SYNTHASES

Abstract: Novel synthases and the corresponding nucleic acids encoding such synthases are disclosed herein. Such synthases possess an active site pocket that includes key amino acid residues that are modified to generate desired terpenoid reaction intermediates and products. Synthase modifications are designed based on, e.g., the three-dimensional coordinates of tobacco 5-epi-aristolochene synthase, with or without a substrate bound in the active site.

Description: SYNTHASES Cross Reference to Related Application This application claims the benefit of provisional application 60/100,993 filed September 18, 1998; provisional application 60/130,628 filed April 22,1999; and provisional application 60/150,262 filed August 23,1999. This work was supported, in part, with funding from Federal agencies. Therefore, the United States Federal Government may have certain rights in the invention. Background of the Invention Isoprenoid compounds are organic molecules produced by a wide range of organisms (e.g., plants, bacteria, fungi, etc). To date, over 23,000 individual isoprenoid molecules have been characterized with tens to hundreds of new structures identified each year. These molecules can fulfill a variety of roles. For example, monoterpenes can be used as fragrances and flavors. Sesquiterpenes and diterpenes can serve as pheromones, defensive agents, visual pigments, antitumor drugs, and components of signal transduction pathways. Triterpenes can serve important functions as membrane constituents and precursors of steroid hormones and bile acids. Polyprenols function as photoreceptive agents and cofactor side chains, and can also exist as natural polymers. The diverse molecular compounds produced by the isoprenoid pathway are created from diphosphate esters of monounsaturated isoprene units. Isoprenes are added together in multiples of 2, 3, or 4 by prenyl transferases to make Cio, C 15 , and C 20 units, respectively. The C 10 , C 15 , and C 2 0 molecules, named geranyl diphosphate (GPP), farnesyl diphosphate (FPP), and geranylgeranyl diphosphate (GGPP), respectively, serve as substrates for terpene synthases. Terpene synthases catalyze the production of isoprenoid compounds via one of the most complex reactions known in chemistry or biology. In general, terpene synthases are moderately sized enzymes having molecular weights of about 40 to 100 kD. As an enzyme, terpene synthases can be classified as having low to moderate turnover rates coupled with exquisite reaction specificity and preservation of chirality. Turnover comprises binding of substrate to the enzyme, establishment of substrate conformation, conversion of substrate to product and product release. Reactions can be performed in vitro in aqueous solvents, typically require magnesium ions as cofactors, and the resulting products, which are often highly hydrophobic, can be recovered by partitioning into an organic solvent. Teφene synthase genes are found in a variety of organisms including bacteria, fungi and plants. Swapping regions approximating exons between different teψene synthases has identified functional domains responsible for terminal enzymatic steps. For example, work performed on 5-epi-aristolochene synthase (TEAS) from Nicotiana tabacum (tobacco) and Hyoscyamus muticus vetispiradiene synthase (HVS) from henbane revealed that exon 4 and exon 6, respectively, were responsible for reaction product specificity. Combining functional domains resulted in novel enzymes capable of synthesizing new reaction products (U.S. Patent 5,824,774). Studies have led to proposed reaction mechanisms for isoprenoid production; see, e.g., Cane et al., 1985, Bioorg. Chem. ,13:246-265; Wheeler and Croteau, 1987, Proc. Natl. Acad. Sci. USA, 84:4856-4859; and Pyun et al., 1994, Arch. Biochem. Biophys., 308:488-496. The studies used substrate analogs and suicide inhibitors (Croteau, 1994, Arch. Biochem. Biophys., 251:777-782; Cane et al., 1995, Biochemistry, 34:2471-2479; and Croteau et al., 1993, Arch. Biochem. Biophys., 307:397-404), as well as chemical-modifying reagents and site-directed mutagenesis in efforts to identify amino acids essential for catalysis (Cane et al., 1995, Biochemistry, 34:2480-2488; Rajaonarivony et al., 1992, Arch. Biochem. Biophys., 296:49-57; and Rajaonarivony et al., 1992, Arch. Biochem. Biophys., 299:77-82). However, these studies have resulted in limited success in defining the active site due to inherent limitations with these techniques. Summary of the Invention The invention describes a method of identifying alpha-carbon atoms found in the active site of a teφene synthase and describes these atoms in three- dimensional space as well as the spatial relationships among them. The present invention also describes R-groups associated with such alpha-carbons and methods of altering these R-groups in order to create novel teφene synthases capable of generating novel reaction products. Until the invention taught in this present application, the active site of synthase proteins, the amino acid residues located therein, the amino acid residues involved in catalysis, and the configuration of α-carbons and R-groups within the active site have not been known. The current invention now teaches the structure of synthases, as well as provides the means of making and using the information obtained therefrom to develop and produce new and novel synthases having new and novel synthetic capabilities. The data generated using the methods described herein are useful for creation and production of synthase mutants that can use a variety of isoprenoid substrates and produce a variety of isoprenoid products. In one embodiment, the invention features an isolated terpene synthase having about 20% or greater sequence identity to residues 265 to 535 of SEQ ID NO: 2. Such a synthase comprises nine α-carbons having interatomic distances in Angstroms between the α-carbons that are ±2.3 Angstroms of the interatomic distances shown in Table 6. The center point of each α-carbon is positioned within a sphere having a radius of 2.3 Angstroms. The center point of each such sphere has the structural coordinates given in Table 5. Each α-carbon has an associated R-group, and the synthase has an ordered arrangement of R- groups associated with each alpha-carbon other than the ordered arrangements of R-groups shown in Table 9. The synthase can have about 25% or greater sequence identity to residues 265 to 535 of SEQ ID 2, or about 35% or greater sequence identity to residues 265 to 535 of SEQ ID 2. Such a synthase can catalyse the formation of a teφenoid product from a monoteφene substrate, a sesquiteφene substrate, or a diteφene substrate. The product can be a cyclic teφenoid hydrocarbon or an acyclic teφenoid hydrocarbon. Either type of product can be hydroxylated or non-hydroxylated. The R-group associated with α-carbon 1 can be selected from one of the following groups: the group consisting of Cys, Ser, and Thr, the group consisting of Phe, Tyr and Tφ, the group consisting of Pro, Gly, and Ala, the group consisting of Glu and Asp, the group consisting of Met, He, Val and Leu, the group consisting of Arg and Lys, and the group consisting of Gin, Asn and His. R-groups associated with α-carbons 2 to 9 can be any amino acid except those having the ordered arrangements of Table 9. Similarly, the R-group associated with each of α-carbons 2-9 can be selected independently from the group consisting of Cys, Ser and Thr, the group consisting of Phe, Tyr and Tφ, the group consisting of Pro, Gly, and Ala, the group consisting of Glu and Asp, the group consisting of Met, He, Val and Leu, the group consisting of Arg and Lys, and the group consisting of Gin, Asn and His. In these embodiments, R-groups associated with the remaining eight α-carbons except those having the ordered arrangements of Table 9. In some embodiments, the ordered arrangement of R-groups associated with α-carbons 1 to 9 is Tφ, He, Thr, Thr, Tyr, Leu, Cys, Thr and Phe, respectively, Ser, He, Thr, Thr, Tyr, Leu, Cys, Thr and Tyr, respectively, Trp, He, Thr, Thr, Tyr, Leu, Trp, Thr and Tyr, respectively, Ser, He, Thr, Thr, Tyr, Leu, Trp, Thr and Tyr, respectively, or Glu, He, Thr, Thr, Tyr, Leu, Cys, Thr and Tyr, respectively. The invention also features a terpene synthase made by aligning the primary amino acid sequence of a preselected teφene synthase polypeptide to the amino acid sequence of residues 265 to 535 of SEQ ID NO: 2, mutating a nucleic acid encoding the preselected polypeptide at one or more codons for nine amino acid residues in a region of the polypeptide primary amino acid sequence having about 20% or greater sequence identity to residues 265 to 535 of SEQ ID NO: 2, the nine residues in the polypeptide aligning with residues 273, 294, 402, 403, 404, 407, 440, 519 and 520 of SEQ ID NO: 2; and expressing the mutated nucleic acid so that a mutated teφene synthase is made. The invention also features an isolated teφene synthase having about 20% or greater sequence identity to residues 265 to 535 of SEQ ID NO: 2, the synthase comprising sixteen α-carbons having interatomic distances in Angstroms between the α-carbons that are ±2.3 Angstroms of the interatomic distances given in Table 4. The center point of each α-carbon is positioned within a sphere having a radius of 2.3 Angstroms. The center point of each of the spheres has the structural coordinates given in Table 3. Each α-carbon has an associated R-group, and the synthase has an ordered arrangement of R-groups other than the ordered arrangements of R-groups given in Table 8. The synthase can have about 25% or greater sequence identity to residues 265 to 535 of SEQ ID NO: 2, or about 35% or greater sequence identity to residues 265 to 535 of SEQ ID NO: 2. The synthase can catalyse the formation of a teφenoid product from a monoteφene substrate, a sesquiteφene substrate, or a diteφene substrate. The product can be, for example, a cyclic teφenoid hydrocarbon. The ordered arrangement of R-groups in the synthase associated with α-carbons 1 to 16 can be Cys, Tφ, He, He, Ser, Thr, Thr, Tyr, Leu, Cys, Val, Thr, Tyr, Asp, Phe and Thr, respectively. The invention also features an isolated teφene synthase having about 20% or greater sequence identity to residues 265 to 535 of SEQ ID NO: 2, the synthase comprising nineteen α-carbons having interatomic distances in Angstroms between the α-carbons that are ±2.3 Angstroms of the interatomic distances given in Table 2. The center point of each α-carbon is positioned within a sphere having a radius of 2.3 Angstroms. The center points of each sphere have the structural coordinates given in Table 1. Each α-carbon has an associated R-group, and the synthase has an ordered arrangement of the R-groups other than the ordered arrangements of R-groups given in Table 7. The synthase can have about 25% or greater sequence identity to residues 265 to 535 of SEQ ID NO: 2, or about 35% or greater sequence identity to residues 265 to 535 of SEQ ID NO: 2. The synthase can catalyse the formation of a teφenoid product from a monoteφene substrate, a sesquiteφene substrate, or a diteφene substrate. The product can be, for example, a cyclic terpenoid hydrocarbon. The invention also features an isolated protein comprising a first domain having an amino terminal end and a carboxyl terminal end. The first domain comprises amino acids that align structurally in three-dimensional space with a glycosyl hydrolase catalytic core, the glycosyl hydrolase catalytic core selected from the group consisting of amino acids 36 to 230 of glucoamylase protein databank (PDB) code 3GLY of Aspergillus awamori and amino acids 36 to 230 of endoglucanase CelD PDB code 1 CLC. The isolated protein also comprises a second domain having an amino terminal end and carboxyl terminal end. The second domain comprises amino acids that align structurally in three-dimensional space with avian FPP synthase. The carboxyl terminal end of the first domain is linked to the amino terminal end of the second domain. The second domain has about 20% or greater sequence identity to residues 265 to 535 of SEQ ID NO: 2, and comprises nine α-carbons having interatomic distances in Angstroms between the α- carbons that are ±2.3 Angstroms of the interatomic distances given in Table 6. The center point of each α-carbon is positioned within a sphere having a radius of 2.3 Angstroms, the center point of each sphere having the structural coordinates given in Table 5. Each α-carbon has an associated R-group, and the synthase has an ordered arrangement of R-groups other than the ordered arrangements of R-groups given in Table 9. The protein can have about 25% or greater sequence identity to SEQ ID NO: 2, or about 35% or greater sequence identity to SEQ ID NO: 2. The synthase can catalyse the formation of a teφenoid product from a monoteφene substrate, a sesquiteφene substrate, or a diteφene substrate. The product can be, for example, a cyclic teφenoid hydrocarbon. The invention also features an isolated synthase having a region with about 40% or greater sequence identity to residues 343 to 606 of SEQ ID NO: 20, wherein one or more amino acid residues of the synthase that align with amino acid residues at positions 348, 351, 372, 375, 376, 454, 479, 480, 481, 482, 485, 519, 523, 597, 600, 601 , 605, 607 and 608 of SEQ ID NO: 20 are residues other than amino acids Y, L, C, I, T, Y, S, C, G, H, S, L, G, F, G, Y, D, Y and S, respectively. In some embodiments, the sequence identity can be about 20% or greater, 25% or greater, or 35% or greater. In some embodiments, one or more of the ordered arrangements of residues as given in Table 7 are not found in such a synthase. The invention also features an isolated synthase having a region with about 40% or greater sequence identity to residues 316 to 586 of SEQ ID NO: 22, wherein one or more amino acid residues of the synthase that align with amino acid residues at positions 321, 324, 345, 348, 349, 427, 452, 453, 454, 455, 458, 492, 496, 569, 572, 573, 577, 579 and 580 of SEQ ID NO: 22 are residues other than amino acids C, W, N, I, T, Y, S, I, S, G, M, L, D, A, M, Y, D, H and G, respectively. In some embodiments, the sequence identity can be about 20% or greater, 25% or greater, or 35% or greater. In some embodiments, one or more ordered arrangements of residues as given in Table 7 are not found in such a synthase. The invention also features an isolated synthase having a region with about 40% or greater sequence identity to residues 352 to 622 of SEQ ID NO: 58, wherein one or more amino acid residues of the synthase that align with amino acid residues at positions 357, 360, 381 , 384, 385, 463, 487, 488, 489, 490, 493, 528, 532, 606, 609, 610, 614, 616 and 617 of SEQ ID NO: 58 are residues other than amino acids Y, M, C, V, T, F, V, S, S, G, I, L, G, F, V, Y, D, Y and T, respectively. In some embodiments, the sequence identity can be about 20% or greater, 25% or greater, or 35% or greater. In some embodiments, one or more of the ordered arrangements of residues as given in Table 7 are not found in such a synthase. The invention also features an isolated synthase having a region with about 40% or greater sequence identity to amino acid residues 272 to 540 encoded by SEQ ID NO: 33, wherein one or more amino acid residues of the synthase that align with amino acid residues at positions 277, 280, 301, 304, 305, 383, 408, 409, 410, 411 , 414, 448, 452, 524, 527, 528, 532, 534 and 535 encoded by SEQ ID NOS: 33 are residues other than amino acids G, W, I, A, S, Y, T, S, G, Y, L, C, D, M, L, Y, D, Y and T, respectively. In some embodiments, the sequence identity can be about 20% or greater, 25% or greater, or 35% or greater. In some embodiments, one or more of the ordered arrangements of residues as given in Table 7 are not found in such a synthase. The invention also features an isolated synthase having a region with about 40% or greater sequence identity to residues 319 to 571 of SEQ ID NO: 42, wherein one or more amino acid residues of the synthase that align with amino acid residues at positions 324, 327, 348, 351, 352, 430, 455, 456, 457, 458, 461, 495, 499, 571 , 574, 575, 579, 581 and 582 of SEQ ID NO: 42 are residues other than amino acids I, W, V, I, S, Y, T, T, G, L, V, I, N, T, S, Y, D, Y, and T, respectively. In some embodiments, the sequence identity can be about 20% or greater, 25% or greater, or 35% or greater. In some embodiments, one or more of the ordered arrangements of residues as given in Table 7 are not found in such a synthase. The invention also features an isolated synthase having a region with about 40% or greater sequence identity to residues 579 to 847 of SEQ ID NO: 44, wherein one or more amino acid residues of the synthase that align with amino acid residues at positions 584, 587, 606, 609, 610, 688, 713, 714, 715, 716, 719, 753, 757, 831 , 834, 835, 839, 841 and 842 of SEQ ID NO: 44 are residues other than amino acids V, S, G, Q, V, Y, S, V, G, L, C, W, N, V, F, Y, D, Y and G, respectively. In some embodiments, the sequence identity can be about 20% or greater, 25% or greater, or 35% or greater. In some embodiments, one or more of the ordered arrangements of residues as given in Table 7 are not found in such a synthase. The invention also features an isolated synthase having a region with about 40% or greater sequence identity to residues 495 to 767 of SEQ ID NO: 46, wherein one or more amino acid residues of the synthase that align with amino acid residues at positions 500, 503, 524, 527, 528, 606, 631 , 632, 633, 634, 637, 674, 678, 751 , 754, 755, 759, 761 and 762 of SEQ ID NO: 46 are residues other than amino acids F, L, A, Q, T, Y, S, I, G, Q, L, S, D, T, I, F, D, F and G, respectively. In some embodiments, the sequence identity can be about 20% or greater, 25% or greater, or 35% or greater. In some embodiments, one or more of the ordered arrangements of residues as given in Table 7 are not found in such a synthase. The invention also features an isolated synthase having a region with about 40% or greater sequence identity to residues 295 to 564 of SEQ ID NO: 48, wherein one or more amino acid residues of the synthase that align with amino acid residues at positions 300, 303, 324, 327, 328, 406, 431 , 432, 433, 434, 437, 471 , 475, 548, 551, 552, 556, 558 and 559 of SEQ ID NO: 48 are residues other than amino acids Y, W, A, C, T, Y, S, S, G, M, L, G, D, L, I, Y, D, L and Y, respectively. In some embodiments, the sequence identity can be about 20% or greater, 25% or greater, or 35% or greater. In some embodiments, one or more of the ordered arrangements of residues as given in Table 7 are not found in such a synthase. The invention also features an isolated synthase having a region with about 40% or greater sequence identity to residues 307 to 578 of SEQ ID NO: 50, wherein one or more amino acid residues of the synthase that align with amino acid residues at positions 312, 315, 336, 339, 340, 419, 444, 445, 446, 447, 450, 484, 488, 562, 565, 566, 570, 572 and 573 of SEQ ID NO: 50 are residues other than amino acids F, W, A, M, T, Y, N, T, G, M, L, S, D, I, M, Y, D, F and S, respectively. In some embodiments, the sequence identity can be about 20% or greater, 25% or greater, or 35% or greater. In some embodiments, one or more of the ordered arrangements of residues as given in Table 7 are not found in such a synthase. The invention also features an isolated synthase having a region with about 40% or greater sequence identity to residues 264 to 533 of SEQ ID NO: 52, wherein one or more amino acid residues of the synthase that align with amino acid residues at positions 269, 272, 293, 296, 297, 375, 401 , 402, 403, 404, 407, 441, 445, 517, 520, 521 , 525, 527 and 528 of SEQ ID NO: 52 are residues other than amino acids C, W, L, T, S, Y, S, A, G, Y, I, A, N, A, L, Y, D, Y and S, respectively. In some embodiments, the sequence identity can be about 20% or greater, 25% or greater, or 35% or greater. In some embodiments, one or more of the ordered arrangements of residues as given in Table 7 are not found in such a synthase. The invention also features an isolated synthase having a region with about 40% or greater sequence identity to residues 585 to 853 of SEQ ID NO: 56, wherein one or more amino acid residues of the synthase that align with amino acid residues at positions 590, 593, 614, 617, 618, 696, 721, 722, 723, 724, 727, 761 , 765, 837, 840, 841, 845, 847 and 848 of SEQ ID NO: 56 are residues other than amino acids I, S, S, T, V, Y, S, I, A, L, V, G, N, M, F, Y, D, L and T, respectively. In some embodiments, the sequence identity can be about 20% or greater, 25% or greater, or 35% or greater. In some embodiments, one or more of the ordered arrangements of residues as given in Table 7 are not found in such a synthase. The invention also features an isolated synthase having a region with about 40% or greater sequence identity to residues 307 to 574 of SEQ ID NO: 54, wherein one or more amino acid residues of the synthase that align with amino acid residues at positions 312, 315, 336, 339, 340, 418, 443, 444, 445, 446, 449, 483, 487, 560, 563, 564, 566, 568 and 569 of SEQ ID NO: 54 are residues other than amino acids C, W, I, I, T, Y, S, I, S, A, I, L, D, A, I, Y, D, D and G, respectively. In some embodiments, the sequence identity can be about 20% or greater, 25% or greater, or 35% or greater. In some embodiments, one or more of the ordered arrangements of residues as given in Table 7 are not found in such a synthase. The invention also features an isolated synthase having a region with about 40% or greater sequence identity to residues 309 to 577 of SEQ ID NO: 24, wherein one or more amino acid residues of the synthase that align with amino acid residues at positions 314, 317, 338, 341, 342, 420, 446, 447, 448, 449, 452, 485, 489, 560, 563, 564, 569, 571 and 572 of SEQ ID NO: 24 are residues other than amino acids C, W, N, V, T, Y, I, G, G, I, L, L, D, A, I, Y, D, F and G, respectively. In some embodiments, the sequence identity can be about 20% or greater, 25% or greater, or 35% or greater. In some embodiments, one or more of the ordered arrangements of residues as given in Table 7 are not found in such a synthase. The invention also features an isolated synthase having a region with about 40% or greater sequence identity to residues 315 to 584 of SEQ ID NO: 26, wherein one or more amino acid residues of the synthase that align with amino acid residues at positions 320, 323, 344, 347, 348, 426, 451 , 452, 453, 454, 457, 492, 496, 568, 571 , 572, 576, 578 and 579 of SEQ ID NO: 26 are residues other than amino acids S, W, I, A, T, Y, S, V, A, S, I, L, D, A, I, Y, D, F, and G, respectively. In some embodiments, the sequence identity can be about 20% or greater, 25% or greater, or 35% or greater. In some embodiments, one or more of the ordered arrangements of residues as given in Table 7 are not found in such a synthase. The invention also features an isolated synthase having a region with about 40% or greater sequence identity to residues 265 to 536 of SEQ ID NO: 28, wherein one or more amino acid residues of the synthase that align with amino acid residues at positions 270, 273, 294, 297, 298, 376, 401, 402, 403, 404, 407, 440, 444, 518, 521, 522, 528, 530 and 531 of SEQ ID NO: 28 are residues other than amino acids A, W, V, C, G, F, T, S, C, I, M, G, N, C, S, Y, D, Y and S, respectively. In some embodiments, the sequence identity can be about 20% or greater, 25% or greater, or 35% or greater. In some embodiments, one or more of the ordered arrangements of residues as given in Table 7 are not found in such a synthase. The invention also features an isolated synthase having a region with about 40% or greater sequence identity to residues 342 to 612 of SEQ ID NO: 30, wherein one or more amino acid residues of the synthase that align with amino acid residues at positions 347, 350, 371, 374, 375, 453, 478, 479, 480, 481, 483, 518, 522, 596, 599, 600, 604, 606 and 607 of SEQ ID NO: 30 are residues other than amino acids F, L, C, V, T, Y, S, S, A, Y, V, L, G, L, L, Y, D, F and S, respectively. In some embodiments, the sequence identity can be about 20% or greater, 25% or greater, or 35% or greater. In some embodiments, one or more of the ordered arrangements of residues as given in Table 7 are not found in such a synthase. The invention also features an isolated synthase having a region with about 40% or greater sequence identity to residues 273 to 541 of SEQ ID NO: 32, wherein one or more amino acid residues of the synthase that align with amino acid residues at positions 278, 281, 302, 305, 306, 384, 409, 410, 411 , 412, 415, 448, 452, 524, 527, 528, 533, 535 and 536 of SEQ ID NO: 32 are residues other than amino acids C, W, I, I, S, Y, T, S, T, Y, L, C, D, I, T, Y, D, Y and T, respectively. In some embodiments, the sequence identity can be about 20% or greater, 25% or greater, or 35% or greater. In some embodiments, one or more ordered arrangements of residues as given in Table 7 are not found in such a synthase. The invention also features a method for making a teφene synthase, comprising identifying, in a preselected polypeptide having a region with 20% or greater sequence identity to residues 265 to 535 of SEQ ID NO: 2, nine amino acid residues whose α-carbons have interatomic distances in Angstroms between the α- carbons that are ±2.3 Angstroms of the interatomic distances given in Table 6. The center point of each α-carbon is positioned within a sphere having a radius of 2.3 Angstroms. The center point of each sphere has the structural coordinates given in Table 5. The method then comprises synthesizing a polypeptide that is modified from the preselected polypeptide. The modified polypeptide has one or more R- groups associated with the nine α-carbons other than the R-groups associated with the α-carbons in the preselected polypeptide. The synthesizing step can comprise the formation of a nucleic acid encoding the preselected polypeptide in which the coding sequence for one or more amino acids corresponding to the nine α-carbons is replaced by a coding sequence that codes for an amino acid different from the amino acid present in the preselected polypeptide. The preselected polypeptide can be, for example, any one of the polypeptides given in SEQ ID NOS: 2, 4, 6, 8, 10, 12, 20, 22, 24, 26, 28, 30, 32, 34-40, 42, 44, 46, 48, 50, 52, 54, 56, or 58. The invention also features a method of using a teφene synthase, comprising identifying, in a preselected polypeptide having a region with 20% or greater sequence identity to residues 265 to 535 of SEQ ID NO: 2, amino acid residues at nine positions that align with amino acid residues 273, 294, 402, 403, 404, 407, 440, 519 and 520 of SEQ ID NO: 2; and synthesizing a polypeptide that is modified from the preselected polypeptide. The novel polypeptide is modified by having amino acid residues at one or more of the nine positions other than the amino acid residues present in the preselected polypeptide. In some embodiments, the identifying step can comprise identifying sixteen amino acid residues in the preselected polypeptide that align with amino acid residues 270, 273, 294, 297, 298, 402, 403, 404, 407, 440, 516, 519, 520, 525, 527 and 528 of SEQ ID NO: 2, and the synthesizing step can comprise synthesizing a polypeptide that is modified from the preselected polypeptide, the modified polypeptide having amino acid residues at one or more of the sixteen positions other than the amino acid residues present in the preselected polypeptide. In some embodiments, the identifying step can comprise identifying nineteen amino acid residues in the preselected polypeptide that align with amino acid residues 270, 273, 294, 297, 298, 376, 401 , 402, 403, 404, 407, 440, 444, 516, 519, 520, 525, 527 and 528 of SEQ ID NO: 2, and the synthesizing step can comprise synthesizing a polypeptide that is modified from the preselected polypeptide, the modified polypeptide having amino acid residues at one or more of the nineteen positions other than the amino acid residues present in the preselected polypeptide. The synthesizing step can comprise the formation of a nucleic acid encoding the preselected polypeptide in which the coding sequence in the nucleic acid coding for one or more of the identified amino acid residues is replaced by a coding sequence that encodes an amino acid different from the amino acid present in the preselected polypeptide. The preselected polypeptide can be, for example, any one of the polypeptides given in SEQ ID NOS: 2, 4, 6, 8, 10, 12, 20, 22, 24, 26, 28, 30, 32, 34-40, 42, 44, 46, 48, 50, 52, 54, 56, or 58. The method can further comprise: contacting the modified polypeptide with an isoprenoid substrate under conditions effective for the compound to bind the polypeptide; and measuring the ability of the modified polypeptide to catalyze the formation of a reaction product from the isoprenoid substrate. The isoprenoid substrate can be a monoteφene, a sesquiteφene, or a diteφene. The invention also features a method of making a teφene synthase, comprising creating a population of nucleic acid molecules that encode polypeptides, the population having members that differ from one another at one or more of nine codons specifying amino acids of a preselected teφene synthase having a region with about 20% or greater sequence identity to residues 265 to 535 of SEQ ID NO: 2, α-carbons of the nine amino acids having interatomic distances in Angstroms between the α-carbons that are ±2.3 Angstroms of the interatomic distances given in Table 6. The center point of each α-carbon is positioned within a sphere having a radius of 2.3 Angstroms, and the center point of each sphere has the structural coordinates given in Table 5. In some embodiments, the codons specify amino acids as described in Tables 1-2 or 3-4 of a preselected teφene synthase. A portion, or all, of the nucleic acid population is expressed so that a population of polypeptides is made. At least one member of the population of polypeptides is a mutant teφene synthase. The expressing step can comprise in vitro transcription and in vitro translation of the nucleic acid population. In some embodiments, the expressing step comprises cloning members of the nucleic acid population into an expression vector; introducing the expression vector into host cells and expressing the cloned nucleic acid population members in the host cells so that the population of polypeptides is made. The preselected teφene synthase polypeptide can be a monoteφene synthase, a sesquiteφene synthase, or a diteφene synthase. The host cells can be prokaryotic cells or eukaryotic cells, including, without limitation, bacterial cells, fungal cells, and animal cells, e.g., mammalian cells or insect cells. The host cells can also be plant cells, e.g., a cell from a Graminaceae plant, a cell from a Legumineae plant, a cell from a Solanaceae plant, a cell from a Brassicaeae plant or a cell from a Conifereae plant. The invention also features a nucleic acid encoding a synthase as described herein, and a host cell containing such a nucleic acid. The invention also features a transgenic plant containing such a nucleic acid, or a transgenic animal cell culture containing such a nucleic acid. In some embodiments, a synthase polypeptide of the invention comprises a domain that contains an active site comprised of nine α-carbon atoms having the coordinates of Table 5, and interatomic distances between the α-carbons ±2.3 angstroms of the distances given in Table 6. The α-carbon atoms align structurally in three dimensional space in the presence or absence of bound substrate or substrate analogue, with avian FPP synthase. In another embodiment, a synthase of this invention comprises the following: (i) a first domain containing amino acid residues that align in three-dimensional space (in solution or crystal form, and either having a bound or unbound substrate) with a glycosyl hydrolase catalytic core selected from the group consisting of (a) amino acids 36-230 of glycosyl hydrolase (PDB code 3GLY) of Aspergillus awarmori, and (b) amino acids 36-230 of endogiuconase CellB (PDB code 1 CLC), and (ii) a second domain that aligns structurally in three dimensional space with or without substrate or substrate analogues bound in the active site with avian FPP synthase. The second domain contains an active site comprised of nine, sixteen or nineteen α-carbon atoms having the structural coordinates and interatomic distances of Tables 1-2, 3-4 or 5-6. These α-carbon atoms have R-groups attached thereto that can interact, either directly or indirectly, with an isoprenoid substrate. The invention also features a method for generating mutant teφene synthases possessing catalytic activity. The method comprises the steps of (a) providing a crystallographic model of a preselected catalyticaily active teφene synthase having an active site, and (b) using the model to design a teφene synthase having at least one altered R-group in the active site relative to the preselected synthase. The invention also features teφene synthases having altered substrate specificity, methods of making the same, and procedures for generating three- dimensional structures thereof. Although methods and materials similar or equivalent to those described herein can be used to practice the invention, suitable methods and materials are described below. All publications, patent applications, patents and other references mentioned herein are incoφorated by reference in their entirety. Other aspects, embodiments, advantages, and features of the present invention will become apparent from the specification. Brief Description of Drawings Figure 1. Schematic representation of tobacco 5-epi-aristolochene synthase (TEAS) with bound farnesyl hydroxyphosphonate (FHP), prepared using the RIBBONS software program of Carson, M. and Bugg, C, J. Mol. Graphics 4:121 (1986). Figure 2. Structure of twenty natural amino acids showing α-carbons and associated R-groups. Figure 3. Autoradiogram of an argentation thin-layer chromatogram of teφenoid hydrocarbon products made by TEAS and mutant TEAS enzymes using GGPP as a substrate. DM: W273S/C440W mutant TEAS enzyme. Figure 4. Autoradiogram of an argentation thin-layer chromatogram of teφenoid hydrocarbon products made by TEAS and mutant TEAS enzymes using FPP as a substrate. Brief Description of Tables Table 1. X-ray crystallographic structural coordinates for 19 α- carbons found in the active site of a teφene synthase. Table 2. Interatomic distances in Angstroms between each α-carbon of Table 1. Each α-carbon occupies a sphere having a radius of 2.3 Angstroms. Interatomic distances are calculated from the center point of each sphere. Table 3. X-ray crystallographic structural coordinates for 16 α- carbons found in the active site of a teφene synthase. Table 4. Interatomic distances in Angstroms between each α-carbon of Table 3. Each α-carbon occupies a sphere having a radius of 2.3 Angstroms. Interatomic distances are calculated from the center point of each sphere. Table 5. X-ray crystallographic structural coordinates for nine α- carbons found in the active site of a teφene synthase. Table 6. Interatomic distances in Angstroms between each α-carbon of Table 5. Each α-carbon occupies a sphere having a radius of 2.3 Angstroms. Interatomic distances are calculated from the center point of each sphere. Table 7. Ordered arrangement of R-groups not found associated with the α-carbons of Table 1. Table 8. Ordered arrangement of R-groups not found associated with the α-carbons of Table 3. Table 9. Ordered arrangement of R-groups not found associated with the α-carbons of Table 5. Table 10. X-ray structural coordinates for TEAS having the substrate analog FHP bound in the active site. Table 11. X-ray structural coordinates for TEAS in the absence of substrate. Table 12. Alignment of residues 265-535 of TEAS with a limonene synthase, SEQ ID NO: 22, using the BLASTp alignment program. Table 13. Alignment of residues 579 to 847 of SEQ ID NO:44 with SEQ ID NO:26, using the BLASTp program. Table 14. Alignment of residues 265 to 535 of TEAS with SEQ ID NO:48, using the BLASTp program. Table 15. Alignment of residues 307 to 593 of SEQ ID NO:50 with SEQ ID NO:56 using the BLASTp program. Brief Description of the Seguence Listing SEQ ID NOJ is the DNA coding sequence for a tobacco 5-epi- aristolochene synthase (TEAS) protein. Genbank No: Q40577. SEQ ID NO:2 is the amino acid sequence for the protein encoded by the DNA of SEQ ID NO:1. SEQ ID NO:3 is the DNA coding sequence for a TEAS protein in which the codon for Tφ273 has been changed to a codon for Glu. SEQ ID NO:4 is the amino acid sequence for the W273E protein encoded by the TEAS DNA of SEQ ID NO:3. SEQ ID NO:5 is the DNA coding sequence for a TEAS protein in which the codon for Tyr520 has been changed to a codon for Phe. SEQ ID NO:6 is the amino acid sequence for the Y520F protein encoded by the TEAS DNA of SEQ ID NO:5. SEQ ID NO:7 is the DNA coding sequence for a TEAS protein in which the codon for Tyr527 has been changed to a codon for Phe. SEQ ID NO:8 is the amino acid sequence for the Y527F protein encoded by the TEAS DNA of SEQ ID NO:7. SEQ ID NO:9 is the DNA coding sequence for a TEAS protein in which the codon for Tφ273 has been changed to a codon for Ser and the codon for Cys440 has been changed to a codon for Tφ. SEQ ID NO: 10 is the amino acid sequence for the W273S/C440W protein encoded by the TEAS DNA of SEQ ID NO:9. SEQ ID NOJ 1 is the DNA coding sequence for TEAS proteins in which the codons for Tyr406 and Leu407 have each been changed to the nucleotides NNS. SEQ ID NO: 12 is the amino acid sequence for the population of Y406X/L407X proteins encoded by the TEAS DNA of SEQ ID NOJ 1 , where X is any naturally occurring amino acid. SEQ ID NO: 13 is a DNA primer sequence. SEQ ID NO:14 is a DNA primer sequence. SEQ ID NO: 15 is a DNA primer sequence. SEQ ID NO: 16 is a DNA primer sequence. SEQ ID NO: 17 is a DNA primer sequence. SEQ ID NO: 18 is a DNA primer sequence. SEQ ID NO: 19 is the DNA coding sequence for a grand fir pinene synthase. Genbank Accession No: U87909. SEQ ID NO:20 is the amino acid sequence for the protein encoded by the DNA of SEQ ID NO: 19. SEQ ID NO:21 is the DNA coding sequence for a spearmint limonene synthase. Genbank Accession No: L13459. SEQ ID NO:22 is the amino acid sequence for the protein encoded by the DNA of SEQ ID NO:21. SEQ ID NO:23 is the DNA coding sequence for a sage 1 , 8 cineole synthase. Genbank Accession No: AF051899. SEQ ID NO:24 is the amino acid sequence for the protein encoded by the DNA of SEQ ID NO:23. SEQ ID NO:25 is the DNA coding sequence for a sage bornyl diphosphate synthase. Genbank Accession No: AF051900. SEQ ID NO:26 is the amino acid sequence for the protein encoded by the DNA of SEQ ID NO:25. SEQ ID NO:27 is the DNA coding sequence for a mint E-b-famesene synthase. Genbank Accession No: AF024615. SEQ ID NO:28 is the amino acid sequence for the protein encoded by the DNA of SEQ ID NO:27. SEQ ID NO:29 is the DNA coding sequence for a grand fir myrcene synthase. Genbank Accession No: U87908. SEQ ID NO:30 is the amino acid sequence for the protein encoded by the DNA of SEQ ID NO:29. SEQ ID NO:31 is the DNA coding sequence for a potato vetaspiradiene synthase. Genbank Accession No: AB022598. SEQ ID NO:32 is the amino acid sequence for the protein encoded by the DNA of SEQ ID NO:31. SEQ ID NO:33 is the genomic DNA coding sequence for a cotton delta-cadinene synthase. Genbank Accession No: Y18484. SEQ ID NOS:34-40 are the amino acid sequences for the exons encoded by the DNA of SEQ ID NO:33. SEQ ID NO:41 is the DNA coding sequence for a castor bean casbene synthase. Genbank Accession No: L32134. SEQ ID NO:42 is the amino acid sequence for the protein encoded by the DNA of SEQ ID NO:41. SEQ ID NO:43 is the DNA coding sequence for a yew taxadiene synthase. Genbank Accession No: U48796. SEQ ID NO:44 is the amino acid sequence for the protein encoded by the DNA of SEQ ID NO:43. SEQ ID NO:45 is the DNA coding sequence for a grand fir E-alpha- bisabolene synthase. Genbank Accession No: AF006194. SEQ ID NO:46 is the amino acid sequence for the protein encoded by the DNA of SEQ ID NO:45. SEQ ID NO:47 is the DNA coding sequence for a grand fir delta- selinene synthase. Genbank Accession No: U92266. SEQ ID NO:48 is the amino acid sequence for the protein encoded by the DNA of SEQ ID O:47. SEQ ID NO:49 is the DNA coding sequence for a grand fir gamma- humulene synthase. Genbank Accession No: U92267. SEQ ID NO:50 is the amino acid sequence for the protein encoded by the DNA of SEQ ID NO:49. SEQ ID NO:51 is the DNA coding sequence for a tomato germacrene C synthase. Genbank Accession No: AF035631. SEQ ID NO:52 is the amino acid sequence for the protein encoded by the DNA of SEQ ID NO:51. SEQ ID NO:53 is the DNA coding sequence for a sage +sabinene synthase. Genbank Accession No: AF051901. SEQ ID NO:54 is the amino acid sequence for the protein encoded by the DNA of SEQ ID NO:53. SEQ ID NO:55 is the DNA coding sequence for a grand fir abietadiene synthase. Genbank Accession No: U50768. SEQ ID NO:56 is the amino acid sequence for the protein encoded by the DNA of SEQ ID NO:55. SEQ ID NO:57 is the DNA coding sequence for a grand fir limonene synthase. Genbank Accession No: AF006193. SEQ ID NO:58 is the amino acid sequence for the protein encoded by the DNA of SEQ ID NO:57. Detailed Description The following terms are used herein: "α-carbon" refers to the chiral carbon atom found in an amino acid residue. Four substituents are covalently bound to the α-carbon, including an amino group, a carboxyl group, a hydrogen atom, and an R-group. "R-group" refers to a substituent attached to the α-carbon of an amino acid residue that is not involved in peptide bond formation in a protein. An R-group is an important determinant of the overall chemical character of an amino acid. The twenty naturally occurring amino acids found in proteins and the R-groups associated with the α-carbon of each amino acid are listed in Figure 2. The three-letter and one- letter abbreviations for naturally occurring amino acids are sometimes used herein to refer to the R-group associated with a particular amino acid. "Naturally occurring amino acid" includes L-isomers of the twenty amino acids naturally occumng in proteins. Naturally occurring amino acids are glycine, alanine, valine, leucine, isoleucine, serine, methionine, threonine, phenylalanine, tyrosine, tryptophan, cysteine, proline, histidine, aspartic acid, asparagine, glutamic acid, glutamine, arginine, and lysine. Unless specially indicated, all amino acids referred to in this application are in the L-form. Three-letter and one-letter abbreviations are sometimes used herein to refer to naturally occurring amino acids. These abbreviations are known in the art. "Unnatural amino acid" includes amino acids that are not naturally found in proteins. Examples of unnatural amino acids included herein are racemic mixtures of selenocysteine and selenomethionine. In addition, unnatural amino acids include the D or L forms of norleucine, para-nitrophenylalanine, homophenylalanine, para-fluorophenylalanine, 3-amino-2-benzylpropionic acid, homoarginine, D- phenylalanine, and the like. "Positively charged amino acid" includes any naturally occurring or unnatural amino acid having an R-group that carries a positive charge under normal physiological conditions. Examples of positively charged, naturally occurring amino acids include arginine and lysine. "Negatively charged amino acid" includes any naturally occurring or unnatural amino acid having an R-group that carries a negative charge under normal physiological conditions. Examples of negatively charged, naturally occurring amino acids include aspartic acid and glutamic acid. "Hydrophobic amino acid" includes any naturally occurring or unnatural amino acid having an uncharged, nonpolar side chain under normal physiological conditions. Examples of naturally occurring hydrophobic amino acids are leucine, isoleucine, valine and methionine. "Hydrophilic amino acid" includes any naturally occurring or unnatural amino acid having a charged polar side chain. Examples of naturally occurring hydrophilic amino acids include serine, threonine and cysteine. "Mutant teφene synthase" or "mutated teφene synthase" refers to a synthase polypeptide having a primary amino acid sequence. The center point of the α-carboπ of nine residues of the polypeptide is positioned within a sphere having a radius of 2.3 Angstroms; the center points of the nine spheres have the structural coordinates of Table 5 or coordinates which can be rotated and/or translated to coincide with the coordinates of Table 5. The relative interatomic distances between the nine α-carbons is ±2.3 angstroms of the interatomic distances given in Table 6. Each α-carbon has an associated R-group. A mutant synthase differs from a non- mutant synthase in the ordered arrangement of R-groups associated with the nine α- carbons. A mutant synthase has an ordered arrangement of R-groups on the nine α- carbons other than the ordered arrangements of R-groups listed in Table 9. R- groups associated with other α-carbons of the synthase primary amino acid sequence may or may not be the same as in a non-mutated synthase. In some embodiments, a mutant synthase refers to a synthase in which the center point of the α-carbon of sixteen residues of the polypeptide is positioned within a sphere having a radius of 2.3 Angstroms; the center points of the sixteen spheres have the structural coordinates of Table 3 or coordinates which can be rotated and/or translated to coincide with the coordinates of Table 3. The relative interatomic distances between the nine α-carbons is ±2.3 angstroms of the interatomic distances given in Table 4. Each α-carbon has an associated R-group. A mutant synthase differs from a non-mutant synthase in the ordered arrangement of R-groups associated with the sixteen α-carbons. A mutant synthase has an ordered arrangement of R-groups on the sixteen α-carbons other than the ordered arrangements of R-groups listed in Table 8. R-groups associated with other α- carbons of the synthase primary amino acid sequence may or may not be the same as in a non-mutated synthase. In some embodiments, a mutant synthase refers to a synthase in which the center point of the α-carbon of nineteen residues of the polypeptide is positioned within a sphere having a radius of 2.3 Angstroms; the center points of the nineteen spheres have the three dimensional coordinates of Table 1 or coordinates which can be rotated and/or translated to coincide with the coordinates of Table 1. The relative interatomic distances between the nineteen α-carbons is ±2.3 angstroms of the interatomic distances given in Table 2. Each α-carbon has an associated R- group. A mutant synthase differs from a non-mutant synthase in the ordered arrangement of R-groups associated with the nineteen α-carbons. A mutant synthase has an ordered arrangement of R-groups on the nineteen α-carbons other than the ordered arrangements of R-groups listed in Table 7. R-groups associated with other α-carbons of the synthase primary amino acid sequence may or may not be the same as in a non-mutated synthase. "Nonmutated synthase" or "non-mutant synthase" includes a synthase having a primary amino acid sequence comprising nine, sixteen, or nineteen amino acid residues. The center point of each α-carbon of these residues is positioned within a sphere having a radius of 2.3 Angstroms; the center points of the spheres have the three dimensional coordinates of Tables 5, 3, or 1 , respectively, or coordinates which can be rotated and/or translated to coincide with the coordinates of Tables 5, 3, or 1. The relative interatomic distances between the nine, sixteen, or nineteen α-carbons is ±2.3 angstroms of the interatomic distances given in Tables 6, 4, or 2, respectively. Each α-carbon has an associated R-group. A non-mutant synthase has an ordered aσangement of R-groups on the nine, sixteen, or nineteen α-carbons as listed in Tables 9, 8, or 7, respectively. "Degenerate variations thereof refers to variants of a gene coding sequence by which the same polypeptide is encoded by different nucleotide sequences, due to the degeneracy of the genetic code. For example, synthases of the present invention have a primary amino acid sequence. Degenerate synthase variations are different nucleic acid coding sequences that nevertheless encode the same primary amino acid sequence due to the degeneracy of the genetic code. "Expression" refers to transcription of a gene or nucleic acid molecule and the translation of that nucleic acid into a polypeptide. Expression of genes also involves processing of RNA into mRNA in eukaryotic systems. It is not necessary for the genes to integrate into the genome of a cell in order to achieve expression. This definition is not limited to expression in a particular system or a particular cell type and includes, without limitation, stable, transient, in vitro, and in vivo expression. "Promoter" and "promoter regulatory element", refers to a nucleic acid that is involved in controlling expression of a gene. Promoter regulatory elements, and the like, from a variety of sources can be used efficiently to promote gene expression. Promoter regulatory elements include constitutive, tissue-specific, developmental-specific, inducible, subgenomic promoters, and the like. Promoter regulatory elements may also include certain enhancer elements or silencing elements that improve or regulate transcriptional efficiency. "Active Site" refers to a site in a teφene synthase that binds the hydrophobic portion of a teφene substrate, GPP, FPP, and/or GGPP. The active site can, under certain conditions, catalyze a biosynthetic reaction that allows one or more reaction products to be produced. "Altered enzymatic specificity" includes an alteration in the ability of a mutant synthase to use a particular teφene substrate or a change in the profile of reaction product(s) from a mutant synthase, compared to the substrate specificity of and the reaction products made by a corresponding non-mutated synthase. Altered specificity may include the ability of a synthase to exhibit different enzymatic parameters relative to a non-mutated synthase (Km, Vmax, etc), and/or to produce products that are different from those that are produced by a corresponding non- mutant synthase. "Structure coordinates" or "structural coordinates" refers to Cartesian coordinates (x, y, and z positions) derived from mathematical equations involving Fourier synthesis as determined from patterns obtained via diffraction of a monochromatic beam of X-rays by the atoms (scattering centers) of a synthase molecule in crystal form. Diffraction data are used to calculate electron density maps of repeating protein units in the crystal (unit cell). Electron density maps are used to establish the positions of individual atoms within a crystal's unit cell. The absolute values for structural coordinates listed herein convey relative spatial relationships between atoms because the absolute values ascribed to structural coordinates can be changed by rotational and/or translational movement along the x, y and/or z axes, together or separately, while maintaining the same relative spatial relationships among atoms. Thus, a teφene synthase whose absolute values for a set of structural coordinates can be rotationally or translationaily adjusted to coincide with the particular values listed in Tables 1 , 3, or 5 is considered to have the same structural coordinates as those of Tables 1 , 3 or 5. An example of structural coordinates that coincide with the absolute values listed herein after rotation and/or translation are the coordinates of Table 11. "Heavy atom derivatization" refers to a method of producing a chemically modified form of a synthase crystal. In practice, a crystal is soaked in a solution containing heavy atom salts or organometallic compounds, e. g., lead chloride, gold thiomalate, thimerosai, uranyl acetate and the like, which can diffuse through the crystal and bind to the protein's surface. Locations of the bound heavy atoms can be determined by X-ray diffraction analysis of the soaked crystal. The information is then used to construct phase information which can then be used to construct three-dimensional structures of the enzyme as described in Blundel, T. L., and Johnson, N. L., Protein Crystallography, Academic Press (1976). "Unit cell" refers to a basic parallelepiped shaped block. Regular assembly of such blocks may construct the entire volume of a crystal. Each unit cell comprises a complete representation of the unit pattern, the repetition of which builds up the crystal. "Mutagenesis" refers to the substitution of a different amino acid residue at a particular position in the primary amino acid sequence of a protein, thereby changing the R-group present at that position. Mutagenesis can be most easily performed by changing the coding sequence of a nucleic acid encoding the protein so that the coding sequence in the nucleic acid specifies an amino acid residue different from the residue initially present at that position. "Space Group" refers to the arrangement of symmetry elements within a crystal. "Molecular replacement" refers to the generation of a preliminary model of a synthase whose structural coordinates are unknown, by orienting and positioning a molecule whose structural coordinates are known within the unit cell of the unknown crystal so as best to account for the observed diffraction pattern of the unknown crystal. Phases can then be calculated from this model and combined with the observed amplitudes to give an approximate Fourier synthesis of the structure whose coordinates are unknown. This in turn can be subject to any of the several forms of refinement to provide a final, accurate structure of the unknown crystal (Lattman, E., 1985, in Methods in Enzymology, 115:55-77; Rossmann, MG., ed., "The Molecular Replacement Method" 1972, Int. Sci. Rev. Ser., No. 13, Gordon & Breach, New York). Using structure coordinates and interatomic distance matrices, molecular replacement may be used to determine the structural coordinates of a crystalline mutant, homologue, or a different crystal form of terpene synthase. "Recombinant protein" includes a protein that is chemically synthesized or derived biosynthetically from an isolated gene. "Gene" includes naturally derived or genetically manipulated nucleic acids that contain the information needed to produce a polypeptide. "Nucleic acid" includes any genetic material comprised of the nucleotides guanine, adenine, thymine, cytosine, uracil, inosine and the like. Nucleic acids may be single-, double-, or triple stranded. Nucleic acids may be deoxyribonucieic acid or ribonucleic acid. "Genetically manipulated" includes genes that have been modified to contain a different nucleotide sequence from that present in a preselected nulceic acid. Genes can be manipulated by synthetically or via traditional cloning, PCR, chemical gene synthesis, direct or random mutagenesis, and gene shuffling. Genetically manipulated also includes the process of making genes that are degenerate variations of nucleic acids encoding preselected proteins. "First domain" includes polypeptides having a first and second end wherein the first end can have an amino terminal amino acid with a free amino group and can be linked by a peptide bond to a second amino acid. The first end may also be modified through acetylation and the like. The second end of the first domain may or may not have a free carboxyl terminal group. "Second domain" includes polypeptides having a first and second end wherein the first end can have an amino terminal amino acid and can be linked by a peptide bond to a second amino acid. The second end of the second domain may or may not have a carboxyl terminal group. Typically, the first end of the second domain is linked to the second end of the first domain via a peptide bond. "Isoprenoid substrate" refers to the C 10 , C 15 , and C20 molecules, named geranyl diphosphate (GPP), farnesyi diphosphate (FPP), and geranyigeranyl diphosphate (GGPP), respectively. "Sequence identity" or "percent sequence identity" refers to the percentage of amino acids or nucleotides that occupy the same relative position when two protein sequences or nucleic acid sequences, a query sequence and a subject sequence, are aligned. The number of amino acid or nucleotide residues that are identical between both the subject and query sequences are counted, divided by the number of residues in the query sequence, and multiplied by 100. The process is repeated until the alignment resulting in the highest percent sequence identity is found. Percent sequence identity can be determined by visual inspection and/or by using various computer programs, e.g., MegAlign (DNASTAR, Inc., Madison, Wisconsin) or BLAST programs available on the world wide web from the National Center for Biotechnology Information (NCBI). Gaps of one or more residues may sometimes be inserted to maximize sequence alignments to structurally conserved domains of the query sequence, i.e., α-heiices, β-sheets and loops. "Monoterpene product" refers to linear, cyclized, and/or hydroxylated reaction products made from the substrate GPP. "Sesquiteφene product" refers to linear, cyclized, and/or hydroxylated reaction products made from the substrate FPP. "Diteφene product" refers to linear, cyclized, and/or hydroxylated reaction products made from the substrate GGPP. The present invention relates to teφene synthases and mutants thereof from which the position of specific α-carbon atoms and R-groups associated therewith comprising the active site can be determined in three-dimensional space. The invention also relates to structural coordinates of the synthases, use of the structural coordinates to develop structural information related to synthase homologues, mutants, and the like, and to crystal forms of such synthases. Furthermore, the invention provides a method whereby α-carbon structural coordinates for atoms comprising the active site of a preselected teφene synthase can be used to develop synthases in which R-groups associated with active site α- carbon atoms are different from the R-groups found in the preselected teφene synthase. In addition, the present invention provides for the production of novel teφene synthases based on the structural information provided herein and for the use of such synthases to make a variety of isoprenoid compounds. The present invention further provides, for the first time, crystals of a synthase, as exemplified by tobacco 5-epi-aristolochene synthase (TEAS), which are grown in the presence or absence of substrate and substrate analogues, thus allowing definition of the structural coordinates associated therewith. The structural coordinates allow determination of the α-carbon atoms comprising the active site and R-groups associated therewith. The crystals of the present invention belong to the tetragonal space group P4 1 2 1 2; the unit cell dimensions vary by a few angstroms between crystals but on average a = 126 angstroms, c = 122 angstroms, a=b, α = 90°, β = 90°, and γ = 90°. Structural coordinates are preferably obtained at a resolution of about 2.2 to about 2.8 angstroms for a synthase in the presence and in the absence of bound substrate or substrate analog. Coordinates for a synthase with a substrate analog bound in the active site are given in Table 10. Coordinates for a synthase in the absence of a substrate analog bound in the active site are given in Table 11. Those skilled in the art understand that a set of structure coordinates determined by X-ray crystallography is not without standard error. Therefore, for the puφose of this invention, any set of structure coordinates wherein the active site α-carbons of a synthase, synthase homologue, or mutants thereof, have a root mean square deviation less than ±2.3 angstroms when superimposed using the structural coordinates listed in Table 1 , 3, or 5, are considered identical. A schematic representation of the three-dimensional shape of a synthase is shown in Figure 1 which was prepared by RIBBONS (Carson and Bugg, 1986, J. Mol. Graphics, 4:121). The synthase shown in Figure 1 consists entirely of α-helices and short connecting loops and turns, organized into first and second structural domains. In one embodiment, an isolated synthase of the invention comprises sixteen active site α-carbons having the structural coordinates of Table 3 and the relative distances ±2.3 angstroms of the distances given in Table 4. The active site α-carbons of Table 3 generally are not all contiguous, i.e., are not adjacent to one another in the primary amino acid sequence of a synthase, due to intervening amino acid residues between various active site α-carbons. On the other hand, it should be appreciated that some of the active site α-carbons can be adjacent to one another in some instances. In the embodiment depicted in the TEAS Y527F protein (SEQ ID NO:8), for example, active site α-carbons are adjacent to one another in the primary amino acid sequence at positions 402, 403 and 404, respectively, whereas active site α-carbons at residues 273 and 294 are separated and thus are not adjacent. Thus, the numbering of active site α-carbons given in Tables 1 , 2, 3, 4, 5, or 6 is merely for convenience and such α-carbons may reside at any position in the primary amino acid sequence that achieves the structural coordinates given in Tables 1 , 3, or 5 and the relative interatomic distances ±2.3 angstroms given in Tables 2, 4, or 6. An appropriate combination of R-groups, linked to active site α- carbons, can facilitate the formation of one or more desired reaction products. The combination of R-groups selected for use in a teφene synthase of the invention can be any combination other than the ordered arrangements of R-groups and corresponding active site α-carbons shown in Tables 7, 8, or 9. An illustrative example of a suitable arrangement of R-groups and α-carbons is Cys, Tφ, He, He, Ser, Thr, Thr, Tyr, Leu, Cys, Val, Thr, Phe, Asp, Tyr and Thr, associated with active site α-carbons 1 to 16, respectively, of Table 3. Another example of a suitable arrangement of R-groups and α-carbons is Cys, Tφ, He, He, Ser, Thr, Thr, Tyr, Leu, Cys, Val, Thr, Tyr, Asp, Phe, and Thr at active site alpha-carbons 1 to 16, respectively, of Table 3. In some embodiments, a synthase of the invention may have primary amino acid sequences as listed in SEQ ID NO:4, SEQ ID NO:6, SEQ ID NO:8, and SEQ ID NO: 10, DNA molecules encoding the same, which are listed in SEQ ID NO:3, SEQ ID NO:5, SEQ ID NO:7, and SEQ ID NO:9, respectively, and degenerate variations thereof. Typically, R-groups found on active site α-carbons are those found in naturally occurring amino acids. See, e.g., Figure 2. In some embodiments, however, R-groups other than naturally occurring amino acids can be used. Some arrangements of R-groups and active site α-carbons result in mutant teφene synthases that form reaction products. Such enzymatically active synthases and their corresponding genes are useful to make known terpenoid hydrocarbons, e.g., monoteφenes such as pinene, sesquiteφenes such as delta- cadinene and diteφenes such as abietadiene. Other enzymatically active synthases can be used to make novel teφenoid products. Some arrangements of R-groups and active site α-carbons may result in mutant teφene synthases that do not form reaction product(s) at a desired rate. Such synthases and their genes are useful as controls in analyses of product formation by enzymatically active mutant synthases. Such synthases and their genes can also be useful in analyses of translation of enzymatically active mutant synthase genes, or as nutritional supplements. Such synthases can be attached to Sepharose beads and used for affinity purification of isoprenoid compounds from crude preparations. In addition, such synthases and their genes can also be useful to develop reagents for various puφoses, e.g., immunological reagents to monitor expression of a teφene synthase protein or nucleic acid probes or primers to monitor inheritance of a teφene synthase gene in a plant breeding program. In some embodiments, the α-carbon backbone of a synthase first domain aligns structurally with the catalytic core of glycosyl hydrolases, as exemplified by giucoamylase (Brookhaven Protein Database (PDB) code 3GLY) from Aspergillus awamori (Aleshin et al., 1994, J. Mol. Biol., 238:575) and endoglucanase CelD (PDB code ICLC) from Clostridium thermocelum (Juy et al., 1992, Nature, 357:89), and the α-carbon backbone of a synthase second domain, which contains the active site, aligns structurally with avian famesyl diphosphate synthase (FPS), wherein the active site is comprised of 9, 16, or 19 amino acid residues with α-carbon structural coordinates as listed in Tables 1, 3, or 5 and interatomic distances as described in Tables 2, 4, or 6. Such α-carbons have an ordered arrangement of R- groups different from that observed in a non-mutated synthase. In the present invention, the first domain forms a twisted α-barrel made up of eight short (10 to 15 amino acid residues) helices surrounding a surface cavity filled by ordered water molecules when hydrated. The second domain comprises a two-layered barrel of α-helices surrounding a hydrophobic and aromatic- rich active site pocket. Typically, the second domain contains a substrate binding site. As exemplified in Figure 1, helix H is disrupted between segments H1 and H2 by an amino acid such as proline, but its interhelical packing with helix G is accommodated by a corresponding kink in helix G between G1 and G2. Within this kink, hydrogen bonds between a hydroxyl group, such as that found on a threonine, and the carbonyl oxygen of other amino acids disrupt the main chain intrahelical hydrogen bonding of helix G thus assisting in producing the structure as determined. As exemplified by TEAS, teφene synthases of the present invention can have a first domain segment comprising helices A, B, and C (an A-C loop), and a second domain comprising helices J and K (a J-K loop) (Figure 1). The ordering of these loops upon substrate binding results in a closed, solvent-inaccessible active site pocket. As the J-K loop becomes ordered, a lid-type structure is formed that clamps down over the active site entrance in the presence of substrate and an extended aromatic patch deep within the active site pocket is formed. As the A-C loop becomes ordered, it translates inward toward the active site, positioning certain R groups in this loop at or near the active site. Thus, substrate binding to the active site results in a change in protein conformation. To identify or create mutant teφene synthases, sequence alignments can be performed to locate specific residues and α-carbons in a preselected polypeptide that have the structural coordinates and interatomic distances of Tables 1-2, 3-4 or 5-6. The preselected polypeptide is used as the subject sequence in the alignment, e.g., the full-length primary amino acid sequence, a region 190 residues in length, a region 220 residues in length, or a region 300 residues in length. The alignment can use residues 265 to 535 of TEAS (SEQ ID NO: 2), which includes the α-carbons of Tables 1 , 3 or 5, as the query sequence to align with the preselected polypeptide. The preselected polypeptide and the query sequence can be aligned using the BLASTp 2.0.9 computer program with a BLOSUM 62 scoring matrix, an expect value of 10, a gap open value of 11 , an x_dropoff value of 50, a gap extension value of 1 , a wordsize of 3 and no filtering of low complexity sequences. As an alternative, the BLASTp 2.0.9 program can be used with a BLOSUM 50 scoring matrix, an expect value of 10, a gap open value 13, an x_dropoff value of 50, a gap extension value of 2, a wordsize of 3 and no filtering of low complexity sequences Other parameter values can also be used, e g , a gap extension value from 0 to 4 See Altschul, et al., Nucl. Acids Res. 25.3389-3402 Regions of the preselected polypeptide with significant sequence identity to residues 265-535 of TEAS, e.g., 20% or greater sequence identity, 25% or greater sequence identity, 35% or greater sequence identity, 40% or greater sequence identity, 50% or greater sequence identity, 60% or greater sequence identity, 70% or greater sequence identity, or 80% or greater sequence identity are examined for specific residues that align with the TEAS residues corresponding to those listed in Tables 1 , 3, or 5. In some cases, the output of the computer program alignment identifies a specific residue in the preselected polypeptide for each of the nine, sixteen, or nineteen residues in the query sequence having the structural coordinates and interatomic distances of Tables 1-2, 3-4 or 5-6, with or without gaps introduced by the alignment program. In other cases, a gap is introduced by the alignment program in either the query sequence or the subject sequence such that no direct alignment or a misalignment occurs between one or more of the nine, sixteen, or nineteen residues in the query sequence that are of interest. In either case, the output can be visually inspected, and specific residues can be chosen in the subject sequence after adjusting the alignment so that alpha-helices and beta- sheet regions in the query sequence are maintained and that gaps or insertions in the subject sequence align with loop regions of the query sentence. Sequence alignments suggest that other teφene synthases have regions with 20% or greater sequence identity to residues 265-535 of TEAS. Therefore, a region of a teφene synthase other than TEAS can be used as the query sequence, e.g., regions of terpene synthases given in SEQ ID NOS: 4, 6, 8, 10, 12, 20, 22, 24, 26, 28, 30, 32, 3 0, 42, 44, 46, 48, 50, 52, 54, 56, or 58, that have significant sequence identity to residues 265-535 of SEQ ID NO: 2. For example, large sequence insertions are present at the ammo terminus in taxadiene synthase (SEQ ID NO: 44) with respect to TEAS, or are within solvent-exposed loops in the ammo-terminal domain. Thus, regions of taxadiene synthase with greater than 20% sequence identity to SEQ ID NO: 2 are closer to the carboxy-terminal end, e.g., from residue 579 to residue 847 of SEQ ID NO: 44. Useful regions of other teφene synthases that can be used as the query sequence include, without limitation, residues 343 to 606 of SEQ ID NO: 20, 316 to 586 of SEQ ID NO: 22, residues 352 to 622 of SEQ ID NO: 58, residues 272 to 540 encoded by SEQ ID NO: 33, residues 319 to 571 of SEQ ID NO: 42, residues 579 to 847 of SEQ ID NO: 44, residues 495 to 767 of SEQ ID NO: 46, residues 295 to 564 of SEQ ID NO: 48, residues 307 to 578 of SEQ ID NO: 50, residues 264 to 533 of SEQ ID NO: 52, residues 585 to 853 of SEQ ID NO: 56, residues 307 to 574 of SEQ ID NO: 54, residues 309 to 577 of SEQ ID NO: 24, residues 315 to 584 of SEQ ID NO: 26, residues 265 to 536 of SEQ ID NO: 28, residues 342 to 612 of SEQ ID NO: 30 and residues 273 to 541 of SEQ ID NO: 32. One or more of the specific residues in the subject sequence that align with residues in the query sequence are mutated in the preselected polypeptide, e.g. by making mutations in a nucleic acid encoding the polypeptide. The mutant terpene synthase thus created can then be expressed in a host cell and the protein evaluated for enzymatic activity, if desired. Mutant proteins of the present invention may be prepared in a number of ways including but not limited to oligonucleotide-directed mutagenesis, deletion, chemical mutagenesis, and the like. One or more R-groups associated with the active site α-carbon atoms in a teφene synthase are changed by altering the nucleotide sequence of the corresponding gene. For example, a mutation can be introduced into SEQ ID NOJ, the nucleotide sequence for TEAS, at codons encoding one or more of the following sixteen α-carbons: α-carbon 1 = Cys 270; α- carbon 2 = Tφ 273; α-carbon 3 = He 294; α-carbon 4 = He 297; α-carbon 5 = Ser298; α-carbon 6 = Thr 402; α-carbon 7 = Thr 403; α-carbon 8 = Tyr 404; α-carbon 9 = Leu 407; α-carbon 10 = Cys 440; α-carbon 11 = Val 516; α-carbon 12 = Thr 519; α-carbon 13 = Tyr 520; α-carbon 14 = Asp 525; α-carbon 15 = Tyr 527; or α-carbon 16 = Thr 528. The protein encoded by the mutant gene is then produced by expressing the gene in, for example, a bacterial or plant expression system. Alternatively, synthase mutants may be generated by site specific replacement of a particular amino acid with an unnaturally occurring amino acid. As such, synthase mutants may be generated through replacement of an amino acid residue or a particular cysteine or methionine residue with selenocysteine or seienomethionine. This may be achieved by growing a host organism capable of expressing either the wild-type or mutant polypeptide on a growth medium depleted of natural cysteine or methionine or both and growing on medium enriched with either selenocysteine, seienomethionine, or both. These and similar techniques are described in Sambrook et al., (Molecular Cloning, A Laboratory Manual, 2 nd Ed. (1989) Cold Spring Harbor Laboratory Press). Another suitable method of creating mutant synthases of the present invention is based on a procedure described in Noel and Tsal (1989) J. Cell. Biochem., 40:309-320. In so doing, the nucleic acid encoding the synthase can be synthetically produced using oligonucleotides having overlapping regions, the oligonucleotides being degenerate at specific bases so that mutations are induced. According to the present invention, nucleic acid sequences encoding a mutated synthase can be produced by the methods described herein, or any alternative methods available to the skilled artisan. In designing the nucleic acid sequence (gene) of interest, it may be desirable to reengineer the gene for improved expression in a particular expression system. For example, it has been shown that many bacterially derived genes do not express well in plant systems. In some cases, plant-derived genes do not express well in bacteria. This phenomenon may be due to the non-optimal G+C content or A+T content of the gene relative to the expression system being used. For example, the very low G+C content of many bacterial genes results in the generation of sequences mimicking or duplicating plant gene control sequences that are highly A+T rich. The presence of A+T rich sequences within the genes introduced into plants (e.g., TATA box regions normally found in gene promoters) may result in aberrant transcription of the gene(s). In addition, the presence of other regulatory sequences residing in the transcribed mRNA (e.g. polyadenylation signal sequences (AAUAAA) or sequences complementary to small nuclear RNAs involved in pre-mRNA splicing) may lead to RNA instability. Therefore, one goal in the design of genes is to generate nucleic acid sequences that have a G+C content that affords mRNA stability and translation accuracy for a particular expression system. Due to the plasticity afforded by the redundancy of the genetic code (i.e., some amino acids are specified by more than one codon), evolution of the genomes of different organisms or classes of organisms has resulted in differential usage of redundant codons. This "codon bias" is reflected in the mean base composition of protein coding regions. For example, organisms with relatively low G+C contents utilize codons having A or T in the third position of redundant codons, whereas those having higher G+C contents utilize codons having G or C in the third position. Therefore, in reengineering genes for expression, one may wish to determine the codon bias of the organism in which the gene is to be expressed. Looking at the usage of the codons as determined for genes of a particular organism deposited in GenBank can provide this information. After determining the bias thereof, the new gene sequence can be analyzed for restriction enzyme sites as well as other sites that could affect transcription such as exon:intron junctions, polyA addition signals, or RNA polymerase termination signals. Genes encoding synthases can be placed in an appropriate vector, depending on the artisan's interest, and can be expressed using a suitable expression system. An expression vector, as is well known in the art, typically includes elements that permit replication of said vector within the host cell and may contain one or more phenotypic markers for selection of cells containing said gene. The expression vector will typically contain sequences that control expression such as promoter sequences, ribosome binding sites, and translational initiation and termination sequences. Expression vectors may also contain elements such as subgenomic promoters, a repressor gene or various activator genes. The artisan may also choose to include nucleic acid sequences that result in secretion of the gene product, movement of said product to a particular organelie such as a plant plastid (see U.S. Patent Nos. 4,762,785; 5,451 ,513 and 5,545,817), or other sequences that increase the ease of peptide purification, such as an affinity tag. A wide variety of expression control sequences are useful in expressing mutated synthases when operably linked thereto. Such expression control sequences include, for example, the early and late promoters of SV40 for animal cells, the lac system, the tφ system, major operator and promoter systems of phage λ, and the control regions of coat proteins, particularly those from RNA viruses in plants. In E. coli, a useful transcriptional control sequence is the T7 RNA polymerase binding promoter, which can be incoφorated into a pET vector as described by Studier et al., (1990) Methods Enzymology, 185:60-89. For expression, a desired gene should be operably linked to the expression control sequence and maintain the appropriate reading frame to permit production of the desired synthase. Any of a wide variety of well-known expression vectors are of use in the present invention. These include, for example, vectors consisting of segments of chromosomal, non-chromosomal and synthetic DNA sequences such as those derived from SV40, bacterial plasmids (including those from E. coli such as col E1, pCR1, pBR322 and derivatives thereof, pMB9), wider host range plasmids such as RP4, phage DNA such as phage λ, NM989, M13, and other such systems as described by Sambrook et al., (Molecular Cloning, A Laboratory Manual, 2 nd Ed. (1989) Cold Spring Harbor Laboratory Press). A wide variety of host cells are available for expressing synthase mutants of the present invention. Such host cells include, without limitation, bacteria such as E. coli, Bacillus and Streptomyces, fungi, yeast, animal cells, plant ceils, insect cells, and the like. Preferred embodiments of the present invention include teφene synthase mutants that are expressed in E. coli or in plant cells. Said plant cells can either be in suspension culture or a culture on a solid support such as an agar-based medium. Genes encoding synthases of the present invention can also be expressed in transgenic plant cells. In order to produce transgenic plants, vectors containing a nucleic acid construct encoding a mutant teφene synthase are inserted into the plant genome. Preferably, these recombinant vectors are capable of stable integration into the plant genome. One variable in making a transgenic plant is the choice of a selectable marker gene. A selectable marker gene is used to identify transformed cells against a high background of untransformed cells. Such selectable marker genes include but are not limited to aminoglycoside phosphotransferase gene of transposon Tπ5 (Aph II) which encodes resistance to the antibiotics kanamycin, neomycin, and G418, as well as those genes which encode for resistance or tolerance to glyphosate, hygromycin, methotrexate, phosphinothricin, imidazolinones, sulfonylureas, and triazolophyrimidine herbicides, such as chlorosulfuron, bromoxynil, dalapon and the like. In addition to a selectable marker gene, it may be desirable to use a reporter gene. In some instances a reporter gene may be used with a selectable marker. Reporter genes allow the detection of transformed cell and may be used at the discretion of the artisan. A list of these reporter genes is provided in K. Weising et al., 1988, Ann. Rev. Genetics, 22:421. The genes are expressed either by promoters expressing in all tissues at all times (constitutive promoters), by promoters expressing in specific tissues (tissue-specific promoters), promoters expressing at specific stages of development (developmental promoters), and/or promoter expression in response to a stimulus or stimuli (inducible promoters). The choice of these is at the discretion of the artisan. Several techniques exist for introducing foreign genes into plant cells, and for obtaining plants that stably maintain and express the introduced gene. Such techniques include acceleration of genetic material coated directly into cells (U.S. Patent 4,945,050). Plant may also be transformed using Agrobacterium technology (U.S. Patents 5,177,010, 5,104,310, 5,149,645, 5,469,976, 5,464,763, 4,940,838, 4,693,976, 5,591,616, 5,231,019, 5,463,174, 4,762,785, 5,004,863, and 5,159,135; European Patent Applications 116718, 290799, 320500, 604662, 627752, 0267159, and 0292435. Other transformation technologies include whiskers technology, see U. S. Patents 5,302,523 and 5,464,765. Electroporation technology has also been used to transform plants, see WO 87/06614, WO 92/09696 and WO 93/21335 and U.S. Patents 5,472,869 and 5,384,253. Viral vector expression systems can also be used such as those described in U.S. Patent 5,316,931, 5,589,367, 5,811,653, and 5,866,785. In addition to numerous technologies for transforming plants, the type of tissue that is contacted with the genes of interest may vary as well. Suitable tissue includes, but is not limited to, embryogenic tissue, callus tissue, hypocotyl, meristem and the like. Almost all plant tissues may be transformed during dedifferentiation using the appropriate techniques described herein. Regardless of the transformation system used, a gene encoding a mutant synthase is preferably incorporated into a gene transfer vector adapted to express said gene in a plant cell by including in the vector an expression control sequence (plant promoter regulatory element). In addition to plant promoter regulatory elements, promoter regulatory elements from a variety of sources can be used efficiently in plant cells to express foreign genes. For example, promoter regulatory elements of bacterial origin, such as the octopine synthase promoter, the nopaline synthase promoter, the mannopine synthase promoter may be used. Promoters of viral origin, such as the cauliflower mosaic virus (35S and 19S) are also desirable. Plant promoter regulatory elements also include, but are not limited to, ribulose-1 ,6-bisphosphate carboxylase small subunit promoter, beta-conglycinin promoter, phaseoiin promoter, ADH promoter, heat-shock promoters, and tissue specific promoters and the like. Numerous promoters are available to skilled artisans for use at their discretion. It should be understood that not ail expression vectors and expression systems function in the same way to express the mutated gene sequences of the present invention. Neither do all host cells function equally well with the same expression system. However, one skilled in the art may make a selection among these vectors, expression control sequences, and host without undue experimentation and without departing from the scope of this invention. Once a synthase of the present invention is expressed, the protein obtained therefrom can be purified so that structural analysis, modeling, and/or biochemical analysis can be performed, as exemplified herein. The nature of the protein obtained can be dependent on the expression system used. For example, genes, when expressed in mammalian or other eukaryotic ceils, may contain latent signal sequences that may result in glycosylation, phosphorylation, or other post- translational modifications, which may or may not alter function. Once the proteins are expressed, they can be easily isolated and purified using techniques common to the person having ordinary skill in the art of protein biochemistry and as described in Colligan et al., (1997) Current Protocols in Protein Science, Chanda, V.B., Ed., John Wiley & Sons, Inc. Such techniques often include the use of cation-exchange or anion-exchange chromatography, gel filtration-size exclusion chromatography, and the like. Another technique that may be commonly used is affinity chromatography. Affinity chromatography can include the use of antibodies, substrate analogs, or histidine residues (His-tag technology). Once purified, mutants of the present invention may be characterized by any of several different properties. For example, such mutants may have altered active site surface charges of one or more charge units. In addition, the mutants may have an altered substrate specificity or spectrum of reaction product relative to a non- mutated synthase. The present invention allows for the characterization of mutant teφene synthase by crystallization followed by X-ray diffraction. Polypeptide crystallization occurs in solutions where the polypeptide concentration exceeds it solubility maximum (i.e., the polypeptide solution is supersaturated). Such solutions may be restored to equilibrium by reducing the polypeptide concentration, preferably through precipitation of the polypeptide crystals. Often polypeptides may be induced to crystallize from supersaturated solutions by adding agents that alter the polypeptide surface charges or perturb the interaction between the polypeptide and bulk water to promote associations that lead to crystallization. Compounds known as "precipitants" are often used to decrease the solubility of the polypeptide in a concentrated solution by forming an energetically unfavorable precipitating depleted layer around the polypeptide molecules (Weber, 1991, Advances in Protein Chemistry, 41:1-36). In addition to precipitants, other materials are sometimes added to the polypeptide crystallization solution. These include buffers to adjust the pH of the solution and salts to reduce the solubility of the polypeptide. Various precipitants are known in the art and include the following: ethanol, 3-ethyl-2-4 pentanediol, and many of the polyglycols, such as polyethylene glycol. Commonly used polypeptide crystallization methods include the following techniques: batch, hanging drop, seed initiation, and dialysis. In each of these methods, it is important to promote continued crystallization after nucleation by maintaining a supersaturated solution, in the batch method, polypeptide is mixed with precipitants to achieve supersaturation, the vessel is sealed and set aside until crystals appear. In the dialysis method, polypeptide is retained in a sealed dialysis membrane that is placed into a solution containing precipitant. Equilibration across the membrane increases the polypeptide and precipitant concentrations thereby causing the polypeptide to reach supersaturation levels. In the preferred hanging drop technique (McPherson, 1976, J. Biol. Chem., 6300-6306), an initial polypeptide mixture is created by adding a precipitant to a concentrated polypeptide solution. The concentrations of the polypeptide and precipitants are such that in this initial form, the polypeptide does not crystallize. A small drop of this mixture is placed on a glass slide that is inverted and suspended over a reservoir of a second solution. The system is then sealed. Typically, the second solution contains a higher concentration of precipitant or other dehydrating agent. The difference in the precipitant concentrations causes the protein solution to have a higher vapor pressure than the solution. Since the system containing the two solutions is sealed, an equilibrium is established, and water from the polypeptide mixture transfers to the second solution. This equilibrium increases the polypeptide and precipitant concentration in the polypeptide solution. At the critical concentration of polypeptide and precipitant, a crystal of the polypeptide may form. Another method of crystallization introduces a nucleation site into a concentrated polypeptide solution. Generally, a concentrated polypeptide solution is prepared and a seed crystal of the polypeptide is introduced into this solution. If the concentration of the polypeptide and any precipitants are correct, the seed crystal will provide a nucleation site around which larger crystal forms. In preferred embodiments, the crystals of the present invention are formed in hanging drops with 15% PEG 8000; 200 mM magnesium acetate or magnesium chloride, 100 mM 3-(N- moφholino)-2-hydroxypropanesulfonic acid (pH 7.0), 1 mM dithiothreitol as precipitant. Some proteins may be recalcitrant to crystallization. However, several techniques are available to the skilled artisan to induce crystallization. The removal of polypeptide segments at the amino or carboxyl terminal end of the protein may facilitate production of crystalline protein samples. Removal of such segments can be done using molecular biology techniques or treatment of the protein with proteases such as trypsin, chymotrypsin, subtilisin. Such procedures can result in the removal of flexible polypeptide segments that may negatively affect crystallization. The crystals so produced 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 a mutant synthase and to design additional mutants thereof. In addition, crystallization can serve as a further purification method. In some instances, a polypeptide or protein will crystallize from a heterogeneous mixture into crystals. Isolation of such crystals by filtration, centrifugation, etc., followed by redissolving the polypeptide affords a purified solution suitable for use in growing the high-quality crystals needed for diffraction studies. The high-quality crystals may also be dissolved in water and then formulated to provide an aqueous solution having other uses as desired. Because synthases may crystallize in more than one crystal form, the structural coordinates of α-carbons of an active site determined from a synthase or portions thereof, as provided by this invention, are particularly useful to solve the structure of other crystal forms of synthases. The structural coordinates, as provided herein, may also be used to solve the structure of synthases having α-carbons position within the active sites in a manner similar to the wild-type yet having R- groups that may or may not be identical. Furthermore, the structural coordinates disclosed herein may be used to determine the structure of the crystalline form of other proteins with significant amino acid or structural homology to any functional domain of a synthase. One method that may be employed for such purpose is molecular replacement. In this method, the unknown crystal structure, whether it is another crystal form of a synthase, a synthase having a mutated active site, or the crystal of some other protein with significant sequence identity and/or structural homology of a synthase may be determined using the coordinates given in Tables 10 and/or 11. This method provides sufficient structural form for the unknown crystal more efficiently than attempting to determine such information ab initio. In addition, this method can be used to determine whether or not a given synthase in question falls within the scope of this invention. As further disclosed herein, synthases and mutants thereof may be crystallized in the presence or absence of substrates and substrate analogs. The crystal structures of a series of complexes may then be solved by molecular replacement and compared to that of the wild-type to assist in determination of suitable replacements for R-groups within the active site, thus making synthase mutants according to the present invention. All mutants of the present inventions may be modeled using the information disclosed herein without necessarily having to crystallize and solve the structure for each and every mutant. For example, one skilled in the art may use one of several specialized computer programs to assist in the process of designing synthases having mutated active sites. Examples of such programs can be as follows: GRID (Goodford, 1985, J. Med. Chem., 28:849-857); MCSS (Miranker and Kaφlus, 1991, Proteins: Structure, Function and Genetics, 11:29-34); AUTODOCK (Goodsell and Olsen, 1990, Proteins: Structure, Function, and Genetics, 8:195-202); and DOCK (Kuntz et al., 1982, J. Mol. Biol., 161:269-288). In addition, specific computer programs are also available to evaluate specific substrate-active site interactions and the deformation energies and electrostatic interactions resulting therefrom. MODELLER is a computer program often used for homology or comparative modeling of the three-dimensional structure of a protein. A. Sali & T.L. Blundell. J.Mol.Biol. 234, 779-815, 1993. A preselected polypeptide sequence to be modeled is aligned with one or more teφene synthases whose crystal structures are known and the MODELLER program is used to calculate a full-atom model, based on optimum satisfaction of spatial restraints. Such restraints can include, inter alia, homologous structures, fluorescence spectroscopy, NMR experiments, or atom-atom potentials of mean force. The present invention enables synthase mutants to be made and crystal structures thereof to be solved. Moreover, by virtue of the present invention, the location of the active site and the interface of substrate therewith permit the identification of desirable R-groups for mutagenesis. The particular embodiments of this invention are further exemplified in the Examples. However, those skilled in the art will readily appreciate that the specific experiments detailed are only illustrative of the invention as described more fully in the claims, which follow thereafter. EXAMPLE 1 GENERATION OF MUTANT TEAS GENES Construct generation and expression. All mutant enzymes were constructed by the QuickChange method (Stratagene). Manufacturer's instructions were followed, except as noted. Mutations were confirmed by DNA sequencing, and plasmids containing the desired mutation were used to transform BL-21(DE3) expression cells. Protein was expressed, purified, and stored at -80°C. TEAS W273S. The TEAS W273S mutant was generated from a TEAS-pET28b(+) template using the following primers: GTTGAATGCTACTTTTCGGCATTAGGAGTTTAT (sense) (SEQ ID NOJ 3) and ATAAACTCCTAATGCCGAAAAGTAGCATTCAAC (antisense) (SEQ ID NO:14). Mutagenesis was carried out according to the manufacturer's instructions, except that sense and antisense strands were generated in separate reactions. For each, 30 plasmid-copying cycles of one minute, annealing at 55°C and 16 minutes extension at 68°C were carried out. The two reaction mixtures were then combined, heated to 95°C for 2.5 minutes, and cooled to room temperature before Dpnl treatment. TEAS C440W. The TEAS C440W mutant was generated from the TEAS-pET28b(+) template using the following primers: GCTAGTGTAATTATATGGCGAGTTATCGATGAC (sense) (SEQ ID NOJ 5) and GTCATCGATAACTCGCCATATAATTACACTAGC (antisense) (SEQ ID NO: 16). TEAS W273S/C440W. The TEAS C440W W273S mutant was constructed from a TEAS W273S-pET28b(+) template using the primers described for generation of TEAS C440W. TEAS 406/407 random library. For generation of a library of TEAS mutants with random amino acids at positions 406 and 407, two 50 microliter QuickChange reactions were carried out with the TEAS-pET28b(+) template and the primers GCACTAGCAACTACCACATATTACNNSNNSGCGACAACATCGTATTTGGGCATG (sense) (SEQ ID NO:17) and CATGCCCAAATACGATGTTGTCGCSNNSNNGTAATATGTGGTAGTTGCTAGTGC (antisense) (SEQ ID NO: 18), in which N denotes A, C, G, or T and S denotes C or G. By this choice of nucleotides, the reaction included primers which coded for all possible amino acid combinations at positions 406 and 407. No adjustment was made for differing numbers of codons among amino acids. In order to ensure efficient reactions, and to minimize the preference for hybridization of wild-type primers to the template, the primers were designed to be longer than those used to generate the mutations described above. In addition, they were HPLC purified prior to use. After 18 cycles of plasmid copying, the reaction was incubated for two hours with Dpnl, ethanol precipitated, and redissolved in 5 microliters water. Each of four 40 microliter aliquots of E. coli NovaBlue (Novagen) cells were electroporated with 1.5 microliters of the redissolved DNA. After a recovery period, the cells were plated on kanamycin-LB-agar plates. In order to transfer the newly constructed plasmids to expression cells, the colonies were scraped from all four plates, and used to start an 8 mL culture grown in liquid LB medium at 37°C for 8 hours. Plasmid purified from this culture was used to transform 20 microliters of competent BL-21 (DE3) cells. For storage of the constructs, each individual colony was used to inoculate 100 microliters of LB medium containing kanamycin (50 micrograms/mL) in 96-well culture plates. The cells were grown at 37°C until the Aβoo reached approximately one; 100 microliters of 30% glycerol in LB were then added, and the plates were frozen at -80°C. A set of randomly selected colonies were grown from individual glycerol stocks of some colonies, and plasmids were extracted for sequencing. Approximately 30 percent of the colonies were found to be wild-type. Nucleotide and amino acid sequences for TEAS 406/407 mutant genes and proteins are shown in SEQ ID NOS:11 and 12. TEAS Y520F The tyrosine residue at position 520 of SEQ1D No:2 was changed to a phenylalanine residue by site-directed mutagenesis with primers, in a manner similar to that described above. For Y520F the TAT codon was changed to TTC. The nucleotide sequence of the mutant gene is shown in SEQ ID No:5. TEAS Y527F The tyrosine residue at position 527 of SEQ ID No:2 was changed to a phenylalanine residue by site-directed mutagenesis with primers, in a manner similar to that described above. For Y527F, the TAC codon at position 527 of the TEAS amino acid sequence was changed to TTC. The nucleotide sequence of the mutant TEAS Y527F gene is shown in SEQ ID No: 7. TEAS W273E The tryptophan residue at position 273 of SEQ ID No:2 was changed to a phenylalanine residue by site-directed mutagenesis with primers, in a manner similar to that described above. For W273E, the TGG codon at position 273 of the TEAS amino acid sequence was changed to GAG. The nucleotide sequence of the mutant gene is shown in SEQ ID No.:3. EXAMPLE 2 EXPRESSION AND ISOLATION OF SYNTHASE POLYPEPTIDES Unless otherwise noted, mutated and non-mutated TEAS proteins were expressed in Escherichia coli, purified by metal chelation, anion exchange, and gel filtration chromatography. Constructs of TEAS and mutant TEAS proteins in the vector pET- 28b(+) (Novagen) were expressed in E. coli cells. For a typical protein preparation of any of these enzymes, E. coli strain BL21(DE3) cells containing the plasmid construct were grown at 37°C in 4 X 1 L terrific broth to an Aβoo = 0. The temperature was dropped to 22°C, and protein expression was induced by adding IPTG to a final concentration of 0J mM. After 15-20 h, the ceils were harvested by centrifugation, resuspended in 5mL buffer A (20 mM Tris , 500 mM NaCl, 20 mM imidazole, pH 7.9) per 1g cells (wet weight), and stirred for 0.5 h at 4°C. The cells were then lysed by sonication, and the resulting lysate was centrifuged for 0.7 h at 82,000 xg. The supernatant, containing the protein, was loaded over a 2-3 mL Ni 2+ chelating histidine affinity column (Qiagen) equilibrated in buffer A, and the column was washed with additional buffer A until the A ∑ βo of the eluent returned to baseline. The protein was then eluted with a 20-200 mM imidazole gradient in buffer A. Protein-containing fractions were pooled and dialyzed against buffer B (50 mM HEPES, 5mM MgCI2, 1mM DTT), then loaded onto an 8 mL MonoQ cation-exchange column (Pharmacia). The column was washed with 20 column volumes buffer B, and the protein was eluted with a 0-500 mM NaCl gradient in buffer B. The resulting protein was further purified by gel filtration on a Superdex-200 column (Pharmacia) in 50 mM Tris, 100 mM NaCl, 5mM MgCI2, 1mM DTT, pH 8.0. Purified protein was then dialyzed against 5mM Tris, 5mM NaCl, 1mM DTT, pH 8.0, concentrated to 18- 22 mg/mL, and stored at -80°C in 100° L aliquots until needed. EXAMPLE 3 CRYSTALLIZATION AND STRUCTURAL ANALYSIS OF SYNTHASE POLYPEPTIDES Crystal Growth and Microseeding: All crystallization attempts were carried out by the hanging-drop vapor diffusion method. Concentrated protein was mixed with an equal volume (2-5 uL each) of reservoir solution on a plastic cover slip. The cover slip was then inverted over a well of a plastic 24-well tissue culture plate, containing 0.5-1.0 mL of reservoir solution, and sealed by a layer of vacuum grease between the well and cover slip. The plates were incubated at 4°C while the protein concentration in the hanging drop slowly increased by vapor diffusion. Approximately 300 different reservoir solutions, ranging pH 4.5-9 with a variety of precipitants and added salts, were assayed for crystallization of TEAS (SEQ ID NO:2). TEAS crystallized with a reservoir solution of 15% PEG 8000, 100 mM MOPSO (3-[N- moφholino]-2-hydroxypropanesulfonic acid), 200 mM magnesium acetate, 1 mM DTT, pH 6.9-7.3. For microseeding, an existing crystal was crushed in a few uL of precipitant solution, then diluted to 50 microliters. After initial centrifugation to remove large particles, the suspension was serially diluted with additional precipitant solution, and a small volume of a diluted seed stock was added to each new crystallization drop. For macroseeding, crystals which were no longer rapidly growing (usually 2 weeks after drops were set up), were "rinsed" by serially transferring them through two to three drops of reservoir solution. The crystal was then transferred to a fresh drop containing protein and reservoir solution, and equilibrated against a reservoir solution as in the initial growth. Individual crystals varied in their degree of internal order. In some cases, several crystals were screened to identify a well-diffracting crystal with low mosaicity. Data collection: Prior to data collection, crystals were transferred to a drop of reservoir solution, or reservoir solution containing a compound to be soaked into the crystal. A small volume of cryoprotectant solution (15% PEG8000, 100 mM MOPSO, 200 mM Mg acetate, 20% ethylene glycol, 1mM DTT, pH 7) was then added to the drop. After a short equilibration time (1-5 minutes), the crystal was transferred to a drop of cryoprotectant, or cryoprotectant with soaking compound added. After another short equilibration time, the crystal was picked up on a nylon loop, and quickly mounted for data collection in a stream of cold nitrogen gas (90- 11 OK). The TEAS crystals belonged to the tetragonal space group P4 ! 2ι2; the unit cell dimensions varied by a few angstroms between crystals, but on average a = 126A, c = 122 A. The uncomplexed TEAS structure was initially refined to 2.8 A (Table 11 ) against data collected from a crystal grown in the presence of 2 mM FHP (Table 10). Electron density at the active site allowed unambiguous modeling of FHP, the A-C and J-K loops, and nine additional residues at the NH 2 terminus. The refined TEAS-FHP model consisted of residues 17 to 548, three Mg 2 + ions, 150 water molecules, and one FHP molecule. The three-dimensional coordinates for TEAS in the presence of bound substrate is shown in Table 10. The three- dimensional coordinates for TEAS in the absence of FHP is shown in Table 11. Crystals of TEAS complexed with trifiuoro-farnesyl diphosphate (F3- FPP) were also prepared. In these crystals, a well-ordered diphosphate binding pocket was also observed. The A-C loop and the NH2-terminai segment exhibited well-defined electron density, the A-C loop was translated toward the active site, and there was strong electron density for the diphosphate moiety of F3-FPP. The hydrophobic pocket, however, remained flexible; the J-K loop and the famesyl moiety of F3-FPP were disordered. Homology models were created and energy-minimized using the Swiss PDB viewer interface of the SwissModel program (Peitsch MC (1996), Biochem. Soc. Trans., 24:274-279 and Guex N. and Peitsch MC, 1997, Electrophoresis., 18:2714-2723). Active site volumes were calculated with VOIDOO (Kleywegt, G.J., and Jones, T.A., CCP4/ESF-EACBM Newsletter on Protein Crystallography., 29, 26-28, 1993). To make closed active site cavities, the energy- minimized diphosphate moiety from the modeled TEAS cyclase reaction was appended to the residue equivalent to TEAS D301. TEAS W273S crystal structures. Two TEAS W273S structures, in the presence of FHP, were determined from different crystals; both crystals appeared to be well ordered, as clear main-chain and side-chain density were apparent for residues throughout the protein, including the frequently mobile helices D1, D2, and E. Initial difference electron density maps from both crystals immediately revealed the W273S mutations. The two crystals were designated W273S-1 and W273S-2. In each structure, the loops surrounding the active site were ordered, resulting in a closed active site pocket. The A/C loop in each structure was translated toward the active site, forming part of its outer rim, as observed in the wild- type TEAS/FHP complex. However, while the J/K loop of W273S-1 adopted the same conformation observed in the wild-type TEAS/FHP complex, the same loop in W273S-2 adopted a different conformation. In this conformation of the J/K loop, Tyr527 moved away from the side chain of residue 273. In addition, Tyr520 and Asp525 were placed distal to the side chain of Asp444. Hydrogen bonds previously observed between the J/K loop, Arg266, and the N-terminal loop were also missing in the W273S-2 structure. The W273S-2 conformation does not appear to be an effect of the W273S mutation, as it was also observed in a wild-type TEAS crystal soaked with the epi-aristolochene mimic deoxycapsidiol, despite the fact that no electron density was readily apparent for the deoxycapsidiol molecule in that structure. Further, the TEAS active site loops were distant from crystal contacts, and their conformations were not likely to be artifacts of crystal packing. It is possible that at different stages of the TEAS reaction, the enzyme's J/K loop exists in different, defined conformations, and that each of these crystal structures has captured an image of a different conformation. In both W273S structures, residues other than Arg266 and those on the J/K loop did not undergo significant rearrangement from the conformations observed in wild-type TEAS. In each W273S crystal structure, electron density in the active site suggested that the substrate mimic FHP binds in multiple conformations. Some regions of this density possibly represented bound water molecules in the mutant active site. The presence of water molecules in the mutant active site is consistent with the observation that TEAS W273S gives rise to multiple hydroxylated teφenoid reaction products. The FHP electron density in each W273S crystal structure was sufficient to suggest that FHP existed in a more extended conformation in the W273S structure, compared to the more tightly folded conformation of FHP in the wild-type TEAS/FHP complex. The observation that the active site of W273S binds multiple conformations of FHP is consistent with the fact that W273S converts FPP to multiple teφenoid hydrocarbon products. TEAS C440W / W273S: TEAS C440W / W273S crystallized under conditions identical to wild-type TEAS. A 0.3 mm crystal was soaked for 20 minutes in reservoir solution saturated in famesyl hydroxy phosphate (FHP). After cryoprotection and flash freezing as described for wild-type TEAS, data were collected on a laboratory source with Cu-Kα radiation (MacScience Coφ., Japan). A starting model of uncomplexed TEAS (Table 11 ) (Brookhaven Protein Database Code 5EAT (PDB 5EAT), with waters and magnesiums removed, was positioned against the mutant data with the rigid body module of the software program X-PLOR (AT. Brunge, X-PLOR Version 3.1 - A System for X-Ray Crystallography and NMR Yale University Press, New Haven, 1992, pp. 187-207). Rounds of positional and restrained b-factor refinement with buik solvent modeling were also carried out in X- PLOR, with manual model building and adjustment carried out in the software program O (Jones, TA, Zou, JY, Cowan, SW, and Kjeldgaard, M., Acta Cryst. D., 49:148-157, 1993). Additional rounds of refinement and map calculation using the CNS program suite resulted in significantly improved maps; this improvement was likely due to improved bulk solvent modeling. TEAS C440W: TEAS C440W crystallized under conditions identical to wild-type TEAS, except that crystals nucleated less readily and were generally smaller. A mutant crystal was soaked for 6 hours in reservoir solution saturated in FHP before flash-freezing and data collection at SSRL beamiine 7-1 (Stanford Synchrotoon Radiation Laboratory, Menlo Park, California). A starting model of TEAS-FHP (Table 10), with water molecules, ligands, and residues 523-532 of SEQ ID NO:2 removed, was positioned against the data with the rigid body module of X- PLOR. Rounds of positional and restrained b-factor refinement with bulk solvent and overall anisotropic temperature factor modeling were also carried out in X-PLOR, and manual model building and adjustment were carried out in the software program O. As with the double mutant, electron density maps were noticeably improved after refinement and map calculation in CNS. EXAMPLE 4 TERPENE SYNTHASE ENZYME ASSAYS Synthase activity assays were carried out based on the assay described in Vogeli and Chappell, Plant Physiol. 94:1860 (1990) and Vogeii, et al., Plant Physiol. 93:182 (1990). In general, radio-labeled ( 3 H or 14 C) substrate was incubated with enzyme at room temperature in a buffered magnesium salt solution (200 mM Tris, pH 8, 50 mM Mg chloride, 1mM DTT, unless otherwise noted); hydrocarbon products were then selectively extracted into an organic solvent such as hexane. The hexane extract generally was treated with silica gel to remove prenyl alcohols and other oxygenated compounds generated by non-enzymatic hydrolysis of substrate, which partition inefficiently into hexane. Hydrocarbon products present in the hexane phase were quantitated by scintillation counting. A subsequent extraction with a more polar organic solvent such as ethyl acetate was sometimes carried out. Oxygenated compounds more efficiently partition into ethyl acetate-type solvents. Compounds present in the ethyl acetate phase were also quantitated by scintillation counting. Substrate concentrations typically ranged from 0.1 nanomolar to 100 micromolar. In some assays, the substrate was not radiolabeled. Reactions generally were carried out in triplicate for each substrate concentration. Protein concentration was determined by the Bradford method. For determination of steady- state kinetic parameters, enzyme concentrations were chosen such that generation of products over time was linear throughout the course of the reaction. Diteφene synthase assays typically were carried out using 3 H geranylgeranyl diphosphate (GGPP) and enzyme in 250 mM Tris, 10 mM Mg chloride, 1 mM DTT, pH 8.0. Sesquiteφene synthase assays typically were carried out using 14 C or 3 H FPP and enzyme in 100mM Tris, 30 mM Mg chloride, 1 mM DTT, pH 8.0. Monoteφene synthase assays typically were carried out using 3 H GPP and enzyme. As a control for nonspecific binding of GPP by protein, identical reactions were set up which contained BSA, rather than enzyme. Product analysis of wild type and mutant TEAS enzymes by Ag- TLC. Teφenoid hydrocarbon products are not readily separated by thin layer chromatography on normal or reverse-phase plates; however, some can be separated by argentation TLC (Ag-TLC), in which silica plates are first treated with silver nitrate. Ag-TLC described here generally followed the procedure described by Back et al., Arch. Biochem. Biophys. 315:527 (1994). A silica TLC plate was dipped in 15% silver nitrate (aqueous), then dried for 3-5 hours at 110°C. After spotting of tritiated enzymatic products (solvent extract), the plate was developed in beπzene:hexane, ethyl acetate (50:50:1, by volume), sprayed with En 3 Hance (NEN) fluorography spray, placed on film, and exposed for several days to several weeks. Long exposure times were generally necessary, as silver-nitrate treatment of the TLC plate appeared to cause quenching of the fluorography reagent's fluorescence. Alternatively, 14 C labelled products were detected after one to two days without the use of fluorography spray. EXAMPLE 5 ACTIVITY OF TEAS W273S Diterpenβ Synthase Activity of TEAS W273S. The TEAS W273S enzyme and radiolabelled GGPP were incubated as described above and hydrocarbon products were extracted with hexane. Oxygenated products were then extracted with ethyl acetate. Reactions using wild-type TEAS gave counts lower than buffer alone. TEAS W273S, on the other hand, gave counts that were significantly higher for both the hexane and ethyl acetate extracts. Hydrocarbon products formed from GGPP by W273S were distinct from the products made by acid-catalyzed loss of diphosphates from GGPP. See Figure 3. Sesquiterpene Synthase Activity of TEAS W273S. Products of FPP turnover by the purified TEAS W273S mutant were analyzed by argentation thin-layer chromatography (Ag-TLC). One major reaction product had an R f of 0.7 by Ag-TLC, which was distinct from both 5-epi-aristolochene (R f = 0.78) and vetispiradiene (R f = 0.63). See Figure 4. Preliminary GC/MS data showed that hexane extracts from FPP turnover by TEAS W273S contained at least four terpene hydrocarbons, with mass spectra distinct from either 5-epi-aristolochene or vetispiradiene. One of these products had a mass spectrum similar to germacrene A. EXAMPLE 6 ACTIVITY OF TEAS C440W/W273S Diterpene Synthase Activity of TEAS C440W/W273S. The mutant TEAS C440W/W273S protein contains a tryptophan residue at position 440 and a serine residue at position 273. Assays with GGPP were carried out using 0.5 micromolar 3 H GGPP, various concentrations of unlabelled GGPP (Echelon), and enzyme. Reactions were incubated for 60 minutes at room temperature. The TEAS C440W W273S mutant protein converted GGPP to hexane-extractable products, whereas the wild-type enzyme did not. The results indicated that the product profile was altered compared to wild-type TEAS. Hexane-extractable products of GGPP turnover by the double mutant were analyzed by Ag-TLC. The products included two species (R f = 0.11 and 0.28) that were distinct from the hydrolysis product geranyl geraniol (R f = 0.0).To verify that products generated by TEAS C440W/W273S from GGPP were not the hydrolysis product, geranylgeraniol, a sample was analyzed by Ag-TLC. A reaction containing 3 H GGPP (5μm) and enzyme (40μm) in 100 microliters buffer was incubated overnight at room temperature. As controls, 3 H GGPP was incubated in reaction buffer alone and in reaction buffer adjusted to pH 1.5. Both the enzymatic and control reactions were extracted with hexane, which was spotted on an argentation TLC plate, and developed and exposed as described above. The results, shown in Figure 3, demonstrated that the products formed by TEAS C440W/W273S were different from those generated by non-enzymatic degradation of geranylgeranyl diphosphate. Sesquiterpene Synthase Activity of TEAS C440W/W273S. Reactions with FPP as substrate were carried out with 14 C FPP (9μm) and enzyme (160μm) in reaction buffer (20μl). After incubating for 30 minutes at room temperature, products made by TEAS C440W / W273S were analyzed by Ag-TLC. The product profile of the double mutant was similar to that of TEAS W273S, with the addition of a major product having an R f of 0.57. The new product was distinct from both 5-epi-aristolochene and vetispiradiene. Several other products were also formed, many of which migrated slowly upon argentation TLC. See Fig. 4. EXAMPLE 7 ACTIVITY OF TEAS C440W Diterpene Synthase Activity of TEAS C440W. Enzyme assays with TEAS C440W were carried out as described in Example 6. As shown in Fig. 3, no hexane-extractable products were detectable by Ag-TLC after an overnight incubation at room temperature with 160 μm of enzyme and 9 μm radiolabeled GGPP in 20 μl volume. Sesquiterpene Synthase Activity of TEAS C440W. Ag-TLC analysis of the products made from radiolabelled by purified TEAS C440W detected the formation at least one major teφenoid hydrocarbon product (R f 0.63) that was distinct from 5-epi-aristolochene (R f 0.78) and vetispiradiene. The reactions product profile on Ag-TLC is shown in Fig. 4. Small amounts of slowly-migrating products (R f 0-0.09) were also formed. GC/MS analysis of the hexane extract of TEAS C440W teφenoid hydrocarbon reaction products confirmed that this mutant formed a single major sesquiteφene hydrocarbon product as well as a small number of minor hydroxylated products. The mass spectrum of the major product closely matched the published mass spectrum of the spirocyclic compound hinesene. Hinesene differs from vetispiradiene in the stereochemistry at the C3 methyl group. EXAMPLE 8 ACTIVITY OF TEAS W273E Sesquiterpene Synthase Activity of TEAS W273E. Reactions to determine the products made by TEAS W273E using FPP as substrate were carried out essentially as described above, using radiolabeled FPP. The results indicated that at least one product other than 5-epi-aristolochene was formed. The results also indicated that alkylation of TEAS by FPP had occurred. The alkylation was dependent upon the presence of MgCI 2 in the reaction mixture. In control experiments, boiled W273E-TEAS, as well as wild-type TEAS and BSA, were not alkylated. These results indicate that alkylation had occurred at position 273 and that the amino acid residue at position 273 is part of the active site. EXAMPLE 9 ACTIVITY OF TEAS Y520F Sesquiterpene Synthase Activity of TEAS Y520F. Reactions with radiolabeled FPP and TEAS Y520F enzyme were carried out essentially as described above. Reaction products were analysed by Ag-TLC and by GC/MS. A major product of the TEAS Y520F reaction had the same GC retention time as authentic germacrene A and the same mass spectrum as authentic germacrene A. The retention time and mass spectrum of this product were different from 5-epi- aristolochene. EXAMPLE 10 ACTIVITY OF TEAS Y527F Enzymatic Activity of TEAS Y527F. A crude extract of TEAS Y527F enzyme was made by inducing expression in E. coli cells, and sonicating the ceils. The sonicate was clarified and the supernatant used for enzyme assays. No products were observed in assays using GPP as a substrate, indicating that TEAS Y527F does not have monoteφene synthase activity. Reaction products were obtained using FPP as a substrate. Analysis of these products by Ag-TLC indicated that products other than 5-epi-aristolochene were generated by the TEAS Y527F enzyme. EXAMPLE 11 ALIGNMENT OF TERPENE SYNTHASE SEQUENCES Residues 265 to 535 of the TEAS primary amino acid sequence (SEQ ID NO: 2) were aligned with the full-length amino acid sequence of a limonene synthase (SEQ ID NO: 22), using the BLASTp program (NCBI) with a BLOSUM 62 scoring matrix, a gap open value of 11 , a gap extension value of 1 , an x_dropoff value of 50, an expect value of 10, a wordsize of 3 and no filtering of low complexity sequences. The output of the alignment program, shown in Table 12, included a gap between residues 527 and 528 of the TEAS sequence (numbered as 263 and 264 in the alignment output). Residues 321, 324, 345, 348, 349, 427, 452, 453, 454, 455, 458, 492, 496, 569, 572, 573, 577, 579 and 580 were selected as having the most suitable alignment with the 19 TEAS residues. Residue 580 of limonene cyclase instead of residue 583 was selected as aligning with residue 528 of TEAS, in order to maintain the spatial orientation of structural aspects found in TEAS, i.e., α-helices, β- sheets and loops shown in Figure 1 and Table 10. A region including residues 579 to 847 of the taxadiene primary amino acid sequence of SEQ ID NO: 44 was aligned with the full-length amino acid sequence of a bomyl diphosphate synthase (SEQ ID NO: 26), using the BLASTp program (NCBI) with a BLOSUM 62 scoring matrix, a gap open value of 11 , a gap extension value of 1 , an x_dropoff value of 50, an expect value of 10, a wordsize of 3 and no filtering of low complexity sequences. The output of the alignment program, shown in Table 13, included a gap between residues 453 and 454 of the bomyl diphosphate synthase sequence. Residues 321, 324, 344, 347, 348, 426, 451, 452, 453, 454, 457, 492, 496, 568, 571, 572, 576, 578 and 579 of the bomyl diphosphate synthase were selected as having the most suitable alignment with residues 584, 587, 606, 609, 610, 688, 713, 714, 715, 716, 719, 753, 757, 831, 834, 835, 839, 841 and 842 of the query region sequence of SEQ ID NO: 44. Residues 453 and 454 of bomyl diphosphate synthase were selected to align with residues 715 and 716 of taxadiene synthase, in order to maintain the spatial orientation of structural aspects expected to be present in taxadiene synthase, i.e., α-helices, β-sheets and loops shown in Figure 1 and Table 10. Residues 265 to 535 of the TEAS primary amino acid sequence (SEQ ID NO: 2) were aligned with the full-length amino acid sequence of a δ-selinene synthase (SEQ ID NO: 48), using the BLASTp program (NCBI) with a BLOSUM 50 scoring matrix, a gap open value of 13, a gap extension value of 2, an x_dropoff value of 50, an expect value of 10, a wordsize of 3 and no filtering of low complexity sequences. The output of the alignment program is shown in Table 14. Residues 300, 303, 324, 327, 328, 406, 431 , 432, 433, 434, 437, 471 , 475, 548, 551 , 552, 556, 558 and 559 of SEQ ID NO:48 were selected as having the most suitable alignment with residues 270, 273, 294, 297, 298, 376, 401 , 402, 403, 404, 407, 440, 444, 516, 519, 520, 525, 527 and 528 of SEQ ID NO: 2. Residues 307 to 593 of the primary amino acid sequence of γ- humulene synthase (SEQ ID NO: 50) were aligned with the full-length amino acid sequence of abietadiene synthase (SEQ ID NO: 56), using the BLASTp program (NCBI) with a BLOSUM 62 scoring matrix, a gap open value of 11 , a gap extension value of 1 , an x_dropoff value of 50, an expect value of 10, a wordsize of 3 and no filtering of low complexity sequences. The output of the alignment program is shown in Table 15. Residues 590, 593, 614, 617, 618, 696, 721, 722, 723, 724, 727, 761, 765, 837, 840, 841, 845, 847 and 848 of the diteφene synthase (SEQ ID NO: 56) were selected as having the most suitable alignment with residues 312, 315, 336, 339, 340, 419. 444, 445, 446, 447, 450, 484, 488, 562, 565, 566, 570, 572 and 573 of the sesquiteφene synthase query sequence (SEQ ID NO: 50). EXAMPLE 12 GENERATION OF NOVEL MONOTERPENE SYNTHASE GENES A DNA sequence encoding a pinene synthase (SEQ ID NO:20) is used to construct a library of mutant pinene synthase genes. Random mutations are introduced at nucleotides encoding one or more of the following nine amino acid residues: L, C, C, G, H, S, L, G and Y, which correspond to positions 351 , 372, 480, 481, 482, 485, 519, 600 and 601 of SEQ ID NO:20. In some cases, the pinene synthase coding sequence is randomly mutated at nucleotides encoding one or more of amino acid residues 348, 375, 376, 597, 605, 607 and 608, which correspond to positions Y, I, T, F, D, Y and S of SEQ ID NO:20. The pinene synthase coding sequence is sometimes mutated at nucleotides encoding one or more of the following amino acid residues: Y, S and G, which correspond to positions 454, 479 and 523 of SEQ ID NO:20. In some cases, mutations at these ten positions are made in addition to mutations at nucleotides encoding the nine residues mentioned above. In other cases, mutations at these ten positions are made without introducing mutations at the nine residues mentioned above. The pinene synthase coding sequence DNA is inserted in the pET28b(+) vector and mutagenized using the QuickChange® method, following a protocol similar to that described in Example 1 for the TEAS 406/407 random library. The primers used to generate mutations are synthesized as indicated in Example 1 , using N or S as nucleotides in the desired codons in order to generate random mutants. Specific mutations at one or more of the above 19 pinene synthase amino acid residues are made by site-directed mutagenesis using a protocol similar to that described in Example 1 for TEAS. Primers are made that have specific A, T, C or G substitutions in the codons to be mutated, in order to generate the desired mutant(s). Random and/or specific mutations are prepared in a manner similar to that described above to alter amino acid residues of other monoteφene synthases, e.g., limonene synthase, (SEQ ID NOS:22 or 58), myrcene synthase (SEQ ID NO:30), +sabinene synthase (SEQ ID NO:54), 1, 8 cineole synthase (SEQ ID NO:24) and +bomyl diphosphate synthase (SEQ ID NO:26), at residues whose α-carbons have the interatomic distances and structural coordinates described in Tables 1-6. EXAMPLE 13 GENERATION OF NOVEL SESQUITERPENE SYNTHASE GENES A DNA sequence encoding a cadinene synthase (SEQ ID NO:33) is used construct a library of mutant cadinene synthases. Random mutations are introduced at nucleotides encoding one or more of the following nine amino acid residues: W, I, S, G, Y, L, C, L and Y, which correspond to amino acid residues 280, 301, 409, 410, 411, 414, 448, 527 and 528 encoded by SEQ ID NO:33. In some cases, the cadinene synthase coding sequence is mutated at nucleotides encoding one or more of amino acid residues G, A, S, M, D, Y and T, which correspond to amino acid residues 277, 304, 305, 524, 532, 534 and 535 encoded by SEQ ID NO:33. In addition, the cadinene synthase coding sequence is sometimes mutated at nucleotides encoding one or more of the following amino acid residues: 383, 408 and 452, which correspond to amino acids Y, T and D encoded by SEQ ID NO:33. In some cases, these mutations are made in addition to mutations at the nine residues mentioned above. In other cases, mutations at these ten residues are made without introducing mutations at the nine residues mentioned above. The cadinene synthase coding sequence is mutated using the QuickChange® method in the pET28b(+) vector, following a protocol similar to that described in Example 1 for the TEAS 406/407 random library. The primers used to generate mutations are synthesized as indicated in Example 11. Specific mutations at one or more of the above cadinene synthase amino acid residues are made by site-directed mutagenesis using a protocol similar to that described in Example 1 for TEAS. Random and/or specific mutations are prepared in a manner similar to that described above to alter amino acid residues of other sesquiteφene synthases, e.g., vetispiradiene synthase (SEQ ID NO:32), germacrene C synthase (SEQ ID NO:52), E-alpha-bisabolene synthase (SEQ ID NO:46), gamma-humuiene synthase (SEQ ID NO:50), δ-selinene synthase (SEQ ID NO:48), e-b-famesene synthase (SEQ ID NO:28), at residues whose α-carbons have the interatomic distances and structural coordinates described in Tables 1-6. EXAMPLE 14 GENERATION OF NOVEL DITERPENE SYNTHASE GENES A DNA sequence encoding an abietadiene synthase (SEQ ID NO:56) is used construct a library of mutant abietadiene synthases. Random mutations are introduced at nucleotides encoding one or more of the following nine amino acid residues: S, S, I, A, L, V, G, F and Y, which correspond to positions 593, 614, 722, 723, 724, 727, 761, 840 and 841 of SEQ ID NO:56. In some cases, the abietadiene synthase coding sequence is mutated at nucleotides encoding one or more of amino acid residues I, S, T, M, D, L and T, which correspond to positions 590, 617, 618, 837, 845, 847 and 848 of SEQ ID NO:56. The abietadiene synthase coding sequence is sometimes mutated at nucleotides encoding one or more of the following amino acid residues: Y, S and N, which correspond to positions 696, 721 and 765 of SEQ ID NO:56. In some caes, these mutations are made in addition to mutations at the nine residues mentioned above. In other cases, mutations are made at these ten residues without introducing mutations at the nine residues mentioned above. The abietadiene synthase coding sequence is mutated using the QuickChange® method in the pET28b(+) vector, following a protocol similar to that described in Example 1 for the TEAS 406/407 random library. The primers used to generate mutations are synthesized as indicated in Example 11. Specific mutations at one or more of the above abietadiene synthase amino acid residues are made by site-directed mutagenesis using a protocol similar to that described in Example 1 for TEAS. Random and/or specific mutations are prepared in a manner similar to that described above to alter amino acid residues of other diteφene synthases at amino acid residues whose α-carbons have the interatomic distances and structural coordinates described in Tables 1-6, e.g., casbene synthase (SEQ ID NO:42) and taxadiene synthase (SEQ ID NO:44). EXAMPLE 15 EXPRESSION OF MUTANT SYNTHASES IN INSECT, MAMMALIAN AND BACTERIAL CELLS Constructs containing nucleic acids encoding mutant synthases of Examples 12, 13 and/or 14 are introduced into cultured ceils of the insect Spodoptera frugiperda using a baculovirus expression vector. After expression of the gene, the mutant enzyme is isolated and purified from each clone. Constructs containing nucleic acids encoding mutant synthases of Examples 12, 13 and/or 14 are introduced into cultured HeLa ceils using an expression vector having an SV40 promoter. After expression of the gene, the mutant enzyme is isolated and purified from each clone. Constructs containing nucleic acids encoding mutant synthases of Examples 12, 13 and/or 14 are introduced into E. coli BL-21 on a plasmid vector as described in Example 1. The mutant synthase gene is expressed and the mutant enzyme is isolated and purified as described in Example 2. OTHER EMBODIMENTS To the extent not already indicated, it will be understood by those of ordinary skill in the art that any one of the various specific embodiments herein described and illustrated may be further modified to incoφorate features shown in other of the specific embodiments. It is to be understood that while the invention has been described in conjunction with the Detailed Description thereof, that the foregoing description is intended to illustrate, and not limit the scope of the invention, which is defined by the scope of the appended claims. Other aspects, advantages, and modifications are within the scope of the following claims. Table 1 CM Table 3 α- X Y Z Carbon Position Position Position 1 119.144 43.487 44.133 2 120.203 38.695 43.506 3 114.058 43.884 41.015 4 109.327 46.145 41.743 5 110.682 46.410 45.284 6 106.807 36.336 45.151 7 107.629 38.010 41.804 8 109.375 34.842 40.617 9 111.944 37.854 37.602 10 110.233 31.098 47.361 11 115.915 32.218 48.369 12 118.846 34.443 51.796 13 116.461 32.848 54.290 14 114.100 38.006 55.620 15 116.617 41.285 51.702 16 114.855 43.486 54.238 CD Table 5 Table 6 _3 .to CD α> co I- Table 10 Structural Coordinates of Tobacco 5-Epi-Aristolochene Synthase With Famesyl Hydroxyphosphonate Bound Atom Atom Residue Residue X Y Z OCC B- Type # factor 1 CB VAL 17 105.641 55.031 61.062 1.00 98.26 2 CG1 VAL 17 104.598 56.123 61.269 1.00 97.24 3 CG2 VAL 17 105.492 53.957 62.133 1.00 94.24 4 c VAL 17 106.842 53.842 59.190 1.00 98.89 5 O VAL 17 107.108 52.650 59.359 1.00 96.64 6 N VAL 17 104.381 53.419 59.594 1.00 99.88 7 CA VAL 17 105.495 54.412 59.646 1.00 99.06 8 N ALA 18 107.671 54.719 58.615 1.00 98.95 9 CA ALA 18 109.015 54.419 58.088 1.00 98.55 10 CB ALA 18 110.007 55.478 58.572 1.00 97.57 11 c ALA 18 109.570 53.012 58.346 1.00 99.86 12 O ALA 18 109.580 52.170 57.447 1.00 100.00 13 N ASP 19 110.068 52.793 59.562 1.00 99.07 14 CA ASP 19 110.616 51.508 60.010 1.00 97.13 15 CB ASP 19 109.507 50.447 60.064 1.00 96.62 16 CG ASP 19 109.503 49.666 61.370 1.00 97.86 17 OD1 ASP 19 110.119 50.130 62.355 1.00 100.00 18 OD2 ASP 19 108.873 48.588 61.415 1.00 97.98 19 C ASP 19 111.849 50.931 59.301 1.00 95.44 20 O ASP 19 112.812 50.539 59.964 1.00 95.55 21 N PHE 20 111.814 50.854 57.971 1.00 91.33 22 CA PHE 20 112.925 50.297 57.190 1.00 84.17 23 CB PHE 20 112.630 50.377 55.686 1.00 81.03 24 CG PHE 20 111.437 49.572 55.251 1.00 77.17 25 CD1 PHE 20 110.691 49.971 54.147 1.00 74.72 26 CD2 PHE 20 111.056 48.422 55.939 1.00 77.18 27 CE1 PHE 20 109.581 49.239 53.733 1.00 72.36 28 CE2 PHE 20 109.947 47.681 55.535 1.00 78.10 29 CZ PHE 20 109.207 48.092 54.428 1.00 75.86 30 C PHE 20 114.280 50.942 57.465 1.00 82.49 31 O PHE 20 114.400 52.167 57.517 1.00 84.00 32 N SER 21 115.294 50.098 57.639 1.00 78.89 33 CA SER 21 116.656 50.560 57.895 1.00 75.96 34 CB SER 21 117.495 49.433 58.515 1.00 75.81 35 OG SER 21 117.449 48.250 57.731 1.00 80.91 36 C SER 21 117.305 51.063 56.602 1.00 69.67 37 O SER 21 117.070 50.513 55.525 1.00 70.74 38 N PRO 22 118.111 52.134 56.691 1.00 63.25 39 CD PRO 22 118.421 52.939 57.887 1.00 60.39 40 CA PRO 22 118.773 52.680 55.501 1.00 56.42 41 CB PRO 22 119.362 53.994 56.018 1.00 53.56 42 CG PRO 22 119.657 53.688 57.458 1.00 61.97 43 C PRO 22 119.847 51.746 54.939 1.00 55.70 44 0 PRO 22 120.236 50.771 55.589 1.00 52.85 45 N SER 23 120.301 52.038 53.724 1.00 56.69 46 CA SER 23 121.327 51.233 53.065 1.00 53.59 47 CB SER 23 121.600 51.775 51.660 1.00 51.37 48 OG SER 23 122.574 50.995 50.991 1.00 45.40 49 C SER 23 122.620 51.210 53.878 1.00 57.52 50 0 SER 23 123.161 52.258 54.236 1.00 61.76 51 N LEU 24 123.101 50.004 54.168 1.00 58.09 52 CA LEU 24 124.326 49.799 54.944 1.00 55.68 53 CB LEU 24 124.545 48.301 55.191 1.00 60.64 54 CG LEU 24 123.413 47.379 55.651 1.00 67.70 55 CD1 LEU 24 123.810 45.934 55.385 1.00 70.01 56 CD2 LEU 24 123.098 47.596 57.124 1.00 70.77 57 C LEU 24 125.554 50.313 54.198 1.00 51.07 58 0 LEU 24 126.529 50.754 54.808 1.00 50.23 59 N TRP 25 125.472 50.267 52.873 1.00 45.50 60 CA TRP 25 126.563 50.636 51.977 1.00 44.42 61 CB TRP 25 126.356 49.908 50.645 1.00 46.22 62 CG TRP 25 125.853 48.510 50.867 1.00 47.97 63 CD2 TRP 25 126.604 47.407 51.384 1.00 50.67 64 CE2 TRP 25 125.700 46.331 51.553 1.00 50.91 65 CE3 TRP 25 127.948 47.219 51.729 1.00 45.66 66 CD1 TRP 25 124.567 48.070 50.732 1.00 49.99 67 NE1 TRP 25 124.466 46.765 51.147 1.00 47.16 68 CZ2 TRP 25 126.101 45.088 52.053 1.00 52.99 69 CZ3 TRP 25 128.347 45.983 52.227 1.00 47.77 70 CH2 TRP 25 127.423 44.934 52.384 1.00 51.93 71 C TRP 25 126.893 52.110 51.744 1.00 44.49 72 0 TRP 25 127.997 52.550 52.063 1.00 43.75 73 N GLY 26 125.958 52.862 51.172 1.00 47.80 74 CA GLY 26 126.210 54.267 50.894 1.00 39.84 75 C GLY 26 126.744 54.449 49.483 1.00 44.69 76 0 GLY 26 126.375 53.696 48.580 1.00 46.55 77 N ASP 27 127.620 55.434 49.287 1.00 46.92 78 CA ASP 27 128.200 55.708 47.966 1.00 50.38 79 CB ASP 27 128.544 57.196 47.827 1.00 57.61 80 CG ASP 27 127.307 58.091 47.770 1.00 66.06 81 OD1 ASP 27 126.168 57.582 47.895 1.00 64.78 82 OD2 ASP 27 127.482 59.318 47.597 1.00 67.46 83 C ASP 27 129.441 54.857 47.686 1.00 46.14 84 0 ASP 27 130.165 55.082 46.711 1.00 47.50 85 N GLN 28 129.642 53.855 48.536 1.00 40.05 86 CA GLN 28 130.759 52.921 48.461 1.00 28.69 87 CB GLN 28 130.591 51.884 49.575 1.00 25.72 88 CG GLN 28 131.624 50.781 49.615 1.00 32.15 89 CD GLN 28 131.331 49.745 50.688 1.00 33.15 90 OE1 GLN 28 131.873 48.643 50.665 1.00 41.21 91 NE2 GLN 28 130.467 50.097 51.638 1.00 18.55 92 C GLN 28 130.904 52.221 47.108 1.00 27.55 93 0 GLN 28 131.974 51.709 46.787 1.00 21.99 94 N PHE 29 129.840 52.223 46.307 1.00 27.43 95 CA PHE 29 129.874 51.561 45.004 1.00 26.63 96 CB PHE 29 128.840 50.432 44.956 1.00 33.69 97 CG PHE 29 129.070 49.349 45.976 1.00 28.13 98 CD1 PHE 29 128.241 49.241 47.089 1.00 26.35 99 CD2 PHE 29 130.103 48.428 45.817 1.00 27.32 100 CE1 PHE 29 128.432 48.231 48.028 1.00 24.27 101 CE2 PHE 29 130.304 47.410 46.751 1.00 28.00 102 CZ PHE 29 129.466 47.311 47.860 1.00 16.26 103 C PHE 29 129.712 52.451 43.771 1.00 31.14 104 0 PHE 29 129.920 51.976 42.648 1.00 31.41 105 N LEU 30 129.336 53.718 43.962 1.00 33.49 106 CA LEU 30 129.164 54.658 42.844 1.00 39.53 107 CB LEU 30 128.857 56.065 43.366 1.00 47.74 108 CG LEU 30 127.443 56.556 43.658 1.00 54.63 109 CD1 LEU 30 127.508 58.033 44.036 1.00 54.01 110 CD2 LEU 30 126.568 56.378 42.429 1.00 53.57 111 C LEU 30 130.433 54.764 42.009 1.00 40.75 112 0 LEU 30 130.384 54.947 40.787 1.00 34.99 113 N SER 31 131.565 54.671 42.696 1.00 44.10 114 CA SER 31 132.873 54.789 42.077 1.00 47.85 115 CB SER 31 133.730 55.737 42.917 1.00 53.74 116 OG SER 31 133.671 55.353 44.281 1.00 52.06 117 C SER 31 133.669 53.515 41.851 1.00 45.38 118 0 SER 31 133.909 52.743 42.782 1.00 45.28 119 N PHE 32 134.064 53.302 40.602 1.00 43.37 120 CA PHE 32 134.905 52.172 40.232 1.00 45.26 121 CB PHE 32 134.213 50.812 40.251 1.00 42.83 122 CG PHE 32 135.181 49.670 40.073 1.00 33.22 123 CD1 PHE 32 136.098 49.365 41.075 1.00 29.45 124 CD2 PHE 32 135.266 48.984 38.858 1.00 32.90 125 CE1 PHE 32 137.096 48.407 40.875 1.00 28.42 126 CE2 PHE 32 136.261 48.023 38.647 1.00 27.39 127 CZ PHE 32 137.179 47.737 39.655 1.00 28.24 128 C PHE 32 135.601 52.358 38.896 1.00 50.87 129 0 PHE 32 134.988 52.256 37.829 1.00 43.81 130 N SER 33 136.899 52.626 38.989 1.00 55.26 131 CA SER 33 137.755 52.816 37.841 1.00 61.21 132 CB SER 33 138.587 54.094 38.017 1.00 61.87 133 OG SER 33 139.024 54.250 39.360 1.00 67.09 134 C SER 33 138.641 51.583 37.731 1.00 59.75 135 0 SER 33 139.488 51.329 38.589 1.00 59.49 136 N ILE 34 138.368 50.771 36.718 1.00 60.14 137 CA ILE 34 139.128 49.552 36.486 1.00 66.15 138 CB ILE 34 138.426 48.639 35.442 1.00 65.50 139 CG2 ILE 34 138.099 49.423 34.163 1.00 69.37 140 CG1 ILE 34 139.291 47.406 35.157 1.00 65.37 141 CD1 ILE 34 138.715 46.458 34.122 1.00 63.17 142 C ILE 34 140.544 49.875 36.013 1.00 70.13 143 0 ILE 34 140.725 50.551 35.001 1.00 76.00 144 N ASP 35 141.545 49.454 36.782 1.00 73.05 145 CA ASP 35 142.935 49.673 36.388 1.00 70.88 146 CB ASP 35 143.895 49.419 37.558 1.00 76.13 147 CG ASP 35 143.288 48.547 38.638 1.00 84.32 148 OD1 ASP 35 142.931 47.387 38.344 1.00 92.06 149 OD2 ASP 35 143.155 49.030 39.784 1.00 86.08 150 C ASP 35 143.198 48.714 35.227 1.00 68.52 151 0 ASP 35 143.555 47.552 35.425 1.00 65.76 152 N ASN 36 142.940 49.214 34.019 1.00 66.53 153 CA ASN 36 143.083 48.471 32.765 1.00 67.50 154 CB ASN 36 142.949 49.430 31.577 1.00 72.78 155 CG ASN 36 141.889 50.497 31.804 1.00 79.82 156 OD1 ASN 36 140.708 50.194 31.962 1.00 78.35 157 ND2 ASN 36 142.319 51.756 31.853 1.00 84.96 158 C ASN 36 144.383 47.686 32.646 1.00 68.26 159 0 ASN 36 144.461 46.704 31.906 1.00 65.02 160 N GLN 37 145.403 48.143 33.364 1.00 71.27 161 CA GLN 37 146.709 47.500 33.370 1.00 71.18 162 CB GLN 37 147.721 48.431 34.048 1.00 78.38 163 CG GLN 37 149.005 47.761 34.524 1.00 90.52 164 CD GLN 37 149.198 47.904 36.027 1.00 100.00 165 OE1 GLN 37 148.538 48.718 36.673 1.00 100.00 166 NE2 GLN 37 150.106 47.105 36.592 1.00 100.00 167 C GLN 37 146.651 46.131 34.069 1.00 65.44 168 0 GLN 37 147.138 45.138 33.533 1.00 63.18 169 N VAL 38 146.023 46.086 35.244 1.00 57.92 170 CA VAL 38 145.883 44.849 36.021 1.00 51.76 171 CB VAL 38 145.388 45.152 37.461 1.00 50.39 172 CG1 VAL 38 145.198 43.862 38.251 1.00 44.02 173 CG2 VAL 38 146.371 46.071 38.166 1.00 43.36 174 C VAL 38 144.916 43.870 35.349 1.00 52.33 175 0 VAL 38 145.142 42.656 35.348 1.00 48.70 176 N ALA 39 143.858 44.412 34.752 1.00 49.41 177 CA ALA 39 142.848 43.610 34.068 1.00 48.03 178 CB ALA 39 141.722 44.502 33.584 1.00 56.98 179 C ALA 39 143.434 42.823 32.900 1.00 47.68 180 0 ALA 39 143.178 41.627 32.759 1.00 52.03 181 N GLU 40 144.219 43.501 32.068 1.00 46.51 182 CA GLU 40 144.855 42.881 30.908 1.00 40.96 183 CB GLU 40 145.507 43.952 30.036 1.00 49.36 184 CG GLU 40 144.507 44.896 29.383 1.00 62.86 185 CD GLU 40 145.161 46.109 28.745 1.00 67.78 186 OE1 GLU 40 146.229 45.957 28.112 1.00 67.66 187 OE2 GLU 40 144.601 47.218 28.880 1.00 70.01 188 C GLU 40 145.893 41.852 31.337 1.00 38.90 189 0 GLU 40 146.076 40.832 30.678 1.00 39.36 190 N LYS 41 146.569 42.135 32.447 1.00 41.55 191 CA LYS 41 147.584 41.243 32.998 1.00 38.43 192 CB LYS 41 148.219 41.884 34.236 1.00 43.42 193 CG LYS 41 149.304 41.056 34.903 1.00 55.00 194 CD LYS 41 149.864 41.780 36.119 1.00 61.88 195 CE LYS 41 151.040 41.028 36.721 1.00 62.99 196 NZ LYS 41 151.665 41.794 37.835 1.00 69.92 197 C LYS 41 146.914 39.926 33.373 1.00 36.30 198 0 LYS 41 147.362 38.855 32.966 1.00 34.80 199 N TYR 42 145.823 40.027 34.132 1.00 35.61 200 CA TYR 42 145.051 38.868 34.572 1.00 29.43 201 CB TYR 42 143.880 39.307 35.457 1.00 29.64 202 CG TYR 42 144.229 39.658 36.890 1.00 30.55 203 CD1 TYR 42 145.556 39.697 37.330 1.00 37.21 204 CE1 TYR 42 145.866 40.002 38.660 1.00 37.30 205 CD2 TYR 42 143.222 39.937 37.814 1.00 28.62 206 CE2 TYR 42 143.519 40.241 39.139 1.00 37.07 207 CZ TYR 42 144.839 40.272 39.556 1.00 40.82 208 OH TYR 42 145.121 40.567 40.869 1.00 43.81 209 C TYR 42 144.499 38.097 33.377 1.00 30.40 210 0 TYR 42 144.603 36.872 33.318 1.00 29.10 211 N ALA 43 143.920 38.827 32.426 1.00 24.33 212 CA ALA 43 143.340 38.227 31.227 1.00 29.09 213 CB ALA 43 142.713 39.308 30.356 1.00 19.04 214 C ALA 43 144.358 37.423 30.421 1.00 29.23 215 0 ALA 43 144.074 36.308 29.984 1.00 29.14 216 N LYS 44 145.559 37.972 30.260 1.00 37.81 217 CA LYS 44 146.637 37.371 29.491 1.00 40.64 218 C LYS 44 147.069 36.041 30.095 1.00 34.80 219 0 LYS 44 147.221 35.048 29.357 1.00 35.25 220 CB LYS 44 147.824 38.329 29.396 1.00 54.18 221 CG LYS 44 149.001 37.784 28.605 1.00 67.03 222 CD LYS 44 150.141 38.787 28.552 1.00 79.04 223 CE LYS 44 151.313 38.247 27.750 1.00 20.00 224 NZ LYS 44 152.431 39.227 27.673 1.00 20.00 225 N GLU 45 147.332 36.000 31.397 1.00 31.47 226 CA GLU 45 147.771 34.779 32.070 1.00 30.36 227 CB GLU 45 148.288 35.080 33.480 1.00 26.58 228 CG GLU 45 149.071 33.920 34.105 1.00 19.97 229 CD GLU 45 149.394 34.128 35.580 1.00 33.35 230 OE1 GLU 45 149.791 33.146 36.246 1.00 31.26 231 OE2 GLU 45 149.249 35.264 36.080 1.00 37.21 232 C GLU 45 146.649 33.747 32.142 1.00 31.64 233 0 GLU 45 146.902 32.545 32.058 1.00 38.67 234 N ILE 46 145.415 34.225 32.299 1.00 34.27 235 CA ILE 46 144.239 33.358 32.373 1.00 30.12 236 CB ILE 46 142.942 34.181 32.608 1.00 33.74 237 CG2 ILE 46 141.706 33.420 32.123 1.00 32.63 238 CG1 ILE 46 142.812 34.534 34.093 1.00 34.26 239 CD1 ILE 46 141.644 35.444 34.407 1.00 30.01 240 C ILE 46 144.099 32.518 31.110 1.00 29.77 241 0 ILE 46 143.850 31.315 31.186 1.00 30.24 242 N GLU 47 144.283 33.156 29.956 1.00 31.42 243 CA GLU 47 144.185 32.482 28.666 1.00 37.34 244 CB GLU 47 144.460 33.476 27.537 1.00 45.72 245 CG GLU 47 144.290 32.896 26.137 1.00 68.61 246 CD GLU 47 144.808 33.813 25.035 1.00 79.62 247 OE1 GLU 47 145.302 34.922 25.339 1.00 89.55 248 OE2 GLU 47 144.728 33.417 23.852 1.00 86.41 249 C GLU 47 145.169 31.314 28.580 1.00 37.12 250 0 GLU 47 144.860 30.275 27.997 1.00 45.60 251 N ALA 48 146.348 31.492 29.171 1.00 33.83 252 CA ALA 48 147.378 30.459 29.170 1.00 30.76 253 CB ALA 48 148.720 31.054 29.575 1.00 33.78 254 C ALA 48 146.986 29.323 30.110 1.00 30.08 255 0 ALA 48 147.071 28.150 29.743 1.00 30.80 256 N LEU 49 146.542 29.685 31.312 1.00 27.01 257 CA LEU 49 146.110 28.720 32.321 1.00 23.68 258 CB LEU 49 145.793 29.445 33.628 1.00 19.74 259 CG LEU 49 146.936 30.167 34.337 1.00 15.12 260 CD1 LEU 49 146.368 31.161 35.328 1.00 8.67 261 CD2 LEU 49 147.844 29.164 35.033 1.00 12.64 262 C LEU 49 144.862 27.985 31.836 1.00 24.27 263 0 LEU 49 144.610 26.842 32.214 1.00 31.26 264 N LYS 50 144.101 28.663 30.983 1.00 27.77 265 CA LYS 50 142.863 28.154 30.394 1.00 30.88 266 CB LYS 50 142.247 29.263 29.548 1.00 31.45 267 CG LYS 50 140.775 29.153 29.242 1.00 31.65 268 CD LYS 50 140.333 30.468 28.621 1.00 33.98 269 CE LYS 50 138.871 30.468 28.250 1.00 42.53 270 NZ LYS 50 138.455 31.817 27.773 1.00 47.24 271 C LYS 50 143.120 26.925 29.527 1.00 32.84 272 0 LYS 50 142.449 25.901 29.675 1.00 31.46 273 N GLU 51 144.092 27.033 28.625 1.00 33.57 274 CA GLU 51 144.439 25.927 27.741 1.00 38.44 275 CB GLU 51 145.286 26.416 26.566 1.00 45.31 276 CG GLU 51 145.241 25.501 25.339 1.00 54.99 277 CD GLU 51 143.953 25.633 24.532 1.00 61.58 278 0E1 GLU 51 143.086 26.463 24.893 1.00 63.41 279 0E2 GLU 51 143.815 24.912 23.519 1.00 63.99 280 C GLU 51 145.179 24.824 28.501 1.00 37.86 281 0 GLU 51 145.145 23.662 28.097 1.00 43.06 282 N GLN 52 145.867 25.192 29.582 1.00 36.20 283 CA GLN 52 146.592 24.212 30.397 1.00 38.10 284 CB GLN 52 147.453 24.897 31.465 1.00 41.72 285 CG GLN 52 148.691 25.615 30.943 1.00 47.34 286 CD GLN 52 149.505 26.249 32.061 1.00 49.46 287 OE1 GLN 52 149.640 25.683 33.145 1.00 43.98 288 NE2 GLN 52 150.049 27.438 31.799 1.00 53.90 289 C GLN 52 145.563 23.339 31.093 1.00 38.87 290 0 GLN 52 145.732 22.122 31.219 1.00 40.47 291 N THR 53 144.501 23.991 31.554 1.00 37.87 292 CA THR 53 143.407 23.323 32.236 1.00 32.77 293 CB THR 53 142.541 24.347 32.992 1.00 31.08 294 OG1 THR 53 143.315 24.933 34.050 1.00 28.04 295 CG2 THR 53 141.296 23.685 33.569 1.00 32.90 296 C THR 53 142.570 22.522 31.233 1.00 32.05 297 0 THR 53 142.013 21.476 31.573 1.00 29.73 298 N ARG 54 142.529 22.992 29.988 1.00 28.01 299 CA ARG 54 141.785 22.312 28.933 1.00 23.69 300 CB ARG 54 141.723 23.176 27.673 1.00 23.31 301 CG ARG 54 140.724 22.682 26.633 1.00 24.23 302 CD ARG 54 140.755 23.527 25.360 1.00 30.78 303 NE ARG 54 140.674 24.969 25.619 1.00 45.26 304 CZ ARG 54 139.564 25.633 25.942 1.00 46.57 305 NH1 ARG 54 138.405 24.999 26.058 1.00 51.75 306 NH2 ARG 54 139.608 26.946 26.140 1.00 43.00 307 C ARG 54 142.487 20.998 28.617 1.00 30.27 308 0 ARG 54 141.842 19.955 28.479 1.00 33.41 309 N ASN 55 143.821 21.050 28.526 1.00 33.72 310 CA ASN 55 144.648 19.899 28.240 1.00 33.22 311 C ASN 55 144.538 18.872 29.348 1.00 35.28 312 0 ASN 55 144.679 17.660 29.105 1.00 35.19 313 CB ASN 55 146.080 20.341 27.963 1.00 36.29 314 CG ASN 55 146.150 21.264 26.761 1.00 20.00 315 OD1 ASN 55 145.473 21.038 25.754 1.00 20.00 316 ND2 ASN 55 146.963 22.307 26.857 1.00 20.00 317 N MET 56 144.309 19.330 30.581 1.00 34.89 318 CA MET 56 144.150 18.442 31.734 1.00 34.60 319 CB MET 56 144.058 19.241 33.039 1.00 27.26 320 CG MET 56 145.378 19.792 33.544 1.00 38.81 321 SD MET 56 145.237 20.594 35.159 1.00 40.35 322 CE MET 56 145.790 22.242 34.734 1.00 41.02 323 C MET 56 142.880 17.606 31.560 1.00 38.38 324 0 MET 56 142.871 16.406 31.847 1.00 36.10 325 N LEU 57 141.816 18.253 31.084 1.00 33.14 326 CA LEU 57 140.535 17.593 30.852 1.00 33.61 327 CB LEU 57 139.444 18.633 30.566 1.00 24.13 328 CG LEU 57 138.939 19.472 31.742 1.00 25.14 329 CD1 LEU 57 138.092 20.624 31.235 1.00 18.69 330 CD2 LEU 57 138.143 18.604 32.703 1.00 10.16 331 C LEU 57 140.610 16.611 29.686 1.00 37.09 332 0 LEU 57 139.922 15.588 29.679 1.00 34.95 333 N LEU 58 141.453 16.924 28.703 1.00 35.34 334 CA LEU 58 141.605 16.071 27.533 1.00 35.75 335 CB LEU 58 141.930 16.926 26.304 1.00 33.37 336 CG LEU 58 140.886 17.987 25.951 1.00 36.57 337 CD1 LEU 58 141.334 18.779 24.736 1.00 34.54 338 CD2 LEU 58 139.540 17.333 25.691 1.00 38.57 339 C LEU 58 142.628 14.946 27.688 1.00 40.17 340 0 LEU 58 143.001 14.298 26.710 1.00 38.69 341 N ALA 59 143.066 14.697 28.922 1.00 45.53 342 CA ALA 59 144.038 13.637 29.198 1.00 52.73 343 CB ALA 59 144.562 13.754 30.626 1.00 52.29 344 C ALA 59 143.402 12.263 28.950 1.00 60.58 345 0 ALA 59 142.320 11.962 29.450 1.00 62.17 346 N THR 60 144.084 11.432 28.168 1.00 63.55 347 CA THR 60 143.575 10.109 27.794 1.00 63.50 348 CB THR 60 144.405 9.528 26.641 1.00 63.61 349 OG1 THR 60 145.776 9.434 27.039 1.00 67.85 350 CG2 THR 60 144.302 10.426 25.420 1.00 59.57 351 C THR 60 143.372 9.004 28.844 1.00 64.51 352 0 THR 60 142.237 8.681 29.198 1.00 69.94 353 N GLY 61 144.470 8.435 29.337 1.00 59.72 354 CA GLY 61 144.394 7.339 30.294 1.00 59.70 355 C GLY 61 144.087 7.572 31.767 1.00 60.15 356 0 GLY 61 144.627 6.862 32.620 1.00 62.75 357 N MET 62 143.233 8.546 32.098 1.00 62.09 358 CA MET 62 142.904 8.860 33.482 1.00 62.20 359 C MET 62 141.787 7.962 34.001 1.00 57.87 360 0 MET 62 140.858 7.592 33.304 1.00 60.93 361 CB MET 62 142.512 10.333 33.619 1.00 65.78 362 CG MET 62 142.374 10.806 35.057 1.00 71.62 363 SD MET 62 141.924 12.547 35.177 1.00 20.00 364 CE MET 62 141.630 12.940 33.455 1.00 20.00 365 N LYS 63 141.877 7.621 35.308 1.00 53.67 366 CA LYS 63 140.886 6.787 35.975 1.00 51.44 367 CB LYS 63 141.401 6.323 37.342 1.00 55.26 368 CG LYS 63 142.607 5.402 37.287 1.00 65.11 369 CD LYS 63 142.968 4.915 38.682 1.00 69.24 370 CE LYS 63 144.127 3.936 38.635 1.00 76.58 371 NZ LYS 63 144.434 3.376 39.980 1.00 78.96 372 C LYS 63 139.576 7.543 36.173 1.00 48.71 373 0 LYS 63 139.559 8.778 36.167 1.00 48.30 374 N LEU 64 138.490 6.802 36.386 1.00 44.07 375 CA LEU 64 137.182 7.413 36.586 1.00 38.53 376 CB LEU 64 136.100 6.343 36.778 1.00 40.14 377 CG LEU 64 134.671 6.886 36.899 1.00 35.60 378 CD1 LEU 64 134.283 7.589 35.606 1.00 32.53 379 CD2 LEU 64 133.689 5.773 37.203 1.00 30.12 380 C LEU 64 137.184 8.363 37.778 1.00 32.66 381 0 LEU 64 136.773 9.515 37.650 1.00 32.91 382 N ALA 65 137.664 7.881 38.923 1.00 26.30 383 CA ALA 65 137.721 8.683 40.141 1.00 27.29 384 CB ALA 65 138.362 7.885 41.265 1.00 26.12 385 C ALA 65 138.482 9.988 39.919 1.00 33.96 386 0 ALA 65 138.019 11.057 40.318 1.00 35.01 387 N ASP 66 139.630 9.897 39.250 1.00 35.46 388 CA ASP 66 140.459 11.064 38.961 1.00 35.10 389 CB ASP 66 141.776 10.646 38.298 1.00 36.60 390 CG ASP 66 142.685 9.867 39.229 1.00 34.65 391 OD1 ASP 66 142.611 10.067 40.461 1.00 25.86 392 OD2 ASP 66 143.488 9.057 38.717 1.00 44.77 393 C ASP 66 139.746 12.065 38.059 1.00 31.14 394 0 ASP 66 139.846 13.276 38.266 1.00 31.51 395 N THR 67 139.045 11.552 37.051 1.00 26.69 396 CA THR 67 138.316 12.392 36.105 1.00 26.40 397 CB THR 67 137.793 11.571 34.918 1.00 25.70 398 OG1 THR 67 138.891 10.917 34.270 1.00 27.33 399 CG2 THR 67 137.095 12.474 33.918 1.00 28.90 400 C THR 67 137.146 13.113 36.769 1.00 24.73 401 0 THR 67 136.899 14.290 36.502 1.00 27.41 402 N LEU 68 136.425 12.401 37.629 1.00 23.13 403 CA LEU 68 135.295 12.985 38.333 1.00 18.00 404 CB LEU 68 134.504 11.909 39.078 1.00 13.23 405 CG LEU 68 133.804 10.871 38.201 1.00 16.24 406 CD1 LEU 68 133.109 9.843 39.078 1.00 17.55 407 CD2 LEU 68 132.811 11.552 37.272 1.00 7.96 408 C LEU 68 135.787 14.047 39.305 1.00 19.40 409 0 LEU 68 135.181 15.113 39.420 1.00 21.96 410 N ASN 69 136.899 13.766 39.980 1.00 17.72 411 CA ASN 69 137.471 14.714 40.931 1.00 23.29 412 CB ASN 69 138.608 14.071 41.728 1.00 27.45 413 CG ASN 69 138.102 13.102 42.783 1.00 44.15 414 OD1 ASN 69 137.171 13.413 43.530 1.00 45.05 415 ND2 ASN 69 138.709 11.921 42.846 1.00 48.60 416 C ASN 69 137.954 15.985 40.240 1.00 21.73 417 0 ASN 69 137.784 17.083 40.764 1.00 19.56 418 N LEU 70 138.526 15.834 39.050 1.00 19.22 419 CA LEU 70 139.012 16.979 38.293 1.00 18.06 420 CB LEU 70 139.736 16.522 37.025 1.00 14.83 421 CG LEU 70 140.274 17.650 36.141 1.00 18.22 422 CD1 LEU 70 141.330 18.446 36.889 1.00 15.05 423 CD2 LEU 70 140.845 17.078 34.862 1.00 20.94 424 C LEU 70 137.835 17.871 37.925 1.00 20.53 425 0 LEU 70 137.844 19.069 38.212 1.00 23.73 426 N ILE 71 136.817 17.269 37.312 1.00 19.75 427 CA ILE 71 135.613 17.986 36.901 1.00 16.33 428 CB ILE 71 134.617 17.043 36.184 1.00 19.20 429 CG2 ILE 71 133.278 17.744 35.950 1.00 17.41 430 CG1 ILE 71 135.216 16.574 34.856 1.00 25.29 431 CD1 ILE 71 134.273 15.748 34.009 1.00 21.71 432 C ILE 71 134.927 18.661 38.088 1.00 15.45 433 0 ILE 71 134.507 19.813 37.991 1.00 10.60 434 N ASP 72 134.846 17.952 39.212 1.00 14.16 435 CA ASP 72 134.222 18.477 40.425 1.00 13.13 436 CB ASP 72 134.206 17.400 41.516 1.00 9.28 437 CG ASP 72 133.456 17.828 42.766 1.00 8J9 438 0D1 ASP 72 132.472 18.591 42.660 1.00 19.56 439 0D2 ASP 72 133.842 17.381 43.865 1.00 24.87 440 C ASP 72 134.969 19.709 40.926 1.00 20.93 441 0 ASP 72 134.357 20.734 41.230 1.00 31.87 442 N THR 73 136.298 19.618 40.980 1.00 26.21 443 CA THR 73 137.162 20.689 41.452 1.00 17.72 444 C THR 73 137.051 21.912 40.558 1.00 16.99 445 0 THR 73 136.913 23.046 41.054 1.00 15.04 446 CB THR 73 138.627 20.258 41.508 1.00 18.68 447 OG1 THR 73 138.771 19.152 42.406 1.00 20.00 448 CG2 THR 73 139.503 21.413 41.971 1.00 23.27 449 N ILE 74 137.124 21.732 39.245 1.00 13.35 450 CA ILE 74 137.024 22.837 38.298 1.00 15.24 451 CB ILE 74 137.214 22.342 36.844 1.00 17.48 452 CG2 ILE 74 136.841 23.434 35.843 1.00 10.21 453 CG1 ILE 74 138.658 21.881 36.637 1.00 16.00 454 CD1 ILE 74 138.936 21.335 35.253 1.00 19.68 455 C ILE 74 135.677 23.554 38.431 1.00 21.97 456 0 ILE 74 135.603 24.774 38.285 1.00 37.27 457 N GLU 75 134.620 22.793 38.712 1.00 24.94 458 CA GLU 75 133.283 23.362 38.869 1.00 17.86 459 CB GLU 75 132.216 22.266 38.893 1.00 22.45 460 CG GLU 75 131.998 21.565 37.557 1.00 23.19 461 CD GLU 75 130.753 20.685 37.539 1.00 24.24 462 OE1 GLU 75 130.485 19.984 38.540 1.00 11.68 463 OE2 GLU 75 130.041 20.699 36.513 1.00 19.29 464 C GLU 75 133.194 24.181 40.142 1.00 16.49 465 0 GLU 75 132.739 25.323 40.119 1.00 18.93 466 N ARG 76 133.640 23.590 41.248 1.00 11.73 467 CA ARG 76 133.626 24.248 42.552 1.00 15.45 468 CB ARG 76 134.114 23.282 43.636 1.00 7J0 469 CG ARG 76 133.198 22.097 43.899 1.00 15.61 470 CD ARG 76 133.785 21.197 44.975 1.00 12.16 471 NE ARG 76 132.824 20.231 45.508 1.00 16.00 472 CZ ARG 76 132.467 20.165 46.789 1.00 19.23 473 NH1 ARG 76 132.982 21.010 47.670 1.00 26.80 474 NH2 ARG 76 131.618 19.234 47.202 1.00 29.06 475 C ARG 76 134.486 25.519 42.564 1.00 20.45 476 0 ARG 76 134.214 26.454 43.319 1.00 19.47 477 N LEU 77 135.525 25.539 41.732 1.00 20.12 478 CA LEU 77 136.419 26.692 41.634 1.00 19.40 479 CB LEU 77 137.756 26.281 41.014 1.00 12.91 480 CG LEU 77 138.678 25.382 41.843 1.00 12.12 481 CD1 LEU 77 139.825 24.903 40.973 1.00 2.00 482 CD2 LEU 77 139.201 26.125 43.070 1.00 4.07 483 C LEU 77 135.796 27.823 40.818 1.00 22.31 484 0 LEU 77 136.374 28.906 40.702 1.00 30.09 485 N GLY 78 134.628 27.551 40.238 1.00 26.16 486 CA GLY 78 133.915 28.542 39.447 1.00 20.26 487 C GLY 78 134.496 28.855 38.082 1.00 16.66 488 0 GLY 78 134.185 29.898 37.504 1.00 19.22 489 N ILE 79 135.323 27.959 37.553 1.00 13.23 490 CA ILE 79 135.938 28.179 36.247 1.00 16.00 491 CB ILE 79 137.488 28.083 36.321 1.00 14.32 492 CG2 ILE 79 138.055 29.257 37.111 1.00 9.65 493 CG1 ILE 79 137.909 26.751 36.944 1.00 15.84 494 CD1 ILE 79 139.413 26.574 37.082 1.00 20.69 495 C ILE 79 135.420 27.216 35.185 1.00 17.13 496 0 ILE 79 135.860 27.256 34.033 1.00 20.55 497 N SER 80 134.459 26.377 35.567 1.00 21.41 498 CA SER 80 133.878 25.392 34.654 1.00 23.76 499 CB SER 80 133.004 24.393 35.419 1.00 20.88 500 OG SER 80 131.996 25.047 36.170 1.00 23.54 501 C SER 80 133.093 25.977 33.485 1.00 20.44 502 0 SER 80 132.839 25.280 32.505 1.00 28.56 503 N TYR 81 132.723 27.252 33.577 1.00 18.39 504 CA TYR 81 131.972 27.907 32.507 1.00 19.66 505 CB TYR 81 131.389 29.244 32.986 1.00 10.58 506 CG TYR 81 132.396 30.362 33.170 1.00 19.55 507 CD1 TYR 81 132.635 31.285 32.151 1.00 26.56 508 CE1 TYR 81 133.540 32.331 32.320 1.00 23.18 509 CD2 TYR 81 133.092 30.513 34.367 1.00 12.72 510 CE2 TYR 81 133.998 31.555 34.546 1.00 18.75 511 CZ TYR 81 134.218 32.460 33.519 1.00 21.59 512 OH TYR 81 135.122 33.487 33.688 1.00 23.90 513 C TYR 81 132.814 28.103 31.240 1.00 23.33 514 0 TYR 81 132.294 28.498 30.195 1.00 26.36 515 N HIS 82 134.114 27.835 31.352 1.00 27.33 516 CA HIS 82 135.044 27.955 30.229 1.00 28.77 517 CB HIS 82 136.471 28.227 30.724 1.00 20.70 518 CG HIS 82 136.676 29.592 31.301 1.00 18.33 519 CD2 HIS 82 137.002 29.989 32.553 1.00 7.90 520 ND1 HIS 82 136.574 30.742 30.548 1.00 14.62 521 CE1 HIS 82 136.829 31.788 31.312 1.00 11.77 522 NE2 HIS 82 137.091 31.359 32.533 1.00 13.85 523 C HIS 82 135.085 26.654 29.440 1.00 28.78 524 0 HIS 82 135.456 26.643 28.265 1.00 31.36 525 N PHE 83 134.719 25.557 30.098 1.00 30.57 526 CA PHE 83 134.774 24.241 29.475 1.00 32.99 527 CB PHE 83 135.829 23.389 30.191 1.00 38.74 528 CG PHE 83 137.052 24.157 30.603 1.00 40.58 529 CD1 PHE 83 137.204 24.583 31.921 1.00 40.06 530 CD2 PHE 83 138.041 24.476 29.675 1.00 41.50 531 CE1 PHE 83 138.320 25.318 32.309 1.00 43.27 532 CE2 PHE 83 139.163 25.211 30.050 1.00 38.18 533 CZ PHE 83 139.303 25.634 31.371 1.00 46.92 534 C PHE 83 133.444 23.496 29.471 1.00 32.87 535 0 PHE 83 133.378 22.340 29.886 1.00 31.33 536 N GLU 84 132.397 24.133 28.960 1.00 33.76 537 CA GLU 84 131.086 23.496 28.929 1.00 38.03 538 CB GLU 84 129.991 24.514 28.601 1.00 47.83 539 CG GLU 84 129.901 25.690 29.578 1.00 58.57 540 CD GLU 84 129.403 25.312 30.975 1.00 69.66 541 OE1 GLU 84 129.719 24.208 31.479 1.00 74.44 542 OE2 GLU 84 128.695 26.146 31.586 1.00 66.21 543 C GLU 84 131.030 22.314 27.966 1.00 39.30 544 0 GLU 84 130.339 21.328 28.228 1.00 37.93 545 N LYS 85 131.780 22.401 26.872 1.00 37.65 546 CA LYS 85 131.815 21.329 25.886 1.00 40.19 547 CB LYS 85 132.367 21.839 24.551 1.00 49.51 548 CG LYS 85 132.443 20.770 23.469 1.00 57.11 549 CD LYS 85 133.176 21.261 22.237 1.00 73.34 550 CE LYS 85 133.280 20.160 21.180 1.00 81.58 551 NZ LYS 85 134.029 20.532 19.952 1.00 94.03 552 C LYS 85 132.661 20.161 26.381 1.00 37.98 553 0 LYS 85 132.200 19.018 26.404 1.00 43.86 554 N GLU 86 133.894 20.461 26.784 1.00 36.06 555 CA GLU 86 134.825 19.448 27.277 1.00 32.72 556 CB GLU 86 136.122 20.102 27.774 1.00 36.71 557 CG GLU 86 136.998 20.743 26.698 1.00 42.45 558 CD GLU 86 136.500 22.103 26.219 1.00 44.54 559 OE1 GLU 86 135.646 22.720 26.891 1.00 49.68 560 OE2 GLU 86 136.977 22.566 25.162 1.00 47.77 561 C GLU 86 134.213 18.618 28.402 1.00 29.96 562 0 GLU 86 134.254 17.389 28.370 1.00 32.06 563 N ILE 87 133.638 19.303 29.388 1.00 28.21 564 CA ILE 87 133.013 18.648 30.534 1.00 27.11 565 CB ILE 87 132.618 19.672 31.617 1.00 28.37 566 CG2 ILE 87 131.813 18.996 32.729 1.00 28.34 567 CG1 ILE 87 133.880 20.338 32.179 1.00 22.12 568 CD1 ILE 87 133.613 21.386 33.241 1.00 21.16 569 C ILE 87 131.795 17.815 30.150 1.00 27.00 570 0 ILE 87 131.581 16.735 30.700 1.00 29.31 571 N ASP 88 131.007 18.309 29.200 1.00 31.52 572 CA ASP 88 129.815 17.593 28.751 1.00 39.20 573 CB ASP 88 129.009 18.445 27.764 1.00 40.43 574 CG ASP 88 127.717 17.774 27.330 1.00 36.63 575 OD1 ASP 88 126.845 17.539 28.194 1.00 36.19 576 OD2 ASP 88 127.577 17.470 26.125 1.00 42.80 577 C ASP 88 130.173 16.253 28.107 1.00 40.12 578 0 ASP 88 129.660 15.210 28.513 1.00 41.11 579 N ASP 89 131.088 16.251 27.130 1.00 37.03 580 CA ASP 89 131.496 15.096 26.397 1.00 33.87 581 C ASP 89 132.107 14.047 27.304 1.00 33.85 582 0 ASP 89 132.047 12.832 26.978 1.00 33.37 583 CB ASP 89 132.464 15.574 25.325 1.00 27.32 584 CG ASP 89 131.779 16.561 24.391 1.00 34.13 585 OD1 ASP 89 130.528 16.553 24.341 1.00 20.00 586 OD2 ASP 89 132.481 17.345 23.721 1.00 20.00 587 N ILE 90 132.765 14.453 28.372 1.00 31.52 588 CA ILE 90 133.385 13.527 29.308 1.00 25.50 589 CB ILE 90 134.370 14.245 30.258 1.00 22.28 590 CG2 ILE 90 134.861 13.285 31.328 1.00 22.91 591 CG1 ILE 90 135.549 14.818 29.465 1.00 31.26 592 CD1 ILE 90 136.543 15.620 30.301 1.00 31.23 593 C ILE 90 132.297 12.836 30.124 1.00 23.61 594 0 ILE 90 132.331 1 1.620 30.316 1.00 27.20 595 N LEU 91 131.331 13.622 30.593 1.00 23.72 596 CA LEU 91 130.218 13.099 31.379 1.00 20.80 597 CB LEU 91 129.469 14.238 32.071 1.00 20.19 598 CG LEU 91 130.232 14.888 33.225 1.00 17.15 599 CD1 LEU 91 129.464 16.078 33.772 1.00 13.18 600 CD2 LEU 91 130.479 13.852 34.318 1.00 9.86 601 C LEU 91 129.270 12.281 30.510 1.00 22.03 602 0 LEU 91 128.649 11.334 30.988 1.00 22.93 603 N ASP 92 129.183 12.640 29.231 1.00 21.86 604 CA ASP 92 128.337 11.930 28.276 1.00 23.86 605 CB ASP 92 128.314 12.668 26.933 1.00 30.84 606 CG ASP 92 127.282 12.105 25.973 1.00 37.16 607 OD1 ASP 92 126.182 12.690 25.879 1.00 34.52 608 OD2 ASP 92 127.568 11.083 25.309 1.00 45.02 609 C ASP 92 128.928 10.539 28.090 1.00 30.87 610 0 ASP 92 128.208 9.542 28.106 1.00 38.64 611 N GLN 93 130.247 10.490 27.914 1.00 33.31 612 CA GLN 93 130.974 9.239 27.738 1.00 34.79 613 CB GLN 93 132.454 9.531 27.466 1.00 46.61 614 CG GLN 93 133.345 8.300 27.331 1.00 60.12 615 CD GLN 93 134.831 8.640 27.354 1.00 75.57 616 OE1 GLN 93 135.217 9.801 27.510 1.00 79.60 617 NE2 GLN 93 135.672 7.621 27.208 1.00 81.92 618 C GLN 93 130.833 8.380 28.994 1.00 35.74 619 0 GLN 93 130.620 7.171 28.906 1.00 39.97 620 N ILE 94 130.933 9.019 30.159 1.00 32.85 621 CA ILE 94 130.817 8.326 31.441 1.00 35.57 622 CB ILE 94 131.191 9.266 32.625 1.00 33.17 623 CG2 ILE 94 130.909 8.588 33.969 1.00 25.21 624 CG1 ILE 94 132.671 9.652 32.538 1.00 32.16 625 CD1 ILE 94 133.120 10.631 33.603 1.00 32.74 626 C ILE 94 129.407 7.770 31.645 1.00 38.37 627 0 ILE 94 129.224 6.716 32.260 1.00 45.31 628 N TYR 95 128.421 8.477 31.102 1.00 38.86 629 CA TYR 95 127.021 8.082 31.212 1.00 39.68 630 CB TYR 95 126.122 9.249 30.784 1.00 34.17 631 CG TYR 95 124.637 8.974 30.877 1.00 27.88 632 CD1 TYR 95 124.060 8.539 32.070 1.00 26.18 633 CE1 TYR 95 122.697 8.279 32.155 1.00 24.69 634 CD2 TYR 95 123.810 9.144 29.770 1.00 21.67 635 CE2 TYR 95 122.447 8.888 29.845 1.00 22.88 636 CZ TYR 95 121.896 8.454 31.039 1.00 23.25 637 OH TYR 95 120.546 8.185 31.112 1.00 32.19 638 C TYR 95 126.715 6.846 30.369 1.00 40.10 639 0 TYR 95 125.987 5.953 30.803 1.00 41.67 640 N ASN 96 127.291 6.796 29.173 1.00 40.40 641 CA ASN 96 127.073 5.682 28.261 1.00 50.10 642 CB ASN 96 127.273 6.146 26.815 1.00 50.46 643 CG ASN 96 126.252 7J89 26.392 1.00 53.74 644 OD1 ASN 96 125.093 7.141 26.806 1.00 52.90 645 ND2 ASN 96 126.679 8.138 25.567 1.00 56.55 646 C ASN 96 127.911 4.434 28.545 1.00 54.46 647 0 ASN 96 127.502 3.324 28.202 1.00 58.60 648 N GLN 97 129.067 4.606 29.183 1.00 57.00 649 CA GLN 97 129.933 3.469 29.494 1.00 62.35 650 CB GLN 97 131.385 3.924 29.690 1.00 63.17 651 CG GLN 97 131.622 4.834 30.885 1.00 68.59 652 CD GLN 97 133.052 5.351 30.970 1.00 68.54 653 OE1 GLN 97 133.659 5.357 32.040 1.00 66.32 654 NE2 GLN 97 133.594 5.798 29.836 1.00 59.07 655 C GLN 97 129.458 2.654 30.698 1.00 66.41 656 0 GLN 97 129.682 1.442 30.754 1.00 66.29 657 N ASN 98 128.790 3.317 31.642 1.00 75.07 658 CA ASN 98 128.274 2.676 32.854 1.00 85.32 659 CB ASN 98 127.000 1.878 32.554 1.00 92.56 660 CG ASN 98 125.798 2.771 32.325 1.00 97.44 661 OD1 ASN 98 125.273 3.375 33.262 1.00 97.63 662 ND2 ASN 98 125.357 2.865 31.074 1.00 98.68 663 C ASN 98 129.314 1.791 33.535 1.00 89.40 664 0 ASN 98 129.073 0.612 33.812 1.00 88.19 665 N SER 99 130.486 2.369 33.779 1.00 94.53 666 CA SER 99 131.560 1.640 34.435 1.00 98.60 667 CB SER 99 132.918 2.248 34.106 1.00 99.63 668 OG SER 99 132.996 3.591 34.559 1.00100.00 669 C SER 99 131.332 1.673 35.926 1.00 99.96 670 0 SER 99 131.030 2.717 36.500 1.00 98.72 671 N ASN 100 131.508 0.532 36.566 1.00100.00 672 CA ASN 100 131.294 0.473 37.995 1.00100.00 673 CB ASN 100 130.733 -0.892 38.382 1.00 97.11 674 CG ASN 100 129.297 -1.056 37.956 1.00 95.75 675 OD1 ASN 100 128.429 -0.279 38.360 1.00 86.86 676 ND2 ASN 100 129.028 -2.069 37.139 1.00 94.51 677 C ASN 100 132.513 0.784 38.857 1.00100.00 678 0 ASN 100 133J96 -0.133 39.303 1.00100.00 679 N CYS 101 132.829 2.068 39.047 1.00 98.98 680 CA CYS 101 133.942 2.429 39.953 1.00 94.29 681 CB CYS 101 134.350 3.905 39.872 1.00 96.36 682 SG CYS 101 135.708 4.382 41.017 1.00100.00 683 C CYS 101 133.151 2.160 41.226 1.00 90.03 684 0 CYS 101 132.261 2.914 41.595 1.00 89.78 685 N ASN 102 133.483 1.057 41.870 1.00 85.97 686 CA ASN 102 132.753 0.573 43.043 1.00 81.73 687 CB ASN 102 133.072 -0.902 43.238 1.00 86.41 688 CG ASN 102 132.971 -1.688 41.962 1.00 88.71 689 OD1 ASN 102 133.978 -2J07 41.412 1.00 90.82 690 ND2 ASN 102 131.750 -1.869 41.462 1.00 81.79 691 C ASN 102 132.652 1.257 44.413 1.00 74.07 692 0 ASN 102 131.770 0.881 45.187 1.00 77.40 693 N ASP 103 133.474 2.260 44.713 1.00 58.82 694 CA ASP 103 133.377 2.904 46.037 1.00 48.91 695 CB ASP 103 134.746 3.418 46.524 1.00 50.06 696 CG ASP 103 135.346 4.487 45.622 1.00 54.31 697 OD1 ASP 103 135.589 4.210 44.429 1.00 68.60 698 OD2 ASP 103 135.616 5.599 46.128 1.00 47.23 699 C ASP 103 132.290 3.974 46.178 1.00 38.98 700 0 ASP 103 131.875 4.585 45.198 1.00 30.42 701 N LEU 104 131.820 4.168 47.408 1.00 25.79 702 CA LEU 104 130.764 5.139 47.702 1.00 26.09 703 CB LEU 104 130.414 5.114 49.195 1.00 14.86 704 CG LEU 104 129.294 6.042 49.674 1.00 13.82 705 CD1 LEU 104 127.971 5.654 49.031 1.00 10.36 706 CD2 LEU 104 129.171 5.996 51.191 1.00 7.52 707 C LEU 104 131.082 6.567 47.274 1.00 26.59 708 0 LEU 104 130.232 7.240 46.696 1.00 27.23 709 N CYS 105 132.297 7.021 47.574 1.00 28.20 710 CA CYS 105 132.735 8.370 47.225 1.00 24.21 711 CB CYS 105 134.164 8.606 47.721 1.00 29.54 712 SG CYS 105 134.889 10.178 47.188 1.00 32.14 713 C CYS 105 132.659 8.634 45.724 1.00 20.98 714 0 CYS 105 132.062 9.618 45.285 1.00 24.94 715 N THR 106 133.258 7.744 44.941 1.00 22.03 716 CA THR 106 133.261 7.890 43.489 1.00 23.52 717 CB THR 106 134.197 6.858 42.823 1.00 18.21 718 OG1 THR 106 135.481 6.893 43.461 1.00 20.18 719 CG2 THR 106 134.372 7.183 41.349 1.00 18.22 720 C THR 106 131.858 7.739 42.906 1.00 22.72 721 0 THR 106 131.481 8.465 41.984 1.00 21.14 722 N SER 107 131.092 6.802 43.461 1.00 26.53 723 CA SER 107 129.730 6.532 43.009 1.00 24.15 724 CB SER 107 129.158 5.312 43.735 1.00 24.72 725 OG SER 107 129.913 4.147 43.453 1.00 34.14 726 C SER 107 128.818 7.731 43.228 1.00 20.49 727 0 SER 107 128.128 8J70 42.306 1.00 15.26 728 N ALA 108 128.822 8.254 44.453 1.00 18.95 729 CA ALA 108 128.002 9.408 44.810 1.00 16.79 730 CB ALA 108 128.168 9.732 46.282 1.00 13.84 731 C ALA 108 128.349 10.623 43.953 1.00 15.33 732 0 ALA 108 127.455 11.340 43.499 1.00 19.47 733 N LEU 109 129.644 10.836 43.722 1.00 10.72 734 CA LEU 109 130.106 11.954 42.907 1.00 11.35 735 CB LEU 109 131.627 12.093 42.993 1.00 15.00 736 CG LEU 109 132.277 13.237 42.203 1.00 19.48 737 CD1 LEU 109 131.670 14.577 42.596 1.00 15.00 738 CD2 LEU 109 133.778 13.239 42.442 1.00 17.22 739 C LEU 109 129.673 11.754 41.459 1.00 15.76 740 0 LEU 109 129.216 12.692 40.807 1.00 28.55 741 N GLN 110 129.813 10.526 40.966 1.00 19.50 742 CA GLN 110 129.417 10.184 39.600 1.00 20.50 743 CB GLN 110 129.679 8.699 39.339 1.00 24.06 744 CG GLN 110 129.287 8.221 37.949 1.00 31.51 745 CD GLN 110 129.373 6.711 37.797 1.00 31.57 746 OE1 GLN 110 129.661 5.990 38.756 1.00 35.16 747 NE2 GLN 110 129.117 6.225 36.586 1.00 34.19 748 C GLN 110 127.926 10.478 39.414 1.00 21.12 749 0 GLN 110 127.508 11.009 38.389 1.00 20.13 750 N PHE 111 127.139 10.140 40.431 1.00 23.63 751 CA PHE 111 125.699 10.356 40.409 1.00 21.06 752 CB PHE 111 125.065 9.729 41.655 1.00 21.44 753 CG PHE 111 123.565 9.806 41.685 1.00 18.29 754 CD1 PHE 111 122.795 8.933 40.924 1.00 18.70 755 CD2 PHE 111 122.921 10.744 42.483 1.00 14.43 756 CE1 PHE 111 121.404 8.990 40.959 1.00 18.31 757 CE2 PHE 111 121.533 10.810 42.523 1.00 21.91 758 CZ PHE 111 120.773 9.929 41.758 1.00 17.47 759 C PHE 111 125.373 11.846 40.345 1.00 19.49 760 0 PHE 111 124.731 12.305 39.399 1.00 17.88 761 N ARG 112 125.857 12.598 41.332 1.00 16.34 762 CA ARG 112 125.606 14.033 41.407 1.00 8.21 763 CB ARG 112 126.326 14.651 42.608 1.00 7.94 764 CG ARG 112 126.081 16.153 42.745 1.00 14.61 765 CD ARG 112 126.507 16.703 44.100 1.00 22.36 766 NE ARG 112 127.955 16.745 44.291 1.00 19.69 767 CZ ARG 112 128.777 17.561 43.639 1.00 22.41 768 NH1 ARG 112 128.300 18.407 42.737 1.00 29.76 769 NH2 ARG 112 130.073 17.555 43.915 1.00 26.92 770 C ARG 112 125.961 14.808 40.145 1.00 13.57 771 0 ARG 112 125.113 15.505 39.588 1.00 17.92 772 N LEU 113 127.205 14.676 39.693 1.00 11.94 773 CA LEU 113 127.671 15.385 38.504 1.00 14.83 774 CB LEU 113 129.151 15.088 38.239 1.00 20.65 775 CG LEU 113 130.149 15.516 39.322 1.00 16.72 776 CD1 LEU 113 131.568 15.259 38.847 1.00 15.77 777 CD2 LEU 113 129.970 16.985 39.651 1.00 21.06 778 C LEU 113 126.840 15.108 37.256 1.00 19.17 779 0 LEU 113 126.484 16.034 36.532 1.00 26.79 780 N LEU 114 126.516 13.841 37.014 1.00 23.83 781 CA LEU 114 125.717 13.464 35.849 1.00 14.66 782 CB LEU 114 125.668 11.943 35.703 1.00 18.52 783 CG LEU 114 126.969 11.251 35.287 1.00 19.65 784 CD1 LEU 114 126.800 9.746 35.362 1.00 22.06 785 CD2 LEU 114 127.352 11.666 33.882 1.00 21.06 786 C LEU 114 124.300 14.030 35.939 1.00 15.67 787 0 LEU 114 123.787 14.596 34.972 1.00 18.67 788 N ARG 115 123.678 13.883 37.104 1.00 9.26 789 CA ARG 115 122.328 14.387 37.328 1.00 7.86 790 CB ARG 115 121.849 14.021 38.736 1.00 10.49 791 CG ARG 115 121.450 12.562 38.901 1.00 12.35 792 CD ARG 115 120.323 12.202 37.949 1.00 17.12 793 NE ARG 115 119.807 10.857 38.179 1.00 21.26 794 CZ ARG 115 118.803 10.570 39.000 1.00 15.94 795 NH1 ARG 115 1 18.199 1 1.537 39.676 1.00 8.20 796 NH2 ARG 115 118.406 9.314 39.152 1.00 17.38 797 C ARG 115 122.250 15.899 37.126 1.00 13.44 798 0 ARG 115 121.379 16.390 36.402 1.00 8.27 799 N GLN 116 123.180 16.629 37.743 1.00 14.35 800 CA GLN 116 123.225 18.086 37.629 1.00 11.93 801 CB GLN 116 124.364 18.664 38.471 1.00 4.12 802 CG GLN 116 124.165 18.534 39.968 1.00 5.13 803 CD GLN 116 125.303 19.142 40.768 1.00 11.78 804 OE1 GLN 116 125.080 19.950 41.669 1.00 21.37 805 NE2 GLN 116 126.530 18.747 40.451 1.00 11.47 806 C GLN 116 123.392 18.530 36.183 1.00 15.48 807 0 GLN 116 123.126 19.682 35.851 1.00 19.88 808 N HIS 117 123.827 17.607 35.328 1.00 19.55 809 CA HIS 117 124.031 17.893 33.912 1.00 15.02 810 CB HIS 117 125.405 17.392 33.460 1.00 13.78 811 CG HIS 117 126.538 18.253 33.925 1.00 17.44 812 CD2 HIS 117 126.999 18.525 35.169 1.00 18.38 813 ND1 HIS 117 127.322 18.983 33.059 1.00 19.26 814 CE1 HIS 117 128.216 19.668 33.748 1.00 20.36 815 NE2 HIS 117 128.042 19.408 35.031 1.00 17.37 816 C HIS 117 122.930 17.349 33.006 1.00 16.42 817 0 HIS 117 123.036 17.419 31.780 1.00 15.29 818 N GLY 118 121.872 16.813 33.613 1.00 17.98 819 CA GLY 118 120.756 16.292 32.839 1.00 21.36 820 C GLY 118 120.761 14.808 32.521 1.00 21.11 821 0 GLY 118 119.760 14.284 32.032 1.00 23.89 822 N PHE 119 121.880 14.134 32.773 1.00 20.97 823 CA PHE 119 121.994 12.702 32.510 1.00 15.97 824 CB PHE 119 123.465 12.282 32.477 1.00 13.26 825 CG PHE 119 124.281 13.007 31.439 1.00 19.34 826 CD1 PHE 119 125.155 14.025 31.808 1.00 18.10 827 CD2 PHE 119 124.160 12.686 30.090 1.00 17.78 828 CE1 PHE 119 125.896 14.714 30.850 1.00 14.61 829 CE2 PHE 119 124.896 13.370 29.122 1.00 16.11 830 CZ PHE 119 125.765 14.386 29.503 1.00 22.05 831 C PHE 119 121.238 11.917 33.576 1.00 20.90 832 0 PHE 119 121.620 11.910 34.749 1.00 17.99 833 N ASN 120 120.157 11.263 33.161 1.00 20.78 834 CA ASN 120 119.326 10.494 34.078 1.00 23.46 835 CB ASN 120 117.928 10.307 33.477 1.00 23.75 836 CG ASN 120 116.919 9.766 34.481 1.00 23.50 837 0D1 ASN 120 117.147 9.782 35.695 1.00 18.94 838 ND2 ASN 120 115.786 9.295 33.973 1.00 24.72 839 C ASN 120 119.940 9.145 34.447 1.00 29.37 840 0 ASN 120 119.467 8.092 34.011 1.00 37.56 841 N ILE 121 120.999 9.183 35.251 1.00 30.57 842 CA ILE 121 121.674 7.965 35.691 1.00 28.30 843 CB ILE 121 123.H8 8.250 36.202 1.00 31.51 844 CG2 ILE 121 123.1 16 9.395 37.212 1.00 18.33 845 CG1 ILE 121 123.734 6.970 36.784 1.00 34.25 846 CD1 ILE 121 125.160 7.119 37.270 1.00 35.18 847 C ILE 121 120.862 7.263 36.774 1.00 24.20 848 0 ILE 121 120.435 7.888 37.746 1.00 29.58 849 N SER 122 120.654 5.963 36.594 1.00 28.31 850 CA SER 122 1 19.886 5.158 37.538 1.00 31.22 851 CB SER 122 119.782 3.711 37.040 1.00 37.94 852 OG SER 122 119.046 2.907 37.948 1.00 37.31 853 C SER 122 120.471 5.193 38.942 1.00 26.25 854 0 SER 122 121.690 5.086 39.121 1.00 36.49 855 N PRO 123 119.606 5.367 39.956 1.00 25.72 856 CD PRO 123 118.162 5.626 39.787 1.00 24.10 857 CA PRO 123 119.995 5.427 41.367 1.00 24.12 858 CB PRO 123 118.807 6J39 42.015 1.00 14.52 859 CG PRO 123 117.635 5.620 41.222 1.00 18.26 860 C PRO 123 120.266 4.057 41.978 1.00 26.29 861 0 PRO 123 120.649 3.957 43.143 1.00 26.93 862 N GLU 124 120.106 3.007 41.176 1.00 31.58 863 CA GLU 124 120.362 1.656 41.665 1.00 42.38 864 CB GLU 124 119.734 0.614 40.749 1.00 52.63 865 CG GLU 124 118.661 -0.182 41.472 1.00 66.87 866 CD GLU 124 117.857 -1.078 40.558 1.00 84.70 867 OE1 GLU 124 118.072 -1.045 39.323 1.00 92.92 868 OE2 GLU 124 116.995 -1.820 41.075 1.00 95.72 869 C GLU 124 121.850 1.396 41.860 1.00 40.43 870 0 GLU 124 122.243 0.345 42.359 1.00 40.69 871 N ILE 125 122.665 2.383 41.493 1.00 40.56 872 CA ILE 125 124.113 2.311 41.658 1.00 33.74 873 CB ILE 125 124.796 3.532 40.995 1.00 34.47 874 CG2 ILE 125 124.231 4.828 41.567 1.00 35.94 875 CG1 ILE 125 126.317 3.471 41.176 1.00 33.47 876 CD1 ILE 125 127.051 4.648 40.560 1.00 33.54 877 C ILE 125 124.397 2.311 43.166 1.00 27.96 878 0 ILE 125 125.450 1.867 43.612 1.00 32.46 879 N PHE 126 123.422 2.783 43.938 1.00 24.55 880 CA PHE 126 123.518 2.850 45.393 1.00 31.56 881 CB PHE 126 122.701 4.034 45.925 1.00 31.55 882 CG PHE 126 123.245 5.377 45.536 1.00 36.38 883 CD1 PHE 126 122.701 6.079 44.465 1.00 32.78 884 CD2 PHE 126 124.300 5.946 46.245 1.00 35.39 885 CE1 PHE 126 123.197 7.328 44.105 1.00 32.25 886 CE2 PHE 126 124.805 7.194 45.894 1.00 31.56 887 CZ PHE 126 124.252 7.889 44.820 1.00 28.07 888 C PHE 126 123.042 1.568 46.079 1.00 37.75 889 0 PHE 126 122.939 1.520 47.308 1.00 36.32 890 N SER 127 122.730 0.542 45.289 1.00 42.49 891 CA SER 127 122.268 -0.732 45.836 1.00 43.38 892 CB SER 127 121.659 -1.601 44.733 1.00 48.30 893 OG SER 127 120.465 -1.025 44.233 1.00 59.77 894 C SER 127 123.401 -1.482 46.527 1.00 39.67 895 0 SER 127 123.228 -2.001 47.632 1.00 35.01 896 N LYS 128 124.567 -1.503 45.886 1.00 35.16 897 CA LYS 128 125.743 -2.179 46.426 1.00 36.47 898 CB LYS 128 126.877 -2.180 45.389 1.00 33.52 899 CG LYS 128 127.146 -0.834 44.732 1.00 37.85 900 CD LYS 128 128.170 -0.947 43.606 1.00 37.35 901 CE LYS 128 128.353 0.388 42.892 1.00 50.12 902 NZ LYS 128 129.338 0.328 41.776 1.00 54.36 903 C LYS 128 126.233 -1.623 47.769 1.00 38.71 904 O LYS 128 127.102 -2.217 48.412 1.00 46.49 905 N PHE 129 125.656 -0.501 48.199 1.00 38.63 906 CA PHE 129 126.028 0.135 49.466 1.00 31.98 907 CB PHE 129 126.309 1.626 49.256 1.00 24.98 908 CG PHE 129 127.324 1.904 48.191 1.00 20.86 909 CD1 PHE 129 126.946 2.506 46.997 1.00 19.33 910 CD2 PHE 129 128.653 1.537 48.368 1.00 17.79 911 CE1 PHE 129 127.877 2.735 45.988 1.00 22.73 912 CE2 PHE 129 129.590 1.760 47.368 1.00 19.77 913 CZ PHE 129 129.201 2.361 46.174 1.00 17.69 914 C PHE 129 124.929 -0.024 50.509 1.00 31.84 915 O PHE 129 125.051 0.462 51.635 1.00 32.60 916 N GLN 130 123.854 -0.700 50.123 1.00 40.45 917 CA GLN 130 122.720 -0.922 51.010 1.00 47.58 918 CB GLN 130 121.456 -0.310 50.403 1.00 51.16 919 CG GLN 130 121.515 1.197 50.231 1.00 50.70 920 CD GLN 130 120.308 1.755 49.505 1.00 54.25 921 OE1 GLN 130 119.310 1.063 49.303 1.00 62.26 922 NE2 GLN 130 120.394 3.017 49.105 1.00 58.79 923 C GLN 130 122.496 -2.405 51.263 1.00 51.99 924 O GLN 130 122.818 -3.245 50.419 1.00 55.44 925 N ASP 131 121.945 -2.723 52.431 1.00 53.38 926 CA ASP 131 121.665 -4.108 52.789 1.00 60.28 927 CB ASP 131 121.556 -4.258 54.314 1.00 58.61 928 CG ASP 131 120.311 -3.596 54.892 1.00 62.05 929 OD1 ASP 131 119.749 -4.145 55.860 1.00 69.31 930 OD2 ASP 131 119.893 -2.532 54.391 1.00 65.85 931 C ASP 131 120.382 -4.583 52.103 1.00 64.98 932 0 ASP 131 119.762 -3.837 51.341 1.00 64.40 933 N GLU 132 119.989 -5.823 52.383 1.00 70.50 934 CA GLU 132 118.786 -6.415 51.803 1.00 72.09 935 CB GLU 132 118.735 -7.913 52.120 1.00 78.41 936 CG GLU 132 119.098 -8.253 53.562 1.00 92.85 937 CD GLU 132 117.997 -8.995 54.303 1.00 100.00 938 OE1 GLU 132 116.803 -8.735 54.037 1.00 100.00 939 OE2 GLU 132 118.331 -9.837 55.165 1.00 100.00 940 C GLU 132 17.486 -5.729 52.236 1.00 69.60 941 O GLU 132 116.424 -5.985 51.666 1.00 67.84 942 N ASN 133 117.575 -4.849 53.230 1.00 69.95 943 CA ASN 133 116.408 -4.124 53.726 1.00 71.81 944 CB ASN 133 1 16.540 -3.882 55.235 1.00 76.32 945 CG ASN 133 115.238 -3.425 55.873 1.00 85.38 946 OD1 ASN 133 1 14.202 -4.076 55.731 1.00 89.18 947 ND2 ASN 133 1 15.288 -2.303 56.583 1.00 85.57 948 C ASN 133 116.214 -2.794 52.982 1.00 70.23 949 0 ASN 133 1 15.184 -2.132 53.136 1.00 67.90 950 N GLY 134 1 17.204 -2.414 52.176 1.00 67.24 951 CA GLY 134 117.120 -1.177 51.416 1.00 63.86 952 C GLY 134 117.758 0.036 52.072 1.00 61.93 953 0 GLY 134 117.712 1.138 51.520 1.00 64.71 954 N LYS 135 118.332 -0.158 53.257 1.00 57.80 955 CA LYS 135 118.989 0.921 53.993 1.00 52.54 956 CB LYS 135 118.628 0.865 55.482 1.00 54.50 957 CG LYS 135 117.298 1.519 55.845 1.00 58.81 958 CD LYS 135 116.106 0.776 55.259 1.00 65.64 959 CE LYS 135 114.795 1.428 55.666 1.00 66.94 960 NZ LYS 135 114.629 1.450 57.145 1.00 67.92 961 C LYS 135 120.505 0.859 53.827 1.00 46.30 962 0 LYS 135 121.062 -0.191 53.506 1.00 39.34 963 N PHE 136 121.168 1.988 54.058 1.00 40.70 964 CA PHE 136 122.619 2.066 53.929 1.00 37.70 965 CB PHE 136 123.082 3.525 53.941 1.00 30.32 966 CG PHE 136 122.848 4.238 52.644 1.00 18.97 967 CD1 PHE 136 121.752 5.079 52.485 1.00 16.88 968 CD2 PHE 136 123.708 4.044 51.569 1.00 2.95 969 CE1 PHE 136 121.512 5.714 51.269 1.00 9.36 970 CE2 PHE 136 123.478 4.674 50.350 1.00 8.37 971 CZ PHE 136 122.376 5.510 50.200 1.00 11.64 972 C PHE 136 123.368 1.280 54.992 1.00 40.03 973 0 PHE 136 123.007 1.310 56.173 1.00 36.07 974 N LYS 137 124.404 0.564 54.554 1.00 35.20 975 CA LYS 137 125.232 -0.232 55.451 1.00 37.62 976 CB LYS 137 126.333 -0.957 54.670 1.00 36.07 977 CG LYS 137 125.845 -2.039 53.721 1.00 43.95 978 CD LYS 137 127.016 -2.672 52.985 1.00 45.68 979 CE LYS 137 126.558 -3.745 52.011 1.00 46.97 980 NZ LYS 137 127.709 -4.340 51.276 1.00 45.41 981 C LYS 137 125.872 0.698 56.472 1.00 42.74 982 0 LYS 137 126.612 1.614 56.108 1.00 49.71 983 N GLU 138 125.569 0.472 57.747 1.00 44.30 984 CA GLU 138 126.116 1.290 58.824 1.00 43.35 985 CB GLU 138 125.482 0.895 60.157 1.00 48.22 986 CG GLU 138 123.997 1.184 60.285 1.00 55.55 987 CD GLU 138 123.703 2.650 60.528 1.00 59.82 988 0E1 GLU 138 124.127 3.180 61.577 1.00 58.06 989 0E2 GLU 138 123.040 3.272 59.674 1.00 70.04 990 C GLU 138 127.641 1.172 58.913 1.00 46.10 991 0 GLU 138 128.283 1.909 59.662 1.00 51.05 992 N SER 139 128.210 0.242 58.149 1.00 40.33 993 CA SER 139 129.653 0.027 58.122 1.00 37.26 994 CB SER 139 129.975 -1.354 57.541 1.00 42.99 995 OG SER 139 129.518 -1.477 56.204 1.00 42.44 996 C SER 139 130.384 1.114 57.326 1.00 38.83 997 O SER 139 131.606 1.247 57.423 1.00 44.35 998 N LEU 140 129.633 1.875 56.531 1.00 35.64 999 CA LEU 140 130.191 2.960 55.721 1.00 26.87 1000 CB LEU 140 129.289 3.244 54.514 1.00 27.15 1001 CG LEU 140 129.037 2.148 53.476 1.00 27.17 1002 CD1 LEU 140 127.955 2.607 52.511 1.00 23.24 1003 CD2 LEU 140 130.317 1.814 52.726 1.00 21.35 1004 C LEU 140 130.325 4.241 56.547 1.00 23.48 1005 O LEU 140 130.817 5.254 56.054 1.00 18.12 1006 N ALA 141 129.883 4J78 57.803 1.00 21.14 1007 CA ALA 141 129.916 5.311 58.725 1.00 23.07 1008 CB ALA 141 129.182 4.951 60.007 1.00 13.93 1009 C ALA 141 131.316 5.829 59.053 1.00 29.68 1010 0 ALA 141 131.465 6.917 59.614 1.00 34.02 1011 N SER 142 132.334 5.045 58.710 1.00 31.98 1012 CA SER 142 133.723 5.413 58.963 1.00 25.78 1013 CB SER 142 134.482 4.211 59.534 1.00 27.76 1014 OG SER 142 134.293 3.059 58.731 1.00 23.34 1015 C SER 142 134.436 5.957 57.719 1.00 26.37 1016 O SER 142 135.629 6.255 57.761 1.00 36.05 1017 N ASP 143 133.699 6.078 56.617 1.00 19.43 1018 CA ASP 143 134.237 6.596 55.361 1.00 13.45 1019 CB ASP 143 133.794 5.701 54.194 1.00 12.41 1020 CG ASP 143 134.284 6.196 52.835 1.00 22.67 1021 OD1 ASP 143 133.710 5.759 51.811 1.00 21.93 1022 OD2 ASP 143 135.239 7.004 52.778 1.00 35.17 1023 C ASP 143 133.727 8.025 55.162 1.00 19.69 1024 O ASP 143 132.675 8.238 54.559 1.00 21.70 1025 N VAL 144 134.485 8.997 55.664 1.00 21.88 1026 CA VAL 144 134.120 10.411 55.566 1.00 19.30 1027 CB VAL 144 135.093 11.295 56.376 1.00 16.67 1028 CG1 VAL 144 134.789 12.769 56.155 1.00 22.12 1029 CG2 VAL 144 134.978 10.961 57.857 1.00 20.43 1030 C VAL 144 133.997 10.942 54.136 1.00 18.93 1031 O VAL 144 133.012 11.603 53.801 1.00 23.53 1032 N LEU 145 134.984 10.657 53.293 1.00 15.19 1033 CA LEU 145 134.940 11.122 51.912 1.00 18.54 1034 CB LEU 145 136.238 10.780 51.181 1.00 22.93 1035 CG LEU 145 137.524 11.410 51.722 1.00 23.25 1036 CD1 LEU 145 138.647 11.189 50.715 1.00 24.40 1037 CD2 LEU 145 137.327 12.898 51.968 1.00 18.75 1038 C LEU 145 133.744 10.535 51.168 1.00 23.90 1039 O LEU 145 133.236 11.135 50.219 1.00 26.81 1040 N GLY 146 133.303 9.358 51.610 1.00 24.92 1041 CA GLY 146 132.159 8.705 50.999 1.00 21.44 1042 C GLY 146 130.868 9.313 51.512 1.00 19.58 1043 O GLY 146 129.953 9.591 50.740 1.00 22.50 1044 N LEU 147 130.805 9.524 52.823 1.00 9.20 1045 CA LEU 147 129.643 10.116 53.467 1.00 7.33 1046 CB LEU 147 129.849 10.163 54.980 1.00 7.87 1047 CG LEU 147 129.927 8.831 55.721 1.00 12.02 1048 CD1 LEU 147 130.341 9.066 57.157 1.00 8.20 1049 CD2 LEU 147 128.583 8.122 55.656 1.00 15.08 1050 C LEU 147 129.388 11.527 52.945 1.00 20.24 1051 0 LEU 147 128.244 11.900 52.680 1.00 27.36 1052 N LEU 148 130.462 12.303 52.795 1.00 20.47 1053 CA LEU 148 130.371 13.676 52.304 1.00 20.11 1054 CB LEU 148 131.751 14.347 52.330 1.00 16.79 1055 CG LEU 148 131.829 15.805 51.857 1.00 13.41 1056 CD1 LEU 148 130.897 16.683 52.683 1.00 6.32 1057 CD2 LEU 148 133.256 16.306 51.961 1.00 9.98 1058 C LEU 148 129.777 13.758 50.895 1.00 16.22 1059 0 LEU 148 128.838 14.520 50.657 1.00 19.05 1060 N ASN 149 130.332 12.985 49.965 1.00 14.19 1061 CA ASN 149 129.840 12.986 48.592 1.00 19.68 1062 CB ASN 149 130.776 12.199 47.678 1.00 17.57 1063 CG ASN 149 132.009 12.987 47.306 1.00 21.68 1064 0D1 ASN 149 132.904 13.181 48.129 1.00 27.23 1065 ND2 ASN 149 132.055 13.469 46.067 1.00 17.93 1066 C ASN 149 128.414 12.461 48.486 1.00 24.02 1067 0 ASN 149 127.676 12.829 47.571 1.00 25.30 1068 N LEU 150 128.033 11.596 49.424 1.00 23.15 1069 CA LEU 150 126.685 11.049 49.449 1.00 19.85 1070 CB LEU 150 126.606 9.844 50.391 1.00 15.00 1071 CG LEU 150 125.224 9.198 50.548 1.00 14.74 1072 CD1 LEU 150 124.735 8.634 49.215 1.00 8.02 1073 CD2 LEU 150 125.287 8.115 51.600 1.00 2.00 1074 C LEU 150 125.745 12.153 49.925 1.00 20.18 1075 0 LEU 150 124.640 12.304 49.404 1.00 22.47 1076 N TYR 151 126.209 12.930 50.904 1.00 18.20 1077 CA TYR 151 125.440 14.041 51.455 1.00 18.43 1078 CB TYR 151 126.226 14.739 52.569 1.00 10.57 1079 CG TYR 151 125.598 16.032 53.044 1.00 11.49 1080 CD1 TYR 151 124.759 16.056 54.156 1.00 5.47 1081 CE1 TYR 151 124.171 17.242 54.586 1.00 8.73 1082 CD2 TYR 151 125.835 17.234 52.372 1.00 10.72 1083 CE2 TYR 151 125.250 18.421 52.791 1.00 9.08 1084 CZ TYR 151 124.421 18.420 53.898 1.00 11.39 1085 OH TYR 151 123.845 19.598 54.316 1.00 11.19 1086 C TYR 151 125.117 15.041 50.355 1.00 17.39 1087 0 TYR 151 123.990 15.521 50.256 1.00 26.93 1088 N GLU 152 126.121 15.374 49.552 1.00 15.23 1089 CA GLU 152 125.937 16.316 48.455 1.00 18.45 1090 CB GLU 152 127.282 16.649 47.798 1.00 14.61 1091 CG GLU 152 128.316 17.293 48.727 1.00 17.73 1092 CD GLU 152 127.962 18.712 49.169 1.00 16.74 1093 0E1 GLU 152 126.980 19.292 48.662 1.00 16.63 1094 0E2 GLU 152 128.681 19.252 50.034 1.00 22.78 1095 C GLU 152 124.977 15.750 47.413 1.00 13.63 1096 0 GLU 152 124.114 16.463 46.904 1.00 20.19 1097 N ALA 153 125.115 14.458 47.125 1.00 18.04 1098 CA ALA 153 124.271 13.778 46.143 1.00 14.37 1099 CB ALA 153 124.859 12.417 45.794 1.00 13.44 1100 C ALA 153 122.815 13.624 46.580 1.00 13.36 1101 0 ALA 153 121.921 13.577 45.738 1.00 11.20 1102 N SER 154 122.574 13.568 47.889 1.00 16.02 1103 CA SER 154 121.218 13.413 48.416 1.00 13.22 1104 CB SER 154 121.250 13.157 49.928 1.00 8.73 1105 OG SER 154 121.581 14.330 50.651 1.00 16.49 1106 C SER 154 120.312 14.607 48.118 1.00 14.26 1107 0 SER 154 119.087 14.504 48.207 1.00 26.54 1108 N HIS 155 120.915 15.735 47.757 1.00 14.00 1109 CA HIS 155 120.154 16.942 47.457 1.00 8.22 1110 CB HIS 155 120.920 18.177 47.928 1.00 2.00 1111 CG HIS 155 120.932 18.340 49.415 1.00 2.00 1112 CD2 HIS 155 120.036 18.914 50.255 1.00 3.97 1113 ND1 HIS 155 121.946 17.856 50.211 1.00 3.74 1114 CE1 HIS 155 121.676 18.123 51.476 1.00 12.80 1115 NE2 HIS 155 120.522 18.764 51.529 1.00 11.17 1116 C HIS 155 119.742 17.092 45.997 1.00 10.18 1117 0 HIS 155 119.025 18.030 45.645 1.00 16.07 1118 N VAL 156 120.182 16.163 45.152 1.00 6.86 1119 CA VAL 156 119.843 16.202 43.733 1.00 7.09 1120 CB VAL 156 121.109 16.099 42.823 1.00 5.97 1121 CG1 VAL 156 122.161 17.113 43.248 1.00 2.00 1122 CG2 VAL 156 121.678 14.682 42.841 1.00 4.04 1123 C VAL 156 118.866 15.087 43.354 1.00 11.84 1124 0 VAL 156 118.644 14.827 42.170 1.00 13.76 1125 N ARG 157 118.264 14.443 44.351 1.00 12.59 1126 CA ARG 157 117.329 13.357 44.074 1.00 21.43 1127 CB ARG 157 117.224 12.398 45.271 1.00 17.56 1128 CG ARG 157 116.482 12.908 46.491 1.00 22.45 1129 CD ARG 157 116.525 11.846 47.583 1.00 26.00 1130 NE ARG 157 115.512 12.037 48.620 1.00 35.19 1131 CZ ARG 157 114.360 11.370 48.676 1.00 40.41 1132 NH1 ARG 157 114.064 10.465 47.753 1.00 42.25 1133 NH2 ARG 157 113.505 11.598 49.664 1.00 42.66 1134 C ARG 157 115.945 13.815 43.609 1.00 22.46 1135 0 ARG 157 115.473 14.885 43.985 1.00 28.62 1136 N THR 158 115.334 13.012 42.740 1.00 30.57 1137 CA THR 158 114.003 13.287 42.200 1.00 23.48 1138 CB THR 158 113.951 13.012 40.675 1.00 18.85 1139 0G1 THR 158 114.132 11.613 40.424 1.00 23.14 1140 CG2 THR 158 115.044 13.781 39.959 1.00 5.29 1141 C THR 158 112.962 12.409 42.911 1.00 26.07 1142 0 THR 158 113.258 11.786 43.936 1.00 29.73 1143 N HIS 159 111.745 12.362 42.373 1.00 25.85 1144 CA HIS 159 110.681 11.551 42.967 1.00 24.71 1145 CB HIS 159 109.312 11.987 42.435 1.00 24.02 1146 CG HIS 159 108.903 13.358 42.872 1.00 20.05 1147 CD2 HIS 159 108.888 14.538 42.209 1.00 14.66 1148 ND1 HIS 159 108.453 13.629 44.147 1.00 22.06 1149 CE1 HIS 159 108.179 14.917 44.250 1.00 20.70 1150 NE2 HIS 159 108.434 15.492 43.088 1.00 18.69 1151 C HIS 159 110.893 10.054 42.723 1.00 28.82 1152 0 HIS 159 110.377 9.211 43.464 1.00 29.90 1153 N ALA 160 111.674 9.733 41.695 1.00 22.36 1154 CA ALA 160 111.966 8.351 41.341 1.00 16.69 1155 CB ALA 160 112.118 8.233 39.835 1.00 12.78 1156 C ALA 160 113.218 7.821 42.038 1.00 24.25 1157 0 ALA 160 113.748 6.775 41.655 1.00 30.58 1158 N ASP 161 113.679 8.531 43.066 1.00 27.69 1159 CA ASP 161 114.880 8.134 43.800 1.00 24.25 1160 CB ASP 161 115.968 9.212 43.669 1.00 22.91 1161 CG ASP 161 116.356 9.495 42.222 1.00 29.35 1162 0D1 ASP 161 116.405 8.550 41.404 1.00 29.54 1163 0D2 ASP 161 116.623 10.672 41.906 1.00 19.16 1164 C ASP 161 114.626 7.840 45.281 1.00 26.01 1165 0 ASP 161 115.308 8.380 46.154 1.00 34.22 1166 N ASP 162 113.670 6.957 45.561 1.00 28.71 1167 CA ASP 162 113.339 6.590 46.939 1.00 28.70 1168 CB ASP 162 111.999 5.859 46.993 1.00 34.90 1169 CG ASP 162 110.851 6.726 46.536 1.00 42.80 1170 0D1 ASP 162 110.426 7.600 47.322 1.00 36.44 1171 0D2 ASP 162 110.386 6.543 45.389 1.00 43.54 1172 C ASP 162 114.423 5.728 47.573 1.00 27.14 1173 0 ASP 162 114.386 5.441 48.769 1.00 28.39 1174 N ILE 163 115.378 5.302 46.756 1.00 26.67 1175 CA ILE 163 116.485 4.486 47.229 1.00 27.39 1176 CB ILE 163 117.250 3.866 46.030 1.00 24.84 1177 CG2 ILE 163 118.201 4.881 45.412 1.00 29.37 1178 CG1 ILE 163 118.015 2.623 46.471 1.00 30.57 1179 CD1 ILE 163 118.639 1.863 45.323 1.00 43.90 1180 C ILE 163 117.407 5.372 48.078 1.00 28.12 1181 0 ILE 163 118.169 4.881 48.912 1.00 29.38 1182 N LEU 164 117.277 6.686 47.890 1.00 30.46 1183 CA LEU 164 118.070 7.684 48.607 1.00 24.33 1184 CB LEU 164 118.646 8.695 47.612 1.00 16.04 1185 CG LEU 164 119.602 8.181 46.538 1.00 20.33 1186 CD1 LEU 164 119.864 9.271 45.514 1.00 22.74 1187 CD2 LEU 164 120.894 7.720 47.184 1.00 17.92 1188 C LEU 164 117.259 8.441 49.658 1.00 23.88 1189 0 LEU 164 117.667 9.518 50.101 1.00 32.16 1190 N GLU 165 116.120 7.882 50.061 1.00 21.56 1191 CA GLU 165 115.256 8.529 51.043 1.00 18.89 1192 CB GLU 165 113.947 7.755 51.202 1.00 24.79 1193 CG GLU 165 114.127 6.324 51.689 1.00 48.18 1194 CD GLU 165 112.819 5.561 51.814 1.00 57.24 1195 0E1 GLU 165 111.765 6.076 51.375 1.00 63.77 1196 0E2 GLU 165 " 12.850 4.434 52.353 1.00 62.32 1197 C GLU 165 115.907 8.727 52.405 1.00 16.81 1198 0 GLU 165 1 15.598 9.687 53.106 1.00 18.04 1199 N ASP 166 116.817 7.828 52.771 1.00 23.03 1200 CA ASP 166 1 17.497 7.914 54.061 1.00 27.94 1201 CB ASP 166 117.383 6.579 54.811 1.00 35.23 1202 CG ASP 166 115.936 6.177 55.082 1.00 50.03 1203 OD1 ASP 166 115.565 5.024 54.771 1.00 57.17 1204 0D2 ASP 166 115.169 7.013 55.606 1.00 53.93 1205 C ASP 166 118.966 8.330 53.943 1.00 24.13 1206 0 ASP 166 119.674 8.409 54.950 1.00 23.24 1207 N ALA 167 119.401 8.638 52.721 1.00 14.78 1208 CA ALA 167 120.780 9.044 52.443 1.00 16.72 1209 CB ALA 167 120.993 9.169 50.948 1.00 12.70 1210 C ALA 167 121.215 10.333 53.136 1.00 24.13 1211 0 ALA 167 122.355 10.443 53.590 1.00 29.67 1212 N LEU 168 120.317 11.313 53.193 1.00 27.80 1213 CA LEU 168 120.614 12.590 53.831 1.00 19.27 1214 CB LEU 168 119.540 13.623 53.487 1.00 23.80 1215 CG LEU 168 119.706 15.016 54.099 1.00 18.12 1216 CD1 LEU 168 121.006 15.642 53.626 1.00 19.21 1217 CD2 LEU 168 118.524 15.890 53.719 1.00 17.36 1218 C LEU 168 120.730 12.450 55.343 1.00 20.39 1219 0 LEU 168 121.663 12.973 55.943 1.00 26.94 1220 N ALA 169 119.776 11.755 55.954 1.00 22.95 1221 CA ALA 169 119.784 11.555 57.400 1.00 28.99 1222 CB ALA 169 118.472 10.934 57.856 1.00 26.34 1223 C ALA 169 120.959 10.676 57.816 1.00 31.11 1224 0 ALA 169 121.529 10.855 58.895 1.00 32.24 1225 N PHE 170 121.319 9.736 56.944 1.00 26.27 1226 CA PHE 170 122.423 8.819 57.197 1.00 22.01 1227 CB PHE 170 122.448 7.714 56.135 1.00 20.64 1228 CG PHE 170 123.592 6.747 56.284 1.00 28.63 1229 CD1 PHE 170 123.622 5.837 57.338 1.00 28.29 1230 CD2 PHE 170 124.642 6.745 55.368 1.00 25.46 1231 CE1 PHE 170 124.683 4.938 57.479 1.00 27.46 1232 CE2 PHE 170 125.706 5.850 55.500 1.00 24.24 1233 CZ PHE 170 125.726 4.945 56.558 1.00 22.35 1234 C PHE 170 123.752 9.564 57.205 1.00 20.63 1235 0 PHE 170 124.440 9.610 58.224 1.00 23.76 1236 N SER 171 124.095 10.156 56.066 1.00 16.15 1237 CA SER 171 125.340 10.899 55.918 1.00 12.93 1238 CB SER 171 125.476 11.429 54.488 1.00 12.97 1239 OG SER 171 124.397 12.281 54.152 1.00 12.50 1240 C SER 171 125.479 12.047 56.912 1.00 13.92 1241 0 SER 171 126.567 12.297 57.420 1.00 15.50 1242 N THR 172 124.372 12.726 57.205 1.00 16.38 1243 CA THR 172 124.383 13.854 58.137 1.00 16.69 1244 CB THR 172 123.000 14.564 58.196 1.00 14.70 1245 0G1 THR 172 122.758 15.259 56.966 1.00 12.00 1246 CG2 THR 172 122.946 15.559 59.348 1.00 6.76 1247 C THR 172 124.813 13.486 59.556 1.00 19.18 1248 0 THR 172 125.759 14.067 60.086 1.00 22.93 1249 N ILE 173 124.129 12.516 60.160 1.00 22.35 1250 CA ILE 173 124.439 12.112 61.529 1.00 26.29 1251 CB ILE 173 123.428 11.061 62.070 1.00 29.19 1252 CG2 ILE 173 123.553 9.747 61.305 1.00 26.89 1253 CG1 ILE 173 123.657 10.844 63.572 1.00 34.59 1254 CD1 ILE 173 122.655 9.928 64.240 1.00 35.92 1255 C ILE 173 125.868 11.602 61.702 1.00 27.07 1256 0 ILE 173 126.481 11.801 62.754 1.00 30.04 1257 N HIS 174 126.404 10.972 60.662 1.00 18.99 1258 CA HIS 174 127.757 10.441 60.721 1.00 26.30 1259 CB HIS 174 127.895 9.228 59.799 1.00 36.54 1260 CG HIS 174 127.114 8.034 60.257 1.00 41.37 1261 CD2 HIS 174 126.355 7J47 59.571 1.00 35.65 1262 ND1 HIS 174 127.057 7.644 61.579 1.00 39.38 1263 CE1 HIS 174 126.295 6.569 61.687 1.00 33.20 1264 NE2 HIS 174 125.857 6.248 60.483 1.00 35.00 1265 C HIS 174 128.804 11.504 60.407 1.00 27.93 1266 0 HIS 174 129.945 11.419 60.872 1.00 25.80 1267 N LEU 175 128.410 12.508 59.626 1.00 25.88 1268 CA LEU 175 129.312 13.600 59.280 1.00 17.20 1269 CB LEU 175 128.804 14.376 58.066 1.00 12.92 1270 CG LEU 175 129.069 13.747 56.696 1.00 4.37 1271 CD1 LEU 175 128.472 14.624 55.606 1.00 2.00 1272 CD2 LEU 175 130.566 13.572 56.482 1.00 6.69 1273 C LEU 175 129.459 14.530 60.470 1.00 17.96 1274 0 LEU 175 130.534 15.074 60.705 1.00 30.10 1275 N GLU 176 128.375 14.699 61.225 1.00 17.67 1276 CA GLU 176 128.386 15.550 62.412 1.00 27.17 1277 CB GLU 176 126.969 15.740 62.959 1.00 26.19 1278 CG GLU 176 125.997 16.452 62.037 1.00 39.91 1279 CD GLU 176 124.606 16.584 62.645 1.00 51.08 1280 0E1 GLU 176 124.184 15.676 63.398 1.00 49.19 1281 0E2 GLU 176 123.932 17.600 62.368 1.00 52.29 1282 C GLU 176 129.241 14.913 63.505 1.00 29.58 1283 0 GLU 176 129.953 15.604 64.237 1.00 37.29 1284 N SER 177 129.156 13.589 63.604 1.00 31.69 1285 CA SER 177 129.883 12.816 64.607 1.00 28.71 1286 CB SER 177 129.310 11.395 64.678 1.00 24.94 1287 OG SER 177 129.868 10.660 65.755 1.00 27.40 1288 C SER 177 131.392 12.758 64.370 1.00 25.55 1289 0 SER 177 132.177 12.795 65.324 1.00 17.66 1290 N ALA 178 131.787 12.682 63.102 1.00 17.70 1291 CA ALA 178 133.195 12.600 62.723 1.00 19.27 1292 CB ALA 178 133.330 11.789 61.441 1.00 22.41 1293 C ALA 178 133.897 13.948 62.558 1.00 24.31 1294 0 ALA 178 135.107 14.054 62.769 1.00 24.74 1295 N ALA 179 133.124 14.975 62.214 1.00 25.32 1296 CA ALA 179 133.630 16.326 61.971 1.00 25.36 1297 CB ALA 179 132.460 17.289 61.779 1.00 32.63 1298 C ALA 179 134.658 16.943 62.928 1.00 23.67 1299 0 ALA 179 135.706 17.420 62.487 1.00 23.47 1300 N PRO 180 134.384 16.929 64.244 1.00 21.48 1301 CD PRO 180 133.196 16.355 64.900 1.00 20.79 1302 CA PRO 180 135.291 17.505 65.247 1.00 20.21 1303 CB PRO 180 134.601 17.155 66.568 1.00 10.68 1304 CG PRO 180 133.162 17.108 66.203 1.00 16.34 1305 C PRO 180 136.747 17.040 65.264 1.00 21.05 1306 0 PRO 180 137.623 17.772 65.722 1.00 30.38 1307 N HIS 181 137.015 15.846 64.750 1.00 24.41 1308 CA HIS 181 138.372 15.310 64.785 1.00 20.38 1309 CB HIS 181 138.359 13.955 65.498 1.00 22.19 1310 CG HIS 181 137.686 13.989 66.837 1.00 20.19 1311 CD2 HIS 181 138.077 14.524 68.018 1.00 22.10 1312 ND1 HIS 181 136.437 13.448 67.055 1.00 24.79 1313 CE1 HIS 181 136.086 13.649 68.313 1.00 28.39 1314 NE2 HIS 181 137.064 14.300 68.919 1.00 34.90 1315 C HIS 181 139.073 15.184 63.443 1.00 16.56 1316 0 HIS 181 140.138 14.575 63.351 1.00 20.78 1317 N LEU 182 138.496 15.775 62.407 1.00 19.38 1318 CA LEU 182 139.095 15.698 61.082 1.00 19.81 1319 CB LEU 182 138.023 15.838 59.999 1.00 12.64 1320 CG LEU 182 136.883 14.822 60.017 1.00 9.36 1321 CD1 LEU 182 135.883 15.191 58.946 1.00 6.26 1322 CD2 LEU 182 137.414 13.405 59.808 1.00 5.44 1323 C LEU 182 140.164 16.760 60.884 1.00 23.01 1324 0 LEU 182 140.177 17.787 61.567 1.00 24.75 1325 N LYS 183 141.071 16.492 59.953 1.00 23.75 1326 CA LYS 183 142.139 17.426 59.646 1.00 25.95 1327 CB LYS 183 143.300 16.712 58.948 1.00 25.08 1328 CG LYS 183 142.946 16.106 57.600 1.00 32.88 1329 CD LYS 183 144.157 15.465 56.949 1.00 39.75 1330 CE LYS 183 143.804 14.905 55.581 1.00 45.64 1331 NZ LYS 183 144.980 14.277 54.913 1.00 50.66 1332 C LYS 183 141.590 18.522 58.747 1.00 26.52 1333 0 LYS 183 140.579 18.333 58.068 1.00 31.05 1334 N SER 184 142.247 19.675 58.769 1.00 25.24 1335 CA SER 184 141.842 20.806 57.949 1.00 18.75 1336 CB SER 184 142.202 22.111 58.656 1.00 15.62 1337 OG SER 184 141.536 22.192 59.906 1.00 17.72 1338 C SER 184 142.553 20.707 56.605 1.00 13.85 1339 0 SER 184 143.666 20.186 56.528 1.00 23.56 1340 N PRO 185 141.930 21.221 55.526 1.00 14.69 1341 CD PRO 185 142.636 21.342 54.235 1.00 6.08 1342 CA PRO 185 140.622 21.886 55.462 1.00 13.32 1343 CB PRO 185 140.758 22.747 54.213 1.00 7.14 1344 CG PRO 185 141.553 21.860 53.309 1.00 4.25 1345 C PRO 185 139.378 20.990 55.368 1.00 19.26 1346 0 PRO 185 138.268 21.502 55.198 1.00 22.11 1347 N LEU 186 139.547 19.671 55.478 1.00 15.43 1348 CA LEU 186 138.410 18.757 55.385 1.00 7.82 1349 CB LEU 186 138.859 17.304 55.533 1.00 10.45 1350 CG LEU 186 137.743 16.259 55.379 1.00 14.68 1351 CD1 LEU 186 137.199 16.257 53.953 1.00 2.00 1352 CD2 LEU 186 138.269 14.885 55.744 1.00 10.39 1353 C LEU 186 137.339 19.061 56.424 1.00 14.43 1354 0 LEU 186 136.147 19.062 56.114 1.00 15.11 1355 N ARG 187 137.774 19.318 57.653 1.00 11.19 1356 CA ARG 187 136.868 19.626 58.755 1.00 10.77 1357 CB ARG 187 137.675 19.929 60.019 1.00 9.64 1358 CG ARG 187 136.839 20.202 61.251 1.00 12.29 1359 CD ARG 187 137.724 20.530 62.429 1.00 17.99 1360 NE ARG 187 136.944 20.796 63.633 1.00 40.99 1361 CZ ARG 187 137.468 20.982 64.841 1.00 53.63 1362 NH1 ARG 187 138.785 20.931 65.014 1.00 54.42 1363 NH2 ARG 187 136.674 21.217 65.879 1.00 49.07 1364 C ARG 187 135.949 20.804 58.424 1.00 19.68 1365 0 ARG 187 134.754 20.771 58.731 1.00 20.19 1366 N GLU 188 136.512 21.831 57.789 1.00 19.04 1367 CA GLU 188 135.758 23.026 57.405 1.00 14.75 1368 CB GLU 188 136.708 24.179 57.052 1.00 18.38 1369 CG GLU 188 137.416 24.825 58.248 1.00 25.44 1370 CD GLU 188 138.326 23.865 59.000 1.00 37.02 1371 0E1 GLU 188 138.143 23.708 60.228 1.00 36.96 1372 OE2 GLU 188 139.224 23.271 58.362 1.00 33.70 1373 C GLU 188 134.819 22.758 56.236 1.00 15.06 1374 0 GLU 188 133.720 23.317 56.176 1.00 16.38 1375 N GLN 189 135.263 21.920 55.301 1.00 12.50 1376 CA GLN 189 134.458 21.567 54.134 1.00 10.80 1377 CB GLN 189 135.269 20.711 53.153 1.00 10.38 1378 CG GLN 189 134.529 20.384 51.856 1.00 9.35 1379 CD GLN 189 135.415 19.722 50.811 1.00 16.04 1380 OE1 GLN 189 135.319 20.022 49.617 1.00 8.08 1381 NE2 GLN 189 136.277 18.812 51.254 1.00 11.78 1382 C GLN 189 133.204 20.814 54.574 1.00 12.51 1383 0 GLN 189 132.117 21.057 54.059 1.00 19.40 1384 N VAL 190 133.363 19.920 55.546 1.00 11.87 1385 CA VAL 190 132.250 19.139 56.070 1.00 14.05 1386 CB VAL 190 132.750 17.975 56.967 1.00 18.34 1387 CG1 VAL 190 131.574 17.265 57.637 1.00 19.94 1388 CG2 VAL 190 133.556 16.986 56.135 1.00 2.59 1389 C VAL 190 131.300 20.031 56.865 1.00 12.69 1390 0 VAL 190 130.091 20.012 56.642 1.00 16.38 1391 N THR 191 131.858 20.822 57.777 1.00 19.11 1392 CA THR 191 131.065 21.727 58.606 1.00 20.76 1393 CB THR 191 131.964 22.557 59.551 1.00 23.59 1394 0G1 THR 191 132.681 21.675 60.424 1.00 29.20 1395 CG2 THR 191 131.130 23.51 1 60.391 1.00 29.68 1396 C THR 191 130.241 22.664 57.731 1.00 19.82 1397 0 THR 191 129.073 22.927 58.023 1.00 24.05 1398 N HIS 192 130.843 23.136 56.641 1.00 11.94 1399 CA HIS 192 130.160 24.032 55.719 1.00 13.13 1400 CB HIS 192 131.148 24.658 54.741 1.00 14.49 1401 CG HIS 192 130.512 25.600 53.764 1.00 13.85 1402 CD2 HIS 192 130.320 25.503 52.428 1.00 14.30 1403 ND1 HIS 192 129.981 26.814 54.141 1.00 17.04 1404 CE1 HIS 192 129.488 27.425 53.078 1.00 22.40 1405 NE2 HIS 192 129.681 26.651 52.025 1.00 9.94 1406 C HIS 192 129.061 23.321 54.939 1.00 15.72 1407 0 HIS 192 128.002 23.896 54.696 1.00 19.37 1408 N ALA 193 129.331 22.085 54.524 1.00 22.40 1409 CA ALA 193 128.367 21.288 53.766 1.00 17.47 1410 CB ALA 193 128.993 19.976 53.333 1.00 13.16 1411 C ALA 193 127.104 21.027 54.584 1.00 18.46 1412 0 ALA 193 125.991 21.093 54.063 1.00 20.11 1413 N LEU 194 127.285 20.747 55.870 1.00 13.26 1414 CA LEU 194 126.165 20.488 56.763 1.00 18.67 1415 CB LEU 194 126.669 19.948 58.103 1.00 22.98 1416 CG LEU 194 127.424 18.615 58.050 1.00 17.83 1417 CD1 LEU 194 127.913 18.249 59.439 1.00 22.28 1418 CD2 LEU 194 126.526 17.524 57.494 1.00 9.41 1419 C LEU 194 125.325 21.745 56.977 1.00 20.18 1420 0 LEU 194 124.169 21.662 57.390 1.00 28.31 1421 N GLU 195 125.913 22.906 56.701 1.00 23.69 1422 CA GLU 195 125.217 24.182 56.845 1.00 23.91 1423 CB GLU 195 126.145 25.235 57.459 1.00 28.38 1424 CG GLU 195 126.558 24.930 58.897 1.00 48.57 1425 CD GLU 195 127.591 25.905 59.449 1.00 61.92 1426 0E1 GLU 195 128.341 26.515 58.652 1.00 66.87 1427 0E2 GLU 195 127.658 26.052 60.690 1.00 55.96 1428 C GLU 195 124.693 24.670 55.497 1.00 14.54 1429 0 GLU 195 123.721 25.422 55.436 1.00 17.77 1430 N GLN 196 125.327 24.207 54.422 1.00 10.51 1431 CA GLN 196 124.951 24.584 53.064 1.00 9.57 1432 CB GLN 196 125.488 25.984 52.740 1.00 9.74 1433 CG GLN 196 125.212 26.461 51.321 1.00 13.51 1434 CD GLN 196 123.737 26.672 51.051 1.00 18.27 1435 OE1 GLN 196 123.111 27.556 51.633 1.00 31.94 1436 NE2 GLN 196 123.174 25.862 50.162 1.00 21.35 1437 C GLN 196 125.484 23.583 52.039 1.00 8.87 1438 0 GLN 196 126.695 23.481 51.830 1.00 16.57 1439 N CYS 197 124.577 22.837 51.415 1.00 11.72 1440 CA CYS 197 124.963 21.865 50.398 1.00 13.36 1441 CB CYS 197 123.821 20.882 50.114 1.00 20.25 1442 SG CYS 197 122.310 21.605 49.432 1.00 16.36 1443 C CYS 197 125.351 22.614 49.126 1.00 11.32 1444 0 CYS 197 124.948 23.758 48.924 1.00 16.69 1445 N LEU 198 126.134 21.965 48.274 1.00 14.40 1446 CA LEU 198 126.594 22.580 47.038 1.00 14.31 1447 CB LEU 198 127.688 21.717 46.394 1.00 14.46 1448 CG LEU 198 128.283 22.186 45.060 1.00 13.58 1449 CD1 LEU 198 128.949 23.541 45.225 1.00 9.55 1450 CD2 LEU 198 129.279 21.162 44.547 1.00 12.33 1451 C LEU 198 125.478 22.848 46.034 1.00 18.46 1452 0 LEU 198 125.389 23.945 45.481 1.00 26.64 1453 N HIS 199 124.614 21.857 45.829 1.00 20.84 1454 CA HIS 199 123.519 21.965 44.869 1.00 13.67 1455 CB HIS 199 122.756 20.640 44.781 1.00 11.33 1456 CG HIS 199 121.733 20.603 43.688 1.00 6J7 1457 CD2 HIS 199 120.389 20.445 43.729 1.00 12.38 1458 ND1 HIS 199 122.061 20.738 42.356 1.00 10.08 1459 CE1 HIS 199 120.964 20.663 41.624 1.00 10.18 1460 NE2 HIS 199 119.935 20.486 42.432 1.00 2.01 1461 C HIS 199 122.540 23.111 45.108 1.00 14.52 1462 0 HIS 199 122.174 23.813 44.166 1.00 13.39 1463 N LYS 200 122.120 23.300 46.357 1.00 15.92 1464 CA LYS 200 121.161 24.353 46.698 1.00 14.65 1465 CB LYS 200 120.205 23.859 47.789 1.00 15.18 1466 CG LYS 200 119.425 22.609 47.416 1.00 12.45 1467 CD LYS 200 118.523 22.158 48.554 1.00 3.23 1468 CE LYS 200 117.827 20.849 48.213 1.00 14.66 1469 NZ LYS 200 116.966 20.369 49.332 1.00 22.03 1470 C LYS 200 121.786 25.688 47.120 1.00 22.11 1471 0 LYS 200 121.101 26.541 47.693 1.00 20.41 1472 N GLY 201 123.078 25.860 46.844 1.00 21.90 1473 CA GLY 201 123.764 27.097 47.191 1.00 14.85 1474 C GLY 201 124.048 27.969 45.978 1.00 16.72 1475 0 GLY 201 123.992 27.489 44.842 1.00 12.09 1476 N VAL 202 124.329 29.253 46.209 1.00 11.53 1477 CA VAL 202 124.627 30.183 45.114 1.00 11.31 1478 CB VAL 202 124.437 31.661 45.555 1.00 9.93 1479 CG1 VAL 202 124.960 32.617 44.491 1.00 2.00 1480 CG2 VAL 202 122.964 31.937 45.803 1.00 6.34 1481 C VAL 202 126.054 29.940 44.612 1.00 10.17 1482 0 VAL 202 126.997 29.883 45.405 1.00 8.95 1483 N PRO 203 126.222 29.774 43.286 1.00 2J0 1484 CD PRO 203 125.136 29.796 42.290 1.00 5.19 1485 CA PRO 203 127.509 29.524 42.628 1.00 8.34 1486 CB PRO 203 127.168 29.704 41.154 1.00 5.82 1487 CG PRO 203 125.785 29.152 41.087 1.00 2.00 1488 C PRO 203 128.699 30.381 43.069 1.00 18.54 1489 0 PRO 203 129.709 29.836 43.516 1.00 26.42 1490 N ARG 204 128.591 31.704 42.951 1.00 11.17 1491 CA ARG 204 129.687 32.582 43.357 1.00 5.94 1492 CB ARG 204 129.366 34.047 43.061 1.00 4.29 1493 CG ARG 204 129.405 34.440 41.587 1.00 10.69 1494 CD ARG 204 130.821 34.543 41.033 1.00 8.35 1495 NE ARG 204 131.410 33.242 40.725 1.00 21.05 1496 CZ ARG 204 132.555 33.071 40.068 1.00 20.78 1497 NH1 ARG 204 133.250 34.121 39.644 1.00 14.75 1498 NH2 ARG 204 132.996 31.844 39.818 1.00 16.69 1499 C ARG 204 130.016 32.420 44.836 1.00 6.43 1500 O ARG 204 131.185 32.304 45.207 1.00 15.01 1501 N VAL 205 128.983 32.380 45.672 1.00 2.00 1502 CA VAL 205 129.159 32.238 47.116 1.00 3.42 1503 CB VAL 205 127.809 32.238 47.855 1.00 2.00 1504 CG1 VAL 205 128.027 32.047 49.342 1.00 13.49 1505 CG2 VAL 205 127.064 33.530 47.594 1.00 2.00 1506 C VAL 205 129.904 30.963 47.488 1.00 7.19 1507 0 VAL 205 130.785 30.982 48.342 1.00 17.39 1508 N GLU 206 129.543 29.854 46.851 1.00 11.33 1509 CA GLU 206 130.188 28.579 47.136 1.00 11.44 1510 CB GLU 206 129.348 27.417 46.606 1.00 10.75 1511 CG GLU 206 128.033 27.237 47.340 1.00 4.42 1512 CD GLU 206 128.208 27.226 48.845 1.00 7.68 1513 0E1 GLU 206 128.858 26.298 49.366 1.00 15.79 1514 0E2 GLU 206 127.700 28.153 49.509 1.00 12.42 1515 C GLU 206 131.598 28.528 46.568 1.00 13.88 1516 0 GLU 206 132.484 27.897 47.144 1.00 16.22 1517 N THR 207 131.792 29.199 45.438 1.00 9.73 1518 CA THR 207 133.090 29.268 44.785 1.00 13.84 1519 CB THR 207 132.970 29.928 43.400 1.00 15.72 1520 0G1 THR 207 132.272 29.045 42.513 1.00 13.12 1521 CG2 THR 207 134.338 30.250 42.827 1.00 11.92 1522 C THR 207 134.059 30.066 45.658 1.00 19.41 1523 0 THR 207 135.177 29.623 45.917 1.00 27.17 1524 N ARG 208 133.608 31.226 46.133 1.00 22.15 1525 CA ARG 208 134.417 32.091 46.988 1.00 17.49 1526 CB ARG 208 133.595 33.309 47.429 1.00 23.71 1527 CG ARG 208 134.349 34.352 48.264 1.00 24.20 1528 CD ARG 208 135.532 34.935 47.501 1.00 35.41 1529 NE ARG 208 136.060 36.169 48.090 1.00 40.81 1530 CZ ARG 208 136.736 36.242 49.235 1.00 40.71 1531 NH1 ARG 208 136.978 35.150 49.947 1.00 42.82 1532 NH2 ARG 208 137.194 37.412 49.658 1.00 37.98 1533 C ARG 208 134.906 31.313 48.208 1.00 19.76 1534 0 ARG 208 136.075 31.395 48.576 1.00 27.03 1535 N PHE 209 134.010 30.534 48.809 1.00 16.90 1536 CA PHE 209 134.350 29.734 49.979 1.00 12.93 1537 CB PHE 209 133.090 29.165 50.632 1.00 3.91 1538 CG PHE 209 133.377 28.292 51.818 1.00 8.27 1539 CD1 PHE 209 133.605 28.852 53.070 1.00 5.35 1540 CD2 PHE 209 133.472 26.912 51.676 1.00 11.24 1541 CE1 PHE 209 133.928 28.052 54.162 1.00 10.99 1542 CE2 PHE 209 133.794 26.105 52.760 1.00 7.23 1543 CZ PHE 209 134.023 26.677 54.007 1.00 2.00 1544 C PHE 209 135.305 28.581 49.664 1.00 16.94 1545 0 PHE 209 136.176 28.248 50.473 1.00 13.43 1546 N PHE 210 135.112 27.942 48.514 1.00 11.91 1547 CA PHE 210 135.960 26.823 48.126 1.00 12.01 1548 CB PHE 210 135.384 26.105 46.901 1.00 5.35 1549 CG PHE 210 136.131 24.854 46.525 1.00 2.00 1550 CD1 PHE 210 136.182 23.773 47.392 1.00 7.13 1551 CD2 PHE 210 136.794 24.763 45.307 1.00 13.50 1552 CE1 PHE 210 136.883 22.617 47.052 1.00 13.12 1553 CE2 PHE 210 137.498 23.613 44.956 1.00 10.64 1554 CZ PHE 210 137.542 22.539 45.830 1.00 12.55 1555 C PHE 210 137.380 27.297 47.844 1.00 15.50 1556 0 PHE 210 138.339 26.801 48.436 1.00 21.01 1557 N ILE 211 137.500 28.290 46.970 1.00 11.89 1558 CA ILE 211 138.798 28.834 46.601 1.00 14.18 1559 CB ILE 211 138.663 30.000 45.604 1.00 13.95 1560 CG2 ILE 211 140.040 30.517 45.218 1.00 23.94 1561 CG1 ILE 211 137.925 29.547 44.346 1.00 14.06 1562 CD1 ILE 211 137.734 30.656 43.335 1.00 19.84 1563 C ILE 211 139.622 29.318 47.790 1.00 11.48 1564 0 ILE 211 140.730 28.838 48.010 1.00 22.99 1565 N SER 212 139.069 30.238 48.574 1.00 11.99 1566 CA SER 212 139.799 30.797 49.708 1.00 19.48 1567 CB SER 212 139.279 32.205 50.044 1.00 10.83 1568 OG SER 212 137.939 32.174 50.500 1.00 32.56 1569 C SER 212 139.902 29.954 50.979 1.00 15.60 1570 0 SER 212 140.992 29.800 51.530 1.00 26.35 1571 N SER 213 138.785 29.398 51.437 1.00 18.79 1572 CA SER 213 138.780 28.607 52.665 1.00 15.21 1573 CB SER 213 137.426 28.737 53.372 1.00 13.39 1574 OG SER 213 137.168 30.074 53.766 1.00 19.66 1575 C SER 213 139.H1 27.126 52.543 1.00 21.19 1576 0 SER 213 139.540 26.503 53.534 1.00 22.69 1577 N ILE 214 139.021 26.558 51.345 1.00 16.22 1578 CA ILE 214 139.308 25.138 51.177 1.00 12.65 1579 CB ILE 214 138.047 24.354 50.712 1.00 17.01 1580 CG2 ILE 214 138.343 22.853 50.628 1.00 14.54 1581 CG1 ILE 214 136.879 24.602 51.673 1.00 7.09 1582 CD1 ILE 214 137.175 24.247 53.124 1.00 2J6 1583 C ILE 214 140.477 24.759 50.276 1.00 14.51 1584 0 ILE 214 141.486 24.247 50.759 1.00 20.94 1585 N TYR 215 140.342 25.006 48.975 1.00 10.71 1586 CA TYR 215 141.378 24.634 48.016 1.00 16.76 1587 CB TYR 215 140.914 24.914 46.587 1.00 10.15 1588 CG TYR 215 141.523 23.975 45.569 1.00 16.49 1589 CD1 TYR 215 141.526 22.595 45.777 1.00 14.36 1590 CE1 TYR 215 142.079 21.722 44.837 1.00 16.84 1591 CD2 TYR 215 142.090 24.463 44.393 1.00 18.93 1592 CE2 TYR 215 142.645 23.601 43.447 1.00 14.61 1593 CZ TYR 215 142.636 22.232 43.676 1.00 18.72 1594 OH TYR 215 143.191 21.375 42.749 1.00 21.97 1595 C TYR 215 142.753 25.251 48.256 1.00 22.56 1596 0 TYR 215 143.772 24.567 48.154 1.00 21.88 1597 N ASP 216 142.780 26.538 48.582 1.00 25.86 1598 CA ASP 216 144.032 27.239 48.841 1.00 28.90 1599 CB ASP 216 143.745 28.708 49.155 1.00 35.55 1600 CG ASP 216 145.000 29.514 49.373 1.00 32.91 1601 OD1 ASP 216 145.170 30.035 50.494 1.00 33.80 1602 OD2 ASP 216 145.811 29.630 48.427 1.00 38.29 1603 C ASP 216 144.782 26.590 50.002 1.00 28.68 1604 0 ASP 216 146.013 26.552 50.017 1.00 35.11 1605 N LYS 217 144.026 26.052 50.954 1.00 24.04 1606 CA LYS 217 144.604 25.406 52.129 1.00 25.31 1607 CB LYS 217 143.768 25.741 53.368 1.00 17.45 1608 CG LYS 217 143.687 27.234 53.646 1.00 28.42 1609 CD LYS 217 142.811 27.551 54.844 1.00 36.77 1610 CE LYS 217 142.729 29.057 55.071 1.00 36.92 1611 NZ LYS 217 141.758 29.426 56.143 1.00 37.10 1612 C LYS 217 144.754 23.892 51.973 1.00 25.97 1613 0 LYS 217 145.170 23.201 52.905 1.00 23.71 1614 N GLU 218 144.429 23.385 50.788 1.00 30.40 1615 CA GLU 218 144.528 21.958 50.504 1.00 34.37 1616 CB GLU 218 143.655 21.603 49.297 1.00 41.93 1617 CG GLU 218 143.462 20.114 49.073 1.00 45.33 1618 CD GLU 218 142.740 19.451 50.226 1.00 52.39 1619 0E1 GLU 218 141.553 19.780 50.449 1.00 49.41 1620 0E2 GLU 218 143.364 18.612 50.916 1.00 46.07 1621 C GLU 218 145.982 21.585 50.228 1.00 34.68 1622 0 GLU 218 146.624 22.166 49.356 1.00 31.92 1623 N GLN 219 146.493 20.611 50.974 1.00 37.87 1624 CA GLN 219 147.872 20.156 50.827 1.00 41.61 1625 CB GLN 219 148.180 19.105 51.896 1.00 52.08 1626 CG GLN 219 149.617 18.615 51.900 1.00 67.09 1627 CD GLN 219 149.709 17.102 51.943 1.00 78.27 1628 0E1 GLN 219 149.305 16.470 52.917 1.00 81.71 1629 NE2 GLN 219 150.233 16.510 50.870 1.00 80.10 1630 C GLN 219 148.173 19.583 49.438 1.00 38.79 1631 0 GLN 219 149.260 19.789 48.893 1.00 34.89 1632 N SER 220 147.205 18.867 48.874 1.00 39.35 1633 CA SER 220 147.359 18.252 47.556 1.00 36.65 1634 CB SER 220 146.658 16.891 47.537 1.00 48.69 1635 OG SER 220 145.291 17.018 47.899 1.00 58.57 1636 C SER 220 146.824 19.117 46.418 1.00 30.45 1637 0 SER 220 146.651 18.639 45.297 1.00 31.98 1638 N LYS 221 146.581 20.392 46.704 1.00 25.39 1639 CA LYS 221 146.052 21.327 45.716 1.00 18.20 1640 CB LYS 221 145.949 22.731 46.316 1.00 17.94 1641 CG LYS 221 147.292 23.352 46.659 1.00 24.63 1642 CD LYS 221 147.136 24.772 47.155 1.00 32.69 1643 CE LYS 221 148.444 25.312 47.716 1.00 42.07 1644 NZ LYS 221 149.547 25.257 46.720 1.00 42.25 1645 C LYS 221 146.879 21.412 44.444 1.00 15.22 1646 0 LYS 221 148.097 21.243 44.467 1.00 21.32 1647 N ASN 222 146.196 21.660 43.333 1.00 11.20 1648 CA ASN 222 146.853 21.818 42.048 1.00 9.54 1649 CB ASN 222 145.993 21.250 40.919 1.00 2.46 1650 CG ASN 222 146.599 21.488 39.550 1.00 12.07 1651 0D1 ASN 222 146.698 22.626 39.097 1.00 10.03 1652 ND2 ASN 222 147.003 20.414 38.881 1.00 11.12 1653 C ASN 222 147.032 23.322 41.885 1.00 17.59 1654 0 ASN 222 146.060 24.061 41.717 1.00 21.24 1655 N ASN 223 148.281 23.765 41.958 1.00 18.52 1656 CA ASN 223 148.619 25.175 41.850 1.00 9.91 1657 CB ASN 223 150.127 25.349 41.972 1.00 11.52 1658 CG ASN 223 150.664 24.821 43.282 1.00 23.77 1659 OD1 ASN 223 150.579 25.491 44.311 1.00 21.40 1660 ND2 ASN 223 151.208 23.605 43.258 1.00 21.52 1661 C ASN 223 148.104 25.870 40.594 1.00 15.35 1662 0 ASN 223 147.668 27.019 40.662 1.00 21.88 1663 N VAL 224 148.157 25.184 39.455 1.00 10.58 1664 CA VAL 224 147.677 25.755 38.195 1.00 18.60 1665 CB VAL 224 147.957 24.811 37.001 1.00 24.63 1666 CG1 VAL 224 147.405 25.406 35.709 1.00 25.94 1667 CG2 VAL 224 149.449 24.558 36.873 1.00 17.27 1668 C VAL 224 146.177 26.049 38.259 1.00 23.24 1669 0 VAL 224 145.716 27.071 37.746 1.00 25.12 1670 N LEU 225 145.423 25.146 38.886 1.00 23.80 1671 CA LEU 225 143.980 25.313 39.032 1.00 18.51 1672 CB LEU 225 143.314 23.994 39.434 1.00 18.23 1673 CG LEU 225 143.337 22.844 38.424 1.00 20.30 1674 CD1 LEU 225 142.613 21.645 39.010 1.00 18.77 1675 CD2 LEU 225 142.691 23.270 37J 15 1.00 10.44 1676 C LEU 225 143.652 26.392 40.061 1.00 18.24 1677 0 LEU 225 142.710 27.162 39.872 1.00 22.06 1678 N LEU 226 144.431 26.448 41.141 1.00 18.51 1679 CA LEU 226 144.230 27.445 42.197 1.00 17.64 1680 CB LEU 226 145.128 27.149 43.401 1.00 15.88 1681 CG LEU 226 145.013 28.096 44.605 1.00 19.63 1682 CD1 LEU 226 143.633 27.996 45.235 1.00 8.24 1683 CD2 LEU 226 146.086 27.764 45.627 1.00 2.89 1684 C LEU 226 144.507 28.855 41.681 1.00 15.54 1685 0 LEU 226 143.753 29.785 41.966 1.00 28.19 1686 N ARG 227 145.595 29.002 40.927 1.00 22.25 1687 CA ARG 227 145.995 30.282 40.338 1.00 21.24 1688 CB ARG 227 147.320 30.108 39.587 1.00 25.23 1689 CG ARG 227 147.831 31.335 38.844 1.00 26.56 1690 CD ARG 227 148.575 32.292 39.760 1.00 33.23 1691 NE ARG 227 149.H4 33.433 39.021 1.00 27.48 1692 CZ ARG 227 149.516 34.568 39.585 1.00 29.44 1693 NH1 ARG 227 149.447 34.722 40.902 1.00 31.95 1694 NH2 ARG 227 149.963 35.561 38.831 1.00 19.58 1695 C ARG 227 144.911 30.745 39.367 1.00 17.48 1696 0 ARG 227 144.475 31.894 39.402 1.00 22.08 1697 N PHE 228 144.474 29.822 38.516 1.00 17.49 1698 CA PHE 228 143.439 30.073 37.516 1.00 20.78 1699 CB PHE 228 143.184 28.770 36.741 1.00 17.58 1700 CG PHE 228 142.261 28.908 35.556 1.00 10.74 1701 CD1 PHE 228 141.685 30.128 35.214 1.00 18.32 1702 CD2 PHE 228 141.958 27.791 34.785 1.00 13.57 1703 CE1 PHE 228 140.819 30.230 34.122 1.00 18.76 1704 CE2 PHE 228 141.095 27.883 33.692 1.00 18.93 1705 CZ PHE 228 140.525 29.106 33.361 1.00 12.22 1706 C PHE 228 142.158 30.552 38.205 1.00 20.33 1707 0 PHE 228 141.585 31.580 37.834 1.00 17.12 1708 N ALA 229 141.746 29.817 39.233 1.00 15.85 1709 CA ALA 229 140.541 30.125 39.989 1.00 14.57 1710 CB ALA 229 140.320 29.069 41.059 1.00 11.49 1711 C ALA 229 140.572 31.513 40.619 1.00 22.21 1712 0 ALA 229 139.606 32.272 40.505 1.00 26.82 1713 N LYS 230 141.683 31.841 41.278 1.00 17.14 1714 CA LYS 230 141.836 33.136 41.933 1.00 13.72 1715 CB LYS 230 143.118 33.168 42.766 1.00 17.71 1716 CG LYS 230 143.067 32.332 44.030 1.00 14.07 1717 CD LYS 230 144.343 32.505 44.835 1.00 23.37 1718 CE LYS 230 144.253 31.802 46.177 1.00 31.01 1719 NZ LYS 230 145.477 32.021 46.994 1.00 32.57 1720 C LYS 230 141.816 34.310 40.956 1.00 16.07 1721 0 LYS 230 141.111 35.292 41.176 1.00 15.73 1722 N LEU 231 142.585 34.202 39.876 1.00 17.93 1723 CA LEU 231 142.646 35.260 38.872 1.00 20.80 1724 CB LEU 231 143.653 34.911 37.775 1.00 18.38 1725 CG LEU 231 145.U1 34.870 38.116 1.00 16.32 1726 CD1 LEU 231 145.920 34.518 36.863 1.00 14.82 1727 CD2 LEU 231 145.593 36.212 38.658 1.00 15.83 1728 C LEU 231 141.287 35.506 38.233 1.00 24.81 1729 0 LEU 231 140.828 36.647 38.151 1.00 28.14 1730 N ASP 232 140.648 34.427 37.790 1.00 28.52 1731 CA ASP 232 139.344 34.503 37.139 1.00 23.60 1732 CB ASP 232 138.878 33.104 36.736 1.00 20.22 1733 CG ASP 232 137.737 33.137 35.742 1.00 29.93 1734 0D1 ASP 232 138.019 33.223 34.527 1.00 24.38 1735 0D2 ASP 232 136.564 33.079 36.174 1.00 26.36 1736 C ASP 232 138.300 35.170 38.032 1.00 20.67 1737 0 ASP 232 137.622 36.111 37.612 1.00 15.86 1738 N PHE 233 138.203 34.707 39.274 1.00 12.27 1739 CA PHE 233 137.244 35.260 40.219 1.00 12.59 1740 CB PHE 233 137.355 34.549 41.569 1.00 14.20 1741 CG PHE 233 136.243 34.887 42.524 1.00 30.75 1742 CD1 PHE 233 135.130 34.058 42.634 1.00 33.32 1743 CD2 PHE 233 136.298 36.042 43.302 1.00 29.41 1744 CE1 PHE 233 134.088 34.372 43.502 1.00 34.63 1745 CE2 PHE 233 135.263 36.365 44.172 1.00 31.81 1746 CZ PHE 233 134.155 35.528 44.272 1.00 32.38 1747 C PHE 233 137.452 36.760 40.407 1.00 18.84 1748 O PHE 233 136.495 37.534 40.394 1.00 24.79 1749 N ASN 234 138.710 37.160 40.572 1.00 25.72 1750 CA ASN 234 139.057 38.563 40.770 1.00 20.56 1751 CB ASN 234 140.509 38.694 41.239 1.00 25.13 1752 CG ASN 234 140.702 38.249 42.683 1.00 30.65 1753 OD1 ASN 234 139.738 37.996 43.406 1.00 21.26 1754 ND2 ASN 234 141.957 38.162 43.109 1.00 35.99 1755 C ASN 234 138.818 39.427 39.536 1.00 18.33 1756 O ASN 234 138.457 40.599 39.662 1.00 15.79 1757 N LEU 235 139.019 38.848 38.353 1.00 17.45 1758 CA LEU 235 138.814 39.567 37.097 1.00 16.13 1759 CB LEU 235 139.402 38.789 35.920 1.00 14.09 1760 CG LEU 235 139.233 39.426 34.534 1.00 25.16 1761 CD1 LEU 235 139.947 40.774 34.472 1.00 16.26 1762 CD2 LEU 235 139.762 38.487 33.458 1.00 11.51 1763 C LEU 235 137.329 39.812 36.866 1.00 23.53 1764 O LEU 235 136.929 40.918 36.502 1.00 30.18 1765 N LEU 236 136.517 38.773 37.065 1.00 26.97 1766 CA LEU 236 135.071 38.894 36.900 1.00 21.97 1767 CB LEU 236 134.375 37.538 37.041 1.00 22.99 1768 CG LEU 236 134.550 36.506 35.931 1.00 24.74 1769 CD1 LEU 236 133.601 35.347 36.187 1.00 22.83 1770 CD2 LEU 236 134.259 37.133 34.579 1.00 26.05 1771 C LEU 236 134.511 39.858 37.935 1.00 15.40 1772 O LEU 236 133.581 40.602 37.646 1.00 21.06 1773 N GLN 237 135.080 39.837 39.139 1.00 13.42 1774 CA GLN 237 134.645 40.721 40.217 1.00 14.55 1775 CB GLN 237 135.477 40.481 41.475 1.00 14.51 1776 CG GLN 237 135.051 41.318 42.671 1.00 12.72 1777 CD GLN 237 135.967 41.131 43.862 1.00 12.21 1778 OE1 GLN 237 137.121 41.566 43.847 1.00 18.76 1779 NE2 GLN 237 135.460 40.483 44.900 1.00 4.88 1780 C GLN 237 134.760 42.180 39.788 1.00 22.23 1781 O GLN 237 133.950 43.011 40.192 1.00 28.74 1782 N MET 238 135.770 42.481 38.970 1.00 29.92 1783 CA MET 238 135.985 43.833 38.458 1.00 23.66 1784 CB MET 238 137.275 43.906 37.638 1.00 25.72 1785 CG MET 238 138.552 43.791 38.454 1.00 26.38 1786 SD MET 238 140.030 43.684 37.408 1.00 30.42 1787 CE MET 238 141.233 43.058 38.580 1.00 23.83 1788 C MET 238 134.801 44.227 37.584 1.00 20.92 1789 O MET 238 134.344 45.367 37.628 1.00 20.70 1790 N LEU 239 134.310 43.274 36.792 1.00 23.17 1791 CA LEU 239 133.159 43.509 35.920 1.00 21.15 1792 CB LEU 239 132.938 42.323 34.978 1.00 10.92 1793 CG LEU 239 131.684 42.381 34.100 1.00 20.20 1794 CD1 LEU 239 131.748 43.579 33.166 1.00 9.66 1795 CD2 LEU 239 131.541 41.089 33.309 1.00 10.55 1796 C LEU 239 131.908 43.732 36.764 1.00 14.68 1797 0 LEU 239 131.129 44.645 36.501 1.00 23.63 1798 N HIS 240 131.735 42.904 37.788 1.00 15.07 1799 CA HIS 240 130.587 43.015 38.680 1.00 19.33 1800 CB HIS 240 130.619 41.913 39.746 1.00 16.76 1801 CG HIS 240 130.661 40.525 39.185 1.00 12.10 1802 CD2 HIS 240 130.296 40.039 37.973 1.00 12.51 1803 ND1 HIS 240 131.144 39.449 39.897 1.00 8.57 1804 CE1 HIS 240 131.077 38.362 39.150 1.00 16.05 1805 NE2 HIS 240 130.567 38.692 37.979 1.00 13.30 1806 C HIS 240 130.610 44.383 39.344 1.00 21.46 1807 0 HIS 240 129.572 45.034 39.481 1.00 28.61 1808 N LYS 241 131.809 44.819 39.728 1.00 24.98 1809 CA LYS 241 132.008 46.118 40.364 1.00 19.85 1810 CB LYS 241 133.469 46.281 40.782 1.00 18.41 1811 CG LYS 241 133.855 45.556 42.057 1.00 18.41 1812 CD LYS 241 135.348 45.688 42.297 1.00 29.39 1813 CE LYS 241 135.667 45.861 43.769 1.00 43.69 1814 NZ LYS 241 137.131 45.987 43.991 1.00 46.04 1815 C LYS 241 131.604 47.252 39.419 1.00 23.69 1816 0 LYS 241 130.983 48.229 39.845 1.00 14.81 1817 N GLN 242 131.954 47.107 38.140 1.00 20.70 1818 CA GLN 242 131.615 48.099 37.120 1.00 28.94 1819 CB GLN 242 132.262 47.748 35.775 1.00 29.06 1820 CG GLN 242 133.775 47.862 35.748 1.00 39.14 1821 CD GLN 242 134.359 47.517 34.392 1.00 42.97 1822 OE1 GLN 242 134.324 46.363 33.962 1.00 48.36 1823 NE2 GLN 242 134.904 48.519 33.710 1.00 39.66 1824 C GLN 242 130.103 48.163 36.943 1.00 33.40 1825 0 GLN 242 129.514 49.246 36.938 1.00 40.80 1826 N GLU 243 129.487 46.992 36.807 1.00 33.80 1827 CA GLU 243 128.044 46.884 36.631 1.00 22.54 1828 CB GLU 243 127.647 45.420 36.466 1.00 15.53 1829 CG GLU 243 128.204 44.778 35.210 1.00 15.70 1830 CD GLU 243 127.938 43.290 35.137 1.00 18.78 1831 OE1 GLU 243 127.639 42.675 36.178 1.00 18.01 1832 OE2 GLU 243 128.040 42.727 34.032 1.00 15.89 1833 C GLU 243 127.290 47.495 37.806 1.00 20.49 1834 0 GLU 243 126.351 48.266 37.611 1.00 18.81 1835 N LEU 244 127.715 47.159 39.022 1.00 12.97 1836 CA LEU 244 127.079 47.675 40.231 1.00 15.01 1837 CB LEU 244 127.676 46.999 41.467 1.00 12.34 1838 CG LEU 244 127.144 47.436 42.832 1.00 12.62 1839 CD1 LEU 244 125.628 47.332 42.881 1.00 24.09 1840 CD2 LEU 244 127.780 46.582 43.908 1.00 9.05 1841 C LEU 244 127.213 49.191 40.335 1.00 22.78 1842 0 LEU 244 126.328 49.868 40.863 1.00 27.46 1843 N ALA 245 128.325 49.725 39.838 1.00 31.72 1844 CA 245 128.560 51.167 39.856 1.00 30.71 1 1884455 C CBB ALA 245 129.998 51.476 39.466 1.00 26.12 1846 C ALA 245 127.589 51.860 38.893 1.00 29.98 1847 0 ALA 245 127.005 52.887 39.226 1.00 32.44 1848 N GLN 246 127.410 51.256 37.718 1.00 29.03 1849 CA GLN 246 126.528 51.754 36.668 1.00 31.14 1850 CB GLN 246 126.689 50.868 35.430 1.00 31.92 1851 CG GLN 246 125.845 51.244 34.232 1.00 41.36 1852 CD GLN 246 125.970 50.235 33.109 1.00 48.09 1853 OE1 GLN 246 127.023 49.627 32.919 1.00 49.29 1854 NE2 GLN 246 124.887 50.043 32.361 1.00 55.11 1855 C GLN 246 125.074 51.762 37.119 1.00 34.84 1856 0 GLN 246 124.297 52.637 36.732 1.00 42.31 1857 N VAL 247 124.719 50.762 37.921 1.00 39.27 1858 CA VAL 247 123.360 50.631 38.441 1.00 38.03 1859 CB VAL 247 123.069 49.138 38.742 1.00 38.04 1860 CG1 VAL 247 122.330 48.954 40.059 1.00 39.31 1861 CG2 VAL 247 122.270 48.526 37.603 1.00 37.60 1862 C VAL 247 123.144 51.507 39.667 1.00 37.49 1863 0 VAL 247 122.012 51.862 39.998 1.00 33.11 1864 N SER 248 124.231 51.871 40.340 1.00 39.80 1865 CA SER 248 124.173 52.736 41.515 1.00 43.54 1866 CB SER 248 125.456 52.604 42.352 1.00 41.35 1867 OG SER 248 125.482 51.368 43.057 1.00 23.81 1868 C SER 248 123.963 54.195 41.093 1.00 41.56 1869 0 SER 248 123.288 54.976 41.783 1.00 39.28 1870 N ARG 249 124.591 54.559 39.974 1.00 40.01 1871 CA ARG 249 124.467 55.901 39.421 1.00 47.97 1872 CB ARG 249 125.475 56.127 38.290 1.00 51.84 1873 CG ARG 249 126.912 56.292 38.747 1.00 62.62 1874 CD ARG 249 127.836 56.501 37.563 1.00 69.45 1875 NE ARG 249 129.065 55.731 37.713 1.00 78.07 1876 CZ ARG 249 129.491 54.824 36.840 1.00 81.11 1877 NH1 ARG 249 128.795 54.570 35.737 1.00 75.69 1878 NH2 ARG 249 130.602 54.145 37.087 1.00 86.20 1879 C ARG 249 123.051 56.058 38.890 1.00 43.68 1880 0 ARG 249 122.402 57.072 39.127 1.00 45.81 1881 N TRP 250 122.588 55.030 38.183 1.00 38.57 1882 CA TRP 250 121.247 55.000 37.613 1.00 34.46 1883 CB TRP 250 121.060 53.682 36.851 1.00 37.42 1884 CG TRP 250 119.635 53.325 36.531 1.00 37.50 1885 CD2 TRP 250 118.745 52.545 37.341 1.00 32.98 1886 CE2 TRP 250 117.516 52.464 36.652 1.00 39.28 1887 CE3 TRP 250 118.867 51.909 38.585 1.00 32.90 1888 CD1 TRP 250 118.931 53.672 35.413 1.00 28.29 1889 NE1 TRP 250 117.658 53.159 35.479 1.00 36.07 1890 CZ2 TRP 250 116.411 51.771 37.167 1.00 40.28 1891 CZ3 TRP 250 117.770 51.221 39.098 1.00 33.00 1892 CH2 TRP 250 116.557 51.159 38.388 1.00 34.10 1893 C TRP 250 120.215 55.131 38.731 1.00 31.76 1894 0 TRP 250 119.207 55.820 38.583 1.00 38.62 1895 N TRP 251 120.499 54.493 39.861 1.00 29.34 1896 CA TRP 251 119.611 54.513 41.017 1.00 28.23 1897 CB TRP 251 120.041 53.431 42.003 1.00 24.43 1898 CG TRP 251 119.164 53.309 43.196 1.00 27.54 1899 CD2 TRP 251 117.813 52.824 43.224 1.00 28.47 1900 CE2 TRP 251 117.394 52.848 44.576 1.00 30.61 1901 CE3 TRP 251 116.921 52.373 42.246 1.00 22.56 1902 CD1 TRP 251 119.493 53.603 44.486 1.00 29.85 1903 NE1 TRP 251 118.439 53.327 45.321 1.00 28.21 1904 CZ2 TRP 251 116.117 52.434 44.974 1.00 27.80 1905 CZ3 TRP 251 115.646 51.959 42.641 1.00 16.40 1906 CH2 TRP 251 115.261 51.995 43.993 1.00 23.32 1907 C TRP 251 119.575 55.877 41.703 1.00 37.98 1908 0 TRP 251 118.564 56.243 42.309 1.00 45.16 1909 N LYS 252 120.685 56.610 41.636 1.00 42.00 1910 CA LYS 252 120.758 57.938 42.238 1.00 42.12 1911 CB LYS 252 122.198 58.328 42.551 1.00 47.95 1912 CG LYS 252 122.598 58.028 43.975 1.00 54.42 1913 CD LYS 252 123.720 58.943 44.418 1.00 63.61 1914 CE LYS 252 123.889 58.896 45.923 1.00 76.47 1915 NZ LYS 252 124.827 59.944 46.407 1.00 82.00 1916 C LYS 252 120.113 58.992 41.348 1.00 43.32 1917 0 LYS 252 119.528 59.955 41.845 1.00 40.24 1918 N ASP 253 120.220 58.802 40.033 1.00 41.81 1919 CA ASP 253 119.621 59.715 39.061 1.00 42.20 1920 CB ASP 253 119.991 59.305 37.632 1.00 46.23 1921 CG ASP 253 121.475 59.448 37.340 1.00 56.62 1922 0D1 ASP 253 122.222 59.973 38.197 1.00 59.66 1923 OD2 ASP 253 121.896 59.029 36.240 1.00 59.43 1924 C ASP 253 118.100 59.701 39.208 1.00 46.95 1925 0 ASP 253 117.404 60.508 38.597 1.00 47.82 1926 N LEU 254 117.600 58.743 39.987 1.00 50.43 1927 CA LEU 254 116.172 58.596 40.253 1.00 52.57 1928 CB LEU 254 115.777 57.116 40.236 1.00 51.09 1929 CG LEU 254 116.036 56.357 38.930 1.00 52.73 1930 CD1 LEU 254 115.673 54.894 39.102 1.00 50.16 1931 CD2 LEU 254 115.244 56.974 37.788 1.00 48.48 1932 C LEU 254 115.867 59.205 41.619 1.00 50.66 1933 0 LEU 254 114.780 59.735 41.848 1.00 48.89 1934 N ASP 255 116.838 59.099 42.522 1.00 54.73 1935 CA ASP 255 116.750 59.641 43.875 1.00 59.42 1936 CB ASP 255 116.930 61.167 43.829 1.00 63.16 1937 CG ASP 255 117.232 61.774 45.193 1.00 70.47 1938 OD1 ASP 255 117.674 61.045 46.110 1.00 70.14 1939 OD2 ASP 255 117.030 62.997 45.344 1.00 79.11 1940 C ASP 255 115.476 59.260 44.640 1.00 56.10 1941 0 ASP 255 114.834 60.106 45.263 1.00 54.97 1942 N PHE 256 115.127 57.977 44.602 1.00 55.78 1943 CA PHE 256 113.946 57.486 45.308 1.00 55.28 1944 CB PHE 256 1 13.556 56.093 44.808 1.00 51.79 1945 CG PHE 256 113.024 56.079 43.407 1.00 52.55 1946 CD1 PHE 256 1 13.356 55.051 42.537 1.00 55.14 1947 CD2 PHE 256 112.186 57.091 42.955 1.00 58.21 1948 CE1 PHE 256 1 12.862 55.028 41.236 1.00 57.90 1949 CE2 PHE 256 1 11.687 57.077 41.656 1.00 60.53 1950 CZ PHE 256 112.026 56.042 40.796 1.00 57.76 1951 C PHE 256 114.199 57.438 46.812 1.00 60.70 1952 O PHE 256 113.292 57.162 47.596 1.00 62.84 1953 N VAL 257 115.442 57.704 47.203 1.00 64.41 1954 CA VAL 257 115.834 57.697 48.606 1.00 64.01 1955 CB VAL 257 117.373 57.799 48.757 1.00 62.36 1956 CG1 VAL 257 117.789 57.482 50.187 1.00 60.29 1957 CG2 VAL 257 118.068 56.864 47.774 1.00 58.27 1958 C VAL 257 115.179 58.870 49.333 1.00 65.72 1959 O VAL 257 114.849 58.771 50.517 1.00 64.55 1960 N THR 258 114.977 59.971 48.609 1.00 66.40 1961 CA THR 258 114.364 61.171 49.175 1.00 65.40 1962 CB THR 258 115.200 62.437 48.870 1.00 65.98 1963 OG1 THR 258 115.282 62.633 47.453 1.00 65.25 1964 CG2 THR 258 116.608 62.302 49.442 1.00 64.28 1965 C THR 258 112.919 61.399 48.716 1.00 62.28 1966 O THR 258 112.066 61.769 49.524 1.00 62.30 1967 N THR 259 112.649 61.182 47.428 1.00 58.00 1968 CA THR 259 111.303 61.372 46.879 1.00 53.45 1969 CB THR 259 111.300 61.402 45.332 1.00 48.24 1970 OG1 THR 259 111.730 60.136 44.818 1.00 47.10 1971 CG2 THR 259 112.221 62.496 44.817 1.00 44.78 1972 C THR 259 110.320 60.303 47.358 1.00 54.85 1973 O THR 259 109.147 60.593 47.593 1.00 58.40 1974 N LEU 260 110.802 59.069 47.492 1.00 54.85 1975 CA LEU 260 109.977 57.952 47.958 1.00 57.07 1976 CB LEU 260 109.811 56.907 46.845 1.00 54.53 1977 CG LEU 260 109.191 57.346 45.511 1.00 54.02 1978 CD1 LEU 260 109.216 56.192 44.523 1.00 47.30 1979 CD2 LEU 260 107.765 57.838 45.715 1.00 53.62 1980 C LEU 260 110.655 57.326 49.183 1.00 59.06 1981 O LEU 260 111.135 56.190 49.132 1.00 61.18 1982 N PRO 261 110.672 58.057 50.314 1.00 59.80 1983 CD PRO 261 110.004 59.362 50.474 1.00 57.03 1984 CA PRO 261 111.281 57.634 51.582 1.00 60.02 1985 CB PRO 261 111.144 58.883 52.452 1.00 59.64 1986 CG PRO 261 109.865 59.476 51.972 1.00 61.83 1987 C PRO 261 110.685 56.401 52.265 1.00 56.67 1988 O PRO 261 111.317 55.811 53.143 1.00 54.94 1989 N TYR 262 109.475 56.019 51.869 1.00 55.28 1990 CA TYR 262 108.813 54.855 52.455 1.00 52.74 1991 CB TYR 262 107.309 54.898 52.167 1.00 46.52 1992 CG TYR 262 106.954 54.869 50.695 1.00 38.58 1993 CD1 TYR 262 106.624 53.671 50.062 1.00 30.09 1994 CE1 TYR 262 106.295 53.636 48.711 1.00 29.27 1995 CD2 TYR 262 106.944 56.039 49.936 1.00 34.60 1996 CE2 TYR 262 106.614 56.015 48.581 1.00 37.08 1997 CZ TYR 262 106.290 54.809 47.974 1.00 32.64 1998 OH TYR 262 105.961 54.776 46.635 1.00 17.43 1999 C TYR 262 109.398 53.534 51.956 1.00 52.07 2000 0 TYR 262 109.356 52.522 52.658 1.00 51.95 2001 N ALA 263 109.957 53.565 50.748 1.00 48.22 2002 CA ALA 263 110.545 52.386 50.120 1.00 49.01 2003 CB ALA 263 110.701 52.627 48.623 1.00 44.24 2004 C ALA 263 111.879 51.943 50.723 1.00 52.04 2005 0 ALA 263 112.458 52.631 51.567 1.00 52.30 2006 N ARG 264 112.333 50.766 50.297 1.00 53.43 2007 CA ARG 264 113.592 50.196 50.752 1.00 48.17 2008 CB ARG 264 113.499 48.670 50.889 1.00 40.34 2009 CG ARG 264 112.624 48.166 52.030 1.00 43.53 2010 CD ARG 264 112.450 46.639 51.996 1.00 35.92 2011 NE ARG 264 111.772 46.200 50.774 1.00 44.75 2012 CZ ARG 264 110.964 45.144 50.679 1.00 49.82 2013 NH1 ARG 264 110.714 44.385 51.738 1.00 51.07 2014 NH2 ARG 264 110.385 44.857 49.518 1.00 37.04 2015 C ARG 264 114.676 50.512 49.742 1.00 49.03 2016 0 ARG 264 114.453 50.444 48.527 1.00 47.55 2017 N ASP 265 115.848 50.870 50.252 1.00 50.80 2018 CA ASP 265 116.987 51.164 49.392 1.00 51.29 2019 CB ASP 265 117.728 52.418 49.877 1.00 52.76 2020 CG ASP 265 118.690 52.955 48.843 1.00 54.37 2021 0D1 ASP 265 118.782 52.363 47.747 1.00 50.00 2022 0D2 ASP 265 119.358 53.972 49.120 1.00 60.30 2023 C ASP 265 117.903 49.933 49.419 1.00 45.08 2024 0 ASP 265 118.824 49.846 50.238 1.00 39.53 2025 N ARG 266 117.614 48.973 48.541 1.00 41.67 2026 CA ARG 266 118.377 47.732 48.462 1.00 37.99 2027 CB ARG 266 117.528 46.574 48.983 1.00 38.78 2028 CG ARG 266 116.957 46.771 50.372 1.00 29.99 2029 CD ARG 266 118.028 46.593 51.418 1.00 37.48 2030 NE ARG 266 117.503 46.781 52.764 1.00 38.27 2031 CZ ARG 266 117.416 47.958 53.376 1.00 45.66 2032 NH1 ARG 266 117.822 49.066 52.763 1.00 38.28 2033 NH2 ARG 266 116.920 48.027 54.603 1.00 42.90 2034 C ARG 266 118.826 47.429 47.034 1.00 33.86 2035 0 ARG 266 118.671 46.306 46.542 1.00 40.81 2036 N VAL 267 119.392 48.431 46.371 1.00 25.69 2037 CA VAL 267 119.845 48.257 45.000 1.00 20.97 2038 CB VAL 267 120.143 49.611 44.326 1.00 21.69 2039 CG1 VAL 267 121.384 50.264 44.933 1.00 20.36 2040 CG2 VAL 267 120.292 49.420 42.828 1.00 8.30 2041 C VAL 267 121.058 47.333 44.913 1.00 27.40 2042 0 VAL 267 121.231 46.616 43.926 1.00 36.12 2043 N VAL 268 121.889 47.347 45.952 1.00 30.76 2044 CA VAL 268 123.080 46.503 46.008 1.00 32.68 2045 CB VAL 268 123.998 46.904 47.190 1.00 35.53 2046 CG1 VAL 268 125.220 46.001 47.245 1.00 32.24 2047 CG2 VAL 268 124.420 48.355 47.058 1.00 33.69 2048 C VAL 268 122.623 45.058 46.196 1.00 29.06 2049 0 VAL 268 123.119 44.144 45.533 1.00 25.58 2050 N GLU 269 121.662 44.878 47.100 1.00 24.94 2051 CA GLU 269 121.087 43.573 47.406 1.00 22.59 2052 CB GLU 269 120.083 43.692 48.558 1.00 16.86 2053 CG GLU 269 120.705 43.939 49.942 1.00 22.84 2054 CD GLU 269 121.136 45.385 50.200 1.00 25.18 2055 0E1 GLU 269 121.417 45.713 51.374 1.00 24.26 2056 0E2 GLU 269 121.194 46.198 49.255 1.00 23.69 2057 C GLU 269 120.404 43.001 46.167 1.00 21.52 2058 0 GLU 269 120.423 41.789 45.941 1.00 22.99 2059 N CYS 270 119.814 43.885 45.365 1.00 16.93 2060 CA CYS 270 119.144 43.487 44.133 1.00 15.61 2061 CB CYS 270 118.305 44.637 43.577 1.00 14.26 2062 SG CYS 270 116.923 45.097 44.637 1.00 24.62 2063 C CYS 270 120.191 43.065 43.117 1.00 19.83 2064 0 CYS 270 119.922 42.239 42.245 1.00 25.94 2065 N TYR 271 121.382 43.648 43.220 1.00 25.82 2066 CA TYR 271 122.464 43.290 42.315 1.00 22.31 2067 CB TYR 271 123.616 44.296 42.366 1.00 15.29 2068 CG TYR 271 124.715 43.914 41.408 1.00 11.26 2069 CD1 TYR 271 124.592 44.174 40.043 1.00 9.23 2070 CE1 TYR 271 125.534 43.705 39.135 1.00 12.75 2071 CD2 TYR 271 125.821 43.184 41.844 1.00 6.39 2072 CE2 TYR 271 126.767 42.709 40.946 1.00 6.94 2073 CZ TYR 271 126.615 42.970 39.594 1.00 11.07 2074 OH TYR 271 127.525 42.467 38.702 1.00 9.47 2075 C TYR 271 122.973 41.904 42.692 1.00 23.07 2076 0 TYR 271 123.318 41.104 41.820 1.00 22.92 2077 N PHE 272 123.037 41.639 43.997 1.00 17.89 2078 CA PHE 272 123.484 40.344 44.500 1.00 17.87 2079 CB PHE 272 123.481 40.329 46.033 1.00 20.14 2080 CG PHE 272 123.722 38.967 46.625 1.00 18.24 2081 CD1 PHE 272 124.998 38.409 46.631 1.00 20.70 2082 CD2 PHE 272 122.669 38.232 47.160 1.00 19.50 2083 CE1 PHE 272 125.219 37.139 47.159 1.00 15.25 2084 CE2 PHE 272 122.881 36.961 47.690 1.00 17.71 2085 CZ PHE 272 124.159 36.414 47.689 1.00 12.72 2086 C PHE 272 122.540 39.273 43.972 1.00 20.61 2087 0 PHE 272 122.974 38.200 43.550 1.00 26.50 2088 N TRP 273 121.248 39.594 43.982 1.00 24.31 2089 CA TRP 273 120.203 38.695 43.506 1.00 20.50 2090 CB TRP 273 118.831 39.335 43.724 1.00 22.07 2091 CG TRP 273 117.820 38.395 44.280 1.00 22.11 2092 CD2 TRP 273 117.499 38.205 45.661 1.00 17.16 2093 CE2 TRP 273 116.513 37.193 45.726 1.00 18.77 2094 CE3 TRP 273 117.949 38.789 46.851 1.00 16.10 2095 CD1 TRP 273 117.036 37.522 43.580 1.00 22.90 2096 NE1 TRP 273 116.250 36.794 44.442 1.00 15.33 2097 CZ2 TRP 273 1 15.969 36.750 46.938 1.00 8.52 2098 CZ3 TRP 273 117.408 38.351 48.057 1.00 19.38 2099 CH2 TRP 273 116.428 37.339 48.088 1.00 25.09 2100 C TRP 273 120.401 38.389 42.024 1.00 19.25 2101 O TRP 273 120.291 37.239 41.596 1.00 26.32 2102 N ALA 274 120.705 39.424 41.247 1.00 15.42 2103 CA ALA 274 120.925 39.267 39.815 1.00 17.00 2104 CB ALA 274 120.927 40.622 39.138 1.00 8J5 2105 C ALA 274 122.240 38.538 39.553 1.00 21.87 2106 O ALA 274 122.394 37.858 38.535 1.00 24.79 2107 N LEU 275 123.188 38.694 40.474 1.00 18.76 2108 CA LEU 275 124.487 38.045 40.354 1.00 20.76 2109 CB LEU 275 125.505 38.712 41.281 1.00 15.67 2110 CG LEU 275 126.937 38.176 41.221 1.00 6.06 2111 CD1 LEU 275 127.475 38.257 39.798 1.00 5.14 2112 CD2 LEU 275 127.812 38.960 42.179 1.00 9.22 2113 C LEU 275 124.351 36.560 40.684 1.00 19.71 2114 O LEU 275 125.130 35.731 40.206 1.00 17.59 2115 N GLY 276 123.356 36.239 41.507 1.00 22.38 2116 CA GLY 276 123.098 34.860 41.880 1.00 15.02 2117 C GLY 276 122.429 34.101 40.747 1.00 8.27 2118 O GLY 276 122.574 32.885 40.641 1.00 21.39 2119 N VAL 277 121.693 34.825 39.904 1.00 9.55 2120 CA VAL 277 120.992 34.245 38.758 1.00 6J9 2121 CB VAL 277 119.950 35.238 38.201 1.00 4.45 2122 CG1 VAL 277 119.236 34.660 36.994 1.00 2.00 2123 CG2 VAL 277 118.946 35.576 39.284 1.00 2.00 2124 C VAL 277 122.003 33.848 37.686 1.00 9.32 2125 O VAL 277 121.872 32.807 37.042 1.00 17.27 2126 N TYR 278 122.992 34.711 37.481 1.00 13.83 2127 CA TYR 278 124.082 34.466 36.543 1.00 17.57 2128 CB TYR 278 123.644 34.476 35.067 1.00 14.31 2129 CG TYR 278 122.485 35.368 34.675 1.00 21.92 2130 CD1 TYR 278 122.304 36.630 35.242 1.00 28.06 2131 CE1 TYR 278 121.249 37.454 34.839 1.00 17.69 2132 CD2 TYR 278 121.581 34.952 33.698 1.00 10.48 2133 CE2 TYR 278 120.532 35.762 33.290 1.00 15.32 2134 CZ TYR 278 120.371 37.012 33.860 1.00 20.32 2135 OH TYR 278 119.341 37.820 33.432 1.00 16.49 2136 C TYR 278 125.236 35.423 36.790 1.00 22.42 2137 O TYR 278 125.024 36.609 37.052 1.00 24.68 2138 N PHE 279 126.454 34.883 36.756 1.00 20.65 2139 CA PHE 279 127.665 35.662 36.998 1.00 24.23 2140 CB PHE 279 128.474 35.036 38.140 1.00 19.97 2141 CG PHE 279 129.063 33.694 37.800 1.00 27.50 2142 CD1 PHE 279 130.278 33.600 37.124 1.00 27.56 2143 CD2 PHE 279 128.387 32.523 38.120 1.00 26.31 2144 CE1 PHE 279 130.804 32.363 36.770 1.00 27.48 2145 CE2 PHE 279 128.906 31.283 37.770 1.00 27.51 2146 CZ PHE 279 130.116 31.202 37.093 1.00 26.58 2147 C PHE 279 128.564 35.797 35.773 1.00 22.60 2148 0 PHE 279 129.420 36.681 35.727 1.00 29.14 2149 N GLU 280 128.404 34.893 34.811 1.00 26.53 2150 CA GLU 280 129.217 34.909 33.599 1.00 25.23 2151 CB GLU 280 128.759 33.832 32.608 1.00 31.74 2152 CG GLU 280 129.004 32.392 33.056 1.00 26.55 2153 CD GLU 280 127.873 31.806 33.899 1.00 40.41 2154 0E1 GLU 280 127.909 30.581 34.149 1.00 41.01 2155 0E2 GLU 280 126.949 32.549 34.307 1.00 31.27 2156 C GLU 280 129.195 36.276 32.928 1.00 28.72 2157 0 GLU 280 128.169 36.958 32.918 1.00 21.31 2158 N PRO 281 130.346 36.702 32.382 1.00 31.20 2159 CD PRO 281 131.607 35.942 32.368 1.00 29.80 2160 CA PRO 281 130.511 37.988 31.697 1.00 31.18 2161 CB PRO 281 131.976 37.949 31.246 1.00 36.16 2162 CG PRO 281 132.274 36.479 31.137 1.00 35.87 2163 C PRO 281 129.561 38.213 30.522 1.00 29.70 2164 0 PRO 281 129.196 39.352 30.226 1.00 29.95 2165 N GLN 282 129.161 37.126 29.866 1.00 27.63 2166 CA GLN 282 128.252 37.194 28.722 1.00 28.39 2167 CB GLN 282 128.174 35.832 28.028 1.00 34.10 2168 CG GLN 282 127.630 34.717 28.912 1.00 45.80 2169 CD GLN 282 127.714 33.351 28.264 1.00 47.83 2170 0E1 GLN 282 128.543 32.523 28.647 1.00 54.06 2171 NE2 GLN 282 126.848 33.101 27.285 1.00 41.38 2172 C GLN 282 126.851 37.640 29.133 1.00 25.75 2173 0 GLN 282 126.061 38.071 28.294 1.00 34.41 2174 N TYR 283 126.553 37.521 30.425 1.00 26.54 2175 CA TYR 283 125.254 37.910 30.972 1.00 26.30 2176 CB TYR 283 124.765 36.853 31.966 1.00 19.61 2177 CG TYR 283 124.537 35.506 31.323 1.00 13.47 2178 CD1 TYR 283 125.030 34.339 31.901 T.00 13.33 2179 CE1 TYR 283 124.852 33.099 31.286 1.00 15.49 2180 CD2 TYR 283 123.853 35.402 30.112 1.00 18.67 2181 CE2 TYR 283 123.669 34.173 29.490 1.00 23.42 2182 CZ TYR 283 124.172 33.026 30.079 1.00 14.24 2183 OH TYR 283 124.002 31.817 29.448 1.00 22.41 2184 C TYR 283 125.304 39.287 31.632 1.00 29.24 2185 0 TYR 283 124.504 39.599 32.517 1.00 27.80 2186 N SER 284 126.244 40.108 31.170 1.00 29.09 2187 CA SER 284 126.438 41.461 31.673 1.00 24.35 2188 CB SER 284 127.644 42.103 30.981 1.00 29.60 2189 OG SER 284 127.873 43.418 31.456 1.00 29.67 2190 C SER 284 125.192 42.315 31.451 1.00 23.95 2191 0 SER 284 124.647 42.882 32.396 1.00 16.24 2192 N GLN 285 124.743 42.393 30.199 1.00 29.77 2193 CA GLN 285 123.556 43.173 29.852 1.00 36.37 2194 CB GLN 285 123.313 43.138 28.339 1.00 36.36 2195 CG GLN 285 122.119 43.974 27.883 1.00 42.33 2196 CD GLN 285 121.887 43.913 26.382 1.00 47.38 2197 OE1 GLN 285 122.208 42.919 25.727 1.00 45.82 2198 NE2 GLN 285 121.321 44.981 25.832 1.00 47.01 2199 C GLN 285 122.328 42.638 30.588 1.00 40.35 2200 0 GLN 285 121.503 43.413 31.076 1.00 46.67 2201 N ALA 286 122.242 41.312 30.686 1.00 38.34 2202 CA ALA 286 121.136 40.637 31.356 1.00 27.14 2203 CB ALA 286 121.252 39.136 31.170 1.00 34.43 2204 C ALA 286 121.067 40.983 32.837 1.00 24.71 2205 0 ALA 286 119.996 41.319 33.346 1.00 32.18 2206 N ARG 287 122.203 40.891 33.526 1.00 17.67 2207 CA ARG 287 122.261 41.212 34.951 1.00 17.77 2208 CB ARG 287 123.680 41.046 35.504 1.00 14.04 2209 CG ARG 287 124.013 39.659 36.008 1.00 21.57 2210 CD ARG 287 125.294 39.673 36.828 1.00 20.38 2211 NE ARG 287 126.451 40.078 36.033 1.00 14.48 2212 CZ ARG 287 127.080 39.293 35.162 1.00 22.09 2213 NH1 ARG 287 126.670 38.049 34.959 1.00 17.96 2214 NH2 ARG 287 128.132 39.749 34.497 1.00 25.61 2215 C ARG 287 121.802 42.642 35.207 1.00 24.30 2216 0 ARG 287 120.942 42.877 36.046 1.00 22.53 2217 N VAL 288 122.358 43.583 34.449 1.00 32.79 2218 CA VAL 288 122.031 45.001 34.586 1.00 35.93 2219 CB VAL 288 122.800 45.853 33.543 1.00 42.80 2220 CG1 VAL 288 122.484 47.329 33.718 1.00 45.42 2221 CG2 VAL 288 124.294 45.622 33.682 1.00 39.26 ???? C VAL 288 120.525 45.246 34.470 1.00 30.79 2223 0 VAL 288 119.927 45.888 35.339 1.00 27.62 2224 N MET 289 119.914 44.698 33.422 1.00 25.59 2225 CA MET 289 118.473 44.837 33.202 1.00 20.40 2226 CB MET 289 118.055 44.123 31.908 1.00 11.02 2227 CG MET 289 118.675 44.684 30.646 1.00 17.69 2228 SD MET 289 118.236 43.769 29.151 1.00 29.61 2229 CE MET 289 117.076 44.873 28.424 1.00 23.00 2230 C MET 289 117.692 44.246 34.383 1.00 20.89 2231 0 MET 289 116.762 44.861 34.901 1.00 25.06 2232 N LEU 290 118.104 43.063 34.825 1.00 20.72 2233 CA LEU 290 117.448 42.379 35.935 1.00 15.74 2234 CB LEU 290 118.020 40.969 36.078 1.00 14.98 2235 CG LEU 290 117.497 40.044 37.174 1.00 16.12 2236 CD1 LEU 290 115.981 39.981 37.142 1.00 16.37 2237 CD2 LEU 290 118.098 38.659 36.964 1.00 19.76 2238 C LEU 290 117.530 43.139 37.261 1.00 21.50 2239 0 LEU 290 116.561 43.172 38.019 1.00 23.53 2240 N VAL 291 118.675 43.761 37.534 1.00 24.67 2241 CA VAL 291 118.858 44.518 38.773 1.00 28.92 2242 CB VAL 291 120.280 45.113 38.893 1.00 30.77 2243 CG1 VAL 291 120.439 45.822 40.234 1.00 27.10 2244 CG2 VAL 291 121.324 44.033 38.742 1.00 35.91 2245 C VAL 291 117.872 45.679 38.826 1.00 33.69 0 VAL 291 1 17.266 45.950 39.867 1.00 38.64 2247 N N LYS 292 117.722 46.360 37.693 1.00 32.65 2248 CA LYS 292 116.819 47.500 37.589 1.00 29.16 2249 CB LYS 292 116.961 48.155 36.213 1.00 28.67 2250 CG LYS 292 118.314 48.814 35.986 1.00 28.14 2251 CD LYS 292 118.440 49.353 34.575 1.00 36.09 2252 CE LYS 292 119.765 50.059 34.370 1.00 37.49 2253 NZ LYS 292 119.962 50.417 32.940 1.00 42.24 2254 C LYS 292 115.369 47.102 37.849 1.00 25.46 2255 0 LYS 292 114.633 47.829 38.514 1.00 23.99 2256 N THR 293 114.984 45.922 37.365 1.00 28.08 2257 CA THR 293 113.627 45.401 37.536 1.00 20.11 2258 CB THR 293 113.385 44.183 36.617 1.00 19.93 2259 OG1 THR 293 113.325 44.619 35.252 1.00 19.22 2260 CG2 THR 293 112.095 43.472 36.972 1.00 14.44 2261 C THR 293 113.326 45.026 38.987 1.00 22.63 2262 0 THR 293 112.286 45.405 39.524 1.00 30.10 2263 N ILE 294 114.239 44.295 39.621 1.00 23.15 2264 CA ILE 294 114.058 43.884 41.015 1.00 22.01 2265 CB ILE 294 115.232 43.007 41.522 1.00 19.34 2266 CG2 ILE 294 114.962 42.546 42.958 1.00 19.45 2267 CG1 ILE 294 115.430 41.799 40.604 1.00 12.44 2268 CD1 ILE 294 116.564 40.876 41.017 1.00 23.70 2269 C ILE 294 113.959 45.113 41.910 1.00 21.14 2270 0 ILE 294 113.097 45.193 42.789 1.00 23.19 2271 N SER 295 114.841 46.075 41.664 1.00 27.23 2272 CA SER 295 114.879 47.310 42.435 1.00 36.44 2273 CB SER 295 116.063 48.167 41.979 1.00 38.02 2274 OG SER 295 116.508 49.015 43.021 1.00 50.33 2275 C SER 295 113.566 48.077 42.265 1.00 33.20 2276 0 SER 295 112.984 48.562 43.239 1.00 27.63 2277 N MET 296 113.083 48.124 41.026 1.00 32.18 2278 CA MET 296 111.843 48.816 40.685 1.00 33.20 2279 CB MET 296 111.659 48.829 39.165 1.00 33.02 2280 CG MET 296 110.820 49.978 38.637 1.00 34.84 2281 SD MET 296 111.653 51.571 38.807 1.00 40.22 2282 CE MET 296 110.937 52.162 40.336 1.00 31.58 2283 C MET 296 110.617 48.181 41.343 1.00 36.25 2284 0 MET 296 109.831 48.871 41.997 1.00 35.27 2285 N ILE 297 110.462 46.867 41.172 1.00 36.41 2286 CA ILE 297 109.327 46.145 41.743 1.00 31.22 2287 CB ILE 297 109.240 44.681 41.222 1.00 30.61 2288 CG2 ILE 297 110.401 43.850 41.748 1.00 32.13 2289 CG1 ILE 297 107.915 44.039 41.647 1.00 25.21 2290 CD1 ILE 297 106.681 44.725 41.088 1.00 9.77 2291 C ILE 297 109.362 46.151 43.266 1.00 28.01 2292 0 ILE 297 108.333 45.964 43.914 1.00 33.37 2293 N SER 298 110.544 46.369 43.834 1.00 26.49 2294 CA SER 298 110.682 46.410 45.284 1.00 31.31 2295 CB SER 298 112.152 46.511 45.692 1.00 36.65 2296 OG SER 298 112.281 46.533 47.106 1.00 34.52 2297 C SER 298 109.921 47.616 45.810 1.00 31.13 2298 0 SER 298 109.331 47.567 46.888 1.00 32.44 2299 N ILE 299 109.932 48.693 45.029 1.00 31.80 2300 CA ILE 299 109.239 49.923 45.390 1.00 37.55 2301 CB ILE 299 109.648 51.086 44.462 1.00 44.76 2302 CG2 ILE 299 108.809 52.326 44.753 1.00 45.64 2303 CG1 ILE 299 111.135 51.390 44.645 1.00 46.63 2304 CD1 ILE 299 111.656 52.438 43.707 1.00 51.58 2305 C ILE 299 107.735 49.710 45.315 1.00 31.48 2306 0 ILE 299 107.008 50.072 46.238 1.00 32.42 2307 N VAL 300 107.277 49.101 44.224 1.00 27.09 2308 CA VAL 300 105.855 48.824 44.037 1.00 23.95 2309 CB VAL 300 105.598 48.080 42.709 1.00 22.51 2310 CG1 VAL 300 104.108 47.876 42.494 1.00 20.37 2311 CG2 VAL 300 106.190 48.867 41.552 1.00 20.21 2312 C VAL 300 105.349 47.990 45.211 1.00 23.59 2313 0 VAL 300 104.247 48.204 45.714 1.00 30.31 2314 N ASP 301 106.186 47.072 45.674 1.00 24.66 2315 CA ASP 301 105.837 46.226 46.802 1.00 31.65 2316 CB ASP 301 106.879 45.121 46.975 1.00 25.48 2317 CG ASP 301 106.523 44.163 48.087 1.00 24.95 2318 0D1 ASP 301 105.672 43.277 47.869 1.00 37.24 2319 OD2 ASP 301 107.075 44.309 49.193 1.00 32.62 2320 C ASP 301 105.762 47.078 48.065 1.00 33.30 2321 0 A ASSPP 301 104.847 46.930 48.874 1.00 36.41 2322 N AASSPP 302 106.737 47.971 48.218 1.00 41.65 2323 CA AASSPP 302 106.805 48.866 49.369 1.00 43.94 2324 CB AASSPP 302 108.124 49.650 49.353 1.00 49.38 2325 CG AASSPP 302 109.322 48.798 49.744 1.00 55.74 2326 OD1 AASSPP 302 109.246 48.101 50.780 1.00 59.49 2327 OD2 AASSPP 302 110.344 48.833 49.024 1.00 52.10 2 2332288 C C AASSPP 302 105.619 49.831 49.416 1.00 43.11 2 2332299 0 0 AASSPP 302 105.198 50.257 50.493 1.00 44.18 2330 N THR 303 105.081 50.159 48.243 1.00 38.88 2331 CA THR 303 103.945 51.069 48.123 1.00 33.20 2332 CB THR 303 103.745 51.514 46.660 1.00 41.14 2333 OG1 THR 303 104.965 52.075 46.158 1.00 39.42 2334 CG2 THR 303 102.643 52.555 46.564 1.00 44.39 2335 C THR 303 102.652 50.426 48.624 1.00 36.28 2336 0 THR 303 101.930 51.016 49.425 1.00 44.91 2337 N PHE 304 102.367 49.218 48.143 1.00 33.21 2338 CA PHE 304 101.167 48.478 48.532 1.00 26.28 2339 CB PHE 304 101.005 47.234 47.653 1.00 23.04 2340 CG PHE 304 100.431 47.509 46.293 1.00 14.95 2341 CD1 PHE 304 101.250 47.901 45.239 1.00 16.64 2342 CD2 PHE 304 99.068 47.352 46.059 1.00 16.64 2343 CE1 PHE 304 100.720 48.132 43.968 1.00 20.58 2344 CE2 PHE 304 98.527 47.580 44.793 1.00 13.24 2345 CZ PHE 304 99.355 47.971 43.746 1.00 15.28 2346 C PHE 304 101.183 48.032 49.993 1.00 34.53 2347 0 PHE 304 100.135 47.926 50.632 1.00 38.46 2348 N ASP 305 102.379 47.778 50.515 1.00 40.19 2349 CA ASP 305 102.544 47.300 51.881 1.00 46.42 2350 CB ASP 305 103.774 46.399 51.968 1.00 58.96 2351 CG ASP 305 103.431 44.933 51.845 1.00 70.39 2352 OD1 ASP 305 102.647 44.572 50.940 1.00 75.74 2353 OD2 ASP 305 103.957 44.140 52.656 1.00 75.60 2354 C ASP 305 102.605 48.324 53.001 1.00 47.79 2355 0 ASP 305 101.936 48.161 54.022 1.00 46.25 2356 N ALA 306 103.425 49.357 52.831 1.00 52.07 2357 CA ALA 306 103.574 50.362 53.875 1.00 54.53 2358 CB ALA 306 104.958 50.240 54.518 1.00 57.28 2359 C ALA 306 103.312 51.807 53.462 1.00 53.39 2360 0 ALA 306 103.971 52.718 53.965 1.00 58.62 2361 N TYR 307 102.345 52.030 52.576 1.00 51.30 2362 CA TYR 307 102.045 53.395 52.165 1.00 53.81 2363 CB TYR 307 103.107 53.918 51.195 1.00 48.52 2364 CG TYR 307 103.396 55.388 51.392 1.00 55.69 2365 CD1 TYR 307 103.963 55.847 52.581 1.00 59.86 2366 CE1 TYR 307 104.206 57.200 52.789 1.00 62.54 2367 CD2 TYR 307 103.077 56.324 50.411 1.00 56.20 2368 CE2 TYR 307 103.315 57.683 50.608 1.00 59.89 2369 CZ TYR 307 103.878 58.112 51.801 1.00 62.92 2370 OH TYR 307 104.112 59.451 52.009 1.00 66.19 2371 C TYR 307 100.647 53.640 51.597 1.00 59.33 2372 0 TYR 307 99.752 54.078 52.320 1.00 66.09 2373 N GLY 308 100.473 53.364 50.307 1.00 59.69 2374 CA GLY 308 99.199 53.580 49.636 1.00 58.39 2375 C GLY 308 97.924 53.122 50.326 1.00 60.86 2376 0 GLY 308 97.925 52.163 51.101 1.00 61.04 2377 N THR 309 96.833 53.833 50.044 1.00 60.72 2378 CA THR 309 95.522 53.524 50.609 1.00 57.07 2379 CB THR 309 94.751 54.807 50.989 1.00 55.19 2380 0G1 THR 309 94.651 55.667 49.847 1.00 47.62 2381 CG2 THR 309 95.461 55.538 52.117 1.00 46.57 2382 C THR 309 94.693 52.722 49.609 1.00 59.08 2383 0 THR 309 94.996 52.709 48.415 1.00 56.21 2384 N VAL 310 93.631 52.089 50.107 1.00 60.80 2385 CA VAL 310 92.737 51.264 49.295 1.00 62.84 2386 CB VAL 310 91.430 50.932 50.059 1.00 64.23 2387 CG1 VAL 310 90.667 49.821 49.351 1.00 66.80 2388 CG2 VAL 310 91.737 50.534 51.498 1.00 61.87 2389 C VAL 310 92.390 51.903 47.947 1.00 63.74 2390 0 VAL 310 92.469 51.244 46.904 1.00 60.65 2391 N LYS 311 92.038 53.189 47.972 1.00 65.40 2392 CA LYS 311 91.687 53.926 46.755 1.00 65.81 2393 CB LYS 311 91.121 55.301 47.105 1.00 70.45 2394 CG LYS 311 89.696 55.305 47.621 1.00 74.65 2395 CD LYS 311 89.175 56.734 47.692 1.00 77.16 2396 CE LYS 311 87.719 56.787 48.120 1.00 75.45 2397 NZ LYS 311 87.239 58.194 48.137 1.00 78.70 2398 C LYS 311 92.889 54.116 45.842 1.00 63.97 2399 0 LYS 311 92.840 53.788 44.658 1.00 64.41 2400 N GLU 312 93.961 54.670 46.403 1.00 60.54 2401 CA GLU 312 95.195 54.931 45.665 1.00 57.43 2402 CB GLU 312 96.263 55.516 46.596 1.00 59.85 2403 CG GLU 312 95.900 56.859 47.194 1.00 66.27 2404 CD GLU 312 97.024 57.438 48.033 1.00 69.45 2405 0E1 GLU 312 97.396 56.817 49.051 1.00 71.29 2406 OE2 GLU 312 97.544 58.514 47.666 1.00 70.23 2407 C GLU 312 95.750 53.679 44.989 1.00 53.28 2408 0 GLU 312 96.133 53.715 43.815 1.00 44.50 2409 N LEU 313 95.787 52.577 45.736 1.00 45.10 2410 CA LEU 313 96.290 51.310 45.222 1.00 40.42 2411 CB LEU 313 96.361 50.267 46.343 1.00 35.64 2412 CG LEU 313 97.263 50.614 47.534 1.00 32.14 2413 CD1 LEU 313 97.226 49.501 48.569 1.00 28.15 2414 CD2 LEU 313 98.687 50.861 47.061 1.00 26.11 2415 C LEU 313 95.430 50.800 44.071 1.00 41.37 2416 0 LEU 313 95.950 50.275 43.085 1.00 39.82 2417 N GLU 314 94.116 50.981 44.193 1.00 41.16 2418 CA GLU 314 93.180 50.553 43.156 1.00 41.35 2419 CB GLU 314 91.737 50.728 43.636 1.00 45.36 2420 CG GLU 314 90.674 50.326 42.612 1.00 51.16 2421 CD GLU 314 90.717 48.848 42.251 1.00 56.61 2422 0E1 GLU 314 90.469 48.007 43.144 1.00 55.46 2423 0E2 GLU 314 90.988 48.530 41.071 1.00 49.16 2424 C GLU 314 93.417 51.357 41.880 1.00 38.64 2425 0 GLU 314 93.315 50.828 40.772 1.00 41.77 2426 N ALA 315 93.742 52.634 42.047 1.00 37.56 2427 CA ALA 315 94.012 53.513 40.917 1.00 37.09 2428 CB ALA 315 94.024 54.961 41.375 1.00 41.02 2429 C ALA 315 95.354 53.146 40.292 1.00 37.51 2430 0 ALA 315 95.522 53.222 39.074 1.00 40.72 2431 N TYR 316 96.301 52.741 41.138 1.00 37.47 2432 CA TYR 316 97.641 52.351 40.698 1.00 36.60 2433 CB TYR 316 98.567 52.189 41.908 1.00 42.76 2434 CG TYR 316 100.045 52.214 41.576 1.00 47.70 2435 CD1 TYR 316 100.701 53.421 41.323 1.00 50.35 2436 CE1 TYR 316 102.064 53.456 41.029 1.00 47.09 2437 CD2 TYR 316 100.792 51.038 41.526 1.00 50.58 2438 CE2 TYR 316 102.158 51.063 41.232 1.00 51.96 2439 CZ TYR 316 102.785 52.276 40.986 1.00 46.31 2440 OH TYR 316 104.130 52.308 40.697 1.00 45.69 2441 C TYR 316 97.582 51.047 39.909 1.00 38.30 2442 0 TYR 316 98.142 50.949 38.812 1.00 29.96 2443 N THR 317 96.890 50.058 40.473 1.00 34.49 2444 CA THR 317 96.731 48.752 39.839 1.00 33.58 2445 CB THR 317 95.811 47.831 40.671 1.00 29.35 2446 0G1 THR 317 96.347 47.676 41.990 1.00 30.19 2447 CG2 THR 317 95.691 46.460 40.020 1.00 28.64 2448 C THR 317 96.125 48.922 38.448 1.00 38.84 2449 0 THR 317 96.624 48.363 37.470 1.00 37.70 2450 N ASP 318 95.070 49.731 38.369 1.00 39.63 2451 CA ASP 318 94.385 49.987 37.110 1.00 43.25 2452 CB ASP 318 93.115 50.806 37.351 1.00 53.81 2453 CG ASP 318 92.282 50.972 36.094 1.00 64.26 2454 OD1 ASP 318 91.830 49.947 35.538 1.00 68.93 2455 OD2 ASP 318 92.088 52.126 35.656 1.00 69.91 2456 C ASP 318 95.292 50.706 36.118 1.00 38.89 2457 0 ASP 318 95.280 50.406 34.922 1.00 35.65 2458 N ALA 319 96.081 51.651 36.622 1.00 39.85 2459 CA ALA 319 97.001 52.409 35.783 1.00 39.48 2460 CB ALA 319 97.716 53.462 36.610 1.00 45.21 2461 C ALA 319 98.007 51.469 35.123 1.00 36.47 2462 0 ALA 319 98.261 51.564 33.920 1.00 28.06 2463 N ILE 320 98.547 50.541 35.912 1.00 36.88 2464 CA ILE 320 99.514 49.560 35.422 1.00 35.98 2465 CB ILE 320 99.994 48.620 36.561 1.00 43.40 2466 CG2 ILE 320 100.784 47.443 35.991 1.00 44.99 2467 CG1 ILE 320 100.834 49.397 37.582 1.00 45.58 2468 CD1 ILE 320 102.173 49.891 37.054 1.00 39.26 2469 C ILE 320 98.911 48.712 34.307 1.00 31.85 2470 0 ILE 320 99.544 48.506 33.271 1.00 32.45 2471 N GLN 321 97.680 48.245 34.518 1.00 27.13 2472 CA GLN 321 96.980 47.414 33.538 1.00 29.80 2473 CB GLN 321 95.592 47.021 34.053 1.00 37.41 2474 CG GLN 321 95.581 46.336 35.422 1.00 37.33 2475 CD GLN 321 96.510 45.136 35.508 1.00 42.33 2476 0E1 GLN 321 96.690 44.398 34.536 1.00 43.16 2477 NE2 GLN 321 97.108 44.938 36.679 1.00 35.06 2478 C GLN 321 96.856 48.101 32.180 1.00 30.46 2479 0 GLN 321 97.066 47.474 31.139 1.00 25.13 2480 N ARG 322 96.519 49.390 32.199 1.00 36.61 2481 CA ARG 322 96.384 50.171 30.971 1.00 40.97 2482 CB ARG 322 95.779 51.549 31.264 1.00 48.13 2483 CG ARG 322 94.261 51.612 31.176 1.00 58.29 2484 CD ARG 322 93.581 50.836 32.290 1.00 66.64 2485 NE ARG 322 92.125 50.822 32.134 1.00 76.38 2486 CZ ARG 322 91.326 51.868 32.344 1.00 74.78 2487 NH1 ARG 322 91.827 53.035 32.727 1.00 73.98 2488 NH2 ARG 322 90.019 51.751 32.157 1.00 73.84 2489 C ARG 322 97.737 50.347 30.290 1.00 39.65 2490 0 ARG 322 97.848 50.233 29.067 1.00 46.16 2491 N TRP 323 98.757 50.635 31.094 1.00 37.39 2492 CA TRP 323 100.118 50.828 30.607 1.00 35.58 2493 CB TRP 323 100.663 49.535 29.990 1.00 36.83 2494 CG TRP 323 102.169 49.447 29.979 1.00 41.47 2495 CD2 TRP 323 103.017 49.048 31.063 1.00 38.37 2496 CE2 TRP 323 104.351 49.089 30.594 1.00 38.29 2497 CE3 TRP 323 102.779 48.656 32.390 1.00 36.27 2498 CD1 TRP 323 103.003 49.714 28.922 1.00 40.25 2499 NE1 TRP 323 104.312 49.500 29.286 1.00 39.37 2500 CZ2 TRP 323 105.439 48.753 31.402 1.00 30.80 2501 CZ3 TRP 323 103.863 48.322 33.192 1.00 34.06 2502 CH2 TRP 323 105.178 48.374 32.691 1.00 37.92 2503 C TRP 323 100.182 51.976 29.606 1.00 36.88 2504 0 TRP 323 100.522 51.788 28.437 1.00 30.80 2505 N ASP 324 99.781 53.157 30.066 1.00 48.71 2506 CA ASP 324 99.797 54.366 29.249 1.00 54.17 2507 CB ASP 324 98.462 54.586 28.537 1.00 56.16 2508 CG ASP 324 98.585 55.547 27.366 1.00 58.43 2509 0D1 ASP 324 98.956 56.724 27.575 1.00 59.06 2510 0D2 ASP 324 98.328 55.120 26.222 1.00 57.24 2511 C ASP 324 100.076 55.543 30.165 1.00 57.09 2512 0 ASP 324 99.468 55.671 31.230 1.00 54.89 2513 N ILE 325 100.977 56.414 29.729 1.00 60.16 2514 CA ILE 325 101.377 57.584 30.495 1.00 64.12 2515 CB ILE 325 102.559 58.286 29.788 1.00 67.78 2516 CG2 ILE 325 102.072 59.013 28.542 1.00 68.84 2517 CG1 ILE 325 103.325 59.185 30.768 1.00 71.40 2518 CD1 ILE 325 104.716 59.579 30.273 1.00 78.93 2519 C ILE 325 100.219 58.560 30.760 1.00 62.87 2520 0 ILE 325 100.248 59.325 31.723 1.00 55.53 2521 N ASN 326 99.181 58.489 29.931 1.00 63.16 2522 CA ASN 326 98.008 59.347 30.075 1.00 60.43 2523 CB ASN 326 97.060 59.157 28.891 1.00 58.85 2524 CG ASN 326 97.208 60.240 27.858 1.00 58.26 2525 0D1 ASN 326 97.005 61.420 28.150 1.00 61.96 2526 ND2 ASN 326 97.564 59.854 26.640 1.00 59.50 2527 C ASN 326 97.247 59.093 31.370 1.00 61.39 2528 0 ASN 326 96.561 59.982 31.875 1.00 62.82 2529 N GLU 327 97.378 57.881 31.904 1.00 59.66 2530 CA GLU 327 96.691 57.498 33.136 1.00 62.98 2531 CB GLU 327 96.563 55.973 33.216 1.00 64.39 2532 CG GLU 327 96.087 55.299 31.933 1.00 69.30 2533 CD GLU 327 94.708 55.750 31.491 1.00 70.48 2534 0E1 GLU 327 93.784 55.783 32.335 1.00 72.78 2535 OE2 GLU 327 94.548 56.067 30.291 1.00 63.31 2536 C GLU 327 97.414 58.011 34.380 1.00 62.97 2537 0 GLU 327 96.972 57.771 35.505 1.00 62.71 2538 N ILE 328 98.510 58.734 34.169 1.00 64.24 2539 CA ILE 328 99.316 59.270 35.264 1.00 67.30 2540 CB ILE 328 100.636 59.886 34.729 1.00 69.70 2541 CG2 ILE 328 100.372 61.245 34.069 1.00 69.85 2542 CG1 ILE 328 101.657 60.013 35.863 1.00 72.49 2543 CD1 ILE 328 103.047 60.424 35.409 1.00 71.67 2544 C ILE 328 98.577 60.298 36.122 1.00 66.37 2545 0 ILE 328 98.763 60.349 37.340 1.00 61.63 2546 N ASP 329 97.711 61.082 35.485 1.00 70.35 2547 CA ASP 329 96.950 62.128 36.163 1.00 73.14 2548 CB ASP 329 96.212 62.987 35.134 1.00 73.34 2549 CG ASP 329 97.154 63.620 34.123 1.00 75.99 2550 OD1 ASP 329 97.861 64.584 34.486 1.00 75.75 2551 OD2 ASP 329 97.198 63.140 32.970 1.00 74.82 2552 C ASP 329 95.978 61.611 37.219 1.00 73.26 2553 0 ASP 329 95.637 62.332 38.159 1.00 73.84 2554 N ARG 330 95.539 60.366 37.065 1.00 70.87 2555 CA ARG 330 94.616 59.756 38.019 1.00 70.53 2556 CB ARG 330 93.932 58.535 37.393 1.00 71.49 2557 CG ARG 330 93.145 58.845 36.129 1.00 78.19 2558 CD ARG 330 92.435 57.612 35.591 1.00 85.11 2559 NE ARG 330 91.756 57.889 34.326 1.00 94.74 2560 CZ ARG 330 90.865 57.082 33.754 1.00 98.54 2561 NH1 ARG 330 90.532 55.934 34.331 1.00 100.00 2562 NH2 ARG 330 90.309 57.424 32.599 1.00 94.40 2563 C ARG 330 95.358 59.345 39.291 1.00 67.20 2564 0 ARG 330 94.749 59.145 40.345 1.00 61.95 2565 N LEU 331 96.681 59.252 39.183 1.00 66.11 2566 CA LEU 331 97.539 58.857 40.295 1.00 65.38 2567 CB LEU 331 98.727 58.047 39.768 1.00 70.15 2568 CG LEU 331 98.430 56.802 38.933 1.00 71.98 2569 CD1 LEU 331 99.710 56.289 38.300 1.00 67.56 2570 CD2 LEU 331 97.789 55.739 39.806 1.00 72.35 2571 C LEU 331 98.081 60.056 41.057 1.00 59.96 2572 0 LEU 331 98.432 61.069 40.456 1.00 60.57 2573 N PRO 332 98.145 59.962 42.397 1.00 56.66 2574 CD PRO 332 97.661 58.870 43.257 1.00 52.18 2575 CA PRO 332 98.666 61.070 43.204 1.00 60.33 2576 CB PRO 332 98.458 60.578 44.640 1.00 54.14 2577 CG PRO 332 98.462 59.090 44.507 1.00 53.96 2578 C PRO 332 100.144 61.294 42.871 1.00 65.03 2579 0 PRO 332 100.817 60.386 42.381 1.00 68.68 2580 N ASP 333 100.637 62.500 43.136 1.00 70.86 2581 CA ASP 333 102.021 62.876 42.839 1.00 72.50 2582 CB ASP 333 102.362 64.220 43.489 1.00 76.30 2583 CG ASP 333 101.737 65.396 42.760 1.00 73.02 2584 0D1 ASP 333 101.290 66.343 43.438 1.00 75.36 2585 0D2 ASP 333 101.700 65.378 41.510 1.00 70.83 2586 C ASP 333 103.146 61.873 43.105 1.00 69.45 2587 0 ASP 333 104.019 61.694 42.254 1.00 64.53 2588 N TYR 334 103.139 61.226 44.269 1.00 65.65 2589 CA TYR 334 104.195 60.267 44.590 1.00 64.14 2590 CB TYR 334 104.180 59.900 46.080 1.00 67.04 2591 CG TYR 334 103.162 58.858 46.484 1.00 71.84 2592 CD1 TYR 334 101.827 59.199 46.688 1.00 74.21 2593 CE1 TYR 334 100.895 58.243 47.086 1.00 74.47 2594 CD2 TYR 334 103.542 57.531 46.685 1.00 72.86 2595 CE2 TYR 334 102.620 56.570 47.081 1.00 72.07 2596 CZ TYR 334 101.299 56.932 47.281 1.00 72.74 2597 OH TYR 334 100.386 55.982 47.675 1.00 69.90 2598 C TYR 334 104.143 59.015 43.714 1.00 59.49 2599 0 TYR 334 105.181 58.466 43.341 1.00 58.89 2600 N MET 335 102.933 58.575 43.379 1.00 51.53 2601 CA MET 335 102.762 57.401 42.533 1.00 48.12 2602 CB MET 335 101.340 56.854 42.637 1.00 45.40 2603 CG MET 335 100.979 56.325 44.006 1.00 34.82 2604 SD MET 335 99.387 55.502 44.005 1.00 37.30 2605 CE MET 335 99.776 53.994 44.867 1.00 41.41 2606 C MET 335 103.082 57.727 41.081 1.00 48.13 2607 0 MET 335 103.354 56.826 40.287 1.00 55.57 2608 N LYS 336 103.032 59.013 40.738 1.00 48.65 2609 CA LYS 336 103.332 59.465 39.380 1.00 50.84 2610 CB LYS 336 103.004 60.953 39.213 1.00 55.94 2611 CG LYS 336 101.524 61.301 39.255 1.00 63.40 2612 CD LYS 336 101.298 62.758 38.857 1.00 63.31 2613 CE LYS 336 99.820 63.092 38.764 1.00 60.22 2614 NZ LYS 336 99.580 64.473 38.271 1.00 62.57 2615 C LYS 336 104.810 59.237 39.080 1.00 51.33 2616 0 LYS 336 105.187 58.938 37.943 1.00 47.74 2617 N ILE 337 105.638 59.382 40.114 1.00 45.10 2618 CA ILE 337 107.079 59.195 39.996 1.00 46.36 2619 CB ILE 337 107.805 59.607 41.297 1.00 48.91 2620 CG2 ILE 337 109.309 59.641 41.067 1.00 50.47 2621 CG1 ILE 337 107.330 60.986 41.759 1.00 50.88 2622 CD1 ILE 337 107.888 61.407 43.105 1.00 47.89 2623 C ILE 337 107.380 57.725 39.712 1.00 47.32 2624 0 ILE 337 108.140 57.402 38.795 1.00 52.27 2625 N SER 338 106.755 56.844 40.491 1.00 42.57 2626 CA SER 338 106.928 55.401 40.351 1.00 32.89 2627 CB SER 338 106.120 54.663 41.424 1.00 29.02 2628 OG SER 338 106.339 55.198 42.718 1.00 33.47 2629 C SER 338 106.465 54.933 38.975 1.00 31.60 2630 0 SER 338 107.214 54.287 38.243 1.00 27.59 2631 N TYR 339 105.239 55.311 38.621 1.00 33.89 2632 CA TYR 339 104.622 54.932 37.353 1.00 39.75 2633 CB TYR 339 103.204 55.508 37.265 1.00 42.11 2634 CG TYR 339 102.367 54.908 36.157 1.00 46.50 2635 CD1 TYR 339 101.682 53.709 36.348 1.00 48.25 2636 CE1 TYR 339 100.924 53.144 35.327 1.00 52.79 2637 CD2 TYR 339 102.270 55.530 34.915 1.00 42.98 2638 CE2 TYR 339 101.515 54.976 33.890 1.00 51.56 2639 CZ TYR 339 100.845 53.784 34.100 1.00 54.29 2640 OH TYR 339 100.100 53.236 33.080 1.00 56.73 2641 C TYR 339 105.414 55.309 36.101 1.00 43.13 2642 0 TYR 339 105.531 54.502 35.174 1.00 41.07 2643 N LYS 340 105.941 56.531 36.064 1.00 49.11 2644 CA LYS 340 106.706 56.989 34.903 1.00 49.74 2645 CB LYS 340 106.894 58.508 34.934 1.00 58.08 2646 CG LYS 340 107.553 59.059 33.674 1.00 64.41 2647 CD LYS 340 107.642 60.573 33.694 1.00 69.77 2648 CE LYS 340 108.246 61.097 32.403 1.00 73.44 2649 NZ LYS 340 108.256 62.584 32.365 1.00 82.14 2650 C LYS 340 108.062 56.297 34.800 1.00 44.71 2651 0 LYS 340 108.506 55.938 33.703 1.00 34.93 2652 N ALA 341 108.712 56.114 35.948 1.00 36.45 2653 CA ALA 341 110.013 55.456 36.003 1.00 36.97 2654 CB ALA 341 110.517 55.415 37.439 1.00 35.42 2655 C ALA 341 109.897 54.041 35.444 1.00 35.71 2656 0 ALA 341 110.791 53.561 34.746 1.00 34.74 2657 N ILE 342 108.766 53.399 35.734 1.00 29.99 2658 CA ILE 342 108.487 52.041 35.283 1.00 21.08 2659 CB ILE 342 107.231 51.472 35.982 1.00 16.81 2660 CG2 ILE 342 106.786 50.171 35.309 1.00 10.96 2661 CG1 ILE 342 107.523 51.275 37.476 1.00 10.78 2662 CD1 I ILLEE 342 106.333 50.884 38.324 1.00 2.00 2663 C I ILLEE 342 108.336 51.939 33.771 1.00 28.67 2664 0 I ILLEE 342 108.949 51.071 33.150 1.00 32.50 2665 N L LEEUU 343 107.530 52.821 33.180 1.00 33.81 2666 CA L LEEUU 343 107.320 52.809 31.732 1.00 37.97 2667 CB L LEEUU 343 106.208 53.774 31.317 1.00 41.50 2668 CG L LEEUU 343 104.822 53.594 31.932 1.00 46.77 2669 CD1 L LEEUU 343 103.831 54.537 31.267 1.00 48.11 2670 CD2 LEU 343 104.375 52.165 31.759 1.00 43.32 2671 C LEU 343 108.596 53.177 30.995 1.00 41.41 2672 0 L LEEUU 343 108.880 52.626 29.932 1.00 43.16 2673 N AASSPP 344 109.348 54.126 31.552 1.00 45.08 2674 CA AASSPP 344 110.601 54.563 30.942 1.00 51.08 2675 CB AASSPP 344 111.144 55.820 31.628 1.00 57.96 2676 CG AASSPP 344 110.754 57.098 30.903 1.00 64.16 2677 0D1 AASSPP 344 110.680 57.090 29.654 1.00 69.36 2678 OD2 ASP 344 110.526 58.117 31.588 1.00 65.04 2679 C ASP 344 111.643 53.461 30.980 1.00 50.69 2680 0 A ASSPP 344 112.415 53.301 30.034 1.00 53.80 2681 N LLEEUU 345 111.661 52.709 32.078 1.00 47.98 2682 CA LLEEUU 345 112.594 51.599 32.242 1.00 43.23 2683 CB LLEEUU 345 112.384 50.925 33.599 1.00 45.16 2684 CG LLEEUU 345 113.317 49.773 33.977 1.00 44.62 2685 CD1 LLEEUU 345 114.752 50.267 34.070 1.00 45.63 2686 CD2 LLEEUU 345 112.875 49.186 35.307 1.00 42.33 2687 C LLEEUU 345 112.364 50.585 31.129 1.00 42.19 2688 0 LLEEUU 345 113.315 50.068 30.541 1.00 47.47 2689 N T TYYRR 346 111.094 50.311 30.844 1.00 38.09 2690 CA TTYYRR 346 110.731 49.372 29.793 1.00 36.61 2691 CB TTYYRR 346 109.298 48.878 29.983 1.00 32.28 2692 CG TTYYRR 346 109.211 47.802 31.038 1.00 30.73 2693 CD1 TTYYRR 346 108.903 48.110 32.361 1.00 22.11 2694 CE1 TYR 346 108.895 47.122 33.346 1.00 24.69 2695 CD2 TYR 346 109.503 46.477 30.722 1.00 35.15 2696 CE2 TYR 346 109.499 45.484 31.694 1.00 26.34 2697 CZ TYR 346 109.198 45.809 33.000 1.00 27.54 2698 OH TYR 346 109.224 44.812 33.948 1.00 22.51 2699 C TYR 346 110.954 49.953 28.403 1.00 39.45 2700 0 TYR 346 111.086 49.213 27.429 1.00 37.79 2701 N LYS 347 110.995 51.281 28.320 1.00 44.42 2702 CA LYS 347 111.256 51.958 27.056 1.00 45.72 2703 CB LYS 347 110.797 53.418 27.105 1.00 49.09 2704 CG LYS 347 109.313 53.604 26.824 1.00 54.73 2705 CD LYS 347 108.959 53.084 25.433 1.00 58.88 2706 CE LYS 347 107.471 53.195 25.149 1.00 58.70 2707 NZ LYS 347 107.129 52.632 23.816 1.00 45.34 2708 C LYS 347 112.756 51.874 26.810 1.00 44.56 2709 0 LYS 347 113.201 51.803 25.666 1.00 44.20 2710 N ASP 348 113.524 51.865 27.901 1.00 45.25 2711 CA ASP 348 114.977 51.748 27.829 1.00 43.43 2712 CB ASP 348 115.630 52.041 29.188 1.00 41.08 2713 CG ASP 348 115.545 53.509 29.584 1.00 45.56 2714 OD1 ASP 348 115.741 54.388 28.716 1.00 50.29 2715 OD2 ASP 348 115.293 53.787 30.775 1.00 46.84 2716 C ASP 348 115.308 50.325 27.394 1.00 44.57 2717 0 ASP 348 116.186 50.116 26.555 1.00 45.03 2718 N TYR 349 114.585 49.355 27.959 1.00 43.55 2719 CA TYR 349 114.773 47.943 27.627 1.00 42.30 2720 CB TYR 349 113.813 47.054 28.429 1.00 41.29 2721 CG TYR 349 114.128 46.916 29.906 1.00 37.24 2722 CD1 TYR 349 113.181 46.393 30.785 1.00 30.06 2723 CE1 TYR 349 113.458 46.247 32.142 1.00 36.46 2724 CD2 TYR 349 115.368 47.293 30.424 1.00 41.76 2725 CE2 TYR 349 115.656 47.151 31.783 1.00 40.50 2726 CZ TYR 349 114.694 46.627 32.633 1.00 36.99 2727 OH TYR 349 114.960 46.491 33.975 1.00 36.59 2728 C TYR 349 114.520 47.741 26.139 1.00 42.51 2729 0 TYR 349 115.308 47.094 25.446 1.00 42.03 2730 N GLU 350 113.411 48.296 25.656 1.00 44.24 2731 CA GLU 350 113.053 48.199 24.244 1.00 46.89 2732 CB GLU 350 111.734 48.929 23.969 1.00 49.81 2733 CG GLU 350 110.509 48.270 24.589 1.00 54.69 2734 CD GLU 350 109.214 49.033 24.347 1.00 58.54 2735 0E1 GLU 350 108.144 48.491 24.695 1.00 62.24 2736 0E2 GLU 350 109.253 50.168 23.822 1.00 64.71 2737 C GLU 350 114.162 48.811 23.397 1.00 48.29 2738 0 GLU 350 114.491 48.294 22.334 1.00 45.94 2739 N LYS 351 114.763 49.884 23.909 1.00 53.89 2740 CA LYS 351 115.841 50.591 23.222 1.00 58.14 2741 CB LYS 351 116.053 51.971 23.855 1.00 63.43 2742 CG LYS 351 116.916 52.921 23.031 1.00 71.72 2743 CD LYS 351 116.247 53.286 21.711 1.00 77.97 2744 CE LYS 351 1 17.122 54.218 20.885 1.00 83.68 2745 NZ LYS 351 116.483 54.588 19.591 1.00 83.73 2746 C LYS 351 1 17.155 49.795 23.215 1.00 57.54 2747 0 LYS 351 1 17.873 49.784 22.209 1.00 56.27 2748 N GLU 352 117.465 49.142 24.336 1.00 56.46 2749 CA GLU 352 1 18.684 48.334 24.458 1.00 52.60 2750 CB GLU 352 118.847 47.801 25.890 1.00 50.25 2751 CG GLU 352 119.239 48.828 26.943 1.00 58.10 2752 CD GLU 352 119.464 48.194 28.311 1.00 59.00 2753 0E1 GLU 352 118.655 48.447 29.232 1.00 57.55 2754 0E2 GLU 352 120.447 47.435 28.468 1.00 53.94 2755 C GLU 352 118.645 47.140 23.508 1.00 49.57 2756 0 GLU 352 119.671 46.735 22.957 1.00 45.55 2757 N LEU 353 117.448 46.587 23.327 1.00 44.88 2758 CA LEU 353 117.239 45.432 22.463 1.00 44.80 2759 CB LEU 353 116.116 44.561 23.034 1.00 35.61 2760 CG LEU 353 116.304 44.125 24.489 1.00 30.68 2761 CD1 LEU 353 115.030 43.507 25.030 1.00 31.93 2762 CD2 LEU 353 117.468 43.156 24.597 1.00 32.93 2763 C LEU 353 116.937 45.806 21.011 1.00 48.25 2764 0 LEU 353 116.878 44.933 20.140 1.00 48.95 2765 N SER 354 116.756 47.101 20.751 1.00 54.12 2766 CA SER 354 116.468 47.595 19.403 1.00 58.83 2767 CB SER 354 116.356 49.122 19.395 1.00 64.47 2768 OG SER 354 115.196 49.571 20.072 1.00 73.04 2769 C SER 354 117.534 47.171 18.400 1.00 58.85 2770 0 SER 354 117.226 46.900 17.237 1.00 60.25 2771 N SER 355 118.784 47.119 18.857 1.00 59.55 2772 CA SER 355 119.918 46.731 18.022 1.00 60.93 2773 CB SER 355 121.219 46.840 18.823 1.00 58.82 2774 OG SER 355 122.333 46.392 18.071 1.00 61.05 2775 C SER 355 119.772 45.316 17.455 1.00 67.50 2776 0 SER 355 119.753 45.125 16.239 1.00 72.60 2777 N ALA 356 119.640 44.338 18.345 1.00 68.57 2778 CA ALA 356 119.501 42.943 17.946 1.00 67.55 2779 CB ALA 356 119.690 42.040 19.152 1.00 63.74 2780 C ALA 356 118.163 42.642 17.278 1.00 69.18 2781 0 ALA 356 118.071 41.754 16.434 1.00 70.23 2782 N GLY 357 117.131 43.385 17.661 1.00 69.13 2783 CA GLY 357 115.811 43.152 17.102 1.00 62.21 2784 C GLY 357 115.027 42.258 18.039 1.00 59.93 2785 0 GLY 357 114.203 41.443 17.604 1.00 60.71 2786 N ARG 358 115.322 42.391 19.332 1.00 54.34 2787 CA ARG 358 114.669 41.616 20.385 1.00 52.71 2788 CB ARG 358 115.713 40.882 21.231 1.00 45.26 2789 CG ARG 358 116.561 39.896 20.442 1.00 47.78 2790 CD ARG 358 117.644 39.275 21.309 1.00 47.12 2791 NE ARG 358 117.083 38.456 22.383 1.00 44.42 2792 CZ ARG 358 117.206 38.724 23.681 1.00 39.46 2793 NH1 ARG 358 117.871 39.797 24.083 1.00 37.90 2794 NH2 ARG 358 116.684 37.905 24.583 1.00 43.78 2795 C ARG 358 113.817 42.522 21.282 1.00 55.62 2796 0 ARG 358 113.676 42.268 22.479 1.00 60.74 2797 N SER 359 113.286 43.596 20.699 1.00 54.17 2798 CA SER 359 112.440 44.548 21.419 1.00 49.75 2799 CB SER 359 112.373 45.887 20.671 1.00 46.10 2800 OG SER 359 113.659 46.424 20.441 1.00 39.24 2801 C SER 359 111.030 43.979 21.584 1.00 51.35 2802 0 SER 359 110.321 44.294 22.549 1.00 51.03 2803 N HIS 360 110.642 43.145 20.619 1.00 48.18 2804 CA HIS 360 109.339 42.484 20.566 1.00 49.55 2805 CB HIS 360 109.165 41.769 19.214 1.00 55.45 2806 CG HIS 360 110.191 40.706 18.955 1.00 57.94 2807 CD2 HIS 360 111.485 40.791 18.565 1.00 58.70 2808 ND1 HIS 360 109.933 39.363 19.134 1.00 62.62 2809 CE1 HIS 360 111.028 38.668 18.875 1.00 63.83 2810 NE2 HIS 360 111.985 39.511 18.527 1.00 63.77 2811 C HIS 360 109.105 41.483 21.705 1.00 51.67 2812 0 HIS 360 108.023 40.886 21.795 1.00 56.00 2813 N ILE 361 110.115 41.294 22.552 1.00 44.35 2814 CA ILE 361 110.005 40.352 23.659 1.00 40.02 2815 CB ILE 361 111.217 39.396 23.719 1.00 40.34 2816 CG2 ILE 361 111.350 38.631 22.412 1.00 38.81 2817 CG1 ILE 361 112.490 40.174 24.052 1.00 45.99 2818 CD1 ILE 361 113.742 39.324 24.096 1.00 38.31 2819 C ILE 361 109.837 41.012 25.022 1.00 38.58 2820 0 ILE 361 109.629 40.323 26.018 1.00 46.53 2821 N VAL 362 109.920 42.339 25.068 1.00 34.37 2822 CA VAL 362 109.784 43.073 26.323 1.00 36.05 2823 CB VAL 362 110.133 44.567 26.131 1.00 44.38 2824 CG1 VAL 362 110.157 45.290 27.474 1.00 28.09 2825 CG2 VAL 362 111.470 44.705 25.420 1.00 50.90 2826 C VAL 362 108.372 42.959 26.899 1.00 35.07 2827 0 VAL 362 08.187 43.012 28.113 1.00 27.77 2828 N CYS 363 107.383 42.770 26.025 1.00 37.13 2829 CA CYS 363 105.980 42.653 26.437 1.00 34.16 2830 CB CYS 363 105.066 42.483 25.215 1.00 29.73 2831 SG CYS 363 105.447 41.051 24.179 1.00 41.96 2832 C CYS 363 105.730 41.520 27.434 1.00 32.61 2833 0 CYS 363 104.887 41.646 28.325 1.00 25.38 2834 N HIS 364 106.481 40.429 27.292 1.00 28.31 2835 CA HIS 364 106.356 39.267 28.168 1.00 20.38 2836 CB HIS 364 107.304 38.159 27.713 1.00 19.91 2837 CG HIS 364 107.064 37.696 26.309 1.00 25.64 2838 CD2 HIS 364 107.777 37.887 25.173 1.00 29.90 2839 ND1 HIS 364 105.976 36.929 25.954 1.00 34.65 2840 CE1 HIS 364 106.028 36.667 24.659 1.00 33.79 2841 NE2 HIS 364 107.111 37.237 24.162 1.00 27.05 2842 C HIS 364 106.646 39.635 29.622 1.00 28.17 2843 0 HIS 364 105.942 39.200 30.537 1.00 27.54 2844 N ALA 365 107.685 40.440 29.826 1.00 30.22 2845 CA ALA 365 108.067 40.880 31.163 1.00 30.86 2846 CB ALA 365 109.427 41.574 31.120 1.00 34.60 2847 C ALA 365 107.007 41.822 31.725 1.00 31.03 2848 0 ALA 365 106.752 41.838 32.931 1.00 31.19 2849 N ILE 366 106.389 42.596 30.835 1.00 36.30 2850 CA ILE 366 105.347 43.550 31.208 1.00 36.55 2851 CB ILE 366 105.016 44.504 30.034 1.00 41.23 2852 CG2 ILE 366 103.857 45.419 30.403 1.00 40.62 2853 CG1 ILE 366 106.253 45.331 29.668 1.00 35.62 2854 CD1 ILE 366 106.065 46.231 28.468 1.00 29.32 2855 C ILE 366 104.070 42.845 31.667 1.00 30.85 2856 0 ILE 366 103.524 43.173 32.722 1.00 28.50 2857 N GLU 367 103.613 41.867 30.886 1.00 25.21 2858 CA GLU 367 102.404 41.117 31.223 1.00 22.77 2859 CB GLU 367 102.095 40.069 30.153 1.00 32.06 2860 CG GLU 367 101.926 40.626 28.736 1.00 41.69 2861 CD GLU 367 100.870 41.721 28.629 1.00 48.62 2862 OE1 GLU 367 99.829 41.633 29.321 1.00 48.68 2863 OE2 GLU 367 101.083 42.670 27.841 1.00 43.16 2864 C GLU 367 102.539 40.448 32.585 1.00 20.02 2865 0 GLU 367 101.555 40.297 33.314 1.00 20.91 2866 N ARG 368 103.766 40.057 32.923 1.00 21.53 2867 CA ARG 368 104.055 39.422 34.205 1.00 14.50 2868 CB ARG 368 105.406 38.709 34.159 1.00 17.59 2869 CG ARG 368 105.427 37.442 33.319 1.00 13.40 2870 CD ARG 368 104.602 36.338 33.960 1.00 17.58 2871 NE ARG 368 104.843 35.044 33.325 1.00 25.37 2872 CZ ARG 368 104.380 33.884 33.784 1.00 29.88 2873 NH1 ARG 368 103.641 33.847 34.887 1.00 15.72 2874 NH2 ARG 368 104.669 32.757 33.146 1.00 25.60 2875 C ARG 368 104.058 40.473 35.306 1.00 22.28 2876 0 ARG 368 103.674 40.193 36.444 1.00 25.28 2877 N MET 369 104.489 41.686 34.965 1.00 23.23 2878 CA MET 369 104.513 42.774 35.933 1.00 22.69 2879 CB MET 369 105.234 44.001 35.371 1.00 21.94 2880 CG MET 369 105.216 45.178 36.332 1.00 33.04 2881 SD MET 369 106.226 46.580 35.855 1.00 30.05 2882 CE MET 369 106.788 47.105 37.492 1.00 22.46 2883 C MET 369 103.088 43.138 36.329 1.00 21.30 2884 0 MET 369 102.794 43.316 37.513 1.00 25.30 2885 N LYS 370 102.207 43.230 35.332 1.00 22.42 2886 CA LYS 370 100.798 43.555 35.562 1.00 21.17 2887 CB LYS 370 100.033 43.596 34.237 1.00 18.37 2888 CG LYS 370 100.498 44.679 33.272 1.00 19.38 2889 CD LYS 370 99.724 44.628 31.959 1.00 22.90 2890 CE LYS 370 100.144 45.754 31.026 1.00 25.30 2891 NZ LYS 370 99.370 45.760 29.753 1.00 26.14 2892 C LYS 370 100.184 42.503 36.480 1.00 22.60 2893 0 LYS 370 99.433 42.830 37.404 1.00 22.82 2894 N GLU 371 100.540 41.243 36.233 1.00 20.87 2895 CA GLU 371 100.060 40.117 37.027 1.00 17.91 2896 CB GLU 371 100.633 38.805 36.473 1.00 17.04 2897 CG GLU 371 100.291 37.558 37.281 1.00 14.89 2898 CD GLU 371 100.951 36.307 36.737 1.00 33.96 2899 OE1 GLU 371 100.246 35.281 36.624 1.00 49.48 2900 OE2 GLU 371 102.162 36.342 36.433 1.00 39.35 2901 C GLU 371 100.459 40.291 38.491 1.00 14.70 2902 0 GLU 371 99.629 40.146 39.389 1.00 15.00 2903 N VAL 372 101.727 40.624 38.718 1.00 16.52 2904 CA VAL 372 102.246 40.830 40.066 1.00 17.45 2905 CB VAL 372 103.747 41.232 40.043 1.00 17.58 2906 CG1 VAL 372 104.258 41.453 41.450 1.00 3.56 2907 CG2 VAL 372 104.575 40.156 39.365 1.00 18.80 2908 C C V VAALL 372 101.455 41.919 40.782 1.00 21.27 2909 O 0 VVAALL 372 101.101 41.767 41.952 1.00 23.46 2910 N VVAALL 373 101.155 43.000 40.063 1.00 26.12 2911 CA VVAALL 373 100.407 44.123 40.629 1.00 29.37 2912 CB VVAALL 373 100.425 45.356 39.694 1.00 33.84 2913 CG1 VVAALL 373 99.736 46.537 40.366 1.00 27.54 2914 CG2 VAL 373 101.861 45.724 39.335 1.00 29.76 2915 C VAL 373 98.962 43.754 40.969 1.00 29.64 2916 0 V VAALL 373 98.462 44.135 42.030 1.00 27.43 2917 N AARRGG 374 98.298 43.015 40.078 1.00 27.06 2918 CA AARRGG 374 96.916 42.587 40.315 1.00 22.92 2919 CB AARRGG 374 96.438 41.626 39.225 1.00 20.10 2920 CG AARRGG 374 96.101 42.257 37.897 1.00 18.80 2921 CD AARRGG 374 95.627 41.191 36.924 1.00 11.40 2922 NE AARRGG 374 96.410 41.194 35.692 1.00 20.17 2923 CZ AARRGG 374 96.956 40.112 35.146 1.00 19.94 2924 NH1 AARRGG 374 96.810 38.924 35.720 1.00 26.31 2925 NH2 ARG 374 97.655 40.218 34.025 1.00 24.45 2926 C ARG 374 96.835 41.858 41.646 1.00 26.89 2927 0 A ARRGG 374 95.964 42.134 42.472 1.00 32.47 2928 N AASSNN 375 97.766 40.931 41.842 1.00 27.68 2929 CA AASSNN 375 97.827 40.133 43.055 1.00 25.57 2930 CB AASSNN 375 98.776 38.955 42.850 1.00 30.36 2931 CG AASSNN 375 98.299 38.009 41.756 1.00 32.94 2932 0D1 AASSNN 375 97.594 38.415 40.827 1.00 25.76 2933 ND2 AASSNN 375 98.677 36.741 41.865 1.00 30.37 2934 C AASSNN 375 98.213 40.958 44.279 1.00 26.96 2935 0 AASSNN 375 97.819 40.632 45.399 1.00 21.31 2936 N T TYYRR 376 98.980 42.026 44.062 1.00 33.99 2937 CA TTYYRR 376 99.381 42.920 45.148 1.00 33.87 2938 CB TTYYRR 376 100.362 43.986 44.645 1.00 39.17 2939 CG TTYYRR 376 101.823 43.579 44.628 1.00 42.30 2940 CD1 TTYYRR 376 102.765 44.344 43.940 1.00 40.53 2941 CE1 TTYYRR 376 104.111 43.997 43.934 1.00 45.46 2942 CD2 TTYYRR 376 102.268 42.446 45.312 1.00 43.05 2943 CE2 TTYYRR 376 103.614 42.088 45.313 1.00 42.63 2944 CZ TYR 376 104.531 42.868 44.623 1.00 48.37 2945 OH TYR 376 105.865 42.523 44.621 1.00 39.23 2946 C TYR 376 98.122 43.605 45.668 1.00 29.88 2947 0 TYR 376 97.942 43.773 46.874 1.00 27.89 2948 N ASN 377 97.252 43.984 44.733 1.00 29.64 2949 CA ASN 377 95.987 44.642 45.043 1.00 31.75 2950 CB ASN 377 95.304 45.094 43.748 1.00 34.90 2951 CG ASN 377 94.116 45.999 43.999 1.00 40.49 2952 OD1 ASN 377 92.992 45.532 44.178 1.00 42.59 2953 ND2 ASN 377 94.360 47.303 44.011 1.00 34.81 2954 C ASN 377 95.084 43.674 45.804 1.00 28.41 2955 0 ASN 377 94.538 44.015 46.857 1.00 30.58 2956 N VAL 378 94.952 42.460 45.274 1.00 17.90 2957 CA VAL 378 94.131 41.426 45.900 1.00 17.33 2958 CB VAL 378 94.186 40.112 45.086 1.00 10.51 2959 CG1 VAL 378 93.423 39.012 45.789 1.00 11.35 2960 CG2 VAL 378 93.612 40.332 43.698 1.00 13.48 2961 C VAL 378 94.616 41.163 47.327 1.00 25.35 2962 0 VAL 378 93.813 40.997 48.248 1.00 27.43 2963 N GLU 379 95.936 41.176 47.497 1.00 31.20 2964 CA GLU 379 96.575 40.938 48.787 1.00 33.04 2965 CB GLU 379 98.100 40.924 48.613 1.00 40.56 2966 CG GLU 379 98.888 40.454 49.836 1.00 52.37 2967 CD GLU 379 100.392 40.399 49.591 1.00 57.31 2968 0E1 GLU 379 101.158 40.762 50.510 1.00 59.83 2969 0E2 GLU 379 100.810 39.986 48.485 1.00 55.53 2970 C GLU 379 96.166 41.984 49.825 1.00 31.53 2971 0 GLU 379 95.922 41.650 50.987 1.00 29.16 2972 N SER 380 96.092 43.245 49.402 1.00 32.96 2973 CA SER 380 95.706 44.331 50.300 1.00 37.42 2974 CB SER 380 96.066 45.695 49.698 1.00 38.70 2975 OG SER 380 95.348 45.945 48.504 1.00 49.17 2976 C SER 380 94.212 44.264 50.604 1.00 38.16 2977 0 SER 380 93.789 44.512 51.737 1.00 31.46 2978 N THR 381 93.424 43.915 49.587 1.00 36.08 2979 CA THR 381 91.976 43.790 49.729 1.00 27.53 2980 CB THR 381 91.320 43.333 48.413 1.00 22.85 2981 0G1 THR 381 91.706 44.212 47.350 1.00 16.53 2982 CG2 THR 381 89.812 43.351 48.543 1.00 23.91 2983 C THR 381 91.662 42.762 50.814 1.00 27.68 2984 0 THR 381 90.813 42.996 51.670 1.00 29.54 2985 N TRP 382 92.375 41.637 50.779 1.00 28.31 2986 CA TRP 382 92.199 40.563 51.755 1.00 28.12 2987 CB TRP 382 93.063 39.353 51.386 1.00 36.50 2988 CG TRP 382 92.583 38.570 50.195 1.00 38.50 2989 CD2 TRP 382 93.258 37.475 49.565 1.00 42.33 2990 CE2 TRP 382 92.430 37.022 48.516 1.00 44.37 2991 CE3 TRP 382 94.483 36.830 49.787 1.00 47.90 2992 CD1 TRP 382 91.408 38.735 49.518 1.00 36.49 2993 NE1 TRP 382 91.308 37.808 48.511 1.00 36.31 2994 CZ2 TRP 382 92.787 35.951 47.688 1.00 51.17 2995 CZ3 TRP 382 94.838 35.764 48.963 1.00 43.35 2996 CH2 TRP 382 93.991 35.337 47.927 1.00 45.79 2997 C TRP 382 92.567 41.030 53.157 1.00 30.09 2998 0 TRP 382 91.926 40.651 54.137 1.00 31.61 2999 N PHE 383 93.617 41.841 53.240 1.00 36.62 3000 CA PHE 383 94.092 42.378 54.510 1.00 38.24 3001 CB PHE 383 95.411 43.138 54.298 1.00 36.46 3002 CG PHE 383 95.885 43.880 55.516 1.00 32.91 3003 CD1 PHE 383 96.157 43.202 56.701 1.00 32.24 3004 CD2 PHE 383 96.020 45.264 55.490 1.00 33.47 3005 CE1 PHE 383 96.553 43.892 57.843 1.00 34.44 3006 CE2 PHE 383 96.415 45.963 56.628 1.00 34.81 3007 CZ PHE 383 96.681 45.275 57.807 1.00 35.83 3008 C PHE 383 93.045 43.296 55.144 1.00 38.45 3009 0 PHE 383 92.793 43.223 56.351 1.00 36.37 3010 N ILE 384 92.436 44.144 54.315 1.00 36.46 3011 CA ILE 384 91.410 45.091 54.756 1.00 34.56 3012 CB ILE 384 91.025 46.062 53.615 1.00 27.26 3013 CG2 ILE 384 89.917 46.996 54.066 1.00 33.92 3014 CG1 ILE 384 92.249 46.870 53.171 1.00 30.39 3015 CD1 ILE 384 92.881 47.691 54.278 1.00 31.10 3016 C ILE 384 90.145 44.391 55.255 1.00 34.50 3017 0 ILE 384 89.634 44.702 56.333 1.00 36.61 3018 N GLU 385 89.643 43.453 54.460 1.00 26.50 3019 CA GLU 385 88.443 42.703 54.811 1.00 26.95 3020 CB GLU 385 87.937 41.926 53.595 1.00 21.63 3021 CG GLU 385 87.650 42.790 52.375 1.00 29.50 3022 CD GLU 385 87.418 41.976 51.115 1.00 38.78 3023 0E1 GLU 385 87.706 40.758 51.124 1.00 42.45 3024 0E2 GLU 385 86.955 42.560 50.110 1.00 36.35 3025 C GLU 385 88.711 41.732 55.954 1.00 32.21 3026 0 GLU 385 87.778 41.289 56.629 1.00 43.97 3027 N GLY 386 89.985 41.419 56.184 1.00 30.98 3028 CA GLY 386 90.341 40.486 57.238 1.00 29.71 3029 C GLY 386 90.069 39.071 56.767 1.00 29.59 3030 0 GLY 386 89.738 38.178 57.557 1.00 27.61 3031 N TYR 387 90.238 38.877 55.461 1.00 23.79 3032 CA TYR 387 89.999 37.595 54.816 1.00 27.24 3033 CB TYR 387 89.744 37.802 53.319 1.00 29.04 3034 CG TYR 387 89.248 36.570 52.580 1.00 23.98 3035 CD1 TYR 387 88.361 35.675 53.179 1.00 22.30 3036 CE1 TYR 387 87.891 34.552 52.493 1.00 29.04 3037 CD2 TYR 387 89.657 36.311 51.271 1.00 26.35 3038 CE2 TYR 387 89.192 35.194 50.575 1.00 24.90 3039 CZ TYR 387 88.311 34.320 51.191 1.00 29.66 3040 OH TYR 387 87.848 33.218 50.510 1.00 26.42 3041 C TYR 387 91.127 36.591 55.014 1.00 30.82 3042 0 TYR 387 92.311 36.917 54.874 1.00 39.13 3043 N THR 388 90.721 35.375 55.364 1.00 37.65 3044 CA THR 388 91.623 34.247 55.568 1.00 31.40 3045 CB THR 388 91.576 33.728 57.025 1.00 33.01 3046 0G1 THR 388 92.090 34.729 57.911 1.00 35.43 3047 CG2 THR 388 92.416 32.462 57.179 1.00 38.16 3048 C THR 388 91.140 33.148 54.609 1.00 31.72 3049 0 THR 388 90.343 32.282 54.981 1.00 39.68 3050 N PRO 389 91.581 33.203 53.335 1.00 25.34 3051 CD PRO 389 92.494 34.204 52.755 1.00 23.99 3052 CA PRO 389 91.190 32.214 52.323 1.00 26.01 3053 CB PRO 389 91.717 32.829 51.030 1.00 21.95 3054 CG PRO 389 92.953 33.531 51.475 1.00 17.85 3055 C PRO 389 91.779 30.825 52.537 1.00 30.44 3056 0 PRO 389 92.711 30.651 53.324 1.00 28.62 3057 N PRO 390 91.177 29.805 51.909 1.00 32.36 3058 CD PRO 390 89.921 29.814 51.135 1.00 26.81 3059 CA PRO 390 91.691 28.442 52.047 1.00 33.56 3060 CB PRO 390 90.600 27.601 51.379 1.00 32.56 3061 CG PRO 390 90.024 28.532 50.356 1.00 23.42 3062 C PRO 390 93.016 28.383 51.277 1.00 34.49 3063 0 PRO 390 93.222 29.160 50.335 1.00 30.76 3064 N VAL 391 93.920 27.494 51.689 1.00 29.65 3065 CA VAL 391 95.230 27.360 51.046 1.00 25.79 3066 CB VAL 391 95.943 26.061 51.479 1.00 23.80 3067 CG1 VAL 391 97.314 25.969 50.831 1.00 20.24 3068 CG2 VAL 391 96.078 26.017 52.981 1.00 16.75 3069 C VAL 391 95.155 27.393 49.523 1.00 25.32 3070 0 VAL 391 95.944 28.075 48.868 1.00 27.66 3071 N SER 392 94.178 26.683 48.970 1.00 25.00 3072 CA SER 392 93.993 26.621 47.527 1.00 25.90 3073 CB SER 392 92.727 25.827 47.194 1.00 26.67 3074 OG SER 392 92.570 25.684 45.794 1.00 47.32 3075 C SER 392 93.911 28.015 46.918 1.00 18.85 3076 0 SER 392 94.671 28.350 46.011 1.00 19.28 3077 N GLU 393 93.013 28.837 47.450 1.00 16.74 3078 CA GLU 393 92.827 30.191 46.949 1.00 24.04 3079 CB GLU 393 91.579 30.821 47.565 1.00 27.67 3080 CG GLU 393 91.105 32.067 46.831 1.00 20.67 3081 CD GLU 393 90.095 32.873 47.618 1.00 19.63 3082 0E1 GLU 393 89.550 32.362 48.619 1.00 20.04 3083 0E2 GLU 393 89.853 34.032 47.232 1.00 26.17 3084 C GLU 393 94.044 31.071 47.226 1.00 27.53 3085 0 GLU 393 94.474 31.837 46.361 1.00 22.89 3086 N TYR 394 94.590 30.960 48.435 1.00 26.05 3087 CA TYR 394 95.762 31.736 48.829 1.00 26.22 3088 CB TYR 394 96.252 31.293 50.211 1.00 32.15 3089 CG TYR 394 97.597 31.868 50.595 1.00 37.24 3090 CD1 TYR 394 97.739 33.224 50.890 1.00 37.33 3091 CE1 TYR 394 98.980 33.762 51.214 1.00 33.89 3092 CD2 TYR 394 98.733 31.061 50.639 1.00 35.64 3093 CE2 TYR 394 99.979 31.590 50.961 1.00 31.95 3094 CZ TYR 394 100.095 32.941 51.248 1.00 34.89 3095 OH TYR 394 101.324 33.471 51.562 1.00 35.44 3096 C TYR 394 96.900 31.615 47.813 1.00 27.71 3097 0 TYR 394 97.400 32.622 47.310 1.00 30.17 3098 N LEU 395 97.278 30.379 47.496 1.00 19.47 3099 CA LEU 395 98.356 30.112 46.551 1.00 18.70 3100 CB LEU 395 98.664 28.615 46.506 1.00 23.07 3101 CG LEU 395 99.219 28.005 47.796 1.00 25.20 3102 CD1 LEU 395 99.416 26.512 47.609 1.00 19.35 3103 CD2 LEU 395 100.532 28.681 48.180 1.00 17.74 3104 C LEU 395 98.106 30.630 45.140 1.00 19.62 3105 0 LEU 395 99.030 31.112 44.485 1.00 19.16 3106 N SER 396 96.862 30.549 44.676 1.00 25.13 3107 CA SER 396 96.521 31.018 43.332 1.00 19.88 3108 CB SER 396 95.047 30.749 43.022 1.00 25.09 3109 OG SER 396 94.196 31.513 43.858 1.00 39.87 3110 C SER 396 96.828 32.504 43.165 1.00 19.03 3111 0 SER 396 96.920 33.005 42.040 1.00 15.70 3112 N ASN 397 96.999 33.198 44.290 1.00 14.51 3113 CA ASN 397 97.308 34.624 44.281 1.00 20.25 3114 CB ASN 397 96.252 35.401 45.072 1.00 21.33 3115 CG ASN 397 96.348 36.901 44.858 1.00 25.70 3116 0D1 ASN 397 95.985 37.411 43.795 1.00 26.44 3117 ND2 ASN 397 96.840 37.617 45.868 1.00 14.18 3118 C ASN 397 98.702 34.926 44.844 1.00 21.44 3119 0 ASN 397 99.446 35.727 44.277 1.00 16.68 3120 N ALA 398 99.053 34.263 45.944 1.00 21.43 3121 CA ALA 398 100.339 34.463 46.611 1.00 18.24 3122 CB ALA 398 100.303 33.853 47.996 1.00 9.21 3123 C ALA 398 101.576 33.973 45.861 1.00 22.03 3124 0 ALA 398 102.693 34.375 46.183 1.00 27.40 3125 N LEU 399 101.392 33.099 44.878 1.00 24.29 3126 CA LEU 399 102.530 32.590 44.123 1.00 21.14 3127 CB LEU 399 102.133 31.379 43.276 1.00 16.51 3128 CG LEU 399 101.814 30.092 44.047 1.00 22.47 3129 CD1 LEU 399 101.475 28.979 43.068 1.00 23.59 3130 CD2 LEU 399 102.986 29.686 44.929 1.00 24.50 3131 C LEU 399 103.189 33.656 43.256 1.00 21.08 3132 0 LEU 399 104.414 33.724 43.181 1.00 27.40 3133 N ALA 400 102.384 34.499 42.618 1.00 23.35 3134 CA ALA 400 102.921 35.556 41.762 1.00 25.45 3135 CB ALA 400 101.860 36.050 40.782 1.00 20.16 3136 C ALA 400 103.500 36.724 42.562 1.00 21.72 3137 0 ALA 400 104.438 37.380 42.109 1.00 16.17 3138 N THR 401 102.960 36.966 43.757 1.00 16.96 3139 CA THR 401 103.445 38.054 44.605 1.00 19.18 3140 CB THR 401 102.535 38.294 45.832 1.00 15.54 3141 0G1 THR 401 102.407 37.090 46.592 1.00 24.65 3142 CG2 THR 401 101.167 38.752 45.393 1.00 12.23 3143 C THR 401 104.893 37.842 45.055 1.00 25.46 3144 0 THR 401 105.512 38.743 45.624 1.00 34.91 3145 N THR 402 105.421 36.644 44.813 1.00 25.90 3146 CA THR 402 106.807 36.336 45.151 1.00 21.29 3147 CB THR 402 107.092 34.812 45.138 1.00 19.71 3148 OG1 THR 402 106.944 34.300 43.806 1.00 12.44 3149 CG2 THR 402 106.152 34.080 46.070 1.00 17.92 3150 C THR 402 107.674 36.988 44.076 1.00 22.11 3151 0 THR 402 108.881 37.135 44.245 1.00 21.20 3152 N THR 403 107.022 37.366 42.974 1.00 21.28 3153 CA THR 403 107.629 38.010 41.804 1.00 18.85 3154 CB THR 403 108.446 39.288 42.167 1.00 15.80 3155 0G1 THR 403 109.662 38.922 42.827 1.00 16.98 3156 CG2 THR 403 107.647 40.210 43.071 1.00 14.55 3157 C THR 403 108.515 37.084 40.980 1.00 17.52 3158 0 THR 403 109.136 37.523 40.013 1.00 14.77 3159 N TYR 404 108.533 35.799 41.326 1.00 19.57 3160 CA TYR 404 109.375 34.842 40.617 1.00 16.03 3161 CB TYR 404 109.560 33.560 41.431 1.00 23.52 3162 CG TYR 404 110.799 33.611 42.295 1.00 19.00 3163 CD1 TYR 404 111.271 34.828 42.785 1.00 20.18 3164 CE1 TYR 404 112.430 34.903 43.536 1.00 26.20 3165 CD2 TYR 404 111.527 32.459 42.586 1.00 21.26 3166 CE2 TYR 404 112.695 32.523 43.345 1.00 26.60 3167 CZ TYR 404 113.139 33.753 43.813 1.00 25.95 3168 OH TYR 404 114.291 33.853 44.553 1.00 17.83 3169 C TYR 404 109.040 34.545 39.164 1.00 16.09 3170 0 TYR 404 109.945 34.265 38.375 1.00 15.20 3171 N TYR 405 107.760 34.593 38.803 1.00 14.07 3172 CA TYR 405 107.375 34.360 37.411 1.00 18.64 3173 CB TYR 405 105.852 34.353 37.250 1.00 21.43 3174 CG TYR 405 105.096 33.276 37.991 1.00 14.20 3175 CD1 TYR 405 104.458 33.557 39.196 1.00 25.61 3176 CE1 TYR 405 103.687 32.599 39.844 1.00 26.54 3177 CD2 TYR 405 104.949 31.998 37.452 1.00 18.03 3178 CE2 TYR 405 104.178 31.031 38.094 1.00 15.71 3179 CZ TYR 405 103.550 31.341 39.290 1.00 17.50 3180 OH TYR 405 102.785 30.404 39.941 1.00 14.13 3181 C TYR 405 107.922 35.558 36.638 1.00 16.83 3182 0 TYR 405 108.450 35.433 35.532 1.00 12.99 3183 N TYR 406 107.784 36.718 37.271 1.00 19.05 3184 CA TYR 406 108.213 38.005 36.749 1.00 20.07 3185 CB TYR 406 107.708 39.095 37.709 1.00 20.76 3186 CG TYR 406 108.060 40.523 37.365 1.00 13.44 3187 CD1 TYR 406 108.092 40.965 36.044 1.00 16.24 3188 CE1 TYR 406 108.412 42.284 35.739 1.00 19.34 3189 CD2 TYR 406 108.355 41.436 38.373 1.00 2.00 3190 CE2 TYR 406 108.673 42.751 38.081 1.00 7.86 3191 CZ TYR 406 108.701 43.171 36.764 1.00 14.60 3192 OH TYR 406 109.015 44.481 36.481 1.00 12.74 3193 C TYR 406 109.735 38.068 36.570 1.00 18.51 3194 0 TYR 406 110.222 38.302 35.462 1.00 20.47 3195 N LEU 407 1 10.478 37.822 37.647 1.00 18.49 3196 CA LEU 407 1 11.944 37.854 37.602 1.00 17.48 3197 CB LEU 407 112.536 37.617 38.994 1.00 9.18 3198 CG LEU 407 112.066 38.535 40.125 1.00 11.41 3199 CD1 LEU 407 112.894 38.261 41.366 1.00 4.35 3200 CD2 LEU 407 112.179 40.001 39.714 1.00 14.20 3201 C LEU 407 112.533 36.843 36.619 1.00 17.93 3202 0 LEU 407 113.506 37.142 35.925 1.00 23.70 3203 N ALA 408 111.944 35.650 36.568 1.00 17.24 3204 CA ALA 408 112.402 34.603 35.662 1.00 15.77 3205 CB ALA 408 111.636 33.320 35.913 1.00 20.39 3206 C ALA 408 112.233 35.046 34.214 1.00 15.32 3207 0 ALA 408 113.108 34.820 33.383 1.00 19.31 3208 N THR 409 111.106 35.685 33.919 1.00 18.97 3209 CA THR 409 110.830 36.174 32.570 1.00 20.42 3210 CB THR 409 109.382 36.705 32.455 1.00 12.64 3211 0G1 THR 409 108.465 35.679 32.853 1.00 23.03 3212 CG2 THR 409 109.074 37.116 31.023 1.00 8.86 3213 C THR 409 111.804 37.302 32.233 1.00 18.76 3214 0 THR 409 112.269 37.426 31.096 1.00 14.71 3215 N THR 410 112.118 38.105 33.245 1.00 23.19 3216 CA THR 410 113.031 39.232 33.105 1.00 22.03 3217 CB THR 410 113.060 40.078 34.390 1.00 17.23 3218 0G1 THR 410 111.751 40.600 34.652 1.00 20.47 3219 CG2 THR 410 114.043 41.228 34.251 1.00 18.91 3220 C THR 410 114.453 38.781 32.790 1.00 25.12 3221 0 THR 410 115.109 39.356 31.918 1.00 24.94 3222 N SER 41 ϊ ■ • 14.913 37.741 33.486 1.00 18.76 3223 CA SER 411 116.264 37.221 33.298 1.00 11.15 3224 CB SER 411 116.517 36.026 34.224 1.00 9.23 3225 OG SER 411 115.722 34.911 33.871 1.00 10.06 3226 C SER 411 116.586 36.859 31.848 1.00 15.22 3227 0 SER 411 117.744 36.915 31.431 1.00 22.78 3228 N TYR 412 115.555 36.525 31.078 1.00 12.29 3229 CA TYR 412 115.715 36.165 29.673 1.00 14.56 3230 CB TYR 412 114.473 35.428 29.160 1.00 21.66 3231 CG TYR 412 114.284 34.000 29.630 1.00 31.85 3232 CD1 TYR 412 113.510 33.110 28.884 1.00 25.46 3233 CE1 TYR 412 113.285 31.807 29.315 1.00 25.33 3234 CD2 TYR 412 114:837 33.544 30.829 1.00 33.63 3235 CE2 TYR 412 114.617 32.236 31.271 1.00 30.87 3236 CZ TYR 412 113.837 31.377 30.508 1.00 30.43 3237 OH TYR 412 113.589 30.095 30.941 1.00 25.14 3238 C TYR 412 115.938 37.382 28.775 1.00 18.89 3239 0 TYR 412 116.473 37.252 27.672 1.00 21.47 3240 N LEU 413 H 5.501 38.553 29.235 1.00 22.06 3241 CA LEU 413 115.620 39.790 28.460 1.00 21.99 3242 CB LEU 413 115.120 40.988 29.274 1.00 21.82 3243 CG LEU 413 113.623 40.999 29.600 1.00 28.58 3244 CD1 LEU 413 1 13.286 42.192 30.481 1.00 24.87 3245 CD2 LEU 413 112.806 41.026 28.316 1.00 20.55 3246 C LEU 413 117.008 40.081 27.901 1.00 23.58 3247 0 LEU 413 117.157 40.329 26.702 1.00 27.31 3248 N GLY 414 1 18.018 40.041 28.764 1.00 17.88 3249 CA GLY 414 119.376 40.309 28.324 1.00 19.54 3250 C GLY 414 120.063 39.141 27.644 1.00 21.66 3251 0 GLY 414 121.088 39.319 26.981 1.00 32.10 3252 N MET 415 119.500 37.947 27.804 1.00 20.71 3253 CA MET 415 120.062 36.741 27.209 1.00 18.08 3254 CB MET 415 119.440 35.504 27.850 1.00 15.67 3255 CG MET 415 119.705 35.424 29.345 1.00 19.68 3256 SD MET 415 118.883 34.052 30.144 1.00 21.56 3257 CE MET 415 119.945 32.725 29.700 1.00 15.56 3258 C MET 415 119.870 36.734 25.702 1.00 23.08 3259 0 MET 415 118.808 36.379 25.199 1.00 35.78 3260 N LYS 416 120.930 37.112 24.996 1.00 32.44 3261 CA LYS 416 120.953 37.207 23.538 1.00 38.05 3262 CB LYS 416 122.360 37.608 23.090 1.00 47.08 3263 CG LYS 416 122.865 38.875 23.776 1.00 61.44 3264 CD LYS 416 124.358 39.084 23.581 1.00 67.69 3265 CE LYS 416 124.846 40.273 24.399 1.00 67.49 3266 NZ LYS 416 126.319 40.457 24.297 1.00 75.93 3267 C LYS 416 120.486 35.970 22.767 1.00 39.94 3268 0 LYS 416 120.113 36.070 21.597 1.00 44.84 3269 N SER 417 120.493 34.813 23.422 1.00 39.76 3270 CA SER 417 120.071 33.571 22.780 1.00 39.16 3271 CB SER 417 120.900 32.398 23.304 1.00 38.83 3272 OG SER 417 122.282 32.610 23.076 1.00 46.53 3273 C SER 417 118.581 33.270 22.956 1.00 40.99 3274 0 SER 417 118.040 32.385 22.289 1.00 41.33 3275 N ALA 418 117.925 34.005 23.853 1.00 38.28 3276 CA ALA 418 116.501 33.814 24.122 1.00 31.24 3277 CB ALA 418 116.087 34.610 25.348 1.00 30.62 3278 C ALA 418 115.628 34.186 22.930 1.00 31.48 3279 0 ALA 418 115.674 35.317 22.440 1.00 35.02 3280 N THR 419 114.841 33.219 22.468 1.00 27.95 3281 CA THR 419 113.942 33.409 21.332 1.00 26.20 3282 CB THR 419 113.996 32.197 20.370 1.00 26.76 3283 0G1 THR 419 113.511 31.027 21.039 1.00 27.32 3284 CG2 THR 419 115.424 31.945 19.901 1.00 18.56 3285 C THR 419 112.502 33.595 21.806 1.00 30.31 3286 0 THR 419 112.241 33.693 23.005 1.00 33.17 3287 N GLU 420 111.573 33.662 20.857 1.00 35.12 3288 CA GLU 420 110.158 33.818 21.183 1.00 39.51 3289 CB GLU 420 109.349 34.179 19.935 1.00 46.05 3290 CG GLU 420 108.972 35.653 19.828 1.00 51.65 3291 CD GLU 420 108.013 36.104 20.919 1.00 54.36 3292 OE1 GLU 420 107.027 35.384 21.192 1.00 55.36 3293 OE2 GLU 420 108.245 37.186 21.500 1.00 58.01 3294 C GLU 420 109.620 32.527 21.781 1.00 37.05 3295 O GLU 420 108.852 32.550 22.742 1.00 36.79 3296 N GLN 421 110.050 31.404 21.215 1.00 37.04 3297 CA GLN 421 109.624 30.090 21.676 1.00 33.78 3298 CB GLN 421 1 10.218 28.999 20.792 1.00 40.49 3299 CG GLN 421 109.711 29.009 19.363 1.00 57.72 3300 CD GLN 421 110.206 27.813 18.564 1.00 74.05 3301 OE1 GLN 421 110.596 26.786 19.128 1.00 68.24 3302 NE2 GLN 421 110.190 27.941 17.242 1.00 83.42 3303 C C GGLLNN 421 109.999 29.826 23.128 1.00 31.12 3304 O 0 GGLLNN 421 109.336 29.041 23.807 1.00 35.81 3305 N AASSPP 422 111.071 30.466 23.592 1.00 27.52 3306 CA AASSPP 422 111.527 30.304 24.971 1.00 25.90 3307 CB AASSPP 422 112.963 30.821 25.137 1.00 25.75 3308 CG AASSPP 422 113.985 29.971 24.396 1.00 29.11 3309 OD1 AASSPP 422 114.983 30.537 23.902 1.00 33.41 3310 OD2 ASP 422 113.800 28.736 24.311 1.00 32.66 3311 C ASP 422 110.590 31.020 25.936 1.00 21.80 3312 0 A ASSPP 422 110.282 30.502 27.011 1.00 19.43 3313 N PPHHEE 423 110.145 32.213 25.545 1.00 24.75 3314 CA PPHHEE 423 109.223 33.004 26.357 1.00 26.23 3315 CB PPHHEE 423 109.117 34.432 25.818 1.00 30.85 3316 CG PPHHEE 423 110.290 35.306 26.166 1.00 32.84 3317 CD1 PPHHEE 423 111.336 35.482 25.268 1.00 34.61 3318 CD2 PHE 423 110.338 35.972 27.388 1.00 33.51 3319 CE1 PHE 423 112.412 36.312 25.579 1.00 30.52 3320 CE2 P PHHEE 423 111.410 36.805 27.708 1.00 35.27 3321 CZ PPHHEE 423 112.448 36.974 26.801 1.00 23.59 3322 C PPHHEE 423 107.849 32.354 26.330 1.00 24.84 3323 0 PPHHEE 423 107.106 32.392 27.311 1.00 31.10 3324 N GGLLUU 424 107.530 31.751 25.191 1.00 29.70 3325 CA GGLLUU 424 106.261 31.070 24.982 1.00 36.07 3326 CB GGLLUU 424 106.187 30.588 23.535 1.00 40.70 3327 CG GGLLUU 424 104.785 30.391 22.992 1.00 63.10 3328 CD GGLLUU 424 104.759 30.296 21.473 1.00 75.17 3329 OE1 GGLLUU 424 105.781 29.898 20.867 1.00 75.10 3330 OE2 GGLLUU 424 103.710 30.630 20.880 1.00 85.30 3331 C GGLLUU 424 106.164 29.892 25.949 1.00 31.83 3332 0 GGLLUU 424 105.138 29.687 26.595 1.00 35.87 3333 N TTRRPP 425 107.258 29.148 26.066 1.00 29.46 3334 CA TTRRPP 425 107.339 27.999 26.958 1.00 23.86 3335 CB TTRRPP 425 108.680 27.285 26.753 1.00 25.55 3336 CG TTRRPP 425 108.991 26.265 27.803 1.00 29.41 3337 CD2 TTRRPP 425 109.808 26.455 28.965 1.00 27.61 3338 CE2 TTRRPP 425 109.779 25.249 29.697 1.00 24.31 3339 CE3 TTRRPP 425 110.557 27.529 29.460 1.00 30.25 3340 CD1 TTRRPP 425 108.521 24.984 27.871 1.00 28.89 3341 NE1 TTRRPP 425 108.987 24.369 29.007 1.00 29.83 3342 CZ2 TTRRPP 425 110.473 25.087 30.900 1.00 16.37 3343 CZ3 TTRRPP 425 111.245 27.367 30.658 1.00 25.72 3344 CH2 TRP 425 111.196 26.154 31.363 1.00 19.53 3345 C TRP 425 107.205 28.437 28.414 1.00 25.64 3346 0 TRP 425 106.523 27.792 29.213 1.00 26.99 3347 N LEU 426 107.852 29.553 28.739 1.00 26.42 3348 CA LEU 426 107.853 30.103 30.088 1.00 21.18 3349 CB LEU 426 108.922 31.191 30.195 1.00 21.43 3350 CG LEU 426 109.379 31.600 31.595 1.00 14.19 3351 CD1 LEU 426 110.106 30.441 32.251 1.00 14.14 3352 CD2 LEU 426 110.297 32.798 31.499 1.00 12.82 3353 C LEU 426 106.504 30.664 30.523 1.00 23.80 3354 0 LEU 426 106.153 30.596 31.702 1.00 31.77 3355 N SER 427 105.754 31.221 29.575 1.00 28.08 3356 CA SER 427 104.444 31.802 29.871 1.00 30.28 3357 CB SER 427 103.915 32.592 28.665 1.00 26.14 3358 OG SER 427 103.742 31.763 27.528 1.00 29.08 3359 C SER 427 103.406 30.773 30.325 1.00 29.36 3360 0 SER 427 102.497 31.099 31.088 1.00 31.12 3361 N LYS 428 103.558 29.530 29.873 1.00 27.92 3362 CA LYS 428 102.637 28.455 30.230 1.00 20.58 3363 CB LYS 428 102.770 27.290 29.251 1.00 23.24 3364 CG LYS 428 102.454 27.613 27.801 1.00 22.85 3365 CD LYS 428 102.509 26.335 26.976 1.00 42.29 3366 CE LYS 428 102.338 26.597 25.493 1.00 49.89 3367 NZ LYS 428 102.345 25.316 24.727 1.00 62.04 3368 C LYS 428 102.844 27.935 31.654 1.00 20.72 3369 O LYS 428 102.183 26.980 32.067 1.00 29.09 3370 N ASN 429 103.762 28.557 32.391 1.00 20.35 3371 CA ASN 429 104.072 28.170 33.770 1.00 14.44 3372 CB ASN 429 102.868 28.406 34.685 1.00 13.93 3373 CG ASN 429 102.581 29.876 34.910 1.00 21.29 3374 OD1 ASN 429 103.306 30.747 34.431 1.00 26.38 3375 ND2 A ASSNN 429 101.522 30.159 35.657 1.00 28.12 3376 C ASN 429 104.545 26.724 33.900 1.00 19.87 3377 O ASN 429 103.831 25.868 34.426 1.00 27.89 3378 N PRO 430 105.764 26.433 33.418 1.00 18.35 3379 CD PRO 430 106.650 27.362 32.701 1.00 19.00 3380 CA PRO 430 106.358 25.096 33.468 1.00 11.22 3381 CB PRO 430 107.711 25.309 32.808 1.00 15.49 3382 CG PRO 430 107.444 26.425 31.859 1.00 26.05 3383 C PRO 430 106.518 24.612 34.902 1.00 17.61 3384 O PRO 430 106.617 25.416 35.828 1.00 19.92 3385 N LYS 431 106.569 23.294 35.073 1.00 18.71 3386 CA LYS 431 106.699 22.681 36.389 1.00 14.83 3387 CB LYS 431 106.682 21.157 36.256 1.00 15.08 3388 CG LYS 431 106.353 20.409 37.539 1.00 26.85 3389 CD LYS 431 106.103 18.937 37.244 1.00 41.27 3390 CE LYS 431 105.561 18.195 38.455 1.00 49.80 3391 NZ LYS 431 105.297 16.760 38.140 1.00 45.04 3392 C LYS 431 107.959 23.137 37.121 1.00 19.80 3393 O LYS 431 107.937 23.333 38.338 1.00 20.81 3394 N ILE 432 109.051 23.316 36.380 1.00 15.93 3395 CA ILE 432 1 0.306 23.757 36.979 1.00 16.86 3396 CB ILE 432 111.497 23.632 35.994 1.00 20.40 3397 CG2 ILE 432 1 11.278 24.502 34.756 1.00 16.63 3398 CG1 ILE 432 1 12.804 23.985 36.709 1.00 14.19 3399 CD1 ILE 432 114.048 23.649 35.920 1.00 13.37 3400 C ILE 432 110.182 25.187 37.499 1.00 17.42 3401 0 ILE 432 110.681 25.508 38.579 1.00 24.54 3402 N LEU 433 109.488 26.035 36.742 1.00 15.09 3403 CA LEU 433 109.277 27.420 37.146 1.00 14.83 3404 CB LEU 433 108.728 28.245 35.978 1.00 13.49 3405 CG LEU 433 108.378 29.708 36.272 1.00 10.45 3406 CD1 LEU 433 109.564 30.430 36.896 1.00 15.23 3407 CD2 LEU 433 107.939 30.400 34.993 1.00 9.30 3408 C LEU 433 108.289 27.433 38.304 1.00 18.07 3409 0 LEU 433 108.481 28.140 39.295 1.00 21.14 3410 N GLU 434 107.245 26.621 38.173 1.00 21.38 3411 CA GLU 434 106.209 26.503 39.188 1.00 16.25 3412 CB GLU 434 105.184 25.452 38.753 1.00 23.52 3413 CG GLU 434 103.812 25.605 39.385 1.00 38.66 3414 CD GLU 434 103.161 26.933 39.037 1.00 42.62 3415 OE1 GLU 434 102.828 27.148 37.851 1.00 32.73 3416 OE2 GLU 434 102.993 27.765 39.953 1.00 37.72 3417 C GLU 434 106.850 26.095 40.511 1.00 14.12 3418 0 GLU 434 106.561 26.676 41.556 1.00 14.76 3419 N ALA 435 107.753 25.120 40.440 1.00 17.75 3420 CA ALA 435 108.465 24.610 41.610 1.00 16.67 3421 CB ALA 435 109.303 23.410 41.214 1.00 8.83 3422 C ALA 435 109.344 25.683 42.254 1.00 11.99 3423 0 ALA 435 109.372 25.827 43.477 1.00 7.99 3424 N SER 436 110.057 26.435 41.422 1.00 15.97 3425 CA SER 436 110.924 27.508 41.900 1.00 21.95 3426 CB SER 436 111.636 28.163 40.713 1.00 24.20 3427 OG SER 436 112.489 29.212 41.135 1.00 40.93 3428 C SER 436 110.110 28.554 42.674 1.00 21.39 3429 0 SER 436 110.519 29.009 43.748 1.00 24.40 3430 N VAL 437 108.951 28.912 42.125 1.00 18.68 3431 CA VAL 437 108.054 29.889 42.739 1.00 8.95 3432 CB VAL 437 106.855 30.188 41.818 1.00 11.54 3433 CG1 VAL 437 105.917 31.169 42.478 1.00 11.34 3434 CG2 VAL 437 107.339 30.734 40.486 1.00 5.44 3435 C VAL 437 107.533 29.401 44.092 1.00 9.21 3436 0 VAL 437 107.452 30.176 45.048 1.00 12.18 3437 N ILE 438 107.185 28.115 44.161 1.00 9.76 3438 CA ILE 438 106.673 27.504 45.388 1.00 8.03 3439 CB ILE 438 106.309 26.015 45.171 1.00 14.49 3440 CG2 ILE 438 105.931 25.360 46.500 1.00 10.62 3441 CG1 ILE 438 105.162 25.896 44.164 1.00 23.13 3442 CD1 ILE 438 104.753 24.468 43.853 1.00 31.20 3443 C ILE 438 107.692 27.603 46.520 1.00 12.21 3444 0 ILE 438 107.349 27.982 47.639 1.00 18.63 3445 N ILE 439 108.941 27.258 46.216 1.00 14.08 3446 CA ILE 439 110.033 27.307 47.188 1.00 9.89 3447 CB ILE 439 1 11.369 26.901 46.525 1.00 12.54 3448 CG2 ILE 439 112.540 27.161 47.459 1.00 11.31 3449 CG1 ILE 439 111.321 25.424 46.136 1.00 2.00 3450 CD1 ILE 439 112.441 24.990 45.233 1.00 14.05 3451 C ILE 439 110.152 28.706 47.783 1.00 9.52 3452 0 ILE 439 110.213 28.871 49.003 1.00 10.13 3453 N CYS 440 110.135 29.714 46.918 1.00 8.13 3454 CA CYS 440 110.233 31.098 47.361 1.00 12.62 3455 CB CYS 440 110.267 32.036 46.153 1.00 5.84 3456 SG CYS 440 110.449 33.774 46.599 1.00 11.97 3457 C CYS 440 109.073 31.482 48.283 1.00 17.47 3458 0 CYS 440 109.264 32.175 49.287 1.00 18.40 3459 N ARG 441 107.875 31.012 47.940 1.00 18.94 3460 CA ARG 441 106.669 31.296 48.714 1.00 11.76 3461 CB ARG 441 105.433 30.810 47.949 1.00 10.60 3462 CG ARG 441 104.093 31.083 48.629 1.00 6.45 3463 CD ARG 441 103.718 32.559 48.590 1.00 19.08 3464 NE ARG 441 104.454 33.353 49.571 1.00 23.16 3465 CZ ARG 441 104.623 34.670 49.500 1.00 20.47 3466 NH1 ARG 441 104.108 35.353 48.489 1.00 12.16 3467 NH2 ARG 441 105.307 35.307 50.441 1.00 30.69 3468 C ARG 441 106.716 30.637 50.089 1.00 17.00 3469 0 ARG 441 106.629 31.307 51.120 1.00 25.77 3470 N VAL 442 106.858 29.317 50.086 1.00 22.16 3471 CA VAL 442 106.920 28.518 51.306 1.00 22.25 3472 CB VAL 442 107.112 27.032 50.959 1.00 23.82 3473 CG1 VAL 442 107.624 26.261 52.164 1.00 26.50 3474 CG2 VAL 442 105.796 26.450 50.471 1.00 31.37 3475 C VAL 442 108.004 28.969 52.283 1.00 21.17 3476 0 VAL 442 107.765 29.058 53.488 1.00 25.05 3477 N ILE 443 109.195 29.243 51.761 1.00 22.99 3478 CA ILE 443 110.305 29.685 52.596 1.00 27.94 3479 CB ILE 443 111.628 29.710 51.805 1.00 34.71 3480 CG2 ILE 443 112.721 30.396 52.612 1.00 32.63 3481 CG1 ILE 443 112.041 28.279 51.458 1.00 35.15 3482 CD1 ILE 443 113.322 28.183 50.669 1.00 41.45 3483 C ILE 443 110.024 31.054 53.208 1.00 24.50 3484 0 ILE 443 110.253 31.263 54.400 1.00 25.69 3485 N ASP 444 109.500 31.972 52.398 1.00 24.21 3486 CA ASP 444 109.178 33.314 52.875 1.00 26.25 3487 CB ASP 444 108.695 34.203 51.721 1.00 29.76 3488 CG ASP 444 108.365 35.624 52.169 1.00 39.45 3489 OD1 ASP 444 109.179 36.535 51.910 1.00 45.87 3490 OD2 ASP 444 107.288 35.841 52.768 1.00 45.57 3491 C ASP 444 108.103 33.247 53.952 1.00 28.37 3492 0 ASP 444 108.228 33.883 54.995 1.00 29.64 3493 N ASP 445 107.061 32.458 53.700 1.00 30.42 3494 CA ASP 445 105.950 32.318 54.637 1.00 32.30 3495 CB ASP 445 104.797 31.544 53.994 1.00 33.98 3496 CG ASP 445 104.151 32.302 52.838 1.00 37.92 3497 OD1 ASP 445 104.356 33.532 52.717 1.00 38.86 3498 OD2 ASP 445 103.429 31.662 52.047 1.00 28.07 3499 C ASP 445 106.335 31.690 55.970 1.00 33.30 3500 0 ASP 445 105.762 32.030 57.009 1.00 42.91 3501 N THR 446 107.302 30.778 55.946 1.00 33.28 3502 CA THR 446 107.758 30.124 57.168 1.00 30.88 3503 CB THR 446 108.625 28.887 56.855 1.00 26.02 3504 0G1 THR 446 107.873 27.969 56.050 1.00 21.99 3505 CG2 THR 446 109.046 28.188 58.143 1.00 25.74 3506 C THR 446 108.570 31.110 58.014 1.00 32.83 3507 0 THR 446 108.459 31.131 59.238 1.00 33.61 3508 N ALA 447 109.357 31.944 57.339 1.00 40.56 3509 CA ALA 447 110.202 32.937 57.996 1.00 45.46 3510 CB ALA 447 111.313 33.374 57.056 1.00 42.21 3511 C ALA 447 109.434 34.155 58.468 1.00 46.97 3512 0 ALA 447 109.596 34.617 59.599 1.00 54.11 3513 N THR 448 108.599 34.690 57.581 1.00 47.28 3514 CA THR 448 107.832 35.884 57.879 1.00 46.44 3515 CB THR 448 107.689 36.787 56.618 1.00 41.12 3516 OG1 THR 448 106.943 36.112 55.607 1.00 30.26 3517 CG2 THR 448 109.064 37.170 56.071 1.00 32.60 3518 C THR 448 106.446 35.694 58.497 1.00 51.30 3519 0 THR 448 105.708 36.657 58.620 1.00 53.69 3520 N TYR 449 106.080 34.481 58.912 1.00 53.28 3521 CA TYR 449 104.751 34.282 59.492 1.00 58.27 3522 CB TYR 449 104.497 32.811 59.888 1.00 58.98 3523 CG TYR 449 103.175 32.661 60.637 1.00 61.56 3524 CD1 TYR 449 101.973 33.066 60.055 1.00 66.72 3525 CE1 TYR 449 100.772 33.026 60.769 1.00 64.98 3526 CD2 TYR 449 103.147 32.198 61.957 1.00 62.94 3527 CE2 TYR 449 101.956 32.155 62.672 1.00 66.76 3528 CZ TYR 449 100.773 32.575 62.080 1.00 67.45 3529 OH TYR 449 99.601 32.590 62.810 1.00 73.04 3530 C TYR 449 104.462 35.189 60.691 1.00 59.96 3531 0 TYR 449 103.576 36.051 60.638 1.00 60.11 3532 N GLU 450 105.199 34.975 61.771 1.00 61.73 3533 CA GLU 450 105.029 35.733 62.995 1.00 61.61 3534 CB GLU 450 106.071 35.308 64.025 1.00 65.21 3535 CG GLU 450 105.833 33.912 64.589 1.00 75.41 3536 CD GLU 450 106.887 33.502 65.610 1.00 85.43 3537 OE1 GLU 450 107.416 34.375 66.331 1.00 91.32 3538 OE2 GLU 450 107.196 32.293 65.686 1.00 90.42 3539 C GLU 450 105.026 37.251 62.841 1.00 59.86 3540 0 GLU 450 104.144 37.918 63.377 1.00 59.89 3541 N VAL 451 105.995 37.787 62.098 1.00 61.44 3542 CA VAL 451 106.092 39.234 61.873 1.00 63.11 3543 CB VAL 451 107.408 39.596 61.116 1.00 64.01 3544 CG1 VAL 451 107.256 40.886 60.304 1.00 63.92 3545 CG2 VAL 451 108.541 39.761 62.123 1.00 71.39 3546 C VAL 451 104.881 39.809 61.152 1.00 62.77 3547 0 VAL 451 104.336 40.841 61.555 1.00 65.95 3548 N GLU 452 104.450 39.118 60.103 1.00 62.77 3549 CA GLU 452 103.304 39.545 59.315 1.00 57.61 3550 CB GLU 452 103.275 38.782 57.991 1.00 56.30 3551 CG GLU 452 104.444 39.130 57.058 1.00 59.48 3552 CD GLU 452 104.469 38.317 55.787 1.00 60.10 3553 OE1 GLU 452 104.787 38.899 54.728 1.00 62.60 3554 OE2 GLU 452 104.183 37.106 55.843 1.00 61.28 3555 C GLU 452 101.984 39.392 60.081 1.00 56.17 3556 0 GLU 452 101.034 40.136 59.838 1.00 51.59 3557 N LYS 453 101.946 38.466 61.040 1.00 58.80 3558 CA LYS 453 100.753 38.241 61.858 1.00 58.04 3559 CB LYS 453 100.863 36.913 62.611 1.00 59.76 3560 CG LYS 453 99.644 36.565 63.453 1.00 60.02 3561 CD LYS 453 99.925 35.384 64.366 1.00 58.67 3562 CE LYS 453 98.732 35.093 65.262 1.00 61.72 3563 NZ LYS 453 99.013 33.991 66.222 1.00 58.55 3564 C LYS 453 100.584 39.385 62.863 1.00 57.99 3565 0 LYS 453 99.461 39.769 63.195 1.00 57.81 3566 N SER 454 101.709 39.920 63.339 1.00 62.23 3567 CA SER 454 101.712 41.026 64.295 1.00 61.09 3568 CB SER 454 103.125 41.265 64.837 1.00 60.66 3569 OG SER 454 103.548 40.191 65.654 1.00 66.36 3570 C SER 454 101.185 42.311 63.665 1.00 58.28 3571 0 SER 454 100.632 43.163 64.360 1.00 56.27 3572 N ARG 455 101.373 42.447 62.354 1.00 58.50 3573 CA ARG 455 100.916 43.623 61.619 1.00 62.35 3574 CB ARG 455 101.827 43.885 60.414 1.00 67.55 3575 CG ARG 455 103.261 44.228 60.797 1.00 76.19 3576 CD ARG 455 104.115 44.547 59.581 1.00 85.72 3577 NE ARG 455 105.444 45.024 59.964 1.00 96.37 3578 CZ ARG 455 106.292 45.634 59.140 1.00 100.00 3579 NH1 ARG 455 105.960 45.845 57.872 1.00 100.00 3580 NH2 ARG 455 107.470 46.051 59.587 1.00 99.29 3581 C ARG 455 99.457 43.503 61.176 1.00 60.13 3582 0 ARG 455 98.922 44.399 60.519 1.00 58.35 3583 N GLY 456 98.824 42.391 61.546 1.00 60.37 3584 CA GLY 456 97.432 42.164 61.201 1.00 62.20 3585 C GLY 456 97.183 41.378 59.925 1.00 67.18 3586 0 GLY 456 96.036 41.048 59.626 1.00 70.98 3587 N GLN 457 98.238 41.091 59.166 1.00 69.31 3588 CA GLN 457 98.108 40.340 57.917 1.00 68.54 3589 CB GLN 457 99.397 40.438 57.089 1.00 69.51 3590 CG GLN 457 99.764 41.859 56.671 1.00 74.48 3591 CD GLN 457 101.105 41.941 55.965 1.00 78.04 3592 OE1 GLN 457 102.099 41.389 56.428 1.00 87.45 3593 NE2 GLN 457 101.140 42.651 54.840 1.00 80.41 3594 C GLN 457 97.765 38.879 58.197 1.00 66.56 3595 0 GLN 457 98.645 38.020 58.262 1.00 70.53 3596 N ILE 458 96.475 38.616 58.384 1.00 64.43 3597 CA ILE 458 95.976 37.272 58.664 1.00 60.84 3598 CB ILE 458 94.652 37.317 59.458 1.00 62.21 3599 CG2 ILE 458 94.940 37.397 60.958 1.00 64.20 3600 CG1 ILE 458 93.769 38.462 58.943 1.00 60.42 3601 CD1 ILE 458 92.437 38.608 59.656 1.00 66.77 3602 C ILE 458 95.768 36.440 57.403 1.00 55.84 3603 0 ILE 458 95.281 35.310 57.468 1.00 51.58 3604 N ALA 459 96.145 37.005 56.259 1.00 58.27 3605 CA ALA 459 96.011 36.318 54.979 1.00 56.90 3606 CB ALA 459 95.609 37.305 53.888 1.00 56.20 3607 C ALA 459 97.296 35.587 54.579 1.00 54.74 3608 0 ALA 459 97.434 35.158 53.433 1.00 54.48 3609 N THR 460 98.236 35.455 55.513 1.00 49.39 3610 CA THR 460 99.494 34.779 55.224 1.00 47.02 3611 CB THR 460 100.603 35.180 56.200 1.00 50.43 3612 OG1 THR 460 100.077 35.259 57.532 1.00 52.34 3613 CG2 THR 460 101.194 36.507 55.781 1.00 56.05 3614 C THR 460 99.399 33.264 55.164 1.00 45.28 3615 0 THR 460 98.566 32.651 55.832 1.00 47.09 3616 N GLY 461 100.303 32.676 54.386 1.00 45.02 3617 CA GLY 461 100.351 31.238 54.190 1.00 41.47 3618 C GLY 461 100.107 30.318 55.367 1.00 38.12 3619 0 GLY 461 99.172 29.516 55.341 1.00 41.90 3620 N ILE 462 100.962 30.399 56.380 1.00 36.28 3621 CA ILE 462 100.825 29.545 57.552 1.00 41.08 3622 CB ILE 462 101.954 29.813 58.580 1.00 34.80 3623 CG2 ILE 462 101.814 28.893 59.792 1.00 33.01 3624 CG1 ILE 462 103.319 29.613 57.917 1.00 21.22 3625 CD1 ILE 462 103.525 28.231 57.322 1.00 17.74 3626 C ILE 462 99.444 29.683 58.197 1.00 47.74 3627 0 ILE 462 98.823 28.682 58.556 1.00 53.27 3628 N GLU 463 98.940 30.915 58.266 1.00 49.04 3629 CA GLU 463 97.626 31.178 58.852 1.00 46.29 3630 CB GLU 463 97.358 32.687 58.929 1.00 44.06 3631 CG GLU 463 96.076 33.063 59.677 1.00 51.03 3632 CD GLU 463 96.101 32.673 61.150 1.00 55.15 3633 OE1 GLU 463 96.861 33.290 61.931 1.00 50.13 3634 OE2 GLU 463 95.348 31.752 61.529 1.00 55.86 3635 C GLU 463 96.530 30.483 58.041 1.00 44.39 3636 0 GLU 463 95.690 29.774 58.600 1.00 47.37 3637 N CYS 464 96.559 30.680 56.723 1.00 39.81 3638 CA CYS 464 95.589 30.068 55.816 1.00 37.44 3639 CB CYS 464 95.916 30.426 54.362 1.00 29.94 3640 SG CYS 464 95.879 32.186 53.990 1.00 33.66 3641 C CYS 464 95.630 28.556 55.973 1.00 39.78 3642 0 CYS 464 94.594 27.903 56.091 1.00 43.58 3643 N CYS 465 96.846 28.016 55.995 1.00 44.06 3644 CA CYS 465 97.072 26.583 56.133 1.00 43.89 3645 CB CYS 465 98.568 26.275 56.009 1.00 39.41 3646 SG CYS 465 98.961 24.513 55.936 1.00 40.79 3647 C CYS 465 96.532 26.052 57.454 1.00 44.77 3648 0 CYS 465 95.883 25.004 57.490 1.00 43.29 3649 N MET 466 96.788 26.794 58.530 1.00 50.46 3650 CA MET 466 96.342 26.418 59.870 1.00 59.83 3651 CB MET 466 96.838 27.429 60.916 1.00 58.39 3652 CG MET 466 98.343 27.424 61.149 1.00 55.57 3653 SD MET 466 98.825 28.416 62.560 1.00 56.88 3654 CE MET 466 98.266 29.965 62.036 1.00 50.47 3655 C MET 466 94.825 26.271 59.979 1.00 64.16 3656 0 MET 466 94.334 25.227 60.409 1.00 65.97 3657 N ARG 467 94.094 27.319 59.598 1.00 67.84 3658 CA ARG 467 92.631 27.320 59.654 1.00 69.35 3659 CB ARG 467 92.083 28.744 59.512 1.00 75.34 3660 CG ARG 467 92.397 29.655 60.684 1.00 84.97 3661 CD ARG 467 91.640 30.965 60.560 1.00 96.41 3662 NE ARG 467 92.020 31.944 61.578 1.00 100.00 3663 CZ ARG 467 91.475 33.152 61.696 1.00 100.00 3664 NH1 ARG 467 90.515 33.541 60.862 1.00 100.00 3665 NH2 ARG 467 91.901 33.982 62.639 1.00 100.00 3666 C ARG 467 91.965 26.415 58.620 1.00 64.55 3667 0 ARG 467 90.863 25.907 58.853 1.00 66.78 3668 N ASP 468 92.631 26.222 57.485 1.00 52.01 3669 CA ASP 468 92.108 25.383 56.412 1.00 45.50 3670 CB ASP 468 92.825 25.707 55.097 1.00 38.83 3671 CG ASP 468 92.140 25.103 53.886 1.00 38.56 3672 0D1 ASP 468 92.817 24.928 52.852 1.00 35.49 3673 0D2 ASP 468 90.925 24.814 53.953 1.00 52.91 3674 C ASP 468 92.201 23.882 56.718 1.00 49.65 3675 0 ASP 468 91.302 23.120 56.358 1.00 53.89 3676 N TYR 469 93.271 23.469 57.397 1.00 48.30 3677 CA TYR 469 93.475 22.059 57.740 1.00 47.34 3678 CB TYR 469 94.887 21.611 57.345 1.00 49.69 3679 CG TYR 469 95.110 21.555 55.851 1.00 50.72 3680 CD1 TYR 469 95.085 20.339 55.169 1.00 53.63 3681 CE1 TYR 469 95.255 20.284 53.787 1.00 51.76 3682 CD2 TYR 469 95.318 22.719 55.113 1.00 50.18 3683 CE2 TYR 469 95.489 22.675 53.732 1.00 50.61 3684 CZ TYR 469 95.455 21.456 53.075 1.00 54.80 3685 OH TYR 469 95.615 21.407 51.708 1.00 57.11 3686 C TYR 469 93.230 21.743 59.215 1.00 46.62 3687 0 TYR 469 93.180 20.573 59.605 1.00 47.10 3688 N GLY 470 93.069 22.788 60.026 1.00 43.51 3689 CA GLY 470 92.837 22.610 61.449 1.00 43.21 3690 C GLY 470 94.055 22.038 62.146 1.00 45.56 3691 0 GLY 470 93.952 21.077 62.912 1.00 44.25 3692 N ILE 471 95.215 22.624 61.860 1.00 50.47 3693 CA ILE 471 96.488 22.188 62.433 1.00 49.97 3694 CB ILE 471 97.415 21.596 61.342 1.00 47.18 3695 CG2 ILE 471 96.844 20.285 60.811 1.00 47.32 3696 CG1 ILE 471 97.613 22.61 1 60.211 1.00 41.43 3697 CD1 ILE 471 98.427 22.094 59.049 1.00 46.18 3698 C ILE 471 97.217 23.339 63.124 1.00 49.28 3699 0 ILE 471 96.894 24.508 62.907 1.00 49.58 3700 N SER 472 98.204 23.000 63.949 1.00 49.04 3701 CA SER 472 98.986 23.998 64.674 1.00 52.64 3702 CB SER 472 99.748 23.340 65.829 1.00 54.48 3703 OG SER 472 100.699 22.404 65.351 1.00 56.26 3704 C SER 472 99.969 24.716 63.753 1.00 53.26 3705 0 SER 472 100.101 24.369 62.578 1.00 53.95 3706 N THR 473 100.650 25.725 64.292 1.00 53.55 3707 CA THR 473 101.634 26.491 63.531 1.00 54.18 3708 CB THR 473 102.233 27.639 64.384 1.00 60.37 3709 OG1 THR 473 101.180 28.490 64.855 1.00 61.07 3710 CG2 THR 473 103.210 28.469 63.562 1.00 58.84 3711 C THR 473 102.760 25.550 63.105 1.00 51.25 3712 0 THR 473 103.203 25.573 61.956 1.00 44.22 3713 N LYS 474 103.173 24.697 ' 64.038 1.00 49.57 3714 CA LYS 474 104.236 23.722 63.821 1.00 51.50 3715 CB LYS 474 104.440 22.903 65.098 1.00 55.84 3716 CG LYS 474 105.605 21.930 65.063 1.00 60.97 3717 CD LYS 474 105.778 21.266 66.421 1.00 66.81 3718 CE LYS 474 107.011 20.382 66.462 1.00 71.89 3719 NZ LYS 474 107.261 19.853 67.832 1.00 72.76 3720 C LYS 474 103.924 22.797 62.646 1.00 53.47 3721 0 LYS 474 104.759 22.603 61.759 1.00 56.55 3722 N GLU 475 102.712 22.249 62.637 1.00 54.30 3723 CA GLU 475 102.271 21.342 61.578 1.00 54.12 3724 CB GLU 475 100.921 20.719 61.946 1.00 49.93 3725 CG GLU 475 100.940 19.925 63.244 1.00 54.09 3726 CD GLU 475 99.559 19.471 63.673 1.00 56.55 3727 0E1 GLU 475 99.055 18.476 63.111 1.00 59.40 3728 0E2 GLU 475 98.977 20.109 64.577 1.00 54.88 3729 C GLU 475 102.170 22.043 60.224 1.00 48.29 3730 0 GLU 475 102.514 21.465 59.192 1.00 43.53 3731 N ALA 476 101.706 23.291 60.240 1.00 47.85 3732 CA ALA 476 101.556 24.085 59.023 1.00 48.40 3733 CB ALA 476 100.857 25.400 59.335 1.00 44.20 3734 C ALA 476 102.906 24.348 58.367 1.00 45.69 3735 0 ALA 476 103.043 24.246 57.148 1.00 40.88 3736 N MET 477 103.897 24.690 59.185 1.00 46.31 3737 CA MET 477 105.241 24.956 58.687 1.00 47.60 3738 CB MET 477 106.097 25.600 59.777 1.00 41.69 3739 CG MET 477 105.533 26.906 60.286 1.00 40.46 3740 SD MET 477 106.643 27.743 61.402 1.00 51.90 3741 CE MET 477 106.373 29.438 60.922 1.00 53.11 3742 C MET 477 105.882 23.659 58.213 1.00 47.15 3743 0 MET 477 106.580 23.637 57.196 1.00 43.34 3744 N ALA 478 105.617 22.580 58.948 1.00 44.29 3745 CA ALA 478 106.146 21.262 58.617 1.00 43.92 3746 CB ALA 478 105.808 20.264 59.716 1.00 37.80 3747 C ALA 478 105.601 20.782 57.272 1.00 43.29 3748 0 ALA 478 106.312 20.127 56.509 1.00 44.64 3749 N LYS 479 104.346 21.116 56.981 1.00 45.34 3750 CA LYS 479 103.736 20.720 55.715 1.00 50.82 3751 CB LYS 479 102.214 20.847 55.762 1.00 57.75 3752 CG LYS 479 101.555 20.268 54.522 1.00 65.44 3753 CD LYS 479 100.167 20.814 54.286 1.00 68.93 3754 CE LYS 479 99.651 20.332 52.943 1.00 68.91 3755 NZ LYS 479 98.384 20.999 52.566 1.00 74.62 3756 C LYS 479 104.283 21.581 54.581 1.00 47.22 3757 0 LYS 479 104.451 21.109 53.455 1.00 50.00 3758 N PHE 480 104.526 22.854 54.878 1.00 43.15 3759 CA PHE 480 105.076 23.776 53.894 1.00 41.41 3760 CB PHE 480 105.089 25.204 54.443 1.00 41.63 3761 CG PHE 480 103.894 26.021 54.033 1.00 44.23 3762 CD1 PHE 480 102.638 25.432 53.905 1.00 41.42 3763 CD2 PHE 480 104.026 27.379 53.756 1.00 39.25 3764 CE1 PHE 480 101.535 26.182 53.503 1.00 36.23 3765 CE2 PHE 480 102.929 28.136 53.353 1.00 32.42 3766 CZ PHE 480 101.682 27.536 53.227 1.00 29.83 3767 C PHE 480 106.485 23.334 53.515 1.00 41.98 3768 0 PHE 480 106.881 23.434 52.353 1.00 37.95 3769 N GLN 481 107.229 22.824 54.495 1.00 41.79 3770 CA GLN 481 108.585 22.342 54.256 1.00 41.10 3771 CB GLN 481 109.236 21.868 55.559 1.00 39.98 3772 CG GLN 481 109.603 22.993 56.513 1.00 47.39 3773 CD GLN 481 110.507 24.034 55.870 1.00 56.58 3774 0E1 GLN 481 111.605 23.720 55.406 1.00 55.49 3775 NE2 GLN 481 110.042 25.279 55.834 1.00 58.30 3776 C GLN 481 108.553 21.204 53.245 1.00 38.69 3777 0 GLN 481 109.386 21.146 52.340 1.00 37.55 3778 N ASN 482 107.564 20.324 53.391 1.00 35.14 3779 CA ASN 482 107.394 19.189 52.491 1.00 35.59 3780 CB ASN 482 106.302 18.250 53.009 1.00 41.18 3781 CG ASN 482 106.647 17.642 54.355 1.00 52.28 3782 0D1 ASN 482 107.756 17.148 54.560 1.00 53.57 3783 ND2 ASN 482 105.697 17.678 55.282 1.00 61.08 3784 C ASN 482 107.057 19.657 51.081 1.00 32.00 3785 0 ASN 482 107.358 18.971 50.105 1.00 35.80 3786 N MET 483 106.421 20.822 50.981 1.00 30.00 3787 CA MET 483 106.063 21.391 49.687 1.00 29.42 3788 CB MET 483 105.092 22.562 49.855 1.00 33.61 3789 CG MET 483 103.693 22.173 50.303 1.00 33.22 3790 SD MET 483 102.589 23.605 50.374 1.00 34.18 3791 CE MET 483 102.294 23.881 48.638 1.00 31.57 3792 C MET 483 107.330 21.870 48.991 1.00 26.58 3793 0 MET 483 107.453 21.778 47.769 1.00 26.98 3794 N ALA 484 108.267 22.386 49.782 1.00 24.14 3795 CA ALA 484 109.539 22.874 49.261 1.00 20.18 3796 CB ALA 484 1 10.260 23.687 50.323 1.00 15.48 3797 C ALA 484 110.399 21.694 48.812 1.00 18.99 3798 0 ALA 484 111.070 21.762 47.777 1.00 18.13 3799 N GLU 485 110.360 20.610 49.587 1.00 15.88 3800 CA GLU 485 111.115 19.398 49.274 1.00 22.72 3801 CB GLU 485 110.965 18.367 50.391 1.00 26.33 3802 CG GLU 485 111.571 18.811 51.719 1.00 57.96 3803 CD GLU 485 111.355 17.814 52.853 1.00 66.33 3804 0E1 GLU 485 110.840 16.702 52.602 1.00 74.62 3805 0E2 GLU 485 111.704 18.149 54.006 1.00 72.14 3806 C GLU 485 110.625 18.806 47.962 1.00 19.07 3807 0 GLU 485 111.422 18.403 47.114 1.00 23.09 3808 N THR 486 109.306 18.768 47.802 1.00 18.34 3809 CA THR 486 108.680 18.247 46.594 1.00 13.68 3810 CB THR 486 107.132 18.239 46.724 1.00 19.42 3811 0G1 THR 486 106.740 17.320 47.753 1.00 18.34 3812 CG2 THR 486 106.474 17.832 45.409 1.00 7J3 3813 C THR 486 109.084 19.126 45.418 1.00 12.40 3814 0 THR 486 109.432 18.628 44.347 1.00 12.64 3815 N ALA 487 109.054 20.437 45.641 1.00 18.37 3816 CA ALA 487 109.420 21.406 44.618 1.00 14.12 3817 CB ALA 487 109.224 22.812 45.137 1.00 12.83 3818 C ALA 487 110.863 21.195 44.178 1.00 11.72 3819 0 ALA 487 111.182 21.312 42.993 1.00 14.71 3820 N TRP 488 111.731 20.860 45.128 1.00 11.21 3821 CA TRP 488 113.129 20.616 44.801 1.00 9.46 3822 CB TRP 488 113.985 20.541 46.061 1.00 2.00 3823 CG TRP 488 114.586 21.864 46.394 1.00 10.22 3824 CD2 TRP 488 115.535 22.596 45.602 1.00 8.75 3825 CE2 TRP 488 115.798 23.807 46.279 1.00 8.09 3826 CE3 TRP 488 116.186 22.345 44.384 1.00 8.76 3827 CD1 TRP 488 114.322 22.636 47.488 1.00 2.81 3828 NE1 TRP 488 115.045 23.807 47.425 1.00 14.28 3829 CZ2 TRP 488 116.686 24.768 45.780 1.00 4.43 3830 CZ3 TRP 488 117.072 23.301 43.885 1.00 8.98 3831 CH2 TRP 488 117.312 24.497 44.585 1.00 9.72 3832 C TRP 488 113.306 19.378 43.936 1.00 9.87 3833 0 TRP 488 114.112 19.380 43.005 1.00 11.24 3834 N LYS 489 112.526 18.335 44.214 1.00 7.93 3835 CA LYS 489 112.601 17.110 43.427 1.00 2.00 3836 CB LYS 489 111.815 15.987 44.096 1.00 7.82 3837 CG LYS 489 112.350 15.603 45.470 1.00 9.24 3838 CD LYS 489 111.550 14.471 46.069 1.00 2J4 3839 CE LYS 489 111.921 14.248 47.517 1.00 16.24 3840 NZ LYS 489 111.056 13.208 48.146 1.00 26.26 3841 C LYS 489 112.051 17.390 42.037 1.00 7.99 3842 0 LYS 489 112.480 16.784 41.055 1.00 11.24 3843 N ASP 490 111.115 18.333 41.960 1.00 9.24 3844 CA ASP 490 110.518 18.716 40.687 1.00 12.50 3845 CB ASP 490 109.234 19.514 40.901 1.00 15.83 3846 CG ASP 490 108.083 18.648 41.360 1.00 23.66 3847 OD1 ASP 490 107.949 17.509 40.856 1.00 20.17 3848 OD2 ASP 490 107.308 19.111 42.221 1.00 28.73 3849 C ASP 490 111.501 19.522 39.856 1.00 11.20 3850 0 ASP 490 111.519 19.409 38.629 1.00 17.78 3851 N ILE 491 112.308 20.345 40.523 1.00 16.49 3852 CA ILE 491 1 13.311 21.149 39.831 1.00 15.96 3853 CB ILE 491 113.973 22.183 40.766 1.00 14.10 3854 CG2 ILE 491 115.138 22.870 40.058 1.00 17.39 3855 CG1 ILE 491 112.938 23.221 41.209 1.00 20.61 3856 CD1 ILE 491 113.493 24.319 42.097 1.00 6.59 3857 C ILE 491 114.372 20.207 39.279 1.00 11.72 3858 0 ILE 491 114.802 20.342 38.132 1.00 18.27 3859 N ASN 492 114.744 19.217 40.084 1.00 9.30 3860 CA ASN 492 115.739 18.232 39.684 1.00 8.49 3861 CB ASN 492 116.078 17.320 40.866 1.00 8.53 3862 CG ASN 492 116.793 18.062 41.986 1.00 2.00 3863 0D1 ASN 492 117.444 19.081 41.756 1.00 2.00 3864 ND2 ASN 492 116.674 17.554 43.204 1.00 9.30 3865 C ASN 492 115.296 17.421 38.458 1.00 6.69 3866 0 ASN 492 116.120 17.067 37.618 1.00 15.10 3867 N GLU 493 113.994 17.157 38.345 1.00 11.11 3868 CA GLU 493 113.452 16.420 37.203 1.00 6.79 3869 CB GLU 493 112.036 15.929 37.490 1.00 14.43 3870 CG GLU 493 111.966 14.681 38.344 1.00 35.11 3871 CD GLU 493 110.554 14.143 38.504 1.00 39.54 3872 0E1 GLU 493 109.669 14.505 37.695 1.00 36.96 3873 0E2 GLU 493 110.335 13.345 39.441 1.00 44.74 3874 C GLU 493 113.420 17.284 35.947 1.00 15.20 3875 0 GLU 493 113.539 16.777 34.828 1.00 19.79 3876 N GLY 494 113.234 18.588 36.140 1.00 15.92 3877 CA GLY 494 113.176 19.512 35.021 1.00 13.61 3878 C GLY 494 114.488 19.613 34.276 1.00 18.91 3879 0 GLY 494 114.507 19.822 33.061 1.00 23.19 3880 N LEU 495 115.583 19.437 35.008 1.00 18.93 3881 CA LEU 495 116.927 19.508 34.445 1.00 18.10 3882 CB LEU 495 117.955 19.662 35.571 1.00 12.15 3883 CG LEU 495 117.764 20.846 36.527 1.00 11.37 3884 CD1 LEU 495 118.788 20.781 37.650 1.00 2.00 3885 CD2 LEU 495 117.866 22.164 35.771 1.00 6J4 3886 C LEU 495 117.279 18.289 33.593 1.00 21.97 3887 0 LEU 495 118.146 18.366 32.717 1.00 20.13 3888 N LEU 496 116.602 17.171 33.849 1.00 21.91 3889 CA LEU 496 116.851 15.931 33.118 1.00 15.41 3890 CB LEU 496 116.126 14.760 33.784 1.00 8.37 3891 CG LEU 496 116.604 14.435 35.204 1.00 10.05 3892 CD1 LEU 496 115.819 13.269 35.769 1.00 2.00 3893 CD2 LEU 496 118.094 14.121 35.206 1.00 5.54 3894 C LEU 496 116.492 16.017 31.641 1.00 14.28 3895 0 LEU 496 1 15.471 16.593 31.269 1.00 19.94 3896 N ARG 497 117.360 15.454 30.808 1.00 16.05 3897 CA ARG 497 117.184 15.456 29.359 1.00 18.50 3898 CB ARG 497 1 18.516 15.107 28.682 1.00 19.50 3899 CG ARG 497 119.665 16.035 29.066 1.00 28.42 3900 CD ARG 497 121.024 15.363 28.908 1.00 24.39 3901 NE ARG 497 121.803 15.905 27.797 1.00 27.16 3902 CZ ARG 497 122.978 16.517 27.927 1.00 26.59 3903 NH1 ARG 497 123.525 16.677 29.125 1.00 14.53 3904 NH2 ARG 497 123.618 16.955 26.850 1.00 32.59 3905 C ARG 497 116.099 14.471 28.922 1.00 23.25 3906 0 ARG 497 115.890 13.441 29.566 1.00 25.86 3907 N PRO 498 115.369 14.793 27.838 1.00 22.25 3908 CD PRO 498 114.524 13.808 27.150 1.00 25.52 3909 CA PRO 498 115.491 16.003 27.017 1.00 25.55 3910 CB PRO 498 114.781 15.612 25.715 1.00 17.40 3911 CG PRO 498 114.819 14.122 25.715 1.00 25.69 3912 C PRO 498 114.785 17.192 27.662 1.00 28.98 3913 0 PRO 498 113.609 17.104 28.021 1.00 33.06 3914 N THR 499 115.506 18.299 27.804 1.00 24.14 3915 CA THR 499 114.949 19.511 28.391 1.00 15.92 3916 CB THR 499 116.070 20.473 28.835 1.00 16.49 3917 OG1 THR 499 116.946 20.735 27.730 1.00 6.47 3918 CG2 THR 499 116.870 19.862 29.983 1.00 10.26 3919 C THR 499 114.043 20.205 27.374 1.00 19.26 3920 0 THR 499 114.329 20.205 26.174 1.00 30.87 3921 N PRO 500 112.919 20.776 27.836 1.00 16.60 3922 CD PRO 500 112.472 20.794 29.239 1.00 9.65 3923 CA PRO 500 111.959 21.473 26.971 1.00 19.15 3924 CB PRO 500 110.870 21.907 27.954 1.00 16.41 3925 CG PRO 500 111.599 22.004 29.267 1.00 14.64 3926 C PRO 500 112.569 22.656 26.213 1.00 26.43 3927 0 PRO 500 112.131 23.001 25.111 1.00 28.97 3928 N VAL 501 113.580 23.266 26.824 1.00 27.74 3929 CA VAL 501 114.317 24.393 26.253 1.00 27.33 3930 CB VAL 501 113.874 25.749 26.867 1.00 25.49 3931 CG1 VAL 501 112.495 26.136 26.367 1.00 27.78 3932 CG2 VAL 501 113.880 25.675 28.386 1.00 25.11 3933 C VAL 501 115.792 24.149 26.572 1.00 27.50 3934 0 VAL 501 116.118 23.190 27.268 1.00 34.26 3935 N SER 502 116.685 24.991 26.059 1.00 27.56 3936 CA SER 502 118.111 24.821 26.336 1.00 26.62 3937 CB SER 502 118.942 25.802 25.513 1.00 31.78 3938 OG SER 502 118.853 25.497 24.133 1.00 55.84 3939 C SER 502 118.407 25.000 27.823 1.00 30.86 3940 0 SER 502 117.759 25.801 28.505 1.00 31.25 3941 N THR 503 119.387 24.247 28.318 1.00 31.45 3942 CA THR 503 119.785 24.296 29.726 1.00 32.20 3943 CB THR 503 121.008 23.389 29.989 1.00 33.25 3944 OG1 THR 503 120.732 22.067 29.511 1.00 46.44 3945 CG2 THR 503 121.316 23.320 31.478 1.00 33.35 3946 C THR 503 120.119 25.722 30.162 1.00 25.43 3947 0 THR 503 119.955 26.087 31.331 1.00 17.17 3948 N GLU 504 120.569 26.522 29.200 1.00 21.60 3949 CA GLU 504 120.931 27.914 29.433 1.00 21.35 3950 CB GLU 504 121.355 28.549 28.104 1.00 16.54 3951 CG GLU 504 121.779 30.009 28.189 1.00 26.78 3952 CD GLU 504 122.043 30.642 26.825 1.00 35.29 3953 OE1 GLU 504 121.832 29.971 25.789 1.00 38.25 3954 OE2 GLU 504 122.460 31.821 26.793 1.00 34.16 3955 C GLU 504 119.747 28.680 30.028 1.00 20.56 3956 O GLU 504 119.924 29.595 30.837 1.00 14.15 3957 N PHE 505 118.541 28.251 29.665 1.00 18.81 3958 CA PHE 505 117.320 28.896 30.126 1.00 15.87 3959 CB PHE 505 116.330 28.995 28.966 1.00 13.36 3960 CG PHE 505 116.892 29.710 27.769 1.00 20.57 3961 CD1 PHE 505 117.193 29.013 26.602 1.00 24.10 3962 CD2 PHE 505 117.183 31.070 27.831 1.00 20.76 3963 CE1 PHE 505 117.782 29.658 25.517 1.00 19.64 3964 CE2 PHE 505 117.772 31.724 26.754 1.00 25.52 3965 CZ PHE 505 118.072 31.015 25.595 1.00 26.72 3966 C PHE 505 116.675 28.274 31.358 1.00 15.98 3967 O PHE 505 115.703 28.808 31.886 1.00 16.03 3968 N LEU 506 117.232 27.162 31.829 1.00 16.47 3969 CA LEU 506 116.712 26.492 33.018 1.00 10.03 3970 CB LEU 506 116.774 24.972 32.856 1.00 19.45 3971 CG LEU 506 115.962 24.330 31.729 1.00 25.84 3972 CD1 LEU 506 116.268 22.852 31.690 1.00 29.46 3973 CD2 LEU 506 114.473 24.557 31.928 1.00 24.50 3974 C LEU 506 117.503 26.895 34.254 1.00 11.68 3975 O LEU 506 116.967 26.926 35.365 1.00 15.18 3976 N THR 507 118.781 27.210 34.054 1.00 10.27 3977 CA THR 507 119.662 27.601 35.151 1.00 7.47 3978 CB THR 507 121.108 27.838 34.671 1.00 10.86 3979 OG1 THR 507 121.492 26.798 33.762 1.00 20.06 3980 CG2 THR 507 122.058 27.824 35.852 1.00 2.66 3981 C THR 507 119.181 28.824 35.936 1.00 10.65 3982 O THR 507 119.229 28.821 37.167 1.00 14.58 3983 N PRO 508 118.718 29.887 35.242 1.00 8.73 3984 CD PRO 508 118.680 30.110 33.784 1.00 7.34 3985 CA PRO 508 118.244 31.080 35.956 1.00 5.70 3986 CB PRO 508 117.717 31.959 34.826 1.00 8.88 3987 CG PRO 508 118.630 31.616 33.688 1.00 2.00 3988 C PRO 508 117.141 30.742 36.955 1.00 16.13 3989 O PRO 508 117.109 31.282 38.064 1.00 19.06 3990 N ILE 509 116.254 29.831 36.555 1.00 12.82 3991 CA ILE 509 115.149 29.390 37.401 1.00 7.60 3992 CB ILE 509 114.201 28.444 36.635 1.00 13.85 3993 CG2 ILE 509 113.160 27.865 37.577 1.00 3.89 3994 CG1 ILE 509 1 13.533 29.189 35.477 1.00 8.63 3995 CD1 ILE 509 112.681 28.301 34.597 1.00 16.09 3996 C ILE 509 115.723 28.657 38.604 1.00 10.09 3997 0 ILE 509 115.320 28.906 39.744 1.00 13.81 3998 N LEU 510 116.670 27.759 38.335 1.00 10.69 3999 CA LEU 510 1 17.347 26.983 39.376 1.00 8.28 4000 CB LEU 510 118.381 26.047 38.738 1.00 13.30 4001 CG LEU 510 119.429 25.349 39.612 1.00 10.83 4002 CD1 LEU 510 118.781 24.553 40.736 1.00 9.01 4003 CD2 LEU 510 120.267 24.444 38.728 1.00 2.40 4004 C LEU 510 118.033 27.927 40.358 1.00 4J3 4005 0 LEU 510 117.860 27.806 41.570 1.00 2.43 4006 N ASN 511 118.778 28.890 39.819 1.00 12.14 4007 CA ASN 511 119.487 29.875 40.627 1.00 11.57 4008 CB ASN 511 120.347 30.773 39.743 1.00 12.88 4009 CG ASN 511 121.567 30.054 39.208 1.00 18.35 4010 OD1 ASN 511 122.137 29.196 39.881 1.00 15.86 4011 ND2 ASN 511 121.972 30.396 37.991 1.00 27.20 4012 C ASN 511 118.553 30.710 41.487 1.00 11.23 4013 0 ASN 511 118.883 31.018 42.634 1.00 9.07 4014 N LEU 512 117.387 31.058 40.941 1.00 13.33 4015 CA LEU 512 116.393 31.837 41.683 1.00 8.79 4016 CB LEU 512 115.168 32.131 40.814 1.00 13.75 4017 CG LEU 512 115.255 33.332 39.865 1.00 12.09 4018 CD1 LEU 512 114.100 33.306 38.884 1.00 2.00 4019 CD2 LEU 512 115.256 34.623 40.667 1.00 2.00 4020 C LEU 512 115.975 31.083 42.940 1.00 10.14 4021 0 LEU 512 115.810 31.682 44.002 1.00 13.04 4022 N ALA 513 115.836 29.764 42.819 1.00 10.74 4023 CA ALA 513 115.464 28.916 43.951 1.00 12.16 4024 CB ALA 513 115.097 27.523 43.464 1.00 14.93 4025 C ALA 513 116.621 28.842 44.947 1.00 13.31 4026 0 ALA 513 116.408 28.757 46.157 1.00 9.13 4027 N ARG 514 117.846 28.879 44.424 1.00 19.25 4028 CA ARG 514 119.048 28.834 45.253 1.00 17.40 4029 CB ARG 514 120.294 28.644 44.382 1.00 14.56 4030 CG ARG 514 120.493 27.229 43.863 1.00 4.10 4031 CD ARG 514 121.602 27.170 42.823 1.00 9.06 4032 NE ARG 514 121.943 25.793 42.471 1.00 17.13 4033 CZ ARG 514 122.653 25.434 41.403 1.00 16.59 4034 NH1 ARG 514 123.107 26.346 40.554 1.00 8.47 4035 NH2 ARG 514 122.929 24.154 41.197 1.00 15.58 4036 C ARG 514 119.190 30.106 46.084 1.00 13.80 4037 0 ARG 514 119.522 30.051 47.270 1.00 10.51 4038 N ILE 515 118.901 31.247 45.466 1.00 15.59 4039 CA ILE 515 119.011 32.535 46.147 1.00 20.36 4040 CB ILE 515 118.764 33.718 45.194 1.00 12.70 4041 CG2 ILE 515 119.221 35.007 45.851 1.00 25.50 4042 CG1 ILE 515 119.567 33.534 43.910 1.00 19.52 4043 CD1 ILE 515 119.220 34.523 42.828 1.00 29.86 4044 C ILE 515 1 18.085 32.672 47.353 1.00 17.44 4045 0 ILE 515 118.477 33.257 48.359 1.00 19.69 4046 N VAL 516 116.868 32.136 47.258 1.00 21.26 4047 CA VAL 516 115.915 32.218 48.369 1.00 23.09 4048 CB VAL 516 1 14.504 31.679 48.008 1.00 32.21 4049 CG1 VAL 516 1 13.444 32.441 48.787 1.00 27.43 4050 CG2 VAL 516 114.244 31.755 46.526 1.00 29.34 4051 C VAL 516 116.424 31.382 49.535 1.00 20.14 4052 0 VAL 516 116.429 31.835 50.681 1.00 22.46 4053 N GGLLUU 517 1 16.833 30.154 49.229 1.00 21.26 4054 CA GGLLUU 517 117.352 29.230 50.231 1.00 23.87 4055 CB GGLLUU 517 117.859 27.949 49.555 1.00 24.13 4056 CG GGLLUU 517 116.765 27.008 49.049 1.00 27.64 4057 CD GGLLUU 517 116.153 26.132 50.143 1.00 36.07 4058 0E1 GGLLUU 517 116.480 26.314 51.336 1.00 40.38 4059 0E2 GGLLUU 517 115.338 25.248 49.804 1.00 38.38 4060 C GGLLUU 517 118.484 29.872 51.024 1.00 25.33 4061 0 GGLLUU 517 118.488 29.840 52.255 1.00 28.96 4062 N VVAALL 518 119.411 30.492 50.297 1.00 22.43 4063 CA VVAALL 518 120.577 31.156 50.874 1.00 22.95 4064 CB VVAALL 518 121.605 31.482 49.762 1.00 24.42 4065 CG1 VVAALL 518 122.767 32.289 50.313 1.00 23.12 4066 CG2 VAL 518 122.105 30.194 49.125 1.00 20.43 4067 C VAL 518 120.239 32.436 51.649 1.00 24.42 4068 0 V VAALL 518 120.850 32.725 52.683 1.00 23.34 4069 N TTHHRR 519 119.267 33.192 51.145 1.00 22.60 4070 CA TTHHRR 519 118.846 34.443 51.769 1.00 20.24 4071 CB TTHHRR 519 118.044 35.305 50.773 1.00 23.46 4072 0G1 TTHHRR 519 118.872 35.615 49.646 1.00 23.28 4073 CG2 TTHHRR 519 117.597 36.601 51.410 1.00 22.46 4074 C TTHHRR 519 118.051 34.232 53.058 1.00 25.34 4075 0 TTHHRR 519 118.164 35.020 54.000 1.00 24.48 4076 N TTYYRR 520 117.261 33.162 53.105 1.00 30.17 4077 CA TTYYRR 520 116.461 32.848 54.290 1.00 34.43 4078 CB TTYYRR 520 115.017 32.528 53.892 1.00 35.49 4079 CG TTYYRR 520 114.238 33.696 53.330 1.00 32.60 4080 CD1 TTYYRR 520 114.481 34.171 52.041 1.00 27.24 4081 CE1 TTYYRR 520 113.758 35.242 51.520 1.00 34.38 4082 CD2 TYR 520 113.247 34.321 54.087 1.00 30.57 4083 CE2 TYR 520 112.516 35.392 53.577 1.00 22.83 4084 CZ T TYYRR 520 112.777 35.848 52.294 1.00 34.91 4085 OH T TYYRR 520 112.070 36.916 51.787 1.00 38.85 4086 C T TYYRR 520 117.047 31.663 55.058 1.00 37.02 4087 0 T TYYRR 520 116.321 30.937 55.740 1.00 41.01 4088 N I ILLEE 521 118.361 31.483 54.956 1.00 39.45 4089 CA I ILLEE 521 119.048 30.380 55.621 1.00 41.53 4090 CB I ILLEE 521 120.561 30.363 55.251 1.00 34.97 4091 CG2 I ILLEE 521 121.263 31.607 55.775 1.00 33.59 4092 CG1 I ILLEE 521 121.228 29.087 55.770 1.00 32.90 4093 CD1 I ILLEE 521 122.620 28.865 55.224 1.00 16.56 4094 C ILE 521 1 18.841 30.384 57.140 1.00 51.61 4095 0 ILE 521 118.649 29.329 57.750 1.00 55.56 4096 N HIS 522 1 18.840 31.573 57.737 1.00 57.98 4097 CA HIS 522 1 18.634 31.715 59.176 1.00 63.52 4098 CB HIS 522 119.500 32.851 59.730 1.00 73.38 4099 CG HIS 522 120.971 32.581 59.659 1.00 84.65 4100 CD2 HIS 522 122.020 33.405 59.421 1.00 85.52 4101 ND1 HIS 522 121.508 31.324 59.848 1.00 87.86 4102 CE1 HIS 522 122.822 31.386 59.729 1.00 88.53 4103 NE2 HIS 522 123.158 32.637 59.470 1.00 88.81 4104 C HIS 522 117.159 31.977 59.482 1.00 63.87 4105 0 HIS 522 116.816 32.500 60.546 1.00 62.90 4106 N ASN 523 116.300 31.606 58.534 1.00 61.66 4107 CA ASN 523 114.850 31.771 58.635 1.00 60.61 4108 CB ASN 523 114.273 30.822 59.691 1.00 60.04 4109 CG ASN 523 112.807 30.509 59.453 1.00 59.80 4110 OD1 ASN 523 112.388 30.266 58.319 1.00 62.26 4111 ND2 ASN 523 112.021 30.510 60.522 1.00 59.58 4112 C ASN 523 114.434 33.220 58.910 1.00 60.32 4113 0 ASN 523 113.481 33.486 59.649 1.00 55.47 4114 N LEU 524 115.162 34.149 58.295 1.00 61.14 4115 CA LEU 524 114.905 35.577 58.436 1.00 59.79 4116 CB LEU 524 115.935 36.223 59.371 1.00 62.62 4117 CG LEU 524 115.945 35.764 60.835 1.00 65.24 4118 CD1 LEU 524 117.147 36.347 61.567 1.00 65.21 4119 CD2 LEU 524 114.642 36.163 61.521 1.00 62.62 4120 C LEU 524 114.966 36.235 57.065 1.00 59.79 4121 0 LEU 524 115.721 35.800 56.189 1.00 56.91 4122 N ASP 525 114.156 37.274 56.882 1.00 62.76 4123 CA ASP 525 114.100 38.006 55.620 1.00 59.59 4124 CB ASP 525 112.987 39.055 55.670 1.00 58.10 4125 CG ASP 525 112.641 39.608 54.302 1.00 60.27 4126 0D1 ASP 525 113.331 39.276 53.315 1.00 58.07 4127 OD2 ASP 525 111.660 40.374 54.210 1.00 64.63 4128 C ASP 525 115.448 38.668 55.332 1.00 59.32 4129 0 ASP 525 115.753 39.740 55.854 1.00 63.36 4130 N GLY 526 116.239 38.028 54.478 1.00 58.65 4131 CA GLY 526 117.557 38.536 54.149 1.00 55.69 4132 C GLY 526 117.641 39.797 53.316 1.00 53.62 4133 0 GLY 526 118.648 40.502 53.372 1.00 60.05 4134 N TYR 527 116.607 40.085 52.534 1.00 51.88 4135 CA TYR 527 116.617 41.285 51.702 1.00 55.73 4136 CB TYR 527 115.648 41.119 50.545 1.00 55.31 4137 CG TYR 527 115.562 42.295 49.598 1.00 57.45 4138 CD1 TYR 527 116.330 42.336 48.433 1.00 58.75 4139 CE1 TYR 527 116.193 43.375 47.518 1.00 59.49 4140 CD2 TYR 527 114.656 43.332 49.824 1.00 58.17 4141 CE2 TYR 527 114.511 44.373 48.917 1.00 56.67 4142 CZ TYR 527 115.282 44.388 47.767 1.00 57.63 4143 OH TYR 527 115.159 45.420 46.868 1.00 55.43 4144 C TYR 527 116.266 42.524 52.517 1.00 58.54 4145 0 TYR 527 116.862 43.593 52.342 1.00 58.64 4146 N THR 528 115.271 42.383 53.386 1.00 59.24 4147 CA THR 528 114.855 43.486 54.238 1.00 59.20 4148 CB THR 528 113.447 43.253 54.836 1.00 54.20 4149 OG1 THR 528 112.504 43.053 53.776 1.00 47.41 4150 CG2 THR 528 113.010 44.458 55.655 1.00 54.59 4151 C THR 528 115.887 43.653 55.356 1.00 60.28 4 4115522 0 0 T THHRR 528 116.168 44.773 55.787 1.00 63.64 4153 N HIS 529 116.464 42.533 55.792 1.00 61.45 4154 CA HIS 529 117.484 42.512 56.842 1.00 66.52 4155 CB HIS 529 116.984 41.721 58.060 1.00 66.73 4156 CG HIS 529 115.652 42.169 58.576 1.00 71.41 4157 CD2 HIS 529 115.119 43.407 58.721 1.00 72.13 4158 ND1 HIS 529 114.688 41.286 59.010 1.00 74.46 4159 CE1 HIS 529 113.618 41.958 59.398 1.00 72.55 4160 NE2 HIS 529 113.856 43.248 59.232 1.00 70.77 4161 C HIS 529 118.743 41.844 56.273 1.00 66.01 4162 0 HIS 529 119.005 40.665 56.528 1.00 68.54 4163 N PRO 530 119.540 42.598 55.492 1.00 63.94 4164 CD PRO 530 119.254 43.981 55.082 1.00 59.34 4165 CA PRO 530 120.778 42.128 54.856 1.00 66.66 4166 CB PRO 530 121.137 43.284 53.914 1.00 62.98 4167 CG PRO 530 119.837 44.009 53.711 1.00 59.02 4168 C PRO 530 121.952 41.819 55.784 1.00 70.87 4169 0 PRO 530 122.567 40.757 55.682 1.00 73.58 4170 N GLU 531 122.248 42.762 56.676 1.00 73.21 4171 CA GLU 531 123.365 42.683 57.621 1.00 73.20 4172 CB GLU 531 123.107 43.597 58.822 1.00 75.84 4173 CG GLU 531 124.335 43.811 59.703 1.00 84.33 4174 CD GLU 531 124.108 44.832 60.799 1.00 87.41 4175 0E1 GLU 531 123.904 46.021 60.474 1.00 95.89 4176 0E2 GLU 531 124.142 44.446 61.986 1.00 83.48 4177 C GLU 531 123.843 41.312 58.106 1.00 71.16 4178 0 GLU 531 125.042 41.026 58.066 1.00 69.83 4179 N GLU 532 122.923 40.470 58.563 1.00 69.84 4180 CA GLU 532 123.299 39.151 59.064 1.00 69.95 4181 CB GLU 532 122.239 38.621 60.028 1.00 76.12 4182 CG GLU 532 122.200 39.350 61.360 1.00 90.10 4183 CD GLU 532 121.231 38.719 62.343 1.00 99.66 4184 0E1 GLU 532 121.294 37.485 62.540 1.00 100.00 4185 0E2 GLU 532 120.407 39.460 62.922 1.00 100.00 4186 C GLU 532 123.601 38.095 58.006 1.00 65.98 4187 0 GLU 532 124.484 37.257 58.202 1.00 65.68 4188 N VAL 533 122.878 38.136 56.891 1.00 60.94 4189 CA VAL 533 123.071 37.152 55.829 1.00 51.25 4190 CB VAL 533 121.727 36.491 55.419 1.00 57.84 4191 CG1 VAL 533 121.983 35.305 54.492 1.00 49.96 4192 CG2 VAL 533 120.942 36.054 56.655 1.00 58.45 4193 C VAL 533 123.741 37.704 54.574 1.00 44.33 4194 0 VAL 533 124.834 37.270 54.208 1.00 42.16 4195 N LEU 534 123.085 38.662 53.925 1.00 37.63 4196 CA LEU 534 123.590 39.249 52.687 1.00 27.92 4197 CB LEU 534 122.499 40.068 52.002 1.00 24.48 4198 CG LEU 534 121.258 39.299 51.554 1.00 25.70 4199 CD1 LEU 534 120.395 40.207 50.696 1.00 29.78 4200 CD2 LEU 534 121.657 38.064 50.769 1.00 19.34 4201 C LEU 534 124.864 40.076 52.770 1.00 29.24 4202 0 LEU 534 125.661 40.069 51.834 1.00 31.85 4203 N LYS 535 125.053 40.793 53.875 1.00 30.62 4204 CA LYS 535 126.239 41.632 54.047 1.00 30.24 4205 CB LYS 535 126.251 42.276 55.439 1.00 33.69 4206 CG LYS 535 127.412 43.232 55.692 1.00 38.92 4207 CD LYS 535 127.429 43.699 57.142 1.00 43.85 4208 CE LYS 535 128.605 44.617 57.425 1.00 46.39 4209 NZ LYS 535 128.657 45.016 58.861 1.00 46.21 4210 C LYS 535 127.548 40.881 53.784 1.00 30.84 4211 0 LYS 535 128.328 41.286 52.918 1.00 28.96 4212 N PRO 536 127.790 39.759 54.495 1.00 26.98 4213 CD PRO 536 126.965 39.148 55.554 1.00 30.04 4214 CA PRO 536 129.018 38.982 54.302 1.00 22.09 4215 CB PRO 536 128.796 37.772 55.206 1.00 22.33 4216 CG PRO 536 127.975 38.330 56.312 1.00 25.59 4217 C PRO 536 129.213 38.551 52.853 1.00 23.63 4218 0 PRO 536 130.313 38.660 52.315 1.00 34.37 4219 N HIS 537 128.137 38.082 52.226 1.00 21.41 4220 CA HIS 537 128.180 37.635 50.836 1.00 16.74 4221 CB HIS 537 126.812 37.108 50.393 1.00 17.36 4222 CG HIS 537 126.392 35.849 51.086 1.00 26.82 4223 CD2 HIS 537 125.171 35.406 51.467 1.00 19.54 4224 ND1 HIS 537 127.289 34.872 51.465 1.00 20.86 4225 CE1 HIS 537 126.638 33.883 52.050 1.00 21.91 4226 NE2 HIS 537 125.351 34.182 52.064 1.00 18.99 4227 C HIS 537 128.611 38.757 49.910 1.00 19.57 4228 0 HIS 537 129.477 38.569 49.060 1.00 24.18 4229 N ILE 538 128.003 39.927 50.091 1.00 25.84 4230 CA ILE 538 128.307 41.101 49.279 1.00 25.72 4231 CB ILE 538 127.331 42.262 49.600 1.00 25.90 4232 CG2 ILE 538 127.739 43.536 48.856 1.00 21.31 4233 CG1 ILE 538 125.905 41.849 49.219 1.00 14.44 4234 CD1 ILE 538 124.847 42.872 49.559 1.00 19.77 4235 C ILE 538 129.760 41.545 49.467 1.00 24.83 4236 0 ILE 538 130.419 41.957 48.510 1.00 17.63 4237 N ILE 539 130.255 41.440 50.698 1.00 19.39 4238 CA ILE 539 131.632 41.809 51.002 1.00 25.84 4239 CB ILE 539 131.882 41.864 52.532 1.00 31.48 4240 CG2 ILE 539 133.375 41.923 52.835 1.00 28.38 4241 CG1 ILE 539 131.172 43.078 53.137 1.00 26.00 4242 CD1 ILE 539 131.381 43.224 54.633 1.00 28.00 4243 C ILE 539 132.598 40.819 50.355 1.00 24.71 4244 0 ILE 539 133.587 41.218 49.742 1.00 30.21 4245 N ASN 540 132.286 39.531 50.461 1.00 22.80 4246 CA ASN 540 133.132 38.487 49.892 1.00 16.68 4247 CB ASN 540 132.802 37.135 50.525 1.00 17.40 4248 CG ASN 540 133.009 37.126 52.032 1.00 26.52 4249 OD1 ASN 540 132.357 36.371 52.755 1.00 29.84 4250 ND2 ASN 540 133.918 37.969 52.511 1.00 25.48 4251 C ASN 540 133.039 38.386 48.371 1.00 16.85 4252 0 ASN 540 133.933 37.832 47.733 1.00 18.60 4253 N LEU 541 131.979 38.944 47.789 1.00 16.65 4254 CA LEU 541 131.791 38.889 46.340 1.00 19.54 4255 CB LEU 541 130.393 38.360 46.001 1.00 16.13 4256 CG LEU 541 130.003 36.954 46.463 1.00 16.63 4257 CD1 LEU 541 128.588 36.662 46.017 1.00 9.71 4258 CD2 LEU 541 130.960 35.919 45.901 1.00 11.40 4259 C LEU 541 132.016 40.198 45.585 1.00 22.24 4260 0 LEU 541 132.528 40.186 44.464 1.00 22.51 4261 N LEU 542 131.642 41.321 46.192 1.00 23.86 4262 CA LEU 542 131.774 42.619 45.531 1.00 27.26 4263 CB LEU 542 130.392 43.266 45.412 1.00 30.85 4264 CG LEU 542 129.374 42.454 44.608 1.00 33.63 4265 CD1 LEU 542 127.960 42.968 44.844 1.00 33.98 4266 CD2 LEU 542 129.741 42.505 43.137 1.00 30.60 4267 C LEU 542 132.770 43.621 46.124 1.00 30.35 4268 0 LEU 542 133.102 44.615 45.474 1.00 32.15 4269 N VAL 543 133.234 43.373 47.348 1.00 20.35 4270 CA VAL 543 134.192 44.263 48.008 1.00 17.15 4271 CB VAL 543 133.758 44.564 49.466 1.00 22.13 4272 CG1 VAL 543 134.761 45.485 50.147 1.00 18.99 4273 CG2 VAL 543 132.369 45.184 49.485 1.00 25.56 4274 C VAL 543 135.608 43.670 48.012 1.00 20.12 4275 0 VAL 543 136.484 44.106 47.259 1.00 14.30 4276 N ASP 544 135.813 42.667 48.860 1.00 22.55 4277 CA ASP 544 137.102 41.999 48.992 1.00 17.64 4278 CB ASP 544 137.183 41.246 50.326 1.00 10.56 4279 CG ASP 544 137.103 42.164 51.532 1.00 22.81 4280 0D1 ASP 544 136.839 41.648 52.639 1.00 23.90 4281 0D2 ASP 544 137.313 43.390 51.385 1.00 33.46 4282 C ASP 544 137.389 41.018 47.868 1.00 18.71 4283 0 ASP 544 136.548 40.191 47.517 1.00 20.02 4284 N SER 545 138.590 41.116 47.310 1.00 23.60 4285 CA SER 545 139.022 40.215 46.253 1.00 27.74 4286 CB SER 545 139.900 40.957 45.243 1.00 27.70 4287 OG SER 545 141.043 41.512 45.871 1.00 32.50 4288 C SER 545 139.823 39.098 46.920 1.00 31.23 4289 0 SER 545 140.409 39.303 47.987 1.00 32.16 4290 N ILE 546 139.816 37.913 46.317 1.00 30.36 4291 CA ILE 546 140.558 36.780 46.863 1.00 33.30 4292 CB ILE 546 140.281 35.475 46.072 1.00 33.46 4293 CG2 ILE 546 141.051 34.310 46.686 1.00 27.25 4294 CG1 ILE 546 138.783 35.165 46.072 1.00 27.20 4295 CD1 ILE 546 138.418 33.915 45.319 1.00 23.76 4296 C ILE 546 142.041 37.1 13 46.765 1.00 35.94 4297 0 ILE 546 142.559 37.332 45.668 1.00 34.27 4298 N LYS 547 142.708 37.200 47.913 1.00 37.96 4299 CA LYS 547 144.131 37.518 47.929 1.00 45.36 4300 CB LYS 547 144.581 37.989 49.318 1.00 53.18 4301 CG LYS 547 144.193 37.086 50.476 1.00 62.91 4302 CD LYS 547 144.627 37.709 51.796 1.00 73.57 4303 CE LYS 547 144.241 36.839 52.982 1.00 81.58 4304 NZ LYS 547 144.683 37.440 54.274 1.00 85.95 4305 C LYS 547 144.986 36.359 47.425 1.00 43.05 4306 0 LYS 547 144.897 35.236 47.921 1.00 34.62 4307 N ILE 548 145.778 36.648 46.396 1.00 45.90 4308 CA ILE 548 146.656 35.666 45.771 1.00 45.52 4309 CB ILE 548 147.148 36.170 44.394 1.00 41.81 4310 CG2 ILE 548 147.927 35.073 43.679 1.00 45.55 4311 CG1 ILE 548 145.951 36.603 43.540 1.00 39.14 4312 CD1 I ILLEE 548 146.327 37.269 42.238 1.00 45.90 4313 C I ILLEE 548 147.856 35.342 46.659 1.00 48.55 4314 OT1 I ILLEE 548 148.019 34.153 47.005 1.00 46.58 4315 OT2 I ILLEE 548 148.606 36.278 47.012 1.00 59.90 4316 OH2 W WAATT 601 109.544 21.898 33.684 1.00 2.00 4317 OH2 W WAATT 602 132.108 38.577 42.342 1.00 3.74 4318 OH2 W WAATT 603 121.652 22.556 52.348 1.00 5.90 4319 OH2 W WAATT 604 136.076 10.222 44.594 1.00 31.07 4320 OH2 W WAATT 605 131.497 21.852 51.678 1.00 7.22 4321 OH2 W WAATT 606 128.656 14.200 45.316 1.00 17.90 4322 OH2 W WAATT 607 124.677 19.198 47.081 1.00 15.60 4323 OH2 W WAATT 608 125.455 29.812 49.014 1.00 8.48 4324 OH2 W WAATT 609 105.474 36.871 39.547 1.00 9.05 4325 OH2 W WAATT 610 133.536 36.915 40.513 1.00 19.37 4326 OH2 W WAATT 611 126.730 22.375 41.980 1.00 17.96 4327 OH2 W WAATT 612 133.379 23.457 50.388 1.00 16.43 4328 OH2 W WAATT 613 136.836 31.698 39.273 1.00 23.48 4329 OH2 W WAATT 614 130.615 20.278 41.368 1.00 11.16 4330 OH2 W WAATT 615 127.633 29.682 51.807 1.00 16.49 4331 OH2 W WAATT 616 100.533 31.281 26.832 1.00 34.28 4332 OH2 WAT 617 121.692 21.167 34.150 1.00 25.91 4333 OH2 WAT 618 131.226 32.257 50.439 1.00 34.81 4334 OH2 WAT 619 88.365 35.120 57.147 1.00 33.73 4335 OH2 WAT 620 1 18.147 18.317 26.341 1.00 21.70 4336 OH2 WAT 621 113.190 8.087 35.703 1.00 36.62 4337 OH2 W WAATT 622 125.312 30.072 37.791 1.00 30.00 4338 OH2 WWAATT 623 92.432 24.852 50.099 1.00 25.65 4339 OH2 WAT 624 108.974 15.165 49.075 1.00 21.10 4340 OH2 WAT 625 135.431 14.884 45.393 1.00 46.74 4341 OH2 W WAATT 626 115.012 4.805 43.826 1.00 30.43 4342 OH2 WWAATT 627 88.415 44.463 58.820 1.00 30.86 4343 OH2 WAT 628 125.976 25.755 43.265 1.00 27.75 4344 OH2 WWAATT 629 117.921 5.153 51.682 1.00 34.87 4345 OH2 WWAATT 630 91.157 43.104 44.532 1.00 27.09 4346 OH2 WWAATT 631 114.902 63.428 42.828 1.00 30.49 4347 OH2 WWAATT 632 99.150 43.135 52.476 1.00 17.32 4348 OH2 WWAATT 633 116.849 14.286 50.256 1.00 20.41 4349 OH2 WWAATT 634 136.092 41.410 33.663 1.00 26.72 4350 OH2 WAT 635 104.683 23.377 25.808 1.00 36.55 4351 OH2 WAT 636 133.163 25.808 57.616 1.00 29.75 4352 OH2 W WAATT 637 130.650 30.337 40.643 1.00 11.08 4353 OH2 WWAATT 638 141.018 40.362 50.563 1.00 27.14 4354 0H2 WWAATT 639 126.744 19.348 30.510 1.00 20.69 4355 OH2 WWAATT 640 99.257 26.859 66.394 1.00 32.76 4356 OH2 WWAATT 641 107.042 13.044 38.812 1.00 37.53 4357 OH2 WWAATT 642 111.411 17.702 31.576 1.00 25.63 4358 OH2 WWAATT 643 136.247 16.841 49.081 1.00 26.74 4359 OH2 WWAATT 644 130.107 34.877 51.432 1.00 22.05 4360 OH2 WWAATT 645 131.572 27.845 36.507 1.00 33.61 4361 OH2 WWAATT 646 139.273 18.921 51.935 1.00 18.69 4362 OH2 WWAATT 647 102.180 34.258 26.188 1.00 38.28 4363 OH2 WWAATT 648 123.655 36.667 26.709 1.00 23.51 4364 OH2 WAT 649 126.661 35.233 55.363 1.00 32.41 4365 OH2 WAT 650 106.153 21.764 42.249 1.00 20.34 4366 OH2 W WAATT 651 135.834 34.833 30.691 1.00 52.17 4367 OH2 WWAATT 652 103.106 38.892 25.426 1.00 26.00 4368 OH2 WAT 653 140.880 35.431 50.226 1.00 26.45 4369 OH2 WAT 654 112.327 13.971 50.722 1.00 46.47 4370 OH2 W WAATT 655 142.876 32.708 49.617 1.00 38.19 4371 OH2 WWAATT 656 136.448 11.686 63.277 1.00 31.93 4372 OH2 WWAATT 657 128.522 28.120 35.575 1.00 25.65 4373 OH2 WWAATT 658 124.837 30.666 35.131 1.00 22.56 4374 OH2 WWAATT 659 130.833 34.205 29.481 1.00 42.51 4375 OH2 WWAATT 660 112.306 35.037 18.431 1.00 22.73 4376 OH2 WWAATT 661 121.695 49.220 48.983 1.00 34.50 4377 OH2 WWAATT 662 134.850 24.747 24.896 1.00 61.06 4378 OH2 WWAATT 663 120.492 22.780 56.510 1.00 33.74 4379 OH2 WWAATT 664 145.265 41.024 28.023 1.00 26.03 4380 OH2 WAT 665 92.325 61.829 41.100 1.00 63.45 4381 OH2 WAT 666 122.583 51.518 33.284 1.00 48.58 4382 OH2 WAT 667 134.126 51.766 45.296 1.00 19.94 4383 OH2 W WAATT 668 99.217 28.001 33.331 1.00 36.10 4384 OH2 WWAATT 669 116.117 48.969 45.889 1.00 27.24 4385 OH2 WWAATT 670 90.118 37.836 45.821 1.00 21.42 4386 OH2 WAT 671 140.530 43.280 48.000 1.00 25.45 4387 OH2 WAT 672 91.812 21.421 53.465 1.00 25.28 4388 OH2 WAT 673 133.156 2.402 49.442 1.00 44.64 4389 OH2 WAT 674 124.710 30.183 52.286 1.00 27.01 4390 OH2 WAT 675 108.046 22.156 30.804 1.00 29.23 4391 OH2 W WAATT 676 141.812 18.051 53.703 1.00 33.60 4392 OH2 WWAATT 677 122.438 4.780 34.061 1.00 22.75 4393 OH2 WWAATT 678 106.890 50.310 27.843 1.00 27.59 4394 OH2 WAT 679 99.813 44.123 49.703 1.00 35.15 4395 OH2 WAT 680 1 14.424 25.540 53.859 1.00 59.82 4396 OH2 WAT 681 120.122 17.036 61.627 1.00 33.13 4397 OH2 WAT 682 123.491 39.726 28.595 1.00 39.84 4398 OH2 WAT 683 120.197 47.611 55.219 1.00 29.64 4399 OH2 WAT 684 103.132 41.401 52.472 1.00 31.67 4400 OH2 WAT 685 95.409 27.232 43.768 1.00 40.36 4401 OH2 WAT 686 93.494 47.869 47.074 1.00 41.27 4402 OH2 WAT 687 101.201 66.857 39.062 1.00 78.46 4403 OH2 WAT 688 117.640 29.026 61.987 1.00 47.48 4404 OH2 WAT 689 125.779 23.773 30.324 1.00 37.41 4405 OH2 WAT 690 118.394 14.351 39.712 1.00 8.48 4406 OH2 WAT 691 115.774 17.384 46.942 1.00 55.16 4407 OH2 WAT 692 125.846 32.742 40.650 1.00 30.56 4408 OH2 WAT 693 134.539 32.766 51.897 1.00 52.33 4409 OH2 WAT 694 132.231 24.088 46.766 1.00 63.16 4410 OH2 WAT 695 120.423 11.828 28.871 1.00 44.89 4411 OH2 WAT 696 109.529 18.849 35.510 1.00 41.86 4412 OH2 WAT 697 126.344 22.049 35.670 1.00 37.93 4413 OH2 WAT 698 140.761 46.564 40.929 1.00 36.10 4414 OH2 WAT 699 149.712 28.211 43.996 1.00 63.77 4415 OH2 WAT 700 122.788 19.483 59.019 1.00 46.07 4416 OH2 WAT 701 133.230 48.486 44.266 1.00 36.68 4417 OH2 WAT 702 121.294 17.890 56.388 1.00 45.00 4418 OH2 WAT 703 129.924 31.321 53.670 1.00 28.12 4419 OH2 WAT 704 130.041 22.759 34.128 1.00 58.80 4420 OH2 WAT 705 120.990 14.019 62.153 1.00 90.42 4421 OH2 WAT 706 144.565 20.274 60.540 1.00 57.31 4422 OH2 WAT 707 122.007 30.989 34.128 1.00 74.81 4423 OH2 WAT 708 136.782 18.854 45.912 1.00 38.89 4424 OH2 WAT 709 148.608 25.064 51.823 1.00 69.75 4425 OH2 WAT 710 129.546 23.547 49.088 1.00 59.55 4426 OH2 WAT 711 98.361 36.814 48.633 1.00 48.61 4427 OH2 WAT 712 135.173 8.831 61.117 1.00 57.62 4428 OH2 WAT 713 125.025 32.134 55.885 1.00 46.77 4429 OH2 WAT 714 109.222 19.287 57.955 1.00 58.38 4430 OH2 WAT 715 137.206 8.347 56.384 1.00 48.16 4431 OH2 WAT 716 105.467 21.522 45.303 1.00 55.42 4432 OH2 WAT 717 108.946 9.853 39.154 1.00 73.91 4433 OH2 WAT 718 96.255 23.880 48.000 1.00 73.23 4434 OH2 WAT 719 101.728 36.619 50.363 1.00 57.83 4435 OH2 WAT 720 116.536 13.569 56.095 1.00 62.99 4436 OH2 WAT 721 128.739 23.611 38.616 1.00 70.69 4437 OH2 WAT 722 126.664 3.370 36.233 1.00 79.09 4438 OH2 WAT 723 120.338 3.428 58.493 1.00 86.19 4439 OH2 WAT 724 132.490 26.185 26.764 1.00 67.03 4440 OH2 WAT 725 119.137 22.564 24.070 1.00 75.84 4441 OH2 WAT 726 98.004 28.038 42.458 1.00 72.19 4442 OH2 WAT 727 99.674 33.037 41.131 1.00 69.00 4443 OH2 WAT 728 113.394 11.413 52.820 1.00 69.11 4444 OH2 WAT 729 129.629 27.848 38.891 1.00 31.80 4445 OH2 WAT 730 138.391 3.193 36.697 1.00 88.33 4446 OH2 WAT 731 101.751 58.675 54.521 1.00 69.41 4447 OH2 WAT 732 146.260 39.908 45.702 1.00 71.98 4448 OH2 WAT 733 99.632 27.238 39.217 1.00 65.15 4449 OH2 WAT 734 139.029 16.241 44.768 1.00 76.36 4450 OH2 WAT 735 93.410 43.367 39.907 1.00 51.51 4451 OH2 WAT 736 99.833 50.411 52.960 1.00 40.10 4452 OH2 WAT 737 121.822 63.145 36.945 1.00 88.71 4453 OH2 WAT 738 123.231 52.111 47.051 1.00 59.41 4454 OH2 WAT 739 112.095 2.568 44.854 1.00 87.55 4455 OH2 WAT 740 105.823 21.588 32.912 1.00 65.78 4456 OH2 WAT 741 112.121 15.677 29.574 1.00 63.57 4457 OH2 WAT 742 116.006 23.098 23.234 1.00 66.58 4458 OH2 WAT 743 101.396 34.063 30.976 1.00 67.78 4459 OH2 WAT 744 105.307 25.170 29.199 1.00 41.04 4460 OH2 WAT 745 138.659 10.582 45.837 1.00 59.51 4461 OH2 WAT 746 114.904 60.800 37.648 1.00 51.77 4462 OH2 WAT 747 124.430 21.295 33.036 1.00 63.60 4463 OH2 WAT 748 107.809 9.528 45.664 1.00 96.91 4464 OH2 WAT 749 129.675 48.310 54.546 1.00 50.35 4465 OH2 WAT 750 104.938 42.943 50.401 1.00 73.99 4466 OH2 WAT 751 127.598 19.431 38.063 1.00 50.28 4467 OH2 WAT 752 107.804 42.960 53.690 1.00 100.00 4468 OH2 WAT 753 106.996 46.067 52.208 1.00 80.89 4469 OH2 WAT 754 115.697 53.285 33.391 1.00 88.83 4470 OH2 W WAATT 755 107.557 43.929 23.164 1.00 97.00 4471 OH2 W WAATT 756 104.503 37.526 36.972 1.00 58.13 4472 MG M MGG 757 105.326 36.717 53.406 1.00 29.00 4473 MG M MGG 758 103.375 43.256 48.861 1.00 41.96 4474 MG M MGG 759 106.905 43.906 51.594 1.00 60.57 4475 PA H HPPHH 900 106.514 40.269 50.769 1.00 64.84 4476 01A H HPPHH 900 106.467 39.079 51.657 1.00 56.34 4477 02A H HPPHH 900 106.738 41.560 51.467 1.00 62.50 4478 03A H HPPHH 900 105.506 40.292 49.674 1.00 62.63 4479 01 H HPPHH 900 108.952 41.335 50.186 1.00 61.96 4480 C1 HPH 900 108.025 40.315 49.769 1.00 64.00 4481 C2 HPH 900 108.690 38.930 49.523 1.00 61.37 4482 C3 HPH 900 109.069 38.562 48.285 1.00 51.27 4483 C4 HPH 900 109.443 37.123 48.011 1.00 49.88 4484 C5 HPH 900 110.870 36.593 48.349 1.00 48.79 4485 C6 HPH 900 112.049 37.566 48.069 1.00 37.71 4486 C7 HPH 900 112.320 38.019 46.829 1.00 34.33 4487 C8 HPH 900 113.476 38.969 46.623 1.00 35.58 4488 C9 HPH 900 113.227 40.333 47.247 1.00 56.66 4489 C10 HPH 900 113.089 40.275 48.776 1.00 68.86 4490 C11 HPH 900 112.157 41.010 49.392 1.00 73.13 4491 C12 HPH 900 112.037 40.934 50.893 1.00 66.86 4492 C15 HPH 900 108.853 39.500 47.137 1.00 54.81 4493 C13 HPH 900 111.421 42.067 48.641 1.00 68.76 4494 C14 HPH 900 111.753 37.299 45.656 1.00 41.06 Table 11 StRjctural Coordinates of Tobacco 5-Epi-Aristolochene Synthase In the Absence of Bound Substrate Atom Atom Residui e Resi idue X Y Z OCC B- Type # factor 1 N LEU 24 121.956 50.261 52.247 1.00124.05 2 CA LEU 24 122.946 50.852 53.202 1.00125.60 3 C LEU 24 124.286 50.797 52.493 1.00125.95 4 O LEU 24 125.338 50.615 53.099 1.00126.05 5 CB LEU 24 123.008 50.020 54.477 1.00127.81 6 CG LEU 24 121.748 50.062 55.337 1.00127.97 7 CD1 LEU 24 121.898 49.121 56.526 1.00126.52 8 CD2 LEU 24 121.487 51.490 55.822 1.00127.81 9 1H LEU 24 122.251 49.292 51.984 1.00 25.00 10 2H LEU 24 121.021 50.239 52.677 1.00 25.00 11 3H LEU 24 121.929 50.798 51.366 1.00 25.00 12 N TRP 25 124.208 51.008 51.190 1.00128.26 13 CA TRP 25 125.348 50.953 50.308 1.00126.64 14 C TRP 25 125.910 52.322 49.937 1.00128.50 15 O TRP 25 127.131 52.480 49.824 1.00130.12 16 CB TRP 25 124.945 50.134 49.078 1.00122.57 17 CG TRP 25 124.537 48.725 49.460 1.00116.55 18 CD1 TRP 25 123.263 48.214 49.513 1.00111.25 19 CD2 TRP 25 125.407 47.685 49.877 1.00114.36 20 NE1 TRP 25 123.302 46.911 49.947 1.00109.76 21 CE2 TRP 25 124.612 46.556 50.178 1.00113.64 22 CE3 TRP 25 126.801 47.577 50.036 1.00114.01 23 CZ2 TRP 25 125.146 45.346 50.624 1.00114.93 24 CZ3 TRP 25 127.340 46.387 50.476 1.00112.58 25 CH2 TRP 25 126.515 45.282 50.767 1.00114.08 26 H TRP 25 123.358 51.275 50.804 1.00 25.00 27 HE1 TRP 25 122.575 46.258 50.073 1.00 25.00 28 N GLY 26 125.028 53.306 49.785 1.00129.69 29 CA GLY 26 125.460 54.647 49.432 1.00129.22 30 C GLY 26 126.079 54.744 48.049 1.00128.72 31 O GLY 26 125.794 53.929 47.177 1.00128.98 32 H GLY 26 124.083 53.132 49.888 1.00 25.00 33 N ASP 27 126.962 55.721 47.868 1.00128.05 34 CA ASP 27 127.635 55.946 46.589 1.00126.16 35 C ASP 27 128.786 54.971 46.340 1.00122.14 36 O ASP 27 129.641 55.215 45.485 1.00121.90 37 CB ASP 27 128.154 57.390 46.495 1.00128.56 38 CG ASP 27 127.036 58.414 46.382 1.00129.57 39 OD1 ASP 27 126.092 58.200 45.590 1.00129.32 40 OD2 ASP 27 127.109 59.446 47.083 1.00128.42 41 H ASP 27 127.188 56.294 48.627 1.00 25.00 42 N GLN 28 128.786 53.863 47.075 1.00117.67 43 CA GLN 28 129.811 52.833 46.950 1.00112.25 44 C GLN 28 129.807 52.195 45.554 1.00112.76 45 O GLN 28 130.803 51.612 45.131 1.001 10.25 46 CB GLN 28 129.581 51.764 48.025 1.00106.94 47 CG GLN 28 130.657 50.691 48.117 1.00101.12 48 CD GLN 28 130.380 49.637 49.179 1.00 99.15 49 OE1 GLN 28 131.021 48.585 49.199 1.00 98.20 50 NE2 GLN 28 129.431 49.911 50.072 1.00 95.39 51 H GLN 28 128.073 53.736 47.724 1.00 25.00 52 1 HE2 GLN 28 129.287 49.206 50.749 1.00 25.00 53 2HE2 GLN 28 128.922 50.738 50.067 1.00 25.00 54 N PHE 29 128.696 52.349 44.833 1.00116.96 55 CA PHE 29 128.536 51.766 43.496 1.00118.70 56 C PHE 29 128.026 52.717 42.398 1.00122.05 57 O PHE 29 127.643 52.249 41.318 1.00123.10 58 CB PHE 29 127.570 50.572 43.539 1.00114.02 59 CG PHE 29 127.906 49.532 44.568 1.00111.57 60 CD1 PHE 29 128.928 48.614 44.349 1.00109.61 61 CD2 PHE 29 127.148 49.429 45.731 1.00108.83 62 CE1 PHE 29 129.193 47.609 45.274 1.00102.49 63 CE2 PHE 29 127.401 48.432 46.663 1.00101.60 64 CZ PHE 29 128.425 47.514 46.434 1.00101.60 65 H PHE 29 127.985 52.899 45.209 1.00 25.00 66 N LEU 30 127.984 54.022 42.669 1.00124.46 67 CA LEU 30 127.509 55.009 41.689 1.00127.15 68 C LEU 30 128.208 54.874 40.335 1.00128.12 69 O LEU 30 127.578 54.916 39.277 1.00126.56 70 CB LEU 30 127.732 56.433 42.230 1.00128.23 71 CG LEU 30 127.357 57.672 41.388 1.00129.74 72 CD1 LEU 30 126.987 58.843 42.316 1.00126.98 73 CD2 LEU 30 128.437 58.089 40.428 1.00126.72 74 H LEU 30 128.261 54.333 43.538 1.00 25.00 75 N SER 331 129.527 54.725 40.400 1.00129.78 76 CA SER 31 130.384 54.608 39.222 1.00130.48 77 C SER 31 131.618 53.722 39.458 1.00129.14 78 O SER 31 132.211 53.745 40.535 1.00127.41 79 CB SER 31 130.831 56.004 38.781 1.00133.08 80 OG SER 31 131.461 56.700 39.845 1.00136.17 81 H SER 31 129.890 54.673 41.303 1.00 25.00 82 HG SER 31 130.880 56.771 40.611 1.00 25.00 83 N PHE 32 132.004 52.973 38.423 1.00127.29 84 CA PHE 32 133.156 52.065 38.458 1.00126.38 85 C PHE 32 134.056 52.249 37.231 1.00129.92 86 O PHE 32 133.693 51.847 36.122 1.00131.71 87 CB PHE 32 132.683 50.601 38.531 1.00120.86 88 CG PHE 32 133.805 49.581 38.475 1.00117.02 89 CD1 PHE 32 134.736 49.488 39.507 1.00114.77 90 CD2 PHE 32 133.912 48.701 37.396 1.00113.67 91 CE1 PHE 32 135.755 48.533 39.472 1.00111.21 92 CE2 PHE 32 134.927 47.742 37.349 1.00111.87 93 CZ PHE 32 135.851 47.658 38.389 1.00111.43 94 H PHE 32 131.485 53.046 37.602 1.00 25.00 95 N SER 33 135.219 52.861 37.434 1.00129.98 96 CA SER 33 136.179 53.082 36.355 1.00128.55 97 C SER 33 137.014 51.819 36.136 1.00128.72 98 0 SER 33 137.973 51.561 36.865 1.00128.38 99 CB SER 33 137.079 54.277 36.684 1.00130.20 100 OG SER 33 137.554 54.211 38.019 1.00130.89 101 H SER 33 135.440 53.163 38.329 1.00 25.00 102 HG SER 33 136.817 54.182 38.626 1.00 25.00 103 N ILE 34 136.616 51.017 35.153 1.00128.06 104 CA ILE 34 137.313 49.773 34.842 1.00127.26 105 C ILE 34 138.715 50.001 34.268 1.00128.81 106 0 ILE 34 138.869 50.556 33.177 1.00132.56 107 CB ILE 34 136.483 48.884 33.865 1.00125.22 108 CG1 ILE 34 137.227 47.570 33.595 1.00124.19 109 CG2 ILE 34 136.174 49.640 32.570 1.00123.27 110 CD1 ILE 34 136.518 46.611 32.665 1.00121.43 111 H ILE 34 135.838 51.274 34.627 1.00 25.00 112 N ASP 35 139.736 49.600 35.020 1.00125.91 113 CA ASP 35 141.105 49.749 34.548 1.00120.92 114 C ASP 35 141.437 48.728 33.464 1.00116.38 115 0 ASP 35 141.993 47.661 33.726 1.00115.56 1 16 CB ASP 35 142.122 49.709 35.700 1.00122.56 117 CG ASP 35 141.780 48.684 36.761 1.00123.82 118 0D1 ASP 35 141.342 47.566 36.414 1.00129.46 119 OD2 ASP 35 141.952 49.002 37.955 1.00123.01 120 H ASP 35 139.577 49.234 35.909 1.00 25.00 121 N ASN 36 141.017 49.067 32.254 1.00111.08 122 CA ASN 36 141.237 48.307 31.037 1.00107.72 123 C ASN 36 142.508 47.462 30.983 1.00104.04 124 O ASN 36 142.486 46.361 30.443 1.00103.31 125 CB ASN 36 141.160 49.215 29.783 1.00108.78 126 CG ASN 36 141.378 50.742 30.076 1.00113.72 127 OD1 ASN 36 141.308 51.535 29.156 1.00115.16 128 ND2 ASN 36 141.666 51.127 31.309 1.00113.86 129 H ASN 36 140.490 49.899 32.196 1.00 25.00 130 1HD2 ASN 36 141.642 52.070 31.558 1.00 25.00 131 2HD2 ASN 36 141.817 50.557 32.067 1.00 25.00 132 N GLN 37 143.593 47.958 31.571 1.00101.33 133 CA GLN 37 144.857 47.226 31.576 1.00 97.84 134 C GLN 37 144.752 45.887 32.306 1.00 91.48 135 O GLN 37 145.120 44.848 31.756 1.00 87.36 136 CB GLN 37 145.964 48.079 32.204 1.00104.38 137 CG GLN 37 147.329 47.907 31.541 1.00109.27 138 CD GLN 37 147.433 48.643 30.213 1.00112.48 139 OE1 GLN 37 148.192 49.604 30.088 1.00116.42 140 NE2 GLN 37 146.670 48.202 29.220 1.00113.85 141 H GLN 37 143.558 48.839 31.989 1.00 25.00 142 1HE2 GLN 37 146.735 48.687 28.371 1.00 25.00 143 2HE2 GLN 37 146.083 47.436 29.358 1.00 25.00 144 N VAL 38 144.242 45.916 33.536 1.00 85.52 145 CA VAL 38 144.092 44.702 34.337 1.00 79.25 146 C VAL 38 143.148 43.731 33.634 1.00 77.63 147 O VAL 38 143.416 42.529 33.568 1.00 78.06 148 CB VAL 38 143.542 45.018 35.752 1.00 78.16 149 CG1 VAL 38 143.484 43.754 36.593 1.00 75.39 150 CG2 VAL 38 144.409 46.061 36.437 1.00 78.10 151 H VAL 38 143.943 46.770 33.907 1.00 25.00 152 N ALA 39 142.060 44.268 33.086 1.00 71.24 153 CA ALA 39 141.071 43.463 32.379 1.00 66.46 154 C ALA 39 141.694 42.736 31.191 1.00 65.26 155 O ALA 39 141.519 41.527 31.038 1.00 59.37 156 CB ALA 39 139.910 44.338 31.916 1.00 64.84 157 H ALA 39 141.924 45.233 33.161 1.00 25.00 158 N GLU 40 142.436 43.472 30.366 1.00 66.68 159 CA GLU 40 143.086 42.896 29.190 1.00 69.85 160 C GLU 40 144.107 41.828 29.559 1.00 66.85 161 O GLU 40 144.233 40.818 28.859 1.00 65.59 162 CB GLU 40 143.744 43.985 28.342 1.00 75.56 163 CG GLU 40 142.752 44.836 27.560 1.00 89.79 164 CD GLU 40 143.409 45.993 26.828 1.00 98.34 165 OE1 GLU 40 144.515 45.807 26.273 1.00101.87 166 OE2 GLU 40 142.814 47.092 26.808 1.00102.72 167 H GLU 40 142.551 44.427 30.550 1.00 25.00 168 N LYS 41 144.830 42.048 30.656 1.00 62.69 169 CA LYS 41 145.821 41.079 31.112 1.00 60.33 170 C LYS 41 145.081 39.798 31.478 1.00 56.90 171 O LYS 41 145.440 38.707 31.024 1.00 56.12 172 CB LYS 41 146.588 41.603 32.331 1.00 64.30 173 CG LYS 41 147.689 40.655 32.802 1.00 70.61 174 CD LYS 41 148.373 41.137 34.070 1.00 74.86 175 CE LYS 41 149.449 40.152 34.505 1.00 79.07 176 NZ LYS 41 150.138 40.584 35.753 1.00 86.06 177 H LYS 41 144.700 42.879 31.160 1.00 25.00 178 1HZ LYS 41 150.588 41.510 35.601 1.00 25.00 179 2HZ LYS 41 149.443 40.661 36.524 1.00 25.00 180 3HZ LYS 41 150.864 39.885 36.010 1.00 25.00 181 N TYR 42 144.027 39.951 32.278 1.00 54.48 182 CA TYR 42 143.200 38.831 32.712 1.00 49.46 183 C TYR 42 142.687 38.048 31.508 1.00 49.51 184 O TYR 42 142.886 36.837 31.418 1.00 46.83 185 CB TYR 42 142.011 39.332 33.535 1.00 49.09 186 CG TYR 42 142.316 39.665 34.981 1.00 51.81 187 CD1 TYR 42 143.609 39.555 35.498 1.00 55.25 188 CD2 TYR 42 141.297 40.067 35.844 1.00 51.34 189 CE1 TYR 42 143.873 39.836 36.843 1.00 60.63 190 CE2 TYR 42 141.548 40.347 37.180 1.00 51.18 191 CZ TYR 42 142.832 40.231 37.677 1.00 57.44 192 OH TYR 42 143.064 40.503 39.009 1.00 57.29 193 H TYR 42 143.796 40.855 32.582 1.00 25.00 194 HH TYR 42 142.245 40.765 39.435 1.00 25.00 195 N ALA 43 142.067 38.756 30.568 1.00 48.90 196 CA ALA 43 141.514 38.150 29.359 1.00 49.75 197 C ALA 43 142.560 37.363 28.576 1.00 49.98 198 O ALA 43 142.331 36.209 28.204 1.00 49.38 199 CB ALA 43 140.897 39.223 28.477 1.00 46.66 200 H ALA 43 141.980 39.722 30.693 1.00 25.00 201 N GLN 44 143.711 37.987 22.344 1.00 52.04 202 CA GLN 44 144.796 37.352 27.607 1.00 51.53 203 C GLN 44 145.219 36.030 28.257 1.00 45.51 204 0 GLN 44 145.304 35.002 27.582 1.00 43.18 205 CB GLN 44 145.994 38.299 27.506 1.00 58.59 206 CG GLN 44 147.101 37.804 26.583 1.00 74.05 207 CD GLN 44 148.364 38.649 26.658 1.00 84.03 208 0E1 GLN 44 148.343 39.784 27.132 1.00 90.02 209 NE2 GLN 44 149.475 38.092 26.187 1.00 84.98 210 H GLN 44 143.837 38.900 28.677 1.00 25.00 211 1 HE2 GLN 44 150.290 38.631 26.238 1.00 25.00 212 2HE2 GLN 44 149.438 37.187 25.820 1.00 25.00 213 N GLU 45 145.466 36.047 29.565 1.00 40.03 214 CA GLU 45 145.874 34.831 30.261 1.00 37.78 215 C GLU 45 144.740 33.813 30.320 1.00 41.99 216 0 GLU 45 144.970 32.609 30.153 1.00 43.40 217 CB GLU 45 146.374 35.134 31.673 1.00 38.09 218 CG GLU 45 147.037 33.924 32.334 1.00 41.87 219 CD GLU 45 147.595 34.209 33.718 1.00 52.34 220 0E1 GLU 45 147.678 35.393 34.116 1.00 58.77 221 0E2 GLU 45 147.962 33.235 34.409 1.00 53.14 222 H GLU 45 145.372 36.890 30.064 1.00 25.00 223 N ILE 46 143.521 34.296 30.553 1.00 38.09 224 CA ILE 46 142.352 33.428 30.622 1.00 35.19 225 C ILE 46 142.239 32.630 29.328 1.00 37.05 226 0 ILE 46 141.923 31.441 29.360 1.00 40.60 227 CB ILE 46 141.054 34.236 30.886 1.00 33.29 228 CG1 ILE 46 140.992 34.650 32.357 1.00 25.99 229 CG2 ILE 46 139.817 33.420 30.528 1.00 33.03 230 CD1 ILE 46 139.889 35.630 32.667 1.00 27.20 231 H ILE 46 143.414 35.255 30.675 1.00 25.00 232 N GLU 47 142.548 33.263 28.199 1.00 37.32 233 CA GLU 47 142.485 32.581 26.910 1.00 43.67 234 C GLU 47 143.420 31.379 26.870 1.00 44.27 235 0 GLU 47 143.061 30.324 26.341 1.00 48.49 236 CB GLU 47 142.817 33.537 25.765 1.00 50.83 237 CG GLU 47 141.700 34.516 25.422 1.00 72.13 238 CD GLU 47 140.408 33.833 24.970 1.00 80.45 239 OE1 GLU 47 140.440 32.643 24.577 1.00 82.39 240 0E2 GLU 47 139.353 34.501 25.001 1.00 87.14 241 H GLU 47 142.813 34.208 28.233 1.00 25.00 242 N ALA 48 144.610 31.538 27.444 1.00 41.56 243 CA ALA 48 145.597 30.464 27.489 1.00 36.13 244 C ALA 48 145.078 29.340 28.375 1.00 38.33 245 0 ALA 48 145.027 28.176 27.964 1.00 40.71 246 CB ALA 48 146.917 30.990 28.031 1.00 33.18 247 H ALA 48 144.824 32.404 27.853 1.00 25.00 248 N LEU 49 144.662 29.708 29.583 1.00 37.02 249 CA LEU 49 144.136 28.757 30.554 1.00 34.21 250 C LEU 49 142.894 28.044 30.029 1.00 33.34 251 0 LEU 49 142.694 26.860 30.296 1.00 34.71 252 CB LEU 49 143.816 29.477 31.862 1.00 32.92 253 CG LEU 49 145.013 30.132 32.551 1.00 29.78 254 CD1 LEU 49 144.541 31.096 33.621 1.00 28.55 255 CD2 LEU 49 145.915 29.062 33.139 1.00 31.1 1 256 H LEU 49 144.717 30.657 29.827 1.00 25.00 257 N LYS 50 142.083 28.759 29.254 1.00 35.43 258 CA LYS 50 140.858 28.208 28.681 1.00 36.99 259 C LYS 50 141.193 27.105 27.687 1.00 39.13 260 0 LYS 50 140.643 26.004 27.762 1.00 39.46 261 CB LYS 50 140.056 29.307 27.981 1.00 38.20 262 CG LYS 50 138.670 28.882 27.520 1.00 37.82 263 CD LYS 50 138.021 29.947 26.638 1.00 41.56 264 CE LYS 50 137.926 31.297 27.341 1.00 44.73 265 NZ LYS 50 137.282 32.342 26.489 1.00 40.08 266 H LYS 50 142.323 29.682 29.055 1.00 25.00 267 1 HZ LYS 50 136.318 32.042 26.239 1.00 25.00 268 2HZ LYS 50 137.245 33.240 27.012 1.00 25.00 269 3HZ LYS 50 137.841 32.474 25.620 1.00 25.00 270 N GLU 51 142.106 27.396 26.765 1.00 41.23 271 CA GLU 51 142.516 26.419 25.762 1.00 44.62 272 C GLU 51 143.174 25.226 26.446 1.00 42.95 273 0 GLU 51 142.931 24.073 26.091 1.00 43.13 274 CB GLU 51 143.489 27.055 24.766 1.00 52.90 275 CG GLU 51 143.846 26.162 23.581 1.00 70.21 276 CD GLU 51 142.623 25.709 22.792 1.00 79.98 277 0E1 GLU 51 141.917 26.575 22.226 1.00 86.16 278 0E2 GLU 51 142.368 24.486 22.739 1.00 81.08 279 H GLU 51 142.510 28.293 26.751 1.00 25.00 280 N GLN 52 143.965 25.514 27.471 1.00 48.21 281 CA GLN 52 144.662 24.480 28.223 1.00 49.28 282 C GLN 52 143.657 23.563 28.933 1.00 44.99 283 0 GLN 52 143.817 22.337 28.936 1.00 42.93 284 CB GLN 52 145.609 25.138 29.230 1.00 51.94 285 CG GLN 52 146.728 24.247 29.736 1.00 57.86 286 CD GLN 52 147.655 24.973 30.696 1.00 61.66 287 OE1 GLN 52 147.719 26.205 30.711 1.00 53.55 288 NE2 GLN 52 148.372 24.211 31.511 1.00 66.48 289 H GLN 52 144.095 26.453 27.720 1.00 25.00 290 1HE2 GLN 52 148.989 24.676 32.114 1.00 25.00 291 2HE2 GLN 52 148.283 23.237 31.480 1.00 25.00 292 N THR 53 142.615 24.160 29.512 1.00 42.37 293 CA THR 53 141.578 23.404 30.214 1.00 41.44 294 C THR 53 140.753 22.584 29.220 1.00 40.96 295 0 THR 53 140.334 21.462 29.519 1.00 38.12 296 CB THR 53 140.648 24.338 31.027 1.00 42.33 297 0G1 THR 53 141.420 25.054 32.001 1.00 42.93 298 CG2 THR 53 139.569 23.534 31.746 1.00 41.61 299 H THR 53 142.537 25.134 29.467 1.00 25.00 300 HG1 THR 53 142.088 25.586 31.555 1.00 25.00 301 N ARG 54 140.553 23.138 28.027 1.00 42.45 302 CA ARG 54 139.802 22.461 26.9976 1.00 41.46 303 C ARG 54 140.516 21.152 26.653 1.00 43.94 304 0 ARG 54 139.891 20.088 26.607 1.00 41.93 305 CB ARG 54 139.731 23.344 25.727 1.0043.17 306 CG ARG 54 138.759 22.861 24.658 1.0049.52 307 CD ARG 54 138.792 23.763 23.428 1.0055.06 308 NE ARG 54 138.600 25.176 23.764 1.0065.13 309 CZ ARG 54 137.416 25.758 23.951 1.0073.50 310 NH1 ARG 54 136.293 25.058 23.836 1.0078.69 311 NH2 ARG 54 137.353 27.046 24.263 1.0072.72 312 H ARG 54 140.919 24.030 27.846 1.0025.00 313 HE ARG 54 139.400 25.734 23.857 1.0025.00 314 1 HH1 ARG 54 136.328 24.086 23.604 1.0025.00 315 2HH1 ARG 54 135.410 25.505 23.976 1.0025.00 316 1 HH2 ARG 54 138.196 27.578 24.357 1.0025.00 317 2HH2 ARG 54 136.466 27.484 24.403 1.0025.00 318 N SER 55 141.834 21.233 26.480 1.0041.53 319 CA SER 55 142.645 20.062 26.176 1.0041.04 320 C SER 55 142.550 19.010 27.284 1.0042.34 321 O SER 55 142.587 17.810 27.005 1.0042.66 322 CB SER 55 144.100 20.469 25.916 1.0046.50 323 OG SER 55 144.208 21.230 24.719 1.0041.12 324 H SER 55 142.280 22.107 26.538 1.0025.00 325 HG SER 55 143.898 20.704 23.977 1.0025.00 326 N MET 56 142.399 19.458 28.531 1.0041.33 327 CA MET 56 142.265 18.544 29.668 1.0040.87 328 C MET 56 141.003 17.703 29.501 1.0043.46 329 O MET 56 141.017 16.489 29.711 1.0041.72 330 CB MET 56 142.164 19.312 30.989 1.0044.45 331 CG MET 56 143.461 19.894 31.500 1.0046.36 332 SD MET 56 143.231 20.659 33.118 1.0045.60 333 CE MET 56 143.715 22.320 32.763 1.0044.30 334 H MET 56 142.383 20.426 28.690 1.0025.00 335 N LEU 57 139.910 18.365 29.132 1.0042.82 336 CA LEU 57 138.632 17.696 28.929 1.0041.38 337 C LEU 57 138.684 16.700 27.779 1.0043.36 338 O LEU 57 138.042 15.653 27.831 1.0045.75 339 CB LEU 57 137.531 18.726 28.670 1.0034.91 340 CG LEU 57 137.047 19..512 29.887 1.0031.36 341 CD1 LEU 57 136.174 20.663 29.441 1.0031.29 342 CD2 LEU 57 136.287 18.592 30.833 1.0025.33 343 H LEU 57 139.968 19.335 28.990 1.0025.00 344 N LEU 58 139.466 17.016 26.754 1.0043.66 345 CA LEU 58 139.577 16.145 25.591 1.0048.27 346 C LEU 58 140.659 15.059 25.683 1.0053.11 347 O LEU 58 141.005 14.441 24.672 1.0054.87 348 CB LEU 58 139.762 16.987 24.325 1.0045.38 349 CG LEU 58 138.682 18.051 24.083 1.0048.84 350 CD1 LEU 58 138.936 18.772 22.772 1.0046.56 351 CD2 LEU 58 137.303 17.413 24.074 1.0049.64 352 H LEU 58 139.978 17.851 26.781 1.0025.00 353 N ALA 59 141.180 14.813 26.884 1.0058.17 354 CA ALA 59 142.208 13.788 27.078 1.0061.28 355 C ALA 59 141.605 12.397 26.874 1.0066.17 356 O ALA 59 140.672 11.998 27.572 1.0065.17 357 CB ALA 59 142.830 13.908 28.460 1.00 61.08 358 H ALA 59 140.859 15.316 27.661 1.00 25.00 359 N THR 60 142.188 11.651 25.943 1.00 71.93 360 CA THR 60 141.717 10.317 25.572 1.00 78.50 361 C THR 60 141.721 9.179 26.599 1.00 77.85 362 0 THR 60 140.694 8.536 26.812 1.00 82.48 363 CB THR 60 142.443 9.828 24.304 1.00 80.20 364 OG1 THR 60 143.852 10.053 24.449 1.00 82.38 365 CG2 THR 60 141.933 10.573 23.076 1.00 82..60 366 H THR 60 142.957 12.026 25.478 1.00 25.00 367 HG1 THR 60 144.029 10.991 24.540 1.00 25.00 368 N GLY 61 142.866 8.914 27.217 1.00 74.94 369 CA GLY 61 142.942 7.813 28.165 1.00 75.87 370 C GLY 61 142.662 8.104 29.626 1.00 73.64 371 0 GLY 61 143.494 7.804 30.484 1.00 73.89 372 H GLY 61 143.654 9.465 27.047 1.00 25.00 373 N ARG 62 141.491 8.651 29.925 1.00 70.85 374 CA ARG 62 141.149 8.960 31.307 1.00 67.41 375 C ARG 62 140.068 8.054 31.870 1.00 61.77 376 0 ARG 62 139.147 7.654 31.160 1.00 63.43 377 CB ARG 62 140.755 10.429 31.444 1.00 69.30 378 CG ARG 62 141.883 11.309 31.967 1.00 75.81 379 CD ARG 62 141.666 12.780 31.647 1.00 78.22 380 NE ARG 62 140.334 13.254 32.009 1.00 79.69 381 CZ ARG 62 139.335 13.405 31.143 1.00 88.12 382 NH1 ARG 62 139.508 13.118 29.859 1.00 90.62 383 NH2 ARG 62 138.160 13.852 31.559 1.00 92.99 384 H ARG 62 140.835 8.835 29.218 1.00 25.00 385 HE ARG 62 140.163 13.477 32.948 1.00 25.00 386 1HH1 ARG 62 140.393 12.785 29.534 1.00 25.00 387 2HH1 ARG 62 138.752 13.233 29.216 1.00 25.00 388 1HH2 ARG 62 138.022 14.076 32.524 1.00 25.00 389 2HH2 ARG 62 137.408 13.963 30.909 1.00 25.00 390 N LYS 63 140.214 7.702 33.143 1.00 56.71 391 CA LYS 63 139.258 6.840 33.830 1.00 53.88 392 C LYS 63 137.986 7.614 34.170 1.00 49.91 393 0 LYS 63 138.024 8.831 34.377 1.00 43.13 394 CB LYS 63 139.876 6.284 35.114 1.00 60.17 395 CG LYS 63 141.181 5.544 34.901 1.00 72.02 396 CD LYS 63 141.807 5.141 36.225 1.00 82.26 397 CE LYS 63 143.131 4.428 36.004 1.00 90.54 398 NZ LYS 63 143.764 4.015 37.286 1.00 94.67 399 H LYS 63 140.988 8.042 33.633 1.00 25.00 400 1 HZ LYS 63 143.130 3.366 37.795 1.00 25.00 401 2HZ LYS 63 144.664 3.533 37.085 1.00 25.00 402 3HZ LYS 63 143.945 4.857 37.868 1.00 25.00 403 N LEU 64 136.877 6.890 34.289 1.00 44.28 404 CA LEU 64 135.583 7.487 34.603 1.00 40.75 405 C LEU 64 135.650 8.425 35.805 1.00 38.00 406 0 LEU 64 135.273 9.592 35.708 1.00 38.34 407 CB LEU 64 134.539 6.395 34.858 1.00 37.20 408 CG LEU 64 133.128 6.897 35.170 1.00 35.50 409 CD1 LEU 64 132.563 7.618 33.964 1.00 30.93 410 CD2 LEU 64 132.232 5.741 35.572 1.00 32.83 411 H LEU 64 136.930 5.926 34.145 1.00 25.00 412 N ALA 65 136.149 7.915 36.927 1.00 34.87 413 CA ALA 65 136.264 8.700 38.152 1.00 33.63 414 C ALA 65 136.977 10.022 37.909 1.00 32.94 415 O ALA 65 136.508 11.073 38.342 1.00 31.36 416 CB ALA 65 136.991 7.900 39.222 1.00 26.54 417 H ALA 65 136.437 6.983 36.932 1.00 25.00 418 N ASP 66 138.094 9.965 37.188 1.00 35.39 419 CA ASP 66 138.887 11.151 36.882 1.00 34.98 420 C ASP 66 138.127 12.136 36.002 1.00 34.90 421 O ASP 66 138.200 13.352 36.210 1.00 34.81 422 CB ASP 66 140.202 10.755 36.202 1.00 42.66 423 CG ASP 66 141.054 9.825 37.059 1.00 51.98 424 OD1 ASP 66 141.008 9.934 38.306 1.00 48.05 425 OD2 ASP 66 141.774 8.982 36.479 1.00 59.40 426 H ASP 66 138.390 9.103 36.840 1.00 25.00 427 N THR 67 137.400 11.607 35.023 1.00 32.76 428 CA THR 67 136.617 12.433 34.110 1.00 29.98 429 C THR 67 135.486 13.131 34.869 1.00 27.93 430 O THR 67 135.262 14.337 34.708 1.00 26.55 431 CB THR 67 136.033 11.582 32.963 1.00 33.36 432 OG1 THR 67 137.102 10.914 32.278 1.00 32.56 433 CG2 THR 67 135.272 12.460 31.972 1.00 24.21 434 H THR 67 137.385 10.635 34.900 1.00 25.00 435 HG1 THR 67 136.746 10.375 31.566 1.00 25.00 436 N LEU 68 134.806 12.382 35.730 1.00 24.35 437 CA LEU 68 133.717 12.938 36.513 1.00 23.41 438 C LEU 68 134.223 14.025 37.449 1.00 28.28 439 O LEU 68 133.644 15.112 37.507 1.00 26.82 440 CB LEU 68 133.004 11.842 37.301 1.00 24.43 441 CG LEU 68 132.221 10.8411 36.447 1.00 32.03 442 CD1 LEU 68 131.651 9.744 37.330 1.00 23.28 443 CD2 LEU 68 131.112 11.556 35.680 1.00 27.61 444 H LEU 68 135.049 11.442 35.844 1.00 25.00 445 N ASN 69 135.323 13.750 38.147 1.00 26.79 446 CA ASN 69 135.894 14.724 39.072 1.00 30.78 447 C ASN 69 136.341 15.981 38.340 1.00 28.43 448 O ASN 69 136.165 17.092 38.837 1.00 30.31 449 CB ASN 69 137.061 14.125 39.867 1.00 40.14 450 CG ASN 69 136.597 13.165 40.959 1.00 53.22 451 OD1 ASN 69 135.478 13.271 41.467 1.00 52.67 452 ND2 ASN 69 137.460 12.224 41.326 1.00 60.05 453 H ASN 69 135.750 12.874 38.043 1.00 25.00 454 1 HD2 ASN 69 137.165 11.608 42.027 1.00 25.00 455 2HD2 ASN 69 138.335 12.185 40.893 1.00 25.00 456 N LEU 70 136.884 15.813 37.140 1.00 26.00 457 CA LEU 70 137.327 16.958 36.358 1.00 27.21 458 C LEU 70 136.135 17.867 36.053 1.00 29.79 459 O LEU 70 136.192 19.076 36.287 1.00 27.18 460 CB LEU 70 137.990 16.498 35.058 1.00 23.13 461 CG LEU 70 138.417 17.624 34.109 1.00 30.77 462 CD1 LEU 70 139.366 18.580 34.821 1.00 21.76 463 CD2 LEU 70 139.062 17.045 32.860 1.00 27.07 464 H LEU 70 136.995 14.908 36.777 1.00 25.00 465 N ILE 71 135.053 17.272 35.553 1.00 30.05 466 CA ILE 71 133.840 18.012 35.217 1.00 24.54 467 C ILE 71 133.221 18.663 36.456 1.00 23.02 468 0 ILE 71 132.849 19.839 36.429 1.00 23.20 469 CB ILE 71 132.809 17.095 34.516 1.00 26.68 470 CG1 ILE 71 133.338 16.693 33.136 1.00 25.05 471 CG2 ILE 71 131.459 17.795 34.383 1.00 23.87 472 CD1 ILE 71 132.442 15.736 32.400 1.00 27.35 473 H ILE 71 135.073 16.300 35.409 1.00 25.00 474 N ASP 72 133.140 17.910 37.546 1.00 19.38 475 CA ASP 72 132.585 18.429 38.789 1.00 22.68 476 C ASP 72 133.376 19.657 39.266 1.00 25.06 477 0 ASP 72 132.784 20.680 39.626 1.00 24.92 478 CB ASP 72 132.593 17.335 39.861 1.00 23.74 479 CG ASP 72 131.900 17.760 41.147 1.00 27.65 480 0D1 ASP 72 130.953 18.575 41.086 1.00 29.89 481 OD2 ASP 72 132.303 17.268 42.223 1.00 30.37 482 H ASP 72 133.459 16.986 37.512 1.00 25.00 483 N ILE 73 134.705 19.565 39.228 1.00 26.02 484 CA ILE 73 135.589 20.656 39.654 1.00 21.86 485 C ILE 73 135.431 21.918 38.797 1.00 23.60 486 0 ILE 73 135.270 23.019 39.329 1.00 25.70 487 CB ILE 73 137.075 20.198 39.671 1.00 20.21 488 CG1 ILE 73 137.245 19.066 40.684 1.00 22.84 489 CG2 ILE 73 137.992 21.351 40.058 1.00 17.62 490 CD1 ILE 73 138.659 18.513 40.788 1.00 53.34 491 H ILE 73 135.108 18.732 38.902 1.00 25.00 492 N ILE 74 135.450 21.755 37.476 1.00 22.39 493 CA ILE 74 135.297 22.884 36.556 1.00 22.15 494 C ILE 74 133.955 23.581 36.784 1.00 24.59 495 0 ILE 74 133.858 24.807 36.702 1.00 29.58 496 CB ILE 74 135.415 22.426 35.079 1.00 24.24 497 CG1 ILE 74 136.835 21.909 34.811 1.00 25.85 498 CG2 ILE 74 135.071 23.571 34.132 1.00 19.61 499 CD1 ILE 74 137.054 21.340 33.420 1.00 23.74 500 H ILE 74 135.571 20.851 37.109 1.00 25.00 501 N GLU 75 132.925 22.797 37.083 1.00 23.15 502 CA GLU 75 131.599 23.343 37.338 1.00 23.53 503 C GLU 75 131.548 24.092 38.658 1.00 21.84 504 0 GLU 75 131.040 25.208 38.722 1.00 25.34 505 CB GLU 75 130.550 22.237 37.342 1.00 26.71 506 CG GLU 75 130.274 21.647 35.978 1.00 30.84 507 CD GLU 75 129.073 20.720 35.969 1.00 36.10 508 OE1 GLU 75 128.644 20.253 37.051 1.00 29.89 509 OE2 GLU 75 128.559 20.460 34.865 1.00 31.50 510 H GLU 75 133.056 21.822 37.122 1.00 25.00 511 N ARG 76 132.060 23.474 39.717 1.00 19.68 512 CA ARG 76 132.066 24.115 41.028 1.00 20.75 513 C ARG 76 132.925 25.385 41.017 1.00 22.83 514 0 ARG 76 132.699 26.303 41.803 1.00 21.89 515 CB ARG 76 132.581 23.148 42.091 1.00 16.07 516 CG ARG 76 131.653 21.989 42.411 1.00 20.22 517 CD ARG 76 132.331 21.061 43.395 1.00 21.08 518 NE ARG 76 131.498 19.939 43.819 1.00 18.53 519 CZ ARG 76 130.847 19.891 44.977 1.00 24.53 520 NH1 ARG 76 130.917 20.907 45.829 1.00 17.48 521 NH2 ARG 76 130.170 18.802 45.311 1.00 26.65 522 H ARG 76 132.440 22.577 39.618 1.00 25.00 523 HE ARG 76 131.417 19.172 43.218 1.00 25.00 524 1 HH1 ARG 76 131.459 21.717 45.606 1.00 25.00 525 2HH1 ARG 76 130.423 20.865 46.697 1.00 25.00 526 1 HH2 ARG 76 130.146 18.021 44.691 1.00 25.00 527 2HH2 ARG 76 129.678 18.766 46.181 1.00 25.00 528 N LEU 77 133.913 25.425 40.126 1.00 22.29 529 CA LEU 77 134.798 26.579 40.001 1.00 23.34 530 C LEU 77 134.156 27.710 39.193 1.00 26.64 531 0 LEU 77 134.752 28.777 39.026 1.00 25.27 532 CB LEU 77 136.131 26.167 39.372 1.00 18.34 533 CG LEU 77 137.076 25.352 40.258 1.00 18.25 534 CD1 LEU 77 138.266 24.893 39.443 1.00 15.60 535 CD2 LEU 77 137.531 26.182 41.459 1.00 17.00 536 H LEU 77 134.063 24.649 39.546 1.00 25.00 537 N GLY 78 132.958 27.455 38.668 1.00 24.42 538 CA GLY 78 132.228 28.464 37.914 1.00 20.32 539 C GLY 78 132.741 28.807 36.531 1.00 20.16 540 0 GLY 78 132.375 29.841 35.970 1.00 22.90 541 H GLY 78 132.553 26.576 38.793 1.00 25.00 542 N ILE 79 133.550 27.927 335.952 1.00 22.82 543 CA ILE 79 134.099 28.170 34.623 1.00 24.96 544 C ILE 79 133.577 27.204 33.560 1.00 29.01 545 0 ILE 79 133.991 27.273 32.398 1.00 28.78 546 CB ILE 79 135.646 28.133 34.635 1.00 24.44 547 CG1 ILE 79 136.142 26.920 35.429 1.00 27.37 548 CG2 ILE 79 136.195 29.426 35.210 1.00 25.45 549 CD1 ILE 79 137.632 26.715 35.381 1.00 25.03 550 H ILE 79 133.782 27.105 36.435 1.00 25.00 551 N SER 80 132.629 26.347 33.935 1.00 27.52 552 CA SER 80 132.079 25.381 32.986 1.00 29.32 553 C SER 80 131.317 26.012 31.816 1.00 31.74 554 0 SER 80 131.187 25.391 30.761 1.00 34.93 555 CB SEER 80 131.205 24.338 33.694 1.00 26.24 556 OG SER 80 130.096 24.932 34.338 1.00 29.78 557 H SER 80 132.308 26.358 34.857 1.00 25.00 558 HG SER 80 130.432 25.530 34.992 1.00 25.00 559 N TYR 81 130.869 27.258 31.966 1.00 25.77 560 CA TYR 81 130.134 27.914 30.887 1.00 23.28 561 C TYR 81 130.965 28.063 29.605 1.00 30.16 562 0 TYR 81 130.418 28.302 28.527 1.00 32.12 563 CB TYR 81 129.556 29.261 31.344 1.00 24.86 564 CG TYR 81 130.557 30.381 31.543 1.00 29.19 565 CD1 TYR 81 131.260 30.519 32.740 1.00 27.27 566 CD2 TYR 81 130.768 31.329 30.545 1.00 28.18 567 CE1 TYR 81 132.148 31.575 32.935 1.00 29.22 568 CE2 TYR 81 131.649 32.384 30.729 1.00 29.85 569 CZ TYR 81 132.336 32.504 31.923 1.00 29.78 570 OH TYR 81 133.220 33.547 32.084 1.00 28.93 571 H TYR 81 131.028 27.734 32.805 1.00 25.00 572 HH TYR 81 133.196 34.121 31.313 1.00 25.00 573 N HIS 82 132.284 27.904 29.727 1.00 32.51 574 CA HIS 82 133.194 27.991 28.581 1.00 29.34 575 C HIS 82 133.237 26.669 27.828 1.00 28.19 576 0 HIS 82 133.658 26.620 26.672 1.00 28.93 577 CB HIS 82 134.631 28.280 29.038 1.00 27.19 578 CG HIS 82 134.839 29.654 29.589 1.00 22.31 579 ND1 HIS 82 134.702 30.793 28.825 1.00 24.56 580 CD2 HIS 82 135.195 30.071 30.827 1.00 20.64 581 CE1 HIS 82 134.964 31.853 29.568 1.00 22.72 582 NE2 HIS 82 135.265 31.442 30.786 1.00 23.06 583 H HIS 82 132.658 27.714 30.612 1.00 25.00 584 HD1 HIS 82 134.458 30.815 27.872 1.00 25.00 585 HE2 HIS 82 135.465 32.016 31.549 1.00 25.00 586 N PHE 83 132.820 25.596 28.493 1.00 26.84 587 CA PHE 83 132.878 24.266 27.903 1.00 33.10 588 C PHE 83 131.549 23.521 27.811 1.00 36.98 589 0 PHE 83 131.511 22.296 27.973 1.00 34.23 590 CB PHE 83 133.895 23.426 28.683 1.00 32.26 591 CG PHE 83 135.171 24.159 28.985 1.00 36.23 592 CD1 PHE 83 136.138 24.336 27.998 1.00 36.38 5993 CD2 PHE 83 135.381 24.724 30.241 1.00 34.95 594 CE1 PHE 83 137.295 25.067 28.254 1.00 36.74 595 CE2 PHE 83 136.533 25.457 30.509 1.00 39.63 596 CZ PHE 83 137.492 25.630 29.511 1.00 41.21 597 H PHE 83 132.457 25.694 29.394 1.00 25.00 598 N GLU 84 130.478 24.241 27.484 1.00 40.92 599 CA GLU 84 129.146 23.641 27.365 1.00 46.14 600 C GLU 84 129.159 22.422 26.431 1.00 42.13 601 0 GLU 84 128.753 21.325 26.819 1.00 38.24 602 CB GLU 84 128.128 24.674 26.851 1.00 56.77 603 CG GLU 84 128.042 25.978 27.660 1.00 74.38 604 CD GLU 84 127.252 25.853 28.960 1.00 81.74 605 OE1 GLU 84 127.654 25.066 29.847 1.00 85.56 606 OE2 GLU 84 126.233 26.564 29.101 1.00 84.80 607 H GLU 84 130.590 25.203 27.330 1.00 25.00 608 N LYS 85 129.674 22.614 25.218 1.00 40.25 609 CA LYS 85 129.740 21.544 24.224 1.00 41.41 610 C LYS 85 130.590 20.348 24.663 1.00 36.27 611 0 LYS 85 130.138 19.204 24.595 1.00 35.16 612 CB LYS 85 130.268 22.085 22.890 1.00 46.40 613 CG LYS 85 130.364 21.025 21.801 1.00 58.06 614 CD LYS 85 131.176 21.498 20.605 1.00 70.05 615 CE LYS 85 131.305 20.389 19.565 1.00 70.91 616 NZ LYS 85 132.101 20.809 18.379 1.00 79.32 617 H LYS 85 130.016 23.501 24.992 1.00 25.00 618 1 HZ LYS 85 133.059 21.080 18.678 1.00 25.00 619 2HZ LYS 85 132.157 20.018 17.706 1.00 25.00 620 3HZ LYS 85 131.636 21.619 17.922 1.00 25.00 621 N GLU 86 131.812 20.620 25.115 1.00 37.17 622 CA GLU 86 132.736 19.573 25.545 1.00 35.98 623 C GLU 86 132.162 18.714 26.663 1.00 36.73 624 0 GLU 86 132.156 17.483 26.571 1.00 38.05 625 CB GLU 86 134.077 20.173 25.990 1.00 36.51 626 CG GLU 86 134.938 20.773 24.866 1.00 40.91 627 CD GLU 86 134.439 22.124 24.349 1.00 43.71 628 OE1 GLU 86 133.728 22.840 25.085 1.00 42.43 629 OE2 GLU 86 134.776 22.480 23.201 1.00 50.53 630 H GLU 86 132.086 21.551 25.172 1.00 25.00 631 N ILE 87 131.666 19.368 27.708 1.00 35.80 632 CA ILE 87 131.092 18.662 28.845 1.00 30.66 633 C ILE 87 129.871 17.844 28.428 1.00 32.98 634 0 ILE 87 129.692 16.711 28.887 1.00 32.50 635 CB ILE 87 130.739 19.640 29.986 1.00 30.27 636 CG1 ILE 87 132.027 20.253 30.546 1.00 29.89 637 CG2 ILE 87 129.972 18.926 31.091 1.00 29.25 638 CD1 ILE 87 131.814 21.264 31.654 1.00 25.52 639 H ILE 87 131.681 20.348 27.719 1.00 25.00 640 N ASP 88 129.054 18.393 27.534 1.00 32.95 641 CA ASP 88 127.870 17.679 27.070 1.00 36.69 642 C ASP 88 128.256 16.407 26.309 1.00 39.28 643 0 ASP 88 127.745 15.324 26.6601 1.00 40.13 644 CB ASP 88 126.994 18.573 26.191 1.00 40.42 645 CG ASP 88 125.682 17.901 25.800 1.00 49.09 646 0D1 ASP 88 124.874 17.586 26.702 1.00 48.29 647 0D2 ASP 88 125.464 17.677 24.590 1.00 57.24 648 H ASP 88 129.245 19.291 27.185 1.00 25.00 649 N GLU 89 129.178 16.532 25.359 1.00 38.92 650 CA GLU 89 129.621 15.385 24.573 1.00 38.06 651 C GLU 89 130.258 14.303 25.433 1.00 35.90 652 0 GLU 89 130.077 13.115 25.168 1.00 39.91 653 CB GLU 89 130.572 15.829 23.466 1.00 44.42 654 CG GLU 89 129.871 16.622 22.379 1.00 61.34 655 CD GLU 89 130.822 17.159 21.333 1.00 75.40 656 0E1 GLU 89 131.776 17.873 21.707 1.00 80.47 657 0E2 GLU 89 130.609 16.878 20.134 1.00 86.74 658 H GLU 89 129.569 17.416 25.185 1.00 25.00 659 N ILE 90 130.985 14.708 26.470 1.00 32.75 660 CA ILE 90 131.619 13.749 27.368 1.00 31.62 661 C ILE 90 130.556 13.052 28.215 1.00 33.52 662 0 ILE 90 130.580 11.830 28.376 1.00 35.53 663 CB ILE 90 132.646 14.427 28.302 1.00 31.23 664 CG1 ILE 90 133.815 14.983 27.485 1.00 32.25 665 CG2 ILE 90 133.153 13.431 29.340 1.00 23.52 666 CD1 ILE 90 134.794 15.802 28.300 1.00 27.90 667 H ILE 90 131.105 15.670 26.630 1.00 25.00 668 N LEU 91 129.617 13.828 28.749 1.00 33.39 669 CA LEU 91 128.551 13.266 29.569 1.00 33.57 670 C LEU 91 127.642 12.351 28.756 1.00 35.23 671 0 LEU 91 127.145 11.346 29.269 1.00 32.55 672 CB LEU 91 127.741 14.373 30.244 1.00 30.86 673 CG LEU 91 128.430 15.017 31.447 1.00 28.62 674 CD1 LEU 91 127.538 16.084 32.040 1.00 25.02 675 CD2 LEU 91 128.752 13.952 32.490 1.00 25.28 676 H LEU 91 129.643 14.796 28.591 1.00 25.00 677 N ASP 92 127.445 12.692 27.486 1.00 34.80 678 CA ASP 92 126.620 11.889 26.595 1.00 37.65 679 C ASP 92 127.273 10.516 26.446 1.00 38.72 680 0 ASP 92 126.594 9.490 26.494 1.00 41.65 681 CB ASP 92 126.491 12..569 25.231 1.00 44.12 682 CG ASP 92 125.426 11.931 24.358 1.00 48.79 683 OD1 ASP 92 124.235 12.268 24.531 1.00 49.33 684 OD2 ASP 92 125.781 11.098 23.498 1.00 52.21 685 H ASP 92 127.856 13.512 27.149 1.00 25.00 686 N GLN 93 128.595 10.499 26.286 1.00 40.62 687 CA GLN 93 129.337 9.247 26.155 1.00 41.87 688 C GLN 93 129.209 8.415 27.424 1.00 41.38 689 0 GLN 93 129.038 7.198 27.356 1.00 44.29 690 CB GLN 93 130.817 9.504 25.883 1.00 47.84 691 CG GLN 93 131.124 10.061 24.511 1.00 65.26 692 CD GLN 93 132.618 10.230 24.286 1.00 76.60 693 OE1 GLN 93 133.402 9.308 24.532 1.00 78.42 694 NE2 GLN 93 133.023 11.413 23.829 1.00 78.28 695 H GLN 93 129.082 11.351 26.254 1.00 25.00 696 1HE2 GLN 93 133.983 11.522 23.685 1.00 25.00 697 2HE2 GLN 93 132.356 12.108 23.664 1.00 25.00 698 N ILE 94 129.302 9.065 28.580 1.00 38.08 699 CA ILE 94 129.186 8.360 29.851 1.00 38.56 700 C ILE 94 127.783 7.763 30.011 1.00 37.25 701 0 ILE 94 127.631 6.623 30.464 1.00 40.45 702 CB ILE 94 129.519 9.284 31.051 1.00 38.10 703 CG1 ILE 94 130.982 9.729 30.973 1.00 33.78 704 CG2 ILE 94 129.265 8.559 32.372 1.00 39.54 705 CD1 ILE 94 131.426 10.590 32.131 1.00 28.73 706 H ILE 94 129.455 10.035 28.576 1.00 25..00 707 N TYR 95 126.769 8.527 29.616 1.00 35.79 708 CA TYR 95 125.383 8.080 29.702 1.00 36.92 709 C TYR 95 125.219 6.814 28.869 1.00 40.95 710 0 TYR 95 124.681 5.812 29.340 1.00 39.72 711 CB TYR 95 124.438 9.170 29.176 1.00 31.04 712 CG TYR 95 122.969 8.799 29.213 1.00 35.51 713 CD1 TYR 95 122.356 8.420 30.407 1.00 37.94 714 CD2 TYR 95 122.189 8.826 28.054 1.00 40.35 715 CE1 TYR 95 121.002 8.073 30.452 1.00 42.00 716 CE2 TYR 95 120.827 8.481 28.088 1.00 44.29 717 CZ TYR 95 120.245 8.107 29.294 1.00 43.88 718 OH TYR 95 118.912 7.763 29.351 1.00 49.08 719 H TYR 95 126.959 9.421 29.265 1.00 25.00 720 HH TYR 95 118.668 7.513 30.254 1.00 25.00 721 N ASN 96 125.744 6.861 27.649 1.00 42.27 722 CA ASN 96 125.664 5.749 26.711 1.00 45.67 723 C ASN 96 126.430 4.484 27.088 1.00 53.96 724 0 ASN 96 125.949 3.383 26.831 1.00 58.48 725 CB ASN 96 126.068 6.215 25.310 1.00 41.30 726 CG ASN 96 125.004 7.072 24.656 1.00 45.95 727 OD1 ASN 96 123.922 6.590 24.339 1.00 50.40 728 ND2 ASN 96 125.299 8.349 24.459 1.00 47.53 729 H ASN 96 126.205 7.682 27.378 1.00 25.00 730 1HD2 ASN 96 124.616 8.910 24.040 1.00 25.00 731 2HD2 ASN 96 126.172 8.686 24.743 1.00 25.00 732 N GLN 97 127.604 4.625 27.702 1.00 62.59 733 CA GLN 97 128.397 3.453 28.081 1.00 69.96 734 C GLN 97 127.898 2.701 29.320 1.00 74.06 735 0 GLN 97 128.255 1.540 29.521 1.00 71.27 736 CB GLN 97 129.885 3.804 28.219 1.00 74.21 737 CG GLN 97 130.227 4.801 29.315 1.00 82.49 738 CD GLN 97 131.723 5.065 29.415 1.00 85.73 739 0E1 GLN 97 132.336 4.837 30.456 1.00 88.41 740 NE2 GLN 97 132.316 5.548 28.329 1.00 82.49 741 H GLN 97 127.943 5.524 27.899 1.00 25.00 742 1 HE2 GLN 97 133.277 5.711 28.402 1.00 25.00 743 2HE2 GLN 97 131.787 5.714 27.528 1.00 25.00 744 N ASN 98 127.091 3.367 30.147 1.00 83.07 745 CA ASN 98 126.517 2.769 31.360 1.00 95.02 746 C ASN 98 127.459 1.854 32.148 1.00101.68 747 0 ASN 98 127.088 0.737 32.517 1.00106.47 748 CB ASN 98 125.233 1.997 31.019 1.00 98.06 749 CG ASN 98 124.034 2.902 30.830 1.00100.62 750 OD1 ASN 98 123.390 3.307 31.799 1.00107.25 751 ND2 ASN 98 123.711 3.207 29.580 1.00100.51 752 H ASN 98 126.876 4.301 29.938 1.00 25.00 753 1 HD2 ASN 98 122.944 3.798 29.449 1.00 25.00 754 2HD2 ASN 98 124.241 2.849 28.838 1.00 25.00 755 N SER 99 128.671 2.326 32.415 1.00105.86 756 CA SER 99 129.649 1.533 33.153 1.00108.38 757 C SER 999 129.389 1.528 34.659 1.00109.53 758 0 SER 99 129.054 2.561 35.243 1.00110.32 759 CB SER 99 131.057 2.049 32.859 1.00107.06 760 OG SER 99 131.078 3.465 32.861 1.00109.07 761 H SER 99 128.927 3.224 32.122 1.00 25.00 762 HG SER 99 130.810 3.805 33.720 1.00 25.00 763 N ASN 100 129.534 0.361 35.280 1.00111.83 764 CA ASN 100 129.325 0.223 36.720 1.00115.28 765 C ASN 100 130.612 0.548 37.462 1.00114.16 766 0 ASN 100 131.577 -0.213 37.402 1.00114.16 767 CB ASN 100 128.873 -1.195 37.072 1.00117.88 768 CG ASN 100 127.451 -1.473 36.640 1.00122.11 769 OD1 ASN 100 126.518 -0.785 37.056 1.00119.89 770 ND2 ASN 100 127.274 -2.485 35.799 1.00124.85 771 H ASN 100 129.794 -0.423 34.757 1.00 25.00 772 1 HD2 ASN 100 126.354 -2.663 35.510 1.00 25.00 773 2HD2 ! ASN 100 128.048 -3.001 35.500 1.00 25.00 774 N CYS 101 130.622 1.678 38.162 1.00112.97 775 CA CYS 101 131.804 2.103 38.902 1.00109.49 776 C CYS 101 132.046 1.309 40.184 1.00104.47 777 0 CYS 101 133.178 1.226 40.662 1.00107.64 778 CB CYS 101 131.735 3.593 39.218 1.00112.66 779 SG CYS 101 133.273 4.224 39.908 1.00125.35 780 H CYS 101 129.822 2.244 38.153 1.00 25.00 781 N ASN 102 130.976 0.765 40.756 1.00 95.01 782 CA ASN 102 131.043 -0.0488 41.975 1.00 88.33 783 C ASN 102 131.235 0.673 43.315 1.00 78.73 784 0 ASN 102 131.005 0.074 44.367 1.00 78.57 785 CB ASN 102 132.071 -1 J82 41.831 1.00 94.60 786 CG ASN 102 131.727 -2J47 40.704 1.00 99.33 787 0D1 ASN 102 130.667 -2.774 40.706 1.00 97.79 788 ND2 ASN 102 132.618 -2.256 39.727 1.00103.54 789 H ASN 102 130.102 0.912 40.350 1.00 25.00 790 1 HD2 ASN 102 132.412 -2.867 38.993 1.00 25.00 791 2HD2 ASN 102 133.439 -1.721 39.766 1.00 25.00 792 N ASP 103 131.684 1.926 43.301 1.00 65.57 793 CA ASP 103 131.845 2.657 44.560 1.00 56.22 794 C ASP 103 130.870 3.833 44.638 1.00 46.49 795 0 ASP 103 130.659 4.550 43.657 1.00 41.71 796 CB ASP 103 133.296 3.102 44.796 1.00 56.91 797 CG ASP 103 133.767 4.133 43.802 1.00 64.49 798 0D1 ASP 103 134.215 3.735 42.707 1.00 74.22 799 0D2 ASP 103 133.707 5.339 44.124 1.00 67.65 800 H ASP 103 131.912 2.367 42.461 1.00 25.00 801 N LEU 104 130.281 4.015 45.816 1.00 38.89 802 CA LEU 104 129.291 5.060 46.071 1.00 36.92 803 C LEU 104 129.672 6.457 45.591 1.00 36.45 804 0 LEU 104 128.898 7.109 44.895 1.00 35.19 805 CB LEU 104 128.943 5.092 47.561 1.00 33.67 806 CG LEU 104 127.824 6.031 48.011 1.00 36.34 807 CD1 LEU 104 126.538 5.713 47.269 1.00 35.38 808 CD2 LEU 104 127.622 5.893 49.510 1.00 35.29 809 H LEU 104 130.509 3.401 46.542 1.00 25.00 810 N CYS 105 130.872 6.895 45.951 1.00 36.36 811 CA CYS 105 131.376 8.212 45.581 1.00 35.11 812 C CYS 105 131.220 8.537 44.092 1.00 34.06 813 0 CYS 105 130.596 9.536 43.725 1.00 37.28 814 CB CYS 105 132.847 8.325 45.993 1.00 35.03 815 SG CYS 105 133.614 9.885 45.573 1.00 53.55 816 H CYS 105 131.437 6.307 46.484 1.00 25.00 817 N THR 106 131.761 7.679 43.236 1.00 30.74 818 CA THR 106 131.697 7.890 41.797 1.00 28.00 819 C THR 106 130.301 7.663 41.227 1.00 25.73 820 0 THR 106 129.870 8.396 40.339 1.00 28.92 821 CB THR 106 132.714 7.000 41.074 1.00 33.61 822 OG1 THR 106 134.000 7.172 41.684 1.00 38.24 823 CG2 THR 106 132.807 7.369 39.598 1.00 30.78 824 H THR 106 132.208 6.874 43.564 1.00 25.00 825 HG1 THR 106 134.270 8.093 41.602 1.0025.00 826 N SER 107 129.592 6.670 41.751 1.0023.29 827 CA SER 107 128.237 6.371 41.294 1.0027.37 828 C SER 107 127.268 7.540 41.539 1.0025.50 829 O SER 107 126.518 7.932 40.643 1.0025.99 830 CB SER 107 127.721 5.101 41.978 1.0026.16 831 OG SER 107 128.552 3.993 41.676 1.0034.57 832 H SER 107 129.981 6.113 42.456 1.0025.00 833 HG SER 107 128.501 3.864 40.726 1.0025.00 834 N ALA 108 127.298 8.096 42.749 1.0023.90 835 CA ALA 108 126.441 9.219 43.121 1.0023.63 836 C ALA 108 126.779 10.466 42.307 1.0025.62 837 O ALA 108 125.887 11.189 41.861 1.0027.88 838 CB ALA 108 126.566 9.509 44.608 1.0018.25 839 H ALA 108 127.913 7.734 43.418 1.0025.00 840 N LEU 109 128.069 10.709 42.099 1.0021.86 841 CA LEU 109 128.493 11.861 41.322 1.0021.96 842 C LEU 109 128.009 11.704 39.881 1.0025.59 843 O LEU 109 127.458 12.640 39.297 1.0026.33 844 CB LEU 109 130.017 12.002 41.359 1.0021.29 845 CG LEU 109 130.611 13.161 40.550 1.0023.03 846 CD1 LEU 109 129.969 14.480 40.962 1.0015.35 847 CD2 LEU 109 132.111 13.210 40.751 1.0017.60 848 H LEU 109 128.742 10.101 42.475 1.0025.00 849 N GLN 110 128.205 10.509 39.325 1.0027.12 850 CA GLN 110 127.796 10.199 37.954 1.0028.41 851 C GLN 110 126.302 10.449 37.803 1.0024.05 852 O GLN 110 125.849 11.049 36.825 1.0023.84 853 CB GLN 110 128.098 8.732 37.632 1.0026.80 854 CG GLN 110 127.790 8.333 36.197 1.0034.89 855 CD GLN 110 127.942 6.843 35.947 1.0037.60 856 OE1 GLN 110 128.418 6.098 36.804 1.0043.99 857 NE2 GLN 110 127.538 6.401 34.765 1.0038.91 858 H GLN 110 128.641 9.810 39.852 1.0025.00 859 1HE2 GLN 110 127.636 5.440 34.604 1.0025.00 860 2HE2 GLN 110 127.167 7.030 34.117 1.0025.00 861 N PHE 111 125.543 9.970 38.779 1.0020.86 862 CA PHE 111 124.104 10.140 38.783 1.0024.95 863 C PHE 111 123.760 11.633 38.792 1.0024.87 864 O PHE 111 123.037 12.H3 37.917 1.0027.29 865 CB PHE 111 123.511 9.442 40.008 1.0021.47 866 CG PHE 111 122.019 9.568 40.120 1.0028.99 867 CD1 PHE 111 121.183 8.649 39.494 1.0024.39 868 CD2 PHE 111 121.448 10.600 40.865 1.0026.46 869 CE1 PHE 111 119.799 8.753 39.610 1.0026.64 870 CE2 PHE 111 120.072 10.713 40.985 1.0025.60 871 CZ PHE 111 119.243 9.787 40.356 1.0030.12 872 H PHE 111 125.966 9.482 39.513 1.0025.00 873 N ARG 112 124.323 12.372 39.747 1.0023.80 874 CA ARG 112 124.055 13.802 39.858 1.0018.05 875 C ARG 112 124.384 14.598 38.601 1.0022.05 876 O ARG 112 123.539 15.341 38.103 1.0028.69 877 CB ARG 112 124.771 14.417 41.066 1.00 18.30 878 CG ARG 112 124.503 15.911 41.209 1.00 16.54 879 CD ARG 112 125.077 16.519 42.479 1.00 17.13 880 NE ARG 112 126.540 16.520 42.517 1.00 19.87 881 CZ ARG 112 127.323 17.379 41.866 1.00 22.23 882 NH1 ARG 112 126.808 18.328 41.099 1.00 19.31 883 NH2 ARG 112 128.636 17.311 42.012 1.00 25.31 884 H ARG 112 124.928 11.945 40.387 1.00 25.00 885 HE ARG 112 126.982 15.846 43.063 1.00 25.00 886 1 HH1 ARG 112 125.815 18.407 40.998 1.00 25.00 887 2HH1 ARG 112 127.408 18.960 40.612 1.00 25.00 888 1 HH2 ARG 112 129.037 16.615 42.608 1.00 25.00 889 2HH2 ARG 112 129.219 17.950 41.520 1.00 25.00 890 N LEU 113 125.596 14.445 38.077 1.00 22.19 891 CA LEU 113 125.994 15.192 36.883 1.00 23.19 892 C LEU 113 125.112 14.907 35.665 1.00 27.49 893 0 LEU 113 124.752 15.828 34.921 1.00 24.19 894 CB LEU 113 127.465 14.937 36.532 1.00 26.29 895 CG LEU 113 128.547 15.323 37.546 1.00 28.48 896 CD1 LEEU 113 129.911 15.110 36.905 1.00 21.83 897 CD2 LEU 113 128.391 16.772 37.993 1.00 17.87 898 H LEU 113 126.225 13.821 38.492 1.00 25.00 899 N LEU 114 124.776 13.638 35.451 1.00 24.90 900 CA LEU 114 123.932 13.268 34.321 1.00 25.28 901 C LEU 114 122.537 13.867 34.485 1.00 23.09 902 0 LEU 114 122.038 14.534 33.580 1.00 26.40 903 CB LEU 114 123.866 11.746 34.168 1.00 23.58 904 CG LEU 114 125.167 11.101 33.671 1.00 25.79 905 CD1 LEU 114 125.043 9.591 33.660 1.00 24.20 906 CD2 LEU 114 125.504 11.607 32.280 1.00 23.62 907 H LEU 114 125.095 12.937 36.062 1.00 25.00 908 N ARG 115 121.948 13.694 35.665 1.00 23.30 909 CA ARG 115 120.620 14.228 35.955 1.00 21.07 910 C ARG 115 120.551 15.748 35.787 1.00 26.37 911 0 ARG 115 119.628 16.267 35.148 1.00 26.34 912 CB ARG 115 120.178 13.844 37.372 1.00 20.95 913 CG ARG 115 119.749 12.394 37.528 1.00 21.24 914 CD ARG 115 118.588 12.057 36.595 1.00 24.51 915 NE ARG 115 118.086 10.702 36.813 1.00 20.45 916 CZ ARG 115 117.090 10.394 37.639 1.00 25.55 917 NH1 ARG 115 116.475 11.347 38.327 1.00 26.55 918 NH2 ARG 115 116.729 9.128 37.807 1.00 21.55 919 H ARG 115 122.416 13.187 36.361 1.00 25.00 920 HE ARG 115 118.508 9.978 36.314 1.00 25.00 921 1HH1 ARG 115 116.757 12.300 38.232 1.00 25.00 922 2HH1 ARG 115 115.725 11.114 38.942 1.00 25.00 923 1HH2 ARG 115 117.205 8.402 37.314 1.00 25.00 924 2HH2 ARG 115 115.980 8.901 38.425 1.00 25.00 925 N GLN 116 121.537 16.458 36.333 1.00 24.98 926 CA GLN 116 121.573 17.917 36.235 1.00 21.36 927 C GLN 116 121.696 18.366 34.792 1.00 23.11 928 0 GLN 116 121.331 19.491 34.450 1.00 20.94 929 CB GLN 116 122.718 18.501 37.066 1.00 21.35 930 CG GLN 116 122.536 18.322 38.561 1.00 24.02 931 CD GLN 116 123.594 19.035 39.371 1.00 23.65 932 0E1 GLN 116 123.278 19.835 40.252 1.00 30.06 933 NE2 GLN 116 124.855 18.744 39.088 1.00 21.53 934 H GLN 116 122.246 15.983 36.814 1.00 25.00 935 1 HE2 GLN 116 125.538 19.210 39.609 1.00 25.00 936 2HE2 GLN 116 125.046 18.089 38.391 1.00 25.00 937 N HIS 117 122.232 17.490 33.950 1.00 21.29 938 CA HIS 117 122.381 17.804 32.537 1.00 21.02 939 C HIS 117 121.264 17.235 31.666 1.00 23.62 940 0 HIS 117 121.389 17.192 30.445 1.00 22.85 941 CB HIS 117 123.755 17.366 32.031 1.00 23.58 942 CG HIS 117 124.863 18.267 32.475 1.00 27.17 943 ND1 HIS 117 125.477 19.165 31.628 1.00 28.70 944 CD2 HIS 117 125.421 18.456 33.693 1.00 26.70 945 CE1 HIS 117 126.361 19.874 32.307 1.00 25.66 946 NE2 HIS 117 126.346 19.464 33.562 1.00 29.17 947 H HIS 117 122.526 16.612 34.277 1.00 25.00 948 HD1 HIS 117 125.301 19.252 30.671 1.00 25.00 949 HE2 HIS 117 126.861 19.825 34.298 1.00 25.00 950 N GLY 118 120.183 16.784 32.301 1.00 24.12 951 CA GLY 118 119.050 16.258 31.562 1.00 25.68 952 C GLY 118 119.037 14.786 31.193 1.00 30.13 953 0 GLY 118 118.028 14.303 30.676 1.00 35.12 954 H GLY 118 120.143 16.804 33.279 1.00 25.00 955 N PHE 119 120.130 14.068 31.432 1.00 29.49 956 CA PHE 119 120.184 12.644 31.102 1.00 26.30 957 C PHE 119 119.435 11.867 32.172 1.00 28.96 958 0 PHE 119 119.836 11.861 33.337 1.00 25.84 959 CB PHE 119 121.633 12.156 31.019 1.00 24.99 960 CG PHE 119 122.447 12.845 29.964 1.00 23.43 961 CD1 PHE 119 122.392 12.421 28.640 1.00 22.02 962 CD2 PHE 119 123.267 13.922 30.291 1.00 23.36 963 CE1 PHE 119 123.145 13.063 27.650 1.00 26.82 964 CE2 PHE 119 124.023 14.572 29.312 1.00 20.73 965 CZ PHE 119 123.962 14.141 27.988 1.00 22.11 966 H PHE 119 120.902 14.496 31.856 1.00 25.00 967 N ASN 120 118.351 11.207 31.779 1.00 31.42 968 CA ASN 120 117.551 10.447 32.733 1.00 36.20 969 C ASN 120 118.208 9.117 33.088 1.00 36.85 970 0 ASN 120 117.727 8.048 32.707 1.00 39.49 971 CB ASN 120 116.126 10.232 32.200 1.00 33.41 972 CG ASN 120 115.142 9.796 33.286 1.00 35.58 973 0D1 ASN 120 115.481 9.721 34.465 1.00 38.24 974 ND2 ASN 120 113.907 9.531 32.886 1.00 40.30 975 H ASN 120 118.092 11.226 30.839 1.00 25.00 976 1 HD2 ASN 120 113.277 9.246 33.576 1.00 25.00 977 2HD2 ASN 120 113.672 9.626 31.940 1.00 25.00 978 N ILE 121 119.347 9.194 33.770 1.00 36.98 979 CA ILE 121 120.054 7.997 34.192 1.00 29.59 980 C ILE 121 119.207 7.323 35.264 1.00 29.55 981 0 ILE 121 118.647 7.984 36.134 1.00 30.63 982 CB ILE 121 121.478 8.319 34.745 1.00 35.93 983 CG1 ILE 121 122.130 7.046 35.300 1.00 34.57 984 CG2 ILE 121 121.419 9.425 35.7798 1.00 27.62 985 CD1 ILE 121 123.558 7.221 35.775 1.00 37.39 986 H ILE 121 119.696 10.074 34.013 1.00 25.00 987 N SER 122 119.086 6.007 35.172 1.00 32.39 988 CA SER 122 118.299 5.245 36.129 1.00 27.80 989 C SER 122 118.912 5.243 37.526 1.00 27.11 990 0 SER 122 120.130 5.143 37.685 1.00 30.59 991 CB SER 122 118.145 3.801 35.642 1.00 28.47 992 OG SER 122 117.529 2.993 36.633 1.00 27.99 993 H SER 122 119.540 5.535 34.444 1.00 25.00 994 HG SER 122 117.442 2.098 36.275 1.00 25.00 995 N PRO 123 118.065 5.325 38.564 1.00 27.95 996 CA PRO 123 118.542 5.323 39.949 1.00 27.26 997 C PRO 123 118.941 3.904 40.372 1.00 33.55 998 0 PRO 123 119.325 3.664 41.521 1.00 34.51 999 CB PRO 123 117.323 5.823 40.723 1.00 26.86 1000 CG PRO 123 116.184 5.252 39.938 1.00 26.05 1001 CD PRO 123 116.605 5.531 38.510 1.00 24.97 1002 N GLU 124 118.849 2.967 39.431 1.00 34.65 1003 CA GLU 124 119.199 1.569 39.673 1.00 42.28 1004 C GLU 124 120.673 1.441 40.056 1.00 39.18 1005 0 GLU 124 121.072 0.492 40.735 1.00 41.59 1006 CB GLU 124 118.902 0.732 38.424 1.00 48.21 1007 CG GLU 124 119.074 -0.773 38.601 1.00 61.85 1008 CD GLU 124 118.112 -1.379 39.615 1.00 71.29 1009 0E1 GLU 124 117.022 -0.803 39.851 1.00 70.67 1010 0E2 GLU 124 118.450 -2.447 40.170 1.00 76.93 1011 H GLU 124 118.522 3.203 38.539 1.00 25.00 1012 N ILE 125 121.466 2.430 39.657 1.00 36.76 1013 CA ILE 125 122.892 2.458 39.955 1.00 35.15 1014 C ILE 125 123.155 2.401 41.472 1.00 35.83 1015 0 ILE 125 124.237 2.016 41.900 1.00 36.05 1016 CB ILE 125 123.557 3.718 39.319 1.00 33.60 1017 CG1 ILE 125 125.082 3.610 39.368 1.00 32.56 1018 CG2 ILE 125 123.087 4.988 40.017 1.00 28.43 1019 CD1 ILE 125 125.789 4.705 38.586 1.00 28.58 1020 H ILE 125 121.080 3.169 39.141 1.00 25.00 1021 N PHE 126 122.145 2.733 42.276 1.00 33.20 1022 CA PHE 126 122.276 2..717 43.731 1.00 33.30 1023 C PHE 126 121.902 1.394 44.402 1.00 38.46 1024 0 PHE 126 122.171 1.211 45.591 1.00 38.34 1025 CB PHE 126 121.444 3.843 44.362 1.00 29.75 1026 CG PHE 126 121.937 5.218 44.030 1.00 32.61 1027 CD1 PHE 126 123.084 5.724 44.631 1.00 29.30 1028 CD2 PHE 126 121.263 6.007 43.103 1.00 33.58 1029 CE1 PHE 126 123.558 6.997 44.310 1.00 31.83 1030 CE2 PHE 126 121.726 7.279 42.775 1.00 36.03 1031 CZ PHE 126 122.877 7.776 43.380 1.00 34.15 1032 H PHE 126 121.286 3.004 41.891 1.00 25.00 1033 N SER 127 121.285 0.477 43.662 1.00 37.94 1034 CA SER 127 120.871 -0.806 44.236 1.00 37.24 1035 C SER 127 122.012 -1.601 44.855 1.00 37.05 1036 0 SER 127 121.842 -2.210 45.908 1.00 37.94 1037 CB SER 127 120.141 -1.658 43.201 1.00 34.22 1038 OG SER 127 118.885 -1.087 42.887 1.00 44.36 1039 H SER 127 121.104 0.658 42.719 1.00 25.00 1040 HG SER 127 119.018 -0.202 42.539 1.00 25.00 1041 N LYS 128 123.184 -1.557 44.228 1.00 37.17 1042 CA LYS 128 124.348 -2.280 44.737 1.00 39.88 1043 C LYS 128 124.840 -1.783 46.097 1.00 42.69 1044 0 LYS 128 125.690 -2.417 46.720 1.00 48.65 1045 CB LYS 128 125.492 -2.257 43.715 1.00 39.92 1046 CG LYS 128 125.877 -0.882 43.210 1.00 41.79 1047 CD LYS 128 126.864 -0.983 42.061 1.00 45..38 1048 CE LYS 128 127.112 0.380 41.430 1.00 57.33 1049 NZ LYS 128 128.057 0.329 40.278 1.00 63.77 1050 H LYS 128 123.266 -1.028 43.408 1.00 25.00 1051 1HZ LYS 128 128.971 -0.047 40.597 1.00 25.00 1052 2HZ LYS 128 127.667 -0.293 39.541 1.00 25.00 1053 3HZ LYS 128 128.187 1.285 39.892 1.00 25.00 1054 N PHE 129 124.305 -0.656 46.556 1.00 41.03 1055 CA PHE 129 124.697 -0.090 47.844 1.00 38.56 1056 C PHE 129 123.574 -0.255 48.848 1.00 42.42 1057 0 PHE 129 123.617 0.319 49.940 1.00 44.74 1058 CB PHE 129 125.013 1.396 47.695 1.00 32.52 1059 CG PHE 129 125.984 1.691 46.604 1.00 28.29 1060 CD1 PHE 129 127.291 1.225 46.677 1.00 27.71 1061 CD2 PHE 129 125.585 2.402 45.481 1.00 27.23 1062 CE1 PHE 129 128.186 1.461 45.645 1.00 27.92 1063 CE2 PHE 129 126.473 2.644 44.442 1.00 29.82 1064 CZ PHE 129 127.776 2.172 44.523 1.00 29.88 1065 H PHE 129 123.617 -0.193 46.037 1.00 25.00 1066 N GLN 130 122.566 -1.036 48.482 1.00 46.51 1067 CA GLN 130 121.425 -1.242 49.356 1.00 52.21 1068 C GLN 130 121.181 -2.700 49.659 1.00 60.08 1069 0 GLN 130 121.565 -3.588 48.891 1.00 57.60 1070 CB GLN 130 120.173 -0.638 48.736 1.00 50.11 1071 CG GLN 130 120.247 0.860 48.526 1.00 50.91 1072 CD GLN 130 119.025 1.399 47.840 1.00 51.21 1073 0E1 GLN 130 118.339 0.677 47.117 1.00 52.53 1074 NE2 GLN 130 118.737 2.677 48.061 1.00 47.70 1075 H GLN 130 122.585 -1.533 47.632 1.00 25.00 1076 1HE2 GLN 130 117.922 2.996 47.623 1.00 25.00 1077 2HE2 GLN 130 119.296 3.221 48.627 1.00 25.00 1078 N ASP 131 120.531 -2.944 50.790 1.00 67.42 1079 CA ASP 131 120.236 -4.306 51.203 1.00 74.82 1080 C ASP 131 118.975 -4.746 50.421 1.00 79.83 1081 0 ASP 131 118.273 -3.905 49.822 1.00 81.73 1082 CB ASP 131 120.046 ^.394 52.745 1.00 75.37 1083 CG ASP 131 118.894 -3.558 53.284 1.00 79.54 1084 0D1 ASP 131 118.173 -2.911 52.501 1.00 89.69 1085 0D2 ASP 131 118.707 -3.540 54.511 1.00 80.32 1086 H ASP 131 120.203 -2J47 51.259 1.00 25.00 1087 N GLU 132 118.671 -6.041 50.521 1.00 86.92 1088 CA GLU 132 117.492 -6.620 49.865 1.00 93.82 1089 C GLU 132 116.183 -5.970 50.310 1.00 94.42 1090 0 GLU 132 115.084 -6.369 49.910 1.00 95.34 1091 CB GLU 132 117.414 -8.108 50.165 1.00 99.58 1092 CG GLU 132 118.603 -8.893 49.626 1.00110.72 1093 CD GLU 132 118.550 -10.369 49.968 1.00117.77 1094 OE1 GLU 132 118.100 -10.716 51.082 1.00122.96 1095 OE2 GLU 132 118.962 -11.187 49.117 1.00118.79 1096 H GLU 132 119.347 -6.569 50.930 1.00 25.00 1097 N ASN 133 116.318 •4.957 51.145 1.00 94.58 1098 CA ASN 1333 115.214 -4.208 51.715 1.00 92.72 1099 C ASN 133 115.107 -2.839 51.042 1.00 90.09 1100 0 ASN 133 114.134 -2.112 51.210 1.00 90.03 1101 CB ASN 133 115.492 ^4.043 53.214 1.00 99.96 1102 CG ASN 133 114.389 -3.337 53.923 1.00106.41 1103 OD1 ASN 133 113.275 -3.847 54.016 1.00108.32 1104 ND2 ASN 133 114.683 -2.159 54.447 1.00111.37 1105 H ASN 133 117.175 -4.667 51.437 1.00 25.00 1106 1 HD2 ASN 133 113.925 -1.736 54.889 1.00 25.00 1107 2HD2 ASN 133 115.561 -1.741 54.365 1.00 25.00 1108 N GLY 134 116.139 -2.501 50.284 1.00 84.16 1109 CA GLY 134 116.195 -1.224 49.597 1.00 77.66 1110 C GLY 134 116.752 -0.121 50.479 1.00 73.68 1111 0 GLY 134 116.780 1.040 50.072 1.00 72.39 1112 H GLY 134 116.840 -3.192 50.233 1.00 25.00 1113 N LYS 135 117.141 -0.462 51.704 1.00 70.01 1114 CA LYS 135 117.724 0.524 52.606 1.00 61.88 1115 C LYS 135 119.229 0.556 52.361 1.00 58.01 1116 0 LYS 135 119.831 -0.473 52.038 1.00 52.64 1117 CB LYS 135 117.429 0.190 54.069 1.00 62.54 1118 CG LYS 135 116.279 0.994 54.661 1.00 69.58 1119 CD LYS 135 114.935 0.594 54.062 1.00 74.13 1120 CE LYS 135 113.799 1.517 54.474 1.00 77.90 1121 NZ LYS 135 113.779 1.824 55.931 1.00 77.60 1122 H LYS 135 117.045 -1.379 52.010 1.00 25.00 1123 1HZ LYS 135 113.687 0.9599 56.499 1.00 25.00 1124 2HZ LYS 135 114.669 2.310 56.155 1.00 25.00 1125 3HZ LYS 135 112.977 2.461 56.110 1.00 25.00 1126 N PHE 136 119.834 1.731 52.491 1.00 53.56 1127 CA PHE 136 121.268 1.864 52.261 1.00 46.60 1128 C PHE 136 122.075 1.074 53.275 1.00 46.58 1129 0 PHE 136 121.797 1.118 54.473 1.00 47.43 1130 CB PHE 136 121.686 3.336 52.270 1.00 39.21 1131 CG PHE 136 121.382 4.056 50.990 1.00 32.34 1132 CD1 PHE 136 122.171 3.854 49.863 1.00 31.37 1133 CD2 PHE 136 120.282 4.898 50.896 1.00 32.38 1134 CE1 PHE 136 121.876 4.491 48.657 1.00 25.70 1135 CE2 PHE 136 119.976 5.540 49.701 1.00 34.62 1136 CZ PHE 136 120.771 5.330 48.573 1.00 28.91 1137 H PHE 136 119.315 2.505 52.789 1.00 25.00 1138 N LYS 137 123.046 0.315 52.776 1.00 48.31 1139 CA LYS 137 123.910 -0.487 53.629 1.00 53.52 1140 C LYS 137 124.551 0.429 54.656 1.00 59.01 1141 0 LYS 137 125.408 1.247 54.316 1.00 64.30 1142 CB LYS 137 125.007 -1.160 52.801 1.00 48.57 1 143 CG LYS 137 124.526 -2.258 51.872 1.00 52.37 1144 CD LYS 137 125.683 -2.796 51.049 1.00 56.61 1145 CE LYS 137 125.266 -3.980 50.199 1.00 55.76 1146 NZ LYS 137 126.388 -4.433 49.330 1.00 62.73 1147 H LYS 137 123.197 0.306 51.808 1.00 25.00 1148 1 HZ LYS 137 127.197 -4.714 49.920 1.00 25.00 1149 2HZ LYS 137 126.077 -5.245 48.758 1.00 25.00 1150 3HZ LYS 137 126.670 -3.656 48.699 1.00 25.00 1151 N GLU 138 124.151 0.281 55.914 1.00 61.30 1152 CA GLU 138 124.688 1.107 56.991 1.00 62.65 1153 C GLU 138 126.219 1.035 57.078 1.00 60.08 1154 0 GLU 138 126.855 1.862 57.732 1.00 61.14 1155 CB GLU 138 124.049 0.720 58.324 1.00 63.46 1156 CG GLU 138 122.561 1.033 58.457 1.00 67.41 1157 CD GLU 138 122.276 2.499 58.743 1.00 68.98 1158 OE1 GLU 138 122.994 3.105 59.568 1.00 67.92 1159 OE2 GLU 138 121.317 3.043 58.154 1.00 72.44 1160 H GLU 138 123.462 -0.385 56.115 1.00 25.00 1161 N SER 139 126.807 0.062 56.390 1.00 54.50 1162 CA SER 139 128.255 -0.105 56.357 1.00 54.27 1163 C SER 139 128.960 1.037 55.609 1.00 51.34 1164 0 SER 139 130.144 1.292 55.828 1.00 53.27 1165 CB SER 139 128.600 -1.453 55.722 1.00 59.61 1166 OG SER 139 127.596 -1.846 54.800 1.00 67.84 1167 H SER 139 126.266 -0.582 55.893 1.00 25.00 1168 HG SER 139 127.548 -1.203 54.087 1.00 25.00 1169 N LEU 140 128.225 1.714 54.728 1.00 46.50 1170 CA LEU 140 128.751 2.839 53.953 1.00 37.91 1171 C LEU 140 128.861 4.092 54.826 1.00 33.78 1172 0 LEU 140 129.454 5.090 54.422 1.00 30.69 1173 CB LEU 140 127.821 3.151 52.777 1.00 39.38 1174 CG LEU 140 127.643 2.142 51.639 1.00 42.09 1175 CD1 LEU 140 126.330 2.417 50.919 1.00 38.48 1176 CD2 LEU 140 128.819 2.212 50.672 1.00 38.39 1177 H LEU 140 127.290 1.456 54.590 1.00 25.00 1178 N ALA 141 128.295 4.024 56.026 1.00 28.75 1179 CA ALA 141 128.288 5.141 56.964 1.00 29.20 1180 C ALA 141 129.646 5.737 57.310 1.00 30.53 1181 0 ALA 141 129.713 6.825 57.882 1.00 30.24 1182 CB ALA 141 127.565 4.742 58.235 1.00 28.51 1183 H ALA 141 127.860 3.193 56.303 1.00 25.00 1184 N SER 142 130.719 5.018 57.002 1.00 28.14 1185 CA SER 142 132.062 5.500 57.297 1.00 30.43 1186 C SER 142 132.788 6.004 56.051 1..0030.66 1187 0 SER 142 133.961 6.371 56.107 1.00 39.46 1188 CB SER 142 132.879 4.409 58.011 1.00 30.29 1189 OG SER 142 132.790 3.146 57.358 1.00 26.69 1190 H SER 142 130.627 4.146 56.569 1.00 25.00 1191 HG SER 142 133.417 2.568 57.780 1.00 25.00 1192 N ASP 143 132.069 6.053 54.937 1.00 27.41 1193 CA ASP 143 132.614 6.512 53.663 1.00 28.00 1194 C ASP 143 132.168 7.966 53.447 1.00 33.02 1195 0 ASP 143 131.211 8.232 52.714 1.00 34.43 1196 CB ASP 143 132.085 5.603 52.540 1.00 26.21 1197 CG ASP 143 132.609 5.978 51.160 1.00 32.37 1198 OD1 ASP 143 133.578 6.762 51.045 1.00 34.10 1199 OD2 ASP 143 132.041 5.465 50.174 1.00 37.80 1200 H ASP 143 131.130 5.790 54.969 1.00 25.00 1201 N VAL 144 132.884 8.906 54.060 1.00 31.09 1202 CA VAL 144 132.548 10.328 53.958 1.00 27.23 1203 C VAL 144 132.392 10.873 52.534 1.00 27.59 1204 0 VAL 144 131.404 11.545 52.243 1.00 25.91 1205 CB VAL 144 133.541 11.204 54.758 1.00 27.72 1206 CG1 VAL 144 133.183 12.684 54.621 1.00 21.28 1207 CG2 VAL 144 133.509 10.804 56.227 1.00 34.69 1208 H VAL 144 133.643 8.619 54.609 1.00 25.00 1209 N LEU 145 133.344 10.580 51.649 1.00 25.30 1210 CA LEU 145 133.266 11.063 50.268 1.00 27.68 1211 C LEU 145 132.039 10.510 49.544 1.00 29.04 1212 0 LEU 145 131.392 11.218 48.773 1.00 26.76 1213 CB LEU 145 134.541 10.722 49.487 1.00 27.26 1214 CG LEU 145 135.839 11.375 49.970 1.00 29.50 1215 CD1 LEU 145 136.956 11.087 48.983 1.00 25.10 1216 CD2 LEU 145 135.648 12.875 50.113 1.00 31.66 1217 H LEU 145 134.098 10.040 51.931 1.00 25.00 1218 N GLY 146 131.717 9.247 49.806 1.00 27.11 1219 CA GLY 146 130.552 8.643 49.185 1.00 25.43 1220 C GLY 146 129.288 9.290 49.726 1.00 27.86 1221 0 GLY 146 128.373 9.621 48.968 1.00 24.45 1222 H GLY 146 132.255 8.727 50.431 1.00 25.00 1223 N LEU 147 129.251 9.485 51.043 1.00 21.13 1224 CA LEU 147 128.114 10.102 551.712 1.00 23.48 1225 C LEU 147 127.867 11.519 51.202 1.00 23.64 1226 0 LEU 147 126.722 11.922 51.002 1.00 25.30 1227 CB LEU 147 128.338 10.140 53.226 1.00 23.15 1228 CG LEU 147 128.286 8.821 54.003 1.00 30.78 1229 CD1 LEU 147 128.667 9.059 55.455 1.00 24.16 1230 CD2 LEU 147 126.892 8.210 53.911 1.00 22.86 1231 H LEU 147 130.010 9.196 51.584 1.00 25.00 1232 N LEU 148 128.943 12.265 50.978 1.00 20.29 1233 CA LEU 148 128.831 13.633 50.498 1.00 24.04 1234 C LEU 148 128.217 13.664 49.106 1.00 23.69 1235 0 LEU 148 127.267 14.408 48.855 1.00 26.51 1236 CB LEU 148 130.198 14.328 50.506 1.00 22.43 1237 CG LEU 148 130.240 15.787 50.033 1.00 24.68 1238 CD1 LEU 148 129.285 16.649 50.853 1.00 16.95 1239 CD2 LEU 148 131.662 16.314 50.136 1.00 19.49 1240 H LEU 148 129.830 11.885 51.143 1.00 25.00 1241 N ASN 149 128.742 12.845 48.203 1.00 23.38 1242 CA ASN 149 128.210 12.801 46.850 1.00 20.71 1243 C ASN 149 126.781 12.269 46.809 1.00 25.14 1244 0 ASN 149 125.990 12.678 45.956 1.00 25.34 1245 CB ASN 149 129.125 12.008 45.932 1.00 15.21 1246 CG ASN 149 130.320 12.817 45.489 1.00 19.96 1247 OD1 ASN 149 " 131.340 12.856 46.167 1.00 34.43 1248 ND2 ASN 149 130.185 13.505 44.369 1.00 25.72 1249 H ASN 149 129.509 12.271 48.444 1.00 25.00 1250 1 HD2 ASN 149 130.969 14.021 44.090 1.00 25.00 1251 2HD2 ASN 149 129.340 13.468 43.887 1.00 25.00 1252 N LEU 150 126.445 11.379 47.743 1.00 21.91 1253 CA LEU 150 125.096 10.829 47.827 1.00 24.64 1254 C LEU 150 124.171 11.938 48.330 1.00 22.13 1255 0 LEU 150 123.058 12.104 47.831 1.00 27.92 1256 CB LEU 150 125.051 9.630 48.780 1.00 17.59 1257 CG LEU 150 123.659 9.057 49.062 1.00 21.25 1258 CD1 LEU 150 123.054 8.510 47.780 1.00 18.26 1259 CD2 LEU 150 123.739 7.976 50.118 1.00 19.18 1260 H LEU 150 127.125 11.076 48.382 1.00 25.00 1261 N TYR 151 124.652 12.706 49.301 1.00 20.18 1262 CA TYR 151 123.892 13.818 49.858 1.00 20.96 1263 C TYR 151 123.533 14.798 48.738 1.00 19.39 1264 0 TYR 151 122.380 15.204 48.592 1.00 21.76 1265 CB TYR 151 124.723 14.535 50.929 1.00 20.29 1266 CG TYR 151 124.115 15.828 51.418 1.00 22.32 1267 CD1 TYR 151 123.202 15.834 52.470 1.00 20.29 1268 CD2 TYR 151 124.432 17.047 50.811 1.00 21.17 1269 CE1 TYR 151 122.614 17.021 52.907 1.00 20.42 1270 CE2 TYR 151 123.850 18.236 51.237 1.00 21.39 1271 CZ TYR 151 122.940 18.214 52.285 1.00 22.07 1272 OH TYR 151 122.337 19.377 52.696 1.00 21.54 1273 H TYR 151 125.542 12.522 49.655 1.00 25.00 1274 HH TYR 151 121.769 19.210 53.457 1.00 25.00 12775 N GLU 152 124.532 15.194 47.959 1.00 21.41 1276 CA GLU 152 124.316 16.128 46.863 1.00 19.05 1277 C GLU 152 123.388 15.546 45.800 1.00 23.34 1278 0 GLU 152 122.540 16.259 45.260 1.00 21.99 1279 CB GLU 152 125.653 16.544 46.235 1.00 23.58 1280 CG GLU 152 126.641 17.236 47.198 1.00 23.54 1281 CD GLU 152 126.245 18.662 47.577 1.00 27.07 1282 0E1 GLU 152 125.046 19.009 47.529 1.00 30.35 1283 0E2 GLU 152 127.145 19.444 47.935 1.00 23.20 1284 H GLU 152 125.434 14.851 48.136 1.00 25.00 1285 N ALA 153 123.530 14.248 45.526 1.00 24.42 1286 CA ALA 153 122.706 13.565 44.526 1.00 22.61 1287 C ALA 153 121.251 13.409 44.964 1.00 19.49 1288 0 ALA 153 120.342 13.450 44.138 1.00 21.30 1289 CB ALA 153 123.300 12.203 44.186 1.00 21.47 1290 H ALA 153 124.211 13.731 46.006 1.00 25.00 1291 N SER 154 121.026 13.262 46.264 1.00 16.33 1292 CA SER 154 119.672 13.105 46.776 1.00 21.77 1293 C SER 154 118.822 14.343 46.464 1.00 27.62 1294 0 SER 154 117.603 14.258 46.351 1.00 29.95 1295 CB SER 154 119.688 12.820 48.288 1.00 15.72 1296 OG SER 154 119.902 13.991 49.060 1.00 20.33 1297 H SER 154 121.776 13.256 46.901 1.00 25.00 1298 HG SER 154 119.193 14.609 48.898 1.00 25.00 1299 N HIS 155 119.470 15.489 46.291 1.00 24.50 1300 CA HIS 155 118.751 16.720 46.001 1.00 20.74 1301 C HIS 155 118.320 16.907 44.552 1.00 22.52 1302 0 HIS 155 117.682 17.905 44.224 1.00 23.13 1303 CB HIS 155 119.543 17.929 46.487 1.00 19.93 1304 CG HIS 155 119.439 18.154 47.961 1.00 14.77 1305 ND1 HIS 155 120.456 17.843 48.838 1.00 20.63 1306 CD2 HIS 155 118.431 18.652 48.716 1.00 13.91 1307 CE1 HIS 155 120.080 18.142 50.069 1.00 21.57 1308 NE2 HIS 155 118.855 18.634 50.022 1.00 17.34 1309 H HIS 155 120.451 15.494 46.346 1.00 25.00 1310 HD1 HIS 155 121.317 17.420 48.603 1.00 25.00 1311 HE2 HIS 155 118.336 18.952 50.793 1.00 25.00 1312 N VAL 156 118.686 15.972 43.678 1.00 22.99 1313 CA VAL 156 118.283 16.063 42.276 1.00 22.09 1314 C VAL 156 117.265 14.970 41.940 1.00 22.99 1315 0 VAL 156 116.954 14.741 40.768 1.00 22.80 1316 CB VAL 156 119.491 15.956 41.299 1.00 18.92 1317 CG1 VAL 156 120.541 16.999 41.636 1.00 20.34 1318 CG2 VAL 156 120.089 14.560 41.329 1.00 20.67 1319 H VAL 156 119.229 15.207 43.966 1.00 25.00 1320 N ARG 157 116.729 14.317 42.968 1.00 19.28 1321 CA ARG 157 115.766 13.239 42.762 1.00 25.29 1322 C ARG 157 114.394 13.708 42.272 1.00 26.91 1323 0 ARG 157 113.988 14.850 42.498 1.00 27.10 1324 CB ARG 157 115.625 12.380 44.024 1.00 19.93 1325 CG ARG 157 114.831 13.011 45.1144 1.00 19.14 1326 CD ARG 157 114.914 12.156 46.397 1.00 20.33 1327 NE ARG 157 114.069 12.674 47.473 1.00 30.46 1328 CZ ARG 157 114.373 13.717 48.242 1.00 36.78 1329 NH1 ARG 157 115.515 14.371 48.071 1.00 39.31 1330 NH2 ARG 157 113.523 14.119 49.176 1.00 36.74 1331 H ARG 157 116.972 14.566 43.881 1.00 25.00 1332 HE ARG 157 113.214 12.230 47.643 1.00 25.00 1333 1HH1 ARG 157 116.149 14.079 47.364 1.00 25.00 1334 2HH1 ARG 157 115.736 15.154 48.652 1.00 25.00 1335 1HH2 ARG 157 112.655 13.643 49.305 1.00 25.00 1336 2HH2 ARG 157 113.751 14.905 49.753 1.00 25.00 1337 N THR 158 113.709 12.813 41.569 1.00 30.13 1338 CA THR 158 112.385 13.066 41.015 1.00 27.65 1339 C THR 158 111.374 12.189 41.763 1.00 25.41 1340 0 THR 158 111.751 11.413 42.642 1.00 23.51 1341 CB THR 158 112.350 12.703 39.513 1.00 24.84 1342 OG1 THR 158 112.630 11.307 39.355 1.00 27.71 1343 CG2 THR 158 113.391 13.496 38.738 1.00 19.09 1344 H THR 158 114.102 11.937 41.427 1.00 25.00 1345 HG1 THR 158 111.995 10.771 39.817 1.00 25.00 1346 N HIS 159 110.103 12.268 41.377 1.00 26.77 1347 CA HIS 159 109.051 11.473 42.016 1.00 27.30 1348 C HIS 159 109.196 9.971 41.741 1.00 33.58 1349 0 HIS 159 108.630 9.150 42.462 1.00 33.82 1350 CB HIS 159 107.663 11.939 41.557 1.00 26.01 1351 CG HIS 159 107.337 13.350 41.941 1.00 23.00 1352 ND1 HIS 159 106.999 13.711 43.226 1.00 24.86 1353 CD2 HIS 159 107.311 14.490 41.210 1.00 18.70 1354 CE1 HIS 159 106.782 15.012 43.275 1.00 24.72 1355 NE2 HIS 159 106.966 15.509 42.064 1.00 23.55 1356 H HIS 159 109.879 12.878 40.646 1.00 25.00 1357 HD1 HIS 159 106.924 13.094 43.988 1.00 25.00 1358 HE2 HIS 159 106.880 16.460 41.845 1.00 25.00 1359 N ALA 160 109.948 9.624 40.697 1.00 32.77 1360 CA ALA 160 110.167 8.229 40.315 1.00 31.64 1361 C ALA 160 111.364 7.581 41.009 1.00 36.31 1362 0 ALA 160 111.509 6.361 41.002 1.00 37.53 1363 CB ALA 160 110.326 8..130 38.803 1.00 25.40 1364 H A ALLAA 160 110.358 10.319 40.160 1.00 25.00 1365 N A ASSPP 161 112.217 8.401 41.612 1.00 40.41 1366 CA A ASSPP 161 113.415 7.904 42.281 1.00 40.26 1367 C A ASSPP 161 113.123 7.414 43.689 1.00 41.77 1368 0 A ASSPP 161 113.634 7.937 44.678 1.00 41.48 1369 CB A ASSPP 161 114.508 8.976 42.291 1.00 34.22 1370 CG A ASSPP 161 114.959 9.354 40.898 1.00 34.94 1371 0D1 A ASSPP 161 114.954 8.486 40.002 1.00 33.51 1372 0D2 ASP 161 115.319 10.532 40.697 1.00 32.35 1373 H ASP 161 112.014 9.350 41.663 1.00 25.00 1374 N ASP 162 112.353 6.342 43.742 1.00 46.26 1375 CA ASP 162 111.932 5.726 44.985 1.00 46.59 1376 C ASP 162 113.108 5.156 45.760 1.00 44.37 1377 0 ASP 162 113.127 5.172 46.990 1.00 37.28 1378 CB ASP 162 110.916 4.630 44.670 1.00 56.78 1379 CG ASP 162 109.654 5.185 44.046 1.00 69.65 1380 0D1 ASP 162 108.899 5.870 44.766 1.00 67.08 1381 0D2 ASP 162 109.435 4.978 42.830 1.00 79.19 1382 H ASP 162 112.114 5.949 42.869 1.00 25.00 1383 N ILE 163 114.106 4.699 45.015 1.00 41.87 1384 CA ILE 163 115.314 4.112 45.575 1.00 43.77 1385 C ILE 163 116.093 5.124 46.426 1.00 42.36 1386 0 ILE 163 116.764 4.757 47.385 1.00 45.56 1387 CB ILE 163 116.200 3.561 44.433 1.00 47.25 1388 CG1 ILE 163 115.385 2.571 43.595 1.00 56..48 1389 CG2 ILE 163 117.433 2.870 44.986 1.00 49.93 1390 CD1 ILE 163 116.134 1.994 42.404 1.00 60.37 1391 H ILE 163 114.031 4.781 44.043 1.00 25.00 1392 N LEU 164 115.955 6.404 46.097 1.00 37.87 1393 CA LEU 164 116.650 7.473 46.805 1.00 33.53 1394 C LEU 164 115.828 8.132 47.897 1.00 32.57 1395 0 LEU 164 116.206 9.192 48.400 1.00 36.58 1396 CB LEU 164 117.102 8.542 45.815 1.00 30.53 1397 CG LEU 164 118.184 8.139 44.815 1.00 36.53 1398 CD1 LEU 164 118.416 9.266 43.820 1.00 26.74 1399 CD2 LEU 164 119.468 7.794 45.562 1.00 30.59 1400 H LEU 164 115.309 6.641 45.397 1.00 25.00 1401 N GLU 165 114.737 7.489 48.290 1.00 32.57 1402 CA GLU 165 113.854 8.022 49.320 1.00 32.62 1403 C GLU 165 114.537 8.326 50.655 1.00 35.56 1404 0 GLU 165 114.298 9.368 51.267 1.00 35.70 1405 CB GLU 165 112.683 7.058 49.551 1.00 39.90 1406 CG GLU 165 111.645 7.571 50.549 1.00 50.03 1407 CD GLU 165 111.021 8.886 50.115 1.00 59.83 1408 OE1 GLU 165 110.492 8.952 48.983 1.00 63.90 1409 OE2 GLU 165 111.069 9.862 50.899 1.00 58.42 1410 H GLU 165 114.553 6.614 47.898 1.00 25.00 1411 N ASP 166 115.411 7.431 51.091 1.00 37.81 1412 CA ASP 166 116.079 7.609 52.369 1.00 43.12 1413 C ASP 166 117.546 8.030 52.268 1.00 40.48 1414 0 ASP 166 118.274 8.039 53.262 1.00 40.91 1415 CB ASP 166 115.899 6.352 53.234 1.00 51.99 1416 CG ASP 166 114.532 6.303 53.902 1.00 67.29 1417 OD1 ASP 166 114.268 7.173 54.761 1.00 74.04 1418 OD2 ASP 166 113.712 5.423 53.552 1.00 74.06 1419 H ASP 166 115.669 6.693 50.506 1.00 25.00 1420 N ALA 167 117.939 8.459 51.075 1.00 34.07 1421 CA ALA 167 119.298 8.902 50.806 1.00 30.06 1422 c C ALA 167 119.664 10.182 51.554 1.00 33.12 1423 o 0 ALA 167 120.759 10.292 52.103 1.00 34.41 1424 CB ALA 167 119.488 9.090 49.308 1.00 25.56 1425 H ALA 167 117.260 8.486 50.375 1.00 25.00 1426 N LEU 168 118.737 11.134 51.593 1.00 34.35 1427 CA LEU 168 118.975 12.403 52.268 1.00 29.26 1428 C LEU 168 119.184 12.226 53.764 1.00 32.06 1429 0 LEU 168 120.199 12.656 54.311 1.00 34.07 1430 CB LEU 168 117.820 13.381 52.024 1.00 25.73 1431 CG LEU 168 117.980 14.767 52.671 1.00 29.40 1432 CD1 LEU 168 119.241 15.454 52.153 1.00 22.56 1433 CD2 LEU 168 116.765 15.635 52.397 1.00 28.30 1434 H LEU 168 117.879 10.944 51.168 1.00 25.00 1435 N ALA 169 118.224 11.593 54.425 1.00 32.55 1436 CA ALA 169 118.317 11.372 55.865 1.00 37.53 1437 C ALA 169 119.561 10.552 56.227 1.00 37.81 1438 0 ALA 169 120.273 10.873 57.185 1.00 38.90 1439 CB ALA 1669 117.058 10.680 56.370 1.00 36.88 1440 H ALA 169 117.444 11.265 53.938 1.00 25.00 1441 N PHE 170 119.830 9.520 55.429 1.00 30.70 1442 CA PHE 170 120.976 8.640 55.635 1.00 29.14 1443 C PHE 170 122.296 9.413 55.592 1.00 31.93 1444 0 PHE 170 123.046 9.432 56.573 1.00 35.80 1445 CB PHE 170 120.978 7.538 54.569 1.00 27.52 1446 CG PHE 170 122.093 6.538 54.719 1.00 29.21 1447 CD1 PHE 170 122.055 5.576 55.722 1.00 32.25 1448 CD2 PHE 170 123.178 6.553 53.850 1.00 31.23 11444499 CCEE11 PHE 170 123.085 4.642 55.854 1.0035.77 1 1445500 C CEE22 PHE 170 124.213 5.624 53.974 1.0028.29 1 1445511 C CZZ PHE 170 124.166 4.668 54.977 1.0033.63 1 1445522 H H PHE 170 119.237 9.336 54.671 1.0025.00 1 1445533 N N SER 171 122.572 10.054 54.460 1.0029.96 1 1445544 C CAA SER 171 123.803 10.817 54.297 1.0023.74 1 1445555 C C SER 171 123.888 11.970 55.293 1.0025.49 1 1445566 o 0 SER 171 124.951 12.232 55.845 1.0030.00 1 1445577 C CBB SER 171 123.927 11.333 52.860 1.0025.16 1 1445588 O OGG SER 171 122.818 12.137 52.501 1.0031.46 1 1445599 H H SER 171 121.937 10.029 53.708 1.0025.00 1 1446600 H HGG SER 171 122.754 12.902 53.078 1.0025.00 1 1446611 N N THR 172 122.761 12.625 55.557 1.0025.72 1 1446622 C CAA THR 172 122.728 13.746 56.490 1.0025.18 1 1446633 C C THR 172 123.183 13.367 57.902 1.0030.69 1 1446644 O O THR 172 124.122 13.961 58.438 1.0029.76 1 1446655 C CBB THR 172 121.311 14.390 56.574 1.0024.33 1 1446666 O OGG11 THR 172 120.958 14.958 55.307 1.0019.73 1467 CG2 THR 172 121.282 15.499 57.620 1.0016.92 1468 H T THHRR 172 121.932 12.351 55.113 1.0025.00 1469 HG1 T THHRR 172 120.938 14.264 54.646 1.0025.00 1470 N I ILLEE 173 122.542 12.363 58.489 1.0034.29 1471 CA I ILLEE 173 122.875 11.951 59.848 1.0037.02 11447722 C I ILLEE 173 124.319 11.488 60.017 1.0031.30 11447733 O I ILLEE 173 124.956 11.777 61.032 1.0034.03 1474 CB I ILLEE 173 121.894 10.870 60.384 1.0042.89 1475 CG1 I ILLEE 173 122.082 10.702 61.893 1.0046,46 1476 CG2 I ILLEE 173 122.115 9.539 59.673 1.0043.32 1477 CD11 ILE 173 121.040 9.829 62.553 1.0058.82 1478 H ILE 173 121.833 11.884 58.002 1.0025.00 1479 N H HIISS 174 124.848 10.790 59.020 1.0027.02 1480 CA HHIISS 174 126.220 10.309 59.100 1.0030.73 1481 C HHIISS 174 127.251 11.412 58.870 1.0030.72 1482 O HHIISS 174 128.261 11.477 59.574 1.0032.05 1483 CB HHIISS 174 126.431 9.118 58.166 1.0032.72 1484 CG HHIISS 174 125.701 7.884 58.603 1.0042.58 1485 ND1 HHIISS 174 125.738 7.418 59.902 1.0043.81 1486 CD2 HHIISS 174 124.891 7.036 57.925 1.0039.61 1487 CE1 HHIISS 174 124.981 6.339 60.005 1.0038.39 1488 NE2 HHIISS 174 124.457 6.086 58.820 1.0038.65 1489 H HHIISS 174 124.304 10.608 58.221 1.0025.00 1490 HD1 HHIISS 174 126.233 7.787 60.656 1.0025.00 1491 HE2 HHIISS 174 123.858 5.338 58.611 1.0025.00 1492 N LLEEUU 175 126.970 12.310 57.931 1.0030.47 1493 CA LLEEUU 175 127.874 13.420 57.655 1.0024.51 1494 C LLEEUU 175 127.926 14.333 58.880 1.0023.90 1495 0 LLEEUU 175 128.999 14.803 59.267 1.0027.49 1496 CB LLEEUU 175 127.429 14.193 56.408 1.0018.74 1497 CG LLEEUU 175 127.687 13.517 55.054 1.0019.75 1498 CD1 LLEEUU 175 127.007 14.295 53.935 1.0019.14 1499 CD2 LLEEUU 175 129.187 13.404 54.789 1.0013.66 1500 H LLEEUU 175 126.143 12.235 57.409 1.0025.00 1501 N GLU 176 126.781 14.535 59.524 1.00 23.45 1502 CA GLU 176 126.7221 15.374 60.717 1.00 29.31 1503 C GLU 176 127.596 14.788 61.814 1.00 29.58 1504 0 GLU 176 128.222 15.519 62.580 1.00 30.33 1505 CB GLU 176 125.292 15.477 61.247 1.00 28.86 1506 CG GLU 176 124.338 16.265 60.381 1.00 41.02 1507 CD GLU 176 122.976 16.431 61.032 1.00 50.96 1508 OE1 GLU 176 122.409 15.422 61.511 1.00 58.24 1509 OE2 GLU 176 122.474 17.574 61.069 1.00 53.02 1510 H GLU 176 125.956 14.127 59.182 1.00 25.00 1511 N SER 177 127.615 13.461 61.890 1.00 31.99 1512 CA SER 177 128.394 12.746 62.894 1.00 33.70 1513 C SER 177 129.905 12.777 62.620 1.00 29.73 1514 0 SER 177 130.710 12.952 63.541 1.00 31.31 1515 CB SER 177 127.896 11.299 62.986 1.00 33.08 1516 OG SER 177 128.446 10.626 64.103 1.00 42.66 1517 H SER 177 127.077 12.944 61.259 1.00 25.00 1518 HG SER 177 128.220 11.094 64.907 1.00 25.00 1519 N ALA 178 130.283 12.652 61.352 1.00 26.67 1520 CA ALA 178 131.692 12.641 60.970 1.00 25.61 1521 C ALA 178 132.351 14.013 60.858 1.00 28.58 1522 0 ALA 178 133.540 14.162 61.153 1.00 23.60 1523 CB ALA 178 131.862 11.884 59.665 1.00 22.60 1524 H ALA 178 129.599 12.566 60.656 1.00 25.00 1525 N ALA 179 131.568 15.018 60.475 1.00 25.11 1526 CA ALA 179 132.068 16.376 60.268 1.00 25.17 1527 C ALA 179 133.071 16.983 61.254 1.00 25.37 1528 0 ALA 179 134.141 17.430 60.844 1.00 25.58 1529 CB ALA 179 130.903 17.340 60.044 1.00 21.50 1530 H ALA 179 130.617 14.840 60.325 1.00 25.00 1531 N PRO 180 132.771 16.963 62.564 1.00 27.61 1532 CA PRO 180 133.680 17.541 63.565 1.00 28.57 1533 C PRO 180 135.132 17.058 63.584 1.00 30.64 1534 0 PRO 180 135.994 17.724 64.155 1.00 37.22 1535 CB PRO 180 132.988 17.206 64.889 1.00 25.80 1536 CG PRO 180 131.540 17.118 64.518 1.00 31.06 1537 CD PRO 180 131.597 16.360 63.221 1.00 30.35 1538 N HIS 181 135.414 15.910 62.980 1.00 28.35 1539 CA HIS 181 136.772 15.377 63.013 1.00 27.57 1540 C HIS 181 137.470 15.237 61.672 1.00 26.99 1541 0 HIS 181 138.529 14.611 61.584 1.00 29.22 1542 CB HIS 181 136.764 14.035 63.740 1.00 30.76 1543 CG HIS 181 136.153 14.103 65.104 1.00 32.51 1544 ND1 HIS 181 134.893 13.619 65.379 1.00 34.64 1545 CD2 HIS 181 136.607 14.652 66.257 1.00 34.04 1546 CE1 HIS 181 134.593 13.870 66.641 1.00 35.16 1547 NE2 HIS 181 135.615 14.495 67.196 1.00 38.60 1548 H HIS 181 134.717 15.429 62.478 1.00 25.00 1549 HD1 HIS 181 134.298 13.158 64.739 1.00 25.00 1550 HE2 HIS 181 135.666 14.802 68.128 1.00 25.00 1551 N LEU 182 136.890 15.827 60.635 1.00 22.56 1552 CA LEU 182 137.468 15.750 59.303 1.00 22.65 1553 C LEU 182 138.532 16.821 59.103 1.00 24.98 1554 O LEU 182 138.494 17.878 59.741 1.00 22.99 1555 CB LEU 182 136.372 15.900 58.243 1.00 25.05 1556 CG LEU 182 135.271 14.835 58.205 1.00 23.65 1557 CD1 LEU 182 134.178 15.274 57.249 1.00 17.28 1558 CD2 LEU 182 135.849 13.483 57.786 1.00 20.03 1559 H LEU 182 136.072 16.351 60.762 1.00 25.00 1560 N LYS 183 139.494 16.528 58.236 1.00 22.16 1561 CA LYS 183 140.556 17.469 57.926 1.00 25.90 1562 C C LYS 183 139.982 18.573 57.045 1.00 30.39 1563 O 0 LYS 183 138.898 18.429 56.468 1.00 31.71 1564 CB LYS 183 141.696 16.767 57.183 1.00 27.62 1565 CG LYS 183 141.274 16.122 555.871 1.00 37.10 1566 CD LYS 183 142.437 15.441 55.169 1.00 45.13 1567 CE LYS 183 141.974 14.764 53.885 1.00 50.33 1568 NZ LYS 183 143.088 14.040 53.210 1.00 57.79 1569 H LYS 183 139.473 15.658 57.786 1.00 25.00 1570 1 HZ LYS 183 143.846 14.713 52.975 1.00 25.00 1571 2HZ LYS 183 143.463 13.311 53.852 1.00 25.00 1572 3HZ LYS 183 142.736 13.592 52.341 1.00 25.00 1573 N SER 184 140.714 19.674 56.944 1.00 27.77 1574 CA SER 184 140.304 20.802 56.122 1.00 28.80 1575 C SER 184 140.970 20.675 54.752 1.00 27.61 1576 0 SER 184 142.084 20.158 54.645 1.00 26.37 1577 CB SER 184 140.702 22.109 56.805 1.00 28.03 1578 OG SEER 184 140.003 22.254 58.031 1.00 32.93 1579 H SER 184 141.565 19.725 57.420 1.00 25.00 1580 HG SER 184 140.193 21.517 58.620 1.00 25.00 1581 N PRO 185 140.312 21.171 53.689 1.00 26.21 1582 CA PRO 185 139.003 21.834 53.680 1.00 23.45 1583 C PRO 185 137.767 20.926 53.597 1.00 24.54 1584 0 PRO 185 136.636 21.425 53.589 1.00 23.22 1585 CB PRO 185 139.109 22.737 52.458 1.00 21.98 1586 CG PRO 185 139.858 21.876 51.503 1.00 21.03 1587 CD PRO 185 140.949 21.263 52.361 1.00 21.80 1588 N LEU 186 137.969 19.608 53.570 1.00 21.43 1589 CA LEU 186 136.852 18.666 53.483 1.00 21.42 1590 C LEU 186 135.780 18.964 54.522 1.00 22.24 1591 0 LEU 186 134.586 18.987 54.210 1.00 20.84 1592 CB LEU 186 137.331 17.220 53.654 1.00 23.63 1593 CG LEU 186 136.217 16.160 53.646 1.00 21.09 1594 CD1 LEU 186 135.491 16.145 52.292 1.00 20.03 1595 CD2 LEU 186 136.800 14.800 53.943 1.00 21.57 1596 H LEU 186 138.882 19.259 53.605 1.00 25.00 1597 N ARG 187 136.221 19.208 55.751 1.00 16.73 1598 CA ARG 187 135.326 19.515 56.859 1.00 22.57 1599 C ARG 187 134.427 20.723 56.564 1.00 27.49 1600 0 ARG 187 133.225 20.693 56.848 1.00 26.35 1601 CB ARG 187 136.146 19.777 58.117 1.00 17.71 1602 CG ARG 187 135.325 20.087 59.343 1.00 21.93 1603 CD ARG 187 136.235 20.478 60.483 1.00 31.75 1604 NE ARG 187 135.507 20.685 61.727 1.00 46.15 1605 CZ ARG 187 136.087 20.961 62.891 1.00 58.70 1606 NH1 ARG 187 137.412 21.066 62.970 1.00 57.84 1607 NH2 ARG 187 135.344 21.111 63.982 1.00 58.69 1608 H ARG 187 137.182 19.161 55.923 1.00 25.00 1609 HE ARG 187 134.530 20.613 61.708 1.00 25.00 1610 1 HH1 ARG 187 137.977 20.941 62.156 1.00 25.00 1611 2HH1 ARG 187 137.843 21.275 63.848 1.00 25.00 1612 1 HH2 ARG 187 134.351 21.012 63.926 1.00 25.00 1613 2HH2 ARG 187 135.779 21.316 64.858 1.00 25.00 1614 N GLU 188 135.010 21.782 56.001 1.00 28.09 1615 CA GLU 188 134.255 22.993 55.667 1.00 26.62 16116 C GLU 188 133.293 22.726 54.516 1.00 22.97 1617 O GLU 188 132.203 23.296 54.462 1.00 21.14 1618 CB GLU 188 135.192 24.153 55.305 1.00 24.01 1619 CG GLU 188 135.934 24.768 56.482 1.00 32.71 1620 CD GLU 188 137.045 23.878 57.014 1.00 42.50 1621 OE1 GLU 188 138.030 23.657 56.279 1.00 43.53 1622 OE2 GLU 188 136.936 23.403 58.165 1.00 47.38 1623 H GLU 188 135.965 21.747 55.798 1.00 25.00 1624 N GLN 189 133.702 21.853 53.601 1.00 19.36 1625 CA GLN 189 132.872 21.496 52.460 1.00 20.62 1626 C GLN 189 131.636 20.728 52.927 1.00 22.47 1627 O GLN 189 130.522 21.010 52.483 1.00 25.58 1628 CB GLN 189 133.672 20.662 51.461 1.00 17.31 1629 CG GLN 189 132.915 20.359 50.187 1.00 24.12 1630 CD GLN 189 133.796 19.780 49.104 1.00 25.67 1631 OE1 GLN 189 133.691 20.162 47.939 1.00 28.92 1632 NE2 GLN 189 134.666 18.850 49.477 1.00 28.68 1633 H GLN 189 134.590 21.445 53.695 1.00 25.00 1634 1HE2 GLN 189 135.235 18.480 48.773 1.00 25.00 1635 2HE2 GLN 189 134.704 18.576 50.413 1.00 25.00 1636 N VAL 190 131.833 19.783 53.846 1.00 22.03 1637 CA VAL 190 130.734 18.983 54.388 1.00 22.50 1638 C VAL 190 129.778 19.864 55.198 1.00 22.00 1639 O VAL 190 128.565 19.846 54.977 1.00 26.49 1640 CB VAL 190 131.255 17.808 55.274 1.00 18.21 1641 CG1 VAL 190 130.093 17.093 55.947 1.00 19.13 1642 CG2 VAL 190 132.037 16.815 54.422 1.00 13.74 1643 H VAL 190 132.742 19.618 54.168 1.00 25.00 1644 N THR 191 130.335 20.638 56.124 1.00 20.35 1645 CA THR 191 129.555 21.541 56.967 1.00 23.43 1646 C THR 191 128.733 22.504 56.116 1.00 23.79 1647 O THR 191 127.564 22.772 56.410 1.00 27.12 1648 CB THR 191 130.478 22.350 57.903 1.00 29.00 1649 OG1 THR 191 131.124 21.454 58.814 1.00 35.12 1650 CG2 THR 191 129.688 23.385 58.691 1.00 32.22 1651 H THR 191 131.304 20.599 56.257 1.00 25.00 1652 HG1 THR 191 131.661 20.824 58.321 1.00 25.00 1653 N HIS 192 129.345 23.015 55.054 1.00 22.27 1654 CA HIS 192 128.658 23.935 54.168 1.00 24.21 1655 C HIS 192 127.530 23.226 53.417 1.00 24.78 1656 O HIS 192 126.421 23.756 53.326 1.00 20.41 1657 CB HIS 192 129.632 24.564 53.173 1.00 17.98 1658 CG HIS 192 128.965 25.446 52.169 1.00 21.55 1659 ND1 HIS 192 128.506 26.707 52.480 1.00 21.86 1660 CD2 HIS 192 128.637 25.234 50.872 1.00 20.40 1661 CE1 HIS 192 127.919 27.234 51.420 1.00 20.03 1662 NE2 HIS 192 127.985 26.360 50.432 1.00 20.23 1663 H HIS 192 130.278 22.766 54.870 1.00 25.00 1664 HD1 HIS 192 128.594 27.143 53.355 1.00 25.00 1665 HE2 HIS 192 127.614 26.486 49.551 1.00 25.00 1666 N ALA 193 127.826 22.038 52.8888 1.00 22.45 1667 CA A ALLAA 193 126.854 21.242 52.139 1.00 20.56 1668 C A ALLAA 193 125.601 20.963 52.964 1.00 22.26 1669 0 A ALLAA 193 124.485 21.072 52.459 1.00 21.49 1670 CB A ALLAA 193 127.483 19.938 51.679 1.00 18.73 1671 H A ALLAA 193 128.729 21.672 53.002 1.00 25.00 1672 N L LEEUU 194 125.791 20.623 54.236 1.00 23.86 1673 CA L LEEUU 194 124.678 20.344 55.136 1.00 25.16 1674 C L LEEUU 194 123.757 21.551 55.298 1.00 26.76 1675 0 L LEEUU 194 122.573 21.391 55.579 1.00 28.61 1676 CB L LEEUU 194 125.194 19.902 56.509 1.00 23.10 1677 CG L LEEUU 194 125.924 18.556 56.579 1.00 26.60 1678 CD1 L LEEUU 194 126.426 18.319 57.992 1.00 20.06 1679 CD2 L LEEUU 194 124.998 17.433 56.149 1.00 18.24 1680 H L LEEUU 194 126.710 20.552 54.574 1.00 25.00 1681 N G GLLUU 195 124.309 22.754 55.149 1.00 33.01 1682 CA G GLLUU 195 123.529 23.987 55.277 1.00 34.61 1683 C G GLLUU 195 123.005 24.448 53.923 1.00 26.09 1684 0 G GLLUU 195 121.952 25.074 53.834 1.00 29.66 1685 CB G GLLUU 195 124.385 25.102 55.884 1.00 38.35 1686 CG G GLLUU 195 124.885 24.816 57.288 1.00 59.66 1687 CD G GLLUU 195 125.945 25.803 57.751 1.00 72.22 1688 OE1 G GLLUU 195 126.800 26.203 56.927 1.00 75.42 1689 OE2 G GLLUU 195 125.931 26.169 58.947 1.00 82.70 1690 H G GLLUU 195 125.263 22.814 54.944 1.00 25.00 1691 N G GLLNN 196 123.747 24.130 52.871 1.00 22.78 1692 CA G GLLNN 196 123.376 24.529 51.527 1.00 20.33 1693 C G GLLNN 196 123.891 23.520 50.515 1.00 19.79 1694 0 G GLLNN 196 125.094 23.463 50.258 1.00 24.78 1695 CB G GLLNN 196 123.980 25.903 51.219 1.00 20.38 1696 CG G GLLNN 196 123.727 26.397 49.807 1.00 24.47 1697 CD G GLLNN 196 122.253 26.591 49.524 1.00 28.74 1698 0E1 G GLLNN 196 121.622 27.490 50.074 1.00 32.30 1699 NE2 G GLLNN 196 121.694 25.744 48.667 1.00 21.06 1700 H G GLLNN 196 124.554 23.592 52.995 1.00 25.00 1701 1 HE2 GLN 196 120.741 25.876 48.480 1.00 25.00 1702 2HE2 GLN 196 122.247 25.045 48.258 1.00 25.00 1703 N CYS 197 122.992 22.727 49.942 1.00 19.52 1704 CA CYS 197 123.399 21..749 48.944 1.00 17.94 1705 C CYS 197 123.782 22.497 47.669 1.00 18.82 1706 0 CYS 197 123.316 23.614 47.428 1.00 19.62 1707 CB CYS 197 122.278 20.743 48.669 1.00 21.42 1708 SG CYS 197 120.832 21.394 47.800 1.00 42.82 1709 H CYS 197 122.056 22.808 50.202 1.00 25.00 1710 N LEU 198 124.626 21.878 46.856 1.00 19.01 1711 CA LEU 198 125.094 22.489 45.620 1.00 20.23 1712 C LEU 198 123.986 22.760 44.610 1.00 23.16 1713 O LEU 198 123.868 23.867 44.096 1.00 26.68 1714 CB LEU 198 126.174 21.608 44.981 1.00 13.53 1715 CG LEU 198 126.762 22.058 43.640 1.00 20.37 1716 CD1 LEU 198 127.388 23.440 43.773 1.00 19.35 1717 CD2 LEU 198 127.789 21.044 43.158 1.00 18.28 1718 H LEU 198 124.968 21.004 47.109 1.00 25.00 1719 N HIS 199 123.160 21.752 44.354 1.00 24.27 1720 CA HIS 199 122.079 21.859 43.379 1.00 22.48 1721 C HIS 199 121.089 23.001 43.608 1.00 19.15 1722 0 HIS 199 120.586 23.582 42.653 1.00 19.66 1723 CB HIS 199 121.327 20.523 43.277 1.00 22.51 1724 CG HIS 199 120.225 20.519 42.261 1.00 16.72 1725 ND1 HIS 199 120.452 20.697 40.911 1.00 19.56 1726 CD2 HIS 199 118.885 20.360 42.396 1.00 15.14 1727 CE1 HIS 199 119.303 20.648 40.261 1.00 15.68 1728 NE2 HIS 199 118.338 20.444 41.138 1.00 19.96 1729 H HIS 199 123.297 20.912 44.822 1.00 25..00 1730 HD1 HIS 199 121.340 20.834 40.498 1.00 25.00 1731 HE2 HIS 199 117.376 20.343 40.929 1.00 25.00 1732 N LYS 200 120.811 23.323 44.864 1.00 18.06 1733 CA LYS 200 119.853 24.377 45.170 1.00 19.34 1734 C LYS 200 120.463 25.726 45.548 1.00 21.28 1735 0 LYS 200 119.755 26.617 46.012 1.00 20.62 1736 CB LYS 200 118.898 23.893 46.264 1.00 17.06 1737 CG LYS 200 118.144 22.630 45.875 1.00 17.06 1738 CD LYS 200 117.287 22.086 47.005 1.00 18.82 1739 CE LYS 200 116.597 20.804 46.559 1.00 16.83 1740 NZ LYS 200 115.820 20.155 47.645 1.00 19.41 1741 H LYS 200 121.264 22.869 45.599 1.00 25.00 1742 1HZ LYS 200 1166.454 19.923 48.436 1.00 25.00 1743 2HZ LYS 200 115.081 20.807 47.978 1.00 25.00 1744 3HZ LYS 200 115.377 19.285 47.288 1.00 25.00 1745 N GLY 201 121.768 25.881 45.343 1.00 23.54 1746 CA GLY 201 122.424 27.136 45.675 1.00 19.60 1747 C GLY 201 122.583 28.062 44.482 1.00 19.35 1748 0 GLY 201 122.569 27.613 43.338 1.00 21.61 1749 H GLY 201 122.299 25.166 44.933 1.00 25.00 1750 N VAL 202 122.685 29.363 44.734 1.00 17.34 1751 CA VAL 202 122.871 30.327 43.653 1.00 17.16 1752 C VAL 202 124.281 30.084 43.108 1.00 20.63 1753 O VAL 202 125.248 30.059 43.874 1.00 22.87 1754 CB V VAALL 202 122.722 31.778 44.168 1.00 17.85 1755 CG1 V VAALL 202 123.062 32.782 43.071 1.00 19.32 1756 CG2 VAL 202 121.301 32.003 44.645 1.00 15.75 1757 H VAL 202 122.625 29.676 45.655 1.00 25.00 1758 N PRO 203 124.414 29.905 41.780 1.00 18.06 1759 CA PRO 203 125.705 29.652 41.128 1.00 19.86 1760 C PRO 203 126.889 30.506 41.588 1.00 23.15 1761 0 PRO 203 127.827 29.974 42.172 1.00 27.00 1762 CB PRO 203 125.378 29.840 39.650 1.00 21.47 1763 CG PRO 203 123.982 29.300 39.574 1.00 19.55 1764 CD PRO 203 123.332 29.952 40.780 1.00 17.62 1765 N ARG 204 126.844 31.817 41.365 1.00 21.91 1766 CA ARG 204 127.949 32.683 41.781 1.00 20.91 1767 C ARG 204 128.283 32.568 43.265 1.00 20.45 1768 0 ARG 204 129.455 32.598 43.638 1.00 25.04 1769 CB ARG 204 127.681 34.149 41.426 1.00 22.61 1770 CG ARG 204 127.940 34.519 39.972 1.00 18.14 1771 CD ARG 204 129.420 34.487 39.618 1.00 21.89 1772 NE ARG 204 129.852 33.202 39.074 1.00 23.42 1773 CZ ARG 204 130.953 33.027 38.345 1.00 28.33 1774 NH1 ARG 204 131.747 34.055 38.069 1.00 25.07 1775 NH2 ARG 204 131.248 31.827 37.862 1.00 26.89 1776 H ARG 204 126.071 32.201 40.913 1.00 25.00 1777 HE ARG 204 129.297 32.416 39.258 1.00 25.00 1778 1 HH1 ARG 204 131.521 34.967 38.404 1.00 25.00 1779 2HH1 ARG 204 132.570 33.921 37.522 1.00 25.00 1780 1 HH2 ARG 2004 130.647 31.051 38.047 1.00 25.00 1781 2HH2 ARG 204 132.077 31.699 37.316 1.00 25.00 1782 N VAL 205 127.264 32.431 44.108 1.00 17.32 1783 CA VAL 205 127.496 32.312 45.545 1.00 18.99 1784 C VAL 205 128.267 31.034 45.866 1.00 20.53 1785 0 VAL 205 129.220 31.048 46.647 1.00 24.18 1786 CB VAL 205 126.175 32.309 46.339 1.00 19.83 1787 CG1 VAL 205 126.442 32.022 47.811 1.00 14.97 1788 CG2 VAL 205 125.473 33.642 46.190 1.00 21.52 1789 H VAL 205 126.353 32.398 43.764 1.00 25.00 1790 N GLU 206 127.862 29.933 45.249 1.00 22.23 1791 CA GLU 206 128.519 28.649 45.478 1.00 22.70 1792 C GLU 206 129.919 28.601 44.876 1.00 18.65 1793 0 GLU 206 130.836 28.029 45.469 1.00 20.84 1794 CB GLU 206 127.648 27.506 44.957 1.00 17.73 1795 CG GLU 206 126.317 27.413 45.683 1.00 20.17 1796 CD GLU 206 126.478 27.407 47.201 1.00 26.03 1797 OE1 GLU 206 127.190 26.523 47.721 1.00 21.64 1798 OE2 GLU 206 125.895 28.283 47.876 1.00 20.28 1799 H GLU 206 127.111 29.981 44.620 1.00 25.00 1800 N THR 207 130.081 29.223 43.714 1.00 18.09 1801 CA THR 207 131.369 29.291 43.038 1.00 21.23 1802 C THR 207 132.373 30.057 43.909 1.00 25.71 1803 0 THR 207 133.474 29.568 44.179 1.00 28.93 1804 CB THR 207 131.219 29.984 41.672 1.00 24.22 1805 0G1 THR 207 130.529 29.1077 40.770 1.00 28.95 1806 CG2 THR 207 132.573 30.379 41.088 1.00 23.10 1807 H THR 207 129.311 29.644 43.289 1.00 25.00 1808 HG1 THR 207 131.030 28.287 40.685 1.00 25.00 1809 N ARG 208 131.973 31.238 44.374 1.00 24.65 1810 CA ARG 208 132.825 32.070 45.221 1.00 25.56 1811 C ARG 208 133.292 31.273 46.432 1.00 25.87 1812 0 ARG 208 134.472 31.289 46.780 1.00 27.73 1813 CB ARG 208 132.059 33.314 45.682 1.00 25.72 1814 CG ARG 208 132.836 34.258 46.588 1.00 31.65 1815 CD ARG 208 134.062 34.826 45.892 1.00 39.53 1816 NE ARG 208 134.374 36.184 46.344 1.00 46.43 1817 CZ ARG 208 135.283 36.488 47.266 1.00 47.18 1818 NH11 ARG 208 135.991 35.534 47.858 1.00 54.31 1819 NH2 ARG 208 135.492 37.754 47.592 1.00 54.01 1820 H ARG 208 131.077 31.566 44.139 1.00 25.00 1821 HE ARG 208 133.881 36.924 45.937 1.00 25.00 1822 1HH1 ARG 208 135.847 34.577 47.610 1.00 25.00 1823 2HH1 ARG 208 136.673 35.775 48.548 1.00 25.00 1824 1 HH2 ARG 208 134.962 38.478 47.150 1.00 25.00 1825 2HH2 ARG 208 136.172 37.986 48.287 1.00 25.00 1826 N PHE 209 132.364 30.556 47.056 1.00 25.17 1827 CA PHE 209 132.688 29.750 48.224 1.00 23.72 1828 C PHE 209 133.677 28.632 47.908 1.00 24.69 1829 0 PHE 209 134.656 28.442 48.626 1.00 24.23 1830 CB PHE 209 131.430 29.135 48.838 1.00 22.94 1831 CG PHE 209 131.721 28.195 49.976 1.00 22.62 1832 CD1 PHE 209 132.019 28.691 51.242 1.00 22.83 1833 CD2 PHE 209 131.745 26.817 49.773 1.00 20.76 1834 CE1 PHE 209 132.336 27.824 52.293 1.00 22.43 1835 CE2 PHE 209 132.060 25.946 50.813 1.00 24.13 1836 CZ PHE 209 132.358 26.450 52.075 1.00 22.16 1837 H PHE 209 131.439 30.580 46.728 1.00 25.00 1838 N PHE 210 133.399 27.872 46.856 1.00 24.89 1839 CA PHE 210 134.263 26.765 46.486 1.00 21.48 1840 C PHE 210 135.671 27.241 46.172 1.00 23.23 1841 0 PHE 210 136.645 26.676 46.671 1.00 24.15 1842 CB PHE 210 133.688 25.989 45.296 1.00 18.25 1843 CG PHE 210 134.4776 24.754 44.944 1.00 20.04 1844 CD1 PHE 210 134.506 23.661 45.811 1.00 17.95 1845 CD2 PHE 210 135.212 24.694 43.763 1.00 19.06 1846 CE1 PHE 210 135.260 22.525 45.510 1.00 17.28 1847 CE2 PHE 210 135.972 23.563 43.450 1.00 21.18 1848 CZ PHE 210 135.995 22.476 44.329 1.00 18.42 1849 H PHE 210 132.602 28.062 46.315 1.00 25.00 1850 N ILE 211 135.781 28.290 45.368 1.00 26.53 1851 CA ILE 211 137.086 28.818 44.997 1.00 27.06 1852 C ILE 211 137.917 29.248 46.205 1.00 27.01 1853 0 ILE 211 138.953 28.652 46.490 1.00 25.02 1854 CB ILE 211 136.967 30.015 44.023 1.00 23.08 1855 CG1 ILE 211 136.317 29.574 42.713 1.00 22.07 1856 CG2 ILE 211 138.344 30.603 43.737 1.00 18.73 1857 CD1 ILE 211 136.163 30.700 41.701 1.00 22.59 1858 H I ILLEE 211 134.968 28.712 45.022 1.00 25.00 1859 N S SEERR 212 137.430 30.233 46.949 1.00 26.45 1860 CA S SEERR 212 138.174 30.758 48.087 1.00 29.47 1 1886611 C S SEERR 212 138.263 29.914 49.355 1.00 29.82 11886622 0 S SEERR 212 139.317 29.873 49.993 1.00 31.08 1863 CB SER 212 137.691 32.173 48.425 1.00 28.90 1864 OG SER 212 136.311 32.186 48.742 1.00 48.04 1865 H SER 212 136.550 30.622 46.740 1.00 25.00 1866 HG SER 212 136.156 31.647 49.517 1.00 25.00 1867 N SER 213 137.175 29.249 49.728 1.00 25.54 1868 CA SER 213 137.173 28.447 50.949 1..0025.42 1869 C SER 213 137.555 26.969 50.823 1.00 23.90 1870 0 SER 213 138.019 26.371 51.794 1.00 29.58 1871 CB SER 213 135.820 28.566 51.662 1.00 19.77 1872 OG SER 213 135.503 29.920 51.942 1.00 36.00 1873 H SER 213 136.366 29.279 49.173 1.00 25.00 1874 HG SER 213 135.449 30.406 51.120 1.00 25.00 1875 N ILE 214 137.390 26.376 49.645 1.00 20.94 1876 CA ILE 214 137.701 24.958 49.502 1.00 20.03 1877 C ILE 214 138.869 24.617 48.591 1.00 20.98 1878 0 ILE 214 139.914 24.174 49.065 1.00 23.05 1879 CB ILE 214 136.463 24.144 49.041 1.00 20.03 1880 CG1 ILE 214 135.255 24.455 49.932 1.00 15.38 1881 CG2 ILE 214 136.778 22.640 49.046 1.00 14.86 1882 CD1 ILE 214 135.488 24.207 51.418 1.00 14.56 1883 H ILE 214 137.066 26.887 48.873 1.00 25.00 1884 N TYR 215 138.696 24.823 47.289 1.00 18.70 1885 CA TYR 215 139.733 24.490 46.323 1.00 22.93 1886 C TYR 215 141.076 25.168 46.582 1.00 25.73 1887 0 TYR 215 142.128 24.545 46.450 1.00 25.96 1888 CB TYR 215 139.258 24.777 44.899 1.00 19.89 1889 CG TYR 215 139.859 23.834 43.884 1.00 17.39 1890 CD1 TYR 215 139.726 22.455 44.030 1.00 18.08 1891 CD2 TYR 215 140.557 24.315 42.782 1.00 19.17 1892 CE1 TYR 215 140.275 21.575 43.102 1.00 17.39 1893 CE2 TYR 215 141.113 23.445 41.843 1.00 16.77 1894 CZ TYR 215 140.967 22.076 42.010 1.00 21.36 1895 OH TYR 215 141.517 21.212 41.088 1.00 25.91 1896 H TYR 215 137.858 25.217 46.973 1.00 25.00 1897 HH TYR 215 141.317 20.302 41.340 1.00 25.00 1898 N ASP 216 141.037 26.434 46.969 1.00 26.71 1899 CA ASP 216 142.254 27.184 47.250 1.00 32.33 1900 C ASP 216 143.057 26.532 48.377 1.00 32.46 1901 0 ASP 216 144.288 26.589 48.387 1.00 33.87 1902 CB ASP 216 141.895 28.621 47.636 1.00 35.77 1903 CG ASP 216 143.111 29.514 47.769 1.00 36.73 1904 0D1 ASP 216 143.842 29.670 46.769 1.00 37.16 1905 OD2 ASP 216 143.327 30.062 48.871 1.00 41.08 1906 H ASP 216 140.170 26.885 447.054 1.00 25.00 1907 N LYS 217 142.350 25.910 49.316 1.00 31.70 1908 CA LYS 217 142.978 25.255 50.459 1.00 29.37 1909 C LYS 217 143.134 23.745 50.269 1.00 30.32 1910 0 LYS 217 143.506 23.029 51.200 1.00 31.00 1911 CB LYS 217 142.170 25.553 51.724 1.00 26.09 1912 CG LYS 217 142.062 27.033 52.017 1.00 27.73 1913 CD LYS 217 141.185 27.312 53.213 1.00 35.35 1914 CE LYS 217 141.091 28.807 53.463 1.00 40.60 1915 NZ LYS 217 140.124 29.115 54.551 1.00 49.88 1916 H LYS 217 141.376 25.876 49.235 1.00 25.00 1917 1 HZ LYS 217 140.429 28.650 55.430 1.00 25.00 1918 2HZ LYS 217 140.083 30.143 54.698 1.00 25.00 1919 3HZ LYS 217 139.181 28.767 54.284 1.00 25.00 1920 N GLU 218 142.864 23.271 49.057 1.00 31.03 1921 CA GLU 218 142.961 21.855 48.750 1.00 33.23 1922 C GLU 218 144.391 21.489 48.357 1.00 42.71 1923 0 GLU 218 144.932 22.012 47.381 1.00 41.53 1924 CB GLU 218 141.983 21.492 47.626 1.00 32.79 1925 CG GLU 218 141.873 20.007 47.345 1.00 49.16 1926 CD GLU 218 141.324 19.228 48.526 1.00 61.57 1927 OE1 GLU 218 140.147 19.456 48.886 1.00 66.99 1928 OE2 GLU 218 142.066 18.391 49.092 1.00 62.96 1929 H GLU 218 142.616 23.896 48.343 1.00 25.00 1930 N GLN 219 144.974 20.551 49.098 1.00 48.16 1931 CA GLN 219 146.339 20.089 48.858 1.00 52.73 1932 C GLN 219 146.533 19.487 47.467 1.00 49.21 1933 0 GLN 219 147.594 19.622 46.870 1.00 51.36 1934 CB GLN 219 146.733 19.063 49.929 1.00 62.56 1935 CG GLN 219 148.127 19.262 50.531 1.00 81.40 1936 CD GLN 219 148.498 18.186 51.534 1.00 90.93 1937 OE1 GLN 219 148.863 17.072 51.156 1.00 97.11 1938 NE2 GLN 219 148.408 18.512 52.825 1.00 96.41 1939 H GLN 219 144.450 20.162 49.821 1.00 25.00 1940 1 HE2 GLN 219 148.113 19.389 53.115 1.00 25.00 1941 2HE2 GLN 219 148.656 17.793 53.455 1.00 25.00 1942 N SER 220 145.496 18.842 46.950 1.00 47.51 1943 CA SER 220 145.552 18.199 45.636 1.00 47.04 1944 C C SER 220 144.945 19.020 44.487 1.00 45.29 1945 O 0 SER 220 144.577 18.467 43.446 1.00 47.02 1946 CB SER 220 144.862 16.833 45.713 1.00 51.73 1947 OG SER 220 143.585 16.948 46.327 1.00 55.26 1948 H SER 220 144.658 18.796 47.447 1.00 25.00 1949 HG SER 220 143.671 17.280 47.217 1.00 25.00 1950 N LYS 221 144.849 20.332 44.679 1.00 38.03 1951 CA LYS 221 144.270 21.233 43.682 1.00 32.98 1952 C LYS 221 145.037 21.284 42.363 1.00 30.63 1953 0 LYS 221 146.249 21.077 42.328 1.00 33.91 1954 CB LYS 221 144.206 22.649 44.255 1.00 33.08 1955 CG LYS 221 145.584 23.257 44.500 1.00 40.24 1956 CD LYS 221 145.512 24.563 45.257 1.00 53.13 19557 CE LYS 221 146.902 25.093 45.561 1.00 55.90 1958 NZ LYS 221 146.843 26.358 46.344 1.00 67.32 1959 H LYS 221 145.198 20.720 45.508 1.00 25.00 1960 1HZ LYS 221 146.350 26.191 47.244 1.00 25.00 1961 2HZ LYS 221 147.807 26.698 46.533 1.00 25.00 1962 3HZ LYS 221 146.326 27.080 45.800 1.00 25.00 1963 N ASN 222 144.322 21.536 41.273 1.00 28.13 1964 CA ASN 222 144.958 21.675 39.970 1.00 25.27 1965 C ASN 222 145.154 23.174 39.816 1.00 30.00 1966 0 ASN 222 144.187 23.933 39.707 1.00 29.84 1967 CB ASN 222 144.077 21.149 38.843 1.00 22.73 1968 CG ASN 222 144.688 21.390 37.473 1.00 24.93 1969 OD1 ASN 222 144.914 22.534 37.072 1.00 31.82 1970 ND2 ASN 222 144.973 20.317 36.755 1.00 23.78 1971 H ASN 222 143.353 21.640 41.343 1.00 25.00 1972 1 HD2 ASN 222 145.364 20.460 35.868 1.00 25.00 1973 2HD2 ASN 222 144.784 19.432 37.125 1.00 25.00 1974 N ASN 223 146.412 23.596 39.819 1.00 31.07 1975 CA ASN 223 146.759 25.009 39.726 1.00 26.94 1976 C ASN 223 146.273 25.730 38.477 1.00 25.82 1977 0 ASN 223 145.933 26.910 38.538 1.00 27.88 1978 CB ASN 223 148.261 25.185 39.915 1.00 23.98 1979 CG ASN 223 148.739 24.633 41.242 1.00 28.15 1980 0D1 ASN 223 148.586 25.271 42.281 1.00 30.20 1981 ND2 ASN 223 149.291 23.423 41.219 1.00 25.49 1982 H ASN 223 147.118 22.925 39.901 1.00 25.00 1983 1HD2 ASN 223 149.595 23.063 42.082 1.00 25.00 1984 2HD2 ASN 223 149.377 22.938 40.382 1.00 25.00 1985 N VAL 224 146.224 25.036 37.346 1.00 24.73 1986 CA VAL 224 145.743 25.667 36.124 1.00 27.15 1987 C VAL 224 144.263 26.026 36.304 1.00 28.87 1988 0 VAL 224 143.852 27.150 36.019 1.00 29.97 1989 CB VAL 224 145.914 24.742 34.900 1.00 31.17 1990 CG1 VAL 224 145.359 25.404 33.651 1.00 30.27 1991 CG2 VAL 224 147.382 24.400 34.707 1.00 30.28 1992 H VAL 224 146.488 24.096 37.329 1.00 25.00 1993 N LEU 225 143.486 25.089 36.843 1.00 25.78 1994 CA LEU 225 142.057 25.303 37.069 1.00 25.90 1995 C LEU 225 141.792 26.380 38.125 1.00 26.51 1996 0 LEU 225 140.900 27.214 37.956 1.00 26.55 1997 CB LEU 225 141.366 23.991 37.463 1.00 20.07 1998 CG LEU 225 141.398 22.848 36.441 1.00 21.81 1999 CD1 LEU 225 140.664 21.638 36.991 1.00 10.56 2000 CD2 LEU 225 140.780 23.295 35.126 1.00 19.02 2001 H LEU 225 143.883 24.229 37.092 1.00 25.00 2002 N LEU 226 142.566 26.369 39.207 1.00 22.12 2003 CA LEU 226 142.400 27.367 40.261 1.00 27.39 2004 C LEU 226 142.724 28.775 39.743 1.00 28.78 2005 0 LEU 226 141.967 29.720 39.969 1.00 34.36 2006 CB LEU 226 143.282 27.033 41.468 1.00 25.60 2007 CG LEU 226 143.170 27.984 42.6665 1.00 26.39 2008 CD1 LEU 226 141.731 28.037 43.183 1.00 20.17 2009 CD2 LEU 226 144.110 27.532 43.763 1.00 26.04 2010 H LEU 226 143.249 25.673 39.298 1.00 25.00 2011 N ARG 227 143.842 28.904 39.036 1.00 28.64 2012 CA ARG 227 144.270 30.183 38.473 1.00 30.51 2013 C ARG 227 143.186 30.688 37.508 1.00 29.19 2014 0 ARG 227 142.770 31.849 37.567 1.00 25.86 2015 CB ARG 227 145.607 29.989 37.742 1.00 30.51 2016 CG ARG 227 146.171 31.215 37.037 1.00 32.00 2017 CD ARG 227 146.883 32.162 37.981 1.00 35.49 2018 NE ARG 227 147.414 33.314 37.256 1.00 34.46 2019 CZ ARG 227 147.799 34.454 37.822 1.00 32.62 2020 NH1 ARG 227 147.727 34.611 39.136 1.00 33.39 2021 NH2 ARG 227 148.214 35.460 37.066 1.0035.87 2022 H ARG 227 144.402 28.114 38.884 1.0025.00 2023 HE ARG 227 147.480 33.245 36.292 1.0025.00 2024 1 HH1 ARG 227 147.381 33.871 39.712 1.0025.00 2025 2HH1 ARG 227 148.020 35.470 39.554 1.0025.00 2026 1 HH2 ARG 227 148.236 35.359 36.073 1.0025.00 2027 2HH2 ARG 227 148.505 36.315 37.491 1.0025.00 2028 N PHE 228 142.723 29.788 36.645 1.0028.49 2029 CA P PHHEE 228 141.678 30.063 35.656 1.0030.24 2030 C PPHHEE 228 140.411 30.575 36.369 1.0029.56 2031 0 PPHHEE 228 139.909 31.662 36.068 1.0031.17 2032 CB PPHHEE 228 141.394 28.752 34.892 1.0032.31 2033 CG PPHHEE 228 140.441 28.879 33.721 1.0030.15 2034 CD1 PPHHEE 228 139.889 30.103 33.348 1.0029.90 2035 CD2 PHE 228 140.084 27.740 32.999 1.0024.53 2036 CE1 PHE 228 138.994 30.186 32.277 1.0028.21 2037 CE2 P PHHEE 228 139.193 27.811 31.930 1.0023.61 2038 CZ PPHHEE 228 138.646 29.036 31.568 1.0029.31 2039 H PPHHEE 228 143.108 28.886 36.672 1.0025.00 2040 N AALLAA 229 139.935 29.809 37.344 1.0025.42 2041 CA AALLAA 229 138.737 30.156 38.099 1.0025.11 2042 C AALLAA 229 138.808 31.533 38.764 1.0029.20 2043 0 AALLAA 229 137.847 32.310 38.703 1.0026.99 2044 CB AALLAA 229 138.456 29.085 39.135 1.0020.89 2045 H AALLAA 229 140.406 28..982 37.565 1.0025.00 2046 N LLYYSS 230 139.944 31.838 39.389 1.0029.21 2047 CA LLYYSS 230 140.127 33.121 40.068 1.0029.75 2048 C LLYYSS 230 140.100 34.306 39.109 1.0030.11 2049 0 LLYYSS 230 139.405 35.298 39.350 1.0030.69 2050 CB LLYYSS 230 141.434 33.136 40.866 1.0030.27 2051 CG LLYYSS 230 141.422 32.247 42.100 1.0029.79 2052 CD LLYYSS 230 142.686 32.430 42.923 1.0024.40 2053 CE LLYYSS 230 142.595 31.664 44.227 1.0029.55 2054 NZ LLYYSS 230 143.790 31.883 45.079 1.0036.37 2055 H LLYYSS 230 140.676 31.183 39.394 1.0025.00 2056 1HZ LYS 230 143.881 32.896 45.296 1.0025.00 2057 2HZ LYS 230 143.689 31.356 45.965 1.0025.00 2058 33HZ LYS 230 144.640 31.560 44.573 1.0025.00 2059 N LEU 231 140.852 34.201 38.016 1.0031.56 2060 CA L LEEUU 231 140.911 35.275 37.032 1.0030.17 2061 C LLEEUU 231 139.549 35.506 36.394 1.0030.20 2062 0 LLEEUU 231 139.085 36.645 36.299 1.0026.72 2063 CB LLEEUU 231 141.941 34.959 35.941 1.0029.21 2064 CG LLEEUU 231 143.408 34.790 36.340 1.0026.11 2065 CD1 LLEEUU 231 144.232 34.631 35.077 1.0022.49 2066 CD2 LEU 231 143.890 35.990 37.139 1.0022.48 2067 H LEU 231 141.374 33.380 37.869 1.0025.00 2068 N A ASSPP 232 138.898 34.417 35.995 1.0029.28 2069 CA AASSPP 232 137.593 34.490 35.351 1.0028.41 2070 C AASSPP 232 136.549 35.149 36.247 1.0025..56 2071 0 AASSPP 232 135.820 36.044 35.813 1.0025.21 2072 CB AASSPP 232 137.131 33.097 34.932 1.0026.05 2073 CG ASP 232 136.143 33.143 33.793 1.00 33.93 2074 OD1 ASP 232 136.587 33.188 32.627 1.00 32.45 2075 OD2 ASP 232 134.927 33.157 34.060 1.00 29.97 2076 H ASP 232 139.310 33.539 36.141 1.00 25.00 2077 N PHE 233 136.510 34.730 37.507 1.00 24.45 2078 CA PHE 233 135.569 35.286 38.466 1.00 22.77 2079 C PHE 233 135.788 36.788 38.603 1.00 28.10 2080 0 PHE 233 134.835 37.568 38.516 1.00 31.99 2081 CB PHE 233 135.732 34.605 39.831 1.00 19.36 2082 CG PHE 233 134.714 35.035 40.854 1.00 22.51 2083 CD1 PHE 233 1344.857 36.241 41.540 1.00 22.18 2084 CD2 PHE 233 133.604 34.237 41.127 1.00 23.90 2085 CE1 PHE 233 133.906 36.646 42.481 1.00 26.05 2086 CE2 PHE 233 132.650 34.631 42.065 1.00 23.08 2087 CZ PHE 233 132.801 35.839 42.743 1.00 24.51 2088 H PHE 233 137.126 34.022 37.802 1.00 25.00 2089 N ASN 234 137.044 37.189 38.801 1.00 28.39 2090 CA ASN 234 137.393 38.602 38.965 1.00 28.37 2091 C ASN 234 137.079 39.446 37.743 1.00 27.25 2092 0 ASN 234 136.606 40.575 37.868 1.00 32.70 2093 CB ASN 234 138.867 38.762 39.342 1.00 27.32 2094 CG ASN 234 139.152 38.353 40.776 1.00 30.63 2095 0D1 ASN 234 138.242 38.219 41.595 1.00 29.34 2096 ND2 ASN 234 140.426 38.166 41.092 1.00 37.28 2097 H ASN 234 137.753 36.513 38.851 1.00 25.00 2098 1HD2 ASN 234 140.628 37.901 42.015 1.00 25.00 2099 2HD2 ASN 234 141.114 38.292 40.408 1.00 25.00 2100 N LEU 235 137.339 38.902 36.561 1.00 28.66 2101 CA LEU 235 137.059 39.616 35.321 1.00 29.93 2102 C LEU 235 135.551 39.830 35.167 1.00 30.84 2103 0 LEU 235 135.106 40.949 34.908 1.00 31.89 2104 CB LEU 235 137.625 38.852 34.119 1.00 29.05 2105 CG LEU 235 137.476 39.509 32.742 1.00 30.21 2106 CD1 LEU 235 138.045 40.922 32.769 1.00 29.02 2107 CD2 LEU 235 138.173 38.667 31.684 1.00 31.45 2108 H LEU 235 137.721 38.001 36.525 1.00 25.00 2109 N LEU 236 134.766 38.769 35.352 1.00 29.90 2110 CA LEU 236 133.311 38.875 35.245 1.00 28.94 2111 C LEU 236 132.774 39.874 36.263 1.00 28.31 2112 0 LEU 236 131.833 40.623 35.979 1.00 29.04 2113 CB LEU 236 132.632 37.518 35.463 1.00 26.96 2114 CG LEU 236 132.722 36.463 34.359 1.00 32.49 2115 CD1 LEU 236 131.797 35.299 34.694 1.00 28.63 2116 CD2 LEU 236 132.326 37.068 33.026 1.00 30.07 2117 H LEU 236 135.173 37.900 35.561 1.00 25.00 2118 N GLN 237 133.362 39.870 37.454 1.00 25.46 2119 CA GLN 237 132.953 40.777 38.521 1.00 25.58 2120 C GLN 237 133.059 42.231 38.062 1.00 27.92 2121 0 GLN 2337 132.201 43.054 38.387 1.00 29.65 2122 CB GLN 237 133.807 40.549 39.769 1.00 20.55 2123 CG GLN 237 133.342 41.314 40.993 1.00 23.60 2124 CD GLN 237 134.216 41.046 42.197 1.00 31.25 22112255 OOEE11 GLN 237 135.435 41.196 42.134 1.00 31.93 2 2112266 N NEE22 GLN 237 133.602 40.634 43.298 1.00 28.03 2127 H GLN 237 134.094 39.237 37.625 1.00 25.00 2128 1HE2 GLN 237 134.156 40.446 44.081 1.00 25.00 2129 2HE2 GLN 237 132.635 40.519 43.287 1.00 25.00 2130 N MET 238 134.096 42.537 37.286 1.00 28.91 2131 CA M MEETT 238 134.288 43.888 36.776 1.00 33.08 2132 C M MEETT 238 133.084 44.282 35.924 1.00 33.53 2133 0 M MEETT 238 132.562 45.391 36.049 1.00 37.31 2134 CB MET 238 135.573 43.976 35.954 1.00 32.86 2135 CG MET 238 136.836 43.837 36.782 1.00 39.06 2136 SD MET 238 138.318 43.815 35.763 1.00 43.74 2137 CE MET 238 139.508 43.186 36.929 1.00 46.28 2138 H MET 238 134.751 41.842 37.055 1.00 25.00 2139 N LEU 239 132.624 43.356 35.087 1.00 31.84 2140 CA LEU 239 131.465 43.599 34.233 1.00 30.89 2141 c LEU 239 130.219 43.801 35.097 1.00 28.36 2142 o LEU 239 129.450 44.742 34.885 1.00 32.90 2143 CB L LEEUU 239 131.255 42.427 33.271 1.00 29.61 2144 CG L LEEUU 239 129.969 42.432 32.436 1.00 29.85 2145 CD1 L LEEUU 239 129.929 43.636 31.499 1.00 25.22 2146 CD2 L LEEUU 239 129.870 41.138 31.649 1.00 26.65 2147 H L LEEUU 239 133.084 42.491 35.043 1.00 25.00 2148 N H HIISS 240 130.042 42.942 36.095 1.00 25.85 2149 CA H HIISS 240 128.891 43.042 36.990 1.00 28.32 2150 C H HIISS 240 128.885 44.406 37.671 1.00 30.20 2151 0 H HIISS 240 127.824 44.974 37.940 1.00 30.10 2152 CB H HIISS 240 128.925 41.926 38.036 1.00 25.55 2153 CG H HIISS 240 128.881 40.545 37.448 1.00 24.20 2154 ND1 H HIISS 240 129.449 39.455 38.058 1.00 25.29 2155 CD2 H HIISS 240 128.358 40.103 36.283 1.00 21.44 2156 CE1 H HIISS 240 129.289 38.394 37.302 1.00 27.58 2157 NE2 H HIISS 240 128.627 38.750 36.209 1.00 21.74 2158 H H HIISS 240 130.713 42.244 36.233 1.00 25.00 2159 HD11 HIS 240 129.918 39.455 38.924 1.00 25.00 2160 HE2 HIS 240 128.362 38.151 35.470 1.00 25.00 2161 N LYS 241 130.079 44.926 37.935 1.00 34.60 2162 CA LYS 241 130.239 46.230 38.563 1.00 32.03 2163 C LYS 241 129.855 47.374 37.613 1.00 31.99 2164 0 LYS 241 129.280 48.374 38.045 1.00 29.66 2165 CB LYS 241 131.675 46.391 39.072 1.00 32.10 2166 CG LYS 241 131.984 45.614 40.356 1.00 34.40 2167 CD LYS 241 133.447 45.807 40.758 1.00 41.19 2168 CE LYS 241 133.701 45.417 42.208 1.00 49.51 2169 NZ LYS 241 135.044 45.881 42.698 1.00 56.06 2170 H LYS 241 130.875 44.403 37.703 1.00 25.00 2171 1HZ LYS 241 135.111 46.916 42.625 1.00 25.00 2172 2HZ LYS 241 135.179 45.610 43.698 1.00 25.00 2173 3HZ LYS 241 135.803 45.446 42.135 1.00 25.00 2174 N GLN 242 130.121 47.201 36.316 1.00 34.13 2175 CA GLN 242 129.799 48.211 35.303 1.00 38.39 2176 C GLN 242 128.288 48.278 35.161 1.00 39.98 2177 0 GLN 242 127.702 49.353 34.990 1.00 45.19 2178 CB GLN 242 130.376 47.827 33.942 1.00 42.52 2179 CG GLN 242 131.883 47.683 33.920 1.00 60.88 2180 CD GLN 242 132.417 47.252 32.574 1.00 69.61 2181 OE1 GLN 242 131.663 47.052 31.620 1.00 75.13 2182 NE2 GLN 242 133.730 47.102 32.488 1.00 78.40 2183 H GLN 242 130.490 46.358 35.996 1.00 25.00 2184 1 HE2 GLN 242 134.0772 46.820 31.621 1.00 25.00 2185 2HE2 GLN 242 134.282 47.272 33.272 1.00 25.00 2186 N GLU 243 127.674 47.105 35.219 1.00 33.89 2187 CA GLU 243 126.233 46.975 35.107 1.00 28.66 2188 C GLU 243 125.568 47.591 36.325 1.00 28.27 2189 0 GLU 243 124.635 48.381 36.193 1.00 32.26 2190 CB GLU 243 125.857 45.505 34.982 1.00 25.09 2191 CG GLU 243 126.416 44.820 33.741 1.00 24.03 2192 CD GLU 243 126.182 43.329 33.738 1.00 26.58 2193 OE1 GLU 243 125.633 42.810 34.726 1.00 24.63 2194 OE2 GLU 243 126.556 42.665 32.750 1.00 29.69 2195 H GLU 243 128.248 46.333 35.341 1.00 25.00 2196 N LEU 244 126.078 47.267 37.508 1.00 24.94 2197 CA LEU 244 125.522 47.798 38.745 1.00 30.48 2198 C LEU 244 125.635 49.324 38.766 1.00 36.45 2199 0 LEU 244 124.700 50.021 39.163 1.00 35.07 2200 CB LEU 244 126.233 47.185 39.957 1.00 28.96 2201 CG LEU 244 125.765 47.658 41.339 1.00 29.10 2202 CD1 LEU 244 124.249 47.527 41.484 1.00 25.23 2203 CD2 LEU 244 126.464 46.859 42.423 1.00 27.57 2204 H LEU 244 126.855 46.662 37.535 1.00 25.00 2205 N ALA 245 126.778 49.832 38.318 1.00 37.15 2206 CA ALA 245 127.023 51.268 38.270 1.00 38.62 2207 C ALA 245 126.030 51.937 37.325 1.00 39.57 2208 0 ALA 245 125.352 52.902 37.692 1.00 43.21 2209 CB ALA 245 128.452 51.539 37.802 1.00 35.23 2210 H ALA 245 127.477 49.215 38.032 1.00 25.00 2211 N GLN 246 125.920 51.380 36.123 1.00 35.82 2212 CA GLN 246 125.025 51.888 35.086 1.00 40.78 2213 C GLN 246 123.577 51.989 35.566 1.00 43.61 2214 0 GLN 246 122.907 53.016 35.404 1.00 43.37 2215 CB GLN 246 125.088 50.963 33.872 1.00 42.45 2216 CG GLN 246 124.151 51.350 32.733 1.00 59.73 2217 CD GLN 246 124.146 50.338 31.610 1.00 65.77 2218 0E1 GLN 246 125.149 49.663 31.357 1.00 67.95 2219 NE2 GLN 246 123.009 50.223 30.920 1.00 66.48 2220 H GLN 246 126.450 50.576 35.964 1.00 25.00 2221 1HE2 GLN 246 123.038 49.559 30.198 1.00 25.00 2222 2HE2 GLN 246 122.232 50.763 31.132 1.00 25.00 2223 N VAL 247 123.115 50.916 36.185 1.00 39.07 2224 CA VAL 247 121.762 50.830 36.692 1.00 37.02 2225 C VAL 247 121.538 51.732 37.908 1.00 40.33 2226 0 VAL 247 120.435 52.248 38.106 1.00 39.92 2227 CB VAL 247 121.387 49.341 36.946 1.00 35.95 2228 CG1 VAL 247 120.417 49.201 38.091 1.00 37.82 2229 CG2 VAL 247 120.794 48.754 35.686 1.00 32.90 2230 H VAL 247 123.730 50.170 36.340 1.00 25.00 2231 N SER 248 122.579 51.926 38.715 1.00 44.51 2232 CA SER 248 122.483 52.798 39.887 1.00 46.80 2233 C SER 248 122.250 54.234 39.410 1.00 47.29 2234 0 SER 248 121.454 54.976 39.997 1.00 46.67 2235 CB SER 248 123.759 52.727 40.726 1.00 44.77 2236 OG SER 248 123.859 51.479 41.381 1.00 45.74 2237 H SER 248 123.423 51.465 38.531 1.00 25.00 2238 HG SER 248 123.876 50.777 40.722 1.00 25.00 2239 N ARG 249 122.938 54.615 38.334 1.00 44.35 2240 CA ARG 249 122.789 55.943 37.750 1.00 48.22 2241 C ARG 249 121.354 56.097 37.256 1.00 47.00 2242 0 ARG 249 120.710 57.119 37.504 1.00 47.12 2243 CB ARG 249 123.785 56.147 36.604 1.00 52.69 2244 CG ARG 249 125.165 56.590 37.075 1.00 66.38 2245 CD ARG 249 126.154 56.712 35.924 1.00 73.20 2246 NE ARG 249 126.919 55.484 35.712 1.00 75.40 2247 CZ ARG 249 126.922 54.778 334.584 1.00 77.33 2248 NH1 ARG 249 126.194 55.165 33.542 1.00 74.66 2249 NH2 ARG 249 127.669 53.686 34.493 1.00 83.65 2250 H ARG 249 123.579 53.986 37.936 1.00 25.00 2251 HE ARG 249 127.471 55.153 36.453 1.00 25.00 2252 1HH1 ARG 249 125.633 55.990 33.598 1.00 25.00 2253 2HH1 ARG 249 126.203 54.625 32.700 1.00 25.00 2254 1HH2 ARG 249 128.229 53.396 35.269 1.00 25.00 2255 2HH2 ARG 249 127.675 53.153 33.646 1.00 25.00 2256 N TRP 250 120.848 55.053 36.603 1.00 46.33 2257 CA TRP 250 119.480 55.024 36.092 1.00 43.84 2258 C TRP 250 118.488 55.311 37.230 1.00 46.38 2259 0 TRP 250 117.566 56.118 37.075 1.00 44.72 2260 CB TRRP 250 119.201 53.652 35.456 1.00 38.48 2261 CG TRP 250 117.747 53.324 35.232 1.00 37.37 2262 CD1 TRP 250 116.986 53.661 34.150 1.00 33.31 2263 CD2 TRP 250 116.891 52.569 36.105 1.00 36.85 2264 NE1 TRP 250 115.713 53.164 34.293 1.00 34.01 2265 CE2 TRP 250 115.626 52.490 35.483 1.00 36.82 2266 CE3 TRP 250 117.070 51.952 37.352 1.00 34.91 2267 CZ2 TRP 250 114.543 51.816 36.065 1.00 39.04 2268 CZ3 TRP 250 115.992 51.281 37.932 1.00 39.64 2269 CH2 TRP 250 114.746 51.220 37.286 1.00 39.49 2270 H TRP 250 121.423 54.272 36.448 1.00 25.00 2271 HE1 TRP 250 114.984 53.281 33.650 1.00 25.00 2272 N TRP 251 118.718 54.683 38.382 1.00 46.65 2273 CA TRP 251 117.859 54.851 39.551 1.00 54.20 2274 C TRP 251 117.864 56.279 40.089 1.00 59.43 2275 0 TRP 251 116.814 56.823 40.445 1.00 62.13 2276 CB TRP 251 118.284 53.889 40.657 1.00 51.89 2277 CG TRP 251 117.358 53.872 41.836 1.00 58.17 2278 CD1 TRP 251 117.596 54.402 43.071 1.00 60.91 2279 CD2 TRP 251 116.069 53.246 41.908 1.00 60.72 2280 NE1 TRP 251 116.541 54.136 43.912 1.00 64.22 2281 CE2 TRP 251 1 15.589 53.429 43.225 1.00 60.87 2282 CE3 TRP 251 115.274 52.546 40.989 1.00 56.90 2283 CZ2 TRP 251 114.351 52.934 43.648 1.00 58.08 2284 CZ3 TRP 251 114.042 52.054 41.410 1.00 53.15 2285 CH2 TRP 251 113.594 52.252 42.729 1.00 53.35 2286 H TRP 251 119.485 54.076 38.442 1.00 25.00 2287 HE1 TRP 251 1 16.481 54.409 44.851 1.00 25.00 2288 N LYS 252 1 19.049 56.875 40.167 1.00 64.71 2289 CA LYS 252 119.191 58.241 40.661 1.00 68.07 2290 C LYS 252 118.440 59.227 39.779 1.00 65.20 2291 O LYS 252 117.831 60.169 40.283 1.00 65.28 2292 CB LYS 252 120.668 58.621 40.755 1.00 75.64 2293 CG LYS 252 121.400 57.815 41.803 1.00 85.57 2294 CD LYS 252 122.890 57.818 41.588 1.00 92.92 2295 CE LYS 252 123.526 56.776 42.486 1.00 95.43 2296 NZ LYS 252 124.902 56.526 42.101 1.00 94.64 2297 H LYS 252 119.849 56.379 39.887 1.00 25.00 22998 1HZ LYS 252 125.056 56.256 41.101 1.00 25.00 2299 2HZ LYS 252 125.376 57.437 42.219 1.00 25.00 2300 3HZ LYS 252 125.417 55.867 42.716 1.00 25.00 2301 N ASP 253 118.453 58.983 38.469 1.00 63.40 2302 CA ASP 253 117.762 59.846 37.515 1.00 63.30 2303 C ASP 253 116.265 59.872 37.796 1.00 63.95 2304 O ASP 253 115.635 60.925 37.729 1.00 68.15 2305 CB ASP 253 118.003 59.376 36.077 1.00 68.18 2306 CG ASP 253 119.467 59.453 35.664 1.00 76.46 2307 OD1 ASP 253 120.293 60.015 36.419 1.00 78.84 2308 OD2 ASP 253 119.793 58.943 34.570 1.00 79.35 2309 H ASP 253 118.948 58.203 38.137 1.00 25.00 2310 N LEU 254 115.697 58.710 38.105 1.00 66.44 2311 CA LEU 254 114.271 58.611 38.409 1.00 65.57 2312 C LEU 254 113.947 59.482 39.616 1.00 67.65 2313 O LEU 254 112.815 59.931 39.784 1.00 68.72 2314 CB LEU 254 113.885 57.162 38.698 1.00 61.14 2315 CG LEU 254 114.124 56.166 37.564 1.00 57.75 2316 CD1 LEU 254 113.718 54.785 38.021 1.00 58.43 2317 CD2 LEU 254 113.343 56.571 36.328 1.00 55.32 2318 H LEU 254 116.252 57.902 38.125 1.00 25.00 2319 N ASP 255 114.947 59.661 40.475 1.00 73.64 2320 CA ASP 255 114.842 60.490 41.670 1.00 78.31 2321 C ASP 255 113.664 60.123 42.574 1.00 79.28 2322 O ASP 255 113.079 60.985 43.230 1.00 81.76 2323 CB ASP 255 114.777 61.971 41.261 1.00 83.27 2324 CG ASP 255 115.238 62.915 42.364 1.00 87.17 2325 OD1 ASP 255 115.719 62.443 43.420 1.00 86.98 2326 OD2 ASP 255 115.121 64.144 42.165 1.00 87.49 2327 H ASP 255 115.805 59.226 40.294 1.00 25.00 2328 N PHE 256 113.357 58.834 42.659 1.00 80.00 2329 CA PHE 256 112.254 58.378 43.500 1.00 84.32 2330 C PHE 256 112.504 58.649 44.976 1.00 89.15 2331 O PHE 256 111.562 58.742 45.759 1.00 87.59 2332 CB PHE 256 111.987 56.887 43.290 1.00 81.00 2333 CG PHE 256 111.352 56.566 41.972 1.00 76.86 2334 CD1 PHE 256 110.671 57.544 41.251 1.00 76.59 2335 CD2 PHE 256 111.431 55.283 41.449 1.00 73.54 2336 CE1 PHE 256 110.080 57.247 40.030 1.00 76.03 2337 CE2 PHE 256 110.844 54.976 40.229 1.00 71.61 2338 CZ PHE 256 110.167 55.958 39.518 1.00 74.95 2339 H PHE 256 113.874 58.189 42.139 1.00 25.00 2340 N VAL 257 113.774 58.796 45.344 1.00 97.79 2341 CA VAL 257 114.160 59.053 46.730 1.00104.36 2342 C VAL 257 113.428 60.269 47.303 1.00105.53 2343 0 VAL 257 112.952 60.239 48.439 1.00106.91 2344 CB VAL 257 115.692 59.270 46.854 1.00107.20 2345 CG1 VAL 257 116.092 59.432 48.316 1.00107.16 2346 CG2 VAL 257 116.445 58.101 46.220 1.00106.33 2347 H VAL 257 114.464 58.732 44.658 1.00 25.00 2348 N THR 258 113.332 61.329 46.5506 1.00105.84 2349 CA THR 258 112.660 62.550 46.935 1.00104.41 2350 C THR 258 111.183 62.608 46.531 1.00104.31 2351 0 THR 258 110.339 63.047 47.314 1.00104.07 2352 CB THR 258 113.392 63.805 46.408 1.00104.30 2353 OG1 THR 258 113.620 63.674 45.000 1.00104.41 2354 CG2 THR 258 114.729 63.982 47.117 1.00105.42 2355 H THR 258 113.711 61.308 45.603 1.00 25.00 2356 HG1 THR 258 114.068 64.458 44.669 1.00 25.00 2357 N THR 259 110.872 62.161 45.317 1.00103.41 2358 CA THR 259 109.497 62.182 44.825 1.00100.89 2359 C THR 259 108.599 61.133 45.482 1.00101.97 2360 0 THR 259 107.414 61.375 45.707 1.00103.53 2361 CB THR 259 109.445 62.022 43.289 1.00 97.37 2362 OG1 THR 259 110.219 60.883 42.894 1.00 95.69 2363 CG2 THR 259 109.988 63.267 42.602 1.00 95.50 2364 H THR 259 111.579 61.811 44.728 1.00 25.00 2365 HG1 THR 259 109.870 60.086 43.290 1.00 25.00 2366 N LEU 260 109.164 59.969 45.783 1.00102.18 2367 CA LEU 260 108.415 58.884 46.412 1.00103.22 2368 C LEU 260 109.112 58.431 47.696 1.00106.86 2369 0 LEU 260 109.742 57.372 47.732 1.00107.73 2370 CB LEU 260 108.282 57.700 45.445 1.00 98.81 2371 CG LEU 260 107.552 57.928 44.119 1.00 94.81 2372 CD1 LEU 260 107.620 56.670 43.269 1.00 89.99 2373 CD2 LEU 260 106.108 58.320 44.380 1.00 92.83 2374 H LEU 260 110.112 59.844 45.595 1.00 25.00 2375 N PRO 261 108.963 59.204 48.784 1.00110.17 2376 CA PRO 261 109.580 58.889 50.077 1.00112.52 2377 C PRO 261 108.951 57.726 50.855 1.00114.04 2378 0 PRO 261 108.783 57.813 52.073 1.00117.31 2379 CB PRO 261 109.441 60.207 50.836 1.00113.40 2380 CG PRO 261 108.124 60.715 50.347 1.00112.70 2381 CD PRO 261 108.223 60.477 48.856 1.00111.17 2382 N TYR 262 108.599 56.646 50.163 1.00113.40 2383 CA TYR 262 108.012 55.479 50.822 1.00112.08 2384 C TYR 262 108.608 54.178 50.284 1.00112.01 2385 0 TYR 262 108.125 53.086 50.582 1.00110.30 2386 CB TYR 262 106.477 55..478 50.702 1.00109.31 2387 CG TYR 262 105.931 55.286 49.303 1.00104.93 2388 CD1 TYR 262 105.777 56.369 48.440 1.00103.18 2389 CD2 TYR 262 105.555 54.021 48.846 1.00102.84 2390 CE1 TYR 262 105.262 56.201 47.159 1.00101.09 2391 CE2 TYR 262 105.040 53.842 47.565 1.00100.35 2392 CZ TYR 262 104.897 54.938 46.727 1.00100.07 2393 OH TYR 262 104.386 54.781 45.459 1.00 97.25 2394 H TYR 262 108.755 56.615 49.199 1.00 25.00 2395 HH TYR 262 104.276 53.862 45.236 1.00 25.00 2396 N ALA 263 109.671 54.310 49.497 1.00113.11 2397 CA ALA 263 110.360 53.166 48.913 1.00114.09 2398 C ALA 263 111.856 53.343 49.146 1.00114.75 2399 0 ALA 263 112.375 54.457 49.055 1.00115.90 2400 CB ALA 263 110.064 53.077 47.428 1.00112.96 2401 H ALA 263 110.034 55.202 49.305 1.00 25.00 2402 N ARG 264 112.543 52.252 49.467 1.00113.69 2403 CA ARG 264 113.979 52.309 49.726 1.00114.09 2404 C ARG 264 114.847 51.948 48.526 1.00109.03 2405 0 ARG 264 114.394 51.280 47.594 1.00109.80 2406 CB ARG 264 114.355 51.448 50.945 1.00116.51 2407 CG ARG 264 113.434 50.258 51.235 1.00118.71 2408 CD ARG 264 113.486 49.190 50.151 1.00120.73 2409 NE ARG 264 112.543 48.105 50.418 1.00118.02 2410 CZ ARG 264 111.607 47.696 49.565 1.00115.79 2411 NH1 ARG 264 111.479 48.277 48.380 1.00114..07 2412 NH2 ARG 264 110.788 46.709 49.904 1.00113.33 2413 H ARG 264 112.079 51.393 49.495 1.00 25.00 2414 HE ARG 264 112.602 47.651 51.284 1.00 25.00 2415 1HH1 ARG 264 112.083 49.029 48.120 1.00 25.00 2416 2HH1 ARG 264 110.766 47.967 47.751 1.00 25.00 2417 1HH2 ARG 264 110.868 46.283 50.807 1.00 25.00 2418 2HH2 ARG 264 110.074 46.408 49.273 1.00 25.00 2419 N ASP 265 116.089 52.421 48.550 1.00103.18 2420 CA ASP 265 117.045 52.152 47.485 1.00 97.60 2421 C ASP 265 117.480 50.688 47.579 1.00 92.70 2422 0 ASP 265 118.533 50.371 48.138 1.00 96.57 2423 CB ASP 265 118.255 53.086 47.619 1.00100.16 2424 CG ASP 265 1199.317 52.826 46.565 1.00106.00 2425 0D1 ASP 265 118.992 52.887 45.363 1.00107.25 2426 0D2 ASP 265 120.479 52.556 46.940 1.00109.23 2427 H ASP 265 116.373 52.965 49.310 1.00 25.00 2428 N ARG 266 116.654 49.799 47.041 1.00 82.19 2429 CA ARG 266 116.942 48.372 47.073 1.00 73.27 2430 C ARG 266 117.613 47.910 45.775 1.00 63.23 2431 0 ARG 266 117.711 46.712 45.511 1.00 66.31 2432 CB ARG 266 115.646 47.585 47.320 1.00 77.54 2433 CG ARG 266 115.801 46.402 48.274 1.00 83.80 2434 CD ARG 266 114.480 45.672 48.520 1.00 86.40 2435 NE ARG 266 114.015 44.911 47.358 1.00 87.97 2436 CZ ARG 266 114.383 43.661 47.077 1.00 87.83 2437 NH1 ARG 266 115.229 43.014 47.869 1.00 86.43 2438 NH2 ARG 266 113.895 43.049 46.005 1.00 80.67 2439 H ARG 266 115.816 50.112 46.631 1.00 25.00 2440 HE ARG 266 113.386 45.348 46.747 1.00 25.00 2441 1 HH1 ARG 266 115.600 43.463 48.681 1.00 25.00 2442 2HH1 ARG 266 115.502 42.079 47.647 1.00 25.00 2443 1 HH2 ARG 266 113.246 43.525 45.410 1.00 25.00 2444 2HH2 ARG 266 114.170 42.111 45.794 1.00 25.00 2445 N VAL 267 118.130 48.859 45.000 1.00 54.00 2446 CA V VAALL 267 118.778 48.560 43.722 1.00 46.85 2447 C VVAALL 267 119.865 47.496 43.784 1.00 44.14 2448 0 VVAALL 267 119.911 46.609 42.935 1.00 45.14 2449 CB VVAALL 267 119.361 49.827 43.076 1.00 45.45 2450 CG1 VVAALL 267 119.991 49.499 41.733 1.00 42.99 2451 CG2 VVAALL 267 118.273 50.848 42.892 1.00 51.05 2452 H VVAALL 267 118.072 49.785 45.299 1.00 25.00 2453 N VVAALL 268 120.738 47.576 44.781 1.00 40.56 2454 CA VVAALL 268 121.813 46.597 44.910 1.00 38.21 2455 C VVAALL 268 121.242 45.185 45.125 1.00 35.40 2456 0 VVAALL 268 121.708 44.220 44.513 1.00 29.56 2457 CB VVAALL 268 122.785 46.976 46.046 1.00 40.34 2458 CG1 VVAALL 268 123.983 46.055 46.040 1.00 41.41 2459 CG2 VAL 268 123.239 48.414 45.880 1.00 43.02 2460 H VAL 268 120.663 48.303 45.428 1.00 25.00 2461 N G GLLUU 269 120.202 45.081 45.952 1.00 33.49 2462 CA GGLLUU 2669 119.553 43.796 46.220 1.00 31.75 2463 C GGLLUU 269 118.910 43.278 44.936 1.00 31.29 2464 0 GGLLUU 269 119.023 42.095 44.607 1.00 34.74 2465 CB GGLLUU 269 118.477 43.940 47.300 1.00 30.42 2466 CG GGLLUU 269 118.998 44.124 48.719 1.00 41.96 2467 CD GGLLUU 269 119.777 45.418 48.921 1.00 53.70 2468 0E1 GGLLUU 269 119.387 46.465 48.356 1.00 52.14 2469 0E2 GGLLUU 269 120.785 45.385 49.658 1.00 60.44 2470 H GGLLUU 269 119.849 45.888 46.369 1.00 25.00 2471 N CCYYSS 270 118.258 44.179 44.204 1.00 25.87 2472 CA CCYYSS 270 117.603 43.829 42.948 1.00 31.04 2473 C CCYYSS 270 118.628 43.330 41.944 1.00 31.66 2474 0 CCYYSS 270 118.352 42.406 41.170 1.00 34.14 2475 CB CCYYSS 270 116.841 45.029 42.380 1.00 31.00 2476 SG CCYYSS 270 115.468 45.566 43.429 1.00 41.23 2477 H CCYYSS 270 118.204 45.102 44.523 1.00 25.00 2478 N T TYYRR 271 119.817 43.927 41.968 1.00 30.55 2479 CA T TYYRR 271 120.875 43.506 41.065 1.00 29.41 2480 C TTYYRR 271 121.365 42.109 41.459 1.00 29.51 2481 0 TTYYRR 271 121.662 41.284 40.592 1.00 30.16 2482 CB TTYYRR 271 122.048 44.496 41.048 1.00 27.85 2483 CG TTYYRR 271 123.125 44.061 40.077 1.00 27.35 2484 CD1 TTYYRR 271 123.006 44.327 38.714 1.00 25.72 2485 CD2 TYR 271 124.198 43.279 40.502 1.00 20.62 2486 CE1 TYR 271 123.923 43.813 37.798 1.00 22.98 2487 CE2 T TYYRR 271 125.116 42.762 39.593 1.00 27.42 2488 CZ TTYYRR 271 124.970 43.030 38.245 1.00 21.79 2489 OH TYR 271 125.859 42.497 37.343 1.00 23.43 2490 H TYR 271 119.985 44.662 42.594 1.00 25.00 2491 HH TYR 271 126.485 41.987 37.843 1.00 25.00 2492 N PHE 272 121.453 41.845 42.760 1.00 26.47 2493 CA PHE 272 121.892 40.535 43.220 1.00 28.71 2494 C PHE 272 120.957 39.486 42.633 1.00 31.32 2495 0 PHE 272 121.408 38.470 42.102 1.00 31.50 2496 CB PHE 272 121.881 40.442 44.747 1.00 32.54 2497 CG PHE 272 122.165 39.058 45.264 1.00 34.15 2498 CD1 PHE 272 123.471 38.577 45.323 1.00 32.37 2499 CD2 PHE 272 121.120 38.211 45.638 1.00 34.09 2500 CE11 PHE 272 123.732 37.271 45.739 1.00 35.66 2501 CE2 PHE 272 121.369 36.902 46.055 1.00 34.18 2502 CZ PHE 272 122.679 36.431 46.105 1.00 36.58 2503 H PHE 272 121.228 42.541 43.413 1.00 25.00 2504 N TRP 273 119.656 39.744 42.712 1.00 29.73 2505 CA TRP 273 118.670 38.817 42.167 1.00 30.60 2506 C TRP 273 118.924 38.551 40.685 1.00 30.33 2507 0 TRP 273 118.971 37.396 40.250 1.00 32.10 2508 CB TRP 273 117.255 39.357 42.365 1.00 28.17 2509 CG TRP 273 116.707 39.092 43.721 1.00 33.41 2510 CD1 TRP 273 117.241 39.478 44.915 1.00 37.71 2511 CD2 TRP 273 115.506 38.381 44.029 1.00 41.82 2512 NE1 TRP 273 116.445 39.053 45.950 1.00 39.11 2513 CE2 TRP 273 115.372 38.378 45.435 1.00 43.90 2514 CE3 TRP 273 114.528 37.747 43.253 1.00 47.13 2515 CZ2 TRP 273 114.296 37.764 46.083 1.00 49.35 2516 CZ3 TRP 273 113.458 37.136 43.898 1.00 53.38 2517 CH2 TRP 273 113.352 37.150 45.300 1.00 53.17 2518 H TRP 273 119.359 40.569 43.153 1.00 25.00 2519 HE1 TRP 273 116.622 39.201 46.903 1.00 25.00 2520 N ALA 274 119.117 39.617 39.915 1.00 26.20 2521 CA ALA 274 119.371 39.472 38.489 1.00 25.12 2522 C ALA 274 120.638 38.657 38.263 1.00 27.03 2523 0 ALA 274 120.686 37.816 37.366 1.00 29.08 2524 CB ALA 274 119.491 40.832 37.831 1.00 22.68 2525 H ALA 274 119.0884 40.514 40.313 1.00 25.00 2526 N LEU 275 121.646 38.886 39.104 1.00 26.74 2527 CA LEU 275 122.922 38.175 39.011 1.00 23.65 2528 C LEU 275 122.727 36.689 39.329 1.00 20.19 2529 0 LEU 275 123.432 35.825 38.798 1.00 18.69 2530 CB LEU 275 123.945 38.802 39.963 1.00 22.77 2531 CG LEU 275 125.377 38.280 39.867 1.00 22.23 2532 CD1 LEU 275 125.859 38.352 38.427 1.00 20.45 2533 CD2 LEU 275 126.274 39.097 40.779 1.00 24.10 2534 H LEU 275 121.532 39.552 39.808 1.00 25.00 2535 N GLY 276 121.765 36.406 40.204 1.00 19.17 2536 CA GLY 276 121.453 35.035 40.561 1.00 19.61 2537 C GLY 276 120.811 34.299 39.392 1.00 25.48 2538 0 GLY 276 121.060 33.108 39.199 1.00 28.59 2539 H GLY 276 121.266 37.137 40.623 1.00 25.00 2540 N VAL 277 120.000 35.006 38.603 1.00 20.84 2541 CA VAL 277 119.323 34.415 37.440 1.00 19.19 2542 C VAL 277 120.304 34.028 36.319 1.00 19.17 2543 0 VAL 277 120.086 33.048 35.606 1.00 21.35 2544 CB VAL 277 118.201 35.355 36.904 1.00 21.19 2545 CG1 VAL 277 117.560 34.777 35.650 1.00 15.33 2546 CG2 VAL 277 117.138 35.550 37.976 1.00 11.13 2547 H VAL 277 119.858 35.954 38.810 1.00 25.00 2548 N TYR 278 121.345 34.834 36.137 1.00 21.16 2549 CA TYR 278 122.401 34.587 35.150 1.00 24.77 2550 C TYR 278 123.583 35.532 35.351 1.00 29.35 2551 0 TYR 278 123.405 36.738 35.531 1.00 27.69 2552 CB TYR 278 121.910 34.611 33.687 1.00 25.96 2553 CG TYR 278 120.741 35.517 33.341 1.00 26.89 2554 CD1 TYR 278 120.580 36.768 33.937 1.00 25.88 2555 CD2 TYR 278 119.800 35.116 32.388 1.00 27.14 2556 CE1 TYR 278 119.508 37.595 33.594 1.00 29.19 2557 CE2 TYR 278 118.729 35.934 32.037 1.00 31.49 2558 CZ TYR 278 118.587 37.171 32.643 1.00 31.78 2559 OH TYR 278 117.522 37.976 32.301 1.00 31.66 2560 H TYR 278 121.419 35.652 36.684 1.00 25.00 2561 HH TYR 278 117.022 37.548 31.600 1.00 25.00 2562 N PHE 279 124.789 34.968 35.332 1.00 31.85 2563 CA PHE 279 126.017 35.732 35.549 1.00 28.28 2564 C PHE 279 126.910 35.844 34.318 1.00 28.86 2565 0 PHE 279 127.855 36.636 34.310 1.00 28.24 2566 CB PHE 279 126.829 35.087 36.678 1.00 24.38 2567 CG PHE 279 127.334 33.707 36.344 1.00 23.04 2568 CD1 PHE 279 128.563 33.535 35.706 1.00 16.44 2569 CD2 PHE 279 126.557 32.582 36.616 1.00 22.61 2570 CE1 PHE 279 129.005 32.265 35.339 1.00 22.82 2571 CE2 PHE 279 126.989 31.309 36.254 1.00 22.81 2572 CZ PHE 279 128.214 31.149 35.613 1.00 20.63 2573 H PHE 279 124.845 34.006 35.181 1.00 25.00 2574 N GLU 280 126.653 35.010 33.315 1.00 25.83 2575 CA GLU 280 127.450 34.995 32.093 1.00 25.96 2576 C GLU 280 127.464 36.347 31.384 1.00 32.09 2577 0 GLU 280 126.461 37.067 31.378 1.00 33.29 2578 CB GLU 280 126.947 33.909 31.140 1.00 29.64 2579 CG GLU 280 127.116 32.479 31.652 1.00 31.98 2580 CD GLU 280 125.873 31.921 32.338 1.00 41.40 2581 0E1 GLU 280 125.089 32.696 32.938 1.00 33.42 2582 0E2 GLU 280 125.681 30.688 32.273 1.00 43.76 2583 H GLU 280 125.894 34.421 33.402 1.00 25.00 2584 N PRO 281 128.593 36.687 30.735 1.00 34.75 2585 CA PRO 281 128.736 37.961 30.018 1.00 32.48 2586 C PRO 281 127.718 38.182 28.899 1.00 30.11 2587 0 PRO 281 127.273 39.309 28.675 1.00 33.55 2588 CB PRO 281 130.177 37.901 : 229.492 1.00 33.45 2589 CG PRO 281 130.447 36.426 29.366 1.00 34.83 2590 CD PRO 281 129.824 35.882 30.625 1.00 32.94 2591 N GLN 282 127.319 37.106 28.226 1.00 30.38 2592 CA GLN 282 126.350 37.195 27.134 1.00 31.74 2593 C GLN 282 124.980 37.704 27.600 1.0033.53 2594 0 GLN 282 124.194 38.202 26.792 1.0034.52 2595 CB GLN 282 126.183 35.829 26.462 1.0035.52 2596 CG GLN 282 125.442 34.819 27.323 1.0047.53 2597 CD GLN 282 125.543 33.400 26.807 1.0054.68 2598 OE1 GLN 282 126.378 32.624 27.273 1.0058.66 2599 NE2 GLN 282 124.675 33.040 25.866 1.0055.48 2600 H GLN 282 127.685 36.233 28.468 1.0025.00 2601 1HE2 GLLN 282 124.740 32.122 25.538 1.0025.00 2602 2HE2 GLN 282 124.018 33.690 25.551 1.0025.00 2603 N TYR 283 124.698 37.577 28.896 1.0027.81 2604 CA TYR 283 123.417 38.015 29.447 1.0026.64 2605 C TYR 283 123.470 39.392 30.099 1.0029.80 2606 O TYR 283 122.615 39.732 30.922 1.0029.85 2607 CB TYR 283 122.885 36.982 30.444 1.0024.82 2608 CG TYR 283 122.670 35.614 29.840 1.0026.77 2609 CD1 TYR 283 121.786 35.432 28.775 1.0028.94 2610 CD2 TYR 283 123.373 34.506 30.313 1.0026.51 2611 CE1 TYR 283 121.610 34.174 28.192 1.0032.76 2612 CE2 TYR 283 123.205 33.247 29.740 1.0028.52 2613 CZ TYR 283 122.324 33.086 28.680 1.0030.97 2614 OH TYR 283 122.164 31.845 28.104 1.0025.13 2615 H TYR 283 125.361 37.198 29.509 1.0025.00 2616 HH TYR 283 122.723 31.208 28.556 1.0025.00 2617 N SER 284 124.449 40.196 29.697 1.0030.66 2618 CA SER 284 124.620 41.539 30.239 1.0033.15 2619 C SER 284 123.375 42.412 30.040 1.0032.37 2620 O SER 284 122.858 42.999 30.999 1.0032.25 2621 CB SER 284 125.848 42.201 29.609 1.0032.60 2622 OG SER 284 126.037 43.511 30.110 1.0038.65 2623 H SER 284 125.090 39.876 29.027 1.0025.00 2624 HG SER 284 126.140 43.520 31.058 1.0025.00 2625 N GLN 285 122.882 42.477 28.805 1.0035.28 2626 CA GLN 285 121.693 43.273 28.505 1.0036.59 2627 C GLN 285 120.489 42.735 29.284 1.0033.06 2628 O GLN 285 119.713 43.504 29.856 1.0033.43 2629 CB GLN 285 121.399 43.255 27.002 1.0036.57 2630 CG GLN 285 120.138 44.020 26.611 1.0048.54 2631 CD GLN 285 119.829 43.943 25.123 1.0054.77 2632 OE1 GLN 285 120.079 42.927 24.470 1.0055.77 2633 NE2 GLN 285 119.280 45.024 24.581 1.0056.33 2634 H GLN 285 123.323 41.984 28.086 1.0025.00 2635 1HE2 GLN 285 119.084 44.982 23.621 1.0025.00 2636 2HE2 GLN 285 119.099 45.802 25.141 1.0025.00 2637 N ALA 286 120.364 41.410 29.324 1.0032.38 2638 CA ALA 286 119.272 40.750 30.032 1.0028.79 2639 C ALA 286 119.254 41.117 31.512 1.0026.70 2640 O ALA 286 118.200 41.438 32.060 1.0031.71 2641 CB ALA 286 119.370 39.244 29.859 1.0030.35 2642 H ALA 286 121.023 40.859 28.861 1.0025.00 2643 N ARG 287 120.422 41.097 32.152 1.0026.48 2644 CA ARG 287 120.517 41.442 33.568 1.0027.31 2645 C ARG 287 120.056 42.870 33.826 1.00 27.08 2646 0 ARG 287 119.290 43.118 34.760 1.00 28.78 2647 CB ARG 287 121.946 41.266 34.096 1.00 28.17 2648 CG ARG 287 122.240 39.891 34.652 1.00 25.50 2649 CD ARG 287 123.566 39.859 35.396 1.00 24.46 2650 NE ARG 287 124.703 40.191 34.535 1.00 20.40 2651 CZ ARG 287 125.252 39.373 33.641 1.00 23.12 2652 NH1 ARG 287 124.781 38.146 33.473 1.00 23.32 2653 NH2 ARG 287 126.268 39.793 32.897 1.00 22.53 2654 H ARG 287 121.232 40.840 31.670 1.00 25.00 2655 HE ARG 287 125.093 41.059 34.627 1.00 25.00 2656 1HH1 ARG 287 124.002 37.833 34.014 1.00 25.00 2657 2HH1 ARG 287 125.192 37.542 32.796 1.00 25.00 2658 1HH2 ARG 287 126.623 40.719 33.014 1.00 25.00 2659 2HH2 ARG 287 126.677 39.179 32.225 1.00 25.00 2660 N VAL 288 120.512 43.802 32.992 1.00 30.28 2661 CA V VAALL 288 120.144 45.208 33.148 1.00 29.94 2 2666622 C VVAALL 288 118.628 45.388 33.043 1.00 28.55 22666633 0 VVAALL 288 118.018 46.044 33.890 1.00 35.55 2664 CB VAL 288 120.874 46.106 32.120 1.00 35.29 2665 CG1 VAL 288 120.536 47.572 32.363 1.00 30.30 2666 CG2 VAL 288 122.378 45.896 32.221 1.00 31.86 2667 H VAL 288 121.107 43.535 32.256 1.00 25.00 2668 N MET 289 118.018 44.775 32.031 1.00 27.91 2669 CA MET 289 116.567 44.856 31.854 1.00 27.36 2670 C MET 289 115.857 44.248 33.066 1.00 27.49 2671 O MET 289 114.938 44.845 33.627 1.00 29.43 2672 CB MET 289 116.136 44.129 30.572 1.00 28.18 2673 CG MET 289 116.578 44.819 29.282 1.00 28.82 2674 SD MET 289 116.207 43.882 27.770 1.00 38.33 2675 CE MET 289 114.526 44.384 27.438 1.00 39.91 2676 H MET 289 118.554 44.257 31.391 1.00 25.00 2677 N LEU 290 116.335 43.089 33.511 1.00 25.99 2678 CA LEU 290 115.743 42.408 34.654 1.00 25.33 2679 C LEU 290 115.805 43.222 35.949 1.00 26.44 2680 0 LEU 290 114.815 43.289 36.687 1.00 30.04 2681 CB LEU 290 116.393 41.035 34.843 1.00 25.26 2682 CG LEU 290 115.880 40.125 35.964 1.00 25.88 2683 CD1 LEU 290 114.357 40.043 35.951 1.00 19.53 2684 CD2 LEU 290 116.499 38.741 35.796 1.00 18.49 2685 H LEU 290 117.098 42.681 33.057 1.00 25.00 2686 N VAL 291 116.947 43.857 36.210 1.00 27.54 2687 CA VAL 291 117.124 44.667 37.421 1.00 28.37 2688 C VAL 291 116.101 45.799 37.502 1.00 27.52 2689 O VAL 291 115.487 46.023 38.5550 1.00 27.61 2690 CB VAL 291 118.544 45.289 37.507 1.00 28.94 2691 CG1 VAL 291 118.706 46.054 38.803 1.00 25.65 2692 CG2 VAL 291 119.592 44.214 37.431 1.00 36.38 2693 H VAL 291 117.687 43.782 35.573 1.00 25.00 2694 N LYS 292 115.911 46.502 36.392 1.00 27.46 2695 CA LYS 292 114.968 47.611 36.345 1.00 28.57 2696 C LYS 292 113.546 47.158 36.677 1.00 30.77 2697 0 LYS 292 112.834 47.824 37.433 1.00 31.18 2698 CB LYS 292 115.029 48.285 34.976 1.00 29.35 2699 CG LYS 292 116.391 48.890 34.676 1.00 29.57 2700 CD LYS 292 116.463 49.431 33.261 1.00 34.35 2701 CE LYS 292 117.810 50.079 32.999 1.00 37.92 2702 NZ LYS 292 117.909 50.619 31.619 1.00 40.64 2703 H LYS 292 116.413 46.260 35.581 1.00 25.00 2704 1HZ LYS 292 117.780 49.846 30.936 1.00 25.00 2705 2HZ LYS 292 117.169 51.334 31.476 1.00 25.00 2706 3HZ LYS 292 118.844 51.052 31.483 1.00 25.00 2707 N THR 293 113.146 46.010 36.137 1.00 34.24 2708 CA THR 293 111.817 45.463 36.395 1.00 27.43 2709 C THR 293 111.657 45.123 37.872 1.00 31.58 2710 0 THR 293 110.655 45.493 38.491 1.00 28.71 2711 CB THR 293 111.561 44.214 35.534 1.00 25.43 2712 OG1 THR 293 111.354 44.616 34.175 1.00 30.49 2713 CG2 THR 293 110.348 43.433 36.029 1.00 22.44 2714 H THR 293 113.756 45.525 35.533 1.00 25.00 2715 HG1 THR 293 110.577 45.180 34.129 1.00 25.00 2716 N ILE 294 112.647 44.439 38.440 1.00 30.35 2717 CA ILE 294 112.596 44.064 39.853 1.00 30.45 2718 C ILE 294 112.481 45.317 40.725 1.00 28.69 2719 0 ILE 294 111.709 45.348 41.685 1.00 30.57 2720 CB ILE 294 113.837 43.230 40.272 1.00 29.95 2721 CG1 ILE 294 113.948 41.977 39.399 1.00 24.34 2722 CG2 ILE 294 113.733 42.818 41.734 1.00 18.35 2723 CD1 ILE 294 115.165 41.133 39.687 1.00 30.84 2724 H ILE 294 113.432 44.182 37.906 1.00 25.00 2725 N SER 295 113.219 46.361 40.359 1.00 32.61 2726 CA SER 295 113.196 47.623 41.097 1.00 37.07 2727 C SER 295 111.820 48..276 41.002 1.00 35.65 2728 0 SER 295 111.227 48.673 42.011 1.00 33.09 2729 CB SER 295 114.246 48.584 40.533 1.00 35.83 2730 OG SER 295 115.543 48.024 40.608 1.00 42.38 2731 H SER 295 113.804 46.290 39.575 1.00 25.00 2732 HG SER 295 115.756 47.823 41.523 1.00 25.00 2733 N MET 296 111.306 48.342 39.779 1.00 34.54 2734 CA MET 296 110.017 48.951 39.506 1.00 35.02 2735 C MET 296 108.864 48.263 40.230 1.00 36.33 2736 0 MET 296 108.080 48.919 40.923 1.00 35.61 2737 CB MET 296 109.768 48.966 37.999 1.00 39.18 2738 CG MET 296 109.109 50.234 37.507 1.00 49.37 2739 SD MET 296 109.993 51.708 38.067 1.00 51.57 2740 CE MET 296 108.888 52.271 39.359 1.00 53.40 2741 H MET 296 111.819 47.966 39.036 1.00 25.00 2742 N ILE 297 108.780 46.941 40.103 1.00 37.42 2743 CA ILE 297 107.709 46.185 40.745 1.00 34.54 2744 C ILE 297 107.813 46.267 42.267 1.00 36.45 2745 0 ILE 297 106.817 46.101 42.976 1.00 35.56 2746 CB ILE 297 107.675 44.709 40.265 1.00 36.67 2747 CG1 ILE 297 106.342 44.059 40.648 1.00 30.90 2748 CG2 ILE 297 108.858 43.925 40.821 1.00 34.15 2749 CD1 ILE 297 105.135 44.654 39.935 1.00 28.47 2750 H ILE 297 109.454 46.468 39.576 1.00 25.00 2751 N SER 298 109.015 46.559 42.761 1.00 37.95 2752 CA SER 298 109.250 46.696 44.195 1.00 40..22 2753 C SER 298 108.531 47.961 44.673 1.00 38.96 2754 0 SER 298 107.934 47.979 45.753 1.00 36.43 2755 CB SER 298 110.751 46.791 44.481 1.00 43.72 2756 OG SER 298 111.00 9 46.764 45.873 1.00 62.08 2757 H SER 298 109.775 46.674 42.153 1.00 25.00 2758 HG SER 298 110.573 47.504 46.304 1.00 25.00 2759 N ILE 299 108.582 49.011 43.857 1.00 39.57 2760 CA ILE 299 107.912 50.271 44.175 1.00 40.91 2761 C ILE 299 106.412 49.996 44.293 1.00 40.75 2762 0 ILE 299 105.771 50.378 45.276 1.00 40.26 2763 CB ILE 299 108.128 51.329 43.060 1.00 37.27 2764 CG1 ILE 299 109.614 51.653 42.908 1.00 37.90 2765 CG2 ILE 299 1077.345 52.592 43.370 1.00 42.54 2766 CD1 ILE 299 110.260 52.146 44.173 1.00 39.79 2767 H ILE 299 109.091 48.942 43.021 1.00 25.00 2768 N VAL 300 105.876 49.290 43.301 1.00 34.47 2769 CA VAL 300 104.462 48.949 43.267 1.00 33.70 2770 C VAL 300 104.050 48.145 44.497 1.00 38.81 2771 0 VAL 300 103.020 48.431 45.116 1.00 39.02 2772 CB VAL 300 104J16 48.166 41.990 1.00 35.45 2773 CG1 VAL 300 102.629 47.848 41.951 1.00 37.16 2774 CG2 VAL 300 104.522 48.970 40.762 1.00 29.01 2775 H VAL 300 106.459 48.994 42.572 1.00 25.00 2776 N ASP 301 104.866 47.162 44.865 1.00 39.28 2777 CA ASP 301 104.585 46.327 46.030 1.00 39.76 2778 C ASP 301 104.477 47.200 47.281 1.00 43.93 2779 0 ASP 301 103.588 47.002 48.113 1.00 43.98 2780 CB ASP 301 105.684 45.270 46.205 1.00 41.93 2781 CG ASP 301 105.401 44.299 47.348 1.00 47.18 2782 0D1 ASP 301 104.219 44.006 47.633 1.00 52.50 2783 0D2 ASP 301 106.375 43.817 47.959 1.00 53.58 2784 H ASP 301 105.672 46.984 44.338 1.00 25.00 2785 N ASP 302 105.373 48.175 47.401 1.00 48.10 2786 CA ASP 302 105.371 49.088 48.541 1.00 51.62 2787 C ASP 302 104.090 49.918 48.560 1.00 50.46 2788 0 ASP 302 103.480 50.114 49.615 1.00 51.17 2789 CB ASP 302 106.587 50.017 48.487 1.00 55.75 2790 CG ASP 302 107.904 49.271 48.619 1.00 62.15 2791 0D1 ASP 302 107.922 48.165 49.207 1.00 63.08 2792 0D2 ASP 302 108.928 49.798 48.133 1.00 68.25 2793 H ASP 302 106.056 48.281 46.704 1.00 25.00 2794 N THR 303 103.684 50.388 47.383 1.00 50.52 2795 CA THR 303 102.479 51.192 47.230 1.00 50.05 2796 C THR 303 101.260 50.472 47.808 1.00 51.84 2797 0 THR 303 100.563 51.013 48.668 1.00 56.07 2798 CB THR 303 102.222 51.512 45.745 1.00 50.09 2799 OG1 THR 303 103.377 52.153 45.190 1.00 45.79 2800 CG2 THR 303 101.015 52.425 45.593 1.00 50.31 2801 H THR 303 104.219 50.190 46.581 1.00 25.00 2802 HG1 THR 303 103.480 52.938 45.719 1.00 25.00 2803 N PHE 304 101.025 49.246 47.352 1.00 50.29 2804 CA PHE 304 99.893 48.450 47.817 1.00 53.29 2805 C PHE 304 99.997 48.024 49.275 1.00 59.68 2806 0 PHE 304 98.981 47.832 49.940 1.00 62.17 2807 CB PHE 304 99.744 47.182 46.971 1.00 43.62 2808 CG PHE 304 99.065 47.398 45.654 1.00 37.53 2809 CD1 PHE 304 99.780 47.857 44.555 1.00 32.17 2810 CD2 PHE 304 97.711 47.113 45.506 1.00 35.92 2811 CE1 PHE 304 99.156 48.029 43.326 1.00 36.26 2812 CE2 PHE 304 97.079 47.280 44.283 1.00 29.26 2813 CZ PHE 304 97.802 47.739 43.189 1.00 34.73 2814 H PHE 304 101.636 48.860 46.683 1.00 25.00 2815 N ASP 305 101.223 47.873 49.765 1.00 69.36 2816 CA ASP 305 101.450 47.405 51.129 1.00 78.46 2817 C ASP 305 101.326 48.406 52.279 1.00 80.92 2818 0 ASP 305 100.774 48.064 53.329 1.00 79.13 2819 CB ASP 305 102.798 46.675 51.210 1.00 84.84 2820 CG ASP 305 102.851 45.663 52.345 1.00 90.63 2821 OD1 ASP 305 102.142 44.635 52.265 1.00 90.70 2822 OD2 ASP 305 103.610 45.891 53.312 1.00 92.23 2823 H ASP 305 101.996 48.072 49.197 1.00 25.00 2824 N ALA 306 101.818 49.631 52.104 1.00 84.70 2825 CA ALA 306 101.752 50.595 53.201 1.00 89.65 2826 C ALA 306 101.457 52.057 52.874 1.00 91.11 2827 0 ALA 306 101.606 52.916 53.745 1.00 93.41 2828 CB ALA 306 103.027 50.500 54.040 1.00 89.50 2829 H ALA 306 102.229 49.879 51.249 1.00 25.00 2830 N TYR 307 101.022 52.359 51.655 1.00 90.94 2831 CA TYR 307 100.743 53.752 51.329 1.00 92.48 2832 C TYR 307 99.374 54.011 50.701 1.00 90.37 2833 0 TYR 307 98.599 54.824 51.207 1.00 91.55 2834 CB TYR 307 101.858 54.336 50.453 1.00 98.27 2835 CG TYR 307 102.031 55.837 50.609 1.00106.75 2836 CD1 TYR 307 101.301 56.732 49.825 1.00109.71 2837 CD2 TYR 307 102.918 56.364 51.552 1.00107.24 2838 CE1 TYR 307 101.447 58.113 49.973 1.00107.24 2839 CE2 TYR 307 103.072 57.744 51.708 1.00106.57 2840 CZ TYR 307 102.332 58.611 50.915 1.00106.75 2841 OH TYR 307 102.477 59.971 51.060 1.00103.97 2842 H TYR 307 100.876 51.657 50.988 1.00 25.00 2843 HH TYR 307 101.900 60.427 50.443 1.00 25.00 2844 N GLY 308 99.079 53.325 49.603 1.00 85.79 2845 CA GLY 308 97.808 53.522 48.930 1.00 82.54 2846 C GLY 308 96.583 53.120 49.730 1.00 81.67 2847 0 GLY 308 96.589 52.105 50.428 1.00 80.43 2848 H GLY 308 99.710 52.666 49.258 1.00 25.00 2849 N THR 309 95.531 53.928 49.637 1.00 82.42 2850 CA THR 309 94.282 53.649 50.338 1.00 82.64 2851 C THR 309 93.397 52.796 49.433 1.00 83.27 2852 0 THR 309 93.592 52.771 48.215 1.00 87.28 2853 CB THR 309 93.519 54.946 50.696 1.00 80.48 2854 OG1 THR 309 93.166 55.648 49.495 1.00 74.90 2855 CG2 THR 309 94.371 55.844 51.583 1.00 75.37 2856 H THR 309 95.600 54.729 49.085 1.00 25.00 2857 HG1 THR 309 92.598 55.106 48.954 1.00 25.00 2858 N VAL 310 92.383 52.172 50.025 1.00 80.18 2859 CA VAL 310 91.447 51.304 49.309 1.00 75.06 2860 C VAL 310 91.067 51.822 47.919 1.00 74.05 2861 0 VAL 310 91.209 51.115 46.921 1.00 73.13 2862 CB VAL 310 90.149 51.103 50.127 1.00 79.21 2863 CG1 VAL 310 89.284 50.020 49.494 1.00 80.28 2864 CG2 VAL 310 90.478 50.760 51.575 1.00 78.07 2865 H VAL 310 92.275 52.293 50.987 1.00 25.00 2866 N LYS 311 90.622 53.072 47.859 1.00 73.34 2867 CA LYS 311 90.210 53.682 46.600 1.00 71.58 2868 C LYS 311 91.366 53.946 45.639 1.00 67.72 2869 0 LYS 311 91.269 53.642 44.448 1.00 65.13 2870 CB LYS 311 89.433 54.977 46.866 1.00 79.85 2871 CG LYS 311 87.977 54.774 47.306 1.00 89.57 2872 CD LYS 311 87.842 53.976 48.607 1.00 98.38 2873 CE LYS 311 88.473 54.694 49.795 1.00102.39 2874 NZ LYS 311 87.808 55.997 50.082 1.00107.12 2875 H LYS 311 90.572 53.594 48.679 1.00 25.00 2876 1HZ LYS 311 87.884 56.617 49.250 1.00 25.00 2877 2HZ LYS 311 86.804 55.833 50.299 1.00 25.00 2878 3HZ LYS 311 88.268 56.452 50.896 1.00 25.00 2879 N GLU 312 92.461 54.495 46.162 1.00 64.41 2880 CA GLU 312 93.634 54.805 45.346 1.00 61.39 2881 C GLU 312 94.189 53.556 44.667 1.00 61.26 2882 0 GLU 312 94.533 53.585 43.483 1.00 59.48 2883 CB GLU 312 94.724 55.465 46.194 1.00 63.39 2884 CG GLU 312 94.348 56.830 46.748 1.00 70.79 2885 CD GLU 312 95.456 57.456 47.578 1.00 75.21 2886 0E1 GLU 312 95.879 56.840 48.579 1.00 77.19 2887 0E2 GLU 312 95.903 58.570 47.233 1.00 79.86 2888 H GLU 312 92.482 54.687 47.112 1.00 25.00 2889 N LEU 313 94.257 52.459 45.418 1.00 57.55 2890 CA LEU 313 94.765 51.198 44.891 1.00 52.69 2891 C LEU 313 93.885 50.678 43.762 1.00 52.82 2892 0 LEU 313 94.391 50.281 42.713 1.00 51.15 2893 CB LEU 313 94.883 50.158 46.005 1.00 48.63 2894 CG LEU 313 95.886 50.519 47.102 1.00 46.47 2895 CD1 LEU 313 95.941 49.416 48.140 1.00 48.38 2896 CD2 LEU 313 97.259 50.748 46.495 1.00 48.00 2897 H LEU 313 93.952 52.495 46.346 1.00 25.00 2898 N GLU 314 92.569 50.724 43.957 1.00 52.92 2899 CA GLU 314 91.634 50.269 42.933 1.00 54.92 2900 C GLU 314 91.840 51.087 41.651 1.00 52.05 2901 0 GLU 314 91.801 50.548 40.541 1.00 49.73 2902 CB GLU 314 90.189 50.400 43.431 1.00 58.82 2903 CG GLU 314 89.137 49.809 42.488 1.00 68.28 2904 CD GLU 314 89.281 48.303 42.292 1.00 74.40 2905 OE1 GLU 314 89.097 47.550 43.275 1.00 76.74 2906 OE2 GLU , 314 89.568 47.871 41.152 1.00 74.09 2907 H GLU 314 92.221 51.057 44.810 1.00 25.00 2908 N ALA 315 92.088 52.383 41.813 1.00 51.92 2909 CA ALA 315 92.323 53.270 40.678 1.00 54.57 2910 C ALA 315 93.649 52.920 39.993 1.00 51.51 2911 0 ALA 315 93.762 52.977 38.763 1.00 49.98 2912 CB ALA 315 92.335 54.722 41.142 1.00 52.19 2913 H ALA 315 92.103 52.753 42.723 1.00 25.00 2914 N TYR 316 94.640 52.542 40.796 1.00 49.90 2915 CA TYR 316 95.960 52.177 40.289 1.00 46.00 2916 C TYR 316 95.911 50.864 39.506 1.00 42.05 2917 0 TYR 316 96.503 50.756 38.424 1.00 36.96 2918 CB TYR 316 96.954 52.070 41.445 1.00 48.32 2919 CG TYR 316 98.405 52.154 41.029 1.00 52.17 2920 CD1 TYR 316 98.975 53.371 40.657 1.00 53.66 2921 CD2 TYR 316 99.218 51.023 41.033 1.00 58.41 2922 CE1 TYR 316 100.320 53.461 40.303 1.00 56.28 2923 CE2 TYR 316 100.566 51.101 40.681 1.00 63.22 2924 CZ TYR 316 101.110 52.323 40.319 1.00 58.59 2925 OH TYR 316 102.442 52.405 39.986 1.00 51.77 2926 H TYR 316 94.483 52.514 41.763 1.00 25.00 2927 HH TYR 316 102.631 53.311 39.758 1.00 25.00 2928 N THR 317 95.186 49.881 40.040 1.00 38.98 2929 CA THR 317 95.044 48.574 39.396 1.00 40.08 2930 C THR 317 94.391 48.732 38.025 1.00 41.19 2931 0 THR 317 94.755 48.046 37.065 1.00 40.64 2932 CB THR 317 94.189 47.619 40.245 1.00 39.21 2933 0G1 THR 317 94.658 47.632 41.598 1.00 40.99 2934 CG2 THR 317 94.277 46.198 39.698 1.00 41.75 2935 H THR 317 94.740 50.022 40.900 1.00 25.00 2936 HG1 THR 317 94.120 47.056 42.134 1.00 25.00 2937 N ASP 318 93.423 49.641 37.945 1.00 46.22 2938 CA ASP 318 92.719 49.920 36.700 1.00 44.99 2939 C ASP 318 93.631 50.595 35.693 1.00 38.74 2940 0 ASP 318 93.695 50.183 34.536 1.00 39.12 2941 CB ASP 318 91.497 50.799 36.959 1.00 55.80 2942 CG ASP 318 90.215 50.006 36.977 1.00 64.67 2943 0D1 ASP 318 89.924 49.364 38.010 1.00 73.33 2944 0D2 ASP 318 89.507 50.014 35.948 1.00 72.06 2945 H ASP 318 93.171 50.138 38.755 1.00 25.00 2946 N ALA 319 94.340 51.628 36.135 1.00 37.74 2947 CA ALA 319 95.258 52.347 35.260 1.00 40.21 2948 C ALA 319 96.245 51.360 34.644 1.00 42.98 2949 0 ALA 319 96.528 51.422 33.446 1.00 41.24 2950 CB ALA 319 95.995 53.426 36.039 1.00 42.19 2951 H ALA 319 94.240 51.923 37.067 1.00 25.00 2952 N ILE 320 96.727 50.423 35.462 1.00 41.94 2953 CA ILE 320 97.670 49.403 35.005 1.00 40.80 2954 C ILE 320 97.064 48.488 33.934 1.00 37.20 2955 0 ILE 320 97.711 48.200 32.923 1.00 31.26 2956 CB ILE 320 98.198 48.549 36.191 1.00 40.22 2957 CG1 ILE 320 99.093 49.404 37.091 1.00 38.13 2958 CG2 ILE 320 98.973 47.332 35.680 1.00 36.19 2959 CD1 ILE 320 100.340 49.924 36.392 1.00 35.64 2960 H ILE 320 96.447 50.429 36.402 1.00 25.00 2961 N GLN 321 95.830 48.037 34.149 1.00 37.70 2962 CA GLN 321 95.167 47.161 33.180 1.00 43.79 2963 C GLN 321 94.959 47.867 31.839 1.00 44.60 2964 0 GLN 321 95.104 47.254 30.777 1.00 43.29 2965 CB GLN 321 93.818 46.662 33.713 1.00 45.39 2966 CG GLN 321 93.879 45.997 35.079 1.00 50.49 2967 CD GLN 321 94.981 44.963 35.182 1.00 52.12 2968 OE1 GLN 321 95.097 44.073 34.341 1.00 53.96 2969 NE2 GLN 321 95.801 45.078 36.220 1.00 49.92 2970 H GLN 321 95.360 48.301 34.967 1.00 25.00 2971 1 HE2 GLN 321 96.511 44.405 36.295 1.00 25.00 2972 2HE2 GLN 321 95.664 45.810 36.855 1.00 25.00 2973 N ARG 322 94.595 49.148 31.894 1.00 48.28 2974 CA ARG 322 94.376 49.935 30.683 1.00 48.66 2975 C ARG 322 95.697 50.181 29.976 1.00 48.74 2976 0 ARG 322 95.756 50.167 28.745 1.00 52.54 2977 CB ARG 322 93.701 51.272 31.003 1.00 53.96 2978 CG ARG 322 92.175 51.230 31.029 1.00 62.97 2979 CD ARG 322 91.642 50.367 32.164 1.00 68.65 29880 NE ARG 322 90.183 50.288 32.167 1.00 71.23 2981 CZ ARG 322 89.377 51.274 32.546 1.00 73.12 2982 NH1 ARG 322 89.878 52.432 32.959 1.00 75.57 2983 NH2 ARG 322 88.064 51.101 32.512 1.00 75.20 2984 H ARG 322 94.477 49.570 32.771 1.00 25.00 2985 HE ARG 322 83.771 49.449 31.873 1.00 25.00 2986 1 HH1 ARG 322 90.868 52.574 32.983 1.00 25.00 2987 2HH1 ARG 322 89.263 53.172 33.235 1.00 25.00 2988 1 HH2 ARG 322 87.684 50.229 32.203 1.00 25.00 2989 2HH2 ARG 322 87.455 51.842 32.793 1.00 25.00 2990 N TRP 323 96.740 50.434 30.765 1.00 48.78 2991 CA TRP 323 98.086 50.674 30.248 1.00 50.53 2992 C TRP 323 98.036 51.721 29.139 1.00 51.62 2993 0 TRP 323 98.368 51.442 27.984 1.00 46.60 2994 CB TRP 323 98.676 49.361 29.719 1.00 45.66 2995 CG TRP 323 100.171 49.334 29.673 1.00 43.84 2996 CD1 TRP 323 100.972 49.778 28.660 1.00 41.07 2997 CD2 TRP 323 101.045 48.811 30.677 1.00 42.00 2998 NE1 TRP 323 102.292 49.559 28.969 1.00 41.37 2999 CE2 TRP 323 102.367 48.967 30.202 1.00 42.95 3000 CE3 TRP 323 100.841 48.222 31.932 1.00 43.56 3001 CZ2 TRP 323 103.483 48.555 30.939 1.00 41.64 3002 CZ3 TRP 323 101.952 47.812 32.666 1.00 46.00 3003 CH2 TRP 323 103.256 47.982 32.164 1.00 42.99 3004 H TRP 323 96.604 50.455 31.735 1.00 25.00 3005 HE1 TRP 323 103.052 49.790 28.396 1.00 25.00 3006 N ASP 324 97.624 52.931 29.503 1.00 59.55 3007 CA ASP 324 97.500 54.015 28.539 1.00 65.59 3008 C ASP 324 98.480 55.143 28.844 1.00 64.51 3009 0 ASP 324 99.591 55.176 28.316 1.00 68.35 3010 CB ASP 324 96.056 54.541 28.552 1.00 70.35 3011 CG ASP 324 95.713 55.365 27.320 1.00 74.75 3012 OD1 ASP 324 96.439 56.333 27.008 1.00 77.92 3013 OD2 ASP 324 94.698 55.043 26.668 1.00 77.68 3014 H ASP 324 97.422 53.067 30.447 1.00 25.00 3015 N ILE 325 98.025 56.067 29.685 1.00 59.63 3016 CA ILE 325 98.765 57.248 30.131 1.00 62.22 3017 C ILE 325 97.699 58.281 30.472 1.00 62.36 3018 0 ILE 325 97.807 58.988 31.467 1.00 57.92 3019 CB ILE 325 99.752 57.824 29.066 1.00 58.28 3020 CG1 ILE 325 100.656 58.874 29.713 1.00 56.91 3021 CG2 ILE 325 99.004 58.424 27.882 1.00 53.60 3022 CD1 ILE 325 101.760 59.364 28.812 1.00 65.51 3023 H ILE 325 97.138 55.950 30.059 1.00 25.00 3024 N ASN 326 96.622 58.287 29.687 1.00 64.69 3025 CA ASN 326 95.504 59.203 29.902 1.00 68.20 3026 C ASN 326 94.857 58.860 31.238 1.00 71.30 3027 0 ASN 326 94.171 59.684 31.846 1.00 76.27 3028 CB ASN 326 94.462 59.058 28.787 1.00 67.58 3029 CG ASN 326 95.041 59.297 27.406 1.00 69.04 3030 0D1 ASN 326 96.055 59.975 27.225 1.00 68.18 3031 ND2 ASN 326 94.410 58.716 26.395 1.00 67.11 3032 H ASN 326 96.599 57.685 28.918 1.00 25.00 3033 1HD2 ASN 326 94.783 58.869 25.501 1.00 25.00 3034 2HD2 ASN 326 93.618 58.173 26.568 1.00 25.00 3035 N GLU 327 95.095 57.631 31.691 1.00 70.98 3036 CA GLU 327 94.553 57.144 32.952 1.00 69.92 3037 C GLU 327 95.259 57.798 34.138 1.00 67.58 3038 0 GLU 327 94.751 57.777 35.260 1.00 68.23 3039 CB GLU 327 94.709 55.622 33.034 1.00 69.72 3040 CG GLU 327 94.147 54.858 31.838 1.00 66.84 3041 CD GLU 327 92.650 55.040 31.659 1.00 69.61 3042 0E1 GLU 327 91.899 54.845 32.639 1.00 69.86 3043 0E2 GLU 327 92.225 55.369 30.530 1.00 66.87 3044 H GLU 327 95.646 57.037 31.159 1.00 25.00 3045 N ILE 328 96.411 58.407 33.872 1.00 64.07 3046 CA ILE 328 97.212 59.065 34.901 1.00 63.90 3047 C ILE 328 96.425 60.142 35.657 1.00 70.44 3048 0 ILE 328 96.624 60.338 36.857 1.00 69.65 3049 CB ILE 328 98.508 59.669 34.286 1.00 56.23 3050 CG1 ILE 328 99.578 59.844 35.359 1.00 56.00 3051 CG2 ILE 328 98.223 61.007 33.618 1.00 53.09 3052 CD1 ILE 328 100.948 60.162 34.799 1.00 58.67 3053 H ILE 328 96.744 58.430 32.958 1.00 25.00 3054 N ASP 329 95.487 60.780 34.961 1.00 75.68 3055 CA ASP 329 94.659 61.844 35.531 1.00 79.88 3056 C ASP 329 93.764 61.377 36.677 1.00 79.44 3057 0 ASP 329 93.303 62.188 37.483 1.00 79.71 3058 CB ASP 329 93.796 62.476 34.435 1.00 85.36 3059 CG ASP 329 94.608 62.912 33.226 1.00 90.96 3060 0D1 ASP 329 95.719 63.461 33.409 1.00 93.02 3061 OD2 ASP 329 94.133 62.699 32.090 1.00 93.14 3062 H A . 329 95.344 60.527 34.026 1.00 25.00 3063 N ARG 330 93.501 60.074 36.730 1.00 76.85 3064 CA ARG 330 92.658 59.501 37.775 1.00 75.38 3065 C ARG 330 93.488 59.059 38.981 1.00 71.57 3066 0 ARG 330 92.935 58.631 39.998 1.00 69.70 3067 CB ARG 330 91.881 58.300 37.227 1.00 75.33 3068 CG ARG 330 91.177 58.562 35.905 1.00 78.99 3069 CD ARG 330 90.383 57.350 35.454 1.00 80.32 3070 NE ARG 330 89.861 57.517 34.100 1.00 86.31 3071 CZ ARG 330 88.851 56.816 33.592 1.00 88.51 3072 NH1 ARG 330 88.239 55.894 34.325 1.00 91.01 3073 NH2 ARG 330 88.458 57.030 32.344 1.00 89.50 3074 H ARG 330 93.891 59.477 36.060 1.00 25.00 3075 HE ARG 330 90.281 58.188 33.523 1.00 25.00 3076 1 HH1 ARG 330 88.533 55.723 35.265 1.00 25.00 3077 2HH1 ARG 330 87.475 55.375 33.942 1.00 25.00 3078 1 HH2 ARG 330 88.917 57.720 31.786 1.00 25.00 3079 2HH2 ARG 330 87.692 56.508 31.966 1.00 25.00 3080 N LEU 331 94.809 59.174 38.867 1.00 67.63 3081 CA LEU 331 95.723 58.761 39.930 1.00 62.95 3082 C LEU 331 96.290 59.919 40.735 1.00 60.42 3083 0 LEU 331 96.590 60.974 40.186 1.00 58.28 3084 CB LEU 331 96.906 57.985 39.338 1.00 58.68 3085 CG LEU 331 96.664 56.739 38.486 1.00 54.70 3086 CD1 LEU 331 97.992 56.255 37.941 1.00 46.64 3087 CD2 LEU 331 95.988 55.654 39.304 1.00 48.82 3088 H LEU 331 95.195 59.574 38.061 1.00 25.00 3089 N PRO 332 96.426 59.743 42.058 1.00 57.70 3090 CA PRO 332 96.981 60.814 42.886 1.00 58.87 3091 C PRO 332 98.455 60.977 42.521 1.00 61.32 3092 0 PRO 332 99.132 59.997 42.207 1.00 63.75 3093 CB PRO 332 96.800 60.278 44.307 1.00 58..32 3094 CG PRO 332 96.819 58.793 44.122 1.00 60.80 3095 CD PRO 332 95.978 58.616 42.892 1.00 59.09 3096 N ASP 333 98.944 62.210 42.585 1.00 68.56 3097 CA ASP 333 100.324 62.554 42.237 1.00 71.37 3098 C ASP 333 101.432 61.520 42.437 1.00 68.42 3099 0 ASP 333 102.188 61.247 41.504 1.00 65.66 3100 CB ASP 333 100.715 63.879 42.891 1.00 79.84 3101 CG ASP 333 99.967 65.057 42.298 1.00 86.67 3102 0D1 ASP 333 100.442 65.608 41.283 1.00 91.38 3103 OD2 ASP 333 98.897 65.418 42.834 1.00 90.77 3104 H ASP 333 98.343 62.928 42.866 1.00 25.00 3105 N TYR 334 101.536 60.936 43.627 1.00 65.59 3106 CA TYR 334 1022.588 59.953 43.861 1.00 63.25 3107 C TYR 334 102.455 58.740 42.938 1.00 60.61 3108 0 TYR 334 103.452 58.243 42.411 1.00 63.00 3109 CB TYR 334 102.664 59.545 45.341 1.00 65.74 3110 CG TYR 334 101.539 58.674 45.852 1.00 68.46 3111 CD1 TYR 334 100.343 59.232 46.303 1.00 69.57 3112 CD2 TYR 334 101.690 57.289 45.929 1.00 68.64 3113 CE1 TYR 334 99.326 58.432 46.824 1.00 69.54 3114 CE2 TYR 334 100.682 56.482 46.446 1.00 69.64 3115 CZ TYR 334 99.504 57.058 46.892 1.00 70.47 3116 OH TYR 334 98.515 56.257 47.413 1.00 68.60 3117 H TYR 334 100.910 61.170 44.337 1.00 25.00 3118 HH TYR 334 97.786 56.812 47.691 1.00 25.00 3119 N MET 335 101.220 58.311 42.691 1.00 51.84 3120 CA MET 335 100.977 57.174 41.809 1.00 46.91 3121 C MET 335 101.236 57.558 40.356 1.00 46.00 3122 0 MET 335 101.540 56.701 39.525 1.00 49.65 3123 CB MET 335 99.552 56.646 41.969 1.00 41.83 3124 CG MET 335 99.268 56.054 43.333 1.00 37.39 3125 SD MET 335 97.625 55.322 43.450 1.00 44.89 3126 CE MET 335 97.914 54.042 44.666 1.00 45.77 3127 H MET 335 100.460 58.772 43.094 1.00 25.00 3128 N LYS 336 101.122 58.848 40.052 1.00 47.61 3129 CA LYS 336 101.366 59.340 38.699 1.00 48.27 3130 C LYS 336 102.836 59.143 38.325 1.00 46.89 3131 0 LYS 336 103.161 58.829 37.177 1.00 49.33 3132 CB LYS 336 101.000 60.824 38.588 1.00 51.58 3133 CG LYS 336 99.517 61.132 38.743 1.00 54.94 3134 CD LYS 336 99.233 62.600 38.446 1.00 60.67 3135 CE LYS 336 97.739 62.882 38.431 1.00 63.81 3136 NZ LYS 336 97.404 64.287 38.083 1.00 68.16 3137 H LYS 336 100.869 59.485 40.750 1.00 25.00 3138 1HZ LYS 336 97.836 64.931 38.776 1.00 25.00 3139 2HZ LYS 336 97.770 64.503 37.134 1.00 25.00 3140 3HZ LYS 336 96.371 64.409 38.092 1.00 25.00 3141 N ILE 337 103.719 59.321 39.303 1.00 44.56 3142 CA ILE 337 105.154 59.162 39.089 1.00 47.99 3143 C ILE 337 105.469 57.701 38.782 1.00 50.21 3144 0 ILE 3337 106.153 57.400 37.800 1.00 52.97 3145 CB ILE 337 105.957 59.595 40.336 1.00 51.57 3146 CG1 ILE 337 105.533 61.001 40.770 1.00 54.20 3147 CG2 ILE 337 107.455 59.569 40.034 1.00 49.66 3148 CD1 ILE 337 106.048 61.406 42.131 1.00 53.35 3149 H ILE 337 103.390 59.566 40.195 1.00 25.00 3150 N SER 338 104.951 56.802 39.618 1.00 46.40 3151 CA SER 338 105.161 55.364 39.458 1.00 41.92 3152 C SER 338 104.640 54.905 38.098 1.00 39.82 3153 0 SER 338 105.385 54.347 37.286 1.00 36.78 3154 CB SER 338 104.423 54.598 40.560 1.00 37.35 3155 OG SER 338 104.502 55.268 41.805 1.00 52.45 3156 H SER 338 104.411 57.109 40.381 1.00 25.00 3157 HG SER 338 105.419 55.324 42.084 1.00 25.00 3158 N TYR 339 103.363 55.183 37.848 1.00 39.53 3159 CA TYR 339 102.697 54.804 36.606 1.00 40.68 3160 C TYR 339 103.468 55.247 35.362 1.00 39.79 3161 0 TYR 339 103.719 54.444 34.458 1.00 3978 3162 CB TYR 339 101.272 55.374 36.586 1.00 39.96 3163 CG TYR 339 100.388 54.833 35.480 1.00 44.71 3164 CD1 TYR 339 99.948 53.507 35.494 1.00 40.18 3165 CD2 TYR 339 99.992 55.646 34.416 1.00 42.64 3166 CE1 TYR 339 99.136 53.004 34.475 1.00 40.02 3167 CE2 TYR 339 99.180 55.151 33.393 1.00 46.52 3168 CZ TYR 339 98.758 53.830 33.431 1.00 40.74 3169 OH TYR 339 97.968 53.3422 32.417 1.00 44.28 3170 H TYR 339 102.843 55.668 38.522 1.00 25.00 3171 HH TYR 339 97.819 54.042 31.792 1.00 25.00 3172 N LYS 340 103.864 56.515 35.324 1.00 42.19 3173 CA LYS 340 104.599 57.032 34.179 1.00 42.37 3174 C LYS 340 105.930 56.306 33.992 1.00 40.71 3175 0 LYS 340 106.264 55.885 32.882 1.00 41.93 3176 CB LYS 340 104.826 58.541 34.306 1.00 48.48 3177 CG LYS 340 105.461 59.136 33.063 1.00 61.36 3178 CD LYS 340 105.412 60.647 33.041 1.00 76.14 3179 CE LYS 340 105.947 61.164 31.713 1.00 85.02 3180 NZ LYS 340 105.783 62.636 31.566 1.00 94.84 3181 H LYS 340 103.661 57.115 36.074 1.00 25.00 3182 1HZ LYS 340 104.774 62.881 31.624 1.00 25.00 3183 2HZ LYS 340 106.302 63.119 32.327 1.00 25.00 3184 3HZ LYS 340 106.160 62.937 30.645 1.00 25.00 3185 N ALA 341 106.668 56.134 35.084 1.00 40.84 3186 CA ALA 341 107.963 55.455 35.052 1.00 36.82 3187 C ALA 341 107.837 54.053 34.469 1.00 35.10 3188 0 ALA 341 108.657 53.635 33.650 1.00 34.92 3189 CB ALA 341 108.548 55.388 36.451 1.00 37.09 3190 H ALA 341 106.336 56.478 35.942 1.00 25.00 3191 N ILE 342 106.796 53.338 34.884 1.00 32.81 3192 CA ILE 342 106.547 51.983 34.409 1.00 31.78 3193 C ILE 342 106.357 51.982 32.891 1.00 38.13 3194 0 ILE 342 107.061 51.269 32.163 1.00 37.84 3195 CB ILE 342 105.306 51.377 35.109 1.00 27.44 3196 CG1 ILE 342 105.585 51.219 36.606 1.00 30.45 3197 CG2 ILE 342 104.943 50.031 34.499 1.00 29.34 3198 CD1 ILE 342 104.399 50.759 37.420 1.00 30.40 3199 H ILE 342 106.179 53.740 35.532 1.00 25.00 3200 N LEU 343 105.447 52.827 32.414 1.00 44.76 3201 CA LEU 343 105.168 52.920 30.984 1.00 42.79 3202 c LEU 343 106.428 53.290 30.214 1.00 40.23 3203 o LEU 343 106.706 52.724 29.153 1.00 39.11 3204 CB LEU 343 104.061 53.943 30.715 1.00 42.96 3205 CG LEU 343 102.731 53.704 31.436 1.00 46.89 3206 CD1 LEU 343 101.704 54.723 30.978 1.00 51.34 3207 CD2 LEU 343 102.233 52.302 31.166 1.00 44.17 3208 H LEU 343 104.954 53.403 33.039 1.00 25.00 3209 N ASP 344 107.202 54.218 30.770 1.00 40.93 3210 CA ASP 344 108.442 54.660 30.144 1.00 43.89 3211 C ASP 344 109.443 53.515 30.053 1.00 43.08 3212 0 ASP 344 110.049 53.299 29.001 1.00 38.31 3213 CB ASP 344 109.056 55.831 30.921 1.00 50.27 3214 CG ASP 344 108.259 57.124 30.775 1.00 58.66 3215 OD1 ASP 344 107.376 57.206 29.891 1.00 59.02 3216 OD2 ASP 344 108.525 58.070 31.549 1.00 62.70 3217 H ASP 344 106.928 54.612 31.623 1.00 25.00 3218 N LEU 345 109.585 52.764 31.144 1.00 40.54 3219 CA LEU 345 110.511 51.633 31.196 1.00 36.66 3220 C LEU 345 110.256 50.661 30.048 1.00 36.17 3221 0 LEU 345 111.188 50.256 29.343 1.00 35.58 3222 CB LEU 345 110.393 50.903 32.540 1.00 38.27 3223 CG LEU 345 111.284 49.672 32.755 1.00 35.02 3224 CD1 LEU 345 112.750 50.043 32.587 1.00 28.76 3225 CD2 LEU 345 111.030 49.087 34.132 1.00 30.95 3226 H LEU 345 109.050 52.975 31.934 1.00 25.00 3227 N TYR 346 108.992 50.304 29.844 1.00 35.43 3228 CA TYR 346 108.650 49.389 28.768 1.00 32.38 3229 C TYR 346 108.906 49.969 27.388 1.00 34.86 3230 0 TYR 346 109.183 49.228 26.446 1.00 36.74 3231 CB TYR 346 107.227 48.870 28.927 1.00 33.82 3232 CG TYR 346 107.173 47.798 29.980 1.00 31.79 3233 CD1 TYR 346 107.531 46.487 29.675 1.00 34.43 3234 CD2 TYR 346 106.856 48.107 31.302 1.00 34.30 3235 CE1 TYR 346 107.585 45.507 30.659 1.00 32.57 3236 CE2 TYR 346 106.906 47.137 32.296 1.00 34.14 3237 CZ TYR 346 107.275 45.839 31.965 1.00 34.31 3238 OH TYR 346 107.351 44.878 32.938 1.00 32.03 3239 H TYR 346 108.288 50.665 30.428 1.00 25.00 3240 HH TYR 346 107.610 44.036 32.562 1.00 25.00 3241 N LYS 347 108.861 51.295 27.276 1.00 44.24 3242 CA LYS 347 109.143 51.955 26.004 1.00 44.41 3243 C LYS 347 110.630 51.792 25.716 1.00 43.81 3244 0 LYS 347 111.030 51.558 24.572 1.00 42.39 3245 CB LYS 347 108.762 53.437 26.060 1.00 51.50 3246 CG LYS 347 107.268 53.672 25.945 1.00 55.25 3247 CD LYS 347 106.759 53.062 24.650 1.00 59.99 3248 CE LYS 347 105.251 52.978 24.608 1.00 60.17 3249 NZ LYS 347 104.841 52.152 23.446 1.00 53.42 3250 H LYS 347 108.627 51.840 28.057 1.00 25.00 3251 1HZ LYS 347 105.241 51.196 23.537 1.00 25.00 3252 2HZ LYS 347 103.803 52.090 23.409 1.00 25.00 3253 3HZ LYS 347 105.190 52.590 22.569 1.00 25.00 3254 N ASP 348 111.439 51.874 26.771 1.00 45.04 3255 CA ASP 348 112.884 51.712 26.654 1.00 47.19 3256 C ASP 348 113.178 50.289 26.211 1.00 44.53 3257 0 ASP 348 113.992 50.074 25.316 1.00 46.94 3258 CB ASP 348 113.582 51.981 27.991 1.00 55.77 3259 CG ASP 348 113.469 53.430 28.441 1.00 63.79 3260 0D1 ASP 348 113.017 54.288 27.648 1.00 66.77 3261 0D2 ASP 348 113.846 53.710 29.600 1.00 65.20 3262 H ASP 348 111.048 52.057 27.652 1.00 25.00 3263 N TYR 349 112.507 49.321 26.835 1.00 39.87 3264 CA TYR 349 112.692 47.913 26.491 1.00 40.93 3265 C TYR 349 112.412 47.704 25.008 1.00 41.26 3266 0 TYR 349 113.189 47.051 24.302 1.00 40.44 3267 CB TYR 349 111.752 47.015 27.310 1.00 35.88 3268 CG TYR 349 112.115 46.841 28.773 1.00 33.98 3269 CD1 TYR 349 113.396 47.144 29.250 1.00 29.99 3270 CD2 TYR 349 111.172 46.360 29.680 1.00 27.01 3271 CE1 TYR 349 113.723 46.971 30.596 1.00 27.43 3272 CE2 TYR 349 111.485 46.182 31.021 1.00 32.24 3273 CZ TYR 349 112.759 46.491 31.476 1.00 34.71 3274 OH TYR 349 113.045 46.346 32.813 1.00 31.76 3275 H TYR 349 111.880 49.567 27.549 1.00 25.00 3276 HH TYR 349 112.295 45.961 33.270 1.00 25.00 3277 N GLU 350 111.302 48.269 24.541 1.00 44.18 3278 CA GLU 350 110.911 48.156 23.140 1.00 47.18 3279 C GLU 350 111.972 48.767 22.235 1.00 45.46 3280 0 GLU 350 112.337 48.175 21.221 1.00 45.14 3281 CB GLU 350 109.557 48.828 22.903 1.00 48.54 3282 CG GLU 350 108.396 48.141 23.609 1.00 52.79 3283 CD GLLU 350 107.076 48.883 23.473 1.00 59.87 3284 OE1 GLU 350 107.070 50.040 23.000 1.00 66.09 3285 OE2 GLU 350 106.037 48.304 23.852 1.00 65.68 3286 H GLU 350 110.728 48.772 25.158 1.00 25.00 3287 N LYS 351 112.497 49.923 22.636 1.00 48.01 3288 CA LYS 351 113.530 50.618 21.871 1.00 51.81 3289 C LYS 351 114.794 49.756 21.788 1.00 52.11 3290 0 LYS 351 115.311 49.505 20.696 1.00 48.04 3291 CB LYS 351 113.861 51.973 22.518 1.00 53.86 3292 CG LYS 351 114.151 53.095 21.520 1.00 60.98 3293 CD LYS 351 115.235 52.708 20.517 1.00 68.26 3294 CE LYS 351 115.153 53.551 19.253 1.00 75.67 3295 NZ LYS 351 115.951 52.975 18.132 1.00 74.32 3296 H LYS 351 112.180 50.322 23.471 1.00 25.00 3297 1HZ LYS 351 116.950 52.914 18.410 1.00 25.00 3298 2HZ LYS 351 115.590 52.025 17.907 1.00 25.00 3299 3HZ LYS 351 115.855 53.584 17.293 1.00 25.00 3300 N GLU 352 115.275 49.297 22.944 1.00 56.12 3301 CA GLU 352 116.474 48.461 23.031 1.00 54.04 3302 C GLU 352 116.409 47.241 22.120 1.00 52.28 3303 0 GLU 352 117.410 46.851 21.514 1.00 52.78 3304 CB GLU 352 116.688 47.971 24.466 1.00 58.92 3305 CG GLU 352 117.135 49.023 25.460 1.00 67.31 3306 CD GLU 352 117.386 48.438 26.842 1.00 71.98 3307 0E1 GLU 352 118.383 47.694 27.004 1.00 69.15 3308 0E2 GLU 352 116.582 48.718 27.760 1.00 65.74 3309 H GLU 352 114.800 49.527 23.762 1.00 25.00 3310 N LEU 353 115.235 46.624 22.052 1.00 49.88 3311 CA LEU 353 115.053 45.435 21.233 1.00 51.47 3312 C LEU 353 114.701 45.732 19.772 1.00 55.82 3313 0 LEU 353 114.606 44.809 18.955 1.00 56.53 3314 CB LEU 353 114.009 44.511 21.876 1.00 44.77 3315 CG LEU 353 114.320 44.017 23.297 1.00 40.31 3316 CD1 LEU 353 113.151 43.224 23.855 1.00 35.62 3317 CD2 LEU 353 115.586 43.172 23.302 1.00 33.71 3318 H LEU 353 114.478 46.975 22.571 1.00 25.00 3319 N SER 354 114.538 47.012 19.437 1.00 62.13 3320 CA SER 354 114.202 47.423 18.071 1.00 66.31 33221 C SER 354 115.245 46.970 17.058 1.00 64.64 3322 0 SER 354 114.904 46.378 16.035 1.00 66.26 3323 CB SER 354 114.043 48.945 17.978 1.00 69.09 3324 OG SER 354 112.959 49.406 18.763 1.00 80.83 3325 H SER 354 114.623 47.710 20.121 1.00 25.00 3326 HG SER 354 112.888 50.360 18.684 1.00 25.00 3327 N SER 355 116.516 47.223 17.359 1.00 65.77 3328 CA SER 355 117.616 46.850 16.472 1.00 67.77 3329 C SER 355 117.631 45.364 16.110 1.00 68.81 3330 0 SER 355 118.082 44.990 15.028 1.00 69.36 3331 CB SER 355 118.956 47.245 17.099 1.00 66.08 3332 OG SER 355 119.067 46.741 18.419 1.00 68.44 3333 H SER 355 116.729 47.670 18.209 1.00 25.00 3334 HG SER 355 119.043 45.780 18.416 1.00 25.00 3335 N ALA 356 117.150 44.525 17.024 1.00 69.39 3336 CA ALA 356 117.115 43.082 16.802 1.00 68.66 3337 C ALA 356 115.741 42.585 16.347 1.00 69.25 3338 0 ALA 356 115.561 41.395 16.084 1.00 71.52 3339 CB ALA 356 117.549 42.347 18.067 1.00 64.46 3340 H ALA 356 116.806 44.884 17.867 1.00 25.00 3341 N GLY 357 114.773 43.493 16.270 1.00 67.77 3342 CA GLY 357 113.432 43.118 15.854 1.00 62.16 3343 C GLY 357 112.754 42.202 16.856 1.00 58.02 3344 0 GLY 357 111.969 41.327 16.481 1.00 58.07 3345 H GLY 357 114.965 44.428 16.477 1.00 25.00 3346 N ARG 358 113.039 42.416 18.138 1.00 53.28 3347 CA ARG 358 112.461 41.601 19.204 1.00 50.96 3348 C ARG 358 111.486 42.359 20.106 1.00 50.55 3349 0 ARG 358 110.885 41.774 20.999 1.00 51.85 3350 CB ARG 358 113.568 40.953 20.047 1.00 44.69 3351 CG ARG 358 114.360 39.872 19.314 1.00 43.66 3352 CD ARG 358 115.389 39.206 20.217 1.00 43.11 3353 NE ARG 358 114.768 38.503 21.338 1.00 42.40 3354 CZ ARG 358 114.997 38.783 22.618 1.00 43.84 3355 NH1 ARG 358 115.836 39.754 22.951 1.00 49.95 3356 NH2 ARG 358 114.389 38.089 23.571 1.00 45.03 3357 H ARG 358 113.664 43.136 18.368 1.00 25.00 3358 HE ARG 358 114.142 37.776 21.138 1.00 25.00 3359 1HH1 ARG 358 116.301 40.282 22.241 1.00 25.00 3360 2HH1 ARG 358 116.006 39.958 23.915 1.00 25.00 3361 1 HH2 ARG 358 113.755 37.355 23.327 1.00 25.00 3362 2HH2 ARG 358 114.562 38.301 24.533 1.00 25.00 3363 N SER 359 111.270 43.639 19.826 1.00 50.59 3364 CA SER 359 110.363 44.464 20.625 1.00 47.98 3365 C SER 359 108.948 43.888 20.767 1.00 48.46 3366 0 SER 359 108.247 44.177 21.737 1.00 46.16 3367 CB SER 359 110.315 45.879 20.050 1.00 51.38 3368 OG SER 359 110.450 45.839 18.639 1.00 63.31 3369 H SER 359 111.730 44.045 19.067 1.00 25.00 3370 HG SER 359 111.323 45.514 18.419 1.00 25.00 3371 N HIS 360 108.559 43.029 19.8829 1.00 46.52 3372 CA HIS 360 107.234 42.401 19.837 1.00 47.05 3373 C HIS 360 106.998 41.398 20.974 1.00 48.80 3374 0 HIS 360 105.893 40.871 21.124 1.00 46.79 3375 CB HIS 360 106.971 41.713 18.492 1.00 47.13 3376 CG HIS 360 108.026 40.724 18.100 1.00 47.23 3377 ND1 HIS 360 107.885 39.365 18.289 1.00 50.30 3378 CD2 HIS 360 109.242 40.899 17.532 1.00 49.82 3379 CE1 HIS 360 108.969 38.746 17.855 1.00 47.18 3380 NE2 HIS 360 109.808 39.655 17.391 1.00 46.40 3381 H HIS 360 109.183 42.837 19.111 1.00 25.00 3382 HD1 HIS 360 107.098 38.919 18.675 1.00 25.00 3383 HE2 HIS 360 110.702 39.494 16.992 1.00 25.00 3384 N ILE 361 108.042 41.098 21.741 1.00 47.17 3385 CA ILE 361 107.922 40.152 22.845 1.00 40.37 3386 C ILE 361 107.657 40.850 24.175 1.00 35.93 3387 0 ILE 361 107.118 40.240 25.103 1.00 41.86 3388 CB ILE 361 109.187 39.277 22.987 1.00 44.49 3389 CG1 ILE 361 110.392 40.152 23.346 1.00 39.20 3390 CG2 ILE 361 109.421 38.477 21.707 1.00 38.28 3391 CD1 ILE 361 111.680 39.405 23.464 1.00 49.02 3392 H ILE 361 108.913 41.517 21.574 1.00 25.00 3393 N VAL 362 108.007 42.131 24.256 1.00 29.83 3394 CA VAL 362 107.818 42.911 25.478 1.00 28.00 3395 C VAL 362 106.396 42.815 26.041 1.00 32.52 3396 0 VAL 362 106.209 42.788 27.262 1.00 34.43 3397 CB VAL 362 108.203 44.401 25.259 1.00 30.93 3398 CG1 VAL 362 107.851 45.233 26.484 1.00 28.70 3399 CG2 VAL 362 109.699 44.524 24.952 1.00 22.99 3400 H VAL 362 108.395 42.568 23.472 1.00 25.00 3401 N CYS 363 105.405 42.701 25.160 1.00 29.77 3402 CA CYS 363 104.011 42.610 25.592 1.00 31.29 3403 C CYS 363 103.757 41.470 26.581 1.00 29.63 3404 0 CYS 363 102.942 41.610 27.499 1.00 25.93 3405 CB CYS 363 103.066 42.504 24.387 1.00 33.73 3406 SG CYS 363 103.387 41.126 23.270 1.00 40.61 3407 H CYS 363 105.612 42.677 24.204 1.00 25.00 3408 N HIS 364 104.480 40.362 26.421 1.00 26.78 3409 CA HIS 364 104.332 39.216 27.315 1.00 24.36 3410 C HIS 364 104.685 39.599 28.754 1.00 31.26 3411 0 HIS 364 104.029 39.163 29.703 1.00 32.48 3412 CB HIS 364 105.220 38.064 26.855 1.00 26.25 3413 CG HIS 364 104.826 37.486 25.531 1.00 29.86 3414 ND1 HIS 364 103.731 36.663 25.372 1.00 39.99 3415 CD2 HIS 364 105.398 37.588 24.308 1.00 32.37 3416 CE1 HIS 364 103.646 36.282 24.110 1.00 36.28 3417 NE2 HIS 364 104.646 36.829 23.444 1.00 32.87 3418 H HIS 364 105.139 40.332 25.695 1.00 25.00 3419 HD1 HIS 364 103.H3 36.392 26.086 1.00 25.00 3420 HE2 HIS 364 104.819 36.718 22.488 1.00 25.00 3421 N ALA 365 105.711 40.431 28.911 1.00 28.85 3422 CA ALA 365 106.134 40.880 30.232 1.00 30.11 3423 C ALA 365 105.075 41.813 30.826 1.00 31.00 3424 O ALA 365 104.727 41.708 32.005 1.00 31.25 3425 CB ALA 365 107.482 41.585 30.140 1.00 31.82 3426 H ALA 365 106.191 40.762 28.123 1.00 25.00 3427 N ILE 366 104.548 42.708 29.992 1.00 33.54 3428 CA ILE 366 103.512 43.653 30.417 1.00 33.21 3429 C ILE 366 102.287 42.889 30.922 1.00 29.56 3430 O ILE 366 101.743 43.199 31.987 1.00 31.04 3431 CB ILE 366 103.086 44.582 29.255 1.00 33.17 3432 CG1 ILE 366 104.264 45.455 28.823 1.00 30.87 3433 CG2 ILE 366 101.908 45.453 29.674 1.00 28.96 3434 CD1 ILE 366 103.987 46.289 27.599 1.00 35..02 3435 H ILE 366 104.869 42.731 29.067 1.00 25.00 3436 N GLU 367 101.874 41.875 30.167 1.00 28.47 3437 CA GLU 367 100.726 41.061 30.548 1.00 30.13 3438 C GLU 367 100.945 40.439 31.929 1.00 30.58 3439 O GLU 367 100.029 40.407 32.754 1.00 31.55 3440 CB GLU 367 100.461 39.966 29.507 1.00 38.78 3441 CG GLU 367 100.228 40.472 28.074 1.00 52.31 3442 CD GLU 367 99.180 41.585 27.970 1.00 62.83 3443 OE1 GLU 367 98.144 41.525 28.675 1.00 55.58 3444 OE2 GLU 367 99.395 42.523 27.168 1.00 63.90 3445 H GLU 367 102.351 41.673 29.337 1.00 25.00 3446 N ARG 368 102.167 39.985 32.196 1.00 28.25 3447 CA ARG 368 102.479 39.385 33.487 1.00 21.98 3448 C ARG 368 102.462 40.420 34.607 1.00 22.36 3449 O ARG 368 102.080 40.108 35.738 1.00 22.36 3450 CB ARG 368 103.821 38.661 33.440 1.00 23.96 3451 CG ARG 368 103.796 37.364 32.642 1.00 17.80 3452 CD ARG 368 102.812 36.352 33.224 1.00 19.62 3453 NE ARG 368 103.008 35.034 32.626 1.00 19.60 3454 CZ ARG 368 102.516 33.897 33.113 1.00 20.41 3455 NH1 ARG 368 101.773 33.898 34.211 1.00 26.21 3456 NH2 ARG 368 102.843 32.743 32.548 1.00 22.02 3457 H ARG 363 102.868 40.046 31.510 1.00 25.00 3458 HE ARG 368 103.526 34.993 31.804 1.00 25.00 3459 1HH1 ARG 368 101.580 34.754 34.685 1.00 25.00 3460 2HH1 ARG 368 101.410 33.036 34.566 1.00 25.00 3461 1HH2 ARG 368 103.454 32.730 31.755 1.00 25.00 3462 2HH2 ARG 368 102.476 31.888 32.904 1.00 25.00 3463 N MET 369 102.849 41.654 34.293 1.00 23.19 3464 CA MET 369 102.845 42.716 35.295 1.00 20.55 3465 C MET 369 101.410 43.060 35.657 1.00 20.66 3466 O MET 369 101.085 43.248 36.833 1.00 24.28 3467 CB MET 369 103.565 43.966 34.789 1.00 24.43 3468 CG MET 369 103.575 45.097 35.806 1.00 27.10 3469 SD MET 369 104.503 46.538 35.283 1.00 33.91 3470 CE MET 369 105.378 46.942 36.804 1.00 36.11 3471 H MET 369 103.151 41.852 33.380 1.00 25.00 3472 N LYS 370 100.550 43.142 34.645 1.00 27.52 3473 CA LYS 370 99.135 43.441 34.865 1.00 27.03 3474 C LYS 370 98.572 42.392 35.817 1.00 26.80 3475 O LYS 370 97.854 42.720 36.766 1.00 31.01 3476 CB 370 98.361 43.415 33.545 1.00 28.62 3 3447777 C CGG LYS 370 98.699 44.546 32.591 1.00 26.77 3 3447788 C CDD LYS 370 97.881 44.437 31.318 1.00 32.86 3 3447799 C CEE LYS 370 98.174 45.591 30.371 1.00 40.98 3 3448800 N NZZ LYS 370 97.397 45.502 29.099 1.00 45.53 3 3448811 H H LYS 370 100.870 43.001 33.729 1.00 25.00 3 3448822 1 1HHZZ LYS 370 96.379 45.511 29.313 1.00 25.00 3 3448833 2 2HHZZ LYS 370 97.630 46.314 28.492 1.00 25.00 3 3448844 3 3HHZZ LYS 370 97.640 44.619 28.607 1.00 25.00 3 3448855 N N GLU 3771 98.959 41.139 35.581 1.00 26.63 3 3448866 C CAA GLU 371 98.541 40.006 36.398 1.00 23.18 3 3448877 C C GLU 371 98.981 40.191 37.854 1.00 31.56 3 3448888 0 0 GLU 371 98.180 40.023 38.782 1.00 33.30 3 3448899 C CBB GLU 371 99.125 38.719 35.815 1.00 24.88 3 3449900 C CGG GLU 371 98.779 37.449 36.569 1.00 25.01 3 3449911 C CDD GLU 371 99.346 36.212 35.892 1.00 38.13 3 3449922 O 0EE11 GLU 371 100.588 36.080 35.815 1.00 34.30 3 3449933 O 0EE22 GLU 371 98.549 35.373 35.425 1.00 44.97 3 3449944 H H GLU 371 99.542 40.972 34.811 1.00 25.00 3 3449955 N N VAL 372 100.243 40.567 38.056 1.00 29.02 3 3449966 C CAA VAL 372 100.765 40.789 39.406 1.00 26.07 3497 C VAL 372 99.952 41.869 40.126 1.00 28.22 3498 0 VAL 372 99.582 41.705 41.293 1.00 27.36 3 3449999 CCBB VAL 372 102.261 41.216 39.388 1.00 27.23 3 3550000 CCGG11 VAL 372 102.738 41.520 40.801 1.00 19.82 3501 CG2 VAL 372 103.124 40.119 38.770 1.00 23.40 3502 H VAL 372 100.836 40.688 37.283 1.00 25.00 3503 N VAL 373 99.657 42.964 39.426 1.00 31.06 3504 CA VAL 373 98.893 44.063 40.018 1.00 32.80 3505 C VAL 373 97.453 43.670 40.378 1.00 33.82 3506 0 VAL 373 96.952 44.054 41.441 1.00 30.74 3507 CB VAL 373 98.908 45.314 39.118 1.00 34.89 3508 CG1 VAL 373 98.134 46.454 39.775 1.00 32.71 3509 CG2 VAL 373 100.345 45.741 38.855 1.00 34.17 3510 H VAL 373 99.960 43.0288 38.495 1.00 25.00 3 3551111 N A ARRGG 374 96.794 42.900 39.512 1.00 31.81 3512 CA ARG 374 95.428 42.447 39.789 1.00 29.59 3513 C ARG 374 95.422 41.667 41.093 1.00 31.35 3514 O ARG 374 94.613 41.933 41.989 1.00 36.45 3515 CB ARG 374 94.910 41.519 38.689 1.00 29.25 3516 CG ARG 374 94.668 42.166 37.349 1.00 32.69 3517 CD ARG 374 94.034 41.169 36.396 1.00 33.05 3518 NE ARG 374 94.840 40.973 35.194 1.00 37.26 3519 CZ ARG 374 95.399 39.817 34.846 1.00 38.15 3520 NH1 ARG 374 95.247 38.741 35.608 1.00 41.80 3521 NH2 ARG 374 96.114 39.738 33.733 1.00 40.61 3522 H ARG 374 97.230 42.625 38.677 1.00 25.00 3523 HE ARG 374 94.974 41.744 34.603 1.00 25.00 3524 1HH1 ARG 374 94.711 38.795 36.448 1.00 25.00 3525 2HH1 ARG 374 95.672 37.878 35.336 1.00 25.00 3526 1HH2 ARG 374 96.232 40.550 33.158 1.00 25.00 3527 2HH2 ARG 374 96.537 38.873 33.467 1.00 25.00 3528 N ASN 375 96.351 40.721 41.202 1.00 31.47 3529 CA ASN 375 96.458 39.883 42.388 1.00 28.79 3530 C ASN 375 96.897 40.652 43.625 1.00 26.40 3531 0 ASN 375 96.561 40.266 44.746 1.00 27.83 3532 CB ASN 375 97.359 38.683 42.112 1.00 35.49 3533 CG ASN 375 96.744 37.720 41.111 1.00 32.04 3534 OD1 ASN 375 95.982 38.125 40.237 1.00 33.82 3535 ND2 ASN 375 97.075 36.442 41.231 1.00 34.73 3536 H ASN 375 96.970 40.566 40.454 1.00 25.00 3537 1 HD2 ASN 375 96.671 35.822 40.590 1.00 25.00 3538 2HD2 ASN 375 97.686 36.184 41.941 1.00 25.00 3539 N TYR 376 97.643 41.736 43.422 1.00 32.41 3540 CA TYR 376 98.075 42.599 44.526 1.00 36.00 3541 C TYR 376 96.803 43.220 45.101 1.00 36.51 3542 0 TYR 376 96.585 43.247 46.316 1.00 32.23 3543 CB TYR 376 98.960 43.739 44.010 1.00 34.19 3544 CG TYR 376 100.447 43.464 43.979 1.00 41.46 3545 CD1 TYR 376 100.993 42.339 44.601 1.00 40.12 3546 CD2 TYR 376 101.315 44.350 43.336 1.00 41.43 3547 CE1 TYR 376 102.365 42.104 44.580 1.00 38.75 3548 CE2 TYR 376 102.688 44.127 43.310 1.00 37.68 3549 CZ TYR 376 103.203 43.005 43.932 1.00 41.58 3550 OH TYR 376 104.560 42.785 43.895 1.00 43.07 3551 H TYR 376 97.915 41.956 42.506 1.00 25.00 3552 HH TYR 376 104.761 41.958 44.341 1.00 25.00 3553 N ASN 377 95.965 43.713 44.194 1.00 37.58 3554 CA ASN 377 94.704 44.343 44.550 1.00 36.82 3555 C ASN 377 93.807 43.352 45.285 1.00 35.16 3556 0 ASN 377 93.276 43.658 46.353 1.00 35.66 3557 CB ASN 377 94.011 44.846 43.287 1.00 38.60 3558 CG ASN 377 92.858 45.770 43.587 1.00 43.38 3559 0D1 ASN 377 92.949 46.628 44.462 1.00 38.97 3560 ND2 ASN 377 91.774 45.622 42.838 1.00 46.57 3561 H ASN 377 96.210 43.651 43.245 1.00 25.00 3562 1HD2 ASN 377 91.023 46.218 43.029 1.00 25.00 3563 2HD2 ASN 377 91.765 44.936 42.143 1.00 25.00 3564 N VAL 378 93.683 42.147 44.735 1.00 32.14 3565 CA VAL 378 92.857 41.106 45.344 1.00 28.96 3566 C VAL 378 93.339 40.801 46.766 1.00 33.76 3567 0 VAL 378 92.532 40.647 47.690 1.00 32.35 3568 CB VAL 378 92.858 39.818 44.490 1.00 30.20 3569 CG1 VAL 378 92.051 38.732 45.169 1.00 28.32 3570 CG2 VAL 378 92.285 40.104 43.105 1.00 26.65 3571 H VAL 378 94.153 41.951 43.897 1.00 25.00 3572 N GLU 379 94.657 40.741 46.940 1.00 36.35 3573 CA GLU 379 95.258 40.478 48.246 1.00 38.43 3574 C GLU 379 94.875 41.598 49.209 1.00 36.80 3575 0 GLU 379 94.579 41.352 50.383 1.00 37.49 3576 CB GLU 379 96.780 40.395 48.114 1.00 43.01 3577 CG GLU 379 97.544 40.416 49.436 1.00 52.96 3578 CD GLU 379 99.055 40.403 49.250 1.00 61.44 3579 0E1 GLU 379 99.526 40.225 48.107 1.00 70.64 3580 0E2 GLU 379 99.776 40.568 50.255 1.00 66.21 3581 H GLU 379 95.247 40.882 46.167 1.00 25.00 3582 N SER 380 94.894 42.827 48.700 1.00 37.49 3583 CA SER 380 94.531 44.003 49.480 1.00 38.42 3584 C SER 380 93.070 43.865 49.906 1.00 37.35 3585 0 SER 380 92.740 44.018 51.085 1.00 38.35 3586 CB SER 380 94.721 45.264 48.634 1.00 37.87 3587 OG SER 380 94.344 46.428 49.349 1.00 51.23 3588 H SER 380 95.167 42.951 47.767 1.00 25.00 3589 HG SER 380 94.903 46.518 50.127 1.00 25.00 3590 N THR 381 92.209 43.535 48.945 1.00 36.73 3591 CA THR 381 90.785 43.349 49.198 1.00 31.81 3592 C THR 381 90.574 42.286 50.278 1.00 33.52 3593 0 THR 381 89.846 42.514 51.245 1.00 35.95 3594 CB THR 381 90.043 42.922 47.912 1.00 27.90 3595 OG1 THR 381 90.230 43.914 46.894 1.00 30.65 3596 CG2 THR 381 88.564 42.762 48.174 1.00 30.75 3597 H THR 381 92.531 43.424 48.030 1.00 25.00 3598 HG1 THR 381 89.901 44.765 47.202 1.00 25.00 3599 N TRP 382 91.246 41.146 50.137 1.00 31.98 3600 CA TRP 382 91.124 40.059 51.106 1.00 34.10 3601 C TRP 382 91.498 40.511 52.513 1.00 37.61 3602 0 TRP 382 90.840 40.145 53.490 1.00 37.71 3603 CB TRP 382 92.001 38.870 50.701 1.00 29.03 3604 CG TRP 382 91.465 38.064 49.553 1.00 34.52 3605 CD1 TRP 382 90.298 38.272 48.872 1.00 32.13 3606 CD2 TRP 382 92.073 36.907 48.962 1.00 41.36 3607 NE1 TRP 382 90.141 37.315 47.897 1.00 33.27 3608 CE2 TRP 382 91.215 36.465 47.929 1.00 39.81 3609 CE3 TRP 382 93.262 36.198 49.205 1.00 42.10 3610 CZ2 TRP 382 91.507 35.344 47.138 1.00 41.24 3611 CZ3 TRP 382 93.552 35.082 48.417 1.00 37.35 3612 CH2 TRP 382 92.676 34.669 47.396 1.00 37.45 3613 H TRP 382 91.841 41.035 49.370 1.00 25.00 3614 HE1 TRP 382 89.384 37.250 47.275 1.00 25.00 3615 N PHE 383 92.551 41.317 52.601 1.00 42.79 3616 CA PHE 383 93.040 41.836 53.875 1.00 44.89 3617 C PHE 383 92.005 42.728 54.561 1.00 45.32 3618 0 PHE 383 91.714 42.557 55.748 1.00 44.05 3619 CB PHE 383 94.346 42.611 53.657 1.00 45.88 3620 CG PHE 383 94.818 43.358 54.869 1.00 46.79 3621 CD1 PHE 383 95.254 42.674 55.997 1.00 47.27 3622 CD2 PHE 383 94.800 44.751 54.893 1.00 50.35 3623 CE1 PHE 383 95.665 43.368 57.137 1.00 53.01 3624 CE2 PHHE 383 95.208 45.453 56.026 1.00 50.27 3625 CZ PHE 383 95.641 44.759 57.151 1.00 48.55 3626 H PHE 383 93.023 41.569 51.778 1.00 25.00 3627 N ILE 384 91.462 43.677 53.803 1.00 46.83 3628 CA ILE 384 90.458 44.610 54.306 1.00 46.17 3629 C ILE 384 89.185 43.894 54.774 1.00 47.27 3630 0 ILE 384 88.608 44.253 55.799 1.00 47.11 3631 CB ILE 384 90.091 45.646 53.227 1.00 41.64 3632 CG1 ILE 384 91.337 46.434 52.817 1.00 42.54 3633 CG2 ILE 384 89.031 46.597 53.750 1.00 46.00 3634 CD1 ILE 384 91.148 47.270 51.568 1.00 40.69 3635 H ILE 384 91.753 43.749 52.867 1.00 25.00 3636 N GLU 385 88.756 42.884 54.022 1.00 45.25 3637 CA GLU 385 87.554 42.123 54.360 1.00 43.73 3638 C GLU 385 87.791 41.137 55.495 1.00 46.22 3639 O GLU 385 86.842 40.636 56.097 1.00 51.43 3640 CB GLU 385 87.051 41.346 53.142 1.00 42.68 3641 CG GLU 385 86.657 42.211 51.956 1.00 46.85 3642 CD GLU 385 86.265 41.397 50.730 1.00 50.00 3643 OE1 GLU 385 86.535 40.175 50.696 1.00 44.05 3644 OE2 GLU 385 85.689 41.988 49.791 1.00 52.88 3645 H GLU 385 89.262 42.652 53.215 1.00 25.00 3646 N GLY 386 89.055 40.846 55.777 1.00 45.48 3647 CA GLY 386 89.371 39.893 56.824 1.00 41.52 3648 C GLY 386 89.038 38.499 56.328 1.00 42.60 3649 O GLY 386 88.656 37.625 57.104 1.00 44.94 3650 H GLY 386 89.784 41.273 55.279 1.00 25.00 3651 N TYR 387 89.190 38.297 55.023 1.00 42.34 3652 CA TYR 387 88.897 37.020 54.382 1.00 43.55 3653 C TYR 387 90.042 36.010 54.474 1.00 45.46 3654 O TYR 387 91.191 36.329 54.162 1.00 49.16 3655 CB TYR 387 88.545 37.254 52.908 1.00 38.26 3656 CG TYR 387 88.082 36.017 52.162 1.00 36.21 3657 CD1 TYR 387 87.152 35.142 52.727 1.00 36.57 3658 CD2 TYR 387 88.555 35.736 50.880 1.00 31.64 3659 CE1 TYR 387 86.704 34.015 52.035 1.00 32.07 3660 CE2 TYR 387 88.112 34.616 50.178 1.00 32.41 3661 CZ TYR 387 87.187 33.759 50.763 1.00 34.67 36662 OH TYR 387 86.749 32.646 50.082 1.00 38.16 3663 H TYR 387 89.541 39.025 54.474 1.00 25.00 3664 HH TYR 387 87.147 32.629 49.211 1.00 25.00 3665 N THR 388 89.706 34.787 54.872 1.00 45.36 3666 CA THR 388 90.671 33.692 54.986 1.00 43.34 3667 C THR 388 90.199 32.571 54.048 1.00 41.02 3668 O THR 388 89.474 31.660 54.459 1.00 45.75 3669 CB THR 388 90.748 33.161 56.444 1.00 42.74 3670 OG1 THR 388 91.169 34.220 57.314 1.00 43.28 3671 CG2 THR 388 91.741 32.008 56.561 1.00 39.83 3672 H THR 388 88.782 34.613 55.129 1.00 25.00 3673 HG1 THR 388 91.243 33.885 58.206 1.00 25.00 3674 N PRO 389 90.575 32.649 52.761 1.00 34.93 3675 CA PRO 389 90.184 31.645 51.769 1.00 34.82 3676 C PRO 389 90.846 30.293 51.974 1.00 39.00 3677 O PRO 389 91.864 30.185 52.658 1.00 44.20 3678 CB PRO 389 90.654 32.273 50.460 1.00 29.22 3679 CG PRO 389 91.878 33.003 50.869 1.00 31.21 3680 CD PRO 389 91.444 33.671 52.151 1.00 33.29 3681 N PRO 390 90.243 29.231 51.425 1.00 39.35 3682 CA PRO 390 90.830 27.896 51.566 1.00 38.80 3683 C PRO 390 92.130 27.894 50.744 1.00 42.47 3684 O PRO 390 92.264 28.683 49.801 1.00 41.59 3685 CB PRO 390 89.756 26.991 50.960 1.00 35.31 3686 CG PRO 390 89.094 27.876 49.944 1.00 39.05 3687 CD PRO 390 88.968 29.177 50.690 1.00 35.38 3688 N VAL 391 93.070 27.015 51.085 1.00 42.92 3689 CA VAL 391 94.367 26.947 50.396 1.00 40.91 3690 C VAL 391 94.310 27.035 48.869 1.00 40.48 3691 O VAL 391 95.026 27.832 48.266 1.00 37.26 3692 CB VAL 391 95.163 25.685 50.800 1.00 42.01 3693 CG1 VAL 391 96.542 25.698 50.149 1.00 37.12 3694 CG2 VAL 391 95.298 25.616 52.307 1.00 37.77 3695 H VAL 391 92.886 26.404 51.823 1.00 25.00 3696 N SER 392 93.455 26.228 48.251 1.00 37.92 3697 CA SER 392 93.316 26.223 46.799 1.00 36.67 3698 C SER 392 93.065 27.627 46.253 1.00 37.70 3699 O SER 392 93.699 28.056 45.289 1.00 39.57 3700 CB SER 392 92.167 25.301 46.399 1.00 41.29 3701 OG SER 392 91.008 25.599 47.163 1.00 53.55 3702 H SER 392 92.894 25.625 48.776 1.00 25.00 3703 HG SER 392 90.720 26.495 46.965 1.00 25.00 3704 N GLU 393 92.140 28.342 46.883 1.00 35.95 3705 CA GLU 393 91.806 29.692 46.455 1.00 34.88 3706 C GLU 393 92.951 30.643 46.783 1.00 31.14 3707 O GLU 393 93.293 31.516 45.984 1.00 29.96 3708 CB GLU 393 90.518 30.159 47.130 1.00 35.59 3709 CG GLU 393 89.956 31.447 46.559 1.00 35.57 3710 CD GLU 393 88.745 31.951 47.318 1.00 39.64 3711 OE1 GLU 393 88.064 31.141 47.985 1.00 40.88 3712 OE2 GLU 393 88.475 33.167 47.2242 1.00 40.96 3713 H GLU 393 91.694 27.967 47.669 1.00 25.00 3714 N TYR 394 93.539 30.476 47.962 1.00 32.04 3715 CA TYR 394 94.655 31.318 48.371 1.00 29.74 3716 C TYR 394 95.743 31.287 47.302 1.00 31.70 3717 O TYR 394 96.180 32.335 46.822 1.00 33.06 3718 CB TYR 394 95.238 30.844 49.706 1.00 33.01 3719 CG TYR 394 96.546 31.520 50.059 1.00 42.08 3720 CD1 TYR 394 96.585 32.876 50.392 1.00 45.51 3721 CD2 TYR 394 97.752 30.815 50.021 1.00 35.80 3722 CE1 TYR 394 97.791 33.517 50.675 1.00 45.10 3723 CE2 TYR 394 98.963 31.448 50.299 1.00 36.76 3724 CZ TYR 394 98.975 32.798 50.627 1.00 42.58 3725 OH TYR 394 100.164 33.430 50.915 1.00 41.43 3726 H TYR 394 93.225 29.778 48.567 1.00 25.00 3727 HH TYR 394 99.991 34.360 51.082 1.00 25.00 3728 N LEU 395 96.145 30.082 46.909 1.00 28.83 3729 CA LEU 395 97.189 29.897 45.910 1.00 26.16 3730 C LEU 395 96.865 30.472 44.541 1.00 29.12 3731 O LEU 395 97.737 31.063 43.901 1.00 28.83 3732 CB LEU 395 97.550 28.415 45.770 1.00 28.06 3733 CG LEU 395 98.263 27.754 46.951 1.00 27.93 3734 CD1 LEU 395 98.511 26.290 46.636 1.00 28.97 3735 CD2 LEU 395 99.575 28.475 47.245 1.00 24.02 3736 H LEU 395 95.720 29.293 47.301 1.00 25.00 3737 N SER 396 95.620 30.324 44.093 1.00 29.97 3738 CA SER 396 95.239 30.836 42.780 1.00 32.88 3739 C SER 396 95.535 32.329 42.624 1.00 28.77 3740 0 SER 396 95.715 32.818 41.508 1.00 27.80 3741 CB SER 396 93.770 30.518 42.465 1.00 39.24 3742 OG SER 396 92.896 30.992 43.472 1.00 46.99 3743 H SER 396 94.943 29.866 44.642 1.00 25.00 3744 HG SER 396 92.971 31.948 43.546 1.00 25.00 3745 N ASN 397 95.597 33.046 43.745 1.00 25.18 3746 CA ASN 397 95.907 34.472 43.723 1.00 29.15 3747 C ASN 397 97.333 34.739 44.226 1.00 27.87 3748 0 ASN 397 98.106 35.459 43.588 1.00 28.50 3749 CB ASN 397 94.909 35.264 44.577 1.00 29.41 3750 CG ASN 397 95.146 36.770 44.505 1.00 35.89 3751 OD1 ASN 397 94.831 37.404 43.502 1.00 37.46 3752 ND2 ASN 397 95.715 37.343 45.564 1.00 30.17 3753 H ASN 397 95.421 32.602 44.603 1.00 25.00 3754 1 HD2 ASN 397 95.872 38.310 45.510 1.00 25.00 3755 2HD2 ASN 397 95.953 36.794 46.336 1.00 25.00 3756 N ALA 398 97.682 34.123 45.351 1.00 26.89 3757 CA A ALLAA 398 98.986 34.300 45.980 1.00 24.87 3758 C AALLAA 398 100.205 33.854 45.178 1.00 28.89 3759 0 AALLAA 398 101.303 34.358 45.395 1.00 31.67 3760 CB AALLAA 398 98.992 33.646 47.337 1.00 24.15 3761 H AALLAA 398 97.035 33.533 45.770 1.00 25.00 3762 N LLEEUU 399 100.039 32.910 44.262 1.00 27.33 3763 CA LLEEUU 399 101.181 32.464 43.474 1.00 29.45 3764 C LLEEUU 399 101.755 33.589 42.617 1.00 32.27 3765 0 LLEEUU 399 102.967 33.807 42.603 1.00 34.30 3766 CB LLEEUU 399 100.823 31.254 42.611 1.00 25.44 3767 CG LLEEUU 399 100.621 29.949 43.390 1.00 24.86 3768 CD1 LLEEUU 399 100.172 28.853 42.451 1.00 20.68 3769 CD2 LLEEUU 399 101.900 29.549 44.104 1.00 22.68 3770 H LLEEUU 399 99.159 32.500 44.121 1.00 25.00 3771 N AALLAA 400 100.887 34.336 41.943 1.00 29.07 3772 CA AALLAA 400 101.343 35.434 41.094 1.00 31.03 3773 C AALLAA 400 101.939 36.601 41.882 1.00 29.34 3 3777744 0 0 AALLAA 400 102.813 37.303 41.373 1.00 26.86 3775 CB ALA 400 100.215 35.925 40.192 1.00 32..40 3776 H ALA 400 99.932 34.143 42.022 1.00 25.00 3777 N THR 401 101.500 36.796 43.125 1.00 27.66 3778 CA THR 401 102.024 37.896 43.929 1.00 30.92 3779 C THR 401 103.505 37.728 44.303 1.00 35.35 3780 0 THR 401 104.118 38.649 44.847 1.00 36.05 3781 CB THR 401 101.170 38.174 45.194 1.00 27.88 3782 OG1 THR 401 101.106 37.007 46.021 1.00 27.11 3783 CG2 THR 401 99.768 38.593 44.803 1.00 25.60 3784 H THR 401 100.837 36.193 43.521 1.00 25.00 3785 HG1 THR 401 101.990 36.769 46.324 1.00 25.00 3786 N THR 402 104.076 36.558 44.016 1.00 30.98 3787 CA THR 402 105.492 36.310 44.295 1.00 28.76 3788 C THR 402 106.317 37.040 43.240 1.00 28.41 3789 0 THR 402 107.509 37.248 43.422 1.00 30.86 3790 CB THR 402 105.861 34.807 44.173 1.00 24.70 3791 OG1 THR 402 105.656 34.372 42.820 1.00 22.39 3792 CG2 THR 402 105.039 33.954 45.117 1.00 21.26 3793 H THR 402 103.554 35.829 43.612 1.00 25.00 3794 HG1 THR 402 105.851 33.431 42.770 1.00 25.00 3795 N THR 403 105.656 37.373 42.130 1.00 28.49 3796 CA THR 403 106.207 38.045 40.946 1.00 25.51 3797 C THR 403 107.032 37.101 40.077 1.00 27.25 3798 0 THR 403 107.499 37.495 39.009 1.00 29.50 3799 CB THR 403 107.060 39.323 41.246 1.00 29.54 3800 0G1 THR 403 108.335 38.954 41.781 1.00 24.64 3801 CG2 THR 403 106.339 40.267 42.203 1.00 26.87 3802 H THR 403 104.707 37.143 42.086 1.00 25.00 3803 HG1 THR 403 108.246 38.543 42.630 1.00 25.00 3804 N TYR 404 107.120 35.833 40.474 1.00 25.89 3805 CA TYR 404 107.914 34.860 39.728 1.00 22.27 3806 C TYR 404 107.544 34.611 38.272 1.00 24.30 3807 0 TYR 404 108.439 34.511 37.434 1.00 26.21 3808 CB TYR 404 108.062 33.551 40.509 1.00 30.29 3809 CG TYR 404 109.278 33.544 41.419 1.00 30.18 3810 CD1 TYR 404 109.800 34.736 41.922 1.00 31.88 3811 CD2 TYR 404 109.925 32.352 41.755 1.00 28.35 3812 CE1 TYR 404 110.937 34.747 42.732 1.00 30.99 3813 CE2 TYR 404 111.065 32.353 42.569 1.00 29.01 3814 CZ TYR 404 111.563 33.558 43.051 1.00 29.70 3815 OH TYR 404 112.683 33.593 43.847 1.00 27.42 3816 H TYR 404 106.644 35.551 41.285 1.00 25.00 3817 HH TYR 404 113.022 32.697 43.955 1.00 25.00 3818 N TYR 405 106.253 34.508 37.952 1.00 24.23 3819 CA TYR 405 105.844 34.306 36.553 1.00 24.60 3820 C TYR 405 106.361 35.507 35.766 1.00 23.35 3821 0 TYR 405 106.912 35.378 34.672 1.00 23.93 3822 CB TYR 405 104.317 34.292 36.406 1.00 25.23 3823 CG TYR 405 103.593 33.163 37.099 1.00 24.35 3824 CD1 TYR 405 103.561 31.879 36.548 1.00 23.45 3825 CD2 TYR 405 102.894 33.390 38.282 1.00 23.55 3826 CE1 TYR 4005 102.846 30.852 37.161 1.00 23.28 3827 CE2 TYR 405 102.179 32.374 38.901 1.00 27.86 3828 CZ TYR 405 102.155 31.111 38.337 1.00 26.80 3829 OH TYR 405 101.428 30.121 38.956 1.00 26.06 3830 H TYR 405 105.577 34.557 38.658 1.00 25.00 3831 HH TYR 405 101.510 29.308 38.452 1.00 25.00 3832 N TYR 406 106.160 36.676 36.363 1.00 23.37 3833 CA TYR 406 106.553 37.964 35.813 1.00 21.93 3834 C TYR 406 108.072 38.084 35.621 1.00 25.55 3835 0 TYR 406 108.535 38.439 34.538 1.00 24.19 3836 CB TYR 406 106.021 39.047 36.751 1.00 22.96 3837 CG TYR 406 106.379 40.468 36.408 1.00 21.90 3838 CD1 TYR 406 106.352 40.926 35.093 1.00 20.58 3839 CD2 TYR 406 106.703 41.375 37.416 1.00 27.70 3840 CE1 TYR 406 106.634 42.252 34.796 1.00 21.17 3841 CE2 TYR 406 106.985 42.700 37.128 1.00 24.51 3842 CZ TYR 406 106.947 43.131 35.820 1.00 23.02 3843 OH TYR 406 107.207 44.449 35.541 1.00 28.99 3844 H TYR 406 105.729 36.670 37.238 1.00 25.00 3845 HH TYR 406 107.398 44.923 36.351 1.00 25.00 3846 N LEU 407 108.844 37.750 36.652 1.00 25.38 3847 CA LEU 407 110.303 37.826 36.574 1.00 23.31 3848 C LEU 407 110.873 36.825 35.575 1.00 20.18 3849 0 LEU 407 111.803 37.147 34.836 1.00 22.15 3850 CB LEU 407 110.940 37.620 37.952 1.00 20.82 3851 CG LEU 407 110.514 38.602 39.048 1.00 25.79 3852 CD1 LEU 407 111.362 38.376 40.287 1.00 24.12 3853 CD2 LEU 407 110.636 40.045 38.562 1.00 15.72 3854 H LEU 407 108.434 37.445 37.475 1.00 25.00 3855 N ALA 408 110.299 35.625 35.539 1.00 14.35 3856 CA ALA 408 110.747 34.591 34.609 1.00 17.38 3857 C ALA 408 110.520 35.083 33.183 1.00 22.75 3858 0 ALA 408 111.382 34.931 32.318 1.00 25.21 3859 CB ALA 408 109.991 33.293 34.852 1.00 17.26 3860 H ALA 408 109.560 35.429 36.149 1.00 25.00 3861 N THR 409 109.362 35.695 32.949 1.00 23.86 3862 CA THR 409 109.037 36.228 31.632 1.00 22.93 3863 c THR 409 110.012 37.353 31.294 1.00 25.61 3864 o THR 409 110.507 37.443 30.165 1.00 26.75 3865 CB THR 409 107.598 36.776 31.589 1.00 26.26 3866 OG1 THR 409 106.689 35.765 32.042 1.00 26.48 3867 CG2 THR 409 107.222 37.170 30.173 1.00 18.58 3868 H THR 409 108.709 35.780 33.672 1.00 25.00 3869 HG1 THR 409 106.917 35.516 32.932 1.00 25.00 3870 N THR 410 110.316 38.185 32.287 1.00 26.70 3871 CA THR 410 111.233 39.299 32.095 1.00 26.67 3872 C THR 410 112.650 38.835 31.757 1.00 29.09 3873 O THR 410 113.298 39.411 30.877 1.00 29.16 3874 CB THR 410 111.281 40.208 33.333 1.00 28.30 3875 OG1 THR 410 109.962 40.684 33.626 1.00 30.05 3876 CG2 THR 410 112.189 41.404 33.082 1.00 28.81 3877 H THR 410 109.905 38.064 33.169 1.00 25.00 3878 HG1 THR 410 109.991 41.259 34.393 1.00 25.00 3879 N SER 411 113.105 37.760 32.399 1.00 24.71 3880 CA SER 411 114.452 37.254 32.155 1.00 24.18 3881 C SER 411 114.688 36.909 30.687 1.00 25.08 3882 O SER 411 115.822 36.964 30.204 1.00 27.75 3883 CB SER 411 114.753 36.046 33.043 1.00 20.40 3884 OG SER 411 114.010 34.914 32.644 1.00 21.48 3885 H SER 411 112.534 37.287 33.041 1.00 25.00 3886 HG SER 411 114.205 34.667 31.738 1.00 25.00 3887 N TYR 412 113.613 36.573 29.979 1.00 23.79 3888 CA TYR 412 113.692 36.227 28.562 1.00 24.39 3889 C TYR 412 113.8774 37.44 27.655 1.00 25.24 3890 O TYR 412 114.437 37.326 26.570 1.00 27.76 3891 CB TYR 412 112.419 35.511 28.116 1.00 25.37 3892 CG T TYYRR 412 112.273 34.072 28.539 1.00 29.38 3893 CD1 T TYYRR 412 113.043 33.531 29.569 1.00 29.32 3894 CD2 TYR 412 111.338 33.248 27.910 1.00 24.28 3895 CE1 TYR 412 112.878 32.199 29.964 1.00 26.36 3896 CE2 T TYYRR 412 111.169 31.927 28.291 1.00 25.08 3897 CZ TTYYRR 412 111.937 31.408 29.318 1.00 29.45 3898 OH TTYYRR 412 111.750 30.099 29.693 1.00 27.61 3899 H TTYYRR 412 112.738 36.552 30.423 1.00 25.00 3900 HH TTYYRR 412 112.347 29.879 30.418 1.00 25.00 3901 N LLEEUU 413 113.396 38.604 28.100 1.00 25.11 3902 CA LLEEUU 413 113.467 39.832 27.304 1.00 27.32 3903 C LLEEUU 413 114.835 40.149 26.726 1.00 30.49 3904 0 LLEEUU 413 114.957 40.434 25.533 1.00 30.50 3905 CB LLEEUU 413 112.959 41.039 28.103 1.00 23.58 3906 CG LLEEUU 413 111.476 41.081 28.478 1.00 31.45 3907 CD1 LLEEUU 413 111.179 42.362 29.242 1.00 31.49 3908 CD2 LEU 413 110.613 40.996 27.231 1.00 30.34 3909 H LEU 413 112.980 38.636 28.989 1.00 25.00 3910 N G GLLYY 414 115.859 40.098 27.573 1.00 28.96 3911 CA G GLLYY 414 117.203 40.404 27.129 1.00 27.47 3 3991122 C C G GLLYY 414 117.990 39.233 26.586 1.00 28.88 3 3991133 0 0 G GLLYY 414 119.186 39.362 26.340 1.00 34.59 3914 H GLY 414 115.698 39.833 28.496 1.00 25.00 3915 N MET 415 117.353 38.079 26.436 1.00 29.79 3916 CA MET 415 118.043 36.909 25.906 1.00 29.75 3917 C MET 415 117.861 36.868 24.393 1.00 35.70 3918 0 MET 415 116.795 36.522 23.893 1.00 39.21 3919 CB MET 415 117.515 35.630 26.554 1.00 22.67 3920 CG MET 415 117.728 35.581 28.050 1.00 23.60 3921 SD MET 415 117.062 34.095 28.794 1.00 32.91 3922 CE MET 415 118.255 32.896 28.242 1.00 24.83 3923 H MET 415 116.398 38.012 26.652 1.00 25.00 3924 N LYS 416 118.933 37.181 23.677 1.00 40.25 3925 CA LYS 416 118.942 37.233 22.218 1.00 43.20 3926 C LYS 416 118.370 36.031 21.466 1.00 42.08 3927 0 LYS 416 118.037 36.143 20.289 1.00 44.24 3928 CB LYS 416 120.362 37.539 21.735 1.00 48.69 3929 CG LYS 416 120.916 38.828 22.333 1.00 60.37 3930 CD LYS 416 122.427 38.949 22.191 1.00 70.42 3931 CE LYS 416 122.936 40.173 22.949 1.00 72.06 3932 NZ LYS 416 124.412 40.319 22.863 1.00 78.00 3933 H LYS 416 119.749 37.416 24.164 1.00 25.00 3934 1HZ LYS 416 124.870 39.475 23.262 1.00 25.00 3935 2HZ LYS 416 124.687 40.423 21.865 1.00 25.00 3936 3HZ LYS 416 124.709 41.163 23.393 1.00 25.00 3937 N SER 417 118.239 34.893 22.138 1.00 39.46 3938 CA SER 417 117.706 33.698 21.491 1.00 36.96 3939 C SER 417 116.247 33.395 21.833 1.00 34.08 3940 0 SER 417 115.637 32.518 21.226 1.00 35.80 3941 CB SER 417 118.580 32.488 21.823 1.00 39.51 3942 OG SER 417 119.907 32.675 21.358 1.00 45.86 3943 H SER 417 118.485 34.856 23.077 1.00 25.00 3944 HG SER 417 120.288 33.461 21.743 1.00 25.00 3945 N ALA 418 115.688 34.106 22.806 1.00 30.28 3946 CA ALA 418 114.303 33.879 23.208 1.00 38.39 3947 C ALA 418 113.331 34.250 22.087 1.00 40.58 3948 0 ALA 418 113.145 35.427 21.779 1.00 42.57 3949 CB ALA 418 113.981 34.659 24.484 1.00 32.32 3950 H ALA 418 116.190 34.823 23.238 1.00 25.00 3951 N THR 419 112.750 33.232 21.457 1.00 41.43 3952 CA THR 419 111.799 33.420 220.362 1.00 41.21 3953 C THR 419 110.357 33.504 20.865 1.00 40.11 3954 0 THR 419 110.077 33.235 22.036 1.00 39.88 3955 CB THR 419 111.892 32.264 19.338 1.00 39.89 3956 OG1 THR 419 111.666 31.016 20.005 1.00 50.18 3957 CG2 THR 419 113.261 32.238 18.672 1.00 37.82 3958 H THR 419 112.987 32.335 21.728 1.00 25.00 3959 HG1 THR 419 112.370 30.881 20.644 1.00 25.00 3960 N GLU 420 109.443 33.848 19.963 1.00 39.64 3961 CA GLU 420 108.027 33.958 20.292 1.00 39.75 3962 C GLU 420 107.496 32.650 20.871 1.00 35.49 3963 0 GLU 420 106.718 32.652 21.828 1.00 35.76 3964 CB GLU 420 107.222 34.321 19.041 1.00 46.65 3965 CG GLU 420 106.741 35.765 18.980 1.00 56.30 3966 CD GLU 420 105.668 36.081 20.015 1.00 65.12 3967 OE1 GLU 420 104.685 35.311 20.130 1.00 62.03 3968 OE2 GLU 420 105.804 37.112 20.707 1.00 72.02 3969 H GLU 420 109.732 34.021 19.047 1.00 25.00 3970 N GLN 421 107.938 31.537 20.291 1.00 32.71 3971 CA GLN 421 107.520 30.206 20.722 1.00 36.14 3972 C GLN 421 107.883 29.959 22.184 1.00 36.63 3973 0 GLN 421 107.105 29.365 22.936 1.00 37.57 3974 CB GLN 421 108.155 29.133 19.830 1.00 40.03 3975 CG GLN 421 107.622 29.086 18.398 1.00 53.07 3976 CD GLN 421 107.819 30.390 17.636 1.00 62.17 3977 OE1 GLN 421 108.877 31.017 17.711 1.00 65.66 3978 NE2 GLN 421 106.788 30.815 16.917 1.00 68.97 3979 H GLN 421 108.580 31.620 19.555 1.00 25.00 3980 1HE2 GLN 421 106.906 31.650 16.419 1.00 25.00 3981 2HE2 GLN 421 105.963 30.289 16.903 1.00 25.00 3982 N ASP 422 109.052 30.448 22.589 1.00 34.98 3983 CA ASP 422 109.521 30.292 23.960 1.00 32.53 3984 C ASP 422 108.607 31.039 24.924 1.00 30.54 3985 0 ASP 422 108.272 30.525 25.992 1.00 33.81 3986 CB ASP 422 110.972 30.767 24.085 1.00 28.20 3987 CG ASP 422 111.929 29.945 23.233 1.00 28.18 3988 OD1 ASP 422 111.755 28.710 23.148 1.00 33.24 3989 OD2 ASP 422 112.855 30.529 22.638 1.00 33.81 3990 H ASP 422 109.610 30.933 21.946 1.00 25.00 3991 N PHE 423 108.166 32.229 24.523 1.00 29.33 3992 CA PHE 423 107.261 33.022 25.348 1.00 28.15 3993 C PHE 423 105.877 32.373 25.407 1.00 29.51 3994 0 PHE 423 105.205 32.424 26.441 1.00 30.32 3995 CB PHE 423 107.143 34.448 24.808 1.00 31.32 3996 CG PHE 423 108.275 35.353 25.214 1.00 27.99 3997 CD1 PHE 423 108.227 36.045 26.421 1.00 26.74 3998 CD2 PHE 423 109.375 35.529 24.387 1.00 26.53 3999 CE1 PHE 423 109.255 36.900 26.794 1.00 21.72 4000 CE2 PHE 423 1 10.412 36.385 24.753 1.00 23.04 4001 CZ PHE 423 110.350 37.070 25.958 1.00 23.46 4002 H PHE 423 108.456 32.575 23.652 1.00 25.00 40003 N GLU 424 105.450 31.771 24.297 1.00 30.80 4004 CA GLU 424 104.146 31.107 24.233 1.00 36.62 4005 C GLU 424 104.128 29.911 25.172 1.00 34.48 4006 O GLU 424 103.131 29.651 25.843 1.00 34.44 4007 CB GLU 424 103.823 30.661 22.805 1.00 42.57 4008 CG GLU 424 103.590 31.813 21.839 1.00 63.38 4009 CD GLU 424 103.322 31.357 20.414 1.00 70.12 4010 OE1 GLU 424 103.895 30.329 19.988 1.00 72.19 4011 OE2 GLU 424 102.543 32.039 19.715 1.00 79.30 4012 H GLU 424 106.023 31.773 23.503 1.00 25.00 4013 N TRP 425 105.242 29.187 25.221 1.00 32.02 4014 CA TRP 425 105.367 28.038 26.107 1.00 28.78 4015 C TRP 425 105.262 28.531 27.553 1.00 33.19 4016 O TRP 425 104.518 27.974 28.365 1.00 30.47 4017 CB TRP 425 106.719 27.352 25.881 1.00 29.01 4018 CG TRP 425 107.077 26.340 26.927 1.00 29.69 4019 CD1 TRP 425 106.621 25.058 27.019 1.00 28.88 4020 CD2 TRP 425 107.970 26.530 28.034 1.00 29.87 4021 NE1 TRP 425 107.171 24.437 28.116 1.00 29.58 4022 CE2 TRP 425 108.003 25.316 28.757 1.00 32.75 4023 CE3 TRP 425 108.742 27.609 28.488 1.00 30.70 4024 CZ2 TRP 425 108.781 25.149 29.912 1.00 27.26 4025 CZ3 TRP 425 109.514 27.444 29.638 1.00 26.04 4026 CH2 TRP 425 109.525 26.222 30.335 1.00 27.12 4027 H TRP 425 105.993 29.429 24.639 1.00 25.00 4028 HE1 TRP 425 106.983 23.517 28.395 1.00 25.00 4029 N LEU 426 105.974 29.615 27.848 1.00 31.46 4030 CA LEU 426 105.994 30.186 29.188 1.00 28.35 4031 C LEU 426 104.627 30.692 29.650 1.00 31.98 4032 O LEU 426 104.293 30.585 30.832 1.00 29.19 4033 CB LEU 426 107.039 31.302 29.268 1.00 21.80 4034 CG LEU 426 107.525 31.703 30.664 1.00 25.44 4035 CD1 LEU 426 108.240 30.535 31.331 1.00 20.60 4036 CD2 LEU 426 108.454 32.900 30.560 1.00 23.92 4037 H LEU 426 106.512 30.035 27.141 1.00 25.00 4038 N SER 427 103.824 31.208 28.720 1.00 33.95 4039 CA SER 427 102.497 31.722 29.066 1.00 33.39 4040 C SER 427 101.502 30.647 29.502 1.00 30.91 4041 O SER 427 100.515 30.951 30.170 1.00 31.38 4042 CB SER 427 101.917 32.568 27.925 1.00 37.83 4043 OG SER 427 101.970 31.892 26.683 1.00 46.06 4044 H SER 427 104.124 31.247 27.790 1.00 25.00 4045 HG SER 427 102.886 31.692 26.470 1.00 25.00 4046 N LYS 428 101.780 29.392 29.151 1.00 30.99 4047 CA LYS 428 100.914 28.271 29.518 1.00 30.38 4048 C LYS 428 101.124 27.817 30.964 1.00 33.22 4049 O LYS 428 100.505 26.845 31.410 1.00 34.36 4050 CB LYS 428 101.166 27.070 28.601 1.00 33.08 4051 CG LYS 428 100.690 27.213 27.166 1.00 40.80 4052 CD LYS 428 100.885 25.888 26.433 1.00 48.04 4053 CE LYS 428 100.314 25.910 25.002 1.00 54.20 4054 NZ LYS 428 100.438 24.571 24.377 1.00 59.29 4055 H LYS 428 102.587 29.209 28.628 1.00 25.00 4056 1 HZ LYS 428 99.919 23.866 24.937 1.00 25.00 4057 2HZ LYS 428 100.037 24.613 23.418 1.00 25.00 4058 3HZ LYS 428 101.440 24.300 24.323 1.00 25.00 4059 N ASN 429 101.992 28.518 31.693 1.00 36.19 4060 CA ASN 429 102.313 28.172 33.081 1.00 31.97 4061 C ASN 429 102.855 26.740 33.172 1.00 29.89 4062 O ASN 429 102.272 25.882 33.839 1.00 25.78 4063 CB ASN 429 101.092 28.334 33.995 1.00 32.22 4064 CG ASN 429 100.814 29.782 34.358 1.00 36.78 4065 OD1 ASN 429 101.488 30.699 33.894 1.00 40.44 4066 ND2 ASN 429 99.826 29.991 35.215 1.00 41.36 4067 H ASN 429 102.436 29.294 31.299 1.00 25.00 4068 1 HD2 ASN 429 99.643 30.918 35.449 1.00 25.00 4069 2HD2 ASN 429 99.331 29.226 35.566 1.00 25.00 4070 N PRO 430 103.997 26.472 32.508 1.00 29.30 4071 CA PRO 430 104.649 25.157 32.492 1.00 25.30 4072 C PRO 430 104.897 24.669 33.913 1.00 27.01 4073 O PRO 430 105.218 25.463 34.801 1.00 27.38 4074 CB PRO 430 105.975 25.447 31.799 1.00 24.23 4075 CG PRO 430 105.664 26.610 30.932 1.00 30.06 4076 CD PRO 430 104.835 27.468 31.820 1.00 30.25 4077 N LYS 431 104.824 23.358 34.108 1.00 25.65 4078 CA LYS 431 105.020 22.774 35.426 1.00 25.93 4079 C LYS 431 106.308 23.248 36.107 1.00 24.81 4080 O LYS 431 106.297 23.570 37.292 1.00 24.36 4081 CB LYS 431 105.000 21.252 35.325 1.00 26.70 4082 CG LYS 431 104.584 20.547 36.604 1.00 40.34 4083 CD LYS 431 104.361 19.068 36.330 1.00 52.65 4084 CE LYS 431 103.775 18.345 37.531 1.00 60.92 4085 NZ LYS 431 103.587 16.892 37.247 1.00 58.59 4086 H LYS 431 104.610 22.777 33.352 1.00 25.00 4087 1HZ LYS 431 102.939 16.775 36.442 1.00 25.00 4088 2HZ LYS 431 104.506 16.462 37.018 1.00 25.00 4089 3HZ LYS 431 103.189 16.424 38.086 1.00 25.00 4090 N ILE 432 107.401 23.338 35.353 1.00 25.03 4091 CA ILE 432 108.667 23.774 35.934 1.00 21.64 4092 C ILE 432 108.561 25.188 36.505 1.00 24.42 4093 O ILE 432 109.058 25.459 37.602 1.00 25.07 4094 CB ILE 432 109.847 23.646 34.928 1.00 22.09 4095 CG1 ILE 432 111.179 23.898 35.647 1.00 20.75 4096 CG2 ILE 432 109.662 24.587 33.739 1.00 20.53 4097 CD1 ILE 432 112.403 23.511 34.838 1.00 17.10 4098 H ILE 432 107.354 23.103 34.410 1.00 25.00 4099 N LEU 433 107.868 26.070 35.788 1.00 25.32 4100 CA LEU 433 107.674 27.448 36.240 1.0023.97 4101 C LEU 433 106.758 27.446 37.464 1.0027.11 4102 O LEU 433 107.051 28.078 38.483 1.0028.11 4103 CB LEU 433 107.057 28.298 35.126 1.0024.53 4104 CG LEU 433 106.721 29.754 35.473 1.0028.30 4105 CD1 LEU 433 107.968 30.488 35.945 1.0023.75 4106 CD2 LEU 433 106.108 30.456 34.265 1.0027.09 4107 H LEU 433 107.456 25.788 34.948 1.0025.00 4108 N GLU 434 105.667 26.698 37.360 1.0026.39 4109 CA GLU 434 104.690 26.566 38.429 1.0028.21 4110 C GLU 434 105.393 26.139 39.723 1.0025.73 4111 O GLU 434 105.159 26.711 40.790 1.0025.92 4112 CB GLU 434 103.656 25.510 38.027 1.0040.62 4113 CG GLU 434 102.371 25.510 38.835 1.0059.16 4114 CD GLU 434 101.447 26.650 38.457 1.0069.11 4115 OE1 GLU 434 101.135 26.803 37.255 1.0076.28 4116 OE2 GLU 434 101.026 27.391 39.366 1.0078..90 4117 H GLU 434 105.516 26.206 36.531 1.0025.00 4118 N ALA 435 106.272 25.147 39.614 1.0023.71 4119 CA ALA 435 107.015 24.632 40.764 1.0021.25 4120 C ALA 435 107.915 25.704 41.377 1.0021.57 4121 0 ALA 435 107.973 25.864 42.599 1.0021.94 4122 CB ALA 435 107.838 23.424 40.353 1.0017.11 4123 H ALA 435 106.427 24.748 38.737 1.0025.00 4124 N SER 436 108.603 26.448 40.519 1.0020.07 4125 CA SER 436 109.486 27.510 40.969 1.0021.72 4126 C SER 436 108.676 28.531 41.759 1.0023.51 4127 0 SER 436 109.095 28.979 42.832 1.0025.11 4128 CB SER 436 110.147 28.179 39.765 1.0021.38 4129 OG SER 436 111.040 29.196 40.173 1.0036.67 4130 H SER 436 108.521 26.272 39.556 1.0025.00 4131 HG SER 436 110.568 29.867 40.669 1.0025.00 4132 N VAL 437 107.501 28.876 41.235 1.0023.94 4133 CA VAL 437 106.622 29.846 41.880 1.0018.07 4134 Cc VAL 437 106.134 29.330 43.226 1.0019.00 4135 0o VAL 437 106.179 30.048 44.227 1.0024.40 4136 CB VAL 437 105.410 30.192 40.990 1.0022.63 4137 CG1 VAL 437 104.498 31.163 41.709 1.0024.13 4138 CG2 VAL 437 105.879 30.794 39.677 1.0013.85 4139 H VAL 437 107.218 28.463 40.391 1.0025.00 4140 N ILE 438 105.693 28.076 43.249 1.0022.97 4141 CA ILE 438 105.204 27.443 44.472 1.0025.17 4142 C ILE 438 106.279 27.478 45.566 1.0027.56 4143 O ILE 438 105.996 27.831 46.718 1.0025.37 4144 CB ILE 438 104.776 25.975 44.200 1.0028.36 4145 CG1 ILE 438 103.565 25.952 43.262 1.0033.63 4146 CG2 ILE 438 104.457 25.255 45.505 1.0031.72 4147 CD1 ILE 438 103.130 24.569 42.836 1.0033.54 4148 H ILE 438 105.697 27.559 42.417 1.0025.00 4149 N ILE 439 107.512 27.134 45.196 1.0027.24 4150 CA ILE 439 108.635 27.130 46.135 1.0024.88 4151 C ILE 439 108.769 28.502 46.787 1.0020.20 4152 0 ILE 439 108.842 28.610 48.007 1.00 20.39 4153 CB ILE 439 109.961 26.739 45.429 1.00 23.09 4154 CG1 ILE 439 109.915 25.264 45.023 1.00 21.73 4155 CG2 ILE 439 111.154 26.989 46.345 1.00 17.14 4156 CD1 ILE 439 110.984 24.859 44.043 1.00 22.40 4157 H ILE 439 107.670 26.870 44.265 1.00 25.00 4158 N CYS 440 108.763 29.552 45.974 1.00 21.23 4159 CA CYS 440 108.873 30.901 46.508 1.00 23.58 4160 C CYS 440 107.718 31.209 47.458 1.00 27.42 4161 0 CYS 440 107.933 31.707 48.563 1.00 29.41 4162 CB CYS 440 108.897 31.928 45.376 1.00 26.26 4163 SG CYS 440 109.015 33.625 45.934 1.00 17.39 4164 H CYS 440 108.685 29.406 45.006 1.00 25.00 4165 N ARG 441 106.502 30.869 47.038 1.00 30.12 4166 CA ARG 441 105.295 31.118 47.825 1.00 28.33 4167 C ARG 4441 105.280 30.448 49.197 1.00 28.78 4168 0 ARG 441 105.225 31.125 50.223 1.00 28.38 4169 CB ARG 441 104.056 30.693 47.031 1.00 26.28 4170 CG ARG 441 102.722 30.927 47.734 1.00 26.09 4171 CD ARG 441 102.312 32.391 47.725 1.00 32.68 4172 NE ARG 441 103.001 33.195 48.731 1.00 35.67 4173 CZ ARG 441 103.243 34.499 48.611 1.00 31.42 4174 NH1 ARG 441 102.861 35.159 47.526 1.00 25.83 4175 NH2 ARG 441 103.851 35.153 49.591 1.00 32.87 4176 H ARG 441 106.413 30.429 46.165 1.00 25.00 4177 HE ARG 441 103.307 32.748 49.547 1.00 25.00 4178 1HH1 ARG 441 102.391 34.678 46.792 1.00 25.00 4179 2HH1 ARG 441 103.043 36.138 47.443 1.00 25.00 4180 1HH2 ARG 441 104.133 34.668 50.417 1.00 25.00 4181 2HH2 ARG 441 104.032 36.133 49.498 1.00 25.00 4182 N VAL 442 105.329 29.120 49.220 1.00 28.03 4183 CA VAL 442 105.289 28.392 50.484 1.00 29.35 4184 C VAL 442 106.443 28.708 51.430 1.00 29.48 4185 O VAL 442 106.248 28.754 52.644 1.00 30.67 4186 CB VAL 442 105.171 26.864 50.272 1.00 28.34 4187 CG1 VAL 442 103.906 26.546 49.489 1.00 20.42 4188 CG2 VAL 442 106.394 26.322 49.562 1.00 28.17 4189 H VAL 442 105.405 28.625 48.376 1.00 25.00 4190 N ILE 443 107.635 28.941 50.885 1.00 32.67 4191 CA ILE 443 108.788 29.266 51.722 1.00 32.60 4192 C ILE 443 108.619 30.6722 52.283 1.00 34.90 4193 O ILE 443 108.866 30.908 53.469 1.00 33.18 4194 CB ILE 443 110.134 29.150 50.955 1.00 34.36 4195 CG1 ILE 443 110.394 27.689 50.574 1.00 27.67 4196 CG2 ILE 443 111.290 29.649 51.822 1.00 28.68 4197 CD1 ILE 443 110.456 26.745 51.765 1.00 31.24 4198 H ILE 443 107.746 28.891 49.910 1.00 25.00 4199 N ASP 444 108.170 31.599 51.441 1.00 33.84 4200 CA ASP 444 107.954 32.968 51.889 1.00 35.72 4201 C ASP 444 106.935 32.959 53.023 1.00 38.14 4202 O ASP 444 107.184 33.520 54.091 1.00 37.60 4203 CB ASP 444 107.450 33.848 50.744 1.00 39.61 4204 CG ASP 444 107.110 35.260 51.199 1.0048.15 4205 OD11 ASP 444 105.972 35.485 51.667 1.0051.59 4206 OD2 ASP 444 107.980 36.147 51.091 1.0051.59 4207 H ASP 444 107.985 31.364 50.507 1.0025.00 4208 N ASP 445 105.812 32.279 52.803 1.0040.33 4209 CA ASP 445 104.749 32.199 53.803 1.0039.63 4210 C ASP 445 105.221 31.599 55.124 1.0036.43 4211 0 ASP 445 104.826 32.060 56.195 1.0038.68 4212 CB ASP 445 103.549 31.415 53.259 1.0034.74 4213 CG ASP 445 102.867 32.115 52.087 1.0037.47 4214 OD1 ASP 445 103.173 33.301 51.818 1.0032.84 4215 OD2 ASP 445 102.022 31.474 51.429 1.0034.75 4216 H ASP 445 105.694 31.823 51.945 1.0025.00 4217 N T THHRR 446 106.061 30.574 55.047 1.0036.21 4218 CA TTHHRR 446 106.586 29.933 56.247 1.0034.20 4219 C TTHHRR 446 107.469 30.902 57.034 1.0034.56 4220 0 TTHHRR 446 107.396 30.968 58.259 1.0036.69 4221 CB TTHHRR 446 107.398 28.674 55.890 1.0029.80 4222 OG1 TTHHRR 446 106.545 27.735 55.227 1.0031.60 4223 CG2 TTHHRR 446 107.970 28.029 57.136 1.0031.33 4224 H TTHHRR 446 106.322 30.221 54.170 1.0025.00 4225 HG1 TTHHRR 446 107.041 26.946 54.992 1.0025.00 4226 N AALLAA 447 108.266 31.687 56.318 1.0039.84 4227 CA AALLAA 447 109.172 32.644 56.941 1.0042.07 4 4222288 C C AA ALLLAAA 447 108.495 33.902 57.483 1.0045.04 4 4222299 0 0 AA ALLLAAA 447 108.675 34.259 58.647 1.0048.71 4230 CB A ALLAA 447 110.2776 33.025 55.959 1.0036.91 4231 H A ALLAA 447 108.237 31.624 55.337 1.0025.00 4232 N T THHRR 448 107.708 34.565 56.644 1.0050.59 4233 CA T THHRR 448 107.036 35.799 57.039 1.0049.97 4234 C T THHRR 448 105.729 35.644 57.818 1.0051.43 4235 0 T THHRR 448 105.100 36.646 58.159 1.0056.61 4236 CB T THHRR 448 106.790 36.715 55.811 1.0047.11 4237 0G1 T THHRR 448 106.095 35.986 54.793 1.0050.09 4238 CG2 THR 448 108.106 37.214 55.245 1.0047.36 4239 H THR 448 107.555 34.230 55.741 1.0025.00 4240 HG1 T THHRR 448 105.951 36.556 54.034 1.0025.00 4241 N TTYYRR 449 105.352 34.415 58.157 1.0051.91 4242 CA TTYYRR 449 104.103 34.182 58.881 1.0053.63 4243 C TTYYRR 449 103.927 35.020 60.148 1.0058.13 4244 0 TTYYRR 449 102.939 35.745 60.282 1.0057.88 4245 CB TTYYRR 449 103.926 32.696 59.218 1.005075 4246 CG TTYYRR 449 102.674 32.406 60.025 1.0055.96 4247 CD1 TTYYRR 449 101.419 32.856 59.596 1.0060.14 4248 CD2 TYR 449 102.746 31.716 61.235 1.0056.00 4249 CE1 TYR 449 100.273 32.629 60.353 1.0055.79 4250 CE2 T TYYRR 449 101.605 31.483 62.000 1.0057.85 4251 CZ TTYYRR 449 100.375 31.943 61.554 1.0060.06 4252 OH TTYYRR 449 99.250 31.724 62.316 1.0061.67 4253 H TTYYRR 449 105.912 33.653 57.905 1.0025.00 4254 HH TTYYRR 449 98.487 32.104 61.878 1.0025.00 4255 N GGLLUU 450 104.883 34.927 61.067 1.0064.21 4256 CA GLU 450 104.810 35.662 62.329 1.00 67.19 4257 C GLU 450 104.604 37.167 62.173 1.00 68.02 4258 0 GLU 450 103.698 37.742 62.781 1.00 68.60 4259 CB GLU 450 106.053 35.386 63.178 1.00 73.69 4260 CG GLU 450 106.228 33.917 63.557 1.00 87.48 4261 CD GLU 450 104.988 33.311 64.211 1.00 95.20 4262 OE1 GLU 450 104.311 34.009 65.000 1.00100.27 4263 OE2 GLU 450 104.690 32.129 63.934 1.00 96.38 4264 H GLU 450 105.651 34.348 60.883 1.00 25.00 4265 N VAL 451 105.427 37.790 61.336 1.00 69.29 4266 CA VAL 451 105.351 39.228 61.091 1.00 69.79 4267 C VAL 451 104.011 39.634 60.479 1.00 71.86 4268 0 VAL 451 103.383 40.594 60.925 1.00 73.87 4269 CB VAL 451 106.482 39.692 60.149 1.00 68.77 4270 CG1 VAL 451 106.490 41.211 60.036 1.00 67.70 4271 CG2 VAL 451 107.825 39.180 60.647 1.00 74.55 4272 H VAL 451 106.100 37.263 60.866 1.00 25.00 4273 N GLU 452 103.572 38.893 59.467 1.00 73.34 4274 CA GLU 452 102.311 39.191 58.798 1.00 74.52 4275 C GLU 452 101.096 38.987 59.700 1.00 75.62 4276 0 GLU 452 100.107 39.715 59.575 1.00 75.03 4277 CB GLU 452 102.176 38.385 57.502 1.00 73.01 4278 CG GLU 452 103.194 38.774 56.427 1.00 77.67 4279 CD GLU 452 103.032 38.007 55.118 1.00 81.85 4280 OE1 GLU 452 102.537 36.858 55.137 1.00 80.20 4281 OE2 GLU 452 103.417 38.558 54.061 1.00 82.09 4282 H GLU 452 104.100 38.124 59.165 1.00 25.00 4283 N LYS 453 101.173 38.038 60.631 1.00 78.11 4284 CA LYS 453 100.050 37.799 61.536 1.00 81.43 4285 c LYS 453 99.887 38.943 62.532 1.00 84.49 4286 o LYS 453 98.768 39.393 62.783 1.00 88.82 4287 CB LYS 453 100.176 36.468 62.280 1.00 79.17 4288 CG LYS 453 98.907 36.134 63.054 1.00 78.09 4289 CD LYS 453 98.928 34.759 63.674 1.00 79.02 4290 CE LYS 453 97.583 34.462 64.319 1.00 81.56 4291 NZ LYS 453 97.525 33.093 64.899 1.00 87.65 4292 H LYS 453 101.981 37.486 60.701 1.00 25.00 4293 1HZ LYS 453 98.261 32.991 665.627 1.00 25.00 4294 2HZ LYS 453 96.590 32.937 65.327 1.00 25.00 4295 3HZ LYS 453 97.682 32.390 64.148 1.00 25.00 4296 N SER 454 100.996 39.424 63.088 1.00 84.86 4297 CA SER 454 100.943 40.535 64.037 1.00 83.61 4298 C SER 454 100.521 41.835 63.336 1.00 83.52 4299 O SER 454 100.210 42.830 63.991 1.00 82.37 4300 CB SER 454 102.286 40.703 64.755 1.00 81.64 4301 OG SER 454 103.363 40.771 63.838 1.00 82.19 4302 H SER 454 101.863 39.025 62.862 1.00 25.00 4303 HG SER 454 103.411 39.963 63.320 1.00 25.00 4304 N ARG 455 100.515 41.813 62.003 1.00 83.63 4305 CA ARG 455 100.102 42.961 61.197 1.00 86.97 4306 C ARRG 455 98.616 42.870 60.854 1.00 89.33 4307 O ARG 455 98.073 43.748 60.183 1.00 89.55 4308 CB ARG 455 100.892 43.025 59.891 1.00 86.51 4309 CG ARG 455 102.319 43.493 60.014 1.00 89.64 4310 CD ARG 455 102.926 43.581 58.632 1.00 98.07 4311 NE ARG 455 104.296 44.078 58.647 1.00109.66 4312 CZ ARG 455 104.976 44.415 57.555 1.00114.68 4313 NH1 ARG 455 104.411 44.309 56.357 1.00117.44 4314 NH2 ARG 455 106.220 44.863 57.659 1.00113.39 4315 H ARG 455 100.816 41.007 61.542 1.00 25.00 4316 HE ARG 455 104.745 44.172 59.512 1.00 25.00 4317 1 HH1 ARG 455 103.471 43.978 56.270 1.00 25.00 4318 2HH1 ARG 455 104.920 44.568 55.536 1.00 25.00 4319 1 HH2 ARG 455 106.646 44.949 58.558 1.00 25.00 4320 2HH2 ARG 455 105.724 45.120 56.834 1.00 25.00 4321 N GLY 456 97.980 41.773 61.259 1.00 90.67 4322 CA GLY 456 96.566 41.584 60.989 1.00 90.27 4323 C GLY 456 96.256 40.876 59.681 1.00 91.84 4324 O GLY 456 95.087 40.636 59.371 1.00 90.99 4325 H GLY 456 98.464 41.081 61.752 1.00 25.00 4326 N GLN 457 97.290 40.528 58.917 1.00 92.16 4327 CA GLN 457 97.107 39.842 57.638 1.00 90.85 4328 C GLN 457 96.662 38.395 57.846 1.00 89.74 4329 O GLN 457 97.442 37.462 57.659 1.00 92.66 4330 CB GLN 457 98.402 39.868 56.817 1.00 89.90 4331 CG GLN 457 98.905 41.257 56.457 1.00 95.19 4332 CD GLN 457 100.145 41.221 55.576 1.00 99.21 4333 OE1 GLN 457 100.325 40.303 54.775 1.00102.27 4334 NE2 GLN 457 101.002 42.225 55.718 1.00 97.71 4335 H GLN 457 98.199 40.716 59.228 1.00 25.00 4336 1 HE2 GLN 457 101.798 42.200 55.151 1.00 25.00 4337 2HE2 GLN 457 100.809 42.931 56.364 1.00 25.00 4338 N ILE 458 95.397 38.207 58.209 1.00 88.19 4339 CA ILE 458 94.859 36.867 58.439 1.00 82.29 4340 C ILE 458 94.715 36.043 57.159 1.00 75.34 4341 O ILE 458 94.305 34.887 57.205 1.00 73.69 4342 CB ILE 458 93.510 36.907 59.199 1.00 85.78 4343 CG1 ILE 458 92.566 37.933 58.562 1.00 86.17 43444 CG2 ILE 458 93.751 37.191 60.681 1.00 85.33 4345 CD1 ILE 458 91.240 38.069 59.277 1.00 89.41 4346 H ILE 458 94.823 38.995 58.338 1.00 25.00 4347 N ALA 459 95.077 36.632 56.025 1.00 68.80 4348 CA ALA 459 95.007 35.936 54.747 1.00 62.63 4349 C ALA 459 96.368 35.324 54.389 1.00 62.33 4350 O ALA 459 96.664 35.093 53.216 1.00 62.33 4351 CB ALA 459 94.549 36.893 53.653 1.00 62.28 4352 H ALA 459 95.387 37.554 56.036 1.00 25.00 4353 N THR 460 97.210 35.097 55.396 1.00 59.27 4354 CA THR 460 98.531 34.513 55.170 1.00 57.11 4355 C THR 460 98.424 33.034 54.826 1.00 53.62 4356 O THR 460 97.587 32.319 55.383 1.00 53.81 4357 CB THR 460 99.453 34.671 56.400 1.00 58.87 4358 OG1 THR 460 98.763 34.257 57.588 1.00 56.81 4359 CG2 THR 460 99.901 36.100 56.541 1.00 60.73 4360 H THR 460 96.933 35.314 56.305 1.0025.00 4361 HG1 THR 460 98.004 34.838 57.727 1.0025.00 4362 N GLY 461 99.298 32.574 53.937 1.0044.28 4363 CA GLY 461 99.289 31.184 53.526 1.0037.76 4364 C GLY 461 99.138 30.186 54.652 1.0039.21 4365 O GLY 461 98.265 29.318 54.599 1.0037.71 4366 H GLY 461 99.947 33.183 53.532 1.0025.00 4367 N ILE 462 99.965 30.320 55.684 1.0041.07 4368 CA ILE 462 99.915 29.405 56.821 1.0043.03 4369 C ILE 462 98.567 29.461 57.539 1.0043.30 4370 0 ILE 462 98.063 28.430 57.991 1.0044.23 4371 CB ILE 462 101.079 29.658 57.814 1.0035.94 4372 CG1 ILE 462 102.418 29.419 57.116 1.0034.23 4373 CG2 ILE 462 100.979 28.720 59.011 1.0026.77 4374 CD1 ILE 462 102.625 27.987 56.675 1.0031.75 4375 H ILE 462 100.618 31.046 55.680 1.0025.00 4376 N GLU 463 97.972 30.652 57.602 1.0047.45 4377 CA GLU 463 96.673 30.842 58.253 1.0048.26 4378 C GLU 463 95.600 30.064 57.495 1.0043.95 4379 O GLU 463 94.876 29.250 58.077 1.0045.29 4380 CB GLU 463 96.307 32.329 58.291 1.0055.50 4381 CG GLU 463 95.120 32.664 59.182 1.0060.77 4382 CD GLU 463 95.448 32.555 60.656 1.0066.36 4383 OE1 GLU 463 96.195 33.419 61.166 1.0070.77 4384 OE2 GLU 463 94.957 31.605 61.303 1.0066.97 4385 H GLU 463 98.403 31.430 57.193 1.0025.00 4386 N CYS 464 95.534 30.295 56.186 1.0038.49 4387 CA CYS 464 94.575 29.616 55.322 1.0040.30 4388 C CYS 464 94.751 28.H3 55.451 1.0040.72 4389 O CYS 464 93.778 27.364 55.550 1.0043.89 4390 CB CYS 464 94.798 30.010 53.860 1.0033.19 4391 SG CYS 464 94.721 31.780 53.533 1.0041.13 4392 H CYS 464 96.143 30.954 55.789 1.0025.00 4393 N CYS 465 96.007 27.682 55.464 1.0042.83 4394 CA CYS 465 96.337 26.271 55.557 1.0045.44 4395 C CYS 465 95.791 25.654 56.852 1.0048.27 4396 O CYS 465 95.165 24.591 56.818 1.0047.36 4397 CB CYS 465 97.850 26.074 55.487 1.0039.55 4398 SG CYS 465 98.332 24.350 55.349 1.0040.18 4399 H CYS 465 96.735 28.334 55.396 1.0025.00 4400 N MET 466 96.000 26.340 57.972 1.0051.35 4401 CA MET 466 95.531 25.854 59.267 1.0055.36 4402 C MET 466 94.019 25.699 59.312 1.0056.30 4403 O MET 466 93.512 24.647 59.698 1.0055.90 4404 CB MET 466 95.977 26.786 60.391 1.0052.93 4405 CG MET 466 97.464 26.797 60.618 1.0049.91 4406 SD MET 466 97.890 27.866 61.980 1.0056.57 4407 CE MET 466 97.679 29.434 61.228 1.0045.63 4408 H MET 466 96.483 27.193 57.936 1.0025.00 4409 N ARG 467 93.303 26.744 58.916 1.0057.72 4410 CA ARG 467 91.849 26.704 58.921 1.0060.99 4411 C ARG 467 91.271 25.700 57.935 1.0057.48 4412 0 ARG 467 90.406 24.901 58.295 1.00 61.64 4413 CB ARG 467 91.270 28.089 58.642 1.00 69.59 4414 CG ARG 467 91.304 29.011 59.839 1.00 84.26 4415 CD ARG 467 90.397 30.202 59.616 1.00 96.57 4416 NE ARG 467 90.163 30.938 60.853 1.00103.82 4417 CZ ARG 467 89.074 31.660 61.099 1.00107.61 4418 NH1 ARG 467 88.109 31.749 60.192 1.00108.04 4419 NH2 ARG 467 88.946 32.284 62.261 1.00109.38 4420 H ARG 467 93.769 27.556 58.623 1.00 25.00 4421 HE ARG 467 90.848 30.890 61.554 1.00 25.00 4422 1 HH1 ARG 467 88.194 31.273 59.318 1.00 25.00 4423 2HH1 ARG 467 87.293 32.293 60.390 1.00 25.00 4424 1HH2 ARG 467 89.669 32.209 62.950 1.00 25.00 4425 2HH2 ARG 467 88.130 32.827 62.457 1.00 25.00 4426 N ASP 468 91.769 25.726 56.704 1.00 52.60 4427 CA ASP 468 91.287 24.832 55.660 1.00 51.80 4428 C ASP 468 91.404 23.354 56.032 1.00 52.54 4429 O ASP 468 90.488 22.574 55.767 1.00 57.49 4430 CB ASP 468 92.026 25.111 54.346 1.00 49.09 4431 CG ASP 468 91.328 24.513 53.133 1.00 52.94 4432 OD1 ASP 468 90.127 24.170 53.218 1.00 55.18 4433 OD2 ASP 468 91.983 24.402 52.076 1.00 54.77 4434 H ASP 468 92.480 26.362 56.496 1.00 25.00 4435 N TYR 469 92.524 22.973 56.646 1.00 52.44 4436 CA TYR 469 92.755 21.581 57.040 1.00 49.37 4437 C TYR 469 92.458 21.283 58.511 1.00 48.25 4438 O TYR 469 92.316 20.121 58.894 1.00 46.98 4439 CB TYR 469 94.200 21.165 56.730 1.00 46.99 4440 CG TYR 469 94.546 21.129 55.260 1.00 47.76 4441 CD1 TYR 469 94.994 22.273 54.602 1.00 51.80 4442 CD2 TYR 469 94.431 19.947 54.524 1.00 50.13 4443 CE1 TYR 469 95.317 22.246 53.248 1.00 56.40 4444 CE2 TYR 469 94.753 19.908 53.167 1.00 54.09 4445 CZ TYR 469 95.195 21.063 52.537 1.00 57.04 4446 OH TYR 469 95.514 21.044 51.198 1.00 62.08 4447 H TYR 469 93.216 23.642 56.837 1.00 25.00 4448 HH TYR 469 95.802 21.916 50.922 1.00 25.00 4449 N GLY 470 92.371 22.328 59.328 1.00 49.37 4450 CA GLY 470 92.113 22.147 60.746 1.00 51.47 4451 C GLY 470 93.332 21.551 61.425 1.00 52.90 4452 O GLY 470 93.247 20.499 62.064 1.00 54.39 4453 H GLY 470 92.471 23.228 58.968 1.00 25.00 4454 N ILE 471 94.467 22.238 61.300 1.00 53.10 4455 CA ILE 471 95.728 21.771 61.874 1.00 48.51 4456 C ILE 471 96.521 22.877 62.571 1.00 49.16 4457 O ILE 471 96.230 24.063 62.408 1.00 48..02 4458 CB ILE 471 96.617 21.131 60.781 1.00 44.19 4459 CG1 ILE 471 96.816 22.116 59.621 1.00 43.37 4460 CG2 ILE 471 95.991 19.829 60.288 1.00 41.20 4461 CD1 ILE 471 97.608 21.558 58.449 1.00 38.24 4462 H ILE 471 94.452 23.094 60.822 1.00 25.00 4463 N SER 472 97.517 22.475 63.357 1.00 53.02 4464 CA SER 472 98.371 23.414 64.085 1.00 57.32 4465 C SER 472 99.352 24.117 63.146 1.00 60.76 4466 0 SER 472 99.689 23.587 62.084 1.00 61.94 4467 CB SER 472 99.148 22.672 65.180 1.00 59.87 4468 OG SER 472 99.873 21.568 64.653 1.00 59.66 4469 H SER 472 97.697 21.518 63.453 1.00 25.00 4470 HG SER 472 100.314 21.103 65.376 1.00 25.00 4471 N THR 473 99.838 25.287 63.557 1.00 61.86 4472 CA THR 473 100.794 26.053 62.755 1.00 63.28 4473 C THR 473 101.959 25.160 62.340 1.00 66.44 4474 0 THR 473 102.374 25.158 61.179 1.00 66.96 4475 CB THR 473 101.366 27.248 63.547 1.00 62.70 4476 0G1 THR 473 100.295 28.083 63.997 1.00 63.68 4477 CG2 THR 473 102.306 28.068 62.677 1.00 63.27 4478 H THR 473 99.529 25.654 64.404 1.00 25.00 4479 HG1 THR 473 99.682 27.608 64.552 1.00 25.00 4480 N LYS 474 102.454 24.380 63.296 1.00 65.27 4481 CA LYS 474 103.568 23.470 63.065 1.00 67.87 4482 C LYS 474 103.248 22.508 61.922 1.00 65.57 4483 0 LYS 474 104.051 22.325 61.001 1.00 66.11 4484 CB LYS 474 103.863 22.686 64.349 1.00 71.33 4485 CG LYS 474 105.150 21.875 64.320 1.00 77.07 4486 CD LYS 474 105.422 21.234 65.673 1.00 77.42 4487 CE LYS 474 106.776 20.544 65.698 1.00 78.55 4488 NZ LYS 474 107.067 19.962 67.037 1.00 75.57 4489 H LYS 474 102.058 24.422 64.186 1.00 25.00 4490 1 HZ LYS 474 106.336 19.263 67.278 1.00 25.00 4491 2HZ LYS 474 107.998 19.500 67.020 1.00 25.00 4492 3HZ LYS 474 107.070 20.720 67.750 1.00 25.00 4493 N GLU 475 102.047 21.944 61.960 1.00 61.44 4494 CA GLU 475 101.612 20.998 60.945 1.00 57.77 4495 C GLU 475 101.378 21.683 59.599 1.00 53.01 4496 0 GLU 475 101.623 21.091 58.545 1.00 55.03 4497 CB GLU 475 100.352 20.282 61.418 1.00 59.71 4498 CG GLU 475 100.104 18.950 60.737 1.00 73.81 4499 CD GLU 475 98.994 18.148 61.399 1.00 84.47 4500 0E1 GLU 475 98.562 18.513 62.518 1.00 88.32 4501 OE2 GLU 475 98.555 17.144 60.797 1.00 88.90 4502 H GLU 475 101.423 22.181 62.675 1.00 25.00 4503 N ALA 476 100.931 22.936 59.637 1.00 46.25 4504 CA ALA 476 100.681 23.703 58.420 1.00 43.91 4505 C ALA 476 102.003 23.972 57.712 1.00 44.05 4506 0 ALA 476 102.124 23.774 56.501 1.00 42.50 4507 CB ALA 476 99.984 25.018 58.749 1.00 34.16 4508 H ALA 4776 100.761 23.358 60.501 1.00 25.00 4509 N MET 477 103.000 24.402 58.480 1.00 45.42 4510 CA MET 477 104.321 24.689 57.932 1.00 46.57 4511 C MET 477 104.954 23.414 57.395 1.00 46.73 4512 0 MET 477 105.640 23.434 56.369 1.00 48.81 4513 CB MET 477 105.217 25.331 58.990 1.00 41.20 4514 CG MET 477 104.699 26.674 59.459 1.00 45.53 4515 SD MET 477 105.842 27.539 60.529 1.00 50.24 4516 CE MET 477 105.403 29.229 60.204 1.0044.87 4517 H MET 477 102.838 24.531 59.436 1.0025.00 4518 N ALA 478 104.689 22.301 58.071 1.0043.88 4519 CA ALA 478 105.214 21.012 57.646 1.0040.24 4520 C ALA 478 104.608 20.664 56.288 1.0039.48 4521 0 ALA 478 105.301 20.158 55.404 1.0042.61 4522 CB ALA 478 104.887 19.941 58.673 1.0038.44 4523 H ALA 478 104.140 22.350 58.883 1.0025.00 4524 N LYS 479 103.324 20.969 56.113 1.0037.41 4525 CA LYS 479 102.642 20.700 54.850 1.0036.91 4526 C LYS 479 103.214 21.598 53.754 1.0033.62 4527 0 LYS 479 103.408 21.164 52.616 1.0032.37 4528 CB LYS 479 101.136 20.931 54.986 1.0039.38 4529 CG LYS 479 100.338 20.573 53.736 1.0046.00 4530 CD LYS 479 98.850 20.797 53.947 1.0051.63 4531 CE LYS 479 98.273 19.858 55.003 1.0053.61 4532 NZ LYS 479 98.180 18.451 54.525 1.0057.01 4533 H LYS 479 102.820 21.377756.852 1.0025.00 4534 1 HZ LYS 479 99.126 18.106 54.269 1.0025.00 4535 2HZ LYS 479 97.776 17.853 55.274 1.0025.00 4536 3HZ LYS 479 97.561 18.416 53.688 1.0025.00 4537 N PHE 480 103.502 22.845 54.107 1.0030.92 4538 CA PHE 480 104.067 23.790 53.157 1.0031.88 4539 C PHE 480 105.457 23.356 52.714 1.0034.12 4540 O PHE 480 105.812 23.493 51.540 1.0037.15 4541 CB PHE 480 104.107 25.198 53.749 1.0029.35 4542 CG PHE 480 102.902 26.028 53.408 1.0037.28 4543 CD1 PHE 480 101.662 25.427 53.190 1.0037.60 4544 CD2 PHE 480 103.008 27.411 53.283 1.0036.73 4545 CE1 PHE 480 100.546 26.192 52.850 1.0036.20 4546 CE22 PHE 480 101.898 28.185 52.942 1.0038.45 4547 CZ PHE 480 100.665 27.574 52.726 1.0036.96 4548 H PHE 480 103.315 23.138 55.024 1.0025.00 4549 N GLN 481 106.238 22.810 53.641 1.0033.79 4550 CA GLN 481 107.573 22.352 53.292 1.0035.43 4551 C GLN 481 107.453 21.180 52.323 1.0035.55 4552 O GLN 481 108.200 21.103 51.347 1.0035.63 4553 CB GLN 481 108.368 21.930 54.524 1.0046.60 4554 CG GLN 481 109.844 21.688 54.210 1.0070.92 4555 CD GLN 481 110.583 20.933 55.302 1.0083.38 4556 OE1 GLN 481 110.036 20.658 56.371 1.0093.92 4557 NE2 GLN 481 111.836 20.588 55.032 1.0088.62 4558 H GLN 481 105.919 22.723 54.562 1.0025.00 4559 1HE2 GLN 481 112.316 20.105 55.735 1.0025.00 4560 2HE2 GLN 481 112.220 20.824 54.166 1.0025.00 4561 N ASN 482 106.486 20.297 52.561 1.0033.51 4562 CA ASN 482 106.272 19.146 51.682 1.0036.28 4563 C ASN 482 105.950 19.606 50.267 1.0036.07 4564 O ASN 482 106.380 18.989 49.288 1.0035.83 4565 CB ASN 482 105.140 18.252 52.200 1.0040.65 4566 CG ASN 482 105.535 17.465 53.436 1.0054.20 4567 OD1 ASN 482 106.698 17.095 53.607 1.0057.37 4568 ND2 ASN 482 104.565 17.204 54.307 1.0059.54 4569 H ASN 482 105.916 20.415 53.350 1.0025.00 4570 1 HD2 ASN 482 104.821 16.698 55.105 1.0025.00 4571 2HD2 ASN 482 103.6661 17.519 54.121 1.0025.00 4572 N MET 483 105.199 20.698 50.163 1.0033.64 4573 CA MET 483 104.831 21.250 48.866 1.0029.91 4574 C MET 483 106.080 21.757 48.152 1.0027.30 4575 0 MET 483 106.240 21.556 46.947 1.0032.31 4576 CB MET 483 103.814 22.373 49.036 1.0029.58 4577 CG MET 483 102.488 21.916 49.626 1.0032.65 4578 SD MET 483 101.388 23.311 49.943 1.0037.42 4579 CE MET 483 100.988 23.770 48.275 1.0033.87 4580 H MET 483 104.879 21.134 50.982 1.0025.00 4581 N ALA 484 106.979 22.385 48.903 1.0024.24 4582 CA ALA 484 108.226 22.895 48.339 1.0025.37 4583 C ALA 484 109.086 21.724 47.845 1.0027.23 4584 O ALA 484 109.696 21.792 46.772 1.0026.13 4585 CB ALA 484 108.979 23.703 49.385 1.0020.73 4586 H ALA 484 106.799 22.516 49.859 1.0025.00 4587 N GLU 485 109.103 20.642 48.622 1.0027.25 4588 CA GLU 485 109.864 19.437 48.289 1.0029.59 4589 C GLU 485 109.317 18.807 47.015 1.0026.53 4590 O GLU 485 110.070 18.386 46.139 1.0032.01 4591 CB GLU 485 109.792 18.425 49.437 1.0039.77 4592 CG GLU 485 110.327 18.942 50.779 1.0061.11 4593 CD GLU 485 110.170 17.953 51.934 1.0069.27 4594 OE1 GLU 485 109.663 16.830 51.716 1.0073.83 4595 OE2 GLU 485 110.561 18.302 53.073 1.0069.26 4596 H GLU 485 108.574 20.683 49.449 1.0025.00 4597 N THR 486 107.997 18.755 46.917 1.0026.56 4598 CA THR 486 107.323 18.207 45.749 1.0026.51 4599 C THR 486 107.673 19.050 44.520 1.0024.78 4600 O THR 486 107.961 18.514 43.437 1.0024.00 4601 CB THR 486 105.790 18.211 45.973 1.0030.57 4602 OG1 THR 486 105.463 17.277 47.010 1.0030.11 4603 CG2 THR 486 105.034 17.855 44.694 1.0027.79 4604 H THR 486 107.446 19.085 47.660 1.0025.00 4605 HG1 THR 486 105.755 16.396 46.782 1.0025.00 4606 N ALA 487 107.672 20.367 44.712 1.0020.69 4607 CA ALA 487 107.980 21.319 43.651 1.0019.32 4608 C ALA 487 109.409 21.127 43.141 1.0018.49 4609 O ALA 487 109.654 21.149 41.929 1.0015.86 4610 CB ALA 487 107.768 22.750 44.152 1.0015.08 4611 H ALA 487 107.454 20.716 45.604 1.0025.00 4612 N TRP 488 110.349 20.909 44.058 1.0020.11 4613 CA TRP 488 111.736 20.695 43.661 1.0019.04 4614 C TRP 488 111.856 19.461 42.781 1.0020.42 4615 O TRP 488 112.555 19.486 41.768 1.0023.27 4616 CB TRP 488 112.656 20.590 44.879 1.0019.13 4617 CG TRP 488 113.256 21.905 45.262 1.0020.79 4618 CD1 TRP 488 113.017 22.619 46.402 1.0019.35 4619 CD2 TRP 488 114.173 22.689 44.481 1.0018.53 4620 NE1 TRP 488 1 13.723 23.801 46.376 1.00 21.34 4621 CE2 TRP 488 114.441 23.869 45.210 1.00 17.70 4622 CE3 TRP 488 114.793 22.507 43.237 1.00 18.03 4623 CZ2 TRP 488 115.305 24.863 44.736 1.00 16.71 4624 CZ3 TRP 488 115.654 23.499 42.765 1.00 15.24 4625 CH2 TRP 488 115.899 24.659 43.515 1.00 14.14 4626 H TRP 488 110.109 20.905 45.009 1.00 25.00 4627 HE1 TRP 488 113.699 24.482 47.075 1.00 25.00 4628 N LYS 489 111.136 18.399 43.138 1.00 21.51 4629 CA LYS 489 111.162 17.175 42.345 1.00 17.89 4630 C LYS 489 110.604 17.476 40.961 1.00 19.66 4631 O LYS 489 111.091 16.947 39.960 1.00 22.89 4632 CB LYS 489 110.351 16.069 43.019 1.00 17.77 4633 CG LYS 489 110.922 15.624 44.344 1.00 15.98 4634 CD LYS 489 110.074 14.540 44.972 1.00 22.31 4635 CE LYS 489 110.525 14.254 46.392 1.00 24.45 4636 NZ LYS 489 109.694 13.199 47.029 1.00 26.46 4637 H LYS 489 110.589 18.443 43.952 1.00 25.00 4638 1 HZ LYS 489 108.703 13.510 47.052 1.00 25.00 4639 2HZ LYS 489 109.772 12.320 46.482 1.00 25.00 4640 3HZ LYS 489 110.028 13.037 47.997 1.00 25.00 4641 N ASP 490 109.590 18.338 40.906 1.00 20.77 4642 CA ASP 490 108.991 18.721 39.630 1.00 21.97 4643 C ASP 490 110.008 19.479 38.786 1.00 24.19 4644 O ASP 490 110.098 19.264 37.575 1.00 21.17 4645 CB ASP 490 107.739 19.585 39.837 1.00 26.18 4646 CG ASP 490 106.561 18.799 40.395 1.00 29.44 4647 OD1 ASSP 490 106.524 17.562 40.236 1.00 35.64 4648 OD2 ASP 490 105.657 19.425 40.982 1.00 29.87 4649 H ASP 490 109.245 18.731 41.736 1.00 25.00 4650 N ILE 491 110.776 20.362 39.419 1.00 20.68 4651 CA ILE 491 111.789 21.120 38.692 1.00 20.37 4652 C ILE 491 112.810 20.146 38.115 1.00 19.25 4653 O ILE 491 113.158 20.221 36.934 1.00 20.39 4654 CB ILE 491 112.508 22.153 39.595 1.00 22.00 4655 CG1 ILE 491 111.540 23.278 39.975 1.00 21.39 4656 CG2 ILE 491 113.737 22.716 38.877 1.00 21.00 4657 CD1 ILE 491 112.159 24.376 40.803 1.00 22.99 4658 H ILE 491 110.657 20.508 40.379 1.00 25.00 4659 N ASN 492 113.239 19.198 38.943 1.00 19.07 4660 CA ASN 492 114.216 18.196 38.529 1.00 18.67 4661 C ASN 492 113.700 17.404 37.332 1.00 20.34 4662 O ASN 492 114.446 17.133 36.393 1.00 20.40 4663 CB ASN 492 114.567 17.271 39.699 1.00 16.62 4664 CG ASN 492 115.269 18.007 40.839 1.00 18.56 4665 OD1 ASN 492 115.924 19.035 40.625 1.00 15.51 4666 ND2 ASN 492 115.140 17.484 42.050 1.00 15.73 4667 H ASN 492 112.899 19.181 39.862 1.00 25.00 4668 1 HD2 ASN 492 115.583 17.939 42.793 1.00 25.00 4669 2HD2 ASN 492 114.613 16.661 42.164 1.00 25.00 4670 N GLU 493 112.412 17.073 37.341 1.00 21.12 4671 CA GLU 493 111.816 16.341 36.225 1.00 22.19 4672 C GLU 493 111.736 17.225 34.985 1.00 24.12 4673 O GLU 493 1 1 1.958 16.755 33.869 1.00 26.10 4674 CB GLU 493 110.416 15.850 36.578 1.00 19.71 4675 CG GLU 493 110.394 14.831 37.690 1.00 30.24 4676 CD GLU 493 109.056 14.143 37.849 1.00 25.61 4677 OE1 GLU 493 108.111 14.460 37.100 1.00 36.10 4678 OE2 GLU 493 108.953 13.268 38.728 1.00 35.77 4679 H GLU 493 111.859 17.328 38.111 1.00 25.00 4680 N GLY 494 111.423 18.504 35.194 1.00 24.81 4681 CA GLY 494 111.311 19.451 34.096 1.00 18.06 4682 C GLY 494 112.614 19.686 33.352 1.00 25.75 4683 O GLY 494 112.605 20.176 32.217 1.00 25.47 4684 H GLY 494 111.263 18.819 36.107 1.00 25.00 46885 N LEU 495 113.735 19.350 33.986 1.00 24.09 4686 CA LEU 495 115.047 19.523 33.367 1.00 23.57 4687 C LEU 495 115.465 18.331 32.503 1.00 23.66 4688 O LEU 495 116.385 18.445 31.700 1.00 25.21 4689 CB LEU 495 116.111 19.781 34.439 1.00 21.29 4690 CG LEU 495 115.968 21.063 35.270 1.00 24.69 4691 CD1 LEU 495 116.913 21.024 36.459 1.00 15.49 4692 CD2 LEU 495 116.230 22.287 34.409 1.00 21.41 4693 H LEU 495 113.681 18.985 34.893 1.00 25.00 4694 N LEU 496 114.781 17.200 32.651 1.00 22.59 4695 CA LEU 496 115.118 15.996 31.889 1.00 20.47 4696 C LEU 496 114.749 16.049 30.409 1.00 24.46 4697 O LEU 496 113.692 16.556 30.033 1.00 22.73 4698 CB LEU 496 114.504 14.758 32.548 1.00 20.18 4699 CG LEU 496 115.016 14.454 33.959 1.00 23.38 4700 CD1 LEU 496 114.276 13.265 34.524 1.00 21.31 4701 CD2 LEU 496 116.523 14.187 33.938 1.00 20.33 4702 H LEU 496 114.020 17.172 33.267 1.00 25.00 4703 N ARG 497 115.642 15.530 29.573 1.00 26.43 4704 CA ARG 497 115.443 15.501 28.128 1.00 31.12 4705 C ARG 497 114.347 14.498 27.766 1.00 32.68 4706 O ARG 497 114.217 13.457 28.411 1.00 27.55 4707 CB ARG 497 116.757 15.124 27.431 1.00 30.06 4708 CG ARG 497 117.863 16.155 27.626 1.00 38.94 4709 CD ARG 497 119.217 15.505 27.851 1.00 37.77 4710 NE ARG 497 120.087 15.584 26.683 1.00 50.61 4711 CZ ARG 497 121.282 16.173 26.676 1.00 51.72 4712 NH1 ARG 497 121.754 16.744 27.777 1.00 46.52 4713 NH2 ARG 497 122.023 16.166 25.575 1.00 51.65 4714 H ARG 497 116.457 15.140 29.946 1.00 25.00 4715 HE ARG 497 119.773 15.180 25.847 1.00 25.00 4716 1HH1 ARG 497 121.213 16.733 28.615 1.00 25.00 4717 2HH1 ARG 497 122.653 17.183 27.766 1.00 25.00 4718 1HH2 ARG 497 121.685 15.718 24.748 1.00 25.00 4719 2HH2 ARG 497 122.920 16.608 25.576 1.00 25.00 4720 N PRO 498 113.542 14.798 26.731 1.00 34.46 4721 CA PRO 498 113.595 16.005 25.897 1.00 31.05 4722 C PRO 498 112.886 17.179 26.568 1.00 32.44 4723 O PRO 498 111.757 17.040 27.043 1.00 32.35 4724 CB PRO 498 1 12.831 15.587 24.635 1.00 30.63 4725 CG PRO 498 1 12.768 14.079 24.707 1.00 38.95 4726 CD PRO 498 1 12.593 13.830 26.162 1.00 34.35 4727 N THR 499 113.544 18.332 26.612 1.00 33.10 4728 CA THR 499 1 12.940 19.513 27.218 1.00 30.18 4729 C THR 499 112.075 20.223 26.170 1.00 31.00 4730 0 THR 499 1 12.369 20.172 24.974 1.00 33.56 4731 CB THR 499 114.016 20.474 27.795 1.00 25.39 4732 0G1 THR 499 115.004 20.752 26.798 1.00 24.84 4733 CG2 THR 499 114.703 19.843 28.996 1.00 22.98 4734 H THR 499 114.435 18.421 26.223 1.00 25.00 4735 HG1 THR 499 115.646 21.357 27.117 1.00 25.00 4736 N PRO 500 110.963 20.844 26.600 1.00 31.06 4737 CA PRO 500 110.053 21.558 25.692 1.00 32.31 4738 C PRO 500 110.705 22.740 24.967 1.00 34.94 4739 0 PRO 500 110.328 23.075 23.843 1.00 39.31 4740 CB PRO 500 108.916 21.994 26.620 1.00 29.71 4741 CG PRO 500 109.576 22.086 27.968 1.00 28.06 4742 CD PRO 500 110.460 20.876 27.984 1.00 23.70 4743 N VAL 501 111.642 23.398 25.641 1.00 32.94 4744 CA VAL 501 112.390 24.523 25.078 1.00 33.22 4745 C VAL 501 113.858 24.257 25.421 1.00 33.52 4746 0 VAL 501 114.154 23.347 26.204 1.00 33.00 4747 CB VAL 501 111.959 25.887 25.686 1.00 29.14 4748 CG1 VAL 501 110.515 26.198 25.330 1.00 26.33 4749 CG2 VAL 501 112.153 25.887 27.195 1.00 24.60 4750 H VAL 501 111.875 23.112 26.546 1.00 25.00 4751 N SER 502 114.775 25.026 24.844 1.00 30.56 4752 CA SER 502 116.194 24.832 25.128 1.00 33.20 4753 C SER 502 116.485 25.025 26.611 1.00 32.05 4754 0 SER 502 115.869 25.869 27.265 1.00 34.57 4755 CB SER 502 117.039 25.807 24.316 1.00 35.54 4756 OG SER 502 116.837 25.601 22.934 1.00 56.52 4757 H SER 502 114.502 25.729 24.224 1.00 25.00 4758 HG SER 502 117.098 24.709 22.686 1.00 25.00 4759 N THR 503 117.443 24.260 27.126 1.00 29.15 4760 CA THR 503 117.836 24.333 28.530 1.00 33.23 4761 C THR 503 118.166 25.771 28.927 1.00 31.90 4762 0 THR 503 117.977 26.177 30.078 1.00 32.13 4763 CB THR 503 119.058 23.443 28.797 1.00 38.70 4764 OG1 THR 503 118.767 22.110 28.366 1.00 51.69 4765 CG2 THR 503 119.395 23.420 30.278 1.00 40.66 4766 H THR 503 117.884 23.611 26.547 1.00 25.00 4767 HG1 THR 503 118.560 22.075 27.436 1.00 25.00 4768 N GLU 504 118.637 26.542 27.956 1.00 27.88 4769 CA GLU 504 118.982 27.935 28.184 1.00 31.30 4770 C GLU 504 117.801 28.706 28.789 1.00 31.46 4771 0 GLU 504 117.987 29.643 29.568 1.00 29.72 4772 CB GLU 504 119.396 28.578 26.863 1.00 32.18 4773 CG GLU 504 119.754 30.042 26.997 1.00 44.47 4774 CD GLU 504 120.045 30.714 25.672 1.00 47.35 4775 OE1 GLU 504 119.634 30.183 24.618 1.00 49.18 4776 OE2 GLU 504 120.683 31.788 25.691 1.00 48.31 4777 H GLU 504 118.771 26.169 27.067 1.00 25.00 4778 N PHE 505 116.588 28.274 28.464 1.00 27.10 4779 CA PHE 505 1 15.390 28.936 28.957 1.00 23.02 4780 C PHE 505 1 14.809 28.314 30.218 1.00 24.14 4781 0 PHE 505 113.888 28.869 30.818 1.00 22.77 4782 CB PHE 505 1 14.356 29.036 27.835 1.00 28.22 4783 CG PHE 505 114.888 29.711 26.602 1.00 28.58 4784 CD1 PHE 505 115.307 31.039 26.651 1.00 28.23 4785 CD2 PHE 505 115.048 29.001 25.417 1.00 28.81 4786 CE1 PHE 505 1 15.884 31.646 25.539 1.00 25.11 4787 CE2 PHE 505 115.623 29.597 24.300 1.00 28.43 4788 CZ PHE 505 116.043 30.922 24.362 1.00 29.72 4789 H PHE 505 116.489 27.504 27.881 1.00 25.00 4790 N LEU 506 115.367 27.182 30.641 1.00 21.53 4791 CA LEU 506 114.915 26.516 31.862 1.00 20.00 4792 C LEU 506 115.763 26.980 33.054 1.00 20.28 4793 0 LEU 506 115.270 27.120 34.176 1.00 21.38 4794 CB LEU 506 115.033 24.995 31.732 1.00 17.84 4795 CG LEU 506 114.265 24.277 30.621 1.00 23.70 4796 CD1 LEU 506 114.409 22.781 30.832 1.00 19.27 4797 CD2 LEU 506 112.797 24.671 30.645 1.00 20.22 4798 H LEU 506 116.092 26.791 30.120 1.00 25..00 4799 N THR 507 117.040 27.237 32.796 1.00 24.00 4800 CA THR 507 117.968 27.666 33.837 1.00 21.87 4801 C THR 507 117.508 28.894 34.634 1.00 21.92 4802 0 THR 507 117.636 28.913 35.858 1.00 25.77 4803 CB THR 507 119.382 27.870 33.260 1.00 22.57 4804 0G1 THR 507 119.728 26.728 32.465 1.00 23.76 4805 CG2 THR 507 120.400 28.014 34.381 1.00 20.42 4806 H THR 507 117.372 27.127 31.883 1.00 25.00 4807 HG1 THR 507 119.106 26.624 31.739 1.00 25.00 4808 N PRO 508 116.960 29.928 33.963 1.00 17.26 4809 CA PRO 508 116.503 31.114 34.698 1.00 18.03 4810 C PRO 508 115.423 30.774 35.735 1.00 19.69 4811 0 PRO 508 1 155.417 31.309 36.847 1.00 22.29 4812 CB PRO 508 115.943 31.999 33.583 1.00 18.28 4813 CG PRO 508 116.841 31.690 32.444 1.00 16.25 4814 CD PRO 508 116.909 30.177 32.510 1.00 14.75 4815 N ILE 509 114.528 29.864 35.362 1.00 21.35 4816 CA ILE 509 113.435 29.420 36.230 1.00 22.73 4817 C ILE 509 114.024 28.653 37.412 1.00 19.96 4818 0 ILE 509 113.627 28.854 38.561 1.00 22.40 4819 CB ILE 509 112.450 28.523 35.441 1.00 18.26 4820 CG1 ILE 509 111.867 29.317 34.267 1.00 20.40 4821 CG2 ILE 509 111.360 27.998 36.351 1.00 12.67 4822 CD1 ILE 509 111.082 28.486 33.280 1.00 22.89 4823 H ILE 509 114.597 29.468 34.470 1.00 25.00 4824 N LEU 510 114.989 27.788 37.114 1.00 21.34 4825 CA LEU 510 115.684 27.003 38.130 1.00 19.45 4826 C LEU 510 116.420 27.956 39.075 1.00 18.03 4827 0 LEU 510 116.372 27.799 40.300 1.00 23.54 4828 CB LEU 510 116.693 26.064 37.454 1.0018.99 4829 CG LEU 510 117.747 25.351 38.309 1.0017.88 4830 CD1 LEU 510 117.092 24.447 39.347 1.0013.70 4831 CD2 LEU 510 118.660 24.548 37.401 1.0012.82 4832 H LEU 510 115.234 27.670 36.174 1.0025.00 4833 N ASN 511 117.070 28.966 38.502 1.0016.84 4834 CA ASN 511 117.816 29.940 39.293 1.0018.52 4835 c ASN 511 116.918 30.774 40.185 1.0019.49 4836 O ASN 511 117.299 31.111 41.307 1.0021.10 4837 CB AASSNN 511 118.704 30.806 38.400 1.0014.99 4838 CG AASSNN 511 119.926 30.046 37.903 1.0019.61 4839 OD1 AASSNN 511 120.276 29.004 38.456 1.0022.94 4840 ND2 AASSNN 511 120.562 30.543 36.849 1.0017.54 4841 H AASSNN 511 117.040 29.059 37.540 1.0025.00 4842 1HD2 ASN 511 121.341 30.052 36.532 1.0025.00 4843 2HD2 ASN 511 120.230 31.364 36.438 1.0025.00 4844 N LEU 512 115.705 31.061 39.719 1.0018.46 4845 CA L LEEUU 512 114.751 31.814 40.527 1.0015.00 4846 C LLEEUU 512 114.415 31.007 41.778 1.0016.15 4847 0 LLEEUU 512 114.304 31.561 42.872 1.0024.00 4848 CB LLEEUU 512 113.484 32.114 39.727 1.0017.19 4849 CG LLEEUU 5112 113.569 33.341 38.818 1.0016.79 4850 CD1 LLEEUU 512 112.331 33.430 37.943 1.0022.39 4851 CD2 LLEEUU 512 113.702 34.591 39.672 1.0014.37 4852 H LLEEUU 512 115.450 30.773 38.817 1.0025.00 4853 N AALLAA 513 114.279 29.692 41.624 1.0019.31 4854 CA AALLAA 513 113.979 28.814 42.760 1.0018.01 4855 C AALLAA 513 115.178 28.789 43.710 1.0018.19 4856 0 AALLAA 513 115.017 28.802 44.933 1.0016.94 4857 CB AALLAA 513 113.654 27.403 42.274 1.0012.64 4858 H AALLAA 513 114.362 29.302 40.726 1.0025.00 4859 N AARRGG 514 116.381 28.767 43.140 1.0019.70 4860 CA AARRGG 514 117.609 28.763 43.934 1.0018.80 4861 C AARRGG 514 117.696 30.031 44.784 1.0017.46 4862 0 AARRGG 514 118.041 29.978 45.967 1.0021.48 4863 CB ARG 514 118.832 28.638 43.024 1.0013.68 4864 CG ARG 514 118.981 27.255 42.404 1.0014.32 4865 CD ARG 514 120.084 27.218 41.354 1.0017.33 4866 NE ARG 514 120.490 25.848 41.066 1.0016.97 4867 CZ ARG 514 121.107 25.453 39.958 1.0019.03 4868 NH1 ARG 514 121.398 26.320 38.998 1.0015.08 4869 NH2 ARG 514 121.450 24.180 39.821 1.0015.36 4870 H ARG 514 116.440 28.744 42.160 1.0025.00 4871 HE A ARRGG 514 120.282 25.180 41.738 1.0025.00 4872 1HH1 ARG 514 121.159 27.283 39.100 1.0025.00 4873 2HH1 ARG 514 121.862 26.006 38.170 1.0025.00 4874 1HH2 ARG 514 121.245 23.524440.547 1.0025.00 4875 2HH2 ARG 514 121.913 23.875 38.988 1.0025.00 4876 N ILE 515 117.330 31.164 44.196 1.0020.52 4877 CA ILE 515 117.352 32.438 44.911 1.0022.89 4878 C ILE 515 116.489 32.357 46.169 1.0025.55 4879 0 ILE 515 116.851 32.914 47.206 1.0028.26 4880 CB ILE 515 1 16.863 33.591 44.018 1.00 18.86 4881 CG1 ILE 515 117.857 33.824 42.883 1.00 18.35 4882 CG2 ILE 515 116.695 34.855 44.832 1.00 23.30 4883 CD1 ILE 515 117.408 34.863 41.885 1.00 19.17 4884 H ILE 515 117.045 31.141 43.257 1.00 25.00 4885 N VAL 516 115.372 31.637 46.082 1.00 27.24 4886 CA VAL 516 114.467 31.463 47.220 1.00 26.85 4887 C VAL 516 115.229 30.838 48.378 1.00 30.63 4888 0 VAL 516 115.219 31.354 49.496 1.00 28.87 4889 CB VAL 516 113.280 30.512 46.881 1.00 28.84 4890 CG1 VAL 516 112.433 30.248 48.122 1.00 23.42 4891 CG2 VAL 516 112.423 31.096 45.776 1.00 22.08 4892 H VAL 516 115.144 31.219 45.225 1.00 25.00 4893 N GLU 517 115.910 29.736 48.085 1.00 35.61 4894 CA GLU 517 116.680 28.997 49.081 1.00 41.24 4895 C GLU 517 117.696 29.890 49.796 1.00 42.08 4896 0 GLU 517 117.872 29.789 51.009 1.00 46.37 4897 CB GLU 517 117.385 27.802 48.424 1.00 41.58 4898 CG GLU 517 116.496 26.950 47.503 1.00 52.96 4899 CD GLU 517 115.344 26.242 48.223 1.00 59.58 4900 0E1 GLU 517 115.593 25.557 49.236 1.00 60.41 4901 OE2 GLU 517 114.187 26.352 47.762 1.00 63.04 4902 H GLU 517 115.899 29.407 47.161 1.00 25.00 4903 N VAL 518 118.314 30.799 49.050 1.00 40.18 4904 CA VAL 518 119.310 31.714 49.600 1.00 42.32 4905 C VAL 518 118.704 32.885 50.386 1.00 47.45 4906 0 VAL 518 119.269 33.326 51.389 1.00 48.49 4907 CB VAL 518 120.219 32.251 48.474 1.00 41.14 4908 CG1 VAL 518 121.133 33.350 48.986 1.00 39.83 4909 CG2 VAL 518 121.034 31.108 47.896 1.00 45.30 4910 H VAL 518 118.097 30.844 48.095 1.00 25.00 4911 N THR 519 117.563 33.387 49.923 1.00 45.49 4912 CA THR 519 116.899 34.505 50.577 1.00 44.49 4913 C THR 519 116.183 34.117 51.884 1.00 44.03 4914 0 THR 519 115.983 34.964 52.754 1.00 41.48 4915 CB THR 519 115.868 35.165 49.622 1.00 45.40 4916 OG1 THR 519 116.518 35.516 48.394 1.00 47.45 4917 CG2 THR 519 115.283 36.424 50.240 1.00 50.81 4918 H THR 519 117.161 32.996 49.123 1.00 25.00 4919 HG1 THR 519 116.872 34.719 47.980 1.00 25.00 4920 N TYR 520 115.827 32.843 52.034 1.00 49.74 4921 CA TYR 520 115.130 32.385 53.240 1.00 54.71 4922 C TYR 520 115.783 31.213 53.984 1.00 60.58 4923 0 TYR 520 115.129 30.191 54.209 1.00 65.16 4924 CB TYR 520 113.686 31.988 52.905 1.00 52.58 4925 CG TYR 520 112.886 33.018 52.142 1.00 53.27 4926 CD1 TYR 520 112.885 33.027 50.748 1.00 54.77 4927 CD2 TYR 520 112.105 33.962 52.809 1.00 50.10 4928 CE1 TYR 520 112.127 33.946 50.032 1.00 57.50 4929 CE2 TYR 520 111.340 34.889 52.102 1.00 54.19 4930 CZ TYR 520 111.357 34.873 50.713 1.00 56.86 4931 OH TYR 520 110.604 35.777 49.999 1.00 58.70 4932 H TYR 520 116.029 32.189 51.330 1.00 25.00 4933 HH TYR 520 1 10.726 35.626 49.057 1.00 25.00 4934 N ILE 521 117.056 31.340 54.350 1.00 67.35 4935 CA ILE 521 1 17.729 30.269 55.091 1.00 74.89 4936 C ILE 521 1 17.425 30.428 56.583 1.00 75.44 4937 0 ILE 521 117.194 29.397 57.255 1.00 76.20 4938 CB ILE 521 119.276 30.258 54.856 1.00 75.70 4939 CG1 ILE 521 119.586 29.919 53.394 1.00 76.18 4940 CG2 ILE 521 119.953 29.222 55.766 1.00 77.50 4941 CD1 ILE 521 121.064 29.755 53.080 1.00 71.61 4942 H ILE 521 117.546 32.156 54.145 1.00 25.00 4943 N VAL 533 120.428 39.967 55.248 1.00 55.02 4944 CA VAL 533 120.478 38.584 54.683 1.00 57.02 4945 C VAL 533 121.277 38.505 53.373 1.00 55.80 4946 0 VAL 533 122.075 37.588 53.181 1.00 56.73 4947 CB VAL 533 119.048 37.995 54.485 1.00 56.30 4948 CG1 VAL 533 118.225 38.868 53.539 1.00 56.90 4949 CG2 VAL 533 119.125 36.552 53.986 1.00 50.74 4950 1 H VAL 533 119.970 40.608 54.578 1.00 25.00 4951 2H VAL 533 119.880 39.938 56.132 1.00 25.00 4952 3H VAL 533 121.396 40.274 55.462 1.00 25.00 4953 N LEU 534 121.095 39.483 52.491 1.00 49.61 4954 CA LEU 534 121.812 39.490 51.218 1.00 48.50 4955 C LEU 534 123.194 40.138 51.300 1.00 47.52 4956 0 LEU 534 124.075 39.830 50.496 1.00 44.98 4957 CB LEU 534 120.983 40.190 50.137 1.00 48.86 4958 CG LEU 534 119.659 39.533 49.744 1.00 50.00 4959 CD1 LEU 534 119.054 40.290 48.567 1.00 46.00 4960 CD2 LEU 534 119.886 38.066 49.384 1.00 42.36 4961 H LEU 534 120.456 40.200 52.652 1.00 25.00 4962 N LYS 535 123.382 40.993 52.303 1.00 45.93 4963 CA LYS 535 124.633 41.722 52.510 1.00 45.11 4964 C LYS 535 125.921 40.923 52.284 1.00 43.08 4965 0 LYS 535 126.729 41.288 51.428 1.00 42.36 4966 CB LYS 535 124.651 42.385 53.895 1.00 46.19 4967 CG LYS 535 125.855 43.288 54.130 1.00 54.44 4968 CD LYS 535 125.868 43.868 55.536 1.00 57.76 4969 CE LYS 535 127.075 44.774 55.747 1.00 61.61 4970 NZ LYS 535 127.099 45.378 57.111 1.00 62.66 4971 H LYS 535 122.651 41.156 52.915 1.00 25.00 4972 1 HZ LYS 535 127.134 44.621 57.824 1.00 25.00 4973 2HZ LYS 535 127.936 45.986 57.207 1.00 25.00 4974 3HZ LYS 535 126.239 45.946 57.252 1.00 25.00 4975 N PRO 536 126.115 39.809 53.019 1.00 39.15 4976 CA PRO 536 127.337 39.020 52.829 1.00 37.51 4977 C PRO 536 127.564 38.579 51.386 1.00 33.92 4978 0 PRO 536 128.684 38.644 50.877 1.00 33.28 4979 CB PRO 536 127.128 37.827 53.770 1.00 38.16 4980 CG PRO 536 125.638 37.724 53.893 1.00 42.17 4981 CD PRO 536 125.233 39.164 54.008 1.00 38.53 4982 N HIS 537 126.488 38.181 50.714 1.00 33.98 4983 CA HIS 537 126.575 37.730 49.327 1.00 34.56 4984 C HIS 537 126.929 38.877 48.390 1.00 34.75 4985 0 HIS 537 127.742 38.714 47.479 1.00 29.05 4986 CB HIS 537 125.264 37.071 48.900 1.00 34.41 4987 CG HIS 537 124.917 35.855 49.703 1.00 41.27 4988 ND1 HIS 537 123.749 35.746 50.426 1.00 43.98 4989 CD2 HIS 537 125.601 34.705 49.917 1.00 37.03 4990 CE1 HIS 537 123.726 34.584 51.053 1.00 40.28 4991 NE2 HIS 537 124.838 33.933 50.760 1.00 39.05 4992 H HIS 537 125.618 38.225 51.154 1.00 25.00 4993 HD1 HIS 537 123.030 36.418 50.483 1.00 25.00 4994 HE2 HIS 537 125.072 33.038 51.088 1.00 25.00 4995 N ILE 538 126.333 40.040 48.634 1.00 34.95 4996 CA ILE 538 126.596 41.225 47.829 1.00 35.08 4997 C ILE 538 128.063 41.612 47.969 1.00 36.46 4998 0 ILE 538 128.703 41.999 46.990 1.00 38.58 4999 CB ILE 538 125.701 42.406 48.263 1.00 35.99 5000 CG1 ILE 538 124.230 42.072 47.983 1.00 37.36 5001 CG2 ILE 538 126.124 43.681 47.542 1.00 34.76 5002 CD1 ILE 538 123.248 43.112 48.460 1.00 36.39 5003 H ILE 538 125.708 40.113 49.385 1.00 25.00 5004 N ILE 539 128.588 41.491 49.185 1.00 34.70 5005 CA ILE 539 129.979 41.807 49.473 1.00 33.68 5006 C ILE 539 130.912 40.828 48.769 1.00 34.74 5007 O ILE 539 131.868 41.239 48.093 1.00 30.49 5008 CB ILE 539 130.253 41.761 51.004 1.00 35.37 5009 CG1 ILE 539 129.559 42.939 51.686 1.00 33.35 5010 CG2 ILE 539 131.749 41.790 51.285 1.00 32.80 5011 CD1 ILE 539 129.684 42.933 53.189 1.00 34.58 5012 H ILE 539 127.999 41.207 49.913 1.00 25.00 5013 N ASN 540 130.603 39.538 48.864 1.00 33.09 5014 CA ASN 540 131.440 38.505 48.263 1.00 33.80 5015 C ASN 540 131.355 38.498 46.749 1.00 34.25 5016 O ASN 540 132.298 38.166 46.065 1.00 33.46 5017 CB ASN 540 131.047 37.127 48.775 1.00 33.03 5018 CG ASN * 540 131.463 36.902 50.198 1.00 39.77 5019 OD1 ASN 540 130.776 36.219 50.965 1.00 45.10 5020 ND2 ASN 540 132.581 37.502 50.579 1.00 36.91 5021 H ASN 540 129.781 39.280 49.311 1.00 25.00 5022 1HD2 ASN 540 132.850 37.386 51.503 1.00 25.00 5023 2HD2 ASN 540 133.079 38.025 49.919 1.00 25.00 5024 N LEU 541 130.185 38.821 46.253 1.00 30.66 5025 CA LEU 541 129.997 38.848 44.821 1.00 31.93 5026 C LEU 541 130.262 40.166 44.110 1.00 33.86 5027 O LEU 541 130.805 40.129 42.977 1.00 30.07 5028 CB LEU 541 128.600 38.308 44.486 1.00 34.62 5029 CG LEU 541 128.194 36.907 44.990 1.00 35.64 5030 CD1 LEU 541 126.882 36.542 44.345 1.00 31.26 5031 CD2 LEU 541 129.256 35.866 44.669 1.00 29.53 5032 H LEU 541 129.518 38.998 46.982 1.00 25.00 5033 N LEU 542 129.910 41.305 44.706 1.00 35.33 5034 CA LEU 542 130.075 42.581 44.033 1.00 39.16 5035 C LEU 542 131.084 43.566 44.635 1.00 42.69 5036 0 LEU 542 131.361 44.614 44.055 1.00 45.28 5037 CB LEU 542 128.721 43.258 43.921 1.00 37.88 5038 CG LEU 542 127.685 42.494 43.105 1.00 37.82 5039 CD1 LEU 542 126.275 42.902 43.505 1.00 37.78 5040 CD2 LEU 542 127.947 42.728 41.619 1.00 33.54 5041 H LEU 542 129.525 41.317 45.569 1.00 25.00 5042 N VAL 543 131.590 43.264 45.822 1.00 40.06 5043 CA VAL 543 132.536 44.167 46.483 1.00 39.62 5044 C VAL 543 133.960 43.601 46.457 1.00 40.35 5045 0 VAL 543 134.834 44.117 45.766 1.00 36.40 5046 CB VAL 543 132.112 44.458 47.951 1.00 38.67 5047 CG1 VAL 543 133.154 45.323 48.643 1.00 41.60 5048 CG2 VAL 543 130.762 45.137 47.966 1.00 33.55 5049 H VAL 543 131.348 42.421 46.245 1.00 25.00 5050 N ASP 544 134.175 42.518 47.191 1.00 39.19 5051 CA ASP 544 135.485 41.887 47.274 1.00 37.12 5052 C ASP 544 135.802 40.970 46.112 1.00 38.65 5053 0 ASP 544 134.991 40.124 45.739 1.00 42.40 5054 CB ASP 544 135.609 41.070 48.566 1.00 37.00 5055 CG ASP 544 135.384 41.894 49.812 1.00 42.35 5056 OD1 ASP 544 135.659 43.114 49.803 1.00 49.35 5057 OD2 ASP 544 134.933 41.304 50.813 1.00 50.35 5058 H ASP 544 133.427 42.119 47.665 1.00 25.00 5059 N SER 545 136.984 41.153 45.543 1.00 36.71 5060 CA SER 545 137.444 40.303 44.464 1.00 39.73 5061 C SER 545 138.200 39.158 45.142 1.00 38.96 5062 0 SER 545 138.585 39.269 46.310 1.00 40.93 5063 CB SER 545 138.379 41.084 43.540 1.00 43.38 5064 OG SER 545 139.362 41.790 44.280 1.00 51.44 5065 H SER 545 137.544 41.896 45.832 1.00 25.00 5066 HG SER 545 139.870 41.166 44.808 1.00 25.00 5067 N ILE 546 138.377 38.046 44.442 1.00 36.92 5068 CA ILE 546 139.109 36.920 45.011 1.00 40.59 5069 C ILE 546 140.602 37.261 44.954 1.00 45.93 5070 0 ILE 546 141.117 37.620 43.889 1.00 46.41 5071 CB ILE 546 138.839 35.612 44.226 1.00 36.34 5072 CG1 ILE 546 137.346 35.288 44.264 1.00 34.10 5073 CG2 ILE 546 139.629 34.456 44.829 1.00 31.04 5074 CD1 ILE 546 136.979 34.011 43.525 1.00 36.46 5075 H ILE 546 138.009 37.990 43.533 1.00 25.00 5076 N LYS 547 141.282 37.201 46.009 1.00 52.49 5077 CA LYS 547 142.706 37.502 46.134 1.00 58.52 5078 C LYS 547 143.483 36.450 45.353 1.00 60.95 5079 0 LYS 547 143.488 35.273 45.713 1.00 60.42 5080 CB LYS 547 143.217 37.599 47.572 1.00 59.36 5081 CG LYS 547 144.684 38.023 47.659 1.00 68.28 5082 CD LYS 547 145.065 38.553 49.037 1.00 72.08 5083 CE LYS 547 146.486 39.105 49.029 1.00 74.86 5084 NZ LYS 547 146.796 39.880 50.265 1.00 78.47 5085 H LYS 547 140.806 36.948 46.910 1.00 25.00 5086 1HZ LYS 547 146.680 39.273 51.099 1.00 25.00 5087 2HZ LYS 547 147.770 40.240 50.222 1.00 25.00 5088 3HZ LYS 547 146.139 40.685 50.334 1.0025.00 5089 N ILE 548 144.086 36.890 44.254 1.0067.72 5090 CA ILE 548 144.868 36.018 43.381 1.0076.79 5091 C ILE 548 146.198 35.622 44.025 1.0083.68 5092 0 ILE 548 146.583 34.440 43.897 1.0086.24 5093 CB ILE 548 145.120 36.678 41.986 1.0075.68 5094 CG1 ILE 548 145.604 38.125 42.152 1.0078.47 5095 CG2 ILE 548 143.855 36.623 41.137 1.0068.49 5096 CD1 ILE 548 145.930 38.827 40.831 1.0078.93 5097 OXT ILE 548 146.823 36.492 44.672 1.0092.78 5098 H ILE 548 144.032 37.836 44.045 1.0025.00 5099 ILE 548 5100 MG MG 851 104.185 36.235 53.030 1.0061.83 5101 MG MG 852 102.138 43.657 49.009 1.0062.23 5102 0 HOH 601 107.742 22.057 32.406 1.0015.11 5103 0 HOH 602 122.540 22.695 37.531 1.0032.44 5104 0 HOH 603 127.188 14.109 43.835 1.0023.85 5105 0 HOH 604 123.257 32.177 37.651 1.0025.21 5106 0 HOH 605 131.975 36.814 38.945 1.0020.08 5107 0 HOH 606 130.320 38.579 40.729 1.0028.69 5108 0 HOH 607 124.735 33.181 39.810 1.0019.46 5109 0 HOH 608 119.958 22.714 50.725 1.0024.82 5110 0 HOH 609 125.172 22.654 40.253 1.0021.47 5111 0 HOH 610 106.047 21.994 29.826 1.0026.03 5112 0 HOH 611 123.659 29.782 47.444 1.0022.10 5113 0o HOH 612 129.924 22.165 49.955 1.0020.33 5114 0o HOH 613 117.254 16..672 36.732 1.0018.88 5115 0o HOH 614 131.911 22.935 48.204 1.0023.59 5116 0o HOH 615 123.421 30.030 35.911 1.0023.89 5117 0o HOH 616 128.952 30.316 38.829 1.0022.41 5118 0o HOH 617 98.347 33.326 40.948 1.0028.07 5119 0o HOH 618 126.062 19.250 36.922 1.0029.11 5120 0o HOH 619 133.788 33.099 36.415 1.0020.10 5121 0o HOH 620 127.252 22.013 48.848 1.0024.10 5122 0o HOH 621 123.122 19.043 45.472 1.0019.68 5123 0o HOH 622 124.636 25.767 41.845 1.0042.37 5124 0o HOH 623 138.021 26.937 54.497 1.0033.32 5125 0o HOH 624 130.604 16.213 44.273 1.0025.46 5126 0o HOH 625 119.735 17.425 55.175 1.0023.51 5127 0o HOH 626 109.560 43.332 32.386 1.0027.79 5128 0o HOH 627 104.016 36.817 39.018 1.0024.34 5129 0o HOH 628 134.051 35.256 29.604 1.0037.22 5130 0o HOH 629 107.947 18.792 36.023 1.0035.84 5131 0o HOH 630 129.821 19.576 48.096 1.0029.63 5132 0o HOH 631 104.550 21.758 41.675 1.0038.10 5133 0o HOH 632 111.970 10.709 47.161 1.0023.86 5134 0o HOH 633 125.976 29.448 50.341 1.0026.42 5135 0 HOH 634 97.143 36.787 48.102 1.0035.12 5136 0 HOH 635 121.582 36.805 25.111 1.0035.51 5137 0 HOH 636 113.756 26.801 22.571 1.0030.58 5138 0 HOH 637 124.698 19.485 28.803 1.0029.60 5139 0 HOH 638 130.563 25.567 43.476 1.0029..93 5140 O HOH 639 121.706 39.646 27.124 1.00 32.61 5141 O HOH 640 104.749 34.099 30.683 1.00 28.14 5142 O HOH 641 1 1 1.751 8.174 35.080 1.00 34.23 5143 O HOH 642 120.339 31.400 41.487 1.00 52.69 5144 O HOH 643 95.163 26.623 43.384 1.00 36.83 5145 O HOH 644 137.113 41.980 40.124 1.00 30.35 5146 O HOH 645 1 16.126 11.318 49.986 1.00 25.34 5147 0 HOH 646 1 10.165 35.328 17.495 1.00 37.81 5148 o HOH 647 118.054 20.287 30.749 1.00 33.12 5149 o HOH 648 115.899 40.354 30.351 1.00 29.82 5150 o HOH 649 113.524 54.000 32.295 1.00 30.14 5151 o HOH 650 127.950 27.982 37.184 1.00 28.39 5152 o HOH 651 108.770 18.109 30.127 1.00 36.94 5153 o HOH 652 112.843 23.036 50.160 1.00 41.87 5154 O HOH 653 132.804 32.747 50.167 1.00 34.56 5155 O HOH 654 99.278 32.670 36.214 1.00 31.88 5156 o HOH 655 93.100 36.093 41.777 1.00 39.13 5157 o HOH 656 114.575 17.087 50.058 1.00 29.96 5158 o HOH 657 134.890 18.651 45.599 1.00 29.79 5159 0 HOH 658 134.764 16.354 47.235 1.00 41.87 5160 O HOH 659 138.146 19.452 46.210 1.00 40.62 5161 O HOH 660 113.498 7.243 37.601 1.00 44.14 5162 o HOH 661 118.735 25.324 49.539 1.00 32.46 5163 o HOH 662 121.072 19.323 57.037 1.00 28.13 5164 o HOH 663 120.647 52.139 31.726 1.00 31.21 5165 o HOH 664 125.201 27.805 35.886 1.00 35.41 5166 O HOH 665 103.040 17.910 41.249 1.00 34.74 5167 O HOH 666 92.281 23.719 49.317 1.00 36.36 5168 o HOH 667 120.731 30.312 30.736 1.00 40.91 5169 o HOH 668 111.010 16.805 31.260 1.00 37.18 5170 o HOH 669 98.374 30.892 39.496 1.00 39.09 5171 o HOH 670 142.913 20.086 59.043 1.00 40.89 5172 o HOH 671 120.070 4.238 32.203 1.00 32.10 5173 o HOH 672 116.885 14.360 38.230 1.00 19.20 5174 0 HOH 673 135.198 31.364 38.159 1.00 21.99 5175 o HOH 674 130.652 23.815 45.653 1.00 22.37 5176 o HOH 675 116.184 18.170 25.042 1.00 33.65 5177 o HOH 676 102.763 37.505 36.535 1.00 29.50 5178 o HOH 677 113.482 17.709 47.318 1.00 24.10 5179 o HOH 678 128.292 24.082 47.295 1.00 27.62 5180 o HOH 679 128.934 20.011 39.747 1.00 26.34 5181 o HOH 680 129.840 32.556 48.799 1.00 34.07 5182 o HOH 681 115.123 17.894 45.342 1.00 23.02 5183 O HOH 682 134.875 11.928 61.810 1.00 24.68 5184 O HOH 683 140.837 17.873 38.782 1.00 33.65 5185 o HOH 684 135.724 8.315 55.152 1.00 37.93 5186 0 HOH 685 131.660 25.765 56.520 1.00 36.71 5187 O HOH 686 148.447 27.966 42.675 1.00 38.11 5188 O HOH 687 110.190 10.176 45.195 1.00 35.74 5189 O HOH 688 109.091 17.883 25.410 1.00 38.94 5190 O HOH 6889 104.860 34.526 28.030 1.00 38.81 5191 O HOH 690 102.070 36.177 27.889 1.00 35.60 5192 0 HOH 691 118.113 1 1.174 28.782 1.00 38.94 5193 0 HOH 692 131.635 20.640 62.725 1.00 33.60 5194 0 HOH 693 136.344 35.530 31.124 1.00 36.08 5195 0 HOH 694 120.257 31.406 33.335 1.00 31.14 5196 0 HOH 695 102.005 32.616 56.124 1.00 33.30 5197 0 HOH 696 124.575 21.994 35.468 1.00 36.59 5198 0 HOH 697 101.923 20.169 46.398 1.00 40.37 5199 o HOH 698 129.243 49.171 40.765 1.00 49.17 5200 0 HOH 699 139.196 35.578 48.616 1.00 31.26 5201 0 HOH 700 134.064 15.022 43.146 1.00 40.48 5202 0 HOH 701 128.514 31.051 51.675 1.00 39.32 5203 0 HOH 702 112.958 10.222 36.694 1.00 47.07 5204 0 HOH 703 109.649 15.841 28.459 1.00 35.43 5205 0 HOH 704 140.094 42.685 39.958 1.00 41.31 5206 0 HOH 705 86.608 31.749 55.350 1.00 36.82 5207 0 HOH 706 128.605 34.147 28.351 1.00 35.79 5208 0 HOH 707 87.075 34.369 56.433 1.00 42.04 5209 0 HOH 708 89.030 34.345 44.620 1.00 40.07 5210 0 HOH 709 104.535 51.407 27.998 1.00 39.44 5211 0 HOH 710 120.125 34.187 24.397 1.00 63.74 5212 0 HOH 711 100.184 37.778 52.580 1.00 43.18 5213 0 HOH 712 109.218 37.444 46.111 1.00 37.68 5214 0 HOH 713 139.550 20.401 60.539 1.00 40.82 5215 0 HOH 714 140.612 17.7933 52.684 1.00 42.33 5216 0 HOH 715 120.330 21.170 32.392 1.00 31.20 5217 0 HOH 716 100.372 35.917 30.033 1.00 43.22 5218 0 HOH 717 120.163 23.899 33.930 1.00 33.67 5219 0 HOH 718 146.383 28.556 40.921 1.00 38.01 5220 0 HOH 719 109.966 20.788 31.041 1.00 38.62 5221 0 HOH 720 105.493 40.925 45.887 1.00 35.53 5222 0 HOH 721 119.171 27.937 23.152 1.00 55.39 5223 0 HOH 722 124.424 41.390 25.938 1.00 43.52 5224 0 HOH 723 102.779 17.993 48.134 1.00 38.38 5225 0 HOH 724 112.387 5.685 33.453 1.00 48.35 5226 0 HOH 725 151.082 25.140 44.349 1.00 35.50 5227 0 HOH 726 127.089 21.203 29.049 1.00 45.21 5228 0 HOH 727 133.178 5.551 47.734 1.00 39.38 5229 0 HOH 728 151.127 34.628 33.927 1.00 42.02 5230 0 HOH 729 150.405 22.240 44.559 1.00 38.43 5231 0 HOH 730 131.660 2.107 47.933 1.00 37.78 5232 0 HOH 731 135.465 8.584 52.047 1.00 40.15 5233 0 HOH 732 147.814 29.664 45.229 1.00 44.50 5234 0 HOH 733 140.989 33.094 47.707 1.00 43.19 5235 0 HOH 734 103.951 49.441 25.596 1.00 38.72 5236 0 HOH 735 86.471 53.747 29.731 1.00 43.56 5237 0 HOH 736 134.470 31.168 25.546 1.00 52.39 5238 0 HOH 737 122.918 25.464 36.469 1.00 42.39 5239 0 HOH 738 99.309 33.456 31.178 1.00 48.32 5240 0 HOH 739 91.548 47.290 47.278 1.00 45.43 5241 0 HOH 740 92.024 43.380 40.690 1.00 42.02 5242 0 HOH 741 149.190 38.195 52.530 1.00 47.74 5243 0 HOH 742 153.088 41.575 36.804 1.00 46.51 5244 0 HOH 743 138.714 31.651 53.657 1.00 43.64 5245 0 HOH 744 143.900 19.054 51.722 1.00 40.32 5246 0 HOH 745 138.795 15.536 49.608 1.00 43.79 5247 0 HOH 746 124.711 -3.430 56.077 1.00 44.40 5248 0 HOH 747 145.969 30.921 42.825 1.00 39.08 5249 0 HOH 748 134.979 10.249 59.470 1.00 35.78 5250 0 HOH 749 133.932 40.151 29.911 1.00 41.40 5251 o HOH 750 114.521 21.309 22.697 1.00 38.72 5252 0 HOH 751 129.614 38.180 25.426 1.00 39.89 5253 0 HOH 752 111.6443 13.087 29.735 1.00 45.90 5254 0 HOH 753 104.216 21.388 44.848 1.00 33.35 5255 0 HOH 754 110.986 12.520 49.459 1.00 49.32 5256 0 HOH 755 139.600 40.725 48.728 1.00 46.07 5257 0 HOH 756 113.295 9.448 29.832 1.00 35.78 5258 0 HOH 757 127.101 23.382 34.156 1.00 48.02 5259 0 HOH 758 127.933 18.490 63.251 1.00 46.33 5260 0 HOH 759 130.420 26.867 25.702 1.00 40.40 5261 0 HOH 760 122.231 3.237 35.918 1.00 44.61 5262 0 HOH 761 128.310 26.484 40.968 1.00 32.14 5263 0 HOH 762 88.443 24.530 48.586 1.00 57.07 5264 0 HOH 763 103.542 23.739 25.080 1.00 45.05 5265 0 HOH 764 116.278 57.331 34.559 1.00 42.40 5266 0 HOH 765 120.787 5.886 61.156 1.00 43.73 5267 0 HOH 766 142.631 40.352 42.775 1.00 65.94 5268 0 HOH 767 124.244 13.057 63.666 1.00 43.68 5269 0 HOH 768 101.830 22.900 29.735 1.00 36.47 5270 0 HOH 769 137.190 5.022 37.071 1.00 50.65 5271 0 HOH 770 135.078 34.403 50.639 1.00 51.53 5272 0 HOH 771 103.266 58.719 26.225 1.00 46.58 5273 0 HOH 772 144.319 16.861 24.565 1.00 53.32 5274 0 HOH 773 127.856 47.718 31.019 1.00 45.45 5275 0 HOH 774 95.530 18.110 49.546 1.00 52.47 5276 0 HOH 775 148.435 20.165 43.831 1.00 49.25 5277 0 HOH 776 118.026 13.535 59.021 1.00 48.41 5278 0 HOH 777 110.119 43.903 16.201 1.00 37.10 5279 0 HOH 778 110.457 61.356 39.879 1.00 44.66 5280 0 HOH 779 105.313 56.879 27.692 1.00 51.08 5281 0 HOH 780 106.267 19.656 28.049 1.00 45.55 5282 0 HOH 781 122.226 20.789 29.638 1.00 45.73 5283 0 HOH 782 107.680 19.165 33.248 1.00 35.37 5284 0 HOH 783 141.434 30.527 58.190 1.00 56.49 5285 0 HOH 784 121.953 27.180 30.544 1.00 43.22 5286 0 HOH 785 116.050 27.492 52.913 1.00 59.86 5287 0 HOH 786 115.271 11.494 53.629 1.00 47.46 5288 0 HOH 787 136.166 43.700 43.430 1.00 44.89 5289 0 HOH 788 123.135 5.923 32.296 1.00 61.24 5290 0 HOH 789 148.342 38.089 38.232 1.00 41.22 5291 0 HOH 790 112.195 39.980 44.065 1.00 44.26 5292 0 HOH 791 108.340 50.773 20.100 1.00 62.55 5293 0 HOH 792 126.140 29.670 29.775 1.00 38.87 5294 0 HOH 793 122.347 26.176 27.904 1.00 47.43 5295 0 HOH 794 105.375 13.283 37.860 1.00 40.63 5296 0 HOH 795 146.608 19.061 33.529 1.00 50.53 5297 0 HOH 796 1 12.240 28.192 56.028 1.00 54.08 5298 0 HOH 797 106.519 16.717 37.160 1.00 39.17 5299 0 HOH 798 122.257 -2.147 57.632 1.00 59.87 5300 0 HOH 799 105.969 47.469 20.174 1.00 42.44 5301 0 HOH 800 124.201 23.387 29.951 1.00 51.85 5302 0 HOH 801 104.010 26.139 23.199 1.00 57.02 5303 0 HOH 802 106.547 37.540 47.839 1.00 46.00 5304 0 HOH 803 126.083 27.795 33.246 1.00 45.66 5305 0 HOH 804 93.229 25.530 63.301 1.00 50.45 5306 0 HOH 805 126.637 14.627 66.291 1.00 54.63 5307 0 HOH 806 117.649 48.031 30.248 1.00 44.41 5308 0 HOH 807 112.889 34.483 46.820 1.00 41.77 5309 0 HOH 808 143.749 8.474 39.051 1.00 58.35 5310 0 HOH 809 117.223 16.467 56.527 1.00 54.55 5311 0 HOH 810 136.640 48.794 42.640 1.00 59.70 5312 0 HOH 811 130.573 47.631 52.219 1.00 43.65 5313 0 HOH 812 119.790 22.620 53.732 1.00 49.88 5314 0 HOH 813 105.220 9.911 43.334 1.00 53.82 5315 0 HOH 814 94.459 22.230 65.891 1.00 53.43 5316 0 HOH 815 145.893 33.119 447.904 1.00 50.15 5317 0 HOH 816 137.540 19.003 49.581 1.00 32.04 5318 0 HOH 817 127.395 18.676 22.177 1.00 58.02 5319 0 HOH 818 135.930 19.361 20.695 1.00 61.65 5320 0 HOH 819 122.368 -4.865 43.028 1.00 43.72 5321 0 HOH 820 117.352 52.131 24.538 1.00 49.67 5322 0 HOH 821 129.874 51.577 33.814 1.00 58.12 5323 0 HOH 822 129.360 28.179 34.594 1.00 43.67 5324 0 HOH 823 97.243 40.051 31.308 1.00 40.94 5325 0 HOH 824 119.361 23.189 24.691 1.00 55.59 5326 0 HOH 825 105.947 8.433 39.961 1.00 47.78 5327 0 HOH 826 124.177 -6.929 48.285 1.00 50.47 5328 0 HOH 827 143.743 41.219 49.977 1.00 54.42 5329 0 HOH 828 117.815 15.765 23.926 1.00 47.10 5330 0 HOH 829 106.852 11.509 45.366 1.00 59.91 5331 0 HOH 830 114.340 49.442 45.031 1.00 54.21 5332 0 HOH 831 107.212 10.319 38.018 1.00 47.91 5333 0 HOH 832 89.843 54.539 37.711 1.00 55.79 5334 0 HOH 833 115.120 21.415 49.941 1.00 40.64 5335 0 HOH 834 119.324 14.942 62.472 1.00 63.27 5336 0 HOH 835 149.479 14.241 50.723 1.00 65.18 5337 0 HOH 836 99.208 46.311 26.331 1.00 59.48 5338 0 HOH 837 146.479 34.108 25.046 1.00 49.79 5339 0 HOH 838 117.731 49.616 19.065 1.00 60.65 5340 0 HOH 839 115.539 6.301 34.276 1.00 51.97 5341 0 HOH 840 97.213 27.831 34.233 1.00 45.30 5342 0 HOH 841 89.788 22.728 43.919 1.00 61.79 5343 0 HOH 842 147.830 32.323 40.885 1.00 46.95 5344 0 HOH 843 132.462 17.381 68.762 1.00 50.53 5345 0 HOH 844 140.816 13.261 39.613 1.00 50.48 5346 0 HOH 845 131.788 48.689 43.107 1.00 55.44 5347 0 HOH 846 106.451 38.430 52.704 1.00 44.59 5348 O HOH 847 112.522 3.225 51.067 1.00 62.24 5349 O HOH 848 1 16.588 33.059 17.286 1.00 51.54 5350 0 HOH 849 121.984 13.530 21.831 1.00 59.69 5351 0 HOH 850 121.351 34.646 19.580 1.00 63.69 5352 O HOH 853 119.444 26.300 52.657 1.00 48.12 5353 O HOH 854 119.223 18.972 28.280 1.00 43.53 5354 0 HOH 855 109.476 29.077 61.498 1.00 46.95 5355 O HOH 856 96.378 36.846 50.773 1.00 37.88 5356 O HOH 857 96.918 46.467 51.605 1.00 69.73 5357 O HOH 858 97.861 35.983 32.096 1.00 48.71 5358 O HOH 859 105.582 44.217 22.626 1.00 52.96 5359 O HOH 860 111.207 54.577 33.852 1.00 44.86 5360 O HOH 861 106.475 45.773 50.620 1.00 52.70 5361 O HOH 862 136.750 45.222 40.123 1.00 53.92 5362 O HOH 863 134.438 43.600 31.414 1.00 51.51 5363 O HOH 864 147.130 24.676 49.884 1.00 42.49 5364 O HOH 865 126.425 22.757 59.405 1.00 54.25 5365 O HOH 866 135.514 7.098 48.245 1.00 59.13 5366 O HOH 867 114.942 1.622 48.125 1.00 56.08 5367 O HOH 868 119.740 -4.108 46.312 1.00 51.35 5368 O HOH 869 134.478 8.308 29.219 1.00 53.23 5369 O HOH 870 127.297 14.232 21.009 1.00 54.19 5370 O HOH 871 134.315 17.294 22.547 1.00 59.58 5371 O HOH 872 130.159 26.543 36.441 1.00 34.46 5372 O HOH 873 136.207 18.694 43.344 1.00 35.20 5373 O HOH 874 134.779 10.368 41.428 1.00 45.81 5374 O HOH 875 137.054 3.899 33.453 1.00 51.47 5375 O HOH 876 145.762 17.318 28.638 1.00 52.42 5376 O HOH 877 146.344 20.944 29.342 1.00 47.62 TABLE 12 Score = 167 bits (419), Expect = 5e-41 Identities = 88/270 (32%), Positives = 152/270 155%) , Gaps = 5/270 (1%) Query: 1 DRVVECYF ALGVYFEPQYSQARVMLVKTISMISIVDDTFDAYGTVKELEAYTDAIQRWD 60 DR+VECYFW G+ Q++ AR+ + K ++I+++DD +D YGT++E E +TD I+RWD Sb-jct: 316 DRLVECYFWNTGIIEPRQHASARIMMGKVNALITVIDDIYDVYGTLEELEQFTDLIRRWD 375 Query: 61 I EIDRLPDYMKISYKAILDLYKDYE E SSAGRSHIVCHAIERMKEVVRNYNVESTWFI 120 IN ID+LPDYM++ + A+ + D ++ +++ + -i- + ■ + Y VE+ WF Sb * jct: 376 INSIDQLPDYMQLCFLALNNFVDDTSYDVMKEKGVNVIPYLRQSWVDLADKYMVEARWFY 435 Query: 121 EGYMPPVSEY SNA ATTTYYY ATTSYLGM-KSATEQDFEWLSKNPKILEASVIICRVI 179 G+ P + EYL N+ + + + T + + S T++ + L K ++ S + R+ Sbjct: 436 GGHKPSLEEYLENSWQSISGPCMLTHIFFRVTDSFTKETVDSLYKYHD VRWSSFVLR A 495 Query: 180 DDTATYEVEKSRGQIATGIECCMRDYGISTKEAMAKFQNMAETAWKDIN-EGLLRPTPVS 238 DD T E SRG + ++C M DY S EA + + WK +N E + + +P Sb * jct: 496 DDLGTSVEEVSRGDVPKSLQCYMSDYNASEAEARKHVK LIAEVWKKMNAERVSKDSPFG 555 Query: 239 TEF TPI NLARIVEVTYIHN DGY--THP 266 +F+ ++L R+ ++ Y HN DG+ HP Sb-jct: 556 KDFIGCAVDLGRMAQLMY-HNGDGHGTQHP 584 TABLE 13 Score = 116 bits (289), Expect = le-25 Identities = 77/270 (28%), Positives = 126/270 (46%), Gaps 6/270 (2%) Query: 3 VAEVYFSSATFEP-EYSATRIAFTKIGCLQV FDDMADIFAT DELKSFTEGVKRWDTSL 61 V +++ FEP ++ R I L + DD+ D++ TLDEL+ FT+ KRWDT Sbjct: 318 VESFF AVGMFEPHQHGYQRKMAATIIVLATVIDDIYDVYGT DELE FTDTFKRWDTES 377 Query: 62 LHEIPECMQTCFKWFKLMEEVNNDVVKVQGRDMLAHIRKPWELYFNCYVQEREWLEAGY 121 + +P MQ C+ + + D++K G L ++RK Y E +W +GY Sbjct: 378 ITRLPYYMQLCYWGVHNYISDAAYDILKEHGFFCLQYLRKSVVDLVEAYFHEAKWYHSGY 437 Query: 122 IPTFEEYL TYAISVGLGPCTLQPILLMGELVKDD—VVEKVHYPSNMFELVSLSWRLTN 179 P+ +EYL ISV P + P D V++ ++ ++ L + RL + Sbjct: 438 TPSLDEYLNIAKISVA-SPAIISPTYFTFANASHDTAVIDSLYQYHDILCLAGIILRLPD 496 Query: 180 DTKTYQAEKARGQQASGIACYMKDNPGATEEDAIKHICRWDRALKEASFEYFKPΞNDIP 239 D T E ARG I CYMK+ A+EE+A++H+ ++ A K+ + P Sbjct: 497 DLGTSYFELARGDVPKTIQCYMKET-NASEEEAVEHVKFLIREAWKDMN-TAIAAGYPFP 554 Query: 240 MGCKSFIFNLRLCVQIFYKFIDGYGIANEE 269 G + N+ Q Y DG+G+ + + Sbjct: 555 DGMVAGAANIGRVAQFIYLHGDGFGVQHSK 584 TABLE 14 Score = 120 bits (299), Expect = 6e-27 Identities = 70/272 (25%), Positive's = 137/272 (49%) , Gaps = 3/272 ( Query: 2 RVVECYFWALGVYFEPQYSQARVMLVKTISMISIVDDTFDAYGTVKELEAYTDAIQRWDI 61 R VE Y W + FEP++S++R+ KT + +++DD +D + T+ E++ T+ ++RWD+ Sbjct: 296 RHVEYYSWVVMCIFEPEFSESRIAFAKTAILCTVLDDLYDTHATLHEIKIMTEGVRRWDL 355 Query: 62 NEIDRLPDYMKISYKAILDLYKDYEKELSSAGRSHIVCHAIERMKEVVRNYNVESTWFIE 121 + D LPDY+KI+++ + + E+ + + K + +Y E+ W Sbjct: 356 SLTDDLPDYIKIAFQFFFNTVNELIVEIVKRQGRDMTTIVKDCWKRYIESYLQEAEWIAT 415 Query: 122 GYMPPVSEYLSNALATTTYYYLATTSYLGM-KSATEQDFEWLSKNPKILEASVIICRVID 180 G++P +EY+ N +A++ L L + K + E + KIL+ + R+ D Sbjct: 416 GHIPTFNEYIKNGMASSGMCILNLNPLLLLDKLLPDNILEQIHSPSKILDLLELTGRIAD 475 Query: 181 DTATYEVEKSRGQIATGIECCMRDYGISTKE-AMAKFQNMAETAWKDINEGLLRPTPVST 239 D +E EK RG++A+ ++C M++ ST E A+ + + + ++ N ++ V Sbjct: 476 DLKDFEDEKERGEMASSLQCYMKENPESTVENALNHIKGILNRSLEEFNWEFMKQDSVPM 535 Query: 240 EFLTPILNLARIVEVTYIHNLDGYTHPEKVLK 271 N+ R ++ Y + DG +K +K Sbjct: 536 CCKKFTFNIGRGLQFIYKYR-DGLYISDKEVK 566 TABLE 15 Score = 221 bits (557), Expect = 4e-57 Identities = 120/283 (42%), Positives = 178/283 (62%), Gaps = 6/283 (2%) Query: 5 EFYFWMAAAISEPEFSGSRVAFTKIAILMTMLDDLYDTHGTLDQLKIFTEGVRRWDVSLV 64 E YF A+ I EPEFS R +TK + +LDDLYD HG+LD LK+FTE V+RWD+SLV Sbjct : 589 EIYFSPASFIFEPEFSKCREVYTKTSNFTVILDDLYDAHGSLDDL LFTESVKRWDLSLV 648 Query: 65 EGLPDFMKIAFEFWLKTSNELIAEAVKAQGQDMAAYIRKNAWERYLEAYLQDAEWIATGH 124 + +P MKI F + T N++ E + QG+D+ Yl +N W+ LEAY ++AEW + Sbjct : 649 DQMPQQMKICFVGFYNTFNDIAKEGRERQGRDVLGYI-QNVWKVQLEAYTKEAEWSEAKY 707 Query: 125 VPTFDEYLNNGTPNTGMCVLNLIPLLLMGEHLPIDILEQIFLPSRFHHLIELASRLVDDA 184 VP+F+EY+ N + + + + LI L GE L ++L +1 SRF L+ L RLV+D Sbjct: 708 VPSFNEYIENASVSIALGTWLISALFTGEVLTDEVLSKIDRESRFLQLMGLTGRLVNDT 767 Query: 185 RDFQAEKDHGDL-SCIECYLKDHPESTVEDALNHVNGLLGNCLLEMNWKFLKKQDSVPLS 243 + +QAE+ G++ S I+CY+KDHP+ + E+AL HV ++ N L E+N +F+ + +P Sbjct: 768 KTYQAERGQGEVASAIQCYMKDHPKISEEEALQHVYSVMENALEELNREFV--NNKIPDI 825 Query: 244 CKKYSFHVLARSIQFMYNQGDGFSISNKV-IKDQVQKVLIVPV 285 K+ F AR +Q Y QGDG ++S+ + IK+ V+ L PV Sbjct: 826 YKRLVFET-ARIMQLFYMQGDGLTLSHDMEIKEHVKNCLFQPV 867 WE CLAIM THE FOLLOWING: 1. An isolated terpene synthase having a region with 20% or greater sequence identity to residues 265 to 535 of SEQ ID NO: 2, said synthase comprising nine α-carbons having interatomic distances in Angstroms between said α-carbons that are ±2.3 Angstroms of the following interatomic distances: the center point of each said α-carbon positioned within a sphere having a radius of 2.3 Angstroms, the center points of each said sphere having the following structural coordinates: , each said α-carbon having an associated R-group, said synthase having an ordered arrangement of said R-groups other than the following ordered arrangements of R- groups:

Claims: 2. The synthase of claim 1 , wherein said synthase has 25% or greater sequence identity to residues 265 to 535 of SEQ ID 2. 3. The synthase of claim 2, wherein said synthase has 35% or greater sequence identity to residues 265 to 535 of SEQ ID 2. 4. The synthase of claim 1 , wherein said synthase catalyses the formation of a terpenoid product from a monoterpene substrate. 5. The synthase of claim 1 , wherein said synthase catalyses the formation of a teφenoid product from a sesquiteφene substrate. 6. The synthase of claim 1 , wherein said synthase catalyses the formation of a terpenoid product from a diteφene substrate. 7. The synthase of claims 4, 5, or 6, wherein said product is a cyclic teφenoid hydrocarbon. 8. The synthase of claim 4, 5, or 6, wherein said product is an acyclic teφenoid hydrocarbon. 9. The synthase of claim 4, 5, or 6 wherein said product is a cyclic hydroxylated teφenoid hydrocarbon. 10. The synthase of claim 4, 5, or 6 wherein said product is an acyclic hydroxylated teφenoid hydrocarbon. 11. The synthase of claim 1 , wherein said R-group associated with said α- carbon 1 is selected from the group consisting of Cys, Ser, and Thr. 12. The synthase of claim 1 , wherein said R-group associated with said α- carbon 1 is selected from the group consisting of Phe, Tyr and Tφ. 13. The synthase of claim 1 , wherein said R-group associated with said α- carbon 1 is selected from the group consisting of Pro, Gly, and Ala. 14. The synthase of claim 1 , wherein said R-group associated with said α- carbon 1 is selected from the group consisting of Glu and Asp. 15. The synthase of claim 1 , wherein said R-group associated with said α- carbon 1 is selected from the group consisting of Met, lie, Val and Leu. 16. The synthase of claim 1 , wherein said R-group associated with said α- carbon 1 is selected from the group consisting of Arg and Lys. 17. The synthase of claim 1 , wherein said R-group associated with said α- carbon 1 is selected from the group consisting of Gin, Asn and His. 18. The synthase of claim 1 , wherein said R-group associated with said α- carbon 2 is selected from the group consisting of Cys, Ser and Thr. 19. The synthase of claim 1 , wherein said R-group associated with said α- carbon 2 is selected from the group consisting of Phe, Tyr and Tφ. 20. The synthase of claim 1 , wherein said R-group associated with said α- carbon 2 is selected from the group consisting of Pro, Gly, and Ala. 21. The synthase of claim 1 , wherein said R-group associated with said α- carbon 2 is selected from the group consisting of Glu and Asp. 22. The synthase of claim 1 , wherein said R-group associated with said α- carbon 2 is selected from the group consisting of Met, He, Val and Leu. 23. The synthase of claim 1 , wherein said R-group associated with said α- carbon 2 is selected from the group consisting of Arg and Lys. 24. The synthase of claim 1 , wherein said R-group associated with said α- carbon 2 is selected from the group consisting of Gin, Asn and His. 25. The synthase of claim 1 , wherein said R-group associated with said α- carbon 3 is selected from the group consisting of Cys, Ser and Thr. 26. The synthase of claim 1 , wherein said R-group associated with said α- carbon 3 is selected from the group consisting of Phe, Tyr and Trp. 27. The synthase of claim 1 , wherein said R-group associated with said α- carbon 3 is selected from the group consisting of Pro, Gly, and Ala. 28. The synthase of claim 1 , wherein said R-group associated with said α- carbon 3 is selected from the group consisting of Glu and Asp. 29. The synthase of claim 1 , wherein said R-group associated with said α- carbon 3 is selected from the group consisting of Met, lie, Val and Leu. 30. The synthase of claim 1 , wherein said R-group associated with said α- carbon 3 is selected from the group consisting of Arg and Lys. 31. The synthase of claim 1 , wherein said R-group associated with said α- carbon 3 is selected from the group consisting of Gin, Asn and His. 32. The synthase of claim 1 , wherein said R-group associated with said α- carbon 4 is selected from the group consisting of Cys, Ser and Thr. 33. The synthase of claim 1 , wherein said R-group associated with said α- carbon 4 is selected from the group consisting of Phe, Tyr and Trp. 34. The synthase of claim 1 , wherein said R-group associated with said α- carbon 4 is selected from the group consisting of Pro, Gly, and Ala. 35. The synthase of claim 1 , wherein said R-group associated with said α- carbon 4 is selected from the group consisting of Glu and Asp. 36. The synthase of claim 1 , wherein said R-group associated with said α- carbon 4 is selected from the group consisting of Met, He, Val and Leu. 37. The synthase of claim 1 , wherein said R-group associated with said α- carbon 4 is selected from the group consisting of Arg and Lys. 38. The synthase of claim 1 , wherein said R-group associated with said α- carbon 4 is selected from the group consisting of Gin, Asn and His. 39. The synthase of claim 1 , wherein said R-group associated with said α- carbon 5 is selected from the group consisting of Cys, Ser and Thr. 40. The synthase of claim 1 , wherein said R-group associated with said α- carbon 5 is selected from the group consisting of Phe, Tyr and Tφ. 41. The synthase of claim 1 , wherein said R-group associated with said α- carbon 5 is selected from the group consisting of Pro, Gly, and Ala. 42. The synthase of claim 1 , wherein said R-group associated with said α- carbon 5 is selected from the group consisting of Glu and Asp. 43. The synthase of claim 1 , wherein said R-group associated with said α- carbon 5 is selected from the group consisting of Met, lie, Val and Leu. 44. The synthase of claim 1 , wherein said R-group associated with said α- carbon 5 is selected from the group consisting of Arg and Lys. 45. The synthase of claim 1 , wherein said R-group associated with said α- carbon 5 is selected from the group consisting of Gin, Asn and His. 46. The synthase of claim 1 , wherein said R-group associated with said α- carbon 6 is selected from the group consisting of Cys, Ser and Thr. 47. The synthase of claim 1 , wherein said R-group associated with said α- carbon 6 is selected from the group consisting of Phe, Tyr and Tφ. 48. The synthase of claim 1 , wherein said R-group associated with said α- carbon 6 is selected from the group consisting of Pro, Gly, and Ala. 49. The synthase of claim 1 , wherein said R-group associated with said α- carbon 6 is selected from the group consisting of Glu and Asp. 50. The synthase of claim 1 , wherein said R-group associated with said α- carbon 6 is selected from the group consisting of Met, He, Val and Leu. 51. The synthase of claim 1 , wherein said R-group associated with said α- carbon 6 is selected from the group consisting of Arg and Lys. 52. The synthase of claim 1 , wherein said R-group associated with said α- carbon 6 is selected from the group consisting of Gin, Asn and His. 53. The synthase of claim 1 , wherein said R-group associated with said α- carbon 7 is selected from the group consisting of Cys, Ser and Thr. 54. The synthase of claim 1 , wherein said R-group associated with said α- carbon 7 is selected from the group consisting of Phe, Tyr and Tφ. 55. The synthase of claim 1 , wherein said R-group associated with said α- carbon 7 is selected from the group consisting of Pro, Gly, and Ala. 56. The synthase of claim 1 , wherein said R-group associated with said α- carbon 7 is selected from the group consisting of Glu and Asp. 57. The synthase of claim 1 , wherein said R-group associated with said α- carbon 7 is selected from the group consisting of Met, lie, Val and Leu. 58. The synthase of claim 1 , wherein said R-group associated with said α- carbon 7 is selected from the group consisting of Arg and Lys. 59. The synthase of claim 1 , wherein said R-group associated with said α- carbon 7 is selected from the group consisting of Gin, Asn and His. 60. The synthase of claim 1 , wherein said R-group associated with said α- carbon 8 is selected from the group consisting of Cys, Ser and Thr. 61. The synthase of claim 1 , wherein said R-group associated with said α- carbon 8 is selected from the group consisting of Phe, Tyr and Trp. 62. The synthase of claim 1 , wherein said R-group associated with said α- carbon 8 is selected from the group consisting of Pro, Gly, and Ala. 63. The synthase of claim 1 , wherein said R-group associated with said α- carbon 8 is selected from the group consisting of Glu and Asp. 64. The synthase of claim 1 , wherein said R-group associated with said α- carbon 8 is selected from the group consisting of Met, He, Val and Leu. 65. The synthase of claim 1 , wherein said R-group associated with said α- carbon 8 is selected from the group consisting of Arg and Lys. 66. The synthase of claim 1 , wherein said R-group associated with said α- carbon 8 is selected from the group consisting of Gin, Asn and His. 67. The synthase of claim 1 , wherein said R-group associated with said α- carbon 9 is selected from the group consisting of Cys, Ser and Thr. 68. The synthase of claim 1 , wherein said R-group associated with said α- carbon 9 is selected from the group consisting of Phe, Tyr and Tφ. 69. The synthase of claim 1 , wherein said R-group associated with said α- carbon 9 is selected from the group consisting of Pro, Gly, and Ala. 70. The synthase of claim 1 , wherein said R-group associated with said α- carbon 9 is selected from the group consisting of Glu and Asp. 71. The synthase of claim 1 , wherein said R-group associated with said α- carbon 9 is selected from the group consisting of Met, lie, Val and Leu. 72. The synthase of claim 1 , wherein said R-group associated with said α- carbon 9 is selected from the group consisting of Arg and Lys. 73. The synthase of claim 1 , wherein said R-group associated with said α- carbon 9 is selected from the group consisting of Gin, Asn and His. 74. The synthase of claim 1 , wherein said ordered arrangement of R- groups in said synthase associated with said α-carbons 1 to 9 is Trp, He, Thr, Thr, Tyr, Leu, Cys, Thr and Phe, respectively. 75. The synthase of claim 1 , wherein said ordered arrangement of R- groups in said synthase associated with said α-carbons 1 to 9 is Ser, He, Thr, Thr, Tyr, Leu, Cys, Thr and Tyr, respectively. 76. The synthase of claim 1 , wherein said ordered arrangement of R- groups in said synthase associated with said α-carbons 1 to 9 is Tφ, He, Thr, Thr, Tyr, Leu, Trp, Thr and Tyr, respectively. 77. The synthase of claim 1 , wherein said ordered arrangement of R- groups in said synthase associated with said α-carbons 1 to 9 is Ser, lie, Thr, Thr, Tyr, Leu, Tφ, Thr and Tyr, respectively. 78. The synthase of claim 1 , wherein said ordered arrangement of R- groups in said synthase associated with said α-carbons 1 to 9 is Glu, He, Thr, Thr, Tyr, Leu, Cys, Thr and Tyr, respectively. 79. A teφene synthase made by aligning a primary amino acid sequence of a teφene synthase polypeptide to the amino acid sequence of residues 265 to 535 of SEQ ID NO: 2, mutating a nucleic acid encoding said polypeptide at one or more codons of nine amino acid residues in a region of said polypeptide having 20% or greater sequence identity to residues 265 to 535 of SEQ ID NO: 2, said nine residues in said polypeptide aligning with residues 273, 294, 402, 403, 404, 407, 440, 519 and 520 of SEQ ID NO: 2; and expressing said mutated nucleic acid so that a mutated terpene synthase is made. 80. An isolated terpene synthase having a region with 20% or greater sequence identity to residues 265 to 535 of SEQ ID NO: 2, said synthase comprising sixteen α-carbons, said α-carbons having interatomic distances in Angstroms between said α-carbons that are ±2.3 Angstroms of the following interatomic distances: the center point of each said α-carbon positioned within a sphere having a radius of 2.3 Angstroms, the center points of each said sphere having the following structural coordinates: α-Carbon [ X Position Y Position Z Position Number ! 1 119.144 43.487 44.133 2 120.203 38.695 43.506 3 114.058 43.884 41.015 4 109.327 46.145 41.743 5 110.682 46.410 45.284 6 106.807 36.336 45.151 7 107.629 38.010 41.804 8 109.375 34.842 40.617 9 111.944 37.854 37.602 10 110.233 31.098 47.361 11 115.915 32.218 48.369 12 118.846 34.443 51.796 13 116.461 32.848 54.290 14 114.100 38.006 55.620 15 116.617 41.285 51.702 16 114.855 43.486 54.238 , each said α-carbon having an associated R-group, said synthase having an ordered arrangement of said R-groups other than the following ordered arrangements of R- groups: I a o όin/όόsαiDd LZ£Ll/00OM. 81. The synthase of claim 80, wherein said synthase has 25% or greater sequence identity to residues 265 to 535 of SEQ ID NO: 2. 82. The synthase of claim 81 , wherein said synthase has 35% or greater sequence identity to residues 265 to 535 of SEQ ID NO: 2. 83. The synthase of claim 81 , wherein said synthase catalyses the formation of a terpenoid product from a monoterpene substrate. 84. The synthase of claim 81 , wherein said synthase catalyses the formation of a terpenoid product from a sesquiterpene substrate. 85. The synthase of claim 81 , wherein said synthase catalyses the formation of a teφenoid product from a diteφene substrate. 86. The synthase of claims 83, 84, or 85, wherein said product is a cyclic teφenoid hydrocarbon. 87. The synthase of claim 81 , wherein said ordered arrangement of R-groups in said synthase associated with said α-carbons 1 to 16 is Cys, Trp, He, He, Ser, Thr, Thr, Tyr, Leu, Cys, Val, Thr, Tyr, Asp, Phe and Thr, respectively. 88. An isolated teφene synthase having a region with 20% or greater sequence identity to residues 265 to 535 of SEQ ID NO: 2, said synthase comprising nineteen α-carbons having interatomic distances in Angstroms between said α-carbons that are ±2.3 Angstroms of the following interatomic distances: the center point of each said α-carbon positioned within a sphere having a radius of 2.2 Angstroms, the center points of each said sphere having the following structural coordinates: α-Carbon Number X Position Y Position Z Position 1 119.144 43.487 44133 2 120.203 38.695 43.506 3 114.058 43.884 41015 4 109.327 46.145 41.743 5 110.682 46.410 45.284 6 99.381 42.920 45.148 7 103.445 38.054 44.605 8 106.807 36.336 45.151 9 107.629 38.010 41.804 10 109.375 34.842 40.617 11 111.944 37.854 37.602 12 110.233 31.098 47.361 13 109.178 33.314 52.875 14 115.915 32.218 48.369 15 118.846 34.443 51.796 16 116.461 32.848 54.290 17 114.100 38.006 55.620 18 116.617 41.285 51.702 19 114.855 43.486 54.238 , each said α-carbon having an associated R-group, said synthase having an ordered arrangement of said R-groups other than the following ordered arrangements of R- groups: lHZ/66SflΛLDcI z.zez,ι/oooΛV 89. The synthase of claim 88, wherein said synthase has 25% or greater sequence identity to residues 265 to 535 of SEQ ID NO: 2. 90. The synthase of claim 88, wherein said synthase has 35% or greater sequence identity to residues 265 to 535 of SEQ ID NO: 2. 91. The synthase of claim 88, wherein said synthase catalyses the formation of a terpenoid product from a monoterpene substrate. 92. The synthase of claim 88, wherein said synthase catalyses the formation of a teφenoid product from a sesquiterpene substrate. 93. The synthase of claim 88, wherein said synthase catalyses the formation of a terpenoid product from a diteφene substrate. 94. The synthase of claims 91 , 92, or 93, wherein said product is a cyclic teφenoid hydrocarbon. 95. A isolated protein comprising: a first domain having an amino terminal end and a carboxyl terminal end; said first domain comprising amino acids that align structurally in three-dimensional space with a glycosyl hydrolase catalytic core, said glycosyl hydrolase catalytic core selected from the group consisting of amino acids 36 to 230 of glucoamylase PDB code 3GLY of Aspergillus awamori and amino acids 36 to 230 of endoglucanase CelD PDB code 1CLC; a second domain having an amino terminal end and carboxyl terminal end, said second domain comprising amino acids that align structurally in three-dimensional space with avian FPP synthase, said carboxyl terminal end of said first domain linked to said amino terminal end of said second domain; wherein a region of said second domain has 20% or greater sequence identity to residues 265 to 535 of SEQ ID NO: 2, and wherein said second domain comprises nine α-carbons having interatomic distances in Angstroms between said α-carbons that are ±2.3 Angstroms of the following interatomic distances: the center point of each said α-carbon positioned within a sphere having a radius of 2.2 Angstroms, the center point of each said sphere having the following structural coordinates: , each said α-carbon having an associated R-group, said synthase having an ordered arrangement of R-groups other than the following ordered arrangements of R-groups: O) β .O. .<o 96. The protein of claim 95, wherein said synthase has 25% or greater sequence identity to SEQ ID NO: 2. 97. The protein of claim 96, wherein said synthase has 35% or greater sequence identity to SEQ ID NO: 2. 98. The synthase of claim 95, wherein said synthase catalyses the formation of a terpenoid product from a monoteφene substrate. 99. The synthase of claim 95, wherein said synthase catalyses the formation of a terpenoid product from a sesquiterpene substrate. 100. The synthase of claim 95, wherein said synthase catalyses the formation of a teφenoid product from a diteφene substrate. 101. The synthase of claims 98, 99, or 100, wherein said product is a cyclic teφenoid hydrocarbon. 102. An isolated synthase having a region with 40% or greater sequence identity to residues 343 to 612 of SEQ ID NO: 20, wherein one or more amino acid residues of said synthase that align with amino acids at positions 348, 351 , 372, 375, 376, 454, 479, 480, 481 , 482, 485, 519, 523, 597, 600, 601 , 605, 607 and 608 of SEQ ID NO: 20 are residues other than the following ordered arrangements of residues: 06? IMZ/66Sfl/IOd LZZLimON. 103. An isolated synthase having a region with 40% or greater sequence identity to residues 316 to 586 of SEQ ID NO: 22, wherein one or more amino acid residues of said synthase that align with amino acids at positions 321 , 324, 345, 348, 349, 427, 452, 453, 454, 455, 458, 492, 496, 569, 572, 573, 577, 579 and 580 of SEQ ID NO: 22 are residues other than the following ordered arrangements of residues: 104. An isolated synthase having a region with 40% or greater sequence identity to residues 352 to 622 of SEQ ID NO: 58, wherein one or more amino acid residues of said synthase that align with amino acids at positions 357, 360, 381 , 384, 385, 463, 487, 488, 489, 490, 493, 528, 532, 606, 609, 610, 614, 616 and 617 of SEQ ID NO: 58 are residues other than the following ordered arrangements of residues: 105. An isolated synthase having a region with 40% or greater sequence identity to amino acid residues 272 to 540 encoded by SEQ ID NO: 33, wherein one or more amino acid residues of said synthase that align with amino acids at positions 277, 280, 301 , 304, 305, 383, 408, 409, 410, 411 , 414, 448, 452, 524, 527, 528, 532, 534 and 535 encoded by SEQ ID NO: 33 are residues other than the following ordered arrangements of residues: 106. An isolated synthase having a region with 40% or greater sequence identity to residues 319 to 571 of SEQ ID NO: 42, wherein one or more amino acid residues of said synthase that align with amino acids at positions 324, 327, 348, 351 , 352, 430, 455, 456, 457, 458, 461 , 495, 499, 571 , 574, 575, 579, 581 and 582 of SEQ ID NO: 42 are residues other than the following ordered arrangements of residues: 107. An isolated synthase having a region with 40% or greater sequence identity to residues 579 to 847 of SEQ ID NO: 44, wherein one or more amino acid residues of said synthase that align with amino acids at positions 584, 587, 606, 609, 610, 688, 713, 714, 715, 716, 719, 753, 757, 831 , 834, 835, 839, 841 and 842 of SEQ ID NO: 44 are residues other than the following ordered arrangements of residues: 108. An isolated synthase having a region with 40% or greater sequence identity to residues 495 to 767 of SEQ ID NO: 46, wherein one or more amino acid residues of said synthase that align with amino acids at positions 500, 503, 524, 527, 528, 606, 631 , 632, 633, 634, 637, 674, 678, 751 , 754, 755, 759, 761 and 762 of SEQ ID NO: 46 are residues other than the following ordered arrangements of residues: 109. An isolated synthase having a region with 40% or greater sequence identity to residues 295 to 564 of SEQ ID NO: 48, wherein one or more amino acid residues of said synthase that align with amino acids at positions 300, 303, 324, 327, 328, 406, 431 , 432, 433, 434, 437, 471 , 475, 548, 551 , 552, 556, 558 and 559 of SEQ ID NO: 48 are residues other than the following ordered arrangements of residues: 110. An isolated synthase having a region with 40% or greater sequence identity to residues 307 to 578 of SEQ ID NO: 50, wherein one or more amino acid residues of said synthase that align with amino acids at positions 312, 315, 336, 339, 340, 419, 444, 445, 446, 447, 450, 484, 488, 562, 565, 566, 570, 572 and 573 of SEQ ID NO: 50 are residues other than the following ordered arrangements of residues: 111. An isolated synthase having a region with 40% or greater sequence identity to residues 264 to 533 of SEQ ID NO: 52, wherein one or more amino acid residues of said synthase that align with amino acids at positions 269, 272, 293, 296, 297, 375, 401 , 402, 403, 404, 407, 441 , 445, 517, 520, 521 , 525, 527 and 528 of SEQ ID NO: 52 are residues other than the following ordered arrangements of residues: 112. An isolated synthase having a region with 40% or greater sequence identity to residues 585 to 853 of SEQ ID NO: 56, wherein one or more amino acid residues of said synthase that align with amino acids at positions 590, 593, 614, 617, 618, 696, 721 , 722, 723, 724, 727, 761 , 765, 837, 840, 841 , 845, 847 and 848 of SEQ ID NO: 56 are residues other than the following ordered arrangements of residues: 113. An isolated synthase having a region with 40% or greater sequence identity to residues 307 to 574 of SEQ ID NO: 54, wherein one or more amino acid residues of said synthase that align with amino acids at positions 312, 315, 336, 339, 340, 418, 443, 444, 445, 446, 449, 483, 487, 560, 563, 564, 566, 568 and 569 of SEQ ID NO: 54 are residues other than the following ordered arrangements of residues: 114. An isolated synthase having a region with 40% or greater sequence identity to residues 309 to 577 of SEQ ID NO: 24, wherein one or more amino acid residues of said synthase that align with amino acids at positions 314, 317, 338, 341 , 342, 420, 446, 447, 448, 449, 452, 485, 489, 560, 563, 564, 569, 571 and 572 of SEQ ID NO: 24 are residues other than the following ordered arrangements of residues: 115. An isolated synthase having a region with 40% or greater sequence identity to residues 315 to 584 of SEQ ID NO: 26, wherein one or more amino acid residues of said synthase that align with amino acids at positions 320, 323, 344, 347, 348, 426, 451 , 452, 453, 454, 457, 492, 496, 568, 571 , 572, 576, 578 and 579 of SEQ ID NO: 26 are residues other than the following ordered arrangements of residues: 9τε 8z| C , - θZ2r- ?ζ <-- l -nrτiD DS > -π-πOO -< — 000< -<τι-n> O-< — τιZCOCO OOZC Z>T)r- OOOOOOOj o >>SSSSξ wι β O>2Sr ξMrwr?ξξ$-cSξ-πSS * πSξSξSξSξS?g — > Z >< O>OZ>τι C0>Z — τι — ι-ZZTl<Z-π< |- ι- r- >D O I H H 0 < 2 < Γ- 0 ιθr> ι—< — I- I- — ι— < HH I- H > > £ H H H C0 C0 H C H H H < H H H H H H H < H H H < H H H H < H H O O D H C0C0 C0 C0 C0 C0 C05 -< -<-<-<-< -< -< 222-<-π-< - Z- -π-< -< -< < -< -n-<-π-<- z-<-<>-n-< -<-<-<- -<-< -< M CO C0 CO H H CO H C C Tl CO < Z CO > C0 C0 C0 C CO CO CO CO C > > CO CO ΓΠ H CO CO CO CO CO H H H H OI < I CO CO H -Π -Π > < CO H CO I- CO CO O < C0 — < O C0 H C0 C0 H < > H > O C0 H H O O > > r- O C0 > H θC0 θ > C0 > C0 C0 H θ O r- C0 C0 H O > O O < coOO-<-<2-— ι- ι- Oι- 2-CC02 <Xr-DC0C0<> 2 — "O>-<0> — Z- X — i- 2 i- r- i- < < O — i- < I- — CO < i- H i- r- i- i— 2 H 2 I- I- — I- Γ- CO Γ- O O — 000-Sr-Cθi-OOι-r-OC -πι-r-r- ι-r-OOr-OOcoτι>θ OOOOOOZZZZZ0O020Z0ZDZOZOZODZ0OZZDOZ0ZODODg> > H > — < r- H < r- r- < -π — i- i- i- > -n 2 H C0 > < > — > > ι- < > — 0 > < > > > 22 — < oo 2 H H — CΛ TI -Π -Π -Π < 2 I- I- — < o τι — 2 l - ϊ ffl r ϊ π » r ) r r < r r r -n s -n -<.-<. <<•<■<<-. <<<-<, -<.-<. • --<. -c -<. -c <-<.-. -e. -e. -<.<-<, < ^ DDD DDDD DOD DDDDDDDDD DDDDDDDDΓΠDDΓΠDDDDDDDDDDS τι-πχ -< - r- -< - -π -n-< -< -π-π-< r-χ-< ι- τι χ τι χ D -< τι χ-π-πχ-π -< -<τι-<-< -< -<-< -< -< 2 ; O O H H -< H H H H H C CΛ Z -< O CO H O O O H O O H H D H CΛ H H C H H H H H H --J όinz/όόsα/xod ,zεt,ι/ooo 116. An isolated synthase having a region with 40% or greater sequence identity to residues 265 to 536 of SEQ ID NO: 28, wherein one or more amino acid residues of said synthase that align with amino acids at positions 270, 273, 294, 297, 298, 376, 401 , 402, 403, 404, 407, 440, 444, 518, 521 , 522, 528, 530 and 531 of SEQ ID NO: 28 are residues other than the following ordered arrangements of residues: 8iε g |pjξfc = |g5|5gog- N x S <cHCΛ θ-oθZ2r--χ .-χc>-nmσoo)> -n-πθOO — 000<-<ll-π>-<0-< — τιZCΛC0Oθr> ZC0OZ>TJr-OO OOOOg > > SSS S S >wwco2Sr->S«ι-cor- SSSS-<SS-πSSτιSS ξS S S S S SS - : j -> Z ><O ωθ>ΩZ>-πθC0>Z--π-ι-ZZ-π<Z-n< ι-r-ι- , >D O IHHD<S<r-0 IDr> ι- < — I- I ι- <HHi-H>> __s HHHC0COHCOHHH<HHHHHHH<HHH<HHHH<HHOODHCrtCoe0C0C0C0w8 <<<<-<<<S5ϊ<ιι-< <Z<ιι-C<-< -C<ι <ιι<<Z C0 CO C0 H H CO H CO C0 T) CO < Z CO > C0 C0 CO CO C0 C C0 CO CO > > C0 CΛ HCn Cβ CO CO CΛ -H4 -Ht -t -4 & < I WC0 H -π -π > < CΛH C/> r- CΛ CΛ O < CΛ — < O CΛH CΛ CO H < > H > CO O CO H έ > OCO H H O O > > I- O W O > H O COO > C) CΛ > CO CΛ H O O I- COCΛ H O > 00 < O Cι ) D0<-C2rrr0r0ϊ<»-E<Ir0Cβ»<>ϊ-TI><0>-02<I<-C< — i- 2 i- i- i- < < — ι-<Hi- — Co<ι- ■ I- I- I- S H S Γ- Γ- έ -5δ to * . r-coι-onθ — OOOSr-cnι-O r-r- Cθ-nr-r-ι-Oι-!-ΩOι-OOCΛτι>0>0000 : DDσoσαzzzzzoσθ2ozozαzσzDzoDzoσzzDσzσzooDD * >H> -<ι- H <r-ι-<-π — Γ - I - I - > -Π S H CΛ > < > — >>r- <>-0> <> > >2S — <2 — S H H — cn -n-n-π-π<sr-ι- — <C5-n — s 1 — 2cnr-2 HC0θr-r-<r-ι-ι- HHiv» -<"n-<-<-<-<-<-<-<-< -<-<-<-<-<-<-<-<-n-<-<-<-<-<-<-<-<-<-<;-<-<-<-<-<-<-<-<-<-<-<S σoσσooσσσσσσooσσoσoσαoσσσσσmσσmooσσooσσoσi τιτιl -< - r- -< -< -π-τι -< - τι-π< r- χ -< r- -τι ι -ηχ o -<τι ι -πτιχ-n-< - -n-< < -< -< -c < OO OHH-< -l-| -|HOHC0C0Z -<OC0 H O OOOC7)HOOHHDHC0HHCn HH HHHHW IHΣV66SriΛLDcI t.zεt.1/00 OΛV 117. An isolated synthase having a region with 40% or greater sequence identity to residues 342 to 612 of SEQ ID NO: 30, wherein one or more amino acid residues of said synthase that align with amino acids at positions 347, 350, 371 , 374, 375, 453, 478, 479, 480, 481 , 483, 518, 522, 596, 599, 600, 604, 606 and 607 of SEQ ID NO: 30 are residues other than the following ordered arrangements of residues: E 118. An isolated synthase having a region with about 40% or greater sequence identity to residues 307 to 541 of SEQ ID NO: 32, wherein one or more amino acid residues of said synthase that align with amino acids at positions 278, 281 , 302, 305, 306, 384, 409, 410, 411 , 412, 415, 448, 452, 524, 527, 528, 533, 535 and 536 of SEQ ID NO: 32 are residues other than the following ordered arrangements of residues: E α 119. A method for making a terpene synthase, comprising: a) identifying, in a preselected polypeptide having a region with 20% or greater sequence identity to residues 265 to 535 of SEQ ID NO: 2, nine amino acid residues whose α-carbons have interatomic distances in Angstroms between said α-carbons that are ±2.3 Angstroms of the following interatomic distances: the center point of each said α-carbon positioned within a sphere having a radius of 2.3 Angstroms, the center point of each said sphere having the following structural coordinates: ; and b) synthesizing a polypeptide that is modified from said preselected polypeptide, said modified polypeptide having one or more R-groups associated with said α-carbons other than the R-groups associated with said α-carbons in said preselected polypeptide, wherein said modified polypeptide has teφene synthase activity. 120. The method of claim 119, wherein said synthesizing step comprises the formation of a nucleic acid encoding said preselected polypeptide in which the coding sequence for one or more amino acids corresponding to said nine α-carbons is replaced by a coding sequence that codes for an amino acid different from the amino acid present in said preselected polypeptide. 121. The method of claim 119, wherein said preselected polypeptide is a pinene synthase. 122. The method of claim 121 , wherein said preselected polypeptide is SEQ ID NO: 20. 123. The method of claim 119, wherein said preselected polypeptide is a taxadiene synthase. 124. The method of claim 123, wherein said preselected polypeptide is SEQ ID NO: 44. 125. A method of using a terpene synthase, comprising: a) identifying, in a preselected polypeptide having a region with 20% or greater sequence identity to residues 265 to 535 of SEQ ID NO: 2, amino acid residues at nine positions that align with amino acid residues at positions 273, 294, 402, 403, 404, 407, 440, 519 and 520 of SEQ ID NO: 2; and b) synthesizing a polypeptide that is modified from said preselected polypeptide, said modified polypeptide having amino acid residues at one or more of said nine positions other than the amino acid residues present in said preselected polypeptide. 126. The method of claim 125, wherein said identifying step comprises identifying sixteen amino acid residues in said preselected polypeptide that align with amino acid residues at positions 270, 273, 294, 297, 298, 402, 403, 404, 407, 440, 516, 519, 520, 525, 527 and 528 of SEQ ID NO: 2, and said synthesizing step comprises synthesizing a polypeptide that is modified from said preselected polypeptide, said modified polypeptide having amino acid residues at one or more of said sixteen positions other than the amino acid residues present in said preselected polypeptide. 127. The method of claim 125, wherein said identifying step comprises identifying nineteen amino acid residues in said preselected polypeptide that align with amino acid residues at positions 270, 273, 294, 297, 298, 376, 401 , 402, 403, 404, 407, 440, 444, 516, 519, 520, 525, 527 and 528 of SEQ ID NO: 2, and said synthesizing step comprises synthesizing a polypeptide that is modified from said preselected polypeptide, said modified polypeptide having amino acid residues at one or more of said nineteen positions other than the amino acid residues present in said preselected polypeptide. 128. The method of claim 125, wherein said synthesizing step comprises the formation of a nucleic acid encoding said preselected polypeptide in which the coding sequence in said nucleic acid coding for one or more of said nine amino acid residues is replaced by a coding sequence that codes for an amino acid different from the amino acid present in said preselected polypeptide. 129. The method of claim 125, wherein said preselected polypeptide is a pinene synthase. 130. The method of claim 129, wherein said preselected polypeptide is SEQ ID NO: 20. 131. The method of claim 125, wherein said preselected polypeptide is a taxadiene synthase. 132. The method of claim 131 , wherein said preselected polypeptide is SEQ ID NO: 44. 133. The method of claim 125, further comprising: c) contacting said modified polypeptide with a isoprenoid substrate under conditions effective for said substrate to bind said synthase; and d) measuring the ability of said modified polypeptide to catalyze the formation of a reaction product from said substrate. 134. The method of claim 133, wherein said isoprenoid substrate is a geranyl diphosphate. 135 The method of claim 133, wherein said isoprenoid substrate is a famesyl diphosphate. 136. The method of claim 133, wherein said isoprenoid substrate is a geranyl genanyl diphosphate. 137. A method of making a terpene synthase, comprising: creating a population of nucleic acid molecules that encode polypeptides, said population having members that differ from one another at one or more of nine codons specifying amino acids in a region of a preselected terpene synthase polypeptide having 20% or greater sequence identity to residues 265 to 535 of SEQ ID NO: 2, α-carbons of said nine amino acids having interatomic distances in Angstroms between said α- carbons that are ±2.3 Angstroms of the following interatomic distances: the center point of each said α-carbon positioned within a sphere having a radius of 2.3 Angstroms, the center point of each said sphere having the following structural coordinates: ; and b) expressing at least a portion of said nucleic acid population so that a population of polypeptides is made, wherein at least one member of said population of polypeptides is a mutant teφene synthase. 138. The method of claim 137, wherein said expressing step comprises in vitro transcription and in vitro translation of said nucleic acid populations. 139. The method of claim 137, wherein said expressing step comprises: i) cloning said members of said nucleic acid population into an expression vector; ii) introducing, into host cells, said cloned nucleic acid population members in said expression vector; and iii) expressing said cloned nucleic acid population members in said host cells so that said population of polypeptides is made. 140. The method of claim 139, wherein said host cells are prokaryotic cells. 141. The method of claim 137, wherein said preselected teφene synthase polypeptide is a monoteφene synthase. 142. The method of claim 137, wherein said preselected teφene synthase polypeptide is a sesquiteφene synthase. 143. The method of claim 137, wherein said preselected terpene synthase polypeptide is a diterpene synthase. 144. An isolated nucleic acid encoding the synthase of claim 1. 145. An isolated nucleic acid encoding the synthase of claim 2. 146. An isolated nucleic acid encoding the synthase of claim 3. 147. An isolated nucleic acid encoding the synthase of claim 7. 148. An isolated nucleic acid encoding a synthase selected from the group consisting of the synthase of claims 11 through 73. 149. An isolated nucleic acid encoding the synthase of claim 80. 150. An isolated nucleic acid encoding the synthase of claim 88. 151. An isolated nucleic acid encoding the synthase of claim 95. 152. An isolated nucleic acid encoding a synthase selected from the group consisting of the synthase of claims 102 through 118. 153. A host cell containing a nucleic acid encoding the synthase of claim 1. 154. The host cell of claim 153, wherein said cell is a prokaryotic cell. 155. The host cell of claim 153, wherein said cell is a eukaryotic cell. 156. The host cell of claim 155, wherein said cell is an insect cell. 157. The host cell of claim 155, wherein said cell is a plant cell. 158. The host cell of claim 157, wherein said host cell is an Angiosperm cell. 159. The host cell of claim 157, wherein said host cell is an Gymnosperm cell. 160. The host cell of claim 157, wherein said host cell is selected from the group consisting of: a cell from a Graminaceae plant, a cell from a Legumineae plant, a cell from a Solanaceae plant, a cell from a Brassicaeae plant and a cell from a Conifereae plant. 161. A transgenic plant containing a nucleic acid encoding the synthase of claim 1. 162. A transgenic animal cell culture containing a nucleic acid encoding the synthase of claim 1.

Inventors: CHAPPELL JOSEPH, MANNA KATHLEEN R, NOEL JOSEPH P, STARKS COURTNEY M, CHAPPELL, JOSEPH, MANNA, KATHLEEN, R., NOEL, JOSEPH, P., STARKS, COURTNEY, M.
Applicants: SALK INST FOR BIOLOGICAL STUDI, UNIV KENTUCKY RESEARCH DEPARTM, THE SALK INSTITUTE FOR BIOLOGICAL STUDIES, UNIVERSITY OF KENTUCKY RESEARCH DEPARTMENT
Application year: 1999
Main classification: C12N9
IPC codes: A01H5, C12N1, C12N5, C12N9, C12N15, C12Q1, C12R1, G01N33