WO2014099850A1 - FACTOR IXa 318R/A MUTANT - Google Patents

FACTOR IXa 318R/A MUTANT Download PDF

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WO2014099850A1
WO2014099850A1 PCT/US2013/075558 US2013075558W WO2014099850A1 WO 2014099850 A1 WO2014099850 A1 WO 2014099850A1 US 2013075558 W US2013075558 W US 2013075558W WO 2014099850 A1 WO2014099850 A1 WO 2014099850A1
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glu
lys
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PCT/US2013/075558
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French (fr)
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Brian Beyer
Alan Hruza
Richard Ingram
Paul Reichert
Corey Strickland
Fumihiko Saitoh
Tomokazu Hirabayashi
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Merck Sharp & Dohme Corp.
Mochida Pharmaceutical Co., Ltd.
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Publication of WO2014099850A1 publication Critical patent/WO2014099850A1/en

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    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/14—Hydrolases (3)
    • C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
    • C12N9/50—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25)
    • C12N9/64—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from animal tissue
    • C12N9/6421—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from animal tissue from mammals
    • C12N9/6424—Serine endopeptidases (3.4.21)
    • C12N9/644—Coagulation factor IXa (3.4.21.22)
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12Y—ENZYMES
    • C12Y304/00—Hydrolases acting on peptide bonds, i.e. peptidases (3.4)
    • C12Y304/21—Serine endopeptidases (3.4.21)
    • C12Y304/21022—Coagulation factor IXa (3.4.21.22)
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K38/00—Medicinal preparations containing peptides

Definitions

  • the present invention relates to a mutant polypeptide of Factor IXa wherein the mutation confers useful properties on the polypeptide.
  • fIXa Human coagulation factor IXa plays a key role in maintaining internal homeostasis in the intrinsic pathway of the clotting cascade. The importance of fIXa in homeostasis is indicated by the frequency of hemophilia, which afflicts 1 in 30,000 males.
  • Human coagulation factor IX (fIX) is a 415 residue single chain molecule circulating in the plasma. Factor IX is converted to activated factor IX (fIXa) through the cleavage of two bonds by either factor Vila or factor XIa, releasing a 35 residue activation peptide. After release of the peptide, factor IXa consists of an N-terminal light chain and a C-terminal heavy chain held together by a disulfide bond. fIXa assembles with factor Villa on the surface of endothelial cells or activated platelets forming the intrinsic Xase, a potent activator of factor X.
  • Inhibition of fIXa presents a viable way of treating thrombosis arising from both venous as well as arterial vascular injuries. It is believed that inhibiting fIXa selectively limits thrombosis at sites with low tissue factor presence, but does not inhibit clotting in high tissue factor environments such as vascular injuries of surgical wounds (McKean, M.L. & Adelman, S.J., Expert Opin Investig Drugs (1998) 7:687; Weitz J.I. & Bates S.M.J. Thromb. Haemost. (2005) 3:1843). Factor IXa-specific inhibitors could provide a choice of anticoagulants with improved therapeutic index compared to existing therapies which target thrombin.
  • factor IXa crystals bound to inhibitor compounds provides, e.g., valuable insight into the requirements for compounds that effectively bind to and inhibit factor IXa, and, thus, factor IXa-dependent clotting events.
  • Factor IXa crystals are known in the art (see U.S. Patent No. 7,968,683). Such crystals also provide useful tools of the generation of novel factor IXa complexes. Summary of the Invention
  • the present invention provides an isolated mutant factor IXa polypeptide comprising the 318R/A mutationm, optionally complexed with a compound such as complexed with:
  • polypeptide comprises the amino acid sequence set forth in SEQ ID NO: 1 .
  • isolated polynucleotides encoding such a mutant polypeptide are also within the scope of the present invention along with isolated vectors comprising the polynucleotides.
  • the present invention also providese an isolated host cell (e.g. , Chinese hamster ovary cell, Pichia or E.coli) comprising the polynucleotide, vector or mutant polypeptide.
  • a composition comprising the 318R/A Factor IXa mutant polypeptide (e.g., SEQ ID NO: 1 ) is also part of the present invention, e.g. , wherein the composition comprises a precipitant and/or is at a pH of about 9.5 or more.
  • the 318R/A mutant polypeptides of the present invention may be crystalline or non-crystalline.
  • the present invention provides an isolated crystal: (a) comprising a polypeptide that comprises the amino acid sequence of SEQ ID NO: 1 complexed with a compound represented by the
  • the present further provides a method for making a crystalline complex comprising a soaked compound bound to factor IXa protein, said method comprising soaking a crystalline composition comprising a 318R/A mutant factor IXa polypeptide of the present invention
  • compound A compound A
  • compound B compound B
  • compound C with the soaked compound, at a pH of at least about 9.5, for example, at about 9.5 (e.g., CHES/citrate buffer at about pH 9.5) such that a complex between the mutant polypeptide and the soaked compound forms.
  • a pH of at least about 9.5 for example, at about 9.5 (e.g., CHES/citrate buffer at about pH 9.5) such that a complex between the mutant polypeptide and the soaked compound forms.
  • the present inveiton also provides a method for making a crystalline complex comprising a compound bound to factor IXa protein, said method comprising: (a) heating the compound, (b) cooling the compound, (c) mixing the an 318R/A mutant Factor IXa polypeptide of the present invention (e.g., SEQ ID NO: 1 ) with the compound under conditions favorable to formation of a complex between the polypeptide and the compound; (b) crystallizing the polypeptide-compound complex.
  • an 318R/A mutant Factor IXa polypeptide of the present invention e.g., SEQ ID NO: 1
  • the present invention further comprises a method for determining the three dimensional structure of a crystalline complex comprising irradiating a crystalline complex between a 318R/A Factor IXa mutant polypeptide (e.g. , SEQ ID NO: 1 ) and a compound (e.g. , compound A, B or C or another compound, e.g., that was soaked into a crystalline complex with compound A, B or C), generating a diffraction pattern from said irradiation of said crystal, employing Fournier transformations to generate an image of the three dimensional structure.
  • a 318R/A Factor IXa mutant polypeptide e.g. , SEQ ID NO: 1
  • a compound e.g. , compound A, B or C or another compound, e.g., that was soaked into a crystalline complex with compound A, B or C
  • Fournier transformations to generate an image of the three dimensional structure.
  • the present invention also provides a method for identifying a candidate compound which binds to factor IXa or inhibits blood clotting comprising: determining the structure of a complex comprising a compound represented by structural formula A, B or C by employing the data of any one of Tables 3, 6, 9 or 12 optionally varied by a root mean square deviation of conserved residue backbone atoms or of alpha carbon atoms of less than about 1.5 A when superimposed on backbone atoms or alpha carbon atoms described in Table 3, 6, 9 or 12; and, employing a computational means to dock the candidate compound with the factor IXa serine protease domain to determine if said candidate compound binds to said serine protease domain; and, optionally, synthesizing said candidate compound; and, optionally, determining if said candidate compound binds to factor IXa or inhibits factor IXa proteolytic activity.
  • the present invention provides a crystal form of factor IXa polypeptide that is particularly useful in generating crystalline complexes with various compounds.
  • high pH e.g. , at least about pH 9.5; e.g., in CHES/citrate buffer
  • the crystals of the present invention exhibit superior affinity for the small molecule inhibitor relative to currently known factor IXa crystals.
  • a factor IXa complex with a first small molecule can be soaked with a second small molecule to generate a new complex with the second molecule.
  • the present invention further provides a method for generating factor IXa crystalline complexes comprising heating a small molecule compound to be complexed with factor IXa, and after cooling, incubating with factor IXa polypeptide; whereby a factor IXa/small molecule complex is formed.
  • the heating process increases the solubility of the small molecule and allows incubation of relatively high concentrations with the factor IXa polypeptide.
  • CHES is (Cyclohexylamino)ethanesulfonic acid; 2-[N- Cyclohexylamino]ethanesulfonic Acid.
  • the R318A mutation in a factor IXa polypeptide confers significant stability against degradation of the apo-protein when compared to the native sequence. This allows for the purification of apo-R318A and for the preparation of protein- inhibitor complexes, e.g., by soaking.
  • the present invention comprises both soluble and crystalline mutant factor IXa polypeptides wherein amino acid arginine 318 is changed to an alanine and fragments thereof, such as an 85-415 fragment, which are optionally complexed with any other molecule, for example any substrate or ligand molecule or any inhibitor molecule such as
  • a 318R/A mutant factor IXa fragment comprising amino acids 85-415 (numbering of processed factor IXa lacking signal peptide) comprises the amino acid sequence:
  • Such a polypeptide may be called "flXa 85 - 4 i 5 318R/A".
  • the 318R/A mutation, wherein arginine 318 is changed to alanine, is in bold, underscored font.
  • factor IXa or "fIXa” may include any form or type of factor IXa from any species (e.g., human).
  • the full length, unprocessed, wild-type factor IXa comprises the amino acid sequence:
  • Factor IXa is produced by activation of Factor IX through the cleavage of two bonds, releasing a 35 residue activation peptide: AETVFPDVDYVNSTEAETILDNITQSTQSFNDFTR (amino acids 192-226 of SEQ ID NO: 2).
  • the FIXa thus formed comprises a light chain: YNSGKLEEFVQGNLERECMEEKCSFEEAREVFENTERTTEFWKQYVDGDQCESNPCLNGGSCKDDINSYECWCPFGF EGKNCELDVTCNIKNGRCEQFCKNSADNKVVCSCTEGYRLAENQKSCEPAVPFPCGRVSVSQTSKLTR (amino acids 47-191 of SEQ ID NO: 2);
  • TKLT amino acids 227-461 of SEQ ID NO: 2
  • the light chain of human fIXa comprises a ⁇ -carboxyl glutamic acid (Gla) domain:
  • CTVFLDHENANKILNRPKRYNSGKLEEFVQGNLERECMEEKCSFEEAREVFENTERTTEFWKQYV (amino adds 28-92 of SEQ ID NO: 2); or, alternatively,
  • EGF epidermal growth factor
  • EGF1 DGDQCESNPCLNGGSCKDDiNSYEcwcPFGFEGKNCE (amino acids 93-129 of SEQ ID NO: 2); and EGF2: LDVTCNIKNGRCEQFCKNSADNKVVCSCTEGYRLAENQKSCE (amino acids 130-171 of SEQ ID NO: 2).
  • the heavy chain of human fIXa comprises a serine protease domain with catalytic residues Ser365, His221 , and Asp269 and helix 330: LVDRATCLR (amino acids 376-384 of SEQ ID NO: 2).
  • Protein or polypeptide sequence homology, or sequence identity is determined by optimizing residue matches, if necessary, by introducing gaps as required. See, e.g. ,
  • the present invention includes any crystal comprising crystalline flXas5 -4 i5 318R/A polypeptide that comprises less than 100% similarity or identity (e.g. , 80, 90, 91 , 92, 93, 94, 95, 96, 97, 98 or 99%) to SEQ ID NO: 1 i.e., that still comprises the 318R/A mutation.
  • sequence “identity” refers to exact matches between the amino acids of two sequences which are being compared. Sequence “similarity” refers to both exact matches between the amino acids of two polypeptides which are being compared in addition to matches between nonidentical, biochemically related amino acids.
  • biochemically related amino acids which share similar properties can fall, in an embodiment of the invention, within the following groups: polar/hydrophilic amino acids including asparagine, glutamine, serine, cysteine, threonine, lysine, arginine, histidine, aspartic acid and glutamic acid;
  • nonpolar/hydrophobic amino acids including glycine, alanine, valine, leucine, isoleucine, proline, tyrosine, phenylalanine, tryptophan and methionine; acidic amino acids including aspartic acid and glutamic acid and basic amino acids including histidine, lysine and arginine.
  • express and expression mean, in an embodiment of the invention, 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 (e.g. , an insect cell or bacterial cell such as E. coli) to form an "expression product” such as an mRNA or a protein.
  • the expression product e.g. the resulting protein, may also be referred to as "expressed".
  • the present invention comprises methods for expressing a flXas5-4i5 318R/A polypeptide in a host cell (e.g. , a mammalian cell such as a Chinese hamster ovary cell, an insect cell, a bacterial cell such as E.coli or a fungal cell such as a Pichia cell such as Pichia pastoris) comprising introducing, into the host cell, a polynucleotide encoding the polypeptide, e.g. , operably liked to a promoter, and culturing the host cell in a growth medium, e.g. , a liquid growth medium, under conditions favorable to expression of the polypeptide (e.g.
  • An insect host cell that can be used in this invention for example for expressing a flXass ⁇ -is 318R/A polypeptide includes any cell derived from an organism of the class Insecta.
  • the insect is Spodoptera fruigiperda (e.g. , Sf9 or Sf21 ) or Trichoplusia ni (e.g. , High FiveTM cells; Invitrogen; Carlsbad, CA)).
  • Other examples of insect expression systems that can be used with the present invention, for example to produce a polypeptide include Bac-To-Bac (Invitrogen Corporation, Carlsbad, CA) or Gateway (Invitrogen Corporation, Carlsbad, CA).
  • the present invention comprises a flXass ⁇ -is 318R/A protein or a flXass ⁇ -is 318R/A compound complex (e.g. , with any of compounds A, B or C) as set forth herein in a crystalline or crystallizable composition or solution.
  • the crystal complexes of the present invention exhibit a superior ability to form new complexes with other compounds,
  • Compounds that may be complexed with a polypeptide such as flXa 8 5 -4 i 5 318R/A include those represented by structural formulas A, B and C as well as other small organic compounds. Compounds may, in an embodiment of the invention, inhibit Factor IXa activity.
  • a soluble flXass ⁇ -is 318R/A polypeptide or flXass ⁇ -is 318R/A polypeptide-inhibitor preparation can contain one or more members selected from the group consisting of a precipitant, a protein stabilizing agent, a salt, a buffering agent and a reducing agent or oxygen scavenger, e.g. , that would aid in the formation of a crystalline polypeptide or complex.
  • reducing agents are dithiothreitol (DTT), dithioerythritol (DTE), ⁇ - mercaptoethanol (BME) and Tris(2-carboxyethyl)phosphine (TCEP).
  • DTT dithiothreitol
  • DTE dithioerythritol
  • BME ⁇ - mercaptoethanol
  • TCEP Tris(2-carboxyethyl)phosphine
  • the term "precipitant” can be used to refer to a change in physical or chemical parameters which decreases protein solubility, including temperature, pH and salt concentrations. Precipitants induce crystallization by forming an energetically unfavorable precipitant-depleted layer around the protein molecules. To minimize the relative amount of this depletion layer, the proteins 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 protein crystallization solution.
  • buffers such as CHES, Tris or Hepes
  • salts such as sodium chloride, lithium chloride and sodium citrate
  • Other additives include citrate, such as sodium citrate, glycerol and ethylene glycol, and detergents, such as n-octyl-p-D-glucopyranoside.
  • Various precipitants are known in the art and include the following: ammonium sulfate, ethanol, isopropanol, 3-methyl-2,4
  • pentanediol and many of the polyglycols, such as polyethylene glycol (e.g., PEG 400).
  • polyethylene glycol e.g., PEG 400
  • Crystallization of a 318R/A polypeptide or flXa 8 5-4i5 318R/A polypeptide- compound complex may be accomplished by using known methods in the art (Giege, et ai, (1994) Acta Crystallogr. D50: 339-350; McPherson, (1990) Eur. J. Biochem. 189: 1-23). Such techniques include hanging drop vapor diffusion, sitting drop vapor diffusion, microbatch and dialysis. In an embodiment of the invention, hanging-drop vapor diffusion (see e.g., McPherson, (1976) J. Biol. Chem. 251 : 6300 -6303) is used.
  • Both hanging drop and sitting drop vapor diffusion entail a droplet containing purified protein, buffer, and precipitant being allowed to equilibrate with a larger reservoir containing similar buffers and precipitants in higher concentrations.
  • the droplet of protein solution contains an insufficient concentration of precipitant for crystallization, but as water and other volatile organic components vaporize from the drop and transfers to the reservoir, the precipitant concentration increases to a level optimal for crystallization. This may occur prior to or after reaching equilibrium. Once the system is in equilibrium, these optimum conditions are maintained until the crystallization is complete.
  • the hanging drop method differs from the sitting drop method in the vertical orientation of the protein solution drop within the system.
  • a factor IXa protein preparation having a concentration of at least about 1 mg/mL ; for example, about 5 mg/mL to about 20 mg/mL (e.g., 6, 10, or 15 mg/mL ).
  • the present invention also comprises methods for using the crystals of the present invention to make a crystalline complex with a compound (e.g., a factor IXa inhibitor) comprising soaking, in a liquid medium, a crystalline composition comprising a flXas5 -4 i5 318R/A polypeptide complexed with a first compound (e.g., compound A, B or C) at an alkaline pH (e.g. , of at least about 9.5, for example, 9, 9.5, 9.75 or 10, e.g. , in the presence of CHES buffer and citrate) with a second compound, e.g. , at a molar excess of the second compound (e.g., 2 mM) relative to the first compound, such that a complex forms between flXa 8 5 -4 i5 318R/A and the second compound.
  • a compound e.g., a factor IXa inhibitor
  • the present invention also provides a method for making a crystalline complex comprising a compound (e.g. , compound A, B or C) bound to 318R/A protein, comprising (a) heating the compound, (b) cooling the compound, (c) mixing the flXas5-4i5 318R/A protein with the compound; and then (d) crystallizing a factor IXa protein- compound complex, for example, using standard crystallization methods.
  • a compound e.g. , compound A, B or C
  • the crystals of the present invention have a wide range of uses.
  • high quality crystals are suitable for X-ray or neutron diffraction analysis to determine the three dimensional structure of flXass ⁇ -is 318R/A polypeptide or flXas5-4i5 318R/A polypeptide- compound complexes.
  • Knowledge of these structures and solvent accessible residues allow structure-based design and construction of inhibitors and antagonists for factor IXa.
  • crystallization itself can be used as a purification method.
  • a polypeptide or protein crystallizes from a heterogeneous mixture into crystals. Isolation of such crystals by filtration and/or centrifugation, followed by redissolving the protein affords a purified solution suitable for use in growing high-quality crystals which are preferred for diffraction analysis.
  • 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.
  • crystals can be characterized by using X-rays produced by a conventional source, such as a sealed tube or a rotating anode.
  • characterization include, but are not limited to, precession photography, oscillation photography and diffractometer data collection.
  • the crystallizable compositions provided by this invention are amenable to X-ray crystallography for providing the three-dimensional structure of a flXass ⁇ -is 318R/A polypeptide or flXass ⁇ -is 318R/A polypeptide-compound complex.
  • the present invention includes crystals which effectively diffract X-rays for the determination of the atomic coordinates of flXa 8 5 -4 i5 318R/A polypeptide or 318R/A polypeptide-inhibitor complexes to a resolution of greater than about 5.0 Angstroms (e.g.
  • the present invention includes flXa 8 5 -4 i 5 318R/A polypeptide or 318R/A polypeptide-compound soluble (non-crystalline) or crystalline complexes whose three- dimensional structure is described by the structure coordinates set forth in any of Tables 3, 6, 9 or 12.
  • the scope of the present invention also includes crystals which possess structural coordinates which are similar to those set forth in any of Tables 3, 6, 9 or 12.
  • 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.
  • a set of structure coordinates, for a polypeptide or an polypeptide-complex or a portion thereof, is a relative set of points that define a shape in three dimensions.
  • the present invention includes crystals exhibiting structural coordinates which are similar to those set forth in any of Tables 3, 6, 9 or 12 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
  • 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 Tables 3, 6, 9 or 12, 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.
  • the Molecular Similarity application permits comparisons between different structures, different conformations of the same structure, and different parts of the same structure.
  • the procedure used in Molecular Similarity to compare structures is, in general, 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.
  • 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, Ca, C and O) or alpha carbon atoms (Ca) only for all conserved residues between the two structures being compared.
  • 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.
  • RMSD root mean square deviation
  • any set of structure coordinates of a molecule that has a RMSD of conserved residue backbone atoms (N, Ca, C, O) or alpha carbon atoms (Ca) only of less than about 1.5 A when superimposed -using backbone atoms or alpha carbon atoms ⁇ on the relevant structure coordinates of Tables 3, 6, 9 or 12 are considered identical and the crystals which they characterize are both within the scope of the present invention.
  • the root mean square deviation is less than about 1.0 A, e.g., less than about 0.5 A, e.g., less than about 0.1 A.
  • 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.
  • Recombinant factor IX (fIX) was cloned to encode the EGF2 domain, the activation peptide, and the catalytic domain corresponding to residues D85 to T415 as previously described (Hopfner et al., EMBO, 16, 6626-6635 (1997)).
  • the DNA was amplified (using manufacturer's recommended conditions) from the pCMVC-XL4 vector containing the nucleotide insert encoding the factor IX EGF2 domain, the activation peptide, and the catalytic domain corresponding to residues D85 to T415 (based on accession #
  • NM_000133.2 The PCR primers utilized were:
  • the primers produced an amplified product that contained additional nucleotides CACCATG (SEQ ID NO: 5) at the 5' end and a stop codon at the 3' end of the amplified product.
  • the PCR product was then inserted into the shuttle vector, pENTR/SD/D-TOPO (Invitrogen), according to the manufacturer's instructions. (Invitrogen, Carlsbad, CA)
  • the 318R/A mutation was introduced using a modification of the QuickChange procedure (Wang, and Malcolm, BioTechniques 26:680-682 (1999).
  • two extension reactions were performed in separate tubes; one contains the forward primer: CCAC AAAG G G G CATCAG CTTTAGTTCTTC (SEQ ID NO: 6) and the other containing the reverse primer: GAAGAACTAAAGCTGATGCCCCTTTGTGG (SEQ ID NO: 7).
  • the two reactions were mixed and the standard QUICKCHANGE mutagenisisis procedure was carried out for an additional 18 cycles.
  • the parental strand was digested with 1 Unit of Dpn1 for 1 hour and an aliquot was transformed into DH5-alpha cells.
  • the expression vector was made by the Gateway LR reaction between the pENTR/SD/D-TOPO shuttle and pDest14 vector. All vectors were sequence confirmed.
  • GKYGIYTKVSRYVNWIKEKTKLT (SEQ ID NO: 1 )
  • the activation peptide is shown in bold (corresponding to residues: 147-181 ).
  • the site of the mutation from Arginine (R) at position 318 to Alanine (A) is indicated as bold with double-underlining.
  • the EGF2 domain is shown with underlining and is part of the light chain (corresponding to residues: 81 -146 ). .
  • the R318A mutation confers significant stability against degradation of the apoprotein when compared to the native sequence. This allows for the purification of apo- R318A and for the preparation of protein-inhibitor complexes.
  • EXAMPLE 2 Expression of Human Factor IX (318R/A).
  • a colony from freshly transformed cells was grown in 10 ml terrific broth with 100 ⁇ g/ml ampicillin for 3 hours at 37°C.
  • the 10 ml of culture was then used to initiate a 1 .0 L culture with the same medium, and it was grown to an OD of approximately 1 .0 at 37°C and stored at 4°C overnight for inoculation of a 10 L tank (terrific broth containing 100 ⁇ g/ml ampicillin).
  • the 10 L culture was grown to an OD of about 0.8 - 1 .0 at 37°C, and was induced with 0.5 mM IPTG.
  • the cells were harvested by centrifugation at 5000 g after 4-6 hours and stored at -20°C.
  • EXAMPLE 4 Purification of Human Factor IX 318R/A.
  • the purification and refolding of fix was performed essentially as described by Hopfner et al. (supra).
  • the pellet from the 6 L fermentation was re-suspended in 150 ml of 50 mM Tris, pH 7.3 and lysed by 2 passes through a micro-fluidizer.
  • DNA was digested by the addition of 2 mM MgCI 2 and 1000 U Benzonase and incubated at room temperature for 30 minutes.
  • the mixture was made with 2% Triton X-100, 0.5 M NaCI and 20 mM EDTA and was incubated for an additional 30 minutes. Inclusion bodies were isolated by centrifugation at 25,000 g for 30 minutes.
  • the inclusion bodies were solubilized in 6 M guanidine HCI, 100 mM Tris-HCI, 20 mM EDTA, 150 mM oxidized glutathione /15 mM reduced glutathione, pH 8.2 at a concentration of 5.0 mg/ml and incubated for 3 hours at room temperature. After adjusting the pH to 5.0 the protein was dialyzed, at 4°C, against several changes of 6 M guanidine HCI, 100 mM Tris-HCI, 20 mM EDTA, pH 5.0.
  • the dialyzed protein was recovered and refolding was initiated by diluting 100-fold into 50 mM Tris, 0.5 M arginine, 1 mM EDTA, 20 mM CaCI 2 , 0.5 mM cysteine, pH 8.5 and incubated with gentle stirring for at least 3 days at 4° C.
  • the refolding solution was concentrated to a minimum volume using an Amicon pellicon device fitted with a 10k filter, clarified by centrifugation at 5000 g for 15 minutes and dialyzed overnight against several changes of 50 mM Tris-HCI, pH 8.0, 0.05 M NaCI.
  • the dialyzed protein was applied to a 10 ml Q-Sepharose FF column equilibrated with 50 mM Tris-HCI pH 8.0, 50 mM NaCI and the refolded rFIX was eluted with a 50-500 mM NaCI gradient.
  • the protein containing fractions were pooled, adjusted to 1 mg/ml, and stored at - 80°C.
  • EXAMPLE 5 Activation and Preparation of Factor IXa Complexes (general). Aliquots of purified fix were defrosted as needed and were activated by incubating overnight at 37°C with 20 pg/ml of Russell's Viper venom (RVV) (Sigma V2501 ). The activated protein was desalted into 50mM Tris-HCI, pH 8.0, 50mM NaCI, using a HiPrep desalting column, and applied to a HiTrap 5ml QHP column. The flow-through containing the purified fIXa was collected, concentrated to and applied to a Superdex S-200 column equilibrated with 25mM Tris-HCI, pH 8.0, 0.15M NaCI. The monomer fractions were pooled and inhibitor is added to 100 ⁇ . The protein was concentrated to 10 mg/ml (330 ⁇ ) and additional inhibitor is added to 660-1000 ⁇ .
  • RVV Russell's Viper venom
  • Compound A ( ) was prepared as a 100 mM stock solution in
  • the Factor IXa 318R/A-Compound A complex from Example 6 was crystallized using a hanging-drop vapor diffusion method.
  • the Factor IXa 318R/A-Compound A complex (0.5 ⁇ ; 1 1 mg/ml) in 25 mM Tris, pH 8.0, 0.15 M sodium chloride, 5 mM calcium chloride buffer was mixed with an equal volume of precipitant solution containing 1.0 M sodium citrate, 0.1 M CHES (N-Cyclohexyl-2-aminoethanesulfonic acid), pH 9.5, placed on the underside of a siliconized Teflon coverslip and sealed in close proximity to 0.08 mL of the precipitant solution. Crystallization plates were incubated at 18° C; crystals (0.01 x 0.05 mm) grew over 1 -18 days.
  • EXAMPLE 8 Factor IXa 318R/A-Compound A Complex Crystals.
  • Factor IXa 318R/A-Compound A complex crystals were formed M sodium citrate, 0.1 M CHES, pH 9.5 and incubation at about 18 ° C for 15 days.
  • EXAMPLE 9 Crystallographic Analysis of Factor IXa 318R/A-Compound A Complex (CHES/Citrate).
  • Factor IXa 318R/A-Com pound A Complex crystals were harvested at 4°C and transferred into the crystallization solution with 25% glycerol added. After a 5-10 minute exposure to the glycerol cryoprotectant, the crystals were frozen in liquid nitrogen. The frozen crystals were then mounted onto the X-Ray detector in a nitrogen cooled stream. X-ray diffraction was collected at the APS using IMCA-CAT 17BM beam line equipped with a Mar m165 detector. Data were integrated and scaled using the HKL package.
  • the Factor IXa 318R/A-Compound A Complex crystal structure was solved using molecular replacement (CCP4) using the search model 1 RFN. Refinement was done using the program AUTOBUSTER (Global Phasing Limited).
  • the following table contains one line for each atom in one Factor IXa 318R/A monomer.
  • the columns are: 1 ) 3-Letter amino acid code, 2) Atom name, 3) Chain, 4) Residue number, 5) X-coordinate, 6) Y-coordinate, 7) Z-coordinate, 8) B-factor.
  • Amino Acid Code NA are Sodium
  • CHE CHESS buffer
  • SCH is Compound A and HOH for water
  • HIS CA A 56 -4 -426 -108 15 ILE 0 A 64 8 -356 -156 20
  • HIS 0 A 56 -4 -417 -130 20 ILE CGI A 64 4 -380 -151 25
  • HIS CD2 A 56 -7 -399 -114 17 80 THR CA A 65 7 -329 -155 16
  • HIS CE1 A 71 -0 -167 -65 17 65 HIS NE2 A 78 13 -137 -139 35
  • ASN CA A 72 1 -185 -121 15 THR C A 79 10 -206 -86 14
  • PRO N A 90 3 -463 -74 19 100 ALA CA A 97 -10 -519 -126 43
  • PRO C A 90 2 -473 -58 24 ALA O A 97 -12 -525 -118 48
  • PRO 0 A 90 3 -482 -57 22 ALA CB A 97 -9 -532 -132 44
  • HIS C A 150 -17 -278 -150 20 GLN CA A 159 -6 -217 -58 10

Abstract

The present invention relates to mutant 318R/A factor IXa polypeptides and complexes thereof wherein the mutation confers favorable properties on the polypeptide. The polypeptides of the present invention may be soluble or crystalline. Methods of making and using the polypeptides are also provided.

Description

FACTOR IXa 318R/A Mutant
This Application claims the benefit of U.S. Provisional Patent Application No.
61/739,202, filed December 19, 2013; which is herein incorporated by reference in its entirety.
Field of the Invention
The present invention relates to a mutant polypeptide of Factor IXa wherein the mutation confers useful properties on the polypeptide. Background of the Invention
Human coagulation factor IXa (fIXa) plays a key role in maintaining internal homeostasis in the intrinsic pathway of the clotting cascade. The importance of fIXa in homeostasis is indicated by the frequency of hemophilia, which afflicts 1 in 30,000 males.
Human coagulation factor IX (fIX) is a 415 residue single chain molecule circulating in the plasma. Factor IX is converted to activated factor IX (fIXa) through the cleavage of two bonds by either factor Vila or factor XIa, releasing a 35 residue activation peptide. After release of the peptide, factor IXa consists of an N-terminal light chain and a C-terminal heavy chain held together by a disulfide bond. fIXa assembles with factor Villa on the surface of endothelial cells or activated platelets forming the intrinsic Xase, a potent activator of factor X.
Inhibition of fIXa presents a viable way of treating thrombosis arising from both venous as well as arterial vascular injuries. It is believed that inhibiting fIXa selectively limits thrombosis at sites with low tissue factor presence, but does not inhibit clotting in high tissue factor environments such as vascular injuries of surgical wounds (McKean, M.L. & Adelman, S.J., Expert Opin Investig Drugs (1998) 7:687; Weitz J.I. & Bates S.M.J. Thromb. Haemost. (2005) 3:1843). Factor IXa-specific inhibitors could provide a choice of anticoagulants with improved therapeutic index compared to existing therapies which target thrombin.
The provision of factor IXa crystals bound to inhibitor compounds provides, e.g., valuable insight into the requirements for compounds that effectively bind to and inhibit factor IXa, and, thus, factor IXa-dependent clotting events. Factor IXa crystals are known in the art (see U.S. Patent No. 7,968,683). Such crystals also provide useful tools of the generation of novel factor IXa complexes. Summary of the Invention
The present invention provides an isolated mutant factor IXa polypeptide comprising the 318R/A mutationm, optionally complexed with a compound such as complexed with:
Figure imgf000003_0001
(compound A);
(compound B); or
Figure imgf000003_0003
(compound C), e.g., comprising amino acids 85-415 and the mutation 318R/A, for example, wherein the polypeptide comprises the amino acid sequence set forth in SEQ ID NO: 1 . Isolated polynucleotides encoding such a mutant polypeptide are also within the scope of the present invention along with isolated vectors comprising the polynucleotides. The present invention also providese an isolated host cell (e.g. , Chinese hamster ovary cell, Pichia or E.coli) comprising the polynucleotide, vector or mutant polypeptide. A composition comprising the 318R/A Factor IXa mutant polypeptide (e.g., SEQ ID NO: 1 ) is also part of the present invention, e.g. , wherein the composition comprises a precipitant and/or is at a pH of about 9.5 or more. The 318R/A mutant polypeptides of the present invention may be crystalline or non-crystalline. The present invention provides an isolated crystal: (a) comprising a polypeptide that comprises the amino acid sequence of SEQ ID NO: 1 complexed with a compound represented by the
Figure imgf000003_0004
structural formula ; having unit cell dimensions a= 99.4A, b=99.4A, c=94.2A, α=β=90°, γ=120° and space group H3;
(b) comprising a polypeptide that comprises the amino acid sequence of SEQ ID NO: 1 complexed with a compound represented by the structural
Figure imgf000004_0001
having unit cell dimensions a= 98.9A, b=98.9A, c=95.4A, α=β=90°, γ =120° and space group H3;
(c) comprising a polypeptide that comprises the amino acid sequence of SEQ ID NO: 1 complexed with a compound represented by the structural
Figure imgf000004_0002
having unit cell dimensions a= 98.9A, b= 98.9A, c=
95.3A, α=β= 90°,γ= 90° and space group H3; or
(d) comprising a polypeptide that comprises the amino acid sequence of SEQ ID NO: 1 complexed with a compound represented by the structural formula
Figure imgf000004_0003
; having unit cell dimensions a= 98.9A, b=98.9A, c=93.9A, α=β= 90°, γ = 90° and space group H3, e.g., characterized by structural coordinates comprising a root mean square deviation of conserved residue backbone atoms or of alpha carbon atoms of less than about 1.5 A when superimposed on backbone atoms described in Table 3, 6, 9 or 12, e.g., characterized by the structural coordinates set forth in any of Tables 3, 6, 9 or 12, e.g., wherein the crystal can diffract X-rays for structural determination of said complex to a resolution of about 1 angstroms.
The present further provides a method for making a crystalline complex comprising a soaked compound bound to factor IXa protein, said method comprising soaking a crystalline composition comprising a 318R/A mutant factor IXa polypeptide of the present invention
Figure imgf000004_0004
xed with: compound A);
Figure imgf000004_0005
(compound B); (compound C), with the soaked compound, at a pH of at least about 9.5, for example, at about 9.5 (e.g., CHES/citrate buffer at about pH 9.5) such that a complex between the mutant polypeptide and the soaked compound forms. The present inveiton also provides a method for making a crystalline complex comprising a compound bound to factor IXa protein, said method comprising: (a) heating the compound, (b) cooling the compound, (c) mixing the an 318R/A mutant Factor IXa polypeptide of the present invention (e.g., SEQ ID NO: 1 ) with the compound under conditions favorable to formation of a complex between the polypeptide and the compound; (b) crystallizing the polypeptide-compound complex.
The present invention further comprises a method for determining the three dimensional structure of a crystalline complex comprising irradiating a crystalline complex between a 318R/A Factor IXa mutant polypeptide (e.g. , SEQ ID NO: 1 ) and a compound (e.g. , compound A, B or C or another compound, e.g., that was soaked into a crystalline complex with compound A, B or C), generating a diffraction pattern from said irradiation of said crystal, employing Fournier transformations to generate an image of the three dimensional structure.
The present invention also provides a method for identifying a candidate compound which binds to factor IXa or inhibits blood clotting comprising: determining the structure of a complex comprising a compound represented by structural formula A, B or C by employing the data of any one of Tables 3, 6, 9 or 12 optionally varied by a root mean square deviation of conserved residue backbone atoms or of alpha carbon atoms of less than about 1.5 A when superimposed on backbone atoms or alpha carbon atoms described in Table 3, 6, 9 or 12; and, employing a computational means to dock the candidate compound with the factor IXa serine protease domain to determine if said candidate compound binds to said serine protease domain; and, optionally, synthesizing said candidate compound; and, optionally, determining if said candidate compound binds to factor IXa or inhibits factor IXa proteolytic activity.
Detailed Description of the Invention
The present invention provides a crystal form of factor IXa polypeptide that is particularly useful in generating crystalline complexes with various compounds. At high pH (e.g. , at least about pH 9.5; e.g., in CHES/citrate buffer), when soaked with a small molecule inhibitor, the crystals of the present invention exhibit superior affinity for the small molecule inhibitor relative to currently known factor IXa crystals. Using such crystals, a factor IXa complex with a first small molecule can be soaked with a second small molecule to generate a new complex with the second molecule. The present invention further provides a method for generating factor IXa crystalline complexes comprising heating a small molecule compound to be complexed with factor IXa, and after cooling, incubating with factor IXa polypeptide; whereby a factor IXa/small molecule complex is formed. The heating process increases the solubility of the small molecule and allows incubation of relatively high concentrations with the factor IXa polypeptide.
CHES is (Cyclohexylamino)ethanesulfonic acid; 2-[N- Cyclohexylamino]ethanesulfonic Acid.
The R318A mutation in a factor IXa polypeptide, such as flXas5-4i5 318R/A, confers significant stability against degradation of the apo-protein when compared to the native sequence. This allows for the purification of apo-R318A and for the preparation of protein- inhibitor complexes, e.g., by soaking.
Figure imgf000006_0001
The present invention comprises both soluble and crystalline mutant factor IXa polypeptides wherein amino acid arginine 318 is changed to an alanine and fragments thereof, such as an 85-415 fragment, which are optionally complexed with any other molecule, for example any substrate or ligand molecule or any inhibitor molecule such as
Figure imgf000006_0002
(compound A);
Figure imgf000006_0003
Factor IXa is known in the art. In an embodiment of the invention, a 318R/A mutant factor IXa fragment comprising amino acids 85-415 (numbering of processed factor IXa lacking signal peptide) comprises the amino acid sequence:
DVTCNIKNGR CEQFCKNSAD NKVVCSCTEG YRLAENQKSC EPAVPFPCGR VSVSQTSKLT RAETVFPDVD YVNSTEAETI LDNITQSTQS FNDFTRVVGG EDAKPGQFPW QVVLNGKVDA FCGGSIVNEK WIVTAAHCVE TGVKITVVAG EHNIEETEHT EQKRNVIRI I PHHNYNAAIN KYNHDIALLE LDEPLVLNSY VTPICIADKE YTNIFLKFGS GYVSGWGRVF HKGASALVLQ YLRVPLVDRA TCLRSTKFTI YNNMFCAGFH EGGRDSCQGD SGGPHVTEVE GTSFLTGIIS WGEECAMKGK YGIYTKVSRY VNWIKEKTKL T
(SEQ ID NO: 1 ). Such a polypeptide may be called "flXa85-4i 5 318R/A". The 318R/A mutation, wherein arginine 318 is changed to alanine, is in bold, underscored font.
The term "factor IXa" or "fIXa" may include any form or type of factor IXa from any species (e.g., human). The full length, unprocessed, wild-type factor IXa comprises the amino acid sequence:
MQRVNMIMAE SPGLITICLL GYLLSAECTV FLDHENANKI LNRPKRYNSG KLEEFVQGNL ERECMEEKCS FEEAREVFEN TERTTEFWKQ YVDGDQCESN PCLNGGSCKD DINSYECWCP FGFEGKNCEL DVTCNIKNGR CEQFCKNSAD NKVVCSCTEG YRLAENQKSC EPAVPFPCGR VSVSQTSKLT RAETVFPDVD YVNSTEAETI LDNITQSTQS FNDFTRVVGG EDAKPGQFPW QVVLNGKVDA FCGGSIVNEK WIVTAAHCVE TGVKITVVAG EHNIEETEHT EQKRNVIRI I PHHNYNAAIN KYNHDIALLE LDEPLVLNSY VTPICIADKE YTNIFLKFGS GYVSGWGRVF HKGRSALVLQ YLRVPLVDRA TCLRSTKFTI YNNMFCAGFH EGGRDSCQGD SGGPHVTEVE GTSFLTGIIS WGEECAMKGK YGIYTKVSRY VNWIKEKTKL T
(SEQ ID NO: 2; with signal peptide underscored)
Factor IXa is produced by activation of Factor IX through the cleavage of two bonds, releasing a 35 residue activation peptide: AETVFPDVDYVNSTEAETILDNITQSTQSFNDFTR (amino acids 192-226 of SEQ ID NO: 2). The FIXa thus formed comprises a light chain: YNSGKLEEFVQGNLERECMEEKCSFEEAREVFENTERTTEFWKQYVDGDQCESNPCLNGGSCKDDINSYECWCPFGF EGKNCELDVTCNIKNGRCEQFCKNSADNKVVCSCTEGYRLAENQKSCEPAVPFPCGRVSVSQTSKLTR (amino acids 47-191 of SEQ ID NO: 2);
and a heavy chain:
VVGGEDAKPGQFPWQVVLNGKVDAFCGGSIVNEKWIVTAAHCVETGVKITVVAGEHNIEETEHTEQKRNVIRI IPHH NYNAAINKYNHDIALLELDEPLVLNSYVTPICIADKEYTNIFLKFGSGYVSGWGRVFHKGRSALVLQYLRVPLVDRA TCLRSTKFTIYNNMFCAGFHEGGRDSCQGDSGGPHVTEVEGTSFLTGI I SWGEECAMKGKYGIYTKVSRYVNWIKEK
TKLT (amino acids 227-461 of SEQ ID NO: 2); held together by a disulfide bond.
The light chain of human fIXa comprises a γ-carboxyl glutamic acid (Gla) domain:
CTVFLDHENANKILNRPKRYNSGKLEEFVQGNLERECMEEKCSFEEAREVFENTERTTEFWKQYV (amino adds 28-92 of SEQ ID NO: 2); or, alternatively,
YNSGKLEEFVQGNLERECMEEKCSFEEAREVFENTERTTEFWKQYV (amino adds 47-92 Of SEQ ID NO:
2) and two epidermal growth factor (EGF)-like domains:
EGF1 : DGDQCESNPCLNGGSCKDDiNSYEcwcPFGFEGKNCE (amino acids 93-129 of SEQ ID NO: 2); and EGF2: LDVTCNIKNGRCEQFCKNSADNKVVCSCTEGYRLAENQKSCE (amino acids 130-171 of SEQ ID NO: 2). The heavy chain of human fIXa comprises a serine protease domain with catalytic residues Ser365, His221 , and Asp269 and helix 330: LVDRATCLR (amino acids 376-384 of SEQ ID NO: 2).
Protein or polypeptide sequence 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 a/., "Time Warps, String Edits, and Macromolecules: The Theory and Practice of Sequence Comparison", Ch. 1 , Addison- Wesley, Reading, MA (1983); and software packages from IntelliGenetics, Mountain View, CA and the University of Wisconsin Genetics Computer Group (GCG), Madison, Wl.
The present invention includes any crystal comprising crystalline flXas5-4i5 318R/A polypeptide that comprises less than 100% similarity or identity (e.g. , 80, 90, 91 , 92, 93, 94, 95, 96, 97, 98 or 99%) to SEQ ID NO: 1 i.e., that still comprises the 318R/A mutation.
Sequence "identity" refers to exact matches between the amino acids of two sequences which are being compared. Sequence "similarity" refers to both exact matches between the amino acids of two polypeptides which are being compared in addition to matches between nonidentical, biochemically related amino acids. For example, biochemically related amino acids which share similar properties can fall, in an embodiment of the invention, within the following groups: polar/hydrophilic amino acids including asparagine, glutamine, serine, cysteine, threonine, lysine, arginine, histidine, aspartic acid and glutamic acid;
nonpolar/hydrophobic amino acids including glycine, alanine, valine, leucine, isoleucine, proline, tyrosine, phenylalanine, tryptophan and methionine; acidic amino acids including aspartic acid and glutamic acid and basic amino acids including histidine, lysine and arginine.
The terms "express" and "expression" mean, in an embodiment of the invention, 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 (e.g. , an insect cell or bacterial cell such as E. coli) to form an "expression product" such as an mRNA or a protein. The expression product, e.g. the resulting protein, may also be referred to as "expressed". The present invention comprises methods for expressing a flXas5-4i5 318R/A polypeptide in a host cell (e.g. , a mammalian cell such as a Chinese hamster ovary cell, an insect cell, a bacterial cell such as E.coli or a fungal cell such as a Pichia cell such as Pichia pastoris) comprising introducing, into the host cell, a polynucleotide encoding the polypeptide, e.g. , operably liked to a promoter, and culturing the host cell in a growth medium, e.g. , a liquid growth medium, under conditions favorable to expression of the polypeptide (e.g. , expression and secretion into the medium) by the cell and, optionally, purifying the polypeptide from the host cells and/or host cell growth medium. An insect host cell that can be used in this invention, for example for expressing a flXass^-is 318R/A polypeptide includes any cell derived from an organism of the class Insecta. In an embodiment of the invention, the insect is Spodoptera fruigiperda (e.g. , Sf9 or Sf21 ) or Trichoplusia ni (e.g. , High Five™ cells; Invitrogen; Carlsbad, CA)). Other examples of insect expression systems that can be used with the present invention, for example to produce a polypeptide, include Bac-To-Bac (Invitrogen Corporation, Carlsbad, CA) or Gateway (Invitrogen Corporation, Carlsbad, CA).
Crystals
The present invention comprises a flXass^-is 318R/A protein or a flXass^-is 318R/A compound complex (e.g. , with any of compounds A, B or C) as set forth herein in a crystalline or crystallizable composition or solution. The crystal complexes of the present invention exhibit a superior ability to form new complexes with other compounds,
particularly under alkaline conditions. Methods of forming such new complexes by soaking the crystalline complexes of the present invention with another compound form part of the present invention along with the soaked crystalline complexes themselves.
Compounds that may be complexed with a polypeptide such as flXa85-4i 5 318R/A include those represented by structural formulas A, B and C as well as other small organic compounds. Compounds may, in an embodiment of the invention, inhibit Factor IXa activity.
A soluble flXass^-is 318R/A polypeptide or flXass^-is 318R/A polypeptide-inhibitor preparation can contain one or more members selected from the group consisting of a precipitant, a protein stabilizing agent, a salt, a buffering agent and a reducing agent or oxygen scavenger, e.g. , that would aid in the formation of a crystalline polypeptide or complex. Examples of reducing agents are dithiothreitol (DTT), dithioerythritol (DTE), β- mercaptoethanol (BME) and Tris(2-carboxyethyl)phosphine (TCEP). A "precipitant" is a compound that decreases the solubility of a protein in a concentrated solution.
Alternatively, the term "precipitant" can be used to refer to a change in physical or chemical parameters which decreases protein solubility, including temperature, pH and salt concentrations. Precipitants induce crystallization by forming an energetically unfavorable precipitant-depleted layer around the protein molecules. To minimize the relative amount of this depletion layer, the proteins 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 protein crystallization solution. These include buffers, such as CHES, Tris or 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 protein. Other additives include citrate, such as sodium citrate, glycerol and ethylene glycol, and detergents, such as n-octyl-p-D-glucopyranoside. Various precipitants are known in the art and include the following: ammonium sulfate, ethanol, isopropanol, 3-methyl-2,4
pentanediol; and many of the polyglycols, such as polyethylene glycol (e.g., PEG 400).
Crystallization of a
Figure imgf000010_0001
318R/A polypeptide or flXa85-4i5 318R/A polypeptide- compound complex may be accomplished by using known methods in the art (Giege, et ai, (1994) Acta Crystallogr. D50: 339-350; McPherson, (1990) Eur. J. Biochem. 189: 1-23). Such techniques include hanging drop vapor diffusion, sitting drop vapor diffusion, microbatch and dialysis. In an embodiment of the invention, hanging-drop vapor diffusion (see e.g., McPherson, (1976) J. Biol. Chem. 251 : 6300 -6303) is used. Both hanging drop and sitting drop vapor diffusion entail a droplet containing purified protein, buffer, and precipitant being allowed to equilibrate with a larger reservoir containing similar buffers and precipitants in higher concentrations. Initially, the droplet of protein solution contains an insufficient concentration of precipitant for crystallization, but as water and other volatile organic components vaporize from the drop and transfers to the reservoir, the precipitant concentration increases to a level optimal for crystallization. This may occur prior to or after reaching equilibrium. Once the system is in equilibrium, these optimum conditions are maintained until the crystallization is complete. The hanging drop method differs from the sitting drop method in the vertical orientation of the protein solution drop within the system. In the microbatch method, protein is mixed with precipitants to achieve supersaturation, the vessel is sealed and set aside until crystals appear. In the dialysis method, protein 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 protein to reach supersaturation levels. It is desirable to use a factor IXa protein preparation having a concentration of at least about 1 mg/mL ; for example, about 5 mg/mL to about 20 mg/mL (e.g., 6, 10, or 15 mg/mL ).
The present invention also comprises methods for using the crystals of the present invention to make a crystalline complex with a compound (e.g., a factor IXa inhibitor) comprising soaking, in a liquid medium, a crystalline composition comprising a flXas5-4i5 318R/A polypeptide complexed with a first compound (e.g., compound A, B or C) at an alkaline pH (e.g. , of at least about 9.5, for example, 9, 9.5, 9.75 or 10, e.g. , in the presence of CHES buffer and citrate) with a second compound, e.g. , at a molar excess of the second compound (e.g., 2 mM) relative to the first compound, such that a complex forms between flXa85-4i5 318R/A and the second compound.
The present invention also provides a method for making a crystalline complex comprising a compound (e.g. , compound A, B or C) bound to
Figure imgf000011_0001
318R/A protein, comprising (a) heating the compound, (b) cooling the compound, (c) mixing the flXas5-4i5 318R/A protein with the compound; and then (d) crystallizing a factor IXa protein- compound complex, for example, using standard crystallization methods.
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 flXass^-is 318R/A polypeptide or flXas5-4i5 318R/A polypeptide- compound complexes. Knowledge of these structures and solvent accessible residues allow structure-based design and construction of inhibitors and antagonists for factor IXa.
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 protein affords a purified solution suitable for use in growing high-quality crystals which are preferred for diffraction analysis.
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.
The crystallizable compositions provided by this invention are amenable to X-ray crystallography for providing the three-dimensional structure of a flXass^-is 318R/A polypeptide or flXass^-is 318R/A polypeptide-compound complex. The present invention includes crystals which effectively diffract X-rays for the determination of the atomic coordinates of flXa85-4i5 318R/A polypeptide or
Figure imgf000011_0002
318R/A polypeptide-inhibitor complexes to a resolution of greater than about 5.0 Angstroms (e.g. , about 4.5 A , about 4.0 A , about 3 A, about 2.5 A, about 2 A, about 1 A, about 0.5 A), preferably greater than about 4.0 Angstroms (e.g., about 3 A, about 2.5 A, about 2 A, about 1 A, about 0.5 A), more preferably greater than about 2.8 Angstroms (e.g. , about 2.5 A, about 2 A, about 1 A, about 0.5 A) and most preferably greater than about 2.0 Angstroms (e.g., about 1.5 A, about 1.0 A, about 0.5 A).
The present invention includes flXa85-4i 5 318R/A polypeptide or
Figure imgf000012_0001
318R/A polypeptide-compound soluble (non-crystalline) or crystalline complexes whose three- dimensional structure is described by the structure coordinates set forth in any of Tables 3, 6, 9 or 12. The scope of the present invention also includes crystals which possess structural coordinates which are similar to those set forth in any of Tables 3, 6, 9 or 12.
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.
Those of skill in the art will understand that a set of structure coordinates, for a polypeptide or an polypeptide-complex or a portion thereof, is a relative set of points that define a shape in three dimensions.
The present invention includes crystals exhibiting structural coordinates which are similar to those set forth in any of Tables 3, 6, 9 or 12 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.
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 Tables 3, 6, 9 or 12, 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.
Various computational analyses may be necessary to determine whether a crystal is sufficiently similar to the crystals whose structural coordinates are set forth in Tables 3, 6, 9 or 12 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, CA) version 4.1 , and as described in the accompanying User's Guide.
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, in general, 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.
Generally, 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, Ca, C and O) or alpha carbon atoms (Ca) only for all conserved residues between the two structures being compared.
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.
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.
For the purpose of this invention, any set of structure coordinates of a molecule that has a RMSD of conserved residue backbone atoms (N, Ca, C, O) or alpha carbon atoms (Ca) only of less than about 1.5 A when superimposed -using backbone atoms or alpha carbon atoms ~ on the relevant structure coordinates of Tables 3, 6, 9 or 12 are considered identical and the crystals which they characterize are both within the scope of the present invention. In an embodiment of the invention, the root mean square deviation is less than about 1.0 A, e.g., less than about 0.5 A, e.g., less than about 0.1 A.
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.
Examples
The following information is provided for more clearly describing the present invention and should not be construed to limit the present invention. Any and all of the compositions and methods described below fall within the scope of the present invention. EXAMPLE 1 : Cloning of Recombinant Human factor IXa (318R/A).
Recombinant factor IX (fIX) was cloned to encode the EGF2 domain, the activation peptide, and the catalytic domain corresponding to residues D85 to T415 as previously described (Hopfner et al., EMBO, 16, 6626-6635 (1997)). The DNA was amplified (using manufacturer's recommended conditions) from the pCMVC-XL4 vector containing the nucleotide insert encoding the factor IX EGF2 domain, the activation peptide, and the catalytic domain corresponding to residues D85 to T415 (based on accession #
NM_000133.2). The PCR primers utilized were:
TCAAGTGAGCTTTGTTTTTTCCTTAATCCAG (SEQ ID NO: 3); and
CACCATGGATGTAACATGTAACATTAAGAATGGC (SEQ ID NO: 4)
The primers produced an amplified product that contained additional nucleotides CACCATG (SEQ ID NO: 5) at the 5' end and a stop codon at the 3' end of the amplified product. The PCR product was then inserted into the shuttle vector, pENTR/SD/D-TOPO (Invitrogen), according to the manufacturer's instructions. (Invitrogen, Carlsbad, CA)
The 318R/A mutation was introduced using a modification of the QuickChange procedure (Wang, and Malcolm, BioTechniques 26:680-682 (1999). In the first stage, two extension reactions were performed in separate tubes; one contains the forward primer: CCAC AAAG G G G CATCAG CTTTAGTTCTTC (SEQ ID NO: 6) and the other containing the reverse primer: GAAGAACTAAAGCTGATGCCCCTTTGTGG (SEQ ID NO: 7). After two cycles, the two reactions were mixed and the standard QUICKCHANGE mutagenisis procedure was carried out for an additional 18 cycles. Following amplification, the parental strand was digested with 1 Unit of Dpn1 for 1 hour and an aliquot was transformed into DH5-alpha cells.
The expression vector was made by the Gateway LR reaction between the pENTR/SD/D-TOPO shuttle and pDest14 vector. All vectors were sequence confirmed.
Figure imgf000014_0001
DVTCNIKNGRCEQFCKNSADNKVVCSCTEGYRLAENQKSCEPAVPFPCGRVSVSQTSKLTRAETVFPDVDYV STEA ETILDNITQSTQSFNDFTRVVGGEDAKPGQFPWQVVLNGKVDAFCGGSIVNEKWIVTAAHCVETGVKITVVAGEHNI
EETEHTEQKRNVIRI IPHHNYNAAINKYNHDIALLELDEPLVLNSYVTPICIADKEYTNIFLKFGSGYVSGWGRVFH KG^SALVLQYLRVPLVDRATCLRSTKF IYNNMFCAGFHEGGRDSCQGDSGGPHVTEVEGTSFLTGI ISWGEECAMK
GKYGIYTKVSRYVNWIKEKTKLT (SEQ ID NO: 1 )
The activation peptide is shown in bold (corresponding to residues: 147-181 ). The site of the mutation from Arginine (R) at position 318 to Alanine (A) is indicated as bold with double-underlining. The EGF2 domain is shown with underlining and is part of the light chain (corresponding to residues: 81 -146 ). .
The R318A mutation confers significant stability against degradation of the apoprotein when compared to the native sequence. This allows for the purification of apo- R318A and for the preparation of protein-inhibitor complexes.
EXAMPLE 2: Expression of Human Factor IX (318R/A).
A colony from freshly transformed cells was grown in 10 ml terrific broth with 100 μg/ml ampicillin for 3 hours at 37°C. The 10 ml of culture was then used to initiate a 1 .0 L culture with the same medium, and it was grown to an OD of approximately 1 .0 at 37°C and stored at 4°C overnight for inoculation of a 10 L tank (terrific broth containing 100 μg/ml ampicillin). The 10 L culture was grown to an OD of about 0.8 - 1 .0 at 37°C, and was induced with 0.5 mM IPTG. The cells were harvested by centrifugation at 5000 g after 4-6 hours and stored at -20°C.
EXAMPLE 4: Purification of Human Factor IX 318R/A.
The purification and refolding of fix was performed essentially as described by Hopfner et al. (supra). The pellet from the 6 L fermentation was re-suspended in 150 ml of 50 mM Tris, pH 7.3 and lysed by 2 passes through a micro-fluidizer. DNA was digested by the addition of 2 mM MgCI2 and 1000 U Benzonase and incubated at room temperature for 30 minutes. The mixture was made with 2% Triton X-100, 0.5 M NaCI and 20 mM EDTA and was incubated for an additional 30 minutes. Inclusion bodies were isolated by centrifugation at 25,000 g for 30 minutes. The inclusion bodies were solubilized in 6 M guanidine HCI, 100 mM Tris-HCI, 20 mM EDTA, 150 mM oxidized glutathione /15 mM reduced glutathione, pH 8.2 at a concentration of 5.0 mg/ml and incubated for 3 hours at room temperature. After adjusting the pH to 5.0 the protein was dialyzed, at 4°C, against several changes of 6 M guanidine HCI, 100 mM Tris-HCI, 20 mM EDTA, pH 5.0. The dialyzed protein was recovered and refolding was initiated by diluting 100-fold into 50 mM Tris, 0.5 M arginine, 1 mM EDTA, 20 mM CaCI2, 0.5 mM cysteine, pH 8.5 and incubated with gentle stirring for at least 3 days at 4° C.
The refolding solution was concentrated to a minimum volume using an Amicon pellicon device fitted with a 10k filter, clarified by centrifugation at 5000 g for 15 minutes and dialyzed overnight against several changes of 50 mM Tris-HCI, pH 8.0, 0.05 M NaCI. The dialyzed protein was applied to a 10 ml Q-Sepharose FF column equilibrated with 50 mM Tris-HCI pH 8.0, 50 mM NaCI and the refolded rFIX was eluted with a 50-500 mM NaCI gradient. The protein containing fractions were pooled, adjusted to 1 mg/ml, and stored at - 80°C.
EXAMPLE 5: Activation and Preparation of Factor IXa Complexes (general). Aliquots of purified fix were defrosted as needed and were activated by incubating overnight at 37°C with 20 pg/ml of Russell's Viper venom (RVV) (Sigma V2501 ). The activated protein was desalted into 50mM Tris-HCI, pH 8.0, 50mM NaCI, using a HiPrep desalting column, and applied to a HiTrap 5ml QHP column. The flow-through containing the purified fIXa was collected, concentrated to and applied to a Superdex S-200 column equilibrated with 25mM Tris-HCI, pH 8.0, 0.15M NaCI. The monomer fractions were pooled and inhibitor is added to 100μΜ. The protein was concentrated to 10 mg/ml (330μΜ) and additional inhibitor is added to 660-1000μΜ.
EXAMPLE 6: Preparation of Factor IXa (318R/A) +Compound A Complex.
Figure imgf000016_0001
Compound A ( ) was prepared as a 100 mM stock solution in
DMSO. Compound A was added to the S-200 Factor IXa (318R/A) monomer fraction to a concentration of 50 μΜ. The protein complex was incubated at 4°C and concentrated to 10 mg/ml after 16 hours. EXAMPLE 7: Crystallization of Factor IXa 318R/A-Compound A Complex
(CHES/Citrate).
The Factor IXa 318R/A-Compound A complex from Example 6 was crystallized using a hanging-drop vapor diffusion method. The Factor IXa 318R/A-Compound A complex (0.5 μΙ; 1 1 mg/ml) in 25 mM Tris, pH 8.0, 0.15 M sodium chloride, 5 mM calcium chloride buffer was mixed with an equal volume of precipitant solution containing 1.0 M sodium citrate, 0.1 M CHES (N-Cyclohexyl-2-aminoethanesulfonic acid), pH 9.5, placed on the underside of a siliconized Teflon coverslip and sealed in close proximity to 0.08 mL of the precipitant solution. Crystallization plates were incubated at 18° C; crystals (0.01 x 0.05 mm) grew over 1 -18 days.
EXAMPLE 8: Factor IXa 318R/A-Compound A Complex Crystals.
Factor IXa 318R/A-Compound A complex crystals (CHES/Citrate) were formed M sodium citrate, 0.1 M CHES, pH 9.5 and incubation at about 18° C for 15 days. EXAMPLE 9: Crystallographic Analysis of Factor IXa 318R/A-Compound A Complex (CHES/Citrate).
Prior to data collection, Factor IXa 318R/A-Com pound A Complex crystals were harvested at 4°C and transferred into the crystallization solution with 25% glycerol added. After a 5-10 minute exposure to the glycerol cryoprotectant, the crystals were frozen in liquid nitrogen. The frozen crystals were then mounted onto the X-Ray detector in a nitrogen cooled stream. X-ray diffraction was collected at the APS using IMCA-CAT 17BM beam line equipped with a Mar m165 detector. Data were integrated and scaled using the HKL package.
Table 1. Data Collection Statistics for Example 9.
Figure imgf000017_0001
EXAMPLE 10: Factor IXa 318R/A-Compound A Complex Structure
Determination (CHES/Citrate).
The Factor IXa 318R/A-Compound A Complex crystal structure was solved using molecular replacement (CCP4) using the search model 1 RFN. Refinement was done using the program AUTOBUSTER (Global Phasing Limited).
Table 2. Crystallization Parameters for Factor IXa 318R/A-Compound A Complex Structure Determination.
Figure imgf000017_0002
Completeness for 99.5%
Range
FREE R TEST SET COUNT & SIZE 3052 (5.0%)
Number of protein 2237
atoms
Number of solvent 182
atoms
R-factor
0.182
R-free
0.197
RMSD bond length 0.010
RMSD bond 1.10°
angles
Table 3. Crystal Structural Coordinates of Factor IXa 318R/A-Compound A Complex (CHES/Citrate).
The following table contains one line for each atom in one Factor IXa 318R/A monomer. The columns are: 1 ) 3-Letter amino acid code, 2) Atom name, 3) Chain, 4) Residue number, 5) X-coordinate, 6) Y-coordinate, 7) Z-coordinate, 8) B-factor. (Amino Acid Code NA are Sodium, CHE is CHESS buffer, SCH is Compound A and HOH for water) Note: B factors greater than 100 appear as 0 in column 8.
VAL N A 16 -10 -261 -85 12 GLY C A 19 -11 -196 -40 16
VAL CA A 16 -11 -257 -73 11 GLY 0 A 19 -12 -188 -46 16
VAL C A 16 -12 -248 -77 14 GLU N A 20 -10 -193 -36 13
VAL 0 A 16 -12 -237 -83 13 35 GLU CA A 20 -10 -180 -37 14
VAL CB A 16 -10 -251 -62 13 GLU C A 20 -8 -181 -42 15
VAL CGI A 16 -11 -247 -49 13 GLU 0 A 20 -8 -192 -41 13
VAL CG2 A 16 -9 -259 -58 13 GLU CB A 20 -10 -173 -23 16
VAL N A 17 -13 -251 -73 12 GLU CG A 20 -11 -169 -17 26
VAL CA A 17 -14 -243 -76 11 40 GLU CD A 20 -11 -166 -2 45
VAL C A 17 -15 -236 -63 14 GLU OE1 A 20 -11 -175 6 28
VAL 0 A 17 -15 -242 -52 13 GLU OE2 A 20 -10 -154 1 40
VAL CB A 17 -16 -251 -80 14 ASP N A 21 -8 -170 -48 13
VAL CGI A 17 -17 -242 -83 14 ASP CA A 21 -6 -170 -52 12
VAL CG2 A 17 -15 -260 -92 14 45 ASP C A 21 -5 -171 -40 14
GLY N A 18 -15 -223 -63 13 ASP 0 A 21 -5 -163 -30 14
GLY CA A 18 -15 -215 -51 13 ASP CB A 21 -6 -157 -59 14
GLY C A 18 -14 -212 -42 14 ASP CG A 21 -7 -154 -72 17
GLY 0 A 18 -15 -209 -30 15 ASP OD1 A 21 -6 -144 -79 20
GLY N A 19 -13 -213 -47 12 50 ASP OD2 A 21 -7 -162 -77 15
GLY CA A 19 -12 -210 -39 13 ALA N A 22 -4 -180 -41 12 ALA CA A 22 -3 -180 -31 12 TRP CE3 A 29 4 -262 29 11
ALA C A 22 -2 -168 -34 14 TRP CZ2 A 29 1 -256 31 13
ALA O A 22 -2 -163 -45 16 TRP CZ3 A 29 3 -252 38 12
ALA CB A 22 -2 -193 -33 13 65 TRP CH2 A 29 2 -250 39 12
LYS N A 23 -2 -164 -23 14 GLN N A 30 3 -272 -25 10
LYS CA A 23 -1 -155 -25 14 GLN CA A 30 2 -276 -37 10
LYS C A 23 1 -163 -28 15 GLN C A 30 3 -277 -49 11
LYS O A 23 1 -175 -25 14 GLN O A 30 4 -268 -52 13
LYS CB A 23 -0 -147 -12 16 70 GLN CB A 30 1 -265 -39 12
LYS CG A 23 -1 -137 -9 23 GLN CG A 30 0 -267 -52 11
LYS CD A 23 -1 -132 5 30 GLN CD A 30 -1 -277 -50 12
LYS CE A 23 -3 -124 8 50 GLN OE1 A 30 -2 -276 -40 14
LYS NZ A 23 -3 -121 22 65 GLN NE2 A 30 -1 -286 -60 11
PRO N A 24 2 -157 -35 14 75 VAL N A 31 3 -288 -57 10
PRO CA A 24 3 -164 -38 14 VAL CA A 31 3 -289 -70 10
PRO C A 24 4 -169 -25 15 VAL C A 31 2 -291 -80 11
PRO O A 24 4 -163 -14 16 VAL O A 31 1 -295 -77 11
PRO CB A 24 4 -153 -44 15 VAL CB A 31 5 -300 -72 12
PRO CG A 24 3 -144 -50 17 80 VAL CGI A 31 6 -297 -61 13
PRO CD A 24 2 -143 -41 15 VAL CG2 A 31 4 -314 -71 13
GLY N A 25 4 -182 -25 15 VAL N A 32 3 -288 -93 11
GLY CA A 25 4 -189 -13 14 VAL CA A 32 2 -291 -104 11
GLY C A 25 4 -193 -2 14 VAL C A 32 2 -302 -113 13
GLY O A 25 4 -196 9 13 85 VAL O A 32 4 -302 -114 13
GLN N A 26 2 -191 -4 12 VAL CB A 32 2 -279 -113 14
GLN CA A 26 1 -195 6 12 VAL CGI A 32 3 -273 -119 14
GLN C A 26 1 -210 8 12 VAL CG2 A 32 0 -282 -123 13
GLN O A 26 1 -214 19 12 LEU N A 33 2 -311 -119 12
GLN CB A 26 -0 -188 3 12 90 LEU CA A 33 2 -321 -128 13
GLN CG A 26 -1 -189 15 14 LEU C A 33 2 -317 -142 14
GLN CD A 26 -2 -183 11 19 LEU O A 33 1 -314 -144 14
GLN OE1 A 26 -3 -175 2 16 LEU CB A 33 2 -335 -124 13
GLN NE2 A 26 -3 -185 19 18 LEU CG A 33 2 -340 -110 17
PHE N A 27 1 -218 -2 10 95 LEU CD1 A 33 1 -355 -109 17
PHE CA A 27 1 -232 -2 10 LEU CD2 A 33 3 -338 -105 19
PHE C A 27 3 -238 -8 12 ASN N A 34 3 -317 -151 14
PHE O A 27 3 -243 -19 11 ASN CA A 34 2 -314 -165 14
PHE CB A 27 0 -237 -9 11 ASN C A 34 3 -326 -174 17
PHE CG A 27 -1 -232 -3 11 100 ASN O A 34 4 -332 -171 16
PHE CD1 A 27 -2 -220 -8 12 ASN CB A 34 3 -302 -169 15
PHE CD2 A 27 -2 -238 8 12 ASN CG A 34 3 -289 -162 15
PHE CE1 A 27 -3 -215 -1 13 ASN OD1 A 34 2 -287 -159 16
PHE CE2 A 27 -3 -233 14 14 ASN ND2 A 34 4 -281 -159 15
PHE CZ A 27 -4 -221 10 13 105 GLY N A 35 2 -328 -184 18
PRO N A 28 4 -236 -1 10 GLY CA A 35 2 -339 -194 19
PRO CA A 28 5 -238 -7 10 GLY C A 35 2 -334 -208 24
PRO C A 28 5 -253 -10 11 GLY O A 35 2 -323 -212 25
PRO O A 28 6 -256 -16 11 LYS N A 36 1 -342 -214 25
PRO CB A 28 6 -231 1 10 110 LYS CA A 36 0 -339 -227 26
PRO CG A 28 5 -231 15 12 LYS C A 36 -1 -328 -225 29
PRO CD A 28 4 -229 12 10 LYS O A 36 -1 -319 -233 29
TRP N A 29 4 -262 -5 10 LYS CB A 36 -0 -351 -234 30
TRP CA A 29 5 -276 -7 10 LYS CG A 36 1 -363 -236 53
TRP C A 29 4 -281 -19 11 115 LYS CD A 36 2 -362 -248 67
TRP O A 29 4 -292 -24 11 LYS CE A 36 3 -372 -248 78
TRP CB A 29 4 -284 5 10 LYS NZ A 36 4 -369 -259 85
TRP CG A 29 3 -278 10 10 VAL N A 37 -1 -327 -212 23
TRP CD1 A 29 1 -281 6 12 VAL CA A 37 -2 -317 -208 20
TRP CD2 A 29 3 -268 21 10 120 VAL C A 37 -1 -310 -196 20
TRP NE1 A 29 1 -273 13 12 VAL O A 37 -1 -317 -188 19
TRP CE2 A 29 1 -265 22 12 VAL CB A 37 -3 -323 -203 24 VAL CGI A 37 -4 -313 -195 23 ASN N A 47 10 -342 3 13
VAL CG2 A 37 -4 -329 -215 24 ASN CA A 47 11 -338 6 13
ASP N A 38 -1 -296 -195 17 ASN C A 47 12 -333 -8 15
ASP CA A 38 -1 -290 -184 17 65 ASN 0 A 47 11 -333 -18 14
ASP C A 38 -2 -290 -172 18 ASN CB A 47 12 -348 13 14
ASP 0 A 38 -3 -289 -174 16 ASN CG A 47 12 -361 6 16
ASP CB A 38 -0 -275 -188 19 ASN OD1 A 47 13 -362 -6 15
ASP CG A 38 1 -275 -198 30 ASN ND2 A 47 12 -372 14 17
ASP 0D1 A 38 2 -284 -198 29 70 GLU N A 48 13 -330 -8 15
ASP OD2 A 38 1 -265 -205 42 GLU CA A 48 14 -325 -20 16
ALA N A 39 -1 -290 -160 15 GLU C A 48 14 -334 -32 17
ALA CA A 39 -2 -290 -148 15 GLU 0 A 48 14 -330 -43 16
ALA C A 39 -3 -301 -148 15 GLU CB A 48 15 -322 -17 19
ALA 0 A 39 -4 -299 -145 15 75 GLU CG A 48 16 -312 -6 27
ALA CB A 39 -3 -276 -145 17 GLU CD A 48 16 -317 8 48
PHE N A 40 -3 -313 -152 14 GLU OE1 A 48 17 -312 15 42
PHE CA A 40 -3 -324 -152 13 GLU OE2 A 48 15 -327 11 26
PHE C A 40 -4 -330 -138 13 LYS N A 49 14 -347 -29 15
PHE 0 A 40 -5 -337 -136 14 80 LYS CA A 49 14 -357 -40 15
PHE CB A 40 -3 -335 -162 14 LYS C A 49 12 -364 -43 17
PHE CG A 40 -2 -344 -158 14 LYS O A 49 12 -372 -53 15
PHE CD1 A 40 -1 -341 -162 15 LYS CB A 49 15 -368 -38 19
PHE CD2 A 40 -2 -355 -149 15 LYS CG A 49 16 -363 -42 25
PHE CE1 A 40 1 -349 -159 15 85 LYS CD A 49 17 -365 -57 33
PHE CE2 A 40 -1 -362 -145 16 LYS CE A 49 17 -379 -60 33
PHE CZ A 40 0 -359 -150 15 LYS NZ A 49 17 -381 -75 29
CYS N A 41 -3 -328 -129 12 TRP N A 50 11 -362 -35 14
CYS CA A 41 -3 -332 -115 13 TRP CA A 50 10 -369 -36 13
CYS C A 41 -2 -323 -107 13 90 TRP C A 50 9 -361 -35 13
CYS 0 A 41 -1 -316 -112 11 TRP O A 50 9 -352 -26 14
CYS CB A 41 -2 -347 -113 13 TRP CB A 50 10 -379 -24 14
CYS SG A 41 -4 -359 -117 16 TRP CG A 50 11 -391 -26 16
GLY N A 42 -2 -325 -93 11 TRP CD1 A 50 12 -391 -21 19
GLY CA A 42 -1 -318 -84 12 95 TRP CD2 A 50 11 -403 -33 16
GLY C A 42 -0 -328 -76 12 TRP NE1 A 50 13 -403 -24 18
GLY 0 A 42 -1 -340 -78 12 TRP CE2 A 50 12 -410 -32 20
GLY N A 43 0 -323 -67 10 TRP CE3 A 50 10 -408 -41 17
GLY CA A 43 1 -332 -58 9 TRP CZ2 A 50 12 -423 -38 20
GLY C A 43 2 -323 -46 10 100 TRP CZ3 A 50 10 -421 -46 20
GLY 0 A 43 1 -311 -46 10 TRP CH2 A 50 11 -428 -45 21
SER N A 44 2 -329 -37 10 ILE N A 51 8 -365 -43 13
SER CA A 44 3 -322 -26 10 ILE CA A 51 7 -359 -44 11
SER C A 44 4 -327 -24 12 ILE C A 51 6 -370 -40 14
SER 0 A 44 5 -338 -26 12 105 ILE O A 51 6 -381 -45 14
SER CB A 44 2 -325 -13 12 ILE CB A 51 6 -354 -58 13
SER OG A 44 1 -322 -14 15 ILE CGI A 51 7 -343 -63 13
ILE N A 45 5 -317 -20 10 ILE CG2 A 51 5 -349 -60 14
ILE CA A 45 7 -320 -17 10 ILE CD1 A 51 8 -331 -54 14
ILE C A 45 7 -328 -4 12 110 VAL N A 52 4 -366 -33 12
ILE 0 A 45 6 -323 7 11 VAL CA A 52 3 -375 -31 11
ILE CB A 45 8 -307 -17 11 VAL C A 52 2 -370 -39 13
ILE CGI A 45 7 -299 -30 12 VAL O A 52 2 -358 -39 11
ILE CG2 A 45 9 -310 -13 13 VAL CB A 52 3 -378 -16 12
ILE CD1 A 45 8 -285 -29 11 115 VAL CGI A 52 2 -389 -14 13
VAL N A 46 7 -340 -5 11 VAL CG2 A 52 3 -365 -8 13
VAL CA A 46 8 -348 8 12 THR N A 53 2 -379 -46 11
VAL C A 46 9 -343 12 13 THR CA A 53 0 -376 -55 11
VAL 0 A 46 9 -341 24 13 THR C A 53 -1 -387 -54 14
VAL CB A 46 8 -363 5 14 120 THR O A 53 -1 -396 -45 13
VAL CGI A 46 8 -371 18 14 THR CB A 53 1 -372 -69 13
VAL CG2 A 46 6 -367 1 13 THR OG1 A 53 -0 -367 -77 13 THR CG2 A 53 2 -384 -76 12 LYS N A 63 6 -397 -196 37
ALA N A 54 -2 -387 -64 12 LYS CA A 63 7 -386 -192 35
ALA CA A 54 -3 -398 -65 12 LYS C A 63 6 -374 -184 33
ALA C A 54 -2 -408 -74 16 65 LYS 0 A 63 5 -367 -190 34
ALA 0 A 54 -1 -405 -85 15 LYS CB A 63 7 -380 -203 37
ALA CB A 54 -4 -393 -70 13 LYS CG A 63 9 -372 -199 53
ALA N A 55 -2 -421 -72 15 LYS CD A 63 9 -367 -211 65
ALA CA A 55 -2 -432 -81 14 LYS CE A 63 9 -352 -214 78
ALA C A 55 -3 -431 -95 16 70 LYS NZ A 63 10 -344 -205 88
ALA 0 A 55 -2 -433 -105 16 ILE N A 64 6 -373 -172 24
ALA CB A 55 -2 -445 -75 15 ILE CA A 64 6 -362 -163 22
HIS N A 56 -4 -426 -95 14 ILE C A 64 7 -352 -159 21
HIS CA A 56 -4 -426 -108 15 ILE 0 A 64 8 -356 -156 20
HIS C A 56 -4 -416 -118 20 75 ILE CB A 64 5 -369 -149 24
HIS 0 A 56 -4 -417 -130 20 ILE CGI A 64 4 -380 -151 25
HIS CB A 56 -6 -423 -107 15 ILE CG2 A 64 5 -358 -139 24
HIS CG A 56 -6 -409 -105 17 ILE CD1 A 64 4 -391 -140 38
HIS ND1 A 56 -7 -404 -92 17 THR N A 65 6 -339 -159 18
HIS CD2 A 56 -7 -399 -114 17 80 THR CA A 65 7 -329 -155 16
HIS CE1 A 56 -7 -392 -94 16 THR C A 65 7 -323 -142 16
HIS NE2 A 56 -7 -388 -107 16 THR 0 A 65 5 -321 -141 16
CYS N A 57 -3 -406 -112 17 THR CB A 65 7 -317 -165 19
CYS CA A 57 -2 -395 -120 16 THR OG1 A 65 8 -323 -177 23
CYS C A 57 -1 -400 -128 21 85 THR CG2 A 65 8 -305 -161 23
CYS 0 A 57 -1 -394 -137 21 VAL N A 66 7 -322 -131 13
CYS CB A 57 -2 -384 -110 15 VAL CA A 66 7 -316 -119 13
CYS SG A 57 -3 -374 -103 18 VAL C A 66 7 -302 -118 15
VAL N A 58 -1 -411 -123 19 VAL 0 A 66 9 -299 -121 15
VAL CA A 58 1 -415 -127 22 90 VAL CB A 66 7 -324 -107 16
VAL C A 58 1 -429 -133 32 VAL CGI A 66 7 -317 -93 16
VAL 0 A 58 2 -434 -135 31 VAL CG2 A 66 7 -338 -106 17
VAL CB A 58 2 -411 -117 27 VAL N A 67 7 -292 -114 12
VAL CGI A 58 2 -396 -115 28 VAL CA A 67 7 -278 -112 12
VAL CG2 A 58 1 -418 -104 27 95 VAL C A 67 7 -274 -98 12
GLU N A 59 -0 -435 -134 35 VAL 0 A 67 5 -274 -94 12
GLU CA A 59 -1 -449 -140 38 VAL CB A 67 6 -268 -122 15
GLU C A 59 -0 -446 -154 49 VAL CGI A 67 7 -255 -121 15
GLU 0 A 59 -1 -436 -160 50 VAL CG2 A 67 7 -273 -136 16
GLU CB A 59 -2 -452 -140 40 100 ALA N A 68 8 -272 -90 11
GLU CG A 59 -3 -458 -126 51 ALA CA A 68 8 -266 -76 11
GLU CD A 59 -4 -465 -128 69 ALA C A 68 8 -251 -77 13
GLU 0E1 A 59 -4 -477 -127 72 ALA 0 A 68 8 -246 -87 13
GLU OE2 A 59 -5 -458 -130 58 ALA CB A 68 9 -273 -67 12
THR N A 60 0 -455 -160 49 105 GLY N A 69 7 -244 -67 11
THR CA A 60 1 -454 -174 50 GLY CA A 69 7 -229 -67 11
THR C A 60 2 -447 -171 56 GLY C A 69 7 -222 -77 13
THR 0 A 60 3 -437 -164 55 GLY 0 A 69 7 -211 -81 13
THR CB A 60 0 -445 -183 63 GLU N A 70 6 -229 -82 12
THR OG1 A 60 -1 -450 -184 66 110 GLU CA A 70 5 -224 -92 13
THR CG2 A 60 1 -444 -197 62 GLU C A 70 4 -215 -85 16
GLY N A 61 3 -454 -176 53 GLU 0 A 70 3 -217 -73 14
GLY CA A 61 5 -449 -174 52 GLU CB A 70 4 -235 -100 15
GLY C A 61 5 -436 -182 54 GLU CG A 70 3 -232 -112 17
GLY 0 A 61 6 -433 -184 55 115 GLU CD A 70 4 -224 -122 16
VAL N A 62 4 -429 -187 47 GLU OE1 A 70 4 -212 -120 16
VAL CA A 62 4 -417 -195 46 GLU OE2 A 70 4 -229 -132 21
VAL C A 62 5 -405 -188 45 HIS N A 71 3 -205 -92 13
VAL 0 A 62 5 -404 -176 45 HIS CA A 71 2 -196 -88 13
VAL CB A 62 3 -413 -202 50 120 HIS C A 71 1 -194 -99 16
VAL CGI A 62 3 -398 -203 50 HIS O A 71 -0 -198 -98 15
VAL CG2 A 62 3 -420 -216 50 HIS CB A 71 3 -183 -82 14 HIS CG A 71 2 -174 -77 16 HIS ND1 A 78 14 -151 -127 33
HIS ND1 A 71 1 -177 -66 18 HIS CD2 A 78 12 -141 -128 35
HIS CD2 A 71 1 -162 -82 18 HIS CE1 A 78 14 -143 -138 34
HIS CE1 A 71 -0 -167 -65 17 65 HIS NE2 A 78 13 -137 -139 35
HIS NE2 A 71 0 -158 -74 18 THR N A 79 11 -182 -93 14
ASN N A 72 2 -187 -110 15 THR CA A 79 11 -192 -82 13
ASN CA A 72 1 -185 -121 15 THR C A 79 10 -206 -86 14
ASN C A 72 1 -194 -132 19 THR O A 79 11 -216 -78 14
ASN 0 A 72 2 -192 -137 19 70 THR CB A 79 10 -188 -71 15
ASN CB A 72 1 -170 -125 15 THR OG1 A 79 8 -188 -77 16
ASN CG A 72 -0 -167 -137 18 THR CG2 A 79 10 -174 -65 15
ASN 0D1 A 72 -0 -176 -146 18 GLU N A 80 10 -208 -99 13
ASN ND2 A 72 -1 -156 -137 22 GLU CA A 80 10 -222 -104 13
ILE N A 73 0 -204 -136 17 75 GLU C A 80 11 -230 -105 14
ILE CA A 73 1 -214 -146 18 GLU O A 80 12 -226 -109 14
ILE C A 73 1 -209 -160 26 GLU CB A 80 9 -222 -117 14
ILE 0 A 73 2 -216 -168 26 GLU CG A 80 8 -213 -118 15
ILE CB A 73 0 -228 -146 21 GLU CD A 80 8 -199 -122 32
ILE CGI A 73 -1 -226 -149 22 80 GLU OE1 A 80 9 -193 -120 29
ILE CG2 A 73 0 -235 -133 22 GLU OE2 A 80 7 -194 -129 28
ILE CD1 A 73 -2 -239 -151 24 GLN N A 81 11 -243 -101 12
GLU N A 74 1 -197 -163 24 GLN CA A 81 12 -253 -102 12
GLU CA A 74 1 -191 -176 25 GLN C A 81 11 -265 -109 15
GLU C A 74 2 -181 -177 30 85 GLN O A 81 10 -272 -103 13
GLU 0 A 74 2 -176 -188 31 GLN CB A 81 12 -258 -88 13
GLU CB A 74 -1 -185 -182 27 GLN CG A 81 13 -246 -81 12
GLU CG A 74 -1 -171 -178 41 GLN CD A 81 14 -251 -69 14
GLU CD A 74 -2 -164 -188 64 GLN OE1 A 81 14 -262 -68 17
GLU OE1 A 74 -2 -170 -196 58 90 GLN NE2 A 81 14 -242 -58 13
GLU OE2 A 74 -2 -151 -186 51 LYS N A 82 12 -267 -122 14
GLU N A 75 3 -177 -165 25 LYS CA A 82 11 -278 -130 14
GLU CA A 75 4 -167 -164 24 LYS C A 82 12 -291 -128 17
GLU C A 75 5 -173 -158 30 LYS O A 82 13 -289 -128 17
GLU 0 A 75 5 -182 -151 26 95 LYS CB A 82 11 -274 -144 16
GLU CB A 75 3 -155 -156 26 LYS CG A 82 11 -284 -155 32
GLU CG A 75 2 -147 -162 37 LYS CD A 82 11 -278 -169 44
GLU CD A 75 2 -133 -156 65 LYS CE A 82 11 -288 -180 61
GLU OE1 A 75 1 -128 -159 52 LYS NZ A 82 10 -281 -193 73
GLU OE2 A 75 3 -128 -150 69 100 ARG N A 83 11 -302 -126 15
THR N A 76 6 -167 -161 29 ARG CA A 83 12 -315 -125 15
THR CA A 76 7 -171 -155 30 ARG C A 83 11 -326 -133 18
THR C A 76 8 -161 -143 36 ARG O A 83 10 -326 -134 18
THR 0 A 76 8 -149 -146 38 ARG CB A 83 12 -319 -110 16
THR CB A 76 9 -171 -166 42 105 ARG CG A 83 13 -310 -102 17
THR OG1 A 76 8 -179 -177 43 ARG CD A 83 15 -308 -106 18
THR CG2 A 76 10 -177 -161 42 ARG NE A 83 15 -301 -96 17
GLU N A 77 8 -166 -131 30 ARG CZ A 83 15 -287 -97 16
GLU CA A 77 8 -158 -118 29 ARG NH1 A 83 15 -280 -106 17
GLU C A 77 9 -159 -110 28 110 ARG NH2 A 83 16 -281 -87 17
GLU 0 A 77 9 -153 -100 31 ASN N A 84 12 -336 -137 18
GLU CB A 77 7 -160 -109 31 ASN CA A 84 12 -347 -144 18
GLU CG A 77 5 -158 -117 40 ASN C A 84 12 -358 -134 20
GLU CD A 77 4 -166 -111 45 ASN O A 84 12 -359 -124 21
GLU OE1 A 77 4 -178 -113 21 115 ASN CB A 84 13 -352 -155 19
GLU OE2 A 77 3 -160 -105 38 ASN CG A 84 13 -342 -165 35
HIS N A 78 10 -167 -116 19 ASN OD1 A 84 12 -337 -173 31
HIS CA A 78 12 -169 -111 20 ASN ND2 A 84 14 -337 -165 33
HIS C A 78 12 -180 -100 21 VAL N A 85 11 -368 -137 21
HIS 0 A 78 13 -187 -99 22 120 VAL CA A 85 10 -379 -128 21
HIS CB A 78 12 -157 -108 25 VAL C A 85 11 -391 -133 26
HIS CG A 78 13 -149 -120 31 VAL O A 85 11 -394 -145 28 VAL CB A 85 9 -382 -128 23 HIS ND1 A 92 3 -514 -11 33
VAL CGI A 85 8 -395 -121 24 HIS CD2 A 92 1 -530 -9 33
VAL CG2 A 85 8 -370 -122 23 HIS CE1 A 92 2 -515 2 33
ILE N A 86 12 -397 -125 22 65 HIS NE2 A 92 1 -525 3 33
ILE CA A 86 13 -409 -128 23 ASN N A 93 -1 -518 -34 28
ILE C A 86 12 -422 -123 29 ASN CA A 93 -3 -522 -34 27
ILE 0 A 86 13 -432 -129 29 ASN C A 93 -4 -515 -43 28
ILE CB A 86 14 -407 -125 26 ASN O A 93 -5 -518 -44 26
ILE CGI A 86 14 -405 -109 26 70 ASN CB A 93 -3 -523 -19 28
ILE CG2 A 86 15 -396 -133 26 ASN CG A 93 -2 -532 -10 49
ILE CD1 A 86 16 -407 -104 34 ASN OD1 A 93 -2 -543 -13 42
ARG N A 87 11 -421 -113 24 ASN ND2 A 93 -2 -528 3 38
ARG CA A 87 11 -433 -107 23 TYR N A 94 -3 -504 -50 24
ARG C A 87 9 -430 -102 22 75 TYR CA A 94 -4 -497 -60 23
ARG 0 A 87 9 -419 -97 20 TYR C A 94 -4 -506 -72 28
ARG CB A 87 12 -438 -95 26 TYR O A 94 -3 -512 -77 29
ARG CG A 87 11 -452 -90 40 TYR CB A 94 -3 -484 -64 23
ARG CD A 87 13 -456 -82 55 TYR CG A 94 -4 -475 -73 22
ARG NE A 87 12 -464 -71 70 80 TYR CD1 A 94 -5 -469 -68 23
ARG CZ A 87 13 -463 -59 87 TYR CD2 A 94 -4 -474 -87 24
ARG NH1 A 87 14 -453 -57 69 TYR CE1 A 94 -6 -462 -76 25
ARG NH2 A 87 12 -470 -49 81 TYR CE2 A 94 -5 -467 -95 26
ILE N A 88 8 -440 -104 19 TYR CZ A 94 -6 -461 -90 31
ILE CA A 88 7 -438 -100 18 85 TYR OH A 94 -7 -454 -98 37
ILE C A 88 7 -450 -91 23 ASN N A 95 -5 -506 -76 28
ILE 0 A 88 7 -462 -95 22 ASN CA A 95 -6 -513 -88 30
ILE CB A 88 6 -438 -111 21 ASN C A 95 -7 -506 -94 36
ILE CGI A 88 6 -426 -121 22 ASN O A 95 -8 -508 -88 36
ILE CG2 A 88 5 -437 -106 22 90 ASN CB A 95 -6 -528 -85 34
ILE CD1 A 88 6 -426 -134 28 ASN CG A 95 -6 -537 -97 56
ILE N A 89 6 -448 -79 19 ASN OD1 A 95 -7 -534 -107 48
ILE CA A 89 6 -458 -69 17 ASN ND2 A 95 -6 -549 -95 47
ILE C A 89 4 -457 -66 21 ALA N A 96 -7 -498 -104 35
ILE 0 A 89 4 -450 -57 19 95 ALA CA A 96 -8 -490 -111 37
ILE CB A 89 7 -458 -56 20 ALA C A 96 -9 -498 -116 44
ILE CGI A 89 8 -458 -59 21 ALA O A 96 -10 -493 -116 44
ILE CG2 A 89 6 -471 -48 22 ALA CB A 96 -7 -481 -122 37
ILE CD1 A 89 9 -457 -47 25 ALA N A 97 -9 -510 -121 43
PRO N A 90 3 -463 -74 19 100 ALA CA A 97 -10 -519 -126 43
PRO CA A 90 2 -464 -70 20 ALA C A 97 -11 -523 -115 47
PRO C A 90 2 -473 -58 24 ALA O A 97 -12 -525 -118 48
PRO 0 A 90 3 -482 -57 22 ALA CB A 97 -9 -532 -132 44
PRO CB A 90 1 -469 -82 22 ILE N A 98 -11 -525 -103 41
PRO CG A 90 2 -474 -92 26 105 ILE CA A 98 -11 -528 -91 40
PRO CD A 90 4 -472 -86 21 ILE C A 98 -12 -516 -85 42
HIS N A 91 1 -470 -50 19 ILE O A 98 -13 -516 -84 41
HIS CA A 91 1 -479 -38 20 ILE CB A 98 -11 -537 -81 43
HIS C A 91 1 -493 -43 24 ILE CGI A 98 -10 -551 -87 43
HIS 0 A 91 -0 -495 -53 23 110 ILE CG2 A 98 -11 -539 -68 44
HIS CB A 91 -0 -475 -29 21 ILE CD1 A 98 -9 -557 -82 51
HIS CG A 91 -0 -481 -16 24 ASN N A 99 -11 -506 -80 37
HIS ND1 A 91 -1 -493 -14 26 ASN CA A 99 -12 -494 -74 36
HIS CD2 A 91 0 -478 -5 25 ASN C A 99 -11 -482 -77 37
HIS CE1 A 91 -1 -497 -1 25 115 ASN O A 99 -10 -483 -75 36
HIS NE2 A 91 0 -488 5 25 ASN CB A 99 -12 -496 -59 33
HIS N A 92 1 -503 -37 26 ASN CG A 99 -13 -486 -51 49
HIS CA A 92 1 -517 -41 27 ASN OD1 A 99 -12 -474 -51 34
HIS C A 92 -0 -523 -42 32 ASN ND2 A 99 -14 -490 -45 43
HIS 0 A 92 -0 -532 -50 33 120 LYS N A 100 -11 -472 -83 34
HIS CB A 92 2 -526 -33 28 LYS CA A 100 -11 -460 -87 32
HIS CG A 92 2 -524 -18 31 LYS C A 100 -10 -451 -75 31 LYS 0 A 100 -9 -444 -76 31 LEU CB A 107 6 -420 -39 14
LYS CB A 100 -11 -451 -98 36 LEU CG A 107 6 -422 -25 17
LYS CG A 100 -13 -445 -93 55 LEU CD1 A 107 6 -431 -16 16
LYS CD A 100 -13 -435 -102 70 65 LEU CD2 A 107 5 -408 -18 19
LYS CE A 100 -15 -431 -98 86 LEU N A 108 7 -400 -64 15
LYS NZ A 100 -15 -419 -105 95 LEU CA A 108 7 -397 -76 14
TYR N A 101 -11 -452 -64 26 LEU C A 108 9 -393 -72 17
TYR CA A 101 -11 -444 -52 25 LEU O A 108 9 -384 -63 16
TYR C A 101 -10 -451 -42 25 70 LEU CB A 108 7 -385 -84 14
TYR 0 A 101 -9 -444 -34 22 LEU CG A 108 5 -385 -87 17
TYR CB A 101 -12 -440 -44 27 LEU CD1 A 108 5 -372 -94 17
TYR CG A 101 -13 -431 -52 28 LEU CD2 A 108 5 -398 -96 19
TYR CD1 A 101 -13 -417 -51 29 GLU N A 109 10 -399 -77 15
TYR CD2 A 101 -14 -435 -60 30 75 GLU CA A 109 11 -396 -74 16
TYR CE1 A 101 -13 -408 -58 28 GLU C A 109 12 -386 -85 19
TYR CE2 A 101 -15 -427 -67 31 GLU O A 109 11 -389 -97 19
TYR CZ A 101 -14 -413 -66 36 GLU CB A 109 12 -408 -74 18
TYR OH A 101 -15 -404 -73 37 GLU CG A 109 14 -404 -69 17
ASN N A 102 -10 -465 -41 23 80 GLU CD A 109 15 -416 -68 35
ASN CA A 102 -9 -473 -31 22 GLU OE1 A 109 14 -427 -73 32
ASN C A 102 -7 -473 -32 21 GLU OE2 A 109 16 -414 -63 28
ASN 0 A 102 -7 -478 -42 23 LEU N A 110 12 -375 -81 16
ASN CB A 102 -10 -487 -30 23 LEU CA A 110 13 -365 -91 16
ASN CG A 102 -9 -494 -18 35 85 LEU C A 110 14 -368 -96 19
ASN OD1 A 102 -9 -489 -7 32 LEU O A 110 15 -373 -88 20
ASN ND2 A 102 -9 -508 -19 28 LEU CB A 110 13 -351 -83 16
HIS N A 103 -7 -468 -22 17 LEU CG A 110 11 -347 -79 17
HIS CA A 103 -5 -467 -22 17 LEU CD1 A 110 11 -334 -71 17
HIS C A 103 -5 -458 -33 19 90 LEU CD2 A 110 10 -347 -90 17
HIS 0 A 103 -4 -460 -38 18 ASP N A 111 14 -364 -108 17
HIS CB A 103 -5 -481 -23 18 ASP CA A 111 16 -366 -114 19
HIS CG A 103 -5 -491 -14 20 ASP C A 111 17 -359 -106 22
HIS ND1 A 103 -5 -490 0 21 ASP O A 111 18 -365 -104 22
HIS CD2 A 103 -6 -503 -16 22 95 ASP CB A 111 16 -362 -129 21
HIS CE1 A 103 -6 -501 5 21 ASP CG A 111 16 -347 -132 27
HIS NE2 A 103 -6 -509 -4 21 ASP OD1 A 111 15 -340 -125 25
ASP N A 104 -6 -447 -35 15 ASP OD2 A 111 16 -343 -142 36
ASP CA A 104 -5 -438 -46 15 GLU N A 112 17 -347 -102 18
ASP C A 104 -4 -428 -41 18 100 GLU CA A 112 18 -339 -94 17
ASP 0 A 104 -4 -416 -38 18 GLU C A 112 17 -332 -83 20
ASP CB A 104 -6 -430 -51 15 GLU O A 112 16 -329 -84 17
ASP CG A 104 -6 -422 -64 14 GLU CB A 112 18 -328 -103 19
ASP OD1 A 104 -5 -425 -70 15 GLU CG A 112 19 -333 -115 22
ASP OD2 A 104 -7 -414 -67 16 105 GLU CD A 112 20 -340 -111 35
ILE N A 105 -3 -433 -41 15 GLU OE1 A 112 21 -339 -99 30
ILE CA A 105 -2 -426 -36 13 GLU OE2 A 112 21 -347 -120 30
ILE C A 105 -0 -432 -43 16 PRO N A 113 18 -330 -71 17
ILE 0 A 105 -0 -444 -46 16 PRO CA A 113 17 -324 -60 17
ILE CB A 105 -2 -427 -20 15 110 PRO C A 113 16 -310 -62 19
ILE CGI A 105 -0 -417 -15 15 PRO O A 113 17 -302 -69 20
ILE CG2 A 105 -1 -441 -15 16 PRO CB A 113 18 -325 -49 19
ILE CD1 A 105 -1 -414 0 16 PRO CG A 113 19 -326 -56 24
ALA N A 106 1 -423 -46 14 PRO CD A 113 19 -334 -68 21
ALA CA A 106 2 -426 -53 14 115 LEU N A 114 15 -308 -55 17
ALA C A 106 3 -417 -50 16 LEU CA A 114 15 -294 -54 15
ALA 0 A 106 3 -405 -45 14 LEU C A 114 16 -287 -45 15
ALA CB A 106 2 -426 -68 15 LEU O A 114 16 -293 -36 17
LEU N A 107 4 -421 -52 15 LEU CB A 114 13 -294 -48 13
LEU CA A 107 5 -413 -49 15 120 LEU CG A 114 12 -301 -57 16
LEU C A 107 6 -412 -62 18 LEU CD1 A 114 11 -303 -49 16
LEU 0 A 107 6 -421 -70 17 LEU CD2 A 114 12 -292 -69 17 VAL N A 115 16 -274 -46 13 PRO CD A 122 10 -286 26 12
VAL CA A 115 16 -265 -37 14 ILE N A 123 6 -304 29 10
VAL C A 115 15 -259 -28 16 ILE CA A 123 5 -305 38 10
VAL 0 A 115 15 -251 -33 15 65 ILE C A 123 5 -314 49 11
VAL CB A 115 17 -254 -45 18 ILE O A 123 6 -324 47 12
VAL CGI A 115 18 -243 -35 17 ILE CB A 123 3 -310 31 11
VAL CG2 A 115 18 -260 -53 18 ILE CGI A 123 2 -309 40 10
LEU N A 116 15 -263 -15 14 ILE CG2 A 123 4 -325 25 11
LEU CA A 116 14 -258 -6 13 70 ILE CD1 A 123 2 -295 44 12
LEU C A 116 15 -243 -3 14 CYS N A 124 5 -311 62 11
LEU 0 A 116 16 -238 -1 16 CYS CA A 124 5 -320 73 10
LEU CB A 116 14 -266 7 13 CYS C A 124 4 -333 72 11
LEU CG A 116 14 -280 5 15 CYS O A 124 3 -332 68 12
LEU CD1 A 116 14 -287 19 16 75 CYS CB A 124 5 -314 86 10
LEU CD2 A 116 13 -284 -4 14 CYS SG A 124 6 -299 89 12
ASN N A 117 13 -236 -3 12 ILE N A 125 5 -344 77 12
ASN CA A 117 13 -221 -0 12 ILE CA A 125 4 -356 77 11
ASN C A 117 12 -217 4 15 ILE C A 125 4 -362 91 14
ASN 0 A 117 11 -226 6 14 80 ILE O A 125 5 -366 95 15
ASN CB A 117 14 -213 -12 12 ILE CB A 125 4 -366 66 13
ASN CG A 117 13 -215 -25 13 ILE CGI A 125 4 -360 52 13
ASN OD1 A 117 12 -215 -24 13 ILE CG2 A 125 3 -379 67 14
ASN ND2 A 117 14 -214 -36 13 ILE CD1 A 125 4 -369 40 15
SER N A 118 12 -204 6 13 85 ALA N A 126 3 -362 99 13
SER CA A 118 10 -200 10 13 ALA CA A 126 3 -367 113 14
SER C A 118 9 -204 1 14 ALA C A 126 3 -382 112 16
SER 0 A 118 8 -204 5 15 ALA O A 126 3 -388 102 15
SER CB A 118 10 -185 12 16 ALA CB A 126 2 -362 121 14
SER OG A 118 11 -182 24 22 90 ASP N A 127 3 -389 124 15
TYR N A 119 10 -206 -12 11 ASP CA A 127 3 -403 124 15
TYR CA A 119 9 -210 -22 11 ASP C A 127 2 -407 122 17
TYR C A 119 9 -225 -25 12 ASP O A 127 1 -398 120 15
TYR 0 A 119 8 -229 -32 12 ASP CB A 127 4 -409 137 16
TYR CB A 119 9 -202 -35 12 95 ASP CG A 127 3 -406 150 22
TYR CG A 119 9 -187 -33 13 ASP OD1 A 127 2 -400 150 21
TYR CD1 A 119 8 -180 -35 13 ASP OD2 A 127 3 -410 161 28
TYR CD2 A 119 10 -180 -30 15 LYS N A 128 1 -420 121 16
TYR CE1 A 119 8 -166 -34 14 LYS CA A 128 -0 -424 118 16
TYR CE2 A 119 10 -167 -28 15 100 LYS C A 128 -1 -419 128 18
TYR CZ A 119 9 -160 -29 16 LYS O A 128 -2 -414 125 18
TYR OH A 119 9 -146 -27 20 LYS CB A 128 -0 -440 118 18
VAL N A 120 10 -232 -20 11 LYS CG A 128 -1 -446 115 26
VAL CA A 120 10 -247 -23 11 LYS CD A 128 -1 -461 116 38
VAL C A 120 10 -253 -9 13 105 LYS CE A 128 -3 -467 115 58
VAL 0 A 120 11 -254 -5 13 LYS NZ A 128 -3 -481 119 74
VAL CB A 120 11 -249 -33 13 GLU N A 129 -1 -420 142 16
VAL CGI A 120 11 -263 -36 12 GLU CA A 129 -2 -415 152 17
VAL CG2 A 120 10 -241 -46 13 GLU C A 129 -2 -400 151 16
THR N A 121 9 -257 -2 11 110 GLU O A 129 -3 -397 151 16
THR CA A 121 9 -262 12 11 GLU CB A 129 -1 -419 166 19
THR C A 121 8 -274 13 12 GLU CG A 129 -2 -413 177 25
THR 0 A 121 7 -275 9 12 GLU CD A 129 -1 -417 191 44
THR CB A 121 8 -251 21 14 GLU OE1 A 129 -2 -418 200 32
THR OG1 A 121 9 -239 20 16 115 GLU OE2 A 129 -0 -418 193 36
THR CG2 A 121 9 -256 36 14 TYR N A 130 -1 -392 149 14
PRO N A 122 9 -285 20 11 TYR CA A 130 -1 -377 149 13
PRO CA A 122 8 -297 22 10 TYR C A 130 -2 -373 136 14
PRO C A 122 7 -295 31 10 TYR O A 130 -3 -364 135 13
PRO 0 A 122 7 -286 39 11 120 TYR CB A 130 0 -370 153 14
PRO CB A 122 9 -307 28 12 TYR CG A 130 -0 -365 168 12
PRO CG A 122 10 -301 26 15 TYR CD1 A 130 1 -372 178 14 TYR CD2 A 130 -1 -355 171 11 PHE CG A 137 -7 -306 144 15
TYR CE1 A 130 0 -369 191 13 PHE CD1 A 137 -7 -315 155 17
TYR CE2 A 130 -1 -351 185 13 PHE CD2 A 137 -6 -297 142 17
TYR CZ A 130 -0 -358 194 14 65 PHE CE1 A 137 -6 -315 163 18
TYR OH A 130 -0 -354 208 15 PHE CE2 A 137 -5 -297 151 19
THR N A 131 -1 -380 124 12 PHE CZ A 137 -5 -306 161 18
THR CA A 131 -2 -376 112 12 GLY N A 138 -11 -315 118 13
THR C A 131 -4 -378 113 14 GLY CA A 138 -12 -313 110 12
THR 0 A 131 -4 -369 109 13 70 GLY C A 138 -12 -302 100 14
THR CB A 131 -1 -384 100 12 GLY 0 A 138 -13 -299 94 14
THR OG1 A 131 -0 -381 99 13 SER N A 139 -11 -296 98 14
THR CG2 A 131 -2 -380 87 13 SER CA A 139 -11 -285 88 13
ASN N A 132 -4 -389 120 13 SER C A 139 -10 -285 82 15
ASN CA A 132 -5 -391 122 14 75 SER 0 A 139 -9 -284 88 15
ASN C A 132 -6 -381 132 14 SER CB A 139 -11 -272 96 16
ASN 0 A 132 -7 -376 129 14 SER OG A 139 -11 -261 87 24
ASN CB A 132 -6 -406 126 16 GLY N A 140 -10 -287 68 14
ASN CG A 132 -7 -411 127 20 GLY CA A 140 -8 -287 61 13
ASN OD1 A 132 -8 -408 118 21 80 GLY C A 140 -8 -278 49 15
ASN ND2 A 132 -7 -418 137 22 GLY O A 140 -9 -273 45 15
ILE N A 133 -5 -378 143 12 TYR N A 141 -7 -276 43 12
ILE CA A 133 -6 -367 152 12 TYR CA A 141 -7 -267 31 13
ILE C A 133 -6 -354 144 13 TYR C A 141 -7 -276 19 14
ILE 0 A 133 -7 -347 146 13 85 TYR O A 141 -6 -283 20 14
ILE CB A 133 -5 -366 164 15 TYR CB A 141 -6 -256 33 15
ILE CGI A 133 -5 -378 173 16 TYR CG A 141 -6 -245 42 19
ILE CG2 A 133 -5 -353 171 16 TYR CD1 A 141 -6 -246 56 22
ILE CD1 A 133 -4 -379 183 18 TYR CD2 A 141 -7 -234 37 22
PHE N A 134 -5 -350 136 13 90 TYR CE1 A 141 -7 -236 64 25
PHE CA A 134 -5 -338 128 12 TYR CE2 A 141 -8 -224 45 23
PHE C A 134 -6 -338 118 13 TYR CZ A 141 -8 -225 58 32
PHE 0 A 134 -7 -328 117 12 TYR OH A 141 -8 -215 66 39
PHE CB A 134 -4 -335 121 12 VAL N A 142 -7 -274 8 11
PHE CG A 134 -3 -332 130 12 95 VAL CA A 142 -7 -281 -4 11
PHE CD1 A 134 -3 -328 143 14 VAL C A 142 -7 -270 -14 12
PHE CD2 A 134 -1 -334 125 12 VAL O A 142 -7 -258 -13 13
PHE CE1 A 134 -2 -325 151 14 VAL CB A 142 -8 -289 -10 14
PHE CE2 A 134 -0 -331 133 14 VAL CGI A 142 -9 -301 -1 15
PHE CZ A 134 -0 -327 146 13 100 VAL CG2 A 142 -9 -281 -13 14
LEU N A 135 -7 -350 112 12 SER N A 143 -6 -273 -23 11
LEU CA A 135 -8 -351 104 12 SER CA A 143 -5 -263 -32 10
LEU C A 135 -9 -348 112 14 SER C A 143 -5 -270 -46 12
LEU 0 A 135 -10 -342 108 13 SER O A 143 -5 -282 -47 12
LEU CB A 135 -8 -364 97 12 105 SER CB A 143 -4 -256 -27 11
LEU CG A 135 -9 -366 88 15 SER OG A 143 -3 -266 -21 11
LEU CD1 A 135 -9 -381 83 16 GLY N A 144 -5 -262 -56 11
LEU CD2 A 135 -9 -357 75 16 GLY CA A 144 -5 -267 -69 11
LYS N A 136 -9 -354 125 12 GLY C A 144 -5 -258 -81 12
LYS CA A 136 -10 -352 134 13 110 GLY O A 144 -5 -247 -79 11
LYS C A 136 -10 -338 138 14 TRP N A 145 -4 -262 -93 11
LYS 0 A 136 -12 -335 142 14 TRP CA A 145 -5 -255 -105 12
LYS CB A 136 -10 -361 146 15 TRP C A 145 -6 -262 -114 13
LYS CG A 136 -10 -376 144 19 TRP O A 145 -6 -259 -126 13
LYS CD A 136 -10 -383 157 22 115 TRP CB A 145 -3 -254 -114 11
LYS CE A 136 -9 -397 156 29 TRP CG A 145 -2 -244 -108 11
LYS NZ A 136 -10 -406 152 30 TRP CD1 A 145 -2 -230 -110 14
PHE N A 137 -9 -329 136 12 TRP CD2 A 145 -1 -247 -99 11
PHE CA A 137 -10 -314 139 13 TRP NE1 A 145 -1 -225 -103 13
PHE C A 137 -11 -310 130 15 120 TRP CE2 A 145 -1 -235 -96 13
PHE 0 A 137 -12 -300 134 15 TRP CE3 A 145 -1 -259 -93 11
PHE CB A 137 -9 -306 135 14 TRP CZ2 A 145 0 -234 -88 12 TRP CZ3 A 145 0 -258 -85 12 ARG 0 A 153 -11 -237 -150 14
TRP CH2 A 145 1 -246 -83 13 ARG CB A 153 -11 -221 -177 14
GLY N A 146 -7 -269 -107 11 SER N A 154 -9 -244 -165 13
GLY CA A 146 -8 -276 -114 12 65 SER CA A 154 -8 -246 -154 12
GLY C A 146 -9 -266 -119 14 SER C A 154 -8 -232 -148 15
GLY 0 A 146 -9 -254 -117 12 SER 0 A 154 -8 -221 -155 15
ARG N A 147 -10 -272 -125 12 SER CB A 154 -7 -251 -160 14
ARG CA A 147 -11 -263 -131 12 SER OG A 154 -7 -264 -165 20
ARG C A 147 -12 -255 -121 14 70 ALA N A 155 -7 -232 -136 13
ARG 0 A 147 -12 -259 -109 13 ALA CA A 155 -7 -220 -129 13
ARG CB A 147 -12 -273 -137 14 ALA C A 155 -6 -215 -135 16
ARG CG A 147 -11 -282 -149 14 ALA 0 A 155 -5 -223 -140 17
ARG CD A 147 -13 -288 -155 15 ALA CB A 155 -7 -222 -114 14
ARG NE A 147 -12 -299 -165 17 75 LEU N A 156 -5 -202 -134 16
ARG CZ A 147 -12 -297 -178 22 LEU CA A 156 -4 -196 -138 17
ARG NH1 A 147 -13 -285 -183 20 LEU C A 156 -3 -195 -125 15
ARG NH2 A 147 -12 -307 -186 21 LEU 0 A 156 -2 -201 -124 16
VAL N A 148 -12 -242 -124 12 LEU CB A 156 -4 -183 -145 19
VAL CA A 148 -13 -233 -115 12 80 LEU CG A 156 -5 -183 -160 26
VAL C A 148 -14 -234 -116 15 LEU CD1 A 156 -4 -169 -166 27
VAL 0 A 148 -15 -227 -107 15 LEU CD2 A 156 -4 -193 -168 34
VAL CB A 148 -12 -219 -116 14 VAL N A 157 -4 -188 -115 14
VAL CGI A 148 -10 -219 -113 15 VAL CA A 157 -3 -186 -102 13
VAL CG2 A 148 -12 -212 -130 14 85 VAL C A 157 -4 -197 -93 13
PHE N A 149 -15 -241 -125 14 VAL 0 A 157 -5 -201 -93 13
PHE CA A 149 -16 -245 -126 14 VAL CB A 157 -4 -172 -96 17
PHE C A 149 -16 -259 -131 17 VAL CGI A 157 -3 -170 -82 17
PHE 0 A 149 -15 -263 -138 15 VAL CG2 A 157 -3 -161 -105 17
PHE CB A 149 -17 -236 -136 16 90 LEU N A 158 -3 -203 -85 11
PHE CG A 149 -17 -221 -133 15 LEU CA A 158 -3 -214 -76 10
PHE CD1 A 149 -16 -212 -139 18 LEU C A 158 -4 -210 -67 11
PHE CD2 A 149 -18 -217 -122 18 LEU 0 A 158 -4 -199 -62 11
PHE CE1 A 149 -16 -198 -136 20 LEU CB A 158 -2 -216 -67 10
PHE CE2 A 149 -18 -204 -118 21 95 LEU CG A 158 -2 -227 -56 10
PHE CZ A 149 -17 -194 -125 21 LEU CD1 A 158 -2 -240 -62 12
HIS N A 150 -17 -266 -129 17 LEU CD2 A 158 -1 -227 -47 13
HIS CA A 150 -17 -280 -134 19 GLN N A 159 -5 -219 -66 10
HIS C A 150 -17 -278 -150 20 GLN CA A 159 -6 -217 -58 10
HIS 0 A 150 -18 -270 -156 19 100 GLN C A 159 -6 -225 -46 12
HIS CB A 150 -19 -286 -130 22 GLN 0 A 159 -6 -236 -45 12
HIS CG A 150 -19 -299 -136 26 GLN CB A 159 -8 -221 -66 12
HIS ND1 A 150 -18 -310 -135 28 GLN CG A 159 -8 -214 -80 12
HIS CD2 A 150 -20 -303 -145 28 GLN CD A 159 -8 -200 -77 13
HIS CE1 A 150 -19 -320 -142 28 105 GLN OE1 A 159 -9 -196 -72 13
HIS NE2 A 150 -20 -316 -148 28 GLN NE2 A 159 -7 -191 -80 12
LYS N A 151 -16 -286 -156 17 TYR N A 160 -7 -220 -35 11
LYS CA A 151 -16 -286 -171 18 TYR CA A 160 -7 -227 -23 11
LYS C A 151 -16 -272 -176 20 TYR C A 160 -9 -226 -17 13
LYS 0 A 151 -16 -270 -188 19 110 TYR 0 A 160 -9 -217 -19 12
LYS CB A 151 -17 -291 -179 21 TYR CB A 160 -6 -223 -12 12
LYS CG A 151 -18 -306 -175 28 TYR CG A 160 -6 -210 -6 12
LYS CD A 151 -19 -311 -183 35 TYR CD1 A 160 -7 -209 7 14
LYS CE A 151 -19 -325 -181 50 TYR CD2 A 160 -6 -198 -12 14
LYS NZ A 151 -20 -330 -190 60 115 TYR CE1 A 160 -7 -197 13 17
GLY N A 152 -15 -264 -167 15 TYR CE2 A 160 -6 -186 -5 14
GLY CA A 152 -15 -251 -170 16 TYR CZ A 160 -7 -185 7 21
GLY C A 152 -13 -250 -171 16 TYR OH A 160 -7 -173 13 25
GLY 0 A 152 -12 -260 -172 16 LEU N A 161 -9 -236 -9 11
ARG N A 153 -13 -238 -172 13 120 LEU CA A 161 -10 -237 -2 11
ARG CA A 153 -11 -235 -174 13 LEU C A 161 -10 -244 11 13
ARG C A 153 -10 -239 -162 14 LEU 0 A 161 -10 -255 11 12 LEU CB A 161 -11 -244 -12 12 ARG NH1 A 168 -20 -467 72 62
LEU CG A 161 -13 -247 -7 13 ARG NH2 A 168 -18 -479 71 70
LEU CD1 A 161 -13 -233 -6 14 ALA N A 169 -22 -414 78 23
LEU CD2 A 161 -13 -256 -16 16 65 ALA CA A 169 -23 -417 72 23
ARG N A 162 -11 -239 21 13 ALA C A 169 -23 -408 60 28
ARG CA A 162 -11 -246 34 13 ALA O A 169 -24 -412 50 27
ARG C A 162 -12 -255 33 16 ALA CB A 169 -24 -417 82 24
ARG 0 A 162 -13 -250 29 16 THR N A 170 -23 -395 62 23
ARG CB A 162 -11 -236 46 17 70 THR CA A 170 -23 -385 52 22
ARG CG A 162 -11 -242 60 20 THR C A 170 -23 -387 39 27
ARG CD A 162 -12 -233 70 22 THR O A 170 -23 -386 28 25
ARG NE A 162 -13 -233 68 32 THR CB A 170 -23 -371 57 25
ARG CZ A 162 -14 -242 73 46 THR OG1 A 170 -24 -369 68 22
ARG NH1 A 162 -14 -253 80 31 75 THR CG2 A 170 -24 -360 47 24
ARG NH2 A 162 -15 -241 71 34 CYS N A 171 -21 -390 42 24
VAL N A 163 -12 -268 36 13 CYS CA A 171 -20 -393 31 25
VAL CA A 163 -13 -278 35 13 CYS C A 171 -21 -404 23 33
VAL C A 163 -13 -285 49 14 CYS O A 171 -21 -403 10 31
VAL 0 A 163 -12 -289 55 15 80 CYS CB A 171 -19 -396 38 26
VAL CB A 163 -13 -288 24 14 CYS SG A 171 -18 -401 27 31
VAL CGI A 163 -13 -282 10 15 LEU N A 172 -21 -415 29 32
VAL CG2 A 163 -12 -295 25 14 LEU CA A 172 -22 -427 22 34
PRO N A 164 -15 -285 53 13 LEU C A 172 -23 -425 14 40
PRO CA A 164 -15 -292 66 13 85 LEU O A 172 -23 -429 3 40
PRO C A 164 -15 -307 64 15 LEU CB A 172 -22 -438 33 34
PRO 0 A 164 -16 -311 54 14 LEU CG A 172 -21 -449 34 40
PRO CB A 164 -16 -286 71 15 LEU CD1 A 172 -20 -444 40 41
PRO CG A 164 -17 -281 58 19 LEU CD2 A 172 -21 -461 42 42
PRO CD A 164 -16 -279 48 15 90 ARG N A 173 -24 -418 20 38
LEU N A 165 -15 -315 74 13 ARG CA A 173 -25 -415 13 38
LEU CA A 165 -15 -329 74 14 ARG C A 173 -25 -405 1 42
LEU C A 165 -16 -333 75 17 ARG O A 173 -26 -405 -7 42
LEU 0 A 165 -17 -326 82 17 ARG CB A 173 -26 -410 23 39
LEU CB A 165 -14 -335 86 14 95 ARG CG A 173 -27 -420 33 55
LEU CG A 165 -14 -350 88 16 ARG CD A 173 -27 -414 47 69
LEU CD1 A 165 -13 -357 77 17 ARG NE A 173 -28 -424 56 81
LEU CD2 A 165 -13 -354 101 16 ARG CZ A 173 -29 -426 57 0
VAL N A 166 -17 -343 67 16 ARG NH1 A 173 -30 -419 49 93
VAL CA A 166 -18 -348 66 15 100 ARG NH2 A 173 -29 -435 65 93
VAL C A 166 -18 -361 74 19 SER N A 174 -24 -398 0 38
VAL 0 A 166 -17 -369 73 19 SER CA A 174 -24 -388 -11 37
VAL CB A 166 -18 -349 51 19 SER C A 174 -24 -394 -24 43
VAL CGI A 166 -20 -355 50 19 SER O A 174 -24 -388 -34 43
VAL CG2 A 166 -18 -335 45 19 105 SER CB A 174 -23 -378 -6 38
ASP N A 167 -19 -362 81 16 SER OG A 174 -22 -383 -5 39
ASP CA A 167 -19 -375 89 17 THR N A 175 -23 -406 -23 41
ASP C A 167 -20 -387 80 21 THR CA A 175 -22 -413 -35 42
ASP 0 A 167 -20 -386 69 20 THR C A 175 -23 -427 -38 50
ASP CB A 167 -21 -373 99 18 110 THR O A 175 -23 -434 -28 49
ASP CG A 167 -22 -373 92 20 THR CB A 175 -21 -412 -36 54
ASP OD1 A 167 -22 -384 90 21 THR OG1 A 175 -20 -418 -47 55
ASP OD2 A 167 -22 -362 88 24 THR CG2 A 175 -20 -418 -23 53
ARG N A 168 -19 -399 86 21 LYS N A 176 -23 -432 -50 48
ARG CA A 168 -19 -411 78 22 115 LYS CA A 176 -23 -446 -54 50
ARG C A 168 -21 -414 71 26 LYS C A 176 -22 -456 -52 56
ARG 0 A 168 -21 -416 59 24 LYS O A 176 -22 -467 -48 56
ARG CB A 168 -19 -423 88 26 LYS CB A 176 -24 -447 -68 52
ARG CG A 168 -18 -436 81 42 LYS CG A 176 -23 -443 -80 70
ARG CD A 168 -18 -448 90 48 120 LYS CD A 176 -23 -446 -93 81
ARG NE A 168 -18 -459 84 64 LYS CE A 176 -22 -442 -104 92
ARG CZ A 168 -18 -468 76 80 LYS NZ A 176 -23 -446 -118 0 PHE N A 177 -21 -451 -53 53 MET CE A 183 -14 -436 -14 31
PHE CA A 177 -20 -459 -51 53 PHE N A 184 -12 -403 31 16
PHE C A 177 -19 -462 -36 53 PHE CA A 184 -13 -395 39 14
PHE 0 A 177 -20 -454 -28 52 65 PHE C A 184 -13 -385 29 15
PHE CB A 177 -18 -454 -58 56 PHE O A 184 -13 -383 18 15
PHE CG A 177 -18 -439 -57 59 PHE CB A 184 -12 -387 50 14
PHE CD1 A 177 -17 -434 -45 63 PHE CG A 184 -11 -377 46 14
PHE CD2 A 177 -18 -430 -68 62 PHE CD1 A 184 -11 -364 45 15
PHE CE1 A 177 -17 -420 -44 64 70 PHE CD2 A 184 -10 -380 45 14
PHE CE2 A 177 -18 -417 -67 65 PHE CE1 A 184 -10 -354 41 15
PHE CZ A 177 -18 -412 -55 63 PHE CE2 A 184 -9 -371 41 15
THR N A 178 -19 -473 -33 47 PHE CZ A 184 -9 -358 39 14
THR CA A 178 -18 -477 -19 45 CYS N A 185 -15 -379 33 17
THR C A 178 -17 -468 -14 44 75 CYS CA A 185 -15 -369 26 18
THR 0 A 178 -16 -466 -20 44 CYS C A 185 -15 -355 33 18
THR CB A 178 -18 -492 -18 56 CYS O A 185 -15 -354 45 16
THR 0G1 A 178 -19 -499 -25 59 CYS CB A 185 -17 -371 25 22
THR CG2 A 178 -18 -496 -3 54 CYS SG A 185 -17 -385 14 30
ILE N A 179 -17 -463 -2 38 80 ALA N A 186 -15 -345 24 14
ILE CA A 179 -16 -455 6 36 ALA CA A 186 -15 -331 30 14
ILE C A 179 -16 -464 16 35 ALA C A 186 -16 -322 20 17
ILE 0 A 179 -16 -468 25 36 ALA O A 186 -16 -325 8 17
ILE CB A 179 -17 -442 12 39 ALA CB A 186 -13 -327 32 15
ILE CGI A 179 -18 -433 2 40 85 GLY N A 187 -16 -311 25 15
ILE CG2 A 179 -16 -435 22 40 GLY CA A 187 -17 -302 16 14
ILE CD1 A 179 -17 -425 -7 48 GLY C A 187 -18 -296 22 19
TYR N A 180 -14 -467 15 27 GLY O A 187 -18 -297 34 20
TYR CA A 180 -14 -475 25 24 PHE N A 188 -19 -291 13 20
TYR C A 180 -13 -466 36 28 90 PHE CA A 188 -20 -284 17 20
TYR 0 A 180 -13 -454 34 26 PHE C A 188 -21 -290 10 28
TYR CB A 180 -13 -484 19 26 PHE O A 188 -21 -295 -1 29
TYR CG A 180 -13 -493 7 29 PHE CB A 188 -20 -269 13 22
TYR CD1 A 180 -12 -495 -4 32 PHE CG A 188 -19 -262 19 21
TYR CD2 A 180 -14 -501 9 29 95 PHE CD1 A 188 -18 -263 12 20
TYR CE1 A 180 -13 -503 -14 33 PHE CD2 A 188 -19 -256 31 21
TYR CE2 A 180 -15 -510 -1 31 PHE CE1 A 188 -16 -256 18 19
TYR CZ A 180 -14 -511 -13 38 PHE CE2 A 188 -18 -250 37 22
TYR OH A 180 -14 -519 -23 40 PHE CZ A 188 -17 -250 30 18
ASN N A 181 -13 -472 47 27 100 HIS N A 189 -23 -291 18 29
ASN CA A 181 -12 -466 58 27 HIS CA A 189 -24 -296 12 31
ASN C A 181 -11 -458 55 28 HIS C A 189 -24 -287 2 34
ASN 0 A 181 -11 -449 63 28 HIS O A 189 -25 -292 -8 34
ASN CB A 181 -12 -477 69 34 HIS CB A 189 -25 -299 23 34
ASN CG A 181 -13 -484 74 73 105 HIS CG A 189 -26 -305 18 39
ASN OD1 A 181 -14 -493 67 72 HIS ND1 A 189 -27 -297 15 41
ASN ND2 A 181 -14 -481 86 68 HIS CD2 A 189 -26 -318 14 41
ASN N A 182 -10 -461 44 21 HIS CE1 A 189 -28 -305 10 41
ASN CA A 182 -9 -454 40 20 HIS NE2 A 189 -28 -318 9 41
ASN C A 182 -9 -441 32 21 110 GLU N A 190 -24 -274 4 29
ASN 0 A 182 -8 -435 26 21 GLU CA A 190 -25 -263 -5 29
ASN CB A 182 -8 -463 32 21 GLU C A 190 -24 -262 -20 34
ASN CG A 182 -9 -469 19 32 GLU O A 190 -25 -256 -27 33
ASN OD1 A 182 -10 -468 18 30 GLU CB A 190 -25 -250 2 30
ASN ND2 A 182 -8 -474 11 31 115 GLU CG A 190 -26 -248 14 44
MET N A 183 -10 -437 32 18 GLU CD A 190 -27 -250 12 68
MET CA A 183 -11 -425 25 19 GLU OE1 A 190 -28 -261 16 58
MET C A 183 -12 -416 35 21 GLU OE2 A 190 -28 -241 6 64
MET 0 A 183 -12 -422 44 19 GLY N A 191 -23 -269 -23 31
MET CB A 183 -12 -429 13 23 120 GLY CA A 191 -23 -268 -37 31
MET CG A 183 -11 -437 3 28 GLY C A 191 -22 -255 -39 32
MET SD A 183 -13 -448 -6 34 GLY O A 191 -22 -246 -30 34 GLY N A 192 -21 -254 -50 24 SER OG A 200 -8 -357 -93 15
GLY CA A 192 -20 -243 -53 22 GLY N A 201 -5 -355 -68 10
GLY C A 192 -19 -242 -48 20 GLY CA A 201 -3 -357 -65 10
GLY 0 A 192 -18 -232 -51 17 65 GLY C A 201 -3 -347 -55 12
ARG N A 193 -19 -251 -39 16 GLY O A 201 -2 -348 -49 11
ARG CA A 193 -17 -251 -33 16 GLY N A 202 -3 -335 -55 11
ARG C A 193 -17 -265 -32 19 GLY CA A 202 -3 -324 -46 10
ARG 0 A 193 -17 -273 -25 21 GLY C A 202 -3 -327 -32 11
ARG CB A 193 -17 -245 -19 15 70 GLY O A 202 -4 -337 -28 11
ARG CG A 193 -17 -230 -19 19 PRO N A 203 -3 -317 -23 10
ARG CD A 193 -17 -224 -4 22 PRO CA A 203 -3 -319 -9 11
ARG NE A 193 -19 -227 2 22 PRO C A 203 -4 -315 -3 13
ARG CZ A 193 -19 -224 15 27 PRO O A 203 -5 -305 -7 13
ARG NH1 A 193 -18 -217 22 23 75 PRO CB A 203 -2 -310 -4 13
ARG NH2 A 193 -20 -226 19 28 PRO CG A 203 -2 -298 -14 14
ASP N A 194 -16 -268 -40 14 PRO CD A 203 -2 -306 -27 11
ASP CA A 194 -15 -282 -40 14 HIS N A 204 -5 -322 8 10
ASP C A 194 -14 -282 -47 15 HIS CA A 204 -5 -317 19 10
ASP 0 A 194 -13 -273 -55 14 80 HIS C A 204 -5 -316 31 11
ASP CB A 194 -16 -291 -48 17 HIS O A 204 -4 -326 35 11
ASP CG A 194 -16 -306 -48 23 HIS CB A 204 -7 -328 21 10
ASP 0D1 A 194 -15 -311 -40 23 HIS CG A 204 -7 -325 32 11
ASP OD2 A 194 -16 -312 -57 24 HIS ND1 A 204 -7 -327 45 12
SER N A 195 -13 -293 -46 14 85 HIS CD2 A 204 -9 -321 33 12
SER CA A 195 -12 -296 -55 14 HIS CE1 A 204 -8 -324 53 11
SER C A 195 -12 -300 -68 17 HIS NE2 A 204 -9 -320 46 12
SER 0 A 195 -14 -303 -69 17 VAL N A 205 -4 -304 36 10
SER CB A 195 -11 -306 -48 16 VAL CA A 205 -4 -301 48 9
SER OG A 195 -12 -317 -45 22 90 VAL C A 205 -4 -296 60 11
CYS N A 196 -12 -300 -79 14 VAL O A 205 -5 -289 58 11
CYS CA A 196 -12 -304 -92 14 VAL CB A 205 -2 -292 44 12
CYS C A 196 -11 -310 -101 15 VAL CGI A 205 -2 -298 32 12
CYS 0 A 196 -10 -313 -96 13 VAL CG2 A 205 -3 -277 42 13
CYS CB A 196 -13 -291 -99 15 95 THR N A 206 -4 -299 72 10
CYS SG A 196 -14 -294 -113 19 THR CA A 206 -4 -293 84 10
GLN N A 197 -12 -314 -113 14 THR C A 206 -3 -285 91 12
GLN CA A 197 -11 -320 -122 13 THR O A 206 -2 -289 92 12
GLN C A 197 -9 -312 -124 14 THR CB A 206 -5 -305 93 11
GLN 0 A 197 -10 -300 -126 15 100 THR OG1 A 206 -6 -312 86 12
GLN CB A 197 -11 -323 -136 14 THR CG2 A 206 -5 -300 106 13
GLN CG A 197 -11 -332 -145 16 GLU N A 207 -4 -272 94 12
GLN CD A 197 -11 -336 -157 23 GLU CA A 207 -3 -263 101 13
GLN OE1 A 197 -12 -327 -164 20 GLU C A 207 -3 -265 115 15
GLN NE2 A 197 -12 -348 -159 22 105 GLU O A 207 -4 -265 122 16
GLY N A 198 -8 -318 -124 13 GLU CB A 207 -3 -249 98 16
GLY CA A 198 -7 -311 -124 12 GLU CG A 207 -3 -245 83 26
GLY C A 198 -6 -309 -110 11 GLU CD A 207 -4 -231 80 46
GLY 0 A 198 -5 -307 -109 13 GLU OE1 A 207 -4 -224 89 35
ASP N A 199 -7 -310 -100 11 110 GLU OE2 A 207 -3 -226 69 34
ASP CA A 199 -7 -309 -86 11 VAL N A 208 -2 -267 121 12
ASP C A 199 -6 -322 -80 13 VAL CA A 208 -1 -271 135 13
ASP 0 A 199 -5 -322 -70 11 VAL C A 208 -1 -260 141 15
ASP CB A 199 -8 -303 -77 11 VAL O A 208 1 -260 140 14
ASP CG A 199 -8 -289 -79 10 115 VAL CB A 208 -1 -285 137 17
ASP OD1 A 199 -7 -281 -82 12 VAL CGI A 208 -1 -288 152 17
ASP OD2 A 199 -9 -285 -79 12 VAL CG2 A 208 -2 -295 130 17
SER N A 200 -7 -333 -86 12 GLU N A 209 -1 -250 148 16
SER CA A 200 -6 -347 -82 11 GLU CA A 209 -0 -239 153 16
SER C A 200 -5 -348 -79 11 120 GLU C A 209 1 -233 144 19
SER 0 A 200 -4 -343 -87 12 GLU O A 209 2 -231 148 19
SER CB A 200 -7 -357 -92 13 GLU CB A 209 0 -243 167 18 GLU CG A 209 -1 -248 177 25 ILE C A 218 -7 -364 -45 13
GLU CD A 209 -2 -238 181 47 ILE O A 218 -6 -367 -52 13
GLU 0E1 A 209 -1 -226 183 37 ILE CB A 218 -7 -339 -42 11
GLU OE2 A 209 -3 -241 182 47 65 ILE CGI A 218 -7 -328 -32 13
GLY N A 210 0 -230 131 18 ILE CG2 A 218 -8 -337 -51 12
GLY CA A 210 1 -224 122 18 ILE CD1 A 218 -7 -314 -38 14
GLY C A 210 2 -234 114 20 SER N A 219 -8 -371 -45 13
GLY 0 A 210 3 -229 106 22 SER CA A 219 -9 -383 -54 13
THR N A 211 2 -247 115 14 70 SER C A 219 -9 -379 -67 17
THR CA A 211 3 -257 108 13 SER O A 219 -9 -368 -72 17
THR C A 211 2 -266 101 12 SER CB A 219 -9 -395 -46 17
THR 0 A 211 1 -272 108 12 SER OG A 219 -9 -407 -53 18
THR CB A 211 4 -265 117 14 TRP N A 220 -10 -389 -72 18
THR OG1 A 211 4 -256 124 15 75 TRP CA A 220 -11 -387 -83 19
THR CG2 A 211 4 -275 109 13 TRP C A 220 -12 -379 -78 22
SER N A 212 2 -267 88 10 TRP O A 220 -12 -376 -66 20
SER CA A 212 1 -275 80 9 TRP CB A 220 -12 -400 -88 19
SER C A 212 1 -290 79 11 TRP CG A 220 -11 -408 -96 21
SER 0 A 212 2 -292 76 11 80 TRP CD1 A 220 -10 -418 -91 25
SER CB A 212 0 -269 67 12 TRP CD2 A 220 -11 -408 -110 22
SER OG A 212 -0 -257 68 13 TRP NE1 A 220 -9 -424 -101 25
PHE N A 213 0 -299 81 11 TRP CE2 A 220 -10 -418 -113 27
PHE CA A 213 1 -313 80 10 TRP CE3 A 220 -11 -400 -120 24
PHE C A 213 -0 -320 70 10 85 TRP CZ2 A 220 -9 -420 -126 27
PHE 0 A 213 -2 -316 69 11 TRP CZ3 A 220 -11 -403 -133 26
PHE CB A 213 0 -320 94 10 TRP CH2 A 220 -10 -413 -136 27
PHE CG A 213 1 -318 104 10 GLY N A 221 -13 -375 -87 21
PHE CD1 A 213 1 -306 112 12 GLY CA A 221 -14 -369 -84 22
PHE CD2 A 213 2 -327 106 11 90 GLY C A 221 -15 -371 -96 27
PHE CE1 A 213 2 -304 121 12 GLY O A 221 -15 -377 -106 25
PHE CE2 A 213 3 -325 116 13 GLU N A 222 -17 -365 -95 27
PHE CZ A 213 3 -313 123 12 GLU CA A 222 -18 -366 -105 29
LEU N A 214 0 -329 62 11 GLU C A 222 -18 -351 -109 33
LEU CA A 214 -1 -336 52 10 95 GLU O A 222 -17 -344 -113 33
LEU C A 214 -2 -345 58 11 GLU CB A 222 -19 -373 -100 31
LEU 0 A 214 -1 -355 65 12 GLU CG A 222 -19 -386 -93 44
LEU CB A 214 0 -343 43 10 GLU CD A 222 -20 -392 -85 68
LEU CG A 214 -0 -349 30 12 GLU OE1 A 222 -20 -390 -73 65
LEU CD1 A 214 -1 -338 20 13 100 GLU OE2 A 222 -21 -398 -92 61
LEU CD2 A 214 1 -358 23 14 GLU N A 223 -19 -347 -108 30
THR N A 215 -3 -343 55 10 GLU CA A 223 -20 -333 -111 29
THR CA A 215 -4 -352 61 10 GLU C A 223 -19 -324 -100 31
THR C A 215 -5 -359 50 11 GLU O A 223 -20 -325 -89 33
THR 0 A 215 -5 -370 53 11 105 GLU CB A 223 -21 -333 -113 30
THR CB A 215 -5 -344 70 10 GLU CG A 223 -22 -319 -119 46
THR OG1 A 215 -5 -331 65 11 GLU CD A 223 -23 -319 -124 74
THR CG2 A 215 -4 -343 84 12 GLU OE1 A 223 -24 -330 -125 77
GLY N A 216 -5 -355 38 10 GLU OE2 A 223 -24 -308 -127 69
GLY CA A 216 -5 -362 27 11 110 CYS N A 224 -18 -316 -102 23
GLY C A 216 -5 -359 13 12 CYS CA A 224 -18 -308 -92 22
GLY 0 A 216 -4 -350 12 10 CYS C A 224 -19 -298 -86 24
ILE N A 217 -5 -368 4 11 CYS O A 224 -19 -292 -93 23
ILE CA A 217 -5 -366 -10 10 CYS CB A 224 -16 -299 -98 20
ILE C A 217 -6 -365 -18 12 115 CYS SG A 224 -15 -309 -107 22
ILE 0 A 217 -7 -373 -17 12 ALA N A 225 -18 -297 -73 19
ILE CB A 217 -4 -378 -16 12 ALA CA A 225 -19 -287 -65 20
ILE CGI A 217 -3 -382 -8 14 ALA C A 225 -21 -288 -66 23
ILE CG2 A 217 -3 -375 -31 12 ALA O A 225 -21 -277 -65 23
ILE CD1 A 217 -2 -372 -6 14 120 ALA CB A 225 -19 -273 -69 21
ILE N A 218 -6 -355 -27 11 MET N A 226 -21 -300 -69 22
ILE CA A 218 -7 -353 -35 11 MET CA A 226 -23 -302 -70 24 MET C A 226 -23 -303 -56 26 TYR CE2 A 233 -10 -333 -8 20
MET 0 A 226 -23 -309 -47 23 TYR CZ A 233 -11 -329 -6 22
MET CB A 226 -23 -315 -78 29 TYR OH A 233 -12 -317 -12 23
MET CG A 226 -24 -317 -80 37 65 THR N A 234 -8 -395 -1 13
MET SD A 226 -25 -332 -90 45 THR CA A 234 -7 -406 5 13
MET CE A 226 -26 -324 -102 42 THR C A 234 -7 -402 18 15
LYS N A 227 -25 -297 -54 23 THR 0 A 234 -6 -391 20 14
LYS CA A 227 -25 -298 -41 25 THR CB A 234 -6 -409 -4 18
LYS C A 227 -25 -312 -38 28 70 THR OG1 A 234 -7 -412 -17 19
LYS 0 A 227 -26 -320 -47 29 THR CG2 A 234 -5 -421 1 18
LYS CB A 227 -27 -290 -42 29 LYS N A 235 -7 -410 29 14
LYS CG A 227 -27 -289 -29 48 LYS CA A 235 -7 -407 42 14
LYS CD A 227 -28 -276 -28 60 LYS C A 235 -5 -410 43 17
LYS CE A 227 -29 -275 -14 73 75 LYS 0 A 235 -5 -422 44 18
LYS NZ A 227 -29 -261 -11 81 LYS CB A 235 -7 -417 52 19
GLY N A 228 -25 -316 -25 27 LYS CG A 235 -9 -411 59 22
GLY CA A 228 -25 -330 -20 27 LYS CD A 235 -9 -421 70 21
GLY C A 228 -24 -339 -22 30 LYS CE A 235 -10 -418 73 24
GLY 0 A 228 -24 -350 -18 30 80 LYS NZ A 235 -11 -430 82 24
LYS N A 229 -23 -334 -29 24 VAL N A 236 -4 -399 45 13
LYS CA A 229 -22 -342 -32 23 VAL CA A 236 -3 -401 45 11
LYS C A 229 -21 -336 -24 22 VAL C A 236 -2 -409 57 14
LYS 0 A 229 -21 -324 -21 21 VAL 0 A 236 -1 -416 56 14
LYS CB A 229 -22 -342 -47 26 85 VAL CB A 236 -2 -387 44 14
LYS CG A 229 -23 -349 -55 41 VAL CGI A 236 -1 -387 48 14
LYS CD A 229 -23 -364 -57 53 VAL CG2 A 236 -2 -382 30 15
LYS CE A 229 -24 -371 -64 66 SER N A 237 -3 -409 69 13
LYS NZ A 229 -23 -386 -64 76 SER CA A 237 -3 -416 81 13
TYR N A 230 -20 -344 -22 21 90 SER C A 237 -2 -431 78 17
TYR CA A 230 -19 -340 -15 19 SER 0 A 237 -2 -436 83 17
TYR C A 230 -17 -345 -21 23 SER CB A 237 -4 -415 92 15
TYR 0 A 230 -17 -355 -28 26 SER OG A 237 -5 -421 88 17
TYR CB A 230 -19 -346 -0 19 ARG N A 238 -3 -437 69 16
TYR CG A 230 -20 -342 7 20 95 ARG CA A 238 -3 -451 65 18
TYR CD1 A 230 -20 -329 13 21 ARG C A 238 -2 -454 58 21
TYR CD2 A 230 -21 -350 8 21 ARG O A 238 -1 -466 57 21
TYR CE1 A 230 -21 -325 20 22 ARG CB A 238 -4 -455 57 20
TYR CE2 A 230 -22 -346 15 22 ARG CG A 238 -4 -468 50 40
TYR CZ A 230 -22 -334 21 25 100 ARG CD A 238 -4 -481 58 55
TYR OH A 230 -23 -330 28 31 ARG NE A 238 -4 -493 49 66
GLY N A 231 -16 -338 -18 19 ARG CZ A 238 -3 -498 45 79
GLY CA A 231 -15 -343 -23 19 ARG NH1 A 238 -2 -493 48 65
GLY C A 231 -14 -355 -16 20 ARG NH2 A 238 -3 -509 37 65
GLY 0 A 231 -15 -357 -4 19 105 TYR N A 239 -1 -444 52 16
ILE N A 232 -14 -364 -23 19 TYR CA A 239 0 -445 44 14
ILE CA A 232 -13 -377 -17 20 TYR C A 239 1 -439 49 16
ILE C A 232 -12 -376 -17 21 TYR O A 239 2 -439 42 15
ILE 0 A 232 -11 -372 -26 21 TYR CB A 239 -0 -440 30 14
ILE CB A 232 -14 -389 -26 25 110 TYR CG A 239 -2 -447 24 14
ILE CGI A 232 -15 -389 -30 29 TYR CD1 A 239 -2 -460 19 17
ILE CG2 A 232 -13 -402 -18 27 TYR CD2 A 239 -3 -441 25 15
ILE CD1 A 232 -16 -389 -19 38 TYR CE1 A 239 -3 -466 14 16
TYR N A 233 -11 -380 -5 16 TYR CE2 A 239 -4 -447 21 16
TYR CA A 233 -10 -379 -3 13 115 TYR CZ A 239 -4 -460 16 20
TYR C A 233 -9 -392 3 15 TYR OH A 239 -5 -466 12 20
TYR 0 A 233 -10 -399 10 17 VAL N A 240 1 -433 61 15
TYR CB A 233 -10 -367 8 14 VAL CA A 240 2 -426 66 16
TYR CG A 233 -10 -354 3 16 VAL C A 240 4 -434 66 19
TYR CD1 A 233 -11 -350 4 16 120 VAL O A 240 5 -430 62 18
TYR CD2 A 233 -9 -345 -3 18 VAL CB A 240 2 -419 79 22
TYR CE1 A 233 -12 -338 -1 17 VAL CGI A 240 3 -415 87 23 VAL CG2 A 240 1 -407 77 22 THR 0 A 247 13 -400 13 20
ASN N A 241 4 -447 71 19 THR CB A 247 10 -403 8 17
ASN CA A 241 5 -455 73 20 THR OG1 A 247 10 -402 21 18
ASN C A 241 5 -459 59 21 65 THR CG2 A 247 9 -405 -2 19
ASN 0 A 241 7 -458 58 22 LYS N A 248 13 -419 25 23
ASN CB A 241 4 -468 81 23 LYS CA A 248 14 -416 34 23
ASN CG A 241 4 -465 95 41 LYS C A 248 15 -413 27 28
ASN 0D1 A 241 5 -455 101 34 LYS 0 A 248 16 -421 17 29
ASN ND2 A 241 3 -473 101 37 70 LYS CB A 248 14 -428 44 27
TRP N A 242 5 -462 49 17 LYS CG A 248 15 -424 58 41
TRP CA A 242 5 -464 35 18 LYS CD A 248 15 -436 67 53
TRP C A 242 6 -452 29 21 LYS CE A 248 15 -433 81 68
TRP 0 A 242 7 -452 23 19 LYS NZ A 248 13 -431 85 78
TRP CB A 242 4 -469 27 18 75 LEU N A 249 16 -402 30 26
TRP CG A 242 4 -470 13 19 LEU CA A 249 17 -398 24 27
TRP CD1 A 242 4 -480 6 22 LEU C A 249 18 -401 32 34
TRP CD2 A 242 3 -461 3 19 LEU 0 A 249 18 -401 45 36
TRP NE1 A 242 4 -478 -8 22 LEU CB A 249 17 -383 20 27
TRP CE2 A 242 4 -466 -10 23 80 LEU CG A 249 16 -379 10 31
TRP CE3 A 242 3 -448 3 20 LEU CD1 A 249 16 -364 8 30
TRP CZ2 A 242 4 -459 -22 21 LEU CD2 A 249 16 -387 -3 33
TRP CZ3 A 242 3 -441 -8 20 MET N B 86 -1 -310 321 45
TRP CH2 A 242 3 -447 -21 21 MET CA B 86 -2 -321 328 44
ILE N A 243 5 -440 32 17 85 MET C B 86 -2 -334 321 38
ILE CA A 243 6 -427 26 15 MET 0 B 86 -1 -344 325 37
ILE C A 243 7 -426 32 19 MET CB B 86 -3 -317 333 48
ILE 0 A 243 8 -423 25 19 MET CG B 86 -3 -315 347 53
ILE CB A 243 5 -415 29 17 MET SD B 86 -5 -317 353 59
ILE CGI A 243 3 -416 21 16 90 MET CE B 86 -5 -335 354 56
ILE CG2 A 243 6 -402 25 17 THR N B 87 -2 -336 310 28
ILE CD1 A 243 2 -405 26 17 THR CA B 87 -3 -348 302 25
LYS N A 244 7 -426 46 18 THR C B 87 -3 -345 287 21
LYS CA A 244 8 -424 53 19 THR 0 B 87 -3 -334 283 19
LYS C A 244 9 -434 49 23 95 THR CB B 87 -4 -357 306 32
LYS 0 A 244 11 -430 46 24 THR OG1 B 87 -5 -352 298 32
LYS CB A 244 8 -424 68 21 THR CG2 B 87 -4 -358 321 35
LYS CG A 244 7 -413 74 30 CYS N B 88 -2 -355 279 18
LYS CD A 244 8 -399 76 36 CYS CA B 88 -2 -352 264 16
LYS CE A 244 7 -389 83 28 100 CYS C B 88 -4 -352 259 18
LYS NZ A 244 8 -375 83 32 CYS O B 88 -4 -347 248 19
GLU N A 245 9 -447 47 22 CYS CB B 88 -2 -363 257 15
GLU CA A 245 10 -457 43 24 CYS SG B 88 0 -363 260 17
GLU C A 245 11 -455 29 27 ASN N B 89 -5 -357 267 18
GLU 0 A 245 12 -455 27 28 105 ASN CA B 89 -6 -356 263 19
GLU CB A 245 9 -471 43 26 ASN C B 89 -7 -343 265 19
GLU CG A 245 9 -478 56 44 ASN O B 89 -8 -340 258 17
GLU CD A 245 9 -491 57 71 ASN CB B 89 -7 -367 269 23
GLU OE1 A 245 9 -499 48 59 ASN CG B 89 -7 -381 262 47
GLU OE2 A 245 8 -493 67 70 110 ASN OD1 B 89 -6 -386 261 47
LYS N A 246 10 -452 19 21 ASN ND2 B 89 -8 -387 257 31
LYS CA A 246 10 -451 5 20 ILE N B 90 -6 -334 272 17
LYS C A 246 11 -438 2 22 ILE CA B 90 -7 -320 275 16
LYS 0 A 246 12 -438 -7 22 ILE C B 90 -6 -310 268 16
LYS CB A 246 9 -452 -5 21 115 ILE O B 90 -5 -308 272 16
LYS CG A 246 8 -464 -4 28 ILE CB B 90 -7 -318 290 19
LYS CD A 246 9 -477 -8 30 ILE CGI B 90 -8 -328 297 19
LYS CE A 246 8 -489 -7 36 ILE CG2 B 90 -7 -303 293 21
LYS NZ A 246 9 -501 -9 45 ILE CD1 B 90 -7 -330 312 24
THR N A 247 11 -427 9 18 120 LYS N B 91 -6 -303 258 15
THR CA A 247 11 -414 7 18 LYS CA B 91 -5 -293 251 14
THR C A 247 12 -410 15 22 LYS C B 91 -4 -298 246 16 LYS 0 B 91 -3 -291 246 15 PHE CE1 I3 98 3 -344 153 12
LYS CB B 91 -5 -280 260 18 PHE CE2 I 3 98 5 -347 155 14
LYS CG B 91 -7 -273 264 25 PHE CZ I 3 98 4 -345 147 13
LYS CD B 91 -6 -262 273 29 65 CYS N I 3 99 2 -348 218 13
LYS CE B 91 -7 -253 276 48 CYS CA I 3 99 2 -350 232 13
LYS NZ B 91 -7 -243 286 61 CYS C I 3 99 2 -365 235 14
ASN N B 92 -4 -311 242 15 CYS 0 I 3 99 2 -373 228 15
ASN CA B 92 -3 -317 237 14 CYS CB I 3 99 1 -344 238 12
ASN C B 92 -2 -316 247 15 70 CYS SG I 3 99 1 -344 256 15
ASN 0 B 92 -0 -314 243 14 LYS N I 3 100 3 -368 246 13
ASN CB B 92 -2 -312 224 13 LYS CA I 3 100 3 -382 251 15
ASN CG B 92 -1 -321 216 15 LYS C I 3 100 3 -381 266 16
ASN 0D1 B 92 -2 -332 214 16 LYS 0 I 3 100 4 -372 273 15
ASN ND2 B 92 -0 -315 210 14 75 LYS CB I 3 100 5 -387 248 17
GLY N B 93 -2 -315 260 15 LYS CG I 3 100 5 -401 253 22
GLY CA B 93 -1 -313 271 14 LYS CD I 3 100 6 -406 250 24
GLY C B 93 -0 -300 270 15 LYS CE I 3 100 7 -418 257 26
GLY 0 B 93 1 -298 275 15 LYS NZ I 3 100 6 -430 253 28
ARG N B 94 -1 -290 262 15 80 ASN N I 3 101 2 -390 272 17
ARG CA B 94 -0 -277 259 15 ASN CA I 3 101 2 -390 286 17
ARG C B 94 1 -278 250 15 ASN C I 3 101 3 -396 293 20
ARG 0 B 94 2 -268 247 16 ASN 0 I 3 101 4 -406 288 20
ARG CB B 94 0 -268 272 17 ASN CB I 3 101 1 -397 290 20
ARG CG B 94 -1 -267 282 30 85 ASN CG I 3 101 -0 -390 286 25
ARG CD B 94 -2 -260 278 46 ASN OD1 I 3 101 -1 -379 290 22
ARG NE B 94 -3 -259 290 61 ASN ND2 I 3 101 -1 -397 278 29
ARG CZ B 94 -3 -247 296 77 SER N I 3 102 4 -389 303 18
ARG NH1 B 94 -3 -236 292 64 SER CA I 3 102 5 -394 310 20
ARG NH2 B 94 -4 -247 306 67 90 SER C I 3 102 5 -396 325 27
CYS N B 95 1 -290 244 12 SER O I 3 102 4 -395 330 26
CYS CA B 95 2 -292 234 12 SER CB I 3 102 6 -384 308 24
CYS C B 95 2 -285 221 14 SER OG I 3 102 6 -371 313 38
CYS 0 B 95 1 -288 216 15 ALA N I 3 103 6 -401 332 25
CYS CB B 95 2 -306 232 12 95 ALA CA I 3 103 6 -404 346 26
CYS SG B 95 3 -315 247 14 ALA C I 3 103 5 -392 355 29
GLU N B 96 3 -278 214 11 ALA O I 3 103 6 -380 351 26
GLU CA B 96 2 -272 201 12 ALA CB I 3 103 7 -409 351 27
GLU C B 96 2 -282 190 14 ASP N I 3 104 5 -394 367 27
GLU 0 B 96 1 -281 183 14 100 ASP CA I 3 104 4 -384 377 27
GLU CB B 96 3 -263 197 12 ASP C I 3 104 3 -374 372 30
GLU CG B 96 3 -256 184 15 ASP O I 3 104 3 -362 375 30
GLU CD B 96 4 -246 180 18 ASP CB I 3 104 6 -378 384 29
GLU OE1 B 96 5 -241 188 17 ASP CG I 3 104 7 -388 390 42
GLU OE2 B 96 4 -244 167 20 105 ASP OD1 I 3 104 6 -395 399 44
GLN N B 97 3 -294 190 12 ASP OD2 I 3 104 8 -388 386 45
GLN CA B 97 3 -304 180 11 ASN N I 3 105 2 -378 364 28
GLN C B 97 2 -317 186 13 ASN CA I 3 105 1 -369 358 28
GLN 0 B 97 1 -320 186 13 ASN C I 3 105 2 -357 350 28
GLN CB B 97 4 -305 171 12 110 ASN O I 3 105 1 -346 351 29
GLN CG B 97 4 -293 161 12 ASN CB I 3 105 0 -365 369 31
GLN CD B 97 5 -293 152 14 ASN CG I 3 105 -0 -377 375 60
GLN OE1 B 97 6 -304 151 14 ASN OD1 I 3 105 -1 -384 368 55
GLN NE2 B 97 5 -282 146 15 ASN ND2 I 3 105 -0 -380 387 53
PHE N B 98 3 -325 191 12 115 LYS N I 3 106 3 -360 342 23
PHE CA B 98 3 -338 197 11 LYS CA I 3 106 4 -350 334 20
PHE C B 98 3 -339 212 13 LYS C I 3 106 3 -354 320 19
PHE 0 B 98 4 -332 217 13 LYS O I 3 106 3 -365 317 19
PHE CB B 98 4 -349 190 12 LYS CB I 3 106 5 -348 338 23
PHE CG B 98 4 -347 175 10 120 LYS CG I 3 106 5 -345 353 27
PHE CD1 B 98 3 -345 167 14 LYS CD I 3 106 6 -330 355 41
PHE CD2 B 98 5 -348 169 12 LYS CE I 3 106 7 -329 360 48 LYS NZ I3 106 8 -316 357 39 TYR CE1 I3 115 9 -258 127 14
VAL N I 3 107 4 -345 310 15 TYR CE2 I 3 115 9 -278 115 11
VAL CA I 3 107 4 -349 296 14 TYR CZ I 3 115 8 -265 116 13
VAL C I 3 107 5 -345 291 14 65 TYR OH I 3 115 8 -258 106 15
VAL 0 I 3 107 6 -337 296 15 ARG N I 3 116 13 -281 167 14
VAL CB I 3 107 3 -342 288 16 ARG CA I 3 116 13 -284 180 15
VAL CGI I 3 107 3 -326 287 17 ARG C I 3 116 12 -281 191 17
VAL CG2 I 3 107 1 -345 294 16 ARG O I 3 116 12 -270 190 15
VAL N I 3 108 5 -351 279 13 70 ARG CB I 3 116 15 -276 182 20
VAL CA I 3 108 7 -348 271 12 ARG CG I 3 116 15 -274 196 32
VAL C I 3 108 6 -344 258 13 ARG CD I 3 116 16 -264 197 28
VAL 0 I 3 108 5 -352 251 14 ARG NE I 3 116 16 -251 192 27
VAL CB I 3 108 8 -360 270 15 ARG CZ I 3 116 16 -241 199 45
VAL CGI I 3 108 9 -358 260 15 75 ARG NH1 I 3 116 15 -242 212 33
VAL CG2 I 3 108 8 -363 284 14 ARG NH2 I 3 116 15 -229 193 39
CYS N I 3 109 6 -332 254 12 LEU N I 3 117 12 -289 202 14
CYS CA I 3 109 6 -327 241 11 LEU CA I 3 117 11 -285 213 15
CYS C I 3 109 7 -330 231 13 LEU C I 3 117 12 -273 220 17
CYS 0 I 3 109 8 -333 235 13 80 LEU O I 3 117 13 -274 223 16
CYS CB I 3 109 6 -312 241 12 LEU CB I 3 117 11 -297 222 15
CYS SG I 3 109 5 -306 253 14 LEU CG I 3 117 10 -295 234 17
SER N I 3 110 7 -330 218 12 LEU CD1 I 3 117 9 -294 229 17
SER CA I 3 110 8 -333 207 11 LEU CD2 I 3 117 10 -307 244 18
SER C I 3 110 7 -326 195 12 85 ALA N I 3 118 11 -262 222 14
SER 0 I 3 110 6 -320 194 12 ALA CA I 3 118 12 -250 228 16
SER CB I 3 110 8 -347 205 16 ALA C I 3 118 12 -251 243 19
SER OG I 3 110 7 -354 201 22 ALA O I 3 118 11 -260 250 17
CYS N I 3 111 8 -326 185 12 ALA CB I 3 118 11 -239 225 18
CYS CA I 3 111 8 -319 172 12 90 GLU N I 3 119 13 -241 248 18
CYS C I 3 111 8 -327 161 14 GLU CA I 3 119 13 -240 263 19
CYS 0 I 3 111 9 -338 162 14 GLU C I 3 119 12 -240 271 20
CYS CB I 3 111 9 -306 172 14 GLU O I 3 119 12 -246 283 21
CYS SG I 3 111 9 -295 187 19 GLU CB I 3 119 14 -228 266 22
THR N I 3 112 8 -323 149 13 95 GLU CG I 3 119 15 -230 261 35
THR CA I 3 112 8 -331 137 11 GLU CD I 3 119 16 -219 266 55
THR C I 3 112 10 -328 132 15 GLU OE1 I 3 119 17 -218 278 42
THR 0 I 3 112 10 -319 138 14 GLU OE2 I 3 119 17 -212 257 50
THR CB I 3 112 7 -327 126 14 ASN N I 3 120 11 -235 266 18
THR OG1 I 3 112 7 -337 115 15 100 ASN CA I 3 120 9 -235 274 17
THR CG2 I 3 112 7 -313 120 15 ASN C I 3 120 9 -249 275 18
GLU N I 3 113 10 -335 122 15 ASN O I 3 120 8 -251 282 17
GLU CA I 3 113 11 -333 117 17 ASN CB I 3 120 8 -225 269 18
GLU C I 3 113 12 -318 113 17 ASN CG I 3 120 8 -228 256 21
GLU 0 I 3 113 11 -312 106 16 105 ASN OD1 I 3 120 8 -239 250 18
GLU CB I 3 113 12 -342 105 19 ASN ND2 I 3 120 7 -219 250 21
GLU CG I 3 113 13 -341 98 36 GLN N I 3 121 9 -259 269 15
GLU CD I 3 113 14 -354 90 69 GLN CA I 3 121 9 -274 269 15
GLU OE1 I 3 113 13 -362 86 61 GLN C I 3 121 8 -277 261 16
GLU OE2 I 3 113 15 -355 88 72 110 GLN O I 3 121 7 -288 261 16
GLY N I 3 114 13 -313 116 15 GLN CB I 3 121 9 -279 283 17
GLY CA I 3 114 13 -299 112 15 GLN CG I 3 121 10 -273 292 18
GLY C I 3 114 13 -289 123 15 GLN CD I 3 121 10 -281 305 32
GLY 0 I 3 114 13 -277 121 15 GLN OE1 I 3 121 9 -289 309 26
TYR N I 3 115 12 -293 134 14 115 GLN NE2 I 3 121 11 -278 311 31
TYR CA I 3 115 12 -285 146 14 LYS N I 3 122 7 -267 254 13
TYR C I 3 115 13 -290 158 16 LYS CA I 3 122 6 -269 247 13
TYR 0 I 3 115 13 -302 159 17 LYS C I 3 122 6 -266 232 16
TYR CB I 3 115 10 -285 148 14 LYS O I 3 122 5 -273 224 15
TYR CG I 3 115 10 -278 137 13 120 LYS CB I 3 122 5 -261 253 15
TYR CD1 I 3 115 9 -264 138 14 LYS CG I 3 122 5 -263 268 17
TYR CD2 I 3 115 9 -285 125 13 LYS CD I 3 122 4 -277 272 19 LYS CE I3 122 4 -278 286 17 PRO CA I3 131 11 -264 80 15
LYS NZ I 3 122 3 -292 289 17 PRO C I 3 131 10 -267 73 15
SER N I 3 123 7 -255 229 14 PRO O I 3 131 9 -258 67 16
SER CA I 3 123 7 -249 215 14 65 PRO CB I 3 131 11 -260 94 17
SER C I 3 123 8 -256 206 16 PRO CG I 3 131 11 -245 94 21
SER 0 I 3 123 9 -263 211 16 PRO CD I 3 131 12 -242 83 16
SER CB I 3 123 7 -234 216 16 CYS N I 3 132 10 -279 73 12
SER OG I 3 123 6 -228 223 19 CYS CA I 3 132 8 -283 67 12
CYS N I 3 124 8 -255 193 14 70 CYS C I 3 132 7 -275 72 12
CYS CA I 3 124 8 -261 183 14 CYS O I 3 132 7 -271 83 13
CYS C I 3 124 9 -250 175 18 CYS CB I 3 132 8 -298 68 11
CYS 0 I 3 124 8 -241 169 19 CYS SG I 3 132 8 -304 85 14
CYS CB I 3 124 8 -270 174 14 GLY N I 3 133 6 -274 63 11
CYS SG I 3 124 7 -284 183 18 75 GLY CA I 3 133 5 -269 66 11
GLU N I 3 125 10 -249 176 15 GLY C I 3 133 5 -255 71 12
GLU CA I 3 125 11 -239 169 17 GLY O I 3 133 4 -251 76 12
GLU C I 3 125 12 -245 157 17 ARG N I 3 134 6 -247 69 12
GLU 0 I 3 125 12 -256 158 16 ARG CA I 3 134 6 -233 73 13
GLU CB I 3 125 12 -232 179 19 80 ARG C I 3 134 6 -224 62 14
GLU CG I 3 125 11 -225 190 32 ARG O I 3 134 6 -225 51 14
GLU CD I 3 125 10 -215 186 56 ARG CB I 3 134 7 -231 80 16
GLU OE1 I 3 125 9 -216 192 50 ARG CG I 3 134 7 -217 87 22
GLU OE2 I 3 125 11 -207 177 53 ARG CD I 3 134 9 -219 96 25
PRO N I 3 126 12 -237 146 16 85 ARG NE I 3 134 9 -207 104 36
PRO CA I 3 126 13 -242 135 17 ARG CZ I 3 134 9 -204 116 51
PRO C I 3 126 14 -246 138 18 ARG NH1 I 3 134 8 -214 123 33
PRO 0 I 3 126 15 -238 146 20 ARG NH2 I 3 134 9 -193 122 45
PRO CB I 3 126 13 -231 124 18 VAL N I 3 135 5 -213 63 12
PRO CG I 3 126 11 -224 127 22 90 VAL CA I 3 135 5 -203 53 13
PRO CD I 3 126 11 -224 143 19 VAL C I 3 135 6 -192 58 17
ALA N I 3 127 15 -257 133 16 VAL O I 3 135 6 -186 69 17
ALA CA I 3 127 16 -262 136 17 VAL CB I 3 135 3 -197 52 17
ALA C I 3 127 17 -263 122 21 VAL CGI I 3 135 3 -185 43 17
ALA 0 I 3 127 18 -268 122 22 95 VAL CG2 I 3 135 2 -208 48 18
ALA CB I 3 127 16 -275 144 18 SER N I 3 136 7 -189 50 15
VAL N I 3 128 16 -260 111 16 SER CA I 3 136 8 -179 53 15
VAL CA I 3 128 17 -261 98 17 SER C I 3 136 8 -167 44 21
VAL C I 3 128 16 -248 90 18 SER O I 3 136 8 -156 49 21
VAL 0 I 3 128 15 -241 95 16 100 SER CB I 3 136 9 -185 53 18
VAL CB I 3 128 16 -274 90 19 SER OG I 3 136 9 -192 41 19
VAL CGI I 3 128 17 -287 97 20 VAL N I 3 137 7 -168 32 20
VAL CG2 I 3 128 15 -274 88 19 VAL CA I 3 137 7 -156 23 21
PRO N I 3 129 17 -245 79 18 VAL C I 3 137 6 -146 30 27
PRO CA I 3 129 17 -232 72 18 105 VAL O I 3 137 5 -151 35 26
PRO C I 3 129 15 -231 67 18 VAL CB I 3 137 6 -160 9 23
PRO 0 I 3 129 15 -220 68 18 VAL CGI I 3 137 6 -147 0 23
PRO CB I 3 129 18 -231 61 20 VAL CG2 I 3 137 7 -169 2 23
PRO CG I 3 129 19 -240 65 25 SER N I 3 138 6 -133 30 27
PRO CD I 3 129 18 -251 73 21 110 SER CA I 3 138 5 -123 36 28
PHE N I 3 130 15 -242 62 15 SER C I 3 138 4 -124 29 32
PHE CA I 3 130 13 -243 56 14 SER O I 3 138 4 -125 16 30
PHE C I 3 130 13 -254 62 15 SER CB I 3 138 6 -109 33 32
PHE 0 I 3 130 12 -265 55 15 SER OG I 3 138 5 -100 37 43
PHE CB I 3 130 13 -243 41 16 115 GLN N I 3 139 3 -125 37 30
PHE CG I 3 130 14 -230 36 15 GLN CA I 3 139 2 -127 32 31
PHE CD1 I 3 130 15 -230 32 18 GLN C I 3 139 1 -114 33 39
PHE CD2 I 3 130 13 -218 36 16 GLN O I 3 139 1 -103 32 42
PHE CE1 I 3 130 16 -217 28 18 GLN CB I 3 139 1 -138 40 31
PHE CE2 I 3 130 14 -206 33 18 120 GLN CG I 3 139 2 -152 38 28
PHE CZ I 3 130 15 -206 29 16 GLN CD I 3 139 1 -157 24 31
PRO N I 3 131 12 -253 74 15 GLN OE1 I 3 139 0 -159 19 29 GLN NE2 B 139 3 -158 17 23 HOH O w 2 -6 -280 -145 16
NA NA Q 499 5 -195 -133 17 HOH O w 3 -8 -244 -92 12
CHE CI Q 801 -14 -165 -96 30 HOH O w 4 -12 -212 -71 17
CHE C2 Q 801 -13 -161 -97 27 65 HOH O w 5 -4 -300 -66 11
CHE C3 Q 801 -12 -170 -104 27 HOH O w 6 -2 -272 6 14
CHE C4 Q 801 -13 -173 -118 29 HOH O w 7 -11 -200 -2 17
CHE N5 Q 801 -11 -166 -103 23 HOH O w 8 -11 -211 23 17
CHE C6 Q 801 -10 -175 -109 25 HOH O w 9 -14 -224 30 24
CHE C7 Q 801 -8 -168 -108 24 70 HOH O w 10 1 -357 87 13
CHE S8 Q 801 -7 -173 -122 24 HOH O w 11 -5 -388 74 14
CHE 09 Q 801 -8 -166 -136 26 HOH O w 12 -8 -313 98 15
CHE O10 Q 801 -6 -168 -120 23 HOH O w 13 -6 -265 89 17
CHE Oil Q 801 -8 -188 -124 26 HOH O w 14 2 -473 55 23
CHE C12 Q 801 -14 -179 -116 29 75 HOH O w 15 3 -260 149 16
CHE C13 Q 801 -15 -170 -109 30 HOH O w 16 5 -298 209 13
CHE CI Q 802 -7 -380 -200 56 HOH O w 17 6 -361 121 20
CHE C2 Q 802 -6 -384 -190 56 HOH O w 18 -0 -345 -25 13
CHE C3 Q 802 -5 -375 -186 57 HOH O w 19 7 -313 273 15
CHE C4 Q 802 -5 -361 -184 56 80 HOH O w 20 11 -213 247 27
CHE N5 Q 802 -3 -379 -187 58 HOH O w 21 14 -260 297 25
CHE C6 Q 802 -2 -372 -179 60 HOH O w 22 6 -195 22 13
CHE C7 Q 802 -1 -374 -183 62 HOH O w 23 3 -135 -8 23
CHE S8 Q 802 -1 -366 -199 64 HOH O w 24 6 -252 -44 19
CHE 09 Q 802 -1 -350 -197 64 85 HOH O w 25 4 -254 -76 15
CHE O10 Q 802 1 -369 -203 62 HOH 0 w 26 2 -214 -30 17
CHE Oil Q 802 -2 -373 -209 64 HOH 0 w 27 4 -232 -50 17
CHE C12 Q 802 -6 -356 -194 55 HOH 0 w 28 2 -202 -53 21
CHE C13 Q 802 -7 -366 -198 55 HOH 0 w 29 13 -215 -64 13
SCH C4 S 1 -5 -396 -153 21 90 HOH 0 w 30 9 -219 39 17
SCH C3 S 1 -4 -383 -149 18 HOH 0 w 31 1 -236 76 19
SCH C5 S 1 -6 -402 -155 20 HOH 0 w 32 -2 -243 50 18
SCH C16 S 1 -9 -334 -177 20 HOH 0 w 33 11 -300 83 20
SCH C18 S 1 -7 -331 -158 18 HOH 0 w 34 8 -343 46 17
SCH C2 S 1 -6 -375 -147 18 95 HOH 0 w 35 -15 -209 -89 17
SCH C6 S 1 -7 -394 -152 19 HOH 0 w 36 -1 -220 41 18
SCH C15 S 1 -8 -321 -181 20 HOH 0 w 37 -3 -204 40 27
SCH C13 S 1 -7 -317 -161 19 HOH 0 w 38 5 -193 -51 19
SCH C12 s 1 -13 -355 -120 17 HOH 0 w 39 5 -214 -37 18
SCH C8 s 1 -11 -349 -100 15 100 HOH 0 w 40 6 -176 -67 19
SCH CIO s 1 -14 -342 -101 16 HOH 0 w 41 5 -213 -152 34
SCH C17 s 1 -8 -340 -165 20 HOH 0 w 42 4 -252 -149 18
SCH C14 s 1 -8 -312 -173 22 HOH 0 w 43 1 -260 -156 24
SCH CI s 1 -7 -380 -148 18 HOH 0 w 44 -5 -269 -182 24
SCH C7 s 1 -11 -355 -113 16 105 HOH 0 w 45 12 -371 43 25
SCH Cll s 1 -14 -348 -114 20 HOH 0 w 46 10 -387 44 21
SCH C9 s 1 -12 -342 -94 16 HOH 0 w 47 8 -371 55 20
SCH C21 s 1 -8 -354 -162 21 HOH 0 w 48 7 -342 87 15
SCH C26 s 1 -10 -368 -129 19 HOH 0 w 49 11 -347 230 15
SCH C20 s 1 -9 -290 -172 30 110 HOH 0 w 50 17 -209 -31 20
SCH C32 s 1 -11 -338 -75 16 HOH 0 w 51 14 -182 5 17
SCH C19 s 1 -7 -298 -177 25 HOH 0 w 52 10 -315 308 18
SCH C24 s 1 -8 -372 -146 18 HOH 0 w 53 8 -336 312 17
SCH C25 s 1 -9 -374 -131 16 HOH 0 w 54 13 -295 328 29
SCH N29 s 1 -10 -361 -117 17 115 HOH 0 w 55 19 -294 -26 29
SCH N23 s 1 -8 -358 -149 19 HOH 0 w 56 18 -278 -4 25
SCH 022 s 1 -9 -362 -170 22 HOH 0 w 57 12 -203 -127 23
SCH 028 s 1 -11 -368 -138 19 HOH 0 w 58 15 -225 -104 16
SCH 030 s 1 -15 -348 -121 23 HOH 0 w 59 14 -253 -133 18
SCH 027 s 1 -8 -368 -122 16 120 HOH 0 w 60 14 -314 203 14
SCH 031 s 1 -12 -336 -83 17 HOH 0 w 61 6 -280 -187 28
HOH 0 w 1 -3 -288 -92 14 HOH 0 w 62 5 -501 -24 35 HOH 0 w 63 -8 -496 -61 27 HOH O w 124 7 -316 329 29
HOH 0 w 64 -0 -505 -78 32 HOH O w 125 6 -308 294 17
HOH 0 w 65 -5 -444 103 36 HOH O w 126 7 -291 311 26
HOH 0 w 66 -7 -402 91 18 65 HOH O w 127 13 -162 20 53
HOH 0 w 67 -5 -413 160 25 HOH O w 128 9 -413 387 39
HOH 0 w 68 -11 -325 85 15 HOH O w 129 9 -371 370 34
HOH 0 w 69 -12 -317 60 14 HOH O w 130 11 -333 186 19
HOH 0 w 70 -16 -386 59 21 HOH O w 131 12 -327 161 19
HOH 0 w 71 -14 -310 -13 26 70 HOH O w 132 16 -312 159 21
HOH 0 w 72 -22 -405 107 21 HOH O w 133 4 -227 208 29
HOH 0 w 73 10 -232 59 20 HOH O w 134 6 -218 182 29
HOH 0 w 74 3 -210 88 20 HOH O w 135 3 -411 -160 35
HOH 0 w 75 -6 -332 233 29 HOH O w 136 -2 -417 -176 57
HOH 0 w 76 1 -411 253 33 75 HOH O w 137 -7 -144 -18 37
HOH 0 w 77 6 -231 159 26 HOH O w 138 -27 -381 66 30
HOH 0 w 78 16 -268 54 24 HOH O w 139 1 -298 -219 45
HOH 0 w 79 -7 -216 -181 25 HOH O w 140 -1 -135 -83 42
HOH 0 w 80 -9 -197 -147 21 HOH O w 141 9 -335 69 26
HOH 0 w 81 -10 -171 -76 21 80 HOH O w 142 11 -406 58 29
HOH 0 w 82 -14 -196 -8 19 HOH O w 143 15 -383 48 34
HOH 0 w 83 0 -371 322 32 HOH O w 144 6 -334 -194 37
HOH 0 w 84 -15 -308 -143 22 HOH O w 145 12 -231 -139 32
HOH 0 w 85 -21 -222 -85 32 HOH O w 146 10 -368 -166 31
HOH 0 w 86 1 -455 83 27 85 HOH O w 147 2 -436 153 28
HOH 0 w 87 4 -439 121 28 HOH 0 w 148 2 -406 185 32
HOH 0 w 88 -3 -306 298 29 HOH 0 w 149 4 -377 150 24
HOH 0 w 89 -8 -327 232 22 HOH 0 w 150 -2 -285 186 26
HOH 0 w 90 -19 -212 -67 20 HOH 0 w 151 -2 -311 182 24
HOH 0 w 91 -4 -339 210 30 90 HOH 0 w 152 -4 -322 190 30
HOH 0 w 92 4 -319 321 24 HOH 0 w 153 -10 -431 145 29
HOH 0 w 93 -9 -145 -48 26 HOH 0 w 154 -19 -336 104 37
HOH 0 w 94 -6 -143 -106 32 HOH 0 w 155 -13 -265 -203 40
HOH 0 w 95 -4 -131 -74 26 HOH 0 w 156 -19 -309 78 32
HOH 0 w 96 -3 -136 -50 29 95 HOH 0 w 157 -15 -327 -165 35
HOH 0 w 97 -5 -156 -3 24 HOH 0 w 158 -12 -284 156 38
HOH 0 w 98 -13 -194 -85 30 HOH 0 w 159 -13 -277 129 36
HOH 0 w 99 -15 -206 15 26 HOH 0 w 160 -17 -277 -209 31
HOH 0 w 100 -10 -197 43 34 HOH 0 w 161 -14 -332 -55 32
HOH 0 w 101 10 -447 246 29 100 HOH 0 w 162 -6 -260 122 33
HOH 0 w 102 6 -190 -97 37 HOH 0 w 163 6 -234 112 26
HOH 0 w 103 14 -309 76 31 HOH 0 w 164 -3 -225 127 31
HOH 0 w 104 16 -407 -37 40 HOH 0 w 165 8 -461 81 38
HOH 0 w 105 -2 -141 -162 34 HOH 0 w 166 14 -467 44 27
HOH 0 w 106 -0 -137 -114 30 105 HOH 0 w 167 -17 -523 -25 33
HOH 0 w 107 15 -292 -148 27 HOH 0 w 168 14 -427 -5 31
HOH 0 w 108 5 -503 -50 39 HOH 0 w 169 -7 -366 307 28
HOH 0 w 109 -6 -399 -37 29 HOH 0 w 170 6 -365 226 26
HOH 0 w 110 1 -490 32 30 HOH 0 w 171 10 -355 175 17
HOH 0 w 111 16 -261 232 25 110 HOH 0 w 172 15 -326 134 29
HOH 0 w 112 8 -367 346 31 HOH 0 w 173 14 -213 207 77
HOH 0 w 113 -8 -277 116 25 HOH 0 w 174 14 -222 231 28
HOH 0 w 114 -19 -254 -114 26 HOH 0 w 175 15 -213 155 41
HOH 0 w 115 -11 -342 -34 30 HOH 0 w 176 18 -267 34 29
HOH 0 w 116 -14 -357 -51 28 115 HOH 0 w 177 18 -289 18 33
HOH 0 w 117 -20 -372 -26 30 HOH 0 w 178 -0 -215 68 32
HOH 0 w 118 -18 -299 -15 27 HOH 0 w 179 1 -197 84 32
HOH 0 w 119 -19 -307 -38 34 HOH 0 w 180 11 -209 74 35
HOH 0 w 120 -20 -275 -27 29 HOH 0 w 181 -20 -328 -67 42
HOH 0 w 121 -21 -298 -27 51 120 HOH 0 w 182 -7 -343 -122 17
60 HOH 0 w 122 -20 -298 55 32
HOH 0 w 123 -4 -383 280 39 EXAMPLE 11 : Factor IXa 318R/A-Compound A Complex Crystals Soaked with Compound B.
A factor IXa 318R/A-Compound A crystal as described in Example 7 was transferred to a 1 microliter hanging drop containing 2 mM Compound B
Figure imgf000039_0001
), 1 % DMSO, 1.0 M sodium citrate, 0.1 M CHES, pH 9.5 solution. The drop was subsequently incubated at 22° C for 3 days.
EXAMPLE 12: Crystallographic Analysis of Factor IXa 318R/A-Compound A Complex Crystals Soaked with Compound B.
Prior to data collection, crystals were harvested and cryoprotected for about 0.5-1 minutes in the crystallization solution containing 20% glycerol, 1.0 M sodium citrate, 0.1 M CHES, pH 9.5. The crystals were then frozen directly into liquid nitrogen. X-ray diffraction was collected at the Cornell High Energy Synchrotron Source on the A1 beam line. This beam line was equipped with an ADSC Quantum 210 CCD detector. Data were integrated and scaled using the HKL package.
Table 4. Data Collection Statistics for Example 12.
Figure imgf000039_0002
EXAMPLE 13: Structure Determination for Factor IXa 318R/A- Compound A Complex Crystals Soaked with Compound B.
The crystal structure was solved using Rigid Body refinement with the starting model Factor IXa 318R/A-Compound A. Refinement was done using the program AUTOBUSTER (Global Phasing Limited.). Table 5. Crystallization Parameters for Structure Determination for Factor IXa
318R/A- Compound A Complex Crystals Soaked with Compound B.
Figure imgf000040_0001
Table 6. Crystal Structural Coordinates of Factor IXa 318R/A-Compound B
Complex.
The following table contains one line for each atom in one Factor IXa 318R/A monomer. The columns are: 1 ) 3-Letter amino acid code, 2) Atom name, 3) Chain, 4) Residue number, 5) X-coordinate, 6) Y-coordinate, 7) Z-coordinate, 8) B-factor. (Amino Acid Code NA are Sodium, CHE is CHESS buffer, SCH is Compound B and HOH for water) Note: B factors greater than 100 appear as 0 in column 8.
VAL N A 16 -10 -310 -230 36 GLY C A 18 -14 -359 -273 39
VAL CA A 16 -11 -315 -242 35 GLY 0 A 18 -14 -361 -285 40
VAL C A 16 -12 -324 -239 37 30 GLY N A 19 -13 -359 -267 37
VAL 0 A 16 -12 -335 -233 36 GLY CA A 19 -12 -362 -275 36
VAL CB A 16 -10 -321 -253 38 GLY C A 19 -11 -377 -273 39
VAL CGI A 16 -11 -326 -265 37 GLY 0 A 19 -12 -384 -266 38
VAL CG2 A 16 -9 -311 -257 37 GLU N A 20 -10 -380 -278 36
VAL N A 17 -13 -320 -242 34 35 GLU CA A 20 -10 -393 -277 35
VAL CA A 17 -14 -327 -240 34 GLU C A 20 -8 -391 -271 41
VAL C A 17 -15 -334 -253 39 GLU 0 A 20 -8 -380 -273 41
VAL 0 A 17 -15 -328 -264 40 GLU CB A 20 -9 -400 -290 36
VAL CB A 17 -16 -318 -235 37 GLU CG A 20 -11 -405 -296 49
VAL CGI A 17 -17 -326 -231 36 40 GLU CD A 20 -11 -411 -310 80
VAL CG2 A 17 -15 -309 -224 36 GLU OE1 A 20 -10 -404 -320 79
GLY N A 18 -15 -347 -252 35 GLU OE2 A 20 -11 -423 -311 68
GLY CA A 18 -15 -355 -264 34 ASP N A 21 -8 -402 -265 37 ASP CA A 21 -6 -402 -260 36 TRP C A 29 4 -289 -297 35
ASP C A 21 -5 -401 -271 40 TRP O A 29 4 -278 -293 36
ASP 0 A 21 -5 -409 -280 39 TRP CB A 29 4 -287 -322 30
ASP CB A 21 -6 -414 -251 37 65 TRP CG A 29 3 -293 -327 31
ASP CG A 21 -7 -415 -238 46 TRP CD1 A 29 1 -291 -322 34
ASP OD1 A 21 -6 -423 -229 48 TRP CD2 A 29 3 -304 -337 31
ASP OD2 A 21 -8 -407 -235 51 TRP NE1 A 29 1 -299 -328 34
ALA N A 22 -4 -391 -271 36 TRP CE2 A 29 1 -307 -337 35
ALA CA A 22 -3 -390 -281 35 70 TRP CE3 A 29 4 -310 -345 33
ALA C A 22 -2 -401 -279 40 TRP CZ2 A 29 1 -317 -346 34
ALA 0 A 22 -2 -405 -267 40 TRP CZ3 A 29 3 -320 -354 34
ALA CB A 22 -3 -376 -280 35 TRP CH2 A 29 2 -323 -354 35
LYS N A 23 -2 -406 -289 38 GLN N A 30 3 -297 -292 31
LYS CA A 23 -1 -416 -288 37 75 GLN CA A 30 2 -294 -280 29
LYS C A 23 1 -409 -285 40 GLN C A 30 3 -293 -267 33
LYS 0 A 23 1 -397 -289 41 GLN O A 30 4 -302 -265 34
LYS CB A 23 -0 -424 -301 39 GLN CB A 30 1 -305 -279 30
LYS CG A 23 -1 -435 -303 50 GLN CG A 30 0 -305 -265 30
LYS CD A 23 -1 -442 -317 64 80 GLN CD A 30 -1 -294 -265 40
LYS CE A 23 -2 -453 -318 85 GLN OE1 A 30 -1 -286 -256 38
LYS NZ A 23 -2 -460 -332 98 GLN NE2 A 30 -2 -295 -273 21
PRO N A 24 2 -415 -279 36 VAL N A 31 3 -283 -259 29
PRO CA A 24 3 -407 -276 35 VAL CA A 31 4 -281 -246 28
PRO C A 24 4 -403 -289 40 85 VAL C A 31 3 -279 -235 33
PRO 0 A 24 4 -411 -298 41 VAL O A 31 1 -275 -239 33
PRO CB A 24 4 -417 -268 36 VAL CB A 31 5 -270 -246 30
PRO CG A 24 3 -427 -262 40 VAL CGI A 31 6 -272 -257 29
PRO CD A 24 2 -428 -273 36 VAL CG2 A 31 4 -256 -245 30
GLY N A 25 4 -390 -290 37 90 VAL N A 32 3 -280 -223 31
GLY CA A 25 5 -383 -301 36 VAL CA A 32 2 -278 -211 31
GLY C A 25 4 -380 -313 40 VAL C A 32 3 -267 -203 35
GLY 0 A 25 4 -377 -324 41 VAL O A 32 4 -268 -201 33
GLN N A 26 2 -380 -310 35 VAL CB A 32 2 -291 -204 34
GLN CA A 26 1 -376 -321 33 95 VAL CGI A 32 3 -297 -196 34
GLN C A 26 1 -361 -323 37 VAL CG2 A 32 0 -288 -194 33
GLN 0 A 26 1 -357 -334 38 LEU N A 33 2 -257 -198 33
GLN CB A 26 -0 -382 -317 33 LEU CA A 33 2 -246 -190 33
GLN CG A 26 -1 -383 -329 28 LEU C A 33 2 -250 -176 39
GLN CD A 26 -2 -388 -325 36 100 LEU O A 33 1 -253 -174 38
GLN OE1 A 26 -2 -396 -316 29 LEU CB A 33 2 -233 -193 33
GLN NE2 A 26 -3 -383 -332 30 LEU CG A 33 2 -228 -208 37
PHE N A 27 2 -353 -313 32 LEU CD1 A 33 1 -214 -209 37
PHE CA A 27 1 -338 -314 31 LEU CD2 A 33 3 -227 -213 38
PHE C A 27 3 -333 -307 37 105 ASN N A 34 3 -250 -166 36
PHE 0 A 27 3 -328 -296 37 ASN CA A 34 3 -252 -152 36
PHE CB A 27 0 -333 -306 32 ASN C A 34 3 -239 -144 42
PHE CG A 27 -1 -339 -312 32 ASN O A 34 4 -232 -148 40
PHE CD1 A 27 -2 -350 -306 34 ASN CB A 34 3 -264 -147 35
PHE CD2 A 27 -2 -333 -323 33 110 ASN CG A 34 3 -278 -153 48
PHE CE1 A 27 -3 -356 -312 34 ASN OD1 A 34 2 -280 -156 40
PHE CE2 A 27 -3 -339 -329 35 ASN ND2 A 34 4 -286 -155 34
PHE CZ A 27 -3 -351 -323 33 GLY N A 35 2 -236 -134 41
PRO N A 28 4 -335 -314 34 GLY CA A 35 2 -224 -125 43
PRO CA A 28 5 -332 -308 33 115 GLY C A 35 2 -227 -111 50
PRO C A 28 6 -317 -306 35 GLY O A 35 2 -236 -104 50
PRO 0 A 28 6 -313 -299 35 LYS N A 36 1 -218 -106 50
PRO CB A 28 6 -339 -317 35 LYS CA A 36 0 -219 -93 51
PRO CG A 28 6 -340 -330 39 LYS C A 36 -0 -232 -92 55
PRO CD A 28 4 -341 -328 34 120 LYS O A 36 -0 -239 -82 54
TRP N A 29 5 -308 -312 31 LYS CB A 36 -1 -207 -90 55
TRP CA A 29 5 -293 -310 31 LYS CG A 36 0 -193 -90 78 LYS CD A 36 -1 -182 -90 91 ILE CD1 A 45 8 -286 -286 22
LYS CE A 36 -0 -168 -91 0 VAL N A 46 7 -231 -314 32
LYS NZ A 36 -1 -157 -92 0 VAL CA A 46 8 -223 -326 32
VAL N A 37 -1 -235 -104 52 65 VAL C A 46 9 -227 -331 37
VAL CA A 37 -2 -247 -107 51 VAL 0 A 46 9 -230 -343 38
VAL C A 37 -1 -254 -119 52 VAL CB A 46 8 -208 -323 35
VAL 0 A 37 -1 -247 -128 51 VAL CGI A 46 8 -200 -335 35
VAL CB A 37 -3 -244 -109 56 VAL CG2 A 46 6 -204 -319 35
VAL CGI A 37 -4 -257 -113 56 70 ASN N A 47 10 -229 -322 32
VAL CG2 A 37 -4 -238 -97 56 ASN CA A 47 11 -234 -323 32
ASP N A 38 -1 -267 -119 47 ASN C A 47 12 -237 -309 37
ASP CA A 38 -0 -275 -130 46 ASN 0 A 47 11 -237 -299 37
ASP C A 38 -1 -276 -142 48 ASN CB A 47 12 -224 -331 29
ASP 0 A 38 -3 -276 -140 49 75 ASN CG A 47 12 -210 -325 40
ASP CB A 38 -0 -289 -125 48 ASN OD1 A 47 12 -208 -312 21
ASP CG A 38 1 -290 -118 60 ASN ND2 A 47 12 -200 -333 31
ASP 0D1 A 38 2 -280 -111 62 GLU N A 48 13 -240 -309 34
ASP OD2 A 38 2 -300 -120 64 GLU CA A 48 14 -244 -297 34
ALA N A 39 -1 -276 -154 41 80 GLU C A 48 14 -235 -285 37
ALA CA A 39 -2 -277 -167 39 GLU 0 A 48 14 -239 -274 37
ALA C A 39 -3 -267 -169 42 GLU CB A 48 16 -246 -301 36
ALA 0 A 39 -4 -270 -173 41 GLU CG A 48 16 -256 -312 49
ALA CB A 39 -2 -291 -169 39 GLU CD A 48 16 -251 -326 73
PHE N A 40 -3 -254 -165 38 85 GLU OE1 A 48 17 -252 -333 80
PHE CA A 40 -4 -243 -165 37 GLU OE2 A 48 15 -246 -330 57
PHE C A 40 -4 -238 -180 43 LYS N A 49 14 -222 -288 33
PHE 0 A 40 -5 -232 -182 42 LYS CA A 49 14 -211 -277 33
PHE CB A 40 -3 -231 -156 38 LYS C A 49 12 -204 -276 38
PHE CG A 40 -2 -224 -160 38 90 LYS O A 49 12 -196 -268 39
PHE CD1 A 40 -1 -228 -155 39 LYS CB A 49 15 -201 -279 35
PHE CD2 A 40 -2 -213 -169 39 LYS CG A 49 16 -205 -275 53
PHE CE1 A 40 1 -221 -159 40 LYS CD A 49 17 -202 -260 62
PHE CE2 A 40 -1 -207 -173 41 LYS CE A 49 17 -187 -258 63
PHE CZ A 40 0 -210 -168 39 95 LYS NZ A 49 18 -185 -244 63
CYS N A 41 -3 -241 -189 40 TRP N A 50 11 -208 -285 34
CYS CA A 41 -3 -237 -203 41 TRP CA A 50 10 -201 -284 34
CYS C A 41 -2 -246 -212 43 TRP C A 50 9 -209 -284 36
CYS 0 A 41 -1 -252 -206 44 TRP O A 50 9 -219 -292 37
CYS CB A 41 -3 -222 -204 42 100 TRP CB A 50 10 -190 -295 33
CYS SG A 41 -4 -211 -203 45 TRP CG A 50 11 -179 -294 34
GLY N A 42 -2 -245 -225 38 TRP CD1 A 50 12 -179 -300 37
GLY CA A 42 -1 -252 -235 37 TRP CD2 A 50 11 -167 -288 34
GLY C A 42 -0 -243 -242 38 TRP NE1 A 50 13 -167 -297 37
GLY 0 A 42 -0 -231 -240 38 105 TRP CE2 A 50 12 -160 -289 38
GLY N A 43 0 -248 -252 33 TRP CE3 A 50 10 -161 -280 36
GLY CA A 43 1 -240 -261 32 TRP CZ2 A 50 12 -147 -284 38
GLY C A 43 2 -248 -272 33 TRP CZ3 A 50 10 -148 -274 37
GLY 0 A 43 2 -260 -272 32 TRP CH2 A 50 11 -142 -276 38
SER N A 44 3 -242 -281 29 110 ILE N A 51 8 -205 -276 30
SER CA A 44 3 -248 -293 28 ILE CA A 51 7 -211 -275 27
SER C A 44 5 -244 -295 32 ILE C A 51 5 -201 -279 30
SER 0 A 44 5 -232 -293 33 ILE O A 51 6 -189 -274 28
SER CB A 44 2 -245 -305 31 ILE CB A 51 6 -217 -261 29
SER OG A 44 1 -251 -305 36 115 ILE CGI A 51 7 -227 -256 29
ILE N A 45 5 -254 -299 27 ILE CG2 A 51 5 -222 -258 28
ILE CA A 45 7 -252 -301 26 ILE CD1 A 51 8 -240 -264 35
ILE C A 45 7 -244 -315 33 VAL N A 52 4 -204 -286 26
ILE 0 A 45 7 -250 -325 33 VAL CA A 52 3 -196 -289 26
ILE CB A 45 8 -265 -301 29 120 VAL C A 52 2 -201 -281 31
ILE CGI A 45 8 -272 -287 28 VAL O A 52 2 -213 -281 32
ILE CG2 A 45 9 -263 -306 29 VAL CB A 52 3 -193 -304 31 VAL CGI A 52 2 -181 -306 30 GLY 0 A 61 6 -131 -117 74
VAL CG2 A 52 2 -206 -312 31 VAL N A 62 5 -135 -132 68
THR N A 53 1 -192 -273 27 VAL CA A 62 4 -148 -127 67
THR CA A 53 0 -195 -264 27 65 VAL C A 62 5 -158 -134 68
THR C A 53 -1 -184 -264 34 VAL 0 A 62 6 -158 -146 67
THR 0 A 53 -1 -174 -272 34 VAL CB A 62 3 -153 -129 71
THR CB A 53 1 -199 -250 32 VAL CGI A 62 3 -165 -121 71
THR OG1 A 53 -0 -204 -242 31 VAL CG2 A 62 2 -141 -124 71
THR CG2 A 53 1 -187 -243 29 70 LYS N A 63 6 -167 -126 62
ALA N A 54 -2 -184 -256 31 LYS CA A 63 7 -177 -130 61
ALA CA A 54 -3 -174 -254 32 LYS C A 63 6 -189 -135 63
ALA C A 54 -2 -164 -244 38 LYS 0 A 63 5 -195 -128 64
ALA 0 A 54 -2 -167 -233 39 LYS CB A 63 8 -181 -120 64
ALA CB A 54 -4 -180 -249 32 75 LYS CG A 63 9 -184 -125 82
ALA N A 55 -3 -151 -246 35 LYS CD A 63 10 -193 -116 92
ALA CA A 55 -2 -140 -238 35 LYS CE A 63 10 -208 -118 0
ALA C A 55 -3 -139 -224 39 LYS NZ A 63 10 -213 -132 0
ALA 0 A 55 -2 -134 -215 39 ILE N A 64 6 -192 -148 56
ALA CB A 55 -2 -127 -245 36 80 ILE CA A 64 6 -203 -155 54
HIS N A 56 -4 -145 -223 36 ILE C A 64 7 -213 -161 52
HIS CA A 56 -5 -146 -210 34 ILE 0 A 64 8 -209 -166 51
HIS C A 56 -4 -156 -201 40 ILE CB A 64 5 -197 -166 58
HIS 0 A 56 -4 -155 -188 41 ILE CGI A 64 4 -188 -160 58
HIS CB A 56 -6 -148 -212 35 85 ILE CG2 A 64 4 -208 -175 59
HIS CG A 56 -7 -162 -216 37 ILE CD1 A 64 3 -194 -147 57
HIS ND1 A 56 -7 -166 -229 39 THR N A 65 7 -226 -159 46
HIS CD2 A 56 -7 -172 -207 38 THR CA A 65 7 -237 -165 45
HIS CE1 A 56 -7 -179 -228 38 THR C A 65 7 -244 -176 46
HIS NE2 A 56 -7 -183 -215 38 90 THR 0 A 65 5 -247 -175 45
CYS N A 57 -3 -166 -206 39 THR CB A 65 8 -247 -154 54
CYS CA A 57 -3 -176 -198 41 THR OG1 A 65 7 -254 -148 61
CYS C A 57 -1 -170 -190 48 THR CG2 A 65 9 -241 -143 49
CYS 0 A 57 -1 -176 -180 46 VAL N A 66 7 -246 -187 41
CYS CB A 57 -2 -187 -207 41 95 VAL CA A 66 7 -252 -200 40
CYS SG A 57 -3 -196 -216 46 VAL C A 66 8 -266 -200 43
VAL N A 58 -1 -159 -196 48 VAL O A 66 9 -269 -196 43
VAL CA A 58 0 -153 -190 49 VAL CB A 66 8 -244 -212 44
VAL C A 58 0 -138 -186 59 VAL CGI A 66 8 -251 -225 44
VAL 0 A 58 -1 -131 -191 59 100 VAL CG2 A 66 7 -230 -213 44
VAL CB A 58 2 -156 -200 52 VAL N A 67 7 -276 -203 38
VAL CGI A 58 2 -170 -199 52 VAL CA A 67 7 -290 -204 38
VAL CG2 A 58 1 -151 -214 52 VAL C A 67 7 -295 -218 42
GLU N A 59 1 -134 -175 60 VAL O A 67 6 -295 -222 41
GLU CA A 59 1 -121 -169 62 105 VAL CB A 67 6 -300 -193 40
GLU C A 59 2 -118 -163 70 VAL CGI A 67 7 -313 -194 39
GLU 0 A 59 3 -124 -153 68 VAL CG2 A 67 7 -293 -179 40
GLU CB A 59 -0 -119 -160 63 ALA N A 68 8 -298 -226 38
GLU CG A 59 -0 -130 -149 73 ALA CA A 68 8 -303 -240 38
GLU CD A 59 -1 -126 -136 86 110 ALA C A 68 8 -318 -239 42
GLU OE1 A 59 -1 -114 -132 80 ALA O A 68 9 -323 -229 42
GLU OE2 A 59 -2 -135 -129 72 ALA CB A 68 9 -296 -249 39
THR N A 60 3 -108 -169 70 GLY N A 69 7 -326 -248 36
THR CA A 60 4 -103 -165 71 GLY CA A 69 8 -341 -248 35
THR C A 60 5 -102 -150 77 115 GLY C A 69 7 -348 -238 35
THR 0 A 60 4 -93 -143 78 GLY O A 69 7 -359 -235 33
THR CB A 60 5 -91 -174 76 GLU N A 70 6 -341 -233 33
THR OG1 A 60 5 -94 -188 73 GLU CA A 70 5 -345 -223 33
THR CG2 A 60 6 -87 -172 75 GLU C A 70 4 -354 -229 35
GLY N A 61 5 -112 -146 72 120 GLU O A 70 3 -352 -241 35
GLY CA A 61 6 -113 -132 72 GLU CB A 70 4 -333 -215 34
GLY C A 61 6 -127 -126 74 GLU CG A 70 3 -336 -202 41 GLU CD A 70 4 -345 -192 51 GLU OE1 A 77 4 -395 -200 63
GLU 0E1 A 70 4 -358 -193 48 GLU OE2 A 77 3 -416 -206 85
GLU OE2 A 70 5 -340 -182 39 HIS N A 78 10 -399 -197 53
HIS N A 71 3 -363 -221 32 65 HIS CA A 78 12 -397 -204 52
HIS CA A 71 2 -372 -225 32 HIS C A 78 12 -388 -216 49
HIS C A 71 1 -374 -214 37 HIS O A 78 13 -382 -218 48
HIS 0 A 71 -0 -369 -214 37 HIS CB A 78 12 -411 -207 54
HIS CB A 71 3 -385 -231 32 HIS CG A 78 13 -418 -194 58
HIS CG A 71 2 -395 -235 36 70 HIS ND1 A 78 14 -417 -187 60
HIS ND1 A 71 1 -393 -246 38 HIS CD2 A 78 12 -426 -187 60
HIS CD2 A 71 1 -407 -230 37 HIS CE1 A 78 14 -424 -176 60
HIS CE1 A 71 -0 -403 -247 37 HIS NE2 A 78 12 -430 -175 60
HIS NE2 A 71 0 -412 -237 37 THR N A 79 11 -386 -223 40
ASN N A 72 2 -381 -203 36 75 THR CA A 79 11 -377 -234 37
ASN CA A 72 1 -384 -191 36 THR C A 79 10 -362 -230 38
ASN C A 72 1 -375 -180 43 THR O A 79 11 -353 -238 36
ASN 0 A 72 2 -377 -175 42 THR CB A 79 9 -382 -244 43
ASN CB A 72 1 -399 -187 34 THR OG1 A 79 8 -381 -238 48
ASN CG A 72 -0 -402 -175 48 80 THR CG2 A 79 10 -396 -249 40
ASN OD1 A 72 -0 -395 -165 34 GLU N A 80 10 -360 -217 34
ASN ND2 A 72 -1 -414 -177 38 GLU CA A 80 10 -346 -211 34
ILE N A 73 1 -364 -176 42 GLU C A 80 11 -338 -210 38
ILE CA A 73 1 -354 -166 43 GLU O A 80 12 -343 -206 39
ILE C A 73 1 -359 -152 51 85 GLU CB A 80 9 -348 -196 35
ILE 0 A 73 2 -353 -146 52 GLU CG A 80 8 -352 -195 42
ILE CB A 73 0 -341 -166 46 GLU CD A 80 8 -366 -191 63
ILE CGI A 73 -1 -345 -162 46 GLU OE1 A 80 8 -375 -199 58
ILE CG2 A 73 0 -334 -179 47 GLU OE2 A 80 7 -369 -181 64
ILE CD1 A 73 -2 -334 -153 53 90 GLN N A 81 11 -325 -214 35
GLU N A 74 1 -369 -147 50 GLN CA A 81 12 -315 -214 34
GLU CA A 74 1 -375 -134 51 GLN C A 81 11 -302 -207 41
GLU C A 74 2 -386 -134 56 GLN O A 81 10 -296 -213 42
GLU 0 A 74 2 -393 -124 56 GLN CB A 81 12 -311 -228 35
GLU CB A 74 -0 -380 -127 52 95 GLN CG A 81 13 -322 -234 44
GLU CG A 74 -1 -392 -133 65 GLN CD A 81 14 -318 -247 57
GLU CD A 74 -2 -402 -124 87 GLN OE1 A 81 14 -307 -248 54
GLU OE1 A 74 -2 -398 -113 81 GLN NE2 A 81 14 -326 -257 48
GLU OE2 A 74 -2 -414 -127 76 LYS N A 82 12 -300 -194 38
GLU N A 75 3 -388 -146 53 100 LYS CA A 82 11 -289 -186 37
GLU CA A 75 4 -398 -148 54 LYS C A 82 12 -277 -188 40
GLU C A 75 5 -392 -154 60 LYS O A 82 13 -278 -188 39
GLU 0 A 75 5 -382 -161 60 LYS CB A 82 11 -294 -171 39
GLU CB A 75 3 -409 -156 56 LYS CG A 82 10 -286 -162 60
GLU CG A 75 4 -423 -155 72 105 LYS CD A 82 10 -292 -148 71
GLU CD A 75 3 -433 -166 98 LYS CE A 82 11 -282 -138 85
GLU OE1 A 75 2 -437 -165 90 LYS NZ A 82 11 -288 -124 96
GLU OE2 A 75 4 -436 -174 95 ARG N A 83 12 -265 -190 36
THR N A 76 6 -398 -152 58 ARG CA A 83 12 -252 -192 36
THR CA A 76 8 -395 -158 58 110 ARG C A 83 12 -241 -184 41
THR C A 76 8 -405 -169 61 ARG O A 83 10 -243 -180 41
THR 0 A 76 8 -417 -166 61 ARG CB A 83 12 -249 -207 37
THR CB A 76 9 -394 -148 64 ARG CG A 83 13 -259 -216 44
THR OG1 A 76 8 -383 -139 61 ARG CD A 83 15 -260 -213 42
THR CG2 A 76 10 -392 -154 64 115 ARG NE A 83 15 -269 -223 43
GLU N A 77 8 -400 -181 58 ARG CZ A 83 16 -283 -220 59
GLU CA A 77 8 -409 -193 58 ARG NH1 A 83 15 -288 -209 47
GLU C A 77 9 -407 -202 60 ARG NH2 A 83 16 -290 -229 42
GLU 0 A 77 10 -413 -212 62 ASN N A 84 12 -230 -183 39
GLU CB A 77 7 -408 -202 60 120 ASN CA A 84 12 -218 -176 39
GLU CG A 77 6 -414 -196 71 ASN C A 84 11 -207 -186 43
GLU CD A 77 4 -408 -201 89 ASN O A 84 12 -205 -195 42 ASN CB A 84 13 -213 -165 41 HIS CE1 A 91 -0 -82 -328 38
ASN CG A 84 13 -223 -154 70 HIS NE2 A 91 -1 -74 -324 38
ASN OD1 A 84 12 -228 -147 68 HIS N A 92 1 -66 -288 39
ASN ND2 A 84 14 -226 -151 58 65 HIS CA A 92 1 -52 -285 38
VAL N A 85 10 -199 -183 38 HIS C A 92 -0 -46 -284 41
VAL CA A 85 10 -187 -192 37 HIS O A 92 -1 -38 -275 42
VAL C A 85 11 -175 -186 40 HIS CB A 92 2 -44 -295 39
VAL 0 A 85 11 -171 -175 41 HIS CG A 92 2 -49 -308 43
VAL CB A 85 9 -184 -193 40 70 HIS ND1 A 92 1 -45 -319 45
VAL CGI A 85 8 -172 -201 38 HIS CD2 A 92 3 -59 -313 45
VAL CG2 A 85 8 -196 -198 39 HIS CE1 A 92 1 -52 -329 45
ILE N A 86 12 -170 -195 35 HIS NE2 A 92 2 -60 -327 45
ILE CA A 86 13 -158 -192 35 ASN N A 93 -1 -52 -292 37
ILE C A 86 12 -145 -197 41 75 ASN CA A 93 -3 -48 -291 37
ILE 0 A 86 12 -135 -191 42 ASN C A 93 -4 -56 -281 40
ILE CB A 86 14 -161 -196 37 ASN O A 93 -5 -54 -280 40
ILE CGI A 86 14 -164 -211 37 ASN CB A 93 -3 -49 -305 38
ILE CG2 A 86 15 -172 -187 35 ASN CG A 93 -3 -42 -316 57
ILE CD1 A 86 16 -160 -217 41 80 ASN OD1 A 93 -2 -47 -326 49
ARG N A 87 11 -146 -207 37 ASN ND2 A 93 -3 -29 -315 55
ARG CA A 87 11 -134 -213 36 TYR N A 94 -3 -65 -273 35
ARG C A 87 9 -137 -218 41 TYR CA A 94 -4 -72 -263 34
ARG 0 A 87 9 -148 -224 41 TYR C A 94 -4 -63 -251 41
ARG CB A 87 11 -129 -225 32 85 TYR O A 94 -3 -56 -247 41
ARG CG A 87 11 -115 -230 34 TYR CB A 94 -3 -85 -259 34
ARG CD A 87 12 -108 -235 52 TYR CG A 94 -4 -93 -248 33
ARG NE A 87 12 -103 -248 77 TYR CD1 A 94 -5 -101 -251 34
ARG CZ A 87 13 -107 -259 0 TYR CD2 A 94 -3 -92 -235 33
ARG NH1 A 87 14 -115 -257 89 90 TYR CE1 A 94 -5 -108 -241 33
ARG NH2 A 87 13 -103 -271 90 TYR CE2 A 94 -4 -99 -225 33
ILE N A 88 8 -128 -215 37 TYR CZ A 94 -5 -107 -228 37
ILE CA A 88 7 -130 -220 36 TYR OH A 94 -5 -114 -218 36
ILE C A 88 6 -119 -230 43 ASN N A 95 -5 -63 -245 39
ILE 0 A 88 7 -107 -227 44 95 ASN CA A 95 -5 -55 -233 38
ILE CB A 88 6 -130 -208 38 ASN C A 95 -6 -62 -224 42
ILE CGI A 88 6 -142 -199 38 ASN O A 95 -7 -61 -227 41
ILE CG2 A 88 4 -131 -214 38 ASN CB A 95 -6 -41 -236 38
ILE CD1 A 88 5 -142 -185 37 ASN CG A 95 -5 -31 -225 54
ILE N A 89 6 -123 -242 38 100 ASN OD1 A 95 -6 -35 -213 43
ILE CA A 89 6 -113 -252 37 ASN ND2 A 95 -5 -19 -228 44
ILE C A 89 4 -113 -257 40 ALA N A 96 -6 -68 -213 39
ILE 0 A 89 4 -119 -267 41 ALA CA A 96 -7 -75 -204 39
ILE CB A 89 7 -112 -265 39 ALA C A 96 -8 -66 -196 45
ILE CGI A 89 8 -112 -260 39 105 ALA O A 96 -9 -71 -192 46
ILE CG2 A 89 6 -101 -275 38 ALA CB A 96 -6 -83 -194 40
ILE CD1 A 89 9 -112 -271 46 ALA N A 97 -7 -53 -196 41
PRO N A 90 3 -107 -249 35 ALA CA A 97 -8 -43 -190 41
PRO CA A 90 2 -107 -254 35 ALA C A 97 -10 -40 -199 44
PRO C A 90 2 -97 -266 40 110 ALA O A 97 -11 -38 -193 44
PRO 0 A 90 3 -88 -267 41 ALA CB A 97 -8 -30 -188 42
PRO CB A 90 1 -102 -242 36 ILE N A 98 -9 -41 -212 39
PRO CG A 90 2 -95 -233 41 ILE CA A 98 -10 -40 -222 38
PRO CD A 90 3 -99 -237 37 ILE C A 98 -11 -53 -225 41
HIS N A 91 1 -99 -275 36 115 ILE O A 98 -12 -54 -223 39
HIS CA A 91 1 -90 -286 36 ILE CB A 98 -10 -32 -235 41
HIS C A 91 1 -76 -281 42 ILE CGI A 98 -9 -18 -231 41
HIS 0 A 91 -0 -74 -271 43 ILE CG2 A 98 -11 -32 -245 42
HIS CB A 91 -0 -94 -295 36 ILE CD1 A 98 -8 -13 -241 45
HIS CG A 91 -1 -87 -308 38 120 ASN N A 99 -10 -63 -230 37
HIS ND1 A 91 0 -90 -318 40 ASN CA A 99 -11 -76 -234 37
HIS CD2 A 91 -1 -78 -311 39 ASN C A 99 -10 -87 -231 42 ASN 0 A 99 -9 -87 -238 43 ALA CA A 106 2 -144 -265 34
ASN CB A 99 -11 -76 -248 36 ALA C A 106 3 -154 -269 38
ASN CG A 99 -12 -88 -252 51 ALA O A 106 3 -166 -271 38
ASN 0D1 A 99 -12 -99 -248 50 65 ALA CB A 106 2 -144 -250 35
ASN ND2 A 99 -13 -85 -262 43 LEU N A 107 4 -149 -270 34
LYS N A 100 -10 -96 -222 37 LEU CA A 107 5 -157 -273 33
LYS CA A 100 -9 -108 -219 36 LEU C A 107 6 -158 -260 37
LYS C A 100 -9 -117 -231 42 LEU O A 107 6 -148 -253 38
LYS 0 A 100 -8 -123 -231 42 70 LEU CB A 107 6 -150 -284 33
LYS CB A 100 -10 -116 -207 36 LEU CG A 107 5 -150 -298 35
LYS CG A 100 -9 -126 -200 45 LEU CD1 A 107 6 -140 -307 34
LYS CD A 100 -10 -135 -190 56 LEU CD2 A 107 5 -164 -305 36
LYS CE A 100 -9 -147 -186 66 LEU N A 108 7 -170 -257 33
LYS NZ A 100 -8 -145 -178 79 75 LEU CA A 108 7 -173 -245 32
TYR N A 101 -10 -118 -240 38 LEU C A 108 9 -176 -248 38
TYR CA A 101 -10 -127 -252 38 LEU O A 108 9 -185 -257 38
TYR C A 101 -10 -121 -266 43 LEU CB A 108 7 -184 -236 32
TYR 0 A 101 -9 -128 -275 42 LEU CG A 108 5 -182 -232 36
TYR CB A 101 -11 -137 -252 39 80 LEU CD1 A 108 5 -194 -224 35
TYR CG A 101 -11 -144 -238 40 LEU CD2 A 108 5 -169 -225 37
TYR CD1 A 101 -10 -154 -234 42 GLU N A 109 10 -170 -242 35
TYR CD2 A 101 -12 -142 -230 40 GLU CA A 109 11 -173 -245 35
TYR CE1 A 101 -10 -161 -222 41 GLU C A 109 12 -182 -234 39
TYR CE2 A 101 -12 -149 -218 41 85 GLU O A 109 11 -178 -222 40
TYR CZ A 101 -11 -158 -214 48 GLU CB A 109 12 -160 -246 37
TYR OH A 101 -11 -165 -202 50 GLU CG A 109 13 -163 -251 45
ASN N A 102 -9 -107 -267 41 GLU CD A 109 14 -152 -252 53
ASN CA A 102 -9 -101 -280 41 GLU OE1 A 109 14 -141 -247 32
ASN C A 102 -8 -99 -281 45 90 GLU OE2 A 109 15 -154 -257 46
ASN 0 A 102 -7 -95 -271 45 LEU N A 110 12 -193 -237 34
ASN CB A 102 -10 -88 -282 40 LEU CA A 110 13 -203 -228 34
ASN CG A 102 -10 -82 -296 58 LEU C A 110 14 -199 -223 41
ASN OD1 A 102 -9 -71 -297 54 LEU O A 110 15 -191 -229 42
ASN ND2 A 102 -10 -91 -306 51 95 LEU CB A 110 13 -217 -234 33
HIS N A 103 -7 -103 -293 42 LEU CG A 110 11 -221 -240 35
HIS CA A 103 -6 -103 -295 41 LEU CD1 A 110 11 -233 -248 34
HIS C A 103 -5 -113 -286 43 LEU CD2 A 110 10 -222 -230 35
HIS 0 A 103 -4 -111 -283 43 ASP N A 111 15 -205 -212 40
HIS CB A 103 -5 -89 -295 42 100 ASP CA A 111 16 -202 -205 41
HIS CG A 103 -6 -80 -306 46 ASP C A 111 17 -209 -214 47
HIS ND1 A 103 -6 -70 -303 48 ASP O A 111 18 -203 -217 47
HIS CD2 A 103 -5 -79 -319 48 ASP CB A 111 16 -207 -191 43
HIS CE1 A 103 -7 -64 -314 47 ASP CG A 111 16 -222 -188 60
HIS NE2 A 103 -6 -69 -324 47 105 ASP OD1 A 111 15 -227 -195 61
ASP N A 104 -6 -124 -282 37 ASP OD2 A 111 16 -228 -180 68
ASP CA A 104 -5 -135 -273 35 GLU N A 112 17 -222 -217 44
ASP C A 104 -4 -143 -278 37 GLU CA A 112 18 -230 -225 45
ASP 0 A 104 -4 -155 -282 37 GLU C A 112 17 -236 -237 49
ASP CB A 104 -6 -143 -269 36 110 GLU O A 112 16 -238 -236 49
ASP CG A 104 -6 -150 -256 40 GLU CB A 112 18 -241 -216 46
ASP OD1 A 104 -5 -148 -249 40 GLU CG A 112 20 -243 -216 59
ASP OD2 A 104 -7 -159 -253 40 GLU CD A 112 21 -231 -210 85
ILE N A 105 -3 -138 -278 33 GLU OE1 A 112 20 -228 -198 74
ILE CA A 105 -2 -144 -283 34 115 GLU OE2 A 112 21 -224 -218 86
ILE C A 105 -0 -139 -276 38 PRO N A 113 18 -237 -249 45
ILE 0 A 105 -0 -126 -274 37 PRO CA A 113 17 -242 -260 43
ILE CB A 105 -2 -144 -299 37 PRO C A 113 17 -257 -259 45
ILE CGI A 105 -0 -153 -304 38 PRO O A 113 17 -264 -251 45
ILE CG2 A 105 -1 -129 -304 38 120 PRO CB A 113 18 -240 -272 45
ILE CD1 A 105 -1 -157 -319 43 PRO CG A 113 19 -232 -267 50
ALA N A 106 0 -148 -272 35 PRO CD A 113 19 -235 -252 46 LEU N A 114 15 -260 -265 39 THR OG1 A 121 10 -333 -336 41
LEU CA A 114 15 -274 -265 36 THR CG2 A 121 9 -317 -352 28
LEU C A 114 16 -283 -274 39 PRO N A 122 9 -287 -336 26
LEU 0 A 114 17 -278 -282 37 65 PRO CA A 122 8 -275 -338 26
LEU CB A 114 13 -275 -270 36 PRO C A 122 7 -277 -347 33
LEU CG A 114 12 -268 -260 40 PRO O A 122 7 -286 -355 32
LEU CD1 A 114 11 -266 -267 39 PRO CB A 122 9 -265 -344 28
LEU CD2 A 114 12 -277 -248 43 PRO CG A 122 10 -270 -341 32
VAL N A 115 16 -296 -271 35 70 PRO CD A 122 10 -285 -342 27
VAL CA A 115 17 -305 -279 35 ILE N A 123 6 -268 -346 31
VAL C A 115 15 -311 -288 40 ILE CA A 123 5 -268 -355 31
VAL 0 A 115 14 -318 -283 40 ILE C A 123 5 -259 -367 37
VAL CB A 115 17 -315 -269 38 ILE O A 123 6 -251 -366 38
VAL CGI A 115 18 -327 -277 37 75 ILE CB A 123 3 -262 -348 33
VAL CG2 A 115 18 -309 -261 37 ILE CGI A 123 2 -264 -356 34
LEU N A 116 15 -308 -301 35 ILE CG2 A 123 4 -247 -343 32
LEU CA A 116 14 -313 -310 35 ILE CD1 A 123 2 -278 -360 44
LEU C A 116 15 -328 -313 41 CYS N A 124 5 -261 -379 33
LEU 0 A 116 16 -333 -315 42 80 CYS CA A 124 5 -253 -390 33
LEU CB A 116 14 -305 -323 34 CYS C A 124 4 -240 -390 34
LEU CG A 116 14 -290 -322 37 CYS O A 124 3 -241 -384 32
LEU CD1 A 116 14 -283 -336 36 CYS CB A 124 5 -260 -403 34
LEU CD2 A 116 13 -286 -315 39 CYS SG A 124 6 -275 -406 38
ASN N A 117 14 -335 -312 37 85 ILE N A 125 5 -229 -395 31
ASN CA A 117 13 -350 -315 37 ILE CA A 125 4 -216 -396 30
ASN C A 117 12 -353 -319 39 ILE C A 125 4 -211 -411 39
ASN 0 A 117 11 -345 -322 39 ILE O A 125 5 -207 -415 40
ASN CB A 117 14 -358 -303 33 ILE CB A 125 4 -206 -385 31
ASN CG A 117 13 -356 -290 46 90 ILE CGI A 125 4 -212 -371 30
ASN 0D1 A 117 12 -357 -289 34 ILE CG2 A 125 3 -193 -387 30
ASN ND2 A 117 14 -354 -279 44 ILE CD1 A 125 5 -207 -359 20
SER N A 118 12 -367 -321 35 ALA N A 126 3 -211 -419 37
SER CA A 118 10 -372 -325 35 ALA CA A 126 3 -206 -432 37
SER C A 118 9 -369 -316 39 95 ALA C A 126 3 -190 -432 40
SER 0 A 118 8 -369 -320 40 ALA O A 126 3 -185 -421 39
SER CB A 118 11 -387 -328 37 ALA CB A 126 2 -212 -440 37
SER OG A 118 12 -390 -336 44 ASP N A 127 3 -183 -443 37
TYR N A 119 10 -365 -303 35 ASP CA A 127 3 -169 -444 36
TYR CA A 119 9 -361 -293 33 100 ASP C A 127 1 -165 -441 43
TYR C A 119 9 -346 -290 36 ASP O A 127 0 -174 -440 44
TYR 0 A 119 8 -341 -284 37 ASP CB A 127 3 -164 -458 37
TYR CB A 119 9 -369 -280 34 ASP CG A 127 2 -167 -470 46
TYR CG A 119 9 -384 -282 35 ASP OD1 A 127 1 -176 -469 46
TYR CD1 A 119 8 -391 -279 36 105 ASP OD2 A 127 3 -162 -481 53
TYR CD2 A 119 10 -392 -285 36 LYS N A 128 1 -152 -439 39
TYR CE1 A 119 8 -405 -281 37 LYS CA A 128 -0 -147 -437 39
TYR CE2 A 119 10 -405 -286 37 LYS C A 128 -1 -154 -446 42
TYR CZ A 119 9 -412 -284 44 LYS O A 128 -3 -159 -441 42
TYR OH A 119 9 -426 -286 41 110 LYS CB A 128 -0 -132 -438 43
VAL N A 120 10 -339 -294 29 LYS CG A 128 -2 -125 -434 61
VAL CA A 120 10 -325 -293 28 LYS CD A 128 -2 -110 -435 71
VAL C A 120 10 -319 -307 33 LYS CE A 128 -3 -104 -433 81
VAL 0 A 120 11 -319 -311 34 LYS NZ A 128 -3 -89 -436 94
VAL CB A 120 11 -322 -282 31 115 GLU N A 129 -1 -154 -459 36
VAL CGI A 120 11 -307 -280 30 GLU CA A 129 -2 -159 -470 35
VAL CG2 A 120 11 -328 -268 30 GLU C A 129 -2 -174 -468 38
THR N A 121 9 -315 -314 30 GLU O A 129 -4 -178 -468 39
THR CA A 121 9 -310 -328 29 GLU CB A 129 -1 -157 -484 36
THR C A 121 8 -297 -329 28 120 GLU CG A 129 -2 -161 -496 48
THR 0 A 121 7 -297 -325 26 GLU CD A 129 -2 -161 -509 77
THR CB A 121 9 -321 -337 35 GLU OE1 A 129 -2 -169 -518 76 GLU 0E2 A 129 -1 -154 -511 69 LYS CD A 136 -11 -186 -456 70
TYR N A 130 -1 -183 -467 30 LYS CE A 136 -10 -175 -461 76
TYR CA A 130 -1 -197 -466 29 LYS NZ A 136 -11 -161 -459 77
TYR C A 130 -2 -202 -453 34 65 PHE N A 137 -10 -246 -450 37
TYR 0 A 130 -3 -211 -454 34 PHE CA A 137 -10 -260 -454 37
TYR CB A 130 -0 -205 -470 29 PHE C A 137 -11 -266 -447 42
TYR CG A 130 -0 -209 -484 29 PHE 0 A 137 -12 -276 -452 42
TYR CD1 A 130 0 -202 -494 29 PHE CB A 137 -9 -269 -451 38
TYR CD2 A 130 -1 -220 -489 30 70 PHE CG A 137 -8 -269 -460 39
TYR CE1 A 130 0 -205 -507 29 PHE CD1 A 137 -7 -259 -470 41
TYR CE2 A 130 -1 -223 -502 30 PHE CD2 A 137 -7 -278 -459 40
TYR CZ A 130 -0 -216 -512 37 PHE CE1 A 137 -6 -259 -479 41
TYR OH A 130 -0 -219 -525 38 PHE CE2 A 137 -5 -278 -468 41
THR N A 131 -2 -196 -442 32 75 PHE CZ A 137 -5 -268 -478 39
THR CA A 131 -2 -199 -429 32 GLY N A 138 -12 -261 -436 40
THR C A 131 -4 -197 -430 37 GLY CA A 138 -13 -264 -428 39
THR 0 A 131 -5 -205 -425 36 GLY C A 138 -13 -274 -416 43
THR CB A 131 -2 -190 -418 38 GLY 0 A 138 -13 -275 -408 42
THR OG1 A 131 -0 -190 -418 37 80 SER N A 139 -11 -280 -416 39
THR CG2 A 131 -2 -194 -404 39 SER CA A 139 -11 -290 -405 38
ASN N A 132 -4 -186 -437 33 SER C A 139 -10 -288 -399 42
ASN CA A 132 -6 -183 -439 33 SER 0 A 139 -9 -286 -406 42
ASN C A 132 -6 -193 -449 37 SER CB A 139 -11 -305 -411 42
ASN 0 A 132 -7 -198 -446 37 85 SER OG A 139 -11 -315 -401 48
ASN CB A 132 -6 -168 -443 34 GLY N A 140 -10 -289 -385 38
ASN CG A 132 -7 -164 -445 53 GLY CA A 140 -9 -287 -377 37
ASN OD1 A 132 -8 -167 -436 52 GLY C A 140 -9 -295 -365 41
ASN ND2 A 132 -8 -158 -456 38 GLY O A 140 -10 -299 -360 40
ILE N A 133 -6 -197 -460 33 90 TYR N A 141 -7 -299 -360 38
ILE CA A 133 -6 -208 -469 33 TYR CA A 141 -7 -307 -348 38
ILE C A 133 -6 -221 -461 37 TYR C A 141 -7 -298 -336 40
ILE 0 A 133 -7 -227 -462 38 TYR O A 141 -6 -290 -337 39
ILE CB A 133 -5 -210 -481 36 TYR CB A 141 -6 -318 -351 40
ILE CGI A 133 -5 -198 -492 36 95 TYR CG A 141 -7 -330 -358 44
ILE CG2 A 133 -5 -224 -488 37 TYR CD1 A 141 -7 -330 -372 47
ILE CD1 A 133 -4 -199 -503 34 TYR CD2 A 141 -7 -340 -351 46
PHE N A 134 -5 -225 -453 33 TYR CE1 A 141 -7 -340 -379 48
PHE CA A 134 -5 -237 -445 32 TYR CE2 A 141 -8 -350 -358 47
PHE C A 134 -6 -237 -435 36 100 TYR CZ A 141 -8 -350 -372 56
PHE 0 A 134 -7 -246 -435 35 TYR OH A 141 -9 -361 -379 60
PHE CB A 134 -4 -239 -438 33 VAL N A 142 -7 -301 -325 34
PHE CG A 134 -3 -242 -447 34 VAL CA A 142 -7 -293 -313 34
PHE CD1 A 134 -3 -247 -459 37 VAL C A 142 -7 -303 -302 38
PHE CD2 A 134 -1 -238 -442 36 105 VAL O A 142 -7 -315 -301 38
PHE CE1 A 134 -2 -250 -468 38 VAL CB A 142 -8 -284 -308 37
PHE CE2 A 134 -0 -241 -451 38 VAL CGI A 142 -8 -272 -316 36
PHE CZ A 134 -1 -246 -463 37 VAL CG2 A 142 -10 -292 -307 37
LEU N A 135 -7 -226 -428 33 SER N A 143 -6 -299 -294 35
LEU CA A 135 -8 -224 -419 33 110 SER CA A 143 -5 -308 -283 35
LEU C A 135 -9 -226 -426 38 SER C A 143 -5 -300 -270 39
LEU 0 A 135 -10 -232 -421 38 SER O A 143 -5 -288 -270 40
LEU CB A 135 -8 -210 -412 33 SER CB A 143 -4 -315 -288 38
LEU CG A 135 -9 -205 -405 37 SER OG A 143 -3 -308 -296 44
LEU CD1 A 135 -9 -190 -402 37 115 GLY N A 144 -5 -307 -259 35
LEU CD2 A 135 -9 -213 -392 38 GLY CA A 144 -5 -302 -246 34
LYS N A 136 -9 -221 -439 34 GLY C A 144 -5 -311 -234 37
LYS CA A 136 -10 -222 -447 34 GLY O A 144 -6 -322 -237 36
LYS C A 136 -11 -236 -454 41 TRP N A 145 -5 -307 -222 34
LYS 0 A 136 -12 -238 -461 42 120 TRP CA A 145 -5 -315 -210 34
LYS CB A 136 -10 -210 -457 36 TRP C A 145 -6 -309 -201 41
LYS CG A 136 -11 -197 -449 57 TRP O A 145 -6 -312 -189 42 TRP CB A 145 -3 -315 -202 33 LYS NZ A 151 -21 -242 -125 82
TRP CG A 145 -2 -326 -207 34 GLY N A 152 -16 -308 -150 44
TRP CD1 A 145 -2 -339 -203 37 GLY CA A 152 -15 -320 -146 44
TRP CD2 A 145 -1 -323 -216 33 65 GLY C A 152 -13 -319 -144 47
TRP NE1 A 145 -1 -345 -209 36 GLY 0 A 152 -13 -308 -144 48
TRP CE2 A 145 -1 -335 -217 37 ARG N A 153 -13 -330 -142 41
TRP CE3 A 145 -1 -312 -223 34 ARG CA A 153 -11 -330 -140 41
TRP CZ2 A 145 0 -337 -225 36 ARG C A 153 -11 -329 -152 46
TRP CZ3 A 145 0 -313 -231 36 70 ARG 0 A 153 -11 -331 -163 46
TRP CH2 A 145 1 -325 -232 36 ARG CB A 153 -11 -343 -132 39
GLY N A 146 -7 -300 -207 36 SER N A 154 -9 -325 -150 42
GLY CA A 146 -8 -294 -200 36 SER CA A 154 -8 -324 -161 42
GLY C A 146 -9 -303 -196 41 SER C A 154 -8 -337 -166 45
GLY 0 A 146 -9 -315 -199 42 75 SER 0 A 154 -8 -348 -160 43
ARG N A 147 -10 -298 -190 37 SER CB A 154 -7 -317 -155 45
ARG CA A 147 -11 -305 -185 36 SER OG A 154 -7 -304 -150 57
ARG C A 147 -12 -314 -195 40 ALA N A 155 -7 -337 -179 42
ARG 0 A 147 -12 -310 -207 39 ALA CA A 155 -7 -349 -185 41
ARG CB A 147 -12 -295 -179 34 80 ALA C A 155 -5 -353 -180 43
ARG CG A 147 -12 -287 -167 36 ALA 0 A 155 -5 -344 -177 42
ARG CD A 147 -13 -278 -162 46 ALA CB A 155 -7 -347 -200 41
ARG NE A 147 -12 -274 -148 62 LEU N A 156 -5 -366 -179 39
ARG CZ A 147 -13 -264 -142 80 LEU CA A 156 -4 -371 -175 38
ARG NH1 A 147 -14 -258 -148 72 85 LEU C A 156 -3 -373 -188 40
ARG NH2 A 147 -13 -261 -130 69 LEU 0 A 156 -2 -367 -189 42
VAL N A 148 -12 -326 -191 34 LEU CB A 156 -4 -385 -168 39
VAL CA A 148 -13 -337 -200 33 LEU CG A 156 -5 -385 -154 43
VAL C A 148 -14 -336 -200 38 LEU CD1 A 156 -5 -399 -149 44
VAL 0 A 148 -15 -343 -207 39 90 LEU CD2 A 156 -4 -376 -144 44
VAL CB A 148 -12 -351 -197 36 VAL N A 157 -4 -381 -197 35
VAL CGI A 148 -11 -351 -199 35 VAL CA A 157 -3 -384 -210 33
VAL CG2 A 148 -12 -356 -183 36 VAL C A 157 -4 -373 -220 35
PHE N A 149 -15 -327 -191 36 VAL 0 A 157 -5 -370 -220 34
PHE CA A 149 -16 -325 -189 35 95 VAL CB A 157 -3 -398 -215 37
PHE C A 149 -16 -310 -186 42 VAL CGI A 157 -3 -400 -230 36
PHE 0 A 149 -15 -304 -181 41 VAL CG2 A 157 -2 -408 -207 37
PHE CB A 149 -17 -333 -178 36 LEU N A 158 -3 -367 -228 29
PHE CG A 149 -17 -348 -181 37 LEU CA A 158 -3 -357 -238 27
PHE CD1 A 149 -16 -357 -174 39 100 LEU C A 158 -4 -361 -247 33
PHE CD2 A 149 -18 -353 -192 38 LEU 0 A 158 -4 -372 -252 33
PHE CE1 A 149 -16 -371 -176 40 LEU CB A 158 -2 -354 -247 27
PHE CE2 A 149 -18 -367 -195 40 LEU CG A 158 -2 -344 -258 30
PHE CZ A 149 -17 -376 -187 38 LEU CD1 A 158 -2 -330 -253 31
HIS N A 150 -18 -304 -188 42 105 LEU CD2 A 158 -1 -343 -266 28
HIS CA A 150 -18 -290 -184 43 GLN N A 159 -5 -352 -248 31
HIS C A 150 -17 -285 -171 49 GLN CA A 159 -6 -354 -256 30
HIS 0 A 150 -16 -275 -172 51 GLN C A 159 -6 -347 -269 34
HIS CB A 150 -19 -285 -186 44 GLN 0 A 159 -6 -336 -271 34
HIS CG A 150 -19 -271 -180 47 110 GLN CB A 159 -8 -349 -249 31
HIS ND1 A 150 -19 -261 -182 49 GLN CG A 159 -8 -354 -235 37
HIS CD2 A 150 -20 -268 -172 50 GLN CD A 159 -8 -369 -235 46
HIS CE1 A 150 -19 -251 -174 49 GLN OE1 A 159 -7 -377 -230 39
HIS NE2 A 150 -20 -255 -168 50 GLN NE2 A 159 -9 -371 -239 45
LYS N A 151 -17 -291 -160 45 115 TYR N A 160 -7 -353 -279 32
LYS CA A 151 -17 -287 -147 44 TYR CA A 160 -7 -346 -293 33
LYS C A 151 -16 -299 -141 48 TYR C A 160 -8 -347 -298 36
LYS 0 A 151 -16 -300 -129 48 TYR 0 A 160 -9 -356 -296 37
LYS CB A 151 -18 -280 -138 46 TYR CB A 160 -6 -352 -302 34
LYS CG A 151 -18 -266 -141 49 120 TYR CG A 160 -6 -365 -309 37
LYS CD A 151 -19 -261 -133 58 TYR CD1 A 160 -7 -366 -322 39
LYS CE A 151 -19 -246 -132 71 TYR CD2 A 160 -6 -378 -302 38 TYR CE1 A 160 -7 -378 -328 41 ARG CA A 168 -19 -163 -391 45
TYR CE2 A 160 -6 -390 -309 39 ARG C A 168 -21 -160 -385 49
TYR CZ A 160 -7 -390 -321 48 ARG O A 168 -21 -156 -374 49
TYR OH A 160 -7 -402 -328 50 65 ARG CB A 168 -19 -152 -399 45
LEU N A 161 -9 -337 -306 30 ARG CG A 168 -18 -140 -391 54
LEU CA A 161 -10 -336 -312 30 ARG CD A 168 -18 -128 -400 58
LEU C A 161 -10 -329 -326 35 ARG NE A 168 -18 -116 -392 63
LEU 0 A 161 -9 -318 -327 35 ARG CZ A 168 -19 -107 -391 74
LEU CB A 161 -11 -329 -303 29 70 ARG NH1 A 168 -20 -109 -396 53
LEU CG A 161 -13 -326 -307 32 ARG NH2 A 168 -19 -96 -384 67
LEU CD1 A 161 -13 -339 -308 32 ALA N A 169 -22 -162 -393 44
LEU CD2 A 161 -13 -317 -297 30 ALA CA A 169 -23 -160 -389 44
ARG N A 162 -11 -334 -336 34 ALA C A 169 -24 -169 -378 48
ARG CA A 162 -11 -328 -349 34 75 ALA O A 169 -24 -164 -368 47
ARG C A 162 -12 -319 -347 42 ALA CB A 169 -24 -161 -401 45
ARG 0 A 162 -13 -324 -344 44 THR N A 170 -23 -182 -379 44
ARG CB A 162 -11 -339 -359 36 THR CA A 170 -24 -192 -369 44
ARG CG A 162 -11 -333 -374 43 THR C A 170 -23 -189 -356 48
ARG CD A 162 -12 -341 -383 50 80 THR O A 170 -24 -190 -345 47
ARG NE A 162 -14 -340 -380 61 THR CB A 170 -24 -206 -375 48
ARG CZ A 162 -14 -331 -384 68 THR OG1 A 170 -24 -207 -387 47
ARG NH1 A 162 -14 -321 -392 61 THR CG2 A 170 -24 -217 -366 43
ARG NH2 A 162 -16 -331 -380 45 CYS N A 171 -22 -185 -357 47
VAL N A 163 -12 -306 -349 39 85 CYS CA A 171 -21 -182 -347 48
VAL CA A 163 -13 -296 -349 39 CYS C A 171 -21 -170 -338 52
VAL C A 163 -13 -289 -362 40 CYS O A 171 -22 -171 -326 52
VAL 0 A 163 -12 -284 -368 40 CYS CB A 171 -20 -178 -353 49
VAL CB A 163 -13 -285 -337 43 CYS SG A 171 -18 -174 -341 53
VAL CGI A 163 -13 -291 -324 43 90 LEU N A 172 -22 -159 -345 47
VAL CG2 A 163 -12 -278 -338 43 LEU CA A 172 -22 -147 -339 46
PRO N A 164 -15 -289 -367 34 LEU C A 172 -24 -149 -333 51
PRO CA A 164 -15 -283 -380 33 LEU O A 172 -24 -142 -322 51
PRO C A 164 -15 -268 -378 37 LEU CB A 172 -22 -135 -350 46
PRO 0 A 164 -16 -264 -368 36 95 LEU CG A 172 -21 -125 -351 50
PRO CB A 164 -16 -290 -385 35 LEU CD1 A 172 -20 -132 -352 51
PRO CG A 164 -17 -294 -373 39 LEU CD2 A 172 -22 -115 -362 52
PRO CD A 164 -16 -295 -361 36 ARG N A 173 -25 -157 -338 48
LEU N A 165 -15 -260 -388 33 ARG CA A 173 -26 -160 -333 48
LEU CA A 165 -15 -245 -389 32 100 ARG C A 173 -26 -168 -320 52
LEU C A 165 -16 -242 -389 39 ARG O A 173 -27 -165 -311 53
LEU 0 A 165 -17 -249 -396 39 ARG CB A 173 -27 -168 -343 50
LEU CB A 165 -14 -239 -401 31 ARG CG A 173 -27 -160 -354 67
LEU CG A 165 -14 -224 -401 35 ARG CD A 173 -28 -168 -362 85
LEU CD1 A 165 -13 -219 -390 33 105 ARG NE A 173 -28 -182 -364 98
LEU CD2 A 165 -14 -218 -414 37 ARG CZ A 173 -27 -187 -374 0
VAL N A 166 -17 -232 -382 38 ARG NH1 A 173 -27 -179 -383 0
VAL CA A 166 -18 -228 -381 39 ARG NH2 A 173 -27 -200 -375 94
VAL C A 166 -18 -214 -387 47 SER N A 174 -25 -177 -318 46
VAL 0 A 166 -18 -205 -384 47 110 SER CA A 174 -25 -186 -307 45
VAL CB A 166 -19 -227 -366 42 SER C A 174 -24 -178 -294 47
VAL CGI A 166 -20 -222 -364 41 SER O A 174 -25 -184 -283 46
VAL CG2 A 166 -19 -241 -360 41 SER CB A 174 -23 -195 -310 47
ASP N A 167 -19 -212 -397 46 SER OG A 174 -22 -189 -306 48
ASP CA A 167 -19 -200 -404 46 115 THR N A 175 -24 -166 -294 43
ASP C A 167 -20 -188 -394 49 THR CA A 175 -23 -158 -283 42
ASP 0 A 167 -20 -190 -384 49 THR C A 175 -24 -144 -283 48
ASP CB A 167 -21 -201 -414 49 THR O A 175 -24 -138 -293 49
ASP CG A 167 -22 -204 -409 70 THR CB A 175 -22 -159 -282 44
ASP OD1 A 167 -23 -195 -407 71 120 THR OG1 A 175 -21 -151 -271 43
ASP OD2 A 167 -22 -216 -406 80 THR CG2 A 175 -21 -154 -295 43
ARG N A 168 -19 -176 -398 46 LYS N A 176 -24 -138 -271 44 LYS CA A 176 -24 -124 -269 43 ASN ND2 A 182 -8 -86 -360 82
LYS C A 176 -23 -115 -269 47 MET N A 183 -11 -136 -347 35
LYS 0 A 176 -23 -103 -272 46 MET CA A 183 -11 -148 -340 34
LYS CB A 176 -25 -121 -255 45 65 MET C A 183 -12 -157 -350 39
LYS CG A 176 -24 -127 -243 61 MET O A 183 -12 -152 -361 39
LYS CD A 176 -25 -129 -231 71 MET CB A 183 -12 -144 -328 36
LYS CE A 176 -25 -136 -220 84 MET CG A 183 -12 -136 -317 38
LYS NZ A 176 -26 -136 -208 92 MET SD A 183 -13 -131 -306 41
PHE N A 177 -22 -122 -267 44 70 MET CE A 183 -12 -117 -298 37
PHE CA A 177 -20 -117 -268 43 PHE N A 184 -12 -169 -346 34
PHE C A 177 -20 -114 -282 48 PHE CA A 184 -13 -179 -354 34
PHE 0 A 177 -21 -120 -291 48 PHE C A 184 -14 -189 -346 41
PHE CB A 177 -20 -126 -260 45 PHE O A 184 -13 -192 -335 40
PHE CG A 177 -20 -127 -246 47 75 PHE CB A 184 -12 -186 -365 35
PHE CD1 A 177 -20 -117 -236 50 PHE CG A 184 -11 -196 -362 36
PHE CD2 A 177 -20 -139 -241 49 PHE CD1 A 184 -11 -210 -360 38
PHE CE1 A 177 -20 -119 -223 50 PHE CD2 A 184 -10 -193 -360 37
PHE CE2 A 177 -21 -140 -228 52 PHE CE1 A 184 -11 -220 -357 39
PHE CZ A 177 -21 -130 -219 50 80 PHE CE2 A 184 -9 -203 -357 39
THR N A 178 -19 -104 -283 44 PHE CZ A 184 -9 -217 -355 38
THR CA A 178 -19 -100 -296 43 CYS N A 185 -15 -194 -351 43
THR C A 178 -17 -109 -301 45 CYS CA A 185 -16 -204 -345 45
THR 0 A 178 -16 -111 -294 44 CYS C A 185 -15 -218 -351 46
THR CB A 178 -18 -85 -295 54 85 CYS O A 185 -15 -219 -363 46
THR 0G1 A 178 -19 -77 -291 56 CYS CB A 185 -17 -201 -346 48
THR CG2 A 178 -18 -80 -309 51 CYS SG A 185 -18 -192 -332 53
ILE N A 179 -18 -114 -313 40 ALA N A 186 -15 -228 -342 42
ILE CA A 179 -17 -122 -320 39 ALA CA A 186 -15 -241 -346 41
ILE C A 179 -16 -113 -331 42 90 ALA C A 186 -16 -250 -336 44
ILE 0 A 179 -17 -109 -341 42 ALA O A 186 -15 -247 -324 44
ILE CB A 179 -17 -135 -327 43 ALA CB A 186 -13 -244 -347 42
ILE CGI A 179 -18 -142 -317 43 GLY N A 187 -16 -260 -340 40
ILE CG2 A 179 -16 -144 -333 43 GLY CA A 187 -17 -270 -331 39
ILE CD1 A 179 -18 -147 -304 48 95 GLY C A 187 -18 -276 -337 43
TYR N A 180 -15 -110 -329 38 GLY O A 187 -18 -276 -349 41
TYR CA A 180 -14 -101 -339 37 PHE N A 188 -19 -282 -328 42
TYR C A 180 -13 -109 -350 44 PHE CA A 188 -20 -290 -331 43
TYR 0 A 180 -13 -122 -349 44 PHE C A 188 -22 -284 -327 53
TYR CB A 180 -13 -93 -332 37 100 PHE O A 188 -22 -279 -315 54
TYR CG A 180 -14 -82 -323 38 PHE CB A 188 -20 -304 -327 44
TYR CD1 A 180 -13 -81 -309 39 PHE CG A 188 -19 -312 -334 44
TYR CD2 A 180 -14 -72 -329 38 PHE CD1 A 188 -18 -311 -329 47
TYR CE1 A 180 -14 -71 -302 40 PHE CD2 A 188 -19 -319 -346 46
TYR CE2 A 180 -15 -62 -321 39 105 PHE CE1 A 188 -17 -318 -336 48
TYR CZ A 180 -15 -62 -308 45 PHE CE2 A 188 -18 -325 -352 48
TYR OH A 180 -15 -52 -300 45 PHE CZ A 188 -17 -325 -347 47
ASN N A 181 -13 -102 -361 42 HIS N A 189 -23 -284 -335 55
ASN CA A 181 -12 -109 -373 42 HIS CA A 189 -24 -279 -333 57
ASN C A 181 -11 -115 -372 46 110 HIS C A 189 -25 -287 -322 60
ASN 0 A 181 -11 -123 -380 47 HIS O A 189 -25 -281 -313 60
ASN CB A 181 -13 -99 -385 44 HIS CB A 189 -25 -278 -346 60
ASN CG A 181 -14 -95 -388 78 HIS CG A 189 -26 -274 -344 65
ASN OD1 A 181 -15 -100 -396 76 HIS ND1 A 189 -27 -282 -347 67
ASN ND2 A 181 -14 -85 -380 72 115 HIS CD2 A 189 -27 -262 -340 67
ASN N A 182 -10 -113 -360 41 HIS CE1 A 189 -28 -276 -344 67
ASN CA A 182 -9 -119 -356 40 HIS NE2 A 189 -28 -263 -340 67
ASN C A 182 -9 -131 -346 40 GLU N A 190 -24 -300 -322 56
ASN 0 A 182 -9 -136 -339 38 GLU CA A 190 -25 -309 -313 55
ASN CB A 182 -8 -109 -352 44 120 GLU C A 190 -24 -310 -299 57
ASN CG A 182 -8 -99 -363 85 GLU O A 190 -25 -317 -290 56
ASN OD1 A 182 -8 -103 -375 77 GLU CB A 190 -25 -323 -319 57 GLU CG A 190 -26 -324 -330 70 ASP CG A 199 -8 -283 -236 43
GLU CD A 190 -28 -321 -326 94 ASP OD1 A 199 -7 -291 -233 44
GLU 0E1 A 190 -28 -310 -330 92 ASP OD2 A 199 -9 -285 -236 49
GLU OE2 A 190 -28 -330 -320 85 65 SER N A 200 -7 -238 -233 33
GLY N A 191 -23 -304 -298 52 SER CA A 200 -6 -225 -239 32
GLY CA A 191 -22 -304 -286 51 SER C A 200 -5 -223 -241 36
GLY C A 191 -22 -316 -284 53 SER O A 200 -4 -227 -233 37
GLY 0 A 191 -21 -324 -293 53 SER CB A 200 -7 -214 -230 35
GLY N A 192 -21 -318 -271 47 70 SER OG A 200 -8 -214 -229 42
GLY CA A 192 -21 -330 -267 45 GLY N A 201 -4 -216 -252 31
GLY C A 192 -19 -331 -270 44 GLY CA A 201 -3 -214 -256 31
GLY 0 A 192 -18 -339 -265 42 GLY C A 201 -2 -226 -264 34
ARG N A 193 -19 -322 -279 37 GLY O A 201 -1 -224 -272 35
ARG CA A 193 -17 -321 -284 35 75 GLY N A 202 -3 -237 -263 29
ARG C A 193 -17 -307 -284 37 GLY CA A 202 -3 -249 -271 29
ARG 0 A 193 -17 -299 -292 36 GLY C A 202 -3 -247 -286 33
ARG CB A 193 -17 -327 -298 32 GLY O A 202 -4 -237 -290 32
ARG CG A 193 -17 -342 -299 33 PRO N A 203 -3 -256 -295 30
ARG CD A 193 -17 -347 -313 34 80 PRO CA A 203 -3 -254 -309 29
ARG NE A 193 -19 -347 -317 44 PRO C A 203 -4 -259 -315 31
ARG CZ A 193 -19 -351 -329 56 PRO O A 203 -5 -269 -310 30
ARG NH1 A 193 -18 -355 -338 34 PRO CB A 203 -2 -262 -315 31
ARG NH2 A 193 -20 -350 -332 45 PRO CG A 203 -1 -273 -306 36
ASP N A 194 -16 -303 -276 32 85 PRO CD A 203 -2 -267 -292 32
ASP CA A 194 -15 -289 -276 32 HIS N A 204 -4 -252 -326 26
ASP C A 194 -14 -289 -268 37 HIS CA A 204 -5 -256 -336 26
ASP 0 A 194 -14 -299 -261 36 HIS C A 204 -5 -258 -349 30
ASP CB A 194 -16 -280 -268 34 HIS O A 204 -4 -248 -354 29
ASP CG A 194 -16 -265 -269 45 90 HIS CB A 204 -7 -245 -337 26
ASP OD1 A 194 -16 -260 -280 47 HIS CG A 204 -8 -249 -348 28
ASP OD2 A 194 -16 -259 -259 51 HIS ND1 A 204 -7 -246 -361 30
SER N A 195 -13 -278 -269 37 HIS CD2 A 204 -9 -254 -347 29
SER CA A 195 -12 -275 -260 37 HIS CE1 A 204 -8 -251 -368 29
SER C A 195 -13 -271 -247 42 95 HIS NE2 A 204 -9 -256 -360 29
SER 0 A 195 -14 -267 -246 42 VAL N A 205 -4 -270 -353 27
SER CB A 195 -11 -263 -267 41 VAL CA A 205 -4 -273 -365 27
SER OG A 195 -11 -266 -280 52 VAL C A 205 -4 -279 -377 33
CYS N A 196 -12 -271 -236 39 VAL O A 205 -5 -285 -375 32
CYS CA A 196 -12 -267 -223 40 100 VAL CB A 205 -2 -281 -361 31
CYS C A 196 -11 -260 -215 41 VAL CGI A 205 -1 -274 -351 31
CYS 0 A 196 -10 -257 -220 39 VAL CG2 A 205 -3 -295 -358 31
CYS CB A 196 -13 -279 -216 42 THR N A 206 -4 -277 -389 30
CYS SG A 196 -14 -275 -203 48 THR CA A 206 -4 -282 -401 30
GLN N A 197 -12 -256 -202 36 105 THR C A 206 -3 -291 -408 37
GLN CA A 197 -11 -249 -192 34 THR O A 206 -2 -286 -410 36
GLN C A 197 -9 -258 -191 36 THR CB A 206 -5 -270 -409 36
GLN 0 A 197 -9 -270 -188 33 THR OG1 A 206 -6 -263 -402 37
GLN CB A 197 -11 -248 -179 35 THR CG2 A 206 -5 -274 -423 34
GLN CG A 197 -12 -234 -175 54 110 GLU N A 207 -4 -304 -409 35
GLN CD A 197 -12 -231 -160 88 GLU CA A 207 -3 -314 -416 35
GLN OE1 A 197 -12 -239 -152 87 GLU C A 207 -3 -310 -431 39
GLN NE2 A 197 -12 -219 -157 85 GLU O A 207 -4 -310 -436 37
GLY N A 198 -8 -252 -194 32 GLU CB A 207 -3 -328 -414 37
GLY CA A 198 -7 -258 -194 32 115 GLU CG A 207 -3 -334 -400 52
GLY C A 198 -6 -261 -207 34 GLU CD A 207 -4 -347 -397 86
GLY 0 A 198 -5 -264 -208 34 GLU OE1 A 207 -4 -352 -407 87
ASP N A 199 -7 -260 -218 31 GLU OE2 A 207 -4 -352 -386 84
ASP CA A 199 -7 -263 -232 31 VAL N A 208 -2 -307 -437 37
ASP C A 199 -6 -250 -238 37 120 VAL CA A 208 -2 -304 -451 37
ASP 0 A 199 -5 -251 -248 37 VAL C A 208 -1 -314 -457 41
ASP CB A 199 -8 -269 -240 33 VAL O A 208 1 -312 -456 41 VAL CB A 208 -1 -289 -454 40 ILE C A 217 -6 -209 -299 38
VAL CGI A 208 -1 -286 -469 40 ILE O A 217 -7 -202 -302 38
VAL CG2 A 208 -2 -280 -446 40 ILE CB A 217 -4 -194 -301 38
GLU N A 209 -1 -325 -463 37 65 ILE CGI A 217 -3 -190 -310 39
GLU CA A 209 -0 -335 -470 36 ILE CG2 A 217 -3 -196 -287 39
GLU C A 209 1 -342 -462 39 ILE CD1 A 217 -1 -200 -312 49
GLU 0 A 209 2 -344 -467 38 ILE N A 218 -6 -219 -290 34
GLU CB A 209 0 -330 -484 38 ILE CA A 218 -7 -221 -282 32
GLU CG A 209 -1 -329 -495 50 70 ILE C A 218 -7 -209 -273 33
GLU CD A 209 -1 -342 -501 81 ILE O A 218 -7 -205 -266 32
GLU 0E1 A 209 -0 -347 -509 82 ILE CB A 218 -7 -235 -275 35
GLU OE2 A 209 -2 -347 -498 79 ILE CGI A 218 -7 -247 -285 34
GLY N A 210 0 -344 -449 35 ILE CG2 A 218 -9 -237 -266 36
GLY CA A 210 1 -350 -439 35 75 ILE CD1 A 218 -7 -260 -279 34
GLY C A 210 2 -341 -430 40 SER N A 219 -9 -203 -274 30
GLY 0 A 210 3 -346 -421 41 SER CA A 219 -9 -191 -266 29
THR N A 211 2 -328 -432 34 SER C A 219 -10 -193 -255 33
THR CA A 211 3 -317 -424 33 SER O A 219 -10 -194 -243 32
THR C A 211 2 -309 -418 34 80 SER CB A 219 -9 -179 -275 31
THR 0 A 211 1 -305 -424 34 SER OG A 219 -9 -167 -267 34
THR CB A 211 3 -309 -434 35 TRP N A 220 -11 -192 -259 33
THR OG1 A 211 4 -318 -442 37 TRP CA A 220 -12 -192 -249 35
THR CG2 A 211 4 -300 -427 29 TRP C A 220 -14 -198 -255 39
SER N A 212 2 -306 -405 30 85 TRP O A 220 -14 -203 -266 38
SER CA A 212 1 -298 -397 28 TRP CB A 220 -13 -177 -245 35
SER C A 212 1 -283 -396 32 TRP CG A 220 -13 -168 -256 37
SER 0 A 212 2 -280 -393 29 TRP CD1 A 220 -12 -162 -266 40
SER CB A 212 0 -304 -383 28 TRP CD2 A 220 -14 -162 -258 37
SER OG A 212 -0 -316 -384 32 90 TRP NE1 A 220 -13 -154 -274 39
PHE N A 213 0 -274 -398 30 TRP CE2 A 220 -14 -154 -269 41
PHE CA A 213 0 -260 -398 29 TRP CE3 A 220 -16 -164 -252 38
PHE C A 213 -1 -254 -387 35 TRP CZ2 A 220 -16 -147 -274 40
PHE 0 A 213 -2 -258 -386 36 TRP CZ3 A 220 -17 -158 -257 40
PHE CB A 213 0 -253 -411 31 95 TRP CH2 A 220 -17 -150 -268 41
PHE CG A 213 1 -255 -421 32 GLY N A 221 -15 -198 -247 36
PHE CD1 A 213 1 -267 -429 34 GLY CA A 221 -16 -202 -250 36
PHE CD2 A 213 2 -245 -423 33 GLY C A 221 -17 -200 -238 42
PHE CE1 A 213 2 -268 -438 35 GLY O A 221 -16 -196 -227 42
PHE CE2 A 213 3 -247 -432 35 100 GLU N A 222 -18 -202 -239 40
PHE CZ A 213 3 -258 -440 33 GLU CA A 222 -19 -200 -229 40
LEU N A 214 -0 -244 -380 32 GLU C A 222 -19 -215 -224 47
LEU CA A 214 -1 -238 -369 31 GLU O A 222 -20 -223 -230 48
LEU C A 214 -2 -228 -376 35 GLU CB A 222 -21 -194 -233 40
LEU 0 A 214 -1 -219 -384 34 105 GLU CG A 222 -20 -179 -235 46
LEU CB A 214 0 -231 -360 31 GLU CD A 222 -22 -173 -243 67
LEU CG A 214 -0 -223 -348 35 GLU OE1 A 222 -22 -176 -255 73
LEU CD1 A 214 -1 -233 -337 35 GLU OE2 A 222 -22 -166 -237 55
LEU CD2 A 214 1 -213 -343 40 GLU N A 223 -19 -218 -212 45
THR N A 215 -3 -229 -373 33 110 GLU CA A 223 -19 -232 -206 45
THR CA A 215 -4 -221 -379 33 GLU C A 223 -18 -242 -215 48
THR C A 215 -5 -213 -368 36 GLU O A 223 -17 -237 -221 48
THR 0 A 215 -5 -203 -370 36 GLU CB A 223 -20 -237 -203 46
THR CB A 215 -5 -229 -388 40 GLU CG A 223 -21 -228 -194 56
THR OG1 A 215 -5 -241 -382 38 115 GLU CD A 223 -23 -232 -190 75
THR CG2 A 215 -4 -232 -402 37 GLU OE1 A 223 -23 -233 -199 73
GLY N A 216 -5 -218 -356 33 GLU OE2 A 223 -23 -235 -178 67
GLY CA A 216 -5 -212 -344 33 CYS N A 224 -18 -254 -216 44
GLY C A 216 -5 -214 -331 37 CYS CA A 224 -18 -264 -225 44
GLY 0 A 216 -4 -224 -330 37 120 CYS C A 224 -19 -274 -231 48
ILE N A 217 -5 -206 -321 34 CYS O A 224 -20 -279 -224 49
ILE CA A 217 -5 -207 -307 35 CYS CB A 224 -17 -272 -217 44 CYS SG A 224 -15 -262 -212 48 TYR CA A 233 -10 -195 -315 30
ALA N A 225 -19 -277 -244 42 TYR C A 233 -9 -182 -321 31
ALA CA A 225 -19 -287 -251 42 TYR 0 A 233 -10 -176 -329 30
ALA C A 225 -21 -285 -251 47 65 TYR CB A 233 -10 -207 -323 31
ALA 0 A 225 -22 -295 -254 47 TYR CG A 233 -10 -220 -317 33
ALA CB A 225 -19 -301 -248 43 TYR CD1 A 233 -12 -223 -319 34
MET N A 226 -21 -273 -247 45 TYR CD2 A 233 -10 -229 -311 34
MET CA A 226 -23 -271 -247 46 TYR CE1 A 233 -12 -235 -314 36
MET C A 226 -23 -270 -260 47 70 TYR CE2 A 233 -10 -241 -305 35
MET 0 A 226 -23 -262 -269 45 TYR CZ A 233 -11 -244 -307 40
MET CB A 226 -23 -258 -238 49 TYR OH A 233 -12 -255 -302 38
MET CG A 226 -23 -259 -224 54 THR N A 234 -8 -178 -316 26
MET SD A 226 -23 -272 -215 59 THR CA A 234 -7 -167 -322 26
MET CE A 226 -23 -270 -198 56 75 THR C A 234 -7 -171 -336 29
LYS N A 227 -25 -276 -262 43 THR 0 A 234 -6 -182 -337 29
LYS CA A 227 -25 -276 -275 43 THR CB A 234 -6 -164 -313 31
LYS C A 227 -26 -261 -278 46 THR OG1 A 234 -7 -163 -299 31
LYS 0 A 227 -26 -254 -269 46 THR CG2 A 234 -6 -151 -317 26
LYS CB A 227 -27 -284 -274 46 80 LYS N A 235 -7 -163 -346 27
LYS CG A 227 -27 -286 -288 63 LYS CA A 235 -7 -165 -360 27
LYS CD A 227 -28 -298 -287 75 LYS C A 235 -5 -162 -361 34
LYS CE A 227 -29 -299 -300 84 LYS 0 A 235 -5 -150 -359 35
LYS NZ A 227 -30 -311 -301 92 LYS CB A 235 -8 -156 -370 29
GLY N A 228 -25 -257 -290 41 85 LYS CG A 235 -9 -163 -376 37
GLY CA A 228 -26 -243 -295 41 LYS CD A 235 -9 -154 -387 46
GLY C A 228 -25 -234 -292 43 LYS CE A 235 -11 -157 -391 51
GLY 0 A 228 -25 -222 -295 43 LYS NZ A 235 -11 -145 -399 56
LYS N A 229 -23 -239 -287 38 VAL N A 236 -5 -172 -362 33
LYS CA A 229 -22 -232 -284 37 90 VAL CA A 236 -3 -172 -363 33
LYS C A 229 -21 -238 -291 38 VAL C A 236 -3 -164 -375 38
LYS 0 A 229 -21 -250 -293 37 VAL 0 A 236 -2 -156 -373 39
LYS CB A 229 -22 -230 -268 39 VAL CB A 236 -2 -186 -362 37
LYS CG A 229 -23 -224 -260 53 VAL CGI A 236 -1 -186 -368 36
LYS CD A 229 -23 -209 -263 59 95 VAL CG2 A 236 -2 -190 -347 36
LYS CE A 229 -24 -203 -255 68 SER N A 237 -3 -165 -387 35
LYS NZ A 229 -24 -188 -256 78 SER CA A 237 -3 -158 -399 35
TYR N A 230 -20 -229 -295 33 SER C A 237 -3 -143 -397 39
TYR CA A 230 -19 -233 -302 32 SER 0 A 237 -2 -138 -403 39
TYR C A 230 -18 -227 -295 35 100 SER CB A 237 -4 -159 -410 36
TYR 0 A 230 -18 -217 -287 36 SER OG A 237 -5 -153 -406 42
TYR CB A 230 -19 -227 -317 32 ARG N A 238 -3 -136 -388 36
TYR CG A 230 -20 -231 -324 31 ARG CA A 238 -3 -122 -385 37
TYR CD1 A 230 -20 -244 -329 34 ARG C A 238 -2 -119 -378 43
TYR CD2 A 230 -21 -222 -326 31 105 ARG O A 238 -1 -108 -379 43
TYR CE1 A 230 -21 -248 -336 35 ARG CB A 238 -4 -117 -378 38
TYR CE2 A 230 -22 -226 -332 31 ARG CG A 238 -4 -104 -369 59
TYR CZ A 230 -23 -239 -337 39 ARG CD A 238 -4 -91 -377 73
TYR OH A 230 -24 -243 -344 40 ARG NE A 238 -5 -79 -368 73
GLY N A 231 -16 -233 -297 28 110 ARG CZ A 238 -4 -72 -361 75
GLY CA A 231 -15 -228 -292 28 ARG NH1 A 238 -2 -75 -362 54
GLY C A 231 -15 -216 -300 34 ARG NH2 A 238 -4 -62 -353 63
GLY 0 A 231 -15 -216 -312 34 TYR N A 239 -1 -129 -370 39
ILE N A 232 -14 -206 -293 30 TYR CA A 239 -0 -127 -362 38
ILE CA A 232 -14 -194 -300 31 115 TYR C A 239 1 -134 -367 43
ILE C A 232 -12 -195 -301 36 TYR O A 239 2 -133 -360 43
ILE 0 A 232 -11 -196 -291 36 TYR CB A 239 -1 -131 -347 39
ILE CB A 232 -14 -180 -294 34 TYR CG A 239 -2 -125 -342 40
ILE CGI A 232 -16 -181 -290 34 TYR CD1 A 239 -2 -112 -337 41
ILE CG2 A 232 -14 -168 -304 34 120 TYR CD2 A 239 -3 -131 -343 40
ILE CD1 A 232 -17 -185 -301 39 TYR CE1 A 239 -3 -106 -333 42
TYR N A 233 -11 -193 -313 31 TYR CE2 A 239 -4 -125 -338 40 TYR CZ A 239 -4 -112 -334 46 LYS CB A 246 9 -118 -318 41
TYR OH A 239 -5 -106 -329 44 LYS CG A 246 8 -105 -319 49
VAL N A 240 1 -141 -379 38 LYS CD A 246 9 -93 -313 55
VAL CA A 240 2 -148 -385 38 65 LYS CE A 246 8 -80 -316 65
VAL C A 240 3 -139 -387 45 LYS NZ A 246 9 -69 -308 73
VAL 0 A 240 4 -144 -384 44 THR N A 247 10 -143 -331 37
VAL CB A 240 2 -154 -398 41 THR CA A 247 11 -157 -329 37
VAL CGI A 240 3 -158 -408 41 THR C A 247 12 -161 -338 43
VAL CG2 A 240 1 -167 -396 41 70 THR 0 A 247 13 -172 -337 44
ASN N A 241 3 -127 -392 44 THR CB A 247 10 -168 -328 42
ASN CA A 241 4 -117 -394 44 THR OG1 A 247 9 -170 -340 38
ASN C A 241 5 -114 -381 47 THR CG2 A 247 9 -164 -318 38
ASN 0 A 241 6 -115 -380 46 LYS N A 248 13 -152 -348 40
ASN CB A 241 4 -105 -402 50 75 LYS CA A 248 14 -155 -357 39
ASN CG A 241 5 -95 -405 94 LYS C A 248 15 -158 -349 45
ASN OD1 A 241 5 -86 -398 93 LYS O A 248 15 -152 -339 45
ASN ND2 A 241 6 -97 -417 91 LYS CB A 248 14 -142 -365 42
TRP N A 242 4 -112 -370 42 LYS CG A 248 14 -143 -380 56
TRP CA A 242 5 -109 -357 42 80 LYS CD A 248 15 -134 -388 67
TRP C A 242 5 -121 -350 43 LYS CE A 248 14 -126 -398 86
TRP 0 A 242 6 -119 -344 43 LYS NZ A 248 13 -114 -392 96
TRP CB A 242 4 -104 -348 40 LEU N A 249 16 -169 -354 42
TRP CG A 242 4 -103 -333 42 LEU CA A 249 17 -173 -347 42
TRP CD1 A 242 4 -92 -327 45 85 LEU C A 249 18 -171 -355 48
TRP CD2 A 242 3 -112 -323 41 LEU O A 249 18 -162 -363 48
TRP NE1 A 242 4 -94 -313 44 LEU CB A 249 17 -188 -343 42
TRP CE2 A 242 4 -106 -311 45 LEU CG A 249 16 -192 -333 46
TRP CE3 A 242 3 -124 -323 42 LEU CD1 A 249 16 -207 -329 45
TRP CZ2 A 242 4 -113 -298 44 90 LEU CD2 A 249 16 -184 -320 49
TRP CZ3 A 242 3 -131 -311 44 MET N B 86 -1 -261 -640 60
TRP CH2 A 242 3 -125 -299 44 MET CA B 86 -1 -249 -649 60
ILE N A 243 5 -133 -352 37 MET C B 86 -1 -236 -640 60
ILE CA A 243 5 -146 -346 35 MET O B 86 -1 -226 -643 60
ILE C A 243 7 -148 -352 40 95 MET CB B 86 -2 -252 -658 63
ILE 0 A 243 8 -150 -345 39 MET CG B 86 -2 -243 -670 69
ILE CB A 243 5 -158 -348 37 MET SD B 86 -3 -249 -683 75
ILE CGI A 243 3 -157 -340 36 MET CE B 86 -4 -234 -694 71
ILE CG2 A 243 5 -171 -345 36 THR N B 87 -2 -237 -630 53
ILE CD1 A 243 2 -164 -346 38 100 THR CA B 87 -2 -225 -622 51
LYS N A 244 7 -146 -365 38 THR C B 87 -3 -229 -607 50
LYS CA A 244 8 -149 -372 39 THR O B 87 -3 -240 -604 51
LYS C A 244 9 -138 -369 44 THR CB B 87 -4 -216 -627 61
LYS 0 A 244 10 -142 -368 43 THR OG1 B 87 -4 -206 -618 63
LYS CB A 244 8 -150 -388 40 105 THR CG2 B 87 -5 -223 -631 61
LYS CG A 244 8 -164 -392 44 CYS N B 88 -2 -221 -598 44
LYS CD A 244 7 -167 -398 50 CYS CA B 88 -2 -223 -583 42
LYS CE A 244 7 -178 -409 60 CYS C B 88 -4 -223 -578 47
LYS NZ A 244 7 -191 -403 64 CYS O B 88 -4 -229 -567 47
GLU N A 245 9 -125 -368 42 110 CYS CB B 88 -2 -212 -576 42
GLU CA A 245 10 -114 -365 43 CYS SG B 88 0 -212 -580 45
GLU C A 245 10 -115 -351 47 ASN N B 89 -5 -217 -585 43
GLU 0 A 245 12 -113 -350 48 ASN CA B 89 -6 -217 -581 42
GLU CB A 245 9 -101 -368 45 ASN C B 89 -7 -230 -584 44
GLU CG A 245 10 -88 -366 63 115 ASN O B 89 -8 -233 -578 44
GLU CD A 245 11 -87 -373 0 ASN CB B 89 -7 -205 -587 42
GLU OE1 A 245 11 -87 -385 0 ASN CG B 89 -6 -200 -601 77
GLU OE2 A 245 12 -86 -366 97 ASN OD1 B 89 -7 -204 -611 79
LYS N A 246 10 -119 -341 41 ASN ND2 B 89 -5 -191 -601 68
LYS CA A 246 10 -120 -327 39 120 ILE N B 90 -6 -239 -592 39
LYS C A 246 11 -132 -324 40 ILE CA B 90 -7 -253 -595 38
LYS 0 A 246 12 -132 -315 38 ILE C B 90 -6 -263 -588 40 ILE 0 B 90 -5 -264 -592 38 PHE N I3 98 3 -249 -509 34
ILE CB B 90 -7 -257 -611 41 PHE CA I 3 98 3 -235 -514 34
ILE CGI B 90 -7 -245 -621 41 PHE C I 3 98 3 -234 -529 41
ILE CG2 B 90 -7 -270 -613 41 65 PHE 0 I 3 98 4 -241 -535 42
ILE CD1 B 90 -8 -238 -618 51 PHE CB I 3 98 4 -225 -507 34
LYS N B 91 -6 -269 -578 37 PHE CG I 3 98 4 -227 -492 35
LYS CA B 91 -6 -279 -569 36 PHE CD1 I 3 98 3 -228 -484 37
LYS C B 91 -4 -275 -565 41 PHE CD2 I 3 98 5 -226 -486 37
LYS 0 B 91 -3 -283 -565 41 70 PHE CE1 I 3 98 3 -230 -470 38
LYS CB B 91 -5 -293 -577 38 PHE CE2 I 3 98 5 -227 -472 39
LYS CG B 91 -7 -300 -579 50 PHE CZ I 3 98 4 -229 -464 36
LYS CD B 91 -7 -313 -586 65 CYS N I 3 99 2 -225 -535 38
LYS CE B 91 -7 -325 -577 83 CYS CA I 3 99 2 -223 -550 38
LYS NZ B 91 -7 -338 -585 90 75 CYS C I 3 99 2 -208 -553 43
ASN N B 92 -4 -262 -560 36 CYS 0 I 3 99 2 -200 -547 42
ASN CA B 92 -3 -256 -555 36 CYS CB I 3 99 1 -229 -556 40
ASN C B 92 -2 -257 -565 40 CYS SG I 3 99 1 -230 -574 44
ASN 0 B 92 -0 -258 -561 42 LYS N I 3 100 3 -205 -564 40
ASN CB B 92 -2 -261 -541 32 80 LYS CA I 3 100 3 -192 -570 39
ASN CG B 92 -1 -254 -534 37 LYS C I 3 100 3 -194 -585 41
ASN 0D1 B 92 -0 -260 -528 23 LYS 0 I 3 100 4 -202 -590 40
ASN ND2 B 92 -1 -241 -533 27 LYS CB I 3 100 4 -184 -565 42
GLY N B 93 -2 -258 -578 35 LYS CG I 3 100 4 -176 -552 68
GLY CA B 93 -1 -261 -589 35 85 LYS CD I 3 100 5 -167 -546 82
GLY C B 93 -0 -274 -587 40 LYS CE I 3 100 4 -160 -534 91
GLY 0 B 93 1 -275 -591 41 LYS NZ I 3 100 6 -152 -527 0
ARG N B 94 -1 -284 -581 37 ASN N I 3 101 2 -186 -592 36
ARG CA B 94 -0 -297 -578 36 ASN CA I 3 101 2 -187 -607 35
ARG C B 94 1 -297 -567 37 90 ASN C I 3 101 3 -183 -615 38
ARG 0 B 94 1 -307 -565 36 ASN 0 I 3 101 4 -179 -610 37
ARG CB B 94 -0 -306 -590 37 ASN CB I 3 101 1 -179 -611 33
ARG CG B 94 -1 -306 -601 51 ASN CG I 3 101 -0 -185 -607 44
ARG CD B 94 -2 -316 -598 69 ASN OD1 I 3 101 -1 -197 -610 29
ARG NE B 94 -4 -312 -605 87 95 ASN ND2 I 3 101 -1 -177 -602 39
ARG CZ B 94 -4 -319 -615 98 VAL N I 3 107 4 -222 -632 32
ARG NH1 B 94 -4 -330 -620 78 VAL CA I 3 107 4 -226 -618 32
ARG NH2 B 94 -5 -314 -620 85 VAL C I 3 107 5 -230 -611 36
CYS N B 95 1 -285 -561 33 VAL O I 3 107 6 -239 -616 37
CYS CA B 95 2 -284 -550 31 100 VAL CB I 3 107 2 -235 -615 35
CYS C B 95 2 -290 -537 36 VAL CGI I 3 107 3 -243 -602 35
CYS 0 B 95 0 -288 -534 34 VAL CG2 I 3 107 1 -226 -614 35
CYS CB B 95 3 -270 -548 30 VAL N I 3 108 5 -224 -599 32
CYS SG B 95 3 -260 -563 34 VAL CA I 3 108 6 -227 -591 31
GLU N B 96 3 -297 -530 32 105 VAL C I 3 108 6 -230 -577 36
GLU CA B 96 2 -303 -517 32 VAL O I 3 108 5 -222 -570 36
GLU C B 96 2 -292 -507 37 VAL CB I 3 108 8 -215 -592 34
GLU 0 B 96 1 -293 -500 38 VAL CGI I 3 108 9 -217 -581 34
GLU CB B 96 4 -311 -512 33 VAL CG2 I 3 108 8 -214 -605 33
GLU CG B 96 3 -319 -500 38 110 CYS N I 3 109 6 -243 -573 33
GLU CD B 96 4 -329 -497 58 CYS CA I 3 109 6 -248 -559 32
GLU OE1 B 96 5 -337 -507 60 CYS C I 3 109 7 -244 -549 37
GLU OE2 B 96 5 -330 -486 55 CYS O I 3 109 8 -242 -553 37
GLN N B 97 3 -281 -507 33 CYS CB I 3 109 6 -263 -560 31
GLN CA B 97 3 -270 -497 32 115 CYS SG I 3 109 5 -268 -571 34
GLN C B 97 2 -257 -504 37 SER N I 3 110 7 -243 -536 33
GLN 0 B 97 1 -254 -504 37 SER CA I 3 110 8 -241 -525 32
GLN CB B 97 4 -268 -488 33 SER C I 3 110 7 -247 -512 39
GLN CG B 97 4 -279 -477 44 SER O I 3 110 6 -251 -511 38
GLN CD B 97 5 -280 -469 49 120 SER CB I 3 110 8 -226 -523 37
GLN OE1 B 97 6 -272 -470 39 SER OG I 3 110 7 -219 -522 59
GLN NE2 B 97 5 -292 -462 43 CYS N I 3 111 8 -249 -503 37 CYS CA I3 111 8 -256 -490 36 GLU N I3 119 13 -335 -566 43
CYS C I 3 111 8 -246 -479 35 GLU CA I 3 119 13 -336 -581 43
CYS 0 I 3 111 9 -236 -481 33 GLU C I 3 119 12 -336 -589 46
CYS CB I 3 111 9 -269 -489 38 65 GLU O I 3 119 12 -332 -601 47
CYS SG I 3 111 9 -280 -503 43 GLU CB I 3 119 14 -348 -583 45
THR N I 3 112 8 -250 -466 28 GLU CG I 3 119 15 -350 -575 65
THR CA I 3 112 8 -242 -454 27 GLU CD I 3 119 15 -357 -562 97
THR C I 3 112 10 -246 -450 33 GLU OE1 I 3 119 15 -370 -562 92
THR 0 I 3 112 10 -254 -456 34 70 GLU OE2 I 3 119 15 -351 -551 90
THR CB I 3 112 7 -245 -444 32 ASN N I 3 120 10 -340 -584 39
THR 0G1 I 3 112 7 -235 -434 27 ASN CA I 3 120 9 -340 -591 38
THR CG2 I 3 112 7 -259 -438 31 ASN C I 3 120 9 -326 -592 41
GLU N I 3 113 10 -239 -439 30 ASN O I 3 120 7 -324 -597 41
GLU CA I 3 113 11 -241 -432 30 75 ASN CB I 3 120 8 -350 -584 36
GLU C I 3 113 12 -256 -429 36 ASN CG I 3 120 8 -347 -570 47
GLU 0 I 3 113 11 -263 -423 37 ASN OD1 I 3 120 8 -335 -565 48
GLU CB I 3 113 12 -232 -420 31 ASN ND2 I 3 120 7 -356 -563 30
GLU CG I 3 113 13 -231 -415 46 GLN N I 3 121 9 -316 -587 36
GLU CD I 3 113 14 -220 -421 82 80 GLN CA I 3 121 9 -302 -586 35
GLU OE1 I 3 113 14 -221 -433 83 GLN C I 3 121 8 -298 -579 40
GLU OE2 I 3 113 14 -210 -413 79 GLN O I 3 121 7 -286 -578 41
GLY N I 3 114 13 -261 -432 33 GLN CB I 3 121 9 -294 -600 36
GLY CA I 3 114 13 -275 -429 33 GLN CG I 3 121 10 -302 -613 60
GLY C I 3 114 13 -285 -440 39 85 GLN CD I 3 121 11 -303 -614 97
GLY 0 I 3 114 13 -297 -438 40 GLN OE1 I 3 121 12 -307 -604 97
TYR N I 3 115 12 -281 -451 35 GLN NE2 I 3 121 12 -299 -625 93
TYR CA I 3 115 12 -289 -462 34 LYS N I 3 122 7 -308 -572 35
TYR C I 3 115 13 -283 -475 39 LYS CA I 3 122 6 -306 -565 35
TYR 0 I 3 115 13 -271 -476 38 90 LYS C I 3 122 6 -309 -550 40
TYR CB I 3 115 10 -289 -464 34 LYS O I 3 122 5 -302 -542 40
TYR CG I 3 115 10 -295 -453 35 LYS CB I 3 122 5 -314 -572 36
TYR CD1 I 3 115 9 -309 -453 37 LYS CG I 3 122 4 -312 -587 35
TYR CD2 I 3 115 9 -288 -441 36 LYS CD I 3 122 4 -300 -590 35
TYR CE1 I 3 115 9 -315 -443 38 95 LYS CE I 3 122 4 -291 -601 39
TYR CE2 I 3 115 9 -294 -431 36 LYS NZ I 3 122 3 -284 -609 42
TYR CZ I 3 115 8 -308 -431 43 SER N I 3 123 6 -321 -547 39
TYR OH I 3 115 8 -313 -421 42 SER CA I 3 123 7 -326 -534 39
ARG N I 3 116 13 -292 -485 36 SER C I 3 123 8 -319 -524 43
ARG CA I 3 116 13 -289 -498 36 100 SER O I 3 123 8 -311 -529 42
ARG C I 3 116 12 -293 -509 42 SER CB I 3 123 7 -341 -534 43
ARG 0 I 3 116 12 -304 -507 41 SER OG I 3 123 6 -348 -541 51
ARG CB I 3 116 15 -294 -501 33 CYS N I 3 124 7 -321 -511 39
ARG CG I 3 116 15 -309 -498 47 CYS CA I 3 124 8 -315 -501 39
ARG CD I 3 116 16 -315 -506 59 105 CYS C I 3 124 9 -327 -493 43
ARG NE I 3 116 16 -329 -502 69 CYS O I 3 124 8 -336 -488 42
ARG CZ I 3 116 17 -333 -492 88 CYS CB I 3 124 7 -306 -491 39
ARG NH1 I 3 116 18 -324 -484 76 CYS SG I 3 124 7 -291 -499 43
ARG NH2 I 3 116 17 -346 -489 81 GLU N I 3 125 10 -326 -493 41
LEU N I 3 117 12 -285 -519 39 110 GLU CA I 3 125 11 -336 -487 42
LEU CA I 3 117 11 -289 -530 39 GLU C I 3 125 12 -330 -475 46
LEU C I 3 117 12 -301 -537 44 GLU O I 3 125 12 -318 -476 47
LEU 0 I 3 117 13 -301 -540 43 GLU CB I 3 125 12 -341 -497 44
LEU CB I 3 117 11 -278 -540 39 GLU CG I 3 125 13 -355 -495 63
LEU CG I 3 117 10 -280 -552 43 115 GLU CD I 3 125 14 -358 -505 97
LEU CD1 I 3 117 9 -282 -547 43 GLU OE1 I 3 125 13 -361 -516 95
LEU CD2 I 3 117 10 -268 -562 43 GLU OE2 I 3 125 15 -358 -501 97
ALA N I 3 118 11 -312 -539 41 PRO N I 3 126 12 -337 -463 42
ALA CA I 3 118 12 -325 -545 40 PRO CA I 3 126 13 -331 -452 41
ALA C I 3 118 12 -324 -561 44 120 PRO C I 3 126 14 -329 -454 45
ALA 0 I 3 118 12 -314 -567 43 PRO O I 3 126 15 -338 -459 46
ALA CB I 3 118 11 -336 -542 40 PRO CB I 3 126 12 -341 -440 43 PRO CG I3 126 11 -349 -445 47 VAL CA B 135 5 -370 -369 35
PRO CD I 3 126 11 -350 -460 43 VAL C B 135 6 -382 -373 42
ALA N I 3 127 15 -317 -452 40 VAL O B 135 6 -387 -384 41
ALA CA I 3 127 16 -313 -454 39 65 VAL CB B 135 3 -374 -367 37
ALA C I 3 127 17 -311 -440 41 VAL CGI B 135 3 -385 -356 37
ALA 0 I 3 127 18 -306 -441 40 VAL CG2 B 135 3 -362 -363 37
ALA CB I 3 127 16 -300 -462 39 SER N B 136 7 -384 -365 41
VAL N I 3 128 16 -314 -429 38 SER CA B 136 8 -394 -368 42
VAL CA I 3 128 17 -312 -415 37 70 SER C B 136 8 -407 -359 49
VAL C I 3 128 16 -325 -407 44 SER O B 136 8 -417 -363 49
VAL 0 I 3 128 15 -332 -411 44 SER CB B 136 9 -388 -367 45
VAL CB I 3 128 16 -299 -408 40 SER OG B 136 9 -378 -358 51
VAL CGI I 3 128 17 -287 -415 39 VAL N B 137 7 -406 -347 49
VAL CG2 I 3 128 15 -298 -406 40 75 VAL CA B 137 7 -417 -338 50
PRO N I 3 129 17 -328 -396 42 VAL C B 137 6 -427 -344 56
PRO CA I 3 129 17 -341 -389 41 VAL O B 137 5 -422 -351 56
PRO C I 3 129 15 -341 -383 44 VAL CB B 137 6 -412 -324 54
PRO 0 I 3 129 15 -352 -383 43 VAL CGI B 137 6 -424 -314 54
PRO CB I 3 129 18 -341 -378 43 80 VAL CG2 B 137 7 -401 -318 54
PRO CG I 3 129 19 -333 -383 48 SER N B 138 6 -440 -343 53
PRO CD I 3 129 18 -322 -391 44 SER CA B 138 5 -450 -348 54
PHE N I 3 130 15 -330 -378 40 SER C B 138 4 -450 -341 58
PHE CA I 3 130 13 -329 -372 39 SER O B 138 4 -446 -329 58
PHE C I 3 130 13 -317 -378 42 85 SER CB B 138 6 -464 -346 57
PHE 0 I 3 130 13 -306 -372 42 SER OG B 138 5 -474 -353 64
PHE CB I 3 130 14 -329 -357 41 GLN N B 139 3 -453 -349 55
PHE CG I 3 130 14 -342 -351 42 GLN CA B 139 1 -452 -343 54
PHE CD1 I 3 130 15 -342 -346 44 GLN C B 139 1 -466 -344 58
PHE CD2 I 3 130 13 -354 -352 43 90 GLN O B 139 1 -476 -345 57
PHE CE1 I 3 130 16 -354 -341 44 GLN CB B 139 1 -441 -351 55
PHE CE2 I 3 130 14 -366 -348 45 GLN CG B 139 1 -427 -352 57
PHE CZ I 3 130 15 -366 -342 43 GLN CD B 139 1 -419 -339 68
PRO N I 3 131 12 -319 -390 36 GLN OE1 B 139 2 -415 -334 61
PRO CA I 3 131 11 -308 -396 35 95 GLN NE2 B 139 0 -416 -335 61
PRO C I 3 131 10 -306 -389 40 NA NA Q 499 5 -376 -183 52
PRO 0 I 3 131 9 -315 -383 42 CHE CI Q 801 -14 -403 -218 54
PRO CB I 3 131 11 -313 -410 36 CHE C2 Q 801 -13 -408 -217 56
PRO CG I 3 131 11 -327 -410 40 CHE C3 Q 801 -12 -399 -209 57
PRO CD I 3 131 12 -331 -399 35 100 CHE C4 Q 801 -13 -393 -197 56
CYS N I 3 132 9 -293 -389 35 CHE N5 Q 801 -11 -404 -210 58
CYS CA I 3 132 8 -289 -383 34 CHE C6 Q 801 -10 -396 -203 59
CYS C I 3 132 7 -298 -388 36 CHE C7 Q 801 -8 -401 -204 60
CYS 0 I 3 132 7 -303 -399 36 CHE S8 Q 801 -7 -396 -189 59
CYS CB I 3 132 8 -274 -385 35 105 CHE 09 Q 801 -8 -401 -176 61
CYS SG I 3 132 8 -269 -402 39 CHE O10 Q 801 -6 -402 -191 60
GLY N I 3 133 6 -298 -380 32 CHE Oil Q 801 -7 -381 -188 60
GLY CA I 3 133 5 -304 -383 32 CHE C12 Q 801 -14 -387 -199 55
GLY C I 3 133 5 -319 -387 36 CHE C13 Q 801 -15 -397 -206 54
GLY 0 I 3 133 4 -325 -391 36 110 SCH C33 S 1 -6 -166 -148 65
ARG N I 3 134 6 -326 -386 35 SCH C22 S 1 -12 -231 -240 35
ARG CA I 3 134 6 -340 -389 35 SCH C23 S 1 -14 -223 -227 34
ARG C I 3 134 6 -349 -377 37 SCH C32 S 1 -5 -171 -143 63
ARG 0 I 3 134 6 -347 -367 36 SCH C31 S 1 -7 -175 -155 64
ARG CB I 3 134 7 -343 -395 39 115 SCH C30 S 1 -11 -225 -231 34
ARG CG I 3 134 8 -342 -411 58 SCH C29 S 1 -13 -217 -218 34
ARG CD I 3 134 7 -352 -418 75 SCH CIO s 1 -5 -193 -152 58
ARG NE I 3 134 6 -348 -432 89 SCH C15 s 1 -13 -230 -239 36
ARG CZ I 3 134 7 -352 -442 0 SCH C8 s 1 -4 -184 -144 59
ARG NH1 I 3 134 8 -362 -441 82 120 SCH C7 s 1 -6 -189 -158 58
ARG NH2 I 3 134 7 -348 -455 87 SCH C20 s 1 -12 -218 -220 35
VAL N I 3 135 5 -360 -379 35 SCH C9 s 1 -2 -177 -136 57 SCH CI S 1 -8 -193 -175 46
SCH C12 S 1 -14 -237 -249 38
SCH C5 S 1 -11 -205 -200 38
SCH C26 S 1 -1 -181 -126 56
SCH C27 S 1 -2 -201 -136 57
SCH C25 S 1 -7 -213 -164 47
SCH C34 S 1 -1 -204 -125 57
SCH C28 S 1 -8 -220 -165 44
SCH C2 S 1 -9 -202 -179 40
SCH C4 S 1 -9 -200 -194 37
SCH N6 S 1 -3 -187 -139 57
SCH N3 S 1 -7 -198 -166 50
SCH N24 S 1 -14 -243 -260 37
SCH Nil S 1 -11 -212 -212 36
SCH N16 S 1 -16 -237 -246 38
SCH 018 S 1 -2 -166 -143 57
SCH 014 s 1 -8 -181 -179 49
SCH 017 s 1 -12 -202 -195 42
SCH 019 s 1 -0 -194 -124 56
SCH 013 s 1 -9 -216 -177 42
SCH 021 s 1 -8 -203 -201 37
HOH 0 w 1 -3 -280 -223 20
HOH 0 w 2 -4 -305 -122 36
HOH 0 w 3 -7 -228 -200 32
EXAMPLE 14: Factor IXa 318R/A-Compound A Complex Crystals Soaked with Compound C.
The factor IXa 318R/A-Compound A complex crystal as described in example 7 was transferred to a 1 microliter hanging drop containing: 2 mM Compound C
Figure imgf000060_0001
), 1 % DMSO, 1.0 M sodium citrate, 0.1 M CHES, pH 9.5 solution. The drop was subsequently incubated at 22° C for 3 days.
EXAMPLE 15: Crystallographic analysis of Soaking experiment; Factor IXa 318R/A-Compound A Complex Crystals with Compound C
Prior to data collection, crystals (from Example 14) were harvested and cryoprotected for 0.5-1 minutes in the crystallization solution containing 20% glycerol, 1.0 M sodium citrate, 0.1 M CHES, pH 9.5. The crystals were then frozen directly into liquid nitrogen. X-ray diffraction was collected at the Cornell High Energy Synchrotron Source on the A1 beam line. This beam line was equipped with an ADSC Quantum 210 CCD detector. Data were integrated and scaled using the HKL package.
Table 7. Data Collection Statistics Example 15.
Figure imgf000060_0002
Example 16: Factor IXa 318R/A-Compound A Complex Crystals Soaked with Compound C.
The crystal structure was solved using Rigid Body refinement with the starting model Factor IXa 318R/A-Compound A. Refinement was done using the program AUTOBUSTER (Global Phasing Limited). Table 8. Crystallization Parameters for Factor IXa 318R/A-Compound A Complex
Crystals Soaked with Compound C.
Figure imgf000061_0001
Table 9. Crystal Structural Coordinates of Factor IXa 318R/A-Compound C
Complex.
The following table contains one line for each atom in one Factor IXa 318R/A monomer. The columns are: 1 ) 3-Letter amino acid code, 2) Atom name, 3) Chain, 4) Residue number, 5) X-coordinate, 6) Y-coordinate, 7) Z-coordinate, 8) B-factor. (Amino Acid Code NA are Sodium, CHE is CHESS buffer, SCH is Compound C (ASCH and BSCH represent double comformation for Compound C with occupancy at 0.5) and HOH for water) Note: B factors greater than 100 appear as 0 in column 8.
VAL N A 16 -10 -309 -231 11 VAL CG2 A 17 -15 -311 -224 14
VAL CA A 16 -11 -314 -243 10 GLY N A 18 -15 -349 -253 18
VAL C A 16 -12 -323 -240 15 GLY CA A 18 -15 -357 -265 17
VAL 0 A 16 -12 -334 -233 12 30 GLY C A 18 -14 -360 -274 19
VAL CB A 16 -10 -320 -254 13 GLY 0 A 18 -14 -363 -286 18
VAL CGI A 16 -11 -326 -266 13 GLY N A 19 -13 -359 -269 16
VAL CG2 A 16 -9 -311 -259 14 GLY CA A 19 -12 -362 -276 16
VAL N A 17 -13 -320 -244 15 GLY C A 19 -11 -376 -274 20
VAL CA A 17 -15 -328 -241 15 35 GLY 0 A 19 -12 -385 -269 20
VAL C A 17 -15 -335 -254 19 GLU N A 20 -10 -380 -279 16
VAL 0 A 17 -15 -329 -265 18 GLU CA A 20 -10 -393 -277 17
VAL CB A 17 -16 -319 -237 16 GLU C A 20 -8 -391 -272 22
VAL CGI A 17 -17 -328 -235 16 GLU 0 A 20 -8 -380 -273 18 GLU CB A 20 -9 -400 -291 19 PRO O A 28 6 -314 -299 17
GLU CG A 20 -11 -404 -298 30 PRO CB A 28 6 -339 -316 14
GLU CD A 20 -11 -407 -313 57 PRO CG A 28 5 -339 -330 19
GLU OE1 A 20 -10 -397 -321 36 65 PRO CD A 28 4 -343 -327 14
GLU OE2 A 20 -11 -418 -317 48 TRP N A 29 4 -309 -311 15
ASP N A 21 -8 -402 -266 18 TRP CA A 29 4 -295 -309 15
ASP CA A 21 -6 -402 -261 18 TRP C A 29 4 -290 -297 17
ASP C A 21 -5 -401 -272 22 TRP O A 29 4 -278 -293 16
ASP 0 A 21 -5 -409 -282 20 70 TRP CB A 29 4 -288 -322 13
ASP CB A 21 -6 -416 -254 20 TRP CG A 29 3 -294 -326 14
ASP CG A 21 -7 -418 -240 24 TRP CD1 A 29 1 -292 -322 16
ASP OD1 A 21 -6 -428 -234 25 TRP CD2 A 29 3 -304 -337 14
ASP OD2 A 21 -7 -409 -236 20 TRP NE1 A 29 0 -300 -329 15
ALA N A 22 -4 -391 -272 17 75 TRP CE2 A 29 1 -307 -338 17
ALA CA A 22 -3 -390 -282 16 TRP CE3 A 29 3 -310 -345 15
ALA C A 22 -2 -402 -280 21 TRP CZ2 A 29 1 -317 -347 16
ALA 0 A 22 -2 -408 -269 18 TRP CZ3 A 29 3 -320 -355 16
ALA CB A 22 -3 -377 -281 17 TRP CH2 A 29 2 -323 -355 16
LYS N A 23 -2 -406 -290 20 80 GLN N A 30 3 -298 -291 12
LYS CA A 23 -1 -416 -287 19 GLN CA A 30 2 -295 -279 12
LYS C A 23 1 -408 -284 22 GLN C A 30 3 -293 -267 15
LYS 0 A 23 1 -397 -289 21 GLN O A 30 4 -301 -264 12
LYS CB A 23 -0 -425 -300 22 GLN CB A 30 1 -306 -276 14
LYS CG A 23 -1 -435 -303 31 85 GLN CG A 30 0 -304 -264 11
LYS CD A 23 -1 -441 -317 41 GLN CD A 30 -1 -294 -266 18
LYS CE A 23 -2 -452 -319 55 GLN OE1 A 30 -2 -296 -275 19
LYS NZ A 23 -2 -458 -333 65 GLN NE2 A 30 -1 -284 -257 12
PRO N A 24 2 -414 -277 19 VAL N A 31 3 -282 -259 12
PRO CA A 24 3 -406 -275 19 90 VAL CA A 31 3 -280 -246 13
PRO C A 24 4 -401 -289 22 VAL C A 31 2 -278 -236 17
PRO 0 A 24 3 -408 -299 22 VAL O A 31 1 -274 -239 16
PRO CB A 24 4 -416 -269 20 VAL CB A 31 5 -270 -245 16
PRO CG A 24 3 -425 -261 24 VAL CGI A 31 6 -272 -256 16
PRO CD A 24 2 -427 -271 19 95 VAL CG2 A 31 4 -256 -246 16
GLY N A 25 4 -389 -289 19 VAL N A 32 3 -281 -223 14
GLY CA A 25 5 -383 -301 18 VAL CA A 32 2 -278 -212 14
GLY C A 25 4 -380 -312 21 VAL C A 32 2 -267 -204 16
GLY 0 A 25 4 -376 -323 21 VAL O A 32 4 -266 -203 16
GLN N A 26 2 -381 -310 16 100 VAL CB A 32 1 -291 -204 17
GLN CA A 26 1 -378 -320 15 VAL CGI A 32 3 -295 -195 16
GLN C A 26 1 -363 -323 17 VAL CG2 A 32 0 -288 -195 16
GLN 0 A 26 1 -358 -334 17 LEU N A 33 2 -258 -198 15
GLN CB A 26 -0 -384 -317 15 LEU CA A 33 2 -247 -190 16
GLN CG A 26 -1 -384 -329 22 105 LEU C A 33 2 -250 -175 18
GLN CD A 26 -2 -390 -325 30 LEU O A 33 0 -252 -173 17
GLN OE1 A 26 -3 -396 -315 22 LEU CB A 33 1 -233 -194 16
GLN NE2 A 26 -3 -387 -334 23 LEU CG A 33 2 -228 -208 20
PHE N A 27 1 -354 -312 14 LEU CD1 A 33 1 -212 -208 19
PHE CA A 27 1 -340 -313 13 110 LEU CD2 A 33 3 -230 -212 19
PHE C A 27 3 -334 -307 17 ASN N A 34 3 -249 -166 15
PHE 0 A 27 3 -329 -296 19 ASN CA A 34 2 -252 -152 16
PHE CB A 27 -0 -334 -306 14 ASN C A 34 3 -239 -143 21
PHE CG A 27 -1 -340 -312 16 ASN O A 34 4 -232 -146 20
PHE CD1 A 27 -2 -351 -307 18 115 ASN CB A 34 3 -264 -147 17
PHE CD2 A 27 -2 -334 -324 19 ASN CG A 34 3 -277 -154 22
PHE CE1 A 27 -3 -357 -314 19 ASN OD1 A 34 2 -280 -157 21
PHE CE2 A 27 -3 -340 -330 21 ASN ND2 A 34 4 -284 -156 17
PHE CZ A 27 -3 -351 -325 19 GLY N A 35 2 -236 -133 22
PRO N A 28 4 -336 -314 14 120 GLY CA A 35 2 -225 -124 23
PRO CA A 28 5 -333 -307 13 GLY C A 35 2 -229 -110 27
PRO C A 28 5 -318 -305 17 GLY O A 35 2 -240 -105 24 LYS N A 36 1 -221 -104 26 ILE CA A 45 7 -251 -300 13
LYS CA A 36 0 -223 -91 27 ILE C A 45 7 -243 -313 16
LYS C A 36 -1 -236 -92 30 ILE 0 A 45 6 -248 -324 15
LYS 0 A 36 -1 -244 -83 32 65 ILE CB A 45 8 -263 -301 16
LYS CB A 36 -1 -211 -86 31 ILE CGI A 45 8 -271 -287 16
LYS CG A 36 0 -198 -84 52 ILE CG2 A 45 9 -260 -305 17
LYS CD A 36 -1 -186 -86 63 ILE CD1 A 45 8 -286 -288 18
LYS CE A 36 -0 -174 -92 69 VAL N A 46 7 -231 -313 15
LYS NZ A 36 -1 -165 -99 80 70 VAL CA A 46 8 -223 -325 15
VAL N A 37 -1 -238 -104 24 VAL C A 46 9 -228 -330 22
VAL CA A 37 -2 -249 -108 24 VAL 0 A 46 9 -230 -342 22
VAL C A 37 -1 -256 -120 26 VAL CB A 46 8 -208 -323 18
VAL 0 A 37 -1 -249 -128 25 VAL CGI A 46 8 -200 -336 17
VAL CB A 37 -4 -244 -112 29 75 VAL CG2 A 46 6 -204 -318 17
VAL CGI A 37 -4 -255 -119 29 ASN N A 47 10 -229 -321 19
VAL CG2 A 37 -4 -238 -100 28 ASN CA A 47 11 -234 -323 18
ASP N A 38 -1 -270 -120 20 ASN C A 47 12 -237 -310 21
ASP CA A 38 -1 -277 -131 20 ASN 0 A 47 11 -237 -300 18
ASP C A 38 -2 -277 -143 21 80 ASN CB A 47 12 -223 -331 18
ASP 0 A 38 -3 -277 -142 19 ASN CG A 47 12 -210 -325 22
ASP CB A 38 -0 -291 -127 22 ASN OD1 A 47 12 -208 -313 17
ASP CG A 38 1 -292 -119 36 ASN ND2 A 47 12 -199 -332 16
ASP 0D1 A 38 2 -283 -121 36 GLU N A 48 13 -240 -310 18
ASP OD2 A 38 1 -302 -111 41 85 GLU CA A 48 14 -244 -297 19
ALA N A 39 -1 -277 -156 17 GLU C A 48 14 -235 -285 21
ALA CA A 39 -2 -278 -168 15 GLU 0 A 48 14 -240 -274 20
ALA C A 39 -3 -268 -169 20 GLU CB A 48 15 -246 -301 21
ALA 0 A 39 -4 -272 -172 21 GLU CG A 48 16 -256 -311 39
ALA CB A 39 -2 -292 -171 15 90 GLU CD A 48 16 -251 -325 54
PHE N A 40 -3 -255 -166 16 GLU OE1 A 48 17 -255 -332 52
PHE CA A 40 -4 -245 -166 16 GLU OE2 A 48 15 -243 -330 35
PHE C A 40 -4 -239 -180 21 LYS N A 49 14 -222 -288 19
PHE 0 A 40 -5 -232 -183 22 LYS CA A 49 14 -212 -277 19
PHE CB A 40 -4 -234 -156 18 95 LYS C A 49 12 -205 -275 20
PHE CG A 40 -2 -225 -160 18 LYS O A 49 12 -197 -265 19
PHE CD1 A 40 -1 -229 -156 19 LYS CB A 49 15 -201 -280 22
PHE CD2 A 40 -3 -213 -167 19 LYS CG A 49 16 -206 -276 34
PHE CE1 A 40 -0 -221 -160 21 LYS CD A 49 16 -203 -261 40
PHE CE2 A 40 -1 -206 -171 21 100 LYS CE A 49 17 -190 -258 46
PHE CZ A 40 -0 -210 -167 19 LYS NZ A 49 17 -187 -243 53
CYS N A 41 -3 -242 -189 19 TRP N A 50 11 -207 -284 16
CYS CA A 41 -3 -237 -203 17 TRP CA A 50 10 -200 -283 17
CYS C A 41 -2 -246 -211 20 TRP C A 50 9 -209 -283 19
CYS 0 A 41 -1 -253 -205 18 105 TRP O A 50 9 -218 -291 18
CYS CB A 41 -3 -222 -204 17 TRP CB A 50 10 -191 -295 16
CYS SG A 41 -4 -211 -202 19 TRP CG A 50 11 -180 -294 17
GLY N A 42 -2 -245 -224 17 TRP CD1 A 50 12 -180 -300 20
GLY CA A 42 -1 -252 -233 16 TRP CD2 A 50 11 -167 -287 17
GLY C A 42 -1 -242 -241 18 110 TRP NE1 A 50 13 -168 -297 20
GLY 0 A 42 -1 -230 -238 16 TRP CE2 A 50 12 -160 -289 21
GLY N A 43 0 -247 -251 14 TRP CE3 A 50 10 -162 -280 17
GLY CA A 43 1 -239 -260 14 TRP CZ2 A 50 12 -147 -284 20
GLY C A 43 2 -248 -271 15 TRP CZ3 A 50 10 -149 -274 19
GLY 0 A 43 1 -260 -271 13 115 TRP CH2 A 50 11 -142 -276 19
SER N A 44 2 -241 -280 12 ILE N A 51 8 -204 -275 15
SER CA A 44 3 -249 -292 12 ILE CA A 51 6 -211 -274 13
SER C A 44 4 -244 -294 16 ILE C A 51 5 -200 -277 17
SER 0 A 44 5 -232 -292 15 ILE O A 51 6 -189 -273 16
SER CB A 44 2 -246 -305 16 120 ILE CB A 51 6 -215 -259 14
SER OG A 44 1 -249 -303 21 ILE CGI A 51 7 -226 -254 13
ILE N A 45 5 -253 -297 13 ILE CG2 A 51 5 -221 -257 15 ILE CD1 A 51 7 -239 -263 12 THR CB A 60 5 -90 -173 64
VAL N A 52 4 -204 -285 14 THR OG1 A 60 5 -92 -187 66
VAL CA A 52 3 -196 -288 13 THR CG2 A 60 6 -85 -171 64
VAL C A 52 2 -201 -280 17 65 GLY N A 61 5 -112 -145 54
VAL 0 A 52 2 -213 -279 16 GLY CA A 61 6 -113 -131 53
VAL CB A 52 3 -194 -303 15 GLY C A 61 5 -127 -125 54
VAL CGI A 52 2 -183 -306 15 GLY 0 A 61 6 -130 -114 54
VAL CG2 A 52 3 -207 -310 15 VAL N A 62 5 -134 -131 46
THR N A 53 1 -192 -273 16 70 VAL CA A 62 4 -148 -126 44
THR CA A 53 0 -195 -264 17 VAL C A 62 5 -159 -133 41
THR C A 53 -1 -184 -265 18 VAL 0 A 62 5 -161 -145 38
THR 0 A 53 -1 -175 -273 18 VAL CB A 62 3 -150 -126 48
THR CB A 53 1 -197 -249 19 VAL CGI A 62 2 -164 -123 48
THR 0G1 A 53 -0 -202 -241 14 75 VAL CG2 A 62 2 -141 -116 48
THR CG2 A 53 1 -184 -243 20 LYS N A 63 6 -167 -125 35
ALA N A 54 -2 -184 -256 14 LYS CA A 63 7 -178 -129 34
ALA CA A 54 -3 -173 -255 15 LYS C A 63 6 -189 -136 35
ALA C A 54 -2 -163 -245 18 LYS 0 A 63 5 -194 -130 35
ALA 0 A 54 -2 -166 -235 17 80 LYS CB A 63 7 -183 -117 37
ALA CB A 54 -4 -179 -251 16 LYS CG A 63 9 -186 -121 63
ALA N A 55 -3 -150 -248 14 LYS CD A 63 10 -195 -111 76
ALA CA A 55 -2 -140 -239 14 LYS CE A 63 9 -210 -113 87
ALA C A 55 -3 -140 -225 17 LYS NZ A 63 10 -214 -126 98
ALA 0 A 55 -2 -137 -215 16 85 ILE N A 64 6 -193 -147 28
ALA CB A 55 -2 -126 -245 15 ILE CA A 64 6 -204 -155 26
HIS N A 56 -4 -144 -224 13 ILE C A 64 7 -214 -159 26
HIS CA A 56 -5 -145 -211 13 ILE 0 A 64 8 -210 -162 23
HIS C A 56 -4 -156 -202 16 ILE CB A 64 5 -198 -168 30
HIS 0 A 56 -4 -155 -190 17 90 ILE CGI A 64 4 -189 -164 31
HIS CB A 56 -6 -147 -214 14 ILE CG2 A 64 4 -208 -179 32
HIS CG A 56 -7 -161 -216 17 ILE CD1 A 64 3 -194 -153 34
HIS ND1 A 56 -7 -166 -228 19 THR N A 65 6 -227 -159 20
HIS CD2 A 56 -7 -171 -207 18 THR CA A 65 7 -238 -163 19
HIS CE1 A 56 -7 -179 -227 18 95 THR C A 65 6 -244 -176 21
HIS NE2 A 56 -7 -182 -214 18 THR 0 A 65 5 -246 -176 21
CYS N A 57 -3 -166 -208 12 THR CB A 65 7 -248 -152 24
CYS CA A 57 -3 -176 -200 14 THR OG1 A 65 8 -243 -140 31
CYS C A 57 -2 -170 -192 20 THR CG2 A 65 8 -261 -156 22
CYS 0 A 57 -1 -175 -182 18 100 VAL N A 66 7 -246 -186 17
CYS CB A 57 -2 -187 -209 15 VAL CA A 66 7 -252 -199 16
CYS SG A 57 -4 -197 -217 20 VAL C A 66 7 -266 -199 19
VAL N A 58 -1 -159 -198 19 VAL O A 66 8 -268 -196 19
VAL CA A 58 0 -154 -192 20 VAL CB A 66 7 -244 -211 20
VAL C A 58 0 -140 -187 32 105 VAL CGI A 66 7 -252 -224 19
VAL 0 A 58 -1 -132 -190 32 VAL CG2 A 66 7 -231 -213 20
VAL CB A 58 1 -158 -201 23 VAL N A 67 6 -276 -202 14
VAL CGI A 58 2 -173 -201 23 VAL CA A 67 7 -290 -204 13
VAL CG2 A 58 1 -153 -215 23 VAL C A 67 7 -295 -218 17
GLU N A 59 1 -136 -177 35 110 VAL O A 67 5 -296 -222 18
GLU CA A 59 1 -123 -171 39 VAL CB A 67 6 -300 -193 17
GLU C A 59 3 -119 -165 50 VAL CGI A 67 7 -313 -194 16
GLU 0 A 59 3 -127 -156 50 VAL CG2 A 67 7 -294 -179 17
GLU CB A 59 -0 -120 -161 40 ALA N A 68 8 -297 -226 14
GLU CG A 59 -0 -128 -148 53 115 ALA CA A 68 8 -303 -239 13
GLU CD A 59 -1 -123 -138 71 ALA C A 68 8 -318 -238 17
GLU OE1 A 59 -1 -110 -136 65 ALA O A 68 8 -322 -229 17
GLU OE2 A 59 -2 -131 -130 67 ALA CB A 68 9 -297 -248 13
THR N A 60 3 -108 -169 52 GLY N A 69 7 -325 -248 15
THR CA A 60 4 -103 -165 53 120 GLY CA A 69 7 -340 -248 14
THR C A 60 5 -102 -150 58 GLY C A 69 7 -347 -237 17
THR 0 A 60 4 -94 -143 58 GLY O A 69 7 -358 -233 16 GLU N A 70 6 -340 -232 14 GLU CA A 77 8 -404 -183 30
GLU CA A 70 5 -345 -222 13 GLU C A 77 10 -400 -188 31
GLU C A 70 4 -354 -228 18 GLU O A 77 10 -392 -181 33
GLU 0 A 70 3 -352 -240 18 65 GLU CB A 77 7 -404 -194 32
GLU CB A 70 4 -333 -214 14 GLU CG A 77 6 -407 -190 43
GLU CG A 70 3 -335 -202 15 GLU CD A 77 5 -402 -198 56
GLU CD A 70 4 -343 -191 19 GLU OE1 A 77 4 -390 -199 26
GLU 0E1 A 70 4 -355 -194 17 GLU OE2 A 77 4 -410 -204 47
GLU OE2 A 70 4 -338 -181 21 70 HIS N A 78 10 -405 -199 23
HIS N A 71 3 -364 -220 15 HIS CA A 78 11 -403 -205 22
HIS CA A 71 2 -372 -225 15 HIS C A 78 12 -390 -214 24
HIS C A 71 1 -374 -214 20 HIS O A 78 13 -384 -214 25
HIS 0 A 71 -0 -370 -216 19 HIS CB A 78 12 -415 -213 23
HIS CB A 71 3 -386 -230 14 75 HIS CG A 78 13 -415 -218 26
HIS CG A 71 2 -395 -235 17 HIS ND1 A 78 14 -422 -212 27
HIS ND1 A 71 1 -393 -247 18 HIS CD2 A 78 14 -410 -230 26
HIS CD2 A 71 1 -407 -230 18 HIS CE1 A 78 15 -421 -219 26
HIS CE1 A 71 0 -403 -248 17 HIS NE2 A 78 15 -414 -230 26
HIS NE2 A 71 0 -412 -238 18 80 THR N A 79 10 -387 -221 18
ASN N A 72 1 -380 -203 17 THR CA A 79 11 -377 -232 17
ASN CA A 72 1 -383 -191 18 THR C A 79 10 -362 -227 20
ASN C A 72 1 -373 -180 24 THR O A 79 11 -353 -235 18
ASN 0 A 72 2 -375 -176 24 THR CB A 79 10 -381 -243 20
ASN CB A 72 1 -398 -186 19 85 THR OG1 A 79 8 -381 -238 17
ASN CG A 72 -0 -401 -175 29 THR CG2 A 79 10 -395 -248 16
ASN OD1 A 72 -0 -394 -165 22 GLU N A 80 10 -360 -215 16
ASN ND2 A 72 -1 -413 -176 26 GLU CA A 80 10 -346 -210 16
ILE N A 73 0 -363 -177 22 GLU C A 80 11 -338 -209 19
ILE CA A 73 1 -353 -167 23 90 GLU O A 80 12 -342 -204 17
ILE C A 73 1 -357 -153 31 GLU CB A 80 9 -346 -196 17
ILE 0 A 73 2 -350 -145 32 GLU CG A 80 8 -353 -195 19
ILE CB A 73 -0 -340 -168 26 GLU CD A 80 8 -367 -190 34
ILE CGI A 73 -2 -342 -165 27 GLU OE1 A 80 8 -375 -196 30
ILE CG2 A 73 0 -332 -181 25 95 GLU OE2 A 80 7 -370 -181 27
ILE CD1 A 73 -2 -329 -160 35 GLN N A 81 11 -325 -214 17
GLU N A 74 1 -369 -149 30 GLN CA A 81 12 -315 -213 17
GLU CA A 74 1 -374 -136 31 GLN C A 81 11 -303 -206 21
GLU C A 74 2 -385 -134 36 GLN O A 81 10 -297 -212 19
GLU 0 A 74 2 -390 -123 36 100 GLN CB A 81 12 -311 -227 18
GLU CB A 74 -1 -378 -129 33 GLN CG A 81 13 -322 -233 23
GLU CG A 74 -1 -392 -133 48 GLN CD A 81 14 -318 -246 20
GLU CD A 74 -2 -398 -122 70 GLN OE1 A 81 14 -307 -248 18
GLU OE1 A 74 -2 -391 -112 72 GLN NE2 A 81 14 -327 -256 18
GLU OE2 A 74 -2 -410 -123 58 105 LYS N A 82 12 -299 -194 19
GLU N A 75 3 -388 -145 34 LYS CA A 82 11 -289 -186 19
GLU CA A 75 4 -397 -144 34 LYS C A 82 12 -276 -188 22
GLU C A 75 5 -392 -151 38 LYS O A 82 13 -277 -188 21
GLU 0 A 75 5 -387 -163 36 LYS CB A 82 11 -293 -171 23
GLU CB A 75 3 -411 -147 36 110 LYS CG A 82 10 -284 -162 49
GLU CG A 75 3 -415 -161 52 LYS CD A 82 10 -289 -148 64
GLU CD A 75 2 -429 -163 83 LYS CE A 82 11 -278 -138 76
GLU OE1 A 75 1 -433 -155 76 LYS NZ A 82 11 -284 -124 84
GLU OE2 A 75 3 -436 -173 83 ARG N A 83 11 -265 -190 19
THR N A 76 6 -392 -144 35 115 ARG CA A 83 12 -252 -192 19
THR CA A 76 7 -387 -150 35 ARG C A 83 11 -240 -184 23
THR C A 76 8 -398 -159 38 ARG O A 83 10 -241 -181 21
THR O A 76 8 -409 -155 38 ARG CB A 83 12 -248 -206 16
THR CB A 76 8 -383 -139 45 ARG CG A 83 13 -257 -215 21
THR OG1 A 76 10 -385 -144 47 120 ARG CD A 83 14 -257 -212 26
THR CG2 A 76 8 -389 -126 43 ARG NE A 83 15 -266 -221 25
GLU N A 77 8 -395 -172 32 ARG CZ A 83 15 -279 -220 39 ARG NH1 A 83 15 -285 -210 25 HIS C A 91 0 -77 -282 25
ARG NH2 A 83 16 -286 -229 31 HIS O A 91 -0 -75 -272 24
ASN N A 84 12 -230 -180 21 HIS CB A 91 -0 -96 -296 21
ASN CA A 84 12 -218 -174 21 65 HIS CG A 91 -0 -89 -309 23
ASN C A 84 11 -207 -184 25 HIS ND1 A 91 -1 -78 -311 24
ASN 0 A 84 12 -206 -194 25 HIS CD2 A 91 0 -91 -320 24
ASN CB A 84 13 -213 -164 26 HIS CE1 A 91 -1 -74 -323 23
ASN CG A 84 13 -223 -153 50 HIS NE2 A 91 0 -81 -329 23
ASN OD1 A 84 12 -226 -144 47 70 HIS N A 92 1 -68 -289 25
ASN ND2 A 84 14 -230 -155 41 HIS CA A 92 1 -53 -285 26
VAL N A 85 10 -199 -182 20 HIS C A 92 -0 -48 -284 27
VAL CA A 85 10 -188 -190 19 HIS O A 92 -1 -39 -277 28
VAL C A 85 11 -176 -185 24 HIS CB A 92 2 -45 -294 27
VAL 0 A 85 11 -173 -173 25 75 HIS CG A 92 2 -48 -308 31
VAL CB A 85 8 -185 -191 22 HIS ND1 A 92 1 -41 -316 33
VAL CGI A 85 8 -173 -200 21 HIS CD2 A 92 3 -57 -316 33
VAL CG2 A 85 8 -198 -197 21 HIS CE1 A 92 1 -46 -328 32
ILE N A 86 12 -170 -193 21 HIS NE2 A 92 2 -56 -329 33
ILE CA A 86 12 -158 -190 20 80 ASN N A 93 -1 -54 -292 23
ILE C A 86 12 -145 -195 25 ASN CA A 93 -3 -50 -291 21
ILE 0 A 86 12 -134 -190 25 ASN C A 93 -4 -57 -280 24
ILE CB A 86 14 -160 -193 22 ASN O A 93 -5 -53 -278 21
ILE CGI A 86 14 -161 -208 23 ASN CB A 93 -3 -52 -305 25
ILE CG2 A 86 14 -172 -185 21 85 ASN CG A 93 -3 -42 -316 47
ILE CD1 A 86 16 -158 -213 32 ASN OD1 A 93 -3 -31 -313 41
ARG N A 87 11 -146 -205 20 ASN ND2 A 93 -3 -47 -328 44
ARG CA A 87 10 -134 -211 19 TYR N A 94 -3 -66 -273 20
ARG C A 87 9 -138 -217 21 TYR CA A 94 -4 -73 -262 19
ARG 0 A 87 9 -149 -223 22 90 TYR C A 94 -4 -64 -250 23
ARG CB A 87 11 -129 -223 15 TYR O A 94 -3 -57 -245 22
ARG CG A 87 11 -115 -229 17 TYR CB A 94 -3 -86 -258 20
ARG CD A 87 12 -110 -238 25 TYR CG A 94 -4 -94 -247 21
ARG NE A 87 13 -112 -233 40 TYR CD1 A 94 -5 -101 -250 21
ARG CZ A 87 14 -103 -226 52 95 TYR CD2 A 94 -3 -93 -234 21
ARG NH1 A 87 13 -91 -224 41 TYR CE1 A 94 -6 -107 -240 20
ARG NH2 A 87 15 -106 -222 38 TYR CE2 A 94 -4 -100 -224 21
ILE N A 88 8 -129 -215 16 TYR CZ A 94 -5 -107 -227 25
ILE CA A 88 7 -131 -219 16 TYR OH A 94 -6 -113 -217 20
ILE C A 88 6 -119 -229 22 100 ASN N A 95 -5 -63 -244 20
ILE 0 A 88 7 -108 -225 21 ASN CA A 95 -5 -55 -232 20
ILE CB A 88 5 -131 -208 20 ASN C A 95 -6 -62 -224 25
ILE CGI A 88 6 -142 -198 20 ASN O A 95 -8 -60 -227 24
ILE CG2 A 88 4 -131 -213 20 ASN CB A 95 -6 -40 -236 20
ILE CD1 A 88 5 -141 -185 23 105 ASN CG A 95 -6 -31 -224 31
ILE N A 89 6 -122 -241 19 ASN OD1 A 95 -6 -36 -212 22
ILE CA A 89 6 -112 -251 17 ASN ND2 A 95 -5 -18 -226 30
ILE C A 89 4 -113 -255 21 ALA N A 96 -6 -69 -214 23
ILE 0 A 89 4 -120 -265 20 ALA CA A 96 -7 -77 -205 23
ILE CB A 89 6 -112 -264 20 110 ALA C A 96 -8 -68 -197 26
ILE CGI A 89 8 -113 -260 19 ALA O A 96 -9 -72 -195 25
ILE CG2 A 89 6 -99 -272 20 ALA CB A 96 -6 -85 -195 24
ILE CD1 A 89 9 -113 -272 24 ALA N A 97 -8 -55 -195 25
PRO N A 90 3 -106 -248 18 ALA CA A 97 -8 -45 -189 25
PRO CA A 90 2 -106 -253 18 115 ALA C A 97 -10 -41 -198 27
PRO C A 90 2 -98 -265 22 ALA O A 97 -11 -36 -193 26
PRO 0 A 90 3 -88 -267 21 ALA CB A 97 -8 -33 -184 25
PRO CB A 90 1 -99 -241 20 ILE N A 98 -9 -43 -211 23
PRO CG A 90 2 -96 -230 24 ILE CA A 98 -10 -40 -221 22
PRO CD A 90 3 -97 -236 20 120 ILE C A 98 -11 -53 -225 24
HIS N A 91 1 -100 -275 20 ILE O A 98 -12 -54 -223 22
HIS CA A 91 1 -92 -287 21 ILE CB A 98 -10 -33 -233 25 ILE CGI A 98 -9 -20 -230 26 ILE O A 105 -1 -127 -276 16
ILE CG2 A 98 -11 -31 -244 26 ILE CB A 105 -2 -145 -300 16
ILE CD1 A 98 -8 -13 -241 35 ILE CGI A 105 -1 -155 -305 16
ASN N A 99 -10 -63 -229 20 65 ILE CG2 A 105 -2 -131 -306 17
ASN CA A 99 -11 -76 -233 20 ILE CD1 A 105 -1 -157 -320 24
ASN C A 99 -10 -87 -231 24 ALA N A 106 0 -148 -273 14
ASN 0 A 99 -9 -88 -238 25 ALA CA A 106 2 -144 -266 14
ASN CB A 99 -12 -75 -248 21 ALA C A 106 3 -154 -269 18
ASN CG A 99 -12 -87 -252 30 70 ALA O A 106 2 -165 -272 15
ASN 0D1 A 99 -12 -98 -248 25 ALA CB A 106 1 -144 -251 14
ASN ND2 A 99 -13 -84 -261 18 LEU N A 107 4 -149 -268 15
LYS N A 100 -10 -96 -222 20 LEU CA A 107 5 -156 -270 16
LYS CA A 100 -9 -107 -218 19 LEU C A 107 6 -158 -257 19
LYS C A 100 -9 -117 -230 21 75 LEU O A 107 6 -148 -250 19
LYS 0 A 100 -8 -123 -230 20 LEU CB A 107 6 -150 -281 16
LYS CB A 100 -10 -116 -207 20 LEU CG A 107 5 -149 -295 19
LYS CG A 100 -9 -126 -199 36 LEU CD1 A 107 6 -140 -304 18
LYS CD A 100 -10 -135 -190 41 LEU CD2 A 107 5 -163 -302 21
LYS CE A 100 -9 -146 -184 39 80 LEU N A 108 6 -170 -255 16
LYS NZ A 100 -10 -158 -181 37 LEU CA A 108 7 -173 -243 16
TYR N A 101 -10 -118 -240 18 LEU C A 108 9 -176 -247 19
TYR CA A 101 -10 -127 -251 18 LEU O A 108 9 -186 -255 19
TYR C A 101 -10 -120 -265 22 LEU CB A 108 7 -185 -235 15
TYR 0 A 101 -10 -128 -275 20 85 LEU CG A 108 5 -185 -233 20
TYR CB A 101 -11 -137 -252 21 LEU CD1 A 108 5 -197 -224 19
TYR CG A 101 -11 -144 -239 22 LEU CD2 A 108 5 -172 -226 21
TYR CD1 A 101 -10 -153 -234 23 GLU N A 109 10 -169 -242 17
TYR CD2 A 101 -12 -142 -231 23 GLU CA A 109 11 -172 -244 16
TYR CE1 A 101 -10 -160 -222 22 90 GLU C A 109 11 -181 -233 20
TYR CE2 A 101 -12 -149 -219 24 GLU O A 109 11 -179 -221 20
TYR CZ A 101 -11 -158 -215 28 GLU CB A 109 12 -159 -245 17
TYR OH A 101 -12 -165 -203 26 GLU CG A 109 13 -162 -250 18
ASN N A 102 -9 -107 -266 19 GLU CD A 109 14 -150 -250 30
ASN CA A 102 -9 -100 -279 19 95 GLU OE1 A 109 14 -138 -247 24
ASN C A 102 -8 -99 -282 23 GLU OE2 A 109 15 -151 -253 23
ASN 0 A 102 -7 -95 -273 23 LEU N A 110 12 -192 -237 17
ASN CB A 102 -10 -86 -280 21 LEU CA A 110 13 -203 -228 15
ASN CG A 102 -10 -82 -295 34 LEU C A 110 14 -199 -223 21
ASN OD1 A 102 -10 -89 -304 24 100 LEU O A 110 15 -193 -230 20
ASN ND2 A 102 -10 -69 -296 25 LEU CB A 110 13 -216 -234 15
HIS N A 103 -7 -103 -294 20 LEU CG A 110 11 -221 -240 18
HIS CA A 103 -6 -104 -298 21 LEU CD1 A 110 11 -235 -246 19
HIS C A 103 -5 -114 -288 21 LEU CD2 A 110 10 -220 -229 20
HIS 0 A 103 -4 -110 -282 20 105 ASP N A 111 14 -204 -210 18
HIS CB A 103 -5 -90 -298 22 ASP CA A 111 16 -201 -205 19
HIS CG A 103 -6 -80 -306 25 ASP C A 111 17 -208 -212 25
HIS ND1 A 103 -6 -80 -320 27 ASP O A 111 18 -202 -214 24
HIS CD2 A 103 -7 -70 -303 27 ASP CB A 111 16 -205 -189 21
HIS CE1 A 103 -6 -70 -325 27 110 ASP CG A 111 16 -219 -186 35
HIS NE2 A 103 -7 -63 -315 27 ASP OD1 A 111 15 -226 -193 36
ASP N A 104 -6 -125 -285 16 ASP OD2 A 111 16 -223 -175 45
ASP CA A 104 -5 -135 -275 14 GLU N A 112 17 -220 -216 23
ASP C A 104 -4 -144 -280 17 GLU CA A 112 18 -229 -224 23
ASP 0 A 104 -4 -156 -282 16 115 GLU C A 112 17 -235 -235 28
ASP CB A 104 -7 -143 -271 15 GLU O A 112 16 -238 -234 26
ASP CG A 104 -6 -150 -257 17 GLU CB A 112 18 -240 -214 26
ASP OD1 A 104 -5 -146 -250 16 GLU CG A 112 20 -242 -214 41
ASP OD2 A 104 -7 -158 -253 18 GLU CD A 112 20 -229 -210 59
ILE N A 105 -3 -138 -280 13 120 GLU OE1 A 112 20 -227 -198 55
ILE CA A 105 -2 -145 -284 13 GLU OE2 A 112 21 -222 -219 63
ILE C A 105 -1 -139 -277 17 PRO N A 113 17 -237 -247 26 PRO CA A 113 17 -243 -258 25 VAL CG2 A 120 10 -328 -268 18
PRO C A 113 16 -257 -256 25 THR N A 121 9 -314 -314 16
PRO 0 A 113 17 -264 -249 25 THR CA A 121 9 -309 -327 16
PRO CB A 113 18 -243 -270 27 65 THR C A 121 8 -296 -329 18
PRO CG A 113 19 -233 -266 32 THR O A 121 7 -296 -324 14
PRO CD A 113 19 -234 -251 28 THR CB A 121 9 -320 -337 23
LEU N A 114 15 -261 -262 19 THR OG1 A 121 9 -332 -335 22
LEU CA A 114 15 -274 -262 17 THR CG2 A 121 9 -316 -352 20
LEU C A 114 16 -282 -271 21 70 PRO N A 122 9 -286 -336 13
LEU 0 A 114 16 -276 -279 19 PRO CA A 122 8 -274 -338 13
LEU CB A 114 13 -275 -267 16 PRO C A 122 7 -276 -347 16
LEU CG A 114 12 -269 -259 20 PRO O A 122 7 -285 -354 16
LEU CD1 A 114 11 -266 -268 19 PRO CB A 122 9 -264 -345 14
LEU CD2 A 114 12 -277 -246 19 75 PRO CG A 122 10 -270 -343 19
VAL N A 115 16 -295 -269 18 PRO CD A 122 10 -285 -343 14
VAL CA A 115 16 -304 -277 17 ILE N A 123 6 -267 -345 13
VAL C A 115 15 -311 -286 19 ILE CA A 123 5 -267 -354 11
VAL 0 A 115 15 -318 -281 17 ILE C A 123 5 -258 -366 16
VAL CB A 115 17 -315 -268 20 80 ILE O A 123 6 -249 -364 15
VAL CGI A 115 18 -326 -277 20 ILE CB A 123 3 -262 -347 13
VAL CG2 A 115 18 -308 -260 20 ILE CGI A 123 2 -263 -356 13
LEU N A 116 15 -307 -299 16 ILE CG2 A 123 3 -247 -342 12
LEU CA A 116 14 -312 -309 16 ILE CD1 A 123 2 -278 -360 14
LEU C A 116 15 -327 -312 19 85 CYS N A 124 5 -261 -379 13
LEU 0 A 116 16 -331 -313 18 CYS CA A 124 5 -252 -390 14
LEU CB A 116 14 -304 -322 16 CYS C A 124 4 -240 -389 18
LEU CG A 116 14 -289 -321 22 CYS O A 124 3 -241 -384 18
LEU CD1 A 116 14 -282 -335 22 CYS CB A 124 5 -259 -403 14
LEU CD2 A 116 13 -286 -313 22 90 CYS SG A 124 6 -274 -405 18
ASN N A 117 13 -334 -312 15 ILE N A 125 5 -229 -395 16
ASN CA A 117 13 -348 -314 15 ILE CA A 125 4 -216 -395 15
ASN C A 117 12 -353 -319 17 ILE C A 125 4 -211 -409 20
ASN 0 A 117 11 -344 -321 17 ILE O A 125 5 -207 -413 16
ASN CB A 117 14 -356 -302 16 95 ILE CB A 125 4 -206 -384 16
ASN CG A 117 13 -355 -289 21 ILE CGI A 125 4 -212 -370 17
ASN OD1 A 117 12 -356 -289 17 ILE CG2 A 125 3 -193 -386 16
ASN ND2 A 117 14 -355 -278 14 ILE CD1 A 125 5 -204 -358 20
SER N A 118 12 -366 -320 15 ALA N A 126 3 -210 -418 17
SER CA A 118 10 -371 -324 15 100 ALA CA A 126 3 -205 -431 17
SER C A 118 9 -367 -315 20 ALA C A 126 3 -190 -430 21
SER 0 A 118 8 -367 -320 19 ALA O A 126 3 -185 -420 20
SER CB A 118 11 -386 -326 19 ALA CB A 126 2 -211 -439 17
SER OG A 118 11 -390 -337 25 ASP N A 127 3 -183 -442 18
TYR N A 119 10 -363 -303 16 105 ASP CA A 127 3 -169 -442 18
TYR CA A 119 8 -360 -293 15 ASP C A 127 1 -165 -440 22
TYR C A 119 8 -345 -290 18 ASP O A 127 0 -174 -438 23
TYR 0 A 119 8 -340 -283 18 ASP CB A 127 3 -163 -456 20
TYR CB A 119 9 -367 -280 17 ASP CG A 127 2 -167 -469 24
TYR CG A 119 9 -382 -281 18 110 ASP OD1 A 127 1 -174 -468 20
TYR CD1 A 119 8 -390 -280 20 ASP OD2 A 127 3 -163 -479 32
TYR CD2 A 119 10 -389 -285 18 LYS N A 128 1 -152 -439 18
TYR CE1 A 119 8 -404 -281 22 LYS CA A 128 -1 -148 -437 19
TYR CE2 A 119 10 -403 -286 19 LYS C A 128 -2 -154 -447 23
TYR CZ A 119 9 -410 -284 28 115 LYS O A 128 -3 -160 -443 23
TYR OH A 119 9 -424 -286 28 LYS CB A 128 -1 -132 -437 22
VAL N A 120 10 -338 -295 16 LYS CG A 128 -2 -126 -434 33
VAL CA A 120 10 -323 -293 15 LYS CD A 128 -2 -111 -436 42
VAL C A 120 10 -317 -306 20 LYS CE A 128 -3 -106 -439 57
VAL 0 A 120 11 -315 -310 19 120 LYS NZ A 128 -3 -93 -445 62
VAL CB A 120 11 -321 -281 19 GLU N A 129 -1 -154 -460 20
VAL CGI A 120 11 -306 -279 18 GLU CA A 129 -2 -159 -471 18 GLU C A 129 -2 -174 -469 19 LYS N A 136 -9 -221 -442 17
GLU 0 A 129 -3 -178 -470 19 LYS CA A 136 -10 -223 -451 16
GLU CB A 129 -1 -155 -484 19 LYS C A 136 -11 -238 -455 20
GLU CG A 129 -2 -161 -496 30 65 LYS O A 136 -12 -242 -460 19
GLU CD A 129 -2 -157 -510 59 LYS CB A 136 -10 -214 -463 19
GLU 0E1 A 129 -2 -155 -519 46 LYS CG A 136 -10 -199 -459 24
GLU OE2 A 129 -0 -155 -512 59 LYS CD A 136 -11 -191 -472 40
TYR N A 130 -1 -182 -468 14 LYS CE A 136 -10 -176 -470 57
TYR CA A 130 -1 -196 -467 13 70 LYS NZ A 136 -11 -169 -461 70
TYR C A 130 -2 -201 -454 19 PHE N A 137 -10 -247 -452 15
TYR 0 A 130 -3 -211 -454 19 PHE CA A 137 -10 -262 -454 14
TYR CB A 130 -0 -204 -471 11 PHE C A 137 -11 -266 -446 17
TYR CG A 130 -0 -208 -485 13 PHE O A 137 -12 -276 -450 15
TYR CD1 A 130 1 -201 -495 15 75 PHE CB A 137 -9 -270 -450 16
TYR CD2 A 130 -1 -219 -489 13 PHE CG A 137 -7 -270 -460 18
TYR CE1 A 130 0 -205 -509 15 PHE CD1 A 137 -7 -261 -470 21
TYR CE2 A 130 -1 -224 -502 13 PHE CD2 A 137 -6 -280 -458 21
TYR CZ A 130 -0 -216 -512 20 PHE CE1 A 137 -6 -261 -478 23
TYR OH A 130 -0 -221 -525 20 80 PHE CE2 A 137 -5 -280 -467 23
THR N A 131 -2 -194 -442 16 PHE CZ A 137 -5 -270 -477 20
THR CA A 131 -2 -197 -429 15 GLY N A 138 -11 -259 -435 15
THR C A 131 -4 -196 -431 18 GLY CA A 138 -13 -261 -427 15
THR 0 A 131 -5 -204 -427 14 GLY C A 138 -12 -272 -416 18
THR CB A 131 -2 -189 -418 16 85 GLY O A 138 -14 -275 -410 17
THR OG1 A 131 -0 -191 -417 15 SER N A 139 -11 -278 -413 15
THR CG2 A 131 -2 -193 -404 18 SER CA A 139 -11 -288 -403 14
ASN N A 132 -4 -185 -438 15 SER C A 139 -10 -288 -397 19
ASN CA A 132 -6 -183 -441 14 SER O A 139 -9 -289 -404 21
ASN C A 132 -6 -194 -450 17 90 SER CB A 139 -11 -302 -410 18
ASN 0 A 132 -7 -198 -447 17 SER OG A 139 -11 -312 -400 34
ASN CB A 132 -6 -169 -446 19 GLY N A 140 -10 -286 -384 15
ASN CG A 132 -7 -164 -447 40 GLY CA A 140 -8 -286 -377 14
ASN OD1 A 132 -8 -167 -438 40 GLY C A 140 -8 -295 -365 17
ASN ND2 A 132 -8 -157 -458 30 95 GLY O A 140 -9 -301 -360 17
ILE N A 133 -6 -198 -460 13 TYR N A 141 -7 -298 -359 15
ILE CA A 133 -6 -208 -470 14 TYR CA A 141 -7 -306 -348 16
ILE C A 133 -6 -222 -462 17 TYR C A 141 -7 -298 -336 19
ILE 0 A 133 -7 -228 -464 17 TYR O A 141 -6 -289 -337 19
ILE CB A 133 -5 -210 -482 18 100 TYR CB A 141 -6 -317 -350 19
ILE CGI A 133 -5 -198 -491 18 TYR CG A 141 -7 -329 -358 26
ILE CG2 A 133 -5 -223 -489 18 TYR CD1 A 141 -7 -328 -372 29
ILE CD1 A 133 -4 -196 -501 22 TYR CD2 A 141 -7 -339 -352 28
PHE N A 134 -5 -225 -453 14 TYR CE1 A 141 -7 -339 -379 32
PHE CA A 134 -5 -237 -445 13 105 TYR CE2 A 141 -8 -350 -359 30
PHE C A 134 -7 -237 -435 17 TYR CZ A 141 -8 -349 -373 41
PHE 0 A 134 -7 -247 -434 17 TYR OH A 141 -8 -360 -380 45
PHE CB A 134 -4 -240 -438 14 VAL N A 142 -7 -299 -325 14
PHE CG A 134 -3 -242 -447 14 VAL CA A 142 -7 -292 -312 14
PHE CD1 A 134 -3 -247 -460 16 110 VAL C A 142 -7 -303 -302 18
PHE CD2 A 134 -2 -240 -443 15 VAL O A 142 -7 -314 -302 18
PHE CE1 A 134 -2 -250 -468 16 VAL CB A 142 -8 -284 -307 17
PHE CE2 A 134 -0 -242 -451 17 VAL CGI A 142 -9 -272 -316 16
PHE CZ A 134 -1 -247 -464 15 VAL CG2 A 142 -10 -292 -305 17
LEU N A 135 -7 -225 -429 14 115 SER N A 143 -6 -299 -293 14
LEU CA A 135 -8 -224 -421 14 SER CA A 143 -5 -308 -283 14
LEU C A 135 -9 -226 -429 20 SER C A 143 -5 -302 -270 17
LEU 0 A 135 -10 -232 -424 20 SER O A 143 -5 -289 -269 17
LEU CB A 135 -8 -210 -414 14 SER CB A 143 -4 -316 -289 16
LEU CG A 135 -9 -209 -404 18 120 SER OG A 143 -3 -307 -295 17
LEU CD1 A 135 -10 -194 -401 18 GLY N A 144 -5 -309 -259 14
LEU CD2 A 135 -9 -217 -392 20 GLY CA A 144 -5 -304 -246 15 GLY C A 144 -5 -312 -234 17 LYS C A 151 -16 -297 -144 24
GLY 0 A 144 -6 -323 -235 16 LYS 0 A 151 -16 -299 -132 23
TRP N A 145 -5 -308 -222 14 LYS CB A 151 -18 -280 -143 24
TRP CA A 145 -5 -315 -210 15 65 LYS CG A 151 -19 -265 -143 40
TRP C A 145 -6 -309 -201 19 LYS CD A 151 -20 -262 -134 53
TRP 0 A 145 -6 -311 -189 19 LYS CE A 151 -20 -248 -129 70
TRP CB A 145 -4 -315 -202 14 LYS NZ A 151 -21 -245 -123 79
TRP CG A 145 -3 -325 -207 16 GLY N A 152 -16 -305 -152 20
TRP CD1 A 145 -2 -338 -204 19 70 GLY CA A 152 -15 -318 -149 19
TRP CD2 A 145 -2 -321 -216 16 GLY C A 152 -14 -317 -146 22
TRP NE1 A 145 -1 -343 -210 18 GLY 0 A 152 -13 -307 -146 21
TRP CE2 A 145 -1 -333 -217 20 ARG N A 153 -13 -329 -144 17
TRP CE3 A 145 -1 -310 -222 17 ARG CA A 153 -12 -330 -141 16
TRP CZ2 A 145 0 -334 -226 19 75 ARG C A 153 -11 -328 -153 19
TRP CZ3 A 145 0 -310 -230 18 ARG 0 A 153 -11 -331 -164 19
TRP CH2 A 145 1 -322 -232 19 ARG CB A 153 -11 -344 -135 17
GLY N A 146 -7 -301 -208 16 SER N A 154 -9 -324 -151 16
GLY CA A 146 -8 -294 -202 14 SER CA A 154 -8 -323 -162 17
GLY C A 146 -9 -303 -197 18 80 SER C A 154 -8 -337 -167 20
GLY 0 A 146 -9 -315 -198 17 SER 0 A 154 -8 -347 -160 18
ARG N A 147 -10 -297 -191 15 SER CB A 154 -7 -317 -156 20
ARG CA A 147 -11 -305 -186 16 SER OG A 154 -7 -304 -152 30
ARG C A 147 -12 -314 -196 19 ALA N A 155 -8 -338 -179 18
ARG 0 A 147 -12 -310 -208 18 85 ALA CA A 155 -7 -350 -185 17
ARG CB A 147 -12 -296 -180 16 ALA C A 155 -6 -354 -179 23
ARG CG A 147 -12 -286 -170 16 ALA 0 A 155 -5 -345 -175 22
ARG CD A 147 -13 -278 -164 22 ALA CB A 155 -7 -349 -200 17
ARG NE A 147 -13 -273 -151 38 LEU N A 156 -6 -367 -179 21
ARG CZ A 147 -13 -263 -145 61 90 LEU CA A 156 -4 -372 -175 22
ARG NH1 A 147 -14 -257 -150 62 LEU C A 156 -3 -374 -187 22
ARG NH2 A 147 -13 -259 -133 47 LEU 0 A 156 -2 -369 -187 21
VAL N A 148 -12 -327 -192 17 LEU CB A 156 -4 -385 -166 23
VAL CA A 148 -13 -337 -201 16 LEU CG A 156 -5 -384 -153 29
VAL C A 148 -14 -337 -201 21 95 LEU CD1 A 156 -5 -398 -146 31
VAL 0 A 148 -15 -344 -210 20 LEU CD2 A 156 -5 -374 -144 34
VAL CB A 148 -12 -351 -198 20 VAL N A 157 -4 -381 -197 19
VAL CGI A 148 -11 -351 -200 19 VAL CA A 157 -3 -384 -210 18
VAL CG2 A 148 -13 -357 -184 20 VAL C A 157 -4 -373 -219 20
PHE N A 149 -15 -329 -193 18 100 VAL 0 A 157 -5 -369 -219 19
PHE CA A 149 -16 -326 -192 18 VAL CB A 157 -4 -398 -215 23
PHE C A 149 -16 -312 -188 21 VAL CGI A 157 -3 -400 -230 22
PHE 0 A 149 -16 -307 -181 21 VAL CG2 A 157 -3 -409 -206 23
PHE CB A 149 -17 -335 -181 20 LEU N A 158 -3 -367 -228 16
PHE CG A 149 -17 -350 -184 21 105 LEU CA A 158 -3 -357 -238 15
PHE CD1 A 149 -16 -359 -175 23 LEU C A 158 -4 -361 -246 17
PHE CD2 A 149 -18 -356 -194 22 LEU 0 A 158 -4 -372 -252 15
PHE CE1 A 149 -16 -373 -177 25 LEU CB A 158 -2 -354 -247 14
PHE CE2 A 149 -18 -370 -196 25 LEU CG A 158 -2 -344 -258 18
PHE CZ A 149 -17 -378 -188 23 110 LEU CD1 A 158 -2 -331 -253 17
HIS N A 150 -18 -305 -191 20 LEU CD2 A 158 -1 -344 -267 20
HIS CA A 150 -18 -291 -187 20 GLN N A 159 -5 -352 -248 14
HIS C A 150 -18 -292 -171 23 GLN CA A 159 -7 -354 -256 14
HIS 0 A 150 -19 -301 -166 23 GLN C A 159 -6 -347 -269 17
HIS CB A 150 -19 -286 -193 22 115 GLN 0 A 159 -6 -336 -270 15
HIS CG A 150 -20 -273 -186 25 GLN CB A 159 -8 -350 -248 15
HIS ND1 A 150 -19 -262 -186 27 GLN CG A 159 -8 -357 -234 14
HIS CD2 A 150 -21 -270 -179 27 GLN CD A 159 -8 -371 -236 21
HIS CE1 A 150 -19 -252 -180 27 GLN OE1 A 159 -7 -380 -233 22
HIS NE2 A 150 -21 -257 -175 27 120 GLN NE2 A 159 -9 -375 -242 11
LYS N A 151 -17 -284 -164 20 TYR N A 160 -7 -352 -279 15
LYS CA A 151 -17 -284 -150 20 TYR CA A 160 -7 -345 -292 15 TYR C A 160 -9 -346 -299 19 ASP O A 167 -21 -191 -383 27
TYR 0 A 160 -9 -356 -297 20 ASP CB A 167 -21 -202 -414 29
TYR CB A 160 -6 -350 -302 17 ASP CG A 167 -22 -202 -408 39
TYR CG A 160 -6 -363 -309 19 65 ASP OD1 A 167 -23 -191 -407 40
TYR CD1 A 160 -7 -363 -322 21 ASP OD2 A 167 -23 -213 -403 49
TYR CD2 A 160 -6 -375 -303 20 ARG N A 168 -20 -177 -397 29
TYR CE1 A 160 -7 -375 -328 22 ARG CA A 168 -20 -165 -390 29
TYR CE2 A 160 -6 -387 -309 21 ARG C A 168 -21 -162 -384 31
TYR CZ A 160 -7 -387 -322 30 70 ARG O A 168 -21 -159 -372 29
TYR OH A 160 -7 -399 -328 31 ARG CB A 168 -19 -153 -399 31
LEU N A 161 -9 -336 -307 14 ARG CG A 168 -19 -141 -392 41
LEU CA A 161 -10 -336 -313 14 ARG CD A 168 -18 -130 -402 44
LEU C A 161 -10 -329 -326 17 ARG NE A 168 -18 -117 -395 54
LEU 0 A 161 -10 -318 -327 17 75 ARG CZ A 168 -19 -109 -391 67
LEU CB A 161 -11 -330 -304 14 ARG NH1 A 168 -20 -111 -393 46
LEU CG A 161 -13 -327 -308 19 ARG NH2 A 168 -19 -97 -385 60
LEU CD1 A 161 -13 -339 -310 20 ALA N A 169 -22 -162 -393 28
LEU CD2 A 161 -13 -317 -299 21 ALA CA A 169 -23 -160 -389 28
ARG N A 162 -11 -334 -337 15 80 ALA C A 169 -24 -169 -378 29
ARG CA A 162 -11 -327 -350 15 ALA O A 169 -25 -164 -368 27
ARG C A 162 -12 -319 -348 19 ALA CB A 169 -24 -161 -401 29
ARG 0 A 162 -13 -324 -344 19 THR N A 170 -24 -182 -378 27
ARG CB A 162 -11 -338 -361 18 THR CA A 170 -24 -192 -368 27
ARG CG A 162 -11 -332 -375 28 85 THR C A 170 -23 -189 -355 30
ARG CD A 162 -12 -341 -385 37 THR O A 170 -24 -189 -344 29
ARG NE A 162 -13 -341 -382 49 THR CB A 170 -24 -206 -374 33
ARG CZ A 162 -14 -332 -386 59 THR OG1 A 170 -25 -207 -386 28
ARG NH1 A 162 -14 -321 -392 45 THR CG2 A 170 -24 -216 -364 31
ARG NH2 A 162 -16 -333 -383 35 90 CYS N A 171 -22 -187 -357 30
VAL N A 163 -12 -306 -351 17 CYS CA A 171 -21 -183 -347 32
VAL CA A 163 -13 -296 -351 17 CYS C A 171 -21 -171 -339 38
VAL C A 163 -13 -290 -364 20 CYS O A 171 -22 -172 -327 38
VAL 0 A 163 -13 -284 -370 18 CYS CB A 171 -20 -180 -355 32
VAL CB A 163 -13 -286 -339 20 95 CYS SG A 171 -18 -172 -346 36
VAL CGI A 163 -13 -293 -325 20 LEU N A 172 -22 -160 -346 37
VAL CG2 A 163 -12 -277 -340 19 LEU CA A 172 -22 -148 -339 38
PRO N A 164 -15 -289 -369 18 LEU C A 172 -24 -150 -331 45
PRO CA A 164 -15 -282 -381 18 LEU O A 172 -24 -146 -320 44
PRO C A 164 -15 -267 -379 20 100 LEU CB A 172 -23 -136 -349 38
PRO 0 A 164 -16 -263 -369 20 LEU CG A 172 -21 -126 -350 43
PRO CB A 164 -16 -289 -387 19 LEU CD1 A 172 -20 -132 -354 43
PRO CG A 164 -17 -293 -375 24 LEU CD2 A 172 -22 -115 -359 46
PRO CD A 164 -16 -295 -364 20 ARG N A 173 -25 -158 -337 44
LEU N A 165 -15 -259 -389 18 105 ARG CA A 173 -26 -161 -331 44
LEU CA A 165 -15 -245 -389 18 ARG C A 173 -26 -168 -318 46
LEU C A 165 -17 -242 -389 23 ARG O A 173 -27 -167 -309 47
LEU 0 A 165 -17 -249 -396 21 ARG CB A 173 -27 -169 -341 48
LEU CB A 165 -14 -240 -402 19 ARG CG A 173 -27 -162 -353 65
LEU CG A 165 -14 -224 -403 24 110 ARG CD A 173 -29 -170 -360 77
LEU CD1 A 165 -13 -219 -392 24 ARG NE A 173 -28 -184 -361 85
LEU CD2 A 165 -14 -221 -417 23 ARG CZ A 173 -28 -191 -371 0
VAL N A 166 -17 -232 -382 20 ARG NH1 A 173 -27 -184 -381 85
VAL CA A 166 -18 -228 -381 21 ARG NH2 A 173 -28 -204 -371 87
VAL C A 166 -19 -215 -388 29 115 SER N A 174 -25 -177 -317 41
VAL 0 A 166 -18 -206 -385 28 SER CA A 174 -25 -185 -305 39
VAL CB A 166 -19 -228 -366 23 SER C A 174 -24 -178 -292 39
VAL CGI A 166 -20 -221 -364 22 SER O A 174 -24 -185 -281 38
VAL CG2 A 166 -19 -243 -361 22 SER CB A 174 -23 -195 -308 40
ASP N A 167 -20 -213 -396 27 120 SER OG A 174 -22 -190 -306 41
ASP CA A 167 -20 -201 -403 27 THR N A 175 -24 -166 -292 34
ASP C A 167 -20 -189 -394 30 THR CA A 175 -23 -158 -281 33 THR C A 175 -24 -144 -280 37 ASN CA A 182 -9 -120 -353 21
THR 0 A 175 -24 -138 -291 38 ASN C A 182 -10 -132 -345 20
THR CB A 175 -22 -160 -280 35 ASN O A 182 -9 -138 -339 19
THR 0G1 A 175 -21 -154 -267 32 65 ASN CB A 182 -8 -110 -346 23
THR CG2 A 175 -21 -154 -292 30 ASN CG A 182 -9 -104 -334 42
LYS N A 176 -24 -138 -268 34 ASN OD1 A 182 -10 -107 -330 38
LYS CA A 176 -24 -124 -266 34 ASN ND2 A 182 -8 -94 -327 34
LYS C A 176 -23 -116 -267 37 MET N A 183 -11 -136 -346 16
LYS 0 A 176 -23 -104 -270 38 70 MET CA A 183 -11 -148 -339 15
LYS CB A 176 -25 -121 -254 36 MET C A 183 -12 -157 -350 18
LYS CG A 176 -24 -126 -241 49 MET O A 183 -13 -151 -359 19
LYS CD A 176 -25 -128 -230 59 MET CB A 183 -12 -145 -328 16
LYS CE A 176 -25 -135 -218 76 MET CG A 183 -12 -136 -317 18
LYS NZ A 176 -26 -137 -207 88 75 MET SD A 183 -13 -131 -306 21
PHE N A 177 -22 -123 -264 32 MET CE A 183 -12 -118 -296 19
PHE CA A 177 -20 -117 -265 31 PHE N A 184 -12 -170 -347 16
PHE C A 177 -20 -114 -279 33 PHE CA A 184 -13 -179 -355 15
PHE 0 A 177 -20 -120 -289 32 PHE C A 184 -14 -189 -346 19
PHE CB A 177 -19 -126 -258 34 80 PHE O A 184 -13 -192 -335 16
PHE CG A 177 -20 -127 -243 37 PHE CB A 184 -12 -186 -367 16
PHE CD1 A 177 -19 -118 -234 41 PHE CG A 184 -11 -196 -363 15
PHE CD2 A 177 -20 -137 -238 40 PHE CD1 A 184 -12 -210 -361 17
PHE CE1 A 177 -19 -120 -220 42 PHE CD2 A 184 -10 -193 -361 16
PHE CE2 A 177 -20 -138 -224 43 85 PHE CE1 A 184 -11 -219 -357 17
PHE CZ A 177 -20 -129 -215 41 PHE CE2 A 184 -9 -203 -358 18
THR N A 178 -19 -105 -281 27 PHE CZ A 184 -9 -216 -356 16
THR CA A 178 -19 -100 -294 26 CYS N A 185 -15 -195 -351 21
THR C A 178 -17 -109 -300 27 CYS CA A 185 -16 -205 -343 24
THR 0 A 178 -16 -112 -294 25 90 CYS C A 185 -15 -218 -349 20
THR CB A 178 -18 -85 -293 34 CYS O A 185 -15 -220 -361 17
THR OG1 A 178 -19 -78 -286 31 CYS CB A 185 -17 -201 -343 28
THR CG2 A 178 -18 -79 -307 28 CYS SG A 185 -17 -186 -334 36
ILE N A 179 -18 -113 -313 23 ALA N A 186 -15 -228 -340 16
ILE CA A 179 -17 -121 -321 23 95 ALA CA A 186 -15 -242 -345 16
ILE C A 179 -16 -112 -331 25 ALA C A 186 -16 -252 -335 20
ILE 0 A 179 -17 -106 -339 26 ALA O A 186 -16 -249 -323 21
ILE CB A 179 -17 -133 -328 26 ALA CB A 186 -14 -246 -347 16
ILE CGI A 179 -18 -142 -318 27 GLY N A 187 -16 -262 -340 17
ILE CG2 A 179 -16 -142 -335 26 100 GLY CA A 187 -17 -272 -332 17
ILE CD1 A 179 -18 -148 -307 32 GLY C A 187 -18 -278 -338 21
TYR N A 180 -15 -110 -330 20 GLY O A 187 -18 -278 -351 18
TYR CA A 180 -14 -101 -339 21 PHE N A 188 -19 -284 -330 19
TYR C A 180 -13 -109 -350 26 PHE CA A 188 -20 -291 -335 20
TYR 0 A 180 -13 -121 -350 25 105 PHE C A 188 -22 -285 -330 27
TYR CB A 180 -13 -92 -331 22 PHE O A 188 -22 -282 -318 26
TYR CG A 180 -14 -81 -323 25 PHE CB A 188 -20 -306 -331 21
TYR CD1 A 180 -13 -80 -309 27 PHE CG A 188 -19 -313 -336 22
TYR CD2 A 180 -15 -72 -328 24 PHE CD1 A 188 -18 -311 -330 24
TYR CE1 A 180 -14 -70 -301 29 110 PHE CD2 A 188 -19 -320 -348 23
TYR CE2 A 180 -15 -62 -321 25 PHE CE1 A 188 -17 -317 -335 24
TYR CZ A 180 -15 -61 -307 33 PHE CE2 A 188 -18 -326 -353 25
TYR OH A 180 -15 -51 -300 31 PHE CZ A 188 -17 -324 -347 23
ASN N A 181 -13 -101 -360 23 HIS N A 189 -23 -284 -338 30
ASN CA A 181 -12 -107 -373 23 115 HIS CA A 189 -24 -279 -336 33
ASN C A 181 -11 -115 -370 25 HIS C A 189 -25 -288 -325 34
ASN 0 A 181 -11 -122 -379 25 HIS O A 189 -25 -282 -316 33
ASN CB A 181 -12 -97 -383 24 HIS CB A 189 -25 -280 -349 37
ASN CG A 181 -13 -94 -393 67 HIS CG A 189 -26 -277 -348 43
ASN OD1 A 181 -13 -94 -405 72 120 HIS ND1 A 189 -27 -288 -349 47
ASN ND2 A 181 -14 -93 -387 58 HIS CD2 A 189 -27 -266 -346 47
ASN N A 182 -10 -113 -358 22 HIS CE1 A 189 -28 -282 -348 47 HIS NE2 A 189 -28 -269 -346 47 GLY O A 198 -5 -262 -207 19
GLU N A 190 -25 -301 -326 30 ASP N A 199 -7 -260 -217 12
GLU CA A 190 -25 -311 -316 30 ASP CA A 199 -7 -262 -231 12
GLU C A 190 -25 -311 -302 32 65 ASP C A 199 -6 -249 -237 16
GLU 0 A 190 -25 -317 -294 30 ASP O A 199 -6 -249 -246 15
GLU CB A 190 -25 -324 -323 31 ASP CB A 199 -8 -267 -240 12
GLU CG A 190 -24 -331 -327 42 ASP CG A 199 -8 -282 -237 15
GLU CD A 190 -23 -328 -341 62 ASP OD1 A 199 -7 -289 -234 15
GLU 0E1 A 190 -23 -317 -345 41 70 ASP OD2 A 199 -9 -285 -238 18
GLU OE2 A 190 -23 -337 -347 59 SER N A 200 -7 -237 -232 15
GLY N A 191 -23 -304 -300 29 SER CA A 200 -6 -224 -238 13
GLY CA A 191 -23 -304 -287 29 SER C A 200 -5 -222 -240 17
GLY C A 191 -22 -317 -286 32 SER O A 200 -4 -227 -232 17
GLY 0 A 191 -22 -324 -295 32 75 SER CB A 200 -7 -213 -230 16
GLY N A 192 -21 -319 -273 27 SER OG A 200 -8 -213 -231 22
GLY CA A 192 -21 -331 -270 26 GLY N A 201 -5 -216 -251 14
GLY C A 192 -19 -331 -273 25 GLY CA A 201 -3 -214 -254 14
GLY 0 A 192 -18 -340 -268 22 GLY C A 201 -3 -225 -263 17
ARG N A 193 -19 -322 -281 20 80 GLY O A 201 -2 -223 -270 16
ARG CA A 193 -17 -321 -286 18 GLY N A 202 -3 -237 -262 15
ARG C A 193 -17 -307 -286 21 GLY CA A 202 -3 -248 -271 13
ARG 0 A 193 -17 -299 -293 22 GLY C A 202 -3 -246 -286 18
ARG CB A 193 -17 -328 -299 18 GLY O A 202 -4 -236 -290 17
ARG CG A 193 -17 -343 -299 22 85 PRO N A 203 -3 -255 -294 14
ARG CD A 193 -17 -349 -313 28 PRO CA A 203 -3 -253 -309 15
ARG NE A 193 -18 -349 -320 25 PRO C A 203 -4 -258 -315 18
ARG CZ A 193 -19 -353 -332 34 PRO O A 203 -5 -268 -310 17
ARG NH1 A 193 -18 -357 -339 25 PRO CB A 203 -2 -261 -315 17
ARG NH2 A 193 -20 -352 -337 25 90 PRO CG A 203 -2 -272 -305 21
ASP N A 194 -16 -304 -278 15 PRO CD A 203 -2 -267 -291 17
ASP CA A 194 -15 -291 -277 14 HIS N A 204 -5 -252 -326 14
ASP C A 194 -14 -290 -270 17 HIS CA A 204 -6 -256 -335 14
ASP 0 A 194 -14 -299 -262 16 HIS C A 204 -5 -258 -348 16
ASP CB A 194 -16 -282 -270 14 95 HIS O A 204 -4 -248 -352 12
ASP CG A 194 -16 -267 -271 21 HIS CB A 204 -7 -245 -338 15
ASP OD1 A 194 -15 -262 -278 22 HIS CG A 204 -8 -248 -349 17
ASP OD2 A 194 -17 -260 -264 20 HIS ND1 A 204 -7 -246 -362 19
SER N A 195 -13 -279 -271 17 HIS CD2 A 204 -9 -252 -349 19
SER CA A 195 -12 -276 -262 16 100 HIS CE1 A 204 -8 -249 -370 18
SER C A 195 -13 -271 -248 18 HIS NE2 A 204 -9 -253 -363 18
SER 0 A 195 -14 -269 -248 17 VAL N A 205 -5 -270 -353 13
SER CB A 195 -11 -265 -268 21 VAL CA A 205 -4 -272 -364 13
SER OG A 195 -12 -254 -272 26 VAL C A 205 -4 -278 -376 17
CYS N A 196 -12 -270 -238 16 105 VAL O A 205 -5 -285 -375 15
CYS CA A 196 -12 -266 -225 17 VAL CB A 205 -2 -281 -361 17
CYS C A 196 -11 -259 -216 19 VAL CGI A 205 -2 -274 -350 15
CYS 0 A 196 -10 -257 -221 17 VAL CG2 A 205 -3 -295 -358 17
CYS CB A 196 -13 -278 -218 18 THR N A 206 -4 -275 -388 14
CYS SG A 196 -14 -275 -205 23 110 THR CA A 206 -4 -280 -401 13
GLN N A 197 -12 -255 -204 17 THR C A 206 -3 -289 -407 17
GLN CA A 197 -11 -248 -195 16 THR O A 206 -2 -284 -409 15
GLN C A 197 -10 -257 -193 20 THR CB A 206 -5 -269 -410 15
GLN 0 A 197 -10 -269 -191 19 THR OG1 A 206 -6 -262 -402 13
GLN CB A 197 -11 -245 -181 16 115 THR CG2 A 206 -5 -273 -423 15
GLN CG A 197 -12 -233 -181 30 GLU N A 207 -4 -302 -410 15
GLN CD A 197 -14 -237 -184 49 GLU CA A 207 -3 -311 -417 17
GLN OE1 A 197 -14 -249 -185 52 GLU C A 207 -3 -308 -432 21
GLN NE2 A 197 -15 -228 -184 41 GLU O A 207 -4 -308 -437 21
GLY N A 198 -8 -251 -194 17 120 GLU CB A 207 -3 -326 -414 19
GLY CA A 198 -7 -258 -193 17 GLU CG A 207 -3 -329 -399 30
GLY C A 198 -7 -261 -206 17 GLU CD A 207 -3 -344 -396 52 GLU 0E1 A 207 -4 -351 -406 52 GLY N A 216 -5 -218 -355 13
GLU OE2 A 207 -3 -348 -384 40 GLY CA A 216 -6 -211 -345 13
VAL N A 208 -2 -306 -438 17 GLY C A 216 -5 -213 -331 17
VAL CA A 208 -1 -303 -452 17 65 GLY O A 216 -4 -222 -329 16
VAL C A 208 -1 -313 -458 21 ILE N A 217 -5 -205 -321 15
VAL 0 A 208 1 -312 -457 20 ILE CA A 217 -5 -207 -307 15
VAL CB A 208 -1 -289 -454 20 ILE C A 217 -6 -209 -300 18
VAL CGI A 208 -1 -286 -469 21 ILE O A 217 -7 -202 -301 15
VAL CG2 A 208 -2 -279 -448 20 70 ILE CB A 217 -4 -194 -301 18
GLU N A 209 -1 -324 -464 21 ILE CGI A 217 -3 -188 -310 17
GLU CA A 209 -0 -335 -470 21 ILE CG2 A 217 -4 -197 -286 20
GLU C A 209 1 -341 -460 27 ILE CD1 A 217 -2 -197 -311 16
GLU 0 A 209 2 -343 -463 27 ILE N A 218 -6 -220 -291 15
GLU CB A 209 0 -331 -483 22 75 ILE CA A 218 -7 -223 -283 13
GLU CG A 209 -1 -327 -494 33 ILE C A 218 -8 -211 -274 16
GLU CD A 209 -1 -340 -500 57 ILE O A 218 -7 -207 -267 14
GLU OE1 A 209 -1 -347 -507 61 ILE CB A 218 -7 -236 -275 15
GLU OE2 A 209 -2 -342 -497 54 ILE CGI A 218 -7 -248 -285 14
GLY N A 210 0 -343 -447 25 80 ILE CG2 A 218 -9 -238 -267 14
GLY CA A 210 1 -349 -437 23 ILE CD1 A 218 -7 -262 -278 16
GLY C A 210 2 -339 -429 23 SER N A 219 -9 -204 -274 14
GLY 0 A 210 3 -344 -421 23 SER CA A 219 -9 -192 -266 13
THR N A 211 2 -326 -431 16 SER C A 219 -10 -193 -256 18
THR CA A 211 3 -316 -424 14 85 SER O A 219 -10 -194 -244 18
THR C A 211 2 -307 -417 17 SER CB A 219 -9 -180 -276 14
THR 0 A 211 1 -301 -424 16 SER OG A 219 -9 -168 -269 19
THR CB A 211 3 -309 -434 18 TRP N A 220 -11 -192 -260 15
THR OG1 A 211 4 -319 -440 16 TRP CA A 220 -13 -192 -251 16
THR CG2 A 211 4 -298 -428 19 90 TRP C A 220 -14 -198 -257 20
SER N A 212 2 -305 -404 15 TRP O A 220 -14 -205 -267 20
SER CA A 212 1 -297 -396 14 TRP CB A 220 -13 -177 -247 16
SER C A 212 1 -283 -395 17 TRP CG A 220 -13 -168 -258 18
SER 0 A 212 2 -280 -393 15 TRP CD1 A 220 -12 -162 -268 21
SER CB A 212 0 -303 -383 17 95 TRP CD2 A 220 -15 -164 -261 18
SER OG A 212 -0 -315 -384 19 TRP NE1 A 220 -13 -154 -276 20
PHE N A 213 0 -274 -398 14 TRP CE2 A 220 -14 -155 -272 22
PHE CA A 213 0 -259 -397 14 TRP CE3 A 220 -16 -166 -254 19
PHE C A 213 -0 -254 -387 18 TRP CZ2 A 220 -16 -149 -277 21
PHE 0 A 213 -2 -258 -385 17 100 TRP CZ3 A 220 -17 -160 -260 20
PHE CB A 213 0 -252 -411 15 TRP CH2 A 220 -17 -152 -271 21
PHE CG A 213 1 -255 -421 15 GLY N A 221 -15 -197 -250 19
PHE CD1 A 213 1 -267 -429 17 GLY CA A 221 -16 -202 -253 19
PHE CD2 A 213 2 -246 -424 14 GLY C A 221 -17 -200 -242 24
PHE CE1 A 213 2 -269 -438 17 105 GLY O A 221 -17 -194 -231 23
PHE CE2 A 213 3 -248 -434 16 GLU N A 222 -18 -205 -243 25
PHE CZ A 213 3 -260 -440 15 GLU CA A 222 -19 -205 -231 26
LEU N A 214 0 -243 -380 13 GLU C A 222 -19 -219 -225 30
LEU CA A 214 -1 -237 -370 12 GLU O A 222 -18 -224 -224 31
LEU C A 214 -2 -228 -376 15 110 GLU CB A 222 -21 -199 -236 27
LEU 0 A 214 -1 -219 -384 14 GLU CG A 222 -21 -183 -235 37
LEU CB A 214 0 -229 -360 12 GLU CD A 222 -22 -175 -242 61
LEU CG A 214 -1 -223 -348 15 GLU OE1 A 222 -22 -179 -254 63
LEU CD1 A 214 -1 -234 -338 15 GLU OE2 A 222 -22 -165 -237 62
LEU CD2 A 214 0 -213 -341 17 115 GLU N A 223 -20 -225 -221 26
THR N A 215 -3 -230 -373 13 GLU CA A 223 -20 -238 -215 26
THR CA A 215 -4 -222 -379 13 GLU C A 223 -20 -249 -225 28
THR C A 215 -5 -214 -368 16 GLU O A 223 -20 -249 -237 28
THR 0 A 215 -6 -204 -371 16 GLU CB A 223 -22 -244 -210 28
THR CB A 215 -5 -230 -388 16 120 GLU CG A 223 -22 -236 -198 41
THR OG1 A 215 -5 -242 -382 13 GLU CD A 223 -23 -226 -201 68
THR CG2 A 215 -4 -232 -402 13 GLU OE1 A 223 -23 -219 -212 52 GLU 0E2 A 223 -24 -225 -193 74 ILE 0 A 232 -12 -197 -290 20
CYS N A 224 -19 -256 -220 20 ILE CB A 232 -14 -182 -294 19
CYS CA A 224 -18 -265 -228 19 ILE CGI A 232 -16 -183 -291 20
CYS C A 224 -19 -276 -234 23 65 ILE CG2 A 232 -14 -169 -304 18
CYS 0 A 224 -19 -283 -226 22 ILE CD1 A 232 -17 -187 -302 21
CYS CB A 224 -17 -272 -219 20 TYR N A 233 -12 -193 -312 14
CYS SG A 224 -16 -261 -213 23 TYR CA A 233 -10 -194 -314 14
ALA N A 225 -19 -278 -247 20 TYR C A 233 -10 -181 -319 17
ALA CA A 225 -19 -288 -255 21 70 TYR 0 A 233 -10 -174 -327 16
ALA C A 225 -21 -288 -253 26 TYR CB A 233 -10 -205 -324 15
ALA 0 A 225 -22 -298 -255 23 TYR CG A 233 -10 -219 -319 15
ALA CB A 225 -19 -302 -252 22 TYR CD1 A 233 -12 -223 -321 17
MET N A 226 -22 -276 -249 24 TYR CD2 A 233 -10 -228 -313 16
MET CA A 226 -23 -276 -248 25 75 TYR CE1 A 233 -12 -235 -316 18
MET C A 226 -24 -273 -262 26 TYR CE2 A 233 -10 -240 -308 16
MET 0 A 226 -23 -265 -270 23 TYR CZ A 233 -11 -244 -309 20
MET CB A 226 -23 -264 -238 28 TYR OH A 233 -12 -256 -304 17
MET CG A 226 -25 -263 -237 34 THR N A 234 -8 -179 -315 15
MET SD A 226 -25 -247 -229 40 80 THR CA A 234 -8 -168 -320 14
MET CE A 226 -25 -252 -212 37 THR C A 234 -7 -172 -335 18
LYS N A 227 -25 -280 -265 25 THR 0 A 234 -7 -182 -336 18
LYS CA A 227 -25 -278 -278 25 THR CB A 234 -6 -164 -312 19
LYS C A 227 -26 -264 -281 28 THR OG1 A 234 -7 -163 -298 18
LYS 0 A 227 -26 -257 -272 28 85 THR CG2 A 234 -6 -152 -317 18
LYS CB A 227 -27 -287 -278 29 LYS N A 235 -7 -163 -344 16
LYS CG A 227 -27 -287 -291 42 LYS CA A 235 -7 -165 -359 16
LYS CD A 227 -29 -298 -292 54 LYS C A 235 -6 -162 -360 20
LYS CE A 227 -29 -297 -304 65 LYS 0 A 235 -5 -150 -360 19
LYS NZ A 227 -30 -308 -305 76 90 LYS CB A 235 -8 -156 -367 18
GLY N A 228 -25 -259 -293 25 LYS CG A 235 -8 -160 -381 23
GLY CA A 228 -26 -245 -297 24 LYS CD A 235 -9 -151 -389 29
GLY C A 228 -24 -236 -293 26 LYS CE A 235 -11 -154 -389 31
GLY 0 A 228 -25 -224 -297 25 LYS NZ A 235 -11 -145 -398 27
LYS N A 229 -23 -240 -286 21 95 VAL N A 236 -5 -173 -362 18
LYS CA A 229 -22 -233 -283 19 VAL CA A 236 -3 -171 -363 18
LYS C A 229 -21 -238 -291 19 VAL C A 236 -3 -163 -375 20
LYS 0 A 229 -21 -250 -295 17 VAL 0 A 236 -2 -156 -374 18
LYS CB A 229 -22 -234 -267 22 VAL CB A 236 -3 -185 -362 21
LYS CG A 229 -23 -229 -258 34 100 VAL CGI A 236 -1 -185 -366 21
LYS CD A 229 -23 -214 -260 39 VAL CG2 A 236 -3 -191 -348 20
LYS CE A 229 -25 -210 -253 46 SER N A 237 -3 -164 -387 18
LYS NZ A 229 -25 -196 -256 53 SER CA A 237 -3 -157 -399 16
TYR N A 230 -20 -230 -293 16 SER C A 237 -3 -142 -397 20
TYR CA A 230 -19 -233 -300 16 105 SER 0 A 237 -2 -137 -402 20
TYR C A 230 -18 -229 -293 19 SER CB A 237 -4 -159 -410 18
TYR 0 A 230 -18 -220 -285 20 SER OG A 237 -5 -152 -406 22
TYR CB A 230 -19 -227 -314 17 ARG N A 238 -4 -135 -388 18
TYR CG A 230 -20 -231 -323 19 ARG CA A 238 -4 -121 -385 19
TYR CD1 A 230 -20 -244 -328 21 110 ARG C A 238 -2 -118 -377 24
TYR CD2 A 230 -21 -223 -324 20 ARG O A 238 -2 -106 -377 24
TYR CE1 A 230 -21 -249 -334 24 ARG CB A 238 -5 -118 -377 22
TYR CE2 A 230 -22 -228 -330 21 ARG CG A 238 -5 -105 -368 38
TYR CZ A 230 -22 -241 -336 31 ARG CD A 238 -5 -92 -375 56
TYR OH A 230 -24 -245 -342 37 115 ARG NE A 238 -5 -81 -365 60
GLY N A 231 -16 -234 -297 14 ARG CZ A 238 -4 -75 -361 71
GLY CA A 231 -15 -229 -292 14 ARG NH1 A 238 -2 -79 -366 52
GLY C A 231 -15 -217 -300 18 ARG NH2 A 238 -4 -65 -353 61
GLY 0 A 231 -15 -217 -312 18 TYR N A 239 -2 -128 -371 17
ILE N A 232 -14 -207 -293 16 120 TYR CA A 239 -0 -126 -363 17
ILE CA A 232 -14 -195 -300 15 TYR C A 239 1 -133 -367 22
ILE C A 232 -12 -195 -300 19 TYR O A 239 2 -131 -360 22 TYR CB A 239 -1 -131 -348 16 GLU OE1 A 245 11 -82 -386 72
TYR CG A 239 -2 -124 -343 16 GLU OE2 A 245 12 -95 -373 84
TYR CD1 A 239 -2 -111 -339 18 LYS N A 246 9 -119 -340 21
TYR CD2 A 239 -3 -131 -342 17 65 LYS CA A 246 10 -120 -326 21
TYR CE1 A 239 -3 -105 -334 18 LYS C A 246 11 -132 -323 22
TYR CE2 A 239 -4 -125 -338 17 LYS 0 A 246 11 -131 -314 22
TYR CZ A 239 -4 -112 -334 24 LYS CB A 246 9 -118 -317 23
TYR OH A 239 -6 -106 -330 23 LYS CG A 246 8 -105 -317 29
VAL N A 240 1 -140 -378 19 70 LYS CD A 246 9 -93 -311 35
VAL CA A 240 2 -147 -384 20 LYS CE A 246 8 -80 -311 48
VAL C A 240 3 -139 -386 22 LYS NZ A 246 9 -70 -303 63
VAL 0 A 240 4 -144 -382 20 THR N A 247 10 -144 -329 17
VAL CB A 240 2 -154 -397 26 THR CA A 247 11 -157 -326 16
VAL CGI A 240 3 -156 -407 27 75 THR C A 247 12 -160 -335 22
VAL CG2 A 240 1 -168 -394 25 THR 0 A 247 13 -171 -333 22
ASN N A 241 3 -127 -391 19 THR CB A 247 10 -168 -327 19
ASN CA A 241 4 -118 -393 20 THR OG1 A 247 9 -169 -340 22
ASN C A 241 5 -114 -380 23 THR CG2 A 247 9 -165 -318 18
ASN 0 A 241 6 -115 -378 21 80 LYS N A 248 12 -152 -346 20
ASN CB A 241 4 -105 -401 23 LYS CA A 248 14 -155 -355 21
ASN CG A 241 4 -108 -415 36 LYS C A 248 15 -157 -347 25
ASN OD1 A 241 4 -118 -421 36 LYS O A 248 15 -150 -339 23
ASN ND2 A 241 3 -99 -422 27 LYS CB A 248 14 -143 -365 23
TRP N A 242 4 -111 -370 21 85 LYS CG A 248 14 -147 -377 34
TRP CA A 242 5 -108 -356 20 LYS CD A 248 15 -135 -387 47
TRP C A 242 5 -120 -349 22 LYS CE A 248 13 -135 -398 68
TRP 0 A 242 6 -118 -343 20 LYS NZ A 248 12 -129 -393 82
TRP CB A 242 3 -103 -348 19 LEU N A 249 16 -169 -350 23
TRP CG A 242 4 -102 -333 20 90 LEU CA A 249 17 -173 -344 25
TRP CD1 A 242 4 -91 -327 22 LEU C A 249 18 -170 -352 31
TRP CD2 A 242 3 -111 -323 20 LEU O A 249 18 -167 -364 31
TRP NE1 A 242 4 -94 -313 22 LEU CB A 249 17 -188 -340 25
TRP CE2 A 242 4 -106 -311 23 LEU CG A 249 16 -192 -330 30
TRP CE3 A 242 3 -124 -324 21 95 LEU CD1 A 249 16 -207 -327 31
TRP CZ2 A 242 3 -113 -299 22 LEU CD2 A 249 16 -185 -316 32
TRP CZ3 A 242 2 -130 -312 22 MET N B 86 -1 -260 -641 49
TRP CH2 A 242 3 -125 -299 22 MET CA B 86 -1 -249 -649 49
ILE N A 243 5 -132 -351 17 MET C B 86 -1 -236 -641 44
ILE CA A 243 5 -144 -345 16 100 MET O B 86 -1 -225 -645 45
ILE C A 243 7 -147 -351 21 MET CB B 86 -2 -252 -658 52
ILE 0 A 243 8 -148 -344 20 MET CG B 86 -3 -243 -669 58
ILE CB A 243 4 -157 -348 18 MET SD B 86 -4 -244 -676 65
ILE CGI A 243 3 -156 -341 18 MET CE B 86 -4 -229 -687 62
ILE CG2 A 243 5 -170 -344 19 105 THR N B 87 -2 -237 -630 35
ILE CD1 A 243 2 -167 -345 20 THR CA B 87 -2 -225 -621 31
LYS N A 244 7 -147 -365 18 THR C B 87 -2 -229 -606 27
LYS CA A 244 8 -149 -372 19 THR O B 87 -3 -240 -603 23
LYS C A 244 9 -139 -369 24 THR CB B 87 -4 -217 -627 47
LYS 0 A 244 10 -142 -367 24 110 THR OG1 B 87 -4 -206 -618 49
LYS CB A 244 8 -149 -387 22 THR CG2 B 87 -5 -225 -629 48
LYS CG A 244 8 -162 -395 39 CYS N B 88 -2 -219 -597 22
LYS CD A 244 7 -169 -395 46 CYS CA B 88 -2 -221 -583 21
LYS CE A 244 7 -181 -405 49 CYS C B 88 -4 -223 -578 25
LYS NZ A 244 7 -193 -400 52 115 CYS O B 88 -4 -228 -567 23
GLU N A 245 9 -126 -367 23 CYS CB B 88 -1 -211 -575 20
GLU CA A 245 10 -115 -364 25 CYS SG B 88 0 -211 -578 22
GLU C A 245 10 -116 -350 27 ASN N B 89 -5 -217 -586 22
GLU 0 A 245 11 -115 -349 27 ASN CA B 89 -6 -218 -582 22
GLU CB A 245 9 -102 -366 27 120 ASN C B 89 -7 -232 -584 24
GLU CG A 245 10 -89 -365 46 ASN O B 89 -8 -235 -578 21
GLU CD A 245 11 -88 -375 80 ASN CB B 89 -7 -207 -588 30 ASN CG B 89 -6 -202 -602 72 GLN 0 I3 97 1 -253 -504 15
ASN 0D1 B 89 -7 -205 -612 69 GLN CB I 3 97 4 -268 -487 15
ASN ND2 B 89 -6 -192 -602 69 GLN CG I 3 97 4 -280 -478 19
ILE N B 90 -6 -241 -592 21 65 GLN CD I 3 97 5 -280 -469 19
ILE CA B 90 -6 -254 -594 22 GLN OE1 I 3 97 6 -270 -468 16
ILE C B 90 -6 -264 -587 23 GLN NE2 I 3 97 5 -290 -462 15
ILE 0 B 90 -4 -266 -591 21 PHE N I 3 98 3 -248 -508 12
ILE CB B 90 -7 -259 -609 26 PHE CA I 3 98 3 -235 -514 12
ILE CGI B 90 -7 -248 -619 27 70 PHE C I 3 98 3 -234 -529 16
ILE CG2 B 90 -7 -271 -610 27 PHE O I 3 98 4 -241 -535 15
ILE CD1 B 90 -8 -238 -615 40 PHE CB I 3 98 4 -224 -507 13
LYS N B 91 -6 -271 -576 19 PHE CG I 3 98 4 -225 -492 16
LYS CA B 91 -5 -281 -569 19 PHE CD1 I 3 98 3 -227 -484 18
LYS C B 91 -4 -276 -564 19 75 PHE CD2 I 3 98 5 -225 -486 18
LYS 0 B 91 -3 -284 -563 16 PHE CE1 I 3 98 3 -228 -470 18
LYS CB B 91 -5 -294 -576 22 PHE CE2 I 3 98 5 -226 -472 20
LYS CG B 91 -7 -300 -581 34 PHE CZ I 3 98 4 -227 -464 17
LYS CD B 91 -6 -314 -588 47 CYS N I 3 99 2 -225 -535 15
LYS CE B 91 -6 -326 -579 66 80 CYS CA I 3 99 2 -223 -550 16
LYS NZ B 91 -6 -339 -586 80 CYS C I 3 99 2 -208 -553 21
ASN N B 92 -4 -263 -560 15 CYS O I 3 99 2 -200 -547 19
ASN CA B 92 -3 -257 -555 15 CYS CB I 3 99 1 -230 -555 17
ASN C B 92 -2 -258 -565 17 CYS SG I 3 99 1 -230 -573 21
ASN 0 B 92 -0 -259 -561 16 85 LYS N I 3 100 3 -205 -564 22
ASN CB B 92 -2 -262 -541 18 LYS CA I 3 100 3 -192 -570 22
ASN CG B 92 -1 -254 -533 25 LYS C I 3 100 3 -193 -585 24
ASN OD1 B 92 -2 -242 -532 17 LYS O I 3 100 4 -202 -591 21
ASN ND2 B 92 -0 -261 -528 11 LYS CB I 3 100 4 -184 -566 26
GLY N B 93 -2 -259 -578 14 90 LYS CG I 3 100 4 -173 -557 52
GLY CA B 93 -1 -261 -588 15 LYS CD I 3 100 5 -163 -557 64
GLY C B 93 -0 -274 -587 20 LYS CE I 3 100 5 -153 -545 74
GLY 0 B 93 1 -276 -592 20 LYS NZ I 3 100 6 -143 -545 83
ARG N B 94 -1 -284 -580 17 ASN N I 3 101 2 -185 -592 21
ARG CA B 94 -0 -297 -576 18 95 ASN CA I 3 101 2 -186 -606 20
ARG C B 94 1 -296 -566 20 ASN C I 3 101 3 -181 -613 23
ARG 0 B 94 2 -307 -563 20 ASN O I 3 101 4 -172 -608 23
ARG CB B 94 0 -307 -589 22 ASN CB I 3 101 1 -178 -610 19
ARG CG B 94 -1 -307 -600 39 ASN CG I 3 101 -0 -185 -606 30
ARG CD B 94 -2 -313 -596 61 100 ASN OD1 I 3 101 -1 -197 -608 24
ARG NE B 94 -3 -306 -603 79 ASN ND2 I 3 101 -1 -178 -601 26
ARG CZ B 94 -4 -310 -614 97 VAL N I 3 107 4 -227 -630 22
ARG NH1 B 94 -3 -321 -621 83 VAL CA I 3 107 4 -226 -615 20
ARG NH2 B 94 -5 -303 -619 84 VAL C I 3 107 5 -230 -609 21
CYS N B 95 1 -284 -561 15 105 VAL O I 3 107 6 -238 -614 18
CYS CA B 95 2 -282 -551 14 VAL CB I 3 107 3 -236 -612 24
CYS C B 95 2 -288 -538 18 VAL CGI I 3 107 3 -246 -601 22
CYS 0 B 95 1 -286 -534 18 VAL CG2 I 3 107 1 -228 -610 23
CYS CB B 95 3 -267 -549 13 VAL N I 3 108 5 -223 -597 17
CYS SG B 95 3 -259 -564 17 110 VAL CA I 3 108 7 -226 -589 16
GLU N B 96 3 -295 -531 15 VAL C I 3 108 6 -230 -575 19
GLU CA B 96 2 -302 -518 15 VAL O I 3 108 6 -221 -569 18
GLU C B 96 2 -291 -507 17 VAL CB I 3 108 8 -214 -588 20
GLU 0 B 96 1 -293 -499 17 VAL CGI I 3 108 9 -216 -578 19
GLU CB B 96 4 -310 -513 16 115 VAL CG2 I 3 108 8 -210 -602 19
GLU CG B 96 3 -319 -501 21 CYS N I 3 109 7 -242 -571 15
GLU CD B 96 4 -328 -496 28 CYS CA I 3 109 6 -247 -558 15
GLU OE1 B 96 5 -333 -504 25 CYS C I 3 109 7 -243 -548 18
GLU OE2 B 96 4 -330 -484 26 CYS O I 3 109 8 -239 -552 17
GLN N B 97 3 -280 -507 14 120 CYS CB I 3 109 6 -262 -558 15
GLN CA B 97 3 -270 -497 13 CYS SG I 3 109 5 -268 -570 18
GLN C B 97 2 -256 -503 17 SER N I 3 110 7 -243 -535 13 SER CA I3 110 8 -239 -524 13 LEU CD2 I3 117 10 -266 -560 18
SER C I 3 110 7 -247 -512 17 ALA N I 3 118 11 -311 -538 18
SER 0 I 3 110 6 -253 -511 15 ALA CA I 3 118 12 -323 -543 18
SER CB I 3 110 8 -224 -521 16 65 ALA C I 3 118 12 -322 -559 20
SER OG I 3 110 9 -221 -514 24 ALA O I 3 118 12 -313 -565 18
CYS N I 3 111 8 -248 -502 16 ALA CB I 3 118 11 -335 -540 18
CYS CA I 3 111 8 -255 -490 16 GLU N I 3 119 13 -332 -564 21
CYS C I 3 111 8 -246 -478 19 GLU CA I 3 119 13 -334 -578 22
CYS 0 I 3 111 9 -236 -479 17 70 GLU C I 3 119 12 -334 -587 25
CYS CB I 3 111 9 -268 -489 17 GLU O I 3 119 12 -328 -598 25
CYS SG I 3 111 9 -279 -504 22 GLU CB I 3 119 14 -346 -581 24
THR N I 3 112 8 -250 -466 15 GLU CG I 3 119 15 -347 -573 47
THR CA I 3 112 8 -242 -454 15 GLU CD I 3 119 15 -355 -560 80
THR C I 3 112 10 -245 -449 20 75 GLU OE1 I 3 119 16 -367 -559 74
THR 0 I 3 112 10 -253 -454 19 GLU OE2 I 3 119 15 -349 -550 75
THR CB I 3 112 7 -245 -443 20 ASN N I 3 120 11 -339 -582 20
THR OG1 I 3 112 7 -235 -433 16 ASN CA I 3 120 9 -339 -590 20
THR CG2 I 3 112 7 -259 -437 22 ASN C I 3 120 9 -325 -591 21
GLU N I 3 113 10 -237 -439 19 80 ASN O I 3 120 8 -324 -597 21
GLU CA I 3 113 11 -238 -433 20 ASN CB I 3 120 8 -349 -584 21
GLU C I 3 113 12 -253 -429 24 ASN CG I 3 120 8 -346 -571 25
GLU 0 I 3 113 11 -259 -423 24 ASN OD1 I 3 120 8 -335 -565 17
GLU CB I 3 113 11 -229 -421 22 ASN ND2 I 3 120 7 -355 -565 21
GLU CG I 3 113 13 -231 -412 40 85 GLN N I 3 121 9 -315 -586 17
GLU CD I 3 113 14 -222 -415 72 GLN CA I 3 121 9 -300 -586 17
GLU OE1 I 3 113 15 -226 -422 75 GLN C I 3 121 8 -297 -578 19
GLU OE2 I 3 113 14 -210 -410 66 GLN O I 3 121 7 -286 -578 19
GLY N I 3 114 13 -258 -432 20 GLN CB I 3 121 9 -294 -600 18
GLY CA I 3 114 13 -272 -429 19 90 GLN CG I 3 121 10 -302 -612 41
GLY C I 3 114 13 -282 -439 23 GLN CD I 3 121 11 -299 -617 74
GLY 0 I 3 114 13 -294 -437 24 GLN OE1 I 3 121 11 -290 -626 71
TYR N I 3 115 12 -279 -450 19 GLN NE2 I 3 121 12 -306 -613 76
TYR CA I 3 115 12 -288 -461 17 LYS N I 3 122 7 -307 -571 17
TYR C I 3 115 13 -283 -474 22 95 LYS CA I 3 122 6 -305 -564 16
TYR 0 I 3 115 13 -271 -475 21 LYS C I 3 122 6 -308 -549 20
TYR CB I 3 115 10 -288 -464 17 LYS O I 3 122 5 -301 -541 19
TYR CG I 3 115 10 -295 -453 17 LYS CB I 3 122 5 -314 -571 19
TYR CD1 I 3 115 9 -308 -453 20 LYS CG I 3 122 5 -311 -586 27
TYR CD2 I 3 115 9 -288 -441 17 100 LYS CD I 3 122 4 -297 -588 31
TYR CE1 I 3 115 9 -315 -443 22 LYS CE I 3 122 4 -292 -602 39
TYR CE2 I 3 115 9 -294 -431 18 LYS NZ I 3 122 3 -299 -611 56
TYR CZ I 3 115 8 -307 -432 22 SER N I 3 123 7 -319 -545 18
TYR OH I 3 115 8 -313 -421 19 SER CA I 3 123 7 -324 -532 18
ARG N I 3 116 13 -292 -484 20 105 SER C I 3 123 8 -317 -522 21
ARG CA I 3 116 13 -288 -497 20 SER O I 3 123 9 -311 -527 20
ARG C I 3 116 12 -293 -508 23 SER CB I 3 123 7 -339 -531 21
ARG 0 I 3 116 12 -303 -507 22 SER OG I 3 123 6 -346 -539 28
ARG CB I 3 116 15 -294 -499 21 CYS N I 3 124 8 -319 -509 18
ARG CG I 3 116 15 -309 -501 31 110 CYS CA I 3 124 8 -313 -499 18
ARG CD I 3 116 16 -313 -507 37 CYS C I 3 124 9 -324 -491 24
ARG NE I 3 116 16 -328 -506 39 CYS O I 3 124 8 -332 -485 24
ARG CZ I 3 116 17 -335 -496 61 CYS CB I 3 124 8 -303 -490 18
ARG NH1 I 3 116 17 -329 -485 49 CYS SG I 3 124 7 -289 -499 22
ARG NH2 I 3 116 17 -348 -496 52 115 GLU N I 3 125 10 -324 -491 21
LEU N I 3 117 12 -284 -518 18 GLU CA I 3 125 11 -334 -484 21
LEU CA I 3 117 11 -288 -530 17 GLU C I 3 125 12 -328 -472 23
LEU C I 3 117 12 -300 -536 21 GLU O I 3 125 12 -317 -473 22
LEU 0 I 3 117 13 -299 -539 20 GLU CB I 3 125 12 -339 -494 23
LEU CB I 3 117 11 -276 -539 16 120 GLU CG I 3 125 12 -347 -506 38
LEU CG I 3 117 10 -277 -551 18 GLU CD I 3 125 13 -353 -514 70
LEU CD1 I 3 117 9 -279 -546 17 GLU OE1 I 3 125 13 -359 -525 72 GLU OE2 I3 125 14 -352 -510 71 ARG CD B 134 6 -346 -421 53
PRO N I 3 126 12 -335 -461 20 ARG NE B 134 6 -340 -434 59
PRO CA I 3 126 13 -330 -449 20 ARG CZ B 134 7 -345 -444 77
PRO C I 3 126 14 -327 -453 24 65 ARG NH1 B 134 8 -356 -443 62
PRO O I 3 126 15 -335 -459 25 ARG NH2 B 134 7 -339 -456 61
PRO CB I 3 126 13 -342 -439 22 VAL N B 135 5 -359 -379 19
PRO CG I 3 126 11 -350 -443 26 VAL CA B 135 5 -370 -369 19
PRO CD I 3 126 11 -349 -458 22 VAL C B 135 6 -380 -373 25
ALA N I 3 127 15 -315 -449 20 70 VAL O B 135 6 -386 -383 24
ALA CA I 3 127 16 -311 -451 20 VAL CB B 135 3 -375 -367 23
ALA C I 3 127 17 -309 -438 24 VAL CGI B 135 3 -386 -357 23
ALA O I 3 127 18 -305 -438 23 VAL CG2 B 135 2 -363 -364 23
ALA CB I 3 127 16 -298 -460 22 SER N B 136 7 -382 -364 22
VAL N I 3 128 16 -311 -427 20 75 SER CA B 136 8 -392 -367 23
VAL CA I 3 128 17 -310 -413 19 SER C B 136 8 -404 -358 30
VAL C I 3 128 16 -323 -406 22 SER O B 136 8 -414 -361 28
VAL O I 3 128 15 -330 -410 18 SER CB B 136 9 -386 -368 25
VAL CB I 3 128 16 -297 -406 23 SER OG B 136 10 -379 -356 27
VAL CGI I 3 128 17 -285 -412 22 80 VAL N B 137 7 -403 -346 29
VAL CG2 I 3 128 15 -297 -404 23 VAL CA B 137 7 -415 -337 31
PRO N I 3 129 17 -327 -395 22 VAL C B 137 6 -425 -344 38
PRO CA I 3 129 17 -339 -387 22 VAL O B 137 5 -420 -350 39
PRO C I 3 129 15 -340 -382 24 VAL CB B 137 6 -410 -323 34
PRO O I 3 129 15 -350 -382 23 85 VAL CGI B 137 6 -422 -314 34
PRO CB I 3 129 18 -339 -376 24 VAL CG2 B 137 7 -400 -317 34
PRO CG I 3 129 19 -331 -380 28 SER N B 138 6 -438 -343 38
PRO CD I 3 129 18 -320 -388 24 SER CA B 138 5 -448 -348 38
PHE N I 3 130 15 -328 -377 18 SER C B 138 4 -447 -341 43
PHE CA I 3 130 13 -328 -371 17 90 SER O B 138 4 -446 -329 43
PHE C I 3 130 13 -316 -377 20 SER CB B 138 6 -462 -345 41
PHE O I 3 130 12 -306 -370 18 SER OG B 138 5 -473 -349 49
PHE CB I 3 130 13 -328 -356 19 GLN N B 139 3 -448 -349 40
PHE CG I 3 130 14 -341 -351 20 GLN CA B 139 2 -447 -344 40
PHE CD1 I 3 130 15 -341 -346 24 95 GLN C B 139 1 -460 -345 47
PHE CD2 I 3 130 13 -352 -351 22 GLN O B 139 1 -470 -343 48
PHE CE1 I 3 130 16 -354 -342 24 GLN CB B 139 1 -435 -352 40
PHE CE2 I 3 130 14 -365 -347 25 GLN CG B 139 2 -422 -351 41
PHE CZ I 3 130 15 -365 -343 23 GLN CD B 139 1 -416 -337 47
PRO N I 3 131 12 -317 -390 17 100 GLN OE1 B 139 0 -414 -332 35
PRO CA I 3 131 11 -306 -396 17 GLN NE2 B 139 3 -413 -330 37
PRO C I 3 131 10 -304 -389 19 NA NA Q 499 4 -373 -180 21
PRO O I 3 131 9 -313 -383 19 CHE CI Q 801 -14 -408 -217 38
PRO CB I 3 131 11 -311 -410 19 CHE C2 Q 801 -13 -411 -216 38
PRO CG I 3 131 11 -326 -409 24 105 CHE C3 Q 801 -12 -400 -210 39
PRO CD I 3 131 12 -329 -399 19 CHE C4 Q 801 -13 -393 -199 38
CYS N I 3 132 9 -292 -390 15 CHE N5 Q 801 -11 -404 -210 40
CYS CA I 3 132 8 -288 -383 15 CHE C6 Q 801 -10 -394 -204 39
CYS C I 3 132 7 -297 -388 20 CHE C7 Q 801 -8 -398 -205 39
CYS O I 3 132 7 -302 -400 19 110 CHE S8 Q 801 -8 -396 -190 38
CYS CB I 3 132 8 -273 -385 15 CHE 09 Q 801 -8 -405 -178 42
CYS SG I 3 132 8 -269 -402 19 CHE O10 Q 801 -6 -401 -191 36
GLY N I 3 133 6 -297 -380 17 CHE Oil Q 801 -8 -381 -186 41
GLY CA I 3 133 5 -304 -383 16 CHE C12 Q 801 -14 -388 -202 37
GLY C I 3 133 5 -318 -387 18 115 CHE C13 Q 801 -15 -399 -207 37
GLY O I 3 133 4 -323 -391 17 ASCH C28 S 1 -4 -180 -167 15
ARG N I 3 134 6 -325 -386 18 BSCH C28 S 1 -4 -180 -167 38
ARG CA I 3 134 6 -340 -389 20 ASCH C19 S 1 -12 -231 -243 11
ARG C I 3 134 6 -349 -377 21 BSCH C19 S 1 -14 -227 -223 24
ARG O I 3 134 6 -346 -367 20 120 ASCH C27 S 1 -4 -182 -154 20
ARG CB I 3 134 7 -344 -397 23 BSCH C27 S 1 -4 -183 -153 40
ARG CG I 3 134 7 -340 -412 46 ASCH C26 S 1 -5 -186 -172 15 BSCH C26 S 1 -6 -187 -171 38 ASCH 018 s 1 -8 -204 -202 7
ASCH C24 S 1 -11 -226 -234 8 BSCH 018 s 1 -9 -204 -203 28
BSCH C24 S 1 -13 -220 -215 24 HOH O w 1 -4 -282 -223 18
ASCH C25 S 1 -13 -218 -219 8 65 HOH O w 2 -7 -228 -201 13
BSCH C25 S 1 -12 -223 -232 25 HOH O w 3 -14 -263 -304 18
ASCH CIO S 1 -6 -197 -150 19 HOH O w 4 -20 -267 -281 35
BSCH CIO S 1 -6 -198 -150 40 HOH O w 5 -12 -257 -376 14
ASCH C31 S 1 -13 -231 -240 10 HOH O w 6 -18 -236 -256 33
BSCH C31 S 1 -14 -231 -236 23 70 HOH O w 7 -16 -262 -178 22
ASCH C30 S 1 -14 -224 -228 9 HOH O w 8 -0 -226 -294 15
BSCH C30 S 1 -13 -229 -240 25 HOH O w 9 -3 -299 -322 20
ASCH C8 S 1 -5 -191 -145 22 HOH O w 10 -8 -326 -223 14
BSCH C8 S 1 -5 -192 -145 42 HOH O w 11 -12 -358 -242 24
ASCH C7 S 1 -6 -195 -163 15 75 HOH O w 12 2 -369 -262 24
BSCH C7 S 1 -6 -196 -163 37 HOH O w 13 3 -338 -265 23
ASCH C17 S 1 -12 -219 -222 8 HOH O w 14 5 -354 -276 26
BSCH C17 S 1 -12 -218 -219 26 HOH O w 15 6 -316 -272 25
ASCH C32 S 1 -15 -236 -246 14 HOH O w 16 4 -314 -240 24
BSCH C32 s 1 -15 -238 -247 23 80 HOH O w 17 14 -344 -209 18
ASCH C9 s 1 -5 -187 -121 33 HOH O w 18 16 -321 -203 20
BSCH C9 s 1 -5 -187 -121 49 HOH O w 19 14 -316 -182 25
ASCH CI s 1 -8 -195 -174 10 HOH O w 20 14 -365 -229 20
BSCH CI s 1 -8 -195 -175 32 HOH O w 21 13 -353 -249 20
ASCH C5 s 1 -11 -206 -202 10 85 HOH 0 w 22 4 -351 -139 41
BSCH C5 s 1 -11 -204 -200 31 HOH 0 w 23 17 -360 -282 28
ASCH C34 s 1 -15 -225 -227 12 HOH 0 w 24 -6 -290 -171 22
BSCH C34 s 1 -12 -234 -253 25 HOH 0 w 25 1 -308 -159 23
ASCH C21 s 1 -5 -192 -107 35 HOH 0 w 26 4 -316 -168 19
BSCH C21 s 1 -4 -192 -108 50 90 HOH 0 w 27 5 -353 -164 27
ASCH C22 s 1 -3 -201 -130 34 HOH 0 w 28 -14 -186 -216 36
BSCH C22 s 1 -3 -203 -131 49 HOH 0 w 29 -7 -76 -254 19
ASCH C20 s 1 -7 -217 -165 14 HOH 0 w 30 -0 -61 -245 35
BSCH C20 s 1 -8 -217 -165 35 HOH 0 w 31 9 -180 -153 29
ASCH C29 s 1 -3 -209 -117 36 95 HOH 0 w 32 1 -195 -116 38
BSCH C29 s 1 -3 -209 -117 51 HOH 0 w 33 3 -193 -107 43
ASCH C23 s 1 -9 -222 -167 14 HOH 0 w 34 6 -226 -121 37
BSCH C23 s 1 -9 -222 -167 34 HOH 0 w 35 -12 -225 -282 23
ASCH C2 s 1 -10 -203 -180 10 HOH 0 w 36 -26 -215 -314 45
BSCH C2 s 1 -10 -203 -180 32 100 HOH 0 w 37 -16 -188 -376 23
ASCH C4 s 1 -10 -200 -196 10 HOH 0 w 38 -8 -129 -306 24
BSCH C4 s 1 -10 -200 -195 31 HOH 0 w 39 -17 -90 -257 30
ASCH N33 s 1 -16 -232 -239 14 HOH 0 w 40 -18 -65 -265 37
BSCH N33 s 1 -14 -240 -257 24 HOH 0 w 41 -16 -106 -268 26
ASCH N6 s 1 -4 -193 -132 30 105 HOH 0 w 42 -13 -76 -363 25
BSCH N6 s 1 -4 -195 -132 47 HOH 0 w 43 -6 -184 -391 19
ASCH N3 s 1 -7 -202 -168 12 HOH 0 w 44 -7 -172 -412 25
BSCH N3 s 1 -7 -202 -168 34 HOH 0 w 45 -5 -164 -481 26
ASCH Nil s 1 -11 -213 -214 8 HOH 0 w 46 0 -215 -405 19
BSCH Nil s 1 -11 -212 -212 29 110 HOH 0 w 47 6 -211 -440 24
ASCH N35 s 1 -15 -242 -258 16 HOH 0 w 48 7 -231 -405 20
BSCH N35 s 1 -16 -241 -247 22 HOH 0 w 49 9 -235 -388 26
ASCH 015 s 1 -6 -177 -122 33 HOH 0 w 50 8 -228 -363 20
BSCH 015 s 1 -5 -177 -122 49 HOH 0 w 51 8 -201 -373 23
ASCH 013 s 1 -8 -183 -175 9 115 HOH 0 w 52 12 -224 -377 37
BSCH 013 s 1 -8 -183 -177 32 HOH 0 w 53 10 -185 -363 18
ASCH 014 s 1 -12 -204 -197 12 HOH 0 w 54 12 -202 -362 28
BSCH 014 s 1 -12 -202 -194 34 HOH 0 w 55 16 -214 -366 41
ASCH 016 s 1 -3 -201 -106 38 HOH 0 w 56 14 -191 -368 29
BSCH 016 s 1 -3 -200 -107 52 120 HOH 0 w 57 11 -272 -400 23
ASCH 012 s 1 -9 -218 -179 12 HOH 0 w 58 16 -304 -370 26
BSCH 012 s 1 -9 -217 -179 33 HOH 0 w 59 18 -320 -327 30 HOH 0 w 60 15 -245 -449 39
HOH 0 w 61 15 -263 -477 45
HOH 0 w 62 11 -242 -504 20
HOH 0 w 63 10 -339 -374 28
HOH 0 w 64 9 -353 -355 23
HOH 0 w 65 6 -376 -337 18
HOH 0 w 66 14 -387 -319 14
HOH 0 w 67 3 -362 -403 23
HOH 0 w 68 1 -336 -392 23
HOH 0 w 69 14 -402 -343 26
HOH 0 w 70 17 -353 -307 20
HOH 0 w 71 18 -294 -312 31
HOH 0 w 72 9 -446 -331 45
HOH 0 w 73 12 -363 -384 41
HOH 0 w 74 16 -373 -376 34
HOH 0 w 75 -9 -261 -413 20
HOH 0 w 76 -11 -248 -400 19
HOH 0 w 77 3 -313 -465 19
HOH 0 w 78 3 -356 -484 31
HOH 0 w 79 -1 -352 -356 21
HOH 0 w 80 -4 -372 -375 46
HOH 0 w 81 -2 -330 -366 21
HOH 0 w 82 2 -355 -284 25
HOH 0 w 83 5 -376 -263 18
HOH 0 w 84 -7 -308 -405 21
HOH 0 w 85 6 -393 -246 22
HOH 0 w 86 6 -417 -241 47
HOH 0 w 87 6 -381 -216 28
HOH 0 w 88 -8 -351 -134 25
HOH 0 w 89 -4 -304 -127 44
HOH 0 w 90 2 -158 -164 25
HOH 0 w 91 0 -171 -158 23
HOH 0 w 92 8 -105 -200 26
HOH 0 w 93 1 -134 -471 28
HOH 0 w 94 5 -275 -525 19
HOH 0 w 95 -1 -265 -498 31
HOH 0 w 96 -4 -253 -509 26
HOH 0 w 97 -4 -236 -527 24
HOH 0 w 98 1 -100 -377 28
HOH 0 w 99 -11 -374 -312 19
HOH 0 w 100 -11 -362 -337 20
HOH 0 w 101 -14 -349 -344 27
HOH 0 w 102 -15 -362 -229 22
HOH 0 w 103 -4 -271 -250 12
Example 17: Crystallization of Factor IXa 318R/A- Compound A Complex (Tris/ AMS04).
The Factor IXa 318R/A-Compound A complex from Example 6 was crystallized using a hanging-drop vapor diffusion method. The Factor IXa 318R/A-Compound A complex (0.5 μΙ; 1 1.8 mg/ml) in 25 mM Tris, pH 8.0, 0.15 M sodium chloride, 5 mM calcium chloride buffer was mixed with an equal volume of precipitant solution containing 1.7 M ammonium sulfate, 2.0 M sodium chloride, 50 mM Tris-HCI
(hydroxymethyl)aminomethane), pH 7.2, placed on the underside of a siliconized Teflon coverslip and sealed in close proximity to 0.08 mL of the precipitant solution.
Crystallization plates were incubated at 18°C; crystals (0.01 x 0.05 mm) grew over a period of 1-18 days.
Example 18: Factor IXa 318R/A-Compound A Complex Crystals
(Tris/AMS04).
Factor IXa 318R/A-Compound A Complex Crystals (Tris/AMS04) were generated under the following conditions: 1.7 M ammonium sulfate, 2.0 M sodium chloride, 50 mM Tris-HCI, at pH -7.2; and incubation at about 18°C for about 5 days. Example 19: Crystallographic Analysis of Factor IXa 318R/A-Compound A
Complex (Tris/ AMS04).
Prior to data collection, Factor IXa 318R/A-Com pound A Complex crystals were harvested at 18°C and transferred into the crystallization solution with 1.5 M ammonium sulfate, 2.0 M sodium chloride, 50 mM Tris-HCI, pH 7.2. After about 0.5-1.0 minutes exposure to cryoprotectant the crystals were frozen in liquid nitrogen. The frozen crystals were then mounted onto the X-Ray detector in a nitrogen cooled stream. X-ray diffraction was collected using a Rigaku FRE superbright X-ray generator equipped with a Rigaku 4++ image plate detector. Data were integrated and scaled using the HKL package.
Table 10. Data Collection Statistics Example 19.
Figure imgf000082_0001
Unit Cell a= 98.9A, b=98.9A, c=93.9A, α=β= 90°, γ =
90°
Space Group H3
Asymmetric unit 1 molecule
Example 20: Factor IXa-318R/A-Compound A Complex Structure
Determination (Tris/ AMS04) ,
The crystal structure was solved using molecular replacement (CCP4) using the search model 1 RFN. Refinement was done using the program AUTOBUSTER (Global Phasing Limited).
Table 11. Crystallization Parameters for Factor IXa-318R/A-Compound A Complex Structure Determination (Tris/ AMS04) .
Figure imgf000083_0001
Table 12. Crystal Structural Coordinates of Factor IXa 318R/A- Compound A Complex (Tris/ AMS04).
The following table contains one line for each atom in one Factor IXa 318R/A monomer. The columns are: 1) 3-Letter amino acid code, 2) Atom name, 3) Chain, 4) Residue number, 5) X-coordinate, 6) Y-coordinate, 7) Z-coordinate, 8) B-factor. (Amino Acid Code NA are Sodium, CHE is CHESS buffer, SCH is Compound A and HOH for water) Note: B factors greater than 100 appear as 0 in column 8.
VAL N A 16 -10 -260 -86 25 60 PRO O A 24 4 -160 -13 28
VAL CA A 16 -11 -257 -74 24 PRO CB A 24 4 -151 -42 29
VAL C A 16 -12 -247 -78 29 PRO CG A 24 3 -141 -50 33
VAL O A 16 -11 -236 -83 28 PRO CD A 24 2 -141 -41 29
VAL CB A 16 -10 -250 -63 28 GLY N A 25 4 -179 -23 27
VAL CGI A 16 -11 -247 -50 28 65 GLY CA A 25 5 -185 -11 26
VAL CG2 A 16 -8 -259 -60 28 GLY C A 25 4 -190 -1 29
VAL N A 17 -13 -251 -75 26 GLY O A 25 4 -193 11 28
VAL CA A 17 -14 -243 -77 26 GLN N A 26 2 -189 -4 24
VAL C A 17 -14 -235 -64 29 GLN CA A 26 1 -193 6 24
VAL O A 17 -15 -242 -54 28 70 GLN C A 26 1 -208 8 28
VAL CB A 17 -15 -251 -82 30 GLN O A 26 1 -212 19 29
VAL CGI A 17 -17 -242 -85 31 GLN CB A 26 -0 -187 3 25
VAL CG2 A 17 -15 -259 -95 29 GLN CG A 26 -1 -186 15 27
GLY N A 18 -15 -222 -65 26 GLN CD A 26 -2 -180 11 37
GLY CA A 18 -15 -214 -54 26 75 GLN OE1 A 26 -2 -173 0 26
GLY C A 18 -14 -211 -44 30 GLN NE2 A 26 -3 -182 18 33
GLY O A 18 -14 -208 -32 29 PHE N A 27 1 -216 -2 23
GLY N A 19 -13 -212 -48 27 PHE CA A 27 1 -231 -1 23
GLY CA A 19 -12 -209 -40 27 PHE C A 27 3 -236 -8 24
GLY C A 19 -11 -194 -42 32 80 PHE O A 27 3 -241 -19 23
GLY O A 19 -12 -186 -49 30 PHE CB A 27 0 -236 -10 25
GLU N A 20 -10 -192 -37 29 PHE CG A 27 -1 -231 -3 27
GLU CA A 20 -9 -178 -38 29 PHE CD1 A 27 -2 -219 -7 28
GLU C A 20 -8 -180 -43 31 PHE CD2 A 27 -2 -238 8 27
GLU O A 20 -7 -191 -42 29 85 PHE CE1 A 27 -3 -214 -0 29
GLU CB A 20 -9 -172 -24 30 PHE CE2 A 27 -3 -233 14 30
GLU CG A 20 -10 -169 -16 48 PHE CZ A 27 -3 -221 10 28
GLU CD A 20 -10 -165 -2 69 PRO N A 28 4 -234 -1 21
GLU OE1 A 20 -10 -173 7 58 PRO CA A 28 5 -237 -8 22
GLU OE2 A 20 -9 -153 0 57 90 PRO C A 28 5 -252 -10 26
ASP N A 21 -7 -169 -49 27 PRO O A 28 6 -255 -16 25
ASP CA A 21 -6 -169 -54 26 PRO CB A 28 6 -229 1 22
ASP C A 21 -5 -170 -42 28 PRO CG A 28 6 -230 15 25
ASP O A 21 -5 -163 -32 26 PRO CD A 28 4 -228 12 21
ASP CB A 21 -6 -156 -61 28 95 TRP N A 29 5 -261 -4 24
ASP CG A 21 -6 -154 -74 39 TRP CA A 29 5 -275 -6 22
ASP OD1 A 21 -6 -144 -81 41 TRP C A 29 4 -280 -18 26
ASP OD2 A 21 -7 -162 -78 37 TRP O A 29 4 -291 -23 26
ALA N A 22 -4 -179 -43 24 TRP CB A 29 4 -282 7 21
ALA CA A 22 -3 -180 -33 24 100 TRP CG A 29 3 -277 11 19
ALA C A 22 -2 -169 -36 30 TRP CD1 A 29 2 -279 6 22
ALA O A 22 -2 -164 -47 29 TRP CD2 A 29 3 -266 21 20
ALA CB A 22 -2 -194 -34 24 TRP NE1 A 29 1 -271 12 21
LYS N A 23 -1 -164 -25 28 TRP CE2 A 29 1 -263 21 23
LYS CA A 23 -0 -154 -26 29 105 TRP CE3 A 29 4 -260 30 21
LYS C A 23 1 -161 -29 32 TRP CZ2 A 29 1 -254 31 23
LYS O A 23 1 -173 -25 29 TRP CZ3 A 29 3 -251 39 22
LYS CB A 23 -0 -146 -13 31 TRP CH2 A 29 2 -248 39 23
LYS CG A 23 -1 -135 -12 38 GLN N A 30 3 -271 -24 24
LYS CD A 23 -1 -128 1 43 110 GLN CA A 30 2 -275 -36 24
LYS CE A 23 -3 -120 3 54 GLN C A 30 3 -276 -49 26
LYS NZ A 23 -3 -114 16 68 GLN O A 30 4 -267 -51 26
PRO N A 24 2 -155 -35 28 GLN CB A 30 1 -264 -38 26
PRO CA A 24 3 -162 -37 27 GLN CG A 30 1 -265 -51 29
PRO C A 24 4 -167 -23 30 115 GLN CD A 30 -1 -275 -50 35 GLN 0E1 A 30 -1 -275 -41 25 ALA CA A 39 -1 -289 -147 36
GLN NE2 A 30 -1 -284 -60 26 ALA C A 39 -2 -300 -148 35
VAL N A 31 3 -286 -57 22 ALA 0 A 39 -4 -297 -145 34
VAL CA A 31 4 -288 -69 22 65 ALA CB A 39 -2 -275 -145 36
VAL C A 31 3 -290 -80 26 PHE N A 40 -2 -312 -152 29
VAL 0 A 31 2 -294 -77 24 PHE CA A 40 -3 -323 -153 29
VAL CB A 31 5 -299 -71 23 PHE C A 40 -3 -329 -138 30
VAL CGI A 31 6 -296 -61 23 PHE 0 A 40 -4 -335 -136 31
VAL CG2 A 31 4 -313 -69 22 70 PHE CB A 40 -3 -334 -163 30
VAL N A 32 3 -287 -92 25 PHE CG A 40 -1 -342 -158 32
VAL CA A 32 2 -290 -104 24 PHE CD1 A 40 -0 -339 -162 33
VAL C A 32 3 -301 -112 28 PHE CD2 A 40 -1 -354 -150 34
VAL 0 A 32 4 -301 -113 26 PHE CE1 A 40 1 -346 -158 33
VAL CB A 32 2 -277 -112 27 75 PHE CE2 A 40 -0 -361 -146 36
VAL CGI A 32 3 -270 -118 26 PHE CZ A 40 1 -358 -150 34
VAL CG2 A 32 1 -280 -122 25 CYS N A 41 -2 -327 -129 26
LEU N A 33 2 -310 -118 27 CYS CA A 41 -2 -332 -116 27
LEU CA A 33 3 -320 -127 28 CYS C A 41 -2 -323 -107 29
LEU C A 33 2 -316 -141 32 80 CYS 0 A 41 -1 -315 -112 30
LEU 0 A 33 1 -313 -143 30 CYS CB A 41 -2 -347 -114 28
LEU CB A 33 2 -334 -124 28 CYS SG A 41 -3 -359 -117 33
LEU CG A 33 2 -339 -109 32 GLY N A 42 -2 -324 -94 26
LEU CD1 A 33 2 -354 -108 31 GLY CA A 42 -1 -317 -84 26
LEU CD2 A 33 4 -336 -104 35 85 GLY C A 42 -0 -327 -76 28
ASN N A 34 3 -316 -151 32 GLY 0 A 42 -0 -339 -78 26
ASN CA A 34 3 -313 -165 34 GLY N A 43 1 -322 -66 25
ASN C A 34 3 -325 -174 39 GLY CA A 43 1 -330 -57 25
ASN 0 A 34 4 -331 -172 38 GLY C A 43 2 -322 -45 28
ASN CB A 34 4 -300 -169 32 90 GLY 0 A 43 2 -309 -45 25
ASN CG A 34 3 -288 -161 42 SER N A 44 3 -328 -36 23
ASN OD1 A 34 2 -286 -158 37 SER CA A 44 3 -321 -25 24
ASN ND2 A 34 4 -279 -158 33 SER C A 44 5 -325 -23 28
GLY N A 35 2 -327 -183 40 SER 0 A 44 5 -337 -25 27
GLY CA A 35 3 -338 -193 41 95 SER CB A 44 3 -325 -12 27
GLY C A 35 2 -333 -207 47 SER OG A 44 1 -322 -13 37
GLY 0 A 35 3 -322 -211 46 ILE N A 45 6 -316 -19 23
LYS N A 36 1 -341 -214 47 ILE CA A 45 7 -319 -16 22
LYS CA A 36 1 -337 -227 48 ILE C A 45 7 -326 -2 24
LYS C A 36 -0 -325 -224 54 100 ILE O A 45 7 -321 8 22
LYS 0 A 36 0 -315 -231 54 ILE CB A 45 8 -306 -15 24
LYS CB A 36 -0 -348 -233 51 ILE CGI A 45 8 -298 -29 23
LYS CG A 36 1 -361 -238 72 ILE CG2 A 45 9 -309 -11 22
LYS CD A 36 -0 -372 -241 87 ILE CD1 A 45 8 -283 -29 20
LYS CE A 36 0 -386 -242 0 105 VAL N A 46 8 -338 -3 21
LYS NZ A 36 -1 -396 -240 0 VAL CA A 46 8 -346 9 21
VAL N A 37 -1 -326 -213 52 VAL C A 46 9 -341 15 24
VAL CA A 37 -2 -315 -208 51 VAL O A 46 9 -338 26 24
VAL C A 37 -1 -309 -196 54 VAL CB A 46 8 -361 7 24
VAL 0 A 37 -0 -316 -188 54 110 VAL CGI A 46 8 -369 19 24
VAL CB A 37 -3 -321 -203 56 VAL CG2 A 46 7 -365 1 23
VAL CGI A 37 -4 -311 -197 55 ASN N A 47 10 -340 6 23
VAL CG2 A 37 -4 -328 -215 55 ASN CA A 47 12 -335 8 24
ASP N A 38 -1 -295 -195 48 ASN C A 47 12 -331 -5 28
ASP CA A 38 -0 -288 -185 47 115 ASN O A 47 12 -331 -15 26
ASP C A 38 -1 -288 -172 45 ASN CB A 47 12 -346 16 25
ASP 0 A 38 -2 -289 -174 44 ASN CG A 47 13 -359 9 35
ASP CB A 38 -0 -274 -189 51 ASN OD1 A 47 13 -359 -4 31
ASP CG A 38 1 -270 -191 67 ASN ND2 A 47 13 -370 16 28
ASP OD1 A 38 2 -279 -198 68 120 GLU N A 48 14 -327 -5 27
ASP OD2 A 38 2 -260 -186 76 GLU CA A 48 14 -322 -18 29
ALA N A 39 -1 -288 -160 38 GLU C A 48 14 -332 -29 31 GLU 0 A 48 14 -328 -41 29 HIS N A 56 -3 -427 -97 27
GLU CB A 48 16 -319 -15 30 HIS CA A 56 -4 -425 -110 27
GLU CG A 48 16 -312 -2 51 HIS C A 56 -3 -414 -119 33
GLU CD A 48 16 -322 9 70 65 HIS 0 A 56 -3 -416 -131 34
GLU 0E1 A 48 17 -327 11 75 HIS CB A 56 -5 -422 -109 27
GLU OE2 A 48 15 -325 16 42 HIS CG A 56 -6 -408 -106 30
LYS N A 49 14 -345 -27 30 HIS ND1 A 56 -6 -405 -93 31
LYS CA A 49 14 -355 -37 31 HIS CD2 A 56 -6 -397 -114 31
LYS C A 49 13 -362 -40 34 70 HIS CE1 A 56 -7 -392 -94 30
LYS 0 A 49 13 -370 -50 32 HIS NE2 A 56 -6 -387 -106 31
LYS CB A 49 15 -366 -34 34 CYS N A 57 -3 -404 -112 30
LYS CG A 49 17 -362 -37 45 CYS CA A 57 -2 -393 -119 30
LYS CD A 49 17 -365 -52 45 CYS C A 57 -1 -398 -126 37
LYS CE A 49 17 -379 -55 46 75 CYS 0 A 57 -0 -392 -135 34
LYS NZ A 49 18 -381 -69 39 CYS CB A 57 -2 -383 -109 29
TRP N A 50 12 -360 -31 30 CYS SG A 57 -3 -373 -103 33
TRP CA A 50 10 -367 -32 29 VAL N A 58 -0 -410 -122 37
TRP C A 50 9 -359 -32 29 VAL CA A 58 1 -415 -127 39
TRP 0 A 50 9 -349 -24 26 80 VAL C A 58 1 -428 -134 49
TRP CB A 50 10 -378 -21 29 VAL 0 A 58 2 -433 -137 49
TRP CG A 50 11 -389 -22 30 VAL CB A 58 2 -414 -115 43
TRP CD1 A 50 13 -389 -17 33 VAL CGI A 58 2 -400 -109 43
TRP CD2 A 50 11 -401 -30 29 VAL CG2 A 58 2 -424 -104 43
TRP NE1 A 50 13 -400 -20 33 85 GLU N A 59 0 -433 -138 51
TRP CE2 A 50 12 -408 -28 34 GLU CA A 59 -0 -446 -145 54
TRP CE3 A 50 10 -407 -37 30 GLU C A 59 -0 -443 -160 63
TRP CZ2 A 50 13 -421 -34 33 GLU 0 A 59 0 -453 -168 63
TRP CZ3 A 50 10 -419 -43 32 GLU CB A 59 -1 -454 -141 56
TRP CH2 A 50 12 -426 -41 33 90 GLU CG A 59 -1 -458 -127 70
ILE N A 51 8 -363 -41 23 GLU CD A 59 -0 -467 -121 98
ILE CA A 51 7 -358 -42 23 GLU OE1 A 59 -0 -479 -125 0
ILE C A 51 6 -369 -39 27 GLU OE2 A 59 0 -463 -111 95
ILE 0 A 51 6 -380 -44 26 THR N A 60 -0 -431 -164 62
ILE CB A 51 7 -352 -57 26 95 THR CA A 60 -0 -425 -178 63
ILE CGI A 51 8 -341 -61 26 THR C A 60 1 -430 -188 69
ILE CG2 A 51 5 -348 -59 26 THR 0 A 60 0 -434 -199 70
ILE CD1 A 51 8 -328 -52 23 THR CB A 60 -1 -410 -177 75
VAL N A 52 5 -365 -32 24 THR OG1 A 60 -2 -409 -172 76
VAL CA A 52 4 -374 -30 22 100 THR CG2 A 60 -1 -404 -191 75
VAL C A 52 2 -369 -38 26 GLY N A 61 2 -428 -185 65
VAL 0 A 52 2 -357 -38 26 GLY CA A 61 3 -431 -194 65
VAL CB A 52 3 -376 -15 25 GLY C A 61 4 -418 -200 68
VAL CGI A 52 2 -388 -13 24 GLY O A 61 5 -419 -208 68
VAL CG2 A 52 3 -364 -8 24 105 VAL N A 62 3 -407 -197 64
THR N A 53 2 -378 -45 22 VAL CA A 62 4 -393 -201 64
THR CA A 53 1 -375 -55 21 VAL C A 62 5 -391 -194 66
THR C A 53 -0 -386 -54 25 VAL O A 62 5 -396 -183 66
THR 0 A 53 -0 -395 -46 25 VAL CB A 62 3 -381 -199 68
THR CB A 53 1 -370 -68 25 110 VAL CGI A 62 1 -382 -208 68
THR OG1 A 53 0 -366 -77 23 VAL CG2 A 62 2 -380 -184 67
THR CG2 A 53 2 -382 -76 27 LYS N A 63 6 -383 -200 59
ALA N A 54 -1 -386 -63 23 LYS CA A 63 7 -379 -194 57
ALA CA A 54 -2 -397 -65 24 LYS C A 63 6 -368 -184 55
ALA C A 54 -2 -407 -74 28 115 LYS O A 63 6 -358 -189 54
ALA 0 A 54 -1 -404 -83 26 LYS CB A 63 8 -373 -205 60
ALA CB A 54 -4 -392 -70 24 LYS CG A 63 9 -373 -200 74
ALA N A 55 -2 -420 -72 26 LYS CD A 63 10 -360 -193 84
ALA CA A 55 -2 -431 -81 27 LYS CE A 63 9 -347 -198 94
ALA C A 55 -2 -430 -95 30 120 LYS NZ A 63 10 -343 -212 0
ALA 0 A 55 -1 -433 -105 30 ILE N A 64 7 -370 -171 48
ALA CB A 55 -2 -445 -75 27 ILE CA A 64 6 -361 -161 46 ILE C A 64 7 -350 -158 43 ASN OD1 A 72 0 -169 -146 33
ILE 0 A 64 8 -354 -155 42 ASN ND2 A 72 -0 -150 -136 33
ILE CB A 64 6 -368 -148 49 ILE N A 73 1 -200 -136 35
ILE CGI A 64 5 -378 -151 49 65 ILE CA A 73 1 -209 -146 37
ILE CG2 A 64 5 -357 -138 49 ILE C A 73 2 -204 -160 42
ILE CD1 A 64 4 -388 -140 56 ILE 0 A 73 2 -211 -167 42
THR N A 65 7 -338 -158 37 ILE CB A 73 1 -223 -147 40
THR CA A 65 8 -327 -154 36 ILE CGI A 73 -1 -220 -151 41
THR C A 65 7 -321 -141 34 70 ILE CG2 A 73 1 -232 -135 40
THR 0 A 65 6 -318 -140 30 ILE CD1 A 73 -2 -232 -158 49
THR CB A 65 8 -316 -165 47 GLU N A 74 1 -191 -162 41
THR 0G1 A 65 8 -321 -176 52 GLU CA A 74 2 -185 -175 42
THR CG2 A 65 8 -303 -160 46 GLU C A 74 3 -173 -174 45
VAL N A 66 8 -321 -130 30 75 GLU 0 A 74 3 -167 -184 47
VAL CA A 66 7 -316 -117 30 GLU CB A 74 1 -181 -183 44
VAL C A 66 8 -301 -116 30 GLU CG A 74 -0 -169 -178 57
VAL 0 A 66 9 -298 -118 30 GLU CD A 74 -1 -164 -187 82
VAL CB A 66 8 -324 -105 34 GLU OE1 A 74 -2 -171 -197 74
VAL CGI A 66 8 -318 -92 34 80 GLU OE2 A 74 -2 -152 -185 72
VAL CG2 A 66 7 -339 -106 34 GLU N A 75 3 -171 -162 39
VAL N A 67 7 -292 -112 24 GLU CA A 75 4 -160 -160 39
VAL CA A 67 7 -278 -110 24 GLU C A 75 6 -165 -152 41
VAL C A 67 7 -273 -96 28 GLU O A 75 5 -172 -143 39
VAL 0 A 67 6 -272 -92 27 85 GLU CB A 75 4 -149 -152 40
VAL CB A 67 7 -268 -121 27 GLU CG A 75 4 -135 -157 59
VAL CGI A 67 8 -255 -120 26 GLU CD A 75 3 -125 -158 86
VAL CG2 A 67 7 -274 -135 27 GLU OE1 A 75 2 -128 -163 73
ALA N A 68 8 -270 -88 25 GLU OE2 A 75 3 -113 -155 87
ALA CA A 68 8 -264 -75 26 90 THR N A 76 7 -160 -156 37
ALA C A 68 8 -249 -76 30 THR CA A 76 8 -164 -149 37
ALA 0 A 68 9 -244 -86 28 THR C A 76 8 -155 -137 39
ALA CB A 68 9 -270 -66 26 THR O A 76 8 -142 -138 39
GLY N A 69 8 -242 -66 28 THR CB A 76 9 -164 -158 42
GLY CA A 69 8 -227 -65 27 95 THR OG1 A 76 9 -175 -168 41
GLY C A 69 7 -220 -75 30 THR CG2 A 76 10 -167 -151 39
GLY 0 A 69 7 -209 -78 31 GLU N A 77 8 -161 -125 33
GLU N A 70 6 -227 -80 27 GLU CA A 77 8 -154 -112 32
GLU CA A 70 5 -221 -90 27 GLU C A 77 10 -155 -105 34
GLU C A 70 4 -214 -84 31 100 GLU O A 77 10 -149 -95 33
GLU 0 A 70 3 -217 -73 30 GLU CB A 77 7 -158 -103 34
GLU CB A 70 4 -233 -99 28 GLU CG A 77 6 -152 -108 41
GLU CG A 70 4 -229 -111 36 GLU CD A 77 5 -160 -106 54
GLU CD A 70 4 -220 -121 44 GLU OE1 A 77 5 -172 -109 37
GLU OE1 A 70 4 -208 -118 26 105 GLU OE2 A 77 4 -154 -100 41
GLU OE2 A 70 5 -225 -131 28 HIS N A 78 11 -162 -111 30
HIS N A 71 3 -203 -90 28 HIS CA A 78 12 -165 -106 31
HIS CA A 71 2 -194 -86 27 HIS C A 78 12 -172 -93 31
HIS C A 71 1 -192 -98 32 HIS O A 78 13 -171 -86 29
HIS 0 A 71 0 -197 -98 30 110 HIS CB A 78 13 -151 -106 33
HIS CB A 71 3 -181 -80 28 HIS CG A 78 13 -146 -120 38
HIS CG A 71 2 -172 -75 31 HIS ND1 A 78 14 -152 -129 40
HIS ND1 A 71 1 -160 -82 33 HIS CD2 A 78 12 -135 -126 41
HIS CD2 A 71 1 -173 -65 33 HIS CE1 A 78 14 -145 -140 40
HIS CE1 A 71 0 -154 -75 32 115 HIS NE2 A 78 13 -135 -139 41
HIS NE2 A 71 0 -161 -65 33 THR N A 79 11 -181 -91 27
ASN N A 72 2 -184 -107 32 THR CA A 79 11 -190 -80 26
ASN CA A 72 1 -181 -120 33 THR C A 79 11 -205 -84 30
ASN C A 72 2 -190 -131 38 THR O A 79 11 -214 -75 29
ASN 0 A 72 3 -188 -134 38 120 THR CB A 79 10 -186 -71 28
ASN CB A 72 1 -166 -123 34 THR OG1 A 79 8 -187 -78 25
ASN CG A 72 0 -162 -136 41 THR CG2 A 79 10 -171 -66 23 GLU N A 80 10 -207 -96 28 ARG N A 87 12 -420 -108 36
GLU CA A 80 10 -220 -102 28 ARG CA A 87 11 -432 -102 35
GLU C A 80 11 -229 -103 32 ARG C A 87 10 -429 -98 37
GLU 0 A 80 12 -224 -108 33 65 ARG O A 87 10 -419 -91 35
GLU CB A 80 9 -219 -115 29 ARG CB A 87 12 -437 -91 35
GLU CG A 80 8 -210 -115 31 ARG CG A 87 12 -452 -87 49
GLU CD A 80 8 -196 -119 39 ARG CD A 87 13 -458 -81 58
GLU OE1 A 80 9 -191 -119 26 ARG NE A 87 13 -465 -68 65
GLU OE2 A 80 7 -189 -123 29 70 ARG CZ A 87 13 -461 -56 78
GLN N A 81 11 -241 -99 27 ARG NH1 A 87 14 -450 -55 55
GLN CA A 81 12 -252 -100 27 ARG NH2 A 87 13 -468 -46 74
GLN C A 81 11 -263 -107 33 ILE N A 88 9 -438 -102 34
GLN 0 A 81 10 -270 -102 31 ILE CA A 88 8 -437 -98 34
GLN CB A 81 13 -255 -86 28 75 ILE C A 88 7 -449 -89 38
GLN CG A 81 13 -244 -80 34 ILE O A 88 7 -461 -93 39
GLN CD A 81 14 -249 -67 38 ILE CB A 88 7 -436 -111 36
GLN OE1 A 81 15 -260 -65 30 ILE CGI A 88 7 -425 -120 37
GLN NE2 A 81 14 -240 -57 30 ILE CG2 A 88 5 -436 -106 36
LYS N A 82 12 -266 -119 31 80 ILE CD1 A 88 6 -425 -135 37
LYS CA A 82 11 -277 -128 32 ILE N A 89 7 -447 -77 33
LYS C A 82 12 -289 -126 35 ILE CA A 89 6 -457 -68 32
LYS 0 A 82 14 -288 -126 34 ILE C A 89 5 -456 -65 34
LYS CB A 82 12 -271 -142 36 ILE O A 89 4 -449 -55 32
LYS CG A 82 11 -279 -153 60 85 ILE CB A 89 7 -457 -55 34
LYS CD A 82 10 -270 -164 77 ILE CGI A 89 9 -456 -57 35
LYS CE A 82 10 -277 -178 93 ILE CG2 A 89 7 -469 -46 35
LYS NZ A 82 9 -273 -187 0 ILE CD1 A 89 10 -455 -44 43
ARG N A 83 12 -301 -124 32 PRO N A 90 4 -462 -74 31
ARG CA A 83 12 -313 -122 31 90 PRO CA A 90 2 -461 -70 32
ARG C A 83 12 -325 -130 34 PRO C A 90 2 -471 -59 36
ARG 0 A 83 11 -326 -131 32 PRO O A 90 3 -481 -58 34
ARG CB A 83 13 -318 -107 30 PRO CB A 90 2 -465 -83 34
ARG CG A 83 13 -308 -99 32 PRO CG A 90 3 -473 -91 37
ARG CD A 83 15 -308 -103 28 95 PRO CD A 90 4 -470 -85 33
ARG NE A 83 16 -299 -93 31 HIS N A 91 1 -469 -50 33
ARG CZ A 83 16 -286 -94 41 HIS CA A 91 1 -478 -40 33
ARG NH1 A 83 15 -279 -103 26 HIS C A 91 1 -492 -46 40
ARG NH2 A 83 17 -280 -85 34 HIS O A 91 -0 -493 -56 38
ASN N A 84 13 -334 -134 32 100 HIS CB A 91 -0 -474 -31 33
ASN CA A 84 12 -347 -141 32 HIS CG A 91 -0 -481 -18 37
ASN C A 84 12 -358 -130 34 HIS ND1 A 91 -1 -492 -16 38
ASN 0 A 84 13 -358 -120 34 HIS CD2 A 91 0 -479 -6 38
ASN CB A 84 13 -351 -151 32 HIS CE1 A 91 -1 -496 -4 37
ASN CG A 84 14 -342 -162 48 105 HIS NE2 A 91 -0 -488 3 38
ASN OD1 A 84 13 -340 -171 43 HIS N A 92 1 -502 -40 43
ASN ND2 A 84 15 -334 -162 36 HIS CA A 92 1 -516 -45 45
VAL N A 85 11 -367 -133 33 HIS C A 92 -0 -522 -47 47
VAL CA A 85 11 -378 -124 33 HIS O A 92 -0 -530 -56 47
VAL C A 85 12 -390 -129 40 110 HIS CB A 92 2 -526 -37 47
VAL 0 A 85 12 -394 -140 38 HIS CG A 92 2 -527 -22 52
VAL CB A 85 9 -382 -124 37 HIS ND1 A 92 2 -517 -14 55
VAL CGI A 85 9 -394 -115 37 HIS CD2 A 92 1 -537 -15 55
VAL CG2 A 85 9 -370 -120 37 HIS CE1 A 92 2 -521 -2 55
ILE N A 86 13 -396 -120 39 115 HIS NE2 A 92 1 -533 -2 55
ILE CA A 86 13 -408 -123 40 ASN N A 93 -1 -517 -39 42
ILE C A 86 13 -421 -118 44 ASN CA A 93 -3 -522 -40 41
ILE 0 A 86 13 -432 -124 45 ASN C A 93 -3 -513 -49 42
ILE CB A 86 15 -408 -119 43 ASN O A 93 -5 -515 -48 39
ILE CGI A 86 15 -403 -104 43 120 ASN CB A 93 -3 -524 -26 42
ILE CG2 A 86 16 -399 -128 45 ASN CG A 93 -2 -533 -17 59
ILE CD1 A 86 16 -409 -97 51 ASN OD1 A 93 -2 -531 -4 55 ASN ND2 A 93 -2 -544 -22 47 TYR CG A 101 -12 -428 -54 45
TYR N A 94 -3 -503 -56 38 TYR CD1 A 101 -12 -414 -54 47
TYR CA A 94 -4 -495 -65 37 TYR CD2 A 101 -14 -433 -61 46
TYR C A 94 -4 -502 -77 44 65 TYR CE1 A 101 -13 -406 -61 48
TYR 0 A 94 -3 -508 -84 44 TYR CE2 A 101 -14 -425 -69 47
TYR CB A 94 -3 -482 -68 36 TYR CZ A 101 -14 -411 -69 55
TYR CG A 94 -4 -473 -76 36 TYR OH A 101 -15 -404 -76 57
TYR CD1 A 94 -5 -467 -70 39 ASN N A 102 -9 -462 -43 39
TYR CD2 A 94 -4 -470 -90 37 70 ASN CA A 102 -9 -470 -33 37
TYR CE1 A 94 -6 -459 -77 39 ASN C A 102 -7 -471 -34 36
TYR CE2 A 94 -5 -462 -97 38 ASN O A 102 -7 -476 -45 37
TYR CZ A 94 -6 -457 -91 45 ASN CB A 102 -9 -484 -31 39
TYR OH A 94 -7 -449 -98 46 ASN CG A 102 -9 -491 -18 49
ASN N A 95 -5 -501 -80 43 75 ASN OD1 A 102 -9 -485 -8 40
ASN CA A 95 -6 -508 -92 44 ASN ND2 A 102 -9 -505 -18 40
ASN C A 95 -7 -500 -97 51 HIS N A 103 -6 -467 -24 30
ASN 0 A 95 -8 -502 -91 51 HIS CA A 103 -5 -467 -24 29
ASN CB A 95 -6 -522 -90 46 HIS C A 103 -4 -458 -34 31
ASN CG A 95 -6 -531 -102 72 80 HIS O A 103 -3 -460 -41 30
ASN OD1 A 95 -7 -527 -113 68 HIS CB A 103 -4 -481 -25 30
ASN ND2 A 95 -6 -543 -102 65 HIS CG A 103 -5 -492 -16 34
ALA N A 96 -7 -491 -107 51 HIS ND1 A 103 -5 -491 -3 36
ALA CA A 96 -8 -483 -112 52 HIS CD2 A 103 -6 -503 -19 36
ALA C A 96 -9 -491 -119 58 85 HIS CE1 A 103 -5 -502 2 36
ALA 0 A 96 -11 -486 -118 57 HIS NE2 A 103 -6 -509 -7 36
ALA CB A 96 -8 -473 -122 54 ASP N A 104 -5 -446 -36 27
ALA N A 97 -9 -503 -124 56 ASP CA A 104 -5 -437 -47 26
ALA CA A 97 -10 -512 -130 57 ASP C A 104 -4 -428 -42 30
ALA C A 97 -11 -518 -120 62 90 ASP O A 104 -4 -416 -39 31
ALA 0 A 97 -12 -521 -123 63 ASP CB A 104 -6 -429 -52 28
ALA CB A 97 -9 -524 -137 58 ASP CG A 104 -6 -422 -65 33
ILE N A 98 -11 -518 -107 56 ASP OD1 A 104 -5 -425 -72 33
ILE CA A 98 -11 -523 -96 55 ASP OD2 A 104 -7 -414 -69 36
ILE C A 98 -12 -511 -88 57 95 ILE N A 105 -2 -433 -42 25
ILE 0 A 98 -13 -510 -88 57 ILE CA A 105 -1 -426 -37 24
ILE CB A 98 -11 -532 -86 57 ILE C A 105 -0 -431 -43 29
ILE CGI A 98 -10 -544 -94 57 ILE O A 105 0 -443 -45 27
ILE CG2 A 98 -11 -537 -74 59 ILE CB A 105 -1 -426 -21 27
ILE CD1 A 98 -9 -552 -87 60 100 ILE CGI A 105 -0 -416 -15 27
ASN N A 99 -11 -502 -82 52 ILE CG2 A 105 -1 -440 -15 27
ASN CA A 99 -12 -490 -75 51 ILE CD1 A 105 -0 -414 0 25
ASN C A 99 -11 -479 -78 54 ALA N A 106 1 -422 -47 25
ASN 0 A 99 -9 -480 -75 53 ALA CA A 106 2 -425 -54 25
ASN CB A 99 -12 -494 -60 49 105 ALA C A 106 3 -416 -49 30
ASN CG A 99 -12 -483 -51 65 ALA O A 106 3 -405 -44 29
ASN OD1 A 99 -12 -471 -52 54 ALA CB A 106 2 -425 -69 25
ASN ND2 A 99 -13 -487 -43 55 LEU N A 107 4 -420 -51 26
LYS N A 100 -11 -468 -84 49 LEU CA A 107 6 -413 -48 27
LYS CA A 100 -10 -456 -87 48 110 LEU C A 107 6 -411 -61 33
LYS C A 100 -10 -448 -75 45 LEU O A 107 7 -420 -69 33
LYS 0 A 100 -9 -442 -76 43 LEU CB A 107 6 -419 -37 27
LYS CB A 100 -11 -448 -97 51 LEU CG A 107 6 -420 -23 33
LYS CG A 100 -11 -451 -112 74 LEU CD1 A 107 7 -429 -14 33
LYS CD A 100 -12 -447 -122 89 115 LEU CD2 A 107 6 -406 -17 32
LYS CE A 100 -11 -453 -136 0 LEU N A 108 7 -399 -63 29
LYS NZ A 100 -13 -450 -145 0 LEU CA A 108 8 -395 -74 28
TYR N A 101 -11 -449 -64 40 LEU C A 108 9 -391 -69 32
TYR CA A 101 -10 -441 -52 40 LEU O A 108 9 -382 -61 30
TYR C A 101 -9 -449 -42 43 120 LEU CB A 108 7 -383 -82 27
TYR 0 A 101 -9 -442 -33 42 LEU CG A 108 6 -384 -87 32
TYR CB A 101 -12 -436 -45 43 LEU CD1 A 108 5 -371 -93 31 LEU CD2 A 108 6 -396 -97 32 LEU CB A 116 15 -266 9 27
GLU N A 109 10 -398 -74 29 LEU CG A 116 14 -281 7 31
GLU CA A 109 12 -394 -71 29 LEU CD1 A 116 14 -287 21 30
GLU C A 109 12 -385 -82 34 65 LEU CD2 A 116 13 -285 -2 30
GLU 0 A 109 12 -389 -93 34 ASN N A 117 14 -235 -0 26
GLU CB A 109 13 -406 -69 29 ASN CA A 117 14 -221 3 27
GLU CG A 109 14 -403 -63 34 ASN C A 117 12 -217 7 31
GLU CD A 109 15 -414 -63 53 ASN O A 117 11 -225 9 30
GLU OE1 A 109 15 -425 -69 40 70 ASN CB A 117 14 -212 -9 21
GLU OE2 A 109 16 -412 -58 55 ASN CG A 117 13 -214 -22 35
LEU N A 110 13 -373 -78 30 ASN OD1 A 117 12 -214 -23 26
LEU CA A 110 13 -363 -87 30 ASN ND2 A 117 14 -214 -33 30
LEU C A 110 15 -367 -91 36 SER N A 118 12 -203 8 27
LEU 0 A 110 15 -373 -83 35 75 SER CA A 118 11 -198 12 26
LEU CB A 110 13 -349 -81 28 SER C A 118 9 -202 3 29
LEU CG A 110 12 -345 -75 31 SER O A 118 8 -201 7 27
LEU CD1 A 110 12 -332 -67 32 SER CB A 118 11 -183 14 28
LEU CD2 A 110 11 -344 -86 29 SER OG A 118 12 -180 24 38
ASP N A 111 15 -364 -103 35 80 TYR N A 119 10 -205 -10 27
ASP CA A 111 16 -367 -108 36 TYR CA A 119 9 -208 -20 26
ASP C A 111 17 -359 -101 40 TYR C A 119 9 -222 -23 27
ASP 0 A 111 18 -365 -96 41 TYR O A 119 8 -226 -30 27
ASP CB A 111 16 -365 -124 38 TYR CB A 119 9 -200 -34 28
ASP CG A 111 18 -369 -130 56 85 TYR CG A 119 9 -185 -32 28
ASP OD1 A 111 18 -379 -126 55 TYR CD1 A 119 8 -178 -34 29
ASP OD2 A 111 18 -362 -140 67 TYR CD2 A 119 10 -178 -29 30
GLU N A 112 17 -346 -99 36 TYR CE1 A 119 8 -165 -33 28
GLU CA A 112 18 -338 -92 35 TYR CE2 A 119 10 -164 -27 31
GLU C A 112 17 -331 -81 38 90 TYR CZ A 119 9 -157 -29 38
GLU 0 A 112 16 -329 -83 36 TYR OH A 119 9 -144 -28 43
GLU CB A 112 19 -327 -101 36 VAL N A 120 10 -230 -19 24
GLU CG A 112 20 -332 -112 44 VAL CA A 120 10 -244 -22 23
GLU CD A 112 21 -339 -107 56 VAL C A 120 10 -251 -8 28
GLU OE1 A 112 21 -349 -113 68 95 VAL O A 120 11 -252 -4 28
GLU OE2 A 112 21 -335 -96 48 VAL CB A 120 11 -247 -32 26
PRO N A 113 18 -329 -69 36 VAL CGI A 120 11 -261 -36 26
PRO CA A 113 17 -324 -58 35 VAL CG2 A 120 11 -239 -45 26
PRO C A 113 17 -309 -60 36 THR N A 121 9 -255 -1 23
PRO 0 A 113 17 -302 -69 35 100 THR CA A 121 9 -260 13 22
PRO CB A 113 18 -324 -46 37 THR C A 121 8 -273 14 24
PRO CG A 113 19 -325 -53 42 THR O A 121 7 -274 10 24
PRO CD A 113 19 -332 -65 38 THR CB A 121 9 -250 22 30
LEU N A 114 16 -306 -53 31 THR OG1 A 121 9 -237 20 30
LEU CA A 114 15 -292 -52 29 105 THR CG2 A 121 9 -253 37 24
LEU C A 114 16 -285 -43 32 PRO N A 122 9 -283 21 22
LEU 0 A 114 17 -291 -34 30 PRO CA A 122 8 -296 23 21
LEU CB A 114 14 -292 -46 28 PRO C A 122 7 -294 32 25
LEU CG A 114 13 -298 -55 32 PRO O A 122 7 -285 40 24
LEU CD1 A 114 11 -300 -47 31 110 PRO CB A 122 9 -305 30 22
LEU CD2 A 114 12 -289 -67 32 PRO CG A 122 11 -300 27 27
VAL N A 115 16 -271 -44 29 PRO CD A 122 10 -285 27 23
VAL CA A 115 17 -263 -35 28 ILE N A 123 6 -302 30 22
VAL C A 115 16 -257 -26 31 ILE CA A 123 5 -303 39 20
VAL 0 A 115 15 -249 -30 29 115 ILE C A 123 5 -312 51 26
VAL CB A 115 17 -251 -43 31 ILE O A 123 6 -321 48 25
VAL CGI A 115 18 -240 -34 30 ILE CB A 123 3 -308 32 23
VAL CG2 A 115 19 -257 -50 31 ILE CGI A 123 2 -307 41 22
LEU N A 116 16 -261 -13 28 ILE CG2 A 123 4 -322 26 25
LEU CA A 116 15 -257 -4 27 120 ILE CD1 A 123 2 -292 44 22
LEU C A 116 15 -242 -1 30 CYS N A 124 5 -309 63 24
LEU 0 A 116 16 -238 1 29 CYS CA A 124 5 -317 74 24 CYS C A 124 4 -330 73 28 THR CG2 A 131 -2 -379 86 24
CYS 0 A 124 3 -329 68 27 ASN N A 132 -4 -387 119 27
CYS CB A 124 5 -310 87 25 ASN CA A 132 -5 -390 121 27
CYS SG A 124 6 -295 89 29 65 ASN C A 132 -6 -379 130 28
ILE N A 125 5 -341 78 25 ASN O A 132 -7 -374 127 29
ILE CA A 125 4 -354 78 24 ASN CB A 132 -6 -404 126 30
ILE C A 125 4 -360 92 27 ASN CG A 132 -7 -408 128 46
ILE 0 A 125 5 -363 96 26 ASN OD1 A 132 -7 -414 138 40
ILE CB A 125 4 -364 67 26 70 ASN ND2 A 132 -8 -406 118 34
ILE CGI A 125 4 -357 53 25 ILE N A 133 -5 -376 141 27
ILE CG2 A 125 4 -377 68 28 ILE CA A 133 -6 -365 151 26
ILE CD1 A 125 5 -366 40 24 ILE C A 133 -6 -352 143 30
ALA N A 126 3 -360 100 23 ILE O A 133 -7 -346 145 28
ALA CA A 126 3 -366 114 24 75 ILE CB A 133 -5 -364 163 29
ALA C A 126 3 -381 113 29 ILE CGI A 133 -5 -376 172 29
ALA 0 A 126 3 -386 102 28 ILE CG2 A 133 -5 -351 170 28
ALA CB A 126 2 -360 122 23 ILE CD1 A 133 -4 -377 183 30
ASP N A 127 3 -388 124 27 PHE N A 134 -5 -348 135 26
ASP CA A 127 3 -403 125 27 80 PHE CA A 134 -5 -336 127 24
ASP C A 127 2 -406 122 31 PHE C A 134 -6 -336 118 27
ASP 0 A 127 1 -396 121 29 PHE O A 134 -7 -326 117 27
ASP CB A 127 3 -409 138 29 PHE CB A 134 -4 -332 120 25
ASP CG A 127 3 -404 151 32 PHE CG A 134 -3 -330 129 25
ASP 0D1 A 127 2 -398 150 33 85 PHE CD1 A 134 -3 -325 142 28
ASP OD2 A 127 3 -407 162 39 PHE CD2 A 134 -1 -332 125 25
LYS N A 128 1 -419 122 29 PHE CE1 A 134 -2 -323 151 28
LYS CA A 128 -0 -423 119 30 PHE CE2 A 134 -0 -330 134 28
LYS C A 128 -1 -417 129 36 PHE CZ A 134 -0 -325 146 26
LYS 0 A 128 -2 -412 125 36 90 LEU N A 135 -7 -347 111 24
LYS CB A 128 -0 -438 119 34 LEU CA A 135 -8 -349 102 24
LYS CG A 128 -2 -444 116 50 LEU C A 135 -9 -347 110 31
LYS CD A 128 -2 -460 117 59 LEU O A 135 -10 -340 105 31
LYS CE A 128 -3 -466 111 72 LEU CB A 135 -8 -363 95 24
LYS NZ A 128 -3 -480 114 87 95 LEU CG A 135 -9 -364 85 29
GLU N A 129 -1 -417 142 33 LEU CD1 A 135 -9 -379 80 29
GLU CA A 129 -2 -412 153 33 LEU CD2 A 135 -9 -355 73 32
GLU C A 129 -2 -397 151 34 LYS N A 136 -9 -353 122 29
GLU 0 A 129 -3 -393 151 33 LYS CA A 136 -10 -352 131 28
GLU CB A 129 -1 -415 167 34 100 LYS C A 136 -11 -337 136 31
GLU CG A 129 -2 -412 177 45 LYS O A 136 -12 -335 139 30
GLU CD A 129 -2 -412 192 69 LYS CB A 136 -10 -361 144 32
GLU OE1 A 129 -3 -411 201 58 LYS CG A 136 -10 -376 141 39
GLU OE2 A 129 -1 -413 195 60 LYS CD A 136 -10 -383 154 50
TYR N A 130 -1 -389 150 28 105 LYS CE A 136 -10 -397 154 70
TYR CA A 130 -1 -375 149 26 LYS NZ A 136 -10 -406 147 85
TYR C A 130 -2 -370 135 31 PHE N A 137 -10 -328 135 29
TYR 0 A 130 -3 -361 136 31 PHE CA A 137 -10 -313 138 29
TYR CB A 130 -0 -367 153 25 PHE C A 137 -11 -309 129 32
TYR CG A 130 -0 -363 168 26 110 PHE O A 137 -12 -300 133 32
TYR CD1 A 130 1 -371 177 27 PHE CB A 137 -9 -304 135 29
TYR CD2 A 130 -1 -353 172 26 PHE CG A 137 -7 -305 144 30
TYR CE1 A 130 0 -368 191 27 PHE CD1 A 137 -7 -314 155 32
TYR CE2 A 130 -1 -349 185 27 PHE CD2 A 137 -6 -296 143 30
TYR CZ A 130 -0 -357 195 33 115 PHE CE1 A 137 -6 -315 164 33
TYR OH A 130 -0 -354 208 27 PHE CE2 A 137 -5 -297 152 32
THR N A 131 -1 -378 124 28 PHE CZ A 137 -5 -306 162 31
THR CA A 131 -2 -374 111 26 GLY N A 138 -11 -315 117 26
THR C A 131 -4 -376 112 30 GLY CA A 138 -12 -312 109 27
THR 0 A 131 -4 -368 107 29 120 GLY C A 138 -12 -301 99 33
THR CB A 131 -1 -383 100 24 GLY O A 138 -13 -298 92 32
THR OG1 A 131 -0 -380 99 26 SER N A 139 -11 -294 97 29 SER CA A 139 -11 -283 88 29 ARG CG A 147 -11 -282 -149 27
SER C A 139 -10 -283 81 33 ARG CD A 147 -13 -289 -155 37
SER 0 A 139 -9 -281 88 34 ARG NE A 147 -12 -299 -165 41
SER CB A 139 -11 -270 94 32 65 ARG CZ A 147 -12 -297 -178 57
SER OG A 139 -11 -260 84 44 ARG NH1 A 147 -12 -285 -183 46
GLY N A 140 -10 -285 68 30 ARG NH2 A 147 -11 -307 -186 43
GLY CA A 140 -8 -285 60 30 VAL N A 148 -12 -242 -125 25
GLY C A 140 -8 -276 48 35 VAL CA A 148 -12 -232 -116 25
GLY 0 A 140 -9 -271 44 35 70 VAL C A 148 -14 -232 -116 29
TYR N A 141 -7 -274 42 30 VAL 0 A 148 -14 -225 -107 28
TYR CA A 141 -7 -266 30 30 VAL CB A 148 -12 -218 -116 29
TYR C A 141 -7 -275 18 30 VAL CGI A 148 -10 -219 -113 29
TYR 0 A 141 -6 -283 19 29 VAL CG2 A 148 -12 -212 -130 28
TYR CB A 141 -6 -255 32 31 75 PHE N A 149 -14 -239 -125 28
TYR CG A 141 -6 -244 41 35 PHE CA A 149 -16 -241 -127 29
TYR CD1 A 141 -6 -244 55 39 PHE C A 149 -16 -256 -132 37
TYR CD2 A 141 -7 -233 36 36 PHE 0 A 149 -15 -260 -139 35
TYR CE1 A 141 -7 -235 63 41 PHE CB A 149 -16 -232 -138 29
TYR CE2 A 141 -8 -224 45 38 80 PHE CG A 149 -16 -217 -134 30
TYR CZ A 141 -7 -224 58 50 PHE CD1 A 149 -15 -208 -140 31
TYR OH A 141 -8 -214 67 57 PHE CD2 A 149 -17 -212 -124 32
VAL N A 142 -7 -273 7 26 PHE CE1 A 149 -15 -195 -136 32
VAL CA A 142 -7 -280 -5 25 PHE CE2 A 149 -17 -199 -120 35
VAL C A 142 -6 -269 -15 29 85 PHE CZ A 149 -16 -190 -126 33
VAL 0 A 142 -7 -257 -13 27 HIS N A 150 -17 -262 -129 40
VAL CB A 142 -8 -289 -12 29 HIS CA A 150 -17 -276 -134 42
VAL CGI A 142 -8 -300 -2 28 HIS C A 150 -17 -276 -150 44
VAL CG2 A 142 -9 -280 -15 29 HIS 0 A 150 -18 -267 -156 43
SER N A 143 -6 -273 -24 25 90 HIS CB A 150 -19 -280 -129 45
SER CA A 143 -5 -263 -34 23 HIS CG A 150 -19 -293 -136 50
SER C A 143 -5 -270 -47 26 HIS ND1 A 150 -19 -305 -132 53
SER 0 A 143 -4 -282 -48 23 HIS CD2 A 150 -20 -294 -145 53
SER CB A 143 -4 -255 -28 25 HIS CE1 A 150 -19 -314 -140 53
SER OG A 143 -3 -263 -22 26 95 HIS NE2 A 150 -20 -308 -148 54
GLY N A 144 -5 -261 -58 22 LYS N A 151 -16 -284 -156 41
GLY CA A 144 -4 -266 -71 22 LYS CA A 151 -16 -285 -170 41
GLY C A 144 -5 -257 -82 26 LYS C A 151 -16 -271 -176 43
GLY 0 A 144 -5 -246 -80 23 LYS 0 A 151 -16 -269 -188 43
TRP N A 145 -4 -260 -95 24 100 LYS CB A 151 -17 -290 -178 44
TRP CA A 145 -4 -253 -107 25 LYS CG A 151 -18 -304 -175 58
TRP C A 145 -5 -260 -115 29 LYS CD A 151 -19 -308 -183 72
TRP 0 A 145 -6 -258 -128 31 LYS CE A 151 -20 -321 -179 87
TRP CB A 145 -3 -253 -115 24 LYS NZ A 151 -21 -324 -185 94
TRP CG A 145 -2 -243 -109 26 105 GLY N A 152 -15 -263 -167 36
TRP CD1 A 145 -2 -230 -112 29 GLY CA A 152 -14 -250 -170 34
TRP CD2 A 145 -1 -246 -100 26 GLY C A 152 -13 -250 -172 35
TRP NE1 A 145 -1 -224 -105 29 GLY 0 A 152 -12 -260 -172 33
TRP CE2 A 145 -0 -234 -97 30 ARG N A 153 -12 -238 -173 29
TRP CE3 A 145 -1 -258 -93 27 110 ARG CA A 153 -11 -236 -175 29
TRP CZ2 A 145 1 -234 -88 29 ARG C A 153 -10 -239 -163 31
TRP CZ3 A 145 0 -257 -85 28 ARG 0 A 153 -11 -238 -152 29
TRP CH2 A 145 1 -245 -82 29 ARG CB A 153 -11 -222 -180 30
GLY N A 146 -6 -268 -109 26 SER N A 154 -9 -243 -165 29
GLY CA A 146 -7 -275 -116 26 115 SER CA A 154 -8 -245 -155 29
GLY C A 146 -9 -266 -120 32 SER C A 154 -7 -231 -149 34
GLY 0 A 146 -8 -253 -118 31 SER 0 A 154 -8 -221 -157 33
ARG N A 147 -10 -271 -126 29 SER CB A 154 -7 -250 -161 32
ARG CA A 147 -11 -264 -131 28 SER OG A 154 -7 -262 -169 48
ARG C A 147 -11 -255 -121 31 120 ALA N A 155 -7 -230 -137 32
ARG 0 A 147 -12 -259 -109 30 ALA CA A 155 -7 -218 -131 32
ARG CB A 147 -12 -273 -137 27 ALA C A 155 -5 -214 -136 36 ALA 0 A 155 -4 -223 -138 34 ARG NE A 162 -13 -231 65 63
ALA CB A 155 -7 -220 -115 33 ARG CZ A 162 -14 -240 68 71
LEU N A 156 -5 -201 -138 34 ARG NH1 A 162 -14 -251 75 45
LEU CA A 156 -4 -196 -142 34 65 ARG NH2 A 162 -16 -238 64 49
LEU C A 156 -3 -194 -128 33 VAL N A 163 -12 -266 34 26
LEU 0 A 156 -2 -198 -128 32 VAL CA A 163 -13 -276 33 26
LEU CB A 156 -4 -182 -149 36 VAL C A 163 -13 -283 46 31
LEU CG A 156 -4 -182 -163 43 VAL O A 163 -12 -288 53 29
LEU CD1 A 156 -5 -168 -168 45 70 VAL CB A 163 -13 -287 21 28
LEU CD2 A 156 -3 -190 -173 47 VAL CGI A 163 -13 -280 8 28
VAL N A 157 -4 -189 -118 29 VAL CG2 A 163 -11 -294 22 28
VAL CA A 157 -3 -186 -105 29 PRO N A 164 -14 -284 51 29
VAL C A 157 -4 -197 -95 30 PRO CA A 164 -15 -291 63 29
VAL 0 A 157 -5 -201 -95 29 75 PRO C A 164 -15 -306 61 31
VAL CB A 157 -3 -172 -100 33 PRO O A 164 -15 -310 51 32
VAL CGI A 157 -3 -169 -86 33 PRO CB A 164 -16 -284 68 31
VAL CG2 A 157 -3 -161 -110 32 PRO CG A 164 -17 -280 55 36
LEU N A 158 -3 -202 -87 25 PRO CD A 164 -16 -279 44 31
LEU CA A 158 -3 -213 -77 24 80 LEU N A 165 -15 -313 71 29
LEU C A 158 -4 -209 -68 28 LEU CA A 165 -15 -328 71 28
LEU 0 A 158 -4 -198 -63 27 LEU C A 165 -16 -331 71 36
LEU CB A 158 -2 -215 -68 23 LEU O A 165 -17 -324 78 35
LEU CG A 158 -2 -225 -56 26 LEU CB A 165 -14 -334 83 27
LEU CD1 A 158 -2 -239 -62 26 85 LEU CG A 165 -14 -350 84 31
LEU CD2 A 158 -1 -226 -47 26 LEU CD1 A 165 -13 -356 74 32
GLN N A 159 -5 -218 -68 25 LEU CD2 A 165 -14 -354 98 31
GLN CA A 159 -6 -216 -60 24 VAL N A 166 -17 -342 64 36
GLN C A 159 -6 -224 -47 27 VAL CA A 166 -18 -346 63 37
GLN 0 A 159 -6 -235 -47 25 90 VAL C A 166 -18 -360 70 44
GLN CB A 159 -8 -221 -68 24 VAL O A 166 -17 -368 67 43
GLN CG A 159 -8 -214 -81 25 VAL CB A 166 -19 -346 48 40
GLN CD A 159 -8 -199 -79 29 VAL CGI A 166 -20 -353 46 40
GLN 0E1 A 159 -7 -191 -82 34 VAL CG2 A 166 -19 -332 42 40
GLN NE2 A 159 -9 -196 -73 20 95 ASP N A 167 -19 -362 78 44
TYR N A 160 -7 -219 -37 24 ASP CA A 167 -19 -374 85 46
TYR CA A 160 -7 -226 -24 25 ASP C A 167 -20 -386 75 52
TYR C A 160 -8 -225 -18 28 ASP O A 167 -20 -384 64 51
TYR 0 A 160 -9 -215 -20 28 ASP CB A 167 -21 -373 95 48
TYR CB A 160 -6 -222 -14 27 100 ASP CG A 167 -22 -374 89 62
TYR CG A 160 -6 -209 -7 29 ASP OD1 A 167 -22 -385 86 63
TYR CD1 A 160 -7 -208 5 31 ASP OD2 A 167 -23 -363 86 70
TYR CD2 A 160 -6 -197 -13 29 ARG N A 168 -19 -398 80 52
TYR CE1 A 160 -7 -196 11 32 ARG CA A 168 -19 -410 72 53
TYR CE2 A 160 -6 -185 -7 30 105 ARG C A 168 -21 -414 65 58
TYR CZ A 160 -7 -184 5 39 ARG O A 168 -21 -418 54 58
TYR OH A 160 -7 -172 11 41 ARG CB A 168 -19 -422 80 58
LEU N A 161 -9 -235 -10 26 ARG CG A 168 -18 -435 72 74
LEU CA A 161 -10 -236 -4 25 ARG CD A 168 -18 -447 81 89
LEU C A 161 -10 -243 9 31 110 ARG NE A 168 -17 -458 74 0
LEU 0 A 161 -9 -254 10 30 ARG CZ A 168 -18 -468 70 0
LEU CB A 161 -11 -243 -14 25 ARG NH1 A 168 -19 -469 71 98
LEU CG A 161 -12 -245 -10 31 ARG NH2 A 168 -18 -478 63 0
LEU CD1 A 161 -13 -232 -9 31 ALA N A 169 -22 -413 73 53
LEU CD2 A 161 -13 -255 -19 33 115 ALA CA A 169 -23 -417 68 53
ARG N A 162 -11 -238 19 27 ALA C A 169 -23 -408 56 56
ARG CA A 162 -11 -245 32 28 ALA O A 169 -24 -412 46 55
ARG C A 162 -12 -254 31 31 ALA CB A 169 -24 -417 79 54
ARG 0 A 162 -13 -249 26 31 THR N A 170 -23 -394 58 52
ARG CB A 162 -11 -234 44 30 120 THR CA A 170 -23 -384 48 51
ARG CG A 162 -11 -240 58 36 THR C A 170 -23 -387 36 55
ARG CD A 162 -12 -232 68 48 THR O A 170 -23 -387 24 54 THR CB A 170 -23 -370 54 58 THR N A 178 -19 -469 -30 75
THR 0G1 A 170 -24 -370 66 58 THR CA A 178 -18 -473 -16 74
THR CG2 A 170 -24 -359 44 56 THR C A 178 -17 -465 -11 73
CYS N A 171 -21 -389 38 53 65 THR 0 A 178 -16 -465 -18 72
CYS CA A 171 -20 -393 29 54 THR CB A 178 -18 -488 -14 86
CYS C A 171 -21 -405 20 65 THR OG1 A 178 -19 -494 -21 88
CYS 0 A 171 -20 -405 8 66 THR CG2 A 178 -18 -492 0 84
CYS CB A 171 -19 -395 36 53 ILE N A 179 -17 -459 1 66
CYS SG A 171 -17 -400 26 56 70 ILE CA A 179 -16 -452 7 64
LEU N A 172 -21 -414 26 64 ILE C A 179 -16 -460 18 63
LEU CA A 172 -22 -426 19 65 ILE O A 179 -16 -463 28 63
LEU C A 172 -23 -424 11 69 ILE CB A 179 -17 -438 13 67
LEU 0 A 172 -23 -429 -0 69 ILE CGI A 179 -18 -430 3 67
LEU CB A 172 -22 -438 29 65 75 ILE CG2 A 179 -15 -430 18 68
LEU CG A 172 -21 -449 29 70 ILE CD1 A 179 -17 -426 -11 75
LEU CD1 A 172 -20 -443 36 71 TYR N A 180 -14 -465 15 55
LEU CD2 A 172 -21 -461 36 74 TYR CA A 180 -14 -473 25 53
ARG N A 173 -24 -417 17 67 TYR C A 180 -13 -464 36 55
ARG CA A 173 -25 -414 11 68 80 TYR O A 180 -13 -452 35 55
ARG C A 173 -25 -405 -1 74 TYR CB A 180 -13 -482 19 54
ARG 0 A 173 -26 -405 -10 73 TYR CG A 180 -13 -492 9 56
ARG CB A 173 -26 -408 21 67 TYR CD1 A 180 -13 -494 -4 59
ARG CG A 173 -27 -418 33 78 TYR CD2 A 180 -14 -499 11 57
ARG CD A 173 -28 -413 42 87 85 TYR CE1 A 180 -13 -503 -13 60
ARG NE A 173 -28 -398 44 97 TYR CE2 A 180 -15 -507 2 58
ARG CZ A 173 -27 -392 53 0 TYR CZ A 180 -14 -509 -10 68
ARG NH1 A 173 -27 -398 61 0 TYR OH A 180 -15 -518 -19 71
ARG NH2 A 173 -27 -378 54 97 ASN N A 181 -12 -470 47 50
SER N A 174 -24 -397 -3 72 90 ASN CA A 181 -12 -464 58 49
SER CA A 174 -24 -388 -14 73 ASN C A 181 -11 -456 55 51
SER C A 174 -24 -395 -27 79 ASN O A 181 -10 -448 63 51
SER 0 A 174 -24 -389 -37 78 ASN CB A 181 -11 -475 69 51
SER CB A 174 -23 -378 -10 75 ASN CG A 181 -13 -480 77 90
SER OG A 174 -22 -383 -8 82 95 ASN OD1 A 181 -13 -479 90 92
THR N A 175 -23 -407 -26 76 ASN ND2 A 181 -14 -484 71 83
THR CA A 175 -23 -414 -37 77 ASN N A 182 -10 -460 44 43
THR C A 175 -23 -429 -39 83 ASN CA A 182 -9 -453 40 41
THR 0 A 175 -23 -435 -29 82 ASN C A 182 -9 -440 31 41
THR CB A 175 -21 -414 -37 86 100 ASN O A 182 -8 -436 23 40
THR OG1 A 175 -20 -420 -49 88 ASN CB A 182 -8 -463 32 41
THR CG2 A 175 -20 -420 -24 82 ASN CG A 182 -8 -470 21 60
LYS N A 176 -23 -434 -51 81 ASN OD1 A 182 -10 -468 17 53
LYS CA A 176 -23 -447 -54 81 ASN ND2 A 182 -8 -480 16 53
LYS C A 176 -22 -456 -52 86 105 MET N A 183 -10 -435 31 37
LYS 0 A 176 -22 -469 -49 86 MET CA A 183 -11 -424 24 38
LYS CB A 176 -24 -448 -69 84 MET C A 183 -12 -415 34 38
LYS CG A 176 -23 -443 -80 99 MET O A 183 -12 -421 44 37
LYS CD A 176 -23 -444 -94 0 MET CB A 183 -12 -428 13 42
LYS CE A 176 -22 -439 -104 0 110 MET CG A 183 -11 -436 2 48
LYS NZ A 176 -23 -440 -118 0 MET SD A 183 -12 -449 -5 56
PHE N A 177 -21 -450 -51 82 MET CE A 183 -13 -439 -12 53
PHE CA A 177 -20 -457 -48 81 PHE N A 184 -12 -403 31 33
PHE C A 177 -20 -459 -34 82 PHE CA A 184 -13 -394 38 31
PHE 0 A 177 -20 -453 -25 81 115 PHE C A 184 -13 -384 28 37
PHE CB A 177 -19 -447 -54 84 PHE O A 184 -13 -382 17 36
PHE CG A 177 -17 -454 -57 86 PHE CB A 184 -12 -386 50 31
PHE CD1 A 177 -17 -461 -69 89 PHE CG A 184 -11 -375 45 32
PHE CD2 A 177 -16 -454 -48 88 PHE CD1 A 184 -11 -362 43 33
PHE CE1 A 177 -16 -467 -72 90 120 PHE CD2 A 184 -10 -378 43 31
PHE CE2 A 177 -15 -461 -51 91 PHE CE1 A 184 -10 -352 40 33
PHE CZ A 177 -15 -467 -63 89 PHE CE2 A 184 -9 -369 39 34 PHE CZ A 184 -9 -356 37 31 ARG NE A 193 -18 -227 1 45
CYS N A 185 -14 -378 33 38 ARG CZ A 193 -19 -222 13 53
CYS CA A 185 -15 -368 25 42 ARG NH1 A 193 -18 -215 20 38
CYS C A 185 -15 -354 31 37 65 ARG NH2 A 193 -20 -224 18 37
CYS 0 A 185 -15 -353 44 35 ASP N A 194 -15 -268 -42 30
CYS CB A 185 -17 -371 25 47 ASP CA A 194 -15 -282 -43 29
CYS SG A 185 -17 -384 13 54 ASP C A 194 -13 -282 -50 32
ALA N A 186 -15 -344 23 31 ASP 0 A 194 -13 -273 -58 30
ALA CA A 186 -15 -330 27 30 70 ASP CB A 194 -16 -291 -51 31
ALA C A 186 -15 -321 17 34 ASP CG A 194 -16 -306 -49 36
ALA 0 A 186 -15 -325 5 32 ASP OD1 A 194 -15 -311 -41 34
ALA CB A 186 -13 -326 29 30 ASP OD2 A 194 -16 -313 -56 41
GLY N A 187 -16 -311 22 32 SER N A 195 -13 -293 -48 29
GLY CA A 187 -17 -301 13 33 75 SER CA A 195 -12 -295 -56 30
GLY C A 187 -18 -296 19 39 SER C A 195 -12 -301 -69 35
GLY 0 A 187 -18 -296 31 39 SER O A 195 -13 -306 -70 33
PHE N A 188 -19 -291 10 37 SER CB A 195 -11 -305 -49 31
PHE CA A 188 -20 -284 13 38 SER OG A 195 -11 -317 -45 37
PHE C A 188 -21 -291 6 48 80 CYS N A 196 -11 -299 -81 36
PHE 0 A 188 -21 -296 -5 49 CYS CA A 196 -12 -303 -94 38
PHE CB A 188 -20 -269 10 38 CYS C A 196 -11 -310 -102 36
PHE CG A 188 -19 -262 16 38 CYS O A 196 -10 -313 -97 33
PHE CD1 A 188 -18 -262 11 40 CYS CB A 196 -12 -291 -101 41
PHE CD2 A 188 -19 -256 28 38 85 CYS SG A 196 -14 -295 -114 48
PHE CE1 A 188 -17 -256 17 39 GLN N A 197 -11 -314 -115 32
PHE CE2 A 188 -18 -249 35 40 GLN CA A 197 -10 -320 -124 31
PHE CZ A 188 -17 -249 29 38 GLN C A 197 -9 -312 -126 33
HIS N A 189 -22 -292 13 50 GLN O A 197 -9 -299 -128 32
HIS CA A 189 -24 -298 7 52 90 GLN CB A 197 -11 -323 -137 33
HIS C A 189 -24 -288 -3 56 GLN CG A 197 -10 -333 -147 36
HIS 0 A 189 -25 -293 -14 56 GLN CD A 197 -11 -336 -158 49
HIS CB A 189 -25 -300 18 54 GLN OE1 A 197 -12 -327 -165 41
HIS CG A 189 -26 -308 13 59 GLN NE2 A 197 -11 -349 -161 35
HIS ND1 A 189 -26 -321 9 61 95 GLY N A 198 -8 -318 -125 30
HIS CD2 A 189 -27 -303 11 61 GLY CA A 198 -7 -310 -125 29
HIS CE1 A 189 -27 -324 5 61 GLY C A 198 -6 -308 -111 30
HIS NE2 A 189 -28 -314 6 61 GLY O A 198 -5 -305 -110 30
GLU N A 190 -24 -275 -1 52 ASP N A 199 -7 -310 -101 27
GLU CA A 190 -25 -264 -10 51 100 ASP CA A 199 -6 -308 -87 26
GLU C A 190 -24 -264 -24 53 ASP C A 199 -6 -321 -81 28
GLU 0 A 190 -25 -258 -33 51 ASP O A 199 -5 -321 -71 27
GLU CB A 190 -25 -251 -3 53 ASP CB A 199 -7 -302 -78 26
GLU CG A 190 -23 -247 3 68 ASP CG A 199 -8 -288 -82 30
GLU CD A 190 -23 -232 5 0 105 ASP OD1 A 199 -7 -280 -84 30
GLU 0E1 A 190 -24 -225 10 0 ASP OD2 A 199 -9 -285 -82 28
GLU OE2 A 190 -22 -228 2 95 SER N A 200 -6 -332 -87 24
GLY N A 191 -23 -270 -26 48 SER CA A 200 -6 -346 -82 24
GLY CA A 191 -22 -269 -39 47 SER C A 200 -5 -348 -80 26
GLY C A 191 -22 -256 -41 48 110 SER O A 200 -4 -342 -87 25
GLY 0 A 191 -22 -247 -33 48 SER CB A 200 -6 -356 -93 28
GLY N A 192 -21 -255 -52 40 SER OG A 200 -8 -357 -94 32
GLY CA A 192 -20 -243 -56 38 GLY N A 201 -4 -355 -69 22
GLY C A 192 -19 -242 -50 37 GLY CA A 201 -3 -356 -65 22
GLY 0 A 192 -18 -233 -52 34 115 GLY C A 201 -2 -346 -55 26
ARG N A 193 -18 -252 -41 32 GLY O A 201 -1 -348 -48 24
ARG CA A 193 -17 -252 -34 32 GLY N A 202 -3 -334 -56 26
ARG C A 193 -16 -266 -34 34 GLY CA A 202 -3 -323 -47 25
ARG 0 A 193 -17 -274 -26 34 GLY C A 202 -3 -325 -33 27
ARG CB A 193 -17 -246 -20 32 120 GLY O A 202 -4 -335 -29 24
ARG CG A 193 -17 -230 -20 41 PRO N A 203 -2 -316 -24 25
ARG CD A 193 -17 -225 -5 45 PRO CA A 203 -3 -319 -10 24 PRO C A 203 -4 -314 -3 27 THR O A 211 1 -270 108 31
PRO 0 A 203 -5 -304 -8 25 THR CB A 211 3 -262 117 27
PRO CB A 203 -1 -310 -4 25 THR OG1 A 211 4 -253 124 29
PRO CG A 203 -1 -299 -13 30 65 THR CG2 A 211 4 -272 110 24
PRO CD A 203 -2 -304 -27 26 SER N A 212 2 -265 88 25
HIS N A 204 -4 -321 8 23 SER CA A 212 1 -273 80 23
HIS CA A 204 -5 -317 17 22 SER C A 212 1 -288 79 27
HIS C A 204 -4 -315 30 25 SER O A 212 2 -290 77 27
HIS 0 A 204 -4 -324 34 25 70 SER CB A 212 0 -267 66 26
HIS CB A 204 -6 -327 20 22 SER OG A 212 -0 -255 68 28
HIS CG A 204 -7 -324 31 25 PHE N A 213 0 -297 81 24
HIS ND1 A 204 -7 -324 44 26 PHE CA A 213 1 -311 80 22
HIS CD2 A 204 -9 -320 30 26 PHE C A 213 -0 -318 69 24
HIS CE1 A 204 -8 -321 51 25 75 PHE O A 213 -1 -314 68 21
HIS NE2 A 204 -9 -318 43 26 PHE CB A 213 0 -318 94 24
VAL N A 205 -4 -302 35 22 PHE CG A 213 1 -315 105 25
VAL CA A 205 -3 -300 47 22 PHE CD1 A 213 1 -304 112 26
VAL C A 205 -4 -294 59 27 PHE CD2 A 213 2 -325 107 26
VAL 0 A 205 -5 -288 57 27 80 PHE CE1 A 213 2 -301 122 26
VAL CB A 205 -2 -292 44 24 PHE CE2 A 213 3 -322 116 27
VAL CGI A 205 -1 -298 32 23 PHE CZ A 213 3 -311 124 24
VAL CG2 A 205 -3 -277 41 24 LEU N A 214 0 -327 62 21
THR N A 206 -4 -297 71 25 LEU CA A 214 -1 -334 51 21
THR CA A 206 -4 -292 83 25 85 LEU C A 214 -2 -344 58 28
THR C A 206 -3 -283 90 29 LEU O A 214 -1 -352 66 28
THR 0 A 206 -2 -287 92 28 LEU CB A 214 1 -341 42 21
THR CB A 206 -5 -303 92 28 LEU CG A 214 -0 -347 29 25
THR OG1 A 206 -6 -311 84 29 LEU CD1 A 214 -1 -337 19 25
THR CG2 A 206 -6 -298 105 24 90 LEU CD2 A 214 1 -357 23 28
GLU N A 207 -4 -271 93 28 THR N A 215 -3 -342 55 25
GLU CA A 207 -3 -261 100 29 THR CA A 215 -4 -350 61 25
GLU C A 207 -3 -263 115 34 THR C A 215 -5 -358 50 29
GLU 0 A 207 -4 -264 121 34 THR O A 215 -5 -368 53 27
GLU CB A 207 -3 -247 97 30 95 THR CB A 215 -5 -342 70 29
GLU CG A 207 -3 -240 85 41 THR OG1 A 215 -5 -329 64 23
GLU CD A 207 -3 -227 80 62 THR CG2 A 215 -4 -340 84 27
GLU OE1 A 207 -4 -221 89 51 GLY N A 216 -4 -354 38 27
GLU OE2 A 207 -3 -224 68 57 GLY CA A 216 -5 -361 26 26
VAL N A 208 -2 -265 121 29 100 GLY C A 216 -4 -358 13 28
VAL CA A 208 -2 -268 135 29 GLY O A 216 -4 -349 11 26
VAL C A 208 -1 -257 140 33 ILE N A 217 -5 -366 3 24
VAL 0 A 208 0 -258 139 30 ILE CA A 217 -4 -365 -11 25
VAL CB A 208 -1 -282 138 33 ILE C A 217 -6 -363 -19 29
VAL CGI A 208 -1 -285 153 33 105 ILE O A 217 -7 -371 -17 27
VAL CG2 A 208 -2 -293 130 32 ILE CB A 217 -4 -377 -16 27
GLU N A 209 -1 -247 146 33 ILE CGI A 217 -2 -381 -8 28
GLU CA A 209 -1 -236 152 33 ILE CG2 A 217 -3 -375 -31 26
GLU C A 209 0 -229 142 36 ILE CD1 A 217 -1 -371 -7 33
GLU 0 A 209 2 -227 147 35 110 ILE N A 218 -6 -353 -28 26
GLU CB A 209 -0 -240 165 35 ILE CA A 218 -7 -351 -36 24
GLU CG A 209 -1 -242 177 48 ILE C A 218 -7 -364 -46 31
GLU CD A 209 -2 -230 181 74 ILE O A 218 -6 -367 -52 30
GLU OE1 A 209 -1 -220 185 83 ILE CB A 218 -7 -338 -44 26
GLU OE2 A 209 -3 -230 181 64 115 ILE CGI A 218 -7 -326 -34 25
GLY N A 210 0 -227 130 32 ILE CG2 A 218 -8 -336 -53 24
GLY CA A 210 1 -221 120 31 ILE CD1 A 218 -6 -311 -41 30
GLY C A 210 2 -231 112 33 SER N A 219 -8 -371 -46 31
GLY 0 A 210 3 -227 105 33 SER CA A 219 -8 -383 -54 33
THR N A 211 2 -244 115 27 120 SER C A 219 -9 -380 -67 39
THR CA A 211 2 -254 108 26 SER O A 219 -9 -369 -73 36
THR C A 211 1 -264 101 29 SER CB A 219 -9 -394 -46 36 SER OG A 219 -9 -406 -53 40 LYS CG A 227 -27 -291 -36 70
TRP N A 220 -10 -390 -72 40 LYS CD A 227 -28 -278 -28 81
TRP CA A 220 -11 -388 -84 42 LYS CE A 227 -28 -281 -16 85
TRP C A 220 -12 -380 -81 46 65 LYS NZ A 227 -29 -269 -7 87
TRP 0 A 220 -12 -376 -69 45 GLY N A 228 -25 -316 -31 46
TRP CB A 220 -11 -401 -90 42 GLY CA A 228 -25 -330 -26 45
TRP CG A 220 -10 -409 -98 44 GLY C A 228 -24 -339 -28 49
TRP CD1 A 220 -9 -419 -93 47 GLY 0 A 228 -24 -351 -23 49
TRP CD2 A 220 -10 -408 -112 45 70 LYS N A 229 -23 -335 -34 45
TRP NE1 A 220 -9 -424 -104 48 LYS CA A 229 -22 -343 -36 45
TRP CE2 A 220 -9 -418 -115 49 LYS C A 229 -21 -336 -28 47
TRP CE3 A 220 -11 -401 -122 46 LYS 0 A 229 -21 -324 -25 46
TRP CZ2 A 220 -9 -420 -129 49 LYS CB A 229 -22 -344 -51 48
TRP CZ3 A 220 -10 -403 -135 49 75 LYS CG A 229 -23 -350 -60 67
TRP CH2 A 220 -9 -412 -138 49 LYS CD A 229 -23 -366 -61 81
GLY N A 221 -13 -378 -90 44 LYS CE A 229 -24 -372 -67 92
GLY CA A 221 -14 -372 -88 45 LYS NZ A 229 -24 -387 -68 0
GLY C A 221 -15 -375 -100 52 TYR N A 230 -20 -344 -25 40
GLY 0 A 221 -15 -381 -110 52 80 TYR CA A 230 -19 -339 -17 39
GLU N A 222 -16 -371 -98 53 TYR C A 230 -17 -345 -24 40
GLU CA A 222 -17 -374 -108 55 TYR 0 A 230 -17 -354 -32 40
GLU C A 222 -18 -361 -114 61 TYR CB A 230 -19 -345 -3 40
GLU 0 A 222 -18 -359 -126 61 TYR CG A 230 -20 -341 5 40
GLU CB A 222 -19 -381 -101 57 85 TYR CD1 A 230 -20 -329 11 41
GLU CG A 222 -18 -390 -89 70 TYR CD2 A 230 -21 -350 6 41
GLU CD A 222 -19 -389 -78 99 TYR CE1 A 230 -21 -326 18 43
GLU OE1 A 222 -19 -387 -66 93 TYR CE2 A 230 -22 -347 13 42
GLU OE2 A 222 -20 -392 -80 95 TYR CZ A 230 -22 -334 19 51
GLU N A 223 -18 -352 -106 57 90 TYR OH A 230 -23 -331 26 56
GLU CA A 223 -19 -339 -111 57 GLY N A 231 -16 -339 -20 34
GLU C A 223 -19 -329 -99 58 GLY CA A 231 -15 -344 -26 32
GLU 0 A 223 -19 -330 -89 60 GLY C A 231 -14 -357 -18 37
GLU CB A 223 -20 -339 -113 58 GLY O A 231 -15 -358 -6 35
GLU CG A 223 -21 -346 -126 75 95 ILE N A 232 -14 -366 -25 36
GLU CD A 223 -22 -344 -128 0 ILE CA A 232 -13 -378 -19 37
GLU OE1 A 223 -23 -351 -121 0 ILE C A 232 -12 -377 -19 38
GLU OE2 A 223 -23 -336 -137 98 ILE O A 232 -11 -373 -29 38
CYS N A 224 -18 -322 -101 50 ILE CB A 232 -14 -391 -28 41
CYS CA A 224 -17 -313 -91 48 100 ILE CGI A 232 -15 -392 -32 42
CYS C A 224 -18 -301 -88 50 ILE CG2 A 232 -13 -404 -20 41
CYS 0 A 224 -19 -297 -97 49 ILE CD1 A 232 -16 -390 -21 55
CYS CB A 224 -16 -308 -94 47 TYR N A 233 -11 -379 -7 31
CYS SG A 224 -16 -294 -105 49 TYR CA A 233 -10 -377 -4 30
ALA N A 225 -18 -297 -75 44 105 TYR C A 233 -9 -390 2 34
ALA CA A 225 -19 -286 -70 44 TYR O A 233 -10 -397 8 35
ALA C A 225 -20 -287 -71 50 TYR CB A 233 -10 -366 6 30
ALA 0 A 225 -21 -277 -69 49 TYR CG A 233 -10 -352 0 32
ALA CB A 225 -18 -273 -75 45 TYR CD1 A 233 -11 -348 2 33
MET N A 226 -21 -299 -74 48 110 TYR CD2 A 233 -9 -344 -7 32
MET CA A 226 -22 -301 -75 49 TYR CE1 A 233 -12 -337 -3 33
MET C A 226 -23 -303 -61 51 TYR CE2 A 233 -10 -332 -12 32
MET 0 A 226 -22 -309 -52 49 TYR CZ A 233 -11 -328 -10 38
MET CB A 226 -23 -314 -83 53 TYR OH A 233 -12 -317 -16 36
MET CG A 226 -22 -313 -98 58 115 THR N A 234 -8 -392 -2 29
MET SD A 226 -23 -300 -107 65 THR CA A 234 -7 -404 4 30
MET CE A 226 -23 -304 -124 62 THR C A 234 -7 -400 18 33
LYS N A 227 -24 -297 -59 47 THR O A 234 -6 -389 19 31
LYS CA A 227 -25 -297 -47 47 THR CB A 234 -6 -407 -6 35
LYS C A 227 -25 -312 -44 50 120 THR OG1 A 234 -6 -411 -18 35
LYS 0 A 227 -26 -320 -53 49 THR CG2 A 234 -5 -417 -0 31
LYS CB A 227 -26 -289 -48 51 LYS N A 235 -7 -408 28 29 LYS CA A 235 -7 -407 42 29 TRP C A 242 6 -450 30 33
LYS C A 235 -5 -409 42 33 TRP 0 A 242 7 -452 24 33
LYS 0 A 235 -5 -421 41 34 TRP CB A 242 4 -467 29 32
LYS CB A 235 -7 -416 51 32 65 TRP CG A 242 4 -469 14 34
LYS CG A 235 -8 -411 58 41 TRP CD1 A 242 5 -479 8 38
LYS CD A 235 -9 -420 70 41 TRP CD2 A 242 4 -459 3 34
LYS CE A 235 -10 -417 75 45 TRP NE1 A 242 5 -477 -6 37
LYS NZ A 235 -11 -429 83 42 TRP CE2 A 242 4 -465 -9 38
VAL N A 236 -4 -399 44 28 70 TRP CE3 A 242 3 -446 3 35
VAL CA A 236 -3 -400 45 27 TRP CZ2 A 242 4 -458 -21 37
VAL C A 236 -2 -408 57 29 TRP CZ3 A 242 3 -440 -9 36
VAL 0 A 236 -1 -415 56 25 TRP CH2 A 242 3 -446 -21 36
VAL CB A 236 -2 -386 43 29 ILE N A 243 5 -438 33 26
VAL CGI A 236 -1 -385 49 27 75 ILE CA A 243 6 -425 28 24
VAL CG2 A 236 -2 -381 29 29 ILE C A 243 7 -423 34 32
SER N A 237 -3 -407 69 26 ILE 0 A 243 8 -421 26 31
SER CA A 237 -3 -414 81 27 ILE CB A 243 5 -413 30 26
SER C A 237 -2 -429 79 32 ILE CGI A 243 4 -414 22 24
SER 0 A 237 -1 -434 84 29 80 ILE CG2 A 243 6 -400 27 25
SER CB A 237 -4 -413 91 29 ILE CD1 A 243 2 -403 26 31
SER OG A 237 -5 -419 87 35 LYS N A 244 7 -424 47 31
ARG N A 238 -3 -435 70 30 LYS CA A 244 9 -421 54 32
ARG CA A 238 -3 -449 66 31 LYS C A 244 10 -431 51 39
ARG C A 238 -2 -453 58 34 85 LYS 0 A 244 11 -427 48 39
ARG 0 A 238 -1 -464 58 33 LYS CB A 244 8 -421 70 35
ARG CB A 238 -4 -454 59 36 LYS CG A 244 7 -411 74 48
ARG CG A 238 -4 -464 48 57 LYS CD A 244 8 -399 81 55
ARG CD A 238 -4 -479 52 73 LYS CE A 244 7 -392 88 56
ARG NE A 238 -4 -488 41 83 90 LYS NZ A 244 7 -383 99 65
ARG CZ A 238 -3 -493 36 97 GLU N A 245 9 -444 50 39
ARG NH1 A 238 -2 -490 42 84 GLU CA A 245 10 -455 46 40
ARG NH2 A 238 -3 -501 26 81 GLU C A 245 11 -453 31 42
TYR N A 239 -1 -442 52 27 GLU 0 A 245 12 -453 30 43
TYR CA A 239 0 -444 43 26 95 GLU CB A 245 10 -469 48 42
TYR C A 239 1 -438 48 31 GLU CG A 245 11 -481 45 63
TYR 0 A 239 2 -439 42 30 GLU CD A 245 12 -482 54 93
TYR CB A 239 -0 -438 29 26 GLU OE1 A 245 12 -478 66 96
TYR CG A 239 -1 -445 23 28 GLU OE2 A 245 13 -487 49 79
TYR CD1 A 239 -1 -458 19 31 100 LYS N A 246 10 -451 21 37
TYR CD2 A 239 -3 -439 23 28 LYS CA A 246 10 -449 7 36
TYR CE1 A 239 -2 -465 14 31 LYS C A 246 11 -436 5 40
TYR CE2 A 239 -4 -445 18 30 LYS O A 246 12 -436 -4 39
TYR CZ A 239 -4 -458 14 34 LYS CB A 246 9 -450 -2 38
TYR OH A 239 -5 -465 9 34 105 LYS CG A 246 8 -463 -1 47
VAL N A 240 1 -431 60 30 LYS CD A 246 9 -475 -9 56
VAL CA A 240 2 -424 67 31 LYS CE A 246 8 -487 -7 68
VAL C A 240 4 -432 67 35 LYS NZ A 246 9 -499 -2 77
VAL 0 A 240 5 -427 63 34 THR N A 247 11 -425 12 36
VAL CB A 240 2 -418 80 37 110 THR CA A 247 11 -412 10 34
VAL CGI A 240 3 -416 89 37 THR C A 247 13 -408 18 39
VAL CG2 A 240 1 -405 78 36 THR O A 247 13 -397 16 38
ASN N A 241 4 -445 73 33 THR CB A 247 10 -401 10 33
ASN CA A 241 5 -453 74 33 THR OG1 A 247 10 -399 24 34
ASN C A 241 6 -457 60 36 115 THR CG2 A 247 9 -403 1 31
ASN 0 A 241 7 -456 58 36 LYS N A 248 13 -416 28 38
ASN CB A 241 5 -466 82 38 LYS CA A 248 14 -414 37 38
ASN CG A 241 4 -463 96 67 LYS C A 248 15 -410 29 43
ASN OD1 A 241 4 -453 102 64 LYS O A 248 16 -417 20 43
ASN ND2 A 241 3 -472 101 64 120 LYS CB A 248 14 -426 46 43
TRP N A 242 5 -460 51 32 LYS CG A 248 14 -424 61 58
TRP CA A 242 5 -463 37 32 LYS CD A 248 14 -436 69 72 LYS CE A 248 14 -438 82 91 ASN CG I3 92 -2 -322 216 32
LYS NZ A 248 12 -444 79 0 ASN OD1 I 3 92 -2 -334 216 30
LEU N A 249 16 -400 33 39 ASN ND2 I 3 92 -1 -315 211 28
LEU CA A 249 17 -395 26 40 65 GLY N I 3 93 -2 -315 261 31
LEU C A 249 19 -399 32 46 GLY CA I 3 93 -1 -313 272 31
LEU 0 A 249 19 -398 44 47 GLY C I 3 93 -0 -299 271 34
LEU CB A 249 17 -380 22 40 GLY 0 I 3 93 1 -297 276 32
LEU CG A 249 16 -375 12 45 ARG N I 3 94 -1 -290 263 31
LEU CD1 A 249 16 -360 10 44 70 ARG CA I 3 94 -1 -276 260 31
LEU CD2 A 249 16 -382 -2 48 ARG C I 3 94 0 -277 250 33
MET N B 86 -1 -316 328 57 ARG 0 I 3 94 1 -266 248 32
MET CA B 86 -2 -326 331 56 ARG CB I 3 94 -0 -267 273 34
MET C B 86 -2 -339 322 53 ARG CG I 3 94 -1 -268 284 45
MET 0 B 86 -1 -348 326 52 75 ARG CD I 3 94 -3 -259 281 60
MET CB B 86 -3 -321 333 60 ARG NE I 3 94 -3 -258 293 72
MET CG B 86 -4 -314 346 65 ARG CZ I 3 94 -4 -246 297 82
MET SD B 86 -5 -314 351 71 ARG NH1 I 3 94 -4 -235 291 58
MET CE B 86 -6 -331 357 67 ARG NH2 I 3 94 -5 -246 308 72
THR N B 87 -3 -339 311 44 80 CYS N I 3 95 1 -289 245 29
THR CA B 87 -3 -351 302 41 CYS CA I 3 95 2 -291 234 28
THR C B 87 -3 -346 287 39 CYS C I 3 95 1 -285 221 31
THR 0 B 87 -3 -335 284 37 CYS 0 I 3 95 0 -288 217 31
THR CB B 87 -4 -360 304 48 CYS CB I 3 95 2 -305 233 27
THR 0G1 B 87 -5 -353 301 48 85 CYS SG I 3 95 3 -314 248 30
THR CG2 B 87 -4 -366 318 46 GLU N I 3 96 2 -277 215 27
CYS N B 88 -2 -356 278 33 GLU CA I 3 96 2 -271 202 26
CYS CA B 88 -3 -354 263 32 GLU C I 3 96 2 -282 191 30
CYS C B 88 -4 -352 258 35 GLU 0 I 3 96 1 -280 183 28
CYS 0 B 88 -4 -346 248 35 90 GLU CB I 3 96 3 -261 198 27
CYS CB B 88 -2 -365 256 31 GLU CG I 3 96 3 -253 186 35
CYS SG B 88 0 -364 259 34 GLU CD I 3 96 4 -244 181 43
ASN N B 89 -5 -358 266 32 GLU OE1 I 3 96 4 -236 189 37
ASN CA B 89 -6 -357 262 32 GLU OE2 I 3 96 4 -244 169 42
ASN C B 89 -7 -342 264 35 95 GLN N I 3 97 3 -292 191 27
ASN 0 B 89 -8 -338 258 35 GLN CA I 3 97 2 -302 180 25
ASN CB B 89 -7 -366 271 36 GLN C I 3 97 2 -316 186 29
ASN CG B 89 -7 -381 267 53 GLN O I 3 97 1 -320 186 28
ASN OD1 B 89 -7 -389 276 54 GLN CB I 3 97 4 -303 171 26
ASN ND2 B 89 -7 -384 255 42 100 GLN CG I 3 97 4 -291 162 30
ILE N B 90 -6 -334 273 32 GLN CD I 3 97 5 -290 153 35
ILE CA B 90 -7 -321 277 32 GLN OE1 I 3 97 6 -299 152 29
ILE C B 90 -6 -311 269 34 GLN NE2 I 3 97 5 -279 146 27
ILE 0 B 90 -5 -309 273 34 PHE N I 3 98 3 -323 192 24
ILE CB B 90 -7 -317 292 36 105 PHE CA I 3 98 3 -336 197 24
ILE CGI B 90 -7 -328 301 37 PHE C I 3 98 3 -337 212 28
ILE CG2 B 90 -7 -303 295 36 PHE O I 3 98 4 -330 218 28
ILE CD1 B 90 -8 -335 297 45 PHE CB I 3 98 4 -346 190 25
LYS N B 91 -6 -304 259 29 PHE CG I 3 98 4 -345 175 27
LYS CA B 91 -6 -293 251 29 110 PHE CD1 I 3 98 3 -344 167 29
LYS C B 91 -4 -299 246 33 PHE CD2 I 3 98 5 -346 169 29
LYS 0 B 91 -3 -291 246 32 PHE CE1 I 3 98 3 -344 153 29
LYS CB B 91 -6 -280 259 31 PHE CE2 I 3 98 5 -346 155 31
LYS CG B 91 -7 -274 264 44 PHE CZ I 3 98 4 -345 147 29
LYS CD B 91 -6 -262 273 48 115 CYS N I 3 99 2 -346 218 26
LYS CE B 91 -8 -252 274 65 CYS CA I 3 99 2 -348 232 27
LYS NZ B 91 -7 -241 284 81 CYS C I 3 99 2 -363 235 30
ASN N B 92 -4 -312 243 28 CYS O I 3 99 2 -371 228 31
ASN CA B 92 -3 -318 238 27 CYS CB I 3 99 1 -343 238 29
ASN C B 92 -2 -316 248 32 120 CYS SG I 3 99 1 -345 256 33
ASN 0 B 92 -1 -315 243 30 LYS N I 3 100 3 -366 246 28
ASN CB B 92 -3 -313 224 25 LYS CA I 3 100 3 -379 251 28 LYS C I3 100 3 -380 266 32 VAL O I3 108 5 -349 252 30
LYS 0 I 3 100 4 -371 273 32 VAL CB I 3 108 7 -357 273 33
LYS CB I 3 100 5 -385 247 29 VAL CGI I 3 108 8 -354 262 33
LYS CG I 3 100 5 -399 253 31 65 VAL CG2 I 3 108 8 -358 286 32
LYS CD I 3 100 6 -405 247 31 CYS N I 3 109 6 -329 255 28
LYS CE I 3 100 7 -417 255 31 CYS CA I 3 109 6 -324 242 26
LYS NZ I 3 100 6 -428 253 40 CYS C I 3 109 7 -327 233 32
ASN N I 3 101 2 -389 272 31 CYS O I 3 109 8 -329 237 31
ASN CA I 3 101 2 -390 286 32 70 CYS CB I 3 109 6 -309 242 26
ASN C I 3 101 3 -396 293 36 CYS SG I 3 109 4 -304 254 31
ASN 0 I 3 101 4 -406 288 34 SER N I 3 110 7 -328 220 28
ASN CB I 3 101 1 -399 289 32 SER CA I 3 110 8 -330 209 28
ASN CG I 3 101 -1 -392 286 43 SER C I 3 110 7 -323 196 33
ASN 0D1 I 3 101 -1 -380 291 35 75 SER O I 3 110 6 -317 196 30
ASN ND2 I 3 101 -1 -398 279 37 SER CB I 3 110 8 -345 206 27
SER N I 3 102 4 -389 303 37 SER OG I 3 110 7 -352 203 34
SER CA I 3 102 5 -394 311 40 CYS N I 3 111 8 -322 187 32
SER C I 3 102 5 -395 326 50 CYS CA I 3 111 8 -314 174 32
SER 0 I 3 102 3 -393 331 50 80 CYS C I 3 111 8 -323 162 32
SER CB I 3 102 6 -386 307 41 CYS O I 3 111 9 -333 164 29
SER OG I 3 102 6 -373 313 45 CYS CB I 3 111 9 -301 174 33
ALA N I 3 103 6 -397 334 52 CYS SG I 3 111 8 -290 189 37
ALA CA I 3 103 6 -398 349 54 THR N I 3 112 8 -319 150 29
ALA C I 3 103 5 -387 357 61 85 THR CA I 3 112 8 -327 138 28
ALA 0 I 3 103 5 -375 353 62 THR C I 3 112 10 -323 134 30
ALA CB I 3 103 7 -398 353 55 THR O I 3 112 10 -314 140 29
ASP N I 3 104 4 -391 368 57 THR CB I 3 112 7 -325 127 30
ASP CA I 3 104 4 -383 379 57 THR OG1 I 3 112 7 -334 117 32
ASP C I 3 104 3 -372 373 57 90 THR CG2 I 3 112 7 -310 122 27
ASP 0 I 3 104 3 -360 376 56 GLU N I 3 113 10 -331 125 27
ASP CB I 3 104 5 -377 389 60 GLU CA I 3 113 11 -328 120 27
ASP CG I 3 104 6 -386 392 77 GLU C I 3 113 12 -314 115 30
ASP OD1 I 3 104 6 -395 400 79 GLU O I 3 113 11 -308 109 31
ASP OD2 I 3 104 7 -383 386 86 95 GLU CB I 3 113 12 -338 108 29
ASN N I 3 105 2 -376 366 52 GLU CG I 3 113 13 -336 102 42
ASN CA I 3 105 1 -367 359 51 GLU CD I 3 113 14 -349 95 74
ASN C I 3 105 1 -356 351 50 GLU OE1 I 3 113 13 -355 87 67
ASN 0 I 3 105 1 -344 353 50 GLU OE2 I 3 113 15 -351 98 79
ASN CB I 3 105 -0 -362 370 54 100 GLY N I 3 114 13 -307 118 27
ASN CG I 3 105 -1 -373 378 94 GLY CA I 3 114 13 -293 115 27
ASN OD1 I 3 105 -1 -385 373 93 GLY C I 3 114 13 -283 126 29
ASN ND2 I 3 105 -1 -370 391 88 GLY O I 3 114 13 -271 124 29
LYS N I 3 106 2 -359 343 43 TYR N I 3 115 12 -288 136 27
LYS CA I 3 106 3 -350 335 41 105 TYR CA I 3 115 12 -280 148 27
LYS C I 3 106 3 -354 320 39 TYR C I 3 115 12 -286 160 33
LYS 0 I 3 106 2 -365 317 36 TYR O I 3 115 12 -298 161 34
LYS CB I 3 106 5 -349 339 43 TYR CB I 3 115 10 -280 149 27
LYS CG I 3 106 5 -339 351 54 TYR CG I 3 115 9 -273 138 27
LYS CD I 3 106 6 -340 356 66 110 TYR CD1 I 3 115 9 -260 138 29
LYS CE I 3 106 7 -328 365 69 TYR CD2 I 3 115 9 -281 127 26
LYS NZ I 3 106 7 -316 357 72 TYR CE1 I 3 115 8 -254 128 28
VAL N I 3 107 3 -345 312 33 TYR CE2 I 3 115 8 -275 116 26
VAL CA I 3 107 3 -347 298 32 TYR CZ I 3 115 8 -261 116 29
VAL C I 3 107 5 -342 292 33 115 TYR OH I 3 115 7 -255 106 27
VAL 0 I 3 107 5 -334 297 31 ARG N I 3 116 12 -277 170 30
VAL CB I 3 107 2 -338 293 35 ARG CA I 3 116 13 -280 183 30
VAL CGI I 3 107 2 -329 282 34 ARG C I 3 116 12 -275 193 34
VAL CG2 I 3 107 1 -347 291 34 ARG O I 3 116 11 -264 191 32
VAL N I 3 108 5 -349 281 29 120 ARG CB I 3 116 14 -274 185 32
VAL CA I 3 108 6 -346 273 29 ARG CG I 3 116 14 -261 193 42
VAL C I 3 108 6 -341 259 31 ARG CD I 3 116 16 -256 196 45 ARG NE I3 116 16 -249 184 59 CYS O I3 124 8 -236 172 37
ARG CZ I 3 116 16 -236 182 68 CYS CB I 3 124 7 -265 176 32
ARG NH1 I 3 116 15 -229 190 53 CYS SG I 3 124 7 -280 184 37
ARG NH2 I 3 116 17 -231 171 54 65 GLU N I 3 125 10 -244 178 32
LEU N I 3 117 12 -282 204 33 GLU CA I 3 125 11 -234 172 32
LEU CA I 3 117 11 -278 215 34 GLU C I 3 125 11 -240 160 34
LEU C I 3 117 11 -266 222 41 GLU O I 3 125 12 -251 161 33
LEU 0 I 3 117 13 -266 225 42 GLU CB I 3 125 12 -229 182 34
LEU CB I 3 117 11 -290 225 35 70 GLU CG I 3 125 11 -219 192 50
LEU CG I 3 117 10 -290 236 41 GLU CD I 3 125 12 -214 202 77
LEU CD1 I 3 117 8 -289 230 41 GLU OE1 I 3 125 12 -206 211 79
LEU CD2 I 3 117 10 -301 246 42 GLU OE2 I 3 125 13 -217 202 63
ALA N I 3 118 11 -255 223 38 PRO N I 3 126 12 -232 149 31
ALA CA I 3 118 11 -242 229 38 75 PRO CA I 3 126 12 -237 137 31
ALA C I 3 118 11 -243 244 43 PRO C I 3 126 14 -240 141 35
ALA 0 I 3 118 11 -254 250 41 PRO O I 3 126 14 -232 149 35
ALA CB I 3 118 10 -232 227 38 PRO CB I 3 126 12 -226 127 33
GLU N I 3 119 12 -232 250 42 PRO CG I 3 126 11 -218 131 37
GLU CA I 3 119 12 -232 264 42 80 PRO CD I 3 126 11 -219 146 32
GLU C I 3 119 11 -233 274 44 ALA N I 3 127 14 -251 137 32
GLU 0 I 3 119 11 -240 284 44 ALA CA I 3 127 16 -256 140 32
GLU CB I 3 119 13 -219 268 44 ALA C I 3 127 17 -256 128 38
GLU CG I 3 119 15 -222 265 60 ALA O I 3 127 18 -259 129 39
GLU CD I 3 119 16 -211 270 92 85 ALA CB I 3 127 16 -269 147 33
GLU 0E1 I 3 119 15 -203 279 94 VAL N I 3 128 16 -254 116 33
GLU OE2 I 3 119 17 -211 265 86 VAL CA I 3 128 17 -255 103 31
ASN N I 3 120 10 -229 269 37 VAL C I 3 128 16 -242 95 35
ASN CA I 3 120 9 -231 277 36 VAL O I 3 128 15 -235 99 33
ASN C I 3 120 8 -245 277 36 90 VAL CB I 3 128 16 -268 95 34
ASN 0 I 3 120 7 -249 284 35 VAL CGI I 3 128 17 -280 102 34
ASN CB I 3 120 7 -221 271 36 VAL CG2 I 3 128 15 -269 92 33
ASN CG I 3 120 7 -225 257 43 PRO N I 3 129 17 -238 84 32
ASN OD1 I 3 120 7 -235 251 42 PRO CA I 3 129 17 -226 77 31
ASN ND2 I 3 120 6 -216 251 36 95 PRO C I 3 129 15 -227 71 32
GLN N I 3 121 9 -254 270 32 PRO O I 3 129 14 -217 71 33
GLN CA I 3 121 9 -269 269 31 PRO CB I 3 129 18 -225 65 33
GLN C I 3 121 7 -273 262 34 PRO CG I 3 129 19 -234 69 38
GLN 0 I 3 121 7 -285 262 34 PRO CD I 3 129 18 -244 78 35
GLN CB I 3 121 9 -275 283 33 100 PHE N I 3 130 15 -238 65 27
GLN CG I 3 121 10 -269 292 36 PHE CA I 3 130 13 -239 59 26
GLN CD I 3 121 10 -276 305 52 PHE C I 3 130 13 -251 65 31
GLN OE1 I 3 121 9 -285 309 49 PHE O I 3 130 13 -262 58 32
GLN NE2 I 3 121 11 -272 311 47 PHE CB I 3 130 13 -239 44 27
LYS N I 3 122 7 -263 255 29 105 PHE CG I 3 130 14 -227 39 28
LYS CA I 3 122 5 -266 249 29 PHE CD1 I 3 130 16 -228 35 31
LYS C I 3 122 5 -262 234 34 PHE CD2 I 3 130 14 -214 38 29
LYS 0 I 3 122 5 -270 226 32 PHE CE1 I 3 130 16 -217 31 32
LYS CB I 3 122 4 -258 256 31 PHE CE2 I 3 130 14 -203 34 31
LYS CG I 3 122 4 -261 271 37 110 PHE CZ I 3 130 16 -205 30 30
LYS CD I 3 122 3 -275 273 39 PRO N I 3 131 12 -250 77 27
LYS CE I 3 122 3 -279 288 37 PRO CA I 3 131 11 -261 83 26
LYS NZ I 3 122 3 -293 290 27 PRO C I 3 131 10 -263 75 30
SER N I 3 123 6 -250 231 32 PRO O I 3 131 9 -254 69 30
SER CA I 3 123 6 -245 217 32 115 PRO CB I 3 131 11 -257 97 27
SER C I 3 123 7 -251 208 35 PRO CG I 3 131 11 -242 96 32
SER 0 I 3 123 8 -257 213 33 PRO CD I 3 131 12 -238 86 28
SER CB I 3 123 6 -230 218 34 CYS N I 3 132 10 -276 75 28
SER OG I 3 123 5 -223 226 40 CYS CA I 3 132 8 -280 68 27
CYS N I 3 124 7 -250 195 32 120 CYS C I 3 132 7 -273 73 28
CYS CA I 3 124 8 -255 185 32 CYS O I 3 132 7 -268 84 28
CYS C I 3 124 9 -244 178 36 CYS CB I 3 132 8 -295 69 27 CYS SG B 132 8 -301 86 31 SCH CIO s 1 -13 -342 -101 31
GLY N B 133 6 -272 64 25 SCH Cll s 1 -13 -349 -113 35
GLY CA B 133 5 -267 67 24 SCH C12 s 1 -12 -356 -119 34
GLY C B 133 5 -252 71 29 65 SCH C13 s 1 -7 -316 -161 44
GLY 0 B 133 4 -248 76 27 SCH C14 s 1 -7 -311 -173 47
ARG N B 134 6 -244 70 27 SCH C15 s 1 -8 -319 -180 47
ARG CA B 134 6 -231 74 27 SCH C16 s 1 -8 -333 -177 47
ARG C B 134 6 -221 62 30 SCH C17 s 1 -8 -339 -166 45
ARG 0 B 134 6 -223 52 29 70 SCH C18 s 1 -7 -330 -158 44
ARG CB B 134 7 -228 81 29 SCH C19 s 1 -7 -296 -176 45
ARG CG B 134 7 -215 88 39 SCH C20 s 1 -8 -289 -168 44
ARG CD B 134 8 -215 96 48 SCH C21 s 1 -8 -353 -163 44
ARG NE B 134 9 -202 104 55 SCH 022 s 1 -8 -361 -172 47
ARG CZ B 134 8 -200 116 71 75 SCH N23 s 1 -7 -357 -149 38
ARG NH1 B 134 7 -209 122 52 SCH C24 s 1 -8 -371 -145 34
ARG NH2 B 134 8 -188 122 62 SCH C25 s 1 -8 -373 -131 33
VAL N B 135 5 -211 64 26 SCH C26 s 1 -9 -367 -129 34
VAL CA B 135 5 -200 54 26 SCH 027 s 1 -7 -368 -122 33
VAL C B 135 6 -189 59 32 80 SCH 028 s 1 -10 -367 -139 37
VAL 0 B 135 6 -183 69 31 SCH N29 s 1 -10 -361 -117 31
VAL CB B 135 3 -194 52 29 SCH O30 s 1 -14 -349 -118 40
VAL CGI B 135 3 -182 43 29 SCH 031 s 1 -12 -335 -83 30
VAL CG2 B 135 2 -204 46 28 SCH C32 s 1 -11 -336 -75 31
SER N B 136 7 -187 51 30 85 HOH O w 1 -3 -287 -94 28
SER CA B 136 8 -178 55 30 HOH O w 2 -6 -280 -145 44
SER C B 136 8 -165 46 37 HOH O w 3 -8 -245 -94 31
SER 0 B 136 8 -155 50 36 HOH O w 4 -11 -212 -73 32
SER CB B 136 9 -184 56 33 HOH O w 5 -4 -298 -66 22
SER OG B 136 10 -190 44 38 90 HOH O w 6 -2 -270 7 31
VAL N B 137 7 -165 34 35 HOH O w 7 -11 -200 -4 39
VAL CA B 137 7 -154 25 36 HOH O w 8 -11 -211 19 33
VAL C B 137 6 -144 31 43 HOH O w 9 -15 -225 21 50
VAL 0 B 137 5 -148 35 42 HOH O w 10 1 -356 87 23
VAL CB B 137 7 -157 11 39 95 HOH O w 11 -5 -387 72 27
VAL CGI B 137 6 -145 2 39 HOH O w 12 -8 -312 96 28
VAL CG2 B 137 8 -166 4 38 HOH O w 13 -6 -262 87 29
SER N B 138 6 -131 31 43 HOH O w 14 2 -470 59 33
SER CA B 138 6 -120 36 43 HOH O w 15 3 -259 149 31
SER C B 138 4 -121 28 45 100 HOH O w 16 5 -296 209 25
SER 0 B 138 4 -123 16 44 HOH O w 17 7 -360 124 35
SER CB B 138 6 -106 34 47 HOH O w 18 0 -344 -25 25
SER OG B 138 5 -96 39 61 HOH O w 19 7 -309 274 29
GLN N B 139 3 -121 35 42 HOH O w 20 10 -206 249 48
GLN CA B 139 2 -123 29 42 105 HOH O w 21 6 -193 23 24
GLN C B 139 1 -110 27 49 HOH O w 22 3 -133 -9 34
GLN 0 B 139 1 -101 35 50 HOH 0 w 23 6 -251 -43 32
GLN CB B 139 1 -133 37 43 HOH 0 w 24 4 -253 -74 28
GLN CG B 139 2 -147 38 44 HOH 0 w 25 3 -214 -31 30
GLN CD B 139 2 -154 24 43 110 HOH 0 w 26 4 -230 -49 35
GLN OE1 B 139 1 -157 19 38 HOH 0 w 27 2 -198 -51 34
GLN NE2 B 139 3 -157 19 27 HOH 0 w 28 13 -213 -61 23
NA NA Q 499 5 -189 -128 21 HOH 0 w 29 9 -216 40 28
SCH CI S 1 -6 -379 -148 31 HOH 0 w 30 1 -233 74 29
SCH C2 S 1 -5 -374 -146 30 115 HOH 0 w 31 -2 -241 50 30
SCH C3 S 1 -4 -382 -149 31 HOH 0 w 32 11 -296 86 32
SCH C4 S 1 -4 -395 -154 31 HOH 0 w 33 8 -340 49 29
SCH C5 S 1 -5 -401 -156 30 HOH 0 w 34 -15 -205 -89 36
SCH C6 S 1 -7 -392 -153 31 HOH 0 w 35 -1 -217 39 35
SCH C7 S 1 -11 -355 -113 31 120 HOH 0 w 36 -3 -202 39 35
SCH C8 S 1 -11 -348 -101 28 HOH 0 w 37 5 -189 -50 29
SCH C9 S 1 -12 -342 -95 28 HOH 0 w 38 6 -210 -35 35 HOH 0 w 39 6 -172 -69 31 HOH O w 100 -7 -214 -183 54
HOH 0 w 40 6 -203 -145 40 HOH O w 101 -10 -198 40 49
HOH 0 w 41 4 -248 -148 44 HOH O w 102 -20 -301 -36 57
HOH 0 w 42 -5 -270 -183 46 65 HOH O w 103 -18 -299 -19 42
HOH 0 w 43 12 -369 46 34 HOH O w 104 12 -324 165 40
HOH 0 w 44 10 -385 47 35 HOH O w 105 9 -364 165 45
HOH 0 w 45 8 -368 58 26 HOH O w 106 11 -327 190 37
HOH 0 w 46 7 -339 88 28 HOH O w 107 15 -321 137 37
HOH 0 w 47 14 -202 -79 36 70 HOH O w 108 5 -185 102 64
HOH 0 w 48 17 -206 -27 30 HOH O w 109 3 -162 77 54
HOH 0 w 49 14 -178 7 20 HOH O w 110 3 -117 66 42
HOH 0 w 50 18 -218 -2 38 HOH O w 111 9 -120 22 47
HOH 0 w 51 17 -187 -2 33 HOH O w 112 6 -231 113 44
HOH 0 w 52 18 -250 13 39 75 HOH O w 113 -4 -199 61 47
HOH 0 w 53 18 -277 -1 38 HOH O w 114 8 -362 86 51
HOH 0 w 54 14 -252 -131 35 HOH O w 115 16 -334 -126 27
HOH 0 w 55 16 -248 -106 18 HOH O w 116 13 -201 -111 47
HOH 0 w 56 7 -279 -176 33 HOH O w 117 10 -460 -122 44
HOH 0 w 57 5 -497 -31 49 80 HOH O w 118 1 -487 33 47
HOH 0 w 58 -7 -494 -63 34 HOH O w 119 -14 -473 -96 49
HOH 0 w 59 -5 -441 105 44 HOH O w 120 -2 -306 181 37
HOH 0 w 60 -7 -400 91 30 HOH O w 121 -7 -179 -121 34
HOH 0 w 61 -5 -411 161 36 HOH O w 122 -7 -437 -18 46
HOH 0 w 62 -11 -324 83 26 85 HOH O w 123 -20 -235 -15 49
HOH 0 w 63 -11 -314 58 28 HOH 0 w 124 3 -210 166 57
HOH 0 w 64 -15 -385 60 34 HOH 0 w 125 -3 -222 126 45
HOH 0 w 65 -14 -309 -14 35 HOH 0 w 126 1 -239 251 52
HOH 0 w 66 -22 -407 104 49 HOH 0 w 127 2 -399 350 66
HOH 0 w 67 10 -227 60 30 90 HOH 0 w 128 5 -307 295 35
HOH 0 w 68 3 -207 87 29 HOH 0 w 129 15 -305 161 43
HOH 0 w 69 -6 -327 230 43 HOH 0 w 130 7 -128 -43 40
HOH 0 w 70 1 -410 252 35 HOH 0 w 131 -7 -341 -123 30
HOH 0 w 71 16 -264 58 32
HOH 0 w 72 -10 -171 -74 39
HOH 0 w 73 -13 -194 -10 38
HOH 0 w 74 -0 -372 319 38
HOH 0 w 75 -15 -309 -145 38
HOH 0 w 76 1 -455 82 32
HOH 0 w 77 3 -439 122 36
HOH 0 w 78 -4 -308 297 41
HOH 0 w 79 -9 -322 231 49
HOH 0 w 80 -9 -305 249 26
HOH 0 w 81 -5 -341 209 46
HOH 0 w 82 4 -317 323 29
HOH 0 w 83 -19 -247 -114 27
HOH 0 w 84 -14 -188 -70 48
HOH 0 w 85 -9 -143 -52 27
HOH 0 w 86 -2 -133 -59 36
HOH 0 w 87 -1 -352 -196 49
HOH 0 w 88 8 -396 -161 38
HOH 0 w 89 6 -329 -193 45
HOH 0 w 90 10 -369 -161 40
HOH 0 w 91 7 -139 -177 42
HOH 0 w 92 0 -133 -105 36
HOH 0 w 93 6 -143 -68 33
HOH 0 w 94 15 -157 -85 29
HOH 0 w 95 12 -202 69 45
HOH 0 w 96 10 -332 70 37
HOH 0 w 97 15 -381 54 36
60 HOH 0 w 98 1 -435 154 34
HOH 0 w 99 -8 -196 -153 56 Example 21 : Factor IXa and Xa Protease Assays.
The following factor IXa and Xa assays can be performed to determine that ability of various compounds to inhibit factor IXa and factor Xa protease activity.
Factor IXa functional assay protocol:
Buffer:
50 mM Tris pH 8.0
5 mM CaCI2*2H20
100 mM NaCI
15% vol/vol Ethylene Glycol Enzyme:
Human plasma factor IXa. (American Diagnostica Inc. product)
Enzyme is diluted 1 :800 in buffer to achieve 0.0057 μg/ml working stock for use in assay. Mixed by inversion.
Substrate:
Spectrozyme factor IXa Fluorogenic substrate (American Diagnostica Inc.; Stamford, CT): Methylsulfonyl-D-cyclohexylglycyl-glycyl-arginine-paranitroanilide monoacetate salt. The substrate (10 umoles lyophilized) is reconstituted with 1 ml water to give a 10 mM stock. The substrate is then further diluted to 300 μΜ in buffer for use in assay and mixed by inversion.
Procedure in 384 well plate:
Added 10 μΙ vehicle or compound
Added 10 μΙ Factor IXa enzyme.
Added 10 μΙ Fluorogenic substrate.
Incubated reaction at room temperature for 2h.
Quenched with 5 ul 50% acetic acid.
Read Fluorescence - Absorbance 360nm; Emission 440nm
Factor Xa functional assay protocol:
Buffer:
20 mM Tris pH 8.0 2.5 mM CaCI2*2H20
200 mM NaCI
Enzyme:
Human plasma factor Xa. (American Diagnostica Inc.; see supra)
Resuspended enyme in water to 80 ug/ml.
Enzyme is diluted to 0.133 μg/ml in buffer. Mix by inversion.
Substrate:
Spectrozyme factor IXa Fluorogenic substrate (American Diagnostica Inc.)
Reconstitute with 1 ml water to give a 10mM stock. The substrate is then further diluted to 300μΜ in buffer for use in assay. Mix by inversion.
Procedure in 384 well plate:
Add 10 μΙ vehicle or compound
Add 10 μΙ Factor Xa enzyme.
Add 10 μΙ Fluorogenic substrate.
Incubate reaction at room temperature for 2h.
Quench with 5 μΙ 50% acetic acid.
Read Fluorescence - Absorbance 360nm; Emission 440nm
Example 22: Generation of Compound A.
Figure imgf000106_0001
2
3
Step 1
(2R,3S)-methyl 3-(4-ethylbenzamido)-2-hydroxy-3-phenylpropanoate (1 )
To a solution of (2R,3S)-methyl 3-amino-2-hydroxy-3-phenylpropanoate (27.3 g) in dichloromethane (1 .4 L), was added pyridine (1 1 .3 mL). Then 4-ethylbenzoyl chloride (20.6 mL) was added into the above mixture at 0°C. The reaction mixture was stirred for 1 hour at ambient temperature. To the mixture, was added sat. NaHCOs and the mixture was extracted with CH2CI2. The oranic layer was concentrated in vacuo. To the resulting residue, was added Et20 and the crude product was triturated to obtain the title compound (31 .6 g) as colorless solid.
Step 2
(2R,3S)-3-(4-ethylbenzamido)-2-hydroxy-3-phenylpropanoic acid (2)
To a solution of (2R,3S)-methyl 3-(4-ethylbenzamido)-2-hydroxy-3-phenylpropanoate (31 .5 g) in MeOH (481 mL), was added 1 N NaOH (481 mL) at 0°C. The reaction mixture was stirred for 1 .5 h at ambient temperature. Then mixture was concentrated in vacuo to remove MeOH. To the resulting residue, was added 1 N HCI to precipitate. The precipitate was collected by filtration and linsed with water then CH2CI2 and dried in vacuo to obtain the title compound (29.2 g) as colorless solid.
Step 3
4-Ethyl-N-((1 S,2R)-2-hydroxy-3-((3-hydroxy-5-methoxyphenyl)amino)-3-oxo-1 - phenylpropyl)benzamide (3)
To a solution of (2R,3S)-3-(4-ethylbenzamido)-2-hydroxy-3-phenylpropanoic acid (0.3 g) and 3-amino-5-methoxyphenol (0.16 g) in N,N-dimethylformamide (5.6 mL), were added 1 - hydroxybenzotriazole (0.16 g) and 1 -(3-dimethaminopropyl)-3-ethylcarbodiimede
hydrochloride (0.17 g) at 0°C. The mixture was stirred at ambient temperature for 2.5 hours. To the mixture, was added water and the mixture was extracted with AcOEt. The organic layer was washed with sat. NaHCOs, brine and dried over anhyd. Na2SO4. The solvent was removed in vacuo and the resulting residue was purified by silica gel column
chromatography (eluent: Hexane/ AcOEt = 2/1 - 1/1 - 1/2) to obtain the title compound (160 mg) as colorless solid. The measurement of nuclear magnetic resonance (NMR) spectrum was performed using a JEOL JNM-ECX300 FT-NMR (manufactured by JEOL Ltd.).
Liquid chromatography-mass spectrometry (LC-MS) was performed using a Waters FractionLynx MS system (manufactured by Waters Corporation). A SunFire column™ (4.6 mm x 5 cm, 5 micron) (manufactured by Waters Corporation) was used as an analytical column. Methanol and 0.05% aqueous acetic acid solution was used as the mobile phase. The analysis was performed under the following gradient conditions: Methanol: 0.05% aqueous acetic acid solution = 1 :9 (0 minutes), 10:0 (5 minutes), and 10:0 (7 minutes).
Figure imgf000108_0001
H-NMR (300MHz, CDCI3) δ: 7.69 (2H, d, J = 9 Hz), 7.47-7.22 (7H, m), 6.93 (1 H, d, J = Hz), 5.74 (1 H, dd, J = 9, 2 Hz), 4.65-4.61 (1 H, m), 3.84 (3H, s), 3.27 (1 H, d, J = 3 Hz), 2 (2H, q, J = 8 Hz), 1.24 (3H, t, J = 8 Hz).
Figure imgf000108_0002
H-NMR (DMSO-de) δ: 12.74 (1 H, br s), 8.47 (1 H, d, J = 9 Hz), 7.77 (2H, d, J = 9 Hz), 7.42- 7.19 (7H, m), 5.54 (1 H, br s), 5.46 (1 H, dd, J = 9, 4 Hz), 4.41-4.33 (1 H, m), 2.66 (2H, q, J = 8 Hz), 1.19 (3H, t, J = 8 Hz)
Figure imgf000108_0003
H-NMR (300MHz, DMSO-de) δ: 9.73 (1 H, s), 9.40 (1 H, s), 8.41 (1 H, d, J = 9 Hz), 7.76 (2H, d, J = 8 Hz), 7.42 (2H, d, J = 7 Hz), 7.35-7.19 (5H, m), 6.77 (1 H, dd, J = 2, 2 Hz), 6.63 (1 H, dd, J = 2, 2 Hz), 6.05-5.95 (2H, m), 5.46 (1 H, dd, J = 9, 4 Hz), 4.45-4.35 (1 H, m), 3.63 (3H, s), 2.65 (2H, q, J = 8 Hz), 1.18 (3H, t, J = 8 Hz)
LCMS m/z = 435 (M+H), RT = 5.28 min
***************************
The present invention is not to be limited in scope by the specific embodiments described herein. Indeed, the scope of the present invention includes embodiments specifically set forth herein and other embodiments not specifically set forth herein; the embodiments specifically set forth herein are not necessarily intended to be exhaustive. 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 claims.
Patents, patent applications, publications, product descriptions, and protocols are cited throughout this application, the disclosures of which are incorporated herein by reference in their entireties for all purposes.

Claims

We claim:
1. An isolated polypeptide comprising the amino acid sequence set forth in SEQ ID NO: 1
2. An isolated polynucleotide encoding the polypeptide of claim 1.
3. An isolated vector comprising the polynucleotide of claim 2.
4. An isolated host cell comprising the polynucleotide or vector of any of claims 2-3 or the polypeptide of claim 1.
5. The polypeptide of claim 1 complexed with:
Figure imgf000110_0001
(compound A);
Figure imgf000110_0002
(compound C).
6. A composition comprising the polypeptide of claim 1 or 5.
7. The composition of claim 6 comprising a precipitant.
8. An isolated crystal:
(a) comprising a polypeptide that comprises the amino acid sequence of SEQ ID NO: 1 complexed with a compound represented by the structural formula
Figure imgf000110_0003
having unit cell dimensions a= 99.4A, b=99.4A, c=94.2A, α=β=90°, γ=120° and space group H3; (b) comprising a polypeptide that comprises the amino acid sequence of SEQ ID NO: 1 complexed with a compound represented by the structural
Figure imgf000111_0001
having unit cell dimensions a= 98.9A, b=98.9A, c=95.4A, α=β=90°, γ =120° and space group H3;
(c) comprising a polypeptide that comprises the amino acid sequence of SEQ ID NO: 1 complexed with a compound represented by the structural
Figure imgf000111_0002
; having unit cell dimensions a= 98.9A, b= 98.9A, c
95.3A, α=β= 90°,γ= 90° and space group H3; or
(d) comprising a polypeptide that comprises the amino acid sequence of SEQ ID NO: 1 complexed with a compound represented by the structural formula
Figure imgf000111_0003
; having unit cell dimensions a= 98.9A, b=98.9A, c=93.9A, α=β
90 , γ = 90° and space group H3.
9. The crystal of claim 8 characterized by structural coordinates comprising a root mean square deviation of conserved residue backbone atoms or of alpha carbon atoms of less than about 1.5 A when superimposed on backbone atoms described in Table 3, 6, 9 or 12.
10. The crystal of any of claims 8-9 which can diffract X-rays for structural determination of said complex to a resolution of about 1 angstroms.
11. A method making a crystalline complex comprising a soaked compound bound to factor IXa protein, said method comprising soaking a crystalline composition comprising the polypeptide of claim 1 complexed with:
(compound A);
Figure imgf000111_0004
Figure imgf000112_0001
(compound C), with the soaked compound, at a pH of at least about 9.5.
12. The method of claim 11 wherein the crystalline composition is soaked in the presence of CHES/citrate buffer at about pH 9.5.
13. A method for making a crystalline complex comprising a compound bound to factor IXa protein, said method comprising: (a) heating the compound, (b) cooling the compound, (c) mixing the polypeptide of claim 1 with the compound under conditions favorable to formation of a complex between the polypeptide and the compound; (b) crystallizing the polypeptide-compound complex. 14. A method for determining the three dimensional structure of a crystalline complex comprising irradiating a crystalline complex that is the product of a method according to any of claims 11 -13, generating a diffraction pattern from said irradiation of said crystal, employing Fournier transformations to generate an image of the three dimensional structure.
15. A method for identifying a candidate compound which binds to factor IXa or inhibits blood clotting comprising: determining the structure of a complex comprising a compound represented by structural formula A, B or C by employing the data of any one of Tables 3, 6, 9 or 12 optionally varied by a root mean square deviation of conserved residue backbone atoms or of alpha carbon atoms of less than about 1.5 A when superimposed on backbone atoms or alpha carbon atoms described in Table 3, 6, 9 or 12; and, employing a
computational means to dock the candidate compound with the factor IXa serine protease domain to determine if said candidate compound binds to said serine protease domain; and, optionally, synthesizing said candidate compound; and, optionally, determining if said candidate compound binds to factor IXa or inhibits factor IXa proteolytic activity.
PCT/US2013/075558 2012-12-19 2013-12-17 FACTOR IXa 318R/A MUTANT WO2014099850A1 (en)

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Citations (3)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US20110059958A1 (en) * 2008-12-05 2011-03-10 Hidemitsu Nishida Morpholinone compounds as factor ixa inhibitors
US7968683B1 (en) * 2008-05-07 2011-06-28 Schering Corporation Factor IXa crystals, related complexes and methods
WO2012061654A1 (en) * 2010-11-03 2012-05-10 Catalyst Biosciences, Inc. Modified factor ix polypeptides and uses thereof

Patent Citations (3)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US7968683B1 (en) * 2008-05-07 2011-06-28 Schering Corporation Factor IXa crystals, related complexes and methods
US20110059958A1 (en) * 2008-12-05 2011-03-10 Hidemitsu Nishida Morpholinone compounds as factor ixa inhibitors
WO2012061654A1 (en) * 2010-11-03 2012-05-10 Catalyst Biosciences, Inc. Modified factor ix polypeptides and uses thereof

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