	34.5	72
SER	OG	A	38	−4.3	−39.2	35.6	74
SER	C	A	38	−2.0	−38.0	32.9	68
SER	O	A	38	−2.5	−38.2	31.8	69
SER	N	A	38	−1.4	−38.6	35.2	69
SER	CA	A	38	−2.4	−38.8	34.1	70
PHE	N	A	39	−1.0	−37.1	33.1	63
PHE	CA	A	39	−0.5	−36.3	32.0	58
PHE	CB	A	39	−1.0	−34.8	32.3	55
PHE	CG	A	39	−2.4	−34.7	32.4	54
PHE	CD1	A	39	−3.1	−35.0	33.6	53
PHE	CD2	A	39	−3.2	−34.2	31.4	54
PHE	CE1	A	39	−4.5	−34.9	33.8	53
PHE	CE2	A	39	−4.6	−34.1	31.5	54
PHE	CZ	A	39	−5.2	−34.4	32.7	55
PHE	C	A	39	1.0	−36.4	31.9	57
PHE	O	A	39	1.7	−35.4	31.6	57
VAL	N	A	40	1.5	−37.6	32.1	56
VAL	CA	A	40	3.0	−37.8	32.0	55
VAL	CB	A	40	3.2	−39.4	32.2	56
VAL	CG1	A	40	4.7	−39.7	32.1	57
VAL	CG2	A	40	2.6	−39.9	33.4	57
VAL	C	A	40	3.6	−37.3	30.8	56
VAL	O	A	40	4.9	−37.1	30.8	55
GLU	N	A	41	2.9	−37.0	29.7	57
GLU	CA	A	41	3.5	−36.5	28.5	55
GLU	CB	A	41	2.6	−36.8	27.2	61
GLU	CG	A	41	2.2	−38.2	27.0	67
GLU	CD	A	41	1.3	−38.8	28.1	70
GLU	OE1	A	41	0.8	−38.1	28.9	70
GLU	OE2	A	41	1.3	−40.1	28.2	72
GLU	C	A	41	3.8	−35.0	28.6	50
GLU	O	A	41	4.5	−34.5	27.8	48
MET	N	A	42	3.1	−34.4	29.5	44
MET	CA	A	42	3.3	−32.9	29.7	40
MET	CB	A	42	1.9	−32.2	29.8	40
MET	CG	A	42	1.1	−32.4	28.5	39
MET	SD	A	42	−0.5	−31.6	28.6	43
MET	CE	A	42	−1.5	−32.9	29.0	44
MET	C	A	42	4.2	−32.6	30.9	37
MET	O	A	42	4.5	−31.4	31.1	38
VAL	N	A	43	4.5	−33.5	31.7	34
VAL	CA	A	43	5.4	−33.3	32.9	33
VAL	CB	A	43	5.4	−34.5	33.8	33
VAL	CG1	A	43	6.4	−34.1	35.0	33
VAL	CG2	A	43	4.0	−34.8	34.4	31
VAL	C	A	43	6.8	−32.9	32.4	31
VAL	O	A	43	7.4	−33.5	31.6	32
ASP	N	A	44	7.2	−31.8	33.0	29
ASP	CA	A	44	8.6	−31.3	32.7	35
ASP	CB	A	44	9.6	−32.3	33.1	42
ASP	CG	A	44	11.0	−31.8	32.9	50
ASP	OD1	A	44	11.7	−31.5	33.9	56
ASP	OD2	A	44	11.5	−31.8	31.8	54
ASP	C	A	44	8.7	−30.7	31.3	32
ASP	O	A	44	9.7	−30.8	30.7	32
ASN	N	A	45	7.6	−30.2	30.7	27
ASN	CA	A	45	7.6	−29.6	29.4	25
ASN	CB	A	45	6.3	−29.8	28.7	27
ASN	CG	A	45	5.2	−29.1	29.4	26
ASN	OD1	A	45	5.3	−28.5	30.4	26
ASN	ND2	A	45	4.0	−29.2	28.8	22
ASN	C	A	45	8.1	−28.2	29.4	27
ASN	O	A	45	8.1	−27.5	28.3	28
LEU	N	A	46	8.3	−27.6	30.6	23
LEU	CA	A	46	8.8	−26.2	30.7	24
LEU	CB	A	46	7.9	−25.4	31.7	23
LEU	CG	A	46	6.4	−25.4	31.4	22
LEU	CD1	A	46	5.7	−24.6	32.4	21
LEU	CD2	A	46	6.2	−24.7	30.0	21
LEU	C	A	46	10.2	−26.1	31.0	29
LEU	O	A	46	10.8	−26.8	31.9	28
ARG	N	A	47	10.9	−25.1	30.4	29
ARG	CA	A	47	12.3	−24.8	30.7	33
ARG	CB	A	47	13.2	−25.3	29.6	34
ARG	CG	A	47	13.2	−26.9	29.5	38
ARG	CD	A	47	14.2	−27.3	28.5	43
ARG	NE	A	47	13.9	−26.7	27.1	45
ARG	CZ	A	47	14.8	−26.6	26.2	47
ARG	NH1	A	47	16.1	−26.9	26.4	48
ARG	NH2	A	47	14.5	−26.1	25.0	47
ARG	C	A	47	12.4	−23.3	30.8	35
ARG	O	A	47	11.5	−22.5	30.5	31
GLY	N	A	48	13.6	−22.8	31.2	36
GLY	CA	A	48	13.8	−21.4	31.3	45
GLY	C	A	48	15.1	−21.0	32.1	50
GLY	O	A	48	15.7	−21.9	32.7	53
LYS	N	A	49	15.4	−19.8	32.0	50
LYS	CA	A	49	16.6	−19.2	32.7	49
LYS	CB	A	49	17.6	−18.6	31.8	52
LYS	CG	A	49	18.2	−19.6	30.8	58
LYS	CD	A	49	19.2	−18.9	29.9	62
LYS	CE	A	49	19.8	−19.9	28.9	65
LYS	NZ	A	49	20.8	−19.2	28.0	66
LYS	C	A	49	16.1	−18.2	33.7	47
LYS	O	A	49	15.2	−17.4	33.4	49
SER	N	A	50	16.6	−18.4	35.0	44
SER	CA	A	50	16.1	−17.5	36.1	42
SER	CB	A	50	17.1	−17.6	37.3	39
SER	OG	A	50	16.6	−16.7	38.3	40
SER	C	A	50	15.9	−16.0	35.7	40
SER	O	A	50	16.8	−15.4	35.1	42
GLY	N	A	51	14.8	−15.5	35.9	37
GLY	CA	A	51	14.5	−14.1	35.6	31
GLY	C	A	51	14.3	−13.8	34.1	32
GLY	O	A	51	14.4	−12.7	33.7	29
GLN	N	A	52	14.0	−14.9	33.4	29
GLN	CA	A	52	13.8	−14.8	32.0	31
GLN	CB	A	52	15.0	−15.2	31.2	33
GLN	CG	A	52	16.3	−14.3	31.5	39
GLN	CD	A	52	17.4	−14.8	30.7	41
GLN	OE1	A	52	17.4	−15.8	30.0	46
GLN	NE2	A	52	18.5	−14.0	30.7	42
GLN	C	A	52	12.5	−15.5	31.5	29
GLN	O	A	52	12.4	−15.7	30.2	29
GLY	N	A	53	11.7	−15.9	32.4	26
GLY	CA	A	53	10.5	−16.6	32.0	22
GLY	C	A	53	10.6	−18.1	31.7	29
GLY	O	A	53	11.7	−18.6	31.6	30
TYR	N	A	54	9.4	−18.8	31.7	29
TYR	CA	A	54	9.3	−20.2	31.4	29
TYR	CB	A	54	8.5	−20.9	32.4	26
TYR	CG	A	54	9.0	−20.9	33.8	26
TYR	CD1	A	54	9.0	−19.8	34.6	27
TYR	CE1	A	54	9.5	−19.9	36.0	29
TYR	CD2	A	54	9.6	−22.1	34.3	27
TYR	CE2	A	54	10.1	−22.2	35.6	29
TYR	CZ	A	54	10.0	−21.0	36.4	32
TYR	OH	A	54	10.5	−21.1	37.7	32
TYR	C	A	54	8.7	−20.4	30.0	31
TYR	O	A	54	7.8	−19.7	29.6	30
TYR	N	A	55	9.4	−21.2	29.2	28
TYR	CA	A	55	8.9	−21.5	27.8	32
TYR	CB	A	55	9.9	−20.9	26.8	33
TYR	CG	A	55	11.3	−21.5	26.9	33
TYR	CD1	A	55	11.6	−22.7	26.2	30
TYR	CE1	A	55	12.8	−23.3	26.3	30
TYR	CD2	A	55	12.3	−20.9	27.6	33
TYR	CE2	A	55	13.6	−21.5	27.6	35
TYR	CZ	A	55	13.8	−22.7	27.0	33
TYR	OH	A	55	15.1	−23.3	27.1	35
TYR	C	A	55	8.6	−22.9	27.5	34
TYR	O	A	55	9.2	−23.9	28.0	28
VAL	N	A	56	7.6	−23.1	26.6	35
VAL	CA	A	56	7.2	−24.4	26.2	33
VAL	CB	A	56	5.7	−24.7	26.4	32
VAL	CG1	A	56	4.8	−23.7	25.6	24
VAL	CG2	A	56	5.3	−26.1	26.1	33
VAL	C	A	56	7.5	−24.6	24.7	33
VAL	O	A	56	7.3	−23.6	23.9	30
GLU	N	A	57	7.9	−25.7	24.2	31
GLU	CA	A	57	8.2	−25.9	22.8	32
GLU	CB	A	57	9.0	−27.2	22.6	33
GLU	CG	A	57	9.4	−27.4	21.1	35
GLU	CD	A	57	10.2	−28.6	20.9	39
GLU	OE1	A	57	11.4	−28.6	21.1	39
GLU	OE2	A	57	9.6	−29.7	20.5	40
GLU	C	A	57	6.9	−26.0	22.0	30
GLU	O	A	57	5.9	−26.6	22.5	33
MET	N	A	58	6.9	−25.3	20.9	30
MET	CA	A	58	5.7	−25.3	20.0	31
MET	CB	A	58	4.8	−24.1	20.3	31
MET	CG	A	58	4.2	−24.0	21.6	30
MET	SD	A	58	3.1	−22.5	21.8	31
MET	CE	A	58	1.5	−23.1	21.3	31
MET	C	A	58	6.2	−25.4	18.6	29
MET	O	A	58	7.3	−25.2	18.3	27
THR	N	A	59	5.2	−25.7	17.7	32
THR	CA	A	59	5.5	−25.8	16.3	35
THR	CB	A	59	5.6	−27.2	15.7	34
THR	OG1	A	59	4.3	−27.9	15.9	40
THR	OG2	A	59	6.7	−28.0	16.4	31
THR	C	A	59	4.4	−25.0	15.5	36
THR	O	A	59	3.2	−25.1	15.7	39
VAL	N	A	60	4.9	−24.1	14.6	35
VAL	CA	A	60	4.0	−23.3	13.7	39
VAL	CB	A	60	4.1	−21.8	14.1	38
VAL	CG1	A	60	3.7	−21.6	15.5	40
VAL	CG2	A	60	5.4	−21.3	13.7	40
VAL	C	A	60	4.3	−23.6	12.3	41
VAL	O	A	60	5.4	−23.7	11.8	36
GLY	N	A	61	3.2	−23.6	11.5	42
GLY	CA	A	61	3.3	−23.8	10.0	44
GLY	C	A	61	3.4	−25.2	9.5	48
GLY	O	A	61	3.4	−26.2	10.2	47
SER	N	A	62	3.3	−25.3	8.2	48
SER	CA	A	62	3.4	−26.6	7.4	50
SER	CB	A	62	2.0	−26.9	6.9	50
SER	OG	A	62	1.0	−27.0	7.9	52
SER	C	A	62	4.4	−26.4	6.3	48
SER	O	A	62	4.2	−25.7	5.4	46
PRO	N	A	63	5.5	−27.2	6.4	48
PRO	CD	A	63	6.7	−27.0	5.6	45
PRO	CA	A	63	5.8	−28.1	7.5	47
PRO	CB	A	63	7.0	−28.9	6.9	43
PRO	CG	A	63	7.8	−27.7	6.4	46
PRO	C	A	63	6.1	−27.3	8.8	45
PRO	O	A	63	6.6	−26.2	8.8	44
PRO	N	A	64	5.8	−27.9	10.0	43
PRO	CD	A	64	5.7	−29.4	10.1	41
PRO	CA	A	64	6.0	−27.4	11.3	42
PRO	CB	A	64	5.5	−28.5	12.2	39
PRO	CG	A	64	6.2	−29.6	11.6	38
PRO	C	A	64	7.4	−26.8	11.7	41
PRO	O	A	64	8.4	−27.5	11.5	41
GLN	N	A	65	7.4	−25.5	12.1	39
GLN	CA	A	65	8.6	−24.9	12.5	37
GLN	CB	A	65	8.7	−23.5	11.9	36
GLN	CG	A	65	8.6	−23.5	10.4	37
GLN	CD	A	65	8.7	−22.0	9.9	38
GLN	OE1	A	65	9.1	−21.1	10.6	40
GLN	NE2	A	65	8.4	−21.9	8.6	40
GLN	C	A	65	8.7	−24.8	14.0	37
GLN	O	A	65	7.8	−24.4	14.7	39
THR	N	A	66	9.8	−25.4	14.5	36
THR	CA	A	66	10.0	−25.4	16.0	35
THR	CB	A	66	11.0	−26.6	16.4	37
THR	OG1	A	66	10.4	−27.8	15.9	38
THR	CG2	A	66	11.2	−26.6	17.9	38
THR	C	A	66	10.5	−24.1	16.6	35
THR	O	A	66	11.4	−23.5	16.1	35
LEU	N	A	67	9.8	−23.7	17.6	33
LEU	CA	A	67	10.0	−22.4	18.3	32
LEU	CB	A	67	9.3	−21.2	17.7	33
LEU	CG	A	67	9.6	−21.0	16.3	38
LEU	CD1	A	67	8.7	−19.9	15.6	39
LEU	CD2	A	67	11.1	−20.6	16.1	37
LEU	C	A	67	9.7	−22.5	19.8	28
LEU	O	A	67	8.7	−23.1	20.2	29
ASN	N	A	68	10.6	−21.9	20.7	30
ASN	CA	A	68	10.3	−21.9	22.1	30
ASN	CE	A	68	11.6	−21.9	23.0	30
ASH	CG	A	68	12.4	−23.1	22.8	32
ASN	OD1	A	68	13.6	−23.1	22.6	37
ASN	ND2	A	68	11.8	−24.3	23.0	25
ASN	C	A	68	9.4	−20.7	22.5	29
ASN	O	A	68	9.6	−19.6	22.1	28
ILE	N	A	69	8.3	−21.0	23.2	26
ILE	CA	A	69	7.3	−20.0	23.5	26
ILE	CB	A	69	6.0	−20.3	22.8	21
ILE	CG2	A	69	4.9	−19.2	23.1	19
ILE	CG1	A	69	6.2	−20.5	21.3	20
ILE	CD1	A	69	6.7	−19.2	20.6	26
ILE	C	A	69	7.1	−19.8	25.0	27
ILE	O	A	69	6.7	−20.7	25.7	27
LEU	N	A	70	7.4	−18.5	25.4	27
LEU	CA	A	70	7.2	−18.1	26.8	27
LEU	CE	A	70	7.9	−16.8	27.1	28
LEU	CG	A	70	7.8	−16.2	28.5	32
LEU	CD1	A	70	8.7	−15.0	28.7	33
LEU	CD2	A	70	6.4	−15.9	28.9	33
LEU	C	A	70	5.8	−18.2	27.2	28
LEU	O	A	70	4.9	−17.6	26.6	29
VAL	N	A	71	5.5	−18.9	28.3	29
VAL	CA	A	71	4.1	−19.0	28.8	31
VAL	CB	A	71	3.9	−20.3	29.6	31
VAL	CG1	A	71	2.5	−20.5	30.1	33
VAL	CG2	A	71	4.3	−21.5	28.8	33
VAL	C	A	71	3.8	−17.8	29.7	31
VAL	O	A	71	4.3	−17.6	30.7	32
ASP	N	A	72	2.9	−17.0	29.2	35
ASP	CA	A	72	2.5	−15.7	29.8	29
ASP	CB	A	72	2.9	−14.5	29.0	31
ASP	CG	A	72	2.6	−13.2	29.6	34
ASP	OD1	A	72	2.6	−13.2	30.9	33
ASP	OD2	A	72	2.4	−12.2	28.9	32
ASP	C	A	72	1.0	−15.6	30.2	28
ASP	O	A	72	0.2	−15.4	29.3	28
THR	N	A	73	0.7	−15.8	31.5	27
THR	CA	A	73	−0.7	−15.7	31.9	25
THR	CB	A	73	−1.0	−16.6	33.1	27
THR	OG1	A	73	−0.2	−16.1	34.2	28
THR	CG2	A	73	−0.8	−18.1	32.9	22
THR	C	A	73	−1.1	−14.3	32.1	27
THR	O	A	73	−2.3	−14.0	32.4	26
GLY	N	A	74	−0.2	−13.4	31.8	29
GLY	CA	A	74	−0.4	−12.0	32.0	27
GLY	C	A	74	−0.9	−11.2	30.8	27
GLY	O	A	74	−1.2	−10.0	30.8	29
SER	N	A	75	−1.0	−11.9	29.6	27
SER	CA	A	75	−1.4	−11.3	28.4	28
SER	CB	A	75	−0.3	−10.8	27.5	24
SER	OG	A	75	0.5	−11.9	27.1	26
SER	C	A	75	−2.3	−12.3	27.6	30
SER	O	A	75	−2.4	−13.5	27.9	32
SER	N	A	76	−3.0	−11.8	26.5	34
SER	CA	A	76	−3.9	−12.6	25.7	34
SER	CB	A	76	−5.3	−12.0	25.8	34
SER	OG	A	76	−5.7	−12.1	27.2	36
SER	C	A	76	−3.5	−12.8	24.2	34
SER	O	A	76	−4.2	−13.3	23.4	31
ASN	N	A	77	−2.3	−12.4	23.9	31
ASN	CA	A	77	−1.7	−12.5	22.5	28
ASN	CB	A	77	−1.3	−11.2	21.9	29
ASN	CG	A	77	−2.4	−10.2	21.7	30
ASN	OD1	A	77	−2.7	−9.4	22.5	32
ASN	ND2	A	77	−3.0	−10.3	20.5	32
ASN	C	A	77	−0.7	−13.6	22.3	30
ASN	O	A	77	0.2	−13.8	23.1	25
PHE	N	A	78	−0.9	−14.4	21.2	32
PHE	CA	A	78	0.0	−15.4	20.8	30
PHE	CB	A	78	−0.7	−16.6	20.1	29
PHE	CG	A	78	0.3	−17.7	19.7	34
PHE	CD1	A	78	0.2	−18.2	18.4	34
PHE	CD2	A	78	1.3	−18.1	20.6	33
PHE	CE1	A	78	1.1	−19.2	18.0	35
PHE	CE2	A	78	2.2	−19.1	20.1	32
PHE	CZ	A	78	2.1	−19.6	18.9	30
PHE	C	A	78	0.9	−14.7	19.7	33
PHE	O	A	78	0.4	−14.2	18.7	34
ALA	N	A	79	2.2	−14.6	20.0	31
ALA	CA	A	79	3.1	−13.9	19.1	29
ALA	CB	A	79	3.2	−12.4	19.5	27
ALA	C	A	79	4.5	−14.5	19.0	30
ALA	O	A	79	5.0	−15.0	19.9	33
VAL	N	A	80	5.0	−14.5	17.8	28
VAL	CA	A	80	6.4	−15.1	17.5	28
VAL	CB	A	80	6.3	−16.5	16.9	26
VAL	CG1	A	80	5.5	−17.4	17.7	22
VAL	CG2	A	80	5.7	−16.3	15.4	24
VAL	C	A	80	7.2	−14.2	16.7	27
VAL	O	A	80	6.7	−13.5	15.8	27
GLY	N	A	81	8.5	−14.1	17.0	25
GLY	CA	A	81	9.4	−13.3	16.2	26
GLY	C	A	81	9.3	−13.8	14.8	32
GLY	O	A	81	9.4	−15.0	14.6	30
ALA	N	A	82	9.2	−12.9	13.9	34
ALA	CA	A	82	9.0	−13.2	12.5	35
ALA	CB	A	82	7.6	−12.9	12.0	35
ALA	C	A	82	10.1	−12.5	11.6	36
ALA	O	A	82	10.0	−12.6	10.4	40
ALA	N	A	83	11.1	−11.9	12.2	35
ALA	CA	A	83	12.1	−11.2	11.5	37
ALA	CB	A	83	11.7	−9.8	11.3	34
ALA	C	A	83	13.4	−11.3	12.3	39
ALA	O	A	83	13.4	−11.4	13.5	42
PRO	N	A	84	14.6	−11.3	11.6	38
PRO	CD	A	84	14.8	−10.7	10.3	37
PRO	CA	A	84	15.8	−11.4	12.3	35
PRO	CB	A	84	16.8	−11.3	11.2	37
PRO	CG	A	84	16.3	−10.2	10.4	40
PRO	C	A	84	16.0	−10.4	13.4	36
PRO	O	A	84	15.6	−9.2	13.2	35
HIS	N	A	85	16.6	−10.8	14.5	36
HIS	CA	A	85	16.8	−10.0	15.7	35
HIS	CB	A	85	15.5	−10.0	16.6	34
HIS	CG	A	85	15.7	−9.1	17.8	35
HIS	CD2	A	85	15.1	−7.9	18.1	35
HIS	ND1	A	85	16.5	−9.5	18.8	35
HIS	CE1	A	85	16.4	−8.5	19.8	34
HIS	NE2	A	85	15.6	−7.6	19.4	35
HIS	C	A	85	18.0	−10.5	16.4	37
HIS	O	A	85	18.2	−11.7	16.5	37
PRO	N	A	86	18.8	−9.6	16.9	36
PRO	CD	A	86	18.8	−8.1	16.7	36
PRO	CA	A	86	20.1	−9.9	17.7	32
PRO	CB	A	86	20.4	−8.5	18.3	32
PRO	CG	A	86	20.2	−7.7	17.1	37
PRO	C	A	86	20.0	−11.0	18.7	33
PRO	O	A	86	20.9	−11.7	19.0	33
PHE	N	A	87	18.8	−11.2	19.2	30
PHE	CA	A	87	18.6	−12.2	20.3	30
PHE	CB	A	87	17.8	−11.6	21.5	29
PHE	CG	A	87	18.5	−10.4	22.1	35
PHE	CD1	A	87	17.9	−9.6	23.0	34
PHE	CD2	A	87	19.9	−10.1	21.8	37
PHE	CE1	A	87	18.5	−8.5	23.6	34
PHE	CE2	A	87	20.5	−9.0	22.3	38
PHE	CZ	A	87	19.9	−8.2	23.2	37
PHE	C	A	87	17.9	−13.4	19.8	30
PHE	O	A	87	17.6	−14.4	20.6	32
LEU	N	A	88	17.5	−13.5	18.5	25
LEU	CA	A	88	16.8	−14.7	18.0	25
LEU	CB	A	88	15.6	−14.3	17.2	23
LEU	CG	A	88	14.5	−13.5	17.9	27
LEU	CD1	A	88	13.4	−13.1	17.0	24
LEU	CD2	A	88	13.9	−14.3	19.1	23
LEU	C	A	88	17.7	−15.6	17.2	27
LEU	O	A	88	18.3	−15.2	16.1	29
HIS	N	A	89	17.9	−16.8	17.6	32
HIS	CA	A	89	18.7	−17.8	16.9	32
HIS	CB	A	89	19.3	−18.9	17.7	36
HIS	CG	A	89	20.2	−18.4	18.8	41
HIS	CD2	A	89	20.4	−17.2	19.3	46
HIS	ND1	A	89	21.0	−19.2	19.5	46
HIS	CE1	A	89	21.7	−18.5	20.4	45
HIS	NE2	A	89	21.4	−17.3	20.3	48
HIS	C	A	89	17.9	−18.4	15.7	30
HIS	O	A	89	18.4	−19.0	14.8	36
ARG	N	A	90	16.6	−18.1	15.8	27
ARG	CA	A	90	15.6	−18.6	14.8	26
ARG	CB	A	90	15.3	−20.1	15.0	25
ARG	CG	A	90	14.8	−20.5	16.4	26
ARG	CD	A	90	14.6	−22.0	16.5	26
ARG	NE	A	90	14.1	−22.4	17.8	26
ARG	CZ	A	90	13.9	−23.7	18.1	26
ARG	NH1	A	90	14.3	−24.6	17.3	22
ARG	NH2	A	90	13.5	−24.0	19.3	26
ARG	C	A	90	14.3	−17.8	15.0	28
ARG	O	A	90	14.0	−17.3	16.0	31
TYR	N	A	91	13.6	−17.8	13.9	29
TYR	CA	A	91	12.3	−17.0	13.9	30
TYR	CB	A	91	12.6	−15.5	13.6	32
TYR	CG	A	91	13.2	−15.2	12.3	35
TYR	CD1	A	91	12.5	−15.1	11.1	35
TYR	CE1	A	91	13.2	−14.9	9.9	40
TYR	CD2	A	91	14.6	−15.1	12.3	37
TYR	CE2	A	91	15.3	−14.8	11.1	37
TYR	CZ	A	91	14.6	−14.8	9.9	38
TYR	OH	A	91	15.2	−14.5	8.7	38
TYR	C	A	91	11.3	−17.6	12.9	30
TYR	O	A	91	11.6	−18.2	11.9	33
TYR	N	A	92	10.0	−17.3	13.2	31
TYR	CA	A	92	8.9	−17.7	12.3	29
TYR	CB	A	92	7.6	−17.3	13.0	31
TYR	CG	A	92	6.3	−17.6	12.2	33
TYR	CD1	A	92	6.2	−18.9	11.5	30
TYR	CE1	A	92	5.0	−19.2	10.9	29
TYR	CD2	A	92	5.2	−16.8	12.2	31
TYR	CE2	A	92	4.0	−17.1	11.5	29
TYR	CZ	A	92	3.9	−18.3	10.9	29
TYR	OH	A	92	2.7	−18.7	10.3	34
TYR	C	A	92	9.0	−17.2	10.9	32
TYR	O	A	92	9.0	−16.0	10.6	33
GLN	N	A	93	9.1	−18.1	9.9	35
GLN	CA	A	93	9.2	−17.8	8.5	39
GLN	CB	A	93	10.5	−18.2	7.9	45
GLN	CG	A	93	11.7	−17.7	8.6	53
GLN	CD	A	93	13.0	−18.1	7.9	52
GLN	OE1	A	93	13.8	−18.8	8.5	56
GLN	NE2	A	93	13.1	−17.8	6.6	52
GLN	C	A	93	8.0	−18.1	7.8	38
GLN	O	A	93	7.8	−19.3	7.4	36
ARG	N	A	94	7.1	−17.1	7.6	41
ARG	CA	A	94	5.8	−17.2	6.9	46
ARG	CB	A	94	5.1	−15.9	7.1	44
ARG	CG	A	94	4.8	−15.6	8.6	43
ARG	CD	A	94	4.2	−14.2	8.8	40
ARG	NE	A	94	5.1	−13.2	8.3	40
ARG	CZ	A	94	4.9	−11.9	8.3	41
ARG	NH1	A	94	3.7	−11.4	8.7	42
ARG	NH2	A	94	5.9	−11.0	8.0	39
ARG	C	A	94	5.9	−17.6	5.5	50
ARG	O	A	94	4.9	−18.1	4.9	51
GLN	N	A	95	7.0	−17.5	4.8	53
GLN	CA	A	95	7.2	−17.8	3.4	58
GLN	CB	A	95	8.2	−16.9	2.7	64
CLN	CG	A	95	7.9	−15.4	2.7	75
GLN	CD	A	95	9.0	−14.7	2.0	80
GLN	OE1	A	95	10.0	−15.3	1.5	83
GLN	NE2	A	95	8.9	−13.4	2.0	83
GLN	C	A	95	7.5	−19.3	3.2	55
GLN	O	A	95	7.5	−19.8	2.1	55
LEU	N	A	96	7.7	−20.0	4.3	50
LEU	CA	A	96	8.0	−21.4	4.3	46
LEU	CB	A	96	9.3	−21.7	5.1	44
LEU	CG	A	96	10.5	−21.0	4.6	46
LEU	CD1	A	96	11.7	−21.3	5.5	45
LEU	CD2	A	96	10.8	−21.3	3.1	46
LEU	C	A	96	6.9	−22.3	4.7	47
LEU	O	A	96	7.0	−23.5	4.8	47
SER	N	A	97	5.8	−21.6	5.1	47
SER	CA	A	97	4.6	−22.3	5.6	46
SER	CB	A	97	4.1	−21.8	6.9	46
SER	OG	A	97	3.0	−22.5	7.4	49
SER	C	A	97	3.5	−22.3	4.5	45
SER	O	A	97	2.9	−21.3	4.2	41
SER	N	A	98	3.1	−23.5	4.1	45
SER	CA	A	98	2.0	−23.6	3.1	49
SER	CB	A	98	2.1	−24.9	2.4	51
SER	OG	A	98	2.0	−26.0	3.3	53
SER	C	A	98	0.6	−23.4	3.7	52
SER	O	A	98	−0.4	−23.2	3.0	53
THR	N	A	99	0.6	−23.3	5.1	50
THR	CA	A	99	−0.7	−23.1	5.7	46
THR	CB	A	99	−1.0	−24.2	6.8	48
THR	OG1	A	99	0.1	−24.3	7.7	49
THR	CG2	A	99	−1.3	−25.5	6.1	48
THR	C	A	99	−0.9	−21.7	6.3	42
THR	O	A	99	−1.9	−21.4	6.9	43
TYR	N	A	100	0.1	−20.8	6.0	44
TYR	CA	A	100	0.0	−19.4	6.5	43
TYR	CB	A	100	1.4	−18.7	6.2	41
TYR	CG	A	100	1.3	−17.2	6.5	42
TYR	CD1	A	100	1.1	−16.7	7.8	40
TYR	CE1	A	100	1.0	−15.3	8.0	40
TYR	CD2	A	100	1.5	−16.3	5.4	41
TYR	CE2	A	100	1.4	−15.0	5.6	44
TYR	CZ	A	100	1.1	−14.5	6.9	42
TYR	OH	A	100	1.0	−13.1	7.1	42
TYR	C	A	100	−1.1	−18.6	5.8	47
TYR	O	A	100	−1.3	−18.7	4.6	48
ARG	N	A	101	−1.8	−17.8	6.6	46
ARG	CA	A	101	−2.9	−17.0	6.1	49
ARG	CB	A	101	−4.3	−17.5	6.4	50
ARG	CG	A	101	−4.5	−18.9	5.9	50
ARG	CD	A	101	−5.9	−19.4	6.3	52
ARG	NE	A	101	−6.2	−20.8	5.8	56
ARG	CZ	A	101	−7.3	−21.4	6.1	55
ARG	NH1	A	101	−8.2	−20.9	6.8	54
ARG	NH2	A	101	−7.4	−22.7	5.6	53
ARG	C	A	101	−2.7	−15.6	6.6	51
ARG	O	A	101	−2.7	−15.4	7.8	54
ASP	N	A	102	−2.5	−14.7	5.7	52
ASP	CA	A	102	−2.3	−13.3	6.0	52
ASP	CB	A	102	−1.5	−12.5	5.0	52
ASP	CG	A	102	−1.2	−11.1	5.3	53
ASP	OD1	A	102	−1.5	−10.7	6.4	53
ASP	OD2	A	102	−0.7	−10.4	4.4	55
ASP	C	A	102	−3.6	−12.6	6.3	52
ASP	O	A	102	−4.5	−12.6	5.5	52
LEU	N	A	103	−3.7	−12.0	7.5	52
LEU	CA	A	103	−4.9	−11.2	7.9	52
LEU	CB	A	103	−5.2	−11.3	9.4	53
LEU	CG	A	103	−5.4	−12.8	9.9	54
LEU	CD1	A	103	−5.5	−12.8	11.4	52
LEU	CD2	A	103	−6.6	−13.4	9.2	54
LEU	C	A	103	−4.9	−9.8	7.4	56
LEU	O	A	103	−5.9	−9.0	7.6	57
ARG	N	A	104	−3.8	−9.4	6.8	59
ARG	CA	A	104	−3.7	−8.0	6.2	65
ARG	CB	A	104	−4.7	−7.8	5.1	68
ARG	CG	A	104	−4.5	−8.8	3.9	72
ARG	CD	A	104	−5.5	−8.6	2.8	76
ARG	NE	A	104	−5.5	−7.3	2.2	80
ARG	CZ	A	104	−6.3	−6.3	2.5	82
ARG	NH1	A	104	−7.1	−6.4	3.5	83
ARG	NH2	A	104	−6.2	−5.1	1.9	81
ARG	C	A	104	−3.9	−6.9	7.3	65
ARG	O	A	104	−4.0	−5.7	6.9	67
LYS	N	A	105	−3.8	−7.2	8.6	63
LYS	CA	A	105	−3.9	−6.2	9.6	60
LYS	CB	A	105	−5.3	−6.3	10.3	59
LYS	CG	A	105	−5.4	−5.3	11.4	62
LYS	CD	A	105	−6.8	−5.3	12.1	64
LYS	CE	A	105	−7.2	−6.7	12.7	66
LYS	NZ	A	105	−8.5	−6.7	13.3	64
LYS	C	A	105	−2.8	−6.2	10.7	57
LYS	O	A	105	−2.4	−7.3	11.2	57
GLY	N	A	106	−2.2	−5.1	10.9	53
GLY	CA	A	106	−1.2	−4.9	11.9	51
GLY	C	A	106	−1.6	−5.1	13.4	49
GLY	O	A	106	−2.8	−5.2	13.7	50
VAL	N	A	107	−0.6	−5.2	14.2	43
VAL	CA	A	107	−0.8	−5.4	15.7	39
VAL	CB	A	107	−1.1	−6.9	16.0	39
VAL	CG1	A	107	0.1	−7.7	15.6	34
VAL	CG2	A	107	−1.5	−7.0	17.5	34
VAL	C	A	107	0.3	−4.8	16.5	39
VAL	O	A	107	1.5	−5.0	16.2	39
TYR	N	A	108	−0.1	−4.2	17.6	39
TYR	CA	A	108	0.8	−3.6	18.6	42
TYR	CB	A	108	0.7	−2.1	18.5	46
TYR	CG	A	108	1.5	−1.4	19.6	50
TYR	CD1	A	108	2.9	−1.5	19.7	53
TYR	CE1	A	108	3.6	−0.9	20.7	52
TYR	CD2	A	108	0.9	−0.5	20.5	50
TYR	CE2	A	108	1.6	0.1	21.5	51
TYR	CZ	A	108	3.0	−0.1	21.6	52
TYR	OH	A	108	3.7	0.6	22.6	52
TYR	C	A	108	0.5	−4.1	20.0	39
TYR	O	A	108	−0.7	−3.9	20.5	40
VAL	N	A	109	1.4	−4.7	20.7	36
VAL	CA	A	109	1.2	−5.1	22.0	35
VAL	CB	A	109	1.1	−6.7	22.2	32
VAL	CG1	A	109	1.0	−7.1	23.7	31
VAL	CG2	A	109	−0.1	−7.2	21.4	32
VAL	C	A	109	2.3	−4.6	23.0	36
VAL	O	A	109	3.5	−5.0	22.9	35
PRO	N	A	110	1.9	−3.7	23.9	35
PRO	CD	A	110	0.6	−3.0	23.9	30
PRO	CA	A	110	2.8	−3.1	24.9	33
PRO	CB	A	110	2.3	−1.7	24.9	35
PRO	CG	A	110	0.8	−1.9	25.0	32
PRO	C	A	110	2.6	−3.8	26.3	32
PRO	O	A	110	1.5	−4.1	26.7	31
TYR	N	A	111	3.8	−4.1	26.9	32
TYR	CA	A	111	3.8	−4.8	28.2	33
TYR	CB	A	111	4.7	−6.0	28.2	30
TYR	CG	A	111	4.2	−7.0	27.1	25
TYR	CD1	A	111	3.3	−8.0	27.5	25
TYR	CE1	A	111	2.9	−9.0	26.5	24
TYR	CD2	A	111	4.7	−7.0	25.9	26
TYR	CE2	A	111	4.3	−8.0	24.9	26
TYR	CZ	A	111	3.4	−8.9	25.3	24
TYR	OH	A	111	3.0	−9.9	24.3	27
TYR	C	A	111	4.3	−3.8	29.3	33
TYR	O	A	111	4.8	−2.7	29.0	35
THR	N	A	112	4.3	−4.3	30.6	29
THR	CA	A	112	4.8	−3.4	31.7	25
THR	CB	A	112	4.7	−4.2	33.0	22
THR	OG1	A	112	3.3	−4.4	33.3	24
THR	CG2	A	112	5.3	−3.4	34.1	23
THR	C	A	112	6.3	−3.1	31.4	28
THR	O	A	112	6.8	−2.1	31.8	31
GLN	N	A	113	6.9	−4.0	30.6	31
GLN	CA	A	113	8.3	−3.8	30.2	32
GLN	CB	A	113	9.4	−4.4	31.2	36
GLN	CG	A	113	9.4	−3.6	32.6	51
GLN	CD	A	113	9.7	−2.1	32.3	57
GLN	OE1	A	113	10.1	−1.8	31.2	61
GLN	NE2	A	113	9.7	−1.3	33.3	59
GLN	C	A	113	8.4	−4.6	28.9	31
GLN	O	A	113	8.2	−5.9	28.9	29
GLY	N	A	114	8.7	−3.9	27.8	23
GLY	CA	A	114	8.8	−4.6	26.6	23
GLY	C	A	114	7.6	−4.3	25.7	30
GLY	O	A	114	6.5	−4.2	26.3	26
LYS	N	A	115	7.8	−4.3	24.4	31
LYS	CA	A	115	6.7	−4.0	23.5	33
LYS	CB	A	115	6.4	−2.5	23.4	35
LYS	CG	A	115	7.6	−1.6	23.0	42
LYS	CD	A	115	7.2	−0.2	22.9	44
LYS	CE	A	115	8.4	0.7	22.5	50
LYS	NZ	A	115	8.1	2.1	22.4	54
LYS	C	A	115	7.1	−4.5	22.1	30
LYS	O	A	115	8.3	−4.6	21.8	32
TRP	N	A	116	6.2	−5.0	21.4	29
TRP	CA	A	116	6.4	−5.4	20.0	33
TRP	CB	A	116	6.7	−7.0	20.0	30
TRP	CG	A	116	5.6	−7.8	20.5	29
TRP	CD2	A	116	4.4	−8.1	19.9	30
TRP	CE2	A	116	3.7	−9.0	20.8	28
TRP	CE3	A	116	3.7	−7.7	18.7	27
TRP	CD1	A	116	5.6	−8.5	21.7	29
TRP	NE1	A	116	4.5	−9.2	21.8	32
TRP	CZ2	A	116	2.4	−9.4	20.5	28
TRP	CZ3	A	116	2.5	−8.2	18.4	25
TRP	CH2	A	116	1.8	−9.0	19.3	25
TRP	C	A	116	5.3	−5.1	19.1	35
TRP	O	A	116	4.2	−4.8	19.5	36
GLU	N	A	117	5.7	−5.0	17.8	40
GLU	CA	A	117	4.7	−4.6	16.8	44
GLU	CB	A	117	4.9	−3.2	16.2	49
GLU	CG	A	117	3.9	−2.7	15.2	59
GLU	CD	A	117	4.3	−1.3	14.8	66
GLU	OE1	A	117	5.3	−0.8	15.3	66
GLU	OE2	A	117	3.6	−0.8	13.9	71
GLU	C	A	117	4.8	−5.7	15.7	39
GLU	O	A	117	5.9	−6.1	15.3	38
GLY	N	A	118	3.6	−6.2	15.2	36
GLY	CA	A	118	3.7	−7.2	14.2	36
GLY	C	A	118	2.6	−7.2	13.2	35
GLY	O	A	118	1.8	−6.2	13.0	35
GLU	N	A	119	2.4	−8.4	12.5	33
GLU	CA	A	119	1.4	−8.5	11.5	32
GLU	CB	A	119	2.1	−8.6	10.1	36
GLU	CG	A	119	3.0	−7.4	9.9	42
GLU	CD	A	119	3.7	−7.5	8.5	45
GLU	OE1	A	119	3.7	−6.6	7.8	50
GLU	OE2	A	119	4.3	−8.6	8.2	47
GLU	C	A	119	0.5	−9.7	11.8	31
GLU	O	A	119	1.0	−10.8	12.0	29
LEU	N	A	120	−0.8	−9.5	11.8	32
LEU	CA	A	120	−1.7	−10.6	12.1	31
LEU	CB	A	120	−3.1	−10.0	12.5	34
LEU	CG	A	120	−3.0	−9.2	13.8	36
LEU	CD1	A	120	−4.3	−8.6	14.2	37
LEU	CD2	A	120	−2.4	−10.1	15.0	35
LEU	C	A	120	−1.9	−11.6	11.0	35
LEU	O	A	120	−2.0	−11.3	9.8	33
GLY	N	A	121	−2.0	−12.9	11.4	34
GLY	CA	A	121	−2.2	−14.0	10.5	31
GLY	C	A	121	−2.7	−15.1	11.3	35
GLY	O	A	121	−2.9	−15.0	12.5	36
THR	N	A	122	−2.9	−16.3	10.6	32
THR	CA	A	122	−3.4	−17.5	11.3	32
THR	CB	A	122	−4.9	−17.8	11.0	34
THR	OG1	A	122	−5.1	−18.0	9.7	39
THR	CG2	A	122	−5.7	−16.6	11.5	32
THR	C	A	122	−2.5	−18.6	10.6	29
THR	O	A	122	−2.1	−18.5	9.5	29
ASP	N	A	123	−2.3	−19.7	11.4	29
ASP	CA	A	123	−1.6	−20.8	10.8	33
ASP	CB	A	123	−0.1	−20.4	10.6	36
ASP	CG	A	123	0.7	−21.5	9.8	40
ASP	OD1	A	123	0.2	−22.5	9.5	35
ASP	OD2	A	123	1.9	−21.2	9.5	44
ASP	C	A	123	−1.8	−22.0	11.8	33
ASP	O	A	123	−2.4	−21.8	12.8	36
LEU	N	A	124	−1.3	−23.2	11.4	34
LEU	CA	A	124	−1.4	−24.3	12.3	35
LEU	CB	A	124	−1.4	−25.6	11.5	36
LEU	CG	A	124	−2.5	−25.6	10.5	39
LEU	CD1	A	124	−2.5	−26.9	9.6	40
LEU	CD2	A	124	−3.9	−25.6	11.2	35
LEU	C	A	124	−0.3	−24.4	13.4	35
LEU	O	A	124	0.9	−24.3	13.1	34
VAL	N	A	125	−0.8	−24.6	14.6	38
VAL	CA	A	125	0.1	−24.6	15.8	35
VAL	CB	A	125	−0.2	−23.4	16.8	33
VAL	CG1	A	125	0.8	−23.5	18.0	31
VAL	CG2	A	125	−0.1	−22.1	16.0	31
VAL	C	A	125	−0.1	−26.0	16.6	39
VAL	O	A	125	−1.2	−26.4	16.8	43
SER	N	A	126	1.0	−26.6	17.0	39
SER	CA	A	126	1.1	−27.8	17.7	41
SER	CB	A	126	1.4	−29.0	16.8	44
SER	OG	A	126	0.5	−29.2	15.8	51
SER	C	A	126	2.0	−27.7	18.9	41
SER	O	A	126	3.0	−27.1	18.9	43
ILE	N	A	127	1.6	−28.4	20.0	39
ILE	CA	A	127	2.5	−28.4	21.2	36
ILE	CB	A	127	1.6	−28.0	22.5	37
ILE	CG2	A	127	2.5	−28.1	23.7	31
ILE	CG1	A	127	1.0	−26.6	22.3	38
ILE	CD1	A	127	0.2	−26.2	23.4	38
ILE	C	A	127	3.0	−29.8	21.3	36
ILE	O	A	127	2.4	−30.7	21.8	35
PRO	N	A	128	4.3	−30.0	20.9	36
PRO	CD	A	128	5.1	−29.0	20.1	36
PRO	CA	A	128	5.0	−31.2	20.9	37
PRO	CB	A	128	6.5	−30.8	20.7	35
PRO	CG	A	128	6.2	−29.9	19.5	36
PRO	C	A	128	4.9	−32.0	22.2	38
PRO	O	A	128	4.7	−33.2	22.2	39
HIS	N	A	129	5.0	−31.3	23.4	38
HIS	CA	A	129	4.9	−32.0	24.7	39
HIS	CB	A	129	6.1	−31.7	25.5	40
HIS	CG	A	129	7.4	−32.2	24.9	42
HIS	CD2	A	129	8.4	−31.6	24.3	41
HIS	ND1	A	129	7.7	−33.6	24.8	41
HIS	CE1	A	129	8.8	−33.8	24.2	41
HIS	NE2	A	129	9.3	−32.6	23.9	39
HIS	C	A	129	3.6	−31.6	25.4	38
HIS	O	A	129	3.6	−31.5	26.7	37
GLY	N	A	130	2.5	−31.4	24.7	38
GLY	CA	A	130	1.3	−31.1	25.3	41
GLY	C	A	130	0.3	−32.2	24.7	41
GLY	O	A	130	0.8	−33.3	24.4	41
PRO	N	A	131	−0.9	−31.8	24.4	43
PRO	CD	A	131	−1.6	−30.5	24.6	42
PRO	CA	A	131	−1.9	−32.8	23.9	45
PRO	CB	A	131	−3.2	−32.2	24.3	44
PRO	CG	A	131	−3.0	−30.8	24.0	45
PRO	C	A	131	−1.7	−32.9	22.4	45
PRO	O	A	131	−1.5	−31.9	21.7	45
ASN	N	A	132	−1.8	−34.1	21.8	48
ASN	CA	A	132	−1.7	−34.3	20.4	53
ASN	CB	A	132	−1.4	−35.8	20.0	60
ASN	CG	A	132	−0.1	−36.3	20.6	66
ASN	OD1	A	132	0.8	−36.7	19.8	69
ASN	ND2	A	132	0.0	−36.2	21.9	70
ASN	C	A	132	−2.9	−33.7	19.6	51
ASN	O	A	132	−3.8	−34.5	19.4	50
VAL	N	A	133	−2.7	−32.5	19.2	49
VAL	CA	A	133	−3.8	−31.8	18.4	50
VAL	CB	A	133	−4.9	−31.2	19.3	50
VAL	CG1	A	133	−5.6	−32.4	20.1	46
VAL	CG2	A	133	−4.4	−30.1	20.3	48
VAL	C	A	133	−3.2	−30.6	17.7	50
VAL	O	A	133	−2.1	−30.1	18.1	52
THR	N	A	134	−3.8	−30.3	16.5	50
THR	CA	A	134	−3.3	−29.2	15.7	49
THR	CB	A	134	−2.9	−29.7	14.3	49
THR	OG1	A	134	−1.9	−30.6	14.4	52
THR	CG2	A	134	−2.5	−28.5	13.4	50
THR	C	A	134	−4.4	−28.2	15.7	49
THR	O	A	134	−5.6	−28.5	15.4	50
VAL	N	A	135	−4.1	−26.9	15.9	47
VAL	CA	A	135	−5.1	−25.9	16.0	44
VAL	CB	A	135	−5.3	−25.4	17.4	44
VAL	CG1	A	135	−6.3	−24.3	17.5	43
VAL	CG2	A	135	−5.6	−26.5	18.4	43
VAL	C	A	135	−4.7	−24.7	15.1	43
VAL	O	A	135	−3.6	−24.2	15.1	46
ARG	N	A	136	−5.7	−24.2	14.3	40
ARG	CA	A	136	−5.4	−23.0	13.6	42
ARG	CB	A	136	−6.2	−22.9	12.2	44
ARG	CG	A	136	−6.0	−21.5	11.6	46
ARG	CD	A	136	−6.7	−21.4	10.2	46
ARG	NE	A	136	−6.2	−22.4	9.3	46
ARG	CZ	A	136	−5.0	−22.2	8.6	46
ARG	NH1	A	136	−4.4	−21.0	8.7	45
ARG	NH2	A	136	−4.6	−23.1	7.7	46
ARG	C	A	136	−5.7	−21.8	14.5	38
ARG	O	A	136	−6.8	−21.6	14.9	39
ALA	N	A	137	−4.6	−21.1	14.8	37
ALA	CA	A	137	−4.7	−20.0	15.8	35
ALA	CB	A	137	−3.9	−20.4	17.0	34
ALA	C	A	137	−4.2	−18.7	15.2	35
ALA	O	A	137	−3.4	−18.7	14.3	34
ASN	N	A	138	−4.7	−17.6	15.8	34
ASN	CA	A	138	−4.2	−16.3	15.3	34
ASN	CB	A	138	−5.0	−15.2	15.9	36
ASN	CG	A	138	−6.5	−15.2	15.6	36
ASN	OD1	A	138	−6.9	−14.6	14.6	41
ASN	ND2	A	138	−7.2	−16.0	16.3	39
ASN	C	A	138	−2.7	−16.2	15.8	34
ASN	O	A	138	−2.4	−16.6	16.9	36
ILE	N	A	139	−1.9	−15.7	14.9	33
ILE	CA	A	139	−0.5	−15.6	15.2	31
ILE	CB	A	139	0.4	−16.6	14.5	31
ILE	CG2	A	139	1.8	−16.4	14.9	31
ILE	CG1	A	139	−0.1	−18.0	14.8	33
ILE	CD1	A	139	0.7	−19.1	14.1	33
ILE	C	A	139	0.0	−14.2	14.9	34
ILE	O	A	139	−0.1	−13.7	13.8	39
ALA	N	A	140	0.6	−13.5	15.9	31
ALA	CA	A	140	1.1	−12.2	15.6	33
ALA	CB	A	140	1.1	−11.3	16.9	31
ALA	C	A	140	2.6	−12.4	15.2	36
ALA	O	A	140	3.4	−12.9	16.0	37
ALA	N	A	141	2.9	−12.0	14.0	31
ALA	CA	A	141	4.3	−12.2	13.5	32
ALA	CB	A	141	4.3	−12.4	11.9	31
ALA	C	A	141	5.0	−10.9	13.9	30
ALA	O	A	141	4.8	−9.9	13.3	31
ILE	N	A	142	6.0	−11.1	14.8	27
ILE	CA	A	142	6.7	−9.9	15.3	30
ILE	CB	A	142	7.4	−10.2	16.6	26
ILE	CG2	A	142	8.2	−9.0	17.1	24
ILE	CG1	A	142	6.3	−10.5	17.7	27
ILE	CD1	A	142	6.9	−10.9	19.1	24
ILE	C	A	142	7.8	−9.4	14.3	35
ILE	O	A	142	8.7	−10.1	13.9	36
THR	N	A	143	7.6	−8.1	13.9	37
THR	CA	A	143	8.5	−7.5	12.9	37
THR	CB	A	143	7.7	−7.0	11.7	37
THR	OG1	A	143	6.7	−6.1	12.1	37
THR	CG2	A	143	7.1	−8.1	10.9	35
THR	C	A	143	9.3	−6.4	13.5	39
THR	O	A	143	10.3	−5.9	12.9	42
GLU	N	A	144	8.9	−5.9	14.7	38
GLU	CA	A	144	9.6	−4.9	15.4	42
GLU	CB	A	144	9.2	−3.5	15.0	50
GLU	CG	A	144	9.5	−3.2	13.5	59
GLU	CD	A	144	9.0	−1.8	13.2	67
GLU	OE1	A	144	8.6	−1.0	14.1	69
GLU	OE2	A	144	9.1	−1.4	12.0	68
GLU	C	A	144	9.4	−5.0	16.9	39
GLU	O	A	144	8.3	−5.2	17.4	37
SER	N	A	145	10.5	−5.0	17.7	35
SER	CA	A	145	10.4	−5.2	19.1	34
SER	CB	A	145	10.6	−6.6	19.5	27
SER	OG	A	145	11.9	−7.1	19.1	35
SER	C	A	145	11.4	−4.3	19.9	33
SER	O	A	145	12.5	−4.0	19.4	31
ASP	N	A	146	11.0	−3.9	21.1	35
ASP	CA	A	146	11.9	−3.1	21.9	35
ASP	CB	A	146	11.4	−1.6	21.9	44
ASP	CG	A	146	12.3	−0.7	22.8	51
ASP	OD1	A	146	11.8	−0.2	23.8	56
ASP	OD2	A	146	13.5	−0.6	22.5	54
ASP	C	A	146	11.9	−3.6	23.4	33
ASP	O	A	146	10.8	−3.7	24.0	28
LYS	N	A	147	13.0	−4.1	23.8	32
LYS	CA	A	147	13.2	−4.6	25.2	35
LYS	CB	A	147	12.9	−3.5	26.2	39
LYS	CG	A	147	13.9	−2.3	26.1	45
LYS	CD	A	147	13.6	−1.2	27.1	52
LYS	CE	A	147	14.6	−0.1	26.9	55
LYS	NZ	A	147	14.3	1.0	27.9	59
LYS	C	A	147	12.3	−5.8	25.5	34
LYS	O	A	147	12.1	−6.1	26.6	36
PHE	N	A	148	11.8	−6.4	24.4	31
PHE	CA	A	148	10.9	−7.6	24.5	27
PHE	CB	A	148	10.0	−7.7	23.3	24
PHE	CG	A	148	9.0	−8.8	23.4	25
PHE	CD1	A	148	8.1	−9.0	24.4	27
PHE	CD2	A	148	9.1	−9.8	22.4	23
PHE	CE1	A	148	7.2	−10.0	24.5	25
PHE	CE2	A	148	8.2	−10.9	22.4	19
PHE	CZ	A	148	7.2	−11.0	23.5	22
PHE	C	A	148	11.8	−8.8	24.6	27
PHE	O	A	148	11.9	−9.5	25.7	27
PHE	N	A	149	12.4	−9.2	23.5	24
PHE	CA	A	149	13.3	−10.4	23.4	28
PHE	CB	A	149	13.7	−10.7	22.0	25
PHE	CG	A	149	12.6	−11.0	21.1	24
PHE	CD1	A	149	12.3	−10.1	20.0	26
PHE	CD2	A	149	11.8	−12.1	21.2	24
PHE	CE1	A	149	11.3	−10.4	19.1	27
PHE	CE2	A	149	10.8	−12.4	20.4	23
PHE	CZ	A	149	10.5	−11.5	19.3	23
PHE	C	A	149	14.5	−10.2	24.4	33
PHE	O	A	149	15.2	−9.2	24.4	34
ILE	N	A	150	14.8	−11.3	25.1	38
ILE	CA	A	150	15.9	−11.3	26.0	37
ILE	CB	A	150	15.5	−11.9	27.4	37
ILE	CG2	A	150	16.7	−12.0	28.3	37
ILE	CG1	A	150	14.4	−11.0	28.0	35
ILE	CD1	A	150	14.0	−11.5	29.4	31
ILE	C	A	150	17.1	−12.1	25.5	38
ILE	O	A	150	16.9	−13.2	24.9	37
ASN	N	A	151	18.3	−11.5	25.6	39
ASN	CA	A	151	19.5	−12.2	25.1	41
ASN	CB	A	151	20.7	−11.2	25.0	46
ASN	CG	A	151	21.9	−11.8	24.4	50
ASN	OD1	A	151	23.0	−11.7	25.0	54
ASN	ND2	A	151	21.8	−12.4	23.2	52
ASN	C	A	151	19.8	−13.5	25.9	40
ASN	O	A	151	20.1	−13.4	27.1	35
GLY	N	A	152	19.8	−14.6	25.2	39
GLY	CA	A	152	20.1	−15.9	25.8	37
GLY	C	A	152	18.9	−16.6	26.5	39
GLY	O	A	152	19.1	−17.6	27.1	41
SER	N	A	153	17.7	−16.0	26.4	36
SER	CA	A	153	16.6	−16.7	27.1	35
SER	CB	A	153	15.4	−15.7	27.2	29
SER	OG	A	153	15.0	−15.4	25.9	23
SER	C	A	153	16.2	−18.0	26.4	34
SER	O	A	153	15.5	−18.8	27.0	35
ASN	N	A	154	16.6	−18.2	25.2	37
ASN	CA	A	154	16.3	−19.3	24.4	37
ASN	CB	A	154	16.8	−20.6	25.1	37
ASN	CG	A	154	16.7	−21.8	24.2	38
ASN	OD1	A	154	16.6	−21.7	22.9	33
ASN	ND2	A	154	16.7	−23.0	24.8	36
ASN	C	A	154	14.9	−19.4	23.9	36
ASN	O	A	154	14.4	−20.4	23.3	38
TRP	N	A	155	14.1	−18.4	24.1	31
TRP	CA	A	155	12.7	−18.4	23.6	31
TRP	CB	A	155	11.6	−18.2	24.7	27
TRP	CG	A	155	11.7	−17.0	25.6	26
TRP	CD2	A	155	11.2	−15.7	25.4	24
TRP	CE2	A	155	11.5	−15.0	26.5	23
TRP	CE3	A	155	10.6	−15.1	24.3	27
TRP	CD1	A	155	12.3	−17.0	26.9	25
TRP	NE1	A	155	12.1	−15.8	27.4	24
TRP	CZ2	A	155	11.2	−13.6	26.6	23
TRP	CZ3	A	155	10.2	−13.8	24.4	28
TRP	CH2	A	155	10.5	−13.0	25.6	25
TRP	C	A	155	12.5	−17.3	22.5	30
TRP	O	A	155	13.0	−16.2	22.5	28
GLU	N	A	156	11.7	−17.7	21.4	32
GLU	CA	A	156	11.5	−16.8	20.3	32
GLU	CB	A	156	11.7	−17.5	18.9	30
GLU	CG	A	156	13.1	−18.1	18.7	36
GLU	CD	A	156	13.4	−19.3	19.6	35
GLU	OE1	A	156	14.4	−19.2	20.3	40
GLU	OE2	A	156	12.6	−20.2	19.7	36
GLU	C	A	156	10.1	−16.2	20.2	30
GLU	O	A	156	9.8	−15.3	19.4	32
GLY	N	A	157	9.2	−16.6	21.1	32
GLY	CA	A	157	7.8	−16.1	21.1	27
CLY	C	A	157	7.1	−16.1	22.4	28
GLY	O	A	157	7.7	−16.3	23.5	29
ILE	N	A	158	5.8	−15.8	22.4	28
ILE	CA	A	158	5.0	−15.7	23.6	24
ILE	CB	A	158	5.0	−14.2	24.2	22
ILE	CG2	A	158	4.4	−13.3	23.1	21
ILE	CG1	A	158	4.3	−14.1	25.5	18
ILE	CD1	A	158	4.3	−12.7	26.1	23
ILE	C	A	158	3.6	−16.2	23.5	25
ILE	O	A	158	2.9	−15.8	22.6	26
LEU	N	A	159	3.2	−17.0	24.5	27
LEU	CA	A	159	1.8	−17.5	24.6	28
LEU	CB	A	159	1.9	−19.0	24.9	25
LEU	CG	A	159	0.5	−19.7	25.0	27
LEU	CD1	A	159	−0.3	−19.5	23.7	30
LEU	CD2	A	159	0.6	−21.2	25.3	24
LEU	C	A	159	1.0	−16.8	25.6	28
LEU	O	A	159	1.1	−16.9	26.8	28
GLY	N	A	160	0.1	−15.9	25.1	29
GLY	CA	A	160	−0.8	−15.2	26.0	29
GLY	C	A	160	−2.0	−16.0	26.4	31
GLY	O	A	160	−2.9	−16.3	25.6	29
LEU	N	A	161	−2.0	−16.4	27.7	32
LEU	CA	A	161	−3.0	−17.3	28.2	30
LEU	CB	A	161	−2.4	−18.3	29.2	31
LEU	CG	A	161	−1.4	−19.3	28.5	34
LEU	CD1	A	161	−0.8	−20.2	29.5	32
LEU	CD2	A	161	−2.1	−20.1	27.4	35
LEU	C	A	161	−4.2	−16.6	28.8	30
LEU	O	A	161	−5.2	−17.2	29.3	26
ALA	N	A	162	−4.2	−15.3	28.9	27
ALA	CA	A	162	−5.3	−14.5	29.5	29
ALA	CB	A	162	−4.9	−13.1	29.9	29
ALA	C	A	162	−6.5	−14.5	28.6	31
ALA	O	A	162	−6.5	−15.1	27.5	29
TYR	N	A	163	−7.5	−13.7	29.0	32
TYR	CA	A	163	−8.8	−13.6	28.2	32
TYR	CB	A	163	−10.0	−13.4	29.1	32
TYR	CG	A	163	−10.1	−14.5	30.1	30
TYR	CD1	A	163	−9.5	−14.4	31.4	31
TYR	CE1	A	163	−9.6	−15.4	32.4	30
TYR	CD2	A	163	−10.8	−15.7	29.8	27
TYR	CE2	A	163	−10.9	−16.7	30.8	28
TYR	CZ	A	163	−10.3	−16.5	32.0	25
TYR	OH	A	163	−10.4	−17.5	33.0	28
TYR	C	A	163	−8.8	−12.6	27.0	33
TYR	O	A	163	−8.1	−11.6	27.1	30
ALA	N	A	164	−9.6	−12.8	26.1	34
ALA	CA	A	164	−9.8	−12.0	24.9	36
ALA	CB	A	164	−10.9	−12.6	24.0	37
ALA	C	A	164	−10.1	−10.5	25.2	35
ALA	O	A	164	−10.0	−9.7	24.2	41
GLU	N	A	165	−10.4	−10.2	26.4	37
GLU	CA	A	165	−10.8	−8.8	26.7	35
GLU	CB	A	165	−11.6	−8.6	28.0	42
GLU	CG	A	165	−11.9	−7.2	28.3	49
GLU	CD	A	165	−12.7	−7.1	29.6	55
GLU	OE1	A	165	−13.0	−8.1	30.2	56
GLU	OE2	A	165	−13.0	−6.0	30.0	56
GLU	C	A	165	−9.5	−7.9	26.7	33
GLU	O	A	165	−9.6	−6.7	26.5	30
ILE	N	A	166	−8.3	−8.4	26.9	34
ILE	CA	A	166	−7.1	−7.6	26.9	31
ILE	CB	A	166	−6.3	−7.8	28.2	31
ILE	CG2	A	166	−7.2	−7.2	29.4	28
ILE	CG1	A	166	−5.9	−9.2	28.5	28
ILE	CD1	A	166	−5.1	−9.5	29.8	27
ILE	C	A	166	−6.2	−7.9	25.7	31
ILE	O	A	166	−5.1	−7.4	25.7	32
ALA	N	A	167	−6.7	−8.7	24.8	33
ALA	CA	A	167	−6.0	−9.0	23.6	33
ALA	CB	A	167	−6.5	−10.2	22.9	28
ALA	C	A	167	−6.0	−7.8	22.6	31
ALA	O	A	167	−7.0	−7.1	22.5	34
ARG	N	A	168	−4.9	−7.6	21.9	34
ARG	CA	A	168	−4.8	−6.5	20.9	36
ARG	CB	A	168	−3.5	−5.8	20.9	38
ARG	CG	A	168	−3.2	−5.0	22.3	42
ARG	CD	A	168	−4.3	−4.0	22.6	44
ARG	NE	A	168	−4.0	−3.3	23.8	51
ARG	CZ	A	168	−3.0	−2.5	24.0	53
ARG	NH1	A	168	−2.1	−2.3	23.0	56
ARG	NH2	A	168	−2.8	−1.9	25.2	51
ARG	C	A	168	−5.0	−7.1	19.5	41
ARG	O	A	168	−4.6	−8.3	19.3	36
PRO	N	A	169	−5.5	−6.4	18.5	42
PRO	CD	A	169	−5.2	−6.7	17.1	46
PRO	CA	A	169	−6.0	−5.0	18.6	46
PRO	CB	A	169	−6.3	−4.7	17.1	49
PRO	CG	A	169	−5.1	−5.3	16.5	50
PRO	C	A	169	−7.2	−4.8	19.5	46
PRO	O	A	169	−7.4	−3.7	20.1	47
ASP	N	A	170	−8.0	−5.9	19.6	47
ASP	CA	A	170	−9.2	−5.8	20.5	49
ASP	CB	A	170	−10.2	−4.9	19.8	53
ASP	CG	A	170	−10.7	−5.4	18.5	59
ASP	OD1	A	170	−11.8	−5.8	18.3	60
ASP	OD2	A	170	−9.9	−5.4	17.6	64
ASP	C	A	170	−9.7	−7.2	20.8	48
ASP	O	A	170	−9.2	−8.2	20.2	45
ASP	N	A	171	−10.7	−7.3	21.7	48
ASP	CA	A	171	−11.3	−8.5	22.1	48
ASP	CB	A	171	−12.4	−8.2	23.1	52
ASP	CG	A	171	−13.5	−7.4	22.5	56
ASP	OD1	A	171	−13.7	−6.2	23.0	57
ASP	OD2	A	171	−14.2	−7.8	21.6	59
ASP	C	A	171	−11.8	−9.5	21.0	49
ASP	O	A	171	−12.2	−10.6	21.3	50
SER	N	A	172	−11.7	−9.0	19.8	49
SER	CA	A	172	−12.2	−9.9	18.7	48
SER	CB	A	172	−12.7	−9.1	17.5	50
SER	OG	A	172	−11.6	−8.2	17.0	54
SER	C	A	172	−11.1	−10.9	18.2	48
SER	O	A	172	−11.4	−11.9	17.5	45
LEU	N	A	173	−9.8	−10.6	18.6	44
LEU	CA	A	173	−8.7	−11.5	18.2	41
LEU	CB	A	173	−7.4	−10.7	18.2	43
LEU	CG	A	173	−6.2	−11.6	17.7	43
LEU	CD1	A	173	−6.4	−12.0	16.3	43
LEU	CD2	A	173	−4.9	−10.8	17.9	39
LEU	C	A	173	−8.7	−12.7	19.2	40
LEU	O	A	173	−8.2	−12.6	20.3	37
GLU	N	A	174	−9.3	−13.8	18.7	40
GLU	CA	A	174	−9.4	−15.0	19.6	40
GLU	CB	A	174	−10.3	−16.1	18.9	40
GLU	CG	A	174	−10.4	−17.3	19.7	43
GLU	CD	A	174	−11.3	−18.3	18.9	45
GLU	OE1	A	174	−12.4	−18.5	19.3	45
GLU	OE2	A	174	−10.8	−18.9	18.0	45
GLU	C	A	174	−8.1	−15.5	20.1	41
GLU	O	A	174	−7.2	−15.9	19.3	37
PRO	N	A	175	−7.9	−15.6	21.4	38
PRO	CD	A	175	−8.7	−14.7	22.3	38
PRO	CA	A	175	−6.8	−16.1	22.1	33
PRO	CB	A	175	−7.2	−15.9	23.6	37
PRO	CG	A	175	−7.7	−14.5	23.5	40
PRO	C	A	175	−6.5	−17.5	21.8	32
PRO	O	A	175	−7.4	−18.3	21.5	28
PHE	N	A	176	−5.2	−17.9	21.8	28
PHE	CA	A	176	−4.8	−19.3	21.5	28
PHE	CB	A	176	−3.3	−19.5	21.6	29
PHE	CG	A	176	−2.8	−20.9	21.4	29
PHE	CD1	A	176	−2.6	−21.4	20.1	30
PHE	CD2	A	176	−2.7	−21.7	22.5	28
PHE	CE1	A	176	−2.3	−22.8	19.9	28
PHE	CE2	A	176	−2.3	−23.1	22.3	28
PHE	CZ	A	176	−2.1	−23.6	21.0	29
PHE	C	A	176	−5.4	−20.4	22.3	32
PHE	O	A	176	−5.6	−21.5	21.8	33
PHE	N	A	177	−5.8	−20.1	23.5	34
PHE	CA	A	177	−6.4	−21.2	24.3	34
PHE	CB	A	177	−6.1	−21.0	25.8	32
PHE	CG	A	177	−6.4	−22.2	26.7	31
PHE	CD1	A	177	−5.5	−23.2	26.9	26
PHE	CD2	A	177	−7.7	−22.4	27.2	30
PHE	CE1	A	177	−5.7	−24.3	27.7	29
PHE	CE2	A	177	−8.0	−23.5	28.0	30
PHE	CZ	A	177	−7.0	−24.5	28.3	28
PHE	C	A	177	−7.9	−21.4	24.0	36
PHE	O	A	177	−8.4	−22.5	24.1	27
ASP	N	A	178	−8.5	−20.3	23.7	36
ASP	CA	A	178	−10.0	−20.4	23.3	41
ASP	CB	A	178	−10.6	−19.0	23.2	45
ASP	CG	A	178	−10.5	−18.2	24.4	50
ASP	OD1	A	178	−11.5	−17.8	25.0	49
ASP	OD2	A	178	−9.4	−17.9	24.9	52
ASP	C	A	178	−10.1	−21.2	22.0	39
ASP	O	A	178	−11.1	−21.9	21.9	40
SER	N	A	179	−9.1	−21.0	21.1	38
SER	CA	A	179	−9.2	−21.7	19.9	37
SER	CB	A	179	−8.2	−21.2	18.9	34
SER	OG	A	179	−8.4	−19.8	18.6	38
SER	C	A	179	−8.8	−23.2	20.1	39
SER	O	A	179	−9.3	−24.1	19.4	42
LEU	N	A	180	−8.0	−23.4	21.2	39
LEU	CA	A	180	−7.6	−24.7	21.5	39
LEU	CB	A	180	−6.6	−24.7	22.6	38
LEU	CG	A	180	−6.1	−26.1	23.1	37
LEU	CD1	A	180	−5.6	−26.9	21.9	35
LEU	CD2	A	180	−5.0	−26.0	24.2	36
LEU	C	A	180	−8.9	−25.5	22.0	37
LEU	O	A	180	−9.0	−26.7	21.6	38
VAL	N	A	181	−9.7	−24.9	22.8	34
VAL	CA	A	181	−10.9	−25.5	23.3	36
VAL	CB	A	181	−11.4	−24.8	24.6	36
VAL	CG1	A	181	−12.7	−25.5	25.1	32
VAL	CG2	A	181	−10.4	−24.7	25.7	35
VAL	C	A	181	−12.0	−25.6	22.3	38
VAL	O	A	181	−12.7	−26.7	22.2	34
LYS	N	A	182	−12.1	−24.6	21.4	41
LYS	CA	A	182	−13.2	−24.7	20.4	44
LYS	CB	A	182	−13.5	−23.3	19.9	44
LYS	CG	A	182	−14.1	−22.3	20.9	44
LYS	CD	A	182	−14.3	−21.0	20.1	49
LYS	CE	A	182	−14.9	−19.9	21.1	53
LYS	NZ	A	182	−16.2	−20.2	21.7	58
LYS	C	A	182	−12.9	−25.6	19.2	44
LYS	O	A	182	−13.7	−25.8	18.4	49
GLN	N	A	183	−11.7	−26.2	19.2	41
GLN	CA	A	183	−11.4	−27.0	18.1	36
GLN	CB	A	183	−10.3	−26.4	17.2	36
GLN	CG	A	183	−10.6	−25.0	16.7	35
GLN	CD	A	183	−9.4	−24.5	15.9	35
GLN	OE1	A	183	−8.5	−25.2	15.6	36
GLN	NE2	A	183	−9.4	−23.2	15.7	37
GLN	C	A	183	−10.9	−28.4	18.5	38
GLN	O	A	183	−10.8	−29.3	17.6	32
THR	N	A	184	−10.7	−28.6	19.8	36
THR	CA	A	184	−10.3	−29.9	20.3	37
THR	CB	A	184	−8.8	−30.0	20.6	39
THR	OG1	A	184	−8.5	−29.1	21.6	39
THR	CG2	A	184	−8.0	−29.6	19.3	40
THR	C	A	184	−11.0	−30.4	21.5	36
THR	O	A	184	−11.9	−29.7	22.0	37
HIS	N	A	185	−10.6	−31.6	22.0	40
HIS	CA	A	185	−11.2	−32.2	23.2	45
HIS	CB	A	185	−11.0	−33.7	23.1	47
HIS	CG	A	185	−9.6	−34.1	23.1	52
HIS	CD2	A	185	−8.8	−34.5	24.1	53
HIS	ND1	A	185	−8.8	−34.0	22.0	55
HIS	CE1	A	185	−7.5	−34.4	22.3	54
HIS	NE2	A	185	−7.5	−34.7	23.6	55
HIS	C	A	185	−10.7	−31.6	24.5	43
HIS	O	A	185	−11.1	−32.0	25.5	44
VAL	N	A	186	−9.6	−30.8	24.3	38
VAL	CA	A	186	−9.0	−30.2	25.5	33
VAL	CB	A	186	−7.7	−29.4	25.1	34
VAL	CG1	A	186	−7.0	−28.8	26.4	35
VAL	CG2	A	186	−6.7	−30.2	24.3	32
VAL	C	A	186	−9.9	−29.4	26.4	27
VAL	O	A	186	−10.5	−28.4	26.0	30
PRO	N	A	187	−10.1	−29.9	27.7	27
PRO	CD	A	187	−9.7	−31.2	28.1	30
PRO	CA	A	187	−10.9	−29.2	28.7	28
PRO	CB	A	187	−10.6	−30.1	29.9	27
PRO	CG	A	187	−10.7	−31.4	29.3	28
PRO	C	A	187	−10.5	−27.8	28.9	29
PRO	O	A	187	−9.3	−27.5	28.7	28
ASN	N	A	188	−11.4	−26.9	29.2	31
ASN	CA	A	188	−11.1	−25.5	29.3	31
ASN	CB	A	188	−12.4	−24.6	29.2	28
ASN	CG	A	188	−12.1	−23.2	29.3	31
ASN	OD1	A	188	−11.0	−22.7	29.1	32
ASN	ND2	A	188	−13.1	−22.4	29.5	27
ASN	C	A	188	−10.5	−25.3	30.7	34
ASN	O	A	188	−11.1	−24.8	31.6	30
LEU	N	A	189	−9.2	−25.7	30.8	35
LEU	CA	A	189	−8.5	−25.7	32.1	36
LEU	CB	A	189	−9.2	−26.6	33.1	33
LEU	CG	A	189	−8.6	−26.7	34.5	36
LEU	CD1	A	189	−9.5	−27.5	35.4	33
LEU	CD2	A	189	−7.1	−27.3	34.5	32
LEU	C	A	189	−7.0	−26.0	31.9	35
LEU	O	A	189	−6.7	−26.9	31.1	35
PHE	N	A	190	−6.1	−25.3	32.5	31
PHE	CA	A	190	−4.7	−25.6	32.4	31
PHE	CB	A	190	−3.9	−24.8	31.3	27
PHE	CG	A	190	−3.9	−23.3	31.6	30
PHE	CD1	A	190	−5.0	−22.5	31.2	32
PHE	CD2	A	190	−2.8	−22.8	32.1	26
PHE	CE1	A	190	−4.9	−21.1	31.4	33
PHE	CE2	A	190	−2.7	−21.4	32.3	28
PHE	CZ	A	190	−3.8	−20.6	32.0	29
PHE	C	A	190	−4.1	−25.4	33.8	28
PHE	O	A	190	−4.6	−24.6	34.6	23
SER	N	A	191	−2.9	−26.1	34.0	26
SER	CA	A	191	−2.2	−25.9	35.3	25
SER	CB	A	191	−2.6	−27.1	36.2	26
SER	OG	A	191	−2.2	−28.4	35.6	25
SER	C	A	191	−0.7	−25.7	35.1	26
SER	O	A	191	−0.1	−26.3	34.2	24
LEU	N	A	192	−0.2	−24.9	36.0	25
LEU	CA	A	192	1.2	−24.6	36.0	26
LEU	CB	A	192	1.5	−23.1	35.7	20
LEU	CG	A	192	1.0	−22.7	34.3	22
LEU	CD1	A	192	1.1	−21.2	34.1	17
LEU	CD2	A	192	1.7	−23.5	33.2	21
LEU	C	A	192	2.1	−24.9	37.3	26
LEU	O	A	192	1.7	−24.4	38.4	25
GLN	N	A	193	3.1	−25.6	37.1	26
GLN	CA	A	193	4.1	−25.9	38.2	25
GLN	CB	A	193	4.3	−27.4	38.4	27
GLN	CG	A	193	5.3	−27.6	39.5	30
GLN	CD	A	193	5.6	−29.1	39.8	34
GLN	OE1	A	193	6.4	−29.7	39.1	36
GLN	NE2	A	193	4.9	−29.7	40.8	34
GLN	C	A	193	5.4	−25.3	37.8	27
GLN	O	A	193	6.1	−25.9	37.0	30
LEU	N	A	194	5.7	−24.1	38.4	29
LEU	CA	A	194	7.0	−23.5	38.0	28
LEU	CB	A	194	6.8	−22.0	38.0	24
LEU	CG	A	194	5.8	−21.6	36.9	26
LEU	CD1	A	194	5.6	−20.1	36.9	24
LEU	CD2	A	194	6.2	−22.1	35.5	26
LEU	C	A	194	8.0	−23.9	39.1	27
LEU	O	A	194	7.7	−23.7	40.3	26
CYS	N	A	195	9.1	−24.5	38.8	28
CYS	CA	A	195	10.0	−25.0	39.8	39
CYS	C	A	195	11.3	−24.2	40.1	45
CYS	O	A	195	12.0	−24.5	41.1	52
CYS	CB	A	195	10.5	−26.4	39.5	39
CYS	SG	A	195	9.1	−27.6	39.4	39
GLY	N	A	196	11.5	−23.1	39.4	50
GLY	CA	A	196	12.7	−22.3	39.6	57
GLY	C	A	196	14.0	−23.2	39.6	60
GLY	O	A	196	14.2	−23.9	38.7	60
ALA	N	A	197	14.7	−23.2	40.7	59
ALA	CA	A	197	15.9	−24.0	40.9	61
ALA	CB	A	197	17.1	−23.3	40.2	62
ALA	C	A	197	16.2	−24.4	42.3	61
ALA	O	A	197	16.4	−25.5	42.7	62
ALA	N	A	208	21.6	−22.0	37.0	75
ALA	CA	A	208	21.0	−20.9	36.3	74
ALA	CB	A	208	22.0	−20.2	35.4	71
ALA	C	A	208	19.8	−21.3	35.5	74
ALA	O	A	208	19.1	−20.5	34.9	75
SER	N	A	209	19.5	−22.6	35.5	71
SER	CA	A	209	18.4	−23.2	34.8	68
SER	CB	A	209	18.9	−24.4	34.0	69
SER	OG	A	209	19.9	−24.1	33.1	69
SER	C	A	209	17.2	−23.5	35.6	66
SER	O	A	209	17.3	−24.1	36.7	65
VAL	N	A	210	16.0	−23.2	35.1	62
VAL	CA	A	210	14.7	−23.4	35.7	57
VAL	CB	A	210	14.0	−22.1	36.0	56
VAL	CG1	A	210	14.8	−21.1	36.9	59
VAL	CG2	A	210	13.5	−21.4	34.7	53
VAL	C	A	210	13.9	−24.3	34.9	54
VAL	O	A	210	13.9	−24.2	33.7	59
GLY	N	A	211	13.1	−25.1	35.5	51
GLY	CA	A	211	12.2	−26.0	34.8	45
GLY	C	A	211	10.8	−26.0	35.4	39
GLY	O	A	211	10.5	−25.2	36.3	42
GLY	N	A	212	9.9	−26.8	34.8	37
GLY	CA	A	212	8.5	−26.8	35.3	33
GLY	C	A	212	7.6	−27.6	34.5	32
GLY	O	A	212	8.1	−28.4	33.6	31
SER	N	A	213	6.3	−27.5	34.7	31
SER	CA	A	213	5.3	−28.3	34.0	30
SER	CB	A	213	4.9	−29.6	34.7	27
SER	OG	A	213	6.0	−30.5	34.9	30
SER	C	A	213	4.0	−27.6	33.6	30
SER	O	A	213	3.4	−27.0	34.5	28
MET	N	A	214	3.6	−27.6	32.4	27
MET	CA	A	214	2.3	−27.0	32.0	27
MET	CB	A	214	2.5	−25.9	30.9	27
MET	CG	A	214	1.1	−25.3	30.5	24
MET	SD	A	214	1.1	−24.0	29.2	26
MET	CE	A	214	1.8	−25.0	27.9	25
MET	C	A	214	1.4	−28.1	31.6	31
MET	O	A	214	1.6	−28.7	30.5	32
ILE	N	A	215	0.4	−28.4	32.4	29
ILE	CA	A	215	−0.5	−29.4	32.1	30
ILE	CB	A	215	−1.0	−30.1	33.4	33
ILE	CG2	A	215	−2.0	−31.2	33.0	31
ILE	CG1	A	215	0.2	−30.7	34.2	31
ILE	CD1	A	215	1.1	−31.7	33.4	33
ILE	C	A	215	−1.7	−28.8	31.4	34
ILE	O	A	215	−2.5	−28.0	32.0	35
ILE	N	A	216	−1.8	−29.0	30.1	35
ILE	CA	A	216	−2.9	−28.5	29.3	37
ILE	CB	A	216	−2.5	−28.3	27.8	36
ILE	CG2	A	216	−3.7	−27.8	27.0	36
ILE	CG1	A	216	−1.4	−27.3	27.6	37
ILE	CD1	A	216	−0.1	−27.7	28.3	35
ILE	C	A	216	−4.2	−29.4	29.3	36
ILE	O	A	216	−4.1	−30.5	29.0	36
GLY	N	A	217	−5.3	−28.8	29.8	35
GLY	CA	A	217	−6.5	−29.5	29.8	38
GLY	C	A	217	−6.8	−30.2	31.1	40
GLY	O	A	217	−7.9	−30.8	31.3	44
GLY	N	A	218	−5.8	−30.3	32.0	39
GLY	CA	A	218	−6.1	−31.1	33.3	39
GLY	C	A	218	−5.3	−30.7	34.5	39
GLY	O	A	218	−4.7	−29.7	34.6	39
ILE	N	A	219	−5.3	−31.7	35.4	39
ILE	CA	A	219	−4.6	−31.5	36.7	35
ILE	CB	A	219	−5.6	−31.3	37.9	34
ILE	CG2	A	219	−4.8	−31.3	39.2	34
ILE	CG1	A	219	−6.4	−30.1	37.7	34
ILE	CD1	A	219	−7.4	−29.8	38.8	32
ILE	C	A	219	−3.8	−32.8	37.0	38
ILE	O	A	219	−4.4	−33.9	37.0	41
ASP	N	A	220	−2.5	−32.7	37.2	33
ASP	CA	A	220	−1.7	−33.9	37.4	35
ASP	CB	A	220	−0.3	−33.9	36.7	34
ASP	CG	A	220	0.5	−35.2	36.9	35
ASP	OD1	A	220	0.8	−35.8	36.0	35
ASP	OD2	A	220	0.7	−35.5	38.1	36
ASP	C	A	220	−1.5	−33.9	39.0	37
ASP	O	A	220	−0.8	−33.0	39.5	38
HIS	N	A	221	−2.0	−34.9	39.6	39
HIS	CA	A	221	−2.0	−35.0	41.1	38
HIS	CB	A	221	−3.1	−36.0	41.6	41
HIS	CG	A	221	−4.5	−35.5	41.2	43
HIS	CD2	A	221	−5.3	−36.0	40.3	45
HIS	ND1	A	221	−5.1	−34.4	41.7	45
HIS	CE1	A	221	−6.3	−34.3	41.2	44
HIS	NE2	A	221	−6.4	−35.2	40.3	45
HIS	C	A	221	−0.6	−35.3	41.7	38
HIS	O	A	221	−0.5	−35.3	43.0	41
SER	N	A	222	0.4	−35.5	40.9	40
SER	CA	A	222	1.7	−35.7	41.5	37
SER	CB	A	222	2.5	−36.8	40.6	38
SER	OG	A	222	2.7	−36.3	39.3	40
SER	C	A	222	2.6	−34.5	41.6	37
SER	O	A	222	3.7	−34.5	42.1	34
LEU	N	A	223	2.0	−33.3	41.1	33
LEU	CA	A	223	2.7	−32.1	41.1	29
LEU	CB	A	223	2.4	−31.2	39.8	27
LEU	CG	A	223	2.8	−31.9	38.5	28
LEU	CD1	A	223	2.4	−31.1	37.3	26
LEU	CD2	A	223	4.3	−32.3	38.5	29
LEU	C	A	223	2.4	−31.2	42.4	32
LEU	O	A	223	3.0	−30.2	42.5	30
TYR	N	A	224	1.6	−31.7	43.3	30
TYR	CA	A	224	1.3	−31.0	44.5	32
TYR	CB	A	224	0.1	−30.1	44.4	34
TYR	CG	A	224	−1.2	−30.8	44.2	34
TYR	CD1	A	224	−1.6	−31.2	43.0	35
TYR	CE1	A	224	−2.8	−31.9	42.8	34
TYR	CD2	A	224	−2.0	−31.0	45.3	35
TYR	CE2	A	224	−3.3	−31.6	45.1	37
TYR	CZ	A	224	−3.7	−32.0	43.9	36
TYR	OH	A	224	−4.9	−32.6	43.7	34
TYR	C	A	224	1.1	−31.9	45.7	34
TYR	O	A	224	1.1	−33.1	45.5	33
THR	N	A	225	1.0	−31.3	46.9	33
THR	CA	A	225	0.8	−32.1	48.1	35
THR	CB	A	225	2.1	−32.2	49.0	35
THR	OG1	A	225	2.6	−30.9	49.3	34
THR	CG2	A	225	3.1	−33.1	48.3	36
THR	C	A	225	−0.3	−31.4	48.9	34
THR	O	A	225	−0.4	−30.1	48.9	35
GLY	N	A	226	−1.1	−32.1	49.6	34
GLY	CA	A	226	−2.2	−31.6	50.4	32
GLY	C	A	226	−3.4	−31.2	49.6	35
GLY	O	A	226	−3.7	−31.9	48.5	36
SER	N	A	227	−4.2	−30.2	50.0	33
SER	CA	A	227	−5.4	−29.8	49.4	35
SER	CB	A	227	−6.5	−29.6	50.5	35
SER	OG	A	227	−6.7	−30.8	51.2	40
SER	C	A	227	−5.3	−28.6	48.5	35
SER	O	A	227	−4.5	−27.7	48.7	30
LEU	N	A	228	−6.1	−28.6	47.4	33
LEU	CA	A	228	−6.2	−27.5	46.5	33
LEU	CB	A	228	−6.7	−27.9	45.1	32
LEU	CG	A	228	−5.7	−28.9	44.3	36
LEU	CD1	A	228	−6.3	−29.4	43.0	35
LEU	CD2	A	228	−4.4	−28.1	44.0	35
LEU	C	A	228	−7.3	−26.5	47.0	33
LEU	O	A	228	−8.4	−26.9	47.3	34
TRP	N	A	229	−6.9	−25.2	47.1	29
TRP	CA	A	229	−7.8	−24.2	47.5	28
TRP	CB	A	229	−7.3	−23.4	48.7	28
TRP	CG	A	229	−7.3	−24.2	50.0	28
TRP	CD2	A	229	−8.3	−24.2	51.0	28
TRP	CE2	A	229	−8.0	−25.1	51.9	30
TRP	CE3	A	229	−9.5	−23.4	51.2	30
TRP	CD1	A	229	−6.4	−25.1	50.3	32
TRP	NE1	A	229	−6.8	−25.7	51.5	32
TRP	CZ2	A	229	−8.8	−25.4	53.1	31
TRP	CZ3	A	229	−10.3	−23.7	52.3	30
TRP	CH2	A	229	−9.9	−24.6	53.2	28
TRP	C	A	229	−8.0	−23.2	46.3	31
TRP	O	A	229	−7.1	−22.7	45.7	29
TYR	N	A	230	−9.3	−22.9	46.1	29
TYR	CA	A	230	−9.7	−22.1	45.0	28
TYR	CB	A	230	−10.8	−22.7	44.1	28
TYR	CG	A	230	−10.3	−24.0	43.5	26
TYR	CD1	A	230	−10.4	−25.2	44.2	26
TYR	CE1	A	230	−10.0	−26.4	43.6	27
TYR	CD2	A	230	−9.9	−24.1	42.2	27
TYR	CE2	A	230	−9.5	−25.2	41.6	25
TYR	CZ	A	230	−9.5	−26.4	42.3	25
TYR	OH	A	230	−9.1	−27.6	41.7	27
TYR	C	A	230	−10.1	−20.7	45.3	26
TYR	O	A	230	−10.9	−20.4	46.3	29
THR	N	A	231	−9.6	−19.7	44.6	26
THR	CA	A	231	−10.0	−18.3	44.7	27
THR	CB	A	231	−8.7	−17.4	45.0	23
THR	OG1	A	231	−9.1	−16.1	45.3	25
THR	CG2	A	231	−7.8	−17.4	43.8	22
THR	C	A	231	−10.7	−17.9	43.5	34
THR	O	A	231	−10.2	−18.1	42.4	32
PRO	N	A	232	−11.9	−17.2	43.6	37
PRO	CD	A	232	−12.7	−17.2	44.8	40
PRO	CA	A	232	−12.7	−16.7	42.5	38
PRO	CB	A	232	−13.8	−16.0	43.2	39
PRO	CG	A	232	−14.1	−17.0	44.3	40
PRO	C	A	232	−12.0	−15.8	41.5	38
PRO	O	A	232	−11.2	−14.9	41.9	41
ILE	N	A	233	−12.2	−16.0	40.2	35
ILE	CA	A	233	−11.7	−15.1	39.2	32
ILE	CB	A	233	−11.5	−15.7	37.8	31
ILE	CG2	A	233	−11.2	−14.7	36.8	26
ILE	CG1	A	233	−10.5	−16.9	37.9	31
ILE	CD1	A	233	−10.3	−17.6	36.5	26
ILE	C	A	233	−12.7	−13.9	39.2	35
ILE	O	A	233	−13.8	−14.1	38.8	40
ARG	N	A	234	−12.2	−12.8	39.7	35
ARG	CA	A	234	−13.1	−11.6	39.8	39
ARG	CB	A	234	−12.4	−10.5	40.5	33
ARG	CG	A	234	−13.2	−9.2	40.7	35
ARG	CD	A	234	−12.4	−8.1	41.4	32
ARG	NE	A	234	−13.2	−6.9	41.6	34
ARG	CZ	A	234	−12.7	−5.7	41.5	38
ARG	NH1	A	234	−11.4	−5.5	41.3	41
ARG	NH2	A	234	−13.5	−4.6	41.7	39
ARG	C	A	234	−13.6	−11.0	38.5	41
ARG	O	A	234	−14.6	−10.4	38.4	44
ARG	N	A	235	−12.9	−11.3	37.4	41
ARG	CA	A	235	−13.2	−10.8	36.1	39
ARG	CB	A	235	−12.9	−9.3	36.1	38
ARG	CG	A	235	−13.1	−8.6	34.7	40
ARG	CD	A	235	−12.8	−7.1	34.9	39
ARG	NE	A	235	−12.9	−6.3	33.6	38
ARG	CZ	A	235	−12.5	−5.1	33.5	40
ARG	NH1	A	235	−11.9	−4.5	34.5	43
ARG	NH2	A	235	−12.6	−4.5	32.3	42
ARG	C	A	235	−12.4	−11.5	35.1	40
ARG	O	A	235	−11.2	−11.8	35.3	43
GLU	N	A	236	−13.0	−11.8	33.9	41
GLU	CA	A	236	−12.2	−12.5	32.9	39
GLU	CB	A	236	−13.1	−13.5	32.2	42
GLU	CG	A	236	−13.7	−14.5	33.2	44
GLU	CD	A	236	−14.6	−15.5	32.6	46
GLU	OE1	A	236	−15.8	−15.4	32.7	50
GLU	OE2	A	236	−14.1	−16.4	31.9	49
GLU	C	A	236	−11.6	−11.5	31.9	40
GLU	O	A	236	−12.2	−11.1	30.9	43
TRP	N	A	237	−10.3	−11.2	32.2	36
TRP	CA	A	237	−9.5	−10.3	31.4	34
TRP	CB	A	237	−9.8	−8.8	31.6	29
TRP	CG	A	237	−9.6	−8.2	33.0	28
TRP	CD2	A	237	−9.2	−6.9	33.3	28
TRP	CE2	A	237	−9.2	−6.8	34.7	27
TRP	CE3	A	237	−8.9	−5.8	32.6	31
TRP	CD1	A	237	−9.8	−8.9	34.2	28
TRP	NE1	A	237	−9.6	−8.0	35.2	25
TRP	CZ2	A	237	−8.9	−5.6	35.4	26
TRP	CZ3	A	237	−8.5	−4.6	33.2	32
TRP	CH2	A	237	−8.6	−4.5	34.6	29
TRP	C	A	237	−8.1	−10.8	31.8	31
TRP	O	A	237	−7.7	−11.8	31.3	32
TYR	N	A	238	−7.5	−10.2	32.8	29
TYR	CA	A	238	−6.2	−10.8	33.3	28
TYR	CB	A	238	−5.5	−9.8	34.2	24
TYR	CG	A	238	−4.9	−8.6	33.5	25
TYR	CD1	A	238	−3.7	−8.6	32.9	26
TYR	CE1	A	238	−3.2	−7.5	32.3	26
TYR	CD2	A	238	−5.7	−7.4	33.5	27
TYR	CE2	A	238	−5.1	−6.2	32.9	27
TYR	CZ	A	238	−3.9	−6.3	32.3	25
TYR	OH	A	238	−3.4	−5.2	31.7	26
TYR	C	A	238	−6.8	−11.8	34.2	26
TYR	O	A	238	−8.0	−11.8	34.4	30
TYR	N	A	239	−6.0	−12.7	34.8	31
TYR	CA	A	239	−6.6	−13.6	35.8	29
TYR	CB	A	239	−5.8	−14.9	35.9	27
TYR	CG	A	239	−5.9	−15.8	34.7	28
TYR	CD1	A	239	−5.0	−15.7	33.6	26
TYR	CE1	A	239	−5.1	−16.5	32.5	25
TYR	CD2	A	239	−6.9	−16.8	34.6	27
TYR	CE2	A	239	−7.1	−17.6	33.4	26
TYR	CZ	A	239	−6.2	−17.4	32.4	27
TYR	OH	A	239	−6.3	−18.2	31.3	20
TYR	C	A	239	−6.5	−12.8	37.1	31
TYR	O	A	239	−5.5	−12.8	37.8	31
GLU	N	A	240	−7.6	−12.2	37.4	31
GLU	CA	A	240	−7.8	−11.3	38.5	33
GLU	CB	A	240	−8.6	−10.1	38.3	33
GLU	CG	A	240	−8.7	−9.2	39.5	33
GLU	CD	A	240	−9.6	−8.0	39.2	35
GLU	OE1	A	240	−10.2	−7.9	38.1	38
GLU	OE2	A	240	−9.7	−7.1	40.0	40
GLU	C	A	240	−8.3	−12.1	39.8	30
GLU	O	A	240	−9.3	−12.8	39.7	27
VAL	N	A	241	−7.6	−11.9	40.9	29
VAL	CA	A	241	−8.0	−12.5	42.1	29
VAL	CB	A	241	−7.0	−13.5	42.6	28
VAL	CG1	A	241	−6.9	−14.7	41.6	26
VAL	CG2	A	241	−5.6	−12.9	42.9	27
VAL	C	A	241	−8.1	−11.3	43.2	30
VAL	O	A	241	−7.8	−10.2	42.9	28
ILE	N	A	242	−8.6	−11.7	44.4	26
ILE	CA	A	242	−8.8	−10.7	45.4	31
ILE	CB	A	242	−10.2	−10.5	45.7	31
ILE	CG2	A	242	−10.4	−9.4	46.9	32
ILE	CG1	A	242	−11.0	−10.0	44.5	33
ILE	CD1	A	242	−12.5	−9.7	44.7	35
ILE	C	A	242	−8.0	−11.1	46.7	30
ILE	O	A	242	−8.2	−12.1	47.3	35
ILE	N	A	243	−7.1	−10.2	47.1	29
ILE	CA	A	243	−6.3	−10.4	48.3	30
ILE	CB	A	243	−4.9	−9.9	48.2	28
ILE	CG2	A	243	−4.1	−10.0	49.5	26
ILE	CG1	A	243	−4.2	−10.6	47.0	26
ILE	CD1	A	243	−2.8	−10.1	46.7	29
ILE	C	A	243	−7.0	−9.7	49.5	31
ILE	O	A	243	−7.4	−8.6	49.4	31
VAL	N	A	244	−7.2	−10.4	50.6	30
VAL	CA	A	244	−8.0	−9.8	51.7	32
VAL	CB	A	244	−9.2	−10.7	52.0	31
VAL	CG1	A	244	−10.1	−10.7	50.8	31
VAL	CG2	A	244	−8.8	−12.1	52.6	26
VAL	C	A	244	−7.2	−9.6	53.0	30
VAL	O	A	244	−7.7	−9.0	54.0	33
ARG	N	A	245	−5.9	−10.0	53.0	30
ARG	CA	A	245	−5.0	−9.9	54.2	27
ARG	CB	A	245	−5.6	−10.7	55.3	25
ARG	CG	A	245	−4.7	−10.8	56.6	31
ARG	CD	A	245	−5.3	−11.7	57.7	31
ARG	NE	A	245	−4.4	−11.9	58.8	31
ARG	CZ	A	245	−4.5	−11.2	60.0	32
ARG	NH1	A	245	−5.5	−10.4	60.2	30
ARG	NH2	A	245	−3.7	−11.5	61.0	26
ARG	C	A	245	−3.6	−10.3	53.8	28
ARG	O	A	245	−3.4	−11.3	53.1	24
VAL	N	A	246	−2.6	−9.6	54.4	27
VAL	CA	A	246	−1.2	−9.8	54.2	22
VAL	CB	A	246	−0.5	−8.8	53.2	19
VAL	CG1	A	246	1.0	−9.2	53.0	13
VAL	CG2	A	246	−1.3	−8.7	51.9	17
VAL	C	A	246	−0.5	−9.9	55.5	25
VAL	O	A	246	−0.6	−9.1	56.4	25
GLU	N	A	247	0.4	−11.0	55.7	21
GLU	CA	A	247	1.1	−11.2	56.9	19
GLU	CB	A	247	0.6	−12.4	57.7	17
GLU	CG	A	247	−0.9	−12.2	58.2	21
GLU	CD	A	247	−1.3	−13.5	58.9	25
GLU	OE1	A	247	−0.5	−14.4	59.0	22
GLU	OE2	A	247	−2.4	−13.5	59.4	22
GLU	C	A	247	2.6	−11.4	56.6	22
GLU	O	A	247	3.0	−12.0	55.6	18
ILE	N	A	248	3.5	−10.9	57.5	21
ILE	CA	A	248	4.9	−11.1	57.3	23
ILE	CB	A	248	5.7	−9.8	57.2	19
ILE	CG2	A	248	7.2	−10.1	57.1	20
ILE	CG1	A	248	5.2	−8.9	56.1	22
ILE	CD1	A	248	5.3	−9.6	54.7	22
ILE	C	A	248	5.2	−11.8	58.7	22
ILE	O	A	248	5.0	−11.2	59.7	20
ASN	N	A	249	5.5	−13.1	58.7	21
ASN	CA	A	249	5.7	−13.8	60.0	21
ASN	CB	A	249	6.9	−13.6	60.7	18
ASN	CG	A	249	8.1	−14.3	60.1	22
ASN	OD1	A	249	8.0	−15.1	59.2	23
ASN	ND2	A	249	9.3	−14.0	60.7	24
ASN	C	A	249	4.5	−13.8	60.9	23
ASN	O	A	249	4.6	−13.7	62.1	24
GLY	N	A	250	3.3	−13.8	60.3	22
GLY	CA	A	250	2.1	−13.8	61.1	21
GLY	C	A	250	1.7	−12.4	61.5	24
GLY	O	A	250	0.6	−12.2	62.0	27
GLN	N	A	251	2.5	−11.4	61.3	20
GLN	CA	A	251	2.2	−10.1	61.6	25
GLN	CB	A	251	3.3	−9.2	62.1	23
GLN	CG	A	251	2.9	−7.8	62.5	31
GLN	CD	A	251	4.0	−7.0	63.0	31
GLN	OE1	A	251	5.2	−7.3	62.8	40
GLN	NE2	A	251	3.7	−5.8	63.6	36
GLN	C	A	251	1.4	−9.4	60.5	21
GLN	O	A	251	1.9	−9.3	59.4	23
ASP	N	A	252	0.2	−9.0	60.8	24
ASP	CA	A	252	−0.7	−8.3	59.9	27
ASP	CB	A	252	−2.1	−8.2	60.6	29
ASP	CG	A	252	−3.1	−7.5	59.7	30
ASP	OD1	A	252	−2.9	−7.4	58.5	30
ASP	OD2	A	252	−4.2	−7.1	60.2	33
ASP	C	A	252	−0.2	−7.0	59.4	28
ASP	O	A	252	0.1	−6.1	60.2	29
LEU	N	A	253	−0.2	−6.8	58.1	28
LEU	CA	A	253	0.2	−5.4	57.6	32
LEU	CB	A	253	0.4	−5.4	56.0	32
LEU	CG	A	253	1.6	−6.2	55.5	36
LEU	CD1	A	253	1.7	−6.1	54.0	36
LEU	CD2	A	253	2.9	−5.8	56.2	35
LEU	C	A	253	−0.8	−4.4	58.0	31
LEU	O	A	253	−0.6	−3.2	58.0	35
LYS	N	A	254	−2.0	−4.9	58.4	32
LYS	CA	A	254	−3.1	−4.0	58.9	42
LYS	CB	A	254	−2.7	−3.5	60.3	46
LYS	CG	A	254	−3.7	−2.6	61.0	55
LYS	CD	A	254	−3.1	−2.2	62.4	58
LYS	CE	A	254	−4.1	−1.3	63.1	62
LYS	NZ	A	254	−5.4	−1.9	63.4	64
LYS	C	A	254	−3.6	−2.9	58.0	42
LYS	O	A	254	−4.2	−1.9	58.4	42
MET	N	A	255	−3.4	−3.1	56.7	39
MET	CA	A	255	−3.8	−2.1	55.7	38
MET	CB	A	255	−2.9	−2.0	54.5	36
MET	CG	A	255	−1.5	−1.7	54.7	38
MET	SD	A	255	−0.6	−1.7	53.2	36
MET	CE	A	255	−1.0	−0.1	52.5	38
MET	C	A	255	−5.3	−2.3	55.2	37
MET	O	A	255	−5.8	−3.4	55.3	41
ASP	N	A	256	−5.9	−1.2	54.8	35
ASP	CA	A	256	−7.3	−1.4	54.2	37
ASP	CB	A	256	−7.8	−0.1	53.7	42
ASP	CG	A	256	−9.2	−0.2	53.0	50
ASP	OD1	A	256	−9.6	−1.3	52.9	51
ASP	OD2	A	256	−9.8	0.8	52.7	57
ASP	C	A	256	−7.0	−2.4	53.1	36
ASP	O	A	256	−6.2	−2.2	52.2	32
CYS	N	A	257	−7.8	−3.5	53.0	38
CYS	CA	A	257	−7.6	−4.5	52.0	42
CYS	C	A	257	−7.7	−4.0	50.5	43
CYS	O	A	257	−7.3	−4.8	49.6	44
CYS	CB	A	257	−8.4	−5.7	52.2	44
CYS	SG	A	257	−10.2	−5.4	52.1	50
LYS	N	A	258	−8.2	−2.8	50.3	43
LYS	CA	A	258	−8.3	−2.4	48.9	43
LYS	CB	A	258	−9.2	−1.2	48.6	47
LYS	CG	A	258	−10.7	−1.5	48.8	52
LYS	CD	A	258	−11.5	−0.2	48.4	55
LYS	CE	A	258	−13.0	−0.3	48.6	56
LYS	NZ	A	258	−13.4	−0.6	50.0	62
LYS	C	A	258	−6.9	−2.0	48.4	41
LYS	O	A	258	−6.6	−1.9	47.2	40
GLU	N	A	259	−6.0	−1.7	49.4	36
GLU	CA	A	259	−4.6	−1.3	49.0	37
GLU	CB	A	259	−3.9	−0.7	50.2	40
GLU	CG	A	259	−4.5	0.5	50.9	45
GLU	CD	A	259	−4.6	1.7	49.9	46
GLU	OE1	A	259	−3.9	1.6	48.9	50
GLU	OE2	A	259	−5.2	2.7	50.2	46
GLU	C	A	259	−3.9	−2.5	48.4	35
GLU	O	A	259	−3.0	−2.3	47.6	32
TYR	N	A	260	−4.3	−3.7	48.8	33
TYR	CA	A	260	−3.6	−4.9	48.3	32
TYR	CB	A	260	−4.0	−6.1	49.2	29
TYR	CG	A	260	−3.6	−5.9	50.7	24
TYR	CD1	A	260	−4.4	−6.5	51.7	24
TYR	CE1	A	260	−4.1	−6.3	53.0	28
TYR	CD2	A	260	−2.5	−5.2	51.1	26
TYR	CE2	A	260	−2.1	−5.1	52.4	22
TYR	CZ	A	260	−2.9	−5.6	53.4	26
TYR	OH	A	260	−2.6	−5.5	54.7	32
TYR	C	A	260	−4.1	−5.2	46.9	35
TYR	O	A	260	−3.5	−6.1	46.3	34
ASN	N	A	261	−5.1	−4.6	46.5	35
ASN	CA	A	261	−5.7	−4.8	45.1	36
ASN	CB	A	261	−7.0	−5.6	45.2	38
ASN	CG	A	261	−6.9	−6.8	46.0	37
ASN	OD1	A	261	−6.8	−7.9	45.5	37
ASN	ND2	A	261	−7.1	−6.7	47.3	41
ASN	C	A	261	−5.8	−3.6	44.3	33
ASN	O	A	261	−6.5	−3.5	43.3	39
TYR	N	A	262	−5.1	−2.5	44.7	34
TYR	CA	A	262	−5.1	−1.3	43.9	37
TYR	CB	A	262	−4.9	−0.1	44.9	37
TYR	CG	A	262	−4.8	1.2	44.2	42
TYR	CD1	A	262	−5.9	1.8	43.5	43
TYR	CE1	A	262	−5.8	3.0	42.8	48
TYR	CD2	A	262	−3.6	2.0	44.2	47
TYR	CE2	A	262	−3.5	3.2	43.5	49
TYR	CZ	A	262	−4.6	3.7	42.9	51
TYR	OH	A	262	−4.5	4.9	42.2	55
TYR	C	A	262	−4.0	−1.3	42.8	38
TYR	O	A	262	−2.8	−1.2	43.1	39
ASP	N	A	263	−4.4	−1.3	41.6	38
ASP	CA	A	263	−5.8	−1.2	41.2	40
ASP	CB	A	263	−6.0	−0.2	40.1	45
ASP	CG	A	263	−5.2	−0.4	38.8	47
ASP	OD1	A	263	−4.4	−1.4	38.8	48
ASP	OD2	A	263	−5.3	0.3	37.9	49
ASP	C	A	263	−6.4	−2.6	40.7	37
ASP	O	A	263	−7.6	−2.7	40.3	38
LYS	N	A	264	−5.6	−3.6	40.9	34
LYS	CA	A	264	−6.0	−5.0	40.6	32
LYS	CB	A	264	−6.3	−5.2	39.1	31
LYS	CG	A	264	−5.0	−5.0	38.2	33
LYS	CD	A	264	−5.3	−5.1	36.7	34
LYS	CE	A	264	−4.0	−4.9	36.0	35
LYS	NZ	A	264	−3.5	−3.5	36.2	37
LYS	C	A	264	−4.9	−6.0	41.0	32
LYS	O	A	264	−3.8	−5.6	41.2	32
SER	N	A	265	−5.3	−7.2	41.2	27
SER	CA	A	265	−4.3	−8.2	41.6	28
SER	CB	A	265	−4.5	−8.8	43.0	25
SER	OG	A	265	−4.4	−7.8	44.0	25
SER	C	A	265	−4.5	−9.3	40.6	25
SER	O	A	265	−5.6	−9.8	40.3	25
ILE	N	A	266	−3.3	−9.7	40.0	25
ILE	CA	A	266	−3.3	−10.8	39.0	27
ILE	CB	A	266	−3.2	−10.2	37.5	26
ILE	CG2	A	266	−4.2	−9.1	37.3	24
ILE	CG1	A	266	−1.8	−9.6	37.4	23
ILE	CD1	A	266	−1.5	−9.0	36.0	25
ILE	C	A	266	−2.3	−11.8	39.1	27
ILE	O	A	266	−1.2	−11.6	39.8	27
VAL	N	A	267	−2.5	−13.0	38.6	25
VAL	CA	A	267	−1.5	−14.1	38.6	26
VAL	CB	A	267	−2.1	−15.5	38.9	25
VAL	CG1	A	267	−1.1	−16.6	38.9	28
VAL	CG2	A	267	−3.0	−15.5	40.2	24
VAL	C	A	267	−0.9	−14.0	37.3	28
VAL	O	A	267	−1.5	−14.2	36.2	28
ASP	N	A	268	0.4	−13.8	37.2	27
ASP	CA	A	268	1.1	−13.7	36.0	25
ASP	CB	A	268	1.4	−12.2	35.6	22
ASP	CG	A	268	2.1	−12.0	34.3	29
ASP	OD1	A	268	2.2	−13.0	33.5	25
ASP	OD2	A	268	2.6	−10.9	34.1	26
ASP	C	A	268	2.4	−14.5	35.9	24
ASP	O	A	268	3.4	−14.1	36.5	24
SER	N	A	269	2.5	−15.6	35.1	21
SER	CA	A	269	3.6	−16.4	34.9	18
SER	CB	A	269	3.3	−17.7	34.3	23
SER	OG	A	269	2.8	−17.5	33.0	28
SER	C	A	269	4.7	−15.7	34.1	22
SER	O	A	269	5.9	−16.1	34.1	22
GLY	N	A	270	4.4	−14.5	33.5	21
GLY	CA	A	270	5.3	−13.8	32.7	19
GLY	C	A	270	6.0	−12.7	33.5	26
GLY	O	A	270	6.7	−11.8	33.0	23
THR	N	A	271	5.8	−12.7	34.8	24
THR	CA	A	271	6.5	−11.8	35.8	24
THR	CB	A	271	5.5	−10.9	36.5	28
THR	OG1	A	271	4.7	−10.1	35.6	28
THR	CG2	A	271	6.2	−10.1	37.6	30
THR	C	A	271	7.4	−12.5	36.7	25
THR	O	A	271	7.0	−13.5	37.4	23
THR	N	A	272	8.6	−12.0	36.8	24
THR	CA	A	272	9.6	−12.6	37.7	25
THR	CB	A	272	11.0	−12.1	37.5	25
THR	OG1	A	272	11.4	−12.3	36.1	26
THR	CG2	A	272	12.1	−12.7	38.4	22
THR	C	A	272	9.3	−12.4	39.2	25
THR	O	A	272	9.1	−13.4	39.9	29
ASN	N	A	273	9.1	−11.2	39.5	22
ASN	CA	A	273	8.8	−10.8	40.9	25
ASN	CB	A	273	9.4	−9.4	41.2	26
ASN	CG	A	273	10.9	−9.3	41.0	29
ASN	OD1	A	273	11.5	−10.2	40.5	21
ASN	ND2	A	273	11.5	−8.1	41.4	31
ASN	C	A	273	7.4	−10.8	41.4	27
ASN	O	A	273	6.5	−11.1	40.7	27
LEU	N	A	274	7.3	−10.5	42.7	24
LEU	CA	A	274	6.0	−10.3	43.4	22
LEU	CB	A	274	6.1	−10.8	44.9	23
LEU	CG	A	274	4.8	−10.5	45.6	24
LEU	CD1	A	274	3.6	−11.1	45.0	26
LEU	CD2	A	274	4.9	−11.0	47.1	25
LEU	C	A	274	6.0	−8.8	43.3	23
LEU	O	A	274	6.7	−8.1	44.0	24
ARG	N	A	275	5.0	−8.3	42.5	25
ARG	CA	A	275	4.9	−6.9	42.4	24
ARG	CB	A	275	4.5	−6.5	40.9	29
ARG	CG	A	275	5.5	−7.0	39.9	34
ARG	CD	A	275	6.9	−6.4	39.9	36
ARG	NE	A	275	7.0	−5.0	39.8	33
ARG	CZ	A	275	7.0	−4.3	38.7	32
ARG	NH1	A	275	7.1	−3.0	38.6	31
ARG	NH2	A	275	6.9	−5.0	37.5	38
ARG	C	A	275	3.8	−6.4	43.4	23
ARG	O	A	275	2.7	−6.9	43.4	22
LEU	N	A	276	4.1	−5.4	44.2	22
LEU	CA	A	276	3.2	−4.8	45.2	23
LEU	CB	A	276	3.6	−5.1	46.6	23
LEU	CG	A	276	3.7	−6.5	47.0	24
LEU	CD1	A	276	4.3	−6.7	48.4	23
LEU	CD2	A	276	2.4	−7.2	46.9	25
LEU	C	A	276	2.9	−3.3	45.0	25
LEU	O	A	276	3.8	−2.5	44.7	23
PRO	N	A	277	1.6	−2.9	45.1	29
PRO	CD	A	277	0.4	−3.8	45.2	28
PRO	CA	A	277	1.2	−1.5	45.0	29
PRO	CB	A	277	−0.2	−1.6	45.5	27
PRO	CG	A	277	−0.7	−2.8	44.8	29
PRO	C	A	277	2.1	−0.7	45.9	31
PRO	O	A	277	2.4	−1.1	47.0	28
LYS	N	A	278	2.6	0.4	45.4	34
LYS	CA	A	278	3.5	1.3	46.1	38
LYS	CB	A	278	3.4	2.8	45.6	43
LYS	CG	A	278	4.3	3.7	46.3	44
LYS	CD	A	278	4.3	5.1	45.8	48
LYS	CE	A	278	5.2	6.1	46.6	50
LYS	NZ	A	278	5.1	7.5	46.1	53
LYS	C	A	278	3.3	1.4	47.6	39
LYS	O	A	278	4.3	1.3	48.4	37
LYS	N	A	279	2.1	1.5	48.1	36
LYS	CA	A	279	1.9	1.6	49.6	39
LYS	CB	A	279	0.5	2.2	49.9	42
LYS	CG	A	279	0.3	3.6	49.4	52
LYS	CD	A	279	−1.1	4.2	49.7	54
LYS	CE	A	279	−1.3	4.2	51.2	55
LYS	NZ	A	279	−2.6	4.7	51.6	56
LYS	C	A	279	2.0	0.2	50.3	39
LYS	O	A	279	2.4	0.2	51.5	38
VAL	N	A	280	1.8	−0.8	49.5	35
VAL	CA	A	280	1.9	−2.2	50.1	30
VAL	CB	A	280	1.0	−3.2	49.4	25
VAL	CG1	A	280	1.2	−4.5	50.0	22
VAL	CG2	A	280	−0.4	−2.7	49.4	22
VAL	C	A	280	3.4	−2.6	50.1	31
VAL	O	A	280	3.9	−3.2	51.0	34
PHE	N	A	281	4.1	−2.1	49.1	27
PHE	CA	A	281	5.5	−2.4	48.9	31
PHE	CB	A	281	6.1	−1.9	47.6	27
PHE	CG	A	281	7.6	−2.2	47.5	31
PHE	CD1	A	281	8.0	−3.5	47.2	29
PHE	CD2	A	281	8.5	−1.2	47.6	30
PHE	CE1	A	281	9.4	−3.7	47.1	30
PHE	CE2	A	281	9.8	−1.4	47.6	30
PHE	CZ	A	281	10.3	−2.7	47.3	29
PHE	C	A	281	6.3	−1.8	50.1	29
PHE	O	A	281	7.1	−2.4	50.8	29
GLU	N	A	282	6.1	−0.5	50.3	32
GLU	CA	A	282	6.8	0.2	51.3	35
GLU	CB	A	282	6.4	1.7	51.3	41
GLU	CG	A	282	6.8	2.5	50.0	47
GLU	CD	A	282	8.3	2.4	49.7	55
GLU	OE1	A	282	9.0	2.0	50.5	56
GLU	OE2	A	282	8.6	2.8	48.5	58
GLU	C	A	282	6.5	−0.4	52.7	33
GLU	O	A	282	7.4	−0.4	53.5	32
ALA	N	A	283	5.3	−0.8	53.0	32
ALA	CA	A	283	5.0	−1.4	54.3	29
ALA	CB	A	283	3.5	−1.4	54.5	30
ALA	C	A	283	5.5	−2.9	54.4	32
ALA	O	A	283	5.9	−3.3	55.5	34
ALA	N	A	284	5.5	−3.6	53.3	23
ALA	CA	A	284	5.9	−5.0	53.3	25
ALA	CB	A	284	5.6	−5.7	52.0	17
ALA	C	A	284	7.4	−5.0	53.5	27
ALA	O	A	284	8.0	−5.8	54.2	30
VAL	N	A	285	8.1	−4.1	52.8	27
VAL	CA	A	285	9.6	−4.0	52.9	30
VAL	CB	A	285	10.2	−3.1	51.8	34
VAL	CG1	A	285	11.7	−3.0	51.9	38
VAL	CG2	A	285	9.8	−3.6	50.4	33
VAL	C	A	285	10.0	−3.5	54.2	30
VAL	O	A	285	11.1	−3.8	54.7	30
LYS	N	A	286	9.2	−2.8	54.9	26
LYS	CA	A	286	9.5	−2.3	56.2	31
LYS	CB	A	286	8.6	−1.1	56.6	30
LYS	CG	A	286	8.8	−0.6	58.0	34
LYS	CD	A	286	7.9	0.6	58.3	37
LYS	CE	A	286	8.2	1.1	59.7	42
LYS	NZ	A	286	7.2	2.2	60.1	45
LYS	C	A	286	9.4	−3.4	57.2	30
LYS	O	A	286	10.2	−3.5	58.1	34
SER	N	A	287	8.4	−4.2	57.1	28
SER	CA	A	287	8.2	−5.4	58.0	27
SER	CB	A	287	6.8	−5.9	57.9	22
SER	OG	A	287	6.7	−7.0	58.8	28
SER	C	A	287	9.3	−6.4	57.7	25
SER	O	A	287	9.8	−7.1	58.6	22
ILE	N	A	288	9.7	−6.5	56.4	27
ILE	CA	A	288	10.7	−7.5	56.1	27
ILE	CB	A	288	10.7	−7.8	54.6	26
ILE	CG2	A	288	11.8	−8.8	54.2	23
ILE	CG1	A	288	9.4	−8.4	54.1	27
ILE	CD1	A	288	9.3	−8.7	52.7	24
ILE	C	A	288	12.1	−7.1	56.6	29
ILE	O	A	288	12.9	−8.0	56.9	30
LYS	N	A	289	12.3	−5.8	56.6	28
LYS	CA	A	289	13.6	−5.3	57.1	28
LYS	CB	A	289	13.9	−3.9	56.8	23
LYS	CG	A	289	14.1	−3.5	55.3	33
LYS	CD	A	289	14.4	−2.0	55.2	33
LYS	CE	A	289	14.6	−1.6	53.8	37
LYS	NZ	A	289	14.9	−0.1	53.7	35
LYS	C	A	289	13.7	−5.5	58.6	23
LYS	O	A	289	14.8	−5.8	59.2	30
ALA	N	A	290	12.6	−5.3	59.3	26
ALA	CA	A	290	12.6	−5.5	60.8	23
ALA	CB	A	290	11.3	−4.8	61.3	21
ALA	C	A	290	12.7	−6.9	61.2	24
ALA	O	A	290	13.2	−7.2	62.3	27
ALA	N	A	291	12.2	−7.8	60.4	25
ALA	CA	A	291	12.2	−9.2	60.8	25
ALA	CB	A	291	11.2	−10.0	60.0	22
ALA	C	A	291	13.6	−9.8	60.5	27
ALA	O	A	291	14.0	−10.8	61.1	28
SER	N	A	292	14.4	−9.2	59.6	29
SER	CA	A	292	15.7	−9.7	59.3	31
SER	CB	A	292	15.9	−9.8	57.7	34
SER	OG	A	292	15.7	−8.6	57.1	36
SER	C	A	292	16.8	−8.8	59.8	31
SER	O	A	292	17.9	−8.9	59.5	31
SER	N	A	293	16.4	−7.8	60.7	32
SER	CA	A	293	17.3	−6.9	61.3	38
SER	CB	A	293	16.6	−6.0	62.3	35
SER	OG	A	293	16.1	−6.7	63.4	35
SER	C	A	293	18.6	−7.4	61.8	42
SER	O	A	293	19.5	−6.6	62.2	44
THR	N	A	294	18.8	−8.7	62.0	45
THR	CA	A	294	20.0	−9.3	62.5	47
THR	CB	A	294	19.9	−10.8	62.9	47
THR	OG1	A	294	19.5	−11.6	61.8	51
THR	CG2	A	294	18.9	−11.0	64.1	49
THR	C	A	294	21.1	−9.1	61.6	48
THR	O	A	294	22.3	−9.2	61.9	51
GLU	N	A	295	20.8	−8.7	60.3	50
GLU	CA	A	295	21.8	−8.4	59.3	49
GLU	CB	A	295	22.1	−9.6	58.4	48
GLU	CG	A	295	22.7	−10.8	59.0	51
GLU	CD	A	295	23.0	−11.9	58.0	51
GLU	OE1	A	295	22.8	−11.6	56.8	47
GLU	OE2	A	295	23.3	−13.0	58.4	53
GLU	C	A	295	21.3	−7.2	58.5	50
GLU	O	A	295	20.1	−7.1	58.1	50
LYS	N	A	296	22.2	−6.3	58.3	53
LYS	CA	A	296	22.0	−5.1	57.5	52
LYS	CB	A	296	22.6	−3.8	58.1	55
LYS	CG	A	296	22.2	−3.6	59.5	58
LYS	CD	A	296	20.6	−3.4	59.5	58
LYS	CE	A	296	20.1	−3.1	60.9	59
LYS	NZ	A	296	20.4	−4.2	61.8	59
LYS	C	A	296	22.3	−5.3	56.0	48
LYS	O	A	296	23.4	−5.7	55.7	49
PHE	N	A	297	21.4	−4.9	55.2	46
PHE	CA	A	297	21.5	−5.0	53.7	47
PHE	CB	A	297	20.5	−5.9	53.1	46
PHE	CG	A	297	20.4	−7.3	53.7	47
PHE	CD1	A	297	19.6	−7.6	54.8	46
PHE	CD2	A	297	21.2	−8.3	53.2	49
PHE	CE1	A	297	19.6	−8.9	55.4	45
PHE	CE2	A	297	21.3	−9.6	53.8	49
PHE	CZ	A	297	20.4	−9.9	54.9	48
PHE	C	A	297	21.5	−3.7	53.0	48
PHE	O	A	297	20.6	−2.8	53.3	42
PRO	N	A	298	22.5	−3.4	52.1	51
PRO	CD	A	298	23.2	−4.5	51.3	51
PRO	CA	A	298	22.5	−2.2	51.4	52
PRO	CB	A	298	23.7	−2.4	50.4	50
PRO	CG	A	298	23.4	−3.7	49.9	52
PRO	C	A	298	21.2	−1.8	50.7	54
PRO	O	A	298	20.6	−2.7	50.0	55
ASP	N	A	299	20.8	−0.6	50.8	57
ASP	CA	A	299	19.5	−0.1	50.2	58
ASP	CB	A	299	19.5	1.5	50.3	63
ASP	CG	A	299	19.5	2.0	51.7	68
ASP	OD1	A	299	19.6	1.2	52.7	71
ASP	OD2	A	299	19.6	3.2	51.9	70
ASP	C	A	299	19.3	−0.5	48.8	58
ASP	O	A	299	18.1	−0.7	48.4	55
GLY	N	A	300	20.4	−0.8	48.1	55
GLY	CA	A	300	20.2	−1.2	46.7	52
GLY	C	A	300	19.6	−2.6	46.7	48
GLY	O	A	300	18.8	−2.9	45.8	45
PHE	N	A	301	19.9	−3.4	47.7	44
PHE	CA	A	301	19.3	−4.7	47.8	41
PHE	CB	A	301	19.8	−5.4	49.1	39
PHE	CG	A	301	19.2	−6.8	49.3	39
PHE	CD1	A	301	19.5	−7.9	48.5	38
PHE	CD2	A	301	18.3	−6.9	50.3	37
PHE	CE1	A	301	18.9	−9.1	48.7	39
PHE	CE2	A	301	17.6	−8.2	50.6	40
PHE	CZ	A	301	18.0	−9.3	49.8	38
PHE	C	A	301	17.8	−4.7	47.9	37
PHE	O	A	301	17.1	−5.4	47.1	37
TRP	N	A	302	17.3	−3.9	48.8	35
TRP	CA	A	302	15.8	−3.8	49.0	34
TRP	CB	A	302	15.5	−3.0	50.2	31
TRP	CG	A	302	16.0	−3.7	51.5	35
TRP	CD2	A	302	15.6	−4.9	52.1	35
TRP	CE2	A	302	16.4	−5.2	53.2	34
TRP	CE3	A	302	14.5	−5.8	51.8	34
TRP	CD1	A	302	17.1	−3.3	52.2	34
TRP	NE1	A	302	17.4	−4.2	53.2	32
TRP	CZ2	A	302	16.3	−6.3	54.0	36
TRP	CZ3	A	302	14.4	−6.9	52.6	33
TRP	CH2	A	302	15.2	−7.2	53.7	37
TRP	C	A	302	15.1	−3.2	47.7	36
TRP	O	A	302	13.9	−3.2	47.6	38
LEU	N	A	303	15.9	−2.6	46.8	37
LEU	CA	A	303	15.4	−2.1	45.6	39
LEU	CB	A	303	16.1	−0.8	45.1	40
LEU	CG	A	303	16.0	0.3	46.1	45
LEU	CD1	A	303	16.8	1.5	45.7	43
LEU	CD2	A	303	14.5	0.8	46.3	42
LEU	C	A	303	15.4	−3.1	44.5	40
LEU	O	A	303	14.9	−3.0	43.4	38
GLY	N	A	304	16.1	−4.2	44.8	38
GLY	CA	A	304	16.3	−5.3	43.9	45
GLY	C	A	304	17.3	−5.0	42.8	49
GLY	O	A	304	17.3	−5.6	41.7	50
GLU	N	A	305	18.2	−4.1	43.1	52
GLU	CA	A	305	19.3	−3.7	42.2	55
GLU	CB	A	305	19.4	−2.2	42.2	54
GLU	CG	A	305	18.2	−1.4	41.8	59
GLU	CD	A	305	18.4	0.1	41.9	62
GLU	OE1	A	305	18.2	0.7	40.9	67
GLU	OE2	A	305	18.8	0.6	42.9	62
GLU	C	A	305	20.6	−4.4	42.4	57
GLU	O	A	305	21.4	−4.5	41.5	58
GLN	N	A	306	20.9	−4.7	43.7	54
GLN	CA	A	306	22.1	−5.4	44.0	55
GLN	CB	A	306	23.1	−4.4	44.7	58
GLN	CG	A	306	22.6	−3.9	46.1	63
GLN	CD	A	306	23.7	−3.0	46.7	66
GLN	OE1	A	306	23.4	−1.8	46.9	64
GLN	NE2	A	306	24.8	−3.5	46.9	65
GLN	C	A	306	22.0	−6.7	44.8	54
GLN	O	A	306	21.2	−6.8	45.7	55
LEU	N	A	307	22.8	−7.7	44.3	53
LEU	CA	A	307	22.8	−9.0	44.9	55
LEU	CB	A	307	23.2	−10.1	43.9	59
LEU	CG	A	307	24.6	−9.8	43.4	60
LEU	CD1	A	307	25.7	−9.8	44.4	61
LEU	CD2	A	307	25.0	−10.9	42.3	62
LEU	C	A	307	23.5	−9.1	46.3	55
LEU	O	A	307	24.5	−8.4	46.5	58
VAL	N	A	308	23.0	−9.9	47.2	52
VAL	CA	A	308	23.6	−10.2	48.5	46
VAL	CB	A	308	22.6	−10.0	49.6	46
VAL	CG1	A	308	23.2	−10.4	51.0	46
VAL	CG2	A	308	22.2	−8.5	49.7	44
VAL	C	A	308	24.1	−11.6	48.4	48
VAL	O	A	308	23.5	−12.5	47.9	45
CYS	N	A	309	25.3	−11.9	49.0	48
CYS	CA	A	309	26.0	−13.2	48.9	46
CYS	C	A	309	26.3	−13.8	50.3	44
CYS	O	A	309	26.4	−13.1	51.3	42
CYS	CB	A	309	27.2	−13.1	48.1	46
CYS	SG	A	309	27.0	−12.4	46.4	49
TRP	N	A	310	26.4	−15.1	50.3	45
TRP	CA	A	310	26.7	−15.9	51.5	47
TRP	CB	A	310	25.5	−16.3	52.3	44
TRP	CG	A	310	24.7	−15.2	52.9	42
TRP	CD2	A	310	23.5	−14.7	52.5	41
TRP	CE2	A	310	23.1	−13.7	53.4	38
TRP	CE3	A	310	22.6	−14.9	51.4	40
TRP	CD1	A	310	25.1	−14.5	54.1	41
TRP	NE1	A	310	24.1	−13.6	54.4	38
TRP	CZ2	A	310	21.9	−12.9	53.3	38
TRP	CZ3	A	310	21.4	−14.2	51.3	39
TRP	CH2	A	310	21.1	−13.2	52.3	38
TRP	C	A	310	27.5	−17.2	51.1	50
TRP	O	A	310	27.3	−17.8	50.0	49
GLN	N	A	311	28.5	−17.5	51.9	52
GLN	CA	A	311	29.4	−18.7	51.6	55
GLN	CB	A	311	30.3	−19.0	52.8	59
GLN	CG	A	311	31.1	−20.3	52.7	68
GLN	CD	A	311	32.0	−20.2	51.5	73
GLN	OE1	A	311	32.1	−19.3	50.7	77
GLN	NE2	A	311	32.8	−21.3	51.3	73
GLN	C	A	311	28.5	−19.9	51.4	54
GLN	O	A	311	27.6	−20.3	52.2	58
ALA	N	A	312	28.6	−20.6	50.2	54
ALA	CA	A	312	27.9	−21.7	49.8	55
ALA	CB	A	312	28.7	−22.7	48.9	54
ALA	C	A	312	27.2	−22.5	50.9	53
ALA	O	A	312	27.9	−23.0	51.8	56
GLY	N	A	313	25.9	−22.5	50.9	51
GLY	CA	A	313	25.1	−23.3	52.0	43
GLY	C	A	313	24.9	−22.6	53.3	42
GLY	O	A	313	24.3	−23.1	54.2	45
THR	N	A	314	25.4	−21.3	53.5	39
THR	CA	A	314	25.2	−20.6	54.7	38
THR	CB	A	314	26.5	−20.0	55.2	42
THR	OG1	A	314	27.0	−19.0	54.2	41
THR	CG2	A	314	27.6	−21.0	55.5	42
THR	C	A	314	24.1	−19.6	54.7	35
THR	O	A	314	24.0	−18.7	55.6	33
THR	N	A	315	23.3	−19.6	53.6	34
THR	CA	A	315	22.2	−18.6	53.5	30
THR	CB	A	315	21.4	−18.8	52.2	33
THR	OG1	A	315	22.3	−18.8	51.1	33
THR	CG2	A	315	20.3	−17.8	52.1	29
THR	C	A	315	21.4	−18.7	54.7	27
THR	O	A	315	20.8	−19.7	55.0	28
PRO	N	A	316	21.3	−17.6	55.5	27
PRO	CD	A	316	21.8	−16.3	55.3	25
PRO	CA	A	316	20.5	−17.7	56.8	27
PRO	CB	A	316	21.1	−16.6	57.6	22
PRO	CG	A	316	21.1	−15.5	56.5	26
PRO	C	A	316	19.0	−17.5	56.5	27
PRO	O	A	316	18.4	−16.5	56.8	25
TRP	N	A	317	18.4	−18.6	55.9	25
TRP	CA	A	317	16.9	−18.5	55.6	25
TRP	CB	A	317	16.5	−19.9	55.0	23
TRP	CG	A	317	17.2	−20.3	53.8	20
TRP	CD2	A	317	17.1	−19.7	52.5	21
TRP	CE2	A	317	18.0	−20.5	51.7	25
TRP	CE3	A	317	16.4	−18.6	52.0	18
TRP	CD1	A	317	18.1	−21.4	53.7	22
TRP	NE1	A	317	18.6	−21.5	52.5	27
TRP	CZ2	A	317	18.2	−20.2	50.3	23
TRP	CZ3	A	317	16.6	−18.3	50.6	18
TRP	CH2	A	317	17.5	−19.1	49.8	23
TRP	C	A	317	16.1	−18.1	56.8	24
TRP	O	A	317	15.1	−17.3	56.6	24
ASN	N	A	318	16.4	−18.7	57.9	23
ASN	CA	A	318	15.6	−18.4	59.1	23
ASN	CB	A	318	16.0	−19.3	60.3	26
ASN	CG	A	318	17.4	−18.9	60.8	29
ASN	OD1	A	318	17.6	−18.3	61.8	32
ASN	ND2	A	318	18.4	−19.3	60.0	27
ASN	C	A	318	15.5	−17.0	59.6	24
ASN	O	A	318	14.6	−16.7	60.4	24
ILE	N	A	319	16.4	−16.1	59.2	26
ILE	CA	A	319	16.3	−14.8	59.7	27
ILE	CB	A	319	17.7	−14.1	59.8	26
ILE	CG2	A	319	18.7	−14.9	60.6	17
ILE	CG1	A	319	18.4	−13.8	58.5	28
ILE	CD1	A	319	17.7	−12.8	57.6	34
ILE	C	A	319	15.3	−14.0	58.8	26
ILE	O	A	319	14.9	−12.9	59.2	29
PHE	N	A	320	14.9	−14.5	57.7	25
PHE	CA	A	320	13.9	−14.0	56.8	26
PHE	CB	A	320	14.3	−14.2	55.3	25
PHE	CG	A	320	15.5	−13.5	54.9	30
PHE	CD1	A	320	15.5	−12.1	54.5	28
PHE	CD2	A	320	16.8	−14.1	54.9	29
PHE	CE1	A	320	16.6	−11.4	54.1	31
PHE	CE2	A	320	17.9	−13.5	54.5	29
PHE	CZ	A	320	17.9	−12.1	54.1	33
PHE	C	A	320	12.6	−14.5	57.2	20
PHE	O	A	320	12.4	−15.7	57.4	19
PRO	N	A	321	11.5	−13.6	57.2	21
PRO	CD	A	321	11.6	−12.2	56.8	18
PRO	CA	A	321	10.2	−14.0	57.4	21
PRO	CB	A	321	9.6	−12.7	57.9	18
PRO	CG	A	321	10.1	−11.8	56.8	20
PRO	C	A	321	9.4	−14.6	56.3	24
PRO	O	A	321	9.8	−14.5	55.1	23
VAL	N	A	322	8.4	−15.4	56.6	22
VAL	CA	A	322	7.5	−16.0	55.6	23
VAL	CB	A	322	6.8	−17.3	56.1	27
VAL	CG1	A	322	7.8	−18.4	56.5	25
VAL	CG2	A	322	5.9	−16.9	57.3	20
VAL	C	A	322	6.5	−15.0	55.2	25
VAL	O	A	322	6.2	−14.1	56.0	24
ILE	N	A	323	6.0	−15.0	54.0	23
ILE	CA	A	323	5.0	−14.1	53.5	20
ILE	CB	A	323	5.5	−13.3	52.3	20
ILE	CG2	A	323	4.4	−12.3	51.8	17
ILE	CG1	A	323	6.8	−12.5	52.6	15
ILE	CD1	A	323	7.4	−11.8	51.5	18
ILE	C	A	323	3.7	−14.8	53.2	23
ILE	O	A	323	3.6	−15.7	52.5	26
SER	N	A	324	2.6	−14.3	53.9	20
SER	CA	A	324	1.3	−14.9	53.7	22
SER	CB	A	324	0.7	−15.5	55.0	23
SER	OG	A	324	1.6	−16.5	55.5	28
SER	C	A	324	0.3	−14.0	53.0	25
SER	O	A	324	0.1	−12.9	53.4	26
LEU	N	A	325	−0.4	−14.6	52.0	25
LEU	CA	A	325	−1.4	−13.8	51.2	25
LEU	CB	A	325	−1.1	−13.7	49.8	28
LEU	CG	A	325	0.2	−13.0	49.4	30
LEU	CD1	A	325	0.4	−13.0	47.9	32
LEU	CD2	A	325	0.3	−11.6	49.9	31
LEU	C	A	325	−2.8	−14.5	51.4	26
LEU	O	A	325	−2.9	−15.7	51.1	27
TYR	N	A	326	−3.7	−13.8	52.0	29
TYR	CA	A	326	−5.1	−14.4	52.1	30
TYR	CB	A	326	−5.8	−13.9	53.4	30
TYR	CG	A	326	−5.2	−14.3	54.7	29
TYR	CD1	A	326	−3.9	−13.9	55.1	30
TYR	CE1	A	326	−3.4	−14.3	56.3	31
TYR	CD2	A	326	−5.9	−15.2	55.5	29
TYR	CE2	A	326	−5.3	−15.7	56.7	33
TYR	CZ	A	326	−4.1	−15.2	57.1	32
TYR	OH	A	326	−3.5	−15.6	58.3	32
TYR	C	A	326	−5.9	−14.1	50.9	31
TYR	O	A	326	−6.1	−12.9	50.5	27
LEU	N	A	327	−6.4	−15.1	50.3	30
LEU	CA	A	327	−7.2	−15.1	49.1	33
LEU	CB	A	327	−6.7	−16.0	48.0	28
LEU	CG	A	327	−5.2	−15.7	47.5	31
LEU	CD1	A	327	−4.7	−16.8	46.5	30
LEU	CD2	A	327	−5.1	−14.3	46.9	30
LEU	C	A	327	−8.6	−15.4	49.4	34
LEU	O	A	327	−8.9	−16.3	50.1	36
MET	N	A	328	−9.5	−14.6	48.8	37
MET	CA	A	328	−11.0	−14.8	48.9	37
MET	CB	A	328	−11.7	−13.8	48.0	41
MET	CG	A	328	−13.2	−13.9	48.1	47
MET	SD	A	328	−13.9	−12.6	47.0	55
MET	CE	A	328	−13.6	−11.1	47.9	50
MET	C	A	328	−11.3	−16.3	48.5	35
MET	O	A	328	−10.8	−16.7	47.4	32
GLY	N	A	329	−12.1	−17.0	49.2	32
GLY	CA	A	329	−12.5	−18.3	48.9	38
GLY	C	A	329	−13.8	−18.4	48.1	38
GLY	O	A	329	−14.4	−17.3	47.9	35
GLU	N	A	330	−14.2	−19.6	47.7	41
GLU	CA	A	330	−15.4	−19.7	46.9	45
GLU	CB	A	330	−15.5	−20.9	46.0	42
GLU	CG	A	330	−14.4	−21.0	45.0	43
GLU	CD	A	330	−14.6	−22.2	44.1	46
GLU	OE1	A	330	−13.9	−23.2	44.3	47
GLU	OE2	A	330	−15.5	−22.2	43.3	48
GLU	C	A	330	−16.7	−19.6	47.9	47
GLU	O	A	330	−17.8	−19.5	47.4	49
VAL	N	A	331	−16.4	−19.8	49.1	48
VAL	CA	A	331	−17.5	−19.8	50.1	46
VAL	CB	A	331	−17.3	−20.9	51.2	46
VAL	CG1	A	331	−18.4	−20.9	52.3	45
VAL	CG2	A	331	−17.2	−22.3	50.6	46
VAL	C	A	331	−17.6	−18.5	50.8	51
VAL	O	A	331	−16.6	−17.9	51.2	50
THR	N	A	332	−18.8	−17.9	50.8	53
THR	CA	A	332	−19.1	−16.6	51.4	54
THR	CB	A	332	−20.6	−16.4	51.5	57
THR	OG1	A	332	−21.2	−16.4	50.1	60
THR	CG2	A	332	−20.9	−15.0	52.1	56
THR	C	A	332	−18.5	−16.5	52.8	52
THR	O	A	332	−18.6	−17.3	53.6	53
ASN	N	A	333	−17.8	−15.3	53.0	51
ASN	CA	A	333	−17.1	−15.1	54.3	53
ASN	CB	A	333	−18.1	−15.0	55.4	58
ASN	CG	A	333	−19.1	−13.8	55.2	63
ASN	OD1	A	333	−19.0	−13.0	54.3	64
ASN	ND2	A	333	−20.1	−13.7	56.1	64
ASN	C	A	333	−16.0	−16.0	54.6	50
ASN	O	A	333	−15.5	−16.0	55.8	55
GLN	N	A	334	−15.6	−16.8	53.7	45
GLN	CA	A	334	−14.5	−17.8	53.9	41
GLN	CB	A	334	−15.0	−19.2	53.7	41
GLN	CG	A	334	−13.9	−20.3	53.9	44
GLN	CD	A	334	−14.6	−21.6	53.7	47
GLN	OE1	A	334	−14.1	−22.4	52.9	46
GLN	NE2	A	334	−15.6	−22.0	54.5	46
GLN	C	A	334	−13.2	−17.5	53.0	41
GLN	O	A	334	−13.4	−17.1	51.9	37
SER	N	A	335	−12.1	−17.6	53.6	40
SER	CA	A	335	−10.8	−17.4	52.9	38
SER	CB	A	335	−10.3	−15.9	53.1	40
SER	OG	A	335	−10.1	−15.7	54.5	43
SER	C	A	335	−9.7	−18.4	53.3	37
SER	O	A	335	−9.8	−19.1	54.2	38
PHE	N	A	336	−8.7	−18.4	52.4	32
PHE	CA	A	336	−7.5	−19.3	52.7	30
PHE	CB	A	336	−7.5	−20.5	51.8	27
PHE	CG	A	336	−7.4	−20.2	50.3	27
PHE	CD1	A	336	−6.2	−20.3	49.7	24
PHE	CD2	A	336	−8.5	−19.8	49.6	24
PHE	CE1	A	336	−6.1	−20.0	48.3	24
PHE	CE2	A	336	−8.4	−19.5	48.2	24
PHE	CZ	A	336	−7.2	−19.6	47.5	20
PHE	C	A	336	−6.3	−18.4	52.5	31
PHE	O	A	336	−6.3	−17.3	52.0	35
ARG	N	A	337	−5.1	−19.0	52.9	28
ARG	CA	A	337	−3.9	−18.2	52.8	27
ARG	CB	A	337	−3.4	−17.7	54.1	25
ARG	CG	A	337	−2.9	−18.8	55.1	31
ARG	CD	A	337	−2.4	−18.2	56.4	30
ARG	NE	A	337	−2.0	−19.3	57.3	30
ARG	CZ	A	337	−2.0	−19.3	58.6	32
ARG	NH1	A	337	−2.4	−18.2	59.3	28
ARG	NH2	A	337	−1.6	−20.4	59.3	32
ARG	C	A	337	−2.8	−19.0	52.1	24
ARG	O	A	337	−2.6	−20.2	52.4	22
ILE	N	A	338	−2.0	−18.3	51.3	23
ILE	CA	A	338	−0.8	−19.0	50.7	23
ILE	CB	A	338	−0.8	−18.9	49.2	21
ILE	CG2	A	338	−2.0	−19.6	48.6	23
ILE	CG1	A	338	−0.8	−17.4	48.7	20
ILE	CD1	A	338	−0.7	−17.2	47.2	23
ILE	C	A	338	0.4	−18.4	51.4	24
ILE	O	A	338	0.5	−17.2	51.5	24
THR	N	A	339	1.4	−19.2	51.7	21
THR	CA	A	339	2.6	−18.8	52.4	21
THR	CB	A	339	2.6	−19.3	53.9	21
THR	OG1	A	339	1.5	−18.8	54.6	21
THR	CG2	A	339	3.9	−18.8	54.6	14
THR	C	A	339	3.9	−19.2	51.7	22
THR	O	A	339	4.1	−20.3	51.4	22
ILE	N	A	340	4.7	−18.2	51.3	20
ILE	CA	A	340	5.9	−18.4	50.6	18
ILE	CB	A	340	6.2	−17.6	49.4	17
ILE	CG2	A	340	5.1	−18.0	48.3	20
ILE	CG1	A	340	6.2	−16.1	49.7	22
ILE	CD1	A	340	6.4	−15.2	48.5	18
ILE	C	A	340	7.1	−18.2	51.6	21
ILE	O	A	340	7.0	−17.6	52.6	21
LEU	N	A	341	8.2	−18.8	51.3	20
LEU	CA	A	341	9.4	−18.8	52.0	19
LEU	CB	A	341	10.1	−20.2	52.1	18
LEU	CG	A	341	9.2	−21.3	52.7	16
LEU	CD1	A	341	9.9	−22.6	52.5	10
LEU	CD2	A	341	8.8	−21.0	54.1	11
LEU	C	A	341	10.5	−17.8	51.4	26
LEU	O	A	341	10.3	−17.4	50.3	19
PRO	N	A	342	11.5	−17.4	52.2	27
PRO	CD	A	342	12.0	−17.8	53.5	24
PRO	CA	A	342	12.4	−16.6	51.6	23
PRO	CB	A	342	13.3	−16.1	52.7	30
PRO	CG	A	342	13.5	−17.4	53.4	28
PRO	C	A	342	13.1	−17.3	50.4	25
PRO	O	A	342	13.8	−16.7	49.6	28
GLN	N	A	343	12.9	−18.6	50.4	20
GLN	CA	A	343	13.5	−19.4	49.2	20
GLN	CB	A	343	13.5	−20.9	49.4	19
GLN	CG	A	343	14.4	−21.6	50.4	21
GLN	CD	A	343	14.1	−21.3	51.8	23
GLN	OE1	A	343	13.2	−20.5	52.1	23
GLN	NE2	A	343	14.7	−22.0	52.8	23
GLN	C	A	343	12.8	−19.0	47.9	22
GLN	O	A	343	13.3	−19.3	46.8	19
GLN	N	A	344	11.6	−18.5	48.1	22
GLN	CA	A	344	10.8	−18.0	46.9	23
GLN	CB	A	344	9.3	−18.3	46.9	20
GLN	CG	A	344	8.8	−19.8	46.9	24
GLN	CD	A	344	9.3	−20.6	48.0	23
GLN	OE1	A	344	10.1	−21.5	47.8	23
GLN	NE2	A	344	8.9	−20.3	49.2	15
GLN	C	A	344	11.0	−16.6	46.6	23
GLN	O	A	344	10.9	−16.2	45.4	24
TYR	N	A	345	11.2	−15.7	47.5	26
TYR	CA	A	345	11.4	−14.3	47.2	25
TYR	CB	A	345	10.6	−13.4	48.1	21
TYR	CG	A	345	10.8	−13.4	49.6	21
TYR	CD1	A	345	11.9	−12.7	50.1	25
TYR	CE1	A	345	12.1	−12.6	51.5	24
TYR	CD2	A	345	10.0	−14.0	50.5	23
TYR	CE2	A	345	10.2	−14.0	51.9	23
TYR	CZ	A	345	11.3	−13.2	52.4	26
TYR	OH	A	345	11.4	−13.1	53.7	23
TYR	C	A	345	12.8	−13.8	47.1	25
TYR	O	A	345	13.1	−12.7	46.7	26
LEU	N	A	346	13.8	−14.7	47.4	22
LEU	CA	A	346	15.2	−14.3	47.2	26
LEU	CB	A	346	16.1	−14.7	48.4	23
LEU	CG	A	346	15.7	−13.9	49.7	28
LEU	CD1	A	346	16.6	−14.3	50.8	26
LEU	CD2	A	346	15.8	−12.4	49.5	28
LEU	C	A	346	15.6	−15.1	45.9	24
LEU	O	A	346	15.9	−16.3	46.0	27
ARG	N	A	347	15.6	−14.4	44.8	26
ARG	CA	A	347	16.0	−15.1	43.6	27
ARG	CB	A	347	15.3	−14.4	42.4	24
ARG	CG	A	347	15.6	−15.0	41.0	26
ARG	CD	A	347	14.9	−14.3	39.9	30
ARG	NE	A	347	15.3	−12.9	39.7	32
ARG	CZ	A	347	16.3	−12.6	39.0	28
ARG	NH1	A	347	17.1	−13.5	38.4	23
ARG	NH2	A	347	16.6	−11.3	38.9	28
ARG	C	A	347	17.5	−15.2	43.4	28
ARG	O	A	347	18.2	−14.3	43.4	23
PRO	N	A	348	17.9	−16.5	43.2	33
PRO	CD	A	348	17.1	−17.7	43.0	33
PRO	CA	A	348	19.3	−16.8	43.0	35
PRO	CB	A	348	19.4	−18.3	43.3	35
PRO	CG	A	348	18.2	−18.7	42.5	37
PRO	C	A	348	19.9	−16.4	41.7	37
PRO	O	A	348	19.3	−16.6	40.6	40
VAL	N	A	349	21.0	−15.7	41.7	39
VAL	CA	A	349	21.7	−15.2	40.5	44
VAL	CB	A	349	21.7	−13.7	40.5	43
VAL	CG1	A	349	20.3	−13.2	40.4	41
VAL	CG2	A	349	22.4	−13.1	41.6	42
VAL	C	A	349	23.1	−15.7	40.4	44
VAL	O	A	349	23.9	−15.6	41.4	47
SER	N	A	355	31.4	−23.5	43.2	90
SER	CA	A	355	30.6	−22.3	42.8	90
SER	CB	A	355	29.1	−22.6	42.6	91
SER	OG	A	355	28.5	−23.1	43.8	92
SER	C	A	355	30.8	−21.2	43.8	89
SER	O	A	355	30.2	−20.1	43.6	91
GLN	N	A	356	31.7	−21.3	44.8	84
GLN	CA	A	356	32.0	−20.3	45.8	78
GLN	CB	A	356	32.8	−19.1	45.2	77
GLN	CG	A	356	32.1	−18.3	44.1	77
GLN	CD	A	356	32.9	−17.2	43.7	77
GLN	OE1	A	356	33.3	−17.1	42.5	80
GLN	NE2	A	356	33.2	−16.3	44.6	77
GLN	C	A	356	30.8	−19.8	46.7	74
GLN	O	A	356	30.4	−20.5	47.5	74
ASP	N	A	357	30.4	−18.6	46.4	69
ASP	CA	A	357	29.3	−17.9	47.1	65
ASP	CB	A	357	29.7	−16.5	47.4	66
ASP	CG	A	357	31.0	−16.3	48.2	69
ASP	OD1	A	357	30.9	−15.7	49.3	66
ASP	OD2	A	357	32.0	−16.8	47.8	74
ASP	C	A	357	27.9	−18.0	46.5	61
ASP	O	A	357	27.8	−17.9	45.3	62
ASP	N	A	358	26.9	−18.1	47.3	55
ASP	CA	A	358	25.5	−18.1	46.9	50
ASP	CB	A	358	24.6	−19.0	47.7	51
ASP	CG	A	358	25.1	−20.5	47.6	52
ASP	OD1	A	358	25.3	−21.1	48.7	53
ASP	OD2	A	358	25.2	−21.0	46.5	54
ASP	C	A	358	25.0	−16.7	46.9	44
ASP	O	A	358	25.0	−16.1	48.0	40
CYS	N	A	359	24.6	−16.1	45.8	42
CYS	CA	A	359	24.1	−14.8	45.8	41
CYS	C	A	359	22.6	−14.7	45.4	37
CYS	O	A	359	22.1	−15.5	44.7	31
CYS	CB	A	359	24.9	−14.0	44.8	44
CYS	SG	A	359	26.7	−14.0	45.1	46
TYR	N	A	360	21.9	−13.7	46.0	37
TYR	CA	A	360	20.5	−13.5	45.7	34
TYR	CB	A	360	19.7	−14.1	46.9	33
TYR	CG	A	360	20.0	−15.5	47.3	32
TYR	CD1	A	360	21.1	−15.8	48.2	33
TYR	CE1	A	360	21.5	−17.0	48.5	29
TYR	CD2	A	360	19.3	−16.6	46.9	27
TYR	CE2	A	360	19.6	−17.9	47.2	27
TYR	CZ	A	360	20.7	−18.1	48.1	30
TYR	OH	A	360	21.1	−19.4	48.5	37
TYR	C	A	360	20.0	−12.1	45.5	35
TYR	O	A	360	20.6	−11.2	46.1	33
LYS	N	A	361	19.0	−11.9	44.7	30
LYS	CA	A	361	18.4	−10.6	44.5	33
LYS	CB	A	361	18.3	−10.1	43.1	33
LYS	CG	A	361	19.6	−9.8	42.4	39
LYS	CD	A	361	19.2	−9.2	41.0	41
LYS	CE	A	361	20.5	−8.9	40.2	41
LYS	NZ	A	361	20.1	−8.3	38.9	41
LYS	C	A	361	17.0	−10.6	45.2	32
LYS	O	A	361	16.3	−11.6	45.1	30
PHE	N	A	362	16.6	−9.5	45.8	28
PHE	CA	A	362	15.3	−9.4	46.5	25
PHE	CB	A	362	15.3	−8.1	47.3	25
PHE	CG	A	362	14.0	−7.8	48.1	26
PHE	CD1	A	362	13.6	−8.7	49.1	23
PHE	CD2	A	362	13.3	−6.7	47.8	26
PHE	CE1	A	362	12.4	−8.5	49.8	24
PHE	CE2	A	362	12.1	−6.4	48.5	25
PHE	CZ	A	362	11.7	−7.3	49.5	24
PHE	C	A	362	14.3	−9.3	45.3	28
PHE	O	A	362	14.3	−8.4	44.5	25
ALA	N	A	363	13.5	−10.3	45.2	27
ALA	CA	A	363	12.5	−10.4	44.1	27
ALA	CB	A	363	12.4	−11.8	43.6	29
ALA	C	A	363	11.1	−9.8	44.4	25
ALA	O	A	363	10.1	−10.3	43.8	22
ILE	N	A	364	11.0	−8.9	45.3	26
ILE	CA	A	364	9.8	−8.2	45.6	25
ILE	CB	A	364	9.4	−8.4	47.1	24
ILE	CG2	A	364	8.0	−7.6	47.3	21
ILE	CG1	A	364	9.2	−9.8	47.5	22
ILE	CD1	A	364	8.8	−10.1	48.9	23
ILE	C	A	364	9.9	−6.8	45.2	25
ILE	O	A	364	10.9	−6.1	45.6	30
SER	N	A	365	9.1	−6.3	44.3	26
SER	CA	A	365	9.2	−4.9	43.9	30
SER	CB	A	365	10.0	−4.9	42.5	32
SER	OG	A	365	9.3	−5.6	41.5	35
SER	C	A	365	7.9	−4.1	43.8	33
SER	O	A	365	6.8	−4.6	43.7	32
GLN	N	A	366	8.1	−2.8	43.8	35
GLN	CA	A	366	7.1	−1.8	43.7	36
GLN	CB	A	366	7.7	−0.4	43.9	38
GLN	CG	A	366	6.7	0.7	43.9	46
GLN	CD	A	366	7.5	2.0	44.2	50
GLN	OE1	A	366	7.3	2.6	45.2	53
GLN	NE2	A	366	8.4	2.3	43.3	55
GLN	C	A	366	6.3	−1.9	42.3	36
GLN	O	A	366	7.0	−2.0	41.3	33
SER	N	A	367	5.0	−1.7	42.4	34
SER	CA	A	367	4.2	−1.7	41.2	34
SER	CB	A	367	3.4	−3.0	41.1	35
SER	OG	A	367	2.5	−2.9	40.0	30
SER	C	A	367	3.2	−0.5	41.2	37
SER	O	A	367	2.7	−0.1	42.2	34
SER	N	A	368	3.0	0.1	40.0	33
SER	CA	A	368	2.1	1.2	39.8	35
SER	CB	A	368	2.8	2.4	39.1	33
SER	OG	A	368	3.2	2.0	37.8	36
SER	C	A	368	0.9	0.8	39.1	33
SER	O	A	368	0.0	1.6	38.9	39
THR	N	A	369	0.8	−0.5	38.8	33
THR	CA	A	369	−0.3	−1.1	38.1	32
THR	CB	A	369	0.0	−1.6	36.7	35
THR	OG1	A	369	1.0	−2.6	36.8	34
THR	CG2	A	369	0.5	−0.4	35.8	35
THR	C	A	369	−1.1	−2.2	38.9	34
THR	O	A	369	−1.8	−3.0	38.4	31
GLY	N	A	370	−0.8	−2.3	40.2	28
GLY	CA	A	370	−1.4	−3.2	41.1	30
GLY	C	A	370	−0.5	−4.4	41.4	29
GLY	O	A	370	0.6	−4.4	41.1	28
THR	N	A	371	−1.1	−5.4	42.2	29
THR	CA	A	371	−0.4	−6.5	42.6	27
THR	CB	A	371	−1.1	−7.3	43.8	28
THR	OG1	A	371	−1.1	−6.4	44.9	27
THR	CG2	A	371	−0.4	−8.6	44.1	24
THR	C	A	371	−0.1	−7.5	41.5	26
THR	O	A	371	−1.0	−7.9	40.7	30
VAL	N	A	372	1.1	−8.0	41.4	27
VAL	CA	A	372	1.4	−9.0	40.4	26
VAL	CB	A	372	2.4	−8.5	39.3	27
VAL	CG1	A	372	2.6	−9.6	38.2	24
VAL	CG2	A	372	1.9	−7.2	38.7	25
VAL	C	A	372	2.0	−10.3	41.1	27
VAL	O	A	372	3.1	−10.2	41.6	25
MET	N	A	373	1.3	−11.4	41.0	23
MET	CA	A	373	1.8	−12.6	41.6	24
MET	CB	A	373	0.6	−13.4	42.1	23
MET	CG	A	373	−0.3	−12.7	43.2	27
MET	SD	A	373	−1.7	−13.6	43.9	30
MET	CE	A	373	−0.9	−15.2	44.3	30
MET	C	A	373	2.5	−13.3	40.5	24
MET	O	A	373	2.0	−14.0	39.7	29
GLY	N	A	374	3.8	−13.1	40.5	25
GLY	CA	A	374	4.7	−13.7	39.5	23
GLY	C	A	374	5.3	−15.0	39.9	24
GLY	O	A	374	4.9	−15.7	40.8	19
ALA	N	A	375	6.4	−15.3	39.2	24
ALA	CA	A	375	7.2	−16.5	39.5	25
ALA	CB	A	375	8.5	−16.5	38.6	26
ALA	C	A	375	7.5	−16.6	41.0	27
ALA	O	A	375	7.6	−17.7	41.5	31
VAL	N	A	376	7.7	−15.5	41.6	28
VAL	CA	A	376	8.0	−15.6	43.1	28
VAL	CB	A	376	8.3	−14.2	43.7	26
VAL	CG1	A	376	8.4	−14.2	45.2	27
VAL	CG2	A	376	9.5	−13.5	43.1	26
VAL	C	A	376	7.0	−16.3	43.8	27
VAL	O	A	376	7.3	−17.2	44.6	36
ILE	N	A	377	5.7	−16.0	43.5	25
ILE	CA	A	377	4.6	−16.7	44.2	24
ILE	CB	A	377	3.3	−15.9	44.2	24
ILE	CG2	A	377	2.1	−16.7	44.7	22
ILE	CG1	A	377	3.4	−14.6	44.9	28
ILE	CD1	A	377	3.8	−14.8	46.4	31
ILE	C	A	377	4.3	−18.1	43.6	24
ILE	O	A	377	4.1	−19.0	44.3	24
MET	N	A	378	4.4	−18.1	42.2	22
MET	CA	A	378	4.1	−19.4	41.6	25
MET	CB	A	378	3.9	−19.2	40.1	23
MET	CG	A	378	2.7	−18.3	39.8	23
MET	SD	A	378	2.4	−18.0	38.0	29
MET	CE	A	378	1.6	−19.6	37.6	18
MET	C	A	378	5.1	−20.5	41.8	26
MET	O	A	378	4.7	−21.7	41.7	31
GLU	N	A	379	6.4	−20.2	42.0	25
GLU	CA	A	379	7.4	−21.3	42.2	28
GLU	CB	A	379	8.8	−20.7	42.1	26
GLU	CG	A	379	9.1	−20.1	40.7	29
GLU	CD	A	379	10.5	−19.6	40.7	30
GLU	OE1	A	379	11.1	−19.6	39.6	30
GLU	OE2	A	379	11.1	−19.3	41.7	35
GLU	C	A	379	7.2	−22.1	43.5	26
GLU	O	A	379	7.9	−23.0	43.8	28
GLY	N	A	380	6.2	−21.7	44.3	24
GLY	CA	A	380	6.0	−22.4	45.5	30
GLY	C	A	380	4.7	−23.1	45.5	26
GLY	O	A	380	4.3	−23.9	46.5	24
PHE	N	A	381	3.9	−23.0	44.5	28
PHE	CA	A	381	2.6	−23.6	44.4	27
PHE	CB	A	381	1.5	−22.5	44.7	25
PHE	CG	A	381	1.7	−21.9	46.1	27
PHE	CD1	A	381	2.2	−20.6	46.1	26
PHE	CD2	A	381	1.5	−22.6	47.3	26
PHE	CE1	A	381	2.5	−19.9	47.3	27
PHE	CE2	A	381	1.8	−21.9	48.5	28
PHE	CZ	A	381	2.3	−20.6	48.5	27
PHE	C	A	381	2.2	−24.2	43.1	28
PHE	O	A	381	2.6	−23.7	42.0	25
TYR	N	A	382	1.4	−25.3	43.1	28
TYR	CA	A	382	0.9	−25.9	41.9	26
TYR	CB	A	382	0.5	−27.3	42.1	25
TYR	CG	A	382	0.0	−28.0	40.9	29
TYR	CD1	A	382	0.7	−27.9	39.7	30
TYR	CE1	A	382	0.2	−28.6	38.5	30
TYR	CD2	A	382	−1.2	−28.7	40.9	28
TYR	CE2	A	382	−1.7	−29.3	39.8	24
TYR	CZ	A	382	−1.0	−29.3	38.6	29
TYR	OH	A	382	−1.5	−29.9	37.5	27
TYR	C	A	382	−0.3	−25.0	41.7	23
TYR	O	A	382	−1.2	−24.9	42.5	23
VAL	N	A	383	−0.3	−24.3	40.5	20
VAL	CA	A	383	−1.4	−23.4	40.2	22
VAL	CB	A	383	−0.9	−22.0	39.9	22
VAL	CG1	A	383	−2.0	−21.0	39.7	20
VAL	CG2	A	383	0.0	−21.5	41.0	19
VAL	C	A	383	−2.4	−23.8	39.2	27
VAL	O	A	383	−2.0	−24.2	38.0	28
VAL	N	A	384	−3.7	−23.9	39.5	25
VAL	CA	A	384	−4.7	−24.4	38.6	25
VAL	CB	A	384	−5.6	−25.5	39.2	25
VAL	CG1	A	384	−6.6	−26.0	38.2	24
VAL	CG2	A	384	−4.7	−26.6	39.8	22
VAL	C	A	384	−5.6	−23.3	38.0	26
VAL	O	A	384	−6.4	−22.7	38.7	29
PHE	N	A	385	−5.4	−23.0	36.7	25
PHE	CA	A	385	−6.3	−22.0	36.1	28
PHE	CB	A	385	−5.5	−21.3	34.9	26
PHE	CG	A	385	−4.3	−20.6	35.4	28
PHE	CD1	A	385	−4.4	−19.2	35.6	25
PHE	CD2	A	385	−3.2	−21.2	35.7	24
PHE	CE1	A	385	−3.3	−18.5	36.0	26
PHE	CE2	A	385	−2.0	−20.5	36.2	25
PHE	CZ	A	385	−2.1	−19.1	36.4	24
PHE	C	A	385	−7.5	−22.8	35.6	31
PHE	O	A	385	−7.5	−23.3	34.5	31
ASP	N	A	386	−8.5	−22.8	36.4	30
ASP	CA	A	386	−9.8	−23.5	36.1	32
ASP	CB	A	386	−10.4	−24.1	37.4	36
ASP	CG	A	386	−11.6	−24.9	37.1	37
ASP	OD1	A	386	−12.1	−24.9	36.0	41
ASP	OD2	A	386	−12.1	−25.5	38.1	39
ASP	C	A	386	−10.7	−22.5	35.4	30
ASP	O	A	386	−11.5	−21.8	36.1	29
ARG	N	A	387	−10.5	−22.4	34.1	30
ARG	CA	A	387	−11.3	−21.5	33.3	33
ARG	CB	A	387	−10.7	−21.5	31.9	35
ARG	CG	A	387	−9.3	−20.9	31.8	34
ARG	CD	A	387	−8.7	−21.0	30.4	37
ARG	NE	A	387	−9.5	−20.3	29.4	41
ARG	CZ	A	387	−9.0	−19.4	28.6	43
ARG	NH1	A	387	−7.7	−19.0	28.7	44
ARG	NH2	A	387	−9.8	−18.9	27.6	47
ARG	C	A	387	−12.8	−21.8	33.2	33
ARG	O	A	387	−13.6	−21.0	33.1	35
ALA	N	A	388	−13.0	−23.1	33.3	34
ALA	CA	A	388	−14.4	−23.6	33.2	38
ALA	CB	A	388	−14.4	−25.1	32.9	36
ALA	C	A	388	−15.2	−23.4	34.5	39
ALA	O	A	388	−16.4	−23.5	34.4	40
ARG	N	A	389	−14.5	−23.0	35.5	38
ARG	CA	A	389	−15.2	−22.7	36.8	38
ARG	CB	A	389	−15.0	−23.8	37.8	38
ARG	CG	A	389	−15.4	−25.2	37.3	37
ARG	CD	A	389	−15.3	−26.3	38.3	38
ARG	NE	A	389	−16.0	−26.0	39.5	46
ARG	CZ	A	389	−16.3	−27.0	40.4	46
ARG	NH1	A	389	−15.8	−28.2	40.3	42
ARG	NH2	A	389	−17.0	−26.6	41.5	47
ARG	C	A	389	−14.9	−21.3	37.3	37
ARG	O	A	389	−15.3	−20.9	38.4	39
LYS	N	A	390	−14.2	−20.6	36.5	36
LYS	CA	A	390	−13.8	−19.2	36.8	42
LYS	CB	A	390	−15.1	−18.3	36.5	43
LYS	CG	A	390	−14.9	−16.8	36.7	49
LYS	CD	A	390	−16.2	−16.1	36.4	51
LYS	CE	A	390	−16.1	−14.6	36.6	54
LYS	NZ	A	390	−17.4	−13.8	36.3	51
LYS	C	A	390	−13.2	−19.1	38.2	39
LYS	O	A	390	−13.6	−18.2	39.0	41
ARG	N	A	391	−12.3	−19.9	38.4	33
ARG	CA	A	391	−11.6	−20.0	39.7	31
ARG	CB	A	391	−12.3	−20.9	40.7	26
ARG	CG	A	391	−12.3	−22.4	40.2	27
ARG	CD	A	391	−13.0	−23.3	41.2	24
ARG	NE	A	391	−12.9	−24.7	40.7	23
ARG	CZ	A	391	−13.1	−25.8	41.4	26
ARG	NH1	A	391	−13.4	−25.6	42.7	26
ARG	NH2	A	391	−13.0	−27.0	40.9	23
ARG	C	A	391	−10.1	−20.4	39.5	34
ARG	O	A	391	−9.8	−21.1	38.6	31
ILE	N	A	392	−9.2	−20.0	40.4	35
ILE	CA	A	392	−7.8	−20.3	40.4	31
ILE	CB	A	392	−6.9	−19.1	40.2	31
ILE	CG2	A	392	−5.4	−19.5	40.4	32
ILE	CG1	A	392	−7.2	−18.4	38.9	30
ILE	CD1	A	392	−6.3	−17.2	38.6	33
ILE	C	A	392	−7.5	−21.1	41.6	33
ILE	O	A	392	−7.7	−20.6	42.8	36
GLY	N	A	393	−6.9	−22.3	41.4	29
GLY	CA	A	393	−6.5	−23.1	42.6	24
GLY	C	A	393	−5.1	−23.1	42.9	29
GLY	O	A	393	−4.2	−23.0	42.1	33
PHE	N	A	394	−4.8	−23.2	44.2	27
PHE	CA	A	394	−3.4	−23.2	44.8	27
PHE	CB	A	394	−3.1	−22.0	45.6	23
PHE	CG	A	394	−3.2	−20.7	44.8	23
PHE	CD1	A	394	−4.4	−20.1	44.4	24
PHE	CD2	A	394	−2.0	−20.1	44.5	22
PHE	CE1	A	394	−4.4	−18.9	43.7	19
PHE	CE2	A	394	−2.0	−18.8	43.8	22
PHE	CZ	A	394	−3.2	−18.3	43.4	20
PHE	C	A	394	−3.2	−24.5	45.7	27
PHE	O	A	394	−4.1	−24.9	46.4	27
ALA	N	A	395	−2.0	−25.0	45.6	28
ALA	CA	A	395	−1.6	−26.2	46.4	28
ALA	CB	A	395	−2.1	−27.5	45.8	26
ALA	C	A	395	−0.1	−26.2	46.6	32
ALA	O	A	395	0.6	−25.7	45.7	31
VAL	N	A	396	0.3	−26.7	47.7	30
VAL	CA	A	396	1.8	−26.8	47.9	29
VAL	CB	A	396	2.1	−27.4	49.3	31
VAL	CG1	A	396	3.6	−27.5	49.5	29
VAL	CG2	A	396	1.5	−26.7	50.4	29
VAL	C	A	396	2.5	−27.5	46.8	29
VAL	O	A	396	2.1	−28.6	46.5	26
SER	N	A	397	3.4	−26.8	46.1	33
SER	CA	A	397	4.1	−27.4	45.0	28
SER	CB	A	397	4.9	−26.3	44.3	27
SER	OG	A	397	5.6	−26.9	43.2	23
SER	C	A	397	5.1	−28.5	45.5	30
SER	O	A	397	5.8	−28.3	46.4	26
ALA	N	A	398	5.0	−29.6	44.8	30
ALA	CA	A	398	5.9	−30.7	45.1	31
ALA	CB	A	398	5.5	−32.0	44.3	29
ALA	C	A	398	7.4	−30.4	44.8	33
ALA	O	A	398	8.3	−31.1	45.2	34
CYS	N	A	399	7.6	−29.3	44.0	31
CYS	CA	A	399	9.0	−28.9	43.7	33
CYS	C	A	399	9.5	−27.6	44.3	34
CYS	O	A	399	10.5	−27.1	44.0	32
CYS	CB	A	399	9.2	−28.9	42.2	35
CYS	SG	A	399	8.3	−27.6	41.2	38
HIS	N	A	400	8.7	−27.0	45.2	33
HIS	CA	A	400	9.1	−25.7	45.7	31
HIS	CB	A	400	8.0	−25.0	46.6	32
HIS	CG	A	400	7.7	−25.6	47.9	31
HIS	CD2	A	400	7.9	−25.2	49.1	29
HIS	ND1	A	400	7.1	−26.9	48.0	30
HIS	CE1	A	400	7.0	−27.1	49.3	32
HIS	NE2	A	400	7.5	−26.1	50.0	29
HIS	C	A	400	10.3	−25.9	46.6	29
HIS	O	A	400	10.5	−26.9	47.2	26
VAL	N	A	401	11.2	−24.9	46.5	27
VAL	CA	A	401	12.4	−24.9	47.3	27
VAL	CB	A	401	13.5	−24.0	46.7	24
VAL	CG1	A	401	14.7	−24.0	47.6	27
VAL	CG2	A	401	13.8	−24.3	45.3	25
VAL	C	A	401	12.1	−24.6	48.8	27
VAL	O	A	401	11.4	−23.6	49.1	28
HIS	N	A	402	12.7	−25.4	49.7	28
HIS	CA	A	402	12.5	−25.1	51.1	29
HIS	CB	A	402	11.2	−25.6	51.6	32
HIS	CG	A	402	11.0	−27.1	51.5	36
HIS	CD2	A	402	11.1	−28.1	52.4	37
HIS	ND1	A	402	10.6	−27.7	50.3	38
HIS	CE1	A	402	10.5	−29.0	50.5	36
HIS	NE2	A	402	10.8	−29.2	51.8	40
HIS	C	A	402	13.7	−25.7	51.9	27
HIS	O	A	402	14.6	−26.2	51.3	31
ASP	N	A	403	13.5	−25.7	53.2	29
ASP	CA	A	403	14.6	−26.2	54.1	28
ASP	CB	A	403	15.3	−25.2	54.8	29
ASP	CG	A	403	14.4	−24.3	55.7	32
ASP	OD1	A	403	13.6	−24.8	56.4	32
ASP	OD2	A	403	14.6	−23.1	55.7	35
ASP	C	A	403	13.9	−27.2	55.0	28
ASP	O	A	403	12.8	−27.6	54.8	27
GLU	N	A	404	14.6	−27.7	56.0	30
GLU	CA	A	404	14.1	−28.7	56.9	33
GLU	CB	A	404	15.1	−29.6	57.5	39
GLU	CG	A	404	16.3	−29.1	58.4	45
GLU	CD	A	404	17.2	−28.1	57.6	50
GLU	OE1	A	404	17.0	−27.8	56.4	51
GLU	OE2	A	404	18.3	−27.8	58.2	48
GLU	C	A	404	13.2	−28.1	58.0	33
GLU	O	A	404	12.5	−28.9	58.7	33
PHE	N	A	405	13.1	−26.8	58.2	28
PHE	CA	A	405	12.3	−26.2	59.2	25
PHE	CB	A	405	13.2	−25.2	60.0	26
PHE	CG	A	405	14.4	−25.8	60.6	30
PHE	CD1	A	405	15.6	−25.6	60.0	30
PHE	CD2	A	405	14.3	−26.7	61.7	29
PHE	CE1	A	405	16.8	−26.3	60.5	32
PHE	CE2	A	405	15.4	−27.3	62.2	32
PHE	CZ	A	405	16.7	−27.1	61.6	30
PHE	C	A	405	11.0	−25.5	58.8	27
PHE	O	A	405	10.1	−25.4	59.5	29
ARG	N	A	406	11.0	−25.1	57.5	25
ARG	CA	A	406	9.8	−24.4	56.9	24
ARG	CB	A	406	9.9	−22.9	57.0	23
ARG	CG	A	406	10.0	−22.3	58.4	24
ARG	CD	A	406	10.0	−20.8	58.3	23
ARG	NE	A	406	11.1	−20.2	57.5	24
ARG	CZ	A	406	11.4	−18.9	57.6	27
ARG	NH1	A	406	10.9	−18.1	58.5	22
ARG	NH2	A	406	12.4	−18.4	56.8	24
ARG	C	A	406	9.5	−24.8	55.5	30
ARG	O	A	406	10.4	−25.1	54.7	29
THR	N	A	407	8.2	−24.9	55.2	28
THR	CA	A	407	7.7	−25.3	53.9	28
THR	CB	A	407	7.2	−26.7	53.9	27
THR	OG1	A	407	6.6	−27.0	52.6	36
THR	CG2	A	407	6.1	−26.8	55.0	29
THR	C	A	407	6.6	−24.3	53.5	29
THR	O	A	407	5.9	−23.7	54.3	28
ALA	N	A	408	6.5	−24.1	52.2	26
ALA	CA	A	408	5.4	−23.2	51.7	28
ALA	CB	A	408	5.5	−23.1	50.1	26
ALA	C	A	408	4.1	−23.9	52.1	27
ALA	O	A	408	4.1	−25.1	52.2	29
ALA	N	A	409	3.1	−23.1	52.3	26
ALA	CA	A	409	1.8	−23.6	52.7	23
ALA	CB	A	409	1.7	−23.5	54.2	23
ALA	C	A	409	0.6	−23.0	52.1	27
ALA	O	A	409	0.6	−21.8	51.6	21
VAL	N	A	410	−0.5	−23.8	52.1	24
VAL	CA	A	410	−1.8	−23.4	51.6	27
VAL	CB	A	410	−2.2	−24.0	50.2	26
VAL	CG1	A	410	−3.6	−23.5	49.8	25
VAL	CG2	A	410	−1.2	−23.8	49.2	24
VAL	C	A	410	−2.7	−23.8	52.7	29
VAL	O	A	410	−2.9	−25.0	53.0	25
GLU	N	A	411	−3.3	−22.9	53.4	28
GLU	CA	A	411	−4.1	−23.2	54.6	30
GLU	CB	A	411	−3.3	−22.9	55.8	32
GLU	CG	A	411	−2.0	−23.7	55.8	39
GLU	CD	A	411	−1.2	−23.3	57.0	44
GLU	OE1	A	411	−0.9	−24.2	57.8	50
GLU	OE2	A	411	−0.9	−22.1	57.2	44
GLU	C	A	411	−5.5	−22.4	54.7	30
GLU	O	A	411	−5.6	−21.3	54.2	23
GLY	N	A	412	−6.5	−23.2	55.2	32
GLY	CA	A	412	−7.8	−22.6	55.3	32
GLY	C	A	412	−8.7	−23.5	56.1	28
GLY	O	A	412	−8.3	−24.6	56.4	29
PRO	N	A	413	−9.9	−23.1	56.4	32
PRO	CD	A	413	−11.0	−24.0	56.9	32
PRO	CA	A	413	−10.5	−21.8	56.1	33
PRO	CB	A	413	−11.9	−22.2	55.7	33
PRO	CG	A	413	−12.3	−23.1	56.9	34
PRO	C	A	413	−10.5	−20.8	57.3	34
PRO	O	A	413	−10.6	−21.1	58.4	38
PHE	N	A	414	−10.4	−19.5	56.9	36
PHE	CA	A	414	−10.4	−18.4	57.9	41
PHE	CB	A	414	−9.1	−17.5	57.7	38
PHE	CG	A	414	−7.9	−18.3	57.9	40
PHE	CD1	A	414	−7.3	−18.9	56.8	39
PHE	CD2	A	414	−7.3	−18.4	59.1	40
PHE	CE1	A	414	−6.1	−19.7	56.9	40
PHE	CE2	A	414	−6.2	−19.2	59.3	40
PHE	CZ	A	414	−5.6	−19.8	58.2	40
PHE	C	A	414	−11.6	−17.6	57.6	46
PHE	O	A	414	−12.0	−17.3	56.4	48
VAL	N	A	415	−12.3	−17.2	58.6	49
VAL	CA	A	415	−13.5	−16.3	58.5	56
VAL	CB	A	415	−14.6	−16.6	59.5	57
VAL	CG1	A	415	−15.8	−15.8	59.3	54
VAL	CG2	A	415	−15.0	−18.1	59.5	56
VAL	C	A	415	−13.2	−14.8	58.4	62
VAL	O	A	415	−12.9	−14.2	59.4	62
THR	N	A	416	−13.4	−14.3	57.2	69
THR	CA	A	416	−13.2	−12.8	57.0	76
THR	CB	A	416	−11.9	−12.6	56.1	78
THR	OG1	A	416	−10.8	−13.1	56.7	81
THR	CG2	A	416	−11.7	−11.1	55.9	79
THR	C	A	416	−14.4	−12.2	56.5	79
THR	O	A	416	−15.0	−12.6	55.5	80
LEU	N	A	417	−14.8	−11.0	57.1	83
LEU	CA	A	417	−16.0	−10.3	56.7	86
LEU	CB	A	417	−16.8	−9.9	57.9	87
LEU	CG	A	417	−17.3	−11.0	58.8	88
LEU	CD1	A	417	−18.0	−10.5	60.0	88
LEU	CD2	A	417	−18.2	−12.0	58.0	87
LEU	C	A	417	−15.7	−9.1	55.8	87
LEU	O	A	417	−14.7	−8.4	56.0	87
ASP	N	A	418	−16.6	−8.8	54.9	88
ASP	CA	A	418	−16.5	−7.7	54.0	88
ASP	CB	A	418	−16.3	−6.4	54.7	90
ASP	CG	A	418	−17.5	−6.1	55.7	92
ASP	OD1	A	418	−17.2	−6.0	56.9	93
ASP	OD2	A	418	−18.6	−6.0	55.2	92
ASP	C	A	418	−15.4	−7.8	52.8	86
ASP	O	A	418	−15.1	−6.8	52.2	87
MET	N	A	419	−14.9	−9.0	52.6	83
MET	CA	A	419	−13.9	−9.3	51.6	81
MET	CB	A	419	−13.6	−10.8	51.4	78
MET	CG	A	419	−13.1	−11.5	52.7	74
MET	SD	A	419	−12.9	−13.2	52.3	73
MET	CE	A	419	−14.6	−13.8	52.4	73
MET	C	A	419	−14.3	−8.7	50.3	83
MET	O	A	419	−13.4	−8.5	49.4	83
GLU	N	A	420	−15.5	−8.3	50.1	84
GLU	CA	A	420	−16.0	−7.7	48.8	86
GLU	CB	A	420	−17.5	−7.9	48.6	90
GLU	CG	A	420	−18.0	−7.3	47.3	93
GLU	CD	A	420	−17.4	−8.0	46.1	96
GLU	OE1	A	420	−16.6	−8.9	46.3	97
GLU	OE2	A	420	−17.6	−7.6	45.0	97
GLU	C	A	420	−15.6	−6.3	48.7	85
GLU	O	A	420	−15.6	−5.7	47.6	89
ASP	N	A	421	−15.2	−5.7	49.8	81
ASP	CA	A	421	−14.8	−4.3	49.8	75
ASP	CB	A	421	−15.1	−3.6	51.2	79
ASP	CG	A	421	−16.5	−3.6	51.5	83
ASP	OD1	A	421	−17.1	−2.5	51.7	85
ASP	OD2	A	421	−17.1	−4.7	51.6	85
ASP	C	A	421	−13.3	−4.2	49.5	69
ASP	O	A	421	−12.7	−3.2	49.5	67
CYS	N	A	422	−12.7	−5.4	49.3	62
CYS	CA	A	422	−11.3	−5.4	49.0	56
CYS	C	A	422	−11.0	−5.2	47.5	53
CYS	O	A	422	−9.8	−5.0	47.1	52
CYS	CB	A	422	−10.7	−6.8	49.4	53
CYS	SG	A	422	−10.9	−7.1	51.2	50
GLY	N	A	423	−12.0	−5.2	46.7	52
GLY	CA	A	423	−11.8	−5.0	45.3	51
GLY	C	A	423	−11.8	−3.6	44.9	54
GLY	O	A	423	−12.4	−2.7	45.6	56
TYR	N	A	424	−11.1	−3.2	43.9	56
TYR	CA	A	424	−10.9	−1.8	43.4	57
TYR	CB	A	424	−9.5	−1.5	43.1	59
TYR	CG	A	424	−9.3	0.0	42.7	61
TYR	CD1	A	424	−9.5	1.0	43.6	61
TYR	CE1	A	424	−9.4	2.4	43.1	64
TYR	CD2	A	424	−9.1	0.3	41.3	61
TYR	CE2	A	424	−9.0	1.6	40.9	62
TYR	CZ	A	424	−9.1	2.6	41.8	63
TYR	OH	A	424	−9.1	3.9	41.4	68
TYR	C	A	424	−11.8	−1.6	42.2	57
TYR	O	A	424	−11.8	−2.4	41.3	59
ASN	N	A	425	−12.6	−0.5	42.1	58
ASN	CA	A	425	−13.4	−0.2	41.0	58
ASN	CB	A	425	−14.9	−0.3	41.4	58
ASN	CG	A	425	−15.3	−1.6	41.9	58
ASN	OD1	A	425	−16.1	−2.3	41.3	59
ASN	ND2	A	425	−14.8	−2.0	43.1	60
ASN	C	A	425	−13.1	1.1	40.3	56
ASN	O	A	425	−12.6	2.1	41.0	53
SER	N	B	38	39.6	7.4	12.8	72
SER	CA	B	38	39.5	6.1	12.0	73
SER	CB	B	38	38.4	5.2	12.6	77
SER	OG	B	38	38.7	4.8	14.0	80
SER	C	B	38	39.2	6.4	10.6	69
SER	O	B	38	39.1	5.5	9.7	69
PHE	N	B	39	39.0	7.7	10.3	63
PHE	CA	B	39	38.7	8.2	8.9	55
PHE	CB	B	39	37.2	8.5	8.7	49
PHE	CG	B	39	36.3	7.4	9.0	46
PHE	CD1	B	39	35.9	7.0	10.3	44
PHE	CD2	B	39	35.8	6.6	7.9	46
PHE	CE1	B	39	35.1	6.0	10.5	45
PHE	CE2	B	39	34.9	5.6	8.1	45
PHE	CZ	B	39	34.6	5.2	9.4	45
PHE	C	B	39	39.6	9.4	8.5	54
PHE	O	B	39	39.2	10.2	7.7	54
VAL	N	B	40	40.8	9.4	9.1	53
VAL	CA	B	40	41.7	10.5	8.9	54
VAL	CB	B	40	43.1	10.2	9.5	58
VAL	CG1	B	40	44.1	11.3	9.2	59
VAL	CG2	B	40	43.0	9.8	10.9	61
VAL	C	B	40	41.9	11.0	7.4	52
VAL	O	B	40	42.2	12.1	7.2	51
GLU	N	B	41	41.7	10.1	6.5	49
GLU	CA	B	41	41.9	10.4	5.0	47
GLU	CB	B	41	42.0	9.2	4.2	53
GLU	CG	B	41	42.1	9.5	2.7	64
GLU	CD	B	41	42.3	8.2	1.9	70
GLU	OE1	B	41	42.2	7.1	2.5	72
GLU	OE2	B	41	42.4	8.2	0.7	71
GLU	C	B	41	40.8	11.4	4.5	42
GLU	O	B	41	41.0	12.0	3.5	38
MET	N	B	42	39.6	11.4	5.2	34
MET	CA	B	42	38.5	12.2	4.7	30
MET	CB	B	42	37.2	11.5	4.7	30
MET	CG	B	42	37.2	10.3	3.8	30
MET	SD	B	42	35.6	9.5	3.9	31
MET	CE	B	42	36.0	8.1	4.8	26
MET	C	B	42	38.4	13.5	5.6	28
MET	O	B	42	37.6	14.4	5.3	27
VAL	N	B	43	39.2	13.5	6.7	27
VAL	CA	B	43	39.2	14.7	7.5	26
VAL	CB	B	43	40.0	14.5	8.8	26
VAL	CG1	B	43	40.0	15.8	9.6	27
VAL	CG2	B	43	39.4	13.4	9.7	24
VAL	C	B	43	39.7	15.9	6.8	29
VAL	O	B	43	40.7	15.9	6.1	26
ASP	N	B	44	38.9	17.0	6.8	33
ASP	CA	B	44	39.3	18.2	6.2	31
ASP	CB	B	44	40.7	18.6	6.6	35
ASP	CG	B	44	41.1	20.0	6.1	42
ASP	OD1	B	44	40.2	20.8	5.9	42
ASP	OD2	B	44	42.3	20.3	6.0	44
ASP	C	B	44	39.2	18.2	4.7	30
ASP	O	B	44	39.8	18.9	3.9	25
ASN	N	B	45	38.3	17.3	4.1	29
ASN	CA	B	45	38.1	17.1	2.7	27
ASN	CB	B	45	37.6	15.7	2.3	24
ASN	CG	B	45	36.3	15.4	2.8	19
ASN	OD1	B	45	35.7	16.1	3.6	18
ASN	ND2	B	45	35.8	14.2	2.5	17
ASN	C	B	45	37.2	18.2	2.1	25
ASN	O	B	45	36.8	18.2	1.0	24
LEU	N	B	46	36.7	19.1	3.0	23
LEU	CA	B	46	35.8	20.2	2.6	27
LEU	CB	B	46	34.6	20.2	3.4	26
LEU	CG	B	46	33.7	19.0	3.4	26
LEU	CD1	B	46	32.5	19.1	4.3	24
LEU	CD2	B	46	33.3	18.6	1.9	24
LEU	C	B	46	36.4	21.6	2.5	27
LEU	O	B	46	37.2	22.0	3.4	27
ARG	N	B	47	36.1	22.3	1.5	30
ARG	CA	B	47	36.5	23.7	1.2	26
ARG	CB	B	47	37.6	23.9	0.2	30
ARG	CG	B	47	38.9	23.3	0.6	34
ARG	CD	B	47	39.5	24.0	1.8	44
ARG	NE	B	47	40.8	23.5	2.3	46
ARG	CZ	B	47	40.9	22.8	3.4	47
ARG	NH1	B	47	39.9	22.6	4.2	46
ARG	NH2	B	47	42.1	22.4	3.8	47
ARG	C	B	47	35.3	24.5	0.8	27
ARG	O	B	47	34.2	24.0	0.5	25
GLY	N	B	48	35.4	25.9	0.9	29
GLY	CA	B	48	34.3	26.7	0.5	34
GLY	C	B	48	34.5	28.1	0.8	38
GLY	O	B	48	35.5	28.5	1.5	39
LYS	N	B	49	33.7	29.0	0.2	37
LYS	CA	B	49	33.8	30.4	0.5	36
LYS	CB	B	49	33.9	31.2	−0.8	39
LYS	CG	B	49	34.0	32.7	−0.6	46
LYS	CD	B	49	34.1	33.5	−1.8	51
LYS	CE	B	49	34.3	35.0	−1.6	55
LYS	NZ	B	49	33.1	35.6	−0.8	54
LYS	C	B	49	32.5	30.8	1.3	33
LYS	O	B	49	31.4	30.4	1.0	35
SER	N	B	50	32.8	31.6	2.4	30
SER	CA	B	50	31.7	32.0	3.2	32
SER	CB	B	50	32.1	33.2	4.1	30
SER	OG	B	50	31.1	33.6	5.0	35
SER	C	B	50	30.4	32.4	2.5	29
SER	O	B	50	30.4	33.3	1.6	29
GLY	N	B	51	29.3	31.8	2.8	25
GLY	CA	B	51	28.0	32.1	2.2	23
GLY	C	B	51	27.9	31.5	0.8	24
GLY	O	B	51	26.9	31.8	0.1	20
GLN	N	B	52	28.8	30.6	0.3	22
GLN	CA	B	52	28.7	30.1	−1.0	21
GLN	CB	B	52	29.8	30.7	−1.9	21
GLN	CG	B	52	29.6	32.2	−2.0	26
GLN	CD	B	52	30.7	32.8	−2.9	29
GLN	OE1	B	52	31.5	32.1	−3.5	30
GLN	NE2	B	52	30.6	34.1	−3.1	32
GLN	C	B	52	28.7	28.5	−1.0	23
GLN	O	B	52	29.0	27.9	−2.0	21
GLY	N	B	53	28.4	28.0	0.2	19
GLY	CA	B	53	28.4	26.5	0.4	20
GLY	C	B	53	29.7	25.8	0.6	24
GLY	O	B	53	30.8	26.5	0.7	29
TYR	N	B	54	29.6	24.5	0.7	24
TYR	CA	B	54	30.8	23.7	0.9	23
TYR	CB	B	54	30.8	23.0	2.3	21
TYR	CG	B	54	30.8	23.9	3.5	21
TYR	CD1	B	54	29.7	24.6	3.9	19
TYR	CE1	B	54	29.7	25.4	5.0	24
TYR	CD2	B	54	32.0	24.1	4.2	25
TYR	CE2	B	54	32.1	24.9	5.3	24
TYR	CZ	B	54	30.9	25.6	5.7	25
TYR	OH	B	54	31.1	26.4	6.8	20
TYR	C	B	54	30.9	22.6	−0.2	23
TYR	O	B	54	29.9	22.1	−0.6	24
TYR	N	B	55	32.2	22.4	−0.7	23
TYR	CA	B	55	32.4	21.5	−1.7	23
TYR	CB	B	55	32.7	22.2	−3.1	22
TYR	CG	B	55	33.9	23.1	−3.0	23
TYR	CD1	B	55	35.2	22.6	−3.3	20
TYR	CE1	B	55	36.3	23.4	−3.3	21
TYR	CD2	B	55	33.8	24.5	−2.8	24
TYR	CE2	B	55	34.9	25.3	−2.8	24
TYR	CZ	B	55	36.2	24.8	−3.0	24
TYR	OH	B	55	37.3	25.6	−3.0	23
TYR	C	B	55	33.5	20.5	−1.4	28
TYR	O	B	55	34.4	20.7	−0.6	20
VAL	N	B	56	33.4	19.3	−2.1	23
VAL	CA	B	56	34.3	18.2	−2.0	21
VAL	CB	B	56	33.6	17.0	−1.4	21
VAL	CG1	B	56	32.6	16.4	−2.4	17
VAL	CG2	B	56	34.7	15.9	−1.1	16
VAL	C	B	56	34.9	18.0	−3.4	24
VAL	O	B	56	34.2	18.2	−4.4	22
GLU	N	B	57	36.1	17.5	−3.4	24
GLU	CA	B	57	36.7	17.2	−4.7	24
GLU	CB	B	57	38.2	17.2	−4.7	24
GLU	CG	B	57	38.8	17.0	−6.1	24
GLU	CD	B	57	40.3	17.0	−6.1	30
GLU	OE1	B	57	40.9	18.1	−6.2	34
GLU	OE2	B	57	40.9	16.0	−5.9	33
GLU	C	B	57	36.2	15.9	−5.3	25
GLU	O	B	57	36.1	14.9	−4.5	22
MET	N	B	58	35.8	15.8	−6.5	21
MET	CA	B	58	35.3	14.6	−7.2	22
MET	CB	B	58	33.8	14.5	−7.2	22
MET	CG	B	58	33.1	14.5	−5.8	18
MET	SD	B	58	31.3	14.4	−6.0	19
MET	CE	B	58	31.1	12.7	−6.3	19
MET	C	B	58	35.8	14.5	−8.6	26
MET	O	B	58	36.3	15.4	−9.2	26
THR	N	B	59	35.8	13.2	−9.1	26
THR	CA	B	59	36.3	13.0	−10.5	24
THR	CB	B	59	37.6	12.2	−10.5	25
THR	OG1	B	59	37.4	10.9	−9.9	29
THR	CG2	B	59	38.7	12.9	−9.9	23
THR	C	B	59	35.1	12.3	−11.2	28
THR	O	B	59	34.4	11.5	−10.6	28
VAL	N	B	60	35.0	12.6	−12.5	24
VAL	CA	B	60	34.0	12.0	−13.3	23
VAL	CB	B	60	32.8	12.9	−13.6	25
VAL	CG1	B	60	32.1	13.3	−12.2	24
VAL	CG2	B	60	33.2	14.1	−14.3	27
VAL	C	B	60	34.6	11.6	−14.6	25
VAL	O	B	60	35.4	12.3	−15.2	28
GLY	N	B	61	34.2	10.4	−15.1	23
GLY	CA	B	61	34.7	9.9	−16.4	22
GLY	C	B	61	36.0	9.1	−16.4	28
GLY	O	B	61	36.7	9.0	−15.4	29
SER	N	B	62	36.3	8.7	−17.7	28
SER	CA	B	62	37.5	7.9	−17.9	33
SER	CB	B	62	37.2	6.4	−18.1	30
SER	OG	B	62	36.6	5.9	−16.9	33
SER	C	B	62	38.2	8.5	−19.2	33
SER	O	B	62	37.6	8.3	−20.3	35
PRO	N	B	63	39.4	9.1	−19.1	29
PRO	CD	B	63	40.0	9.8	−20.2	27
PRO	CA	B	63	40.1	9.3	−17.9	29
PRO	CB	B	63	41.5	9.7	−18.4	31
PRO	CG	B	63	41.1	10.6	−19.5	28
PRO	C	B	63	39.5	10.4	−16.9	32
PRO	O	B	63	38.9	11.4	−17.4	32
PRO	N	B	64	39.6	10.2	−15.6	29
PRO	CD	B	64	40.2	9.0	−15.0	34
PRO	CA	B	64	39.2	11.0	−14.5	29
PRO	CB	B	64	40.0	10.6	−13.4	33
PRO	CG	B	64	39.9	9.1	−13.5	37
PRO	C	B	64	39.2	12.6	−14.7	26
PRO	O	B	64	40.3	13.1	−14.9	22
GLN	N	B	65	38.0	13.2	−14.7	26
GLN	CA	B	65	38.0	14.7	−14.8	23
GLN	CB	B	65	36.9	15.1	−15.9	20
GLN	CG	B	65	37.1	14.5	−17.3	22
GLN	CD	B	65	36.0	15.0	−18.2	26
GLN	OE1	B	65	35.3	16.0	−17.9	27
GLN	NE2	B	65	35.8	14.3	−19.3	27
GLN	C	B	65	37.7	15.2	−13.4	26
GLN	O	B	65	36.7	14.9	−12.8	22
THR	N	B	66	38.5	16.1	−13.0	25
THR	CA	B	66	38.4	16.7	−11.7	25
THR	CB	B	66	39.8	17.1	−11.1	24
THR	OG1	B	66	40.7	16.0	−11.1	29
THR	CG2	B	66	39.6	17.7	−9.7	24
THR	C	B	66	37.4	17.9	−11.6	26
THR	O	B	66	37.4	18.8	−12.4	23
LEU	N	B	67	36.6	17.8	−10.6	26
LEU	CA	B	67	35.5	18.8	−10.4	21
LEU	CB	B	67	34.2	18.4	−11.1	21
LEU	CG	B	67	34.4	18.3	−12.6	21
LEU	CD1	B	67	33.2	17.7	−13.3	25
LEU	CD2	B	67	34.8	19.7	−13.3	22
LEU	C	B	67	35.2	19.0	−8.9	22
LEU	O	B	67	35.2	18.1	−8.1	24
ASN	N	B	68	35.0	20.3	−8.5	19
ASN	CA	B	68	34.6	20.6	−7.1	20
ASN	CB	B	68	35.1	21.9	−6.6	19
ASN	CG	B	68	36.6	21.9	−6.4	21
ASN	OD1	B	68	37.2	22.9	−6.7	27
ASN	ND2	B	68	37.2	20.8	−6.0	14
ASN	C	B	68	33.0	20.5	−7.1	23
ASN	O	B	68	32.4	21.1	−7.9	23
ILE	N	B	69	32.5	19.7	−6.1	21
ILE	CA	B	69	31.1	19.5	−6.0	21
ILE	CB	B	69	30.7	18.0	−6.3	23
ILE	CG2	B	69	29.2	17.9	−6.3	23
ILE	CG1	B	69	31.3	17.5	−7.6	22
ILE	CD1	B	69	30.8	18.2	−8.9	29
ILE	C	B	69	30.6	19.9	−4.7	22
ILE	O	B	69	31.0	19.5	−3.6	19
LEU	N	B	70	29.6	20.8	−4.7	20
LEU	CA	B	70	28.9	21.3	−3.6	20
LEU	CB	B	70	28.1	22.6	−3.9	20
LEU	CG	B	70	27.4	23.2	−2.7	24
LEU	CD1	B	70	26.8	24.6	−3.1	24
LEU	CD2	B	70	26.2	22.4	−2.2	26
LEU	C	B	70	28.1	20.3	−2.9	22
LEU	O	B	70	27.2	19.7	−3.5	29
VAL	N	B	71	28.3	20.0	−1.6	26
VAL	CA	B	71	27.6	19.0	−0.9	26
VAL	CB	B	71	28.4	18.5	0.3	27
VAL	CG1	B	71	27.6	17.5	1.1	33
VAL	CG2	B	71	29.7	17.8	−0.2	26
VAL	C	B	71	26.3	19.6	−0.4	29
VAL	O	B	71	26.2	20.5	0.4	26
ASP	N	B	72	25.2	19.0	−0.9	28
ASP	CA	B	72	23.8	19.5	−0.6	26
ASP	CB	B	72	23.2	20.1	−1.8	27
ASP	CG	B	72	21.9	20.7	−1.6	28
ASP	OD1	B	72	21.5	21.0	−0.5	33
ASP	OD2	B	72	21.1	20.9	−2.6	24
ASP	C	B	72	22.9	18.4	0.0	27
ASP	O	B	72	22.4	17.6	−0.8	25
THR	N	B	73	22.6	18.5	1.3	25
THR	CA	B	73	21.6	17.5	1.8	22
THR	CB	B	73	21.9	17.3	3.4	23
THR	OG1	B	73	21.7	18.5	4.1	23
THR	CG2	B	73	23.2	16.7	3.7	18
THR	C	B	73	20.2	17.9	1.6	29
THR	O	B	73	19.3	17.2	1.9	27
GLY	N	B	74	20.0	19.0	0.9	27
GLY	CA	B	74	18.7	19.5	0.6	28
GLY	C	B	74	18.1	19.1	−0.8	27
GLY	O	B	74	17.0	19.5	−1.1	23
SER	N	B	75	18.9	18.3	−1.5	26
SER	CA	B	75	18.4	17.8	−2.9	22
SER	CB	B	75	18.9	18.7	−4.0	23
SER	OG	B	75	20.3	18.8	−4.1	28
SER	C	B	75	18.9	16.4	−3.1	22
SER	O	B	75	19.7	15.9	−2.3	24
SER	N	B	76	18.4	15.8	−4.2	20
SER	CA	B	76	18.8	14.4	−4.4	23
SER	CB	B	76	17.6	13.5	−4.2	22
SER	OG	B	76	17.2	13.7	−2.9	28
SER	C	B	76	19.4	14.2	−5.8	26
SER	O	B	76	19.6	13.0	−6.2	24
ASN	N	B	77	19.8	15.2	−6.5	26
ASN	CA	B	77	20.4	15.1	−7.8	23
ASN	CB	B	77	19.7	15.9	−8.9	23
ASN	CG	B	77	18.3	15.4	−9.2	24
ASN	OD1	B	77	17.3	15.7	−8.5	24
ASN	ND2	B	77	18.2	14.6	−10.2	18
ASN	C	B	77	21.9	15.4	−7.8	23
ASN	O	B	77	22.4	16.3	−7.2	25
PHE	N	B	78	22.6	14.6	−8.6	21
PHE	CA	B	78	24.1	14.8	−8.8	22
PHE	CB	B	78	24.8	13.5	−8.8	23
PHE	CG	B	78	26.3	13.6	−9.0	22
PHE	CD1	B	78	27.0	12.7	−9.6	24
PHE	CD2	B	78	27.0	14.8	−8.6	23
PHE	CE1	B	78	28.4	12.8	−9.9	23
PHE	CE2	B	78	28.3	15.0	−8.8	22
PHE	CZ	B	78	29.1	14.0	−9.4	20
PHE	C	B	78	24.1	15.5	−10.1	22
PHE	O	B	78	23.7	15.0	−11.1	22
ALA	N	B	79	24.7	16.7	−10.1	24
ALA	CA	B	79	24.8	17.5	−11.4	22
ALA	CB	B	79	23.6	18.5	−11.5	23
ALA	C	B	79	26.1	18.2	−11.4	23
ALA	O	B	79	26.6	18.7	−10.4	22
VAL	N	B	80	26.6	18.4	−12.7	24
VAL	CA	B	80	27.9	19.0	−12.9	24
VAL	CB	B	80	29.0	18.1	−13.1	25
VAL	CG1	B	80	29.2	17.2	−11.9	26
VAL	CG2	B	80	28.8	17.2	−14.4	19
VAL	C	B	80	27.8	20.0	−14.2	25
VAL	O	B	80	27.0	19.7	−15.1	25
GLY	N	B	81	28.5	21.1	−14.1	25
GLY	CA	B	81	28.5	21.9	−15.3	19
GLY	C	B	81	29.0	21.1	−16.4	25
GLY	O	B	81	30.0	20.4	−16.3	19
ALA	N	B	82	28.3	21.1	−17.6	20
ALA	CA	B	82	28.7	20.3	−18.8	23
ALA	CB	B	82	27.7	19.2	−19.0	23
ALA	C	B	82	28.8	21.2	−20.0	26
ALA	O	B	82	28.9	20.6	−21.1	24
ALA	N	B	83	28.8	22.5	−19.9	25
ALA	CA	B	83	28.9	23.4	−21.0	28
ALA	CB	B	83	27.5	23.6	−21.6	27
ALA	C	B	83	29.5	24.7	−20.4	33
ALA	O	B	83	29.3	25.0	−19.2	32
PRO	N	B	84	30.1	25.5	−21.3	34
PRO	CD	B	84	30.6	25.1	−22.7	35
PRO	CA	B	84	30.7	26.8	−21.0	31
PRO	CB	B	84	31.0	27.4	−22.3	36
PRO	CG	B	84	31.7	26.2	−23.0	37
PRO	C	B	84	29.8	27.7	−20.2	29
PRO	O	B	84	28.6	27.7	−20.4	29
HIS	N	B	85	30.3	28.4	−19.2	29
HIS	CA	B	85	29.5	29.3	−18.4	29
HIS	CB	B	85	28.6	28.6	−17.3	25
HIS	CG	B	85	27.8	29.5	−16.5	25
HIS	CD2	B	85	26.4	29.8	−16.5	23
HIS	ND1	B	85	28.3	30.4	−15.6	25
HIS	CE1	B	85	27.3	31.2	−15.1	23
HIS	NE2	B	85	26.2	30.8	−15.6	24
HIS	C	B	85	30.4	30.3	−17.7	30
HIS	O	B	85	31.5	30.0	−17.1	34
PRO	N	B	86	30.1	31.6	−17.7	32
PRO	CD	B	86	29.0	32.2	−18.5	30
PRO	CA	B	86	30.9	32.7	−17.2	29
PRO	CB	B	86	29.9	33.8	−17.1	31
PRO	CG	B	86	29.3	33.7	−18.5	33
PRO	C	B	86	31.4	32.4	−15.8	27
PRO	O	B	86	32.5	32.8	−15.4	27
PHE	N	B	87	30.7	31.6	−15.0	27
PHE	CA	B	87	31.1	31.3	−13.7	26
PHE	CB	B	87	29.9	31.5	−12.7	30
PHE	CG	B	87	29.4	32.9	−12.7	31
PHE	CD1	B	87	28.2	33.2	−12.1	30
PHE	CD2	B	87	30.1	34.0	−13.3	29
PHE	CE1	B	87	27.7	34.6	−12.0	33
PHE	CE2	B	87	29.6	35.3	−13.3	31
PHE	CZ	B	87	28.4	35.6	−12.6	28
PHE	C	B	87	31.7	29.9	−13.5	24
PHE	O	B	87	32.0	29.6	−12.4	27
LEU	N	B	88	31.9	29.2	−14.6	19
LEU	CA	B	88	32.6	27.9	−14.5	22
LEU	CB	B	88	31.8	26.9	−15.4	25
LEU	CG	B	88	30.4	26.5	−14.9	21
LEU	CD1	B	88	29.7	25.6	−15.8	21
LEU	CD2	B	88	30.5	25.9	−13.5	25
LEU	C	B	88	34.0	27.9	−14.9	25
LEU	O	B	88	34.4	28.3	−16.0	29
HIS	N	B	89	34.9	27.6	−13.9	20
HIS	CA	B	89	36.3	27.5	−14.2	26
HIS	CB	B	89	37.1	27.2	−12.9	26
HIS	CG	B	89	37.0	28.3	−11.8	23
HIS	CD2	B	89	36.9	28.1	−10.5	19
HIS	ND1	B	89	37.0	29.6	−12.1	26
HIS	CE1	B	89	37.0	30.3	−10.9	22
HIS	NE2	B	89	36.9	29.4	−9.9	24
HIS	C	B	89	36.6	26.3	−15.1	28
HIS	O	B	89	37.6	26.3	−15.8	29
ARG	N	B	90	35.7	25.4	−15.2	24
ARG	CA	B	90	35.9	24.2	−15.9	22
ARG	CB	B	90	37.0	23.3	−15.3	22
ARG	CG	B	90	36.8	23.0	−13.8	23
ARG	CD	B	90	37.9	22.2	−13.2	22
ARG	NE	B	90	37.6	22.0	−11.8	21
ARG	CZ	B	90	38.5	21.6	−10.9	21
ARG	NH1	B	90	39.7	21.3	−11.3	22
ARG	NH2	B	90	38.2	21.5	−9.6	21
ARG	C	B	90	34.6	23.4	−15.9	24
ARG	O	B	90	33.7	23.6	−15.0	22
TYR	N	B	91	34.4	22.4	−16.8	27
TYR	CA	B	91	33.2	21.6	−16.9	29
TYR	CB	B	91	32.1	22.4	−17.7	31
TYR	CG	B	91	32.5	22.6	−19.1	31
TYR	CD1	B	91	32.3	21.6	−20.1	31
TYR	CE1	B	91	32.7	21.9	−21.4	37
TYR	CD2	B	91	33.0	23.9	−19.5	32
TYR	CE2	B	91	33.4	24.1	−20.9	30
TYR	CZ	B	91	33.2	23.1	−21.8	34
TYR	OH	B	91	33.5	23.3	−23.1	35
TYR	C	B	91	33.4	20.2	−17.5	28
TYR	O	B	91	34.4	19.9	−18.2	25
TYR	N	B	92	32.5	19.4	−17.1	28
TYR	CA	B	92	32.4	18.0	−17.5	25
TYR	CB	B	92	31.2	17.3	−16.8	23
TYR	CG	B	92	30.9	15.9	−17.2	26
TYR	CD1	B	92	31.9	14.9	−17.5	24
TYR	CE1	B	92	31.6	13.6	−17.7	22
TYR	CD2	B	92	29.6	15.4	−17.2	21
TYR	CE2	B	92	29.3	14.1	−17.5	26
TYR	CZ	B	92	30.3	13.2	−17.7	24
TYR	OH	B	92	29.9	11.9	−18.0	27
TYR	C	B	92	32.4	17.9	−19.0	26
TYR	O	B	92	31.5	18.4	−19.6	24
GLN	N	B	93	33.4	17.2	−19.6	25
GLN	CA	B	93	33.4	17.0	−21.0	30
GLN	CB	B	93	34.7	17.5	−21.7	30
GLN	CG	B	93	35.0	18.9	−21.4	39
GLN	CD	B	93	36.3	19.3	−22.1	38
GLN	OE1	B	93	37.3	19.6	−21.5	45
GLN	NE2	B	93	36.3	19.3	−23.4	35
GLN	C	B	93	33.1	15.6	−21.4	28
GLN	O	B	93	34.0	14.7	−21.4	26
ARG	N	B	94	31.8	15.3	−21.6	24
ARG	CA	B	94	31.3	14.0	−21.9	30
ARG	CB	B	94	29.8	14.1	−22.1	29
ARG	CG	B	94	29.1	14.4	−20.8	28
ARG	CD	B	94	27.6	14.6	−21.0	27
ARG	NE	B	94	27.4	15.7	−21.8	30
ARG	CZ	B	94	26.2	16.1	−22.3	32
ARG	NH1	B	94	25.1	15.5	−21.9	32
ARG	NH2	B	94	26.1	17.2	−23.0	30
ARG	C	B	94	32.0	13.3	−23.1	32
ARG	O	B	94	32.2	12.1	−23.0	30
GLN	N	B	95	32.4	14.0	−24.1	35
GLN	CA	B	95	33.0	13.4	−25.3	37
GLN	CB	B	95	33.0	14.4	−26.5	43
GLN	CG	B	95	31.6	14.8	−26.9	55
GLN	CD	B	95	31.7	15.8	−28.1	62
GLN	OE1	B	95	31.2	15.5	−29.2	65
GLN	NE2	B	95	32.2	17.0	−27.8	65
GLN	C	B	95	34.4	12.9	−25.0	36
GLN	O	B	95	35.0	12.2	−25.8	34
LEU	N	B	96	35.0	13.3	−23.8	33
LEU	CA	B	96	36.3	12.9	−23.5	30
LEU	CB	B	96	37.1	14.0	−22.9	28
LEU	CG	B	96	37.3	15.2	−23.8	31
LEU	CD1	B	96	38.2	16.3	−23.2	25
LEU	CD2	B	96	38.0	14.7	−25.1	30
LEU	C	B	96	36.3	11.7	−22.5	28
LEU	O	B	96	37.4	11.2	−22.1	31
SER	N	B	97	35.1	11.2	−22.2	28
SER	CA	B	97	35.0	10.0	−21.3	28
SER	CB	B	97	34.1	10.3	−20.1	22
SER	OG	B	97	34.0	9.2	−19.3	28
SER	C	B	97	34.6	8.7	−22.0	28
SER	O	B	97	33.5	8.7	−22.6	25
SER	N	B	98	35.4	7.7	−22.0	31
SER	CA	B	98	35.1	6.5	−22.6	32
SER	CB	B	98	36.3	5.6	−22.8	32
SER	OG	B	98	36.9	5.3	−21.6	40
SER	C	B	98	34.0	5.7	−21.9	31
SER	O	B	98	33.3	4.8	−22.4	37
THR	N	B	99	33.8	6.0	−20.6	29
THR	CA	B	99	32.8	5.4	−19.8	27
THR	CB	B	99	33.4	5.1	−18.4	28
THR	OG1	B	99	33.8	6.4	−17.8	29
THR	CG2	B	99	34.5	4.1	−18.4	32
THR	C	B	99	31.4	6.1	−19.7	27
THR	O	B	99	30.5	5.6	−19.1	29
TYR	N	B	100	31.4	7.2	−20.4	27
TYR	CA	B	100	30.1	7.9	−20.6	27
TYR	CB	B	100	30.3	9.3	−21.2	29
TYR	CG	B	100	29.0	10.0	−21.5	33
TYR	CD1	B	100	28.2	10.5	−20.5	31
TYR	CE1	B	100	27.0	11.1	−20.8	32
TYR	CD2	B	100	28.6	10.1	−22.8	34
TYR	CE2	B	100	27.4	10.7	−23.1	33
TYR	CZ	B	100	26.6	11.2	−22.1	35
TYR	OH	B	100	25.3	11.8	−22.4	38
TYR	C	B	100	29.0	7.2	−21.3	27
TYR	O	B	100	29.1	6.7	−22.4	28
ARG	N	B	101	27.8	7.2	−20.7	28
ARG	CA	B	101	26.6	6.6	−21.2	32
ARG	CB	B	101	26.1	5.4	−20.5	35
ARG	CG	B	101	26.9	4.2	−20.4	42
ARG	CD	B	101	26.1	3.2	−19.6	45
ARG	NE	B	101	26.8	1.9	−19.4	47
ARG	CZ	B	101	26.4	1.0	−18.5	50
ARG	NH1	B	101	25.4	1.3	−17.7	51
ARG	NH2	B	101	27.1	−0.1	−18.3	57
ARG	C	B	101	25.5	7.7	−21.3	32
ARG	O	B	101	25.2	8.3	−20.2	32
ASP	N	B	102	24.9	7.8	−22.4	27
ASP	CA	B	102	23.9	8.8	−22.6	31
ASP	CB	B	102	23.9	9.4	−24.0	32
ASP	CG	B	102	22.8	10.5	−24.2	35
ASP	OD1	B	102	22.0	10.8	−23.3	37
ASP	OD2	B	102	22.8	11.1	−25.3	37
ASP	C	B	102	22.5	8.2	−22.3	29
ASP	O	B	102	22.2	7.2	−22.9	31
LEU	N	B	103	21.8	8.7	−21.3	28
LEU	CA	B	103	20.4	8.2	−21.0	31
LEU	CB	B	103	20.1	8.4	−19.5	28
LEU	CG	B	103	20.9	7.6	−18.5	31
LEU	CD1	B	103	20.7	7.9	−17.1	29
LEU	CD2	B	103	20.7	6.1	−18.8	26
LEU	C	B	103	19.4	8.7	−21.9	32
LEU	O	B	103	18.2	8.3	−21.7	28
ARG	N	B	104	19.7	9.6	−22.8	38
ARG	CA	B	104	18.8	10.1	−23.8	45
ARG	CB	B	104	18.4	8.9	−24.8	46
ARG	CG	B	104	19.5	8.4	−25.6	53
ARG	CD	B	104	19.2	7.3	−26.5	60
ARG	NE	B	104	18.1	7.6	−27.5	70
ARG	CZ	B	104	16.8	7.3	−27.3	74
ARG	NH1	B	104	16.4	6.7	−26.2	74
ARG	NH2	B	104	16.0	7.7	−28.2	75
ARG	C	B	104	17.5	10.7	−23.1	44
ARG	O	B	104	16.4	10.6	−23.7	47
LYS	N	B	105	17.8	11.4	−22.0	42
LYS	CA	B	105	16.7	12.0	−21.3	41
LYS	CB	B	105	15.9	11.0	−20.4	42
LYS	CG	B	105	14.8	11.5	−19.6	48
LYS	CD	B	105	14.1	10.3	−18.8	54
LYS	CE	B	105	15.1	9.7	−17.9	55
LYS	NZ	B	105	14.5	8.6	−17.1	58
LYS	C	B	105	17.0	13.3	−20.5	40
LYS	O	B	105	18.0	13.4	−19.8	40
GLY	N	B	106	16.2	14.3	−20.7	38
GLY	CA	B	106	16.4	15.6	−20.1	33
GLY	C	B	106	15.9	15.7	−18.6	32
GLY	O	B	106	15.1	14.9	−18.2	33
VAL	N	B	107	16.5	16.6	−17.9	30
VAL	CA	B	107	16.2	16.9	−16.5	27
VAL	CB	B	107	17.1	16.1	−15.6	26
VAL	CG1	B	107	18.6	16.5	−15.8	23
VAL	CG2	B	107	16.7	16.3	−14.1	26
VAL	C	B	107	16.2	18.3	−16.1	26
VAL	O	B	107	17.0	19.1	−16.6	30
TYR	N	B	108	15.2	18.7	−15.3	28
TYR	CA	B	108	15.0	20.1	−14.8	26
TYR	CB	B	108	13.7	20.7	−15.4	27
TYR	CG	B	108	13.5	22.1	−14.9	29
TYR	CD1	B	108	14.3	23.1	−15.2	27
TYR	CE1	B	108	14.1	24.4	−14.8	28
TYR	CD2	B	108	12.4	22.4	−14.1	29
TYR	CE2	B	108	12.1	23.7	−13.6	29
TYR	CZ	B	108	13.0	24.7	−13.9	27
TYR	OH	B	108	12.8	26.0	−13.5	28
TYR	C	B	108	14.9	20.1	−13.3	27
TYR	O	B	108	14.1	19.5	−12.7	31
VAL	N	B	109	15.9	20.9	−12.7	27
VAL	CA	B	109	15.9	21.0	−11.3	23
VAL	CB	B	109	17.1	20.2	−10.7	24
VAL	CG1	B	109	17.1	20.4	−9.1	21
VAL	CG2	B	109	17.0	18.7	−11.0	24
VAL	C	B	109	15.9	22.4	−10.7	22
VAL	O	B	109	16.8	23.2	−10.8	23
PRO	N	B	110	14.7	22.8	−10.1	24
PRO	CD	B	110	13.4	22.1	−10.2	21
PRO	CA	B	110	14.6	24.1	−9.5	25
PRO	CB	B	110	13.2	24.5	−9.9	24
PRO	CG	B	110	12.4	23.2	−9.6	22
PRO	C	B	110	14.8	24.1	−8.0	24
PRO	O	B	110	14.2	23.2	−7.3	26
TYR	N	B	111	15.6	25.0	−7.4	24
TYR	CA	B	111	15.8	25.0	−6.0	23
TYR	CB	B	111	17.4	25.1	−5.7	22
TYR	CG	B	111	18.2	24.0	−6.3	20
TYR	CD1	B	111	18.3	22.7	−5.6	22
TYR	CE1	B	111	19.1	21.7	−6.2	23
TYR	CD2	B	111	18.8	24.1	−7.5	20
TYR	CE2	B	111	19.6	23.1	−8.1	24
TYR	CZ	B	111	19.7	21.9	−7.4	25
TYR	OH	B	111	20.5	20.9	−7.9	24
TYR	C	B	111	15.1	26.2	−5.4	26
TYR	O	B	111	14.4	26.9	−6.1	22
THR	N	B	112	15.4	26.5	−4.1	23
THR	CA	B	112	14.7	27.7	−3.5	23
THR	CB	B	112	14.9	27.7	−2.0	23
THR	OG1	B	112	14.4	26.5	−1.4	21
THR	CG2	B	112	14.4	29.0	−1.4	22
THR	C	B	112	15.3	28.9	−4.2	28
THR	O	B	112	14.6	29.9	−4.4	29
GLN	N	B	113	16.6	28.9	−4.5	31
GLN	CA	B	113	17.3	30.0	−5.2	33
GLN	CB	B	113	18.1	30.8	−4.2	40
GLN	CG	B	113	17.3	31.4	−3.1	53
GLN	CD	B	113	16.3	32.4	−3.6	59
GLN	OE1	B	113	16.2	32.7	−4.8	64
GLN	NE2	B	113	15.5	33.0	−2.7	60
GLN	C	B	113	18.2	29.3	−6.2	31
GLN	O	B	113	19.1	28.5	−5.9	25
GLY	N	B	114	17.9	29.5	−7.5	26
GLY	CA	B	114	18.7	28.9	−8.6	27
GLY	C	B	114	18.0	27.8	−9.2	26
GLY	O	B	114	17.2	27.1	−8.6	26
LYS	N	B	115	18.3	27.5	−10.5	29
LYS	CA	B	115	17.6	26.5	−11.3	27
LYS	CB	B	115	16.3	26.9	−11.8	32
LYS	CG	B	115	16.3	28.1	−12.7	39
LYS	CD	B	115	15.0	28.5	−13.3	47
LYS	CE	B	115	14.0	28.9	−12.2	49
LYS	NZ	B	115	12.7	29.4	−12.8	55
LYS	C	B	115	18.5	26.1	−12.4	26
LYS	O	B	115	19.3	26.9	−12.9	27
TRP	N	B	116	18.4	24.8	−12.9	25
TRP	CA	B	116	19.2	24.4	−14.0	24
TRP	CB	B	116	20.6	24.0	−13.6	23
TRP	CG	B	116	20.7	22.9	−12.6	25
TRP	CD2	B	116	20.4	21.5	−12.9	24
TRP	CE2	B	116	20.6	20.8	−11.6	24
TRP	CE3	B	116	20.1	20.7	−14.0	28
TRP	CD1	B	116	21.0	23.0	−11.3	23
TRP	NE1	B	116	20.9	21.8	−10.7	25
TRP	CZ2	B	116	20.3	19.4	−11.5	22
TRP	CZ3	B	116	19.9	19.3	−13.8	24
TRP	CH2	B	116	20.0	18.7	−12.6	25
TRP	C	B	116	18.5	23.3	−14.9	25
TRP	O	B	116	17.8	22.5	−14.3	26
GLU	N	B	117	18.8	23.3	−16.2	32
GLU	CA	B	117	18.3	22.3	−17.1	36
GLU	CB	B	117	17.6	22.9	−18.2	41
GLU	CG	B	117	17.0	21.8	−19.2	54
GLU	CD	B	117	16.2	22.4	−20.3	61
GLU	OE1	B	117	15.0	22.2	−20.5	65
GLU	OE2	B	117	16.9	23.2	−21.1	62
GLU	C	B	117	19.5	21.5	−17.5	33
GLU	O	B	117	20.6	22.0	−17.8	30
GLY	N	B	118	19.4	20.1	−17.6	31
GLY	CA	B	118	20.5	19.3	−18.0	32
GLY	C	B	118	20.1	18.1	−18.8	30
GLY	O	B	118	18.9	17.8	−19.2	29
GLU	N	B	119	21.1	17.2	−19.0	28
GLU	CA	B	119	20.9	16.0	−19.8	28
GLU	CB	B	119	21.6	16.0	−21.1	31
GLU	CG	B	119	21.2	17.3	−21.9	37
GLU	CD	B	119	21.9	17.3	−23.3	42
GLU	OE1	B	119	21.3	17.6	−24.3	50
GLU	OE2	B	119	23.1	17.1	−23.3	43
GLU	C	B	119	21.4	14.7	−19.0	26
GLU	O	B	119	22.5	14.7	−18.6	26
LEU	N	B	120	20.5	13.8	−18.7	25
LEU	CA	B	120	20.8	12.6	−17.9	25
LEU	CB	B	120	19.6	11.8	−17.5	24
LEU	CG	B	120	18.7	12.6	−16.5	25
LEU	CD1	B	120	17.4	11.8	−16.2	27
LEU	CD2	B	120	19.4	13.0	−15.2	28
LEU	C	B	120	21.8	11.7	−18.6	27
LEU	O	B	120	21.8	11.5	−19.8	31
GLY	N	B	121	22.6	11.0	−17.7	29
GLY	CA	B	121	23.6	10.1	−18.2	30
GLY	C	B	121	24.2	9.3	−17.0	32
GLY	O	B	121	23.8	9.5	−15.9	29
THR	N	B	122	25.1	8.4	−17.3	31
THR	CA	B	122	25.8	7.6	−16.2	29
THR	CB	B	122	25.3	6.2	−16.1	26
THR	OG1	B	122	25.6	5.5	−17.3	33
THR	CG2	B	122	23.8	6.1	−15.8	26
THR	C	B	122	27.3	7.6	−16.5	29
THR	O	B	122	27.6	7.8	−17.7	28
ASP	N	B	123	28.1	7.5	−15.5	28
ASP	CA	B	123	29.5	7.5	−15.8	25
ASP	CB	B	123	30.0	8.8	−16.4	25
ASP	CG	B	123	31.4	8.8	−17.0	26
ASP	OD1	B	123	32.1	7.8	−16.8	21
ASP	OD2	B	123	31.7	9.8	−17.6	21
ASP	C	B	123	30.2	7.1	−14.5	27
ASP	O	B	123	29.6	7.1	−13.4	27
LEU	N	B	124	31.5	6.8	−14.5	26
LEU	CA	B	124	32.3	6.4	−13.3	27
LEU	CB	B	124	33.6	5.7	−13.6	25
LEU	CG	B	124	33.3	4.4	−14.5	26
LEU	CD1	B	124	34.6	3.7	−14.8	21
LEU	CD2	B	124	32.4	3.4	−13.8	25
LEU	C	B	124	32.6	7.6	−12.5	29
LEU	O	B	124	33.0	8.7	−13.0	30
VAL	N	B	125	32.3	7.5	−11.2	28
VAL	CA	B	125	32.4	8.6	−10.2	23
VAL	CB	B	125	31.1	9.2	−9.8	22
VAL	CG1	B	125	31.3	10.4	−8.8	19
VAL	CG2	B	125	30.3	9.7	−11.0	14
VAL	C	B	125	33.2	8.2	−8.9	26
VAL	O	B	125	32.9	7.1	−8.4	27
SER	N	B	126	34.1	9.0	−8.5	21
SER	CA	B	126	34.9	8.8	−7.3	28
SER	CB	B	126	36.2	8.1	−7.6	22
SER	OG	B	126	37.1	8.9	−8.4	31
SER	C	B	126	35.2	10.0	−6.5	28
SER	O	B	126	35.2	11.1	−7.1	27
ILE	N	B	127	35.4	9.9	−5.2	27
ILE	CA	B	127	35.7	11.0	−4.3	27
ILE	CB	B	127	34.7	11.0	−3.1	22
ILE	CG2	B	127	35.1	12.2	−2.2	23
ILE	CG1	B	127	33.3	11.1	−3.6	23
ILE	CD1	B	127	32.3	11.1	−2.4	27
ILE	C	B	127	37.1	10.7	−3.9	28
ILE	O	B	127	37.4	9.9	−3.0	28
PRO	N	B	128	38.1	11.5	−4.4	26
PRO	CD	B	128	38.0	12.3	−5.6	24
PRO	CA	B	128	39.5	11.4	−4.1	27
PRO	CB	B	128	40.1	12.6	−4.8	26
PRO	CG	B	128	39.5	12.5	−6.1	25
PRO	C	B	128	39.8	11.3	−2.6	28
PRO	O	B	128	40.7	10.5	−2.1	34
HIS	N	B	129	39.2	12.2	−1.8	28
HIS	CA	B	129	39.4	12.3	−0.4	28
HIS	CB	B	129	39.7	13.7	0.0	28
HIS	CG	B	129	40.9	14.3	−0.6	32
HIS	CD2	B	129	41.0	15.2	−1.6	34
HIS	ND1	B	129	42.2	13.9	−0.3	29
HIS	CE1	B	129	43.0	14.5	−1.1	32
HIS	NE2	B	129	42.4	15.3	−1.9	35
HIS	C	B	129	38.3	11.6	0.4	27
HIS	O	B	129	37.7	12.2	1.3	28
GLY	N	B	130	37.8	10.5	−0.1	31
GLY	CA	B	130	36.8	9.7	0.5	32
GLY	C	B	130	37.2	8.3	0.4	29
GLY	O	B	130	38.4	8.0	0.4	27
PRO	N	B	131	36.2	7.3	0.3	31
PRO	CD	B	131	34.8	7.5	0.0	31
PRO	CA	B	131	36.6	5.9	0.2	31
PRO	CB	B	131	35.2	5.2	0.4	31
PRO	CG	B	131	34.4	6.1	−0.5	35
PRO	C	B	131	37.3	5.5	−1.1	29
PRO	O	B	131	37.0	6.2	−2.1	29
ASN	N	B	132	38.2	4.6	−1.0	29
ASN	CA	B	132	38.9	4.1	−2.2	33
ASN	CB	B	132	40.1	3.2	−1.8	36
ASN	CG	B	132	39.7	2.0	−1.1	38
ASN	OD1	B	132	38.6	1.9	−0.6	42
ASN	ND2	B	132	40.6	1.0	−1.1	37
ASN	C	B	132	38.0	3.4	−3.2	32
ASN	O	B	132	38.4	2.3	−3.6	35
VAL	N	B	133	36.9	4.0	−3.6	28
VAL	CA	B	133	36.0	3.3	−4.5	27
VAL	CB	B	133	34.8	2.7	−3.8	25
VAL	CG1	B	133	35.2	1.7	−2.8	23
VAL	CG2	B	133	33.9	3.8	−3.2	27
VAL	C	B	133	35.5	4.2	−5.7	28
VAL	O	B	133	35.4	5.4	−5.6	28
THR	N	B	134	35.3	3.5	−6.8	26
THR	CA	B	134	34.8	4.1	−8.0	23
THR	CB	B	134	35.7	4.0	−9.2	23
THR	OG1	B	134	37.0	4.6	−8.9	23
THR	CG2	B	134	35.1	4.6	−10.5	22
THR	C	B	134	33.4	3.4	−8.3	26
THR	O	B	134	33.3	2.2	−8.2	26
VAL	N	B	135	32.4	4.2	−8.6	27
VAL	CA	B	135	31.1	3.7	−8.9	28
VAL	CB	B	135	30.2	3.8	−7.6	30
VAL	CG1	B	135	30.8	3.0	−6.5	29
VAL	CG2	B	135	29.9	5.2	−7.2	32
VAL	C	B	135	30.4	4.4	−10.0	30
VAL	O	B	135	30.6	5.6	−10.3	29
ARG	N	B	136	29.6	3.6	−10.8	30
ARG	CA	B	136	28.8	4.2	−11.8	28
ARG	CB	B	136	28.4	3.3	−13.0	27
ARG	CG	B	136	27.5	3.8	−14.0	25
ARG	CD	B	136	27.3	2.9	−15.2	24
ARG	NE	B	136	28.5	2.5	−15.8	20
ARG	CZ	B	136	29.1	3.3	−16.7	24
ARG	NH1	B	136	28.5	4.4	−17.1	25
ARG	NH2	B	136	30.3	2.9	−17.3	23
ARG	C	B	136	27.6	4.9	−11.2	27
ARG	O	B	136	26.9	4.3	−10.4	28
ALA	N	B	137	27.4	6.1	−11.5	23
ALA	CA	B	137	26.2	6.9	−11.0	24
ALA	CB	B	137	26.7	7.8	−9.8	15
ALA	C	B	137	25.6	7.7	−12.1	23
ALA	O	B	137	26.1	8.0	−13.1	23
ASN	N	B	138	24.3	8.1	−11.8	21
ASN	CA	B	138	23.6	9.0	−12.7	23
ASN	CB	B	138	22.1	9.0	−12.3	23
ASN	CG	B	138	21.5	7.7	−12.4	22
ASN	OD1	B	138	21.6	7.0	−13.5	25
ASN	ND2	B	138	20.8	7.2	−11.4	22
ASN	C	B	138	24.2	10.4	−12.5	28
ASN	O	B	138	24.6	10.8	−11.4	27
ILE	N	B	139	24.4	11.1	−13.7	26
ILE	CA	B	139	24.9	12.4	−13.7	26
ILE	CB	B	139	26.4	12.4	−14.2	26
ILE	CG2	B	139	26.9	13.8	−14.3	27
ILE	CG1	B	139	27.3	11.5	−13.3	22
ILE	CD1	B	139	28.7	11.5	−13.8	25
ILE	C	B	139	24.1	13.3	−14.6	30
ILE	O	B	139	23.9	13.0	−15.7	29
ALA	N	B	140	23.6	14.4	−14.0	29
ALA	CA	B	140	22.9	15.4	−14.8	27
ALA	CB	B	140	21.9	16.1	−13.9	25
ALA	C	B	140	23.9	16.4	−15.4	29
ALA	O	B	140	24.6	17.1	−14.6	28
ALA	N	B	141	24.0	16.4	−16.7	26
ALA	CA	B	141	25.0	17.2	−17.3	28
ALA	CB	B	141	25.3	16.7	−18.7	25
ALA	C	B	141	24.2	18.6	−17.5	28
ALA	O	B	141	23.3	18.7	−18.3	33
ILE	N	B	142	24.7	19.6	−16.8	27
ILE	CA	B	142	24.1	20.9	−16.8	26
ILE	CB	B	142	24.3	21.7	−15.6	24
ILE	CG2	B	142	23.7	23.1	−15.7	22
ILE	CG1	B	142	23.8	21.0	−14.3	19
ILE	CD1	B	142	24.1	21.7	−13.0	24
ILE	C	B	142	24.4	21.7	−18.1	27
ILE	O	B	142	25.6	22.0	−18.3	23
THR	N	B	143	23.4	22.0	−18.9	28
THR	CA	B	143	23.6	22.7	−20.2	29
THR	CB	B	143	22.9	22.0	−21.3	27
THR	OG1	B	143	21.5	21.8	−21.1	24
THR	CG2	B	143	23.6	20.6	−21.6	25
THR	C	B	143	23.1	24.2	−20.1	30
THR	O	B	143	23.5	25.0	−20.9	30
GLU	N	B	144	22.2	24.5	−19.2	35
GLU	CA	B	144	21.7	25.8	−19.0	39
GLU	CB	B	144	20.4	26.0	−19.8	47
GLU	CG	B	144	20.7	25.9	−21.3	61
GLU	CD	B	144	19.4	26.2	−22.1	72
GLU	OE1	B	144	18.9	25.3	−22.8	77
GLU	OE2	B	144	18.8	27.3	−21.9	76
GLU	C	B	144	21.4	26.0	−17.5	34
GLU	O	B	144	20.9	25.0	−16.9	34
SER	N	B	145	21.7	27.2	−17.0	30
SER	CA	B	145	21.4	27.4	−15.6	31
SER	CB	B	145	22.6	27.1	−14.7	29
SER	OG	B	145	23.7	27.9	−15.1	27
SER	C	B	145	21.0	28.9	−15.3	32
SER	O	B	145	21.4	29.8	−16.1	31
ASP	N	B	146	20.2	29.1	−14.3	31
ASP	CA	B	146	19.7	30.4	−14.0	32
ASP	CB	B	146	18.2	30.6	−14.3	39
ASP	CG	B	146	17.7	32.0	−14.1	46
ASP	OD1	B	146	18.5	32.9	−13.8	45
ASP	OD2	B	146	16.5	32.2	−14.2	52
ASP	C	B	146	19.9	30.6	−12.5	29
ASP	O	B	146	19.3	30.0	−11.6	28
LYS	N	B	147	20.9	31.5	−12.1	23
LYS	CA	B	147	21.2	31.8	−10.7	29
LYS	CB	B	147	20.0	32.5	−10.0	28
LYS	CG	B	147	19.6	33.9	−10.6	38
LYS	CD	B	147	18.5	34.5	−9.9	41
LYS	CE	B	147	18.1	35.8	−10.5	47
LYS	NZ	B	147	16.9	36.4	−9.8	55
LYS	C	B	147	21.7	30.6	−9.9	27
LYS	O	B	147	21.5	30.6	−8.7	25
PHE	N	B	148	22.2	29.6	−10.6	28
PHE	CA	B	148	22.7	28.4	−9.9	28
PHE	CB	B	148	22.5	27.2	−10.7	29
PHE	CG	B	148	23.0	25.9	−10.1	26
PHE	CD1	B	148	22.3	25.4	−9.0	26
PHE	CD2	B	148	24.1	25.2	−10.6	23
PHE	CE1	B	148	22.8	24.2	−8.4	26
PHE	CE2	B	148	24.6	24.1	−10.0	24
PHE	CZ	B	148	23.9	23.5	−8.9	26
PHE	C	B	148	24.2	28.7	−9.5	25
PHE	O	B	148	24.5	28.7	−8.4	28
PHE	N	B	149	25.0	28.8	−10.6	28
PHE	CA	B	149	26.4	29.0	−10.4	29
PHE	CB	B	149	27.2	28.8	−11.7	29
PHE	CG	B	149	27.0	27.4	−12.3	29
PHE	CD1	B	149	26.4	27.2	−13.5	27
PHE	CD2	B	149	27.4	26.3	−11.5	28
PHE	CE1	B	149	26.3	25.9	−14.0	28
PHE	CE2	B	149	27.2	25.0	−12.0	26
PHE	CZ	B	149	26.6	24.8	−13.3	27
PHE	C	B	149	26.8	30.4	−9.8	31
PHE	O	B	149	26.2	31.4	−10.1	30
ILE	N	B	150	27.8	30.4	−8.9	32
ILE	CA	B	150	28.3	31.6	−8.2	33
ILE	CB	B	150	28.3	31.4	−6.7	35
ILE	CG2	B	150	28.8	32.7	−6.1	34
ILE	CG1	B	150	27.0	31.0	−6.2	34
ILE	CD1	B	150	27.0	30.8	−4.7	36
ILE	C	B	150	29.7	32.0	−8.8	35
ILE	O	B	150	30.6	31.1	−8.8	33
ASN	N	B	151	29.8	33.2	−9.1	33
ASN	CA	B	151	31.1	33.7	−9.6	32
ASN	CB	B	151	31.0	35.2	−10.0	36
ASN	CG	B	151	32.3	35.8	−10.6	37
ASN	OD1	B	151	32.3	36.9	−11.2	37
ASN	ND2	B	151	33.4	35.1	−10.4	36
ASN	C	B	151	32.2	33.6	−8.6	35
ASN	O	B	151	32.1	34.2	−7.5	35
GLY	N	B	152	33.2	32.7	−8.8	34
GLY	CA	B	152	34.2	32.5	−7.9	31
GLY	C	B	152	34.0	31.6	−6.7	34
GLY	O	B	152	34.9	31.5	−5.8	31
SER	N	B	153	32.9	30.8	−6.7	31
SER	CA	B	153	32.7	29.9	−5.6	31
SER	CB	B	153	31.3	29.3	−5.7	27
SER	OG	B	153	31.1	28.5	−6.9	24
SER	C	B	153	33.7	28.7	−5.6	31
SER	O	B	153	33.9	28.1	−4.5	30
ASN	N	B	154	34.3	28.5	−6.7	26
ASN	CA	B	154	35.3	27.5	−6.9	29
ASN	CB	B	154	36.4	27.5	−5.9	29
ASN	CG	B	154	37.6	26.7	−6.3	35
ASN	OD1	B	154	37.8	26.4	−7.5	38
ASN	ND2	B	154	38.3	26.2	−5.3	37
ASN	C	B	154	34.7	26.1	−7.1	28
ASN	O	B	154	35.5	25.1	−7.0	29
TRP	N	B	155	33.4	26.0	−7.2	24
TRP	CA	B	155	32.8	24.7	−7.4	25
TRP	CB	B	155	31.9	24.2	−6.2	25
TRP	CG	B	155	30.8	25.2	−5.8	28
TRP	CD2	B	155	29.5	25.3	−6.4	23
TRP	CE2	B	155	28.7	26.2	−5.7	27
TRP	CE3	B	155	28.9	24.7	−7.5	24
TRP	CD1	B	155	30.7	26.0	−4.7	27
TRP	NE1	B	155	29.5	26.6	−4.6	26
TRP	CZ2	B	155	27.4	26.6	−6.0	26
TRP	CZ3	B	155	27.6	25.1	−7.9	20
TRP	CH2	B	155	26.9	26.0	−7.1	27
TRP	C	B	155	32.0	24.6	−8.7	28
TRP	O	B	155	31.4	25.6	−9.1	28
GLU	N	B	156	32.0	23.4	−9.4	23
GLU	CA	B	156	31.4	23.3	−10.7	22
GLU	CB	B	156	32.3	22.8	−11.8	26
GLU	CG	B	156	33.6	23.6	−12.1	26
GLU	CD	B	156	34.6	23.6	−10.9	24
GLU	OE1	B	156	34.9	24.7	−10.4	23
GLU	OE2	B	156	35.0	22.5	−10.4	24
GLU	C	B	156	30.1	22.4	−10.7	24
GLU	O	B	156	29.5	22.2	−11.7	22
GLY	N	B	157	29.8	21.8	−9.5	24
GLY	CA	B	157	28.7	20.9	−9.5	22
GLY	C	B	157	28.0	20.8	−8.1	24
GLY	O	B	157	28.3	21.6	−7.2	25
ILE	N	B	158	27.0	20.0	−8.0	23
ILE	CA	B	158	26.2	19.8	−6.8	23
ILE	CB	B	158	24.9	20.6	−6.9	26
ILE	CG2	B	158	24.0	20.1	−8.0	21
ILE	CG1	B	158	24.1	20.4	−5.6	22
ILE	CD1	B	158	22.9	21.2	−5.5	21
ILE	C	B	158	26.0	18.3	−6.6	26
ILE	O	B	158	25.6	17.5	−7.5	24
LEU	N	B	159	26.2	17.9	−5.3	21
LEU	CA	B	159	26.0	16.5	−4.9	20
LEU	CB	B	159	27.2	16.0	−4.2	20
LEU	CG	B	159	27.1	14.5	−3.7	22
LEU	CD1	B	159	26.9	13.6	−4.9	19
LEU	CD2	B	159	28.4	14.1	−3.0	16
LEU	C	B	159	24.7	16.4	−4.0	25
LEU	O	B	159	24.8	16.8	−2.9	24
GLY	N	B	160	23.6	15.9	−4.6	21
GLY	CA	B	160	22.4	15.8	−3.8	21
GLY	C	B	160	22.4	14.6	−3.0	24
GLY	O	B	160	22.3	13.4	−3.5	23
LEU	N	B	161	22.5	14.8	−1.7	22
LEU	CA	B	161	22.5	13.7	−0.7	19
LEU	CB	B	161	23.6	14.0	0.4	21
LEU	CG	B	161	25.0	14.1	−0.2	21
LEU	CD1	B	161	26.0	14.6	0.9	20
LEU	CD2	B	161	25.4	12.8	−0.8	21
LEU	C	B	161	21.2	13.2	−0.1	19
LEU	O	B	161	21.2	12.3	0.7	19
ALA	N	B	162	20.1	13.8	−0.4	17
ALA	CA	B	162	18.8	13.4	0.1	22
ALA	CB	B	162	17.8	14.6	0.2	20
ALA	C	B	162	18.2	12.2	−0.6	21
ALA	O	B	162	18.9	11.7	−1.5	20
TYR	N	B	163	17.0	11.8	−0.2	26
TYR	CA	B	163	16.4	10.6	−0.8	26
TYR	CB	B	163	15.3	10.1	0.2	23
TYR	CG	B	163	15.9	9.8	1.6	26
TYR	CD1	B	163	16.0	10.7	2.5	23
TYR	CE1	B	163	16.6	10.5	3.8	27
TYR	CD2	B	163	16.5	8.5	1.9	26
TYR	CE2	B	163	17.1	8.2	3.1	23
TYR	CZ	B	163	17.1	9.2	4.1	27
TYR	OH	B	163	17.7	9.0	5.3	24
TYR	C	B	163	15.8	10.7	−2.2	27
TYR	O	B	163	15.5	11.8	−2.7	24
ALA	N	B	164	15.7	9.5	−2.8	26
ALA	CA	B	164	15.2	9.5	−4.2	27
ALA	CB	B	164	15.1	8.0	−4.6	28
ALA	C	B	164	13.8	10.1	−4.3	26
ALA	O	B	164	13.4	10.5	−5.4	26
GLU	N	B	165	13.0	10.2	−3.2	30
GLU	CA	B	165	11.7	10.7	−3.2	31
GLU	CB	B	165	11.1	10.8	−1.8	39
GLU	CG	B	165	9.7	11.4	−1.7	46
GLU	CD	B	165	8.7	10.6	−2.5	53
GLU	OE1	B	165	7.7	10.1	−1.8	57
GLU	OE2	B	165	8.8	10.5	−3.7	57
GLU	C	B	165	11.6	12.1	−3.9	31
GLU	O	B	165	10.6	12.4	−4.5	29
ILE	N	B	166	12.7	12.9	−3.7	28
ILE	CA	B	166	12.7	14.2	−4.3	27
ILE	CB	B	166	13.0	15.3	−3.2	25
ILE	CG2	B	166	11.9	15.3	−2.1	22
ILE	CG1	B	166	14.4	15.0	−2.6	22
ILE	CD1	B	166	14.7	16.1	−1.5	18
ILE	C	B	166	13.6	14.4	−5.5	25
ILE	O	B	166	13.8	15.6	−5.9	24
ALA	N	B	167	14.1	13.3	−6.0	25
ALA	CA	B	167	14.9	13.4	−7.2	28
ALA	CB	B	167	15.7	12.0	−7.3	23
ALA	C	B	167	14.1	13.6	−8.5	28
ALA	O	B	167	13.0	13.2	−8.6	32
ARG	N	B	168	14.8	14.4	−9.4	31
ARG	CA	B	168	14.2	14.7	−10.7	29
ARG	CB	B	168	14.4	16.2	−11.1	34
ARG	CG	B	168	13.7	17.2	−10.2	38
ARG	CD	B	168	12.2	16.9	−10.1	40
ARG	NE	B	168	11.6	17.9	−9.3	44
ARG	CZ	B	168	11.3	19.2	−9.6	45
ARG	NH1	B	168	11.7	19.6	−10.8	44
ARG	NH2	B	168	10.7	20.0	−8.7	43
ARG	C	B	168	14.9	13.8	−11.7	27
ARG	O	B	168	16.1	13.5	−11.6	23
PRO	N	B	169	14.1	13.3	−12.8	28
PRO	CD	B	169	14.8	13.0	−14.0	25
PRO	CA	B	169	12.7	13.6	−13.1	24
PRO	CB	B	169	12.6	12.9	−14.4	25
PRO	CG	B	169	13.8	13.4	−15.1	27
PRO	C	B	169	11.8	13.0	−12.1	25
PRO	O	B	169	10.7	13.5	−11.8	31
ASP	N	B	170	12.2	11.9	−11.4	28
ASP	CA	B	170	11.3	11.2	−10.5	28
ASP	CB	B	170	10.1	10.5	−11.1	33
ASP	CG	B	170	10.5	9.5	−12.2	38
ASP	OD1	B	170	10.0	9.6	−13.3	40
ASP	OD2	B	170	11.4	8.6	−11.9	35
ASP	C	B	170	12.1	10.3	−9.5	29
ASP	O	B	170	13.3	10.1	−9.7	26
ASP	N	B	171	11.5	9.7	−8.6	28
ASP	CA	B	171	12.1	8.8	−7.6	32
ASP	CB	B	171	11.2	8.4	−6.5	38
ASP	CG	B	171	10.0	7.5	−6.9	40
ASP	OD1	B	171	10.0	7.1	−8.1	41
ASP	OD2	B	171	9.1	7.2	−6.1	43
ASP	C	B	171	12.9	7.6	−8.2	31
ASP	O	B	171	13.5	6.8	−7.4	33
SER	N	B	172	12.8	7.4	−9.5	30
SER	CA	B	172	13.5	6.3	−10.1	31
SER	CB	B	172	12.7	5.7	−11.2	32
SER	OG	B	172	12.6	6.6	−12.3	39
SER	C	B	172	14.9	6.6	−10.5	29
SER	O	B	172	15.7	5.7	−10.9	27
LEU	N	B	173	15.3	7.9	−10.4	28
LEU	CA	B	173	16.6	8.3	−10.7	28
LEU	CB	B	173	16.7	9.7	−11.2	25
LEU	CG	B	173	18.1	10.1	−11.7	26
LEU	CD1	B	173	18.4	9.2	−12.9	24
LEU	CD2	B	173	18.2	11.6	−12.1	29
LEU	C	B	173	17.4	8.1	−9.4	29
LEU	O	B	173	17.3	8.9	−8.5	24
GLU	N	B	174	18.2	7.0	−9.4	28
GLU	CA	B	174	18.9	6.7	−8.2	25
GLU	CB	B	174	19.6	5.3	−8.4	27
GLU	CG	B	174	20.4	4.8	−7.1	29
GLU	CD	B	174	21.0	3.4	−7.5	31
GLU	OE1	B	174	20.5	2.4	−6.9	33
GLU	OE2	B	174	22.0	3.4	−8.2	32
GLU	C	B	174	20.0	7.7	−7.8	22
GLU	O	B	174	20.8	8.1	−8.6	20
PRO	N	B	175	19.9	8.3	−6.5	25
PRO	CD	B	175	18.6	8.3	−5.8	26
PRO	CA	B	175	20.8	9.3	−6.0	21
PRO	CB	B	175	20.1	9.5	−4.6	22
PRO	CG	B	175	18.7	9.7	−5.0	26
PRO	C	B	175	22.2	8.7	−5.9	24
PRO	O	B	175	22.3	7.5	−5.7	28
PHE	N	B	176	23.2	9.5	−6.0	22
PHE	CA	B	176	24.6	9.1	−5.9	19
PHE	CB	B	176	25.5	10.3	−5.9	19
PHE	CG	B	176	27.0	9.9	−5.6	21
PHE	CD1	B	176	27.7	9.3	−6.6	24
PHE	CD2	B	176	27.5	10.1	−4.3	22
PHE	CE1	B	176	29.0	8.9	−6.3	22
PHE	CE2	B	176	28.8	9.6	−4.0	22
PHE	CZ	B	176	29.6	9.1	−5.0	20
PHE	C	B	176	24.9	8.2	−4.7	21
PHE	O	B	176	25.6	7.2	−4.8	18
PHE	N	B	177	24.4	8.7	−3.5	20
PHE	CA	B	177	24.8	7.9	−2.3	21
PHE	CB	B	177	24.5	8.8	−1.1	21
PHE	CG	B	177	25.1	8.2	0.2	22
PHE	CD1	B	177	26.4	8.5	0.5	18
PHE	CD2	B	177	24.4	7.3	1.0	22
PHE	CE1	B	177	27.1	8.0	1.6	19
PHE	CE2	B	177	25.0	6.8	2.1	22
PHE	CZ	B	177	26.3	7.1	2.5	18
PHE	C	B	177	24.2	6.6	−2.3	24
PHE	O	B	177	24.7	5.6	−1.7	28
ASP	N	B	178	23.0	6.4	−2.9	25
ASP	CA	B	178	22.3	5.1	−3.0	27
ASP	CB	B	178	20.9	5.2	−3.5	27
ASP	CG	B	178	20.0	6.0	−2.5	33
ASP	OD1	B	178	19.0	5.4	−2.0	31
ASP	OD2	B	178	20.2	7.2	−2.3	34
ASP	C	B	178	23.1	4.2	−3.9	26
ASP	O	B	178	23.3	3.0	−3.6	23
SER	N	B	179	23.7	4.8	−4.9	24
SER	CA	B	179	24.5	4.0	−5.9	23
SER	CB	B	179	24.8	4.7	−7.1	19
SER	OG	B	179	23.7	5.2	−7.8	24
SER	C	B	179	25.7	3.5	−5.1	25
SER	O	B	179	26.2	2.4	−5.3	24
LEU	N	B	180	26.3	4.4	−4.4	24
LEU	CA	B	180	27.5	4.2	−3.6	25
LEU	CB	B	180	28.0	5.4	−2.9	20
LEU	CG	B	180	29.2	5.1	−2.0	23
LEU	CD1	B	180	30.4	4.6	−2.9	19
LEU	CD2	B	180	29.7	6.4	−1.3	21
LEU	C	B	180	27.3	3.0	−2.7	24
LEU	O	B	180	28.2	2.1	−2.6	23
VAL	N	B	181	26.2	3.0	−1.9	23
VAL	CA	B	181	26.0	1.9	−1.0	24
VAL	CB	B	181	24.9	2.4	0.1	22
VAL	CG1	B	181	24.6	1.2	1.0	22
VAL	CG2	B	181	25.5	3.6	0.9	22
VAL	C	B	181	25.5	0.6	−1.6	26
VAL	O	B	181	25.8	−0.4	−1.1	28
LYS	N	B	182	24.9	0.7	−2.8	25
LYS	CA	B	182	24.4	−0.6	−3.4	29
LYS	CB	B	182	23.3	−0.3	−4.4	29
LYS	CG	B	182	22.8	−1.6	−5.1	32
LYS	CD	B	182	21.7	−1.3	−6.1	37
LYS	CE	B	182	22.1	−0.4	−7.3	37
LYS	NZ	B	182	21.0	−0.2	−8.3	35
LYS	C	B	182	25.6	−1.3	−4.1	27
LYS	O	B	182	25.5	−2.5	−4.2	33
GLN	N	B	183	26.6	−0.6	−4.5	25
GLN	CA	B	183	27.7	−1.2	−5.2	22
GLN	CB	B	183	28.1	−0.3	−6.4	23
GLN	CG	B	183	27.0	0.0	−7.4	22
GLN	CD	B	183	27.5	0.9	−8.5	21
GLN	OE1	B	183	28.7	1.0	−8.7	26
GLN	NE2	B	183	26.6	1.6	−9.1	27
GLN	C	B	183	28.9	−1.5	−4.3	21
GLN	O	B	183	29.8	−2.3	−4.7	19
THR	N	B	184	29.0	−0.9	−3.2	20
THR	CA	B	184	30.2	−1.1	−2.3	23
THR	CB	B	184	31.1	0.1	−2.3	26
THR	OG1	B	184	30.5	1.2	−1.6	24
THR	CG2	B	184	31.5	0.6	−3.7	27
THR	C	B	184	29.9	−1.5	−0.9	25
THR	O	B	184	28.7	−1.7	−0.6	26
HIS	N	B	185	30.9	−1.6	−0.1	22
HIS	CA	B	185	30.8	−1.9	1.3	30
HIS	CB	B	185	31.8	−2.9	1.8	33
HIS	CG	B	185	31.9	−4.2	1.1	38
HIS	CD2	B	185	30.9	−5.2	1.0	41
HIS	ND1	B	185	32.9	−4.6	0.3	39
HIS	CE1	B	185	32.6	−5.8	−0.2	41
HIS	NE2	B	185	31.4	−6.1	0.2	43
HIS	C	B	185	30.7	−0.7	2.2	25
HIS	O	B	185	30.7	−0.8	3.4	25
VAL	N	B	186	30.6	0.5	1.6	24
VAL	CA	B	186	30.5	1.8	2.3	22
VAL	CB	B	186	30.6	3.0	1.4	17
VAL	CG1	B	186	30.5	4.3	2.2	19
VAL	CG2	B	186	32.0	3.0	0.7	18
VAL	C	B	186	29.2	1.8	3.1	24
VAL	O	B	186	28.1	1.7	2.5	23
PRO	N	B	187	29.3	1.9	4.4	25
PRO	CD	B	187	30.5	1.7	5.2	23
PRO	CA	B	187	28.1	2.0	5.3	25
PRO	CB	B	187	28.8	2.3	6.7	25
PRO	CG	B	187	29.9	1.3	6.6	23
PRO	C	B	187	27.1	3.0	4.9	25
PRO	O	B	187	27.5	4.1	4.4	23
ASN	N	B	188	25.8	2.7	5.0	23
ASN	CA	B	188	24.8	3.7	4.6	22
ASN	CB	B	188	23.5	3.0	4.4	22
ASN	CG	B	188	22.4	3.9	3.9	25
ASN	OD1	B	188	22.7	5.0	3.4	28
ASN	ND2	B	188	21.1	3.5	4.0	23
ASN	C	B	188	24.7	4.8	5.7	23
ASN	O	B	188	23.8	4.8	6.4	25
LEU	N	B	189	25.8	5.6	5.7	21
LEU	CA	B	189	25.9	6.7	6.7	22
LEU	CB	B	189	26.0	6.1	8.1	29
LEU	CG	B	189	26.1	7.0	9.3	34
LEU	CD1	B	189	26.1	6.3	10.6	33
LEU	CD2	B	189	27.4	8.0	9.2	38
LEU	C	B	189	27.0	7.7	6.3	21
LEU	O	B	189	28.0	7.3	5.8	20
PHE	N	B	190	26.7	8.9	6.5	19
PHE	CA	B	190	27.7	10.0	6.3	20
PHE	CB	B	190	27.7	10.6	4.9	19
PHE	CG	B	190	26.4	11.3	4.6	21
PHE	CD1	B	190	25.3	10.7	4.0	19
PHE	CD2	B	190	26.3	12.7	4.8	21
PHE	CE1	B	190	24.2	11.4	3.7	21
PHE	CE2	B	190	25.2	13.4	4.5	18
PHE	CZ	B	190	24.1	12.8	4.0	18
PHE	C	B	190	27.6	11.0	7.4	19
PHE	O	B	190	26.5	11.2	8.0	20
SER	N	B	191	28.7	11.7	7.7	23
SER	CA	B	191	28.6	12.7	8.7	23
SER	CB	B	191	29.3	12.2	10.0	19
SER	OG	B	191	30.6	11.9	9.8	22
SER	C	B	191	29.3	14.0	8.2	22
SER	O	B	191	30.2	14.0	7.4	23
LEU	N	B	192	28.8	15.2	8.7	21
LEU	CA	B	192	29.3	16.5	8.3	24
LEU	CB	B	192	28.2	17.2	7.4	22
LEU	CG	B	192	27.9	16.6	6.1	23
LEU	CD1	B	192	26.8	17.3	5.4	16
LEU	CD2	B	192	29.2	16.5	5.2	19
LEU	C	B	192	29.7	17.4	9.4	22
LEU	O	B	192	29.0	17.6	10.4	20
GLN	N	B	193	31.0	17.9	9.3	24
GLN	CA	B	193	31.5	18.9	10.2	25
GLN	CB	B	193	32.8	18.5	10.8	27
GLN	CG	B	193	33.3	19.7	11.7	29
GLN	CD	B	193	34.7	19.3	12.3	30
GLN	OE1	B	193	35.7	19.4	11.7	30
GLN	NE2	B	193	34.7	18.9	13.6	30
GLN	C	B	193	31.8	20.2	9.3	26
GLN	O	B	193	32.7	20.2	8.6	21
LEU	N	B	194	30.9	21.2	9.4	24
LEU	CA	B	194	31.1	22.4	8.7	23
LEU	CB	B	194	29.7	22.9	8.1	26
LEU	CG	B	194	29.0	21.9	7.3	24
LEU	CD1	B	194	27.6	22.5	6.8	24
LEU	CD2	B	194	29.8	21.4	6.1	20
LEU	C	B	194	31.7	23.4	9.6	24
LEU	O	B	194	31.2	23.6	10.7	23
CYS	N	B	195	32.9	23.9	9.3	25
CYS	CA	B	195	33.5	24.8	10.2	33
CYS	C	B	195	33.4	26.3	10.0	39
CYS	O	B	195	33.3	27.1	10.9	47
CYS	CB	B	195	35.0	24.4	10.4	31
CYS	SG	B	195	35.2	22.7	11.0	32
GLY	N	B	196	33.3	26.7	8.7	44
GLY	CA	B	196	33.1	28.1	8.4	54
GLY	C	B	196	33.9	29.2	9.2	58
GLY	O	B	196	33.6	30.4	9.1	62
ALA	N	B	197	35.0	28.7	9.9	62
ALA	CA	B	197	35.8	29.7	10.6	64
ALA	CB	B	197	37.0	28.9	11.3	63
ALA	C	B	197	36.4	30.8	9.7	65
ALA	O	B	197	36.3	31.9	10.0	66
SER	N	B	209	39.0	30.5	3.6	49
SER	CA	B	209	37.8	31.0	4.3	53
SER	CB	B	209	36.8	31.6	3.2	55
SER	OG	B	209	37.4	32.6	2.5	61
SER	C	B	209	37.1	30.0	5.2	49
SER	O	B	209	37.1	30.2	6.4	55
VAL	N	B	210	36.5	29.0	4.6	44
VAL	CA	B	210	35.8	28.0	5.3	38
VAL	CB	B	210	34.3	28.2	5.2	36
VAL	CG1	B	210	33.8	29.6	5.7	39
VAL	CG2	B	210	33.7	27.9	3.8	36
VAL	C	B	210	36.2	26.6	4.9	34
VAL	O	B	210	36.5	26.4	3.7	39
GLY	N	B	211	36.2	25.7	5.8	31
GLY	CA	B	211	36.5	24.3	5.5	29
GLY	C	B	211	35.7	23.4	6.4	25
GLY	O	B	211	34.8	23.8	7.1	25
GLY	N	B	212	35.9	22.1	6.2	22
GLY	CA	B	212	35.2	21.1	7.0	22
GLY	C	B	212	35.5	19.7	6.6	23
GLY	O	B	212	36.4	19.4	5.8	21
SER	N	B	213	34.7	18.7	7.1	20
SER	CA	B	213	34.8	17.3	6.8	20
SER	CB	B	213	35.5	16.6	8.0	22
SER	OG	B	213	36.8	17.1	8.3	26
SER	C	B	213	33.5	16.6	6.5	21
SER	O	B	213	32.5	16.7	7.2	24
MET	N	B	214	33.6	15.8	5.4	20
MET	CA	B	214	32.4	15.0	5.1	23
MET	CB	B	214	31.9	15.2	3.7	23
MET	CG	B	214	30.8	14.3	3.3	25
MET	SD	B	214	30.0	14.5	1.7	27
MET	CE	B	214	31.5	14.3	0.6	27
MET	C	B	214	33.0	13.6	5.2	21
MET	O	B	214	33.8	13.1	4.4	22
ILE	N	B	215	32.6	12.9	6.2	19
ILE	CA	B	215	33.1	11.5	6.5	19
ILE	CB	B	215	33.2	11.2	8.0	20
ILE	CG2	B	215	33.8	9.8	8.1	13
ILE	CG1	B	215	34.1	12.2	8.7	20
ILE	CD1	B	215	35.6	12.3	8.1	20
ILE	C	B	215	32.1	10.6	5.8	22
ILE	O	B	215	30.9	10.5	6.3	21
ILE	N	B	216	32.5	9.9	4.7	22
ILE	CA	B	216	31.7	9.0	4.0	28
ILE	CB	B	216	32.0	9.0	2.5	30
ILE	CG2	B	216	31.1	8.0	1.8	28
ILE	CG1	B	216	32.0	10.3	1.9	30
ILE	CD1	B	216	30.7	11.0	1.9	39
ILE	C	B	216	31.7	7.6	4.6	26
ILE	O	B	216	32.8	7.0	4.7	29
GLY	N	B	217	30.5	7.1	5.0	27
GLY	CA	B	217	30.5	5.8	5.6	23
GLY	C	B	217	30.8	5.7	7.1	26
GLY	O	B	217	30.9	4.5	7.6	30
GLY	N	B	218	31.0	6.8	7.8	27
GLY	CA	B	218	31.3	6.7	9.2	28
GLY	C	B	218	31.3	7.9	10.0	32
GLY	O	B	218	30.9	9.0	9.6	30
ILE	N	B	219	31.7	7.7	11.3	30
ILE	CA	B	219	31.7	8.8	12.2	28
ILE	CB	B	219	30.8	8.5	13.4	26
ILE	CG2	B	219	30.9	9.6	14.5	26
ILE	CG1	B	219	29.4	8.3	12.9	24
ILE	CD1	B	219	28.4	8.0	14.0	21
ILE	C	B	219	33.2	9.0	12.8	30
ILE	O	B	219	33.7	8.0	13.3	35
ASP	N	B	220	33.7	10.2	12.7	29
ASP	CA	B	220	35.1	10.4	13.2	27
ASP	CB	B	220	36.0	11.2	12.2	26
ASP	CG	B	220	37.4	11.3	12.7	32
ASP	OD1	B	220	38.3	11.1	11.9	32
ASP	OD2	B	220	37.6	11.7	13.8	34
ASP	C	B	220	35.0	11.1	14.5	31
ASP	O	B	220	34.5	12.2	14.6	24
HIS	N	B	221	35.4	10.4	15.6	28
HIS	CA	B	221	35.2	10.9	16.9	30
HIS	CB	B	221	35.4	9.7	17.9	35
HIS	CG	B	221	34.3	8.7	17.7	38
HIS	CD2	B	221	34.4	7.4	17.2	40
HIS	ND1	B	221	33.0	8.9	18.0	41
HIS	CE1	B	221	32.3	7.8	17.7	40
HIS	NE2	B	221	33.1	6.9	17.2	40
HIS	C	B	221	36.1	12.1	17.3	31
HIS	O	B	221	35.9	12.6	18.4	34
SER	N	B	222	37.0	12.6	16.5	31
SER	CA	B	222	37.8	13.7	16.8	30
SER	CB	B	222	39.2	13.6	16.2	27
SER	OG	B	222	39.1	13.7	14.8	28
SER	C	B	222	37.1	15.0	16.4	29
SER	O	B	222	37.6	16.1	16.6	30
LEU	N	B	223	36.0	14.8	15.7	27
LEU	CA	B	223	35.2	16.0	15.2	29
LEU	CB	B	223	34.6	15.6	13.8	25
LEU	CG	B	223	35.6	15.1	12.8	26
LEU	CD1	B	223	34.8	14.7	11.5	22
LEU	CD2	B	223	36.6	16.2	12.5	23
LEU	C	B	223	34.2	16.6	16.1	27
LEU	O	B	223	33.7	17.6	15.9	27
TYR	N	B	224	34.0	15.9	17.3	24
TYR	CA	B	224	33.1	16.5	18.3	24
TYR	CB	B	224	31.7	15.9	18.1	26
TYR	CG	B	224	31.6	14.4	18.3	27
TYR	CD1	B	224	32.0	13.5	17.3	28
TYR	CE1	B	224	31.8	12.1	17.5	29
TYR	CD2	B	224	31.0	13.9	19.5	26
TYR	CE2	B	224	30.9	12.5	19.7	28
TYR	CZ	B	224	31.3	11.7	18.7	30
TYR	OH	B	224	31.1	10.3	18.9	31
TYR	C	B	224	33.5	16.2	19.7	27
TYR	O	B	224	34.5	15.4	19.9	24
THR	N	B	225	32.9	16.8	20.6	27
THR	CA	B	225	33.1	16.6	22.0	28
THR	CB	B	225	33.7	17.9	22.7	29
THR	OG1	B	225	32.8	19.0	22.6	27
THR	CG2	B	225	35.1	18.3	22.1	26
THR	C	B	225	31.8	16.3	22.6	28
THR	O	B	225	30.8	16.7	22.1	29
GLY	N	B	226	31.8	15.7	23.8	28
GLY	CA	B	226	30.5	15.3	24.4	25
GLY	C	B	226	29.8	14.2	23.8	28
GLY	O	B	226	30.3	13.4	23.1	28
SER	N	B	227	28.4	14.2	24.0	29
SER	CA	B	227	27.6	13.1	23.5	32
SER	CB	B	227	26.7	12.5	24.6	36
SER	OG	B	227	27.5	12.0	25.6	42
SER	C	B	227	26.8	13.3	22.2	29
SER	O	B	227	26.4	14.5	22.0	22
LEU	N	B	228	26.6	12.3	21.4	28
LEU	CA	B	228	25.8	12.4	20.2	28
LEU	CB	B	228	26.1	11.3	19.2	31
LEU	CG	B	228	27.5	11.4	18.5	34
LEU	CD1	B	228	27.8	10.2	17.6	33
LEU	CD2	B	228	27.5	12.7	17.7	34
LEU	C	B	228	24.3	12.2	20.6	27
LEU	O	B	228	24.0	11.2	21.2	30
TRP	N	B	229	23.5	13.1	20.2	24
TRP	CA	B	229	22.0	13.0	20.4	27
TRP	CB	B	229	21.4	14.1	21.2	23
TRP	CG	B	229	21.8	14.1	22.6	24
TRP	CD2	B	229	21.0	13.6	23.7	24
TRP	CE2	B	229	21.8	13.7	24.9	24
TRP	CE3	B	229	19.7	13.1	23.8	25
TRP	CD1	B	229	23.0	14.5	23.2	23
TRP	NE1	B	229	23.0	14.3	24.5	26
TRP	CZ2	B	229	21.3	13.4	26.2	27
TRP	CZ3	B	229	19.2	12.7	25.1	28
TRP	CH2	B	229	20.0	12.8	26.2	27
TRP	C	B	229	21.3	12.8	19.0	27
TRP	O	B	229	21.6	13.6	18.1	27
TYR	N	B	230	20.5	11.8	19.0	26
TYR	CA	B	230	19.7	11.5	17.8	27
TYR	CB	B	230	19.9	10.0	17.4	27
TYR	CG	B	230	21.3	9.6	17.1	24
TYR	CD1	B	230	22.1	9.2	18.1	23
TYR	CE1	B	230	23.5	8.9	17.8	24
TYR	CD2	B	230	21.8	9.7	15.8	20
TYR	CE2	B	230	23.1	9.3	15.5	17
TYR	CZ	B	230	23.9	8.9	16.5	22
TYR	OH	B	230	25.2	8.6	16.2	27
TYR	C	B	230	18.3	11.9	17.7	26
TYR	O	B	230	17.5	11.7	18.7	26
THR	N	B	231	17.9	12.5	16.6	26
THR	CA	B	231	16.5	12.9	16.4	23
THR	CB	B	231	16.4	14.4	16.1	18
THR	OG1	B	231	15.0	14.8	16.0	23
THR	CG2	B	231	17.0	14.8	14.8	20
THR	C	B	231	16.0	12.0	15.2	26
THR	O	B	231	16.8	11.8	14.2	26
PRO	N	B	232	14.8	11.5	15.2	24
PRO	CD	B	232	14.0	11.3	16.5	25
PRO	CA	B	232	14.2	10.7	14.2	28
PRO	CB	B	232	12.9	10.4	14.7	27
PRO	CG	B	232	13.2	10.0	16.1	29
PRO	C	B	232	14.1	11.4	12.8	28
PRO	O	B	232	13.7	12.5	12.7	30
ILE	N	B	233	14.5	10.7	11.7	28
ILE	CA	B	233	14.3	11.3	10.4	28
ILE	CB	B	233	15.1	10.6	9.3	27
ILE	CG2	B	233	14.6	11.0	7.9	27
ILE	CG1	B	233	16.6	10.9	9.5	21
ILE	CD1	B	233	17.5	10.3	8.5	14
ILE	C	B	233	12.8	10.9	10.2	30
ILE	O	B	233	12.4	9.8	10.1	29
ARG	N	B	234	11.9	11.9	10.1	33
ARG	CA	B	234	10.5	11.7	10.0	38
ARG	CB	B	234	9.7	13.0	10.2	35
ARG	CG	B	234	8.2	12.9	10.2	34
ARG	CD	B	234	7.5	14.2	10.4	36
ARG	NE	B	234	6.1	14.1	10.4	39
ARG	CZ	B	234	5.2	15.1	9.9	37
ARG	NH1	B	234	5.7	16.2	9.4	37
ARG	NH2	B	234	3.9	14.9	10.1	37
ARG	C	B	234	10.0	11.0	8.8	39
ARG	O	B	234	9.2	10.1	8.8	41
ARG	N	B	235	10.6	11.4	7.7	40
ARG	CA	B	235	10.3	10.9	6.3	39
ARG	CB	B	235	9.1	11.8	5.7	41
ARG	CG	B	235	8.8	11.4	4.3	38
ARG	CD	B	235	7.7	12.3	3.8	42
ARG	NE	B	235	7.4	12.0	2.4	44
ARG	CZ	B	235	6.8	12.8	1.5	47
ARG	NH1	B	235	6.4	14.0	2.0	47
ARG	NH2	B	235	6.5	12.5	0.3	53
ARG	C	B	235	11.5	10.9	5.4	36
ARG	O	B	235	12.2	11.9	5.4	36
GLU	N	B	236	11.7	9.8	4.7	32
GLU	CA	B	236	12.8	9.7	3.8	32
GLU	CB	B	236	13.3	8.3	3.6	36
GLU	CG	B	236	13.8	7.7	4.9	43
GLU	CD	B	236	14.2	6.2	4.7	46
GLU	OE1	B	236	13.8	5.4	5.5	51
GLU	OE2	B	236	14.9	6.0	3.8	52
GLU	C	B	236	12.6	10.4	2.4	32
GLU	O	B	236	12.2	9.8	1.4	32
TRP	N	B	237	12.8	11.7	2.4	30
TRP	CA	B	237	12.6	12.6	1.2	28
TRP	CB	B	237	11.2	13.1	1.0	27
TRP	CG	B	237	10.6	14.0	2.1	29
TRP	CD2	B	237	9.7	15.0	2.0	27
TRP	CE2	B	237	9.4	15.5	3.3	28
TRP	CE3	B	237	9.0	15.6	0.9	31
TRP	CD1	B	237	10.9	13.9	3.5	28
TRP	NE1	B	237	10.1	14.8	4.2	28
TRP	CZ2	B	237	8.4	16.6	3.5	29
TRP	CZ3	B	237	8.1	16.6	1.1	32
TRP	CH2	B	237	7.8	17.1	2.4	30
TRP	C	B	237	13.7	13.6	1.5	27
TRP	O	B	237	14.8	13.4	1.0	28
TYR	N	B	238	13.4	14.7	2.2	27
TYR	CA	B	238	14.5	15.7	2.6	24
TYR	CB	B	238	13.9	17.1	2.9	25
TYR	CG	B	238	13.3	17.8	1.7	23
TYR	CD1	B	238	14.1	18.5	0.8	20
TYR	CE1	B	238	13.5	19.2	−0.2	22
TYR	CD2	B	238	11.9	17.8	1.6	21
TYR	CE2	B	238	11.3	18.5	0.5	20
TYR	CZ	B	238	12.1	19.2	−0.3	22
TYR	OH	B	238	11.5	19.9	−1.4	26
TYR	C	B	238	14.9	15.0	3.9	24
TYR	O	B	238	14.2	14.0	4.3	23
TYR	N	B	239	15.9	15.5	4.5	28
TYR	CA	B	239	16.2	15.0	5.9	27
TYR	CB	B	239	17.7	15.1	6.3	25
TYR	CG	B	239	18.5	14.2	5.4	22
TYR	CD1	B	239	19.2	14.6	4.3	19
TYR	CE1	B	239	20.0	13.8	3.5	18
TYR	CD2	B	239	18.7	12.8	5.8	17
TYR	CE2	B	239	19.4	12.0	5.0	14
TYR	CZ	B	239	20.1	12.4	3.9	19
TYR	OH	B	239	20.8	11.5	3.2	16
TYR	C	B	239	15.3	15.8	6.8	29
TYR	O	B	239	15.6	16.9	7.3	28
GLU	N	B	240	14.1	15.3	7.0	30
GLU	CA	B	240	13.1	15.9	7.8	29
GLU	CB	B	240	11.6	15.7	7.3	28
GLU	CG	B	240	10.6	16.4	8.2	31
GLU	CD	B	240	9.2	16.1	7.6	32
GLU	OE1	B	240	9.1	15.3	6.7	36
GLU	OE2	B	240	8.3	16.7	8.1	36
GLU	C	B	240	13.1	15.6	9.3	27
GLU	O	B	240	13.2	14.4	9.7	31
VAL	N	B	241	13.1	16.6	10.1	24
VAL	CA	B	241	13.1	16.4	11.6	24
VAL	CB	B	241	14.4	16.9	12.2	27
VAL	CG1	B	241	15.6	16.1	11.6	22
VAL	CG2	B	241	14.7	18.4	11.9	21
VAL	C	B	241	11.9	17.2	12.2	24
VAL	O	B	241	11.2	17.9	11.5	20
ILE	N	B	242	11.7	17.0	13.5	23
ILE	CA	B	242	10.6	17.7	14.1	28
ILE	CB	B	242	9.5	16.7	14.6	29
ILE	CG2	B	242	8.5	17.4	15.4	28
ILE	CG1	B	242	8.9	16.0	13.4	33
ILE	CD1	B	242	7.9	15.0	13.8	32
ILE	C	B	242	11.1	18.5	15.3	26
ILE	O	B	242	11.7	18.0	16.3	25
ILE	N	B	243	10.9	19.8	15.3	28
ILE	CA	B	243	11.2	20.7	16.3	24
ILE	CB	B	243	11.6	22.1	15.8	24
ILE	CG2	B	243	11.9	23.1	16.9	21
ILE	CG1	B	243	12.7	22.0	14.8	25
ILE	CD1	B	243	13.1	23.4	14.1	23
ILE	C	B	243	10.1	20.8	17.3	25
ILE	O	B	243	8.9	21.1	16.9	26
VAL	N	B	244	10.3	20.6	18.6	24
VAL	CA	B	244	9.2	20.7	19.5	28
VAL	CB	B	244	9.2	19.3	20.3	30
VAL	CG1	B	244	9.0	18.1	19.4	26
VAL	CG2	B	244	10.4	19.2	21.2	28
VAL	C	B	244	9.2	21.8	20.5	29
VAL	O	B	244	8.2	22.0	21.3	31
ARG	N	B	245	10.2	22.7	20.5	29
ARG	CA	B	245	10.3	23.8	21.4	24
ARG	CB	B	245	10.6	23.4	22.8	26
ARG	CG	B	245	10.8	24.5	23.8	28
ARG	CD	B	245	11.1	23.9	25.2	26
ARG	NE	B	245	11.4	24.9	26.3	30
ARG	CZ	B	245	10.5	25.6	27.0	32
ARG	NH1	B	245	9.2	25.4	26.8	30
ARG	NH2	B	245	10.9	26.4	27.9	31
ARG	C	B	245	11.5	24.8	20.9	28
ARG	O	B	245	12.5	24.3	20.5	30
VAL	N	B	246	11.2	26.1	21.0	24
VAL	CA	B	246	12.2	27.1	20.7	21
VAL	CB	B	246	11.8	27.8	19.4	20
VAL	CG1	B	246	12.9	28.8	19.0	20
VAL	CG2	B	246	11.6	26.8	18.2	18
VAL	C	B	246	12.4	28.1	21.8	22
VAL	O	B	246	11.5	28.6	22.4	19
GLU	N	B	247	13.7	28.4	22.1	21
GLU	CA	B	247	14.1	29.3	23.1	22
GLU	CB	B	247	14.7	28.6	24.4	26
GLU	CG	B	247	13.7	27.6	25.1	28
GLU	CD	B	247	14.4	26.9	26.3	29
GLU	OE1	B	247	15.6	27.2	26.5	30
GLU	OE2	B	247	13.8	26.1	27.0	31
GLU	C	B	247	15.1	30.3	22.7	23
GLU	O	B	247	16.0	30.0	21.8	23
ILE	N	B	248	15.0	31.5	23.1	23
ILE	CA	B	248	16.0	32.6	22.8	22
ILE	CB	B	248	15.3	33.8	22.2	25
ILE	CG2	B	248	16.3	35.0	21.9	24
ILE	CG1	B	248	14.6	33.4	20.9	26
ILE	CD1	B	248	15.4	32.8	19.8	23
ILE	C	B	248	16.5	32.9	24.2	21
ILE	O	B	248	15.6	33.3	25.1	20
ASN	N	B	249	17.8	32.7	24.6	21
ASN	CA	B	249	18.2	32.9	26.0	18
ASN	CB	B	249	18.5	34.4	26.4	18
ASN	CG	B	249	19.9	34.8	25.9	16
ASN	OD1	B	249	20.7	34.0	25.4	17
ASN	ND2	B	249	20.2	36.1	26.1	15
ASN	C	B	249	17.3	32.3	27.0	17
ASN	O	B	249	17.0	32.9	28.0	20
GLY	N	B	250	16.9	31.1	26.8	21
GLY	CA	B	250	16.1	30.4	27.7	18
GLY	C	B	250	14.6	30.8	27.7	22
GLY	O	B	250	13.8	30.1	28.4	23
GLN	N	B	251	14.2	31.8	27.0	24
GLN	CA	B	251	12.8	32.2	27.0	28
GLN	CB	B	251	12.7	33.8	27.0	23
GLN	CG	B	251	11.2	34.2	27.1	29
GLN	CD	B	251	11.1	35.7	27.0	33
GLN	OE1	B	251	12.0	36.4	26.6	38
GLN	NE2	B	251	9.9	36.2	27.4	32
GLN	C	B	251	12.0	31.5	26.0	23
GLN	O	B	251	12.3	31.7	24.8	24
ASP	N	B	252	11.1	30.7	26.4	25
ASP	CA	B	252	10.2	30.0	25.5	26
ASP	CB	B	252	9.1	29.3	26.4	27
ASP	CG	B	252	8.2	28.4	25.5	29
ASP	OD1	B	252	8.4	28.2	24.3	31
ASP	OD2	B	252	7.2	27.9	26.1	33
ASP	C	B	252	9.6	30.9	24.5	25
ASP	O	B	252	9.0	32.0	24.8	24
LEU	N	B	253	9.7	30.5	23.2	25
LEU	CA	B	253	9.2	31.4	22.2	30
LEU	CB	B	253	9.8	30.9	20.8	31
LEU	CG	B	253	9.5	31.9	19.7	35
LEU	CD1	B	253	9.9	33.3	20.0	32
LEU	CD2	B	253	10.1	31.4	18.4	31
LEU	C	B	253	7.6	31.2	22.2	32
LEU	O	B	253	6.9	32.0	21.6	31
LYS	N	B	254	7.2	30.3	23.0	33
LYS	CA	B	254	5.8	29.9	23.3	40
LYS	CB	B	254	5.3	30.8	24.5	46
LYS	CG	B	254	3.9	30.6	25.0	52
LYS	CD	B	254	3.6	31.5	26.1	56
LYS	CE	B	254	2.2	31.2	26.7	60
LYS	NZ	B	254	1.8	32.1	27.8	62
LYS	C	B	254	4.8	29.9	22.1	42
LYS	O	B	254	3.7	30.4	22.2	45
MET	N	B	255	5.1	29.2	21.1	41
MET	CA	B	255	4.3	29.0	19.9	39
MET	CB	B	255	5.0	29.4	18.6	37
MET	CG	B	255	5.4	30.9	18.5	35
MET	SD	B	255	6.2	31.1	16.9	36
MET	CE	B	255	4.8	31.3	15.8	38
MET	C	B	255	3.8	27.5	19.8	42
MET	O	B	255	4.5	26.7	20.3	39
ASP	N	B	256	2.7	27.3	19.2	45
ASP	CA	B	256	2.2	25.9	18.9	45
ASP	CB	B	256	0.9	25.9	18.0	52
ASP	CG	B	256	0.4	24.5	17.7	56
ASP	OD1	B	256	1.1	23.6	18.1	60
ASP	OD2	B	256	−0.6	24.4	17.0	61
ASP	C	B	256	3.4	25.3	18.2	40
ASP	O	B	256	3.8	25.8	17.1	38
CYS	N	B	257	3.9	24.2	18.7	36
CYS	CA	B	257	5.1	23.6	18.1	38
CYS	C	B	257	4.9	23.3	16.7	38
CYS	O	B	257	5.9	23.0	15.9	39
CYS	CB	B	257	5.6	22.4	18.9	37
CYS	SG	B	257	4.3	21.1	19.0	45
LYS	N	B	258	3.7	23.2	16.2	39
LYS	CA	B	258	3.4	22.9	14.8	37
LYS	CB	B	258	2.0	22.4	14.7	39
LYS	CG	B	258	1.6	22.0	13.3	45
LYS	CD	B	258	0.1	21.6	13.3	48
LYS	CE	B	258	−0.1	20.4	14.2	50
LYS	NZ	B	258	−1.5	19.9	14.3	52
LYS	C	B	258	3.8	24.0	13.9	36
LYS	O	B	258	4.1	23.8	12.7	34
GLU	N	B	259	4.0	25.2	14.4	34
GLU	CA	B	259	4.4	26.4	13.6	32
GLU	CB	B	259	4.1	27.7	14.3	33
GLU	CG	B	259	2.7	28.0	14.6	36
GLU	CD	B	259	1.9	28.2	13.3	42
GLU	OE1	B	259	2.5	28.2	12.3	43
GLU	OE2	B	259	0.6	28.3	13.4	43
GLU	C	B	259	5.9	26.3	13.3	31
GLU	O	B	259	6.4	26.8	12.3	30
TYR	N	B	260	6.6	25.6	14.1	28
TYR	CA	B	260	8.1	25.4	14.0	27
TYR	CB	B	260	8.7	24.8	15.3	20
TYR	CG	B	260	8.4	25.7	16.5	20
TYR	CD1	B	260	8.2	25.0	17.7	21
TYR	CE1	B	260	8.0	25.8	18.9	19
TYR	CD2	B	260	8.5	27.0	16.5	16
TYR	CE2	B	260	8.3	27.8	17.6	17
TYR	CZ	B	260	8.1	27.2	18.8	21
TYR	OH	B	260	7.9	27.9	20.0	21
TYR	C	B	260	8.4	24.4	12.8	30
TYR	O	B	260	9.5	24.3	12.4	30
ASN	N	B	261	7.3	23.7	12.4	32
ASN	CA	B	261	7.5	22.7	11.4	33
ASN	CB	B	261	7.3	21.3	12.0	32
ASN	CG	B	261	8.3	21.1	13.1	33
ASN	OD1	B	261	9.5	21.3	13.0	30
ASN	ND2	B	261	7.8	20.6	14.3	34
ASN	C	B	261	6.5	22.9	10.2	31
ASN	O	B	261	6.3	21.9	9.4	29
TYR	N	B	262	6.0	24.1	10.0	32
TYR	CA	B	262	5.1	24.4	9.0	34
TYR	CB	B	262	4.1	25.5	9.4	37
TYR	CG	B	262	3.2	26.0	8.4	42
TYR	CD1	B	262	2.3	25.1	7.7	41
TYR	CE1	B	262	1.4	25.6	6.7	46
TYR	CD2	B	262	3.1	27.3	8.0	43
TYR	CE2	B	262	2.3	27.8	7.1	46
TYR	CZ	B	262	1.4	26.9	6.4	47
TYR	OH	B	262	0.6	27.4	5.4	48
TYR	C	B	262	5.9	25.0	7.8	34
TYR	O	B	262	6.5	26.0	7.8	37
ASP	N	B	263	5.9	24.3	6.6	32
ASP	CA	B	263	5.2	23.0	6.5	35
ASP	CB	B	263	4.5	22.9	5.1	39
ASP	CG	B	263	5.5	23.0	3.9	44
ASP	OD1	B	263	6.7	23.2	4.1	46
ASP	OD2	B	263	5.0	22.9	2.8	48
ASP	C	B	263	6.2	21.8	6.7	34
ASP	O	B	263	5.8	20.6	6.6	31
LYS	N	B	264	7.4	22.1	7.0	30
LYS	CA	B	264	8.4	21.1	7.3	30
LYS	CB	B	264	8.7	20.3	6.0	27
LYS	CG	B	264	9.3	21.1	4.9	26
LYS	CD	B	264	9.6	20.2	3.7	24
LYS	CE	B	264	10.2	21.1	2.6	31
LYS	NZ	B	264	9.3	22.1	2.1	31
LYS	C	B	264	9.7	21.7	7.8	27
LYS	O	B	264	9.9	22.9	7.7	29
SER	N	B	265	10.5	20.8	8.5	23
SER	CA	B	265	11.8	21.2	9.1	26
SER	CB	B	265	11.8	21.2	10.6	25
SER	OG	B	265	10.9	22.2	11.1	28
SER	C	B	265	12.8	20.3	8.5	23
SER	O	B	265	12.7	19.1	8.6	24
ILE	N	B	266	13.8	20.8	7.8	24
ILE	CA	B	266	14.9	20.0	7.2	24
ILE	CB	B	266	14.8	20.0	5.7	23
ILE	CG2	B	266	13.4	19.5	5.3	21
ILE	CG1	B	266	15.1	21.3	5.1	26
ILE	CD1	B	266	15.1	21.4	3.5	22
ILE	C	B	266	16.3	20.5	7.6	25
ILE	O	B	266	16.5	21.6	8.0	20
VAL	N	B	267	17.2	19.6	7.4	22
VAL	CA	B	267	18.6	19.9	7.7	26
VAL	CB	B	267	19.3	18.8	8.5	24
VAL	CG1	B	267	20.8	19.2	8.8	28
VAL	CG2	B	267	18.6	18.5	9.8	18
VAL	C	B	267	19.2	20.0	6.3	29
VAL	O	B	267	19.3	19.0	5.6	26
ASP	N	B	268	19.7	21.2	6.0	27
ASP	CA	B	268	20.3	21.4	4.6	25
ASP	CB	B	268	19.3	22.2	3.8	23
ASP	CG	B	268	19.7	22.4	2.4	26
ASP	OD1	B	268	20.7	21.8	2.0	24
ASP	OD2	B	268	19.2	23.3	1.7	29
ASP	C	B	268	21.7	22.1	4.6	21
ASP	O	B	268	21.8	23.3	4.8	24
SER	N	B	269	22.7	21.3	4.2	20
SER	CA	B	269	24.0	21.8	4.1	16
SER	CB	B	269	25.0	20.6	3.9	17
SER	OG	B	269	24.7	19.9	2.7	18
SER	C	B	269	24.2	22.8	3.0	18
SER	O	B	269	25.2	23.5	2.9	17
GLY	N	B	270	23.2	22.8	2.1	18
GLY	CA	B	270	23.3	23.7	0.9	18
GLY	C	B	270	22.6	25.0	1.2	19
GLY	O	B	270	22.4	25.8	0.2	21
THR	N	B	271	22.2	25.3	2.4	17
THR	CA	B	271	21.6	26.5	2.8	20
THR	CB	B	271	20.2	26.4	3.4	20
THR	OG1	B	271	19.3	25.8	2.4	22
THR	CG2	B	271	19.6	27.7	3.9	19
THR	C	B	271	22.5	27.3	3.8	19
THR	O	B	271	22.9	26.7	4.8	20
THR	N	B	272	22.8	28.5	3.5	24
THR	CA	B	272	23.6	29.4	4.3	22
THR	CB	B	272	24.0	30.7	3.7	21
THR	OG1	B	272	24.6	30.4	2.4	25
THR	CG2	B	272	24.9	31.5	4.6	22
THR	C	B	272	23.0	29.7	5.7	21
THR	O	B	272	23.6	29.5	6.7	21
ASN	N	B	273	21.7	30.2	5.7	24
ASN	CA	B	273	21.0	30.6	6.9	21
ASN	CB	B	273	20.1	31.7	6.5	23
ASN	CG	B	273	20.8	32.9	6.0	23
ASN	OD1	B	273	22.1	32.9	5.9	22
ASN	ND2	B	273	20.1	34.0	5.7	24
ASN	C	B	273	20.2	29.5	7.6	22
ASN	O	B	273	20.1	28.4	7.2	21
LEU	N	B	274	19.6	30.1	8.7	20
LEU	CA	B	274	18.7	29.4	9.5	24
LEU	CB	B	274	18.8	29.7	11.0	21
LEU	CG	B	274	17.7	29.1	11.8	20
LEU	CD1	B	274	17.6	27.5	11.7	17
LEU	CD2	B	274	17.9	29.4	13.3	19
LEU	C	B	274	17.4	30.0	9.0	26
LEU	O	B	274	17.2	31.2	9.1	21
ARG	N	B	275	16.6	29.2	8.2	23
ARG	CA	B	275	15.4	29.8	7.7	23
ARG	CB	B	275	15.2	29.6	6.2	25
ARG	CG	B	275	16.4	30.2	5.5	29
ARG	CD	B	275	16.3	30.1	4.0	32
ARG	NE	B	275	15.1	30.8	3.6	35
ARG	CZ	B	275	14.9	31.4	2.4	35
ARG	NH1	B	275	13.8	32.0	2.2	34
ARG	NH2	B	275	15.9	31.4	1.6	37
ARG	C	B	275	14.2	29.3	8.6	25
ARG	O	B	275	14.1	28.2	8.9	22
LEU	N	B	276	13.4	30.3	8.9	24
LEU	CA	B	276	12.2	30.1	9.7	25
LEU	CB	B	276	12.3	30.9	11.1	23
LEU	CG	B	276	13.5	30.5	11.9	24
LEU	CD1	B	276	13.7	31.4	13.1	22
LEU	CD2	B	276	13.5	29.0	12.3	23
LEU	C	B	276	10.9	30.5	9.1	25
LEU	O	B	276	10.8	31.5	8.4	27
PRO	N	B	277	9.8	29.7	9.3	28
PRO	CD	B	277	9.9	28.3	9.8	30
PRO	CA	B	277	8.5	29.9	8.7	30
PRO	CB	B	277	7.7	28.9	9.4	32
PRO	CG	B	277	8.6	27.7	9.2	33
PRO	C	B	277	8.1	31.3	9.1	31
PRO	O	B	277	8.3	31.7	10.3	31
LYS	N	B	278	7.6	32.1	8.2	34
LYS	CA	B	278	7.1	33.5	8.5	36
LYS	CB	B	278	6.0	33.9	7.5	41
LYS	CG	B	278	5.4	35.3	7.8	47
LYS	CD	B	278	6.5	36.4	7.6	53
LYS	CE	B	278	5.9	37.8	7.8	57
LYS	NZ	B	278	7.0	38.8	7.6	55
LYS	C	B	278	6.7	33.9	9.9	33
LYS	O	B	278	7.4	34.7	10.5	32
LYS	N	B	279	5.7	33.2	10.5	32
LYS	CA	B	279	5.3	33.5	11.8	37
LYS	CB	B	279	4.0	32.7	12.2	40
LYS	CG	B	279	2.8	33.1	11.3	51
LYS	CD	B	279	1.6	32.2	11.7	54
LYS	CE	B	279	1.2	32.5	13.2	57
LYS	NZ	B	279	0.0	31.6	13.5	62
LYS	C	B	279	6.4	33.2	12.9	33
LYS	O	B	279	6.4	33.9	13.9	32
VAL	N	B	280	7.2	32.3	12.7	29
VAL	CA	B	280	8.3	31.9	13.6	26
VAL	CB	B	280	8.8	30.5	13.5	24
VAL	CG1	B	280	9.9	30.2	14.5	25
VAL	CG2	B	280	7.6	29.5	13.6	23
VAL	C	B	280	9.4	32.9	13.5	26
VAL	O	B	280	10.1	33.3	14.5	27
PHE	N	B	281	9.7	33.4	12.3	24
PHE	CA	B	281	10.7	34.3	12.1	29
PHE	CB	B	281	10.9	34.6	10.6	28
PHE	CG	B	281	12.0	35.6	10.3	29
PHE	CD1	B	281	13.3	35.3	10.4	31
PHE	CD2	B	281	11.6	36.9	9.9	28
PHE	CE1	B	281	14.3	36.2	10.2	31
PHE	CE2	B	281	12.6	37.8	9.6	32
PHE	CZ	B	281	14.0	37.5	9.8	31
PHE	C	B	281	10.4	35.6	12.8	31
PHE	O	B	281	11.2	36.2	13.5	29
GLU	N	B	282	9.1	36.1	12.6	34
GLU	CA	B	282	8.6	37.3	13.2	36
GLU	CB	B	282	7.2	37.6	12.8	41
GLU	CG	B	282	6.9	37.8	11.3	54
GLU	CD	B	282	7.7	38.9	10.7	62
GLU	OE1	B	282	7.1	39.9	10.2	69
GLU	OE2	B	282	9.0	38.9	10.7	65
GLU	C	B	282	8.7	37.2	14.7	33
GLU	O	B	282	9.1	38.2	15.3	34
ALA	N	B	283	8.5	36.1	15.3	29
ALA	CA	B	283	8.5	35.9	16.7	27
ALA	CB	B	283	7.7	34.7	17.1	26
ALA	C	B	283	10.0	35.8	17.2	31
ALA	O	B	283	10.3	36.2	18.3	34
ALA	N	B	284	10.8	35.2	16.4	28
ALA	CA	B	284	12.2	35.0	16.8	27
ALA	CB	B	284	12.9	33.9	15.9	22
ALA	C	B	284	13.0	36.3	16.7	26
ALA	O	B	284	13.7	36.6	17.6	26
VAL	N	B	285	12.7	37.1	15.7	24
VAL	CA	B	285	13.4	38.4	15.5	27
VAL	CB	B	285	13.2	39.0	14.1	27
VAL	CG1	B	285	13.9	40.3	14.0	32
VAL	CG2	B	285	13.8	38.0	13.0	32
VAL	C	B	285	13.0	39.4	16.6	27
VAL	O	B	285	13.7	40.2	17.0	28
LYS	N	B	286	11.7	39.3	16.9	26
LYS	CA	B	286	11.2	40.2	18.0	24
LYS	CB	B	286	9.7	40.1	18.1	25
LYS	CG	B	286	9.1	41.0	19.2	28
LYS	CD	B	286	7.6	40.9	19.4	30
LYS	CE	B	286	7.1	41.8	20.4	37
LYS	NZ	B	286	5.6	41.7	20.6	41
LYS	C	B	286	11.9	39.9	19.3	25
LYS	O	B	286	12.3	40.8	20.0	23
SER	N	B	287	12.0	38.6	19.6	22
SER	CA	B	287	12.7	38.2	20.8	21
SER	CB	B	287	12.4	36.8	21.1	22
SER	OG	B	287	13.0	36.3	22.3	24
SER	C	B	287	14.2	38.4	20.8	23
SER	O	B	287	14.8	38.7	21.8	27
ILE	N	B	288	14.8	38.3	19.6	24
ILE	CA	B	288	16.2	38.5	19.4	26
ILE	CB	B	288	16.8	37.9	18.2	27
ILE	CG2	B	288	18.2	38.3	18.0	24
ILE	CG1	B	288	16.5	36.4	18.2	24
ILE	CD1	B	288	17.0	35.7	16.9	23
ILE	C	B	288	16.6	40.0	19.5	27
ILE	O	B	288	17.7	40.4	20.0	30
LYS	N	B	289	15.6	40.9	19.2	26
LYS	CA	B	289	15.9	42.3	19.3	25
LYS	CB	B	289	14.9	43.2	18.4	25
LYS	CG	B	289	14.9	42.9	16.9	32
LYS	CD	B	289	13.9	43.9	16.3	33
LYS	CE	B	289	13.9	43.7	14.8	37
LYS	NZ	B	289	12.8	44.7	14.2	38
LYS	C	B	289	15.8	42.8	20.7	23
LYS	O	B	289	16.6	43.6	21.2	25
ALA	N	B	290	14.8	42.2	21.4	18
ALA	CA	B	290	14.6	42.6	22.8	22
ALA	CB	B	290	13.3	41.9	23.3	13
ALA	C	B	290	15.8	42.2	23.7	20
ALA	O	B	290	16.1	42.9	24.6	21
ALA	N	B	291	16.3	41.0	23.4	20
ALA	CA	B	291	17.5	40.5	24.2	24
ALA	CB	B	291	17.7	39.0	23.9	21
ALA	C	B	291	18.7	41.3	23.9	22
ALA	O	B	291	19.6	41.4	24.8	24
SER	N	B	292	18.9	41.8	22.7	23
SER	CA	B	292	20.0	42.6	22.3	26
SER	CB	B	292	20.5	42.2	20.9	27
SER	OG	B	292	19.5	42.4	19.9	28
SER	C	B	292	19.8	44.1	22.4	26
SER	O	B	292	20.7	44.9	21.9	25
SER	N	B	293	18.7	44.5	22.9	25
SER	CA	B	293	18.3	45.9	23.0	27
SER	CB	B	293	16.9	46.0	23.7	27
SER	OG	B	293	16.9	45.5	25.0	35
SER	C	B	293	19.2	46.9	23.6	30
SER	O	B	293	19.0	48.1	23.6	31
THR	N	B	294	20.4	46.5	24.2	29
THR	CA	B	294	21.3	47.5	24.7	30
THR	CB	B	294	22.4	46.9	25.7	31
THR	OG1	B	294	23.2	46.0	24.9	32
THR	CG2	B	294	21.8	46.3	26.9	34
THR	C	B	294	21.9	48.2	23.6	28
THR	O	B	294	22.6	49.2	23.7	26
GLU	N	B	295	21.7	47.7	22.4	29
GLU	CA	B	295	22.2	48.4	21.2	34
GLU	CB	B	295	23.6	47.9	20.8	32
GLU	CG	B	295	24.0	48.6	19.5	36
GLU	CD	B	295	25.4	48.1	19.1	42
GLU	OE1	B	295	26.1	47.4	19.9	46
GLU	OE2	B	295	25.8	48.4	18.0	43
GLU	C	B	295	21.2	48.2	20.1	34
GLU	O	B	295	20.7	47.1	19.8	38
LYS	N	B	296	20.8	49.3	19.5	34
LYS	CA	B	296	19.8	49.3	18.4	33
LYS	CB	B	296	18.8	50.5	18.6	38
LYS	CG	B	296	17.7	50.6	17.6	47
LYS	CD	B	296	16.8	51.8	17.9	52
LYS	CE	B	296	15.6	51.9	16.9	56
LYS	NZ	B	296	14.7	53.1	17.3	60
LYS	C	B	296	20.4	49.3	17.0	27
LYS	O	B	296	21.3	50.1	16.7	28
PHE	N	B	297	20.0	48.4	16.1	21
PHE	CA	B	297	20.5	48.3	14.8	24
PHE	CB	B	297	21.0	46.9	14.5	23
PHE	CG	B	297	22.0	46.4	15.5	24
PHE	CD1	B	297	21.6	45.6	16.6	22
PHE	CD2	B	297	23.3	46.7	15.4	26
PHE	CE1	B	297	22.5	45.1	17.5	27
PHE	CE2	B	297	24.2	46.3	16.3	24
PHE	CZ	B	297	23.8	45.5	17.4	25
PHE	C	B	297	19.5	48.7	13.7	26
PHE	O	B	297	18.3	48.7	13.9	27
PRO	N	B	298	20.0	49.2	12.5	25
PRO	CD	B	298	21.4	49.5	12.3	25
PRO	CA	B	298	19.3	49.6	11.4	26
PRO	CB	B	298	20.3	49.8	10.3	27
PRO	CG	B	298	21.4	50.5	11.1	26
PRO	C	B	298	18.3	48.5	11.0	26
PRO	O	B	298	18.6	47.3	11.1	24
ASP	N	B	299	17.1	48.8	10.5	27
ASP	CA	B	299	16.2	47.8	10.1	32
ASP	CB	B	299	14.8	48.3	9.8	38
ASP	CG	B	299	14.1	49.0	10.9	44
ASP	OD1	B	299	14.7	49.0	12.0	46
ASP	OD2	B	299	12.9	49.4	10.8	45
ASP	C	B	299	16.7	46.9	9.0	34
ASP	O	B	299	16.4	45.8	8.8	35
GLY	N	B	300	17.6	47.5	8.2	34
GLY	CA	B	300	18.2	46.8	7.1	31
GLY	C	B	300	18.9	45.5	7.6	34
GLY	O	B	300	18.9	44.5	7.0	32
PHE	N	B	301	19.6	45.7	8.8	30
PHE	CA	B	301	20.3	44.6	9.4	30
PHE	CB	B	301	20.9	45.0	10.8	30
PHE	CG	B	301	21.5	43.9	11.5	29
PHE	CD1	B	301	22.7	43.3	11.1	30
PHE	CD2	B	301	21.0	43.5	12.7	27
PHE	CE1	B	301	23.3	42.3	11.8	29
PHE	CE2	B	301	21.6	42.5	13.5	29
PHE	CZ	B	301	22.8	41.9	13.0	27
PHE	C	B	301	19.4	43.4	9.7	30
PHE	O	B	301	19.7	42.3	9.2	26
TRP	N	B	302	18.3	43.6	10.4	30
TRP	CA	B	302	17.4	42.5	10.7	28
TRP	CB	B	302	16.3	42.9	11.7	29
TRP	CG	B	302	16.9	43.4	12.9	26
TRP	CD2	B	302	17.5	42.7	14.0	23
TRP	CE2	B	302	17.9	43.6	15.0	23
TRP	CE3	B	302	17.8	41.3	14.1	22
TRP	CD1	B	302	16.9	44.7	13.4	26
TRP	NE1	B	302	17.6	44.8	14.6	23
TRP	CZ2	B	302	18.6	43.1	16.1	22
TRP	CZ3	B	302	18.5	40.9	15.3	22
TRP	CH2	B	302	18.9	41.8	16.3	23
TRP	C	B	302	16.8	41.8	9.5	30
TRP	O	B	302	16.3	40.7	9.5	24
LEU	N	B	303	16.9	42.5	8.3	28
LEU	CA	B	303	16.3	42.0	7.1	30
LEU	CB	B	303	15.7	43.1	6.2	33
LEU	CG	B	303	14.6	43.8	6.9	33
LEU	CD1	B	303	14.1	45.0	6.0	34
LEU	CD2	B	303	13.4	42.9	7.2	30
LEU	C	B	303	17.4	41.3	6.3	29
LEU	O	B	303	17.2	40.7	5.2	28
GLY	N	B	304	18.6	41.3	6.8	28
GLY	CA	B	304	19.7	40.7	6.1	31
GLY	C	B	304	20.1	41.4	4.8	32
GLY	O	B	304	20.6	40.9	3.9	34
GLU	N	B	305	19.9	42.7	4.8	33
GLU	CA	B	305	20.2	43.6	3.7	33
GLU	CB	B	305	19.0	44.4	3.3	35
GLU	CG	B	305	17.8	43.7	2.9	45
GLU	CD	B	305	16.7	44.7	2.5	53
GLU	OE1	B	305	16.1	44.6	1.4	62
GLU	OE2	B	305	16.4	45.5	3.3	55
GLU	C	B	305	21.4	44.5	4.0	33
GLU	O	B	305	22.0	45.1	3.1	34
GLN	N	B	306	21.8	44.5	5.3	29
GLN	CA	B	306	22.9	45.4	5.7	28
GLN	CB	B	306	22.3	46.7	6.3	27
GLN	CG	B	306	21.6	47.5	5.3	32
GLN	CD	B	306	21.1	48.8	5.9	34
GLN	OE1	B	306	20.0	49.2	5.8	32
GLN	NE2	B	306	21.9	49.4	6.8	36
GLN	C	B	306	23.8	44.7	6.8	28
GLN	O	B	306	23.4	43.9	7.6	30
LEU	N	B	307	25.1	45.1	6.6	24
LEU	CA	B	307	26.1	44.7	7.6	25
LEU	CB	B	307	27.5	44.7	6.9	21
LEU	CG	B	307	27.6	43.8	5.6	28
LEU	CD1	B	307	29.0	44.0	5.1	22
LEU	CD2	B	307	27.2	42.4	5.9	25
LEU	C	B	307	26.2	45.6	8.8	26
LEU	O	B	307	26.0	46.8	8.7	30
VAL	N	B	308	26.5	45.0	9.9	24
VAL	CA	B	308	26.7	45.8	11.2	25
VAL	CB	B	308	25.8	45.3	12.3	27
VAL	CG1	B	308	26.2	46.0	13.6	30
VAL	CG2	B	308	24.3	45.7	12.1	30
VAL	C	B	308	28.1	45.6	11.4	29
VAL	O	B	308	28.7	44.5	11.3	30
CYS	N	B	309	28.8	46.7	11.8	28
CYS	CA	B	309	30.2	46.7	12.1	26
CYS	C	B	309	30.6	47.2	13.5	28
CYS	O	B	309	29.9	48.0	14.0	29
CYS	CB	B	309	31.0	47.5	11.0	29
CYS	SG	B	309	30.7	47.1	9.3	33
TRP	N	B	310	31.7	46.6	14.0	25
TRP	CA	B	310	32.3	46.9	15.3	26
TRP	CB	B	310	31.9	46.0	16.4	27
TRP	CG	B	310	30.4	45.9	16.8	25
TRP	CD2	B	310	29.4	44.9	16.4	24
TRP	CE2	B	310	28.2	45.3	17.1	25
TRP	CE3	B	310	29.5	43.8	15.6	27
TRP	CD1	B	310	29.8	46.8	17.6	28
TRP	NE1	B	310	28.5	46.4	17.8	29
TRP	CZ2	B	310	27.1	44.5	16.9	26
TRP	CZ3	B	310	28.3	43.0	15.4	26
TRP	CH2	B	310	27.1	43.4	16.1	28
TRP	C	B	310	33.8	47.0	15.1	27
TRP	O	B	310	34.3	46.2	14.3	25
GLN	N	B	311	34.4	47.8	15.9	28
GLN	CA	B	311	35.9	47.9	15.8	36
GLN	CB	B	311	36.4	48.8	16.9	41
GLN	CG	B	311	38.0	48.9	16.9	49
GLN	CD	B	311	38.4	49.8	18.1	56
GLN	OE1	B	311	39.2	49.4	18.9	55
GLN	NE2	B	311	37.9	51.0	18.1	59
GLN	C	B	311	36.5	46.5	15.9	34
GLN	O	B	311	36.1	45.8	16.8	32
ALA	N	B	312	37.4	46.2	15.0	33
ALA	CA	B	312	38.0	44.9	15.0	34
ALA	CB	B	312	39.3	44.9	14.3	36
ALA	C	B	312	38.2	44.3	16.5	37
ALA	O	B	312	38.8	45.0	17.3	37
GLY	N	B	313	37.8	43.1	16.7	37
GLY	CA	B	313	38.0	42.5	18.0	37
GLY	C	B	313	37.1	42.9	19.1	36
GLY	O	B	313	37.3	42.5	20.3	38
THR	N	B	314	36.1	43.8	18.8	36
THR	CA	B	314	35.2	44.3	19.9	32
THR	CB	B	314	35.3	45.8	20.0	32
THR	OG1	B	314	34.8	46.4	18.8	29
THR	CG2	B	314	36.7	46.3	20.4	34
THR	C	B	314	33.8	43.8	19.8	31
THR	O	B	314	32.9	44.2	20.5	33
THR	N	B	315	33.5	42.9	18.8	29
THR	CA	B	315	32.2	42.4	18.6	29
THR	CB	B	315	32.1	41.2	17.7	30
THR	OG1	B	315	32.6	41.5	16.4	27
THR	CG2	B	315	30.7	40.6	17.6	30
THR	C	B	315	31.6	42.0	20.0	29
THR	O	B	315	32.2	41.2	20.7	28
PRO	N	B	316	30.5	42.6	20.4	27
PRO	CD	B	316	29.7	43.6	19.7	25
PRO	CA	B	316	29.9	42.3	21.7	22
PRO	CB	B	316	29.2	43.6	22.0	25
PRO	CG	B	316	28.5	43.8	20.7	30
PRO	C	B	316	29.0	41.1	21.6	23
PRO	O	B	316	27.7	41.2	21.7	21
TRP	N	B	317	29.6	39.9	21.6	23
TRP	CA	B	317	28.8	38.7	21.5	20
TRP	CB	B	317	29.7	37.5	21.4	21
TRP	CG	B	317	30.7	37.5	20.3	24
TRP	CD2	B	317	30.5	37.3	18.9	19
TRP	CE2	B	317	31.7	37.5	18.2	22
TRP	CE3	B	317	29.4	37.1	18.1	18
TRP	CD1	B	317	32.1	37.7	20.4	23
TRP	NE1	B	317	32.7	37.7	19.2	23
TRP	CZ2	B	317	31.9	37.3	16.9	19
TRP	CZ3	B	317	29.5	37.0	16.7	18
TRP	CH2	B	317	30.7	37.1	16.1	23
TRP	C	B	317	27.8	38.5	22.6	21
TRP	O	B	317	26.7	38.0	22.4	16
ASN	N	B	318	28.2	39.0	23.8	17
ASN	CA	B	318	27.4	38.8	25.0	16
ASN	CB	B	318	28.1	39.1	26.3	18
ASN	CG	B	318	28.4	40.6	26.3	20
ASN	OD1	B	318	27.8	41.3	27.1	22
ASN	ND2	B	318	29.4	41.0	25.5	21
ASN	C	B	318	26.0	39.5	25.0	17
ASN	O	B	318	25.1	39.1	25.7	20
ILE	N	B	319	25.8	40.5	24.1	20
ILE	CA	B	319	24.5	41.2	24.2	21
ILE	CB	B	319	24.6	42.6	23.7	26
ILE	CG2	B	319	25.6	43.4	24.6	21
ILE	CG1	B	319	25.1	42.7	22.2	29
ILE	CD1	B	319	25.2	44.1	21.6	30
ILE	C	B	319	23.5	40.4	23.3	22
ILE	O	B	319	22.3	40.6	23.4	22
PHE	N	B	320	24.1	39.5	22.5	18
PHE	CA	B	320	23.2	38.6	21.7	23
PHE	CB	B	320	23.9	38.4	20.3	21
PHE	CG	B	320	24.0	39.6	19.4	22
PHE	CD1	B	320	23.0	40.0	18.5	22
PHE	CD2	B	320	25.1	40.5	19.5	19
PHE	CE1	B	320	23.1	41.1	17.7	21
PHE	CE2	B	320	25.2	41.6	18.8	19
PHE	CZ	B	320	24.2	41.9	17.9	20
PHE	C	B	320	22.9	37.3	22.3	20
PHE	O	B	320	23.8	36.7	22.9	22
PRO	N	B	321	21.6	36.9	22.3	21
PRO	CD	B	321	20.6	37.6	21.5	18
PRO	CA	B	321	21.1	35.7	22.9	19
PRO	CB	B	321	19.6	36.0	23.0	19
PRO	CG	B	321	19.4	36.5	21.6	20
PRO	C	B	321	21.4	34.4	22.1	21
PRO	O	B	321	21.6	34.4	20.9	23
VAL	N	B	322	21.5	33.3	22.9	20
VAL	CA	B	322	21.7	32.0	22.3	19
VAL	CB	B	322	22.3	31.0	23.3	17
VAL	CG1	B	322	23.7	31.5	23.8	19
VAL	CG2	B	322	21.3	30.7	24.5	18
VAL	C	B	322	20.3	31.5	21.8	21
VAL	O	B	322	19.3	31.9	22.3	18
ILE	N	B	323	20.3	30.6	20.8	23
ILE	CA	B	323	19.1	30.1	20.3	23
ILE	CB	B	323	18.9	30.4	18.8	25
ILE	CG2	B	323	17.6	29.9	18.2	22
ILE	CG1	B	323	19.0	32.0	18.6	28
ILE	CD1	B	323	18.9	32.4	17.1	35
ILE	C	B	323	19.1	28.6	20.5	21
ILE	O	B	323	20.0	27.9	20.1	19
SER	N	B	324	18.0	28.1	21.1	19
SER	CA	B	324	17.9	26.7	21.4	21
SER	CB	B	324	17.8	26.4	22.9	20
SER	OG	B	324	18.9	26.8	23.6	23
SER	C	B	324	16.7	26.0	20.7	26
SER	O	B	324	15.6	26.4	20.8	30
LEU	N	B	325	17.0	24.9	19.9	21
LEU	CA	B	325	16.0	24.2	19.2	17
LEU	CB	B	325	16.3	24.0	17.7	21
LEU	CG	B	325	16.4	25.3	17.0	22
LEU	CD1	B	325	16.7	25.0	15.5	22
LEU	CD2	B	325	15.1	26.1	17.0	23
LEU	C	B	325	15.9	22.8	19.9	22
LEU	O	B	325	16.8	22.1	20.0	23
TYR	N	B	326	14.7	22.5	20.4	24
TYR	CA	B	326	14.4	21.2	21.0	22
TYR	CB	B	326	13.4	21.2	22.1	23
TYR	CG	B	326	13.9	21.9	23.4	20
TYR	CD1	B	326	14.0	23.3	23.4	19
TYR	CE1	B	326	14.4	23.9	24.6	19
TYR	CD2	B	326	14.1	21.2	24.5	20
TYR	CE2	B	326	14.5	21.8	25.7	22
TYR	CZ	B	326	14.7	23.2	25.7	21
TYR	OH	B	326	15.1	23.8	26.9	21
TYR	C	B	326	14.0	20.2	19.9	27
TYR	O	B	326	13.0	20.5	19.1	24
LEU	N	B	327	14.7	19.1	19.8	24
LEU	CA	B	327	14.4	18.1	18.7	25
LEU	CB	B	327	15.6	17.8	17.9	24
LEU	CG	B	327	16.2	19.0	17.2	20
LEU	CD1	B	327	17.5	18.6	16.5	17
LEU	CD2	B	327	15.2	19.6	16.2	20
LEU	C	B	327	13.9	16.8	19.4	27
LEU	O	B	327	14.3	16.4	20.4	31
MET	N	B	328	12.9	16.2	18.7	30
MET	CA	B	328	12.3	15.0	19.1	33
MET	CB	B	328	11.3	14.5	18.1	36
MET	CG	B	328	10.6	13.2	18.5	39
MET	SD	B	328	9.4	12.7	17.2	47
MET	CE	B	328	8.2	14.0	17.4	38
MET	C	B	328	13.4	13.9	19.3	35
MET	O	B	328	14.2	13.7	18.5	37
GLY	N	B	329	13.4	13.3	20.5	33
GLY	CA	B	329	14.4	12.3	20.8	33
GLY	C	B	329	14.1	10.9	20.3	33
GLY	O	B	329	13.0	10.7	19.7	32
GLU	N	B	330	14.9	9.9	20.5	36
GLU	CA	B	330	14.6	8.5	20.0	40
GLU	CB	B	330	15.9	7.7	19.8	38
GLU	CG	B	330	16.9	8.3	18.8	41
GLU	CD	B	330	18.1	7.4	18.6	44
GLU	OE1	B	330	19.1	7.6	19.4	42
GLU	OE2	B	330	18.0	6.4	17.8	36
GLU	C	B	330	13.7	7.8	21.0	38
GLU	O	B	330	13.1	6.8	20.7	41
VAL	N	B	331	13.6	8.3	22.2	40
VAL	CA	B	331	12.8	7.7	23.3	42
VAL	CB	B	331	13.5	7.6	24.6	44
VAL	CG1	B	331	12.6	7.0	25.7	45
VAL	CG2	B	331	14.9	6.9	24.5	45
VAL	C	B	331	11.5	8.4	23.4	44
VAL	O	B	331	11.4	9.6	23.5	44
THR	N	B	332	10.4	7.6	23.5	42
THR	CA	B	332	9.1	8.2	23.7	42
THR	CB	B	332	8.0	7.1	24.0	46
THR	OG1	B	332	8.0	6.1	22.9	48
THR	CG2	B	332	6.6	7.6	24.2	44
THR	C	B	332	9.0	9.2	24.8	38
THR	O	B	332	9.6	9.0	25.8	35
ASN	N	B	333	8.4	10.4	24.5	37
ASN	CA	B	333	8.3	11.4	25.5	41
ASN	CB	B	333	7.5	11.0	26.7	46
ASN	CG	B	333	6.1	10.6	26.4	52
ASN	OD1	B	333	5.6	10.8	25.3	52
ASN	ND2	B	333	5.4	10.0	27.4	54
ASN	C	B	333	9.6	12.1	25.9	41
ASN	O	B	333	9.7	12.8	26.9	43
GLN	N	B	334	10.6	11.9	25.1	40
GLN	CA	B	334	11.9	12.4	25.4	40
GLN	CB	B	334	12.9	11.3	25.8	43
GLN	CG	B	334	14.3	11.7	26.2	45
GLN	CD	B	334	15.1	10.5	26.6	48
GLN	OE1	B	334	16.1	10.2	26.0	52
GLN	NE2	B	334	14.6	9.8	27.6	45
GLN	C	B	334	12.5	13.3	24.3	39
GLN	O	B	334	12.5	12.9	23.1	38
SER	N	B	335	13.0	14.4	24.6	36
SER	CA	B	335	13.6	15.4	23.6	35
SER	CB	B	335	12.7	16.5	23.3	36
SER	OG	B	335	12.5	17.3	24.5	41
SER	C	B	335	15.0	15.9	24.2	30
SER	O	B	335	15.3	15.7	25.3	28
PHE	N	B	336	15.8	16.5	23.3	28
PHE	CA	B	336	17.1	17.0	23.6	28
PHE	CB	B	336	18.2	16.1	23.1	26
PHE	CG	B	336	18.3	15.9	21.6	27
PHE	CD1	B	336	19.1	16.8	20.8	27
PHE	CD2	B	336	17.6	14.9	21.0	26
PHE	CE1	B	336	19.2	16.6	19.5	24
PHE	CE2	B	336	17.7	14.7	19.6	27
PHE	CZ	B	336	18.5	15.5	18.9	27
PHE	C	B	336	17.1	18.4	22.9	26
PHE	O	B	336	16.3	18.7	22.0	26
ARG	N	B	337	18.0	19.3	23.3	22
ARG	CA	B	337	18.1	20.6	22.6	25
ARG	CB	B	337	17.7	21.7	23.5	23
ARG	CG	B	337	18.6	21.9	24.7	26
ARG	CD	B	337	18.1	23.1	25.6	26
ARG	NE	B	337	19.0	23.2	26.7	28
ARG	CZ	B	337	18.7	23.6	27.9	28
ARG	NH1	B	337	17.4	23.9	28.2	27
ARG	NH2	B	337	19.6	23.7	28.9	21
ARG	C	B	337	19.5	20.9	22.1	24
ARG	O	B	337	20.5	20.5	22.6	26
ILE	N	B	338	19.5	21.6	20.9	26
ILE	CA	B	338	20.8	22.0	20.3	24
ILE	CB	B	338	20.9	21.6	18.9	23
ILE	CG2	B	338	21.0	20.1	18.8	19
ILE	CG1	B	338	19.8	22.1	18.0	22
ILE	CD1	B	338	19.9	21.7	16.6	23
ILE	C	B	338	20.8	23.6	20.5	23
ILE	O	B	338	19.8	24.2	20.3	20
THR	N	B	339	21.9	24.1	20.9	20
THR	CA	B	339	22.0	25.5	21.1	16
THR	CB	B	339	22.1	25.8	22.6	19
THR	OG1	B	339	21.0	25.3	23.3	21
THR	CG2	B	339	22.2	27.3	22.9	18
THR	C	B	339	23.2	26.2	20.4	19
THR	O	B	339	24.3	25.7	20.5	18
ILE	N	B	340	22.8	27.2	19.6	19
ILE	CA	B	340	23.8	27.9	18.8	19
ILE	CB	B	340	23.5	28.1	17.3	20
ILE	CG2	B	340	23.4	26.7	16.7	14
ILE	CG1	B	340	22.3	28.9	17.1	18
ILE	CD1	B	340	21.9	29.2	15.7	19
ILE	C	B	340	24.1	29.3	19.4	23
ILE	O	B	340	23.2	29.8	20.1	22
LEU	N	B	341	25.2	29.8	19.1	20
LEU	CA	B	341	25.7	31.1	19.6	19
LEU	CB	B	341	27.1	31.1	20.1	16
LEU	CG	B	341	27.4	30.1	21.2	18
LEU	CD1	B	341	28.9	30.1	21.5	19
LEU	CD2	B	341	26.6	30.3	22.4	16
LEU	C	B	341	25.5	32.2	18.5	16
LEU	O	B	341	25.4	31.9	17.3	14
PRO	N	B	342	25.6	33.5	18.9	15
PRO	CD	B	342	25.9	34.2	20.2	16
PRO	CA	B	342	25.5	34.5	17.9	16
PRO	CB	B	342	25.3	35.8	18.6	19
PRO	CG	B	342	26.3	35.6	19.7	16
PRO	C	B	342	26.7	34.4	16.9	17
PRO	O	B	342	26.7	34.9	15.8	16
GLN	N	B	343	27.8	33.7	17.4	18
GLN	CA	B	343	28.9	33.5	16.5	17
GLN	CB	B	343	30.2	32.8	17.1	17
GLN	CG	B	343	31.0	33.6	18.2	18
GLN	CD	B	343	30.3	33.8	19.5	20
GLN	OE1	B	343	29.1	33.6	19.6	24
GLN	NE2	B	343	31.1	34.3	20.4	21
GLN	C	B	343	28.5	32.6	15.3	22
GLN	O	B	343	29.1	32.6	14.2	23
GLN	N	B	344	27.4	31.8	15.5	23
GLN	CA	B	344	26.8	31.0	14.4	20
GLN	CB	B	344	26.2	29.7	14.8	16
GLN	CG	B	344	27.1	28.5	15.3	17
GLN	CD	B	344	27.9	28.8	16.6	18
GLN	OE1	B	344	29.1	28.9	16.6	23
GLN	NE2	B	344	27.1	29.0	17.7	16
GLN	C	B	344	25.8	31.8	13.5	23
GLN	O	B	344	25.7	31.5	12.3	23
TYR	N	B	345	25.0	32.7	14.1	21
TYR	CA	B	345	24.0	33.3	13.3	21
TYR	CB	B	345	22.6	33.3	14.0	18
TYR	CG	B	345	22.5	34.1	15.3	19
TYR	CD1	B	345	22.4	35.5	15.3	18
TYR	CE1	B	345	22.1	36.1	16.5	20
TYR	CD2	B	345	22.4	33.4	16.5	19
TYR	CE2	B	345	22.2	34.1	17.7	20
TYR	CZ	B	345	22.0	35.4	17.7	21
TYR	OH	B	345	21.8	36.1	18.9	21
TYR	C	B	345	24.4	34.7	12.8	22
TYR	O	B	345	23.6	35.3	12.0	22
LEU	N	B	346	25.5	35.2	13.2	23
LEU	CA	B	346	26.1	36.5	12.7	22
LEU	CB	B	346	26.6	37.4	13.8	22
LEU	CG	B	346	25.5	37.8	14.8	24
LEU	CD1	B	346	26.1	38.7	15.9	26
LEU	CD2	B	346	24.3	38.6	14.1	23
LEU	C	B	346	27.2	36.1	11.8	23
LEU	O	B	346	28.3	35.8	12.3	26
ARG	N	B	347	27.0	36.1	10.5	23
ARG	CA	B	347	28.0	35.7	9.5	24
ARG	CB	B	347	27.3	35.1	8.3	21
ARG	CG	B	347	28.3	34.6	7.2	26
ARG	CD	B	347	27.5	33.9	6.0	30
ARG	NE	B	347	26.5	34.8	5.3	32
ARG	CZ	B	347	26.8	35.6	4.3	37
ARG	NH1	B	347	28.1	35.7	3.9	39
ARG	NH2	B	347	25.9	36.2	3.6	40
ARG	C	B	347	29.1	36.7	9.1	28
ARG	O	B	347	28.8	37.8	8.7	24
PRO	N	B	348	30.3	36.4	9.4	31
PRO	CD	B	348	30.8	35.3	10.3	31
PRO	CA	B	348	31.5	37.2	9.0	31
PRO	CB	B	348	32.7	36.3	9.4	33
PRO	CG	B	348	32.2	35.8	10.7	34
PRO	C	B	348	31.5	37.6	7.6	33
PRO	O	B	348	31.5	36.7	6.7	31
VAL	N	B	349	31.5	38.9	7.3	34
VAL	CA	B	349	31.5	39.4	5.9	40
VAL	CB	B	349	30.3	40.2	5.5	39
VAL	CG1	B	349	30.4	40.7	4.1	41
VAL	CG2	B	349	29.0	39.3	5.6	37
VAL	C	B	349	32.8	40.2	5.7	47
VAL	O	B	349	32.9	41.3	6.2	45
GLU	N	B	350	33.7	39.7	4.9	57
GLU	CA	B	350	34.9	40.4	4.5	68
GLU	CB	B	350	36.1	39.4	4.6	71
GLU	CG	B	350	37.5	40.0	4.3	76
GLU	CD	B	350	37.8	41.2	5.2	78
GLU	OE1	B	350	37.9	42.3	4.7	78
GLU	OE2	B	350	37.9	40.9	6.4	79
GLU	C	B	350	34.7	40.9	3.1	75
GLU	O	B	350	34.6	40.1	2.2	78
ASP	N	B	351	34.8	42.2	2.9	81
ASP	CA	B	351	34.6	42.7	1.6	88
ASP	CB	B	351	34.2	44.2	1.7	92
ASP	CG	B	351	34.0	44.8	0.3	94
ASP	OD1	B	351	32.8	45.2	0.0	96
ASP	OD2	B	351	34.9	44.9	−0.5	96
ASP	C	B	351	35.9	42.6	0.7	89
ASP	O	B	351	37.0	42.6	1.2	90
SER	N	B	355	39.0	45.0	7.3	74
SER	CA	B	355	39.9	46.1	7.6	74
SER	CB	B	355	39.6	47.4	6.9	75
SER	OG	B	355	38.3	47.8	7.3	77
SER	C	B	355	40.1	46.3	9.1	72
SER	O	B	355	40.5	45.4	9.8	73
GLN	N	B	356	39.7	47.5	9.6	69
GLN	CA	B	356	39.8	47.8	11.0	65
GLN	CB	B	356	40.3	49.2	11.2	70
GLN	CG	B	356	40.5	49.6	12.7	77
GLN	CD	B	356	41.5	48.7	13.3	79
GLN	OE1	B	356	42.6	49.2	13.8	81
GLN	NE2	B	356	41.2	47.4	13.4	80
GLN	C	B	356	38.5	47.5	11.7	58
GLN	O	B	356	38.4	47.7	12.9	56
ASP	N	B	357	37.5	47.0	11.0	52
ASP	CA	B	357	36.2	46.7	11.5	45
ASP	CB	B	357	35.1	47.7	11.0	48
ASP	CG	B	357	35.3	49.1	11.4	52
ASP	OD1	B	357	36.2	49.4	12.2	54
ASP	OD2	B	357	34.6	50.0	10.9	53
ASP	C	B	357	35.8	45.3	11.2	43
ASP	O	B	357	36.0	44.8	10.1	42
ASP	N	B	358	35.1	44.6	12.1	39
ASP	CA	B	358	34.6	43.3	11.9	32
ASP	CB	B	358	34.8	42.4	13.1	33
ASP	CG	B	358	36.3	42.1	13.4	36
ASP	OD1	B	358	36.6	42.1	14.6	37
ASP	OD2	B	358	37.1	42.0	12.5	38
ASP	C	B	358	33.1	43.6	11.6	26
ASP	O	B	358	32.4	44.1	12.4	24
CYS	N	B	359	32.7	43.2	10.4	22
CYS	CA	B	359	31.3	43.4	10.0	24
CYS	C	B	359	30.6	42.1	9.8	29
CYS	O	B	359	31.2	41.0	9.5	26
CYS	CB	B	359	31.3	44.2	8.7	28
CYS	SG	B	359	32.1	45.8	8.7	33
TYR	N	B	360	29.3	42.1	10.1	27
TYR	CA	B	360	28.5	40.8	10.1	27
TYR	CB	B	360	28.3	40.3	11.5	27
TYR	CG	B	360	29.6	40.1	12.3	26
TYR	CD1	B	360	30.2	41.2	12.9	25
TYR	CE1	B	360	31.4	41.1	13.6	26
TYR	CD2	B	360	30.2	38.8	12.4	24
TYR	CE2	B	360	31.4	38.7	13.1	26
TYR	CZ	B	360	32.0	39.8	13.7	27
TYR	OH	B	360	33.1	39.7	14.4	29
TYR	C	B	360	27.1	41.0	9.5	29
TYR	O	B	360	26.5	42.0	9.5	27
LYS	N	B	361	26.7	39.9	8.8	25
LYS	CA	B	361	25.3	39.9	8.3	27
LYS	CB	B	361	25.3	39.5	6.8	31
LYS	CG	B	361	23.9	39.4	6.2	39
LYS	CD	B	361	23.9	39.1	4.7	45
LYS	CE	B	361	24.7	40.1	3.9	50
LYS	NZ	B	361	24.7	39.8	2.5	56
LYS	C	B	361	24.5	38.9	9.1	28
LYS	O	B	361	24.9	37.9	9.5	30
PHE	N	B	362	23.3	39.4	9.4	27
PHE	CA	B	362	22.3	38.6	10.2	22
PHE	CB	B	362	21.2	39.5	10.6	21
PHE	CG	B	362	20.1	38.8	11.5	22
PHE	CD1	B	362	20.5	38.3	12.7	20
PHE	CD2	B	362	18.8	38.6	11.0	23
PHE	CE1	B	362	19.5	37.6	13.5	21
PHE	CE2	B	362	17.9	38.0	11.8	22
PHE	CZ	B	362	18.2	37.5	13.1	22
PHE	C	B	362	21.9	37.4	9.3	23
PHE	O	B	362	21.2	37.6	8.3	25
ALA	N	B	363	22.3	36.2	9.7	23
ALA	CA	B	363	22.1	35.0	8.9	20
ALA	CB	B	363	23.3	34.1	8.9	21
ALA	C	B	363	20.8	34.2	9.2	23
ALA	O	B	363	20.7	33.0	9.0	25
ILE	N	B	364	19.8	34.9	9.8	21
ILE	CA	B	364	18.5	34.2	10.1	23
ILE	CB	B	364	18.1	34.3	11.6	22
ILE	CG2	B	364	16.8	33.7	11.8	19
ILE	CG1	B	364	19.2	33.7	12.5	19
ILE	CD1	B	364	18.9	33.8	14.0	21
ILE	C	B	364	17.5	34.9	9.2	25
ILE	O	B	364	17.4	36.1	9.2	24
SER	N	B	365	16.8	34.1	8.4	24
SER	CA	B	365	15.8	34.7	7.5	26
SER	CB	B	365	16.4	34.9	6.1	24
SER	OG	B	365	16.9	33.7	5.6	32
SER	C	B	365	14.5	34.0	7.4	27
SER	O	B	365	14.3	32.8	7.7	30
GLN	N	B	366	13.5	34.7	6.9	28
GLN	CA	B	366	12.1	34.2	6.6	31
GLN	CB	B	366	11.2	35.4	6.3	37
GLN	CG	B	366	9.8	35.0	6.1	45
GLN	CD	B	366	9.0	36.3	5.8	51
GLN	OE1	B	366	8.3	36.4	4.7	54
GLN	NE2	B	366	9.1	37.3	6.6	50
GLN	C	B	366	12.0	33.1	5.6	28
GLN	O	B	366	12.7	33.2	4.6	27
SER	N	B	367	11.2	32.2	5.8	27
SER	CA	B	367	11.0	31.1	4.9	27
SER	CB	B	367	11.5	29.7	5.4	26
SER	OG	B	367	11.3	28.7	4.5	28
SER	C	B	367	9.5	30.9	4.6	29
SER	O	B	367	8.6	31.1	5.5	27
SER	N	B	368	9.2	30.5	3.4	29
SER	CA	B	368	7.8	30.2	3.0	36
SER	CB	B	368	7.4	31.0	1.7	37
SER	OG	B	368	8.2	30.7	0.6	40
SER	C	B	368	7.6	28.7	2.7	36
SER	O	B	368	6.5	28.3	2.3	39
THR	N	B	369	8.7	28.0	3.0	36
THR	CA	B	369	8.7	26.5	2.7	31
THR	CB	B	369	9.4	26.1	1.5	33
THR	OG1	B	369	10.8	26.5	1.6	34
THR	CG2	B	369	8.8	26.7	0.2	33
THR	C	B	369	9.1	25.7	3.9	32
THR	O	B	369	9.6	24.6	3.8	32
GLY	N	B	370	8.9	26.2	5.1	29
GLY	CA	B	370	9.3	25.5	6.3	28
GLY	C	B	370	10.6	25.9	6.9	29
GLY	O	B	370	11.3	26.8	6.4	28
THR	N	B	371	11.0	25.2	8.0	27
THR	CA	B	371	12.3	25.5	8.7	23
THR	CB	B	371	12.3	25.1	10.1	23
THR	OG1	B	371	11.4	25.9	10.9	24
THR	CG2	B	371	13.7	25.3	10.7	17
THR	C	B	371	13.5	24.9	7.9	25
THR	O	B	371	13.4	23.7	7.6	26
VAL	N	B	372	14.5	25.7	7.7	20
VAL	CA	B	372	15.7	25.2	7.1	20
VAL	CB	B	372	16.0	25.8	5.7	21
VAL	CG1	B	372	17.3	25.2	5.1	16
VAL	CG2	B	372	14.8	25.6	4.7	15
VAL	C	B	372	16.9	25.3	8.0	22
VAL	O	B	372	17.4	26.4	8.2	18
MET	N	B	373	17.4	24.2	8.5	21
MET	CA	B	373	18.5	24.3	9.4	20
MET	CB	B	373	18.5	23.1	10.4	23
MET	CG	B	373	17.3	23.1	11.2	22
MET	SD	B	373	17.2	21.6	12.4	31
MET	CE	B	373	18.9	21.5	12.8	25
MET	C	B	373	19.7	24.2	8.5	21
MET	O	B	373	20.2	23.1	8.1	18
GLY	N	B	374	20.2	25.4	8.1	18
GLY	CA	B	374	21.4	25.5	7.2	20
GLY	C	B	374	22.7	25.6	7.9	18
GLY	O	B	374	22.8	25.1	9.0	20
ALA	N	B	375	23.7	26.1	7.2	19
ALA	CA	B	375	25.0	26.2	7.8	21
ALA	CB	B	375	26.0	26.9	6.8	15
ALA	C	B	375	25.0	27.0	9.1	22
ALA	O	B	375	25.9	26.7	9.9	24
VAL	N	B	376	24.1	27.8	9.4	22
VAL	CA	B	376	24.1	28.5	10.7	18
VAL	CB	B	376	22.9	29.6	10.7	19
VAL	CG1	B	376	22.9	30.2	12.1	18
VAL	CG2	B	376	23.2	30.7	9.7	22
VAL	C	B	376	23.9	27.6	11.8	22
VAL	O	B	376	24.5	27.8	12.9	20
ILE	N	B	377	23.2	26.5	11.6	20
ILE	CA	B	377	23.0	25.5	12.6	22
ILE	CB	B	377	21.6	24.8	12.4	25
ILE	CG2	B	377	21.5	23.5	13.3	21
ILE	CG1	B	377	20.5	25.7	12.7	25
ILE	CD1	B	377	20.4	26.3	14.1	29
ILE	C	B	377	24.1	24.4	12.5	21
ILE	O	B	377	24.7	24.1	13.5	23
MET	N	B	378	24.5	24.0	11.3	20
MET	CA	B	378	25.5	23.0	11.2	24
MET	CB	B	378	25.5	22.4	9.7	22
MET	CG	B	378	24.1	21.7	9.4	24
MET	SD	B	378	24.1	21.0	7.8	25
MET	CE	B	378	25.1	19.5	8.0	18
MET	C	B	378	26.9	23.4	11.6	24
MET	O	B	378	27.7	22.5	12.0	24
GLU	N	B	379	27.2	24.6	11.5	23
GLU	CA	B	379	28.6	25.1	11.9	22
GLU	CB	B	379	28.9	26.4	11.3	18
GLU	CG	B	379	28.8	26.4	9.7	24
GLU	CD	B	379	29.1	27.8	9.2	24
GLU	OE1	B	379	29.5	27.9	8.1	23
GLU	OE2	B	379	28.8	28.8	9.9	27
GLU	C	B	379	28.9	25.0	13.4	20
GLU	O	B	379	30.0	25.3	13.8	23
GLY	N	B	380	27.8	24.7	14.1	19
GLY	CA	B	380	28.1	24.6	15.6	20
GLY	C	B	380	28.0	23.1	16.0	18
GLY	O	B	380	28.3	22.8	17.1	19
PHE	N	B	381	27.7	22.2	15.0	17
PHE	CA	B	381	27.6	20.8	15.4	19
PHE	CB	B	381	26.1	20.5	15.6	17
PHE	CG	B	381	25.4	21.4	16.5	24
PHE	CD1	B	381	24.6	22.4	16.0	22
PHE	CD2	B	381	25.6	21.3	17.9	24
PHE	CE1	B	381	24.0	23.3	16.9	25
PHE	CE2	B	381	25.0	22.2	18.8	23
PHE	CZ	B	381	24.2	23.2	18.3	22
PHE	C	B	381	28.2	19.9	14.4	19
PHE	O	B	381	28.2	20.1	13.2	21
TYR	N	B	382	28.6	18.7	14.9	21
TYR	CA	B	382	29.1	17.6	14.0	18
TYR	CB	B	382	30.0	16.7	14.8	14
TYR	CG	B	382	30.5	15.5	14.0	21
TYR	CD1	B	382	30.9	15.7	12.6	20
TYR	CE1	B	382	31.4	14.6	11.9	21
TYR	CD2	B	382	30.6	14.3	14.5	20
TYR	CE2	B	382	31.1	13.2	13.8	25
TYR	CZ	B	382	31.5	13.3	12.5	19
TYR	OH	B	382	32.0	12.3	11.8	23
TYR	C	B	382	27.7	17.0	13.8	17
TYR	O	B	382	27.0	16.6	14.7	19
VAL	N	B	383	27.3	16.8	12.5	16
VAL	CA	B	383	26.0	16.2	12.2	17
VAL	CB	B	383	25.2	17.2	11.3	16
VAL	CG1	B	383	23.8	16.6	11.0	13
VAL	CG2	B	383	25.1	18.6	12.0	12
VAL	C	B	383	26.1	14.8	11.5	17
VAL	O	B	383	26.8	14.7	10.5	20
VAL	N	B	384	25.5	13.9	12.1	19
VAL	CA	B	384	25.5	12.5	11.6	20
VAL	CB	B	384	25.7	11.4	12.6	20
VAL	CG1	B	384	25.8	10.0	12.0	16
VAL	CG2	B	384	27.0	11.8	13.5	13
VAL	C	B	384	24.2	12.1	10.8	21
VAL	O	B	384	23.1	12.0	11.4	20
PHE	N	B	385	24.3	11.9	9.5	18
PHE	CA	B	385	23.2	11.5	8.7	19
PHE	CB	B	385	23.2	12.1	7.3	14
PHE	CG	B	385	23.1	13.6	7.3	19
PHE	CD1	B	385	21.9	14.2	6.9	10
PHE	CD2	B	385	24.2	14.3	7.7	16
PHE	CE1	B	385	21.8	15.6	7.0	16
PHE	CE2	B	385	24.1	15.7	7.7	15
PHE	CZ	B	385	22.9	16.4	7.4	17
PHE	C	B	385	23.2	10.0	8.8	17
PHE	O	B	385	23.8	9.4	7.9	17
ASP	N	B	386	22.5	9.4	9.7	23
ASP	CA	B	386	22.5	8.0	9.9	25
ASP	CB	B	386	22.5	7.6	11.4	25
ASP	CG	B	386	22.5	6.1	11.7	32
ASP	OD1	B	386	22.5	5.4	10.7	32
ASP	OD2	B	386	22.6	5.8	12.9	33
ASP	C	B	386	21.3	7.4	9.2	26
ASP	O	B	386	20.2	7.1	9.7	26
ARG	N	B	387	21.5	7.2	7.9	19
ARG	CA	B	387	20.5	6.7	6.9	24
ARG	CB	B	387	21.1	6.7	5.5	25
ARG	CG	B	387	21.4	8.1	5.0	23
ARG	CD	B	387	22.1	8.0	3.6	27
ARG	NE	B	387	21.4	7.4	2.5	27
ARG	CZ	B	387	20.8	8.0	1.5	26
ARG	NH1	B	387	20.8	9.3	1.4	21
ARG	NH2	B	387	20.3	7.2	0.6	28
ARG	C	B	387	20.1	5.3	7.3	25
ARG	O	B	387	18.9	5.0	7.3	23
ALA	N	B	388	21.0	4.4	7.7	27
ALA	CA	B	388	20.6	3.1	8.1	29
ALA	CB	B	388	21.9	2.3	8.4	27
ALA	C	B	388	19.7	3.0	9.3	31
ALA	O	B	388	19.0	2.0	9.4	31
ARG	N	B	389	19.7	4.0	10.1	31
ARG	CA	B	389	18.8	3.9	11.3	31
ARG	CB	B	389	19.6	4.1	12.6	35
ARG	CG	B	389	20.7	3.0	12.7	37
ARG	CD	B	389	21.4	3.2	14.0	46
ARG	NE	B	389	22.4	2.1	14.2	54
ARG	CZ	B	389	23.5	2.0	13.4	57
ARG	NH1	B	389	23.7	2.9	12.4	55
ARG	NH2	B	389	24.4	1.1	13.6	58
ARG	C	B	389	17.7	5.0	11.2	31
ARG	O	B	389	17.0	5.2	12.1	32
LYS	N	B	390	17.7	5.7	10.1	31
LYS	CA	B	390	16.7	6.7	9.9	35
LYS	CB	B	390	15.3	6.0	9.8	41
LYS	CG	B	390	14.1	6.8	9.5	50
LYS	CD	B	390	12.9	5.9	9.4	58
LYS	CE	B	390	11.6	6.7	9.1	60
LYS	NZ	B	390	10.4	5.8	9.0	63
LYS	C	B	390	16.7	7.8	11.0	31
LYS	O	B	390	15.6	8.1	11.5	27
ARG	N	B	391	17.9	8.2	11.3	24
ARG	CA	B	391	18.0	9.2	12.4	24
ARG	CB	B	391	18.2	8.6	13.7	21
ARG	CG	B	391	19.5	7.8	13.8	21
ARG	CD	B	391	19.7	7.1	15.1	16
ARG	NE	B	391	21.0	6.4	15.1	22
ARG	CZ	B	391	21.6	5.9	16.2	21
ARG	NH1	B	391	21.0	6.0	17.4	20
ARG	NH2	B	391	22.7	5.3	16.1	21
ARG	C	B	391	19.1	10.2	12.1	23
ARG	O	B	391	20.1	9.9	11.4	20
ILE	N	B	392	19.0	11.4	12.7	26
ILE	CA	B	392	20.0	12.5	12.5	23
ILE	CB	B	392	19.4	13.8	12.0	24
ILE	CG2	B	392	20.5	14.9	11.9	22
ILE	CG1	B	392	18.8	13.6	10.6	24
ILE	CD1	B	392	19.7	13.2	9.5	26
ILE	C	B	392	20.6	12.7	13.9	24
ILE	O	B	392	19.9	13.1	14.8	21
GLY	N	B	393	22.0	12.6	13.9	24
GLY	CA	B	393	22.7	12.9	15.2	23
GLY	C	B	393	23.4	14.2	15.3	26
GLY	O	B	393	24.0	14.7	14.3	24
PHE	N	B	394	23.3	14.8	16.5	26
PHE	CA	B	394	23.9	16.1	16.8	22
PHE	CB	B	394	22.9	17.2	17.0	19
PHE	CG	B	394	22.1	17.5	15.8	23
PHE	CD1	B	394	20.9	16.8	15.5	23
PHE	CD2	B	394	22.4	18.6	14.9	20
PHE	CE1	B	394	20.1	17.1	14.4	18
PHE	CE2	B	394	21.6	18.9	13.8	22
PHE	CZ	B	394	20.4	18.1	13.6	23
PHE	C	B	394	24.9	16.1	17.9	25
PHE	O	B	394	24.6	15.5	19.0	27
ALA	N	B	395	26.0	16.7	17.8	28
ALA	CA	B	395	27.1	16.8	18.8	25
ALA	CB	B	395	28.0	15.5	18.7	26
ALA	C	B	395	27.9	18.0	18.7	23
ALA	O	B	395	28.1	18.5	17.6	24
VAL	N	B	396	28.2	18.6	19.8	17
VAL	CA	B	396	29.0	19.9	19.8	18
VAL	CB	B	396	29.4	20.3	21.2	20
VAL	CG1	B	396	30.3	21.6	21.2	17
VAL	CG2	B	396	28.2	20.5	22.1	16
VAL	C	B	396	30.2	19.7	18.9	22
VAL	O	B	396	31.0	18.8	19.1	20
SER	N	B	397	30.3	20.6	17.9	22
SER	CA	B	397	31.4	20.6	17.0	24
SER	CB	B	397	31.1	21.4	15.7	22
SER	OG	B	397	32.2	21.3	14.8	26
SER	C	B	397	32.8	21.0	17.5	25
SER	O	B	397	32.9	22.1	18.1	27
ALA	N	B	398	33.8	20.2	17.3	22
ALA	CA	B	398	35.1	20.6	17.8	25
ALA	CB	B	398	36.1	19.4	17.6	24
ALA	C	B	398	35.7	21.8	17.1	27
ALA	O	B	398	36.8	22.3	17.4	33
CYS	N	B	399	35.0	22.3	16.1	30
CYS	CA	B	399	35.5	23.5	15.4	25
CYS	C	B	399	34.5	24.7	15.4	27
CYS	O	B	399	34.7	25.6	14.6	25
CYS	CB	B	399	35.8	23.2	13.9	29
CYS	SG	B	399	34.4	22.7	12.9	30
HIS	N	B	400	33.5	24.6	16.2	24
HIS	CA	B	400	32.5	25.7	16.1	23
HIS	CB	B	400	31.2	25.5	16.8	21
HIS	CG	B	400	31.3	25.4	18.3	21
HIS	CD2	B	400	30.8	26.3	19.3	20
HIS	ND1	B	400	31.8	24.3	19.0	21
HIS	CE1	B	400	31.7	24.5	20.3	24
HIS	NE2	B	400	31.1	25.7	20.5	22
HIS	C	B	400	33.2	27.0	16.8	23
HIS	O	B	400	34.0	26.9	17.7	22
VAL	N	B	401	32.8	28.1	16.2	23
VAL	CA	B	401	33.3	29.4	16.7	23
VAL	CB	B	401	33.2	30.5	15.7	26
VAL	CG1	B	401	33.7	31.8	16.2	23
VAL	CG2	B	401	33.9	30.1	14.4	22
VAL	C	B	401	32.6	29.8	18.0	27
VAL	O	B	401	31.4	29.8	18.1	27
HIS	N	B	402	33.4	30.1	19.0	28
HIS	CA	B	402	32.8	30.5	20.3	31
HIS	CB	B	402	32.3	29.3	21.2	32
HIS	CG	B	402	33.4	28.4	21.5	39
HIS	CD2	B	402	34.1	28.2	22.7	40
HIS	ND1	B	402	33.9	27.5	20.7	38
HIS	CE1	B	402	34.9	26.8	21.3	40
HIS	NE2	B	402	35.0	27.2	22.5	40
HIS	C	B	402	33.8	31.3	21.1	33
HIS	O	B	402	35.0	31.2	20.8	39
ASP	N	B	403	33.4	32.0	22.1	32
ASP	CA	B	403	34.3	32.8	23.0	30
ASP	CB	B	403	33.7	34.2	23.3	30
ASP	CG	B	403	32.3	34.0	23.9	35
ASP	OD1	B	403	32.2	33.7	25.1	31
ASP	OD2	B	403	31.3	34.3	23.3	36
ASP	C	B	403	34.5	32.0	24.2	32
ASP	O	B	403	34.1	30.8	24.3	28
GLU	N	B	404	35.2	32.6	25.2	34
GLU	CA	B	404	35.5	31.8	26.4	40
GLU	CB	B	404	36.8	32.3	27.1	48
GLU	CG	B	404	36.9	33.8	27.5	59
GLU	CD	B	404	36.7	34.8	26.3	66
GLU	OE1	B	404	36.8	34.3	25.2	71
GLU	OE2	B	404	36.6	36.0	26.5	67
GLU	C	B	404	34.4	31.8	27.5	35
GLU	O	B	404	34.5	31.1	28.5	37
PHE	N	B	405	33.3	32.5	27.2	28
PHE	CA	B	405	32.2	32.5	28.1	27
PHE	CB	B	405	31.8	34.0	28.4	29
PHE	CG	B	405	32.9	34.8	28.9	31
PHE	CD1	B	405	33.4	35.8	28.1	33
PHE	CD2	B	405	33.4	34.6	30.1	31
PHE	CE1	B	405	34.5	36.6	28.5	34
PHE	CE2	B	405	34.5	35.4	30.6	35
PHE	CZ	B	405	35.0	36.4	29.8	31
PHE	C	B	405	31.0	31.7	27.8	27
PHE	O	B	405	30.2	31.3	28.6	27
ARG	N	B	406	30.9	31.3	26.5	21
ARG	CA	B	406	29.8	30.5	26.0	24
ARG	CB	B	406	28.5	31.3	25.5	22
ARG	CG	B	406	27.9	32.1	26.6	24
ARG	CD	B	406	26.6	32.8	26.0	23
ARG	NE	B	406	26.9	33.7	24.8	22
ARG	CZ	B	406	26.1	34.6	24.4	22
ARG	NH1	B	406	24.9	34.8	25.0	20
ARG	NH2	B	406	26.4	35.3	23.3	18
ARG	C	B	406	30.2	29.5	24.9	23
ARG	O	B	406	31.1	29.8	24.1	25
THR	N	B	407	29.5	28.4	24.9	24
THR	CA	B	407	29.8	27.4	23.9	27
THR	CB	B	407	30.7	26.2	24.5	29
THR	OG1	B	407	30.9	25.2	23.5	36
THR	CG2	B	407	30.0	25.6	25.7	30
THR	C	B	407	28.5	26.8	23.3	23
THR	O	B	407	27.5	26.8	23.9	20
ALA	N	B	408	28.6	26.3	22.1	22
ALA	CA	B	408	27.4	25.7	21.4	24
ALA	CB	B	408	27.8	25.3	20.0	24
ALA	C	B	408	27.2	24.5	22.3	25
ALA	O	B	408	28.1	24.0	22.9	26
ALA	N	B	409	25.9	24.0	22.4	24
ALA	CA	B	409	25.6	22.9	23.2	24
ALA	CB	B	409	25.2	23.4	24.6	19
ALA	C	B	409	24.6	21.9	22.7	26
ALA	O	B	409	23.7	22.3	22.0	26
VAL	N	B	410	24.7	20.7	23.1	24
VAL	CA	B	410	23.8	19.6	22.7	24
VAL	CB	B	410	24.4	18.5	21.8	21
VAL	CG1	B	410	23.3	17.5	21.4	22
VAL	CG2	B	410	25.0	19.2	20.6	25
VAL	C	B	410	23.4	19.0	24.1	25
VAL	O	B	410	24.3	18.4	24.7	30
GLU	N	B	411	22.2	19.2	24.6	26
GLU	CA	B	411	21.8	18.7	25.9	28
GLU	CB	B	411	21.8	19.9	26.8	29
GLU	CG	B	411	23.2	20.7	26.9	38
GLU	CD	B	411	23.1	21.9	27.8	41
GLU	OE1	B	411	23.9	22.0	28.7	46
GLU	OE2	B	411	22.2	22.8	27.5	41
GLU	C	B	411	20.5	18.0	26.0	26
GLU	O	B	411	19.6	18.3	25.3	26
GLY	N	B	412	20.5	17.0	26.9	26
GLY	CA	B	412	19.3	16.2	27.1	24
GLY	C	B	412	19.4	15.2	28.3	27
GLY	O	B	412	20.4	15.1	28.9	25
PRO	N	B	413	18.3	14.5	28.6	28
PRO	CD	B	413	18.3	13.4	29.6	32
PRO	CA	B	413	17.0	14.5	28.0	31
PRO	CB	B	413	16.6	13.1	28.1	30
PRO	CG	B	413	16.9	12.8	29.5	30
PRO	C	B	413	16.0	15.4	28.7	31
PRO	O	B	413	16.1	15.8	29.8	31
PHE	N	B	414	14.9	15.8	27.9	34
PHE	CA	B	414	13.8	16.6	28.4	34
PHE	CB	B	414	13.8	18.0	27.7	29
PHE	CG	B	414	15.0	18.8	27.9	30
PHE	CD1	B	414	16.0	18.7	26.9	30
PHE	CD2	B	414	15.2	19.6	29.0	30
PHE	CE1	B	414	17.2	19.4	27.1	26
PHE	CE2	B	414	16.4	20.3	29.1	32
PHE	CZ	B	414	17.4	20.2	28.2	29
PHE	C	B	414	12.5	15.9	28.3	36
PHE	O	B	414	12.3	15.3	27.2	36
VAL	N	B	415	11.7	15.8	29.3	43
VAL	CA	B	415	10.5	15.1	29.3	48
VAL	CB	B	415	9.8	14.9	30.7	49
VAL	CG1	B	415	8.5	14.2	30.5	48
VAL	CG2	B	415	10.8	14.1	31.6	45
VAL	C	B	415	9.5	16.0	28.4	51
VAL	O	B	415	9.2	17.1	28.8	52
THR	N	B	416	9.1	15.4	27.3	56
THR	CA	B	416	8.3	16.2	26.4	59
THR	CB	B	416	9.0	16.7	25.2	59
THR	OG1	B	416	10.2	17.5	25.6	57
THR	CG2	B	416	8.2	17.6	24.3	61
THR	C	B	416	7.1	15.3	25.9	60
THR	O	B	416	7.3	14.2	25.4	59
LEU	N	B	417	5.9	15.8	26.1	62
LEU	CA	B	417	4.6	15.1	25.7	64
LEU	CB	B	417	3.6	15.1	26.8	64
LEU	CG	B	417	4.1	14.4	28.1	66
LEU	CD1	B	417	3.1	14.6	29.2	68
LEU	CD2	B	417	4.5	13.0	27.9	64
LEU	C	B	417	4.0	15.6	24.4	64
LEU	O	B	417	4.1	16.8	24.1	64
ASP	N	B	418	3.4	14.7	23.6	64
ASP	CA	B	418	2.7	15.1	22.4	65
ASP	CB	B	418	1.6	16.1	22.7	69
ASP	CG	B	418	0.5	15.6	23.6	74
ASP	OD1	B	418	−0.6	15.3	23.2	77
ASP	OD2	B	418	0.8	15.4	24.8	75
ASP	C	B	418	3.6	15.5	21.3	61
ASP	O	B	418	3.2	16.1	20.3	57
MET	N	B	419	4.9	15.3	21.4	61
MET	CA	B	419	5.9	15.8	20.4	63
MET	CB	B	419	7.3	15.2	20.7	58
MET	CG	B	419	7.9	15.6	22.0	55
MET	SD	B	419	9.6	14.9	22.1	54
MET	CE	B	419	9.2	13.2	22.4	53
MET	C	B	419	5.5	15.4	19.0	65
MET	O	B	419	6.0	16.0	18.0	65
GLU	N	B	420	4.6	14.4	18.9	67
GLU	CA	B	420	4.2	14.0	17.6	68
GLU	CB	B	420	3.6	12.6	17.6	72
GLU	CG	B	420	3.2	11.9	16.3	80
GLU	CD	B	420	4.5	11.9	15.4	84
GLU	OE1	B	420	5.0	10.8	15.1	85
GLU	OE2	B	420	4.9	13.0	15.0	86
GLU	C	B	420	3.1	14.9	16.9	65
GLU	O	B	420	3.0	15.0	15.7	61
ASP	N	B	421	2.5	15.7	17.8	63
ASP	CA	B	421	1.5	16.7	17.4	61
ASP	CB	B	421	0.6	17.1	18.5	65
ASP	CG	B	421	−0.2	15.9	19.1	71
ASP	OD1	B	421	−0.1	14.8	18.6	73
ASP	OD2	B	421	−0.8	16.1	20.1	73
ASP	C	B	421	2.2	17.9	16.8	57
ASP	O	B	421	1.6	18.9	16.3	55
CYS	N	B	422	3.5	17.9	16.9	51
CYS	CA	B	422	4.3	19.0	16.3	45
CYS	C	B	422	4.5	18.9	14.9	43
CYS	O	B	422	5.0	19.8	14.2	38
CYS	CB	B	422	5.6	19.1	17.1	42
CYS	SG	B	422	5.4	19.4	18.9	41
GLY	N	B	423	4.3	17.7	14.4	41
GLY	CA	B	423	4.5	17.4	12.9	41
GLY	C	B	423	3.3	17.9	12.1	43
GLY	O	B	423	2.1	17.8	12.6	47
TYR	N	B	424	3.6	18.5	11.0	44
TYR	CA	B	424	2.6	19.1	10.1	42
TYR	CB	B	424	3.1	20.4	9.5	44
TYR	CG	B	424	2.1	21.0	8.6	46
TYR	CD1	B	424	1.0	21.8	9.0	47
TYR	CE1	B	424	0.1	22.4	8.1	48
TYR	CD2	B	424	2.2	20.9	7.2	47
TYR	CE2	B	424	1.4	21.5	6.3	48
TYR	CZ	B	424	0.3	22.2	6.8	49
TYR	OH	B	424	−0.6	22.8	5.9	52
TYR	C	B	424	2.3	18.1	9.0	47
TYR	O	B	424	3.2	17.5	8.4	47
ASN	N	B	425	1.0	17.9	8.7	48
ASN	CA	B	425	0.7	17.0	7.6	52
ASN	CB	B	425	−0.4	16.0	8.1	51
ASN	CG	B	425	0.1	15.2	9.3	49
ASN	OD1	B	425	0.4	14.0	9.2	51
ASN	ND2	B	425	0.1	15.8	10.5	44
ASN	C	B	425	0.2	17.6	6.3	51
ASN	O	B	425	−0.7	18.5	6.4	51
CAL	Ca	M	1	26.5	−2.3	0.2	34
CAL	Ca	M	2	−13.9	−28.7	22.7	53
SCH	N1	S	1	15.2	−10.2	34.2	31
SCH	C1	S	1	13.9	−10.1	34.8	32
SCH	C2	S	1	12.8	−9.8	33.8	31
SCH	O1	S	1	13.0	−9.0	32.9	31
SCH	C3	S	1	13.9	−9.1	35.9	34
SCH	C4	S	1	12.6	−8.8	36.6	36
SCH	C5	S	1	12.6	−7.6	37.5	37
SCH	O2	S	1	13.7	−7.1	37.8	35
SCH	O3	S	1	11.6	−7.1	37.8	39
SCH	N2	S	1	11.7	−10.5	34.0	29
SCH	C6	S	1	10.6	−10.2	33.0	27
SCH	C7	S	1	9.4	−9.6	33.6	29
SCH	O4	S	1	9.1	−9.8	34.8	30
SCH	C8	S	1	10.2	−11.4	32.2	27
SCH	C9	S	1	11.1	−11.7	31.0	29
SCH	C10	S	1	10.0	−12.7	33.1	30
SCH	N3	S	1	8.7	−8.8	32.8	28
SCH	C11	S	1	7.5	−8.1	33.3	26
SCH	C12	S	1	6.5	−8.1	32.1	25
SCH	O5	S	1	6.1	−7.0	31.6	28
SCH	C13	S	1	7.8	−6.7	33.8	27
SCH	C14	S	1	8.5	−6.8	35.2	28
SCH	O6	S	1	9.8	−6.5	35.3	31
SCH	N4	S	1	7.7	−7.1	36.2	20
SCH	C15	S	1	7.6	−11.6	28.6	24
SCH	C16	S	1	7.2	−9.1	28.3	26
SCH	C17	S	1	7.0	−10.3	29.2	25
SCH	C18	S	1	5.6	−10.5	29.6	23
SCH	N5	S	1	6.1	−9.3	31.7	21
SCH	C19	S	1	5.1	−9.4	30.6	23
SCH	C20	S	1	3.7	−9.6	31.0	21
SCH	O7	S	1	3.6	−10.8	31.8	23
SCH	C21	S	1	3.2	−8.5	32.0	23
SCH	C22	S	1	1.7	−8.3	31.9	25
SCH	C23	S	1	1.2	−7.7	33.2	25
SCH	C24	S	1	1.4	−7.3	30.8	30
SCH	O8	S	1	2.0	−6.2	30.6	29
SCH	N6	S	1	0.3	−7.6	30.0	29
SCH	C25	S	1	−0.1	−6.7	29.0	32
SCH	C26	S	1	−0.6	−5.4	29.5	36
SCH	O9	S	1	−1.2	−5.4	30.6	33
SCH	C27	S	1	−1.1	−7.4	28.1	30
SCH	N7	S	1	−0.3	−4.3	28.8	46
SCH	C28	S	1	−0.8	−3.1	29.3	54
SCH	C29	S	1	−2.2	−2.8	28.9	61
SCH	O10	S	1	−2.6	−3.0	27.8	64
SCH	C30	S	1	0.1	−1.9	28.9	54
SCH	C31	S	1	1.4	−1.7	29.7	56
SCH	C32	S	1	2.1	−0.4	29.3	60
SCH	O11	S	1	1.6	0.3	28.4	59
SCH	O12	S	1	3.1	−0.1	29.9	60
SCH	N8	S	1	−3.1	−2.5	29.9	71
SCH	C33	S	1	−4.5	−2.2	29.7	79
SCH	C34	S	1	−4.7	−1.3	28.4	82
SCH	O13	S	1	−5.8	−1.5	27.8	84
SCH	C35	S	1	−5.2	−1.8	30.9	85
SCH	C36	S	1	−5.1	−0.3	31.1	89
SCH	C37	S	1	−6.2	0.6	30.8	91
SCH	C38	S	1	−3.9	0.3	31.6	91
SCH	C39	S	1	−6.1	2.0	30.9	92
SCH	C40	S	1	−3.8	1.8	31.7	92
SCH	C41	S	1	−4.9	2.6	31.4	92
SCH	O14	S	1	−3.9	−0.5	28.1	86
SCH	N1	S	2	25.2	33.9	−0.7	29
SCH	C1	S	2	24.2	33.1	0.0	31
SCH	C2	S	2	23.6	32.0	−0.8	29
SCH	O1	S	2	23.2	32.2	−2.0	30
SCH	C3	S	2	23.1	33.9	0.6	31
SCH	C4	S	2	22.1	33.2	1.4	35
SCH	C5	S	2	21.0	34.1	1.9	40
SCH	O2	S	2	21.2	35.3	2.0	43
SCH	O3	S	2	19.9	33.6	2.1	38
SCH	N2	S	2	23.6	30.8	−0.2	27
SCH	C6	S	2	23.0	29.7	−1.0	25
SCH	C7	S	2	21.7	29.1	−0.4	23
SCH	O4	S	2	21.5	29.2	0.8	25
SCH	C8	S	2	24.0	28.5	−1.2	24
SCH	C9	S	2	25.1	28.9	−2.2	23
SCH	C10	S	2	24.6	28.0	0.1	23
SCH	N3	S	2	20.8	28.7	−1.3	25
SCH	C11	S	2	19.6	28.1	−0.8	26
SCH	C12	S	2	19.2	27.0	−1.8	28
SCH	O5	S	2	18.2	27.0	−2.5	22
SCH	C13	S	2	18.5	29.2	−0.8	26
SCH	C14	S	2	18.7	30.2	0.3	26
SCH	O6	S	2	19.3	31.4	−0.1	27
SCH	N4	S	2	18.2	29.9	1.5	24
SCH	C15	S	2	23.4	25.2	−3.7	24
SCH	C16	S	2	21.4	25.5	−5.2	25
SCH	C17	S	2	21.9	25.4	−3.8	25
SCH	C18	S	2	21.2	24.3	−3.1	22
SCH	N5	S	2	20.1	25.9	−1.7	22
SCH	C19	S	2	19.8	24.8	−2.5	25
SCH	C20	S	2	19.1	23.7	−1.8	27
SCH	O7	S	2	19.9	23.2	−0.7	31
SCH	C21	S	2	17.8	24.2	−1.2	29
SCH	C22	S	2	16.8	23.1	−1.1	30
SCH	C23	S	2	15.8	23.4	0.1	31
SCH	C24	S	2	16.0	22.9	−2.4	31
SCH	O8	S	2	15.7	23.9	−3.0	28
SCH	N6	S	2	15.8	21.6	−2.7	29
SCH	C25	S	2	15.1	21.4	−4.0	32
SCH	C26	S	2	13.6	21.6	−3.8	35
SCH	O9	S	2	13.1	21.4	−2.7	32
SCH	C27	S	2	15.4	20.0	−4.5	30
SCH	N7	S	2	13.0	21.9	−4.9	38
SCH	C28	S	2	11.5	22.1	−4.8	44
SCH	C29	S	2	10.8	20.8	−4.9	47
SCH	O10	S	2	11.3	19.8	−5.5	47
SCH	C30	S	2	11.0	23.1	−5.9	43
SCH	C31	S	2	11.2	24.5	−5.6	45
SCH	C32	S	2	10.5	25.3	−6.7	48
SCH	O11	S	2	9.7	24.8	−7.4	48
SCH	O12	S	2	10.9	26.5	−6.9	49
SCH	N8	S	2	9.6	20.7	−4.3	53
SCH	C33	S	2	8.8	19.5	−4.3	55
SCH	C34	S	2	7.4	19.7	−4.0	57
SCH	O13	S	2	6.5	19.4	−4.8	58
SCH	C35	S	2	9.5	18.4	−3.5	54
SCH	C36	S	2	8.8	17.1	−3.7	54
SCH	C37	S	2	7.9	16.6	−2.8	52
SCH	C38	S	2	9.1	16.3	−4.9	52
SCH	C39	S	2	7.3	15.3	−3.0	52
SCH	C40	S	2	8.5	15.0	−5.1	53
SCH	C41	S	2	7.6	14.5	−4.1	53
SCH	O14	S	2	7.1	20.1	−2.8	59
WAT	OH2	W	1	22.7	10.9	−2.7	16
WAT	OH2	W	2	23.5	7.4	−9.0	18
WAT	OH2	W	3	20.5	18.5	−6.7	17
WAT	OH2	W	4	3.4	−22.6	39.4	23
WAT	OH2	W	5	8.2	26.5	22.1	24
WAT	OH2	W	6	25.9	30.8	7.6	16
WAT	OH2	W	7	16.6	38.5	8.0	18
WAT	OH2	W	8	20.4	31.0	3.4	22
WAT	OH2	W	9	9.5	−9.0	37.8	20
WAT	OH2	W	10	8.9	18.6	10.0	20
WAT	OH2	W	11	−6.1	−18.0	18.4	30
WAT	OH2	W	12	21.2	29.2	−4.0	20
WAT	OH2	W	13	37.9	17.2	−1.4	26
WAT	OH2	W	14	22.5	12.5	−5.9	15
WAT	OH2	W	15	28.7	34.0	22.5	21
WAT	OH2	W	16	26.9	20.4	25.3	22
WAT	OH2	W	17	17.5	17.9	3.5	18
WAT	OH2	W	18	33.9	29.2	−9.2	21
WAT	OH2	W	19	37.8	14.3	−2.5	26
WAT	OH2	W	20	16.6	16.6	−6.2	22
WAT	OH2	W	21	28.1	20.4	10.3	17
WAT	OH2	W	22	18.1	−7.2	45.4	34
WAT	OH2	W	23	4.1	−12.6	64.4	24
WAT	OH2	W	24	−3.2	−16.3	22.7	24
WAT	OH2	W	25	16.3	26.7	29.2	23
WAT	OH2	W	26	15.2	33.5	30.1	17
WAT	OH2	W	27	21.1	13.7	−11.5	19
WAT	OH2	W	28	7.0	28.1	5.9	21
WAT	OH2	W	29	12.1	23.4	4.7	30
WAT	OH2	W	30	37.3	20.3	−1.1	22
WAT	OH2	W	31	33.7	27.1	−11.3	24
WAT	OH2	W	32	38.2	18.9	−15.0	22
WAT	OH2	W	33	18.3	50.3	7.5	22
WAT	OH2	W	34	25.5	26.3	3.4	20
WAT	OH2	W	35	24.1	13.4	−20.4	34
WAT	OH2	W	36	30.6	34.8	13.5	31
WAT	OH2	W	37	−5.4	−12.9	21.0	29
WAT	OH2	W	38	8.4	−15.4	35.5	28
WAT	OH2	W	39	9.6	−7.8	30.3	30
WAT	OH2	W	40	12.8	−20.8	55.1	19
WAT	OH2	W	41	37.4	25.1	−9.7	28
WAT	OH2	W	42	35.2	7.5	−3.9	25
WAT	OH2	W	43	32.1	5.1	12.2	25
WAT	OH2	W	44	19.1	11.3	−8.4	19
WAT	OH2	W	45	21.6	11.9	−9.4	17
WAT	OH2	W	46	5.5	30.4	6.5	21
WAT	OH2	W	47	14.2	28.1	30.4	20
WAT	OH2	W	48	16.6	−24.1	51.3	31
WAT	OH2	W	49	−5.0	−18.0	25.4	29
WAT	OH2	W	50	6.0	−28.8	23.9	25
WAT	OH2	W	51	20.6	9.7	−1.3	24
WAT	OH2	W	52	11.2	−14.8	35.3	24
WAT	OH2	W	53	30.6	28.1	2.8	28
WAT	OH2	W	54	−7.4	−17.2	26.5	26
WAT	OH2	W	55	12.4	−16.8	36.7	27
WAT	OH2	W	56	34.6	32.2	−13.6	26
WAT	OH2	W	57	26.7	29.0	2.7	22
WAT	OH2	W	58	15.7	−22.1	20.6	30
WAT	OH2	W	59	6.1	19.1	9.8	28
WAT	OH2	W	60	14.2	−18.3	29.9	23
WAT	OH2	W	61	33.3	34.9	14.2	29
WAT	OH2	W	62	16.0	−19.2	46.5	23
WAT	OH2	W	63	12.6	−18.3	34.6	30
WAT	OH2	W	64	5.1	−7.3	35.8	18
WAT	OH2	W	65	23.8	10.3	−8.8	23
WAT	OH2	W	66	12.1	−12.1	62.9	27
WAT	OH2	W	67	−1.8	−27.9	49.3	25
WAT	OH2	W	68	2.7	−26.7	13.1	34
WAT	OH2	W	69	8.5	−18.3	60.2	31
WAT	OH2	W	70	19.4	−17.2	63.5	19
WAT	OH2	W	71	5.7	−25.0	41.6	20
WAT	OH2	W	72	27.1	23.3	0.8	25
WAT	OH2	W	73	−3.2	−12.6	34.6	22
WAT	OH2	W	74	20.6	12.8	−22.0	25
WAT	OH2	W	75	8.5	37.0	20.2	32
WAT	OH2	W	76	27.0	−0.9	2.0	32
WAT	OH2	W	77	4.6	30.9	9.2	29
WAT	OH2	W	78	12.9	24.6	2.2	27
WAT	OH2	W	79	10.3	−26.1	27.0	27
WAT	OH2	W	80	14.0	38.5	24.3	37
WAT	OH2	W	81	17.4	34.1	3.0	34
WAT	OH2	W	82	22.2	41.5	8.0	21
WAT	OH2	W	83	−1.1	−14.1	63.1	28
WAT	OH2	W	84	12.2	−16.9	39.2	27
WAT	OH2	W	85	12.8	−6.9	21.6	30
WAT	OH2	W	86	13.8	−13.7	24.2	31
WAT	OH2	W	87	−2.7	−9.5	25.3	32
WAT	OH2	W	88	28.8	29.5	4.3	31
WAT	OH2	W	89	28.6	22.6	25.2	33
WAT	OH2	W	90	25.4	13.2	−18.0	24
WAT	OH2	W	91	14.6	−24.7	14.4	44
WAT	OH2	W	92	18.6	−25.1	53.5	40
WAT	OH2	W	93	30.8	19.0	24.4	24
WAT	OH2	W	94	−1.9	−12.5	18.5	36
WAT	OH2	W	95	15.7	47.8	14.2	26
WAT	OH2	W	96	0.5	−5.5	36.3	31
WAT	OH2	W	97	1.0	−11.5	24.4	26
WAT	OH2	W	98	14.9	−8.0	42.0	27
WAT	OH2	W	99	9.4	−12.1	63.0	19
WAT	OH2	W	100	2.3	−15.4	58.0	24
WAT	OH2	W	101	14.5	26.6	1.2	24
WAT	OH2	W	102	11.5	43.5	20.1	31
WAT	OH2	W	103	11.4	−10.2	15.0	31
WAT	OH2	W	104	18.1	28.5	25.4	37
WAT	OH2	W	105	12.3	−3.8	45.3	28
WAT	OH2	W	106	32.4	27.9	−1.9	23
WAT	OH2	W	107	11.7	34.2	23.3	36
WAT	OH2	W	108	28.9	28.0	−8.6	31
WAT	OH2	W	109	1.0	−30.0	51.7	33
WAT	OH2	W	110	17.7	10.9	21.4	23
WAT	OH2	W	111	30.7	21.6	12.6	16
WAT	OH2	W	112	24.7	26.7	−17.4	20
WAT	OH2	W	113	31.1	28.0	−10.4	33
WAT	OH2	W	114	23.2	31.6	−16.0	30
WAT	OH2	W	115	23.4	33.4	26.9	48
WAT	OH2	W	116	21.3	38.9	25.2	24
WAT	OH2	W	117	14.0	37.7	6.4	29
WAT	OH2	W	118	32.7	23.2	24.3	41
WAT	OH2	W	119	18.7	45.3	19.3	24
WAT	OH2	W	120	18.2	−13.7	13.8	30
WAT	OH2	W	121	40.5	17.3	−14.8	30
WAT	OH2	W	122	3.1	−5.5	35.8	22
WAT	OH2	W	123	−0.9	−16.2	61.2	27
WAT	OH2	W	124	15.0	−4.9	19.8	30
WAT	OH2	W	125	27.0	30.8	10.2	26
WAT	OH2	W	126	14.3	−10.2	40.5	27
WAT	OH2	W	127	29.8	17.5	−21.7	26
WAT	OH2	W	128	−1.4	−6.2	38.4	27
WAT	OH2	W	129	−0.3	−5.8	62.9	25
WAT	OH2	W	130	−9.0	−5.0	42.8	29
WAT	OH2	W	131	17.1	7.5	−1.5	38
WAT	OH2	W	132	17.7	46.7	17.1	27
WAT	OH2	W	133	21.4	−21.8	18.7	32
WAT	OH2	W	134	17.1	27.2	1.7	35
WAT	OH2	W	135	28.0	16.8	22.2	21
WAT	OH2	W	136	26.8	−3.8	−1.7	38
WAT	OH2	W	137	27.6	15.8	26.1	30
WAT	OH2	W	138	13.0	14.7	14.4	28
WAT	OH2	W	139	17.4	−6.4	57.5	34
WAT	OH2	W	140	36.0	8.9	−12.4	35
WAT	OH2	W	141	−10.3	−13.9	44.2	28
WAT	OH2	W	142	11.6	−15.1	41.0	44
WAT	OH2	W	143	8.1	−28.5	25.7	36
WAT	OH2	W	144	5.0	28.7	11.0	27
WAT	OH2	W	145	15.9	5.5	−7.1	40
WAT	OH2	W	146	15.0	−21.8	58.2	28
WAT	OH2	W	147	18.3	−21.1	58.0	35
WAT	OH2	W	148	19.4	39.8	27.2	26
WAT	OH2	W	149	34.6	35.2	16.6	26
WAT	OH2	W	150	30.9	21.4	25.6	34
WAT	OH2	W	151	34.1	34.5	19.3	40
WAT	OH2	W	152	33.7	31.3	−11.0	32
WAT	OH2	W	153	36.7	22.4	−18.8	29
WAT	OH2	W	154	27.1	10.9	−17.6	36
WAT	OH2	W	155	10.5	−22.7	44.9	28
WAT	OH2	W	156	6.1	17.8	6.4	34
WAT	OH2	W	157	30.9	−0.7	−8.8	29
WAT	OH2	W	158	30.3	29.8	12.3	43
WAT	OH2	W	159	28.5	30.3	6.9	22
WAT	OH2	W	160	17.2	41.6	27.3	33
WAT	OH2	W	161	0.5	1.9	43.7	26
WAT	OH2	W	162	23.8	34.9	5.3	21
WAT	OH2	W	163	−3.6	−17.3	19.2	28
WAT	OH2	W	164	12.2	−23.2	13.4	41
WAT	OH2	W	165	25.0	6.5	14.1	36
WAT	OH2	W	166	10.8	−1.8	44.1	25
WAT	OH2	W	167	12.6	−13.5	60.7	35
WAT	OH2	W	168	30.0	3.7	−22.7	42
WAT	OH2	W	169	30.8	31.6	6.8	36
WAT	OH2	W	170	37.5	12.1	−19.6	36
WAT	OH2	W	171	7.5	23.8	25.5	32
WAT	OH2	W	172	15.2	−7.1	22.7	28
WAT	OH2	W	173	11.2	30.1	1.2	39
WAT	OH2	W	174	23.8	29.8	−13.2	26
WAT	OH2	W	175	18.0	−23.6	48.7	40
WAT	OH2	W	176	17.0	−18.0	20.0	41
WAT	OH2	W	177	17.4	−21.5	46.9	46
WAT	OH2	W	178	3.8	−6.8	59.1	27
WAT	OH2	W	179	15.1	−3.5	22.2	38
WAT	OH2	W	180	40.5	18.3	−1.7	45
WAT	OH2	W	181	−14.0	−20.7	50.6	37
WAT	OH2	W	182	15.0	36.1	25.4	24
WAT	OH2	W	183	−2.7	−3.3	17.9	34
WAT	OH2	W	184	37.1	33.0	−10.3	27
WAT	OH2	W	185	−1.1	−28.3	52.0	31
WAT	OH2	W	186	4.0	−4.1	38.1	26
WAT	OH2	W	187	8.6	10.1	−8.1	44
WAT	OH2	W	188	23.1	29.7	−6.3	37
WAT	OH2	W	189	−4.6	−7.2	63.1	35
WAT	OH2	W	190	13.7	6.5	13.1	21
WAT	OH2	W	191	30.7	27.8	14.2	26
WAT	OH2	W	192	15.5	−27.2	18.2	39
WAT	OH2	W	193	26.8	24.5	−18.1	33
WAT	OH2	W	194	26.2	31.6	29.3	34
WAT	OH2	W	195	32.9	49.6	17.8	41
WAT	OH2	W	196	21.7	4.3	0.7	33
WAT	OH2	W	197	−7.1	−9.0	58.5	36
WAT	OH2	W	198	16.6	3.9	15.1	43
WAT	OH2	W	199	27.9	48.9	15.6	32
WAT	OH2	W	200	−0.1	−26.3	53.6	32
WAT	OH2	W	201	6.8	−9.5	60.9	29
WAT	OH2	W	202	23.8	50.2	16.4	32
WAT	OH2	W	203	11.2	−8.5	28.2	34
WAT	OH2	W	204	35.5	34.3	−12.1	37
WAT	OH2	W	205	13.3	−6.3	40.5	35
WAT	OH2	W	206	8.2	−22.1	60.9	26
WAT	OH2	W	207	13.4	28.7	2.6	34
WAT	OH2	W	208	28.1	18.1	24.6	34
WAT	OH2	W	209	19.7	5.4	−14.5	41
WAT	OH2	W	210	14.8	−18.9	11.5	39
WAT	OH2	W	211	20.3	32.4	−2.8	45
WAT	OH2	W	212	27.8	−4.3	1.0	47
WAT	OH2	W	213	36.8	7.9	15.1	51
WAT	OH2	W	214	19.6	−15.1	22.4	51
WAT	OH2	W	215	−8.1	−7.6	42.1	28
WAT	OH2	W	216	11.8	−26.5	24.6	42
WAT	OH2	W	217	36.5	18.2	−17.4	38
WAT	OH2	W	218	−10.4	−27.3	39.0	38
WAT	OH2	W	219	7.6	35.2	26.6	34
WAT	OH2	W	220	20.9	47.8	2.0	44
WAT	OH2	W	221	−13.3	−28.9	25.1	39
WAT	OH2	W	222	12.9	−5.5	64.4	34
WAT	OH2	W	223	−4.3	−7.3	56.1	40
WAT	OH2	W	224	−7.6	−33.4	35.5	39
WAT	OH2	W	225	7.1	−17.2	31.9	21
WAT	OH2	W	226	20.2	31.6	28.2	48
WAT	OH2	W	227	12.6	−9.3	64.3	38
WAT	OH2	W	228	−11.1	−21.5	17.0	41
WAT	OH2	W	229	1.2	29.5	17.8	38
WAT	OH2	W	230	13.6	14.2	−22.1	40
WAT	OH2	W	231	20.4	9.8	21.5	31
WAT	OH2	W	232	2.9	23.2	21.5	41
WAT	OH2	W	233	2.7	−26.9	53.8	30
WAT	OH2	W	234	20.3	28.5	27.3	41
WAT	OH2	W	235	38.7	20.9	−3.7	37
WAT	OH2	W	236	29.9	36.1	25.3	34
WAT	OH2	W	237	−13.4	−27.6	35.9	43
WAT	OH2	W	238	24.2	−2.6	0.1	39
WAT	OH2	W	239	10.4	−5.0	39.0	33
WAT	OH2	W	240	21.0	43.8	25.3	25
WAT	OH2	W	241	26.3	6.5	−24.8	37
WAT	OH2	W	242	15.5	10.5	23.5	35
WAT	OH2	W	243	31.0	3.0	9.8	55
WAT	OH2	W	244	30.8	36.2	−6.4	39
WAT	OH2	W	245	19.0	−9.2	27.0	35
WAT	OH2	W	246	10.7	4.5	23.4	38
WAT	OH2	W	247	7.2	−33.2	28.9	34
WAT	OH2	W	248	20.7	−22.9	51.0	49
WAT	OH2	W	249	25.0	0.0	6.8	30
WAT	OH2	W	250	32.9	12.4	22.9	37
WAT	OH2	W	251	13.4	45.3	21.0	34
WAT	OH2	W	252	14.2	−27.9	49.0	37
WAT	OH2	W	253	19.6	−11.0	37.5	36
WAT	OH2	W	254	35.7	25.2	18.7	35
WAT	OH2	W	255	40.1	20.0	1.0	35
WAT	OH2	W	256	21.4	−22.8	54.5	43
WAT	OH2	W	257	9.2	35.5	23.8	41
WAT	OH2	W	258	15.0	47.7	16.9	41
WAT	OH2	W	259	15.8	−16.2	22.3	36
WAT	OH2	W	260	12.3	−20.6	44.3	44
WAT	OH2	W	261	37.6	25.9	−18.4	50
WAT	OH2	W	262	27.9	35.2	−8.8	41
WAT	OH2	W	263	36.7	27.9	−1.8	42
WAT	OH2	W	264	−11.7	−24.3	47.6	51
WAT	OH2	W	265	4.6	2.6	41.8	39
WAT	OH2	W	266	1.3	−13.9	11.4	44
WAT	OH2	W	267	21.2	1.7	−1.5	41
WAT	OH2	W	268	11.5	29.2	−5.5	42
WAT	OH2	W	269	12.1	17.6	−6.5	45
WAT	OH2	W	270	−12.3	−21.4	48.4	31
WAT	OH2	W	271	5.8	37.3	19.1	29
WAT	OH2	W	272	40.0	25.2	−11.2	43
WAT	OH2	W	273	30.2	38.7	−11.4	26
WAT	OH2	W	274	−3.7	−29.2	52.5	34
WAT	OH2	W	275	11.7	−21.1	11.7	40
WAT	OH2	W	276	27.6	27.2	−22.7	40
WAT	OH2	W	277	41.0	15.0	3.2	32
WAT	OH2	W	278	5.5	26.1	25.0	39
WAT	OH2	W	279	40.0	20.8	−16.0	35
WAT	OH2	W	280	13.0	17.1	−14.6	38
WAT	OH2	W	281	18.3	4.6	−11.4	41
WAT	OH2	W	282	−11.6	−13.7	61.7	46
WAT	OH2	W	283	16.1	46.2	20.2	31
WAT	OH2	W	284	6.3	14.4	6.1	34
WAT	OH2	W	285	−9.4	−4.4	39.1	34
WAT	OH2	W	286	10.4	44.5	17.8	35
WAT	OH2	W	287	10.7	12.8	−7.1	35
WAT	OH2	W	288	9.6	−29.7	47.3	44
WAT	OH2	W	289	−9.7	−29.8	42.8	35
WAT	OH2	W	290	12.1	−7.9	16.5	33
WAT	OH2	W	291	21.1	−18.9	61.8	53
WAT	OH2	W	292	24.8	32.2	−12.3	27
WAT	OH2	W	293	−0.7	0.2	41.7	36
WAT	OH2	W	294	−16.1	−19.1	42.6	47
WAT	OH2	W	295	31.0	39.5	24.1	22
WAT	OH2	W	296	16.5	−11.0	62.1	35
WAT	OH2	W	297	4.5	36.0	14.6	43
WAT	OH2	W	298	27.7	49.2	12.0	32
WAT	OH2	W	299	14.3	−26.7	38.5	42
WAT	OH2	W	300	10.4	26.2	−11.8	29
WAT	OH2	W	301	40.6	27.8	−8.2	49
WAT	OH2	W	302	15.4	−9.3	64.1	47
WAT	OH2	W	303	23.0	−21.2	50.9	36
WAT	OH2	W	304	14.7	−18.5	39.5	47
WAT	OH2	W	305	5.8	38.1	16.4	39
WAT	OH2	W	306	26.2	6.9	18.0	32
WAT	OH2	W	307	12.3	−1.6	59.3	32
WAT	OH2	W	308	43.8	16.5	−4.7	36
WAT	OH2	W	309	24.8	15.8	26.4	35
WAT	OH2	W	310	18.4	44.2	26.6	41
WAT	OH2	W	311	39.7	14.0	−19.9	34
WAT	OH2	W	312	37.4	27.0	9.0	50
WAT	OH2	W	313	−3.5	−14.5	19.8	34
WAT	OH2	W	314	−10.7	−15.4	26.2	36
WAT	OH2	W	315	9.1	−29.9	17.7	45
WAT	OH2	W	316	12.8	7.9	−1.1	34
WAT	OH2	W	317	27.9	36.5	−5.6	48
WAT	OH2	W	318	6.4	27.9	28.7	44
WAT	OH2	W	319	23.3	16.6	28.5	40
WAT	OH2	W	320	1.6	31.2	8.8	37
WAT	OH2	W	321	5.0	−17.0	61.3	53
WAT	OH2	W	322	23.8	30.9	27.6	38
WAT	OH2	W	323	0.8	−12.0	9.5	51
WAT	OH2	W	324	33.1	34.1	−4.7	40
WAT	OH2	W	325	23.5	3.6	−18.2	33
WAT	OH2	W	326	5.3	−2.3	58.0	31
WAT	OH2	W	327	17.1	−21.9	28.6	54
WAT	OH2	W	328	16.5	−7.7	26.9	43
WAT	OH2	W	329	−5.0	−10.2	63.3	52
WAT	OH2	W	330	27.0	4.3	13.9	40
WAT	OH2	W	331	42.4	17.2	1.8	61
WAT	OH2	W	332	17.3	−16.3	7.5	59
WAT	OH2	W	333	−4.5	1.6	54.6	39
WAT	OH2	W	334	38.3	24.4	8.5	49
WAT	OH2	W	335	20.1	44.6	28.9	39
WAT	OH2	W	336	36.6	26.8	13.3	60
WAT	OH2	W	337	−2.6	2.3	40.5	49
WAT	OH2	W	338	8.6	−7.5	60.8	29
WAT	OH2	W	339	2.8	−17.9	59.1	30
WAT	OH2	W	340	43.3	12.1	1.5	47
WAT	OH2	W	341	8.9	40.5	14.0	45
The structural coordinates for the above-described BACE/OM-99-2 Complex crystal are set forth below.
“Res.” refers to the amino acid whose atomic coordinates have been determined.
“At.” refers to the atom, of the corresponding residue, whose coordinates have been determined.
“Ch.” refers to the molecule to which the corresponding residue belongs
“#” refers to the amino acid number of the corresponding residue.
“X”, “Y” and Z” refer to the crystallographically determined atomic position determined for each atom.
“B” refers to a thermal factor that measures movement of the atom around its atomic center.
“WAT” is the residue name corresponding to water molecules.
“SCH” is the residue name corresponding to the OM-99-2 inhibitors. There are two BACE molecules, called “A” and “B”, each with an OM-99-2 inhibitor called “1” and “2”.
“CAL” is the residue name corresponding to the two calcium ions.

[0109] The underlying structure of the β-secretase crystals was solved using molecular replacement as implemented in CNX (MSI Inc.). The molecular replacement protocol as described in the CNX manual was followed with minor modifications. The search model consisted of molecule A from the β-secretase structure deposited in the PDB (pdb code 1FKN). Analysis of the molecular replacement solution shows two molecules in the asymmetric unit. The active site of both molecules is open and not blocked by crystal contacts.

[0110] The present invention is not to be limited in scope by specific embodiments described herein. Indeed, various modifications of the invention, in addition to those described herein will become apparent to those skilled in the art from the foregoing description. Such modifications are intended to fall within the scope of the appended claims.

[0111] Patents, patent applications, publications, product descriptions and protocols are cited throughout this application; the disclosures of which are herein incorporated by reference in their entireties for all purposes.

Claims

1. A crystal comprising a polypeptide selected from: (a) a glycosylated, human β-secretase polypeptide characterized by structural coordinates comprising a root mean square deviation of conserved residue backbone atoms of less than about 1.5 Å when superimposed on backbone atoms described by structural coordinates of Table 2; (b) a glycosylated, human β-secretase polypeptide complexed with 4(OM-99-2) characterized by structural coordinates comprising a root mean square deviation of conserved residue backbone atoms of less than about 1.5 Å when superimposed on backbone atoms described by structural coordinates of Table 3; and (c) a glycosylated, human β-secretase polypeptide which comprises a pyramidal structure.

2. A crystal of claim 1 wherein the root mean square deviation is less than about 1.0 Å.

3. A crystal of claim 2 wherein the root mean square deviation is less than about 0.5 Å.

4. A crystal of claim 3 wherein the root mean square deviation is less than about 0.1 Å.

5. A crystal of claim I comprising a polypeptide selected from: (a) a glycosylated, human, β-secretase polypeptide comprising the amino acid sequence set forth in SEQ ID NO: 1; (b) a glycosylated, human, β-secretase polypeptide comprising the amino acid sequence set forth in SEQ ID NO: 5 complexed with 5(OM-99-2); and (c) a glycosylated, human β-secretase polypeptide comprising the amino acid sequence set forth in SEQ ID NO: 4 which crystal is characterized by a pyramidal structure.

6. A crystal of claim 1 comprising a polypeptide selected from: (a) a glycosylated, human β-secretase polypeptide comprising the amino acid sequence set forth in SEQ ID NO: 1 characterized by structural coordinates of Table 2; and (b) a glycosylated, human β-secretase polypeptide comprising the amino acid sequence set forth in SEQ ID NO: 5 complexed with 6(OM-99-2) characterized by structural coordinates of Table 3.

7. A crystal of claim 1 which crystal is able to proteolytically cleave a peptide comprising the amino acid sequence KSEVNLDAEFRK (SEQ ID NO: 3).

8. A crystal of claim 1, wherein the β-secretase polypeptide comprises an active site in an open configuration.

9. A crystal of claim I which effectively diffracts x-rays for determination of structural coordinates of the polypeptide to a resolution greater than about 5 Å.

10. A computer for producing a three-dimensional representation of BACE characterized by the structural coordinates of Table 2 or BACE complexed with

11. The computer of claim 10 wherein the root mean square deviation between the homologue and the structure coordinates set forth in Table 2 or 3 is less than about 1 Å.

12. The computer of claim 11 wherein the root mean square deviation between the homologue and the structure coordinates set forth in Table 2 or 3 is less than about 0.5 Å.

13. The computer of claim 12 wherein the root mean square deviation between the homologue and the structure coordinates set forth in Table 2 or 3 is less than about 0.1 Å.

14. The computer of claim 10 wherein the display unit is displaying the three dimensional representation.

15. A method for preparing crystalline, glycosylated, human β-secretase polypeptide, comprising subjecting a composition comprising a proBACE polypeptide (SEQ ID NO: 2) to a process selected from a microbatch method and a vapor diffusion method wherein said composition is at about pH 4.0.

16. The method of claim 15, wherein the proBACE polypeptide is first purified by a process selected from anion exchange chromatography, nickel chelate chromatography and gel filtration chromatography.

17. The method of claim 15, wherein the composition further comprises a member selected from a protein stabilizing agent, a salt and a precipitant.

18. A method for obtaining structural information concerning a molecule of unknown structure, comprising generating x-ray diffraction data from a crystallized form of the molecule, and applying crystallographic phases derived from at least a portion of structure coordinates set forth in Table 2 or 3 to said x-ray diffraction pattern to generate a three-dimensional electron density map of at least a portion of the molecule.