Background Art [0002] Human tumor necrosis factors, e. g., TNF-a and TNF-p, are related members of a broad class of polypeptide mediators, which includes the interferons, interleukins and growth factors, collectively called cytokines (Beutler, B. and Cerami, A., Annu. Rev. Immunol. 7: 625-655 (1989) ). Sequence analysis of cytokine receptors has defined several subfamilies of membrane proteins (1) the Ig superfamily, (2) the hematopoietin (cytokine receptor superfamily) and (3) the tumor necrosis factor (TNF) /nerve growth factor (NGF) receptor superfamily. For a review of the TNF superfamily, see Gruss and Dower, Blood 85 : 3378-3404 (1995) and Aggarwal and Natarajan, Eur. Cytokine Netw. 7: 93-124 (1996). The TNF/NGF receptor superfamily contains at least 10 different proteins. Ligands for these receptors have been identified and belong to at least two cytokine superfamilies.

[0003] Some of the known members of the TNF-ligand superfamily include TNF-a, TNF-P (lymphotoxin-a), LT-/3, OX40L, Fas ligand, CD30L, CD27L, CD40L, and 4-IBBL. The ligands, members of the TNF ligand superfamily, are acidic, TNF-like molecules with approximately 20% sequence homology in the extracellular domains (range, 12%-36%) and exist mainly as membrane-bound forms with the biologically active form being a trimeric/multimeric complex.

Soluble forms of the TNF ligand superfamily have only been identified so far for TNF-a, LT- (3, and Fas ligand. For a general review, see Gruss, H. and Dower, S. K., Blood 85 : 3378-3404 (1995). These proteins participate in the regulation of cell proliferation, activation, and differentiation, including control of cell survival or death by apoptosis or cytotoxicity (Armitage, R. J., Curr. Opin. Immunol. 6 : 407 (1994) and Smith, C. A., Cell 75 : 959 (1994)).

[0004] An additional member of the TNF-ligand superfamily has recently been discovered. Neutrokine-alpha (also known as BLySTM (B-Lymphocyte Stimulator); also known as TALL-1, THANK, BAFF, zTNF4, and TNSF13B) is a member of the tumor necrosis factor (TNF) superfamily that induces B cell proliferation and immunoglobulin secretion and appears to be a key regulator of peripheral B cell populations in vivo (Moore et al., Science 285 : 260-263 (1999); Mackay et al., J, Exp. Med. 190 : 1697-1710 (1999) ). Like other members of the TNF family, Neutrokine-alpha is a type-II membrane protein that may be cleaved at the cell surface to form a soluble protein (Mariani et al., J. Cell Biol. 137 : 221- 229 (1997) ). The crystal structures of a number of TNF ligands have been determined (Eck et al., J. Biol. Chem. 267 : 2119-2122 (1992) ; Eck et al., J Biol.

Chem. 264 : 17595-17605 (1989); Hymowitz et al., Biochemistry 39 : 633-640 (2000); Cha et al., J. Biol. Chem. 275 : 31171-31177 (2000); Lam et al., J. Clin.

Invest. 108 : 971-979 (2001) ), two in complex with the respective receptors [Banner et al., Cell 73: 431-445 (1993); Cha et al., J Biol. Chem. 275 : 31171- 31177 (2000); Singhetal., ProteinSci. 7: 1124-1135 (1998); Mongkolsapaya et al., Nat. Struct. Biol. 6 : 1048-1053 (1999) ). While the TNF ligand family shows significant sequence diversity, members are closely related in terms of their structures. All ligands described so far are active as trimers, and Neutrokine- alpha has activity as a trimer as well. l0005] Like other members of the TNF family, Neutrokine-alpha is a ligand that interacts with several receptors. Neutrokine-alpha was initially shown to interact with TACI (trans-membrane activator and CAML interactor) and BCMA (B cell maturation antigen) (Gross et al., Nature 404 : 995-999 (2000) ). Both receptors were found to bind APRIL as well [Marsters et al., Curr. Biol. 10 : 785-788 (2000); Wu et al., J. Biol. Chem. 275 : 35478-35485 (2000) ), APRIL being the TNF-like ligand that has the highest degree of sequence homology with Neutrokine-alpha. Most recently, a third receptor, termed BAFF-R, has been identified. This receptor apparently does not interact with APRIL or any TNF-like ligand other than Neutrokine-alpha (Thompson et al., Science 293 : 2108-2111 (2001) ). Experiments using transgenic animals have shown that the interaction of Neutrokine-alpha with TACI and BCMA plays a role in the development of autoimmune disease (Gross et al., Nature 404 : 995-999 (2000)).

At the same time, Neutrokine-alpha is a crucial factor for the normal development of B cells, and apparently this function is mediated through a B CMA-independent pathway (Schiemann et al., Science 293 : 2111-2114 (2001).

[0006] The biological actions of Neutrokine-alpha suggest several potential therapies in which the action of Neutrokine-alpha is mimicked or enhanced. For example, common variable immunodeficiency (CVID) is a group of immunodeficiency syndromes in which B cell immunity is abnormal. Most patients have normal or near-normal numbers of circulating B cells, but the cells fail to differentiate into effective plasma B cells. As a result, patients have low or undetectable amounts of serum antibodies. The condition may result from insufficient stimulation of B cells rather than from a failure intrinsic to B cells (Rosen et al., New Eng. J Med 333 : 7 (1995) ). Most patients with CVID experience acute, recurring bacterial infections, including pneumonia, bronchitis, and sinusitis ("Immune Deficiency and Allied Disorders: Clinical Updates," Immune Deficiency Foundation Vol. II, Issue 1, July 1995). Current treatment involves regular administration of intravenous antibodies, which are prepared from pooled blood samples from thousands of individual donors. The administration of Neutrokine-alpha protein may boost antibody levels in patients with CVID, as well as in other immunodeficiency conditions that effectively mimic CVID. l0007] Immunoglobulin-A deficiency is a disorder of the immune system characterized by increased susceptibility to infection. Patients with this disease fail to produce normal amounts of immunoglobulin-A, which provides the first line of defense for the inner surfaces of the body against infections of the lung, the intestine, the mouth, the urogenital tract, and other areas lined by mucosal membranes. It is believed that immunoglobulin-A deficiency may result from the failure of the B lymphocyte to mature into plasma cells that produce immunoglobulin-A antibodies. Symptomatic patients suffer from recurrent and serious infections, including infections of the gastrointestinal tract, lungs and sinuses, as well as allergic disorders, epilepsy, and cancer. There are currently no available therapies that address the underlying cause of immunoglobulin-A deficiency. Treatment with Neutrokine-alpha may help immunoglobulin-A deficient patients produce their own antibodies. The Neutrokine-alpha protein is known to be able to stimulate B cells to produce immunoglobulin-A antibodies as well as other types of antibodies. Preclinical studies have also shown that Neutrokine-alpha proteins can stimulate the B cells of some immunoglobulin-A deficient patients to enhance the production of immunoglobulin-A antibodies.

[0008] Several types of cancer, including chronic lymphocytic leukemia and multiple myeloma, affect the immune system's ability to fight off infections by impairing antibody production. Neutrokine-alpha may help these patients fend off infectious disease. Cancer therapies also damage the immune system. In some cases it may take years for the full antibody response to recover following cancer treatment. Treatment with Neutrokine-alpha after cancer therapy may speed recovery of a fully competent immune system.

[0009] Other uses of Neutrokine-alpha include treating patients that receive immunosuppressive drugs that make them vulnerable to infections; treating patients infected with antibiotic-resistant bacteria; use as a vaccine adjuvant; use as Neutrokine-alpha linked to radionucleotides that have potential application as therapy for B-cell malignancies such as non-Hodgkin's lymphoma, chronic lymphocytic leukemia, and multiple myeloma.

[0010] Compounds that prevent or inhibit the activity of Neutrokine-alpha also have therapeutic uses. The positive regulatory effects of Neutrokine-alpha on B cells and on T-cell-dependent humoral responses, the autoimmune phenotype of Neutrokine-alpha transgenic mice, and the high levels of Neutrokine-alpha in lupus-prone mice suggest that blocking the interaction betweenNeutrokine-alpha and its receptors may be a useful therapeutic approach in lupus.

[0011] Additionally, the immune system has to distinguish the body's own cells and tissues from those of pathogens so that it can avoid attacking itself while maintaining a diverse repertoire of antibodies. Abnormalities in the induction or maintenance of self-tolerance-the process that prevents the immune system from attacking the body's own tissues-can lead to inflammatory immune responses developing against self-antigens and thus to autoimmune disease.

B cells that produce antibodies that recognize parts of the normal body play an important role in many autoimmune diseases. Systemic lupus erythromatosus, rheumatoid arthritis, multiple sclerosis, Crohn's disease, diabetes, and some forms of asthma are all examples of autoimmune diseases. Thus, agents that inhibit the proliferation of B cells, i. e., antagonists of Neutrokine-alpha activity, have potential to treat or prevent diseases such as systemic lupus erythromatosus, rheumatoid arthritis, multiple sclerosis, Crohn's disease, diabetes, Wegener's granulomatous, myasthenia gravis, and some forms of asthma.

[0012] Although Neutrokine-alpha may be used as an effective agent to treat some of the aforementioned conditions, there exists a need for additional, effective therapeutic agents that mimic the biological activity of Neutrokine- alpha. Moreover, there exists the need for additional, effective therapeutic agents that inhibit the biological activity of Neutrokine-alpha. The three dimensional structure of a Neutrokine-alpha protein would permit the more efficient development and design of both agonists and antagonists of Neutrokine-alpha.

Additionally, the three dimensional structure of Neutrokine-alpha would allow the elucidation of the three-dimensional structures of related proteins. Moreover, computer systems comprising the three-dimensional structure of a Neutrokine- alpha protein would facilitate the preparation of biologically active molecules that are useful for the above indications.

SUMMARY OF THE INVENTION [0013] One aspect of the present invention is a Neutrokine-alpha protein in crystalline form. In particular, human Neutrokine-alpha protein in crystalline form is one aspect of the present invention.

[0014] An additional aspect of the present invention is a composition comprising a Neutrokine-alpha protein, wherein said composition is suitable for forming Neutrokine-alpha in crystalline form.

[0015] Another aspect of the present invention is a method of crystallizing a Neutrokine-alpha protein. The crystallized Neutrokine-alpha protein can be analyzed to provide X-ray diffraction patterns of sufficiently high resolution to be useful for determining the three-dimensional protein structure.

[0016] Another aspect of the present invention is directed to determining the three-dimensional structure of a Neutrokine-alpha protein by using X-ray diffraction crystallography methods. The X-ray diffraction patterns can be either analyzed directly to provide the three-dimensional structure (if sufficient data is collected), or atomic coordinates for the crystallized Neutrokine-alpha, as provided herein, can be used for structure determination.

[0017] An additional aspect of the present invention is a method of determining the three-dimensional structure of a Neutrokine-alpha protein by using the atomic coordinates of human Neutrokine-alpha protein in crystalline form. The atomic coordinates ofhumanNeutrokine-alphaprotein in crystalline form and the amino acid sequence of a second Neutrokine-alpha protein are entered into one or more computer programs for molecular modeling. Such molecular modeling programs generate atomic coordinates that reflect the secondary, tertiary, and/or quaternary structures of the protein which contribute to its overall three-dimensional structure and provide information related to binding and/or active sites of the second Neutrokine-alpha protein.

[0018] An additional aspect of the present invention is a method of designing a biologically active compound that enhances, mimics, inhibits, or antagonizes the activity of a Neutrokine-alpha protein. The three-dimensional structure of a Neutrokine-alpha protein is used to design said biologically active compound.

Additionally, said biologically active compound is optionally synthesized and optionally assayed to test for biological activity.

[0019] Another aspect of the present invention is a computer-readable medium comprising the three-dimensional structure of a Neutrokine-alpha protein. An additional aspect of the present invention is a computer system comprising a memory and a processor, wherein said memory comprises the three-dimensional structure of a Neutrokine-alpha protein BRIEF DESCRIPTION OF THE FIGURES [0020] Figure 1 provides the sequence of soluble human Neutrokine-alpha. Also provided is a structure-based sequence alignment of human Neutrokine-alpha with other members of the cytokine family, including TNF-a, TNF-P, TRAIL, CD40L, and RANKL. Figure 1 additionally displays a ribbon diagram of the three-dimensional structure of a monomer of human Neutrokine-alpha.

[0021] Figures 2A, 2B, 2C and 2D provide ribbon diagrams of three dimensional structure of trimerized human Neutrokine-alpha. Figure 2A depicts a hydrated magnesium ion at the center of the trimer. Figure 2B'additionally provides a more detailed view of the bound magnesium ions along with certain amino acid residues of Neutrokine-alpha. Figure 2E shows a portion of the electron density map determined from the X-ray diffraction data. Specifically, Figure 2E details the region of the disulfide bond between residues 232 and 245.

[0022] Figure 3 provides images of the three-dimensional structures, including the solvent accessible surface, of Neutrokine-alpha, TNF-oc, TNF-p, TRAIL, CD40L, and RANKL. The arrows in the images point to areas on the surface of the protein, and illustrate how the structure of Neutrokine-alpha is unique among the proteins.

[0023] Figure 4 provides the image of three-dimensional structures of TNF- (3/TNF-R complex; TRAIL/DR5 complex; Neutrokine-alpha; and Neutrokine-alpha rotated 90° about the x-axis. Additionally, the residues of Neutrokine-alpha comprising the putative receptor-binding site (the"groove") are listed. The residues of each of the receptors that are believed to comprise the binding site for cytokine ligand are listed for each of TNF-R, DR5, TNR2, BAFF-R, BCMA, and TACI.

[0024] Figure 5 provides the results of a receptor binding study by SELDI affinity mass spectrometry. The results show that, for the interaction of Neutrokine-alpha with both recombinant BCMA and TACI receptors, the AA" and the DE loops of the molecule are centrally involved.

[0025] Figure 6 provides the structure of a computer system as described herein.

[0026] Figure 7 provides the image of solvent accessible surface of a trimer of monomers of Neutrokine-alpha. Additionally, several of the amino acids which compose a major groove are indicated. This major groove is herein identified as a target for drug design or identification using the methods disclosed herein.

[0027] Figure 8 provides the image of the solvent accessible surface of a trimer of monomers of hNeutrokine-alpha. The image in Figure 8 is of the same protein structure as in Figure 7 but from a different perspective, rotated approximately 90° along one axis. Additionally, several of the amino acids which compose grooves on the surface are indicated. These grooves are herein identified as a target for drug design or identification using the methods disclosed herein.

[0028] Figure 9 provides the image of the solvent accessible surface of a monomer of hNeutrokine-alpha. The major portion that is visible in the image represent the surface of the monomer that participates in trimerization of monomers. Several amino acids which compose grooves on the surface are indicated. The areas identified in the figure are herein indicated as being useful for drug design or identification using the methods disclosed herein.

[0029] Figures 10A and 10B provide the graphical results of neutrokine- alpha/receptor interactions. 10A. Superimposed TNF-receptor peptide (TNF-R) (ribbon) docked on neutrokine-alpha surface representation, with TNF-R peptide shown binding to major surface groove. The middle image of I OA is the same but rotated 90 degrees. On the right, groove residues in common between hneutrokine-alpha and APRIL are colored in shaded. The residues forming the groove from adjacent monomers are GLN148, ILE150, ALA151, ASP152, SER153, GLU154, LEU169, LEU170, PHE172, LEU200, THR202, ILE270, SER271, LEU272, ASP273, GLU274, ASP275, and PHE278 from one monomer, and THR190, TYR192, ALA207, GLY209, HIS210, LEU211, GLN213, ARG214, LYS216, HIS218, PHE220, ASP222, GLU223, LEU224, LEU226, VAL227, THR228, LEU229, PHE230, ARG231, ILE233, ALA251, LYS252, LEU253, GLU254, and ASP257 from another monomer. Those in common with APRIL are underlined. FiglOB. PAWS coverage analysis, mapping fragments found in SELDI binding assays of TACI and BMCA to areas in the neutrokine- alpha sequence. Boxes highlight areas of strongest coverage. Binding site mapping was done by in situ trypsin digestion of the captured ligand, followed by mass spectrometric identification of retained fragments. Arrows indicate neutrokine-alpha beta-strands.

DETAILED DESCRIPTION OF THE INVENTION [0030] The present invention provides a Neutrokine-alpha protein in crystalline form. A Neutrokine-alpha protein in crystalline form has the characteristics as described herein. The space group of said Neutrokine-alpha protein in crystalline form is preferably hexagonal. The unit cell dimensions of said space group are defined by a, b, c, a, ß, and y, wherein a is from about 120 A to about 125 A, b is from about 120 A to about 125 A, and c is from about 158 A to about 164 A, ex is from about 85 to about 95, f3 is from about 85 to about 95, and y is from about 115 to about 125. Preferably, a is about 90, (3 is about 90, and y is about 120.

[0031] A Neutrokine-alpha protein in crystalline form can also be characterized by crystal density measurements using Ficoll gradients (Z). According to the present invention, Z is from about 1 to about 12. Preferably, Z is about 6, indicating that there are six Neutrokine-alpha monomers per asymmetric unit.

For more details regarding Ficoll gradients, see Westbrook, E. M. Methods Enzymol. 114 : 187-96 (1. 985).

[0032] A Neutrokine-alpha protein in crystalline form can also be characterized by Matthew's coefficient. For a Neutrokine-alpha protein in crystalline form according to the present invention, Matthew's coefficient is from about 2 A'per Dalton (Da) to about 5 A'per Da. Preferably, Matthew's coefficient is from about 3 A3 per Da to about 4 A'per Da. Preferably, Matthew's coefficient is about 3. 1,3. 2,3. 3,3. 4,3. 5,3. 6,3. 7,3. 8, or 3. 9 A'per Da to about 4 A'per Da' Preferably, Matthew's coefficient is about 3.58 A3 per Da. Solvent content is from about 40% to about 90%, preferably from about 55% to about 75%, preferably about 65%.

[0033] As used herein, the term"Neutrokine-alpha protein"includes naturally and recombinantly produced Neutrokine-alpha proteins; natural, synthetic, and recombinant biologically active polypeptide fragments of Neutrokine-alpha protein; biologically active polypeptide variants of Neutrokine-alpha protein or fragments thereof, including hybrid fusion proteins and dimers; biologically active polypeptide analogs of Neutrokine-alpha protein or fragments or variants thereof, including cysteine-substituted analogs. The Neutrokine-alpha protein may be generated and/or isolated by any means known in the art. Neutrokine- alpha proteins and methods of producing Neutrokine-alpha proteins are disclosed in U. S. Pat. Appl. Nos. 60/225,628, filed August 15,2000 ; 60/227,008, filed August 23,2000 ; 60/234,338, filed September 22,2000 ; 60/240,806, filed October 17,2000 ; 60/250,020, filedNovember30, 2000; 60/276,248, filed March 6,2001 ; 60/293,499, filed May 25,2001 ; 60/296, 122, filed June 7,2001 ; and 60/304, 809, filed July, 13 2001 ; all of which are fully incorporated by reference herein.

[0034] Preferably, the Neutrokine-alpha protein is a protein comprising, or alternatively consisting of, the sequence listed in Table 5, or is a homologue of the protein comprising, or alternatively consisting of, the sequence listed in Table 5.

[0035] The term"hNeutrokine-alpha"refers to human Neutrokine-alpha and preferentially refers to a protein comprising, or alternatively consisting of, the sequence listed in Table 5.

[0036] A homologue is a protein that may include one or more amino acid substitutions, deletions, or additions, either from natural mutations of human manipulation. Thus, a Neutrokine-alpha protein in crystalline form may include one or more amino acid substitutions, deletions or additions, either from natural mutations or human manipulation. As indicated, changes are preferably of a minor nature, such as conservative amino acid substitutions that do not significantly affect the folding or activity of the protein (see Table 1).

TABLE 1. Conservative Amino Acid Substitutions. Amino Acid Type Examples of Amino Acids Aromatic Phenylalanine, Tryptophan, Tyrosine, Histidine Hydrophobic Leucine, Isoleucine, Valine, Methionine, Histidine Polar Glutamine, Asparagine, Serine, Cysteine, Threonine Basic Arginine, Lysine, Histidine Acidic Aspartic Acid, Glutamic Acid Small Alanine, Serine, Threonine, Methionine, Glycine [0037] In one embodiment of the invention, a Neutrokine-alpha protein in crystalline form comprises, or alternatively consists of, the amino acid sequence of a Neutrokine-alpha having an amino acid sequence which contains at least one conservative amino acid substitution, but not more than 50 conservative amino acid substitutions, even more preferably, not more than 40 conservative amino acid substitutions, still more preferably, not more than 30 conservative amino acid substitutions, and still even more preferably, not more than 20 conservative amino acid substitutions. Of course, in order of ever-increasing preference, it is highly preferable for the Neutrokine-alpha protein to have an amino acid sequence which comprises the amino acid sequence of human Neutrokine-alpha, which contains at least one, but not more than 10,9, 8,7, 6,5, 4,3, 2 or 1 conservative amino acid substitutions.

[0038] For example, site directed changes at the amino acid level of a Neutrokine-alpha protein can be made by replacing a particular amino acid with a conservative substitution. Preferred conservative substitution mutations of the Neutrokine-alpha amino acid sequence provided in Table 5 include: T141 replaced with A, G, I, L, S, M, or V; V142 replaced with A, G, I, L, S, T, or M; T143 replaced with A, G, I, L, S, M, or V; Q144 replaced withN ; D145 replaced with E; L147 replaced with A, G, I, S, T, M, or V; Q148 replaced with N ; L149 replaced with A, G, I, S, T, M, or V; I150 replaced with A, G, L, S, T, M, or V; Al 51 replaced with G, I, L, S, T, M, or V; D 152 replaced with E; S 153 replaced with A, G, I, L, T, M, or V; E154 replaced with D; T155 replaced with A, G, I, L, S, M, or V; T157 replaced with A, G, I, L, S, M, or V; I158 replaced with A, G, L, S, T, M, or V; Q159 replaced with N; K160 replaced with H, or R; G161 replaced with A, I, L, S, T, M, or V; S162 replaced with A, G, I, L, T, M, or V; Y163 replaced with F, or W; T164 replaced with A, G, I, L, S, M, or V; F165 replaced with W, or Y; V 166 replaced with A, G, I, L, S, T, or M; W 168 replaced with F, or Y; L169 replaced with A, G, I, S, T, M, or V; L170 replaced with A, G, I, S, T, M, or V; S 171 replaced with A, G, I, L, T, M, or V; F172 replaced with W, or Y; K173 replaced with H, or R; R174 replaced with H, or K; G175 replaced with A, I, L, S, T, M, or V; S176 replaced with A, G, I, L, T, M, or V; A177 replaced with G, I, L, S, T, M, or V; L178 replaced with A, G, I, S, T, M, or V; E179 replaced with D; El 80 replaced with D; K181 replaced with H, or R; E182 replaced with D; N183 replaced with Q; Kl 84 replaced with H, or R; I185 replaced with A, G, L, S, T, M, or V; L 186 replaced with A, G, I, S, T, M, or V; V187 replaced with A, G, I, L, S, T, or M; K188 replaced with H, or R; E189 replaced with D ; T190 replaced with A, G, I, L, S, M, or V ; G191 replaced with A, I, L, S, T, M, or V; Y192 replaced with F, or W; F193 replaced with W, or Y; F194 replaced with W, or Y; I195 replaced with A, G, L, S, T, M, or V; Y196 replaced with F, or W; G197 replaced with A, I, L, S, T, M, or V; Q 198 replaced with N; V 199 replaced with A, G, I, L, S, T, or M; L200 replaced with A, G, I, S, T, M, or V ; Y201 replaced with F, or W; T202 replaced with A, G, I, L, S, M, or V; D203 replaced with E; K204 replaced with H, or R; T205 replaced with A, G, I, L, S, M, or V; Y206 replaced with F, or W; A207 replaced with G, I, L, S, T, M, or V; M208 replaced with A, G, I, L, S, T, or V; G209 replaced with A, I, L, S, T, M, or V; H210 replaced with K, or R; L211 replaced with A, G, I, S, T, M, or V ; I212 replaced with A, G, L, S, T, M, or V ; Q213 replaced with N ; R214 replaced with H, or K ; K215 replaced with H, or R; K216 replaced with H, or R; V217 replaced with A, G, I, L, S, T, or M; H218 replaced with K, or R; V219 replaced with A, G, I, L, S, T, or M; F220 replaced with W, or Y; G221 replaced with A, I, L, S, T, M, or V; D222 replaced with E; E223 replaced with D; L224 replaced with A, G, I, S, T, M, or V; S225 replaced with A, G, I, L, T, M, or V; L226 replaced with A, G, I, S, T, M, or V; V227 replaced with A, G, I, L, S, T, or M; T228 replaced with A, G, I, L, S, M, or V; L229 replaced with A, G, I, S, T, M, or V; F230 replaced with W, or Y; R231 replaced with H, or K; I233 replaced with A, G, L, S, T, M, or V; Q234 replaced with N ; N235 replaced with Q; M236 replaced with A, G, I, L, S, T, or V; E238 replaced with D; T239 replaced with A, G, I, L, S, M, or V; L240 replaced with A, G, I, S, T, M, or V; N242 replaced with Q; N243 replaced with Q; S244 replaced with A, G, I, L, T, M, or V; Y246 replaced with F, or W; S247 replaced with A, G, I, L, T, M, or V ; A248 replaced with G, I, L, S, T, M, or V; G249 replaced with A, I, L, S, T, M, or V; I250 replaced with A, G, L, S, T, M, or V; A251 replaced with G, I, L, S, T, M, or V; K252 replaced with H, or R; L253 replaced with A, G, I, S, T, M, or V; E254 replaced with D; E255 replaced with D; G256 replaced with A, I, L, S, T, M, or V; D257 replaced with E; E258 replaced with D; L259 replaced with A, G, I, S, T, M, or V; Q260 replaced with N; L261 replaced with A, G, I, S, T, M, or V; A262 replaced with G, I, L, S, T, M, or V; I263 replaced with A, G, L, S, T, M, or V; R265 replaced with H, or K; E266 replaced with D; N267 replaced with Q; A268 replaced with G, I, L, S, T, M, or V; Q269 replaced with N; I270 replaced with A, G, L, S, T, M, or V; S271 replaced with A, G, I, L, T, M, or V; L272 replaced with A, G, I, S, T, M, or V; D273 replaced with E; G274 replaced with A, I, L, S, T, M, or V; D275 replaced with E; V276 replaced with A, G, I, L, S, T, or M; T277 replaced with A, G, I, L, S, M, or V; F278 replaced with W, or Y; F279 replaced with W, or Y; G280 replaced with A, I, L, S, T, M, or V; A281 replaced with G, I, L, S, T, M, or V; L282 replaced with A, G, I, S, T, M, or V ; K283 replaced with H, or R; L284 replaced with A, G, I, S, T, M, or V; and/or L285 replaced with A, G, I, S, T, M, or V. The resulting Neutrokine-alpha proteins may be routinely screened for Neutrokine-alpha functional activity and/or physical properties (such as, for example, enhanced or reduced stability and/or solubility). The resulting Neutrokine-alpha proteins may be used according the present invention as described herein.

[0039] In another embodiment, the invention provides for a Neutrokine-alpha protein in crystalline form having amino acid sequences containing non-conservative substitutions of the amino acid sequence provided in Table 5.

For example, non-conservative substitutions of the Neutrokine-alpha protein sequence provided in Table 5 include: T141 replaced with D, E, H, K, R, N, Q, F, W, Y, P, or C; V 142 replaced with D, E, H, K, R, N, Q, F, W, Y, P, or C; T143 replaced with D, E, H, K, R, N, Q, F, W, Y, P, or C; Q144 replaced with D, E, H, K, R, A, G, I, L, S, T, M, V, F, W, Y, P, or C ; D 145 replaced with H, K, R, A, G, I, L, S, T, M, V, N, Q, F, W, Y, P, or C ; C 146 replaced with D, E, H, K, R, A, G, I, L, S, T, M, V, N, Q, F, W, Y, or P; L147 replaced with D, E, H, K, R, N, Q, F, W, Y, P, or C; Q148 replaced with D, E, H, K, R, A, G, I, L, S, T, M, V, F, W, Y, P, or C; L149 replaced with D, E, H, K, R, N, Q, F, W, Y, P, or C; I150 replaced with D, E, H, K, R, N, Q, F, W, Y, P, or C; Al 51 replaced with D, E, H, K, R, N, Q, F, W, Y, P, or C ;D152 replaced with H, K, R, A, G, I, L, S, T, M, V, N, Q, F, W, Y, P, or C; S153 replaced with D, E, H, K, R, N, Q, F, W, Y, P, or C; E 154 replaced with H, K, R, A, G, I, L, S, T, M, V, N, Q, F, W, Y, P, or C ; Tl 55 replaced with D, E, H, K, R, N, Q, F, W, Y, P, or C; P 156 replaced with D, E, H, K, R, A, G, I, L, S, T, M, V, N, Q, F, W, Y, or C ; T157 replaced with D, E, H, K, R, N, Q, F, W, Y, P, or C ; 115 8 replaced with D, E, H, K, R, N, Q, F, W, Y, P, or C; Q 159 replaced with D, E, H, K, R, A, G, I, L, S, T, M, V, F, W, Y, P, or C ; K160 replaced with D, E, A, G, I, L, S, T, M, V, N, Q, F, W, Y, P, or C ; G161 replaced with D, E, H, K, R, N, Q, F, W, Y, P, or C ; S 162 replaced with D, E, H, K, R, N, Q, F, W, Y, P, or C; Y163 replaced with D, E, H, K, R, N, Q, A, G, I, L, S, T, M, V, P, or C ; T164 replaced with D, E, H, K, R, N, Q, F, W, Y, P, or C ; F165 replaced with D, E, H, K, R, N, Q, A, G, I, L, S, T, M, V, P, or C ; V 166 replaced with D, E, H, K, R, N, Q, F, W, Y, P, or C; P 167 replaced with D, E, H, K, R, A, G, I, L, S, T, M, V, N, Q, F, W, Y, or C ; W168 replaced with D, E, H, K, R, N, Q, A, G, I, L, S, T, M, V, P, or C ; L 169 replaced with D, E, H, K, R, N, Q, F, W, Y, P, or C ; L 170 replaced with D, E, H, K, R, N, Q, F, W, Y, P, or C; S171 replaced with D, E, H, K, R, N, Q, F, W, Y, P, or C; F172 replaced with D, E, H, K, R, N, Q, A, G, I, L, S, T, M, V, P, or C ; K173 replaced with D, E, A, G, I, L, S, T, M, V, N, Q, F, W, Y, P, or C ; R174 replaced with D, E, A, G, I, L, S, T, M, V, N, Q, F, W, Y, P, or C; G175 replaced with D, E, H, K, R, N, Q, F, W, Y, P, or C ; S 176 replaced with D, E, H, K, R, N, Q, F, W, Y, P, or C ; Al 77 replaced with D, E, H, K, R, N, Q, F, W, Y, P, or C ; D178 replaced with D, E, H, K, R, N, Q, F, W, Y, P, or C; El 79 replaced with H, K, R, A, G, I, L, S, T, M, V, N, Q, F, W, Y, P, or C; El 80 replaced with H, K, R, A, G, I, L, S, T, M, V, N, Q, F, W, Y, P, or C ; K181 replaced with D, E, A, G, I, L, S, T, M, V, N, Q, F, W, Y, P, or C; E182 replaced with H, K, R, A, G, I, L, S, T, M, V, N, Q, F, W, Y, P, or C ; N183 replaced with D, E, H, K, R, A, G, I, L, S, T, M, V, F, W, Y, P, or C ; K184 replaced with D, E, A, G, I, L, S, T, M, V, N, Q, F, W, Y, P, or C ; I185 replaced with D, E, H, K, R, N, Q, F, W, Y, P, or C; L 186 replaced with D, E, H, K, R, N, Q, F, W, Y, P, or C ; V 187 replaced with D, E, H, K, R, N, Q, F, W, Y, P, or C; Kl 88 replaced with D, E, A, G, I, L, S, T, M, V, N, Q, F, W, Y, P, or C; E189 replaced with H, K, R, A, G, I, L, S, T, M, V, N, Q, F, W, Y, P, or C; T190 replaced with D, E, H, K, R, N, Q, F, W, Y, P, or C; G191 replaced with D, E, H, K, R, N, Q, F, W, Y, P, or C; Y192 replaced with D, E, H, K, R, N, Q, A, G, I, L, S, T, M, V, P, or C; F193 replaced with D, E, H, K, R, N, Q, A, G, I, L, S, T, M, V, P, or C ; F 194 replaced with D, E, H, K, R, N, Q, A, G, I, L, S, T, M, V, P, or C; I195 replaced with D, E, H, K, R, N, Q, F, W, Y, P, or C; Y196 replaced with D, E, H, K, R, N, Q, A, G, I, L, S, T, M, V, P, or C; G197 replaced with D, E, H, K, R, N, Q, F, W, Y, P, or C ; Q198 replaced with D, E, H, K, R, A, G, I, L, S, T, M, V, F, W, Y, P, or C; V 199 replaced with D, E, H, K, R, N, Q, F, W, Y, P, or C; L200 replaced with D, E, H, K, R, N, Q, F, W, Y, P, or C; Y201 replaced with D, E, H, K, R, N, Q, A, G, I, L, S, T, M, V, P, or C; T202 replaced with D, E, H, K, R, N, Q, F, W, Y, P, or C ; D203 replaced with H, K, R, A, G, I, L, S, T, M, V, N, Q, F, W, Y, P, or C ; K204 replaced with D, E, A, G, I, L, S, T, M, V, N, Q, F, W, Y, P, or C ; T205 replaced with D, E, H, K, R, N, Q, F, W, Y, P, or C; Y206 replaced with D, E, H, K, R, N, Q, A, G, I, L, S, T, M, V, P, or C ; A207 replaced with D, E, H, K, R, N, Q, F, W, Y, P, or C; M208 replaced with D, E, H, K, R, N, Q, F, W, Y, P, or C; G209 replaced with D, E, H, K, R, N, Q, F, W, Y, P, or C ; H210 replaced with D, E, A, G, I, L, S, T, M, V, N, Q, F, W, Y, P, or C; L211 replaced with D, E, H, K, R, N, Q, F, W, Y, P, or C; I212 replaced with D, E, H, K, R, N, Q, F, W, Y, P, or C; Q213 replaced with D, E, H, K, R, A, G, I, L, S, T, M, V, F, W, Y, P, or C; R214 replaced with D, E, A, G, I, L, S, T, M, V, N, Q, F, W, Y, P, or C; K215 replaced with D, E, A, G, I, L, S, T, M, V, N, Q, F, W, Y, P, or C; K216 replaced with D, E, A, G, I, L, S, T, M, V, N, Q, F, W, Y, P, or C; V217 replaced with D, E, H, K, R, N, Q, F, W, Y, P, or C; H218 replaced with D, E, A, G, I, L, S, T, M, V, N, Q, F, W, Y, P, or C; V219 replaced with D, E, H, K, R, N, Q, F, W, Y, P, or C ; F220 replaced with D, E, H, K, R, N, Q, A, G, I, L, S, T, M, V, P, or C ; G221 replaced with D, E, H, K, R, N, Q, F, W, Y, P, or C; D222 replaced with H, K, R, A, G, I, L, S, T, M, V, N, Q, F, W, Y, P, or C ; E223 replaced with H, K, R, A, G, I, L, S, T, M, V, N, Q, F, W, Y, P, or C; L224 replaced with D, E, H, K, R, N, Q, F, W, Y, P, or C; S225 replaced with D, E, H, K, R, N, Q, F, W, Y, P, or C; L226 replaced with D, E, H, K, R, N, Q, F, W, Y, P, or C; V227 replaced with D, E, H, K, R, N, Q, F, W, Y, P, or C; T228 replaced with D, E, H, K, R, N, Q, F, W, Y, P, or C; L229 replaced with D, E, H, K, R, N, Q, F, W, Y, P, or C ; F230 replaced with D, E, H, K, R, N, Q, A, G, I, L, S, T, M, V, P, or C ; R231 replaced with D, E, A, G, I, L, S, T, M, V, N, Q, F, W, Y, P, or C ; C232 replaced with D, E, H, K, R, A, G, I, L, S, T, M, V, N, Q, F, W, Y, or P; I233 replaced with D, E, H, K, R, N, Q, F, W, Y, P, or C; Q234 replaced with D, E, H, K, R, A, G, I, L, S, T, M, V, F, W, Y, P, or C; N235 replaced with D, E, H, K, R, A, G, I, L, S, T, M, V, F, W, Y, P, or C ; M236 replaced with D, E, H, K, R, N, Q, F, W, Y, P, or C ; P237 replaced with D, E, H, K, R, A, G, 1, L, S, T, M, V, N, Q, F, W, Y, or C ; E23 8 replaced with H, K, R, A, G, I, L, S, T, M, V, N, Q, F, W, Y, P, or C ; T239 replaced with D, E, H, K, R, N, Q, F, W, Y, P, or C ;. L240 replaced with D, E, H, K, R, N, Q, F, W, Y, P, or C; P241 replaced with D, E, H, K, R, A, G, I, L, S, T, M, V, N, Q, F, W, Y, or C; N242 replaced with D, E, H, K, R, A, G, I, L, S, T, M, V, F, W, Y, P, or C ; N243 replaced with D, E, H, K, R, A, G, I, L, S, T, M, V, F, W, Y, P, or C ; S244 replaced with D, E, H, K, R, N, Q, F, W, Y, P, or C ; C245 replaced with D, E, H, K, R, A, G, I, L, S, T, M, V, N, Q, F, W, Y, or P ; Y246 replaced with D, E, H, K, R, N, Q, A, G, I, L, S, T, M, V, P, or C ; S247 replaced'with D, E, H, K, R, N, Q, F, W, Y, P, or C ; A248 replaced with D, E, H, K, R, N, Q, F, W, Y, P, or C ; G249 replaced with D, E, H, K, R, N, Q, F, W, Y, P, or C ; 1250 replaced with D, E, H, K, R, N, Q, F, W, Y, P, or C; A251 replaced with D, E, H, K, R, N, Q, F, W, Y, P, or C; K252 replaced with D, E, A, G, I, L, S, T, M, V, N, Q, F, W, Y, P, or C; L253 replaced with D, E, H, K, R, N, Q, F, W, Y, P, or C; E254 replaced with H, K, R, A, G, I, L, S, T, M, V, N, Q, F, W, Y, P, or C ; E255 replaced with H, K, R, A, G, I, L, S, T, M, V, N, Q, F, W, Y, P, or C; G256 replaced with D, E, H, K, R, N, Q, F, W, Y, P, or C ; D257 replaced with H, K, R, A, G, I, L, S, T, M, V, N, Q, F, W, Y, P, or C ; E258 replaced with H, K, R, A, G, I, L, S, T, M, V, N, Q, F, W, Y, P, or C; L259 replaced with D, E, H, K, R, N, Q, F, W, Y, P, or C; Q260 replaced with D, E, H, K, R, A, G, I, L, S, T, M, V, F, W, Y, P, or C ; L261 replaced with D, E, H, K, R, N, Q, F, W, Y, P, or C ; A262 replaced with D, E, H, K, R, N, Q, F, W, Y, P, or C; I263 replaced with D, E, H, K, R, N, Q, F, W, Y, P, or C; P264 replaced with D, E, H, K, R, A, G, I, L, S, T, M, V, N, Q, F, W, Y, or C ; R265 replaced with D, E, A, G, I, L, S, T, M, V, N, Q, F, W, Y, P, or C; E266 replaced with H, K, R, A, G, I, L, S, T, M, V, N, Q, F, W, Y, P, or C; N267 replaced with D, E, H, K, R, A, G, I, L, S, T, M, V, F, W, Y, P, or C ; A268 replaced with D, E, H, K, R, N, Q, F, W, Y, P, or C; Q269 replaced with D, E, H, K, R, A, G, I, L, S, T, M, V, F, W, Y, P, or C ; 1270 replaced with D, E, H, K, R, N, Q, F, W, Y, P, or C; S271 replaced with D, E, H, K, R, N, Q, F, W, Y, P, or C; L272 replaced with D, E, H, K, R, N, Q, F, W, Y, P, or C ; D273 replaced with H, K, R, A, G, I, L, S, T, M, V, N, Q, F, W, Y, P, or C ; G274 replaced with D, E, H, K, R, N, Q, F, W, Y, P, or C; D275 replaced with H, K, R, A, G, I, L, S, T, M, V, N, Q, F, W, Y, P, or C; V276 replaced with D, E, H, K, R, N, Q, F, W, Y, P, or C; T277 replaced with D, E, H, K, R, N, Q, F, W, Y, P, or C; F278 replaced with D, E, H, K, R, N, Q, A, G, I, L, S, T, M, V, P, or C ; F279 replaced with D, E, H, K, R, N, Q, A, G, I, L, S, T, M, V, P, or C; G280 replaced with D, E, H, K, R, N, Q, F, W, Y, P, or C; A281 replaced with D, E, H, K, R, N, Q, F, W, Y, P, or C; L282 replaced with D, E, H, K, R, N, Q, F, W, Y, P, or C; K283 replaced with D, E, A, G, I, L, S, T, M, V, N, Q, F, W, Y, P, or C ; L284 replaced with D, E, H, K, R, N, Q, F, W, Y, P, or C; and/or L285 replaced with D, E, H, K, R, N, Q, F, W, Y, P, or C. The resulting Neutrokine-alpha protein in crystalline form may be routinely screened for Neutrokine-alpha functional activities and/or physical properties (such as, for example, enhanced or reduced stability and/or solubility and/or oligomeric state) described throughout the specification and known in the art.

Preferably, the resulting proteins of the invention have an increased and/or a decreased Neutrokine-alpha functional activity. More preferably, the resulting Neutrokine-alpha proteins of the invention have more than one increased and/or decreased Neutrokine-alpha functional activity and/or physical property.

[0040] In an additional embodiment, a Neutrokine-alpha protein in crystalline form of the present invention comprises, or alternatively consists of, a Neutrokine-alpha protein with more than one amino acid (e. g. , 2,3, 4,5, 6,7, 8, 9,10, 15,20, 30 and 50) replaced with the substituted amino acids as described above (either conservative or nonconservative). <BR> <BR> <BR> <BR> <P>[0041] Preferred modifiedNeutrokine-alphaproteins include aprotein having the sequence as listed in Figure 1A with one or more of the following amino acid residues mutated: V-142; T-143; Q-144; D-145; C-146; L-147; Q-148; L-149; I-150 ; A-151; D-152; S-153; E-154; T-155; P-156; T-157; 1-158 ; Q-159; and K-160.

[0042] By a protein having an amino acid sequence at least, for example, 95% "identical"to a reference amino acid sequence of a Neutrokine-alpha protein is intended that the amino acid sequence of the protein is identical to the reference sequence except that the protein sequence may include up to five amino acid alterations per each 100 amino acids of the reference amino acid of the Neutrokine-alpha protein. In other words, to obtain a protein having an amino acid sequence at least 95% identical to a reference amino acid sequence, up to 5% of the amino acid residues in the reference sequence may be deleted or substituted with another amino acid, or a number of amino acids up to 5% of the total amino acid residues in the reference sequence may be inserted into the reference sequence. These alterations of the reference sequence may occur at the amino or carboxy terminal positions of the reference amino acid sequence or anywhere between those terminal positions, interspersed either individually among residues in the reference sequence or in one or more contiguous groups within the reference sequence.

[0043] As a practical matter, whether any particular polypeptide or protein is at least 80%, 85%, 90%, 95%, 96%, 97%, 98% or 99% identical to, for instance, the amino acid sequences shown in TABLES 4 and 5, or fragments thereof, can be determined conventionally using known computer programs such the Bestfit program (Wisconsin Sequence Analysis Package, Version 8 for Unix, Genetics Computer Group, University Research Park, 575 Science Drive, Madison, WI 53711). When using Bestfit or any other sequence alignment program to determine whether a particular sequence is, for instance, 95% identical to a reference sequence according to the present invention, the parameters are set, of course, such that the percentage of identity is calculated over the full length of the reference amino acid sequence and that gaps in homology of up to 5% of the total number of amino acid residues in the reference sequence are allowed.

[0044] In a specific embodiment, the identity between a reference (query) sequence (a sequence of the present invention) and a subject sequence, also referred to as a global sequence alignment, is determined using the FASTDB computer program based on the algorithm of Brutlag et al. Comp. App.

Biosci. 6 : 237-245 (1990). Preferred parameters used in a FASTDB amino acid alignment are: Matrix=PAM 0, k-tuple=2, Mismatch Penalty=l, Joining Penalty=20, Randomization Group Length=0, Cutoff Score=l, Window Size=sequence length, Gap Penalty=5, Gap Size Penalty=0.05, Window Size=500 or the length of the subj ect amino acid sequence, whichever is shorter. According to this embodiment, if the subject sequence is shorter than the query sequence due to N-or C-terminal deletions, not because of internal deletions, a manual correction is made to the results to take into consideration the fact that the FASTDB program does not account for N-and C-terminal truncations of the subject sequence when calculating global percent identity. For subject sequences truncated at the N-and C-termini, relative to the query sequence, the percent identity is corrected by calculating the number of residues of the query sequence that are N-and C-terminal of the subject sequence, which are not matched/aligned with a corresponding subject residue, as a percent of the total bases of the query sequence. A determination of whether a residue is matched/aligned is determined by results of the FASTDB sequence alignment.

This percentage is then subtracted from the percent identity, calculated by the above FASTDB program using the specified parameters, to arrive at a final percent identity score. This final percent identity score is what is used for the purposes of this embodiment. Only residues to the N-and C-termini of the subject sequence, which are not matched/aligned with the query sequence, are considered for the purposes of manually adjusting the percent identity score.

That is, only query residue positions outside the farthest N-and C-terminal residues of the subject sequence. For example, a 90 amino acid residue subject sequence is aligned with a 100 residue query sequence to determine percent identity. The deletion occurs at the N-terminus of the subject sequence and therefore, the FASTDB alignment does not show a matching/alignment of the first 10 residues at the N-terminus. The 10 unpaired residues represent 10% of the sequence (number of residues at the N-and C-termini not matched/total number of residues in the query sequence) so 10% is subtracted from the percent identity score calculated by the FASTDB program. If the remaining 90 residues were perfectly matched the final percent identity would be 90%. In another example, a 90 residue subject sequence is compared with a 100 residue query sequence. This time the deletions are internal deletions so there are no residues at the N-or C-termini of the subject sequence which are not matched/aligned with the query. In this case the percent identity calculated by FASTDB is not manually corrected. Once again, only residue positions outside the N-and C-terminal ends of the subject sequence, as displayed in the FASTDB alignment, which are not matched/aligned with the query sequence are manually corrected for. No other manual corrections are made for the purposes of this embodiment.

[0045] An additional aspect of the present invention is a composition comprising a Neutrokine-alpha protein that is suitable for producing a Neutrokine-alpha protein in crystalline form.

Protein Crystallization Methods [0046] The present invention provides methods for preparing aNeutrokine-alpha protein in crystalline form. Preferably, the method produces a Neutrokine-alpha protein in crystalline form, wherein said Neutrokine-alpha protein diffracts X-rays with sufficiently high resolution to allow determination of the three- dimensional structure of saidNeutrokine-alphaproteinproduct, including atomic coordinates. The three-dimensional structure is useful in a number of methods of the present invention, as described herein. Specifically provided is a method for crystallizing a recombinant, non-glycosylated human Neutrokine-alpha protein comprising the amino acid sequence listed in Figure 1 A and Table 5.

[0047] Said protein can be obtained from suitable sources, such as eukaryotic cells or tissues. In general, a protein comprising a Neutrokine-alpha protein or a portion thereof is isolated in soluble form in sufficient purity and concentrated for crystallization. The polypeptide is optionally assayed for lack of aggregation (which may interfere with crystallization). The purified polypeptide is preferably crystallized under varying conditions of at least one of the following factors: pH, buffering agent, buffer concentration, salt, polymer, polymer concentration, other precipitating agents, and concentration of purified Neutrokine-alpha protein or portion thereof. See, e. g., Blundell et al., Protein Crystallography, Academic Press, London (1976) ; McPherson, The Preparation and Analysis of Protein Crystals, Wiley Interscience, N. Y. (1982). The crystallized polypeptide is optionally tested for Neutrokine-alpha activity and differently sized and shaped crystals are further tested for suitability for X-ray diffraction. Generally, larger crystals provide better crystallographic data than smaller crystals, and thicker crystals provide better crystallographic data than thinner crystals. l0048] The pH of the solution is from about 4-9, preferably from about 6-7.

Preferably, the pH of the solution is about 6.

[0049] The buffering agent can be any buffering agent. Buffering agents are well-known in the art. Exemplary buffering agents include citrate, phosphate, cacodylate, acetates, imidazole, Tris HC1, and sodium HEPES.

[0050] The buffer concentration is from about 10 millimolar (mM) to about 200 mM. Alternatively, the buffer concentration is about 10,20, 30,40, 50,60, 70, 80,90, 100,110, 120,130, 140,150, 160,170, 180,190 or 200 mM.

[0051] The salt is an ionic salt, which is well known in the art. Exemplary salts include calcium chloride, sodium citrate, magnesium chloride, ammonium acetate, ammonium sulfate, potassium phosphate, magnesium acetate, zinc acetate, and calcium acetate.

[0052] The polymer is a compound that contains repeating subunits. Exemplary polymers that are useful in the present invention include polyethylene glycol (PEG), polypropyleneglycol (PPG), and others. The average molecular weight of the polymer is from about 200 to about 100,000. Other suitable values for the average molecular weight of the polymer include from about 200 to about 10,000 ; from about 1,000 to about 10,000 ; from about 5,000 to about 100,000 ; from about 5,000 to about 10,000.

[0053] The concentration of the polymer is the concentration of the polymer in the solution suitable for crystallization. The concentration of the polymer is from about 1% to about 50%. The concentration of the polymer is about 1%, 5%, 10%, 15%, 20%, 25%, 30%, 35%, 40%, 45%, or 50%.

[0054] The solution suitable for crystallization optionally comprises one or more additional agents selected from the group consisting of potassium tartrate, sodium tartrate, ammonium sulfate (NH4SO4), sodium acetate (CH3CO2Na), lithium sulfate (LiS04), sodium formate (HC02Na), sodium citrate, magnesium formate ((HCO2) 2Mg), sodium phosphate, potassium phosphate; NH4PO4 ; 2-propanol; 2-methyl-2,4-pentanediol ; and dioxane.

[0055] According to the present invention, the solution preferably contains dioxane. The concentration of the dioxane is from about 10% to about 60%, preferably from about 20% to about 50%, preferably from 30% to about 40%, preferably about 35%.

[0056] Any suitable crystallization method is used for crystallizing the Neutrokine-alpha protein or portion thereof, such as the hanging-drop, vapor diffusion method, microbatch, sitting drop, and dialysis. Preferably, hanging drop method is used. The crystals should be grown for from about 6 hours to about 72 hours.

[0057] According to the present invention, a preferred method of preparing a Neutrokine-alpha protein in crystalline form uses hanging drops containing about 1 mL of about 20 mg/mL hNeutrokine-alpha in about 25 mM sodium citrate, about 125 mM NaCl, pH of about 6 and about 1 ml of about 25% dioxane, about 25 mM MgCl2 suspended over a reservoir of about 25% dioxane and about 25 mM MgClz.

[0058] According to the present invention, a preferred method of preparing a Neutrokine-alpha protein in crystalline form uses hanging drops containing about 1 I1L of about 20 mg/mL hNeutrokine-alpha in about 25 mM sodium citrate, about 125 mM NaCl, pH of about 6 and about 1 ; j. l of about 25% dioxane, about 25 mM MgCl2 suspended over a reservoir of about 25% dioxane and about 25 mM MgCl2.

[0059] Crystals grown according to the present invention diffract X-rays to at least 10 A resolution, such as 0.15-10. 0 A, or any range of value therein, such as 1.5, 1.6, 1.7, 1.8, 1.9, 2.0, 2.1, 2.2, 2.3, 2.4, 2.5, 2.6, 2.7, 2.8, 2.9, 3.0, 3.1, 3.2, 3.3, 3.4 or 3.5, with 3.5 A or higher resolution being preferred for determining the crystal structure. However, diffraction patterns with a lower resolution, such as 25-3.5 A, are also useful.

[0060] According to the present invention, during growth, some of the crystals are optionally removed, washed, and assayed for biological activity. Other washed crystals are optionally run on a gel and stained, and those that migrate at the same molecular weight as the corresponding purified polypeptide comprising the Neutrokine-alpha protein or portion thereof are preferably used. From one to two hundred crystals can be observed in one drop. When fewer crystals are produced in a drop, the crystals may be a much larger size, for example from about 0.1 to about 0.4 mm [0061] Heavy atom derivatives used for multiple isomorphous replacement are obtained by either soaking the crystals with a mercurial reagent or placing crystals in a gaseous xenon (Xe) atmosphere during data collection (Schiltz et al., J Appl. Cryst. 27: 950-960 (1994) ). Suitable mercurial reagents include sodium p-chloromercuribenzylsulphonate (PCMBS). The concentration of the mercurial reagent is from about 0.1 mM to about 0.5 mM or from about 0.1 mM to about 10 mM.

X-ray Crystallography [0062] Another aspect of the present invention is directed to determining the three-dimensional structure of a Neutrokine-alpha protein by using X-ray diffraction crystallography methods. The X-ray diffraction patterns can be either analyzed directly to provide the three-dimensional structure (if sufficient data are collected), or atomic coordinates for human Neutrokine-alpha protein in crystalline form, as provided herein, can be used for structure determination. The X-ray diffraction patterns obtained by methods of the present invention, and optionally provided on computer readable media, are used to provide electron density maps. The amino acid sequence is also useful for three-dimensional structure determination. The data are then used in combination with phase determination (e. g., using multiple isomorphous replacement (MIR) molecular replacement techniques) to generate electron density maps of Neutrokine-alpha, using a suitable computer system.

[0063] The electron density maps, provided by analysis of either the X-ray diffraction patterns or working backwards from the atomic coordinates, provided herein, are then fitted using suitable computer algorithms to generate secondary, tertiary, and/or quaternary structures and/or domains of Neutrokine-alpha, which structures and/or domains are then used to provide an overall three-dimensional structure, as well as binding sites of Neutrokine-alpha.

[0064] A Neutrokine-alpha protein in crystalline form produced according to the present invention is X-ray analyzed using a suitable X-ray source to obtain diffraction patterns. Preferably, said crystalline Neutrokine-alpha protein is used which is stable for at least 10 hrs in the X-ray beam. Frozen crystalline Neutrokine-alpha (e. g. ,-220 to-50°C) is optionally used for longer X-ray exposures (e. g. , 5-72 hrs), the crystals being relatively more stable to the X-rays in the frozen state. To collect the maximum number of useful reflections, preferably multiple frames are collected as the crystal is rotated in the X-ray beam. Larger crystals of crystalline Neutrokine-alpha (i. e. , greater than about 150 , um) are preferred to increase the resolution of the X-ray diffraction patterns obtained. In one embodiment, crystals are analyzed using a synchrotron high energy X-ray source. Using frozen crystals, X-ray diffraction data are collected on crystals that diffract to at least a relatively high resolution of about 10 A to about 1.5 A. Diffraction data may also be collected on crystals that diffract at lower resolutions, such as from about 25 to about 10 A.

[0065] Passing an X-ray beam through a crystal produces a diffraction pattern as a result of the X-rays interacting and being scattered by the contents of the crystal. The diffraction pattern are visualized using a method well-known in the art, e. g. , an image plate or film, resulting in an image with spots corresponding to the diffracted X-rays. The positions of the spots in the diffraction pattern are used to determine parameters intrinsic to the crystal (such as unicell parameters) and to gain information on the packing of the molecules in the crystal. The intensity of the spots contains the Fourier transformation of the molecules in the crystal, i. e., information on the position of each atom in the crystal and hence of the crystallized molecule.

[0066] Although the diffraction patterns are usually themselves sufficient for three-dimensional structure determination, the amino acid sequence of the Neutrokine-alpha protein is also useful. The electron density maps, provided by analysis of the X-ray diffraction patterns, are then fitted using suitable computer algorithms as described below to generate secondary, tertiary and/or quaternary structure of the Neutrokine-alpha protein providing an overall three-dimensional model.

[0067] After data collection of diffraction patterns, the data are processed using methods well known in the art. One such suitable method to process the diffraction data is the MarXDS package Kabsch, W. J AppL Crystallogr. 21 : 916- 924 (1988)). The MarXDS package is a Fortran program developed for the reduction of single-crystal diffraction data from a sequence of adjacent rotation pictures recorded at a fixed X-ray wavelength by an electronic area detector.

Patterson and cross Fourier analyses and SIR phasing can be performed using programs from the CCP4 package (Collaborative Computational Project No. 4, Acta Cryst. D50 : 760-763 (1994) ), which is a suite of programs for the reduction and analysis of intensity data, structure solution by isomorphous replacement and molecular replacement, least-squares refinement, analysis of the structure, displaying electron-density maps and plotting molecules.

[0068] Electron density maps can be calculated using one of several well-known programs, such as those from the CCP4 computing package described above.

Cycles of two-fold averaging can further be used, such as with the program RAVE (Kleywegt & Jones, Bailey et al., eds., First Map to Final Model, SERC Daresbury Laboratory, UK, pp. 59-66 (1994) ) and gradual model expansion. The interpretation of electron density maps phased by multiple isomorphous replacement (MIR) to produce an initial molecular model is a critical step during the model building process. Three-dimensional computer graphics workstations are now widely used in the art for constructing models in MIR maps. One computer program in particular, FRODO, is commonly used and is available on a range of workstations (Jones, T. A., J : Appl. Cryst. 11 : 268-272 (1978) ). In an attempt to improve the ability to interpret maps and then to construct more accuratemodels, Jones & Thirup, EMBOJ. 5 : 819-822 (1986), introduced the use of skeletons coupled with a protein database of the best refined protein structures to build the initial model. This work suggested that all protein models could be built from fragments of existing structures. Jones et al. (Jones et al., Acta Cryst.

A47 : 110-119 (1991) ), extended these ideas with a computer graphics program called"O,"which allows the user to go from an initial Ca trace to a well refined model. An overview of the strategy used is provided below: Map Calculate Skeletonized Map Edit Skeletfnized Map Assign Ca positions from skeleton Autobuild Main Chain I Autobuild Side Chain I RSRrotamer each residue RSR rigid each residue Restore Stereochemistry Crystallographic Refinement [0069] The three-dimensional structure of aNeutrokine-alpha protein can be built into a 3 A resolution map through several cycles of model building using the"0" graphics program and phase combination using the Sigma A algorithm, which is part of the CCP4 package discussed above.

[0070] Refrnement andModel Validation. Rigid body and positionalrefinement can be carried out using a program such as X-PLOR (Brunger, A. T. , X-PLOR Version 3.1, Yale University Press (1992) ) to a suitable crystallographic Factor If the model at this stage in the averaged maps still misses residues (e. g. , at least 5-10 per subunit), then some or all of the missing residues can be incorporated in the model during additional cycles of positional refinement and model building.

The refinement procedure can start using data from lower resolution (e. g. , 25-10 A to 10-3.0 A) and then gradually be extended to include data from 12-6 A to 3.0- 1.5 A. B-values (also termed temperature factors) for individual atoms can be refined once data of 2. 8A or higher (e. g. , up to 1.0 or 1. 5 Å) has been added.

Subsequently waters can be gradually added. A program such as ARP (Lamzin and Wilson, Acta Cryst. D49 : 129-147 (1993) ) can be used to add crystallographic waters and as a tool to check for bad areas in the model. Programs such as PROCHECK (Lackowski et al., J : Appl. Cryst. 26 : 283-291 (1993)), WHATIF (Vriend, J. Mol. Graph. 8 : 52-56 (1990) ) and PROFILE 3D (Liithy et al., Nature 356 : 83-85 (1992) ), as well as the geometrical analysis generated by X-PLOR can be been used to check the structure for errors. A program such as DSSP can be used to assign the secondary structure elements (Kabsch and Sander, Biopolymers 22 : 2577-2637 (1983) ). The model data are then saved on computer readable media for use in further analysis, such as, for example, in a method for modeling the structure of a related Neutrokine-alpha protein or in a computer-based system for the rational design of ligand that bind to, mimic, or inhibit a Neutrokine-alpha protein.

[0071] In general, X-ray diffraction data processing includes measuring the spots on each diffraction pattern in terms of position and intensity. This information is processed as indicated above (i. e., mathematical operations are performed on the data (such as scaling, merging and converting the data from intensity of diffracted beams to amplitudes) ) to yield a set of data which is in a form as can be used for the further structure determination of the molecule. The amplitudes of the diffracted X-rays are then combined with calculated phases to produce an electron density map of the contents of the crystal. In the electron density map, the structure of the molecules (as present in the crystal) is built. The phases can be determined with various known techniques, one being molecular replacement.

[0072] For the molecular replacement technique, one takes a known three dimensional structure thought to share structural homology with the structure to be determined, to generate, after calculations, a first set of initial phases. These phases can be combined with the diffraction information of the molecule whose structure you want to solve.

[0073] The phases can be further optimized using a technique called density modification, which allows electron density maps of better quality to be produced facilitating interpretation and model building therein. The model is then refined by allowing the atoms in the model to move in order to match the diffraction data as well as possible while continuing to satisfy stereochemical constraints, such as reasonably bond lengths and bond angles.

[0074] In general, the R factor is preferably between about 0.15 and about 0. 35 for a well-determined structure of a Neutrokine-alpha protein. The residual difference is a consequence of errors and imperfections in the data. These derive from various sources, including slight variations in the conformation of the protein molecules, as well as inaccurate corrections both for the presence of solvent and for differences in the orientation of the microcrystals from which the crystal is built.

Three-Dimensional Structure of Human Neutrokine-alpha (hNeutrokine- alpha) [0075] The monomer of luNeutrokine-alpha adopts the TNF-like jellyroll fold consisting of two five-stranded 3-sheets with similar arrangement as the other representatives of this family. A structure-based sequence alignment among members of this cytokine family (see Figure 1 A) reveals that the Greek-key motif of the strands is conserved throughout the family despite the low identity in sequence. Using these structural alignments, the calculated identities between hNeutrokine-alpha and the other TNF-like proteins are: about 15% to TNF-a, about 16% to CD40L, about 19% TRANCE/RANKL, about 18% to Apo2L/TRAIL, and about 20% to TNF-ß. The identities occur primarily in the p-strands C, D, F, G, and H that constitute the core of the jellyroll fold (see Figure 1B). However, major differences are observed in the loop regions AA", CD, DE, EF, and GH of the related cytokines. In contrast with related cytokines, hNeutrokine-alpha does not have the short GH a-helix, is truncated in loops CD and EF, and contains large inserts between strands A and A"and between strands D and E. In hNeutrokine-alpha, the AA"loop is modified by insertion of two short (3-strands forming a hairpin motif (a and a', Figure 1B) that does not participate in (3-sheet formation but widens the molecule. Similarly, the DE loop that has a four-residue insert, protrudes from the surface and forms inter-trimer contacts reminiscent of a handshake. As a result of these differences, the hNeutrokine-alpha homotrimer measures about 52 A high (along the three-fold axis) and about 60 A wide as compared to about 58 A and about 57 A, respectively, in TNF-p (see Figure 2B). A sample of the experimental electron density is shown in Figure 2E, in the region of the disulfide bond between residues 232 and 245. This disulfide bond holds strands E and F together, thereby stabilizing loop EF. The disulfide bond found in both TNF-a and CD40L connect loops CD and EF. Three hNeutrokine-alpha monomers make extensive contacts within the trimer (about 5700 A of buried surface) with the sheets inclined about 30° relative to the three-fold axis (Fig. 2A). By analogy with other cytokine-receptor complexes, the narrow end of the trimer (displaying the CD and EF loops) is predicted to be proximal to the B-cell membrane when hNeutrokine-alpha is bound to its receptor (s).

[0076] A complex of two hydrated Mg2+ ions binds to the hNeutrokine-alpha trimer along the three-fold axis, near the trimer's narrow end (Figure 2A). A complex formation of two magnesium ions bound to the protein is observed (Fig.

2B). One ion (Mgl) is bound to the side chains of Gln234 residues from each monomer and interacts with the other (Mg2) via bridging water molecules (Figure 2B'). The water molecules are bound to the protein via residues N243 and the main chain oxygen of N235. A zinc ion was identified in a related position (about 6.4 A from Mgl) in the Apo2L/TRAIL, along the three-fold axis, interacting with Cys230 sulfhydryls from each monomer (Hymowitz et al., Biochemistry 39 : 633-640 (2000). Mutating residue Q234 to X had deleterious effects on the formation ofthe hNeutrokine-alphatrimer, resulting in aggregation.

The metal ions are assigned to be magnesium because a) the crystals were grown in a solution containing 25 mM MgCl2, b) each metal ion coordinates 6 oxygen atoms, and c) the B refined factors are reasonable (about 28-33 A2) for magnesium. Other molecules were also observed bound to the protein. Dioxane molecules were found along the three-fold axis interacting with phenyl rings of Phel65 and Phel94. Also, a citrate molecule was located at the interface between two trimers in the asymmetric unit where the DE loops shake hands and is situated on a local two-fold axis and is two-fold disordered. The carboxylates of the citrate bind to His218, Arg214, Glu223, LYS252, ASP254, and LYS216.

[0077] A comparison of the molecular surface of the biologically active trimeric form of hNeutokine-alpha (Fig. 3) to that of other cytokines has revealed that this protein has a unique shape with three pronounced grooves on the surface. A similar shape is found in the other cytokines but in none is it as extensive or as deep. The groove winds around the surface of the trimer and has a shape appropriate for binding elongated receptors. As seen in Figure 3, the TNF-R and the DR5 receptors bind to this region of the cytosine. This putative receptor-binding site is created by loops from two monomers coming together to each form the sides of the groove. The walls of this groove consist on one side of loop DE with some residues of loops aa'and GH, and on the other side are found loops EF, Aa, and a'A". These residues are highly variable within the TNF family. In the structures of cytokines complexed to their receptors (PDB entries 1TNR and 1D4V or 1DOG), these loops form the most extensive contacts within the complexes. The protruding DE loop that is unique to Neutrokine-alpha and the additional p-hairpin in the AA"loop of Neutrokine-alpha when docked onto the TNF/TNF-R structure come in close contact along the ridges of the groove (Fig. 4A and 4B). These residues would discriminate between TNF (or other cytokines) and Neutrokine-alpha, which does not bind to TNF-R.

[0078] The three receptors known to bind and be activated by Neutrokine-alpha share little sequence identity, yet they all contain at least one cysteine-rich domain. As seen in the complex between TNF and TNF-R, the receptor's cysteine-rich region (Fig. 4C) forms contacts with loops AA"and DE of TNF.

Baff-R, the receptor with the highest affinity towards Neutrokine-alpha, is the shortest sequence, containing only one cysteine-rich domain. An alignment of the cysteine-rich regions of BAFF-R, BCMA, and TACI that align best with the TNF-R recognition region is shown in Fig. 4C. The cysteines are structural and are somewhat conserved. The cysteine pair formed by the 3rd and 5th cysteines is found in all but BAFF-R. The Neutrokine-alpha receptors all contain proline residues that may shorten this (3-strand (residues 60-80 of TNF-R). The recognition residues on TNF-R within this stretch are all unique to TNF-R which could explain the discriminatory ability of the receptors. The sequence in Figure 4 is an elongated strand running from residue 65 to residue 80 and extends about 32.5 A in length before turning at either end. Residues 55-59 and 69-81 contact the AA"loop of TNF while residues 75-81 contact loops CD and GH. Loop DE binds to residues 60-70.

[0079] The structure of Neutokine-alpha determined to 2 A resolution reveals a distinctive binding groove at the interfaces between adjacent monomers in the trimer. This binding groove may allow the cytokine to discriminate between receptors. Receptors that cannot access the deep crevice may be excluded from binding. The receptor residues that participate in specific recognition of Neutrokine-alpha might be part of the consensus sequence: ExFDxLLRxCxxCxLxxT (S) xxPKP.

[0080] The groove is created by loops from two adjacent monomers. One wall of the groove contains loop DE with some residues of loops aa'and GH, and the other wall of the groove contains loops EF, Aa, and a'A". The deepest portion of the groove consists primarily of beta-strands D, E, and F. Residues with surface accessible side chains are ALA207, LEU211, GLN213, and ARG214 from strand D; THR228, LEU229, PHE230, ARG231, and ILE233 from strand E; and ALA251, LYS252, LEU253, GLU254, and ASP257 from strand F. The groove winds around the surface of the trimer and has a shape appropriate for binding elongated receptors. Loops DE and AA"form the most extensive contacts with cytokine receptors. Modeling interactions of neutrokine-alpha with TNF-R indicate that the outer rim of the groove (loops DE and the beta-hairpin of loop AA") would lead to steric conflict. These residues would permit receptors to discriminate between TNF or other cytokines and neutrokine-alpha. The residues involved in creating the surface of this groove and putative receptor-binding site are from adjacent monomers (green, Fig 4a). Of those residues, the homology APRIL shares residues Leu 200, Arg 214, Thr 228, Leu 229, Phe 230, Arg 231, Ile 233, Leu 253, Asp 257 and Phe 278 with neutrokine-alpha (Fig. 4a, red). The majority of these shared residues are located on the floor of the groove, suggesting that the floor is used as a common binding motif for TACI, BCMA and BAFF-R to neutrokine-alpha and APRIL. Variations in residues on the groove walls would permit BAFF-R to discriminate against APRIL.

[0081] The three receptors known to bind and be activated by neutrokine-alpha share little sequence identity, but they all contain at least one Cys-rich domain.

As seen in the complex between TNF and TNF-R, the Cys-rich region of the receptor forms contacts with loops AA"and DE of TNF-alpha. BAFF-R, the receptor with the highest affinity for neutrokine-alpha, has the shortest sequence, containing only one Cys-rich domain. A ProDom24 database search (aided by PredictProtein25) probed using the BAFF-R sequence revealed BCMA as the most similar, specifically in the Cys-rich region, the transmembrane domain and an intracellular portion consisting of residues GEDPGTTPGHSVPVPA. In a receptor-binding study using SELDI affinity mass spectrometry26, we show that the a'A"loop, the B'and B strands, and strands C and D of the molecule are centrally involved (Fig. 4b) in the interaction of BlyS with both recombinant BCMA and TACI receptors, as indicated by the relatively large number of retained fragments of neutrokine-alpha that map to these areas. The data support the assumption that neutrokine-alpha interacts similarly with its receptors as other TNF ligands interact with their respective receptors. TACI and BCMA are unable to mediate the survival activity of BlyS, and the interaction of BAFF-R with neutrokine-alpha was recently determined to be important to peripheral B-cell survival. This highlights the ability of the unique surface of BlyS to interact differently with several receptors.

[0082] In summary, the structure of neutrokine-alpha has revealed a distinctive binding groove formed by adjacent monomers within the trimer that permits the cytokine to discriminate among closely related receptors. The floor of the groove seems to harbor shared receptor-binding elements that permit recognition of the three receptors TACI, BCMA and BAFF-R, whereas variations on the outer rims of the groove confer specificity to the interaction. This model, supported by evidence obtained using SELDI affinity mass spectrometry, provides a basis for understanding cytokine receptor-binding specificity and the unique regulation of immune function by neutrokine-alpha. We now have a model that explains both cross-reactivity and specificity. By targeting areas that are implicated in receptor discrimination, developing drugs that can selectively modulate the immunoregulatory functions of neutrokine-alpha should be possible. In particular, a drug which binds to or fits into the groove is useful for selectively modulate the immunoregulatory functions of neutrokine-alpha. Furthermore, a drug that binds to or fits into a portion of the surface of a monomer, wherein said surface is involved in trimerization of neutrokine-alpha monomers, would be useful for modulating the effects of neutrokine-alpha.

[0083] Representations of the major groove on the surface of the neutrokine- alpha protein are provided in Figures 7 and 8. Representation of the surface of neutrokine-alpha involved in trimerization is shown in Figure 9.

Visualiztion of Protein Structure [0084] Although diagrams, such as those in the Figures herein, are useful for visualizing the three dimensional structure of a Neutrokine-alpha protein, a computer program which allows for stereoscopic viewing of the molecule is contemplated as preferred. This stereoscopic viewing, or"virtual reality"as those in the art sometimes refer to it, allows one to visualize the structure in its three dimensional form from every angle in a wide range of resolution, from macromolecular structure down to the atomic level. The computer programs contemplated herein also allow one to change perspective of the viewing angle of the molecule, for example by rotating the molecule. The contemplated programs also respond to changes so that one may, for example, delete, add, or substitute one or more images of atoms, including entire amino acid residues, or add chemical moieties to existing or substituted groups, and visualize the change in structure.

[0085] Other computer based systems may be used; the elements being: (a) a means for entering information, such as orthogonal coordinates or other numerically assigned coordinates of the three dimensional structure of a Neutrokine-alpha protein; (b) a means for expressing such coordinates, such as visual means so that one may view the three dimensional structure and correlate such three dimensional structure with the atomic composition of the Neutrokine- alpha protein, such as the amino acid composition; (c) optionally, means for entering information which alters the composition of the Neutrokine-alpha protein expressed, so that the image of such three dimensional structure displays the altered composition.

[0086] Once the coordinates are entered into the computer program, one easily displays the three dimensional Neutrokine-alpha protein representation on a computer screen. In one embodiment, the computer system for display is a SGI Octane (San Diego, Calif.). For stereoscopic viewing, one may wear eyewear (Crystal Eyes, SGI) which allows one to visualize the Neutrokine-alpha protein in three dimensions stereoscopically, so one may turn the molecule and envision molecular design.

[0087] Several additional, publically and commercially available software programs can be used according to the present invention. Such programs include WHATIF, Sybyl, Insight II, and RasMol (Sayle and Milner-White, "RasMol : Biomolecular graphics for all,"Trends Biochem. Sci. 20: 374 (1995)).

[0088] Any portion of the Neutrokine-alpha protein may be visualized.

[0089] Other preferred characteristics of the three dimensional structure of a Neutrokine-alpha protein, or portion thereof, may be visualized and include lipophilic potential, electrostatic potential, hydrogen bonding ability, local curvature, distance, van der Waals surface, Connolly surface, and solvent accessible surface.

Use of the Coordinates to Determine the Three-Dimensional Structures of Other Neutrokine-alpha Proteins [0090] Because a Neutrokine-alpha protein may crystallize in more than one crystal form, the structure coordinates of hNeutrokine-alpha protein, or portions thereof, as provided in Table 2, are particularly useful to solve the structure of those other crystal forms of hNeutrokine-alpha or of other Neutrokine-alpha proteins. The coordinates may also be used to solve the structure of Neutrokine- alpha mutants, of a co-complex comprising a neutrokine-alpha protein and one or more small molecules, peptides, or proteins, or of the crystalline form of any other protein with significant amino acid sequence homology to any functional domain of Neutrokine-alpha. Alternatively, the coordinates of hNeutrokine- alpha, or portions thereof, may be used to determine the three-dimensional structure of a Neutrokine-alpha protein of another animal.

[0091] One aspect of the present invention that may be employed for this purpose is molecular replacement. In this method, the unknown crystal structure, whether it is another crystal form of hNeutrokine-alpha, a non-human Neutrokine-alpha protein, a Neutrokine-alpha mutant, or a Neutrokine-alpha co-complex, or the crystal of some other protein with significant amino acid sequence homology to any functional domain of Neutrokine-alpha, may be determined using the hNeutrokine-alpha structure coordinates of this invention as provided in Table 2.

This method will provide an accurate structural form for the unknown crystal more quickly and efficiently than attempting to determine such information ab initio.

[0092] A second aspect of the present invention that may be employed for determining the three-dimensional structure of a Neutrokine-alpha protein, as described above, includes the manual manipulation of the coordinates for hNeutrokine-alpha comprising the coordinates of Table 2, or a portion thereof.

In particular, the coordinates are manipulated so that the coordinates of hNeutrokine-alpha, or a portion thereof, are converted into coordinates that encode the three-dimensional structure of a non-human Neutrokine-alpha protein, a Neutrokine-alpha mutant, or a Neutrokine-alpha co-complex, or the crystal of some other protein with significant amino acid sequence homology to any functional domain of Neutrokine-alpha. Preferably, the resulting coordinates encode the three-dimensional structure of a non-human Neutrokine-alpha protein or a Neutrokine-alpha mutant. The method as described comprises the steps of a) displaying the three-dimensional structure of hNeutrokine-alpha using a suitable computer system and a suitable computer program; and b) modifying the three-dimensional structure of hNeutrokine-alpha, thereby producing a three- dimensional structure of a non-human Neutrokine-alpha protein, a Neutrokine- alpha mutant, or a Neutrokine-alpha co-complex, or the crystal of some other protein with significant amino acid sequence homology to any functional domain of Neutrokine-alpha. Said three-dimensional structure of a non-human Neutrokine-alpha protein, a Neutrokine-alpha mutant, or a Neutrokine-alpha co- complex, or the crystal of some other protein with significant amino acid sequence homology to any functional domain of Neutrokine-alpha has one or more atoms or amino acid residues are added, deleted, or modified, compared to hNeutrokine-alpha. The method optionally further comprises a step of using a suitable energy minimization program to minimize the energy of the structure of the modified.

[0093] Another aspect of the present invention is a method of determining the structure of a Neutrokine-alpha protein, or portion thereof, complexed with a Neutrokine-alpha receptor, or portion thereof. A suitable Neutrokine-alpha receptor includes BCMA, TACI, or BAFF-R. The structure of the Neutrokine- alpha receptor is determined based on homology modeling to a the known structure of a related receptor, such as TNF-R or DR5. The amino acid composition of the Neutrokine-alpha receptors are known.

Use of Three Dimensional Structure to Design Biologically Active Molecules [0094] Another aspect of the present invention is a method of designing a biologically active molecule that binds to a Neutrokine-alpha protein. Another aspect of the present invention is a method of screening for a biologically active compound that binds to a Neutrokine-alpha protein. The three dimensional structure of aNeutrokine-alphaprotein, as provided herein, permits the screening of known molecules and/or the designing of new molecules which bind to a Neutrokine-alpha protein via the use of computerized evaluation systems. For example, computer modeling systems are available in which the sequence of the coordinates of a Neutrokine-alpha protein may be input. Thus, a machine readable medium may be encoded with data representing the coordinates, or a portion thereof, listed in Table 2. The computer then generates structural and/or physicochemical details of a site on the Neutrokine-alpha protein into which a test compound should bind, thereby enabling the determination of the complementary structural details of said test compound.

[0095] More particularly, the design of a compound that binds to or inhibits a Neutrokine-alpha protein, in particular hNeutrokine-alpha or a homologue thereof, according to this invention generally involves consideration of two factors. First, said compound must be capable of physically and structurally associating with a Neutokine-alpha protein. Non-covalent molecular interactions important in the association of said compound with a Neutrokine-alpha protein include hydrogen bonding, van der Waals, hydrophobic, ionic, dipole-dipole, and s-cation interactions. In another embodiment, covalent molecular interactions may be important for the association of said compound with a neutrokine-alpha protein.

[0096] Second, the compound must be able to assume a conformation that allows it to associate with a Neutrokine-alpha protein. Although certain portions of the compound will not directly participate in this association with aNeutokine-alpha protein, those portions may still influence the overall conformation of the molecule. This, in turn, may have a significant impact on potency. Such conformational requirements include the overall three-dimensional structure and orientation of the chemical entity or compound in relation to all or a portion of a binding site on a Neutrokine-alpha protein, or the spacing between functional groups of a compound comprising several chemical entities that directly interact with a Neutrokine-alpha protein.

[0097] In one embodiment of the invention, the molecule that is identified or designed according to the methods disclosed herein is a small molecule. In another embodiment of the invention, the molecule that is identified or designed according to the methods disclosed herein is peptide or peptide-mimetic. In a particular embodiment, the molecule that is identified or designed according to the methods disclosed herein is a peptide or peptide-mimetic that has alpha- helical character. In another embodiment of the invention, the molecule that is identified or designed according to the methods disclosed herein is a molecule which binds to or fits into the site in which the citrate molecule is located according to the crystal structure disclosed herein. In another embodiment of the invention, the molecule that is identified or designed according to the methods disclosed herein is a molecule which binds to or fits into the site in which the hydrated magnesium ion is located according to the crystal structure disclosed herein.

Identification of a Molecule that Binds to a Neutrokine-alpha [0098] There are a number of well-known processes that can be employed to identify a molecule which binds to a Neutrokine-alpha protein. Any number of processes which are known in the art can be employed to identify a molecule which binds to or fits into a site on the neutrokine-alpha protein. In general, a computational method of identifying a molecule according to the present invention is preferred. The particular aspects of computational drug design are well known in the art.

[0099] According to the present invention, a NMR-based process may be used to identify a molecule that fits into or binds to a site on the neutrokine-alpha protein. Such methods are known in the art. See, e. g. , van Dongen, M., et al.

"Structure-based screening and design in drug discovery,"Drug Discov. Today 7: 471-478 (2002); Jahnke, W. "Spin labels as a tool to identify and characterize protein-ligand interactions by NMR spectroscopy,"Chembiocheni. 3: 167-173 (2002); Pochapsky, S. S. and Pochapsky, T. C. "Nuclear magnetic resonance as a tool in drug discovery, metabolism and disposition,"Curr. Top. Med. Chem.

1 : 427-41 (2001); Sem, D. S. and Pellecchia M."NMR in the acceleration of drug discovery,"Curr. Opin. DrugDiscov. Devel. 4 : 479-92 (2001); Diercks, T. , etal., "Applications of NMR in drug discovery,"Curr. Opin. Chem. Biol. 5 : 285-91 (2001); Stockman, B. J., et al.,"Screening of compound libraries for protein binding using flow-injection nuclear magnetic resonance spectroscopy,"Methods Enzymol. 338 : 230-46 (2001); Peng, J. W., et al.,"Nuclear magnetic resonance-based approaches for lead generation in drug discovery,"Methods En. zymol. 338 : 202-30 (2001) ; Hicks, R. P. "Recent advances in NMR : expanding its role in rational drug design,"Curr. Med. Chem. 8 : 627-50 (2001); Hajduk, P. J., et al.,"NMR-based screening in drug discovery,"Q. Rev. Biophys. 32: 211-40 (1999).

[0100] According to the present invention, a screening process may be used to identify a molecule which binds to a Neutrokine-alpha protein. For example, a process which utilizes monoclonal antibody technology can be used to screen for a molecule which binds to a site on a Neutrokine-alpha protein. A monoclonal antibody that binds to a Neutrokine-alpha protein can be used in this process. For example, using an assay system comprising a Neutrokine-alpha protein or model thereof, and a monoclonal antibody which binds to Neutrokine-alpha, a molecule can be tested to determine if the molecule binds to the high affinity site. Such screening technology using monoclonal antibodies is known in the art.

[0101] Other traditional assays may be used to identify a molecule which binds to Neutrokine-alpha. For example, a radiolabelled ligand which is known to bind to Neutrokine-alpha can be used to screen for additional molecules which bind to Neutrokine-alpha. Such assays are known to those skilled in the art. A molecule, which is not radiolabelled and which is to be tested, is added to the assay system. After a certain equilibration period, the assay system is tested to determine the amount of radioactivity remaining, i. e. , the amount of tritiated compound that is still bound to Neutrokine-alpha. The higher the amount of radioactivity, the lower the affinity of the tested molecule, as can be calculated using known relationships, as disclosed in, e. g., Cheng, Y. and Prusoff, W. H.

"Relationship between the inhibition constant (Ki) and the concentration of inhibitor which causes 50 per cent inhibition (I50) of an enzymatic reaction," Biochem. Pharmacol. 22: 3099-3108 (1973).

[0102] A high throughput screening process can be employed to identify a molecule which binds to Neutrokine-alpha. Such high throughput screening processes are known.

[0103] Other processes suitable for identifying a molecule which fits into or binds to the high affinity site may utilize the atomic coordinates to the high affinity site.

[0104] According to the present invention, a molecular docking process can be employed to identify a molecule which binds to Neutroline-alpha. Such docking processes are known in the art. See, e. g., Martin, Y. C., J. Med. Chem.

35 : 2145-2154 (1992); Halperin, I., Proteins 47 : 409-43 (2002); Perez, C. et al., J. Med. Chem. 44 : 3768-85 (2001); Chen et al., Proteins 43 : 217-26 (2001).

[0105] The molecular docking process allows the molecule to be tested as a flexible molecule or as a rigid molecule. When a molecule is tested as a flexible molecule, the three-dimensional conformation of the molecule is subject to change during the process of docking. See, e. g., Anderson, et al., Chem. Biol.

8: 445-57 (2001). Alternatively, the molecule may be docked as a rigid molecule, wherein the three-dimensional conformation of the molecule is fixed. The three-dimensional conformation of the molecule may be fixed based on a number of factors known in the art, including, but not limited to, an energy-minimization calculation or a known crystal structure of said molecule. Alternatively, the three-dimensional conformation may be fixed based on the structure of a known Neutrokine-alpha ligand.

[0106] The molecular docking process may allow for the conformation of the site on the neutrokine-alpha protein to be flexible. That is, the exact conformation of the Neutrokine-alpha protein may change during the docking process. The exact conformation of the side chains of the amino acids may change due to the molecule binding to or fitting into the site on the neutrokine-alpha protein. A change in the conformation of the protein upon binding of a molecule is a known phenomenon and is often referred to as"induced fit."Several docking algorithms known in the art allow for flexibility in the site on the neutrokine-alpha protein.

[0107] Alternatively, the molecular docking process may allow for the site on the neutrokine-alpha protein to be rigid. Setting the site on the neutrokine-alpha protein to be rigid has an advantage of permitting the molecular docking process to be performed more quickly.

[0108] According to the present invention, a molecule which is used in the above identifying process may be selected from any number of sources. Screening a library, or database, of molecules is a useful method. Structure-based processes of screening one or more libraries of molecules are known in the art. See, e. g., Diller et al., Proteins 43 : 113-24 (2001). For example, a user may randomly select a molecule from a database. A computer may randomly select a molecule from a database. A number of commercially available databases, or libraries, are available, including, but not limited to, Cambridge Structural Database (Cambridge Crystallographic Data Centre); Ligand (Databases of Chemical Compounds and Reactions in Biological Pathways; http ://www. genome. ad. jp/ligand/) ; World Drug Index; National Cancer Institute databases (see http://dtp. nci. nih. gov/docs/33d_database/structural_ information/structuraldata. html); TRIADTM (Paul A. Bartlett, University of California, Berkley); Unity (Tripos, Inc. ) and others.

[0109] A user may build a molecule according to the user's predetermined criteria and then use that molecule in the identifying process.

[0110] A user or computer may apply one or more initial filters to the database, or library, of compounds, thereby producing a smaller and more focused database. Such filtering methods are known in the art. For example, a user or computer may apply"Lipinski's Rules"to remove compounds which are believed to be poor drug candidates. See, e. g. , Lipinski, C. A., J. Pharmacol. Toxicol.

Methods 44 : 235-249 (2000). A molecule, selected from the resulting database containing molecules that are believed to be more drug like, is then used in the above identifying process.

[0111] Additionally, a user or computer may apply one or more filters to the molecules selected for testing so that one or more chemical groups are either present in or absent from the molecules selected. For example, a user or computer may select molecules which contain at least one or two aromatic rings.

Alternatively, a user or computer may select molecules which contain one or more negatively charged functional groups. Other parameters which may be used to filter molecules comprise the presence or absence of one or more phenyl rings; one or more pyridine rings; and one or more aromatic rings.

[0112] Additionally, a user or computer may apply a filter which selects a molecule based on its ADME properties. ADME properties refer to absorption, distribution, metabolism, and excretion properties of a molecule. For a molecule to be selected as a drug candidate to be developed into a drug, the ADME properties of the molecule should be acceptable, as is known in the art. See, e. g., Selick, H. E. et al.,"The emerging importance of predictive ADME simulation in drug discovery,"DrugDiscov. Today 7: 109-116 (2002).

[0113] Alternatively, a user may construct a molecule using a software program and then subject said molecule to a docking algorithm. Such a process may utilize the user's knowledge and intuition regarding the identification of biologically active molecules.

[0114] Certain of the processes described herein as being suitable to be employed to identify a molecule which binds to a Neutrokine-alpha protein may also be referred to as processes of virtual screening. Virtual screening is known in the art and is as described more fully in Walters et al.,"Virtual screening-an overview,"Drug Discov. Today 3 : 160-178 (1998). It is understood that a process of virtual screening can be employed to identify a molecule which binds to a Neutrokine-alpha protein.

[0115] A number of software programs can be employed to identify a molecule that binds to or fits into a site on the neutrokine-alpha protein. Such programs include, but are not limited to, Dock (Ewing et al., J. Comput. Aided Mol. Des.

15 : 411-28 (2001)) ; AutoDockTM (Scripps ResearchInstitute ; Morris, G. M. , et al., J. Comp. Chem. 19: 1639-1662 (1998) ) ; Slide (Leslie Kuhn of Michigan State University); Flex (Tripos, Inc. ) ; FlexE (Claussen, H., et al., J. Mol. Biol.

308 : 377-95 (2001); ICMTM (Internal Coordinate Mechanics); QXPTM ; Ecepp/ProdockTM ; ProLEADSTM ; Hammerhead ; FLOGTM ; GOLD ; LUDITM ; GREENTM ; X-Ligands (Accelrys, Inc. ) ; Glide (Schrödinger, Inc. ); and Galaxy (AM Technologies, Inc.).

[0116] According to the present invention, a genetic algorithm may be employed to identify or design a molecule which binds to a Neutrokine-alpha protein. Such genetic algorithms are known in the art. See, e. g. , Pegg, S. C., et aL, J Coniput.

Aided Mol. Des. 15 : 911-33 (2001).

[0117] Additional, suitable processes which can be employed to identifying or designing a molecule which binds to a Neutrokine-alpha protein include those processes disclosed in U. S. Patent Nos. 6,389, 378; and 6,308, 145.

Design of a Molecule that Binds to a Neutrokine-alpha [0118] There are a number of well-known processes that can be employed to design a molecule which binds to a Neutrokine-alpha protein. Any number of processes which are known in the art can be employed to design a molecule which binds to a Neutrokine-alpha protein. In general, computational methods of designing a molecule according to the present invention are preferred. The particular aspects of computational drug design are well known in the art.

[0119] According to the present invention, a NMR-based process of designing a molecule which binds to a Neutrokine-alpha protein can be used. For example, a method commonly known as"SAR by NMR"can be used to design a molecule.

SAR by NMR is described in detail in Shuker, S. B., et al.,"Discovering High-Affinity Ligands for Proteins: SAR by NMR,"Science 274 : 1531-1534 (1996) and in U. S. Patent Nos. 5,989, 827 and 5,891, 643. Briefly and in general, the SAR by NMR method comprises using 15N-and'H-amide chemical shift changes of the protein upon ligand binding to determine binding location and orientation. The process is repeated with a second ligand in order to identify a second ligand which binds to portion of the protein which is spatially near the binding location of the first ligand. Upon identification of two ligands which bind closely on the protein, a molecule can be designed, said molecule comprising both identified ligands, or portions thereof, and a linker moiety connecting said ligands, or portion thereof.

[0120] According to a SAR by NMR process to be used according to the present invention, a'5N-labeled Neutrokine-alpha protein is prepared according to known methods. The Neutrokine-alpha protein is used in the SAR by NMR process, along with various small molecules which are thought to be capable of binding to the high affinity site. Examples of such small molecule include: benzene, pyrimidine, acetylcholine, amino acids, dipeptides, each of which are optionally substituted. Using the identified ligands, a molecule is designed incorporating a molecule, or fragment thereof, which binds to or fits into the right subsite, and a molecule, or fragment thereof, which binds to or fits into the left subsite. Said designed molecule also incorporates a linker moiety which connects the two identified molecules, or fragments thereof. Such linker moieties may be any suitable functional group or chemical moiety.

[0121] Another suitable process which can be employed to design a molecule which binds to a Neutrokine-alpha protein comprises modifying a known ligand which binds to a Neutrokine-alpha protein, and testing said modified ligand to determine if said modified ligand inhibits, modulates, or regulates said Neutrokine-alpha protein. A starting compound may contain a phenyl ring, for example. A suitable modification may include making a similar compound with a bromine on the phenyl ring. When the bromo compound is made, it can be tested to determine if it inhibits, modulates, or regulates a Neutrokine-alpha protein. The compound may further be modeled using a molecular modeling program and docked onto a model of a Neutrokine-alpha protein.

[0122] Other processes suitable for designing a molecule which binds to a Neutrokine-alpha protein may utilize the atomic coordinates to the high affinity site.

[0123] According to the present invention, a fragment-based design process may be employed to design a molecule which binds to a Neutrokine-alpha protein. In general, a fragment-based process determines which molecular fragments are most likely to have a high affinity for certain portions of the protein. Fragments used may be individual atoms, small fragments of molecules such as a hydroxyl radical, or small molecules such as a water molecule. The process by which the fragments are determined to have a high affinity can vary and can included processes using empirical force fields, random distribution of fragments, Monte Carlo-based approach, a molecular docking process, or other processes. After the given algorithm determines the types of fragments with high affinity for the protein and the location on the protein to which said fragments bind, an overall three-dimensional picture of fragments is produced. All or some of the fragments are then joined to form a molecule, said molecule being one that binds to or fits into the high affinity site. The fragments may be joined to form a molecule using an automated process or a user-based process. In an automated process, a computer determines which chemical linkers are used to connect the fragments.

In a user-based process, a user determines which chemical linkers are used to connect the fragments.

[0124] As described above, in using a fragment-based design process, any number of molecular fragments can be used, such as an oxygen atom, a hydroxyl radical, or a water molecule.

[0125] Additional, suitable processes which can be employed to design a molecule according to the present invention include those processes disclosed in U. S. Patent Nos. 6,226, 603 ; and 5,854, 992.

[0126] Alternatively, a template-based process of designing a molecule can be employed. In a template-based process, a first molecule, which is known to bind to a Neutrokine-alpha protein, is used as a template to design or identify a second molecule which binds to said protein. In this process, the first molecule, herein referred to as the known ligand, may be positioned in a binding site by, for example, using a molecular docking process, which may be either automated or user-controlled. The known ligand may optionally be subjected to an energy minimization process within the binding site. By subjecting the known ligand to such an energy minimization process, the user may determine the most probable three-dimensional conformation of the known ligand when bound to the protein.

[0127] When the known ligand is positioned in the binding site, the known ligand may be used in an automated process to design a molecule. For example, an algorithm which systematically adds a chemical group to or deletes a chemical group from the known ligand can be employed. After the change in the structure of the known ligand, the effect of the change can be determined by computationally determining the interaction between the protein and the modified ligand. If the interaction between the modified ligand and the protein is greater (i. e. , higher affinity) than the interaction between the known ligand and the protein, then the structural modification is determined to beneficial. Provided that the modified ligand binds to the binding site as required herein, the modified ligand is thus determined to be a molecule as designed according to the present invention.

[0128] Alternatively, when the known ligand is positioned in the binding site, the known ligand may be used in a manual process to design a molecule. For example, a user may add a chemical group to or delete a chemical group from the known ligand. Such changes can be made using the knowledge or intuition of the user in conjunction with the teachings herein. After the change in the structure of the known ligand, the effect of the change can be determined by computationally determining the interaction between the protein and the modified ligand. If the interaction between the modified ligand and the protein is greater than the interaction between the known ligand and the protein, then the structural modification is determined to beneficial. Provided that the modified ligand binds to the binding site as required herein, the modified ligand is thus determined to be a molecule as designed according to the present invention.

[0129] A number of software programs can be employed to design a molecule which binds to a Neutrokine-alpha protein. Such programs include, but are not limited to, the following: MCSSTM (Accelrys, Inc.) ; LUDITM (Accelrys, Inc. ) ; SMoG (Harvard University) ; SPROUTTM (University of Leeds); RASSETM (SeeJ : Chem. Inf : Comput. Sci. 36 : 1187-1196 (1996) ) ; MCSS/Hook (Accelrys, Inc.) ; Cerius2TM (Accelrys, Inc. ); CAVEATTM (Lauris etal., J. Comp.-AidedMol.

Design 8 : 51-66 (1994); LeapFrogTM (Tripos, Inc. ) ; GRIDTM (Oxford University ; : Goodford, P., et al., J. Med. Chem. 36 : 148-56 (1993) ) ; and GroupBuild (Vertex, Inc.).

[0130] A further aspect of the present invention is directed to employing a pharmacophore-based process to identify or design a molecule which binds to a Neutrokine-alphaprotein. Pharmacophore-basedprocesses are known in the art.

See, e. g., Kurogi and Guner, "Pharmacophore modeling and three-dimensional database searching for drug design using catalyst,"Curr. Med. Chem.

8 : 1035-1055 (2001). Generally, the process involves the determination of the optimal chemical functional groups that are required in a molecule to bind to or fit into a certain target. The pharmacophore will also usually specify the two-dimensional or three-dimensional relationship among the functional groups.

Using the pharmacophore, one may identify or design a molecule which contains all or most of the functional groups specified by the pharmacophore. Having successfully identified or designed said molecule, one may optionally further test said molecule in a computational manner. One may further synthesize or prepare said molecule. Having synthesized and tested said molecule, one may test said molecule in one or more biological assays, as described below.

[0131] The methods described herein can be employed to design or identify compounds that bind to a Neutrokine-alpha protein.

[0132] In the above processes which utilize the three-dimensional coordinates of a Neutrokine-alpha protein, whether for identifying or designing a molecule according to the present invention, said processes may utilize one or more general processes to determine whether said molecule binds to or fits into the site on the neutrokine-alpha protein. For example, some of processes described herein may utilize a molecular mechanics based process to determine the interaction between said molecule and said site on the neutrokine-alpha protein. Alternatively, certain processes described herein may utilize a semi-empirical based process, such as AMI force field, to determine the interaction between said molecule and said site on the neutrokine-alpha protein. Certain processes described herein may utilize a quantum mechanical based process, such as GAMESS or GAUSSIAN, to determine the interaction between said molecule and said site on the neutrokine-alpha protein. Certain processes described herein may utilize a molecular dynamics based process to determine the interaction between said molecule and said site on the neutrokine-alpha protein. Such processes are known in the art. See, e. g, Halperin, I., et al.,"Principles of docking: An overview of search algorithms and a guide to scoring functions."Proteins 47 : 409-43 (2002).

[0133] For example, according to the present invention, the major groove on the surface of the Neutrokine-alpha trimer has herein been identified as a target for drug discovery and design. A variety of amino acids comprise the groove as described herein. For example, GLU223 forms part of the wall of the groove and prominently displays its terminal carboxyl group. The presence of this negatively charged group of GLU223 can be used to design or identify a compound that will bind to the pocket. Said compound can incorporate a positively charged functional group to interact with the negatively charged carboxyl group of GLU223. Such positively charged groups are well known in the art and include, but are not limited to, amino, guanidinium, histidine, and pyridyl. Other amino acids that form the major groove, or other depressions or cavities, can be similarly identified and used to design or identify, according to the present invention, a compound that binds to a Neutrokine-alpha protein.

[0134] Second, the compound must be able to assume a conformation that allows it to associate with a Neutrokine-alpha protein. Although certain portions of the compound will not directly participate in this association with aNeutrokine-alpha protein, those portions may still influence the overall conformation of the molecule. This, in turn, may have a significant impact on potency. Such conformational requirements include the overall three-dimensional structure and orientation of the chemical entity or compound in relation to all or a portion of a binding site on a Neutrokine-alpha protein, or the spacing between functional groups of a compound comprising several chemical entities that directly interact with a Neutrokine-alpha protein.

[0135] The potential inhibitory or binding effect of a chemical compound on a Neutrolcine-alpha protein may be analyzed prior to its actual synthesis and testing by the use of computer modeling techniques. If the theoretical structure of the given compound suggests insufficient interaction and association between said compound and aNeutrokine-alphaprotein, synthesis andtesting ofthe compound is obviated. However, if computer modeling indicates a strong interaction, the molecule may then be synthesized and tested for its ability to bind to and/or inhibit a Neutrokine-alpha protein using a suitable assay. In this manner, synthesis of inoperative compounds may be avoided or minimized.

[0136] As is known in the art, a number of methods are available to determine whether a compound will interact with a protein. Such methods include general molecular mechanics calculations, semi-empirical methods such as AM1, and quantum mechanical or ab initio calculations such as Jaguar, HondoTM, Games, and Gaussian. Another suitable method includes Hint (eduSoft).

[0137] An inhibitory or other binding compound of a Neutrokine-alpha protein, or portion thereof, may be computationally evaluated and designed by means of a series of steps in which chemical entities or fragments are screened and selected for their ability to associate with the individual binding pockets or other areas of the Neutrokine-alpha protein.

[0138] According to the methods of the present invention, one may design or identify a compound that inhibits or reduces that activity of a Neutrokine-alpha protein. In particular, a compound that inhibits or reduces that activity of a Neutrokine-alpha protein may be a compound that binds to the surface of said Neutrokine-alpha protein and inhibits or reduces the protein's ability to bind to or activate a receptor, such as TACI, BAFF-R, and BCMA. Alternatively, a compound that inhibits or reduces that activity of a Neutrokine-alpha protein may be a compound that binds to the surface of a monomer of said Neutrokine-alpha protein and inhibits or reduces the ability of said monomer to form trimers of Neutrokine-alpha. Alternatively, a compound that inhibits or reduces that activity of a Neutrokine-alpha protein may be a compound that binds to the surface of a trimer of said Neutrokine-alpha protein and inhibits or reduces the ability of said monomer to form dimers of trimers or to form other assemblies of monomers or trimers, of Neutrokine-alpha.

[0139] According to the present invention, one may also design or identify a compound that enhances the activity of aNeutrokine-alpha protein. For example, a compound that enhances the activity of a Neutrokine-alpha protein may be a compound that binds to the surface of a monomer of said Neutrokine-alpha protein and increases the ability of said monomer to form trimers of Neutrokine- alpha. Alternatively, a compound that enhances that activity of a Neutrokine- alpha protein may be a compound that binds to the surface of a trimer of said Neutrokine-alpha protein and increases the ability of said monomer to form dimers of trimers or to form other assemblies of monomers or trimers, of Neutrokine-alpha.

[0140] By way of example, a starting compound used to design a compound that enhances the activity of a Neutrokine-alpha protein is citric acid. As identified in the crystal structure disclosed herein, a citrate molecule interacts with two monomers of the trimeric form of hNeutrokine-alpha protein. Specifically, the negatively charged carboxylate groups of the citrate molecule interact with the positively charged Arg214, Lys 216, His218, and Lys252. By using the molecular modeling methods as described herein, a new compound that binds to the two monomers of hNeutrokine-alpha can be designed using citrate as a template molecule. A model of the citrate molecule may be modified so that a new molecule forms closer and stronger interactions with certain proximate amino acids such as Glu254 and Lys252. Alternatively, a compound can be designed to interact with Phe220 via a pi-cation, hydrophobic, or aromatic interaction. Energy calculations, e. g. , molecular mechanics, Gibbs free energy, HINT, can be performed using the modified compound compared to citrate.

If the interaction energy among the modified compound and the two Neutrokine- alpha monomers is more favorable than the interaction energy among citrate and the two Neutrokine-alpha monomers, then the modified compound is expected to be able to enhance the association of the two monomers.

[0141] One skilled in the art may use one of several methods to screen chemical entities or fragments for their ability to associate with a Neutrokine-alpha protein, or portion thereof, and more particularly with one or more individual binding pockets of the a Neutrokine-alpha protein, or portion thereof. This process may begin by visual inspection of, for example, the three dimensional structure of a Neutrokine-alpha protein on a computer screen, based on the atomic coordinates, or portion thereof, in Table 2. Selected fragments or chemical entities may then be positioned in a variety of orientations, or docked, within a binding pocket of a Neutrokine-alpha protein. Docking may be accomplished using software such as Quanta and SybylTM, followed by energy minimization and molecular dynamics with standard molecular mechanics force fields, such as CHARMMTM (Chemistry at HARvard Macromolecular Mechanics) and AMBERTM.

[0142] Specialized computer programs may also assist in the process of selecting fragments or chemical entities. These include: GRIDTM ; MCSSTM (Multiple Copy Simultaneous Search); AUTODOCKTM ; Flex ; and DOCK.

[0143] Once suitable chemical entities or fragments have been selected, the chemical entities or fragments can be modeled into a single compound or inhibitor. Assembly may be proceed by visual inspection of the relationship of the fragments to each other on the three-dimensional image displayed on a computer screen in relation to the structure coordinates of the Neutrokine-alpha protein. This would be followed by manual model building using software such as Quanta, InsightIITM, or SybylTM.

[0144] Useful programs to aid one of skill in the art in connecting the individual chemical entities or fragments include: CAVEATTM ; MACCS-3DTM ; and HOOK.

[0145] Instead of proceeding to construct a compound that binds to Neutrokine- alpha in a step-wise fashion one fragment or chemical entity at a time as described above, inhibitory or other Neutrokine-alpha-binding compounds may be designed as a whole, or de novo, using either at least a portion of the coordinates of a Neutrokine-alpha protein or optionally including at least a portion of one or more known inhibitors. Computer programs useful for this method include: LUDITM ; LEGENDTM ; LeapFrog, and SMoG (Harvard University).

[0146] In another aspect of the present invention, a library of molecules is searched for one or more compounds that can bind to aNeutrokine-alpha protein, or portion thereof. The library of molecules to be searched can be any library, such as a database (i. e. , online, offline, internal, external) which comprises crystal structures, coordinates, chemical configurations or structures of molecules, compounds, or drugs (referred to collectively as to be assessed or screened for their ability to bind to a Neutrokine-alpha protein). For example, databases for drug design, such as the Cambridge Structural Database (CSD), which includes about 100,000 molecules whose crystal structures have been determined or the Fine Chemical Director (FCD) distributed by Molecular Design Limited (San Leandro, Calif. ) can be used. [CSD: Allen et al., Acta Crystallogr. Section B 35 : 2331 (1979) ]. In addition, a library, such as a database, biased to include an increased number of members which comprise indole rings, hydrophobic moieties and/or negatively-charged molecules can be used.

[0147] According to the present invention, any portion of the structure of a Neutrokine-alpha protein may be used to design a compound that binds to or inhibits a Neutrokine-alpha protein. Preferred portions of the structure include amino acid residues that define a pocket or groove on the surface of the Neutrokine-alpha protein. One set of preferred residues comprises Q148, I150, A151, D152, S153, E154, L169, L170, F172, L201 T202, D203. 1270, S271, L272, D273, G274, and D275 of the A monomer together with T190, Y192, A207, G209, H210, L211, Q213, R214, K216, H218, F220, D222, E223, L224, L226, V227, T228, L229, F230, R231, I233, A251, K252, and E254 of the C monomer. Thus, a preferred aspect of the present invention is a method of designing a compound that binds to a Neutrokine-alpha protein, said method comprising the steps of analyzing computationally a compound to determine if said compound binds to a portion of a Neutrokine-alpha protein wherein said portion comprises Q148, I150, A151, D152, S153, E154, L169, L170, F172, L200, T202, D203, I270, S271, L272, D273, E274, and D275 of the A monomer together with T190, Y192, A207, G209, H210, L211, Q213, R214, K216, H218, F220, D222, E223, L224, L226, V227, T228, L229, F230, R231, I233, A251, K252, and E254 of the C monomer. Preferably, the compound is substantially complementary to the portion of Neutrokine-alpha with respect to polar and lipophilic character of said portion of Neutrokine-alpha.

[0148] Other areas of Neutrokine-alpha are suitable targets for designing or identifying a drug that inhibits or binds to Neutrokine-alpha. Such portions of the Neutrokine-alpha include an area selected from the following: 1) an area defined by Q148, 1150, A151, D152, S153, E154, L169, L170, F172, L200, T202, D203, I270, S271, L272, D273, E274, and D275 of a first monomer together with T190, Y192, A207, G209, H210, L211, Q213, R214, K216, H218, F220, D222, E223, L224, L226, V227, T228, L229, F230, R231, I233, A251, K252, and E254 of a second monomer; 2) an area defined by Q148, I150, A151, D152, S153, E154, L169, L170, F172, L200, T202, D203, I270, S271, L272, D273, E274, D275, and F278 of a first monomer together with T190, Y192, A207, G209, H210, L211, Q213, R214, K216, H218, F220, D222, E223, L224, L226, V227, T228, L229, F230, R231, I233, A251, K252, L253, E254, and D257 of second monomer; and 3) an area defined by the amino acids from A251 to L229, inclusive.

[0149] Another suitable area of a Neutrokine-alpha protein includes an area which comprises amino acids that are within about 30A, 25A, 20A, 15A, 10A, or 5A of an amino acid selectedfromthe group consistingofTHR141-LEU285. In one embodiment, the are comprises amino acids within about 10A or 5A of an amino acid selected from the group consisting of THR141-LEU285.

[0150] An additional aspect of the present invention is a method of designing a compound that mimics the biological activity of aNeutrokine-alpha protein. Said method comprises identifying or designing a compound based on a three- dimensional structure of a Neutrokine-alpha protein, so that said compound resembles at least partially structurally and chemically similar to at least a portion of said Neutrokine-alpha protein. The method further comprises synthesizing and testing said compound for biological activity, preferably for Neutrokine-alpha- like activity.

[0151] An additional aspect of the present invention is a method of designing a compound that is structurally and chemically similar to a Neutrokine-alpha protein, or portion thereof, wherein said method comprises analyzing said compound to determine if said compound is structurally and chemically similar to a Neutrokine-alpha protein, or portion thereof. According to the present invention, the compound is analyzed using the three dimensional structure of a Neutrokine-alpha protein or portion thereof.

[0152] One advantage of the present method is that the method allows one to determine potentially if a compound will have biological activity before synthesizing and assaying said compound. Thus, large numbers of compounds can be analyzed using computational means. Preferred biological activities are either Neutrokine-alpha-inhibitor activity or Neutrokine-alpha-like activity.

[0153] Various computational analyses are necessary to determine whether a molecule or portion thereof is sufficiently similar to all or part of a three- dimensional structure of a Neutrokine-alpha protein. Such analyses may be carried out with computer programs that are well known in the art, such as QUANTA. In particular, the Molecular Similarity module of QUANTA is used.

[0154] The Molecular Similarity module permits the comparisons between different structures, different conformations of the same structure, and different parts of the same structure. The procedure used in Molecular Similarity to compare structures comprises the following four steps: 1) input the structures to be compared; 2) define the atom equivalence in the structures; 3) perform a fitting, i. e. , superposition, operation; and 4) analyze the results.

[0155] In the above steps, one structure is identified as the target, i. e., the fixed structure; all the remaining structures are working structures, i. e., moving structures. Since atom equivalency within QUANTA is defined by user input, root mean square deviation (RMSD) values can be determined in a number of ways. When comparing the structures of peptides, using the C, backbone carbons provides preferable results.

[0156] According to the methods of the present invention, a compound will be chemically similar to a Neutrokine-alpha protein, or portion thereof, if said compound resembles said Neutrokine-alpha protein or portion thereof in terms of one of more of the following chemical characteristics: lipophilicity; logP ; hydrophilicity; polarity; aromatic character; hydrogen bonding character; and presence of charged moieties. Thus, after determining that a compound is structurally similar to a Neutrokine-alpha protein, or portion thereof, one may determine if said compound is chemically similar to the Neutrokine-alpha protein, or portion thereof. Comparisons may be made based on the presence or absence of chemical functional groups. Additionally, comparisons may be made based on the overall lipophilicity of the compound compared to the overall lipophilicity of the Neutrokine-alpha protein, or portion thereof.

[0157] A preferred aspect of the present invention is identifying or designing a compound that mimics, antagonizes, or inhibits Neutrokine-alpha activity, wherein said compound is a cyclic or rigid peptide that is structurally and chemically similar to a Neutrokine-alpha protein or portion thereof.

[0158] Another preferred aspect of the present invention designing a compound that mimics, antagonizes, or inhibits Neutrokine-alpha activity, wherein said compound is a cyclic or rigid peptidomimetic that is structurally and chemically similar to a Neutrokine-alpha protein or portion thereof.

[0159] In an additional embodiment, the present invention is directed to a method of designing or identifying a drug which fits into or binds to a groove on the surface of a neutrokine-alpha protein trimer. Preferably the groove is as described above, although other grooves are included within the scope of the invention. In particular, the groove is created by loops from two adjacent monomers. One wall of the groove contains loop DE with some residues of loops aa'and GH, and the other wall of the groove contains loops EF, Aa, and a'A".

The deepest portion of the groove consists primarily of beta-strands D, E, and F.

Residues with surface accessible side chains are ALA207, LEU211, GLN213, and ARG214 from strand D; THR228, LEU229, PHE230, ARG231, and ILE233 from strand E; and ALA251, LYS252, LEU253, GLU254, and ASP257 from strand F. Any of the methods described herein can be used to identify or design a drug that binds to or fits into said groove.

[0160] In another embodiment of the present invention, the binding affinity of said a molecule designed or identified according to the present invention is determine. The binding affinity can be calculated using computational methods which are known in the art, or can be calculated empirically using assays as described herein or are known in the art.

[0161] In another embodiment, the present invention is directed to a method of designing or identifying a compound which binds to or fits into the hydrated magnesium ion binding site. A compound which binds to or fits into the hydrated magnesium ion binding site is able to disrupt the trimerization of the monomers and thus would inhibit, decrease, or modulate the activity of neutrokine-alpha.

[0162] Any portion of the three dimensional structure of a Neutrokine-alpha protein may be used to design, or screen for, a compound that is structurally and chemically similar to said Neutrokine-alpha protein or portion thereof. Preferred portions of the three-dimensional structure of a Neutrokine-alpha protein for use in the aforementioned methods include one or more of the p-sheets a, a', A, A', B, B', C, D, E, F, G, and H; one or more of the loops between a and a' ; between a and A; between A and A" ; between A"and B' ; between B'and B; between B and C; between C and D; between D and E; between E and F; between F and G; and between G and H. Additionally, portions of each of the aforementioned ß- sheets and loops may be used. Particularly preferred portions of the three dimensional structure of a Neutrokine-alpha protein are one or more of (3-sheets a, a', A, and A' ; and one or more of loops between a and a' ; between a and A; between C and D; between D and E; between E and F; between F and G; and between G and H.

[0163] Additionally, combinations of the aforementioned (3-sheets and loops may be used to design, or screen for, a compound that is structurally and chemically similar to said Neutrokine-alpha protein or portion thereof. For example, the method of the present invention can be used to design, or screen for, a compound that is similar in shape and chemical attributes to a the overall shape of the D and E p-sheets.

[0164] As used herein, with respect to a Neutrokine-alpha protein or analogue thereof, or with respect to a region of a Neutrokine-alpha protein or analogue thereof, the phrase"at least a portion of the three-dimensional structure of'or"at least a portion of'is understood to mean a portion of the three-dimensional surface structure of the Neutrokine-alpha protein, or region of the Neutrokine- alpha protein, optionally including charge distribution and hydrophilicity/hydrophobicity characteristics, formed by at least three, more preferably at least three to ten, and most preferably at least ten contiguous amino . acid residues of the Neutrokine-alpha monomer, dimer or trimer. The contiguous residues forming such a portion may be residues which form a contiguous portion of the primary structure of the Neutrokine-alpha molecule, residues which form a contiguous portion of the three-dimensional surface of the Neutrokine-alpha monomer, residues which form a contiguous portion of the three-dimensional surface of the Neutrokine-alpha dimer, residues which form a contiguous portion of the three-dimensional surface of the Neutrokine-alpha trimer, or a combination thereof. Thus, the residues forming a portion of the three-dimensional structure of the Neutrokine-alpha protein need not be contiguous in the primary sequence of the Neutrokine-alpha protein but, rather, must form a contiguous portion of the surface of the Neutrokine-alpha protein. In particular, such residues may be non-contiguous in the primary structure of a single Neutrokine-alpha protein monomer or may comprise residues from different Neutrokine-alpha protein monomers in the dimeric or trimeric form of the Neutrokine-alpha protein. As used herein, the residues forming"aportion of the three-dimensional structure of' a Neutrokine-alpha protein, or"a portion of'a Neutrokine-alpha protein, form a contiguous three-dimensional surface in which each atom or functional group forming the portion of the surface is separated from the nearest atom or functional group forming the portion of the surface by no more than about 40 A, preferably by no more than about 20 Å, more preferably by no more than about 5-10 Å, and most preferably by no more than about 1-5 Å.

[0165] As used herein, the term"X-ray crystallographic co-ordinates"refers to a series of mathematical co-ordinates (represented as"X","Y"and"Z"values) that relate to the spatial distribution of reflections produced by the diffraction of a monochromatic beam of X-rays by atoms of a molecule in crystal form. The diffraction data are used to generate electron density maps of the repeating units of a crystal, and the resulting electron density maps are used to define the positions of individual atoms within the unit cell of the crystal.

[0166] As will be apparent to those of ordinary skill in the art, the hNeutrokine- alpha structure presented herein, and other three dimensional structures of Neutrokine-alpha proteins determined according to the methods described herein, are independent of their orientation, and that the atomic coordinates listed in TABLE 2 merely represent one possible orientation of the human Neutrokine- alpha structure. It is apparent, therefore, that the atomic coordinates listed in TABLE 2 may be mathematically rotated, translated, scaled, or a combination thereof, without changing the relative positions of atoms or features of the hNeutrokine-alpha structure. Such mathematical manipulations are intended to be embraced herein. Furthermore, it will be apparent to the skilled artisan that the X-ray atomic coordinates defined herein have some degree of uncertainty in location. Accordingly, for purposes of this invention, a preselected protein or peptide having the same amino acid sequence as at least a portion of Neutrokine- alpha is considered to have the same structure as the corresponding portion of Neutrokine-alpha, when a set of atomic co-ordinates defining backbone Ca atoms of the preselected protein or peptide can be superimposed onto the corresponding Ca atoms for Neutrokine-alpha to a root mean square deviation of preferably less than about 3.0, 2.5, 2.0, 1.5, 1.4, 1.3, 1.2. 1.1. or 1. 0 A, and most preferably less than about 0.95, 0.90, 0.85, 0.80, 0.75, 0.70, 0.65, 0.60. 0.55, or 0.50 A. In one embodiment, the neutrokine-alpha structure comprises the coordinates shown in Table 2, or a portion thereof. In another embodiment, the neutrokine-alpha structure comprises the coordinates provided in Accession I. D. No.: 1KXG, (deposited January 31,2002) of the Protein Data Bank, or a portion thereof.

(H. M. Berman, et al., The Protein Data Bank. Nucleic Acids Research, 28 pp.

235-242 (2000) ). In another embodiment, the neutrokine-alpha structure comprises the coordinates provided in Table 2, or portion thereof, having undergone a routine energy-minimization process. In another embodiment, the neutrokine-alpha structure comprises the coordinates provided in Accession I. D.

No.: 1KXG, or portion thereof, having undergone a routine energy-minimization process.

[0167] According to the methods of the present invention, the atomic coordinates of a Neutrokine-alpha protein in crystalline form may be used in various ways.

When the atomic coordinates of a Neutrokine-alpha protein in crystalline form are used, the entire set of coordinates of the protein, including associated water molecules, citrate molecules, dioxane molecules, and magnesium ions, may be used. Alternatively, a portion of the atomic coordinates of Neutrokine-alpha in crystalline form may be used according to the methods of the present invention.

A portion of the coordinates that may be used according to the present invention include coordinates that comprise, or alternatively consist of, the coordinates of an amino acid sequence selected from the group consisting of residues: T-141 to T-155; V-142to P-156 ; T-143 to T-157; Q-144 to I-158 ; D-145 to Q-159; C-146 to K-160; L-147 to G-161; Q-148 to S-162; L-149 to Y-163; I-150 to T-164; A-151 to F-165 ; D-152 to V-166; S-153 to P-167; E-154 to W-168; T-155 to L-169; P-156 to L-170; T-157 to S-171; I-158 to F-172; Q-159 to K-173; K-160 to R-174; G-161 to G-175; S-162 to S-176; Y-163 to A-177; T-164 to L-178 ; F-165 to E-179; V-166 to E-180; P-167 to K-181; W-168 to E-182; L-169 to N-183 ; L-170 to K-184 ; S-171 to I-185 ; F-172 to L-186 ; K-173 to V-187; R-174 to K-188 ; G-175 to E-189 ; S-176 to T-190; A-177 to G-191; L-178 to Y-192; E-179 to F-193; E-180 to F-194; K-181 to I-195 ; E-182 to Y-196; N-183 to G-197; K-184 to Q-198 ; I-185 to V-199 ; L-186 to L-200 ; V-187 to Y-201 ; K-188 to T-202; E-189 to D-203; T-190 to K-204; G-191 to T-205; Y-192 to Y-206; F-193 to A-207; F-194 to M-208; I-195 to G-209; Y-196 to H-210; G-197 to L-211 ; Q-198 to I-212 ; V-199 to Q-213 ; L-200 to R-214 ; Y-201 to K-215 ; T-202 to K-216; D-203 to V-217; K-204 to H-218; T-205 to V-219; Y-206 to F-220; A-207 to G-221; M-208 to D-222; G-209 to E-223; H-210 to L-224; L-211 to S-225; I-212 to L-226; Q-213 to V-227; R-214 to T-228; K-215 to L-229; K-216 to F-230; V-217 to R-231; H-218 to C-232; V-219 to I-233 ; F-220 to Q-234; G-221 to N-235; D-222 to M-236; E-223 to P-237; L-224 to E-238; S-225 to T-239; L-226 to L-240; V-227 to P-241; T-228 to N-242; L-229 to N-243; F-230 to S-244; R-231 to C-245; C-232 to Y-246; I-233 to S-247; Q-234 to A-248; N-235 to G-249; M-236 to I-250 ; P-237 to A-251; E-238 to K-252; T-239 to L-253; L-240 to E-254; P-241 to E-255; N-242 to G-256; N-243 to D-257; S-244 to E-258; C-245 to L-259; Y-246 to Q-260; S-247 to L-261; A-248 to A-262; G-249 to I-263 ; I-250 to P-264; A-251 to R-265; K-252 to E-266; L-253 to N-267; E-254 to A-268; E-255 to Q-269; G-256 to I-270 ; D-257 to S-271; E-258 to L-272; L-259 to D-273; Q-260 to G-274; L-261 to D-275; A-262 to V-276; I-263 to T-277; P-264 to F-278; R-265 to F-279; E-266 to G-280; N-267 to A-281; A-268 to L-282; Q-269 to K-283; I-270 to L-284; and S-271 to L-285 of the sequence listed in Table 2. Additionally, coordinates comprising, or alternatively, consisting of, coordinates of an amino acid sequence at least 80%, 85%, 90%, 92%, 95%, 96%, 97%, 98% or 99% identical to an amino acid sequence described above.

Methods of Assaying Compounds that Interact with Neutrokine-alpha [0168] It is possible to define ligand interactions with a Neutrokine-alpha protein.

Exemplary methods include the following.

[0169] (1) Effects of ligand binding upon protein intrinsic fluorescence (e. g., of tryptophan). Binding of either natural ligands or inhibitors may result in enzyme conformational changes which alter the fluorescence of a Neutrokine-alpha protein.

[0170] (2) Spectral effects of ligands. Where the ligands themselves are either fluorescent or possess chromophores that overlap with enzyme tryptophan fluorescence, binding can be detected either via changes in the ligand fluorescence properties (e. g., intensity, lifetime, or polarization) or fluorescence resonance energy transfer with enzyme tryptophans.

0171l (3) Thermal analysis of the Neutrokine-alpha: ligand complex. Using calorimetric techniques (e. g., isothermal calorimetry or differential scanning calorimetry), it is possible to detect thermal changes, or shifts in the stability of a Neutrokine-alpha protein which reports and therefore allows the characterization of ligand binding.

[0172] (4) Surface plasmon resonance spectroscopy. A BIACORE Surface plasmon resonance analyzer can be used to measure binding of a ligand to a Neutrokine-alpha protein.

[0173] Additional methods are known in the art and are disclosed in, for example, WO 98/18921, published May 7,1998 ; and WO 00/50597, published August 31,2000.

Computer-Related Embodiments [0174] Another aspect of the present invention is a computer readable medium comprising a the three-dimensional structure of a Neutrokine-alpha protein or a portion thereof. The X-ray diffraction data, atomic coordinate data, and amino acid sequence data of the present invention can be provided as a manufacture in a variety of media to facilitate use thereof. As used herein, "computer readable medium refers to any medium which can be read and accessed directly by a computer. Such a medium includes, but is not limited to, magnetic storage media, such as floppy discs, hard disc storage medium, and magnetic tape; optical storage media such as optical discs or CD-ROM; electrical storage media such as RAM and ROM; and hybrids of these categories such as magnetic/optical storage media. A skilled artisan can readily appreciate how any of the presently known computer readable media can be used to create a manufacture comprising a computer readable medium having recorded thereon the X-ray diffraction data, atomic coordinate data, or amino acid sequence data of the present invention.

[0175] A variety of data storage structures are available to a skilled artisan for creating a computer readable medium having recorded thereon the above- described data. The choice of the data storage structure will generally be based on the means chosen to access the stored information. For example, the data can be represented in a word processing text file, formatted in commercially-available software such as WordPerfect and MICROSOFT Word, or represented in the form of an ASCII file, stored in a database application, such as DB2, Sybase, Oracle, or the like. A skilled artisan can readily adapt any number of data processor structuring formats (e. g. , text file or database) in order to obtain a computer readable medium according to the present invention.

[0176] By providing on computer readable media having stored thereon the above-described data, a skilled artisan can routinely access the amino acid sequence, atomic coordinate, or X-ray diffraction data to model a nuclear receptor ligand using model building methods known in the art or described herein.

Computer algorithms are publicly and commercially available which allow a skilled artisan to access this data provided on a computer readable medium and analyze it for structure determination and rational design of ligands. See, e. g., Biotechnology Software Directory, Mary Ann Liebert Publ. , New York (1995).

[0177] The present invention further provides systems, particularly computer- based systems, which contain the amino acid sequence data, diffraction data, and/or atomic coordinate data described herein. Such systems are designed to perform structure determinations of nuclear receptors and the rational design of their ligands. Non-limiting examples are microcomputer workstations available from SGI or Sun Microsystems running Unix-based, Windows NT, or IBM OS/2 operating systems.

[0178] As used herein, "a computer-based system"refers to the hardware means, software means, and data storage means used to analyze the amino acid sequence data, X-ray diffraction data, and/or atomic coordinate data of the present invention. The minimum hardware means of the computer-based systems of the present invention comprises a central processing unit (CPU), input means, output means, and data storage means. A skilled artisan can readily appreciate which of the currently available computer-based system are suitable for use in the present invention. A monitor is optionally provided to visualize structure data.

[0179] As used herein, "data storage means"refers to memory which can store the data of the present invention, or a memory access means which can access manufactures having the data recorded thereon. As used herein,"data-analyzing means"refers to one or more of the above-described or art-known computer algorithms which are capable of analyzing stored amino acid sequence data, X-ray diffraction data, and/or atomic coordinate data and producing a refined model of the three dimensional structure of a neutrokine-alpha protein.

[0180] Alternatively, the three dimensional structure of a Neutrokine-alpha protein, or portion thereof, can be stored on a computer readable medium via the "data storage means"described above. After being retrieved, data corresponding to the model can be analyzed by the"data analyzing means. "In such a scenario, the data-analyzing means refers to any of the known computer algorithms (described below), which, based on the model of the neutrokine-alpha protein, indicates the three dimensional structure of compounds capable of binding to the neutrokine-alpha protein. Such candidate ligands, may act as a agonist or antagonist of the neutrokine-alpha protein pathway. Methods for determining whether a compound acts as an agonist or antagonist of a neutrokine-alpha protein are described above.

EXAMPLES Example 1 Human Neutrokine-alpha in Crystalline Form [0181] Human Neutrokine-alpha protein in crystalline form was prepared according to the method described in Example 2 or 3. The space group was hexagonal having unit cell dimensions of a = 123.58 A, b = 123. 58 A, c = 161.23 A, a = 90, p = 90, and y = 120 and was later determined to be P65.

Crystal density measurements using Ficoll gradients indicated (Z=6) six Neutrokine-alpha monomers/asymmetric unit. For more details regarding Ficoll gradients, see Westbrook, E. M. Methods Enzymol. 114 : 187-96 (1985). The Matthew's coefficient for these crystals was calculated to be 3.58 A3/Da with solvent content of 65%, using 912 residues.

Example 2 Preparing Human Neutrokine-alpha in Crystalline Form [0182] Isolation of full length Neutrokine-alpha cDNA. The BLAST algorithm was used to search the Human Genome Sciences Inc. expressed sequence tag (EST) database for sequences with homology to the receptor-binding domain of the TNF family. A full lengthNeutrokine-alpha clone was identified, sequenced and submitted to GenBank (Accession number AF132600). The Neutrokine- alpha open reading frame was PCR amplified utilizing a 5'primer (5'-CAG ACT GGA TCC GCC ACC ATG GAT GAC TCC ACA GAA AG-3') annealing at the predicted start codon and a 3'primer (5'-CAG ACT GGT ACC GTC CTG CGT GCA CTA CAT GGC-3') designed to anneal at the predicted downstream stop codon. The resulting amplicon was tailed with Bam HI and Asp 718 restriction sites and subcloned into a mammalian expression vector. Neutrokine-alpha was also expressed in p-CMV-1 (Sigma Chemicals).

[0183] Purification of recombinant human Neutrokine-alpha. Neutrokine-alpha protein was expressed in insect Sf9 cells using a recombinant baculovirus system as described in Moore et al., Science 285 : 260-263 (1999). Sf9 cell supernatant was treated with 10 mM calcium chloride in slightly alkaline conditions.

Neutrokine-alpha was purified through a Poros PI-50 (Applied BioSystem, Framingham, MA) column and a Toyopearl Hexyl 650C (TosoHaas, Montgomeryville, PA) column. The final purified Neutrokine-alpha protein was diafiltered into a buffer containing 10 mM sodium citrate, 140 mM sodium chloride pH 6.

[0184] Crystallization. The sparse matrix approach was used to screen for crystals. See Jancarik, J. & Kim, S. H. ,"Sparse matrix sampling: a screening method for crystallization of proteins."J. Appl. Cryst. 24 : 409-411 (1991) for full details.

[0185] Crystal Screen II (Hampton Research, Riverside CA), condition #4, 35% (w/v) dioxane in water provided crystals. Using a fresh Hampton kit required the addition of divalent cations (Mg2+ or Zn2+) to obtain high-resolution crystals.

Crystals were grown in hanging drops containing 1 mL of 20 mg/mL hNeutrokine-alpha in 25 mM sodium citrate, 125 mM NaCl, pH 6 and 1 mL of 25% dioxane, 25 mM MgCl2 suspended over a reservoir of 25% dioxane, 25 mM MgCl2. Crystals formed overnight.

Example 3 Preparing Human Neutrokine-alpha in Crystalline Form [0186] Isolation of full length Neutrokine-alpha cDNA. The BLAST algorithm was used to search the Human Genome Sciences Inc. expressed sequence tag (EST) database for sequences with homology to the receptor-binding domain of the TNF family. A full length Neutrokine-alpha clone was identified, sequenced and submitted to GenBank (Accession number AF132600). The Neutrokine- alpha open reading frame was PCR amplified utilizing a 5'primer (5'-CAG ACT GGA TCC GCC ACC ATG GAT GAC TCC ACA GAA AG-3') annealing at the predicted start codon and a 3'primer (5'-CAG ACT GGT ACC GTC CTG CGT GCA CTA CAT GGC-3') designed to anneal at the predicted downstream stop codon. The resulting amplicon was tailed with Bam HI and Asp 718 restriction sites and subcloned into a mammalian expression vector. Neutrokine-alpha was also expressed in p-CMV-1 (Sigma Chemicals).

[0187] Purification of recombinant human Neutrokine-alpha. Neutrokine-alpha protein was expressed in insect Sf9 cells using a recombinant baculovirus system as described in Moore et al., Science 285 : 260-263 (1999). Sf9 cell supernatant was treated with 10 mM calcium chloride in slightly alkaline conditions.

Neutrokine-alpha was purified through a Poros PI-50 (Applied BioSystem, Framingham, MA) column, Sephacryl S200 size exclusion (Amersham Pharmacia Biotech), a Toyopearl Hexyl 650C (TosoHaas, Montgomeryville, PA) column, and a DEAE sepharose column (Amersham Pharmacia Biotech). The final purifiedNeutrokine-alphaprotein was diafiltered into a buffer containing 25 mM sodium citrate, 125 mM sodium chloride pH 6.

[0188] Crystallization. The sparse matrix approach was used to screen for crystals. See Jancarik, J. & Kim, S. H. ,"Sparse matrix sampling: a screening method for crystallization ofproteins."J 4ppL Cryst. 24 : 409-411 (1991) for full details.

[0189] Crystal Screen II (Hampton Research, Riverside CA), condition #4, 3 5% (v/v) dioxane in water provided crystals. Using a fresh Hampton kit required the addition of divalent cations (Mg2+ or Zn2+) to obtain high-resolution crystals.

Crystals were grown in hanging drops containing 1 tL of 20 mg/mL hNeutrokine-alpha in 25 mM sodium citrate, 125 mM NaCl, pH 6 and 1 pL of 25% dioxane, 25 mM MgCl2 suspended over a reservoir of 25% dioxane, 25 mM MgCl2. Crystals formed overnight.

[0190] Crystals were flash-cooled for data collection by rapid transfer into 25% (v/v) glycerol, 25% (v/v) dioxane and 25 mM MgCl2, followed by direct replacement into the liquid nitrogen stream.

Example 4 Preparing NonHuman Neutrokine-alpha in Crystalline Form [0191] Mouse Neutrokine-alpha in crystalline form is prepared according to the method as described for human Neutrokine-alpha. Mouse Neutrokine-alpha has the following sequence: 1 mdesaktlpp pclcfcsekg edmkvgydpi tpqkeegawf gicrdgrlla atlllallss 61 sftamslyql aalqadlmnl rmelqsyrgs atpaaagape ltagvklltp aaprphnssr 121ghrnrrafqg peeteqdvdl sappapclpg crhsqhddng mnlrniiqdc lqliadsdtp 181 tirkgtytfv pwllsfkrgn aleekenkiv vrqtgyffiy sqvlytdpif amghviqrkk 241 vhvfgdelsl vtlfrciqnm pktlpnnscy sagiarleeg deiqlaipre naqisrngdd 301 tffgalkll (GenBank Accession No.: AAD22475; Schneider et al., J. Exp. Med.

189 : 1747-1756 (1999) ). The protein used comprises residues 131-301.

Example 5 Determining the Three-Dimensional Structure of Human Neutrokine-alpha in Crystalline Form [0192] Data collection and processing. The flash cooling of crystals was performed by a quick-transfer of the crystal into an aqueous solution comprising 25% glycerol, 25% dioxane, and 25 mM MgCl2. The solution containing the crystal was directly placed it in the liquid N2 stream. All data were collected from one frozen crystal on the Cornell High Energy Synchrotron Source (CHESS) in Ithaca, NY, on the F1 beam line using the Quantum4 detector. The wavelength was 0.942 A. At a crystal-to-film distance of 190 mm, 40-second exposures of 1° oscillation were collected through 180 degrees of rotation. The crystal was moved, and an additional 70 degrees of data were collected.

Intensities were integrated, reduced, and scaled with the Denzo/Scalepack package. The data collection statistics are shown in below.

[0193] Molecular Replacement. Starting models were chosen from the homologs: TNF (Protein Data Bank Entry Number: 1TNR), Apo2L/TRAIL (Protein Data Bank Entry Number: 1 DOG) and CD40 Ligand (Protein Data Bank Entry Number: lALY) using monomers and/or trimers that have been stripped of side-chains. A model for Amore (Navaza, 2001) was created from Apo2L/TRAIL in which the side-chains of residues identical (based on sequence alignments) between it and Neutrokine-alpha were not removed. This"pruned" model gave the best statistics (see Tables 1A and 1B) and was used to find first one trimer and then the other trimer to complete the asymmetric unit. The TNF- (3 model had offered the same solution. CNS (Brunger, A. T. et al., ActaCrystallogr.

D. 54 : 905-921 (1998) ) was used to calculate the phases and to create a solvent flattened map calculated with 60% solvent content using SIGMAA weighting (Read, R. J. Acta Crystallogr. A 42 : 140-149 (1986) ). This solvent flattened map, with the phases calculated from the model and Amore solution at both 3.5 A and 2.0 A, was fully interpretable. All the segments of protein structure that differed between the model and Neutrokine-alpha were apparent in this map, including new loops, disulfide bonds, and density of ligand.

[0194] Model building and Refinement. One monomer of 143 amino acids was modeled within 48 hours and then duplicated using the"lsq"module in O (http ://www. imsb. au. dk/-mok/o/) onto the other 5 location in the asymmetric unit. One round of simulated annealing at 2000 °C with maximum likelihood refinement resulted in R of 25.97% and Rif,, Subsequent cycles of refinement involved addition of metals, ligands (citrate and dioxane), and water molecules to a values of R and Rfree of 19.2% and 21.2% and final values of R and Rfree of 18.9% and 20.9%, respectively. The calculations were performed on data with F>la (F) using 7486 scattering atoms. Residues 134-141 of each of the monomers were unobserved, and residues 104-106 in each monomer had weak density.

@ Table 1A. Resolution limits (A) of data collected 30. 0-2.0 Number of reflections-total 1, 940,104 - unique 93,234 Completeness (%) -overall 99.3 - last shell (2. 03 A-2. 0 A) 86.6 Rsym (%) -overall 8.3 - last shell (2. 03 Å -2.0 Å) 39. 4 Molecular replacement-model PDB entry 1DOG - resolution range (A) 30.0-4. 5 - factor for a trimer 52.4 - correlation for trimer 12.2 - factor for two trimers 49.8 - correlation for two trimers 25.8 Refinement-resolution range (A) 25.0-2. 0 - number of reflections in working set 91,331 - number of reflections used for Rfree 1849 (5%) - Rcryst 19.2 - Rfree 21. 2 - number of atoms in protein 6865 - number of ligand atoms 108 - number of water molecules 513 Geometry-deviations in bond length (A) 0.007 - deviations in bond angles (°) 1.31 Table 1B. Resolution limits (A) of data collected 30. 0-2.0 Number of reflections-total 1,940, 104 - unique 93, 234 Completeness (%)-overall 99.3 - last shell (2. 03 A-2. 0 Å) 86. 6 Rsym (%)-overall 8. 3 -last shell (2. 03 A-2. 0 A) 39.4 Molecular replacement-model PDB entry 1DOG - resolution range (A) 30.0-4. 5 - Rfactor for a trimer 52.4 - correlation for trimer 12.2 - Rfactor for two trimers 49.8 - correlation for two trimers 25.8 Refinement-resolution range (A) 25.0-2. 0 - number of reflections in working set 91,331 - number of reflections used for Rfree 1849 (5%) - Rcryst 18.9 - Rfree 20.9 - number of atoms in protein 6858 - number of ligand atoms 153 - number of water molecules 462 Geometry-deviations in bond length (A) 0.007 - deviations in bond angles (°) 1.30 Example 6 Energy Minimization of Neutrokine-Alpha Structure [0195] The coordinates of IKXG were subjected to an energy minimization process. Specifically, missing atoms, such as hydrogen atoms were removed, as well as water molecules. The resulting dimer of trimers was minimized using the Powell minimization algorithm, first without electrostatics for 100 cycles. The coordinates resulting from the Powell minimization were then subjected to a second minimization using electrostatic and van der Waals forces using the Tripos60 algorithm. The resulting total energy of the minimized dimer of trimers was approximately-2639 Kcal/mol. The root mean square deviation between the minimized protein structure and the unminimized protein structure (i. e., IKXG) was about 0.27 A, calculated based on alpha-carbon backbone. Table 6 below provides the coordinates a single monomer of the energy-minimized neutrokine- alpha protein.

Example 7 Determining the Solvent Accessible Surface of Human Neutrokine-alpha in Crystalline Form [0196] The coordinates of Table 2 are used to display the structure of hNeutrokine-alpha using a suitable computer program, such as Sybyl 6.5.

Oxygen atoms of associated water molecules are deleted. According to accepted and standard protocol, hydrogen atoms and atomic charges are added to the structure. The structure is then minimized using a standard molecular mechanics force field, such as the Tripos force field. The solvent accessible surface is then calculated and displayed using the MOLCADTM module. The resulting structure and visualization provide a graphical display of the solvent accessible surface of a dimer of trimerized human Neutrokine-alpha. This graphical display can then be further used to identify potential binding sites for molecules and receptors.

Example 8 Determining the Molecular Lipophilic Potential Surface of Human Neutrokine-alpha in Crystalline Form [0197] The coordinates of Table 2 corresponding to one trimer are used to display the structure of hNeutrokine-alpha using a suitable computer program, such as Sybyl 6.5. Oxygen atoms of associated water molecules are deleted. According to accepted and standard protocol, hydrogen atoms and atomic charges are added to the structure. The structure is then minimized using a standard molecular mechanics force field, such as the Tripos force field. The solvent accessible surface is then calculated and displayed using the MOLCADTM module. The resulting structure and visualization provides the a graphical display of the lipophilic potential surface of a dimer of trimerized human Neutrokine-alpha.

This graphical display can then be further used to identify potential binding sites for molecules and receptors. Specifically, an area of low lipophilic potential is identified as potential binding site for a hydrophilic moiety of a compound.

Example 9 Determining the Structure of Modified Human Neutrokine-alpha by Molecular Modeling [0198] The coordinates of hNeutrokine-alpha listed in Table 2 are entered into a computer system using a standard molecular modeling software program such as SYBYL 6.5, according to the known procedures. Hydrogen atoms are added to the coordinates. Charges are assigned to each of the atoms according to known routines. The structure of human Neutrokine-alpha is then further minimized using a molecular mechanics force field such as AMBER. Phenylalanine-220, located in the D-E loop is changed to an alanine residue (i. e., F220--> A220 mutation). The local region ofthe structure comprising the atoms ofthe D-E loop are then subject to molecular mechanics minimization again. The resulting structure provides the three dimensional structure of a modified hNeutrokine- alpha protein, specifically of F220A hNeutrokine-alpha. The solvent accessible surface is optionally calculated and displayed to provide an additional representation of the three dimensional structure of a modified human Neutrokine-alpha protein.

Example 10 Determining the Structure of mouse Neutrokine-alpha by Homology Modeling [0199] A model of the mouse Neutrokine-alpha is constructed using Quanta version 4.1 [Molecular Simulations Inc, Burlington, Mass.]. Specifically, the MODELER module within Quanta is used. Alternatively, the MODELER module of INSIGHT II may be used. The coordinates of hNeutrokine-alpha, as listed in Table 2, are used as the template structure. The sequence of mouse Neutrokine-alpha is provided in Example 3.

[0200] Residues 131-301 of mouse Neutrokine-alpha are used to construct the three-dimensional model of mouse Neutrokine-alpha. According to standard and well-known methods, hydrogen atoms and atomic charges are added to the resulting three-dimensional model of mouse Neutrokine-alpha. A representation of the solvent accessible surface of the mouse Neutrokine-alpha is optionally added to and displayed on the three-dimensional model of mouse Neutrokine- alpha. A representation of the lipophilic potential is optionally added to and displayed on the three-dimensional model of mouse Neutrokine-alpha.

Example 11 Designing A Compound that Binds to hNeutrokine-alpha [0201] The three-dimensional structure of hNeutrokine-alpha as a trimer is displayed on a suitable computer system. Specifically, hNeutrokine-alpha as a trimer corresponds to atoms 1-3436 of Table 2. In particular, all amino acid residues within 10 A of the groove defined by one side of loop DE with some residues of loops aa'and GH, and on the other side are found loops EF, Aa, and a'A". Hydrogen atoms are added, and the structure further minimized using AMBER forcefield. A peptide of the sequence EYFDSLLHACIPCQLRCSSNTPPLTC is constructed and minimized. The minimized peptide is then docked manually to the groove on the hNeutrokine- alpha structure. Alternatively, the program AUTODOCK is used to dock the peptide to the hNeutrokine-alpha trimer. Based on the binding mode analysis, portions of the peptide are changed to enhance binding to hNeutrokine-alpha. A compound designed according to this method is useful as an antagonist of hNeutrokine-alpha binding to and activating one or all of the receptors to which hNeutrokine-alpha binds.

Example 12 Designing A Compound that is Similar to a Portion of Neutrokine-alpha [0202] A cyclic'peptide corresponding to the loop between D and E is prepared as a compound that binds to Neutrokine-alpha. The sequence is: CRKKVHVFGDELSC. The two terminal cysteines are used to form an intramolecular disulfide bond. The structure of the cyclic peptide is first modeled using standard molecular modeling techniques. The model of the cyclic peptide is compared to the DE loop of the three-dimensional structure of hNeutrokine- alpha. Sufficient structural and chemical similarity is observed to prepare the cyclic peptide. The cyclic peptide is synthesized on an Advanced ChemTech 440 Automated Solid Phase Organic Synthesizer (Advanced ChemTech, Inc., Louisville, KY) using standard Fmoc chemistry (e. g., see Jameson et al., Nature 368 : 744-746 (1994) ). The linear peptide is then cyclized under standard oxidizing conditions. The peptide is monitored for purity using reverse-phase high-performance liquid chromatography. The peptide is then preparatively fractioned to greater than 99% purity on an HPLC and its mass verified by mass spectrometry. The cyclic peptide is then assayed for activity.

[0203] Other cyclic peptides may be prepared in which certain residues are modified. For example, the phenylalanine of the above cyclic peptide may be mutated to a tyrosine.

Example 13 Computer system comprising [0204] One application of the present invention is provided in Figure 10, which provides a block diagram of a computer system 102 that can be used to implement the present invention. The computer system 102 includes a processor 106 connected to a bus 104. Also connected to the bus 104 are a main memory 108 (preferably implemented as random access memory, RAM) and a variety of secondary storage memory 110, such as a hard drive 112, a removable storage medium 114, and a monitor 120. The removable medium storage device 114 may represent, for example, a floppy disk drive, a CD-ROM drive, a magnetic tape drive, or a ZIP disk. A removable storage medium 116 (such as a floppy disk, a compact disk, a magnetic tape, or a ZIP disk) containing control logic and/or data recorded therein may be inserted into the removable medium storage medium 114. The computer system 102 includes appropriate software for reading the control logic and/or the data from the removable medium storage device 114 once inserted in the removable medium storage device 114.

[0205] Amino acid sequence data, X-ray diffraction data, and/or atomic coordinate data of the present invention or data corresponding to a model of a nuclear receptor may be stored in a well known manner in the main memory 108, any of the secondary storage devices 110, and/or a removable storage device 116.

Software for accessing and processing the data resides in main memory 108 during execution. The monitor 120 is optionally used for visualization.

Example 14 SELDI Experiment [0206] [0207] SELDI mass spectrometry and data analysis. A surface-enhanced laser desorption-ionization (SELDI) approach was used to identify regions involved in neutrokine-alpha protein binding to receptors TACI and BCMA. Recombinant receptor proteins, tagged with an immunoglobulin Fc domain, were expressed in CHO cells (TACI) or baculovirus-infected insect cells (BCMA) and tested for binding activity by BIACORE and cell-based assays. The receptors were then covalently bound to PS2 ProteinChipT Arrays (Ciphergen Biosystems) and subsequently incubated with recombinant neutrokine-alpha. After removal of unbound material, the complexes were digested with a high concentration of trypsin. Unretained digest fragments were removed by a stringency wash. The energy-absorbing molecule, a-hydroxy-cinnaminic acid (CHCA) in 10% (v/v) formic acid and 10% (v/v) ethanol, was added, and chips were analyzed on a Ciphergen PBS 2, as well as a PE Sciex Qstar with protein chip interface. PS2 data with four-point external calibration achieve a mass accuracy of-50-100 p. p. m. , and QStar data have 5 p. p. m. accuracy. Fragment matches and distributions were analyzed using PAWS (Protein Analysis Worksheet, Proteometrics).

TABLE 2 Coordinates of Human Neutrokine-alpha Dimer of Trimers 2 3 4 5 6 7 8 9 10 1 CB THR A 141-9.946 48. 680-9. 356 1.00 63.79 2 OG1 THR A 141-8.708 48.909-8. 669 1.00 64.00 3 CG2 THR A 141-9. 697 47.792-10. 569 1.00 64.34 4 C THR A 141-10.885 50.835-8. 533 1.00 61.14 5 O THR A 141-10.017 51.064-7. 687 1.00 61.65 6 N THR A 141-9.629 50. 788-10. 687 1.00 63.54 7 CA THR A 141-10.556 50.036-9. 790 1.00 62.80 8 N VAL A 142-12.142 51.257-8. 421 1.00 58.68 9 CA VAL A 142-12.611 52.022-7. 270 1.00 55.59 10 CB VAL A 142-12.542 51.176-5. 976 1.00 56. 78 11 CG1 VAL A 142-13.210 51.920-4. 826 1.00 57.03 12 CG2 VAL A 142-13.204 49.827-6. 201 1.00 57.00 13 C VAL A 142-11.819 53. 314-7. 049 1.00 52.58 14 O VAL A 142-10.955 53. 386-6. 173 1.00 52. 00 15 N THR A 143-12.121 54.330-7. 850 1.00 48.54 16 CA THR A 143-11.457 55. 623-7. 739 1.00 44.49 17 CB THR A 143-10.124 55.639-8. 520 1.00 45.47 18 OG1 THR A 143-9.465 56. 895-8. 320 1.00 46.54 19 CG2 THR A 143-10.372 55. 431-10. 006 1.00 47.18 20 C THR A 143-12. 384 56.700-8. 291 1.00 40.67 21 O THR A 143-13.050 56.489-9. 302 1.00 40.45 22 N GLN A 144-12.431 57.849-7. 623 1.00 36.20 23 CA GLN A 144-13.297 58.945-8. 050 1.00 32. 02 24 CB GLN A 144-13.870 59.669-6. 834 1.00 32.75 25 CG GLN A 144-14.818 58.840-6. 005 1.00 34.33 26 CD GLN A 144-15.303 59.585-4. 782 1.00 35. 48 27 OE1 GLN A 144-14.560 59.768-3. 819 1.00 34.14 28 NE2 GLN A 144-16.554 60.033-4. 819 1.00 36.17 29 C GLN A 144-12.592 59.965-8. 926 1. 00 28. 95 30 O GLN A 144-11. 738 60.708-8. 450 1.00 26. 99 1 2 3 4 5 6 7 8 9 10 31 N ASP A 145-12.953 60.011-10. 204 1.00 25.43 32 CA ASP A 145-12.342 60. 977-11. 101 1.00 24.50 33 CB ASP A 145-12.700 60.669-12. 558 1.00 25.56 34 CG ASP A 145-12.125 59.343-13. 040 1.00 28. 81 35 OD1 ASP A 145-11.458 58.648-12. 238 1. 00 26. 36 36 OD2 ASP A 145-12.346 59.000-14. 223 1. 00 27.49 37 C ASP A 145-12.849 62. 370-10. 722 1.00 23.11 38 O ASP A 145-13.949 62. 520-10. 192 1.00 22. 39 39 N CYS A 146-12.034 63.386-10. 976 1.00 20.35 40 CA CYS A 146-12.422 64.751-10. 673 1.00 18.89 41 CB CYS A 146-12.340 65.027-9. 159 1.00 19.98 42 SG CYS A 146-10.896 64. 357-8. 281 1.00 25. 28 43 C CYS A 146-11.567 65.735-11. 451 1.00 19.36 44 O CYS A 146-10.506 65. 382-11. 975 1.00 18.92 45 N LEU A 147-12.044 66.968-11. 539 1.00 17. 33 46 CA LEU A 147-11.327 68.002-12. 263 1.00 18.56 47 CB LEU A 147-11.754 68.008-13. 734 1.00 18.49 48 CG LEU A 147-11.029 68.988-14. 663 1. 00 18.77 49 CD1 LEU A 147-10.906 68.374-16. 050 1.00 18.69 50 CD2 LEU A 147-11.771 70.304-14. 708 1. 00 17.81 51 C LEU A 147-11.648 69. 332-11. 611 1.00 19.43 52 O LEU A 147-12.785 69.574-11. 201 1.00 18.99 53 N GLN A 148-10.641 70.190-11. 511 1.00 17.52 54 CA GLN A 148-10.822 71.489-10. 890 1.00 16.30 55 CB GLN A 148-10.269 71.443-9. 457 1.00 15.90 56 CG GLN A 148-10.297 72.762-8. 688 1.00 17.92 57 CD GLN A 148-9.936 72.566-7. 219 1.00 20. 11 58 DE1 GLN A 148-10.802 72.284-6. 382 1.00 18.46 59 NE2 GLN A 148-8.648 72.690-6. 905 1.00 18.31 60 C GLN A 148-10.141 72.579-11. 706 1.00 16. 16 61 0 GLN A 148-9. 057 72.373-12. 262 1.00 16.56 62 N LEU A 149-10.803 73.729-11. 780 1.00 17.06 63 CA LEU A 149-10.311 74. 887-12.511 1. 00 16.84 1 2 3 4 5 6 7 8 9 10 64 CB LEU A 149-11.314 75.279-13. 598 1.00 16.97 65 CG LEU A 149-11.666 74. 209-14. 633 1.00 14.61 66 CD1 LEU A 149-12.806 74.710-15. 522 1.00 17.71 67 CD2 LEU A 149-10. 439 73. 878-15. 464 1. 00 15. 08 68 C LEU A 149-10.148 76.057-11. 542 1. 00 18. 44 69 O LEU A 149-10.919 76.185-10. 589 1.00 17.43 70 N ILE A 150-9.141 76.898-11. 777 1.00 17.99 71 CA ILE A 150-8. 910 78.073-10. 937 1.00 17.48 72 CB ILE A 150-7. 644 77. 916-10. 041 1.00 19.45 73 CG2 ILE A 150-7. 903 76.882-8. 955 1.00 20.12 74 CG1 ILE A 150-6.427 77. 532-10. 889 1.00 20.67 75 CD1 ILE A 150-5.137 77.447-10. 093 1.00 20.84 76 C ILE A 150-8.755 79.297-11. 841 1.00 19.14 77 O ILE A 150-8. 263 79. 185-12. 964 1.00 19.36 78 N ALA A 151-9.181 80. 459-11. 355 1.00 18.10 79 CA ALA A 151-9.111 81.691-12. 138 1.00 20.90 80 CB ALA A 151-9.643 82.863-11. 312 1.00 19.24 81 C ALA A 151-7. 704 82.011-12. 653 1.00 23.05 82 O ALA A 151-6.710 81.777-11. 968 1.00 21.37 83 N ASP A 152-7.643 82.541-13. 871 1.00 25.69 84 CA ASP A 152-6. 382 82.919-14. 515 1.00 29.62 85 CB ASP A 152-6.405 82. 491-15. 986 1.00 31.09 86 CG ASP A 152-5. 152 82. 909-16. 744 1.00 35.05 87 OD1 ASP A 152-4.231 83. 488-16. 130 1.00 37.18 88 OD2 ASP A 152-5. 093 82. 653-17. 963 1.00 35.15 89 C ASP A 152-6.230 84. 437-14. 407 1.00 30.93 90 O ASP A 152-6.892 85.188-15. 123 1.00 31.43 91 N SER A 153-5. 356 84.883-13. 510 1.00 33. 39 92 CA SER A 153-5.146 86. 310-13. 279 1.00 37.73 93 CB SER A 153-4.312 86.512-12. 011 1.00 37. 67 94 OG SER A 153-3.025 85.934-12. 154 1.00 40.23 95 C SER A 153-4. 493 87. 077-14. 427 1.00 39.76 96 O SER A 153-4.585 88. 305-14. 480 1.00 41.42 2 3 4 5 6 7 8 9 to 97 N GLU A 154-3.843 86.364-15. 340 1.00 42.02 98 CA GLU A 154-3.160 87. 003-16.463 1.00 44.60 99 CB GLU A 154-1.885 86.225-16. 803 1.00 47. 25 100 CG GLU A 154-0.846 86.209-15. 690 1.00 52.32 101 CD GLU A 154-0.395 87.604-15. 292 1.00 55.63 102 OE1 GLU A 154 0.110 88.341-16. 165 1.00 58.04 103 OE2 GLU A 154-0. 543 87. 965-14.103 1.00 58.35 104 C GLU A 154-4.004 87.154-17. 726 1.00 45.09 105 O GLU A 154-3.479 87. 483-18. 793 1.00 45.38 106 N THR A 155-5. 307 86.929-17. 614 1. 00 44.44 107 CA THR A 155-6.180 87.037-18. 775 1. 00 45.01 108 CB THR A 155-6.536 85. 643-19. 321 1.00 44.96 109 OG1 THR A 155-5.378 84.806-19. 270 1.00 47. 26 110 CG2 THR A 155-6.996 85.735-20. 763 1.00 47.16 111 C THR A 155-7.471 87.761-18. 418 1.00 44.20 112 O THR A 155-7.997 87.601-17. 317 1.00 43.46 113 N PRO A 156-7.991 88.583-19. 343 1.00 43.74 114 CD PRO A 156-7.408 88.967-20. 642 1.00 44.28 115 CA PRO A 156-9.232 89. 319-19. 092 1.00 42.74 116 CB PRO A 156-9.226 90. 377-20. 190 1.00 43.64 117 CG PRO A 156-8.572 89.652-21. 325 1.00 44.59 118 C PRO A 156-10.447 88.393-19. 181 1.00 41.57 119 O PRO A 156-10.404 87.359-19. 852 1.00 39.42 120 N THR A 157-11.524 88.770-18. 498 1.00 40. 44 121 CA THR A 157-12.747 87.976-18. 495 1.00 40.18 122 CB THR A 157-13. 783 88.554-17. 506 1.00 41. 08 123 OG1 THR A 157-14.120 89.894-17. 889 1.00 40.92 124 CG2 THR A 157-13.219 88.564-16. 091 1.00 39.80 125 C THR A 157-13. 372"87. 933-19.885 1.00 40.24 126 O THR A 157-13.187 88.848-20. 686 1.00 39.98 127 N ILE A 158-14.101 86.862-20. 173 1.00 39.93 128 CA ILE A 158-14.754 86.720-21. 467 1.00 40. 37 129 CB ILE A 158-14. 901 85. 231-21.872 1.00 41. 12 1 2 3 4 5 6 7 8 9 10 130 CG2 ILE A 158-15.744 85. 113-23.131 1.00 41.27 131 CG1 ILE A 158-13.523 84.600-22. 102 1.00 42.96 132 CD1 ILE A 158-12.764 84.273-20. 840 1.00 43.56 133 C ILE A 158-16.144 87. 353-21. 418 1.00 40. 99 134 O ILE A 158-16.923 87.088-20. 501 1.00 39.17 135 N GLN A 159-16.447 88.196-22. 400 1.00 41.25 136 CA GLN A 159-17.749 88.853-22. 468 1.00 42. 31 137 CB GLN A 159-17.581 90.361-22. 672 1.00 42.25 138 CG GLN A 159-16.833 91.074-21. 553 1.00 40.39 139 CD GLN A 159-17.577 91.040-20. 232 1. 00 40.42 140 OE1 GLN A 159-18.743 91.434-20. 151 1. 00 38. 95 141 NE2 GLN A 159-16.904 90.577-19. 186 1.00 37.64 142 C GLN A 159-18.540 88.263-23. 627 1.00 43.25 143 O GLN A 159-18.099 88. 312-24. 775 1.00 43.20 144 N LYS A 160-19.707 87.705-23. 324 1.00 44.24 145 CA LYS A 160-20.542 87. 094-24. 350 1.00 46.33 146 CB LYS A 160-19.941 85.748-24. 760 1.00 47.60 147 CG LYS A 160-20.930 84.775-25. 378 1.00 49.38 148 CD LYS A 160-20.263 83.434-25. 613 1.00 50.76 149 CE LYS A 160-21.290 82.336-25. 811 1.00 51.67 150 NZ LYS A 160-20.753 81. 022-25. 362 1.00 51.78 151 C LYS A 160-21.986 86.897-23. 901 1.00 46.81 152 O LYS A 160-22.245 86.414-22. 798 1.00 46.79 153 N GLY A 161-22.921 87.273-24. 769 1.00 46.62 154 CA GLY A 161-24. 331 87.126-24. 456 1. 00 45.89 155 C GLY A 161-24.786 87.938-23. 260 1.00 45.77 156 O GLY A 161-25.747 87.565-22. 585 1.00 46.87 157 N SER A 162-24.100 89. 049-22. 999 1. 00 44.64 158 CA SER A 162-24. 427 89.928-21. 874 1.00 43.48 159 CB SER A 162-25.929 90.231-21. 850 1.00 45.23 160 OG SER A 162-26.344 90.843-23. 060 1. 00 49. 35 161 C SER A 162-24.006 89.332-20. 529 1.00 40.89 162 O SER A 162-24.351 89. 859-19. 472 1. 00 40.12 1 2 3 4 5 6 7 8 9 10 163 N TYR A 163-23.268 88. 227-20.581 1.00 37.91 164 CA TYR A 163-22.779 87. 555-19. 379 1.00 34.91 165 CB TYR A 163-23.132 86.063-19. 413 1.00 37.03 166 CG TYR A 163-24.560 85.729-19. 039 1.00 39.72 167 CD1 TYR A 163-25.637 86. 368-19. 654 1.00 42.64 168 CEI TYR A 163-26.954 86.036-19. 331 1.00 44.20 169 CD2 TYR A 163-24.835 84.748-18. 089 1.00 41.69 170 CE2 TYR A 163-26.148 84.407-17. 759 1.00 43.82 171 CZ TYR A 163-27.201 85.054-18. 384 1.00 44.77 172 OH TYR A 163-28.498 84. 712-18.067 1. 00 47. 39 173 C TYR A 163-21.263 87.694-19. 305 1.00 32.32 174 O TYR A 163-20.609 87. 971-20. 309 1.00 30.98 175 N THR A 164-20.707 87.507-18. 113 1.00 28.43 176 CA THR A 164-19.264 87.584-17. 931 1.00 25.45 177 CB THR A 164-18.874 88. 557-16.786 1.00 26.22 178 OG1 THR A 164-19.222 89.900-17. 148 1.00 26.23 179 CG2 THR A 164-17. 377 88.487-16. 516 1.00 23.91 180 C THR A 164-18.777 86.187-17. 573 1.00 24. 64 181 O THR A 164-19.354 85.535-16. 703 1.00 21.85 182 N PHE A 165-17.737 85.717-18. 255 1.00 22.94 183 CA PHE A 165-17.190 84.396-17. 969 1.00 23.06 184 CB PHE A 165-17.251 83.493-19. 203 1.00 21. 74 185 CG PHE A 165-18.646 83.102-19. 601 1.00 24. 39 186 CD1 PHE A 165-19. 386 83.898-20. 473 1.00 23.81 187 CD2 PHE A 165-19.233 81.950-19. 079 1.00 23.62 188 CE1 PHE A 165-20.697 83.550-20. 828 1.00 24.99 189 CE2 PHE A 165-20.539 81. 593-19. 421 1. 00 23. 78 190 CZ PHE A 165-21.272 82.395-20. 296 1.00 25. 21 191 C PHE A 165-15.752 84.463-17. 465 1.00 24.33 192 O PHE A 165-14.885 85.090-18. 084 1.00 23.98 193 N VAL A 166-15.516 83. 816-16. 331 1.00 22.59 194 CA VAL A 166-14.193 83.761-15. 721 1.00 22.54 195 CB VAL A 166-14.248 83.070-14. 325 1. 00 21. 11 1 2 3 4 5 6 7 8 9 10 196 CG1 VAL A 166-12.847 82.936-13. 743 1.00 21.11 197 CG2 VAL A 166-15.134 83.854-13. 382 1. 00 22.53 198 C VAL A 166-13. 263 82.937-16. 607 1.00 22.60 199 O VAL A 166-13.653 81.876-17. 099 1.00 23.91 200 N PRO A 167-12.032 83.426-16. 848 1.00 21.85 201 CD PRO A 167-11. 526 84.781-16. 564 1.00 22.31 202 CA PRO A 167-11.086 82.675-17. 677 1.00 22.07 203 CB PRO A 167-10.119 83.753-18. 161 1.00 23. 00 204 CG PRO A 167-10.068 84.690-16. 995 1.00 22.59 205 C PRO A 167-10. 416 81.651-16. 758 1.00 22.90 206 O PRO A 167-9.850 82.021-15. 727 1.00 22.88 207 N TRP A 168-10.482 80.373-17. 123 1.00 21. 50 208 CA TRP A 168-9.916 79.317-16. 286 1.00 21.25 209 CB TRP A 168-10. 875 78.119-16. 228 1.00 18.10 210 CG TRP A 168-12.254 78.441-15. 711 1.00 17. 75 211 CD2 TRP A 168-12.596 78.906-14. 395 1.00 15.41 212 CE2 TRP A 168-14.001 79.075-14. 364 1. 00 16.30 213 CE3 TRP A 168-11.856 79.185-13. 238 1.00 15.68 214 CD1 TRP A 168-13.430 78.354-16. 404 1.00 16.05 215 NE1 TRP A 168-14.482 78.735-15. 602 1.00 15.72 216 CZ2 TRP A 168-14. 679 79.525-13. 220 1.00 15.55 217 CZ3 TRP A 168-12. 533 79.632-12. 095 1.00 15.76 218 CH2 TRP A 168-13.930 79.793-12. 098 1.00 16.22 219 C TRP A 168-8.538 78.786-16. 666 1.00 22.95 220 O TRP A 168-8.082 78.924-17. 796 1.00 24.11 221 N LEU A 169-7.904 78.161-15. 680 1.00 23.29 222 CA LEU A 169-6.605 77.513-15. 803 1.00 24.67 223 CB LEU A 169-5.541 78. 311-15. 046 1.00 29.42 224 CG LEU A 169-4. 332 78.835-15. 830 1.00 34.72 225 CD1 LEU A 169-4.781 79.564-17. 086 1.00 35.27 226 CD2 LEU A 169-3.524 79.765-14. 934 1.00 36.82 227 C LEU A 169-6.853 76.170-15. 109 1.00 23.24 228 0LEU A 169-7.606 76.106-14. 137 1. 00 20. 73 1 2 3 4 5 6 7 8 9 10 229 N LEU A 170-6.246 75.100-15. 603 1.00 22.03 230 CA LEU A 170-6.443 73.792-14. 996 1.00 21.20 231 CB LEU A 170-5.981 72.688-15. 953 1.00 22.13 232 CG LEU A 170-6.225 71.250-15. 484 1.00 23.03 233 CD1 LEU A 170-7.729 70.971-15. 463 1.00 20.81 234 CD2 LEU A 170-5.527 70.270-16. 422 1.00 24. 20 235 C LEU A 170-5. 690 73.650-13. 676 1.00 22.53 236 O LEU A 170-4.482 73.879-13. 617 1.00 23.09 237 N SER A 171-6.412 73.293-12. 617 1.00 19.78 238 CA SER A 171-5.808 73.066-11. 304 1.00 19. 41 239 CB SER A 171-6.853 73.243-10. 197 1.00 19.13 240 OG SER A 171-6.342 72.856-8. 935 1.00 22.31 241 C SER A 171-5.316 71. 619-11. 346 1.00 19.82 242 O SER A 171-4.168 71.325-11. 003 1.00 20.37 243 N PHE A 172-6.193 70.714-11. 774 1. 00 18.71 244 CA PHE A 172-5.827 69. 306-11. 917 1.00 19.56 245 CB PHE A 172-5.545 68.659-10. 549 1.00 21.30 246 CG PHE A 172-6.788 68. 358-9. 741 1. 00 20.51 247 CD1 PHE A 172-7.538 67.209-9. 986 1.00 19. 64 248 CD2 PHE A 172-7.205 69.226-8. 734 1.00 20.70 249 CE1 PHE A 172-8.696 66.936-9. 248 1.00 20.88 250 CE2 PHE A 172-8.361 68.965-7. 990 1.00 19.81 251 CZ PHE A 172-9.104 67.814-8. 244 1.00 20.54 252 C PHE A 172-6.914 68.514-12. 623 1.00 20.46 253 O PHE A 172-8.086 68.900-12. 622 1.00 19.76 254 N LYS A 173-6.506 67.408-13. 231 1.00 20.18 255 CA LYS A 173-7.421 66.495-13. 905 1.00 21.99 256 CB LYS A 173-7.261 66.572-15. 428 1.00 22.28 257 CG LYS A 173-8.055 65.505-16. 190 1.00 24.51 258 CD LYS A 173-7.962 65.716-17. 702 1.00 26. 36 259 CE LYS A 173-8.529 64.530-18. 475 1.00 26.87 260 NZ LYS A 173-7.752 63. 282-18.223 1.00 29. 86 261 C LYS A 173-7. 050 65.101-13. 416 1. 00 23. 03 1 2 3 4 5 6 7 8 9 10 262 O LYS A 173 -5.945 64.622 -13.679 1.00 23.09 263 N ARG A 174 -7.962 64.462 -12.688 1.00 21.42 264 CA ARG A 174 -7.718 63.118 -12.170 1.00 21.72 265 CB ARG A 174-7.976 63.071-10. 663 1.00 21.13 266 CG ARG A 174-7. 609 61.739-10. 013 1.00 22.32 267 CD ARG A 174-8.268 61.593-8. 653 1.00 24.86 268 NE ARG A 174-7. 734 60. 461-7. 900 1.00 26.70 269 CZ ARG A 174-8. 317 59.930-6. 831 1.00 27.40 270 NH1 ARG A 174-9.465 60.419-6. 383 1.00 28.63 271 NH2 ARG A 174-7.741 58.917-6. 196 1.00 30.22 272 C ARG A 174-8.638 62.121-12. 870 1.00 22.48 273 O ARG A 174-9.861 62.243-12. 807 1.00 20.43 274 N GLY A 175-8.054 61.135-13. 539 1.00 22.09 275 CA GLY A 175-8.872 60.152-14. 232 1.00 23.56 276 C GLY A 175-9.292 60.603-15. 622 1.00 24.18 277 O GLY A 175-8.706 61.528-16. 191 1.00 24.86 278 N SER A 176-10.323 59.967-16. 168 1.00 23.90 279 CA SER A 176-10.778 60.296-17. 516 1.00 25.40 280 CB SER A 176-10.499 59.106-18. 434 1.00 25.85 281 OG SER A 176-11.152 57.946-17. 940 1.00 27.93 282 C SER A 176-12.244 60.710-17. 675 1.00 24.52 283 O SER A 176-12.663 61.063-18. 775 1.00 26.06 284 N ALA A 177-13.019 60.677-16. 597 1.00 24. 03 285 CA ALA A 177-14.436 61.039-16. 675 1.00 23.43 286 CB ALA A 177-15.147 60.645-15. 383 1.00 23.71 287 C ALA A 177-14.702 62.511-16. 983 1.00 23.16 288 O ALA A 177-15.775 62.859-17. 483 1.00 22.75 289 N LEU A 178-13.732 63.373-16. 694 1.00 20.36 290 CA LEU A 178-13.890 64.803-16. 931 1.00 20.93 291 CB LEU A 178-14. 105 65.530-15. 598 1.00 21.06 292 CG LEU A 178-15. 355 65.161-14. 795 1.00 22.37 293 CD1 LEU A 178-15.213 65.679-13. 373 1.00 23.53 294 CD2 LEU A 178-16.597 65. 744-15. 468 1.00 20.99 1 2 3 4 5 6 7 8 9 10 295 C LEU A 178-12.685 65.415-17. 642 1.00 21.20 296 O LEU A 178-11.548 65.031-17. 381 1.00 20.70 297 N GLU A 179-12. 952 66. 377-18. 525 1. 00 20.79 298 CA GLU A 179-11.916 67.074-19. 288 1.00 22.81 299 CB GLU A 179-11.848 66.532-20. 719 1.00 25.45 300 CG GLU A 179-11.183 65.186-20. 882 1.00 30.46 301 CD GLU A 179-11.197 64.720-22. 328 1.00 32.89 302 OE1 GLU A 179-11.220 65.588-23. 231 1.00 35.28 303 OE2 GLU A 179-11.176 63.492-22. 563 1.00 34.43 304 C GLU A 179-12.228 68.563-19. 376 1.00 23.83 305 O GLU A 179-13.355 68.975-19. 142 1.00 22.77 306 N GLU A 180-11.224 69.370-19. 708 1.00 25.20 307 CA GLU A 180-11.439 70.800-19. 880 1.00 27.82 308 CB GLU A 180-10.283 71.625-19. 315 1.00 30.54 309 CG GLU A 180-10. 326 73.071-19. 793 1.00 34.85 310 CD GLU A 180-9.263 73.947-19. 165 1.00 38.58 311 OE1 GLU A 180-8.112 73.480-19. 011 1.00 38.90 312 OE2 GLU A 180-9.582 75.111-18. 840 1.00 40.47 313 C GLU A 180-11.539 71.043-21. 379 1.00 27.53 314 O GLU A 180-10.754 70.497-22. 150 1.00 28.26 315 N LYS A 181-12.504 71.854-21. 792 1.00 27.57 316 CA LYS A 181-12.690 72.140-23. 208 1.00 26.79 317 CB LYS A 181-13.577 71.065-23. 846 1.00 29.42 318 CG LYS A 181-13.936 71.304-25. 309 1.00 33.32 319 CD LYS A 181-14.880 70.217-25. 814 1. 00 37.20 320 CE LYS A 181-15.487 70.575-27. 163 1.00 40.57 321 NZ LYS A 181-14.450 70.750-28. 217 1.00 42.65 322 C LYS A 181-13. 315 73.512-23. 403 1.00 26.20 323 O LYS A 181-14.428 73.769-22. 954 1.00 24.97 324 N GLU A 182-12.579 74.395-24. 068 1.00 25. 64 325 CA GLU A 182-13.047 75.744-24. 337 1.00 26.52 326 CB GLU A 182-14.086 75.716-25. 461 1.00 30.89 327 CG GLU A 182-13.507 75.283-26. 803 1.00 37.13 1 2 3 4 5 6 7 8 9 10 328 CD GLU A 182-14.558 75. 184-27. 892 1.00 42.46 329 OE1 GLU A 182-15.275 76.185-28. 123 1.00 47.30 330 OE2 GLU A 182-14.668 74.110-28. 519 1.00 44.17 331 C GLU A 182-13.610 76.458-23. 109 1.00 25.62 332 O GLU A 182-14.724 76.991-23. 136 1.00 24.70 333 N ASN A 183-12.832 76.447-22. 028 1.00 23.32 334 CA ASN A 183-13.203 77.125-20. 788 1.00 23. 36 335 CB ASN A 183-13.474 78.604-21. 078 1.00 21.32 336 CG ASN A 183-13.179 79.491-19. 889 1.00 24.03 337 OD1 ASN A 183-14. 022 80.286-19. 457 1.00 25.01 338 ND2 ASN A 183-11.972 79. 366-19. 352 1.00 19.63 339 C ASN A 183-14.404 76.517-20. 061 1.00 21.75 340 O ASN A 183-15.031 77.172-19. 222 1.00 21.77 341 N LYS A 184-14.714 75. 266-20. 381 1.00 21.13 342 CA LYS A 184-15.828 74.566-19. 757 1. 00 21.27 343 CB LYS A 184-16.995 74.460-20. 748 1. 00 22.90 344 CG LYS A 184-17.644 75.801-21. 064 1.00 23.90 345 CD LYS A 184-18.633 75.711-22. 222 1.00 27.84 346 CE LYS A 184-17.917 75.712-23. 573 1.00 31.15 347 NZ LYS A 184-18.887 75.693-24. 702 1.00 36. 37 348 C LYS A 184-15. 380 73.174-19. 329 1. 00 20.70 349 O LYS A 184-14. 301 72.714-19. 712 1.00 19.70 350 N ILE A 185-16.200 72.512-18. 521 1.00 19.52 351 CA ILE A 185-15.891 71.159-18. 074 1.00 19.44 352 CB ILE A 185-16.249 70.953-16. 589 1.00 18.82 353 CG2 ILE A 185-15.939 69.509-16. 181 1.00 18.47 354 CG1 ILE A 185-15.446 71.924-15. 717 1.00 17.92 355 CD1 ILE A 185-15.716 71.788-14. 233 1.00 18.68 356 C ILE A 185-16.705 70.186-18. 924 1.00 22.42 357 O ILE A 185-17.941 70.201-18. 893 1.00 22.62 358 N LEU A 186-16. 008 69. 347-19. 685 1.00 22.17 359 CA LEU A 186-16.652 68. 364-20. 557 1.00 22. 64 360 CB LEU A 186-15.833 68.187-21. 842 1.00 20.83 123 4 56 7 8 9 10 361 CG LEU A 186-16. 267 67.074-22. 808 1.00 24. 21 362 CD1 LEU A 186-17.651 67. 382-23. 382 1.00 21.17 363 CD2 LEU A 186-15.235 66.945-23. 928 1.00 21. 56 364 C LEU A 186-16.821 67. 015-19. 868 1.00 22.83 365 O LEU A 186-15.871 66.471-19. 304 1.00 22.89 366 N VAL A 187-18.036 66.475-19. 919 1.00 21.46 367 CA VAL A 187-18.329 65. 185-19. 304 1.00 20.02 368 CB VAL A 187-19.805 65.117-18. 841 1.00 19.67 369 CG1 VAL A 187-20.100 63.759-18. 216 1.00 19. 33 370 CG2 VAL A 187-20.087 66.245-17. 834 1.00 19.81 371 C VAL A 187-18.058 64.063-20. 306 1.00 22.24 372 O VAL A 187-18.632 64.050-21. 400 1.00 21.73 373 N LYS A 188-17.193 63.126-19. 924 1.00 21.47 374 CA LYS A 188-16.823 62.002-20. 783 1.00 24.99 375 CB LYS A 188-15. 303 61.781-20. 755 1.00 25.34 376 CG LYS A 188-14.470 62. 995-21.157 1.00 26.61 377 CD LYS A 188-14.725 63. 403-22.600 1.00 28.12 378 CE LYS A 188-14. 309 62.311-23. 580 1.00 30.74 379 NZ LYS A 188-14.517 62.755-24. 991 1.00 33.58 380 C LYS A 188-17. 505 60.706-20. 368 1.00 25.90 381 O LYS A 188-17. 528 59.743-21. 132 1. 00 26. 87 382 N GLU A 189-18.050 60.681-19. 157 1.00 25.42 383 CA GLU A 189-18.719 59.495-18. 636 1. 00 26.30 384 CB GLU A 189-17.775 58.733-17. 701 1.00 29. 79 385 CG GLU A 189-16.601 58.084-18. 410 1.00 32.91 386 CD GLU A 189-15.543 57.575-17. 452 1.00 36.78 387 OBI GLU A 189-15.909 57.099-16. 353 1.00 38. 18 388 OE2 GLU A 189-14. 345 57.640-17. 806 1. 00 36.68 389 C GLU A 189-20.004 59. 836-17. 892 1.00 26.02 390 O GLU A 189-20.006 60.646-16. 968 1. 00 24.64 391 N THR A 190-21.094 59. 195-18. 301 1.00 24.19 392 CA THR A 190-22.408 59. 395-17. 697 1.00 23.88 393 CB THR A 190-23. 472 58.564-18. 455 1.00 23.57 2 3 4 5 6 7 8 9 10 394 OG1 THR A 190-23.596 59.063-19. 791 1.00 22.70 395 CG2 THR A 190-24.824 58.627-17. 748 1.00 23.05 396 C THR A 190-22.419 58.980-16. 229 1.00 23.44 397 O THR A 190-21.848 57.953-15. 870 1.00 24.03 398 N GLY A 191-23.072 59.774-15. 382 1.00 22.26 399 CA GLY A 191-23.146 59.434-13. 970 1.00 21.11 400 C GLY A 191-23.538 60.590-13. 063 1.00 19.80 401 O GLY A 191-23.959 61.646-13. 531 1.00 18.04 402 N TYR A 192-23.404 60. 378-11. 758 1.00 19.87 403 CA TYR A 192-23.727 61.401-10. 767 1.00 20.18 404 CB TYR A 192-24.346 60.751-9. 526 1.00 21.35 405 CG TYR A 192-25.812 60.417-9. 693 1.00 25.53 406 CD1 TYR A 192-26.798 61. 358-9. 397 1.00 23.95 407 CE1 TYR A 192-28.146 61.076-9. 599 1.00 29.04 408 CD2 TYR A 192-26. 211 59.177-10. 196 1.00 25.73 409 CE2 TYR A 192-27.558 58.885-10. 404 1.00 29. 34 410 CZ TYR A 192-28.518 59.838-10. 104 1.00 29.19 411 OH TYR A 192-29.843 59.560-10. 313 1.00 32.73 412 C TYR A 192-22.451 62.151-10. 387 1. 00 20.43 413 O TYR A 192-21.404 61.531-10. 150 1.00 18.28 414 N PHE A 193-22.546 63. 476-10. 327 1.00 17.71 415 CA PHE A 193-21.400 64.320-9. 996 1.00 18. 33 416 CB PHE A 193-20.902 65.064-11. 247 1.00 17. 57 417 CG PHE A 193-20.389 64.162-12. 344 1.00 19.23 418 CD1 PHE A 193-21.273 63.465-13. 170 1.00 20.21 419 CD2 PHE A 193-19.020 64.024-12. 557 1.00 19.48 420 CE1 PHE A 193-20.796 62.634-14. 192 1.00 18.79 421 CE2 PHE A 193-18.529 63.197-13. 574 1.00 21.40 422 CZ PHE A 193-19.422 62.504-14. 396 1.00 20.45 423 C PHE A 193-21.698 65.376-8. 931 1.00 17. 06 424 0 PHE A 193-22. 782 65.949-8. 909 1. 00 16.35 425 N PHE A 194-20.728 65.619-8. 051 1.00 16.00 426 CA PHE A 194-20.837 66.671-7. 037 1.00 14.60 1 2 3 4 5 6 7 8 9 10 427 CB PHE A 194-20.043 66.313-5. 774 1. 00 15. 63 428 CG PHE A 194-19.959 67.436-4. 769 1.00 18.95 429 CD 1 PHE A 194-21.077 67.824-4. 040 1.00 20.51 430 CD2 PHE A 194-18.753 68.102-4. 549 1.00 21.08 431 CE1 PHE A 194-21.002 68.863-3. 108 1.00 22.31 432 CE2 PHE A 194-18.669 69.144-3. 619 1.00 22.11 433 CZ PHE A 194-19.794 69. 520-2. 896 1.00 20.15 434 C PHE A 194-20.147 67.820-7. 777 1. 00 15.65 435 O PHE A 194-19.030 67.643-8. 274 1.00 16.55 436 N ILE A 195-20.809 68.971-7. 867 1.00 14.71 437 CA ILE A 195-20.281 70.125-8. 601 1.00 14.08 438 CB ILE A 195-21.186 70.448-9. 812 1.00 14.86 439 CG2 ILE A 195-20.551 71.536-10. 669 1.00 16.44 440 CG1 ILE A 195-21.386 69.187-10. 663 1.00 16.83 441 CD1 ILE A 195-22. 481 69.335-11. 711 1.00 18.73 442 C ILE A 195-20.248 71.339-7. 681 1.00 14.48 443 O ILE A 195-21.204 71.578-6. 951 1.00 13.73 444 N TYR A 196-19.156 72.105-7. 730 1.00 14.64 445 CA TYR A 196-19.000 73.273-6. 863 1.00 14.50 446 CB TYR A 196-18.150 72.884-5. 648 1.00 15. 76 447 CG TYR A 196-16.765 72. 352-6. 006 1.00 16.40 448 CD1 TYR A 196-15.652 73.196-6. 034 1.00 16.86 449 CE1 TYR A 196-14. 375 72.707-6. 382 1.00 17.09 450 CD2 TYR A 196-16.578 71. 004-6. 334 1.00 17.55 451 CE2 TYR A 196-15.316 70.507-6. 685 1.00 18.70 452 CZ TYR A 196-14.220 71. 365-6. 706 1. 00 19.74 453 OH TYR A 196-12.980 70.877-7. 050 1.00 20.26 454 C TYR A 196-18. 376 74.480-7. 570 1. 00 15.68 455 O TYR A 196-17. 631 74.336-8. 542 1.00 16.11 456 N GLY A 197-18.684 75.675-7. 078 1. 00 16. 38 457 CA GLY A 197-18.133 76.878-7. 681 1.00 15.90 458 C GLY A 197-18.131 78.062-6. 738 1. 00 16.64 459 O GLY A 197-19. 053 78. 235-5. 941 1.00 16.60 1 2 3 4 5 6 7 8 9 10 460 N GLN A 198-17.095 78.886-6. 827 1. 00 16. 64 461 CA GLN A 198-16.985 80.068-5. 981 1.00 14.75 462 CB GLN A 198-16.112 79.778-4. 755 1. 00 16.55 463 CG GLN A 198-15.931 80. 998-3.851 1.00 16.73 464 CD GLN A 198-15. 108 80.715-2. 615 1.00 18.85 465 OE1 GLN A 198-15.494 79.913-1. 768 1.00 19.64 466 NE2 GLN A 198-13.964 81.386-2. 500 1.00 18.33 467 C GLN A 198-16.387 81.236-6. 756 1.00 16.25 468 O GLN A 198-15.507 81.051-7. 597 1.00 16.21 469 N VAL A 199-16. 882 82.436-6. 470 1.00 16.57 470 CA VAL A 199-16.402 83.654-7. 116 1.00 17.19 471 CB VAL A 199-17.366 84.110-8. 253 1.00 17. 35 472 CG1 VAL A 199-16.905 85.447-8. 828 1.00 20.74 473 CG2 VAL A 199-17.417 83.049-9. 361 1.00 18.51 474 C VAL A 199-16.326 84.771-6. 070 1.00 19.06 475 O VAL A 199-17.151 84.825-5. 156 1.00 18.21 476 N LEU A 200-15. 325 85.642-6. 189 1.00 19.43 477 CA LEU A 200-15.192 86.774-5. 277 1.00 20.05 478 CB LEU A 200-13.744 86.947-4. 787 1.00 18.23 479 CG LEU A 200-13.429 88.297-4. 104 1.00 19.34 480 CD1 LEU A 200-14.437 88.583-3. 002 1.00 18.78 481 CD2 LEU A 200-12.018 88.288-3. 541 1.00 19.17 482 C LEU A 200-15.628 88.019-6. 036 1.00 21.92 483 O LEU A 200-15.034 88. 376-7. 050 1.00 21.03 484 N TYR A 201-16.679 88.668-5. 547 1.00 26.14 485 CA TYR A 201-17.189 89.873-6. 185 1.00 28. 92 486 CB TYR A 201-18.720 89.872-6. 169 1.00 29.67 487 CG TYR A 201-19.268 88.704-6. 930 1.00 31.01 488 CD1 TYR A 201-19.653 87.532-6. 274 1.00 32.44 489 CE1 TYR A 201-20. 146 86.424-6. 991 1.00 30.90 490 CD2 TYR A 201-19.394 88.744-8. 317 1.00 29.14 491 CE2 TYR A 201-19.850 87.652-9. 039 1.00 31.06 492 CZ TYR A 201-20.221 86.495-8. 372 1.00 30.76 1 2 3 4 5 6 7 8 9 10 493 OH TYR A 201-20.674 85.412-9. 102 1.00 31.99 494 C TYR A 201-16. 658 91.134-5. 518 1.00 31.35 495 O TYR A 201-16.651 91.253-4. 292 1.00 29.72 496 N THR A 202-16.201 92.066-6. 347 1. 00 33.63 497 CA. THR A 202-15.655 93. 334-5. 884 1.00 36.54 498 CB THR A 202-14.162 93.448-6. 255 1.00 36.16 499 OG1 THR A 202-14.010 93.355-7. 676 1.00 34.30 500 CG2 THR A 202-13.363 92.342-5. 577 1.00 35.63 501 C THR A 202-16.431 94.453-6. 569 1.00 39.55 502 O THR A 202-15.922 95.558-6. 757 1.00 39.44 503 N ASP A 203-17.675 94.149-6. 924 1.00 42.05 504 CA ASP A 203-18.556 95.083-7. 612 1.00 45.38 505 CB ASP A 203-19. 353 94.317-8. 667 1.00 47.42 506 CG ASP A 203-19.795 95.195-9. 809 1.00 50.00 507 OD1 ASP A 203-20.430 96.238-9. 545 1.00 50.72 508 OD2 ASP A 203-19.512 94.835-10. 974 1.00 50.23 509 C ASP A 203-19.511 95.782-6. 639 1.00 46.58 510 O ASP A 203-19.962 95.183-5. 664 1.00 45.54 511 N LYS A 204-19.831 97.044-6. 918 1.00 48. 95 512 CA LYS A 204-20.721 97.823-6. 056 1.00 50.93 513 CB LYS A 204-20.377 99. 313-6.179 1.00 53.36 514 CG LYS A 204-19.005 99.663-5. 639 1.00 57.00 511 N LYS A 204 -19.831 97.044 -6.918 1.00 48.95 512 CA LYS A 204 -20.721 97.823 -6.056 1.00 5093 513 CB LYS A 204 -20.377 99.313 -6.179 1.00 53.36 514 CG LYS A 204 -19.005 99.663 -5.639 1.00 57.00 515 CD LYS A 204 -18.793 101.164 -5.583 1.00 59.51 516 CE LYS A 204 -17.420 101.510 -5.033 1.00 60.51 517 NZ LYS A 204 -17.204 102.983 -4.977 1.00 61.90 520 N THR A 205 -22.590 96.874 -7.319 1.00 52.00 521 CA THR A 205 -24.008 96.657 -7.609 1.00 53.41 517 NZ LYS A 204-17.204 102.983-4. 977 1.00 61.90 518 C LYS A 204-22.218 97.650-6. 305 1.00 50.88 519 0 LYS A 204-23.031 98.222-5. 580 1.00 50. 86 520 N THR A 205-22.590 96. 874-7. 319 1.00 52.00 521 CA THR A 205-24. 008 96.657-7. 609 1.00 53.41 522 CB THR A 205-24.209 95.694-8. 789 1.00 54.12 523 OG1 THR A 205-23.733 96.313-9. 986 1.00 54.92 524 CG2 THR A 205-25.688 95. 358-8.965 1.00 55.02 525 C THR A 205-24. 724 96. 091-6. 391 1.00 53.22 2 3 4 5 6 7 8 9 10 526 O THR A 205-24.147 95. 319-5. 624 1.00 54. 37 527 N TYR A 206-25.987 96.470-6. 227 1.00 51.90 528 CA TYR A 206 -26.778 96.028 -5.087 1.00 51.49 529 CB TYR A 206 -28.235 96-496 -5.248 1.00 55.44 530 CG TYR A 206-29.058 95.717-6. 256 1.00 59.99 531 CDI TYR A 206 -29.721 94.549 -5.887 1.00 61.39 532 CE1 TYR A 206 -30.482 93.829 -6.805 1.00 63.23 533 CD2 TYR A 206 -29.178 96.150 -7.578 1.00 61.56 534 CE2 TYR A 206 -29.939 95.433 -8.506 1.00 63.07 535 CZ TYR A 206 -30.587 94.274 -8.110 1.00 63.66 536 OH TYR A 206-31. 334 93.551-9. 010 1.00 65.15 537 C TYR A 206-26.717 94.519-4. 828 1.00 48.02 538 O TYR A 206-26.855 94.082-3. 682 1.00 47.09 539 N ALA A 207-26.504 93.727-5. 879 1.00 43.19 540 CA ALA A 207-26.418 92.271-5. 735 1.00 39.35 541 CB ALA A 207-27.816 91.673-5. 617 1.00 38.44 542 C ALA A 207-25.664 91.614-6. 896 1.00 36.50 543 O ALA A 207-25.883 91.945-8. 063 1.00 34.04 544 N MET A 208-24.787 90.673-6. 558 1.00 32.77 545 CA MET A 208-23.981 89.959-7. 548 1.00 31.48 546 CB MET A 208-22.515 90.391-7. 455 1.00 32.94 547 CG MET A 208-22.244 91.863-7. 753 1.00 36.57 548 SD MET A 208-22.572 92.292-9. 475 1.00 40.48 549 CE MET A 208-21.180 91.484-10. 314 1.00 38.50 550 C MET A 208-24.063 88.449-7. 303 1.00 29.60 551 O MET A 208-24.317 88.017-6. 175 1.00 29.20 552 N GLY A 209-23.819 87. 646-8. 336 1.00 28.04 553 CA GLY A 209-23.903 86.205-8. 167 1.00 26.58 554 C GLY A 209-23.484 85.447-9. 414 1.00 24.85 555 O GLY A 209-23.138 86.070-10. 394 1.00 25.35 556 N HIS A 210-23. 495 84.111-9. 338 1.00 21.49 557 CA HIS A 210-23.123 83.307-10. 487 1.00 19.77 558 CB HIS A 210-21.619 82.910-10. 420 1.00 19. 73 123 4 56 7 8 9 10 559 CG HIS A 210-21. 241 82.072-9. 249 1.00 21.00 560 CD2 HIS A 210-20.708 82.388-8. 039 1. 00 20.67 561 ND1 HIS A 210-21.374 80.697-9. 243 1.00 23.25 562 CE1 HIS A 210-20.952 80.203-8. 103 1.00 20.80 563 NE2 HIS A 210-20.545 81. 212-7. 353 1.00 20.62 564 C HIS A 210-23.976 82.109-10. 636 1.00 20. 33 565 O HIS A 210-24.665 81.719-9. 702 1.00 18.30 566 N LEU A 211-23.989 81. 577-11. 853 1.00 18.95 567 CA LEU A 211-24.805 80. 407-12. 178 1.00 19.34 568 CB LEU A 211-25.759 80.750-13. 332 1.00 19.50 569 CG LEU A 211-26.602 82. 028-13. 328 1. 00 21.64 570 CD1 LEU A 211-27. 246 82.186-14. 706 1.00 22.83 571 CD2 LEU A 211-27.670 81. 950-12. 249 1.00 21.71 572 C LEU A 211-23.961 79.208-12. 605 1.00 19.68 573 O LEU A 211-23.100 79. 322-13. 476 1.00 18.93 574 N ILE A 212-24.205 78.060-11. 987 1.00 16. 77 575 CA ILE A 212-23.501 76. 841-12. 385 1.00 18.99 576 CB ILE A 212-23.242 75.914-11. 191 1.00 21. 38 577 CG2 ILE A 212-22.744 74. 567-11. 679 1.00 20.48 578 CG1 ILE A 212-22.225 76.575-10. 253 1.00 22.50 579 CD1 ILE A 212-21.949 75.786-8. 986 1.00 25.23 580 C ILE A 212-24.482 76.193-13. 363 1.00 18.75 581 O ILE A 212-25.549 75.733-12. 960 1.00 17.19 582 N GLN A 213-24.124 76. 176-14. 646 1.00 18.68 583 CA GLN A 213-25.023 75. 663-15. 672 1.00 19.74 584 CB GLN A 213-25.320 76. 781-16. 668 1.00 19.87 585 CG GLN A 213-25.747 78.088-16. 006 1.00 19.81 586 CD GLN A 213-26.093 79. 161-17. 016 1.00 22.63 587 OE1 GLN A 213-25.249 79. 572-17. 814 1.00 22.95 588 NE2 GLN A 213-27.345 79. 619-16. 991 1.00 21.15 589 C GLN A 213-24.593 74. 416-16. 433 1.00 21.00 590 O GLN A 213-23.403 74.117-16. 577 1.00 20.60 591 N ARG A. 598 73.706-16. 937 1. 00 19. 54 1 2 3 4 5 6 7 8 9 10 592 CA ARG A 214-25.400 72.480-17. 697 1.00 19. 35 593 CB ARG A 214-26.200 71.337-17. 057 1.00 19.57 594 CG ARG A 214-26.125 70.008-17. 801 1.00 21.95 595 CD ARG A 214-27.240 69. 044-17. 364 1.00 22.78 596 NE ARG A 214-27.146 67.771-18. 077 1.00 23.47 597 CZ ARG A 214-28.086 66.828-18. 088 1.00 24.64 598 NH1 ARG A 214-29.223 66. 996-17. 422 1.00 23.78 599 NH2 ARG A 214-27.881 65.709-18. 772 1.00 23.73 600 C ARG A 214-25.849 72.657-19. 146 1.00 19.93 601 O ARG A 214-27.022 72.947-19. 408. 1. 00 18.69 602 N LYS A 215-24. 911 72.507-20. 079 1.00 19.42 603 CA LYS A 215-25.224 72. 589-21. 503 1.00 22.08 604 CB LYS A 215-24. 032 73.131-22. 302 1.00 24.77 605 CG LYS A 215-23.599 74.535-21. 909 1.00 31.40 606 CD LYS A 215-22. 301 74.945-22. 607 1.00 34.85 607 CE LYS A 215-22.509 75.193-24. 089 1.00 37.19 608 NZ LYS A 215-23.378 76.380-24. 308 1.00 39.12 609 C LYS A 215-25.487 71.136-21. 894 1.00 21.62 610 0 LYS A 215-24.553 70.332-21. 969 1.00 19.27 611 N LYS A 216-26.757 70.806-22. 114 1.00 19. 76 612 CA LYS A 216-27.182 69.447-22. 463 1.00 20.26 613 CB LYS A 216-28.711 69. 339-22. 349 1.00 19.25 614 CG LYS A 216-29.256 69. 352-20. 913 1.00 18.85 615 CD LYS A 216-30.683 69.910-20. 854 1.00 21.17 616 CE LYS A 216-31.635 69.209-21. 817 1.00 22.62 617 NZ LYS A 216-31.842 67.781-21. 464 1.00 24.68 618 C LYS A 216-26.765 68.990-23. 856 1.00 20.41 619 O LYS A 216-26.851 69.749-24. 815 1.00 21.78 620 N VAL A 217-26.329 67.739-23. 965 1.00 21.33 621 CA VAL A 217-25.941 67.184-25. 256 1.00 22.38 622 CB VAL A 217-24.933 66.002-25. 097 1.00 22.15 623 CG1 VAL A 217-25.596 64.822-24. 418 1.00 19. 68 624 CG2 VAL A 217-24. 368 65.604-26. 465 1. 00 21. 22 1 2 3 4 5 6 7 8 9 10 625 C VAL A 217-27.216 66.698-25. 969 1.00 22.72 626 O VAL A 217-27.301 66.730-27. 194 1.00 23.92 627 N HIS A 218-28. 209 66.273-25. 189 1.00 22.57 628 CA HIS A 218-29.488 65.798-25. 729 1.00 22.03 629 CB HIS A 218-29.739 64.349-25. 305 1.00 24.54 630 CG HIS A 218-28.759 63.373-25. 881 1.00 26.97 631 CD2 HIS A 218-27.986 63.432-26. 991 1.00 28.14 632 ND1 HIS A 218-28.486 62.158-25. 292 1.00 29.71 633 CE1 HIS A 218-27.585 61.512-26. 010 1. 00 29. 88 634 NE2 HIS A 218-27.266 62.263-27. 048 1.00 28.64 635 C HIS A 218-30.637 66.681-25. 230 1.00 21.95 636 0 HIS A 218-30.747 66.955-24. 032 1.00 22.22 637 N VAL A 219-31.495 67.109-26. 151 1.00 19.61 638 CA VAL A 219-32.623 67.977-25. 818 1.00 19.50 639 CB VAL A 219-32.365 69.425-26. 311 1.00 21.04 640 CG1 VAL A 219-33.405 70.365-25. 734 1.00 21.97 641 CG2 VAL A 219-30.963 69.872-25. 921 1.00 24.02 642 C VAL A 219-33.898 67.463-26. 492 1.00 18. 69 643 O VAL A 219-33.872 67.101-27. 670 1.00 16.26 644 N PHE A 220-35.005 67.421-25. 751 1.00 18. 75 645 CA PHE A 220-36.281 66. 953-26. 311 1.00 20.28 646 CB PHE A 220-36.690 65.602-25. 709 1.00 18.89 647 CG PHE A 220-35.693 64.506-25. 932 1.00 19.85 648 CD1 PHE A 220-34.559 64.412-25. 136 1.00 19.20 649 CD2 PHE A 220-35.891 63.564-26. 938 1.00 17.74 650 CE1 PHE A 220-33.620 63.397-25. 339 1.00 19.12 651 CE2 PHE A 220-34.966 62.548-27. 153 1.00 17.40 652 CZ PHE A 220-33.825 62. 462-26. 344 1.00 17.29 653 C PHE A 220-37.423 67.931-26. 056 1.00 20.66 654 O PHE A 220-37.438 68.641-25. 046 1.00 20.63 655 N GLY A 221-38. 380 67.949-26. 979 1.00 19.88 656 CA GLY A 221-39.556 68.794-26. 842 1.00 20.69 657 C GLY A 221-39.319 70.226-26. 418 1.00 20. 94 1 2 3 4 5 6 7 8 9 10 658 0 GLY A 221-38.586 70. 957-27. 083 1. 00 19.86 659 N ASP A 222-39.939 70. 636-25. 312 1. 00 20.04 660 CA ASP A 222-39. 780 72. 007-24. 844 1.00 22. 07 661 CB ASP A 222-41.147 72.598-24. 436 1.00 23.25 662 CG ASP A 222-41.730 71.951-23. 183 1.00 26.13 663 OD1 ASP A 222-41.228 70.888-22. 756 1.00 27.01 664 OD2 ASP A 222-42.707 72.508-22. 628 1.00 28.38 665 C ASP A 222-38.767 72.178-23. 709 1.00 21.80 666 O ASP A 222-38. 829 73.160-22. 971 1.00 21.80 667 N GLU A 223-37.839 71.232-23. 571 1.00 21. 86 668 CA GLU A 223-36.802 71. 327-22. 535 1.00 23.57 669 CB GLU A 223-35.931 70.064-22. 471 1.00 23.52 670 CG GLU A 223-36.604 68.752-22. 113 1.00 27.42 671 CD GLU A 223-35.601 67.606-22. 081 1.00 26.86 672 OE1 GLU A 223-34.619 67.665-22. 853 1.00 25.62 673 OE2 GLU A 223-35.794 66. 647-21. 301 1.00 29.56 674 C GLU A 223-35.854 72.472-22. 878 1.00 22.93 675 0 GLU A 223-35.654 72.791-24. 049 1.00 22.57 676 N LEU A 224-35.267 73.084-21. 858 1.00 24.10 677 CA LEU A 224-34.289 74.138-22. 087 1.00 25.24 678 CB LEU A 224-34.113 75.000-20. 834 1.00 29.19 679 CG LEU A 224-35.231 75.948-20. 400 1.00 34.51 680 CD1 LEU A 224-34.897 76.521-19. 026 1.00 35.66 681 CD2 LEU A 224-35.389 77.059-21. 424 1.00 35.01 682 C LEU A 224-32.987 73.379-22. 346 1.00 23.30 683 O LEU A 224-32.714 72. 389-21. 667 1.00 22.12 684 N SER A 225-32.195 73.825-23. 317 1.00 21.48 685 CA SER A 225-30.925 73.162-23. 617 1.00 22.99 686 CB SER A 225-30.458 73.511-25. 030 1.00 24.88 687 OG SER A 225-30.269 74.906-25. 156 1.00 29.76 688 C SER A 225-29. 849 73.579-22. 610 1.00 23. 04 689 O SER A 225-28.822 72.914-22. 474 1.00 21.43 690 N LEU A 226-30.088 74.693-21. 921 1.00 21.76 1 2 3 4 5 6 7 8 9 10 691 CA LEU A 226-29.158 75.191-20. 913 1. 00 22.48 692 CB LEU A 226-28.661 76.596-21. 275 1.00 22.79 693 CG LEU A 226-27. 661 77.222-20. 289 1.00 23.12 694 CD1 LEU A 226-26.382 76.392-20. 250 1.00 23. 36 695 CD2 LEU A 226-27.350 78.652-20. 708 1.00 25.47 696 C LEU A 226-29.884 75.226-19. 571 1.00 22.39 697 O LEU A 226-30. 796 76.025-19. 369 1.00 25.42 698 N VAL A 227-29.479 74. 345-18. 664 1.00 20.67 699 CA VAL A 227-30. 089 74. 249-17. 343 1.00 20.48 700 CB VAL A 227-30.293 72.757-16. 943 1.00 23. 37 701 CG1 VAL A 227-30.813 72.656-15. 509 1.00 24.41 702 CG2 VAL A 227-31.249 72.079-17. 914 1.00 22.67 703 C VAL A 227-29.228 74.894-16. 249 1.00 20.91 704 O VAL A 227-28.021 74.658-16. 183 1.00 18.08 705 N THR A 228-29.839 75.718-15. 402 1.00 18.87 706 CA THR A 228-29.096 76.293-14. 285 1.00 19.92 707 CB THR A 228-29.636 77.669-13. 851 1.00 19.25 708 OG1 THR A 228-29.436 78.616-14. 907 1.00 21.14 709 CG2 THR A 228-28.891 78.163-12. 610 1.00 18.71 710 C THR A 228-29.299 75.290-13. 151 1.00 19.52 711 O THR A 228-30.414 75.115-12. 650 1.00 20.06 712 N LEU A 229-28.224 74.614-12. 770 1.00 18.53 713 CA LEU A 229-28.288 73.610-11. 714 1.00 16.82 714 CB LEU A 229-27.089 72.669-11. 830 1.00 17.13 715 CG LEU A 229-27.021 71.831-13. 111 1.00 18.72 716 CD1 LEU A 229-25.651 71.171-13. 208 1.00 17. 12 717 CD2 LEU A 229-28.140 70.776-13. 117 1.00 18. 68 718 C LEU A 229-28. 326 74.239-10. 328 1.00 18.58 719 O LEU A 229-29.209 73.936-9. 516 1.00 16.60 720 N PHE A 230-27. 363 75.116-10. 063 1.00 16.69 721 CA PHE A 230-27.274 75.795-8. 776 1.00 18. 85 722 CB PHE A 230-26. 245 75.108-7. 865 1.00 18.97 723 CG PHE A 230-26.279 73.608-7. 923 1.00 22.96 1 2 3 4 5 6 7 8 9 10 724 CD1 PHE A 230-25.322 72.907-8. 652 1.00 23.71 725 CD2 PHE A 230-27.277 72.897-7. 265 1.00 24. 35 726 CE1 PHE A 230-25.363 71.518-8. 732 1.00 26.34 727 CE2 PHE A 230-27.330 71.505-7. 339 1.00 26.31 728 CZ PHE A 230-26.370 70.815-8. 072 1.00 26.75 729 C PHE A 230-26.815 77.228-9. 010 1.00 20.16 730 O PHE A 230-26.082 77.501-9. 964 1. 00 19. 96 731 N ARG A 231-27.251 78.147-8. 158 1.00 19.93 732 CA ARG A 231-26.799 79.525-8. 286 1.00 19.20 733 CB ARG A 231-27.794 80. 378-9. 081 1.00 21.09 734 CG ARG A 231-29.129 80.648-8. 443 1.00 23.76 735 CD ARG A 231-30.030 81.398-9. 437 1.00 26.41 736 NE ARG A 231-31.368 81.675-8. 909 1.00 29.90 737 CZ ARG A 231-31.686 82.724-8. 152 1.00 31. 65 738 NH1 ARG A 231-30.764 83.622-7. 821 1.00 30.53 739 NH2 ARG A 231-32.932 82.866-7. 714 1.00 31.38 740 C ARG A 231-26.514 80.124-6. 915 1.00 20.98 741 O ARG A 231-27. 019 79.643-5. 892 1.00 18.78 742 N CYS A 232-25.684 81.163-6. 915 1. 00 20.55 743 CA CYS A 232-25.246 81.853-5. 706 1.00 23.47 744 C CYS A 232-25.530 83. 350-5. 867 1.00 22.93 745 O CYS A 232-25.416 83.879-6. 968 1.00 21.31 746 CB CYS A 232-23.726 81.634-5. 532 1.00 25.13 747 SG CYS A 232-23.104 81.962-3. 857 1.00 36.00 748 N ILE A 233-25.903 84.033-4. 785 1.00 22.35 749 CA ILE A 233-26.152 85.475-4. 870 1.00 23.25 750 CB ILE A 233-27.610 85.772-5. 330 1.00 26.86 751 CG2 ILE A 233-28.611 85.223-4. 328 1.00 25. 75 752 CG1 ILE A 233-27.795 87.283-5. 519 1.00 27. 81 753 CD1 ILE A 233-29.089 87.661-6. 212 1.00 30.72 754 C ILE A 233-25.846 86.211-3. 560 1.00 23.49 755 0 ILE A 233-26.144 85.716-2. 472 1.00 22.21 756 N GLN A 234-25.234 87.390-3. 673 1.00 22.71 1 2 3 4 5 6 7 8 9 10 757 CA GLN A 234-24.863 88.199-2. 508 1.00 23.56 758 CB GLN A 234-23. 361 88.050-2. 212 1.00 24.39 759 CG GLN A 234-22. 906 86.655-1. 785 1.00 24.62 760 CD GLN A 234-23.130 86.405-0. 308 1.00 26.45 761 OEI GLN A 234-22.409 86.939 0.536 1.00 25.26 762 NE2 GLN A 234-24.139 85.602 0.015 1.00 25.91 763 C GLN A 234-25.144 89.695-2. 692 1.00 24.88 764 O GLN A 234-24.867 90. 253-3. 753 1.00 23.58 765 N ASN A 235-25.691 90.343-1. 664 1.00 25.68 766 CA ASN A 235-25.914 91.789-1. 732 1.00 25.53 767 CB ASN A 235-26.813 92.275-0. 587 1.00 25.18 768 CG ASN A 235-28. 287 92.042-0. 858 1.00 25. 77 769 OD1 ASN A 235-28.837 92. 549-1. 839 1.00 28.20 770 ND2 ASN A 235-28.936 91.279 0.011 1.00 23.24 771 C ASN A 235-24.523 92.399-1. 566 1.00 27. 70 772 O ASN A 235-23.687 91.854-0. 835 1.00 26.93 773 N MET A 236-24.268 93.515-2. 243 1.00 28.96 774 CA MET A 236-22.969 94.179-2. 160 1.00 28.89 775 CB MET A 236-22.363 94. 327-3.558 1.00 27.92 776 CG MET A 236-22.297 93. 044-4. 372 1. 00 26. 93 777 SD MET A 236-21. 306 91.751-3. 592 1. 00 27.17 778 CE MET A 236-19.670 92.533-3. 622 1.00 25. 87 779 C MET A 236-23.115 95.568-1. 531 1.00 31.38 780 O MET A 236-24.109 96.256-1. 762 1.00 29. 79 781 N PRO A 237-22.127 95.993-0. 721 1.00 32.65 782 CD PRO A 237-20.962 95.228-0. 236 1.00 33.29 783 CA PRO A 237-22.185 97.311-0. 083 1.00 35.23 784 CB PRO A 237-21.232 97.161 1.094 1.00 34. 30 785 CG PRO A 237-20.160 96.285 0.512 1.00 34. 12 786 C PRO A 237-21.741 98.407-1. 052 1.00 37.76 787 O PRO A 237-21.291 98.126-2. 166 1.00 36.93 788 N GLU A 238-21.857 99.656-0. 616 1.00 41. 30 789 CA GLU A 238-21 *479 100.787-1. 453 1.00 44.42 1 2 3 4 5 6 7 8 9 10 790 CB GLU A 238-22. 205 102. 049-0. 984 1. 00 48. 19 791 CG GLU A 238-22.293 103.128-2. 045 1.00 54.32 792 CD GLU A 238-23.257 102.759-3. 158 1.00 57. 59 793 OE1 GLU A 238-24.484 102.776-2. 914 1.00 59.22 794 OE2 GLU A 238-22. 787 102. 443-4.273 1.00 60.84 795 C GLU A 238-19.973 101.034-1. 421 1.00 44.19 796 O GLU A 238-19. 396 101.508-2. 400 1.00 44.52 797 N THR A 239-19.345 100.704-0. 296 1.00 43.16 798 CA THR A 239-17.910 100.912-0. 125 1.00 43.04 799 CB THR A 239-17.627 101.775 1.127 1.00 43.33 800 OG1 THR A 239-18.393 102.984 1.059 1.00 46.02 801 CG2 THR A 239-16.150 102.127 1.210 1.00 44.85 802 C THR A 239-17.127 99.608 0.015 1.00 41.67 803 O THR A 239-17.578 98.669 0.672 1.00 42. 02 804 N LEU A 240-15.950 99.575-0. 605 1.00 39.81 805 CA LEU A 240-15.053 98.421-0. 568 1.00 38.51 806 CB LEU A 240-14.223 98.458 0.721 1.00 39.40 807 CG LEU A 240-13.347 99.704 0.915 1.00 40.71 808 CD1 LEU A 240-12.654 99.652 2.275 1.00 40.94 809 CD2 LEU A 240-12.319 99.786-0. 207 1.00 40.23 810 C LEU A 240-15.753 97.062-0. 697 1.00 36.28 811 O LEU A 240-15.691 96.231 0.211 1.00 34.37 812 N PRO A 241-16.424 96.820-1. 836 1.00 35. 38 813 CD PRO A 241-16.591 97.731-2. 982 1.00 34.73 814 CA PRO A 241-17. 130 95.554-2. 070 1.00 33.84 815 CB PRO A 241-17.725 95.741-3. 465 1.00 34.25 816 CG PRO A 241-17.869 97.236-3. 585 1.00 35. 67 817 C PRO A 241-16.162 94. 372-2. 021 1.00 32.62 818 O PRO A 241-15.086 94.420-2. 619 1. 00 31.23 819 N ASN A 242-16.542 93.314-1. 312 1.00 30.81 820 CA ASN A 242-15.690 92.135-1. 206 1.00 31. 37 821 CB ASN A 242-14.425 92.468-0. 409 1.00 34.40 822 CG ASN A 242-13.155 92.173-1. 184 1. 00 38.42 1 2 3 4 5 6 7 8 9 10 823 ODI ASN A 242-12.937 92.715-2. 268 1.00 43.44 824 ND2 ASN A 242-12.313 91. 310-0. 636 1. 00 41.11 825 C ASN A 242-16.412 90.960-0. 552 1.00 28. 94 826 O ASN A 242-16.236 90.695 0.638 1.00 28.61 827 N ASN A 243-17.227 90.262-1. 337 1.00 25.95 828 CA ASN A 243-17.969 89.103-0. 845 1.00 24.09 829 CB ASN A 243-19.478 89. 375-0. 840 1. 00 23.38 830 CG ASN A 243-19.924 90.220 0.333 1.00 25.03 831 ODI ASN A 243-19.575 89.945 1.478 1. 00 25.12 832 ND2 ASN A 243-20.725 91.244 0.053 1.00 26. 32 833 C ASN A 243-17.724 87.887-1. 730 1.00 21.55 834 O ASN A 243-17.938 87.956-2. 937 1.00 23.63 835 N SER A 244-17.267 86.784-1. 146 < 1. 00 20.09 836 CA SER A 244-17.081 85.568-1. 931 1.00 19.98 837 CB SER A 244-15. 972 84.681-1. 341 1.00 17. 68 838 OG SER A 244-16.271 84.248-0. 029 1.00 20.55 839 C SER A 244-18.445 84.854-1. 887 1.00 21.86 840 O SER A 244-19.193 84.991-0. 914 1.00 20. 31 841 N CYS A 245-18.771 84.121-2. 949 1. 00 21.55 842 CA CYS A 245-20.053 83.418-3. 055 1.00 22. 45 843 C CYS A 245-19.793 81.964-3. 446 1.00 19. 31 844 O CYS A 245-19.239 81.712-4. 505 1. 00 18.58 845 CB CYS A 245-20.922 84.082-4. 138 1.00 26.01 846 SG CYS A 245-22.710 83.955-3. 835 1. 00 33.25 847 N TYR A 246-20.204 81.021-2. 598 1.00 19.04 848 CA TYR A 246-20.006 79.590-2. 851 1.00 17.51 849 CB TYR A 246-19.129 78.981-1. 743 1.00 16. 88 850 CG TYR A 246-18.877 77.482-1. 858 1.00 16. 53 851 CD1 TYR A 246-19.868 76.546-1. 517 1.00 15.32 852 CE1 TYR A 246-19.636 75.169-1. 630 1.00 13.58 853 CD2 TYR A 246-17.653 76.999-2. 314 1. 00 15.48 854 CE2 TYR A 246-17.412 75.624-2. 434 1.00 16.02 855 CZ TYR A 246-18.405 74. 719-2.091 1. 00 16. 73 1 2 3 4 5 6 7 8 9 10 856 OH TYR A 246-18.161 73.368-2. 216 1. 00 17.20 857 C TYR A 246-21. 328 78.818-2. 921 1.00 18.85 858 O TYR A 246-22.263 79.091-2. 158 1.00 16.06 859 N SER A 247-21. 396 77.861-3. 842 1.00 17. 42 860 CA SER A 247-22.570 77. 003-3. 981 1.00 19.21 861 CB SER A 247-23.631 77.649-4. 876 1.00 18. 51 862 OG SER A 247-24.854 76.933-4. 758 1.00 23.10 863 C SER A 247-22.120 75.668-4. 575 1. 00 18. 51 864 O SER A 247-21.140 75. 619-5. 319 1.00 15.76 865 N ALA A 248-22.830 74.594-4. 234 1.00 17.47 866 CA ALA A 248-22.491 73.258-4. 715 1.00 17.55 867 CB ALA A 248-21. 300 72.701-3. 923 1.00 15.08 868 C ALA A 248-23.678 72.314-4. 569 1.00 17.97 869 O ALA A 248-24.562 72.539-3. 741 1.00 17.04 870 N GLY A 249-23.673 71. 246-5. 358 1.00 16.58 871 CA GLY A 249-24.749 70.275-5. 297 1.00 17.39 872 C GLY A 249-24.449 69.054-6. 144 1.00 17.96 873 O GLY A 249-23. 353 68.928-6. 702 1.00 16.98 874 N ILE A 250-25.431 68.159-6. 246 1.00 17.14 875 CA ILE A 250-25.289 66. 930-7. 024 1.00 16.29 876 CB ILE A 250-25.619 65.684-6. 155 1.00 17. 57 877 CG2 ILE A 250-25.511 64.399-6. 998 1.00 14.86 878 CG1 ILE A 250-24.663 65.621-4. 958 1.00 16.46 879 CD1 ILE A 250-25.060 64.590-3. 896 1.00 18.29 880 C ILE A 250-26.220 66.947-8. 238 1.00 18. 49 881 O ILE A 250-27.381 67.363-8. 146 1.00 16.29 882 N ALA A 251-25. 702 66. 508-9. 379 1. 00 17.43 883 CA ALA A 251-26.499 66.453-10. 598 1.00 19.63 884 CB ALA A 251-26.245 67. 701-11. 458 1.00 19. 35 885 C ALA A 251-26.176 65.200-11. 401 1.00 19. 18 886 O ALA A 251-25. 088 64.631-11. 279 1.00 18.94 887 N LYS A 252-27. 141 64.767-12. 205 1.00 19.65 888 CA LYS A 252-26. 982 63.604-13. 078 1.00 20.03 1 2 3 4 5 6 7 9 10 889 CB LYS A 252-28. 319 62. 852-13. 188 1. 00 22. 29 890 CG LYS A 252-28. 445 61.847-14. 338 1.00 25.87 891 CD LYS A 252-27. 384 60.756-14. 290 1.00 30.58 892 CE LYS A 252-27.701 59.617-15. 267 1.00 35.14 893 NZ LYS A 252-28. 378 58.478-14. 581 1.00 41.33 894 C LYS A 252-26.567 64.177-14. 435 1.00 20.86 895 O LYS A 252-27.308 64.966-15. 040 1.00 21.89 896 N LEU A 253-25.376 63.810-14. 901 1.00 18.93 897 CA LEU A 253-24.879 64.313-16. 178 1.00 20.06 898 CB LEU A 253-23.555 65.063-15. 970 1.00 18.55 899 CG LEU A 253-23.599 66.190-14. 925 1.00 19.56 900 CD1 LEU A 253-22.195 66.760-14. 719 1.00 18.04 901 CD2 LEU A 253-24.570 67. 282-15. 377 1.00 18.05 902 C LEU A 253-24.698 63.198-17. 205 1.00 20.37 903 O LEU A 253-24.480 62.041-16. 854 1.00 19.56 904 N GLU A 254-24.779 63.570-18. 477 1.00 20.57 905 CA GLU A 254-24.662 62.623-19. 581 1.00 23.15 906 CB GLU A 254-25.872 62.806-20. 516 1.00 26. 32 907 CG GLU A 254-25.940 61.895-21. 737 1.00 30.97 908 CD GLU A 254-26. 345 60. 472-21. 396 1.00 34.66 909 OE1 GLU A 254-26.966 60.265-20. 331 1.00 35.01 910 OE2 GLU A 254-26.057 59.561-22. 205 1.00 38.93 911 C GLU A 254-23. 367 62.850-20. 357 1.00 22.68 912 O GLU A 254-22.919 63.986-20. 500 1. 00 22.23 913 N GLU A 255-22.765 61.771-20. 852 1.00 22.99 914 CA GLU A 255-21.545 61.885-21. 644 1.00 22.76 915 CB GLU A 255-21.176 60.528-22. 249 1.00 24.99 916 CG GLU A 255-19.856 60.543-22. 999 1.00 32.85 917 CD GLU A 255-19.539 59.218-23. 666 1.00 37.45 918 OE1 GLU A 255-19.969 58.163-23. 148 1.00 39.55 919 OE2 GLU A 255-18. 841 59.235-24. 705 1.00 41.52 920 C GLU A 255-21.819 62.878-22. 770 1.00 21.33 921 O GLU A 255-22.779 62.710-23. 522 1.00 19.65 1 2 3 4 5 6 7 8 9 10 922 N GLY A 256-20.987 63.911-22. 887 1.00 20.68 923 CA GLY A 256-21.192 64.907-23. 928 1.00 18.70 924 C GLY A 256-21.636 66.257-23. 386 1.00 18.43 925 O GLY A 256-21.433 67.290-24. 029 1.00 17.58 926 N ASP A 257-22.258 66.253-22. 211 1.00 18.15 927 CA ASP A 257-22.704 67.490-21. 570 1.00 19.85 928 CB ASP A 257-23.427 67.216-20. 243 1.00 21.12 929 CG ASP A 257-24.809 66.618-20. 418 1.00 24.44 930 OD1 ASP A 257-25.344 66.612-21. 547 1.00 24.95 931 OD2 ASP A 257-25. 366 66. 167-19. 396 1. 00 26. 05 932 C ASP A 257-21.483 68.331-21. 220 1.00 20.95 933 O ASP A 257-20.376 67.807-21. 089 1.00 20.21 934 N GLU A 258-21.699 69.630-21. 049 1.00 21. 79 935 CA GLU A 258-20.635 70.540-20. 652 1.00 22.12 936 CB GLU A 258-20.205 71.435-21. 818 1. 00 25.14 937 CG GLU A 258-19.616 70.677-22. 999 1.00 28.99 938 CD GLU A 258-19.000 71.602-24. 033 1.00 34.89 939 OE1 GLU A 258-19.668 72.576-24. 436 1.00 37.00 940 OE2 GLU A 258-17.846 71.353-24. 446 1.00 39.24 941 C GLU A 258-21.167 71.402-19. 510 1.00 22.31 942 O GLU A 258-22. 366 71.697-19. 449 1.00 22. 45 943 N LEU A 259-20.280 71.783-18. 597 1.00 19.58 944 CA LEU A 259-20.652 72.626-17. 462 1.00 19.68 945 CB LEU A 259-20.280 71.950-16. 140 1. 00 19. 10 946 CG LEU A 259-20.791 70.544-15. 834 1.00 21.15 947 CD1 LEU A 259-20.090 70.016-14. 579 1.00 19.50 948 CD2 LEU A 259-22. 310 70.572-15. 647 1.00 20.67 949 C LEU A 259-19.891 73.941-17. 561 1.00 19.30 950 O LEU A 259-18.707 73.954-17. 922 1.00 17.33 951 N GLN A 260-20.564 75.041-17. 236 1.00 18.14 952 CA GLN A 260-19.932 76. 355-17. 259 1.00 18.11 953 CB GLN A 260-20. 329 77.136-18. 519 1. 00 17. 50 954 CG GLN A 260-21.827 77.390-18. 650 1.00 20. 55 2 3 4 5 6 7 8 9 10 955 CD GLN A 260-22.188 78.166-19. 904 1.00 23.38 956 OE1 GLN A 260-21.544 78.021-20. 942 1.00 24.52 957 NE2 GLN A 260-23. 233 78.981-19. 818 1. 00 21.05 958 C GLN A 260-20.379 77.131-16. 032 1.00 18.47 959 O GLN A 260-21.414 76.826-15. 436 1.00 17.16 960 N LEU A 261-19.582 78.122-15. 649 1.00 18.33 961 CA LEU A 261-19.909 78.982-14. 517 1.00 19.02 962 CB LEU A 261-18.767 78.995-13. 495 1.00 18.42 963 CG LEU A 261-19.070 79.765-12. 198 1.00 17.98 964 CD1 LEU A 261-18.243 79.207-11. 067 1.00 18.99 965 CD2 LEU A 261-18. 805 81.255-12. 398 1.00 19.34 966 C LEU A 261-20.103 80. 364-15. 140 1.00 21.26 967 O LEU A 261-19.163 80.933-15. 704 1.00 20.65 968 N ALA A 262-21. 321 80.894-15. 047 1.00 20.42 969 CA ALA A 262-21.643 82.186-15. 650 1.00 22.25 970 CB ALA A 262-22. 748 81.998-16. 709 1.00 20.86 971 C ALA A 262-22.064 83.272-14. 669 1.00 23.14 972 O ALA A 262-22.724 82.998-13. 667 1.00 24.04 973 N ILE A 263-21.681 84.508-14. 980 1.00 22.48 974 CA ILE A 263-22.030 85.669-14. 165 1.00 22.57 975 CB ILE A 263-20.770 86.477-13. 799 1. 00 23. 59 976 CG2 ILE A 263-21.155 87.747-13. 038 1.00 19. 74 977 CG1 ILE A 263-19.839 85.600-12. 954 1.00 23.50 978 CD1 ILE A 263-18.497 86.221-12. 662 1.00 24.01 979 C ILE A 263-22.984 86.509-15. 014 1.00 24.73 980 O ILE A 263-22.584 87.084-16. 027 1.00 23.63 981 N PRO A 264-24.265 86.582-14. 612 1.00 26. 89 982 CD PRO A 264-24.853 85.915-13. 435 1.00 28.13 983 CA PRO A 264-25.289 87. 339-15. 339 1.00 30.28 984 CB PRO A 264-26. 588 86.812-14. 738 1. 00 29.83 985 CG PRO A 264-26.212 86.575-13. 324 1.00 27.91 986 C PRO A 264-25.191 88.855-15. 275 1.00 33.31 987 O PRO A 264-26. 100 89.526-14. 783 1. 00 34. 98 1 2 3 4 5 6 7 8 9 10 988 N ARG A 265-24.090 89.392-15. 785 1. 00 35. 69 989 CA ARG A 265-23.885 90.831-15. 804 1.00 37.53 990 CB ARG A 265-23.610 91.352-14. 399 1.00 41. 40 991 CG ARG A 265-23.489 92.857-14. 366 1.00 47.23 992 CD ARG A 265-23.116 93. 360-13. 002 1.00 51.81 993 NE ARG A 265-22.905 94.801-13. 026 1.00 57.18 994 CZ ARG A 265-22.419 95.489-12. 004 1.00 59.61 995 NH1 ARG A 265-22.100 94.854-10. 886 1. 00 61.64 996 NH2 ARG A 265-22.256 96.803-12. 093 1.00 60.71 997 C ARG A 265-22.718 91.193-16. 709 1.00 37. 40 998 O ARG A 265-21.699 90.503-16. 726 1.00 35.08 999 N GLU A 266-22.867 92.280-17. 459 1.00 37.18 1000 CA GLU A 266-21.816 92.727-18. 364 1.00 38. 24 1001 CB GLU A 266-22. 368 93.760-19. 347 1.00 41.50 1002 CG GLU A 266-23.518 93.251-20. 197 1. 00 46.71 1003 CD GLU A 266-24.053 94. 309-21. 146 1.00 50.47 1004 OE1 GLU A 266-23.286 94.766-22. 023 1. 00 51. 15 1005 OE2 GLU A 266-25.238 94.685-21. 011 1.00 52.22 1006 C GLU A 266-20.650 93.330-17. 593 1.00 36.03 1007 O GLU A 266-20.846 94.073-16. 633 1.00 35.92 1008 N ASN A 267 -19.437 92.998 -18.020 1.00 36.17 1009 CA ASN A 267 -18.226 93.501 -17.383 1.00 35.56 1010 CB ASN A 267-17.951 94.933-17. 848 1. 00 38. 97 1011 CG ASN A 267-17.677 95. 014-19. 335 1.00 41.43 1012 OD1 ASN A 267-16.700 94.448-19. 829 1.00 42.41 1013 ND2 ASN A 267-18.543 95.716-20. 060 1. 00 42.67 1014 C ASN A 267-18.285 93.459-15. 859 1.00 34.66 1015 O ASN A 267-17.998 94.454-15. 188 1.00 33.26 1016 N ALA A 268-18.653 92. 304-15. 311 1.00 32.17 1017 CA ALA A 268-18. 733 92.154-13. 864 1.00 31.86 1018 CB ALA A 268-19.309 90.774-13. 506 1.00 29.35 1019 C ALA A 268-17.345 92. 328-13. 244 1.00 31.26 1020 O ALA A 268-16.344 91.865-13. 799 1.00 31.15 1 2 3 4 5 6 7 8 9 10 1021 N GLN A 269-17.290 93.004-12. 100 1.00 30.89 1022 CA GLN A 269-16.025 93.229-11. 405 1.00 31.88 1023 CB GLN A 269-16.046 94.585-10. 693 1.00 33.93 1024 CG GLN A 269-16.209 95.761-11. 650 1.00 37.66 1025 CD GLN A 269-15.096 95.824-12. 688 1.00 40.45 1026 OE1 GLN A 269-13.951 96. 152-12. 370 1.00 42.35 1027 NE2 GLN A 269-15.427 95.498-13. 934 1.00 39.82 1028 C GLN A 269-15. 774 92. 109-10. 399 1.00 29.72 1029 O GLN A 269-16.486 91.987-9. 396 1.00 28.87 1030 N ILE A 270-14. 762 91.291-10. 672 1.00 28.40 1031 CA ILE A 270-14.432 90.167-9. 798 1.00 28.75 1032 CB ILE A 270-14.933 88.845-10. 401 1.00 28. 36 1033 CG2 ILE A 270-16.442 88.898-10. 601 1.00 27. 35 1034 CG1 ILE A 270-14. 225 88.597-11. 738 1.00 29. 38 1035 CD1 ILE A 270-14.535 87. 264-12. 367 1.00 30.52 1036 C ILE A 270-12.929 90.021-9. 565 1.00 29.37 1037 O ILE A 270-12. 120 90.688-10. 207 1.00 30.26 1038 N SER A 271 -12.565 89.135 -8.642 1.00 28.35 1069 CA SER A 271 -11.164 88.873 -8.346 1.00 26.75 1040 CB SER A 271-10. 943 88.707-6. 843 1.00 25.77 1041 OG SER A 271-9.667 88.139-6. 585 1. 00 26.62 1042 C SER A 271-10.763 87. 593-9. 059 1.00 26. 32 1043 O SER A 271-11.465 86.581-8. 979 1. 00 25.70 1044 N LEU A 272-9.639 87.636-9. 763 1.00 24.11 1045 CA LEU A 272-9.173 86.464-10. 480 1.00 24.05 1046 CB LEU A 272-8.718 86.855-11. 890 1.00 23. 90 1047 CG LEU A 272-9.807 87.486-12. 769 1.00 26. 27 1048 CD1 LEU A 272-9.223 87.826-14. 130 1.00 28.50 1049 CD2 LEU A 272-10.990 86.534-12. 921 1. 00 26.39 1050 C LEU A 272-8. 062 85.712-9. 748 1.00 24.08 1051 O LEU A 272-7.199 85.103-10. 379 1.00 26.09 1052 N ASP A 273-8.079 85.762-8. 418 1.00 23.07 1053 CA ASP A 273-7.088 85.040-7. 620 1.00 23. 98 1 2 3 4 5 6 7 8 9 10 1054 CB ASP A 273-7.034 85.555-6. 174 1.00 26.92 1055 CG ASP A 273-6.375 86.923-6. 044 1.00 32.04 1056 OD1 ASP A 273-5. 669 87. 359-6. 979 1.00 34.01 1057 OD2 ASP A 273-6.554 87.557-4. 978 1.00 33.19 1058 C ASP A 273-7.540 83.577-7. 602 1.00 22.53 1059 O ASP A 273-8.702 83. 293-7. 315 1.00 21.40 1060 N GLY A 274-6.623 82.664-7. 901 1.00 20.35 1061 CA GLY A 274-6.944 81.248-7. 925 1.00 19.85 1062 C GLY A 274-7.410 80.644-6. 614 1.00 20.01 1063 O GLY A 274-8.051 79.593-6. 612 1.00 20.66 1064 N ASP A 275-7.099 81.292-5. 494 1.00 19.09 1065 CA ASP A 275-7.518 80.764-4. 200 1.00 19. 19 1066 CB ASP A 275-6.517 81.154-3. 094 1.00 20.60 1067 CG ASP A 275-6.412 82.665-2. 879 1.00 23.32 1068 OD 1 ASP A 275-7.232 83.424-3. 430 1.00 25.32 1069 OD2 ASP A 275-5.501 83.097-2. 139 1.00 25.38 1070 C ASP A 275-8. 924 81.202-3. 787 1.00 18. 63 1071 O ASP A 275-9.431 80.754-2. 762 1. 00 19.22 1072 N VAL A 276-9.566 82.048-4. 586 1.00 17.37 1073 CA VAL A 276-10.900 82.520-4. 217 1.00 17.42 1074 CB VAL A 276-10.833 83.993-3. 726 1.00 16.73 1075 CG1 VAL A 276-10.710 84.940-4. 904 1.00 16.81 1076 CG2 VAL A 276-12.050 84.309-2. 867 1.00 17.50 1077 C VAL A 276-11.956 82.376-5. 318 1.00 17.14 1078 O VAL A 276-13.158 82.428-5. 045 1.00 17.43 1079 N THR A 277-11.513 82.193-6. 558 1.00 16.66 1080 CA THR A 277-12.435 82.003-7. 680 1.00 16.66 1081 CB THR A 277-12. 348 83.188-8. 667 1.00 17.41 1082 OG1 THR A 277-12.717 84.388-7. 980 1.00 16.86 1083 CG2 THR A 277-13.282 82.984-9. 856 1.00 16.66 1084 C THR A 277-12.030 80. 696-8. 350 1.00 15. 82 1085 O THR A 277-10.975 80.613-8. 995 1. 00 15.15 1086 N PHE A 278-12. 861 79. 669-8. 167 1.00 14. 12 1 2 3 4 5 6 7 8 9 10 1087 CA PHE A 278-12.586 78.340-8. 700 1.00 15.26 1088 CB PHE A 278-11.720 77.547-7. 700 1.00 16.02 1089 CG PHE A 278-12.251 77.543-6. 290 1.00 17.38 1090 CD1 PHE A 278-13.172 76.582-5. 877 1.00 17.94 1091 CD2 PHE A 278-11.815 78.497-5. 366 1.00 17. 19 1092 CE1 PHE A 278-13.653 76.564-4. 564 1.00 17.19 1093 CE2 PHE A 278-12.286 78.491-4. 052 1.00 15. 36 1094 CZ PHE A 278-13.209 77.519-3. 648 1.00 17.09 1095 C PHE A 278-13.873 77.582-9. 052 1. 00 15. 50 1096 O PHE A 278-14.967 78. 003-8. 675 1.00 15.05 1097 N PHE A 279-13.724 76.455-9. 744 1. 00 16.00 1098 CA PHE A 279-14.866 75.683-10. 248 1.00 16.88 1099 CB PHE A 279-15.286 76.371-11. 568 1.00 16.37 1100 CG PHE A 279-16.391 75. 686-12. 344 1. 00 18.06 1101 CD1 PHE A 279-17.539 75.210-11. 715 1.00 19.68 1102 CD2 PHE A 279-16. 317 75.626-13. 737 1.00 17.63 1103 CE1 PHE A 279-18.598 74.682-12. 464 1.00 19.89 1104 CE2 PHE A 279-17.376 75.099-14. 498 1.00 18.95 1105 CZ PHE A 279-18.517 74.631-13. 856 1.00 17.92 1106 C PHE A 279-14.427 74.228-10. 470 1.00 16. 55 1107 O PHE A 279-13. 365 73.982-11. 038 1. 00 17.46 1108 N GLY A 280-15.224 73.264-10. 013 1.00 16.47 1109 CA GLY A 280-14.839 71. 875-10. 202 1. 00 15.48 1110 C GLY A 280-15.962 70. 852-10. 106 1. 00 16.77 1111 O GLY A 280-17.098 71.178-9. 753 1.00 14.69 1112 N ALA A 281-15.639 69.602-10. 421 1.00 16.27 1113 CA ALA A 281-16.624 68.522-10. 365 1.00 17. 58 1114 CB ALA A 281-17.333 68.390-11. 700 1.00 16.84 1115 C ALA A 281-15.962 67.202-9. 983 1.00 17.19 1116 O ALA A 281-14.788 66.959-10. 285 1.00 17.14 , 1117 N LEU A 282-16. 735 66. 346-9. 329 1.00 17. 55 1118 CA LEU A 282-16.258 65.056-8. 853 1.00 19.19 1119 CB LEU A 282-16.022 65.158-7. 346 1. 00 19.51 2 3 4-5 6 7 8 9 10 1120 CG LEU A 282-15.754 63. 923-6. 486 1.00 23.82 1121 CD1 LEU A 282-14.359 63.377-6. 721 1.00 24.75 1122 CD2 LEU A 282-15. 892 64. 338-5. 036 1.00 26. 07 1123 C LEU A 282-17.280 63. 957-9. 150 1.00 19.21 1124 O LEU A 282-18.459 64.092-8. 807 1.00 16.65 1125 N LYS A 283-16.835 62.873-9. 785 1.00 19.47 1126 CA LYS A 283-17.745 61.774-10. 103 1.00 22.29 1127 CB LYS A 283-17. 209 60. 940-11. 279 1.00 23. 77 1128 CG LYS A 283-18.134 59.783-11. 704 1.00 27. 37 1129 CD LYS A 283-17.806 59.287-13. 109 1.00 29.25 1130 CE LYS A 283-18. 324 57.871-13. 371 1.00 31.61 1131 NZ LYS A 283-19.746 57.672-12. 979 1.00 33.87 1132 C LYS A 283-17.950 60.893-8. 879 1.00 22.55 1133 O LYS A 283-16.998 60. 365-8. 310 1.00 24. 21 1134 N LEU A 284-19.206 60.745-8. 473 1.00 22.27 1135 CA LEU A 284-19.549 59. 947-7. 308 1.00 24. 18 1136 CB LEU A 284-20.903 60.405-6. 755 1.00 22. 68 1137 CG LEU A 284-21.014 61.901-6. 426 1.00 22.67 1138 CD1 LEU A 284-22.451 62.248-6. 039 1.00 22.39 1139 CD2 LEU A 284-20.059 62. 245-5.293 1.00 22.61 1140 C LEU A 284-19.605 58.460-7. 649 1.00 28.22 1141 O LEU A 284-20.189 58.070-8. 659 1. 00 29. 05 1142 N LEU A 285-18.987 57.632-6. 814 1.00 31.65 1143 CA LEU A 285-19.006 56.193-7. 045 1.00 36.60 1144 CB LEU A 285-17.988 55.479-6. 151 1.00 38.80 1145 CG LEU A 285-16.539 55.459-6. 651 1.00 40. 99 1146 CD1 LEU A 285-15.652 54.752-5. 644 1.00 40.75 1147 CD2 LEU A 285-16. 476 54. 745-7. 995 1.00 41.81 1148 C LEU A 285 -20.407 55.671 -6.755 1.00 38.46 1149 O LEU A 285 -20.909 54.847 -7.545 1.00 40.59 1150 OXT LEU A 285-20.984 56.101-5. 734 1.00 41.57 1151 CB VAL B 142-18.194 49. 606-3.949 1.00 48.61 1152 CG1 VAL B 142-17. 830 50.631-2. 891 1. 00 49. 88 1 2 3 4 5 6 7 8 9 10 1153 CG2 VAL B 142-17.792 48.212-3. 498 1. 00 49. 53 1154 C VAL B 142-20.073 51.035-4. 760 1.00 46.20 1155 O VAL B 142-19.503 51.507-5. 746 1.00 45. 45 1156 N VAL B 142-20.108 48.591-5. 202 1.00 47.58 1157 CA VAL B 142-19.711 49.651-4. 228 1.00 47.33 1158 N THR B 143-21.022 51.683-4. 093 1.00 44.49 1159 CA THR B 143-21.481 53.002-4. 506 1.00 42.70 1160 CB THR B 143-22.714 52.873-5. 440 1.00 43.09 1161 OG1 THR B 143-23. 430 54.111-5. 478 1.00 47.29 1162 CG2 THR B 143-23.636 51.763-4. 957 1.00 43.39 1163 C THR B 143-21.824 53.891-3. 314 1.00 40.83 1164 O THR B 143-21.896 53.426-2. 176 1.00 40.80 1165 N GLN B 144-22.013 55.179-3. 577 1.00 36.67 1166 CA GLN B 144-22. 359 56.123-2. 527 1.00 34.10 1167 CB GLN B 144-21.476 57. 371-2. 612 1.00 33.73 1168 CG GLN B 144-19.995 57.074-2. 745 1.00 36.84 1169 CD GLN B 144-19.144 58. 329-2. 770 1.00 37.09 1170 OE1 GLN B 144-18.908 58.952-1. 739 1.00 41. 38 1171 NE2 GLN B 144-18.686 58.710-3. 954 1.00 36.04 1172 C GLN B 144-23.821 56. 519-2.692 1.00 31.39 1173 O GLN B 144-24.169 57.272-3. 600 1.00 31.63 1174 N ASP B 145-24. 676 55.992-1. 824 1.00 28.68 1175 CA ASP B 145-26.093 56.316-1. 872 1.00 28.33 1176 CB ASP B 145-26.872 55.482-0. 849 1.00 30. 29 1177 CG ASP B 145-26.918 54.005-1. 203 1.00 35.41 1178 OD1 ASP B 145-27. 534 53.233-0. 433 1.00 36.42 1179 OD2 ASP B 145-26.346 53.613-2. 247 1.00 35.65 1180 C ASP B 145-26.250 57.795-1. 534 1.00 26.53 1181 O ASP B 145-25. 483 58. 340-0. 738 1.00 24.49 1182 N CYS B 146-27. 234 58. 444-2. 143 1.00 24.09 1183 CA CYS B 146-27.479 59.853-1. 876 1.00 23.43 1184 CB CYS B 146-26.449 60.736-2. 603 1.00 25.63 1185 SG CYS B 146-26.087 60. 312-4.330 1. 00 25 30 2 3 4 5 6 7 8 9 10 1186 C CYS B 146-28.891 60.264-2. 250 1.00 24.56 1187 O CYS B 146-29.589 59.564-2. 990 1.00 23.05 1188 N LEU B 147-29. 314 61.401-1. 715 1. 00 23.23 1189 CA LEU B 147-30.647 61.919-1. 965 1.00 23.43 1190 CB LEU B 147-31.606 61.396-0. 888 1. 00 24.87 1191 CG LEU B 147-33.098 61.711-1. 005 1.00 28.05 1192 CD1 LEU B 147-33.894 60.652-0. 260 1.00 29.69 1193 CD2 LEU B 147-33. 388 63.094-0. 453 1.00 28.70 1194 C LEU B 147-30.587 63.442-1. 938 1.00 23.26 1195 O LEU B 147-29.872 64.028-1. 126 1.00 22. 32 1196 N GLN B 148-31. 335 64.080-2. 830 1.00 21.66 1197 CA GLN B 148-31.352 65.532-2. 893 1.00 19.17 1198 CB GLN B 148-30.466 65.999-4. 055 1.00 19. 35 1199 CG GLN B 148-30.507 67.485-4. 355 1.00 18.67 1200 CD GLN B 148-29.453 67. 879-5. 374 1.00 23.95 1201 OE1 GLN B 148-28. 311 68.188-5. 019 1.00 21. 80 1202 NE2 GLN B 148-29.827 67.849-6. 653 1.00 20.97 1203 C GLN B 148-32.773 66.064-3. 038 1.00 19.00 1204 O GLN B 148-33.593 65.507-3. 771 1. 00 19.76 1205 N LEU B 149-33.060 67. 134-2. 310 1.00 18.21 1206 CA LEU B 149-34. 369 67. 772-2. 336 1.00 18.62 1207 CB LEU B 149-34.971 67.792-0. 929 1.00 19.78 1208 CG LEU B 149-35.126 66.455-0. 202 1.00 21.45 1209 CD1 LEU B 149-35.463 66.705 1.270 1.00 20.36 1210 CD2 LEU B 149-36.210 65.631-0. 880 1.00 22.43 1211 C LEU B 149-34.222 69.212-2. 814 1.00 19.85 1212 O LEU B 149-33.249 69.882-2. 467 1.00 19.01 1213 N ILE B 150-35.183 69. 685-3. 606 1.00 19.26 1214 CA ILE B 150-35.164 71.065-4. 083 1.00 21.05 1215 CB ILE B 150-34.931 71.145-5. 612 1.00 21.41 1216 CG2 ILE B 150-33.544 70.594-5. 951 1.00 19. 39 1217 CG1 ILE B 150-36.007 70. 361-6. 364 1.00 22. 30 1218 CD1 ILE B 150-35. 902 70. 498-7.873 1.00 23.93 2 3 4 5 6 7 8 9 10 1219 C ILE B 150-36.504 71.702-3. 721 1.00 21.48 1220 O ILE B 150-37.497 70.997-3. 556 1.00 21.95 1221 N ALA B 151-36.528 73.021-3. 567 1. 00 21. 35 1222 CA ALA B 151-37. 758 73.718-3. 194 1.00 25.13 1223 CB ALA B 151-37.476 75.201-2. 990 1.00 22.77 1224 C ALA B 151-38.903 73.546-4. 198 1.00 28. 21 1225 O ALA B 151-38.695 73.567-5. 411 1.00 25.50 1226 N ASP B 152-40.112 73.385-3. 666 1.00 31.02 1227 CA ASP B 152-41. 320 73.220-4. 474 1.00 35.51 1228 CB ASP B 152-42.231 72.170-3. 824 1.00 37. 65, 1229 CG ASP B 152-43.515 71.933-4. 607 1.00 41.12 1230 OD1 ASP B 152-44.355 71.140-4. 128 1.00 43.68 1231 OD2 ASP B 152-43.684 72.529-5. 694 1.00 41. 62 1232 C ASP B 152-42.044 74.566-4. 545 1.00 36.80 1233 O ASP B 152-42.694 74.980-3. 586 1.00 36.70 1234 N SER B 153-41.930 75.252-5. 676 1.00 39.00 1235 CA SER B 153-42.569 76.557-5. 822 1.00 41. 52 1236 CB SER B 153-42.036 77.270-7. 070 1.00 40.74 1237 OG SER B 153-42.147 76.455-8. 223 1.00 41.45 1238 C SER B 153-44.099 76.526-5. 856 1. 00 43.61 1239 O SER B 153-44.745 77.546-5. 614 1.00 43.67 1240 N GLU B 154-44.681 75.366-6. 144 1.00 46.03 1241 CA GLU B 154-46.137 75.256-6. 194 1.00 48.51 1242 CB GLU B 154-46.560 74.145-7. 158 1.00 50.89 1243 CG GLU B 154-46.571 74.572-8. 621 1.00 56.71 1244 CD GLU B 154-47.266 75.909-8. 829 1.00 59.55 1245 OE1 GLU B 154-46.719 76. 939-8. 381 1.00 61.64 1246 OE2 GLU B 154-48.359 75.931-9. 430 1.00 61.49 1247 C GLU B 154-46.786 75.017-4. 835 1.00 48.26 1248 O GLU B 154-47.978 74. 708-4. 754 1.00 48. 08 1249 N THR B 155-46.013 75.180-3. 767 1. 00 47. 37 1250 CA THR B 155-46.535 74.957-2. 426 1.00 47.19 1251 CB THR B 155-46.096 73. 580-1.896 1.00 47. 49 1 2 3 4 5 6 7 8 9 10 1252 OG1 THR B 155-46.583 72.556-2. 772 1.00 49.11 1253 CG2 THR B 155-46.643 73.347-0. 494 1.00 48.30 1254 C THR B 155-46. 097 76.024-1. 431 1. 00 46.68 1255 O THR B 155-44.967 76.510-1. 483 1.00 47.18 1256 N PRO B 156-46. 998 76.412-0. 514 1.00 45.92 1257 CD PRO B 156-48.438 76.106-0. 496 1.00 46.59 1258 CA PRO B 156-46.675 77.428 0.493 1. 00 45.03 1259 CB PRO B 156-48.037 77.761 1.104 1.00 46.13 1260 CG PRO B 156-49.014 77. 393 0.018 1. 00 47.26 1261 C PRO B 156-45.725 76.834 1.528 1.00 43.21 1262 O PRO B 156-45.656 75.614 1.682 1.00 40.95 1263 N THR B 157-44.992 77.691 2.229 1.00 42.85 1264 CA THR B 157-44.064 77.223 3.251 1.00 42.50 1265 CB THR B 157-43.185 78.367 3.786 1.00 41.60 1266 OG1 THR B 157-44.016 79. 367 4.386 1.00 43.87 1267 CG2 THR B 157-42. 371 78.989 2.657 1.00 40.95 1268 C THR B 157-44.856 76.638 4.412 1.00 42.78 1269 O THR B 157-46.015 76.997 4.625 1.00 42.97 1270 N ILE B 158-44.227 75.740 5.162 1.00 42.06 1271 CA ILE B 158-44.874 75.102 6.300 1.00 42.30 1272 CB ILE B 158-44.454 73.624 6.393 1.00 41.90 1273 CG2 ILE B 158-45.116 72.960 7.588 1.00 41.84 1274 CG1 ILE B 158-44.841 72.907 5.099 1. 00 41.68 1275 CD1 ILE B 158-44. 274 71.509 4. 973 1.00 42.66 1276 C ILE B 158-44.519 75.822 7.599 1.00 43.51 1277 O ILE B 158-43. 347 75.924 7.961 1.00 43.05 1278 N GLN B 159-45.538 76.331 8.288 1.00 43. 69 1279 CA GLN B 159 -45.345 77. 047 9.545 1.00 44. 70 1280 CB GLN B 159-46.298 78.241 9.630 1.00 44.60 1281 CG GLN B 159-46.102 79.277 8.538 1.00 45.92 1282 CD GLN B 159-44. 717 79.895 8.555 1.00 45.81 1283 OEIL GLN B 159-44. 300 80.492 9.551 1.00 44.76 1284 NE2 GLN B 159-43. 998 79. 758 7.449 1.00 45. 28 1 2 3 4 5 6 7 8 9 10 1285 C GLN B 159-45.597 76.116 10.721 1.00 45.65 1286 O GLN B 159-46.720 75.662 10.932 1.00 46. 38 1287 N LYS B 160-44. 553 75.837 11.490 1.00 45.99 1288 CA LYS B 160-44.686 74.946 12.632 1.00 46.92 1289 CB LYS B 160-44.474 73.501 12.180 1.00 47.36 1290 CG LYS B 160-44.683 72.466 13.265 1.00 49.69 1291 CD LYS B 160-44.579 71.060 12.702 1.00 50.71 1292 CE LYS B 160-44.868 70.019 13.772 1.00 52.51 1293 NZ LYS B 160-44.872 68.637 13.218 1.00 53.38 1294 C LYS B 160-43.705 75.295 13.746 1.00 47.37 1295 O LYS B 160-42.522 75.525 13.497 1.00 46. 88 1296 N GLY B 161-44.215 75. 343 14.974 1.00 47.11 1297 CA GLY B 161-43.381 75.650 16.123 1.00 46.59 1298 C GLY B 161-42.632 76.965 16.046 1.00 46.40 1299 O GLY B 161-41.526 77.078 16.577 1.00 46.97 1300 N SER B 162-43.230 77.958 15. 393 1.00 45. 90 1301 CA SER B 162-42.618 79.278 15.245 1.00 46.37 1302 CB SER B 162-42.133 79.792 16.605 1.00 48. 02 1303 OG SER B 162 -41.590 81.095 16.493 1.00 50.92 1304 C SER B 162 -41.457 79.269 14.247 1.00 44.76 1305 0 SER B 162-40.700 80.234 14.147 1.00 44.37 1306 N TYR B 163-41.324 78.168 13.515 1. 00 43. 46 1307 CA TYR B 163-40.278 78.016 12.507 1.00 42. 01 1308 CB TYR B 163-39.481 76.730 12.743 1.00 44.55 1309 CG TYR B 163-38.414 76.816 13.811 1.00 49.51 1310 CDI TYR B 163-38.690 77.362 15.065 1.00 51.60 1311 CE1 TYR B 163-37.714 77.408 16.062 1.00 53.82 1312 CD2 TYR B 163-37.133 76. 319 13.577 1. 00 50.68 1313 CE2 TYR B 163-36.152 76. 359 14.564 1.00 52.94 1314 CZ TYR B 163-36.448 76.904 15.803 1.00 54.07 1315 OH TYR B 163-35.480 76.941 16.783 1.00 56.46 1316 C TYR B 163-40.915 77.938 11. 128 1.00 39.32 1317 O TYR B 163-42.101 77. 635 10.999 1.00 37. 90 1 2 3 4 5 6 7 8 9 10 1318 N THR B 164-40.121 78.211 10. 100 1. 00 35. 83 1319 CA THR B 164-40.596 78.134 8. 727 1.00 32.83 1320 CB THR B 164-40. 288 79.426 7. 936 1.00 33.40 1321 OG1 THR B 164-41.012 80.526 8.503 1.00 32.18 1322 CG2 THR B 164-40.688 79.262 6.479 1.00 32.06 1323 C THR B 164-39.877 76.968 8.056 1.00 31.60 1324 O THR B 164-38.649 76.860 8.131 1.00 29.16 1325 N PHE B 165-40. 643 76.087 7.421 1.00 29.92 1326 CA PHE B 165-40.067 74.945 6.731 1.00 29. 89 1327 CB PHE B 165-40.615 73.625 7.293 1.00 29.64 1328 CG PHE B 165-40.163 73.327 8.695 1.00 29.88 1329 CDI PHE B 165-40.853 73.841 9.789 1.00 29.84 1330 CD2 PHE B 165-39.011 72.578 8.922 1.00 28. 69 1331 CE1 PHE B 165-40.409 73.605 11.088 1. 00 29.20 1332 CE2 PHE B 165-38.559 72. 337 10.218 1.00 29. 30 1333 CZ PHE B 165-39.258 72.858 11. 303 1.00 29.28 1334 C PHE B 165-40. 319 75.001 5.232 1.00 30.02 1335 O PHE B 165-41.455 75.140 4.779 1.00 29.65 1336 N VAL B 166-39.241 74.900 4.466 1.00 29.46 1337 CA VAL B 166-39.324 74.911 3.016 1.00 27. 74 1338 CB VAL B 166-37.914 74.904 2. 367 1.00 27.63 1339 CG1 VAL B 166-38.036 74.802 0.854 1. 00 26. 82 1340 CG2 VAL B 166-37.145 76.152 2.759 1.00 27.06 1341 C VAL B 166-40.034 73.645 2.559 1.00 27.87 1342 O VAL B 166-39.719 72.547 3.027 1.00 28.16 1343 N PRO B 167-41.018 73.779 1.658 1.00 27.62 1344 CD PRO B 167-41.655 75.005 1.144 1.00 28.01 1345 CA PRO B 167-41.711 72.579 1.183 1.00 27.61 1346 CB PRO B 167-42. 984 73.144 0.553 1.00 28.59 1347 CG PRO B 167-42.533 74.473 0.023 1.00 29. 41 1348 C PRO B 167-40.768 71.949 0.161 1.00 27.73 1349 O PRO B 167-40.364 72.610-0. 795 1.00 28.12 1350 N TRP B 168-40.401 70.688 0.363 1.00 27. 32 2 3 4 5 6 7 8 9 10 1351 CA TRP B 168-39.467 70.031-0. 542 1.00 27. 39 1352 CB TRP B 168-38.490 69.147 0.243 1.00 25.19 1353 CG TRP B 168-37.608 69.899 1.194 1.00 24.27 1354 CD2 TRP B 168-36.678 70.941 0.866 1.00 22.19 1355 CE2 TRP B 168-36.064 71.348 2.073 1.00 22.86 1356 CE3 TRP B 168-36.288 71.557-0. 331 1.00 20. 84 1357 CDI TRP B 168-37. 531 69.729 2.548 1.00 23.96 1358 NE1 TRP B 168-36.608 70.599 3.084 1.00 24.61 1359 CZ2 TRP B 168-35.099 72.364 2.120 1.00 22.39 1360 CZ3 TRP B 168-35. 327 72.566-0. 286 1.00 21.22 1361 CH2 TRP B 168-34. 738 72.951 0.934 1. 00 20.32 1362 C TRP B 168-40.087 69.190-1. 644 1.00 29.56 1363 O TRP B 168-41.214 68.706-1. 532 1.00 30.60 1364 N LEU B 169-39.311 69.026-2. 708 1.00 29.12 1365 CA LEU B 169-39. 680 68.231-3. 865 1.00 30.07 1366 CB LEU B 169-39.852 69.150-5. 079 1.00 33.73 1367 CG LEU B 169-40.599 68.673-6. 321 1. 00 38.99 1368 CD1 LEU B 169-40.813 69.860-7. 257 1.00 41.32 1369 CD2 LEU B 169-39.820 67. 571-7. 016 1.00 41.13 1370 C LEU B 169-38.464 67. 317-4. 040 1.00 29.53 1371 O LEU B 169-37.324 67.776-3. 929 1.00 29.10 1372 N LEU B 170-38.687 66. 031-4. 285 1.00 26. 97 1373 CA LEU B 170-37.568 65.113-4. 455 1.00 27.29 1374 CB LEU B 170-38.052 63. 664-4. 389 1.00 30.62 1375 CG LEU B 170-36. 970 62.584-4. 530 1.00 31. 90 1376 CD1 LEU B 170-36.050 62.598-3. 317 1.00 30. 68 1377 CD2 LEU B 170-37.629 61.222-4. 679 1.00 34.11 1378 C LEU B 170-36. 856 65. 350-5. 786 1.00 28.25 1379 O LEU B 170-37. 482 65. 319-6. 844 1.00 28.28 1380 N SER B 171-35.548 65.597-5. 727 1.00 25. 57 1381 CA SER B 171-34.754 65.819-6. 933 1.00 24.40 1382 CB SER B 171-33. 486 66. 619-6.596 1.00 24.06 1383 OG SER B 171-32.611 66. 697-7. 705 1. 00 21.12 2 3 4 5 6 7 8 9 10 1384 C SER B 171-34. 386 64.443-7. 477 1.00 24.05 1385 O SER B 171-34.586 64.148-8. 655 1.00 23.87 1386 N PHE B 172-33.851 63.601-6. 599 1.00 23.65 1387 CA PHE B 172-33.479 62.242-6. 958 1.00 24.81 1388 CB PHE B 172-32.285 62.241-7. 924 1.00 24.43 1389 CG PHE B 172-30.957 62.451-7. 250 1.00 25.12 1390 CD1 PHE B 172-30.268 61.376-6. 686 1.00 24.66 1391 CD2 PHE B 172-30.402 63.723-7. 161 1.00 24.04 1392 CE1 PHE B 172-29.047 61.571-6. 033 1.00 25.55 1393 CE2 PHE B 172-29.182 63.929-6. 511 1.00 24.33 1394 CZ PHE B 172-28.504 62.851-5. 950 1.00 24.16 1395 C PHE B 172-33.118 61.458-5. 702 1.00 25.98 1396 0 PHE B 172-32.823 62.036-4. 653 1.00 23.47 1397 N LYS B 173-33.142 60.137-5. 832 1.00 26. 13 1398 CA LYS B 173-32.801 59.224-4. 753 1.00 28. 37 1399 CB LYS B 173-34.075 58. 630-4.134 1.00 30.07 1400 CG LYS B 173-33.856 57.435-3. 204 1.00 31.27 1401 CD LYS B 173-35.190 56.958-2. 626 1.00 35.27 1402 CE LYS B 173-35. 145 55.498-2. 181 1.00 37.02 1403 NZ LYS B 173-34.196 55.251-1. 059 1. 00 39. 77 1404 C LYS B 173-31.958 58.120-5. 379 1.00 28.65 1405 0 LYS B 173-32. 377 57.496-6. 352 1.00 27.39 1406 N ARG B 174-30.763 57.893-4. 844 1.00 27.47 1407 CA ARG B 174-29.912 56.842-5. 378 1.00 29.19 1408 CB ARG B 174-28.667 57.428-6. 056 1.00 29.89 1409 CG ARG B 174-27.882 56.378-6. 820 1.00 34.00 1410 CD ARG B 174-26.745 56.953-7. 656 1.00 36.67 1411 NE ARG B 174-25.581 57.292-6. 852 1.00 38.12 1412 CZ ARG B 174-24.329 56.993-7. 186 1.00 37.73 1413 NH1 ARG B 174-24.072 56.342-8. 312 1.00 35.57 1414 NH2 ARG B 174-23.330 57. 346-6. 390 1.00 39.03 1415 C ARG B 174-29.500 55.899-4. 259 1. 00 29.12 1416 0ARG B 174-28.936 56.325-3. 253 1. 00 27. 17 1 2 3 4 5 6 7 8 9 10 1417 N GLY B 175-29.787 54.614-4. 436 1.00 29. 31 1418 CA GLY B 175-29.442 53.644-3. 414 1.00 30.41 1419 C GLY B 175-30. 583 53.496-2. 427 1.00 31.22 1420 O GLY B 175-31.688 53.978-2. 673 1.00 32.83 1421 N SER B 176-30.321 52.851-1. 298 1.00 32.75 1422 CA SER B 176-31.370 52.638-0. 306 1.00 33.59 1423 CB SER B 176-31.636 51.138-0. 175 1.00 35.19 1424 OG SER B 176-30.437 50.445 0.142 1.00 38.23 1425 C SER B 176-31.090 53.226 1.078 1.00 32.08 1426 O SER B 176-31.980 53.257 1.930 1.00 32.47 1427 N ALA B 177-29.867 53.698 1.297 1.00 31. 20 1428 CA ALA B 177-29.481 54.262 2.591 1.00 28.60 1429 CB ALA B 177-27.989 54.576 2.595 1.00 30.48 1430 C ALA B 177-30.265 55.498 3.032 1.00 26.75 1431 O ALA B 177-30. 369 55.770 4.229 1. 00 26.53 1432 N LEU B 178-30.816 56.241 2.078 1. 00 24.59 1433 CA LEU B 178-31.565 57.456 2. 399 1.00 25.00 1434 CB LEU B 178-30.730 58.689 2.021 1.00 22.67 1435 CG LEU B 178-29.375 58.873 2.716 1.00 22. 15 1436 CD1 LEU B 178-28.488 59.808 1.901 1.00 22.73 1437 CD2 LEU B 178-29.594 59.417 4.118 1. 00 21. 79 1438 C LEU B 178-32.914 57.523 1.680 1. 00 25.44 1439 O LEU B 178-33.018 57.138 0.519 1.00 27.84 1440 N GLU B 179-33.935 58.022 2. 372 1.00 25.84 1441 CA GLU B 179-35.278 58. 160 1.802 1.00 29.02 1442 CB GLU B 179-36.212 57.040 2.290 1. 00 29. 28 1443 CG GLU B 179-35.675 55.627 2.157 1.00 32.70 1444 CD GLU B 179-36.693 54.577 2.598 1.00 36.09 1445 OE1 GLU B 179-37. 617 54.925 3.368 1.00 35.18 1446 OE2 GLU B 179-36.564 53.404 2.186 1.00 35.93 1447 C GLU B 179-35.872 59.487 2.256 1.00 29. 37 1448 O GLU B 179-35.367 60.110 3.184 1.00 30. 16 1449 N GLU B 180-36.940 59.922 1.595 1.00 29.15 1 2 3 4 5 6 7 8 9 10 1450 CA GLU B 180-37.614 61.149 1.989 1.00 31.11 1451 CB GLU B 180-38.036 61.977 0. 773 1.00 32.56 1452 CG GLU B 180-39.017 63.093 1. 125 1.00 35. 58 1453 CD GLU B 180-39.592 63.791-0. 095 1.00 38.50 1454 OBI GLU B 180-39.872 63.106-1. 101 1.00 40. 94 1455 OE2 GLU B 180-39. 782 65.023-0. 042 1.00 40.90 1456 C GLU B 180-38. 855 60.729 2. 769 1.00 32.46 1457 O GLU B 180-39.567 59.812 2.361 1.00 32.28 1458 N LYS B 181-39.105 61.389 3.893 1.00 32.25 1459 CA LYS B 181-40.262 61.065 4.718 1.00 33.66 1460 CB LYS B 181-39.895 60.006 5.763 1.00 35.62 1461 CG LYS B 181-41.035 59.646 6.709 1.00 37.47 1462 CD LYS B 181-40.614 58.566 7.698 1.00 41.03 1463 CE LYS B 181-41.767 58.158 8.610 1.00 41.96 1464 NZ LYS B 181-41.386 57.025 9.504 1.00 43. 93 1465 C LYS B 181-40.796 62.298 5.418 1.00 33.33 1466 O LYS B 181-40.092 62.931 6.208 1.00 33.46 1467 N GLU B 182-42.041 62.641 5.113 1.00 33.19 1468 CA GLU B 182-42.697 63.793 5. 715 1.00 34. 29 1469 CB GLU B 182-43.083 63.461 7.161 1.00 38.47 1470 CG GLU B 182-44.094 62. 319 7.269 1.00 43.56 1471 CD GLU B 182-44.169 61.714 8.664 1.00 47. 35 1472 OE1 GLU B 182-45.058 60.862 8.891 1.00 48.61 1473 OE2 GLU B 182-43. 339 62.081 9.528 1.00 47.50 1474 C GLU B 182 -41.847 65.064 5.668 1.00 32.49 1475 O GLU B 182 -41.610 65.705 6.693 1.00 30.99 1476 N ASN B 183-41.400 65.416 4.463 1.00 30.55 1477 CA ASN B 183-40.591 66.613 4.228 1.00 27.72 1478 CB ASN B 183-41.365 67.864 4.655 1.00 26.59 1479 CG ASN B 183-40.955 69. 101 3.868 1.00 27. 97 1480 OD1 ASN B 183-40.733 70.176 4.434 1.00 28. 96 1481 ND2 ASN B 183-40.869 68.955 2.552 1.00 27.01 1482 C ASN B 183-39.233 66. 597 4. 931 1. 00 26. 47 1 2 3 4 5 6 7 8 9 10 1483 O ASN B 183-38.646 67.651 5.181 1.00 27.18 1484 N LYS B 184-38.735 65.404 5.240 1.00 25.86 1485 CA LYS B 184-37.444 65.249 5.904 1.00 24.56 1486 CB LYS B 184-37.643 64.916 7.386 1.00 26.48 1487 CG LYS B 184-38. 374 65.990 8.178 1. 00 29. 19 1488 CD LYS B 184-38.520 65.598 9.641 1.00 32.17 1489 CE LYS B 184-39.586 64.532 9.836 1.00 34.01 1490 NZ LYS B 184-40.931 65.034 9.449 1.00 38.00 1491 C LYS B 184-36.666 64.118 5.248 1.00 24.46 1492 O LYS B 184-37.220 63. 351 4.465 1.00 22.65 1493 N ILE B 185-35. 381 64.016 5.574 1.00 22.92 1494 CA ILE B 185-34.543 62.958 5.034 1.00 23. 24 1495 CB ILE B 185-33. 138 63.487 4.652 1.00 23.04 1496 CG2 ILE B 185-32.258 62. 344 4.160 1. 00 23.61 1497 CG1 ILE B 185-33.272 64.562 3.566 1.00 23. 34 1498 CD1 ILE B 185-31.950 65.153 3.101 1.00 24.85 1499 C ILE B 185-34.415 61.873 6.102 1.00 25. 68 1500 O ILE B 185-34. 006 62.146 7.231 1.00 24.87 1501 N LEU B 186-34.777 60.646 5.733 1.00 25.44 1502 CA LEU B 186-34. 732 59.501 6.639 1.00 25. 55 1503 CB LEU B 186-36.009 58.661 6.477 1.00 25.93 1504 CG LEU B 186-36.090 57.354 7.276 1.00 27.82 1505 CD1 LEU B 186-36.064 57.661 8.772 1.00 26.97 1506 CD2 LEU B 186-37. 373 56.601 6.902 1.00 28.08 1507 C LEU B 186-33.512 58.618 6.402 1.00 23.45 1508 O LEU B 186-33.246 58.196 5.278 1.00 22. 35 1509 N VAL B 187-32.777 58. 337 7.473 1. 00 22.16 1510 CA VAL B 187-31.587 57.497 7.397 1. 00 24.13 1511 CB VAL B 187-30.563 57.899 8. 477 1.00 22.78 1512 CG1 VAL B 187-29. 362 56.965 8.432 1. 00 24.01 1513 CG2 VAL B 187-30.131 59.343 8@ 263 1.00 23.99 1514 C VAL B 187-31. 973 56.033 7.601 1.00 25.51 1515 O VAL B 187-32. 582 55.686 8. 612 1.00 25.20 1 2 3 4 5 6 7 8 9 10 1516 N LYS B 188'-31. 606 55.182 6.644 1. 00 26.00 1517 CA LYS B 188-31.928 53.758 6.702 1.00 27.67 1518 CB LYS B 188-32. 457 53.280 5.343 1.00 27.54 1519 CG LYS B 188-33.650 54. 064 4.817 1.00 28.07 1520 CD LYS B 188-34.883 53.885 5.693 1.00 30.03 1521 CE LYS B 188-35.406 52.450 5.630 1.00 34. 00 1522 NZ LYS B 188-36.611 52.262 6.492 1.00 36. 42 1523 C LYS B 188-30.725 52.907 7.090 1.00 29.28 1524 O LYS B 188 -30.869 51-737 7.442 1.00 29.66 1525 N GLU B 189 -29.538 53.495 7.016 1.00 29.49 1526 CA GLU B 189-28. 313 52.781 7.351 1.00 30.35 1527 CB GLU B 189-27.600 52.326 6.076 1. 00 31. 78 1528 CG GLU B 189-28.327 51.242 5.299 1.00 37.97 1529 CD GLU B 189-27.781 51.063 3.891 1.00 41.08 1530 OEIL GLU B 189-26. 544 51.129 3.716 1. 00 43.41 1531 OE2 GLU B 189-28.588 50.848 2.960 1.00 42.59 1532 C GLU B 189-27. 382 53.670 8.163 1.00 29.61 1533 O GLU B 189-27. 172 54.836 7. 828 1.00 29.07 1534 N THR B 190-26.830 53.112 9.234 1.00 27. 79 1535 CA THR B 190-25.911 53.851 10.082 1.00 27.10 1536 CB THR B 190-25.597 53.061 11. 366 1.00 28.82 1537 OG1 THR B 190-26. 799 52.904 12.128 1.00 28. 76 1538 CG2 THR B 190-24.549 53.791 12.213 1.00 28. 86 1539 C THR B 190-24.619 54.090 9. 304 1.00 27.06 1540 O THR B 190-24.180 53.228 8.540 1.00 24.82 1541 N GLY B 191-24. 023 55.266 9.489 1.00 25.80 1542 CA GLY B 191-22.786 55.575 8.795 1.00 25.54 1543 C GLY B 191-22. 396 57.039 8.872 1.00 24.58 1544 O GLY B 191-22.926 57.789 9.689 1. 00 25.06 1545 N TYR B 192-21.457 57.436 8.018 1.00 24.97 1546 CA TYR B 192-20.971 58.815 7.952 1.00 25.51 1547 CB TYR B 192-19.451 58.826 7.796 1.00 28.94 1548 CG TYR B 192-18. 699 58.379 9.026 1. 00 34.28 1 2 3 4 5 6 7 8 9 10 1549 CD1 TYR B 192-18.199 59. 309 9.937 1.00 37.68 1550 CE1 TYR B 192-17.510 58.900 11.079 1.00 39.74 1551 CD2 TYR B 192-18. 495 57.024 9.287 1.00 36.16 1552 CE2 TYR B 192-17.810 56.605 10.425 1.00 38.75 1553 CZ TYR B 192-17. 320 57.548 11.315 1.00 40.13 1554 OH TYR B 192-16.636 57.138 12.436 1.00 43.63 1555 C TYR B 192-21. 613. 59.473 6.737 1.00 23.27 1556 O TYR B 192-21.623 58.889 5.657 1.00 22.94 1557 N PHE B 193-22.136 60. 684 6.910 1.00 20.80 1558 CA PHE B 193-22. 806 61.383 5.818 1.00 20.67 1559 CB PHE B 193-24.328 61. 394 6.044 1.00 19.46 1560 CG PHE B 193-24.959 60.028 6.078 1.00 21.92 1561 CD1 PHE B 193-24.851 59.216 7.209 1.00 21.01 1562 CD2 PHE B 193-25.684 59.561 4.983 1.00 19.95 1563 CE1 PHE B 193-25.462 57.955 7.247 1.00 19.96 1564 CE2 PHE B 193-26.298 58.304 5.012 1.00 21.99 1565 CZ PHE B 193-26.186 57. 504 6. 147 1.00 19.85 1566 C PHE B 193-22.378 62.829 5.593 1.00 19.92 1567 O PHE B 193-22.209 63.598 6.545 1.00 18.58 1568 N PHE B 194-22.217 63.192 4. 324 1.00 19.24 1569 CA PHE B 194-21.897 64.566 3.951 1.00 19.10 1570 CB PHE B 194-21.114 64.612 2.638 1.00 20.11 1571 CG PHE B 194-20.932 65.999 2.092 1.00 21.19 1572 CD1 PHE B 194-20.124 66.918 2.751 1.00 21.67 1573 CD2 PHE B 194-21.599 66.398 0.938 1.00 21.53 1574 CE1 PHE B 194-19.976 68.216 2.265 1.00 22.11 1575 CE2 PHE B 194-21.458 67.697 0.442 1.00 23.44 1576 CZ PHE B 194-20.648 68.606 1.111 1.00 21.91 1577 C PHE B 194-23.287 65.180 3.759 1.00 19. 27 1578 O PHE B 194-24.103 64.655 3.000 1.00 19.14 1579 N ILE B 195-23.562 66.272 4.461 1. 00 17.40 1580 CA ILE B 195-24.866 66.929 4.401 1.00 18.32 1581 CB ILE B 195-25.544 66. 895 5.784 1.00 19.26 123 4 56 7 8 9 10 1582 CG2 ILE B 195-26.950 67. 487 5. 701 1.00 20.00 1583 CG1 ILE B 195 -25.590 65.453 6.297 1.00 19.42 1584 CDI ILE B 195 -25.828 65-364 7.801 1.00 23.49 1585 C ILE B 195-24. 696 68.383 3.982 1.00 18.55 1586 O ILE B 195-23.774 69.056 4.445 1.00 16.82 1587 N TYR B 196-25.589 68. 870 3.122 1.00 16.41 1588 CA TYR B 196-25.497 70.246 2.638 1.00 16.48 1589 CB TYR B 196-24.733 70.281 1.307 1.00 15.31 1590 CG TYR B 196-25. 382 69.481 0.191 1.00 16.88 1591 CD 1 TYR B 196-26.294 70.072-0. 695 1.00 17.96 1592 CE1 TYR B 196-26.917 69. 320-1. 700 1.00 19.51 1593 CD2 TYR B 196-25. 111 68.124 0.045 1.00 16.67 1594 CE2 TYR B 196-25.730 67.363-0. 948 1.00 19.22 1595 CZ TYR B 196-26.630 67.965-1. 814 1.00 18.58 1596 OH TYR B 196-27.247 67.201-2. 777 1.00 21.82 1597 C TYR B 196-26.862 70.899 2.462 1. 00 18.04 1598 O TYR B 196-27.858 70.221 2.227 1.00 18. 28 1599 N GLY B 197-26.896 72.223 2.578 1.00 17.96 1600 CA GLY B 197-28. 144 72.946 2.427 1.00 17.18 1601 C GLY B 197-27.953 74.410 2.080 1.00 17.78 1602 O GLY B 197-27.008 75.055 2.538 1.00 18.71 1603 N GLN B 198-28.852 74.939 1.258 1.00 17.17 1604 CA GLN B 198-28.786 76. 335 0.867 1.00 16.79 1605 CB GLN B 198-28.082 76.487-0. 483 1.00 15.86 1606 CG GLN B 198-28.009 77.931-0. 969 1.00 16. 18 1607 CD GLN B 198-27.289 78.066-2. 300 1.00 17.74 1608 OE1 GLN B 198-26.106 77.752-2. 408 1.00 19.65 1609 NE2 GLN B 198-28.004 78.532-3. 320 1.00 17.26 1610 C GLN B 198-30.181 76.926 0.767 1.00 17.71 1611 O GLN B 198-31.121 76.252 0.355 1.00 17.18 1612 N VAL B 199-30.301 78.194 1.146 1.00 17.61 1613 CA VAL B 199-31.570 78.904 1.081 1.00 17.42 1614 CB VAL B 199-32.265 78.953 2.470 1.00 18. 18 2 3 4 5 6 7 8 9 10 1615 CG1 VAL B 199-33. 560 79.763 2. 377 1.00 18.47 1616 CG2 VAL B 199-32.555 77. 527 2.965 1.00 15.51 1617 C VAL B 199-31. 311 80.335 0.620 1.00 19. 33 1618 O VAL B 199-30.290 80.926 0.978 1.00 19.16 1619 N LEU B 200-32.218 80.880-0. 187 1.00 20.21 1620 CA LEU B 200-32.096 82.262-0. 647 1.00 20.18 1621 CB LEU B 200-32.413 82. 391-2. 143 1.00 19.02 1622 CG LEU B 200-32.621 83.834-2. 653 1.00 19.94 1623 CD1 LEU B 200-31.441 84. 706-2.256 1.00 20.84 1624 CD2 LEU B 200-32.806 83.842-4. 170 1.00 19.12 1625 C LEU B 200-33.075 83.113 0.153 1.00 23. 10 1626 O LEU B 200-34.289 82.917 0.063 1.00 22. 38 1627 N TYR B 201-32.539 84.045 0.938 1.00 24.91 1628 CA TYR B 201-33.349 84.930 1.760 1.00 29.79 1629 CB TYR B 201-32.670 85. 173 3.111 1.00 29. 26 1630 CG TYR B 201-32.482 83.903 3.904 1.00 30.54 1631 CD1 TYR B 201-31.297 83.168 3.818 1.00 30. 13 1632 CE1 TYR B 201-31.155 81.951 4.484 1.00 29.04 1633 CD2 TYR B 201-33.520 83.392 4.683 1.00 29.35 1634 CE2 TYR B 201-33.390 82.179 5. 349 1.00 29.81 1635 CZ TYR B 201-32.207 81.461 5.243 1.00 30.42 1636 OH TYR B 201-32.092 80.241 5.871 1.00 33.09 1637 C TYR B 201-33.614 86.261 1.076 1.00 32.62 1638 O TYR B 201-32. 713 86.871 0.493 1.00 31.86 1639 N THR B 202-34.866 86.699 1.157 1.00 35.54 1640 CA THR B 202-35.294 87.956 0.565 1.00 38.93 1641 CB THR B 202-36.262 87.700-0. 611 1. 00 38. 24 1642 OG1 THR B 202-37. 387 86.941-0. 154 1.00 36.09 1643 CG2 THR B 202-35.562 86.909-1. 715 1.00 37.56 1644 C THR B 202-35.992 88.806 1.624 1.00 42. 67 1645 0 THR B 202-36.794 89.683 1.307 1.00 43. 92 1646 N ASP B 203-35.576 88.500 2.703 1.00 42.05 1647 CA ASP B 203-36.183 89.180 3.839 1.00 45.38 1 2 3 4 5 6 7 8 9 10 1648 CB ASP B 203-36. 346 88. 176 4. 979 1. 00 47. 42 1649 CG ASP B 203-37.468 88.542 5.917 1.00 50.00 1650 OD1 ASP B 203-37. 470 89.685 6.421 1. 00 50.72 1651 OD2 ASP B 203-38. 344 87.681 6.155 1.00 50.23 1652 C ASP B 203-35.337 90.369 4.305 1.00 46.58 1653 O ASP B 203-34.109 90.323 4.255 1.00 45.54 1654 N LYS B 204-36.471 93.649 5.373 1.00 48. 95 1655 CA LYS B 204-35.218 92.892 5. 375 1.00 50.93 1656 CB LYS B 204-34. 573 92.932 3. 987 1.00 53. 36 1657 CG LYS B 204-35.379 92.231 2.912 1.00 57.00 1658 CD LYS B 204-34.614 92.170 1.605 1.00 59.51 1659 CE LYS B 204 -35.423 91-459 0.534 1.00 60.51 1660 NZ LYS B 204 -34.675 91.368 -0.751 1.00 61.90 1661 C LYS B 204-34.179 93.318 6.411 1.00 50.88 1662 O LYS B 204-33.126 92.690 6.518 1.00 50.86 1663 N THR B 205-34. 459 94.374 7.169 1. 00 52.00 1664 CA THR B 205-33.512 94.832 8.187 1.00 53.41 1665 CB THR B 205-34. 055 96. 034 8.973 1.00 54.12 1666 OG1 THR B 205-34.149 97.162 8.101 1.00 54.92 1667 CG2 THR B 205-33.124 96.386 10.131 1.00 55.02 1668 C THR B 205-33.196 93.711 9.167 1.00 53.22 1669 O THR B 205-34.056 92.887 9.479 1.00 54.37 1670 N TYR B 206-31.961 93.695 9.657 1.00 51.90 1671 CA TYR B 206-31.516 92.659 10.580 1.00 51.49 1672 CB. TYR B 206-30.104 92.988 11.094 1.00 55.44 1673 CG TYR B 206-30.033 94.092 12.132 1.00 59.99 1674 CD1 TYR B 206-30. 205 93.812 13.485 1.00 61.39 1675 CE1 TYR B 206-30.138 94.819 14.446 1.00 63.23 1676 CD2 TYR B 206-29.788 95. 416 11.761 1.00 61.56 1677 CE2 TYR B 206-29.719 96.432 12.718 1.00 63.07 1678 CZ TYR B 206-29.896 96.124 14.058 1.00 63.66 1679 OH TYR B 206-29.840 97.111 15.013 1.00 65.15 1680 C TYR B 206-32.475 92.406 11.748 1.00 48. 02 1 2 3 4 5 6 7 8 9 10 1681 O TYR B 206-32.537 91.288 12.267 1.00 47.09 1682 N ALA B 207-30.839 89.945 10.156 1.00 46.21 1683 CA ALA B 207-30.087 88.708 9.938 1.00 42.61 1684 CB ALA B 207-29.123 88. 461 11.124 1.00 41.73 1685 C ALA B 207-30. 968 87.502 9.706 1.00 40.10 1686 O ALA B 207-31.919 87.278 10.444 1.00 38. 84 1687 N MET B 208-30.629 86.708 8.696 1.00 36.86 1688 CA MET B 208-31.412 85.517 8. 367 1.00 34.95 1689 CB MET B 208-32.156 85.723 7.046 1.00 34.84 1690 CG MET B 208-33.130 86.892 7.040 1.00 38.60 1691 SD MET B 208-34.541 86.621 8.137 1.00 42.51 1692 CE MET B 208-35.515 85.492 7.144 1.00 41.10 1693 C MET B 208-30.511 84.290 8.241 1.00 33. 37 1694 O MET B 208-29. 310 84.416 8.001 1.00 32.57 1695 N GLY B 209-31.091 83.105 8. 394 1.00 30.76 1696 CA GLY B 209-30.303 81.892 8.279 1.00 29.77 1697 C GLY B 209-31.107 80.642 8.561 1.00 28.84 1698 O GLY B 209-32.275 80.723 8.950 1.00 29.00 1699 N HIS B 210-30.488 79.482 8.359 1.00 25.83 1700 CA HIS B 210-31.162 78.219 8.610 1.00 23.73 1701 CB HIS B 210-31.560 77.534 7.294 1.00 23. 37 1702 CG HIS B 210-30.410 77.238 6.381 1.00 23. 58 1703 CD2 HIS B 210-29.711 76.097 6.168 1.00 23. 36 1704 ND1 HIS B 210-29.879 78.177 5.523 1.00 23.90 1705 CE1 HIS B 210-28.909 77.626 4.816 1.00 24. 10 1706 NE2 HIS B 210-28.786 76. 365 5.188 1.00 24.83 1707 C HIS B 210-30. 339 77.255 9.453 1.00 23.60 1708 O HIS B 210-29.133 77.447 9.661 1.00 21.53 1709 N LEU B 211-31.015 76.214 9.928 1.00 22. 59 1710 CA LEU B 211-30.411 75.185 10.755 1.00 22.40 1711 CB LEU B 211-31.074 75.165 12.134 1.00 25. 79 1712 CG LEU B 211-31. 184 76.476 12.910 1. 00 27. 54 1713 CD1 LEU B 211-32.223 76.339 14.014 1. 00 29. 42 1 2 3 4 5 6 7 8 9 10 1714 CD2 LEU B 211-29. 828 76.829 13.483 1.00 28.91 1715 C-LEU B 211-30.630 73.819 10.117 1. 00 23.62 1716 O LEU B 211-31. 741 73.500 9.692 1.00 24.51 1717 N ILE B 212-29.570 73.024 10.030 1.00 21.69 1718 CA ILE B 212-29.687 71.672 9.518 1.00 23.45 1719 CB ILE B 212-28. 476 71.274 8. 651 1.00 24.12 1720 CG2 ILE B 212-28. 506 69.773 8.375 1. 00 26.05 1721 CG1 ILE B 212-28.509 72.067 7.337 1. 00 25.17 1722 CD1 ILE B 212-27.356 71.767 6.388 1.00 27.74 1723 C ILE B 212-29.718 70.875 10.817 1.00 24.69 1724 O ILE B 212-28. 726 70. 827 11.556 1.00 24.42 1725 N GLN B 213-30. 874 70.284 11.108 1.00 23.95 1726 CA GLN B 213-31.071 69.535 12.345 1.00 24.48 1727 CB GLN B 213-32.299 70.085 13.072 1. 00 25.35 1728 CG GLN B 213-32.244 71.587 13. 319 1.00 28.54 1729 CD GLN B 213-33.517 72.122 13.948 1. 00 29.54 1730 OE1 GLN B 213-34. 599 72.010 13.376 1.00 29.63 1731 NE2 GLN B 213-33. 391 72.710 15.134 1.00 31.12 1732 C GLN B 213-31.209 68.022 12.212 1.00 24.49 1733 O GLN B 213-31.709 67.510 11.212 1.00 24.71 1734 N ARG B 214-30.758 67. 323 13.252 1.00 24.01 1735 CA ARG B 214-30.815 65.868 13.330 1.00 23.77 1736 CB ARG B 214-29.455 65. 309 13.755 1. 00 24.22 1737 CG ARG B 214-29.441 63.809 14.016 1.00 24.49 1738 CD ARG B 214-28.197 63.401 14.789 1.00 27. 06 1739 NE ARG B 214-28.122 61.958 14.986 1.00 28. 38 1740 CZ ARG B 214-27.246 61.355 15.786 1.00 30.40 1741 NH1 ARG B 214-26.363 62.073 16.472 1.00 29.46 1742 NH2 ARG B 214-27.253 60.032 15.901 1.00 28. 63 1743 C ARG B 214-31.857 65.467 14. 374 1.00 25.20 1744 O ARG B 214-31.781 65.890 15.529 1.00 24.15 1745 N LYS B 215-32.838 64.670 13.963 1. 00 26. 73 1746 CA LYS B 215-33.868 64.192 14.881 1. 00 28. 74 1 2 3 4 5 6 7 8 9 10 1747 CB LYS B 215-35.237 64.156 14.191 1.00 31.73 1748 CG LYS B 215-36.399 63.748 15.098 1.00 35.41 1749 CD LYS B 215-36.642 64.780 16.191 1.00 39.82 1750 CE LYS B 215-37.824 64.398 17.081 1.00 41.96 1751 NZ LYS B 215-38.089 65.431 18.129 1.00 42.63 1752 C LYS B 215-33.423 62.779 15.242 1.00 29.35 1753 O LYS B 215-33.538 61.861 14.432 1.00 25.47 1754 N LYS B 216-32.901 62.617 16.453 1.00 30.12 1755 CA LYS B 216-32.409 61.325 16.910 1.00 32.83 1756 CB LYS B 216-31.543 61. 508 18.164 1.00 34.51 1757 CG LYS B 216-30.296 62.368 17.940 1.00 37. 80 1758 CD LYS B 216-29. 389 62.393 19.169 1.00 41.99 1759 CE LYS B 216-30.084 63.028 20.366 1.00 45.73 1760 NZ LYS B 216-29.247 62.975 21.606 1.00 48.20 1761 C LYS B 216-33.513 60.315 17.196 1.00 34.27 1762 O LYS B 216-34.545 60.650 17. 778 1.00 33.47 1763 N VAL B 217-33.287 59.073 16.777 1.00 35.50 1764 CA VAL B 217-34.251 58.004 17.010 1.00 38.56 1765 CB VAL B 217-34.099 56.872 15.957 1.00 37.25 1766 CG1 VAL B 217-32.757 56.175 16.121 1.00 36.46 1767 CG2 VAL B 217-35.244 55.880 16.086 1.00 36.61 1768 C VAL B 217 -34.007 57.440 18.416 1.00 41.27 1769 P VAM B 217 -34.928 56.949 19.070 1.00 43.42 1770 N HIS B 218-32.756 57.531 18.868 1.00 43. 36 1771 CA HIS B 218-32.333 57. 054 20.189 1.00 45.06 1772 CB HIS B 218-30.963 56.368 20.095 1. 00 48.49 1773 CG HIS B 218-30.966 55.086 19.319 1.00 52.18 1774 CD2 HIS B 218-31.955 54.199 19.060 1.00 54.01 1775 ND1 HIS B 218-29.829 54.574 18.730 1.00 54.56 1776 CE1 HIS B 218-30.117 53.428 18.140 1.00 54.78 1777 NE2 HIS B 218-31.401 53.177 18.326 1.00 55.72 1778 C HIS B 218-32. 206 58.238 21.150 1.00 43.18 1779 0HIS B 218-31.298 59.057 20. 999 1.00 43. 17 1 2 3 4 5 6 7 8 9 10 1780 N VAL B 219-33-101 58. 329 22.131 1.00 40.51 1781 CA VAL B 219-33.047 59.420 23.103 1.00 38. 76 1782 CB VAL B 219-34.176 60.443 22.858 1.00 39. 96 1783 CG1 VAL B 219-34.038 61. 611 23.819 1.00 38.60 1784 CG2 VAL B 219-34.132 60.933 21.415 1.00 40.94 1785 C VAL B 219-33.155 58.904 24.539 1.00 37.03 1786 O VAL B 219-34.074 58.156 24. 870 1.00 36.64 1787 N PHE B 220-32.220 59.315 25.391 1.00 34.40 1788 CA PHE B 220-32.218 58.881 26.786 1. 00 32.04 1789 CB PHE B 220-30.793 58.532 27.231 1.00 30.24 1790 CG PHE B 220-30.710 58.017 28.645 1. 00 29. 37 1791 CD1 PHE B 220-30.962 56.677 28.929 1.00 28.40 1792 CD2 PHE B 220-30.394 58.876 29.696 1.00 29.11 1793 CE1 PHE B 220-30.911 56.202 30.241 1.00 29.12 1794 CE2 PHE B 220-30. 341 58.412 31.013 1.00 28. 45 1795 CZ PHE B 220-30.596 57.073 31.284 1.00 28.83 1796 C PHE B 220-32.789 59.932 27.732 1.00 31.31 1797 O PHE B 220-32. 375 61.092 27.711 1.00 30.79 1798 N GLY B 221-33. 741 59.514 28.559 1.00 32.20 1799 CA GLY B 221-34. 342 60.410 29.533 1.00 33.20 1800 C GLY B 221-34.831 61.752 29.021 1.00 34.98 1801 O GLY B 221-35. 673 61.812 28.126 1. 00 33.71 1802 N ASP B 222-34.304 62.831 29.596 1.00 36.44 1803 CA ASP B 222-34.703 64.179 29.205 1.00 39.33 1804 CB ASP B 222-34.841 65.070 30.448 1.00 42.09 1805 CG ASP B 222-33.531 65.240 31.202 1.00 45.29 1806 OD1 ASP B 222-33.536 65.934 32.242 1.00 47.57 1807 OD2 ASP B 222-32.498 64.688 30.762 1.00 47.04 1808 C ASP B 222-33.750 64.833 28. 206 1.00 38.86 1809 O ASP B 222-33.780 66.049 28.018 1.00 40.04 1810 N GLU B 223-32.910 64.027 27.566 1.00 37.53 1811 CA GLU B 223-31. 967 64.542 26. 582 1. 00 36. 92 1812 CB GLU B 223-30. 975 63. 446 26. 194 1. 00 37. 07 2 3 4 5 6 7 8 9 10 1813 CG GLU B 223-29. 886 63.236 27.239 1.00 40.78 1814 CD GLU B 223-29.021 62.017 26.975 1.00 42.76 1815 OE1 GLU B 223-28.774 61.699 25.792 1. 00 43. 30 1816 OE2 GLU B 223-28.574 61. 387 27.958 1.00 43. 18 1817 C GLU B 223-32.703 65.068 25. 348 1.00 36.26 1818 O GLU B 223-33. 798 64.608 25.025 1.00 34.40 1819 N LEU B 224-32.096 66.036 24.668 1.00 36.36 1820 CA LEU B 224-32.695 66.638 23.478 1. 00 36.85 1821 CB LEU B 224-31.870 67.847 23.021 1.00 39.83 1822 CG LEU B 224-31.524 68.922 24.056 1. 00 42.84 1823 CD1 LEU B 224-30. 504 68.376 25.056 1.00 44. 37 1824 CD2 LEU B 224-30.951 70.142 23. 344 1.00 44.78 1825 C LEU B 224-32.808 65.653 22. 318 1. 00 35. 39 1826 O LEU B 224-31.846 64.959 21.985 1.00 34.60 1827 N SER B 225-33. 989 65.596 21.708 1.00 33.86 1828 CA SER B 225-34.228 64.714 20.569 1.00 34.79 1829 CB SER B 225-35. 717 64. 365 20.456 1.00 36.28 1830 OG SER B 225-36.174 63.659 21.594 1.00 43.91 1831 C SER B 225-33. 785 65.404 19.278 1.00 32.59 1832 O SER B 225-33. 330 64.754 18.341 1.00 32. 37 1833 N LEU B 226-33.917 66.726 19.246 1.00 31.17 1834 CA LEU B 226-33. 557 67.510 18.072 1.00 31.61 1835 CB LEU B 226-34.717 68.443 17.718 1. 00 31. 95 1836 CG LEU B 226-34. 720 69.089 16. 334 1.00 32.21 1837 CD1 LEU B 226-34.791 68.007 15.258 1.00 31.51 1838 CD2 LEU B 226-35. 915 70.023 16.227 1.00 32.69 1839 C LEU B 226-32.286 68.318 18.311 1.00 31.56 1840 O LEU B 226-32.245 69.177 19.191 1.00 33.73 1841 N VAL B 227-31.249 68.041 17.526 1.00 30.81 1842 CA VAL B 227-29. 977 68.740 17.670 1.00 29.62 1843 CB VAL B 227-28.874 67.783 18.182 1.00 30.57 1844 CG1 VAL B 227-29.275 67.197 19.528 1.00 32.42 1845 CG2 VAL B 227-28. 642 66.673 17.180 1.00 32.80 1 2 3 4 5 6 7 8 9 10 1846 C VAL B 227-29.494 69. 379 16. 366 1.00 28.66 1847 O VAL B 227-29.551 68.766 15.296 1.00 26.77 1848 N THR B 228 -29.010 70.614 16.466 1.00 26.47 1849 CA THR B 228 -28.505 71.331 15.300 1.00 26.14 1850 CB THR B 228-28.435 72.850 15.563 1.00 26.00 1851 OG1 THR B 228-29.761 73. 360 15.749 1.00 25.78 1852 CG2 THR B 228-27.782 73.572 14.382 1.00 24.38 1853 C THR B 228-27.111 70.838 14.925 1.00 25.92 1854 O THR B 228-26.197 70.857 15.747 1.00 27.10 1855 N LEU B 229-26.953 70. 396 13.682 1.00 23.56 1856 CA LEU B 229-25.661 69.911 13.205 1.00 23.17 1857 CB LEU B 229-25.848 68.845 12.123 1.00 20.62 1858 CG LEU B 229-26.542 67.541 12.510 1.00 21.92 1859 CD1 LEU B 229-26.659 66.645 11.279 1.00 19.00 1860 CD2 LEU B 229-25.749 66.847 13.610 1. 00 22.75 1861 C LEU B 229-24.832 71.051 12.629 1.00 24.05 1862 O LEU B 229-23.671 71.231 12.998 1.00 25.78 1863 N PHE B 230-25.433 71.807 11.714 1.00 23.26 1864 CA PHE B 230-24.764 72.930 11.060 1.00 23. 43 1865 CB PHE B 230 -24.307 72.541 9.646 1.00 24.24 1866 CG PHE B 230 -23.517 71.269 9.595 1.00 28.11 1867 CDI PHE B 230-24.104 70.086 9.149 1.00 27.41 1868 CD2 PHE B 230-22.192 71.242 10.027 1.00 28.94 1869 CE1 PHE B 230-23. 381 68.892 9.135 1.00 28.64 1870 CE2 PHE B 230-21. 460 70.053 10.019 1. 00 30.77 1871 CZ PHE B 230-22.057 68.876 9.572 1.00 29.23 1872 C PHE B 230-25.727 74.102 10.966 1.00 22.94 1873 O PHE B 230-26.941 73.911 10.885 1.00 22.60 1874 N ARG B 231-25.173 75. 308 10.953 1.00 22.70 1875 CA ARG B 231-25.960 76.534 10.897 1.00 23.67 1876 CB ARG B 231-25.980 77.161 12.299 1.00 27.17 1877 CG ARG B 231-26.760 78.447 12.438 1.00 33.51 1878 CD ARG B 231-27.188 78.656 13.896 1. 00 35. 99 1 2 3 4 5 6 7 8 9 10 1879 NE ARG B 231-26.072 78.868 14.817 1. 00 38.60 1880 CZ ARG B 231-25.419 80.019 14.946 1.00 39.98 1881 NH1 ARG B 231-25. 770 81.063 14.208 1.00 40.83 1882 NH2 ARG B 231-24.429 80.135 15.823 1.00 40.71 1883 C ARG B 231-25.376 77.516 9.877 1.00 23.81 1884 O ARG B 231-24.159 77.581 9.699 1.00 23.01 1885 N CYS B 232-26.253 78.266 9.210 1.00 22.54 1886 CA CYS B 232-25.863 79.259 8.208 1.00 25.12 1887 C CYS B 232-26.514 80.600 8.577 1. 00 23.97 1888 O CYS B 232-27.694 80.629 8.928 1.00 24.28 1889 CB CYS B 232-26.360 78.834 6.812 1.00 26.75 1890 SG CYS B 232-25.430 79.616 5.459 1.00 35.51 1891 N ILE B 233-25. 765 81.700 8.506 1.00 22.43 1892 CA ILE B 233-26. 341 83.010 8.821 1.00 24.60 1893 CB ILE B 233-26.151 83.356 10.320 1.00 26.23 1894 CG2 ILE B 233-24.683 83.541 10.639 1.00 26.47 1895 CG1 ILE B 233-26.940 84.621 10.662 1.00 29.12 1896 CD1 ILE B 233 -27.002 84.922 12.147 1.00 31.42 1897 C ILE B 233 -25.807 84.157 7.950 1.00 25.43 1898 O ILE B 233-24.619 84.204 7.624 1.00 25.08 1899 N GLN B 234-26.699 85.075 7.574 1.00 24.93 1900 CA GLN B 234-26.345 86.220 6.730 1.00 26.66 1901 CB GLN B 234-26.735 85.935 5.275 1.00 26.82 1902 CG GLN B 234-25.907 84.872 4.577 1.00 25.95 1903 CD GLN B 234-24.601 85.423 4.052 1.00 27.02 1904 OE1 GLN B 234-24.581 86.170 3.074 1.00 26.07 1905 NE2 GLN B 234-23.502 85.067 4.705 1.00 27.06 1906 C GLN B 234-27.029 87.528 7.145 1.00 28. 31 1907 O GLN B 234-28.231 87.541 7.411 1.00 26. 44 1908 N ASN B 235-26.268 88.622 7.185 1.00 29. 13 1909 CA ASN B 235-26.840 89.937 7.500 1.00 30.85 1910 CB ASN B 235-25.748 90.979 7.782 1.00 29.39 1911 CG ASN B 235-25.223 90.915 9.195 1.00 29.71 1 2 3 4 5 6 7 8 9 10 1912 OD1 ASN B 235-25.973 91.088 10.161 1.00 32.05 1913 ND2 ASN B 235-23.924 90.677 9.329 1.00 27.73 1914 C ASN B 235-27.588 90.367 6.241 1.00 31.55 1915 O ASN B 235-27.124 90.110 5.128 1.00 32. 03 1916 N MET B 236-28.733 91.021 6.410 1.00 30.99 1917 CA MET B 236-29. 523 91.475 5.270 1.00 32. 37 1918 CB MET B 236-30.955 90.945 5. 375 1.00 32.09 1919 CG MET B 236-31.064 89.442 5.593 1.00 31.77 1920 SD MET B 236-30.277 88.444 4.306 1.00 31.52 1921 CE MET B 236-31. 305 88.836 2.871 1.00 31.71 1922 C MET B 236-29.555 93.005 5.194 1.00 34.40 1923 O MET B 236-29.568 93.686 6.219 1.00 33.25 1924 N PRO B 237-29.562 93.563 3.973 1.00 36.45 1925 CD PRO B 237-29.387 92. 899 2.668 1.00 36.12 1926 CA PRO B 237-29. 594 95.020 3.815 1.00 38.81 1927 CB PRO B 237-29.064 95.217 2.400 1.00 37.87 1928 CG PRO B 237-29.633 94.030 1.685 1. 00 36.50 1929 C PRO B 237-31.006 95.584 3.993 1.00 41.49 1930 O PRO B 237-31.962 94.842 4.228 1.00 40.65 1931 N GLU B 238-31.121 96.903 3.878 1.00 44.82 1932 CA GLU B 238-32.400 97.589 4.018 1.00 47. 69 1933 CB GLU B 238-32.156 99.046 4.405 1.00 50.49 1934 CG GLU B 238-31.409 99.195 5.721 1.00 55.09 1935 CD GLU B 238-32.212 98.681 6.903 1.00 57.74 1936 OE1 GLU B 238-31.630 98.548 7.999 1.00 59.34 1937 OE2 GLU B 238-33.417 98.420 6.733 1.00 58.56 1938 C GLU B 238-33.213 97.529 2.733 1.00 47.45 1939 O GLU B 238-34.435 97.367 2. 762 1.00 48.53 1940 N THR B 239-32.521 97.631 1.606 1.00 47.02 1941 CA THR B 239-33.174 97.615 0. 307 1.00 46.97 1942 CB THR B 239-32. 867 98.917-0. 458 1.00 48.02 1943 OG1 THR B 239-31. 475 98.961-0. 795 1.00 50.40 1944 CG2 THR B 239-33.189 100.128 0.412 1.00 48.33 1 2 3 4 5 6 7 8 9 10 1945 C THR B 239-32. 780 96. 421-0. 567 1. 00 46. 27 1946 O THR B 239-31.620 96.006-0. 587 1.00 46. 32 1947 N LEU B 240-33.761 95. 883-1. 287 1.00 44. 66 1948 CA LEU B 240-33.561 94.746-2. 183 1.00 43.37 1949 CB LEU B 240-32.888 95.204-3. 481 1.00 44.82 1950 CG LEU B 240-33.617 96.220-4. 365 1.00 46.67 1951 CD1 LEU B 240-35.028 95.729-4. 650 1.00 46. 30 1952 CD2 LEU B 240-33.653 97.573 -3. 676 1.00 48.31 1953 C LEU B 240-32.743 93.609-1. 573 1.00 41.52 1954 O LEU B 240-31.717 93.216-2. 122 1.00 40.90 1955 N PRO B 241-33.192 93.062-0. 432 1.00 40.55 1956 CD PRO B 241-34. 444 93.347 0.294 1.00 39.51 1957 CA PRO B 241-32.454 91.963 0.204 1.00 38. 54 1958 CB PRO B 241-33.242 91.721 1.490 1.00 38.58 1959 CG PRO B 241-34. 650 92.076 1.089 1.00 39.76 1960 C PRO B 241-32.402 90.730-0. 702 1.00 37.11 1961 O PRO B 241-33.426 90. 306-1. 241 1.00 35. 49 1962 N ASN B 242-31.205 90.162-0. 859 1.00 34.79 1963 CA ASN B 242-30. 990 88.992-1. 712 1.00 33.90 1964 CB ASN B 242-30.976 89.410-3. 188 1.00 37.24 1965 CG ASN B 242-32.239 89. 026-3.922 1.00 40.97 1966 OD1 ASN B 242-32.584 87.849-4. 016 1.00 43.60 1967 ND2 ASN B 242-32.936 90.022-4. 458 1.00 44.45 1968 C ASN B 242-29.665 88.291-1. 407 1.00 30.53 1969 O ASN B 242-28.685 88.501-2. 116 1.00 31.24 1970 N ASN B 243-29.632 87. 466-0. 364 1.00 28.29 1971 CA ASN B 243-28.421 86.728 0.004 1.00 25.21 1972 CB ASN B 243-27.869 87.193 1.363 1.00 26.22 1973 CG ASN B 243-27.180 88.538 1.298 1.00 28.00 1974 OD1 ASN B 243-26. 339 88.777 0.433 1.00 26.05 1975 ND2 ASN B 243-27.517 89.424 2.239 1.00 27.94 1976 C ASN B 243-28.701 85.231 0.127 1.00 23.75 1977 O ASN B 243-29.591 84. 834 0.886 1.00 22. 49 _ 2 __ 5 6 7 8 9 10 1978 N SER B 244-27.962 84.402-0. 609 1.00 20.48 1979 CA SER B 244-28. 135 82. 957-0.478 1. 00 20.05 1980 CB SER B 244-27. 787 82.202-1. 778 1.00 17.82 1981 OG SER B 244-26.448 82.398-2. 196 1.00 18.20 1982 C SER B 244-27.188 82.554 0.646 1.00 21.23 1983 O SER B 244-26.175 83.221 0.873 1.00 20.19 1984 N CYS B 245-27. 529 81.488 1.364 1.00 21.13 1985 CA CYS B 245-26.712 81.018 2.476 1.00 23.69 1986 C CYS B 245-26.470 79.523 2.325 1.00 22.92 1987 O CYS B 245-27.419 78.739 2. 322 1.00 22.51 1988 CB CYS B 245-27.425 81.272 3.814 1.00 26.79 1989 SG CYS B 245-26.267 81.455 5.204 1.00 33.48 1990 N TYR B 246-25.204 79.130 2.204 1.00 19.85 1991 CA TYR B 246-24.860 77.722 2.056 1. 00 19.10 1992 CB TYR B 246-24.135 77.497 0.717 1.00 18.94 1993 CG TYR B 246-23.627 76.082 0.479 1.00 18.45 1994 CD1 TYR B 246-22.489 75.601 1.137 1.00 16.43 1995 CE1 TYR B 246-22.009 74.306 0.900 1.00 15.90 1996 CD2 TYR B 246-24.275 75. 230-0. 420 1.00 17.20 1997 CE2 TYR B 246-23.807 73.934-0. 662 1.00 16.97 1998 CZ TYR B 246-22.677 73.479-0. 001 1.00 17.27 1999 OH TYR B 246-22.215 72.199-0. 235 1.00 17.35 2000 C TYR B 246-23.986 77. 222 3.199 1.00 19.41 2001 O TYR B 246-23. 147 77.954 3.722 1.00 19.55 2002 N SER B 247-24.209 75.974 3.597 1.00 18.63 2003 CA SER B 247-23.394 75.344 4.625 1.00 19.71 2004 CB SER B 247-23.882 75.686 6.033 1.00 21.86 2005 OG SER B 247-22.940 75.224 6.992 1.00 22.68 2006 C SER B 247-23.439 73.837 4.415 1.00 18.95 2007 O SER B 247-24.429 73.296 3.916 1.00 17. 64 2008 N ALA B 248-22. 354 73.166 4.786 1.00 17.67 2009 CA ALA B 248-22.253 71.723 4.624 1.00 16.93 2010 CB ALA B 248-21.823 71. 389 3.199 1.00 17.16 1 2 3 4 5 6 7 8 9 10 2011 C ALA B 248-21.241 71.161 5.604 1.00 18.27 2012 O ALA B 248-20.363 71.881 6.090 1.00 16.07 2013 N GLY B 249-21. 360 69.869 5.878 1.00 17.12 2014 CA GLY B 249-20.446 69.216 6.795 1.00 18.50 2015 C GLY B 249-20.687 67.721 6.844 1.00 20.13 2016 O GLY B 249-21.575 67.199 6.163 1.00 20.98 2017 N ILE B 250-19.892 67.027 7.650 1. 00 20. 58 2018 CA ILE B 250-20.016 65.581 7.782 1.00 20.37 2019 CB ILE B 250-18.658 64.877 7.583 1.00 20.55 2020 CG2 ILE B 250-18.806 63.371 7.831 1.00 19.65 2021 CG1 ILE B 250-18.144 65.138 6.165 1.00 20.86 2022 CD1 ILE B 250-16.750 64.613 5.909 1.00 23.90 2023 C ILE B 250-20.539 65.244 9.164 1.00 21.56 2024 O ILE B 250-20.189 65.906 10.139 1.00 19.47 2025 N ALA B 251-21.382 64.217 9.248 1.00 21. 92 2026 CA ALA B 251-21.938 63.809 10.533 1.00 22. 41 2027 CB ALA B 251-23.237 64.582 10.810 1.00 22.34 2028 C ALA B 251-22.205 62.306 10.593 1.00 23.69 2029 O ALA B 251-22.491 61.672 9.575 1.00 21.96 2030 N LYS B 252-22.084 61. 740 11.791 1.00 24.95 2031 CA LYS B 252-22. 347 60.319 12.007 1.00 27.58 2032 CB LYS B 252-21.596 59.785 13.228 1.00 29. 20 2033 CG LYS B 252-20.090 59.788 13.159 1.00 36.27 2034 CD LYS B 252-19.560 59.128 14.427 1.00 39.68 2035 CE LYS B 252-18.053 59.006 14.445 1.00 42.69 2036 NZ LYS B 252-17.608 58.325 15.695 1.00 42.13 2037 C LYS B 252-23.833 60.222 12. 313 1.00 26.35 2038 O LYS B 252-24.307 60.848 13.258 1.00 25.53 2039 N LEU B 253-24.562 59.440 11.529 1.00 24.53 2040 CA LEU B 253-25.995 59.287 11. 752 1.00 24.85 2041 CB LEU B 253-26.780 59.857 10.561 1.00 22.48 2042 CG LEU B 253-26.500 61. 320 10.193 1. 00 21. 69 2043 CD1 LEU B 253-27.260 61.694 8.928 1.00 20.33 1 2 3 4 5 6 7 8 9 10 2044 CD2 LEU B 253-26.896 62.224 11. 348 1. 00 20. 56 2045 C LEU B 253-26.327 57.809 11.941 1.00 25.44 2046 O LEU B 253-25.616 56.935 11.444 1.00 25.16 2047 N GLU B 254-27.401 57.536 12.669 1.00 26.65 2048 CA GLU B 254-27.827 56.164 12.924 1.00 29.17 2049 CB GLU B 254-27.962 55.930 14.433 1. 00 31.98 2050 CG GLU B 254-26. 629 55.850 15.158 1.00 41. 46 2051 CD GLU B 254-26.766 55.968 16.663 1.00 46.47 2052 OE1 GLU B 254-25.770 55.697 17.369 1. 00 50.97 2053 OE2 GLU B 254-27.861 56.340 17.141 1.00 50. 31 2054 C GLU B 254-29.149 55.844 12.238 1.00 27.10 2055 O GLU B 254-29.994 56.722 12.043 1.00 23.49 2056 N GLU B 255-29.315 54.579 11.866 1.00 28.66 2057 CA GLU B 255-30.540 54.131 11.217 1.00 29.68 2058 CB GLU B 255-30.557 52.606 11.147 1.00 32.37 2059 CG GLU B 255-31.777 52.030 10.463 1.00 37.57 2060 CD GLU B 255-31.818 50.520 10.553 1.00 40.57 2061 OE1 GLU B 255-30.795 49.874 10. 239 1.00 42. 39 2062 OE2 GLU B 255-32.876 49.981 10.937 1.00 44.82 2063 C GLU B 255-31.726 54.622 12.038 1. 00 27.17 2064 O GLU B 255-31.761 54.435 13.252 1.00 28. 75 2065 N GLY B 256-32.688 55.256 11.376 1.00 26.59 2066 CA GLY B 256-33.852 55.774 12.072 1.00 25.02 2067 C GLY B 256-33.816 57.282 12.266 1.00 25.05 2068 0 GLY B 256-34.854 57.916 12.459 1.00 23.75 2069 N ASP B 257-32.619 57.862 12.235 1.00 25.40 2070 CA ASP B 257-32.479 59. 308 12.394 1.00 25.90 2071 CB ASP B 257-31.003 59.721 12.455 1.00 26.28 2072 CG ASP B 257-30. 315 59.292 13.738 1.00 29. 60 2073 OD1 ASP B 257-31.019 58.977 14.725 1.00 28.77 2074 OD2 ASP B 257 -29.061 59.292 13.757 1.00 29.12 2075 C ASP B 257 -33.116 60.019 11.207 1.00 26.14 2076 O ASP B 257-33. 247 59.445 10.127 1.00 26. 07 1 2 3 4 5 6 7 8 9 10 2077 N GLU B 258-33. 505 61.270 11.415 1.00 25.48 2078 CA GLU B 258-34. 093 62.079 10.356 1.00 27.35 2079 CB GLU B 258-35.583 62.326 10.616 1.00 28.78 2080 CG GLU B 258-36.447 61.071 10.635 1.00 33.80 2081 CD GLU B 258-37. 935 61.392 10.641 1.00 36.70 2082 OE1 GLU B 258-38. 390 62.142 11.533 1.00 37.44 2083 OE2 GLU B 258-38.652 60.893 9.748 1. 00 41. 14 2084 C GLU B 258-33.367 63.423 10.304 1.00 26.22 2085 O GLU B 258-32.859 63.903 11. 323 1.00 26.01 2086 N LEU B 259-33. 315 64.026 9.120 1.00 23.74 2087 CA LEU B 259-32.674 65. 328 8.956 1.00 23.18 2088 CB LEU B 259-31.503 65.241 7.972 1.00 23.94 2089 CG LEU B 259-30. 356 64.272 8.260 1.00 25.18 2090 CD1 LEU B 259-29.390 64.293 7.082 1.00 23.38 2091 CD2 LEU B 259-29.639 64.670 9.550 1.00 25.83 2092 C LEU B 259-33.691 66. 326 8.417 1.00 22. 32 2093 0 LEU B 259-34.496 65.994 7.541 1.00 21.73 2094 N GLN B 260-33.662 67.545 8.943 1.00 20.95 2095 CA GLN B 260-34.568 68.589 8.478 1. 00 21.79 2096 CB GLN B 260-35.776 68.729 9.416 1. 00 22.77 2097 CG GLN B 260-35.431 69.098 10.857 1. 00 26.13 2098 CD GLN B 260-36.672 69.248 11.731 1.00 29.50 2099 OE1 GLN B 260-37. 579 68.421 11.680 1.00 27. 32 2100 NE2 GLN B 260-36.708 70. 302 12.540 1.00 28. 39 2101 C GLN B 260-33.838 69.922 8. 395 1.00 20. 69 2102 O GLN B 260-32.863 70.151 9.113 1.00 20.65 2103 N LEU B 261-34. 304 70.791 7.506 1.00 19.67 2104 CA LEU B 261-33.713 72.117 7.355 1.00 21.17 2105 CB LEU B 261-33.365 72.390 5.884 1.00 18.65 2106 CG LEU B 261-32.592 73.683 5.571 1.00 20.72 2107 CD1 LEU B 261-31.889 73. 547 4.216 1.00 17.71 2108 CD2 LEU B 261-33.531 74.880 5.576 1.00 19.09 2109 C LEU B 261-34. 758 73. 105 7.866 1.00 21. 90 1 2 3 4 5 6 7 8 9 10 2110 O LEU B 261-35.837 73.242 7.280 1.00 22. 92 2111 N ALA B 262-34.435 73.785 8.961 1.00 22.07 2112 CA ALA B 262-35. 361 74.731 9.579 1.00 23.92 2113 CB ALA B 262-35.673 74.278 11.004 1.00 23.17 2114 C ALA B 262-34.881 76.175 9.607 1.00 25.34 2115 O ALA B 262-33.694 76.446 9.793 1.00 24.14 2116 N ILE B 263-35.826 77.095 9. 426 1.00 26.06 2117 CA ILE B 263-35. 558 78.526 9.460 1.00 27.76 2118 CB ILE B 263-36.174 79.236 8.239 1.00 25.99 2119 CG2 ILE B 263-35. 922 80.739 8. 329 1.00 26.47 2120 CG1 ILE B 263-35.567 78.664 6.954 1. 00 27.54 2121 CD1 ILE B 263-36.235 79.141 5.677 1.00 27.36 2122 C ILE B 263-36. 213 79.046 10.747 1.00 30.93 2123 O ILE B 263-37. 441 79.110 10.843 1.00 28.36 2124 N PRO B 264-35.395 79.413 11.754 1.00 33.41 2125 CD PRO B 264-33. 922 79.444 11.675 1.00 34.64 2126 CA PRO B 264-35.849 79.920 13.054 1.00 35.55 2127 CB PRO B 264-34.563 79.954 13.871 1.00 36.13 2128 CG PRO B 264-33.551 80.339 12.843 1.00 36.30 2129 C PRO B 264-36.542 81.275 13.014 1.00 37.80 2130 O PRO B 264-36.125 82.215 13.689 1.00 39.17 2131 N ARG B 265-37. 604 81.365 12. 225 1.00 39. 32 2132 CA ARG B 265-38.362 82.599 12.100 1.00 40.71 2133 CB ARG B 265-37.601 83.605 11.235 1.00 43.22 2134 CG ARG B 265-38.287 84.950 11.125 1.00 47.22 2135 CD ARG B 265-37. 543 85.880 10.187 1.00 51.11 2136 NE ARG B 265-38.181 87.191 10.121 1.00 55.16 2137 CZ ARG B 265-38.202 88.065 11.124 1.00 57.26 2138 NH1 ARG B 265-37.615 87.771 12.278 1.00 57.89 2139 NH2 ARG B 265-38. 816 89.231 10.974 1.00 58.16 2140 C ARG B 265-39.720 82.303 11.473 1.00 39.68 2141 O ARG B 265-39.821 81.518 10.532 1.00 37.42 2142 N GLU B 266-40.759 82. 934 12. 007 1. 00 39.69 1 2 3 4 5 6 7 8 9 10 2143 CA GLU B 266-42.119 82.749 11.516 1.00 39. 85 2144 CB GLU B 266-43.126 83. 180 12.592 1.00 42.89 2145 CG GLU B 266-42.756 84.471 13.319 1.00 46.91 2146 CD GLU B 266-41.497 84.333 14.176 1.00 50.45 2147 OBI GLU B 266-41.513 83.538 15.143 1.00 53. 30 2148 OE2 GLU B 266-40.490 85.016 13.880 1.00 50.45 2149 C GLU B 266-42. 355 83.532 10.229 1.00 37.82 2150 O GLU B 266-41.949 84.687 10.110 1.00 37.35 2151 N ASN B 267-43.002 82.887 9.265 1.00 37.53 2152 CA ASN B 267-43.301 83.504 7.973 1.00 39.00 2153 CB ASN B 267-44. 356 84.602 8.146 1.00 40.45 2154 CG ASN B 267-45.667 84.065 8.684 1.00 42.19 2155 OD1 ASN B 267-46.280 83. 179 8.084 1.00 43.81 2156 ND2 ASN B 267-46.105 84.596 9.822 1.00 43.30 2157 C ASN B 267-42.064 84.082 7.287 1.00 37.58 2158 O ASN B 267-42.103 85.185 6.741 1.00 36.78 2159 N ALA B 268-40.970 83.328 7. 307 1.00 37.02 2160 CA ALA B 268-39.725 83.774 6.687 1.00 36.93 2161 CB ALA B 268-38.623 82.751 6.944 1.00 35.90 2162 C ALA B 268-39.899 83.991 5.184 1.00 37.13 2163 O ALA B 268-40.477 83.151 4.490 1.00 36.75 2164 N GLN B 269-39.404 85.122 4.688 1.00 37.32 2165 CA GLN B 269-39.496 85.433 3.265 1.00 38.06 2166 CB GLN B 269-39.584 86.949 3.055 1.00 39.95 2167 CG GLN B 269-40.821 87.586 3.675 1.00 42.15 2168 CD GLN B 269-42.116 86.966 3.170 1.00 43.57 2169 OBI GLN B 269-42.426 87.024 1.978 1.00 44.58 2170 NE2 GLN B 269-42.877 86.365 4.079 1.00 44.56 2171 C GLN B 269-38.271 84.872 2.537 1.00 37.21 2172 O GLN B 269-37.147 85.320 2.761 1.00 36.64 2173 N ILE B 270-38.506 83.893 1.667 1.00 35.33 2174 CA ILE B 270-37.438 83.240 0.913 1.00 35.22 2175 CB ILE B 270-37. 048 81. 895 1. 563 1. 00 34. 98 1 2 3 4 5 6 7 8 9 10 2176 CG2 ILE B 270-36.542 82.121 2.991 1.00 32.72 2177 CG1 ILE B 270-38. 265 80.964 1. 572 1.00 34. 72 2178 CUL IULE B 270-37.990 79.579 2. 113 1. 00 34. 26 2179 C ILE B 270-37.871 82. 939-0.518 1.00 35. 02 2180 O ILE B 270-39.038 83.115-0. 880 1.00 35. 49 2181 N SER B 271-36.923 82.479-1. 327 1.00 33.24 2182 CA SER B 271-37.206 82.117-2. 710 1. 00 32.60 2183 CB SER B 271-36.057 82.532-3. 631 1. 00 32. 35 2184 OG SER B 271-36.214 81.947-4. 915 1. 00 30. 78 2185 C SER B 271-37. 383 80.612-2. 787 1.00 32. 68 2186 O SER B 271-36.633 79.863-2. 161 1.00 32.95 2187 N LEU B 272-38.371 80.169-3. 558 1. 00 31.29 2188 CA LEU B 272-38.627 78.745-3. 709 1.00 31.67 2189 CB LEU B 272-40.123 78.445-3. 535 1.00 32.68 2190 CG LEU B 272-40.740 78.777-2. 170 1.00 33.47 2191 CD1 LEU B 272-42.208 78.367-2. 164 1.00 35.64 2192 CD2 LEU B 272-39.988 78.051-1. 061 1.00 33.45 2193 C LEU B 272-38.144 78.195-5. 050 1.00 31.29 2194 0 LEU B 272-38.714 77.237-5. 575 1.00 31.71 2195 N ASP B 273-37.104 78.808-5. 611 1.00 29.80 2196 CA ASP B 273-36.540 78. 327-6. 869 1.00 28. 87 2197 CB ASP B 273-35.624 79. 378-7. 517 1.00 32. 36 2198 CG ASP B 273-36. 385 80. 563-8. 095 1.00 37.24 2199 OD1 ASP B 273-37. 625 80.481-8. 242 1.00 39.80 2200 OD2 ASP B 273-35.728 81.579-8. 416 1.00 39. 96 2201 C ASP B 273-35.704 77.088-6. 549 1.00 26.51 2202 O ASP B 273-34.902 77.100-5. 611 1.00 24.13 2203 N GLY B 274-35.882 76.033-7. 336 1. 00 23.77 2204 CA GLY B 274-35.136 74.807-7. 119 1.00 22.49 2205 C GLY B 274-33.628 74.922-7. 288 1.00 23.35 2206 O GLY B 274-32.884 74.076-6. 783 1.00 22.04 2207 N ASP B 275-33.158 75.950-7. 993 1.00 22.00 2208 CA ASP B 275-31. 718 76. 092-8. 176 1. 00 21. 77 1 2 3 4 5 6 7 8 9 10 2209 CB ASP B 275-31.390 76.624-9. 586 1.00 22. 35 2210 CG ASP B 275-31.996 77.991-9. 870 1.00 24. 35 2211 OD1 ASP B 275-32. 507 78.642-8. 938 1.00 26.12 2212 OD2 ASP B 275-31.947 78.423-11. 040 1.00 26.75 2213 C ASP B 275-31.036 76.957-7. 110 1.00 20.59 2214 O ASP B 275-29.815 77.119-7. 135 1.00 19.57 2215 N VAL B 276-31.813 77.494-6. 168 1. 00 18.06 2216 CA VAL B 276-31.244 78. 333-5. 108 1.00 19. 25 2217 CB VAL B 276-31.728 79.788-5. 200 1.00 21.88 2218 CG1 VAL B 276-31.461 80. 305-6. 552 1.00 27. 32 2219 CG2 VAL B 276-33.216 79.888-4. 888 1.00 21.15 2220 C VAL B 276-31.536 77. 862-3. 698 1.00 18.04 2221 O VAL B 276-30.831 78.230-2. 761 1.00 15.97 2222 N THR B 277-32.595 77.074-3. 544 1.00 18. 26 2223 CA THR B 277-32.970 76.553-2. 233 1.00 18.03 2224 CB THR B 277-34. 318 77.137-1. 770 1.00 19.15 2225 OG1 THR B 277-34.178 78.553-1. 610 1.00 20.25 2226 CG2 THR B 277-34.747 76.528-0. 428 1.00 18. 96 2227 C THR B 277-33.054 75. 047-2. 385 1.00 18.06 2228 O THR B 277-33.944 74.529-3. 066 1.00 16.87 2229 N PHE B 278-32.090 74.353-1. 783 1.00 17.78 2230 CA PHE B 278-32.017 72.905-1. 880 1.00 16.99 2231 CB PHE B 278-31.244 72.508-3. 152 1.00 17.40 2232 CG PHE B 278-29.911 73.205-3. 311 1.00 19.33 2233 CD1 PHE B 278-28.767 72.701-2. 699 1.00 18.82 2234 CD2 PHE B 278-29.799 74.356-4. 093 1.00 18.77 2235 CE1 PHE B 278-27.529 73.330-2. 859 1.00 19.20 2236 CE2 PHE B 278-28.561 74.995-4. 258 1.00 19.28 2237 CZ PHE B 278-27.428 74.478-3. 644 1.00 16.48 2238 C PHE B 278-31.405 72.281-0. 623 1.00 17.90 2239 O PHE B 278-30.844 72.985 0.225 1.00 16.35 2240 N PHE B 279-31.495 70.957-0. 522 1.00 17.01 2241 CA PHE B 279-31.046 70.243 0.671 1.00 17. 86 1 2 3 4 5 6 7 8 9 10 2242 CB PHE B 279-32.202 70.361 1.689 1.00 17.83 2243 CG PHE B 279-32.025 69.588 2.974 1.00 18.44 2244 CD1 PHE B 279-30.803 69.550 3.641 1. 00 19.57 2245 CD2 PHE B 279-33.132 68.974 3.569 1.00 18.51 2246 CE1 PHE B 279-30.686 68.914 4.893 1.00 21.66 2247 CE2 PHE B 279-33.032 68.338 4.815 1.00 20.47 2248 CZ PHE B 279-31.805 68. 308 5. 481 1.00 19. 85 2249 C PHE B 279-30.736 68.786 0.305 1.00 19.61 2250 O PHE B 279-31.520 68.136-0. 385 1.00 18.92 2251 N GLY B 280-29.595 68.269 0.753 1.00 18.40 2252 CA GLY B 280-29.262 66.896 0.414 1.00 19.14 2253 C GLY B 280-28.252 66.201 1.307 1.00 19. 87 2254 O GLY B 280-27.661 66.814 2.199 1.00 18.48 2255 N ALA B 281-28.051 64.910 1.057 1.00 17. 75 2256 CA ALA B 281-27.113 64.112 1.834 1.00 19. 48 2257 CB ALA B 281-27.800 63.564 3.085 1.00 19. 30 2258 C ALA B 281-26.534 62.964 1.014 1.00 20.33 2259 O ALA B 281-27.174 62.456 0.084 1.00 19.17 2260 N LEU B 282-25. 322 62.555 1.372 1.00 20.40 2261 CA LEU B 282-24.638 61.465 0.685 1.00 22. 87 2262 CB LEU B 282-23.642 62. 035-0. 327 1. 00 24.57 2263 CG LEU B 282-22.732 61.029-1. 036 1.00 26.20 2264 CD1 LEU B 282-22.358 61.549-2. 408 1.00 28.82 2265 CD2 LEU B 282-21.496 60.766-0. 192 1.00 28.91 2266 C LEU B 282-23.910 60.572 1.688 1.00 24.16 2267 O LEU B 282-23.241 61.065 2.598 1.00 23.48 2268 N LYS B 283-24.042 59.258 1.522 1.00 23.42 2269 CA LYS B 283-23.387 58. 314 2.422 1.00 26.45 2270 CB LYS B 283-24.182 57.008 2.483 1.00 27. 75 2271 CG LYS B 283-23.598 55.949 3.410 1.00 29.06 2272 CD LYS B 283-24.617 54.844 3.657 1.00 30. 55 2273 CE LYS B 283-23.959 53.572 4.160 1.00 32.55 2274 NZ LYS B 283-23.162 53.785 5. 387 1. 00 32. 02 1 2 3 4 5 6 7 8 9 10 2275 C LYS B 283-21. 957 58.045 1.963 1.00 27.96 2276 O LYS B 283-21.727 57.574 0.850 1.00 27.99 2277 N LEU B 284-20. 995 58. 359 2. 824 1.00 28. 86 2278 CA LEU B 284-19.591 58.153 2.500 1.00 32.18 2279 CB LEU B 284-18.707 58.958 3.454 1.00 31.62 2280 CG LEU B 284-18.991 60.460 3.525 1.00 33.74 2281 CDl LEU B 284-18.105 61.094 4.588 1.00 35.02 2282 CD2 LEU B 284-18.754 61.095 2.166 1.00 30. 49 2283 C LEU B 284-19.245 56.677 2.612 1.00 34. 50 2284 O LEU B 284-19.640 56.013 3.565 1.00 33.55 2285 N LEU B 285-18.507 56.164 1.635 1.00 38.23 2286 CA LEU B 285-18. 110 54.763 1. 653 1.00 42.58 2287 CB LEU B 285-17.479 54.375 0.315 1.00 43.61 2288 CG LEU B 285-18.497 54.199-0. 816 1.00 45. 88 2289 CD1 LEU B 285-17.788 53.966-2. 138 1.00 46.30 2290 CD2 LEU B 285-19.414 53. 031-0. 481 1.00 46. 85 2291 C LEU B 285-17.134 54.503 2.792 1.00 44. 34 2292 O LEU B 285-17.438 53.647 3.649 1.00 46.36 2293 OXT LEU B 285-16.079 55.167 2.821 1.00 47.61 2294 CB VAL C 142-12.227 50.782-0. 685 1.00 53. 24 2295 CG1 VAL C 142-11.088 50.048-1. 378 1.00 53.59 2296 CG2 VAL C 142-13.554 50. 456-1. 358 1. 00 53.67 2297 C VAL C 142-13.220 51. 341 1.539 1.00 50.07 2298 O VAL C 142-14.441 51.242 1.416 1.00 49.71 2299 N VAL C 142-12.701 48.969 0.986 1.00 52.67 2300 CA VAL C 142-12.277 50.388 0.812 1.00 51.84 2301 N THR C 143-12.642 52.264 2.300 1.00 47. 76 2302 CA THR C 143-13.419 53.236 3.055 1.00 44.98 2303 CB THR C 143-13.503 52.826 4.537 1.00 46. 13 2304 OG1 THR C 143-14.255 53.804 5.264 1.00 49.10 2305 CG2 THR C 143-12.112 52.707 5.136 1.00 46.73 2306 C THR C 143-12. 785 54.623 2.945 1.00 41.95 2307 O THR C 143-11. 586 54.745 2.691 1.00 42.15 1 2 3 4 5 6 7 8 9 10 2308 N GLN C 144-13.593 55.663 3.133 1.00 37.64 2309 CA GLN C 144-13.111 57.039 3.044 1.00 33.48 2310 CB GLN C 144-14.153 57.921 2. 352 1.00 33.92 2311 CG GLN C 144-14. 303 57.658 0.868 1.00 35.46 2312 CD GLN C 144 -15.344 58.552 0.228 1.00 35.53 2313 OBI GLN C 144-16.539 58.427 0. 496 1.00 35.87 2314 NE2 GLN C 144-14.895 59.466-0. 618 1.00 36.11 2315 C GLN C 144-12.768 57.647 4. 399 1.00 30.01 2316 O GLN C 144-13.657 58.014 5.168 1.00 28.24 2317 N ASP C 145-11.474 57.757 4.682 1.00 25.54 2318 CA ASP C 145-11.021 58337 5. 939 1.00 25.56 2319 CB ASP C 145-9.498 58.212 6.079 1.00 25.32 2320 CG ASP C 145-9.027 56.769 6.167 1.00 29.51 2321 OD1 ASP C 145-7.799 56.556 6.289 1.00 28.92 2322 OD2 ASP C 145-9.873 55.848 6.116 1.00 29.62 2323 C ASP C 145-11.403 59.813 5.963 1.00 23.50 2324 O ASP C 145-11.436 60.474 4.927 1.00 24.14 2325 N CYS C 146-11.709 60.328 7.146 1.00 23.79 2326 CA CYS C 146-12.056 61.731 7.274 1.00 23. 39 2327 CB CYS C 146-13.504 61.986 6.826 1.00 24.72 2328 SG CYS C 146-14.789 61.040 7.669 1.00 31.34 2329 C CYS C 146-11.840 62.216 8.697 1.00 22.76 2330 O CYS C 146-11.646 61.421 9.622 1.00 22.56 2331 N LEU C 147-11.844 63.531 8.861 1.00 21.12 2332 CA LEU C 147-11.640 64.128 10.166 1.00 23.66 2333 CB LEU C 147-10. 13, 8 64.240 10.456 1.00 24.07 2334 CG LEU C 147-9.714 64.837 11.801 1.00 27.99 2335 CD1 LEU C 147-8. 355 64.289 12.181 1.00 28.28 2336 CD2 LEU C 147-9.691 66. 356 11.721 1.00 27.06 2337 C LEU C 147-12.291 65.498 10.192 1.00 22.23 2338 O LEU C 147-12.133 66.286 9.260 1.00 23.61 2339 N GLN C 148-13.031 65.775 11.260 1.00 22.28 2340 CA GLN C 148-13. 698 67.060 11.399 1.00 20.70 1 2 3 4 5 6 7 8 9 10 2341 CB GLN C 148-15.209 66.906 11.217 1. 00 21.14 2342 CG GLN C 148-15.953 68.234 11.110 1. 00 22.82 2343 CD GLN C 148-17.423 68.050 10.756 1.00 26.70 2344 OE1 GLN C 148-18.265 67.819 11.628 1.00 29.00 2345 NE2 GLN C 148-17.731 68.130 9.470 1.00 23.24 2346 C GLN C 148-13.412 67.680 12.762 1.00 20.56 2347 O GLN C 148-13.516 67.017 13.803 1.00 19.68 2348 N LEU C 149-13.056 68.960 12.734 1.00 18.27 2349 CA LEU C 149-12.754 69.728 13.934 1.00 19.92 2350 CB LEU C 149-11. 396 70.425 13.782 1.00 19.05 2351 CG LEU C 149-10.184 69.551 13.450 1.00 18.40 2352 CD1 LEU C 149-8.984 70.441 13.130 1.00 19.92 2353 CD2 LEU C 149-9.878 68.610 14.620 1.00 17.99 2354 C LEU C 149-13. 837 70.786 14.114 1. 00 21.15 2355 O LEU C 149-14.410 71.270 13.138 1.00 22.99 2356 N ILE C 150-14.130 71.138 15.359 1.00 20.76 2357 CA ILE C 150-15.127 72.166 15.636 1.00 21.71 2358 CB ILE C 150-16.443 71.556 16.187 1.00 23.98 2359 CG2 ILE C 150-17.063 70.616 15.142 1.00 23.21 2360 CG1 ILE C 150-16.168 70.789 17.485 1.00 25.61 2361 CD1 ILE C 150-17.419 70.181 18.107 1.00 26.54 2362 C ILE C 150-14.529 73.130 16.656 1.00 21.92 2363 O ILE C 150-13.686 72.743 17.467 1.00 23.30 2364 N ALA C 151-14.956 74.386 16.610 1.00 24.21 2365 CA ALA C 151-14.427 75. 397 17.521 1.00 25.60 2366 CB ALA C 151-15.113 76.737 17.266 1. 00 22.07 2367 C ALA C 151-14.576 75.000 18.989 1.00 27.79 2368 O ALA C 151-15.586 74.412 19. 387 1.00 26.25 2369 N ASP C 152-13.556 75. 323 19.782 1.00 28. 59 2370 CA ASP C 152-13.544 75.027 21.215 1.00 30.99 2371 CB ASP C 152-12.138 74.616 21.648 1. 00 30. 25 2372 CG ASP C 152-12.072 74.196 23.105 1.00 32.23 2373 OD1 ASP C 152-13.076 74. 372 23.835 1.00 31. 62 1 2 3 4 5 6 7 8 9 10 2374 OD2 ASP C 152-11.004 73.696 23.521 1.00 33.28 2375 C ASP C 152-13.966 76.293 21.969 1.00 33.85 2376 O ASP C 152-13.160 77. 206 22.160 1.00 33.51 2377 N SER C 153-15.223 76.337 22.400 1. 00 35. 88 2378 CA SER C 153-15.761 77.503 23.097 1.00 39.66 2379 CB SER C 153-17.273 77.348 23.274 1.00 40.81 2380 OG SER C 153-17. 574 76.192 24.035 1. 00 44.96 2381 C SER C 153-15.134 77.842 24.448 1.00 40.68 2382 O SER C 153-15.319 78.949 24.952 1.00 41.68 2383 N GLU C 154-14.402 76.907 25.043 1.00 42.48 2384 CA GLU C 154-13.786 77.178 26.337 1.00 44. 39 2385 CB GLU C 154-14.141 76.068 27.335 1.00 45.86 2386 CG GLU C 154-13.897 74.657 26.849 1.00 49. 31 2387 CD GLU C 154-14.551 73.620 27.753 1.00 51.48 2388 OE1 GLU C 154-14.214 73.577 28.956 1.00 51.40 2389 OE2 GLU C 154-15.406 72.854 27.260 1.00 51.74 2390 C GLU C 154-12.276 77. 385 26.273 1.00 44.21 2391 O GLU C 154-11.544 77.031 27.196 1.00 44.78 2392 N THR C 155-11.822 77.978 25.174 1.00 43. 90 2393 CA THR C 155-10.408 78.270 24.962 1.00 42.12 2394 CB THR C 155-9.698 77.117 24.224 1.00 43. 32 2395 OG1 THR C 155-9.874 75.900 24.958 1.00 44.96 2396 CG2 THR C 155-8.208 77.408 24.083 1.00 42.65 2397 C THR C 155-10.310 79.535 24.110 1.00 40.69 2398 O THR C 155-11. 073 79.714 23.159 1.00 39.86 2399 N PRO C 156-9.378 80.439 24.449 1.00 39. 46 2400 CD PRO C 156-8.473 80.433 25.613 1. 00 39.60 2401 CA PRO C 156-9.227 81.676 23.675 1.00 37.95 2402 CB PRO C 156-8.403 82.559 24.606 1.00 39. 48 2403 CG PRO C 156-7.512 81.562 25.285 1.00 40. 38 2404 C PRO C 156-8.527 81.429 22.341 1.00 35.69 2405 O PRO C 156-7. 756 80.478 22.208 1.00 33. 71 2406 N THR C 157-8. 803 82.280 21.354 1.00 33.91 1 2 3 4 5 6 7 8 9 10 2407 CA THR C 157-8.173 82.145 20.042 1.00 32. 30 2408 CB THR C 157-8.632 83.248 19.075 1.00 32.45 2409 OG1 THR C 157-8.323 84.530 19. 633 1.00 32. 86 2410 CG2 THR C 157-10. 128 83.150 18.822 1.00 31.38 2411 C THR C 157-6.662 82.260 20. 208 1.00 32.36 2412 O THR C 157-6.181 82. 841 21.182 1.00 31.83 2413 N ILE C 158-5.917 81.704 19.261 1.00 31.09 2414 CA ILE C 158-4. 466 81.757 19.317 1.00 31.40 2415 CB ILE C 158-3.848 80.414 18.861 1.00 33.03 2416 CG2 ILE C 158-2.322 80.491 18.901 1.00 32.49 2417 CG1 ILE C 158-4. 377 79.285 19.754 1.00 34. 48 2418 CD1 ILE C 158-3.626 77.976 19.625 1.00 37.11 2419 C ILE C 158-3. 947 82.886 18.430 1.00 31.52 2420 O ILE C 158-4.329 82.994 17.268 1.00 29.85 2421 N GLN C 159-3.090 83.734 18.994 1.00 30.88 2422 CA GLN C 159-2.515 84.858 18.260 1.00 31. 31 2423 CB GLN C 159-2.483 86.109 19.145 1.00 30.29 2424 CG GLN C 159-3.847 86.583 19.618 1.00 28.47 2425 CD GLN C 159-4.777 86.939 18.469 1.00 29.78 2426 OE1 GLN C 159-4.426 87.732 17.596 1.00 29.07 2427 NE2 GLN C 159-5.977 86.356 18.471 1.00 28. 38 2428 C GLN C 159-1.099 84.498 17.818 1.00 32.51 2429 O GLN C 159-0.205 84. 340 18.645 1.00 33.85 2430 N LYS C 160-0.898 84. 372 16.512 1.00 33.71 2431 CA LYS C 160 0.408 84.004 15.976 1.00 35.34 2432 CB LYS C 160 0.482 82.489 15.782 1.00 39.09 2433 CG LYS C 160 0.861 81.709 17.020 1.00 45.00 2434 CD LYS C 160 2.363 81.723 17.226 1.00 48.90 2435 CE LYS C 160 3.070 81.072 16.048 1.00 51.33 2436 NZ LYS C 160 2.571 79.688 15.822 1.00 53.57 2437 C LYS C 160 0.724 84.684 14.654 1.00 34.04 2438 O LYS C 160-0.071 84.630 13.715 1.00 33.20 2439 N GLY C 161 1.897 85. 309 14.586 1. 00 33. 33 1 2 3 4 5 6 7 8 9 10 2440 CA GLY C 161 2. 324 85.987 13. 375 1.00 31.56 2441 C GLY C 161 1. 304 86.955 12.809 1.00 31.25 2442 O GLY C 161 1. 174 87.076 11.590 1. 00 31.41 2443 N SER C 162 0.584 87.642 13.692 1.00 29.97 2444 CA SER C 162-0.438 88.612 13. 301 1.00 30.61 2445 CB SER C 162 0.132 89.591 12.269 1.00 33.50 2446 OG SER C 162 1.271 90.255 12.795 1.00 34.79 2447 C SER C 162-1.724 87.974 12.762 1.00 30.14 2448 O SER C 162-2.579 88.662 12.196 1.00 29.18 2449 N TYR C 163-1.848 86.661 12.938 1.00 28.35 2450 CA TYR C 163 -3.038 85.919 12.513 1.00 28.16 2451 CB TYR C 163 -2.662 84.617 11.794 1.00 31.99 2452 CG TYR C 163 -2.127 84.731 10.386 1.00 37.36 2453 CD1 TYR C 163-2.929 85.198 9.347 1.00 39.91 2454 CE1 TYR C 163-2.458 85.236 8.034 1.00 42.98 2455 CD2 TYR C 163-0.833 84. 307 10.082 1.00 40.52 2456 CE2 TYR C 163-0. 351 84.338 8.774 1.00 44.48 2457 CZ TYR C 163-1.169 84.804 7.756 1.00 44.95 2458 OH TYR C 163-0.698 84.838 6.463 1.00 48.66 2459 C TYR C 163-3.811 85.506 13.762 1.00 26.15 2460 O TYR C 163-3.244 85.419 14.852 1.00 23.72 2461 N THR C 164-5.103 85.242 13.598 1.00 23. 19 2462 CA THR C 164-5.923 84.758 14.697 1.00 21. 37 2463 CB THR C 164-7.226 85.562 14.855 1.00 21.52 2464 OG1 THR C 164-6.928 86.868 15.360 1.00 23.59 2465 CG2 THR C 164-8.167 84.858 15.824 1.00 22.30 2466 C THR C 164-6.280 83.315 14.342 1.00 21.64 2467 O THR C 164-6.834 83.055 13. 274 1.00 21.59 2468 N PHE C 165-5.950 82.374 15.217 1.00 21.13 2469 CA PHE C 165-6.266 80.980 14.941 1.00 21.47 2470 CB PHE C 165-5.006 80.105 15.020 1.00 21.90 2471 CG PHE C 165-3.989 80.403 13.947 1.00 22.63 2472 CD1 PHE C 165-2. 967 81.323 14.169 1. 00 22. 99 1 2 3 4 5 6 7 8 9 10 2473 CD2 PHE C 165-4.054 79.763 12.713 1.00 22. 11 2474 CE1 PHE C 165-2.024 81.605 13.172 1.00 23.00 2475 CE2 PHE C 165-3.117 80.036 11. 708 1.00 24. 82 2476 CZ PHE C 165-2.099 80.956 11.941 1.00 24.26 2477 C PHE C 165-7. 325 80. 430 15.887 1.00 22. 14 2478 O PHE C 165-7.192 80.510 17.109 1.00 22.59 2479 N VAL C 166-8.388 79.888 15.306 1. 00 22. 66 2480 CA VAL C 166-9.469 79.294 16.079 1. 00 22.68 2481 CB VAL C 166-10.632 78.852 15.151 1.00 23.36 2482 CG1 VAL C 166-11.742 78.182 15.968 1.00 22.78 2483 CG2 VAL C 166-11.176 80.049 14.390 1.00 22. 28 2484 C VAL C 166-8.933 78.053 16.791 1.00 22.99 2485 O VAL C 166-8.213 77.251 16.191 1. 00 24.89 2486 N PRO C 167-9.248 77.890 18.087 1.00 23.05 2487 CD PRO C 167-9.883 78.858 19.000 1.00 23.87 2488 CA PRO C 167-8.775 76.711 18.823 1.00 24. 30 2489 CB PRO C 167-8.852 77.167 20.277 1.00 22.94 2490 CG PRO C 167-10.055 78.046 20.272 1.00 23.93 2491 C PRO C 167-9.739 75.557 18.502 1.00 23.40 2492 O PRO C 167-10.947 75.689 18.684 1.00 24.02 2493 N TRP C 168-9.201 74.439 18.024 1.00 24.13 2494 CA TRP C 168-10.022 73. 294 17. 626 1.00 24.82 2495 CB TRP C 168-9.516 72.725 16.293 1.00 22. 36 2496 CG TRP C 168-9.455 73.699 15.166 1.00 19.87 2497 CD2 TRP C 168-10.563 74.349 14.525 1.00 18.75 2498 CE2 TRP C 168-10.033 75.157 13.494 1.00 18.06 2499 CE3 TRP C 168-11.953 74.325 14.720 1.00 19.37 2500 CD1 TRP C 168-8.332 74.130 14.518 1.00 18.95 2501 NE1 TRP C 168-8.671 75.004 13.513 1.00 18.69 2502 CZ2 TRP C 168-10.841 75.939 12.662 1.00 17.25 2503 CZ3 TRP C 168-12.761 75.105 13.890 1.00 18. 55 2504 CH2 TRP C 168-12.201 75.899 12.875 1.00 20.02 2505 C TRP C 168-10.139 72.116 18. 591 1. 00 26.48 1 2 3 4 5 6 7 8 9 10 2506 O TRP C 168-9.239 71.838 19. 384 1.00 26.97 2507 N LEU C 169-11.266 71.419 18.478 1.00 27.81 2508 CA LEU C 169-11. 556 70.215 19.248 1.00 28.55 2509 CB LEU C 169-12.741 70. 426 20.193 1.00 32.61 2510 CG LEU C 169-12.466 71.072 21.551 1.00 36.30 2511 CD1 LEU C 169-13.779 71.220 22.302 1.00 36.58 2512 CD2 LEU C 169-11.482 70.214 22. 345 1.00 35.93 2513 C LEU C 169-11.931 69.152 18.220 1.00 28.04 2514 O LEU C 169-12.611 69.449 17.240 1.00 24.92 2515 N LEU C 170-11.486 67.921 18.432 1.00 28.25 2516 CA LEU C 170-11.808 66.848 17.501 1.00 30. 42 2517 CB LEU C 170-10.935 65.622 17.771 1.00 31.59 2518 CG LEU C 170-11.175 64.445 16.820 1.00 33. 37 2519 CD1 LEU C 170-10.696 64.818 15.419 1.00 31.97 2520 CD2 LEU C 170-10.435 63.215 17. 321 1.00 34. 80 2521 C LEU C 170-13.272 66. 458 17.645 1.00 31. 87 2522 O LEU C 170-13.716 66.107 18.736 1.00 33.66 2523 N SER C 171-14.023 66.535 16.552 1.00 31.78 2524 CA SER C 171-15.434 66.159 16.566 1.00 31. 56 2525 CB SER C 171-16.185 66.902 15.462 1.00 33.33 2526 OG SER C 171-17. 564 66.594 15.488 1.00 37.94 2527 C SER C 171-15.499 64.644 16. 342 1.00 30.61 2528 O SER C 171-16.204 63.919 17.047 1.00 30.95 2529 N PHE C 172-14.755 64.175 15. 349 1.00 28.51 2530 CA PHE C 172-14.667 62.752 15.049 1.00 26.29 2531 CB PHE C 172-15.997 62.203 14.498 1.00 27.04 2532 CG PHE C 172-16. 393 62.763 13.159 1.00 28.14 2533 CD1 PHE C 172-15.769 62.332 11.992 1.00 28.55 2534 CD2 PHE C 172-17.389 63.726 13.068 1. 00 30.00 2535 CE1 PHE C 172-16.139 62.850 10.754 1.00 30.13 2536 CE2 PHE C 172-17.763 64.248 11.833 1. 00 29.56 2537 CZ PHE C 172-17.133 63.809 10.678 1.00 29.04 2538 C PHE C 172-13.537 62. 537 14.059 1.00 25. 38 1 2 3 4 5 6 7 8 9 10 2539 O PHE C 172-13.145 63.453 13. 332 1.00 24.15 2540 N LYS C 173-13. 008 61.322 14.060 1.00 24.70 2541 CA LYS C 173-11.914 60.927 13. 188 1.00 26. 00 2542 CB LYS C 173-10.601 60.908 13.977 1.00 27.76 2543 CG LYS C 173-9.414 60.324 13.238 1.00 31.52 2544 CD LYS C 173-8.158 60. 426 14.093 1.00 35. 39 2545 CE LYS C 173-7.016 59.613 13.512 1.00 38.16 2546 NZ LYS C 173-7.307 58.150 13.547 1.00 42. 35 2547 C LYS C 173-12.237 59.532 12.676 1.00 26.43 2548 O LYS C 173-12.669 58.666 13.439 1.00 26.87 2549 N ARG C 174-12.037 59.316 11.385 1.00 25.96 2550 CA ARG C 174-12. 324 58.020 10.789 1.00 27. 30 2551 CB ARG C 174-13.544 58.141 9.879 1.00 28. 10 2552 CG ARG C 174-14.047 56.836 9.310 1.00 31. 38 2553 CD ARG C 174-15.049 57.108 8.202 1.00 32.26 2554 NE ARG C 174-15. 746 55.898 7.788 1.00 35.79 2555 CZ ARG C 174-16. 397 55.772 6.638 1.00 36.38 2556 NH1 ARG C 174-16.435 56.783 5.779 1. 00 35.94 2557 NH2 ARG C 174-17.017 54.635 6.349 1.00 39.63 2558 C ARG C 174-11.122 57.564 9.981 1.00 26.25 2559 O ARG C 174-10.679 58.266 9.079 1.00 25.13 2560 N GLY C 175-10.586 56. 393 10.308 1.00 26. 09 2561 CA GLY C 175-9.437 55.891 9.572 1.00 26.87 2562 C GLY C 175-8.103 56.434 10.058 1.00, 28.00 2563 O GLY C 175-8.005 56.952 11.172 1.00 29.61 2564 N SER C 176-7.078 56. 342 9.216 1.00 27.76 2565 CA SER C 176-5.742 56.790 9.603 1.00 29.17 2566 CB SER C 176-4.836 55.566 9.771 1.00 31. 26 2567 OG SER C 176-4.766 54.827 8.558 1.00 33. 30 2568 C SER C 176-5.048 57.789 8.674 1.00 27.80 2569 O SER C 176-3.946 58.247 8.978 1. 00 28.24 2570 N ALA C 177-5.675 58.129 7.554 1.00 25.07 2571 CA ALA C 177-5.065 59.062 6.606 1.00 24.00 1 2 3 4 5 6 7 8 9 10 2572 CB ALA C 177-5. 864 59.079 5.309 1.00 25.77 2573 C ALA C 177-4.918 60.491 7.129 1.00 23.06 2574 O ALA C 177-4. 053 61.237 6.667 1.00 22.82 2575 N LEU C 178-5.757 60.861 8.091 1.00 21.09 2576 CA LEU C 178-5.754 62.208 8.656 1.00 23.36 2577 CB LEU C 178-7.007 62.955 8.196 1.00 21.51 2578 CG LEU C 178-7.150 63.178 6.688 1.00 21.31 2579 CD1 LEU C 178-8.598 63.529 6. 344 1.00 19. 54 2580 CD2 LEU C 178-6. 199 64.297 6.249 1.00 18.75 2581 C LEU C 178-5.714 62.202 10.181 1.00 25.04 2582 O LEU C 178-6.423 61.428 10.823 1.00 25.52 2583 N GLU C 179-4.891 63.079 10.751 1.00 26. 37 2584 CA GLU C 179-4. 742 63.200 12.205 1.00 28.13 2585 CB GLU C 179-3.414 62.589 12. 665 1.00 29.44 2586 CG GLU C 179-3. 354 61.082 12.728 1.00 35.31 2587 CD GLU C 179-1.962 60.589 13.096 1.00 37.53 2588 OE1 GLU C 179-1.250 61. 315 13.824 1.00 36.85 2589 OE2 GLU C 179-1.581 59.479 12. 669 1.00 39.76 2590 C GLU C 179-4.739 64.664 12.631 1.00 27.39 2591 O GLU C 179-4.444 65. 547 11.833 1.00 26.91 2592 N GLU C 180-5.069 64.919 13.891 1.00 27.88 2593 CA GLU C 180-5.039 66.281 14.405 1.00 29.45 2594 CB GLU C 180-6.182 66.538 15. 388 1.00 31.28 2595 CG GLU C 180-6.027 67.859 16.149 1.00 36.96 2596 CD GLU C 180-7.135 68.110 17.160 1.00 40.47 2597 OE1 GLU C 180-7.522 67.162 17.876 1.00 43. 37 2598 OE2 GLU C 180-7.611 69.262 17.249 1.00 41.60 2599 C GLU C 180-3.708 66.432 15.130 1.00 30.11 2600 O GLU C 180-3.357 65.597 15.960 1.00 29.51 2601 N LYS C 181-2.961 67.482 14.808 1. 00 30. 43 2602 CA LYS C 181-1.672 67.715 15.447 1.00 31.45 2603 CB LYS C 181-0.539 67.116 14.609 1.00 34.57 2604 CG LYS C 181 0. 854 67. 381 15. 170 1. 00 38.18 1 2 3 4 5 6 7 8 9 10 2605 CD LYS C 181 1.941 66.955 14. 192 1. 00 42.02 2606 CE LYS C 181 3. 326 67.295 14.722 1. 00 44. 31 2607 NZ LYS C 181 4. 397 67.032 13.715 1.00 47. 89 2608 C LYS C 181-1. 415 69.202 15.644 1.00 30.67 2609 O LYS C 181-1. 388 69.969 14. 682 1.00 27.98 2610 N GLU C 182-1.234 69.596 16.900 1.00 30.71 2611 CA GLU C 182-0.965 70.986 17.250 1.00 31. 37 2612 CB GLU C 182 0.484 71.325 16.898 1.00 34.80 2613 CG GLU C 182 1.491 70.373 17.536 1.00 42.05 2614 CD GLU C 182 2.919 70.675 17.127 1.00 46.18 2615 OEI GLU C 182 3.186 70.742 15.905 1.00 49. 41 2616 OE2 GLU C 182 3.774 70.841 18.023 1.00 48.48 2617 C GLU C 182-1.917 71.971 16.573 1.00 29.11 2618 O GLU C 182-1. 486 72.956 15. 963 1.00 28.38 2619 N ASN C 183-3.211 71.690 16.688 1. 00 26.31 2620 CA ASN C 183-4.265 72.533 16.123 1.00 25.24 2621 CB ASN C 183-4.184 73.949 16.720 1.00 23.91 2622 CG ASN C 183-5.542 74.638 16. 783 1.00 25.29 2623 OD1 ASN C 183-6.485 74.120 17. 389 1.00 22.62 2624 ND2 ASN C 183-5.646 75.809 16.163 1.00 22.08 2625 C ASN C 183-4. 256 72.603 14.594 1.00 23.24 2626 O ASN C 183-4.746 73.565 14.006 1.00 24.44 2627 N LYS C 184-3.693 71.581 13.960 1.00 23.14 2628 CA LYS C 184-3.648 71.497 12.504 1.00 22.95 2629 CB LYS C 184-2.231 71.739 11.974 1. 00 24.03 2630 CG LYS C 184-1.564 73.012 12.459 1.00 27.12 2631 CD LYS C 184-0.266 73.241 11.707 1.00 30.20 2632 CE LYS C 184 0.787 73.880 12.588 1. 00 33.25 2633 NZ LYS C 184 1.187 72.953 13.679 1.00 37.09 2634 C LYS C 184-4.075 70.093 12.082 1.00 21.90 2635 O LYS C 184-4. 142 69.180 12.907 1.00 20.83 2636 N ILE C 185-4.364 69.929 10.796 1.00 19.65 2637 CA ILE C 185-4. 732 68. 622 10.263 1. 00 20. 48 1 2 3 4 5 6 7 8 9 10 2638 CB ILE C 185-5.910 68.728 9.264 1.00 20.04 2639 CG2 ILE C 185-6.173 67. 374 8.613 1. 00 19.68 2640 CG1 ILE C 185-7.166 69.215 9.999 1.00 19.21 2641 CDI ILE C 185-8.389 69. 367 9.113 1. 00 20. 52 2642 C ILE C 185-3.485 68.096 9.550 1.00 21.73 2643 O ILE C 185-2.985 68.718 8.612 1.00 23.86 2644 N LEU C 186-2.973 66.963 10.018 1.00 22.16 2645 CA LEU C 186-1.774 66. 358 9.441 1.00 22.63 2646 CB LEU C 186-0.873 65.813 10. 558 1.00 21.90 2647 CG LEU C 186 0.289 64.905 10.137 1.00 24.48 2648 CD1 LEU C 186 1.322 65.711 9.365 1.00 22.49 2649 CD2 LEU C 186 0.921 64.273 11.. 381 1.00 25.09 2650 C LEU C 186-2.135 65.227 8.480 1.00 21.90 2651 O LEU C 186-2.954 64. 368 8.802 1.00 21. 39 2652 N VAL C 187-1.514 65.239 7.306 1.00 21.17 2653 CA VAL C 187-1.751 64.225 6.287 1.00 22.09 2654 CB VAL C 187-1.579 64.825 4.871 1.00 21.91 2655, CG1 VAL C 187-1.846 63.769 3.810 1.00 21.55 2656 CG2 VAL C 187-2.515 66.014 4.701 1.00 20.91 2657 C VAL C 187-0.765 63.072 6.477 1. 00 22.98 2658 O VAL C 187 0.449 63.274 6.456 1.00 21.73 2659 N LYS C 188-1.297 61.868 6.671 1.00 22.97 2660 CA LYS C 188-0.476 60.676 6.878 1.00 25.37 2661 CB LYS C 188 -1.067 59.820 8.003 1.00 24.90 2662 CG LYS C 188 -1.235 60.541 9.326 1.00 27.75 2663 CD LYS C 188 0.101 61.006 9.888 1.00 31.67 2664 CE LYS C 188 1.005 59.828 10.240 1.00 35.13 2665 NZ LYS C 188 2.281 60.292 10.860 1.00 38.20 2666 C LYS C 188-0.360 59.825 5.613 1.00 26.93 2667 O LYS C 188 0.490 58.936 5.531 1.00 27.32 2668 N GLU C 189-1.225 60.090 4. 636 1.00 25.34 2669 CA GLU C 189-1.226 59. 347 3. 377 1.00 25.74 2670 CB GLU C 189-2.356 58. 308 3.369 1.00 28.08 1 2 3 4 5 6 7 8 9 10 2671 CG GLU C 189-2. 132 57.103 4.272 1.00 33.12 2672 CD GLU C 189-3.403 56.296 4.500 1.00 35.81 2673 OE1 GLU C 189-4. 206 56.156 3.551 1.00 36.59 2674 OE2 GLU C 189-3.595 55.792 5.628 1.00 36.85 2675 C GLU C 189-1.416 60.292 2.198 1.00 25.18 2676 O GLU C 189-2.296 61.151 2.221 1.00 25.69 2677 N THR C 190-0.592 60.129 1.169 1.00 23.23 2678 CA THR C 190-0.686 60.965-0. 019 1.00 23.58 2679 CB THR C 190 0.530 60.737-0. 940 1.00 23.41 2680 OG1 THR C 190 1.725 61.101-0. 237 1.00 24.45 2681 CG2 THR C 190 0. 422 61.577-2. 204 1.00 24.04 2682 C THR C 190-1.976 60.636-0. 769 1.00 23.44 2683 O THR C 190-2. 367 59.475-0. 854 1.00 24.48 2684 N GLY C 191-2.643 61.662-1. 295 1.00 22.93 2685 CA GLY C 191-3.882 61.441-2. 027 1.00 21.06 2686 C GLY C 191-4.671 62.715-2. 277 1.00 20.64 2687 O GLY C 191-4.186 63.819-2. 016 1.00 19.34 2688 N TYR C 192-5.888 62.562-2. 791 1.00 19.61 2689 CA TYR C 192-6.762 63. 701-3. 073 1.00 19.63 2690 CB TYR C 192-7.542 63.462-4. 373 1.00 19.81 2691 CG TYR C 192-6.721 63.657-5. 630 1.00 21.94 2692 CD1 TYR C 192-6.713 64.885-6. 298 1.00 23.99 2693 E1 TYR C 192-5.958 65.072-7. 457 1.00 23. 67 2694 CD2 TYR C 192-5. 949 62.620-6. 151 1.00 22.56 2695 CE2 TYR C 192-5.187 62. 798-7. 309 1.00 24.48 2696 CZ TYR C 192-5.198 64.025-7. 954 1.00 24.26 2697 OH TYR C 192-4.448 64.205-9. 089 1.00 27. 88 2698 C TYR C 192-7.732 63.869-1. 908 1.00 20.10 2699 O TYR C 192-8.336 62.889-1. 455 1.00 19.80 2700 N PHE C 193-7.875 65.104-1. 424 1.00 17. 36 2701 CA PHE C 193-8.758 65.388-0. 298 1.00 17. 33 2702 CB PHE C 193-7. 944 65.748 0.957 1.00 18. 76 2703 CG PHE C 193-7. 016 64.654 1.430 1.00 20. 21 1 2 3 4 5 6 7 8 9 10 2704 CD 1 PHE C 193-5.791 64.438 0.805 1.00 19.90 2705 CD2 PHE C 193-7. 362 63.856 2.517 1.00 20.06 2706 CE1 PHE C 193-4.928 63.426 1.242 1.00 20. 31 2707 CE2 PHE C 193-6.508 62.839 2.964 1.00 20.04 2708 CZ PHE C 193-5.287 62.631 2.331 1.00 20.02 2709 C PHE C 193-9.744 66.534-0. 544 1.00 17.55 2710 0 PHE C 193-9.402 67.539-1. 171 1.00 17. 26 2711 N PHE C 194-10.964 66.366-0. 042 1.00 15.25 2712 CA PHE C 194-11.992 67.404-0. 121 1.00 16. 92 2713 CB PHE C 194-13. 395 66.790-0. 189 1.00 16.83 2714 CG PHE C 194-14.507 67.805-0. 126 1.00 17.52 2715 CD1 PHE C 194-14.705 68.705-1. 168 1.00 18.04 2716 CD2 PHE C 194-15.343 67.875 0.987 1.00 19.52 2717 CE1 PHE C 194-15. 723 69. 662-1.109 1.00 21.91 2718 CE2 PHE C 194-16. 366 68.830 1.059 1.00 18.72 2719 CZ PHE C 194-16.552 69.727 0.006 1.00 18.27 2720 C PHE C 194-11.799 68.120 1.216 1.00 16.76 2721 O PHE C 194-11.878 67.489 2. 278 1.00 17. 35 2722 N ILE C 195-11. 531 69.421 1.163 1.00 17.08 2723 CA ILE C 195-11.277 70.215 2.369 1.00 16.43 2724 CB ILE C 195-9.861 70.842 2.288 1.00 17.68 2725 CG2 ILE C 195-9.514 71.549 3. 598 1.00 19.90 2726 CG1 ILE C 195-8.834 69.744 1.989 1.00 18.80 2727 CD 1 ILE C 195-7.512 70.264 1.413 1.00 20.64 2728 C ILE C 195-12. 319 71.324 2.511 1.00 15.01 2729 O ILE C 195-12.644 72.001 1.537 1.00 16. 18 2730 N TYR C 196-12.841 71.516 3.719 1.00 14. 64 2731 CA TYR C 196-13.852 72.553 3.934 1.00 15.70 2732 CB TYR C 196-15.253 71.938 3.854 1.00 13.13 2733 CG TYR C 196-15.466 70.812 4.842 1.00 16. 07 2734 CD1 TYR C 196-16.026 71.050 6.102 1.00 17.56 2735 CE1 TYR C 196-16.189 70.010 7. 028 1.00 18.15 2736 CD2 TYR C 196-15.074 69.510 4.531 1.00 17. 51 2 3 4 5 6 7 8 9 10 2737 CE2 TYR C 196-15.229 68.464 5.454 1. 00 18. 40 2738 CZ TYR C 196-15.786 68.726 6.695 1.00 18.54 2739 OH TYR C 196-15.922 67.711 7.610 1.00 21.42 2740 C TYR C 196-13.690 73.280 5.267 1.00 15.35 2741 O TYR C 196-13.152 72.733 6.225 1.00 17.19 2742 N GLY C 197-14.175 74.515 5.319 1.00 15.88 2743 CA GLY C 197-14.091 75.299 6. 539 1.00 16.26 2744 C GLY C 197-15.108 76.428 6.585 1.00 17.06 2745 O GLY C 197-15.378 77.068 5.572 1.00 18. 32 2746 N GLN C 198-15.685 76.663 7.760 1.00 17.42 2747 CA GLN C 198-16.656 77.738 7.937 1.00 16.67 2748 CB GLN C 198-18. 085 77.185 7.969 1.00 17.11 2749 CG GLN C 198 -19.145 78.257 8.212 1.00 18.98 2750 CD GLN C 198 -20.562 77.717 8.127 1.00 20.30 2751 OE1 GLN C 198-20.984 77.217 7.085 1.00 21.51 2752 NE2 GLN C 198-21.303 77.818 9.226 1.00 17.57 2753 C GLN C 198-16. 387 78.482 9.239 1.00 16. 36 2754 O GLN C 198-15.991 77.883 10.233 1. 00 16. 70 2755 N VAL C 199-16.603 79.791 9.227 1.00 16.45 2756 CA VAL C 199-16.402 80.608 10.417 1.00 18. 15 2757 CB VAL C 199-15.046 81. 367 10.366 1.00 17.81 2758 CG1 VAL C 199-14.899 82.264 11.588 1.00 18. 24 2759 CG2 VAL C 199-13.897 80. 383 10.302 1.00 18.95 2760 C VAL C 199-17.517 81.640 10.502 1.00 18.45 2761 O VAL C 199-17.972 82.148 9.479 1.00 20.19 2762 N LEU C 200-17.968 81.939 11.715 1.00 18.97 2763 CA LEU C 200-18.993 82. 960 11.900 1.00 20.02 2764 CB LEU C 200-20.085 82.494 12.876 1.00 18.18 2765 CG LEU C 200-21.057 83.607 13. 313 1. 00 21. 23 2766 CD1 LEU C 200-21.612 84. 320 12.081 1.00 22.02 2767 CD2 LEU C 200-22.193 83.031 14.144 1.00 21.05 2768 C LEU C 200-18.306 84.207 12.455 1.00 22. 85 2769 0LEU C 200-17.735 84.177 13.549 1.00 22. 26 2 3 4-5 6 7 8 9 10 2770 N TYR C 201-18.352 85.291 11.685 1.00 23.52 2771 CA TYR C 201-17.734 86.546 12. 086 1.00 26. 15 2772 CB TYR C 201-17. 079 87.231 10.882 1.00 25.69 2773 CG TYR C 201-15.974 86.410 10.262 1.00 26.64 2774 CD1 TYR C 201-16.228 85.551 9.187 1.00 27.69 2775 CE1 TYR C 201-15.218 84.743 8.657 1.00 26.11 2776 CD2 TYR C 201-14. 686 86.445 10.788 1. 00 25.24 2777 CE2 TYR C 201-13.676 85.645 10.270 1. 00 26. 39 2778 CZ TYR C 201-13.944 84.796 9.208 1. 00 26. 17 2779 OH TYR C 201-12.938 83.990 8.720 1.00 26.84 2780 C TYR C 201-18. 758 87.476 12.713 1.00 29. 30 2781 O TYR C 201-19. 885 87.602 12.224 1.00 27. 35 2782 N THR C 202-18. 351 88.125 13.799 1.00 32.47 2783 CA THR C 202-19.212 89.053 14.527 1.00 36.58 2784 CB THR C 202-19.573 88.475 15.904 1.00 35.69 2785 OG1 THR C 202-18.374 88.242 16.652 1.00 34.60 2786 CG2 THR C 202-20.308 87.153 15.745 1.00 36.28 2787 C THR C 202-18.464 90.373 14.714 1.00 39.92 2788 O THR C 202-18.713 91.122 15.656 1.00 40.44 2789 N ASP C 203-17.551 90.639 13.787 1.00 43.93 2790 CA ASP C 203-16.708 91.830 13.794 1.00 47.69 2791 CB ASP C 203-15.325 91.439 13.263 1.00 50.72 2792 CG ASP C 203-14.241 92.412 13.665 1.00 52.69 2793 OD1 ASP C 203-14. 368 93.612 13. 342 1.00 54. 57 2794 OD2 ASP C 203-13.257 91.969 14.298 1.00 53.59 2795 C ASP C 203-17. 328 92.916 12.909 1.00 48.35 2796 O ASP C 203-17.999 92.610 11.926 1.00 47.70 2797 N LYS C 204-17.103 94.181 13.250 1.00 49.76 2798 CA LYS C 204-17.656 95.278 12.458 1.00 52.02 2799 CB LYS C 204-17.981 96.479 13.357 1.00 54.30 2800 CG LYS C 204-18.911 96.154 14.517 1.00 57.73 2801 CD LYS C 204-19. 581 97.407 15.075 1. 00 60. 40 2802 CE LYS C 204-18. 570 98. 462 15. 507 1. 00 62. 00 1 2 3 4 5 6 7 8 9 10 2803 NZ LYS C 204-19.244 99.705 15.979 1.00 64.12 2804 C LYS C 204-16.739 95.727 11.316 1.00 51.83 2805 O LYS C 204-17.110 96.600 10.531 1.00 51.41 2806 N THR C 205-15. 551 95.130 11. 220 1. 00 53.23 2807 CA THR C 205-14.598 95.473 10.160 1.00 54.07 2808 CB THR C 205-13.337 94.579 10.209 1.00 54. 93 2809 OG1 THR C 205-12.679 94.740 11.473 1.00 56.03 2810 CG2 THR C 205-12. 375 94.962 9.089 1.00 54.87 2811 C THR C 205-15.252 95.304 8.790 1.00 53.69 2812 O THR C 205-15.912 94.297 8.530 1. 00 54. 24 2813 N TYR C 206-15.045 96.285 7.918 1.00 52.25 2814 CA TYR C 206-15. 635 96.281 6.581 1.00 52. 11 2815 CB TYR C 206-14.936 97.327 5.698 1.00 55.41 2816 CG TYR C 206-13.599 96.906 5.126 1.00 58.55 2817 CD1 TYR C 206-13.525 96.197 3.927 1.00 59.22 2818 CE1 TYR C 206-12.299 95.820 3. 387 1.00 62.07 2819 CD2 TYR C 206-12.408 97.229 5.776 1.00 60.90 2820 CE2 TYR C 206-11.173 96.856 5.246 1.00 62.09 2821 CZ TYR C 206-11.127 96.154 4.051 1.00 62.94 2822 OH TYR C 206-9.909 95.787 3.521 1.00 64.59 2823 C TYR C 206-15.661 94.920 5.873 1.00 48. 75 2824 O TYR C 206-16.591 94.641 5.111 1.00 47.86 2825 N ALA C 207-14.654 94.082 6.121 1.00 43.92 2826 CA ALA C 207-14.593 92.755 5.501 1.00 39.88 2827 CB ALA C 207-14.006 92.859 4.098 1.00 39. 66 2828 C ALA C 207-13.784 91.755 6.337 1.00 37.22 2829 O ALA C 207-12.671 92.053 6.771 1.00 35.06 2830 N MET C 208-14. 352 90.571 6.557 1.00 33.90 2831 CA MET C 208-13.694 89.520 7.338 1.00 30.86 2832 CB MET C 208-14.450 89.275 8.647 1.00 30.71 2833 CG MET C 208-14. 549 90.480 9.566 1.00 35.28 2834 SD MET C 208-12.923 91.055 10.102 1.00 38.99 2835 CE MET C 208-12.501 89.813 11.317 1.00 37. 31 1 2 3 4 5 6 7 8 9 10 2836 C MET C 208-13.650 88.212 6.544 1.00 29.34 2837 O MET C 208-14. 509 87.963 5.698 1.00 27.64 2838 N GLY C 209-12. 657 87.376 6.829 1.00 27.18 2839 CA GLY C 209-12.548 86.108 6.127 1.00 26.66 2840 C GLY C 209-11.429 85.243 6.668 1.00 25.61 2841 O GLY C 209-10.675 85.674 7.540 1. 00 25.83 2842 N HIS C 210-11. 324 84.019 6.159 1.00 22.15 2843 CA HIS C 210-10.278 83.110 6.598 1.00 20.62 2844 CB HIS C 210-10.840 82.028 7.527 1.00 20.82 2845 CG HIS C 210-11.993 81.263 6.952 1.00 22.88 2846 CD2 HIS C 210-12.043 80.064 6.322 1.00 22.62 2847 ND1 HIS C 210-13.293 81.718 7.013 1.00 23.93 2848 CE1 HIS C 210-14.095 80.830 6.451 1.00 22.89 2849 NE2 HIS C 210-13. 362 79.817 6.024 1.00 23.10 2850 C HIS C 210-9.579 82.457 5.419 1.00 18.69 2851 O HIS C 210-10.064 82.501 4.288 1.00 18.57 2852 N LEU C 211-8.433 81.851 5.702 1.00 18. 71 2853 CA LEU C 211-7.634 81.178 4.690 1.00 19. 36 2854 CB LEU C 211-6.254 81.838 4.593 1.00 21. 36 2855 CG LEU C 211-6.147 83.370 4.548 1.00 23.44 2856 CD1 LEU C 211-4.685 83.788 4.691 1.00 23.81 2857 CD2 LEU C 211-6.723 83.886 3.243 1.00 23. 40 2858 C LEU C 211-7.430 79.714 5.084 1.00 21. 03 2859 0 LEU C 211-7.153 79.418 6.248 1.00 20.99 2860 N ILE C 212-7.596 78.803 4.127 1.00 19.86 2861 CA ILE C 212-7. 325 77.392 4.384 1.00 20.51 2862 CB ILE C 212-8.280 76.439 3.625 1.00 23.01 2863 CG2 ILE C 212-7.888 74.993 3.900 1.00 22.02 2864 CG1 ILE C 212 -9.729 76-675 4.068 1.00 24.25 2865 CD1 ILE C 212 -9.966 76.452 5.529 1.00 27.96 2866 C ILE C 212-5.925 77.285 3.788 1.00 19. 53 2867 0 ILE C 212-5.757 77.394 2.577 1.00 19.31 2868 N GLN C 213-4.928 77.106 4.647 1.00 18.67 1 2 3 4 5 6 7 8 9 10 2869 CA GLN C 213-3. 534 77.050 4.219 1. 00 20. 10 2870 CB GLN C 213-2.683 77.992 5.076 1.00 18.95 2871 CG GLN C 213-3. 217 79.403 5.192 1.00 22.27 2872 CD GLN C 213-2. 373 80.259 6.116 1.00 23.26 2873 OE1 GLN C 213-2.194 79.935 7.290 1.00 26.88 2874 NE2 GLN C 213-1.850 81. 355 5.591 1.00 27.50 2875 C GLN C 213-2.909 75.671 4.290 1.00 19.08 2876 O GLN C 213-3.296 74.838 5.104 1. 00 19.65 2877 N ARG C 214-1. 914 75.461 3.436 1.00 18.27 2878 CA ARG C 214-1.185 74.203 3.373 1.00 18.94 2879 CB ARG C 214-1.291 73.620 1.965 1.00 19.55 2880 CG ARG C 214-0.441 72. 379 1.708 1.00 20.93 2881 CD ARG C 214-0.328 72.133 0.214 1.00 20.81 2882 NE ARG C 214 0.378 70.894-0. 091 1.00 25.98 2883 CZ ARG C 214 0.728 70.514-1. 315 1.00 27.30 2884 NH1 ARG C 214 0.438 71. 281-2. 360 1.00 28.19 2885 NH2 ARG C 214 1. 371 69.367-1. 495 1.00 27.67 2886 C ARG C 214 0.287 74.456 3. 701 1.00 18.81 2887 O ARG C 214 0.928 75.296 3.075 1.00 16.78 2888 N LYS C 215 0.803 73.746 4.697 1.00 19. 84 2889 CA LYS C 215 2.212 73.855 5.071 1.00 22.15 2890 CB LYS C 215 2. 381 73.712 6.587 1.00 24.72 2891 CG LYS C 215 3.828 73.836 7.072 1.00 29.14 2892 CD LYS C 215 4. 389 75.224 6. 805 1.00 32. 20 2893 CE LYS C 215 5.788 75.392 7.404 1.00 37. 21 2894 NZ LYS C 215 6.300 76.798 7.257 1.00 38. 46 2895 C LYS C 215 2.867 72.678 4.350 1.00 21.24 2896 O LYS C 215 2.741 71.536 4.778 1.00 22. 58 2897 N LYS C 216 3.543 72.964 3.242 1.00 20.88 2898 CA LYS C 216 4.180 71.934 2.430 1.00 22.90 2899 CB LYS C 216 4.592 72.520 1.072 1.00 23. 51 2900 CG LYS C 216 3.416 73.054 0.249 1.00 25.50 2901 CD LYS C 216 3.836 73. 490-1.151 1. 00 29. 66 1 2 3 4 5 6 7 8 9 10 2902 CE LYS C 216 4.777 74. 670-1. 111 1.00 32.26 2903 NZ LYS C 216 5.191 75.123-2. 468 1.00 32.90 2904 C LYS C 216 5. 383 71.265 3.078 1.00 24.16 2905 O LYS C 216 6.191 71.918 3.734 1.00 24.88 2906 N VAL C 217 5.491 69.956 2.876 1.00 24.57 2907 CA VAL C 217 6.593 69.175 3.422 1.00 27.25 2908 CB VAL C 217 6.152 67.696 3.636 1.00 26. 35 2909 CUL VAL C 217 5.975 66.998 2.296 1.00 26.35 2910 CG2 VAL C 217 7. 154 66.972 4.514 1.00 28.38 2911 C VAL C 217 7.799 69.260 2.466 1.00 27.78 2912 O VAL C 217 8.939 69.020 2.867 1.00 29.48 2913 N HIS C 218 7.535 69.614 1.208 1.00 26.34 2914 CA HIS C 218 8.578 69.767 0.187 1.00 27.30 2915 CB HIS C 218 8.438 68.700-0. 904 1.00 30.37 2916 CG HIS C 218 8.625 67. 300-0. 411 1.00 33. 99 2917 CD2 HIS C 218 9.241 66.815 0.694 1.00 35.15 2918 ND1 HIS C 218 8.151 66.203-1. 096 1.00 35. 32 2919 CE1 HIS C 218 8.463 65. 103-0.435 1. 00 35. 31 2920 NE2 HIS C 218 9.125 65.447 0.655 1.00 37.01 2921 C HIS C 218 8.438 71.146-0. 455 1.00 26.23 2922 O HIS C 218 7. 346 71.529-0. 874 1.00 26.07 2923 N VAL C 219 9.542 71.884-0. 534 1.00 22.56 2924 CA VAL C 219 9.545 73.224-1. 117 1.00 21.86 2925 CB VAL C 219 9.714 74. 305-0.020 1.00 22.19 2926 CG1 VAL C 219 9.661 75.698-0. 634 1.00 23.18 2927 CG2 VAL C 219 8.633 74.140 1.037 1.00 25.18 2928 C VAL C 219 10.703 73.351-2. 103 1.00 22.18 2929 O VAL C 219 11.825 72.955-1. 790 1. 00 19. 54 2930 N PHE C 220 10.434 73.899-3. 287 1.00 21. 02 2931 CA PHE C 220 11.480 74.065-4. 295 1. 00 23.75 2932 CB PHE C 220 11. 324 73.030-5. 415 1.00 22.52 2933 CG PHE C 220 11.312 71.617-4. 930 1.00 24.05 2934 CD1 PHE C 220 10.108 70.959-4. 693 1.00 25.06 1 2 3 4 5 6 7 8 9 10 2935 CD2 PHE C 220 12.507 70.959-4. 651 1.00 21. 79 2936 CE1 PHE C 220 10.094 69.659-4. 191 1.00 24.88 2937 CE2 PHE C 220 12.506 69.665-4. 151 1.00 21. 31 2938 CZ PHE C 220 11.299 69. 013-3. 915 1.00 23.99 2939 C PHE C 220 11.508 75.450-4. 917 1.00 24.74 2940 O PHE C 220 10.502 76.169-4. 923 1.00 25.58 2941 N GLY C 221 12.673 75.811-5. 444 1.00 24.44 2942 CA GLY C 221 12.839 77.096-6. 097 1.00 24. 68 2943 C GLY C 221 12.430 78.273-5. 241 1. 00 25. 02 2944 O GLY C 221 12.851 78.389-4. 088 1.00 21. 88 2945 N ASP C 222 11.597 79.144-5. 805 1.00 25.00 2946 CA ASP C 222 11.138 80. 327-5. 092 1.00 28.17 2947 CB ASP C 222 11.085 81.521-6. 047 1.00 31.52 2948 CG ASP C 222 12. 369 81.693-6. 833 1.00 36.21 2949 OD1 ASP C 222 12.328 81.536-8. 074 1.00 39.93 2950 OD2 ASP C 222 13.416 81.972-6. 209 1.00 33.72 2951 C ASP C 222 9.777 80.172-4. 416 1.00 29.51 2952 O ASP C 222 9.277 81.126-3. 809 1.00 29.97 2953 N GLU C 223 9.169 78.992-4. 509 1.00 28.88 2954 CA GLU C 223 7.862 78.794-3. 883 1.00 28.72 2955 CB GLU C 223 7.238 77.465-4. 333 1.00 28. 69 2956 CG GLU C 223 6.861 77.461-5. 822 1.00 30.26 2957 CD GLU C 223 5.969 76.289-6. 226 1.00 33.86 2958 OE1 GLU C 223 6.333 75.126-5. 931 1.00 34.10 2959 OE2 GLU C 223 4.906 76.532-6. 848 1.00 30.11 2960 C GLU C 223 7.949 78.874-2. 362 1.00 28.47 2961 O GLU C 223 9.008 78.645-1. 772 1.00 27.28 2962 N LEU C 224 6.830 79.220-1. 731 1.00 29.14 2963 CA LEU C 224 6.766 79.364-0. 278 1.00 29.39 2964 CB LEU C 224 5.723 80.425 0.096 1.00 32.11 2965 CG LEU C 224 5.921 81.852-0. 432 1.00 36.13 2966 CD1 LEU C 224 4.621 82. 640-0. 291 1. 00 37.17 2967 CD2 LEU C 224 7.043 82.530 0. 332 1. 00 36. 52 1 2 3 4 5 6 7 8 9 10 2968 C LEU C 224 6.422 78.058 0.427 1. 00 27.40 2969 O LEU C 224 5.867 77.142-0. 176 1.00 25.70 2970 N SER C 225 6.747 77.993 1. 714 1.00 26. 18 2971 CA SER C 225 6.474 76.819 2.534 1.00 26.93 2972 CB SER C 225 7. 367 76.839 3.775 1.00 28.67 2973 OG SER C 225 7.162 75.689 4.577 1. 00 36.70 2974 C SER C 225 5.001 76.776 2.960 1.00 26.65 2975 O SER C 225 4. 377 75.719 2.964 1.00 26.53 2976 N LEU C 226 4.459 77.935 3. 317 1.00 24.70 2977 CA LEU C 226 3.069 78.047 3.750 1.00 26.12 2978 CB LEU C 226 2.986 78.826 5.067 1.00 26.58 2979 CG LEU C 226 1.586 79.006 5.668 1.00 30.01 2980 CD1 LEU C 226 1.005 77.640 6.046 1. 00 26.61 2981 CD2 LEU C 226 1.668 79.913 6.897 1.00 29.13 2982 C LEU C 226 2.287 78.780 2.673 1.00 24.59 2983 O LEU C 226 2.582 79.932 2.373 1.00 25.40 2984 N VAL C 227 1.291 78.113 2.096 1.00 23.57 2985 CA VAL C 227 0.495 78.708 1.030 1.00 22. 64 2986 CB VAL C 227 0.849 78. 072-0. 324 1.00 24.19 2987 CG1 VAL C 227 2.354 78.189-0. 573 1. 00 25.33 2988 CG2 VAL C 227 0.424 76.606-0. 337 1.00 23.36 2989 C VAL C 227-1.017 78.568 1.231 1.00 23.58 2990 O VAL C 227-1.488 77.641 1.888 1.00 22.73 2991 N THR C 228-1.773 79.491 0.643 1.00 22.33 2992 CA THR C 228-3.228 79.465 0.741 1.00 21.29 2993 CB THR C 228-3.830 80.886 0.573 1.00 21.31 2994 OGI THR C 228-3.332 81.745 1.606 1.00 19. 77 2995 CG2 THR C 228-5.349 80.842 0.652 1.00 18.44 2996 C THR C 228-3.792 78.574-0. 362 1.00 21. 69 2997 O THR C 228-3.400 78.701-1. 524 1.00 20.87 2998 N LEU C 229-4.702 77. 673 0.005 1.00 19.71 2999 CA LEU C 229-5. 350 76.791-0. 970 1.00 20. 39 3000 CB LEU C 229-5. 654 75.417-0. 360 1. 00 20. 28 2 3 4 5 6 7 8 9 10 3001 CG LEU C 229-4.494 74.486-0. 019 1.00 20.59 3002 CD1 LEU C 229-5.047 73.203 0.614 1.00 20.29 3003 CD2 LEU C 229-3. 706 74.162-1. 286 1.00 19.70 3004 C LEU C 229-6.663 77.429-1. 415 1.00 20.91 3005 O LEU C 229-6.909 77.597-2. 611 1.00 21.60 3006 N PHE C 230-7.503 77.771-0. 439 1.00 19.62 3007 CA PHE C 230-8.801 78.397-0. 696 1.00 20.46 3008 CB PHE C 230-9.945 77. 371-0. 617 1.00 22.14 3009 CG PHE C 230-9.650 76.062-1. 286 1. 00 25.25 3010 CD1 PHE C 230-9.416 74.919-0. 523 1.00 27.00 3011 CD2 PHE C 230-9.595 75.970-2. 676 1.00 28.14 3012 CE1 PHE C 230-9.127 73.696-1. 135 1.00 30.28 3013 CE2 PHE C 230-9. 304 74.752-3. 305 1.00 28.59 3014 CZ PHE C 230-9.070 73.612-2. 530 1.00 29.07 3015 C PHE C 230-9.052 79.444 0.387 1.00 19.64 3016 O PHE C 230-8.538 79.322 1.500 1.00 18. 23 3017 N ARG C 231-9.844 80.464 0.064 1.00 18.48 3018 CA ARG C 231-10. 177 81.492 1.042 1.00 19.46 3019 CB ARG C 231-9.195 82.679 0.960 1.00 20.80 3020 CG ARG C 231-9.248 83.547-0. 289 1.00 22. 68 3021 CD ARG C 231-8.105 84.581-0. 239 1.00 22. 54 3022 NE ARG C 231-8.054 85. 482-1. 394 1. 00 24.45 3023 CZ ARG C 231-8.769 86.599-1. 525 1.00 25.01 3024 NH1 ARG C 231-9. 614 86.981-0. 576 1.00 26.72 3025 NH2 ARG C 231-8.628 87.352-2. 607 1.00 24.38 3026 C ARG C 231-11.626 81.966 0.900 1. 00 19.98 3027 O ARG C 231-12.236 81.844-0. 162 1.00 20.70 3028 N CYS C 232-12.163 82.494 1.995 1.00 19.97 3029 CA CYS C 232-13.540 82.977 2.068 1.00 21.56 3030 C CYS C 232-13.509 84.422 2.584 1. 00 20. 49 3031 O CYS C 232-12.661 84.759 3.406 1. 00 18.52 3032 CB CYS C 232-14.332 82.089 3.061 1.00 22. 25 3033 SG CYS C 232-16. 141 82. 268 2.973 1. 00 34. 03 2 3 4 5 6 7 8 9 10 3034 N ILE C 233-14.407 85.278 2.104 1.00 20.60 3035 CA ILE C 233-14.457 86.655 2.606 1.00 21.92 3036 CB ILE C 233-13. 484 87.592 1.848 1.00 23.09 3037 CG2 ILE C 233-13.920 87.768 0.411 1.00 19.94 3038 CG1 ILE C 233-13.434 88.950 2.555 1.00 22.71 3039 CD1 ILE C 233-12. 360 89.880 2.024 1.00 26.14 3040 C ILE C 233-15.871 87.241 2.566 1.00 22.49 3041 0 ILE C 233-16.641 86.961 1.648 1. 00 20.58 3042 N GLN C 234-16.196 88.051 3.576 1.00 23. 47 3043 CA GLN C 234-17.517 88.670 3.700 1.00 24.14 3044 CB GLN C 234-18. 363 87.867 4.695 1.00 25.79 3045 CG GLN C 234-18.753 86.475 4.232 1.00 26.60 3046 CD GLN C 234-19.951 86.497 3.305 1.00 26. 67 3047 OE1 GLN C 234-21.085 86.687 3.751 1. 00 26.60 3048 NE2 GLN C 234-19.707 86.313 2.007 1.00 25.14 3049 C GLN C 234-17.472 90.121 4.193 1. 00 25.23 3050 O GLN C 234-16.761 90.426 5.146 1.00 23.91 3051 N ASN C 235-18.230 91.007 3.548 1.00 25.79 3052 CA ASN C 235-18.312 92.402 3.993 1.00 27.22 3053 CB ASN C 235-19.035 93.277 2.957 1.00 26.79 3054 CG ASN C 235-18.125 93.742 1.834 1.00 28.44 3055 OD1 ASN C 235-17.145 94.457 2.062 1.00 30.52 3056 ND2 ASN C 235-18.451 93.346 0.611 1.00 25.62 3057 C ASN C 235-19.152 92. 353 5.274 1.00 28.07 3058 O ASN C 235-20. 051 91.520 5. 390 1.00 27.86 3059 N MET C 236-18.868 93.235 6.227 1.00 28.90 3060 CA MET C 236-19.613 93.256 7. 485 1. 00 29.67 3061 CB MET C 236-18.661 93.056 8. 670 1.00 29.44 3062 CG MET C 236-17.759 91.827 8.574 1.00 29.54 3063 SD MET C 236-18.665 90.267 8.426 1.00 30. 97 3064 CE MET C 236-19.533 90.246 10.009 1.00 30.80 3065 C MET C 236-20. 360 94.581 7.654 1.00 31.84 3066 0MET C 236-19.855 95.640 7.276 1.00 31.45 1 2 3 4 5 6 7 8 9 10 3067 N PRO C 237-21.579 94.537 8. 223 1.00 34.12 3068 CD PRO C 237-22. 313 93.341 8.678 1.00 33.65 3069 CA PRO C 237-22. 383 95.746 8.435 1. 00 35. 39 3070 CB PRO C 237-23.780 95.186 8.670 1.00 35.13 3071 CG PRO C 237-23.488 93.943 9.447 1.00 33.76 3072 C PRO C 237-21. 873 96.536 9.634 1.00 37.95 3073 O PRO C 237-21.062 96.034 10.414 1.00 37.38 3074 N GLU C 238-22.358 97.766 9.779 1.00 41.03 3075 CA GLU C 238-21.946 98.628 10.883 1.00 45.31 3076 CB GLU C 238-22.383 100.075 10.616 1.00 48.47 3077 CG GLU C 238-21.906 100.625 9.277 1. 00 53.41 3078 CD GLU C 238-20.392 100.631 9.151 1.00 55.67 3079 OE1 GLU C 238-19.892 100.746 8.010 1.00 57.50 3080 OE2 GLU C 238-19.702 100.529 10.189 1. 00 57. 75 3081 C GLU C 238-22.509 98.171 12.226 1.00 45.37 3082 O GLU C 238-21.860 98. 327 13.260 1.00 46.07 3083 N THR C 239-23.711 97.602 12. 208 1. 00 45.52 3084 CA THR C 239-24.347 97.147 13.441 1. 00 45.47 3085 CB THR C 239-25. 580 98.017 13.776 1.00 46.95 3086 OG1 THR C 239-26.613 97.779 12.811 1.00 48.47 3087 CG2 THR C 239-25.209 99.499 13.749 1.00 47. 34 3088 C THR C 239-24.788 95.681 13.404 1.00 44.53 3089 O THR C 239-25.193 95.163 12.360 1.00 43.75 3090 N LEU C 240-24.706 95.027 14.560 1.00 43.45 3091 CA LEU C 240-25.090 93.626 14.716 1.00 42.14 3092 CB LEU C 240-26.618 93.498 14.685 1.00 43. 06 3093 CG LEU C 240-27. 375 94.316 15.739 1.00 45.00 3094 CD1 LEU C 240-28. 876 94.195 15.515 1.00 45.23 3095 CD2 LEU C 240-27.000 93.829 17.134 1.00 45. 78 3096 C LEU C 240-24. 471 92.704 13.663 1.00 40.60 3097 O LEU C 240-25.178 91.957 12.986 1.00 39.56 3098 N PRO C 241-23.134 92.740 13.519 1.00 39.50 3099 CD PRO C 241-22.181 93.603 14.239 1.00 38.76 1 2 3 4 5 6 7 8 9 10 3100 CA PRO C 241-22.432 91.900 12.542 1.00 37. 38 3101 CB PRO C 241-20.965 92.267 12.762 1.00 37.88 3102 CG PRO C 241-21. 036 93.673 13.268 1.00 39.15 3103 C PRO C 241-22.695 90.419 12.800 1.00 35.68 3104 O PRO C 241-22.521 89.936 13.920 1.00 33.79 3105 N ASN C 242-23.101 89.702 11.757 1.00 34.68 3106 CA ASN C 242-23.404 88.280 11.874 1.00 33.36 3107 CB ASN C 242-24.787 88.094 12.516 1.00 37.16 3108 CG ASN C 242-24.715 87.660 13.966 1.00 40.40 3109 OD1 ASN C 242-24. 142 86.618 14.288 1. 00 41. 41 3110 ND2 ASN C 242-25.310 88.454 14.851 1.00 43.42 3111 C ASN C 242-23.403 87.584 10.516 1.00 30.04 3112 O ASN C 242-24.467 87.330 9.967 1.00 30.63 3113 N ASN C 243-22. 225 87.274 9.978 1.00 28. 29 3114 CA ASN C 243-22.124 86.584 8.680 1.00 26.15 3115 CB ASN C 243-21.491 87.483 7.609 1.00 27.27 3116 CG ASN C 243-22.447 88.508 7.045 1.00 28.81 3117 OD1 ASN C 243-23.572 88.186 6.655 1.00 27.24 3118 ND2 ASN C 243-21.991 89.755 6.975 1.00 29.58 3119 C ASN C 243-21.253 85.335 8.770 1.00 23.73 3120 O ASN C 243-20.102 85.425 9.197 1.00 23.83 3121 N SER C 244-21.788 84.179 8. 376 1.00 21.71 3122 CA SER C 244-20.984 82.954 8.372 1. 00 21. 10 3123 CB SER C 244-21.854 81.692 8.561 1. 00 19. 59 3124 OG SER C 244-22. 819 81.532 7.534 1.00 19.76 3125 C SER C 244-20.307 82. 949 7. 000 1.00 19.66 3126 O SER C 244-20.840 83.514 6.045 1.00 20.01 3127 N CYS C 245-19.133 82.335 6.908 1.00 21.27 3128 CA CYS C 245-18.383 82.285 5. 651 1.00 21. 77 3129 C CYS C 245-17.948 80.847 5.406 1.00 19.82 3130 O CYS C 245-17.189 80. 300 6.197 1.00 18.41 3131 CB CYS C 245-17.126 83.165 5.746 1.00 24. 26 3132 SG CYS C 245-16. 576 83.862 4. 154 1.00 29. 94 1 2 3 4 5 6 7 8 9 10 3133 N TYR C 246-18.416 80.246 4.314 1.00 18. 68 3134 CA TYR C 246-18.060 78. 869 3.985 1.00 17.51 3135 CB TYR C 246-19.321 77.989 3. 912 1.00 17. 53 3136 CG TYR C 246-19.077 76.544 3.489 1.00 16. 62 3137 CD1 TYR C 246-18.851 76.208 2.152 1.00 15.66 3138 CE1 TYR C 246-18.628 74.875 1.767 1.00 15.11 3139 CD2 TYR C 246-19.071 75.513 4.432 1. 00 16.49 3140 CE2 TYR C 246-18.846 74.184 4.056 1.00 17.00 3141 CZ TYR C 246-18.627 73.875 2.727 1.00 15.51 3142 OH TYR C 246-18.405 72.571 2.356 1.00 14.63 3143 C TYR C 246-17.321 78.771 2.656 1.00 17.46 3144 O TYR C 246-17.631 79.487 1.707 1.00 16.78 3145 N SER C 247-16. 334 77.880 2.607 1.00 16. 62 3146 CA SER C 247-15.586 77.621 1. 382 1.00 17.28 3147 CB SER C 247-14.442 78.617 1.194 1.00 17. 49 3148 OG SER C 247-13.839 78.428-0. 083 1.00 19.85 3149 C SER C 247-15.027 76.205 1.446 1.00 16.77 3150 O SER C 247-14.740 75.694 2.532 1.00 15.27 3151 N ALA C 248-14.877 75.579 0.284 1. 00 14.97 3152 CA ALA C 248-14.357 74.220 0.206 1.00 16.78 3153 CB ALA C 248-15.476 73.204 0.523 1.00 16.11 3154 C ALA C 248-13.785 73.946-1. 181 1.00 16.55 3155 O ALA C 248-14.157 74.602-2. 155 1.00 16.86 3156 N GLY C 249-12.882 72.973-1. 262 1.00 15.13 3157 CA GLY C 249-12.284 72.624-2. 538 1.00 15.83 3158 C GLY C 249-11.540 71.303-2. 458 1.00 16.78 3159 O GLY C 249-11.544 70.645-1. 422 1.00 16.64 3160 N ILE C 250-10.892 70. 913-3.549 1.00 17.40 3161 CA ILE C 250-10.146 69.661-3. 580 1. 00 17. 61 3162 CB ILE C 250-10.660 68.732-4. 703 1. 00 18.06 3163 CG2 ILE C 250-9.800 67.472-4. 767 1.00 17.55 3164 CG1 ILE C 250-12.132 68. 380-4. 460 1.00 21. 32 3165 CD1 ILE C 250-12.768 67.542-5. 577 1.00 21.13 1 2 3 4 5 6. 7 8 9 10 3166 C ILE C 250-8.666 69.940-3. 832 1.00 18. 51 3167 O ILE C 250-8. 322 70.821-4. 614 1.00 15.56 3168 N ALA C 251-7.796 69.187-3. 169 1.00 18.02 3169 CA ALA C 251-6.357 69. 353-3. 353 1.00 20.15 3170 CB ALA C 251-5. 803 70.359-2. 336 1.00 19.01 3171 C ALA C 251-5.644 68.018-3. 187 1.00 19.26 3172 O ALA C 251-6.095 67.159-2. 429 1.00 19. 15 3173 N LYS C 252-4.545 67.832-3. 912 1.00 19. 57 3174 CA LYS C 252-3.763 66.612-3. 760 1. 00 20.93 3175 CB LYS C 252-3.086 66.200-5. 070 1.00 23.97 3176 CG LYS C 252-2. 328 64.883-4. 925 1.00 27.61 3177 CD LYS C 252-1.762 64. 360-6. 236 1.00 31.41 3178 CE LYS C 252-1.143 62.978-6. 019 1. 00 35.78 3179 NZ LYS C 252-0.653 62.350-7. 280 1.00 39. 18 3180 C LYS C 252-2.703 66.974-2. 725 1.00 20. 32 3181 O LYS C 252-1.928 67.905-2. 930 1.00 18.93 3182 N LEU C 253-2.685 66.258-1. 607 1.00 20.21 3183 CA LEU C 253-1.729 66.541-0. 542 1.00 21. 26 3184 CB LEU C 253-2.476 66.791 0.769 1. 00 19. 03 3185 CG LEU C 253-3.570 67.865 0.701 1.00 19.77 3186 CD1 LEU C 253-4.365 67.872 1.992 1.00 18.95 3187 CD2 LEU C 253-2.941 69.232 0.428 1.00 17.98 3188 C LEU C 253-0.750 65. 389-0. 365 1.00 23.09 3189 O LEU C 253-1.074 64.238-0. 671 1.00 23.40 3190 N GLU C 254 0.441 65.698 0.141 1.00 23.27 3191 CA GLU C 254 1.468 64.678 0.349 1.00 25.55 3192 CB GLU C 254 2.832 65.169-0. 143 1.00 29.57 3193 CG GLU C 254 2.862 65.696-1. 560 1.00 38.40 3194 CD GLU C 254 4.270 66.040-2. 010 1.00 43.82 3195 OBI GLU C 254 5. 102 65.110-2. 116 1.00 46.67 3196 OE2 GLU C 254 4.548 67.237-2. 252 1.00 48. 22 3197 C GLU C 254 1.619 64. 301 1.815 1.00 22.98 3198 O GLU C 254 1.410 65.130 2.705 1. 00 20. 54 1 2 3 4-5 6 7 8 9 10 3199 N GLU C 255 1.991 63.047 2.054 1.00 22.59 3200 CA GLU C 255 2.224 62.570 3.410 1.00 23.87 3201 CB GLU C 255 2.866 61.178 3. 397 1.00 26.49 3202 CG GLU C 255 3.525 60.826 4.731 1.00 34.12 3203 CD GLU C 255 3.695 59.333 4.956 1.00 39.70 3204 OE1 GLU C 255 3. 963 58.948 6.115 1.00 43.06 3205 OE2 GLU C 255 3.565 58.544 3.992 1.00 42.15 3206 C GLU C 255 3.188 63.560 4.057 1.00 22.59 3207 O GLU C 255 4.247 63.850 3.499 1.00 23.59 3208 N GLY C 256 2.824 64.082 5.224 1.00 21.96 3209 CA GLY C 256 3.687 65.044 5.888 1.00 22.01 3210 C GLY C 256 3.161 66.469 5.805 1.00 21.89 3211 O GLY C 256 3.533 67.312 6.621 1.00 21.85 3212 N ASP C 257 2.315 66.751 4.814 1.00 21.43 3213 CA ASP C 257 1.720 68.082 4.663 1.00 20.61 3214 CB ASP C 257 0. 875 68.181 3. 380 1.00 21. 07 3215 CG ASP C 257 1.701 68. 380 2.124 1. 00 23.40 3216 ODI ASP C 257 2.923 68.621 2.219 1.00 23.80 3217 OD2 ASP C 257 1.106 68.306 1.023 1.00 23. 34 3218 C ASP C 257 0.783 68. 344 5.844 1.00 20.52 3219 O ASP C 257 0.276 67.405 6.465 1. 00 21.08 3220 N GLU C 258 0.546 69.621 6.135 1.00 19.72 3221 CA GLU C 258-0. 353 70.024 7.209 1.00 21.10 3222 CB GLU C 258 0.439 70.584 8.393 1.00 23. 59 3223 CG GLU C 258 1.201 69.535 9.185 1.00 28.03 3224 CD GLU C 258 2.062 70.144 10.279 1.00 33.01 3225 OE1 GLU C 258 2.478 69. 396 11.188 1.00 37.92 3226 OE2 GLU C 258 2.331 71.363 10.230 1. 00 34. 84 3227 C GLU C 258-1.323 71.088 6.705 1.00 20.61 3228 O GLU C 258-0.988 71.859 5.808 1.00 20.29 3229 N LEU C 259-2.523 71.121 7.280 1.00 19.42 3230 CA LEU C 259-3. 533 72.110 6.909 1.00 19.17 3231 CB LEU C 259-4.788 71.431 6.347 1.00 18.93 1 2 3 4 5 6 7 8 9 10 3232 CG LEU C 259-4.695 70.554 5.101 1.00 19.48 3233 CD1 LEU C 259-6.052 69. 885 4.857 1.00 18.85 3234 CD2 LEU C 259-4. 282 71.401 3.899 1. 00 18.52 3235 C LEU C 259-3.939 72.908 8. 145 1.00 19.36 3236 O LEU C 259-4.098 72.345 9.222 1.00 20.38 3237 N GLN C 260-4.109 74.216 7.989 1.00 18.57 3238 CA GLN C 260-4.520 75.064 9.102 1.00 18.84 3239 CB GLN C 260-3. 291 75.735 9.752 1.00 18.71 3240 CG GLN C 260-2.593 76.794 8. 900 1.00 20. 47 3241 CD GLN C 260-1.275 77.295 9.515 1. 00 23.66 3242 OE1 GLN C 260-0. 845 78.418 9.254 1.00 25.52 3243 NE2 GLN C 260-0.631 76.454 10. 315 1.00 23.18 3244 C GLN C 260-5.499 76.118 8.584 1.00 19.57 3245 O GLN C 260-5.459 76.477 7.407 1.00 21.00 3246 N LEU C 261-6. 396 76.587 9.450 1. 00 19.74 3247 CA LEU C 261-7. 368 77.611 9.066 1.00 20.58 3248 CB LEU C 261-8.791 77.180 9.453 1.00 18. 26 3249 CG LEU C 261-9.963 78.025 8.935 1. 00 18.61 3250 CD1 LEU C 261-11.199 77.147 8.822 1. 00 19.29 3251 CD2 LEU C 261-10.227 79.206 9.851 1.00 16.97 3252 C LEU C 261-6. 982 78.895 9.797 1.00 21. 71 3253 O LEU C 261-7.050 78.963 11.028 1.00 21.40 3254 N ALA C 262-6.585 79.911 9. 035 1. 00 19.75 3255 CA ALA C 262-6. 143 81.176 9.614 1.00 21.56 3256 CB ALA C 262-4. 684 81.434 9.205 1.00 21. 48 3257 C ALA C 262-6.990 82.392 9. 249 1. 00 22.21 3258 O ALA C 262-7.521 82.484 8.144 1.00 23.44 3259 N ILE C 263-7.099 83.326 10.190 1.00 22.27 3260 CA ILE C 263 -7.832 84.574 9.986 1.00 21.84 3261 CB ILE C 263 -8.852 84.812 11.111 1.00 21.59 3262 CG2 ILE C 263-9.547 86.151 10.904 1.00 21.40 3263 CG1 ILE C 263-9. 885 83.678 11.107 1.00 22.90 3264 CD1 ILE C 263-10.790 83.651 12.305 1.00 22. 72 1 2 3 4 5 6 7 8 9 10 3265 C ILE C 263-6. 760 85. 666 10. 003 1. 00 24. 62 3266 O ILE C 263-6. 170 85. 950 11. 047 1. 00 23. 13 3267 N PRO C 264-6. 495 86. 289 8. 841 1. 00 26. 20 3268 CD PRO C 264-7. 195 86. 066 7. 562 1. 00 26.30 3269 CA PRO C 264-5. 483 87.341 8. 699 1. 00 28. 88 3270 CB PRO C 264-5. 332 87. 459 7. 184 1. 00 28. 70 3271 CG PRO C 264-6. 724 87. 241 6. 716 1. 00 29.8 3272 C PRO C 264-5. 762 88. 684 9.370 1. 00 30. 26 3273 O PRO C 264-5. 746 89. 727 8. 720 1. 00 31.35 3274 N ARG C 265-6. 006 88. 646 10. 674 1. 00 29. 59 3275 CA ARG C 265-6. 263 89. 849 11. 455 1. 00 31. 21 3276 CB ARG C 265-7. 703 90. 328 11. 260 1. 00 33. 98 3277 CG ARG C 265-8. 135 91. 421 12. 232 1. 00 39. 20 3278 CD ARG C 265-9. 522 91. 950 11. 894 1. 00 43. 43 3279 NE ARG C 265-9. 488 92. 833 10. 733 1. 00 47. 36 3280 CZ ARG C 265-9. 103 94. 106 10. 774 1. 00 50. 06 3281 NH1 ARG C 265-8. 725 94. 652 11. 925 1. 00 49. 89 3282 NH2 ARG C 265-9. 081 94. 829 9. 662 1. 00 51. 18 3283 C ARG C 265-6. 010 89. 549 12. 929 1. 00 30. 44 3284 O ARG C 265-6. 386 88. 488 13. 432 1. 00 28. 39 3285 N GLU C 266-5. 354 90. 481 13. 613 1. 00 28. 60 3286 CA GLU C 266-5. 060 90. 318 15. 029 1. 00 29. 00 3287 CB GLU C 266-4. 057 91. 387 15. 479 1. 00 31. 41 3288 CG GLU C 266-2. 687 91. 280 14. 814 1. 00 33. 95 3289 CD GLU C 266-1. 790 92. 476 15. 117 1. 00 38. 35 3290 OE1 GLU C 266-1. 615 92. 811 16.308 1. 00 41. 38 3291 OE2 GLU C 266-1. 254 93. 077 14. 164 1. 00 37. 78 3292 C GLU C 266-6. 344 90. 437 15. 849 1. 00 27. 78 3293 O GLU C 266-7. 172 91311 15. 596 1. 00 27. 36 3294 N ASN C 267-6. 508 89. 543 16. 818 1. 00 26. 67 3295 CA ASN C 267-7. 675 89. 546 17. 696 1. 00 28. 47 3296 CB ASN C 267-7. 560 90. 690 18. 705 1. 00 30. 20 3297 ASN C 267-6. 271 90. 639 19. 490 1. 00 31. 20 _ 3 4 5 3298 OD1 ASN C 267-5.384 91.473 19.301 1.00 34. 32 3299 ND2 ASN C 267-6.151 89.649 20.367 1.00 30.49 3300 C ASN C 267-9.015 89.652 16.974 1.00 28.41 3301 O ASN C 267-9.856 90.478 17.330 1.00 28.82 3302 N ALA C 268-9.221 88. 808 15.969 1.00 27.92 3303 CA ALA C 268-10.471 88.815 15.216 1.00 28.15 3304 CB ALA C 268-10.365 87.864 14.018 1.00 28.52 3305 C ALA C 268-11.629 88.393 16.120 1.00 28.32 3306 O ALA C 268-11.462 87.542 16.998 1.00 27.60 3307 N GLN C 269-12.798 88.992 15.903 1.00 29.02 3308 CA GLN C 269-13.984 88.675 16.696 1.00 30.90 3309 CB GLN C 269-14.790 89.949 16.963 1.00 32.48 3310 CG GLN C 269-14.015 90.997 17.758 1.00 34.53 3311 CD GLN C 269-13.577 90.479 19.115 1.00 35.49 3312 OE1 GLN C 269-14. 399 90.266 20.002 1.00 37.41 3313 NE2 GLN C 269-12.276 90.261 19.278 1.00 36.64 3314 C GLN C 269-14.843 87.646 15.963 1. 00 30.09 3315 O GLN C 269-15.399 87.928 14.900 1.00 29.53 3316 N ILE C 270-14.952 86.455 16.540 1.00 30.05 3317 CA ILE C 270-15.715 85. 373 15.924 1. 00 30.52 3318 CB ILE C 270-14.779 84.436 15.134 1.00 30. 16 3319 CG2 ILE C 270-14.016 85.223 14.070 1.00 28. 04 3320 CG1 ILE C 270-13.797 83.767 16.102 1.00 31.41 3321 CD1 ILE C 270-12.839 82.809 15.446 1.00 33.58 3322 C ILE C 270-16.462 84.524 16.953 1. 00 30.46 3323 O ILE C 270-16.232 84.640 18.153 1.00 31.65 3324 N SER C 271-17.349 83.662 16.465 1.00 28.09 3325 CA SER C 271-18.118 82.776 17.331 1.00 27.12 3326 CB SER C 271-19.532 82.592 16. 775 1. 00 26. 47 3327 OG SER C 271-20.241 81.602 17.500 1.00 25.99 3328 C SER C 271-17.430 81.420 17.428 1.00 26.82 3329 O SER C 271-17.000 80.856 16.419 1.00 25.59 3330 N LEU C 272-17. 325 80. 895 18.643 1.00 26.85 1 2 3 4 5 6 7 8 9 10 3331 CA LEU C 272-16.689 79.603 18.846 1.00 28.43 3332 CB LEU C 272-15.747 79.663 20.055 1.00 27.93 3333 CG LEU C 272-14. 549 80.615 19.918 1.00 28.44 3334 CD1 LEU C 272-13.678 80.514 21.159 1.00 30.20 3335 CD2 LEU C 272-13.729 80.263 18.685 1.00 27.88 3336 C LEU C 272-17.723 78.492 19.015 1.00 28. 54 3337 O LEU C 272-17.474 77. 482 19.670 1.00 29.66 3338 N ASP C 273-18.886 78.689 18.406 1.00 29.28 3339 CA ASP C 273-19.973 77.712 18.447 1.00 30.59 3340 CB ASP C 273-21.277 78. 398 18.037 1.00 36.17 3341 CG ASP C 273-22. 392 78.171 19.028 1.00 43.66 3342 OD1 ASP C 273-22.124 78.269 20.248 1.00 49. 64 3343 OD2 ASP C 273-23.533 77.904 18.590 1.00 47.11 3344 C ASP C 273-19.623 76.601 17.447 1.00 28.52 3345 O ASP C 273-19. 390 76.871 16.271 1.00 26.27 3346 N GLY C 274-19.592 75.359 17.921 1.00 27.25 3347 CA GLY C 274-19.247 74.227 17.073 1.00 26.21 3348 C GLY C 274-20.102 73.954 15.845 1.00 26.68 3349 O GLY C 274-19.642 73. 305 14.902 1.00 26.10 3350 N ASP C 275-21.342 74.432 15.833 1.00 24.81 3351 CA ASP C 275-22. 204 74.195 14.682 1.00 25.64 3352 CB ASP C 275 -23.663 74.006 15.117 1.00 27.80 3353 CG ASP C 275 -24.271 75.260 15.716 1.00 31.74 3354 OD1 ASP C 275 -23.622 76.323 15.690 1.00 32.08 3355 OD2 ASP C 275 -25.415 75.180 16.210 1.00 36.58 3356 C ASP C 275-22.124 75.298 13.631 1.00 23.25 3357 O ASP C 275-22.834 75.253 12. 629 1.00 23. 33 3358 N VAL C 276-21.261 76.287 13.849 1. 00 21. 79 3359 CA VAL C 276-21.131 77.366 12.879 1.00 20.33 3360 CB VAL C 276-21.841 78.649 13. 371 1.00 21. 38 3361 CG1 VAL C 276-21.010 79. 350 14.445 1.00 20.88 3362 CG2 VAL C 276-22.117 79.560 12.188 1.00 23.59 3363 C VAL C 276-19.675 77.669 12.498 1. 00 18. 60 1 2 3 4 7 8 9 10 3364 O VAL C 276-19.416 78.278 11.463 1. 00 19.03 3365 N THR C 277-18.730 77.241 13.329 1. 00 16.88 3366 CA THR C 277-17. 308 77.431 13.036 1.00 18.12 3367 CB THR C 277-16.629 78. 392 14.044 1.00 18.69 3368 OG1 THR C 277-17.237 79.684 13.947 1. 00 18. 37 3369 CG2 THR C 277-15.137 78.533 13.736 1.00 17.93 3370 C THR C 277-16.694 76.036 13.126 1.00 17.26 3371 O THR C 277-16.606 75.449 14.203 1.00 18.40 3372 N PHE C 278-16.304 75.500 11.973 1.00 16.40 3373 CA PHE C 278-15.754 74.154 11.894 1.00 16. 39 3374 CB PHE C 278-16.903 73.133 11.810 1.00 16.53 3375 CG PHE C 278-17. 915 73.432 10.736 1.00 17.75 3376 CD1 PHE C 278-17.719 72.983 9.432 1.00 16.54 3377 CD2 PHE C 278-19.071 74.154 11.032 1.00 18. 39 3378 CE1 PHE C 278-18.663 73.242 8.430 1.00 18. 06 3379 CE2 PHE C 278-20.023 74.425 10.038 1. 00 17.21 3380 CZ PHE C 278-19.818 73.965 8.736 1.00 18.28 3381 C PHE C 278-14.782 74.003 10.723 1.00 16.29 3382 O PHE C 278-14.721 74.860 9.837 1. 00 14. 88 3383 N PHE C 279-14.048 72.894 10.708 1.00 15.98 3384 CA PHE C 279-12.996 72.683 9.709 1.00 16.77 3385 CB PHE C 279-11.756 73.426 10.251 1.00 17.26 3386 CG PHE C 279-10.489 73.252 9.455 1.00 18.27 3387 CD1 PHE C 279-10.486 73.309 8.069 1. 00 18.01 3388 CD2 PHE C 279-9.270 73.120 10.125 1. 00 18.43 3389 CE1 PHE C 279-9. 283 73.240 7.351 1.00 20.18 3390 CE2 PHE C 279-8.063 73.051 9.423 1.00 19.04 3391 CZ PHE C 279-8.068 73.112 8.036 1.00 20.61 3392 C PHE C 279-12.765 71.181 9.554 1.00 17.71 3393 O PHE C 279-12.672 70.459 10.546 1.00 17.94 3394 N GLY C 280-12.699 70.699 8.316 1.00 18.60 3395 CA GLY C 280-12.500 69.274 8.118 1.00 18.58 3396 C GLY C 280-11. 935 68. 864 6.774 1. 00 IS43 123 4 5 6 7 8 9 10 3397 O GLY C 280-11.740 69.697 5.887 1.00 18.30 3398 N ALA C 281-11.670 67. 568 6.630 1.00 16.46 3399 CA ALA C 281-11. 121 67.019 5.397 1. 00 17.83 3400 CB ALA C 281-9.593 67.095 5.408 1.00 18.46 3401 C ALA C 281-11.580 65.575 5.208 1.00 19.58 3402 O ALA C 281-11.819 64.839 6.174 1.00 19.57 3403 N LEU C 282-11.683 65.180 3.947 1.00 20.53 3404 CA LEU C 282-12. 150 63.855 3.573 1.00 22.62 3405'CB LEU C 282-13.622 63.980 3.148 1.00 25.22 3406 CG LEU C 282-14.500 62.839 2.623 1.00 30.02 3407 CD1 LEU C 282-14.642 62.970 1.121 1.00 32.21 3408 CD2 LEU C 282-13.938 61.492 3.022 1.00 29.48 3409 C LEU C 282-11. 285 63.309 2.436 1. 00 22. 35 3410 O LEU C 282-11.041 64.002 1.445 1.00 20.56 3411 N LYS C 283-10.804 62.077 2.585 1.00 22.24 3412 CA LYS C 283-9.973 61.479 1.547 1.00 22.60 3413 CB LYS C 283-9.029 60.429 2.142 1.00 23. 79 3414 CG LYS C 283-7.939 59.970 1.173 1.00 24. 81 3415 CD LYS C 283-6.952 59.036 1.849 1.00 28.13 3416 CE LYS C 283-5.709 58.808 0.995 1.00 27.83 3417 NZ LYS C 283-6.021 58.154-0. 305 1.00 30. 84 3418 C LYS C 283-10.858 60.839 0.486 1.00 24.21 3419 O LYS C 283-11.679 59.973 0.779 1.00 25.23 3420 N LEU C 284-10.689 61.274-0. 753 1.00 24.03 3421 CA LEU C 284-11. 482 60.756-1. 854 1.00 27.23 3422 CB LEU C 284-11.457 61.758-3. 012 1.00 25.00 3423 CG LEU C 284-11.927 63.167-2. 634 1.00 25.63 3424 CD1 LEU C 284-11.644 64.139-3. 766 1.00 24.02 3425 CD2 LEU C 284-13.407 63.133-2. 307 1.00 23.41 3426 C LEU C 284-10. 954 59.405-2. 322 1.00 30. 37 3427 O LEU C 284-9.744 59. 187-2. 382 1.00 31.96 3428 N LEU C 285-11.862 58.491-2. 643 1.00 34.63 3429 CA LEU C 285-11.459 57.176-3. 126 1. 00 38. 39 1 2 3 4 5 6 7 8 9 10 3430 CB LEU C 285-12. 678 56.268-3. 296 1. 00 40.41 3431 CG LEU C 285-13.281 55.713-2. 005 1.00 42.82 3432 CD1 LEU C 285-14.580 54.990-2. 309 1.00 44.85 3433 CD2 LEU C 285-12.287 54. 773-1. 350 1.00 43.74 3434 C LEU C 285-10.752 57. 349-4. 463 1.00 39.73 3435 O LEU C 285-9.667 56.756-4. 644 1.00 42.47 3436 OXT LEU C 285-11.297 58.079-5. 315 1.00 41.65 3437 CB VAL D 142-29.663 43.138-32. 478 1.00 46.59 3438 CG1 VAL D 142-28.991 41.960-33. 171 1. 00 47.85 3439 CG2 VAL D 142-30.458 42.654-31. 264 1.00 47.73 3440 C VAL D 142-29.288 45.411-31. 492 1.00 43.18 3441 O VAL D 142-29.923 45. 371-30. 438 1.00 42. 99 3442 N VAL D 142-27.659 43.584-31. 041 1.00 45. 35 3443 CA VAL D 142-28.593 44.168-32. 044 1.00 44.59 3444 N THR D 143-29.164 46.517-32. 213 1. 00 41. 40 3445 CA THR D 143-29.768 47.771-31. 786 1.00 38.41 3446 CB THR D 143-28.750 48.615-30. 989 1.00 38.69 3447 OG1 THR D 143-29.362 49.839-30. 563 1.00 39. 34 3448 CG2 THR D 143-27.537 48.927-31. 849 1.00 38.74 3449 C THR D 143-30.245 48.558-33. 001 1.00 36.87 3450 O THR D 143-29.865 48.254-34. 135 1.00 36. 90 3451 N GLN D 144-31.089 49.558-32. 765 1.00 32.86 3452 CA GLN D 144-31.609 50. 379-33. 851 1.00 30.43 3453 CB GLN D 144-33.139 50.407-33. 827 1.00 30. 14 3454 CG GLN D 144-33. 788 49.036-33. 805 1.00 31.51 3455 CD GLN D 144-35.296 49. 109-33. 904 1.00 32.53 3456 OBI GLN D 144-35.856 49.180-34. 998 1.00 35.67 3457 NE2 GLN D 144-35.962 49.109-32. 760 1.00 29. 86 3458 C GLN D 144-31.080 51.798-33. 741 1.00 28.60 3459 O GLN D 144-31.504 52. 568-32. 875 1.00 27.17 3460 N ASP D 145-30.136 52.130-34. 614 1.00 25. 89 3461 CA ASP D 145-29.557 53.464-34. 639 1. 00 24. 87 3462 CB ASP D 145-28.403 53.523-35. 647 1. 00 26. 75 1 2 3 4 5 6 7 8 9 10 3463 CG ASP D 145-27. 192 52.715-35. 206 1.00 29. 98 3464 OD1 ASP D 145-27. 238 52.110-34. 113 1.00 30.51 3465 OD2 ASP D 145-26.189 52.689-35. 954 1.00 30.08 3466 C ASP D 145-30.642 54. 462-35. 051 1.00 23. 30 3467 O ASP D 145-31.524 54.140-35. 844 1.00 21. 08 3468 N CYS D 146-30.581 55.667-34. 501 1.00 21.20 3469 CA CYS D 146-31.551 56. 691-34. 848 1.00 19.65 3470 CB CYS D 146-32.899 56.453-34. 136 1.00 19.69 3471 SG CYS D 146-32.838 55.944-32. 410 1.00 25.29 3472 C CYS D 146-31.013 58.071-34. 539 1.00 19. 39 3473 O CYS D 146-30.048 58.226-33. 782 1.00 19. 33 3474 N LEU D 147-31.626 59.074-35. 154 1.00 16.37 3475 CA LEU D 147-31.211 60.455-34. 958 1.00 17.73 3476 CB LEU D 147-30.177 60.848-36. 021 1.00 18.87 3477 CG LEU D 147-29.610 62.274-35. 980 1.00 21. 30 3478 CD1 LEU D 147-28. 217 62.278-36. 606 1.00 21.93 3479 CD2 LEU D 147-30.535 63.237-36. 705 1.00 20.43 3480 C LEU D 147-32.443 61. 340-35. 071 1.00 17.80 3481 O LEU D 147-33.294 61.121-35. 937 1.00 17.54 3482 N GLN D 148-32.538 62.336-34. 196 1.00 17.01 3483 CA GLN D 148-33.675 63.246-34. 207 1.00 15. 98 3484 CB GLN D 148-34.622 62.886-33. 059 1.00 16.74 3485 CG GLN D 148-35.796 63.836-32. 867 1.00 17.23 3486 CD GLN D 148-36.830 63.250-31. 921 1.00 20. 28 3487 OE1 GLN D 148-37.770 62. 570-32. 348 1.00 18. 16 3488 NE2 GLN D 148-36.643 63.485-30. 626 1.00 17.03 3489 C GLN D 148-33.235 64.708-34. 105 1.00 15.83 3490 O GLN D 148-32. 300 65.041-33. 372 1.00 16.05 3491 N LEU D 149-33.912 65.566-34. 860 1.00 15. 02 3492 CA LEU D 149-33.629 66.997-34. 887 1.00 17.13 3493 CB LEU D 149-33.201 67. 410-36. 301 1.00 15.85 3494 CG LEU D 149-32.006 66.679-36. 936 1.00 17.92 3495 CD1 LEU D 149-31.940 66.990-38. 424 1.00 18. 38 1 2 3 4 5 6 7 8 9 10 3496 CD2 LEU D 149-30.722 67.094-36. 248 1.00 18.08 3497 C LEU D 149-34.903 67.763-34. 508 1.00 17.56 3498 O LEU D 149-36. 007 67.354-34. 880 1. 00 16.14 3499 N ILE D 150-34.758 68.855-33. 760 1.00 15.87 3500 CA ILE D 150-35.915 69.680-33. 396 1.00 17.02 3501 CB ILE D 150-36.228 69.641-31. 873 1.00 17.39 3502 CG2 ILE D 150-36.725 68.255-31. 472 1.00 16.97 3503 CG1 ILE D 150-34.990 70.027-31. 055 1.00 17.84 3504 CD1 ILE D 150-35.247 70. 049-29. 550 1.00 20. 15 3505 C ILE D 150-35.615 71. 115-33. 819 1.00 18.23 3506 O ILE D 150-34.450 71.500-33. 918 1.00 18. 28 3507 N ALA D 151-36.653 71.901-34. 088 1.00 17.33 3508 CA ALA D 151-36.460 73.283-34. 512 1.00 19.17 3509 CB ALA D 151-37.807 73.959-34. 731 1.00 18. 39 3510 C ALA D 151-35.636 74.077-33. 496 1.00 21.02 3511 O ALA D 151-35.736 73.851-32. 289 1.00 19.89 3512 N ASP D 152-34.813 74.994-34. 005 1.00 22.30 3513 CA ASP D 152-33.957 75.846-33. 176 1.00 24.08 3514 CB ASP D 152-32.562 75.936-33. 808 1.00 26.98 3515 CG ASP D 152-31.570 76.739-32. 965 1.00 29.25 3516 OD1 ASP D 152-30.396 76.822-33. 373 1.00 30.29 3517 OD2 ASP D 152-31.947 77.289-31. 910 1.00 29. 38 3518 C ASP D 152-34.605 77.226-33. 121 1.00 25.79 3519 O ASP D 152-34.556 77.982-34. 093 1.00 25.37 3520 N SER D 153-35.229 77.549-31. 995 1. 00 26.55 3521 CA SER D 153-35.901 78.838-31. 860 1.00 31.28 3522 CB SER D 153-36.811 78.826-30. 625 1.00 29.44 3523 OG SER D 153-36.079 78.553-29. 442 1.00 31.10 3524 C SER D 153-34.948 80.031-31. 767 1.00 33.00 3525 O SER D 153-35.367 81.178-31. 936 1.00 34.59 3526 N GLU D 154-33.675 79.753-31. 504 1.00 35.71 3527 CA GLU D 154-32.676 80.820-31. 374 1.00 39.49 3528 CB GLU D 154-31. 525 80.353-30. 479 1. 00 42.33 2 3 4 5 6 7 8 9 10 3529 CG GLU D 154-31.962 79.959-29. 064 1.00 48.87 3530 CD GLU D 154-30.808 79.443-28. 211 1.00 53.21 3531 OE1 GLU D 154-29.655 79.416-28. 708 1.00 55.43 3532 OE2 GLU D 154-31.054 79.063-27. 042 1.00 54.07 3533 C GLU D 154-32.088 81.329-32. 700 1.00 39.60 3534 O GLU D 154-31.282 82.261-32. 700 1.00 39.93 3535 N THR D 155-32.509 80.729-33. 813 1.00 38.52 3536 CA THR D 155-31.999 81.167-35. 113 1.00 38.04 3537 CB THR D 155-30. 908 80.197-35. 638 1. 00 39.33 3538 OG1 THR D 155-30.582 80. 517-36.992 1.00 43. 38 3539 CG2 THR D 155-31. 373 78.765-35. 560 1.00 40.65 3540 C THR D 155-33.110 81.293-36. 157 1.00 36.34 3541 O THR D 155-34.117 80.578-36. 102 1.00 35. 30 3542 N PRO D 156-32. 941 82.208-37. 123 1.00 34.47 3543 CD PRO D 156-31.902 83. 251-37. 129 1. 00 35. 19 3544 CA PRO D 156-33.919 82.443-38. 196 1.00 33.97 3545 CB PRO D 156-33.406 83.722-38. 866 1.00 34.78 3546 CG PRO D 156-32.627 84.405-37. 766 1.00 35.68 3547 C PRO D 156-34. 012 81.291-39. 197 1.00 32.42 3548 O PRO D 156-33.106 80.462-39. 286 1.00 30.52 3549 N THR D 157-35.114 81. 248-39. 944 1.00 31.96 3550 CA THR D 157-35.303 80.211-40. 947 1. 00 31. 46 3551 CB THR D 157-36.713 80.254-41. 560 1.00 32.02 3552 OG1 THR D 157-36.941 81.543-42. 142 1.00 33.80 3553 CG2 THR D 157-37.769 79.979-40. 495 1.00 32.68 3554 C THR D 157-34.287 80.457-42. 052 1.00 31.88 3555 O THR D 157-33.812 81.581-42. 230 1.00 29.90 3556 N ILE D 158-33.960 79.404-42. 790 1.00 30.57 3557 CA ILE D 158-32.988 79.487-43. 874 1.00 32. 03 3558 CB ILE D 158-32.061 78.250-43. 852 1. 00 31. 60 3559 CG2 ILE D 158-31. 041 78.332-44. 988 1. 00 32. 56 3560 CG 1 ILE D 158-31. 374 78.155-42. 486 1.00 31.82 3561 CD1 ILE D 158-30. 707 76.825-42. 211 1.00 32.61 1 2 3 4 5 6 7 8 9 10 3562 C ILE D 158-33.680 79.570-45. 233 1.00 33. 32 3563 O ILE D 158-34.556 78.759-45. 543 1.00 33.34 3564 N GLN D 159-33.291 80. 560-46. 034 1.00 33.90 3565 CA GLN D 159-33.860 80. 745-47. 366 1.00 34.94 3566 CB GLN D 159-34.207 82.218-47. 603 1.00 35.35 3567 CG GLN D 159-35.233 82.796-46. 638 1.00 33.67 3568 CD GLN D 159-36.571 82. 093-46.718 1.00 33.23 3569 OBI GLN D 159-37.200 82. 050-47.774 1.00 32.45 3570 NE2 GLN D 159-37.017 81.538-45. 596 1.00 32.83 3571 C GLN D 159-32.848 80.291-48. 411 1.00 36.41 3572 O GLN D 159-31.702 80. 733-48.400 1.00 37.67 3573 N LYS D 160-33.266 79.407-49. 311. 1.00 36.69 3574 CA LYS D 160-32.373 78.915-50. 353 1.00 37. 24 3575 CB LYS D 160-31.427 77.848-49. 787 1.00 36.97 3576 CG LYS D 160-30.348 77.392-50. 769 1.00 38.83 3577 CD LYS D 160-29. 262 76.562-50. 089 1. 00 39.52 3578 CE LYS D 160-28.109 76.265-51. 052 1.00 41.44 3579 NZ LYS D 160-26.977 75. 544-50. 396 1.00 40. 12 3580 C LYS D 160-33.162 78. 342-51. 526 1.00 38.42 3581 O LYS D 160-33.957 77. 417-51. 359 1.00 37.83 3582 N GLY D 161-32.942 78.909-52. 710 1.00 38.55 3583 CA GLY D 161-33.629 78.448-53. 904 1.00 38.92 3584 C GLY D 161-35.144 78.534-53. 852 1.00 39.71 3585 O GLY D 161-35.825 77.646-54. 364 1.00 40.91 3586 N SER D 162-35.664 79.599-53. 243 1.00 39.23 3587 CA SER D 162-37.107 79.836-53. 108 1.00 39.86 3588 CB SER D 162 -37.796 79.818 -54.479 1.00 41.80 3589 OG SER D 162 -37.948 78.497 -54.972 1.00 46.92 3590 C SER D 162 -37.806 78.845 -52.170 1.00 38.00 3591 O SER D 162-39.028 78.681-52. 215 1.00 37.20 3592 N TYR D 163-37.018 78. 187-51. 328 1.00 36.03 3593 CA TYR D 163-37.535 77. 229-50. 354 1.00 33.48 3594 CB TYR D 163-36.906 75.849-50. 556 1.00 36.84 2 3 4 5 6 7 8 9 10 3595 CG TYR D 163-37.537 74.994-51. 633 1.00 42.01 3596 CD1 TYR D 163-37.732 75.483-52. 923 1.00 44.48 3597 CE1 TYR D 163-38.270 74.672-53. 925 1.00 47.14 3598 CD2 TYR D 163-37.900 73.674-51. 368 1.00 43.62 3599 CE2 TYR D 163-38.436 72.859-52. 358 1.00 45. 31 3600 CZ TYR D 163-38.618 73.360-53. 632 1. 00 46.19 3601 OH TYR D 163-39.137 72.545-54. 611 1.00 49.70 3602 C TYR D 163-37.147 77.730-48. 977 1.00 30.49 3603 O TYR D 163-36.139 78.424-48. 825 1. 00 29. 09 3604 N THR D 164-37. 945 77.384-47. 974 1.00 24.93 3605 CA THR D 164-37.644 77.773-46. 609 1.00 22. 75 3606 CB THR D 164-38.883 78.354-45. 890 1.00 22.26 3607 OG1 THR D 164-39. 331 79.534-46. 574 1.00 24.97 3608 CG2 THR D 164-38.537 78.707-44. 449 1.00 22.08 3609 C THR D 164-37.193 76.509-45. 882 1.00 23.38 3610 O THR D 164-37.848 75.464-45. 974 1.00 21.40 3611 N PHE D 165-36.066 76.593-45. 186 1.00 21.02 3612 CA PHE D 165-35.552 75.455-44. 443 1.00 21.53 3613 CB PHE D 165-34.145 75. 077-44. 915 1.00 22.22 3614 CG PHE D 165-34.110 74. 515-46. 302 1 00 22 70 3615 CD1 PHE D 165-33. 967 75. 353-47. 402 1.00 22.87 3616 CD2 PHE D 165-34.254 73.144-46. 513 1.00 22.16 3617 CE1 PHE D 165-33.977 74.837-48. 694 1.00 23.52 3618 CE2 PHE D 165-34.266 72.618-47. 799 1.00 23.03 3619 CZ PHE D 165-34.124 73.464-48. 891 1.00 24.57 3620 C PHE D 165-35. 522 75.764-42. 962 1.00 23.84 3621 O PHE D 165-35.074 76.834-42. 545 1.00 24.40 3622 N VAL D 166-36.012 74.819-42. 169 1.00 23.31 3623 CA VAL D 166-36.035 74.962-40. 723 1.00 21.61 3624 CB VAL D 166-36.928 73. 872-40. 059 1. 00 19. 98 3625 CG1 VAL D 166-36.896 74.019-38. 544 1.00 19.50 3626 CG2 VAL D 166-38. 365 73. 964-40. 577 1.00 20.28 3627 C VAL D 166-34.619 74. 777-40.202 1.00 22.07 1 2 3 4 5 6 7 8 9 10 3628 O VAL D 166-33.917 73.859-40. 625 1.00 22.59 3629 N PRO D 167-34. 167 75.662-39. 299 1.00 21.97 3630 CD PRO D 167-34.776 76. 948-38. 904 1.00 23.18 3631 CA PRO D 167-32.816 75.524-38. 746 1.00 21.26 3632 CB PRO D 167-32.524 76.916-38. 197 1.00 22.82 3633 CG PRO D 167-33. 888 77.398-37. 757 1.00 22.58 3634 C PRO D 167-32.916 74.462-37. 647 1.00 21. 34 3635 O PRO D 167-33.704 74.611-36. 708 1.00 20. 39 3636 N TRP D 168-32.132 73. 394-37. 760 1.00 19.44 3637 CA TRP D 168-32.205 72. 317-36. 782 1.00 20.72 3638 CB TRP D 168-32. 104 70.950-37. 477 1.00 18.75 3639 CG TRP D 168-33.154 70.669-38. 519 1.00 19.74 3640 CD2 TRP D 168-34.572 70.555-38. 315 1.00 19.15 3641 CE2 TRP D 168-35.153 70.265-39. 573 1.00 19.03 3642 CE3 TRP D 168-35.405 70.665-37. 193 1.00 18.04 3643 CD1 TRP D 168-32.944 70.450-39. 854 1.00 19.61 3644 NE1 TRP D 168-34.137 70.207-40. 492 1.00 19.26 3645 CZ2 TRP D 168-36.538 70.088-39. 741 1.00 19.23 3646 CZ3 TRP D 168-36.787 70.488-37. 360 1.00 18.06 3647 CH2 TRP D 168-37.334 70.202-38. 627 1.00 17.33 3648 C TRP D 168-31.180 72. 332-35. 656 1.00 22. 06 3649 O TRP D 168-30.060 72.812-35. 807 1.00 23.57 3650 N LEU D 169-31.605 71.790-34. 522 1.00 20.81 3651 CA LEU D 169-30.775 71.616-33. 344 1.00 23.46 3652 CB LEU D 169-31.406 72.285-32. 119 1.00 25.75 3653 CG LEU D 169-30.789 71.880-30. 777 1.00 30. 34 3654 CD1 LEU D 169-29. 333 72.353-30. 722 1. 00 32.19 3655 CD2 LEU D 169-31.593 72.482-29. 632 1. 00 33.10 3656 C LEU D 169-30.801 70.099-33. 156 1.00 23.22 3657 O LEU D 169-31.854 69.477-33. 325 1.00 23.25 3658 N LEU D 170-29.665 69.497-32. 828 1.00 21.30 3659 CA LEU D 170-29.624 68.056-32. 622 1.00 22.04 3660 CB LEU D 170-28.175 67.561-32. 530 1.00 24.26 1 2 3 4 5 6 7 8 9 10- 3661 CG LEU D 170-28.004 66.049-32. 319 1.00 25.09 3662 CD1 LEU D 170-28.418 65.305-33. 587 1.00 26.00 3663 CD2 LEU D 170-26.559 65.731-31. 973 1.00 28.44 3664 C LEU D 170-30. 362 67.685-31. 335 1. 00 22.64 3665 O LEU D 170-30.045 68.198-30. 262 1.00 21.67 3666 N SER D 171-31.359 66.810-31. 446 1.00 20.12 3667 CA SER D 171-32.107 66.361-30. 279 1.00 18.42 3668 CB SER D 171-33.503 65.878-30. 703 1.00 18. 30 3669 OG SER D 171-34.159 65.203-29. 646 1.00 18.31 3670 C SER D 171-31.294 65.217-29. 664 1.00 18. 72 3671 O SER D 171-31.028 65.197-28. 461 1.00 18.88 3672 N PHE D 172-30. 902 64. 261-30. 500 1.00 19.74 3673 CA PHE D 172-30.082 63.143-30. 051 1. 00 19. 72 3674 CB PHE D 172-30.855 62.243-29. 067 1.00 20.48 3675 CG PHE D 172-31.790 61.259-29. 734 1.00 21.25 3676 CD1 PHE D 172-31. 318 60.029-30. 194 1.00 22. 30 3677 CD2 PHE D 172-33. 140 61.562-29. 900 1.00 19.89 3678 CE1 PHE D 172-32.177 59.117-30. 825 1.00 21. 52 3679 CE2 PHE D 172-34.009 60.660-30. 529 1.00 18.20 3680 CZ PHE D 172-33.527 59.435-30. 986 1.00 19.92 3681 C PHE D 172-29.608 62.321-31. 244 1.00 21.81 3682 O PHE D 172-30.214 62. 350-32. 317 1.00 18.32 3683 N LYS D 173-28.501 61.612-31. 043 1.00 21.66 3684 CA LYS D 173-27.926 60.732-32. 050 1.00 24.56 3685 CB LYS D 173-26.650 61.345-32. 639 1. 00 26.41 3686 CG LYS D 173-25.790 60. 374-33. 456 1.00 27.71 3687 CD LYS D 173-24.551 61. 078-34. 003 1.00 31. 81 3688 CE LYS D 173-23.578 60.110-34. 665 1.00 34.68 3689 NZ LYS D 173-22.954 59.194-33. 678 1.00 37.03 3690 C LYS D 173-27.590 59. 432-31. 327 1.00 25.18 3691 O LYS D 173-26.860 59.440-30. 336 1.00 26.27 3692 N ARG D 174-28.149 58.321-31. 789 1.00 24. 05 3693 CA ARG D 174-27. 851 57.037-31. 168 1.00 25.00 1 2 3 4 5 6 7 8 9 10 3694 CB ARG D 174-29.098 56. 408-30. 535 1.00 26.14 3695 CG ARG D 174-28.746 55.127-29. 788 1.00 29.61 3696 CD ARG D 174-29. 877 54.554-28. 956 1.00 33.41 3697 NE ARG D 174-30.856 53.844-29. 761 1.00 35.02 3698 CZ ARG D 174-31.478 52.736-29. 373 1.00 33.14 3699 NHI ARG D 174-31.218 52.201-28. 188 1.00 32.94 3700 NH2 ARG D 174-32.373 52.168-30. 169 1.00 30.59 3701 C ARG D 174-27.280 56.088-32. 213 1.00 25.83 3702 O ARG D 174-27.898 55.854-33. 256 1.00 21.60 3703 N GLY D 175-26.100 55.543-31. 929 1.00 25.92 3704 CA GLY D 175-25.464 54.640-32. 870 1.00 26.90 3705 C GLY D 175-24.629 55.418-33. 869 1.00 27. 34 3706 O GLY D 175-24. 389 56.613-33. 684 1.00 29.23 3707 N SER D 176-24.207 54.757-34. 942 1.00 27.85 3708 CA SER D 176-23. 369 55. 406-35. 946 1.00 28.36 3709 CB SER D 176-22.001 54.725-35. 973 1.00 30.68 3710 OG SER D 176-22.151 53.350-36. 292 1.00 34.07 3711 C SER D 176-23.934 55.426-37. 366 1.00 26.75 3712 O SER D 176-23.353 56.047-38. 254 1.00 26.02 3713 N ALA D 177-25.060 54. 757-37. 583 1.00 24.92 3714 CA ALA D 177-25.658 54.701-38. 914 1.00 23.54 3715 CB ALA D 177-26.793 53.684-38. 922 1.00 24.02 3716 C ALA D 177-26.158 56.041-39. 463 1.00 22.87 3717 O ALA D 177-26.289 56.204-40. 681 1. 00 22. 54 3718 N LEU D 178-26.429 56.996-38. 574 1.00 20.64 3719 CA LEU D 178-26.944 58.307-38. 970 1.00 20.40 3720 CB LEU D 178-28.442 58.390-38. 642 1.00 21.58 3721 CG LEU D 178-29.373 57. 413-39. 371 1.00 23. 04 3722 CD1 LEU D 178-30.654 57.215-38. 580 1.00 22.30 3723 CD2 LEU D 178-29.668 57.945-40. 771 1.00 20. 24 3724 C LEU D 178-26.211 59.453-38. 271 1.00 20.06 3725 O LEU D 178-25.872 59. 354-37. 094 1.00 21.32 3726 N GLU D 179-25.982 60. 541-39. 000 1.00 20.79 1 2 3 4 5 6 7 8 9 10 3727 CA GLU D 179-25. 294 61.716-38. 457 1. 00 22.46 3728 CB GLU D 179-23.825 61.755-38. 920 1.00 22.78 3729 CG GLU D 179-22. 962 60.585-38. 489 1.00 25.19 3730 CD GLU D 179-21.532 60.686-39. 026 1.00 28.87 3731 OE1 GLU D 179-21.207 61.696-39. 690 1.00 28. 31 3732 OE2 GLU D 179-20.735 59.755-38. 782 1.00 27. 69 3733 C GLU D 179-25.964 62.981-38. 965 1.00 21.33 3734 O GLU D 179-26.738 62.941-39. 917 1.00 20.99 3735 N GLU D 180-25.674 64. 108-38. 326 1.00 21.25 3736 CA GLU D 180-26.213 65.375-38. 797 1.00 23.92 3737 CB GLU D 180-26.622 66.298-37. 642 1.00 26.78 3738 CG GLU D 180-26. 907 67.729-38. 127 1.00 29.72 3739 CD GLU D 180-27. 336 68.683-37. 024 1.00 34.26 3740 OE1 GLU D 180-26.952 68.469-35. 852 1.00 33.97 3741 OE2 GLU D 180-28.046 69.666-37. 339 1.00 35. 69 3742 C GLU D 180-25.100 66.046-39. 591 1.00 25.11 3743 O GLU D 180-23.943 66.050-39. 166 1.00 26.87 3744 N LYS D 181-25.443 66.602-40. 744 1.00 24.10 3745 CA LYS D 181-24.455 67.283-41. 573 1.00 27.16 3746 CB LYS D 181-23.809 66. 317-42. 577 1.00 29. 22 3747 CG LYS D 181-22.770 66.993-43. 466 1.00 34.41 3748 CD LYS D 181-22. 228 66.060-44. 533 1.00 38.59 3749 CE LYS D 181-21.139 66.750-45. 347 1.00 42.03 3750 NZ LYS D 181-20.709 65.932-46. 516 1.00 43. 97 3751 C LYS D 181-25.082 68. 435-42. 336 1.00 25.30 3752 O LYS D 181-25.960 68.232-43. 167 1.00 23. 96 3753 N GLU D 182-24.622 69.647-42. 042 1.00 26.27 3754 CA GLU D 182-25.113 70.849-42. 704 1.00 26.70 3755 CB GLU D 182-24.566 70.915-44. 130 1.00 31. 80 3756 CG GLU D 182-23.046 70.823-44. 209 1.00 38. 96 3757 CD GLU D 182-22.547 70.732-45. 640 1.00 44.08 3758 OE1 GLU D 182-22.953 69.789-46. 355 1.00 45.88 3759 OE2 GLU D 182-21.749 71.602-46. 049 1.00 48. 82 1 2 3 4 5 6 7 8 9 10 3760 C GLU D 182-26.638 70.944-42. 733 1.00 24.98 3761 O GLU D 182-27.236 71. 129-43. 793 1.00 23. 67 3762 N ASN D 183-27.253 70. 809-41. 562 1.00 23.15 3763 CA ASN D 183-28.706 70.909-41. 416 1.00 22. 88 3764 CB ASN D 183-29.196 72.255-41. 967 1.00 21. 89 3765 CG ASN D 183-30.436 72.776-41. 239 1.00 23.16 3766 OD1 ASN D 183-31.406 73.210-41. 864 1.00 24. 05 3767 ND2 ASN D 183-30.398 72.743-39. 912 1.00 19.49 3768 C ASN D 183-29.470 69.773-42. 109 1. 00 22.75 3769 O ASN D 183-30.671 69.897-42. 363 1.00 24. 33 3770 N LYS D 184-28.772 68.678-42. 409 1.00 20.92 3771 CA LYS D 184-29.378 67. 516-43. 059 1. 00 20. 26 3772 CB LYS D 184-28.884 67. 395-44. 507 1.00 21.70 3773 CG LYS D 184-29.295 68. 557-45. 401 1.00 23.68 3774 CD LYS D 184-28.775 68.394-46. 824 1.00 27.68 3775 CE LYS D 184-27.272 68.596-46. 895 1.00 32.05 3776 NZ LYS D 184-26.893 69.988-46. 543 1. 00 37.05 3777 C LYS D 184-29. 017 66. 245-42.302 1.00 19.59 3778 O LYS D 184-28.142 66.258-41. 439 1.00 19.68 3779 N ILE D 185-29.703 65.149-42. 616 1.00 18.66 3780 CA ILE D 185-29.412 63.871-41. 982 1.00 19.44 3781 CB ILE D 185-30. 707 63.100-41. 622 1.00 19. 22 3782 CG2 ILE D 185-30. 351 61.759-40. 991 1.00 19.09 3783 CG1 ILE D 185-31.548 63.922-40. 634 1. 00 18.72 3784 CD1 ILE D 185-32.844 63.244-40. 198 1.00 18.86 3785 C ILE D 185-28.583 63.050-42. 972 1.00 20.12 3786 O ILE D 185-29. 014 62. 803-44. 102 1.00 21.27 3787 N LEU D 186-27.387 62.644-42. 552 1.00 20.92 3788 CA LEU D 186-26.495 61. 863-43. 407 1.00 20.50 3789 CB LEU D 186-25.048 62. 357-43. 265 1.00 21. 83 3790 CG LEU D 186-23.968 61. 539-43. 995 1.00 23.01 3791 CD1 LEU D 186-24.142 61. 677-45. 507 1.00 22.15 3792 CD2 LEU D 186-22. 584 62. 028-43. 576 1.00 23.13 1 2 3 4 5 6 7 8 9 10 3793 C LEU D 186-26.547 60.378-43. 081 1.00 20.89 3794 O LEU D 186-26.448 59.984-41. 917 1.00 20.00 3795 N VAL D 187-26. 703 59.560-44. 121 1.00 20.23 3796 CA VAL D 187-26.757 58.109-43. 972 1.00 20. 32 3797 CB VAL D 187-27.634 57.474-45. 075 1.00 20.73 3798 CG1 VAL D 187-27.633 55. 961-44. 932 1.00 20.40 3799 CG2 VAL D 187-29.055 58.020-44. 987 1.00 20.13 3800 C VAL D 187-25.344 57.537-44. 079 1.00 22. 31 3801 O VAL D 187-24.650 57.775-45. 067 1.00 20.88 3802 N LYS D 188-24.932 56.781-43. 064 1.00 24.13 3803 CA LYS D 188-23.601 56.179-43. 030 1.00 27.94 3804 CB LYS D 189-22. 934 56.489-41. 685 1.00 27.89 3805 CG LYS D 188-22.882 57.981-41. 369 1.00 31.55 3806 CD LYS D 188-21.462 58.527-41. 377 1.00 35.60 3807 CE LYS D 188-20.764 58.333-42. 708 1.00 37.85 3808 NZ LYS D 188-19. 364 58.857-42. 656 1.00 38.76 3809 C LYS D 188-23.628 54.664-43. 258 1.00 28. 90 3810 O LYS D 188-22.579 54.029-43. 387 1.00 29.59 3811 N GLU D 189-24.826 54. 089-43. 306 1.00 28.83 3812 CA GLU D 189-24.983 52.649-43. 516 1.00 28.65 3813 CB GLU D 189-25.114 51.928-42. 172 1. 00 30.64 3814 CG GLU D 189-23. 832 51.858-41. 374 1.00 35.59 3815 CD GLU D 189-24.061 51.403-39. 947 1.00 38.70 3816 OE1 GLU D 189-24.842 50.444-39. 748 1.00 40.78 3817 OE2 GLU D 189-23.455 51.999-39. 027 1.00 40.93 3818 C GLU D 189-26.210 52. 356-44. 367 1.00 27.65 3819 0 GLU D 189-27.303 52. 838-44. 074 1.00 26.96 3820 N THR D 190-26.027 51.562-45. 420 1. 00 24.39 3821 CA THR D 190-27.127 51.213-46. 314 1.00 23.52 3822 CB THR D 190-26.597 50.472-47. 574 1.00 23. 78 3823 OG1 THR D 190-25.705 51.338-48. 290 1. 00 22.15 3824 CG2 THR D 190-27.750 50. 074-48. 500 1.00 22.39 3825 C THR D 190-28.155 50.342-45. 593 1. 00 22. 11 1 2 3 4 5 6 7 8 9 10 3826 0 THR D 190-27.790 49.475-44. 796 1.00 22.64 3827 N GLY D 191-29.438 50.585-45. 865 1.00 21.98 3828 CA GLY D 191-30.493 49. 810-45. 226 1.00 20.63 3829 C GLY D 191-31.894 50.398-45. 350 1.00 20.50 3830 O GLY D 191-32.145 51. 257-46. 193 1.00 19.64 3831 N TYR D 192-32.807 49.915-44. 509 1.00 20.40 3832 CA TYR D 192-34.199 50.376-44. 487 1.00 20.21 3833 CB TYR D 192-35.146 49. 182-44. 325 1.00 21.21 3834 CG TYR D 192-35.201 48.261-45. 529 1.00 23.62 3835 CD1 TYR D 192-36.338 48.204-46. 336 1.00 23.87 3836 CE1 TYR D 192-36. 394 47. 355-47. 446 1. 00 26.95 3837 CD2 TYR D 192-34.116 47.448-45. 860 1.00 25.41 3838 CE2 TYR D 192-34.161 46.597-46. 968 1.00 27.83 3839 CZ TYR D 192-35. 302 46.556-47. 755 1.00 27.86 3840 OH TYR D 192-35.349 45.715-48. 843 1.00 30.89 3841 C TYR D 192-34.386 51. 335-43. 311 1.00 18.19 3842 O TYR D 192-34.018 51.012-42. 186 1.00 18.28 3843 N PHE D 193-34.978 52.496-43. 571 1.00 18. 40 3844 CA PHE D 193-35.176 53.503-42. 530 1.00 18.26 3845 CB PHE D 193-34. 276 54.723-42. 787 1.00 17.91 3846 CG PHE D 193-32.803 54.426-42. 759 1.00 19.72 3847 CD1 PHE D 193-32.178 53.814-43. 844 1.00 19.68 3848 CD2 PHE D 193-32.038 54.767-41. 646 1.00 17.63 3849 CE1 PHE D 193-30.807 53.548-43. 824 1.00 19.69 3850 CE2 PHE D 193-30.665 54.506-41. 613 1.00 20.21 3851 CZ PHE D 193-30. 049 53.894-42. 706 1.00 21.05 3852 C PHE D 193-36.602 54. 036-42. 392 1.00 17. 59 3853 O PHE D 193-37.282 54.284-43. 390 1.00 17. 10 3854 N PHE D 194-37.035 54.227-41. 149 1.00 17.24 3855 CA PHE D 194-38.338 54.825-40. 875 1.00 16.80 3856 CB PHE D 194-38.931 54.314-39. 561 1.00 17. 53 3857 CG PHE D 194-40.201 55. 023-39. 154 1.00 19.44 3858 CD1 PHE D 194-41. 354 54.908-39. 924 1 00 19. 75 1 2 3 4 5 6 7 8 9 10 3859 CD2 PHE D 194-40. 235 55. 820-38. 013 1.00 20.16 3860 CE1 PHE D 194-42.539 55.558-39. 548 1.00 20.47 3861 CE2 PHE D 194-41.405 56.471-37. 629 1.00 20. 80 3862 CZ PHE D 194-42.559 56.347-38. 407 1.00 19.62 3863 C PHE D 194-37.998 56.307-40. 723 1.00 17.69 3864 O PHE D 194-37. 132 56.666-39. 914 1.00 16.77 3865 N ILE D 195-38.673 57.157-41. 491 1. 00 16.06 3866 CA ILE D 195-38.416 58.593-41. 480 1.00 16.47 3867 CB ILE D 195-37.873 59.029-42. 849 1.00 18.65 3868 CG2 ILE D 195-37.552 60.514-42. 848 1. 00 20.03 3869 CG1 ILE D 195-36.628 58. 204-43. 185 1.00 18.77 3870 CD1 ILE D 195-36.275 58.232-44. 658 1.00 22.86 3871 C ILE D 195-39.686 59. 380-41. 172 1.00 18. 06 3872 O ILE D 195-40.761 59.063-41. 690 1.00 16.61 3873 N TYR D 196-39.556 60. 417-40. 349 1.00 15.60 3874 CA TYR D 196-40.706 61. 225-39. 959 1.00 16.70 3875 CB TYR D 196-41.256 60.708-38. 625 1.00 15.16 3876 CG TYR D 196-40. 240 60. 738-37. 493 1.00 16.88 3877 CD1 TYR D 196-40. 173 61.820-36. 606 1.00 15. 49 3878 CEI TYR D 196-39.226 61.851-35. 572 1. 00 16.68 3879 CD2 TYR D 196-39. 335 59.690-37. 319 1.00 16.85 3880 CE2 TYR D 196-38.387 59.712-36. 289 1.00 16.41 3881 CZ TYR D 196-38. 341 60.795-35. 420 1.00 17.97 3882 OH TYR D 196-37. 407 60. 814-34. 400 1.00 17.56 3883 C TYR D 196-40. 380 62.712-39. 842 1.00 17.76 3884 O TYR D 196-39. 240 63.094-39. 561 1.00 16.14 3885 N GLY D 197-41.396 63. 542-40. 057 1.00 16.30 3886 CA GLY D 197-41.224 64. 978-39. 970 1.00 17.19 3887 C GLY D 197-42.538 65.717-39. 766 1.00 18. 55 3888 O GLY D 197-43.560 65. 364-40. 361 1.00 18.18 3889 N GLN D 198-42.511 66.737-38. 915 1.00 16.20 3890 CA GLN D 198-43. 693 67.553-38. 641 1.00 15.84 3891 CB GLN D 198-44.324 67. 152-37. 305 1.00 14.05 1 2 3 4 5 6 7 8 9 10 3892 CG GLN D 198-45.527 68.002-36. 907 1.00 14.84 3893 CD GLN D 198-46.112 67.583-35. 570 1.00 16.26 3894 OE1 GLN D 198-46.510 66.434-35. 395 1.00 19.78 3895 NE2 GLN D 198-46.164 68.515-34. 619 1.00 15.13 3896 C GLN D 198-43. 300 69.027-38. 579 1.00 16.24 3897 O GLN D 198-42.201 69.363-38. 144 1.00 14.71 3898 N VAL D 199-44.211 69.894-39. 007 1.00 15.20 3899 CA VAL D 199-44.001 71. 338-39. 001 1.00 14.67 3900 CB VAL D 199-43.595 71.859-40. 402 1.00 13.14 3901 CG1 VAL D 199-43.508 73. 385-40. 389 1.00 15.63 3902 CG2 VAL D 199-42.258 71.245-40. 829 1.00 14.86 3903 C VAL D 199-45. 320 72.008-38. 633 1.00 17.12 3904 O VAL D 199-46.383 71.536-39. 037 1.00 16.26 3905 N LEU D 200-45. 250 73.089-37. 861 1. 00 18.08 3906 CA LEU D 200-46.446 73.845-37. 492 1.00 19.71 3907 CB LEU D 200-46.448 74.208-36. 004 1.00 18.16 3908 CG LEU D 200-47.530 75. 221-35. 580 1.00 19.58 3909 CD1 LEU D 200-48.923 74.737-36. 007 1.00 18.64 3910 CD2 LEU D 200-47.479 75.413-34. 069 1.00 19.38 3911 C LEU D 200-46.471 75.120-38. 325 1.00 21.03 3912 O LEU D 200-45.589 75.976-38. 197 1.00 20.88 3913 N TYR D 201-47.484 75.239-39. 178 1.00 20.55 3914 CA TYR D 201-47.633 76.397-40. 049 1.00 24.04 3915 CB TYR D 201-48. 152 75.959-41. 419 1.00 24. 80 3916 CG TYR D 201-47.221 74.990-42. 106 1.00 25. 72 3917 CD1 TYR D 201-47.395 73.610-41. 982 1.00 26.78 3918 CE1 TYR D 201-46.493 72.714-42. 566 1.00 26. 48 3919 CD2 TYR D 201-46.129 75.454-42. 832 1.00 26. 18 3920 CE2 TYR D 201-45. 223 74.574-43. 419 1. 00 26.82 3921 CZ TYR D 201-45.406 73.208-43. 280 1.00 26.73 3922 OH TYR D 201-44.482 72.347-43. 836 1.00 26.44 3923 C TYR D 201-48. 554 77.446-39. 459 1.00 26.64 3924 O TYR D 201-49. 621 77. 130-38. 927 1.00 23.43 -2 3 4 5 6 7 8 9 10 3925 N THR D 202-48.125 78.701-39. 555 1.00 28.22 3926 CA THR D 202-48.890 79.818-39. 001 1.00 32.05 3927 CB THR D 202-48. 146 80.483-37. 852 1.00 31.68 3928 OG1 THR D 202-46.903 81.002-38. 328 1.00 31.90 3929 CG2 THR D 202-47.891 79.473-36. 735 1.00 31.13 3930 C THR D 202-49.112 80.818-40. 103 1.00 36.27 3931 O THR D 202-49.285 82.010-39. 855 1. 00 37. 04 3932 N ASP D 203-49.087 80. 320-41. 317 1.00 43.93 3933 CA ASP D 203-49.248 81.114-42. 513 1.00 47.69 3934 CB ASP D 203-48.345 80.523-43. 601 1.00 50.72 3935 CG ASP D 203-48.003 81.515-44. 688 1.00 52.69 3936 OD1 ASP D 203-48.938 82.051-45. 320 1.00 54.57 3937 OD2 ASP D 203-46.795 81.748-44. 914 1.00 53.59 3938 C ASP D 203-50.705 81.129-42. 984 1.00 48.35 3939 O ASP D 203-51.431 80. 156-42. 793 1.00 47.70 3940 N LYS D 204-51.135 82.226-43. 601 1.00 49.76 3941 CA LYS D 204-52.511 82. 321-44. 084 1.00 52.02 3942 CB LYS D 204-53.010 83.770-44. 002 1.00 54. 30 3943 CG LYS D 204-52.900 84.388-42. 615 1.00 57. 73 3944 CD LYS D 204-53.818 85.598-42. 460 1.00 60. 40 3945 CE LYS D 204-53.559 86. 663-43. 519 1.00 62.00 3946 NZ LYS D 204-54.513 87.801-43. 395 1.00 64.12 3947 C LYS D 204-52.693 81.797-45. 512 1.00 51.83 3948 O LYS D 204-53.814 81.760-46. 019 1.00 51.41 3949 N THR D 205-51.598 81. 390-46. 154 1.00 53.23 3950 CA THR D 205-51.656 80.860-47. 520 1.00 54.07 3951 CB THR D 205 -50.271 80.371 -48.006 1.00 54.93 3952 OG1 THR D 205 -49.339 81.461 -47.986 1.00 56.03 3953 CG2 THR D 205-50.375 79.823-49. 425 1.00 54.87 3954 C THR D 205-52. 630 79.686-47. 587 1.00 53.69 3955 O THR D 205-52.603 78.799-46. 733 1.00 54.24 3956 N TYR D 206-53.500 79.681-48. 617 1.00 52.25 3957 CA TYR D 206-54.513 78. 611-48.827 1.00 52.11 1 2 3 4 5 6 7 8 9 10 3958 CB TYR D 206-55.036 78.694-50. 260 1.00 55.41 3959 CG TYR D 206-54.166 78.050-51. 287 1.00 58.55 3960 CD1 TYR D 206-54. 261 76.685-51. 558 1.00 59.22 3961 CE1 TYR D 206-53. 475 76.089-52. 540 1.00 62.07 3962 CD2 TYR D 206-53.259 78.808-52. 027 1.00 60.90 3963 CE2 TYR D 206-52.465 78.223-53. 013 1. 00 62. 09 3964 CZ TYR D 206-52.580 76.864-53. 264 1.00 62.94 3965 OH TYR D 206-51.801 76.281-54. 240 1.00 64.59 3966 C TYR D 206-54. 003 77.215-48. 421 1.00 48.75 3967 O TYR D 206-54. 721 76.508-47. 698 1.00 47.86 3968 N ALA D 207-52.791 76.812-48. 814 1.00 42.07 3969 CA ALA D 207-52.253 75.480-48. 434 1. 00 36. 44 3970 CB ALA D 207-52.498 74. 469-49. 553 1. 00 35.32 3971 C ALA D 207-50.763 75.606-48. 137 1.00 32.85 3972 O ALA D 207-50. 033 76.235-48. 906 1.00 29.67 3973 N MET D 208--50. 332 75. 025-47. 039 1.00 29.85 3974 CA MET D 208-48.934 75.009-46. 610 1.00 28. 76 3975 CB MET D 208-48.721 75.804-45. 323 1.00 28.73 3976 CG MET D 208-49.131 77.257-45. 410 1.00 34.25 3977 SD MET D 208-47.968 78.240-46. 366 1.00 38.35 3978 CE MET D 208-49.072 79.360-47. 226 1.00 41. 06 3979 C MET D 208-48.518 73.549-46. 395 1.00 28. 58 3980 O MET D 208-49. 342 72.715-46. 013 1.00 26.65 3981 N GLY D 209-47.249 73.238-46. 637 1.00 26. 31 3982 CA GLY D 209-46.788 71.872-46. 445 1.00 25.13 3983 C GLY D 209-45. 289 71.723-46. 603 1.00 24. 34 3984 O GLY D 209-44.589 72.697-46. 899 1.00 24.32 3985 N HIS D 210-44.788 70.508-46. 405 1.00 20.81 3986 CA HIS D 210-43.360 70.263-46. 535 1.00 19.23 3987 CB HIS D 210-42. 667 70.270-45. 164 1. 00 19. 11 3988 CG HIS D 210-43.182 69.242-44. 204 1.00 19.58 3989 CD2 HIS D 210-42.769 67.978-43. 942 1.00 19.76 3990 ND1 HnS D 210-44. 233 69. 485-43347 1.00 19. 98 1 2 3 4 5 6 7 8 9 10 3991 CE1 HIS D 210-44. 444 68.417-42. 596 1.00 19.01 3992 NE2 HIS D 210-43. 569 67.489-42. 937 1.00 20.67 3993 C HIS D 210-43. 052 68.964-47. 253 1.00 20.74 3994 O HIS D 210-43. 903 68.071-47. 368 1. 00 20.08 3995 N LEU D 211-41.821 68. 873-47. 739 1.00 20.34 3996 CA LEU D 211-41.359 67. 702-48. 461 1.00 20.94 3997 CB LEU D 211-40.911 68.101-49. 870 1.00 23. 33 3998 CG LEU D 211-41.786 69.077-50. 658 1.00 23.66 3999 CD1 LEU D 211-41.005 69. 594-51. 857 1.00 26.48 4000 CD2 LEU D 211-43. 079 68. 398-51. 094 1.00 24.26 4001 C LEU D 211-40.164 67.112-47. 729 1.00 21.89 4002 O LEU D 211-39.283 67.848-47. 277 1.00 23.43 4003 N ILE D 212-40. 147 65.794-47. 591 1. 00 19. 68 4004 CA ILE D 212-39.019 65.116-46. 976 1.00 22.91 4005 CB ILE D 212-39. 477 63.999-46. 010 1.00 23.85 4006 CG2 ILE D 212-38.282 63. 158-45. 576 1.00 23.82 4007 CG1 ILE D 212-40.155 64.638-44. 789 1. 00 24.03 4008 CD 1 ILE D 212-40. 754 63. 643-43. 804 1.00 27.04 4009 C ILE D 212-38.334 64.549-48. 212 1.00 23.75 4010 O ILE D 212-38.902 63. 708-48. 916 1. 00 23.21 4011 N GLN D 213-37.130 65.039-48. 494 1.00 22. 78 4012 CA GLN D 213-36.408 64.632-49. 691 1.00 22.55 4013 CB GLN D 213-36.111 65. 874-50. 540 1.00 24.71 4014 CG GLN D 213-37. 330 66.738-50. 817 1.00 24. 33 4015 CD GLN D 213-36.986 68.014-51. 571 1.00 28.06 4016 OE1 GLN D 213-36.219 68.846-51. 086 1.00 28.36 4017 NE2 GLN D 213-37.558 68.173-52. 763 1.00 28.71 4018 C GLN D 213-35. 117 63.860-49. 482 1.00 22.79 4019 O GLN D 213-34. 449 63.987-48. 459 1.00 21.59 4020 N ARG D 214-34. 774 63. 061-50. 486 1.00 21.47 4021 CA ARG D 214-33. 559 62.259-50. 476 1.00 22. 96 4022 CB ARG D 214-33. 892 60.807-50. 829 1.00 23.29 4023 CG ARG D 214-32. 679 59. 889-50. 996 1. 00 24.71 1 2 3 4 5 6 7 8 9 10 4024 CD ARG D 214-33.091 58.570-51. 651 1.00 24.91 4025 NE ARG D 214-31. 980 57.626-51. 759 1.00 28.12 4026 CZ ARG D 214-32. 000 56.534-52. 522 1.00 29.48 4027 NH1 ARG D 214-33. 074 56.247-53. 249 1.00 28.89 4028 NH2 ARG D 214-30. 945 55.731-52. 566 1.00 27.52 4029 C ARG D 214-32.584 62. 812-51. 517 1.00 24. 62 4030 O ARG D 214-32.954 63.022-52. 674 1.00 24.03 4031 N LYS D 215-31. 349 63.060-51. 097 1.00 25.87 4032 CA LYS D 215-30.311 63.539-52. 006 1.00 28.52 4033 CB LYS D 215-29.531 64.700-51. 381 1.00 30.96 4034 CG LYS D 215-28.494 65.311-52. 311 1.00 36.40 4035 CD LYS D 215-27.792 66.493-51. 669 1.00 42.34 4036 CE LYS D 215-26.775 67. 110-52. 624 1.00 46.50 4037 NZ LYS D 215-26.130 68.329-52. 056 1.00 49.54 4038 C LYS D 215-29. 403 62.323-52. 204 1.00 29.32 4039 O LYS D 215-28.633 61. 958-51. 312 1. 00 26. 09 4040 N LYS D 216-29.524 61.684-53. 364 1.00 32.49 4041 CA LYS D 216-28.749 60.487-53. 676 1.00 36. 04 4042 CB LYS D 216-29.282 59. 837-54. 954 1.00 36.86 4043 CG LYS D 216-30.762 59.502-54. 912 1.00 39.10 4044 CD LYS D 216-31.227 58.940-56. 245 1.00 39.79 4045 CE LYS D 216-32.737 58.797-56. 295 1.00 41.10 4046 NZ LYS D 216-33.206 58.389-57. 653 1.00 43. 39 4047 C LYS D 216-27.262 60.764-53. 837 1.00 38. 32 4048 O LYS D 216-26.870 61. 762-54. 439 1.00 37.48 4049 N VAL D 217-26.437 59.871-53. 297 1. 00 41. 00 4050 CA VAL D 217-24.992 60.024-53. 392 1.00 44.83 4051 CB VAL D 217-24.262 59.182-52. 314 1.00 43.96 4052 CG1 VAL D 217-24.507 57.696-52. 542 1. 00 43. 14 4053 CG2 VAL D 217-22.777 59. 495-52. 333 1.00 44. 39 4054 C VAL D 217-24.513 59.603-54. 782 1.00 47.71 4055 O VAL D 217-23. 542 60. 149-55. 303 1.00 48.35 4056 N HIS D 218-25.206 58. 637-55.380 1. 00 50.98 1 2 3 4 5 6 7 8 9 10 4057 CA HIS D 218-24. 858 58.152-56. 715 1. 00 54. 37 4058 CB HIS D 218-24.170 56.785-56. 629 1.00 57.09 4059 CG HIS D 218-22.762 56.851-56. 125 1.00 60. 33 4060 CD2 HIS D 218-22.155 56.230-55. 085 1.00 61. 37 4061 ND1 HIS D 218-21.799 57.644-56. 713 1.00 62. 10 4062 CE1 HIS D 218-20.660 57.510-56. 056 1.00 63.36 4063 NE2 HIS D 218-20.849 56.658-55. 064 1.00 62.85 4064 C HIS D 218-26.075 58.052-57. 627 1.00 54.40 4065 O HIS D 218-27.113 57.508-57. 246 1.00 54.11 4066 N VAL D 219-25.933 58.580-58. 837 1. 00 54.92 4067 CA VAL D 219-27.007 58.561-59. 820 1.00 56. 85 4068 CB VAL D 219-27.390 59.993-60. 246 1.00 56.43 4069 CG1 VAL D 219-28. 489 59.949-61. 290 1. 00 57.82 4070 CG2 VAL D 219-27.839 60. 790-59. 034 1. 00 57. 36 4071 C VAL D 219-26.587 57.779-61. 063 1.00 58.33 4072 O VAL D 219-25.523 58.025-61. 631 1.00 58.18 4073 N PHE D 220-27.425 56.831-61. 473 1.00 60.13 4074 CA PHE D 220-27.149 56.021-62. 657 1. 00 62.09 4075 CB PHE D 220-26.979 54.541-62. 292 1.00 62.82 4076 CG PHE D 220-25.914 54.273-61. 267 1.00 63.32 4077 CD1 PHE D 220-26. 144 54. 530-59. 919 1.00 63. 32 4078 CD2 PHE D 220-24.675 53.769-61. 651 1.00 63.64 4079 CE1 PHE D 220-25.160 54.272-58. 964 1.00 64.26 4080 CE2 PHE D 220-23.684 53. 508-60. 705 1.00 64.13 4081 CZ PHE D 220-23.925 53. 767-59. 359 1.00 64.22 4082 C PHE D 220-28. 302 56.151-63. 642 1.00 62.98 4083 O PHE D 220-29.410 56.535-63. 267 1.00 62.84 4084 N GLY D 221-28.035 55.825-64. 903 1. 00 64.10 4085 CA GLY D 221-29.064 55.899-65. 923 1.00 64.74 4086 C GLY D 221-29.765 57.240-66. 020 1.00 65.35 4087 O GLY D 221-29.146 58. 250-66. 360 1.00 65. 89 4088 N ASP D 222-31.059 57.250-65. 714 1.00 65. 34 4089 CA ASP D 222-31.854 58. 471-65. 790 1.00 66.03 1 2 3 4 5 6 7 8 9 10 4090 CB ASP D 222-33.015 58. 266-66.773 1.00 67.56 4091 CG ASP D 222-33.891 57.076-66. 409 1.00 69.25 4092 OD1 ASP D 222-33. 357 55.957-66. 253 1.00 70. 34 4093 OD2 ASP D 222-35.121 57. 259-66. 286 1.00 70.14 4094 C ASP D 222-32.393 58. 969-64.446 1.00 65.15 4095 O ASP D 222-33.295 59.807-64. 411 1.00 65. 35 4096 N GLU D 223-31.839 58.462-63. 348 1.00 63.57 4097 CA GLU D 223-32.272 58.875-62. 013 1.00 61.58 4098 CB GLU D 223-31.519 58.098-60. 931 1.00 62.86 4099 CG GLU D 223-31.908 56.649-60. 770 1.00 65.63 4100 CD GLU D 223-31.304 56. 042-59. 515 1. 00 67.01 4101 OE1 GLU D 223-30.063 56. 085-59. 372 1. 00 67.07 4102 OE2 GLU D 223-32.071 55.525-58. 673 1.00 67.69 4103 C GLU D 223-32.039 60.359-61. 763 1.00 58.93 4104 O GLU D 223-31.164 60.973-62. 374 1.00 58.90 4105 N LEU D 224-32.825 60.925-60. 852 1.00 55.92 4106 CA LEU D 224-32.692 62. 328-60. 480 1.00 52.07 4107 CB LEU D 224-34.069 62. 973-60. 312 1.00 53. 46 4108 CG LEU D 224-35. 047 62.807-61. 476 1.00 54.26 4109 CD1 LEU D 224-36. 352 63.513-61. 145 1.00 54.23 4110 CD2 LEU D 224-34. 438 63.369-62. 750 1.00 54.74 4111 C LEU D 224-31.947 62.341-59. 149 1.00 49.11 4112 O LEU D 224-32.095 61. 419-58. 347 1.00 48.47 4113 N SER D 225-31. 149 63. 376-58. 914 1.00 45. 36 4114 CA SER D 225-30. 379 63.475-57. 677 1.00 43. 36 4115 CB SER D 225-29.335 64. 585-57. 797 1.00 44.03 4116 OG SER D 225-28.346 64.241-58. 750 1.00 50.09 4117 C SER D 225-31.227 63.724-56. 434 1.00 39.75 4118 O SER D 225-30.992 63. 127-55. 389 1.00 38.83 4119 N LEU D 226-32.207 64.610-56. 557 1.00 37.02 4120 CA LEU D 226-33. 074 64.956-55. 438 1.00 35.59 4121 CB LEU D 226-33.071 66.473-55. 243 1.00 35.50 4122 CG LEU D 226-33.783 67. 033-54. 007 1.00 35. 88 1 2 3 4 5 6 7 8 9 10 4123 CDl LEU D 226-33.029 66. 629-52. 743 1. 00 34. 69 4124 CD2 LEU D 226-33.856 68.545-54. 115 1.00 34.85 4125 C LEU D 226-34. 499 64.472-55. 687 1. 00 34.06 4126 O LEU D 226-35.148 64.909-56. 634 1.00 33.60 4127 N VAL D 227-34.984 63.573-54. 835 1.00 31.22 4128 CA VAL D 227-36.336 63.048-54. 989 1.00 30. 15 4129 CB VAL D 227-36. 310 61. 566-55. 435 1.00 31.10 4130 CG1 VAL D 227-35.563 61.435-56. 755 1.00 32.22 4131 CG2 VAL D 227-35.649 60. 710-54. 372 1.00 33. 12 4132 C VAL D 227-37.155 63.166-53. 706 1.00 28.69 4133 O VAL D 227-36.643 62.954-52. 608 1.00 28.02 4134 N THR D 228-38.429 63. 519-53. 853 1.00 26.70 4135 CA THR D 228-39. 318 63.653-52. 708 1.00 25. 91 4136 CB THR D 228-40.541 64. 548-53. 053 1.00 26.69 4137 OUI THR D 228-40.101 65.887-53. 317 1.00 26.31 4138 CG2 THR D 228-41.538 64.567-51. 899 1. 00 25.43 4139 C THR D 228-39. 804 62.265-52. 276 1.00 25. 27 4140 O THR D 228-40.380 61. 521-53. 075 1.00 25.25 4141 N LEU D 229-39. 560 61.915-51. 017 1. 00 23.21 4142 CA LEU D 229-39. 979 60.620-50. 486 1.00 23. 18 4143 CB LEU D 229-39. 042 60. 177-49358 1.00 22.60 4144 CG LEU D 229-37.562 59.968-49. 694 1.00 23.58 4145 CD1 LEU D 229-36.800 59.661-48. 419 1.00 22. 17 4146 CD2 LEU D 229-37. 405 58. 831-50. 705 1.00 23.59 4147 C LEU D 229-41.415 60. 696-49. 958 1.00 23.69 4148 O LEU D 229-42.263 59. 872-50. 313 1.00 22.97 4149 N PHE D 230-41.676 61. 686-49. 108 1.00 22.15 4150 CA PHE D 230-43. 000 61.885-48. 527 1.00 22.78 4151 CB PHE D 230-43. 079 61.310-47. 102 1.00 22.10 4152 CG PHE D 230-42.499 59.937-46. 966 1.00 25. 89 4153 CD1 PHE D 230-41.208 59.764-46. 482 1.00 26.48 4154 CD2 PHE D 230-43. 228 58. 816-47. 350 1.00 28.52 4155 CE1 PHE D 230-40. 649 58. 488-46.376 1.00 28.27 1 2 3 4 5 6 7 8 9 10 4156 CE2 PHE D 230-42. 678 57. 536-47. 250 1. 00 28. 60 4157 CZ PHE D 230-41.384 57.374-46. 764 1.00 28.64 4158 C PHE D 230-43. 297 63. 370-48. 466 1.00 22.90 4159 O PHE D 230-42.387 64. 200-48. 368 1.00 21.94 4160 N ARG D 231 -44.576 63.710 -48.517 1.00 22.03 4161 CA ARG D 231 -44.972 65.105 -48.461 1.00 23.34 4162 CB ARG D 231 -45.123 65.620 -49.899 1.00 27.29 4163 CG ARG D 231 -46.469 66.113 -50.330 1.00 31.23 4164 CD ARG D 231-46.514 66. 110-51. 858 1. 00 35.96 4165 NE ARG D 231-47.618 66.908-52. 382 1. 00 38.47 4166 CZ ARG D 231-48.422 66. 504-53358 1.00 38.49 4167 NH1 ARG D 231-48.257 65. 318-53. 916 1.00 39.93 4168 NH2 ARG D 231-49. 389 67. 286-53. 789 1.00 44.14 4169 C ARG D 231-46.241 65.257-47. 621 1.00 24.09 4170 O ARG D 231-47.069 64.344-47. 551 1.00 23.74 4171 N CYS D 232-46.367 66.404-46. 963 1.00 23.66 4172 CA CYS D 232-47. 500 66.704-46. 088 1.00 24.86 4173 C CYS D 232-48.135 68.018-46. 547 1.00 25.01 4174 O CYS D 232-47.424 68. 916-47. 000 1.00 23.73 4175 CB CYS D 232-46.992 66.860-44. 641 1.00 26.77 4176 SG CYS D 232-48.288 66.719-43. 381 1.00 35.90 4177 N ILE D 233-49. 457 68.144-46. 438 1.00 24.26 4178 CA ILE D 233-50.107 69.398-46. 831 1.00 24.70 4179 CB ILE D 233-50. 365 69.451-48. 357 1.00 26.50 4180 CG2 ILE D 233-51.340 68.366-48. 775 1.00 28.53 4181 CG1 ILE D 233-50. 904 70.833-48. 742 1.00 29.06 4182 CD1 ILE D 233-50. 770 71.149-50. 218 1.00 29.78 4183 C ILE D 233-51. 401 69.698-46. 074 1.00 24.22 4184 O ILE D 233-52.186 68. 796-45. 783 1.00 24.53 4185 N GLN D 234-51.605 70. 979-45. 759 1.00 22.14 4186 CA GLN D 234-52.778 71. 440-45. 012 1.00 22.68 4187 CB GLN D 234-52.410 71. 648-43. 538 1.00 22.19 4188 CG GLN D 234-52.037 70.385-42. 776 1.00 21. 57 123 4 56 7 8 9 10 4189 CD GLN D 234-53.254 69.636-42. 282 1.00 22.37 4190 OE1 GLN D 234-53.942 70. 092-41. 367 1.00 22.75 4191 NE2 GLN D 234-53. 532 68. 485-42. 887 1.00 20. 32 4192 C GLN D 234-53. 339 72.761-45. 532 1.00 24.15 4193 O GLN D 234-52. 579 73. 692-45. 813 1.00 23. 28 4194 N ASN D 235-54.664 72. 838-45. 660 1.00 25.01 4195 CA ASN D 235-55. 323 74.080-46. 073 1.00 25. 14 4196 CB ASN D 235-56.800 73.851-46. 425 1.00 27.18 4197 CG ASN D 235-57. 000 73. 316-47. 829 1.00 28.33 4198 ODI ASN D 235-56.599 73.942-48. 814 1.00 30. 49 4199 ND2 ASN D 235-57. 638 72. 161-47. 929 1.00 25.87 4200 C ASN D 235-55. 263 74.952-44. 821 1.00 25.65 4201 O ASN D 235-55339 74. 434-43. 705 1.00 24.72 4202 N MET D 236-55. 135 76.264-45. 001 1.00 25.27 4203 CA MET D 236-55.061 77.188-43. 872 1.00 26.21 4204 CB MET D 236-53. 745 77. 975-43. 917 1.00 26.28 4205 CG MET D 236-52.485 77.142-44. 113 1.00 24.23 4206 SD MET D 236-52.144 76.000-42. 753 1.00 23.04 4207 CE MET D 236-51.955 77.126-41. 394 1.00 20.96 4208 C MET D 236-56.228 78. 180-43. 901 1. 00 28.00 4209 O MET D 236-56.615 78.661-44. 965 1. 00 28. 16 4210 N PRO D 237-56.801 78.499-42. 730 1.00 29.68 4211 CD PRO D 237-56.466 77.981-41. 390 1.00 29.48 4212 CA PRO D 237-57. 921 79.445-42. 656 1. 00 31.47 4213 CB PRO D 237-58.501 79.169-41. 279 1.00 30.50 4214 CG PRO D 237-57.262 78. 906-40. 473 1.00 29.84 4215 C PRO D 237-57.391 80.878-42. 778 1.00 35.70 4216 O PRO D 237-56.187 81.105-42. 700 1. 00 35. 26 4217 N GLU D 238-58.281 81.845-42. 955 1.00 38.66 4218 CA GLU D 238-57. 840 83. 228-43. 080 1.00 42.25 4219 CB GLU D 238-58.867 84. 031-43. 882 1.00 45.78 4220 CG GLU D 238-58.883 83. 657-45. 356 1. 00 51.30 4221 CD GLU D 238-59.920 84.424-46. 153 1.00 55.05 1 2 3 4 5 6 7 8 9 10 4222 OE1 GLU D 238-59. 945 84. 266-47. 395 1.00 57.47 4223 OE2 GLU D 238-60.709 85.177-45. 542 1.00 57. 38 4224 C GLU D 238-57.572 83.900-41. 733 1. 00 41.40 4225 0 GLU D 238-56.890 84.920-41. 671 1.00 41.66 4226 N THR D 239-58.091 83. 318-40. 657 1.00 40.96 4227 CA THR D 239-57.901 83.881-39. 324 1.00 41. 16 4228 CB THR D 239-59.256 84.258-38. 689 1.00 42.71 4229 OGI THR D 239-59. 914 85.229-39. 512 1.00 45. 80 4230 CG2 THR D 239-59. 052 84.836-37. 299 1.00 44.00 4231 C THR D 239-57.174 82.931-38. 374 1.00 39.29 4232 O THR D 239-57.483 81. 743-38. 316 1. 00 39. 45 4233 N LEU D 240-56.209 83.474-37. 634 1.00 37.08 4234 CA LEU D 240-55.419 82.718-36. 661 1.00 36.06 4235 CB LEU D 240-56.226 82.546-35. 369 1.00 37.46 4236 CG LEU D 240-56.709 83.831-34. 685 1.00 40. 38 4237 CD1 LEU D 240-57.692 83. 484-33. 577 1.00 40.32 4238 CD2 LEU D 240-55.520 84. 607-34. 134 1.00 40.27 4239 C LEU D 240-54. 949 81. 345-37. 159 1.00 33.83 4240 O LEU D 240-55.254 80.316-36. 550 1.00 31. 84 4241 N PRO D 241-54.187 81. 314-38. 266 1.00 32.64 4242 CD PRO D 241-53. 747 82. 460-39. 080 1.00 33.16 4243 CA PRO D 241-53.685 80. 054-38. 830 1.00 31.35 4244 CB PRO D 241-52.879 80. 510-40. 045 1.00 32. 79 4245 CG PRO D 241-53.513 81.818-40. 415 1.00 34.24 4246 C PRO D 241-52.821 79.275-37. 843 1.00 31.58 4247 O PRO D 241-51.916 79.835-37. 221 1.00 30.43 4248 N ASN D 242-53. 101 77. 984-37. 703 1.00 28.74 4249 CA ASN D 242-52. 332 77.152-36. 789 1.00 28.82 4250 CB ASN D 242-52.676 77.499-35. 336 1.00 32.06 4251 CG ASN D 242-51.448 77. 835-34. 510 1.00 35.26 4252 ODI ASN D 242-51.489 77.818-33. 283 1.00 40.01 4253 ND2 242-50. 349 78.153-35. 184 1.00 38. 90 4254 C ASN D 242-52.585 75. 670-37. 030 1.00 26.11 1 2 3 4 5 6 7 8 9 10 4255 O ASN D 242 -53.355 75.045-36. 303 1. 00 25.45 4256 N ASN D 243-51.946 75.118-38. 059 1.00 23.55 4257 CA ASN D 243-52.084 73. 698-38. 385 1.00 22. 38 4258 CB ASN D 243-52.702 73. 504-39. 775 1.00 22.13 4259 CG ASN D 243-54.189 73. 778-39. 811 1.00 23.48 4260 OD1 ASN D 243-54. 943 73.302-38. 960 1.00 22.59 4261 ND2 ASN D 243-54.626 74.532-40. 816 1.00 23.84 4262 C ASN D 243-50. 737 72.978-38. 398 1.00 21.11 4263 O ASN D 243-49.831 73. 392-39. 116 1.00 21.00 4264 N SER D 244-50.596 71.911-37. 612 1.00 20.07 4265 CA SER D 244-49. 358 71.144-37. 656 1.00 19. 87 4266 CB SER D 244-49. 046 70. 470-36. 307 1.00 20.44 4267 OG SER D 244-50.042 69. 537-35. 923 1.00 21.88 4268 C SER D 244-49.601 70.103-38. 744 1.00 21.28 4269 O SER D 244-50.748 69.700-38. 987 1.00 21. 31 4270 N CYS D 245-48.534 69.685-39. 415 1.00 19.66 4271 CA CYS D 245-48.628 68.704-40. 492 1.00 20.86 4272 C CYS D 245-47.589 67.615-40. 244 1. 00 21.24 4273 O CYS D 245-46.398 67. 914-40. 184 1.00 20.38 4274 CB CYS D 245-48.327 69. 376-41. 839 1.00 24.42 4275 SG CYS D 245-49.115 68. 571-43. 264 1. 00 32. 54 4276 N TYR D 246 -48.035 66.366 -40.111 1.00 18.29 4277 CA TYR D 246 -47.126 65.244 -39.866 1.00 18.01 4278 CB TYR D 246-47.452 64.581-38. 515 1. 00 16.94 4279 CG TYR D 246 -46.637 63.332 -38.184 1.00 15.14 4280 CD1 TYR D 246 -46.891 62.108 -38.815 1.00 14.79 4281 CE1 TYR D 246-46.149 60.956-38. 498 1.00 12. 51 4282 CD2 TYR D 246-45. 616 63. 375-37. 231 1.00 14.80 4283 CE2 TYR D 246-44.870 62.236-36. 913 1.00 14.33 4284 CZ TYR D 246-45. 143 61. 034-37. 549 1.00 15.28 4285 OH TYR D 246-44.404 59.919-37. 236 1.00 15.08 4286 C TYR D 246-47. 190 64.189-40. 961 1.00 19.53 4287 O TYR D 246-48.261 63. 893-41. 493 1.00 18. 05 1 2 3 4 5 6 7 8 9 10 4288 N SER D 247-46.028 63.640-41. 304 1.00 18.98 4289 CA SER D 247-45. 945 62.569-42. 287 1.00 19.03 4290 CB SER D 247-45.833 63. 121-43. 710 1. 00 21.66 4291 OG SER D 247-46.025 62. 073-44. 651 1.00 22.45 4292 C SER D 247-44. 734 61. 694-41.962 1.00 19.00 4293 O SER D 247-43. 743 62. 166-41. 394 1.00 18. 31 4294 N ALA D 248-44. 829 60. 413-42. 301 1. 00 16.33 4295 CA ALA D 248-43. 749 59.464-42. 050 1. 00 16.81 4296 CB ALA D 248-43. 742 59. 045-40. 579 1.00 15.28 4297 C ALA D 248-43. 910 58.234-42. 934 1.00 17.19 4298 O ALA D 248-44. 997 57. 965-43. 460 1. 00 17. 40 4299 N GLY D 249-42.820 57. 494-43. 095 1.00 15.34 4300 CA GLY D 249-42.850 56. 288-43. 903 1. 00 16.43 4301 C GLY D 249-41.499 55. 604-43. 927 1.00 17.99 4302 O GLY D 249-40.548 56. 066-43. 288 1.00 17.79 4303 N ILE D 250-41.407 54.512-44. 678 1. 00 16.71 4304 CA ILE D 250-40.168 53.755-44. 778 1. 00 18. 36 4305 CB ILE D 250-40. 449 52.245-44. 591 1.00 18.84 4306 CG2 ILE D 250-39.157 51.448-44. 701 1.00 18.69 4307 CG1 ILE D 250-41.111 52.015-43. 229 1.00 18.41 4308 CD1 ILE D 250-41.575 50. 578-43. 005 1.00 20.70 4309 C ILE D 250-39. 490 53.988-46. 127 1.00 19.19 4310 O ILE D 250-40.158 54. 168-47. 144 1.00 18. 98 4311 N ALA D 251-38.160 54.000-46. 129 1.00 19.76 4312 CA ALA D 251-37.410 54.199-47. 363 1.00 20.61 4313 CB ALA D 251-37. 147 55.680-47. 580 1.00 21.11 4314 C ALA D 251-36.095 53. 433-47. 368 1.00 20.95 4315 O ALA D 251-35. 475 53.229-46. 324 1.00 21.07 4316 N LYS D 252-35. 680 52.997-48. 553 1.00 20.42 4317 CA LYS D 252-34. 419 52.274-48. 704 1.00 21.93 4318 CB LYS D 252-34. 538 51.222-49. 820 1.00 23.95 4319 CG LYS D 252-35.616 50. 171-49. 537 1.00 28. 39 4320 CD LYS D 252-35.382 48. 846-50. 274 1.00 31.74 1 2 3 4 5 6 7 8 9 10 4321 CE LYS D 252-35.619 48.951-51. 765 1.00 34.41 4322 NZ LYS D 252-35.468 47.613-52. 418 1.00 34.65 4323 C LYS D 252-33.360 53. 323-49. 046 1.00 21.04 4324 O LYS D 252-33. 450 53. 987-50. 075 1.00 21.47 4325 N LEU D 253-32. 372 53.483-48. 170 1.00 20.91 4326 CA LEU D 253-31.330 54.485-48. 372 1.00 21.67 4327 CB LEU D 253-31.386 55.521-47. 241 1. 00 19.56 4328 CG LEU D 253-32.752 56.176-46. 983 1.00 19.99 4329 CD1 LEU D 253-32.669 57. 066-45. 749 1.00 19.67 4330 CD2 LEU D 253-33.180 56.988-48. 205 1.00 19.93 4331 C LEU D 253-29.933 53. 879-48. 434 1.00 21.80 4332 O LEU D 253-29.653 52.869-47. 792 1.00 21.26 4333 N GLU D 254-29.053 54.515-49. 201 1.00 22.64 4334 CA GLU D 254-27.687 54. 034-49. 349 1.00 24.78 4335 CB GLU D 254-27.340 53.969-50. 842 1.00 28.52 4336 CG GLU D 254-28.086 52. 865-51. 590 1.00 34.01 4337 CD GLU D 254-27.965 52.979-53. 100 1.00 39.36 4338 OE1 GLU D 254-28.108 51. 945-53. 790 1.00 40.67 4339 OE2 GLU D 254-27.746 54.103-53. 602 1.00 43.48 4340 C GLU D 254-26.670 54.906-48. 607 1.00 22.77 4341 O GLU D 254-26.891 56.097-48. 417 1.00 22.06 4342 N GLU D 255-25. 563 54.305-48. 175 1.00 23.91 4343 CA GLU D 255-24.514 55. 058-47. 487 1.00 24.93 4344 CB GLU D 255-23.287 54.165-47. 243 1.00 26.69 4345 CG GLU D 255-22.004 54.930-46. 915 1.00 32. 45 4346 CD GLU D 255-20. 865 54. 025-46. 465 1.00 36.49 4347 OE1 GLU D 255-20.832 52.846-46. 884 1.00 39.41 4348 OE2 GLU D 255-19.994 54.500-45. 702 1.00 39.19 4349 C GLU D 255-24.130 56. 254-48. 363 1.00 24.28 4350 O GLU D 255-23. 880 56.100-49. 558 1.00 23.04 4351 N GLY D 256-24. 104 57. 446-47. 775 1.00 23.30 4352 CA GLY D 256-23.765 58.634-48. 539 1.00 23.05 4353 C GLY D 256-24.961 59.524-48. 834 1. 00 23.65 1 2 3 4 5 6 7 8 9 10 4354 O GLY D 256-24.805 60.725-49. 066 1.00 23.57 4355 N ASP D 257-26.157 58.939-48. 832 1.00 23.34 4356 CA ASP D 257-27. 390 59. 688-49. 093 1.00 23.03 4357 CB ASP D 257-28.593 58.736-49. 175 1. 00 23.35 4358 CG ASP D 257-28.634 57. 931-50. 470 1. 00 26.74 4359 OD1 ASP D 257-29.515 57. 048-50. 579 1.00 26.04 4360 OD2 ASP D 257-27.806 58.181-51. 376 1.00 24.98 4361 C ASP D 257-27.647 60.685-47. 963 1. 00 21.87 4362 O ASP D 257-27.207 60.472-46. 841 1.00 21.01 4363 N GLU D 258-28. 361 61.765-48. 266 1.00 22.06 4364 CA GLU D 258-28.701 62.766-47. 260 1.00 23.80 4365 CB GLU D 258-27. 954 64.082-47. 513 1.00 26.00 4366 CG GLU D 258-26.441 63.956-47. 542 1.00 31.59 4367 CD GLU D 258-25.746 65. 300-47. 687 1.00 35.61 4368 OE1 GLU D 258-26. 168 66.106-48. 542 1.00 37.06 4369 OE2 GLU D 258-24.770 65.547-46. 949 1.00 38.68 4370 C GLU D 258-30.204 63. 033-47. 300 1.00 23.58 4371 O GLU D 258-30. 829 62. 948-48. 358 1.00 24.50 4372 N LEU D 259-30. 778 63.360-46. 146 1.00 21.27 4373 CA LEU D 259-32.204 63.654-46. 056 1.00 20.62 4374 CB LEU D 259-32. 883 62. 710-45. 057 1.00 20.91 4375 CG LEU D 259-32. 873 61. 206-45334 1.00 21.64 4376 CD1 LEU D 259-33.462 60. 463-44. 135 1.00 22.64 4377 CD2 LEU D 259-33.676 60.908-46. 591 1.00 22.42 4378 C LEU D 259-32. 394 65. 090-45. 584 1.00 20.63 4379 O LEU D 259-31. 674 65.552-44. 692 1.00 19.07 4380 N GLN D 260-33.356 65.784-46. 186 1. 00 17.85 4381 CA GLN D 260-33.672 67.160-45. 812 1. 00 21. 34 4382 CB GLN D 260-33.008 68.164-46. 765 1.00 21.12 4383 CG GLN D 260-33. 424 68.046-48. 227 1.00 23.10 4384 CD GLN D 260-32.781 69. 121-49. 097 1.00 25.49 4385 OE1 GLN D 260-31. 623 69. 476-48. 895 1. 00 27.13 4386 NE2 GLN D 260-33. 526 69. 630-50. 074 1.00 22.88 1 2 3 4 5 6 7 8 9 10 4387 C GLN D 260-35. 176 67. 388-45. 834 1.00 20. 35 4388 O GLN D 260-35. 894 66.744-46. 596 1.00 18.99 4389 N LEU D 261-35.643 68.300-44. 983 1.00 20.27 4390 CA LEU D 261-37.060 68. 644-44. 918 1.00 20.20 4391 CB LEU D 261-37.562 68. 567-43. 471 1.00 18.66 4392 CG LEU D 261-39.065 68. 753-43. 216 1.00 20.00 4393 CD1 LEU D 261-39.425 68.147-41. 856 1.00 17.61 4394 CD2 LEU D 261-39. 438 70. 238-43. 264 1.00 19.01 4395 C LEU D 261-37. 163 70. 066-45. 460 1.00 20.66 4396 O LEU D 261-36.626 71.006-44. 871 1.00 22.54 4397 N ALA D 262-37.853 70.217-46. 586 1.00 20.68 4398 CA ALA D 262-37. 984 71.513-47. 241 1.00 21.30 4399 CB ALA D 262-37.327 71.443-48. 614 1.00 19.89 4400 C ALA D 262-39. 421 71. 996-47. 388 1. 00 22. 62 4401 O ALA D 262-40. 325'71. 205-47. 657 1.00 22.49 4402 N ILE D 263-39.619 73. 301-47. 210 1.00 21.93 4403 CA ILE D 263-40. 934 73. 929-47. 350 1.00 24.14 4404 CB ILE D 263-41.221 74.883-46. 172 1.00 23. 95 4405 CG2 ILE D 263-42.576 75.568-46. 369 1.00 23.58 4406 CG1 ILE D 263-41.192 74. 099-44. 858 1.00 24.24 4407 CD1 ILE D 263-41.233 74. 972-43. 614 1.00 23.27 4408 C ILE D 263-40.912 74.723-48. 659 1.00 26.35 4409 0 ILE D 263-40. 184 75.711-48. 781 1.00 25.21 4410 N PRO D 264-41.715 74. 302-49. 653 1.00 27.96 4411 CD PRO D 264-42.579 73. 114-49. 579 1.00 29. 13 4412 CA PRO D 264-41.821 74.923-50. 980 1.00 30.35 4413 CB PRO D 264-42.651 73.908-51. 779 1.00 30.84 4414 CG PRO D 264-42.539 72.630-50. 991 1.00 30.84 4415 C PRO D 264-42.447 76. 312-51. 029 1.00 31.62 4416 O PRO D 264-43. 344 76.562-51. 833 1.00 32.10 4417 N ARG D 265-41.981 77. 211-50. 173 1.00 32.93 4418 CA ARG D 265-42.503 78. 570-50. 154 1.00 34.59 4419 CB ARG D 265-43. 779 78. 649-49. 312 1.00 37.75 1 2 3 4 5 6 7 8 9 10 4420 CG ARG D 265-44. 457 80.004-49. 383 1. 00 42. 56 4421 CD ARG D 265-45.669 80.096-48. 472 1.00 47.44 4422 NE ARG D 265-46.416 81. 327-48. 713 1.00 52.17 4423 CZ ARG D 265-47.072 81.592-49. 840 1.00 54.53 4424 NH1 ARG D 265-47. 077 80.707-50. 830 1.00 55.17 4425 NH2 ARG D 265-47.717 82.744-49. 981 1. 00 55.47 4426 C ARG D 265-41.466 79.527-49. 587 1. 00 33.28 4427 O ARG D 265-40. 781 79.209-48. 614 1.00 30.92 4428 N GLU D 266-41.356 80.700-50. 204 1.00 33. 33 4429 CA GLU D 266-40.408 81.712-49. 760 1.00 33. 53 4430 CB GLU D 266-40.220 82.775-50. 851 1. 00 37.19 4431 CG GLU D 266-39. 316 82. 338-51. 999 1.00 42. 38 4432 CD GLU D 266-39.237 83.369-53. 118 1.00 46.99 4433 OE1 GLU D 266-39.081 84.573-52. 816 1.00 49.13 4434 OE2 GLU D 266-39. 321 82.974-54. 301 1.00 49.48 4435 C GLU D 266-40.894 82.366-48. 474 1.00 31.99 4436 O GLU D 266-42.073 82.699-48. 345 1.00 32.10 4437 N ASN D 267-39. 979 82.538-47. 524 1.00 30.44 4438 CA ASN D 267-40.287 83.153-46. 236 1.00 30.72 4439 CB ASN D 267-40. 430 84.668-46. 403 1.00 33.15 4440 CG ASN D 267-39.178 85. 307-46. 981 1.00 34.70 4441 OD1 ASN D 267-38.101 85.256-46. 378 1.00 35.20 4442 ND2 ASN D 267-39.312 85.901-48. 159 1.00 36.39 4443 C ASN D 267-41. 547 82.577-45. 588 1.00 31.37 4444 O ASN D 267-42.431 83.316-45. 150 1.00 30.36 4445 N ALA D 268-41.621 81.252-45. 523 1.00 29.51 4446 CA ALA D 268-42.770 80.588-44. 923 1.00 28.15 4447 CB ALA D 268-42.675 79.080-45. 145 1.00 27.77 4448 C ALA D 268-42.840 80.896-43. 431 1.00 27.55 4449 O ALA D 268-41.818 80.918-42. 741 1. 00 26.99 4450 N GLN D 269-44. 054 81.134-42. 942 1.00 27.79 4451 CA GLN D 269-44.278 81.435-41. 535 1.00 28. 18 4452 CB GLN D 269-45. 440 82.419-41. 397 1.00 30.84 1 2 3 4 5 6 7 8 9 10 4453 CG GLN D 269-45. 221 83.728-42. 149 1.00 32.97 4454 CD GLN D 269-43. 977 84.462-41. 676 1.00 35. 58 4455 OBI GLN D 269-43. 872 84. 832-40. 507 1.00 35.90 4456 NE2 GLN D 269-43. 024 84.669-42. 584 1.00 37.06 4457 C GLN D 269-44.582 80. 145-40. 775 1.00 28.10 4458 O GLN D 269-45. 612 79.504-40. 998 1. 00 29. 80 4459 N ILE D 270-43. 679 79.774-39. 875 1.00 25.91 4460 CA ILE D 270-43. 825 78.554-39. 091 1.00 25.67 4461 CB ILE D 270-42.939 77.411-39. 664 1.00 25.26 4462 CG2 ILE D 270-43333 77.107-41. 101 1.00 23.20 4463 CG1 ILE D 270-41.460 77. 821-39. 587 1.00 25.73 4464 CD1 ILE D 270-40. 488 76. 733-39. 993 1.00 24.30 4465 C ILE D 270-43. 386 78.778-37. 652 1.00 26.08 4466 O ILE D 270-42.752 79.788-37. 331 1.00 25.29 4467 N SER D 271-43. 717 77.821-36. 792 1.00 23.46 4468 CA SER D 271-43. 328 77. 889-35393 1.00 24.60 4469 CB SER D 271-44. 389 77. 251-34. 503 1.00 25. 86 4470 OG SER D 271-43. 855 77. 021-33. 207 1.00 25. 83 4471 C SER D 271-42.022 77. 131-35. 213 1.00 25.25 4472 O SER D 271-41.856 76.038-35. 756 1.00 23.90 4473 N LEU D 272-41.099 77. 703-34. 447 1.00 24.73 4474 CA LEU D 272-39. 819 77.052-34. 208 1.00 25.07 4475 CB LEU D 272-38.673 78. 067-34. 350 1.00 26.42 4476 CG LEU D 272-38.525 78. 701-35. 740 1.00 26.74 4477 CD1 LEU D 272-37. 330 79. 659-35. 746 1.00 30.13 4478 CD2 LEU D 272-38. 333 77.614-36. 792 1.00 26.75 4479 C LEU D 272-39. 746 76.360-32. 849 1.00 24.67 4480 O LEU D 272-38. 662 76.184-32. 297 1.00 25.26 4481 N ASP D 273-40. 898 75. 974-32. 305 1.00 23.69 4482 CA ASP D 273-40.938 75.272-31. 021 1.00 23. 29 4483 CB ASP D 273-42. 362 75. 232-30. 450 1.00 27.52 4484 CG ASP D 273-42.826 76.572-29. 898 1. 00 33.86 4485 OD1 ASP D 273-41. 979 77. 453-29. 640 1. 00 35.38 2 3 4 5 6 7 8 9 10 4486 OD2 ASP D 273-44. 054 76.729-29. 698 1.00 37.00 4487 C ASP D 273-40.469 73.832-31. 247 1.00 20.27 4488 O ASP D 273-40. 944 73.162-32. 162 1.00 18.41 4489 N GLY D 274-39.558 73. 359-30. 401 1.00 18.19 4490 CA GLY D 274-39.036 72.008-30. 528 1. 00 19.26 4491 C GLY D 274-40. 045 70.875-30. 366 1.00 19.70 4492 O GLY D 274-39.801 69.761-30. 839 1.00 19.17 4493 N ASP D 275-41.172 71.136-29. 702 1.00 18.03 4494 CA ASP D 275-42.177 70.091-29. 522 1.00 18.46 4495 CB ASP D 275-42.922 70.257-28. 180 1. 00 17.52 4496 CG ASP D 275-43. 626 71.602-28. 037 1.00 20.25 4497 OD1 ASP D 275-43. 799 72. 328-29. 036 1.00 19.22 4498 OD2 ASP D 275-44.031 71.926-26. 899 1.00 22.60 4499 C ASP D 275-43. 194 69.998-30. 662 1.00 18.18 4500 O ASP D 275-44.038 69.103-30. 661 1.00 19.01 4501 N VAL D 276-43. 111 70.893-31. 644 1.00 17.23 4502 CA VAL D 276-44.072 70.849-32. 742 1.00 16.85 4503 CB VAL D 276-45. 084 72.024-32. 636 1.00 18.68 4504 CGl VAL D 276-44. 433 73.335-33. 061 1. 00 17.80 4505 CG2 VAL D 276-46. 329 71. 714-33. 466 1.00 19.05 4506 C VAL D 276-43. 456 70. 812-34. 141 1.00 17.44 4507 O VAL D 276-44. 133 70. 454-35. 104 1.00 15. 35 4508 N THR D 277-42.178 71.172-34. 254 1.00 16.27 4509 CA THR D 277-41.473 71. 142-35. 543 1.00 16.56 4510 CB THR D 277-41.095 72.573-36. 014 1.00 18.53 4511 OG1 THR D 277-42.294 73. 325-36. 250 1.00 19.21 4512 CG2 THR D 277-40. 278 72. 528-37. 305 1.00 15.46 4513 C THR D 277-40.221 70. 297-35. 306 1. 00 17.20 4514 O THR D 277-39.311 70.708-34. 581 1. 00 15.79 4515 N PHE D 278-40. 194 69.104-35. 898 1.00 16.05 4516 CA PHE D 278-39.091 68. 169 35. 701 1.00 14.97 4517 CB PHE D 278 -39.308 67.382 -34.392 1.00 14.96 4518 CB PHE D 278 -40.674 66.724 -34.273 1.00 16.37 1 2 3 4 5 6 7 8 9 10 4519 CD1 PHE D 278-40.920 65.479-34. 849 1.00 15. 08 4520 CD2 PHE D 278-41.705 67.349-33. 561 1.00 17.54 4521 CE1 PHE D 278-42. 175 64.855-34. 713 1.00 16.52 4522 CE2 PHE D 278-42.965 66.737-33. 419 1.00 15.03 4523 CZ PHE D 278-43.200 65.492-33. 996 1.00 12.80 4524 C PHE D 278-38.916 67. 234-36.899 1.00 15.01 4525 O PHE D 278-39. 790 67. 162-37. 762 1.00 15. 20 4526 N PHE D 279-37.801 66. 505-36.933 1.00 14. 30 4527 CA PHE D 279-37. 459 65.658-38. 083 1.00 14.50 4528 CB PHE D 279-36.805 66.604-39. 120 1. 00 14.98 4529 CG PHE D 279-36.264 65.947-40. 376 1.00 15.97 4530 CDl PHE D 279-36.956 64.934-41. 034 1. 00 18.03 4531 CD2 PHE D 279-35. 093 66.440-40. 958 1.00 16. 90 4532 CE1 PHE D 279-36.497 64.432-42. 262 1.00 18.64 4533 CE2 PHE D 279-34.624 65.950-42. 181 1.00 18.02 4534 CZ PHE D 279-35.327 64.941-42. 835 1.00 20.37 4535 C PHE D 279-36.518 64.539-37. 614 1.00 16.03 4536 O PHE D 279-35.591 64.786-36. 844 1.00 17.56 4537 N GLY D 280-36.765 63.305-38. 049 1.00 14.78 4538 CA GLY D 280-35. 909 62.209-37. 615 1.00 15.60 4539 C GLY D 280-35.920 60 : 957-38. 481 1.00 15.45 4540 O GLY D 280-36.686 60. 851-39. 439 1.00 15.07 4541 N ALA D 281-35.061 60.004-38. 131 1.00 16. 62 4542 CA ALA D 281-34. 950 58.749-38. 867 1.00 16.96 4543 CB ALA D 281-34.019 58. 928-40. 073 1.00 17.76 4544 C ALA D 281-34.416 57. 652-37. 962 1. 00 17.07 4545 O ALA D 281-33.662 57.917-37. 019 1.00 16.45 4546 N LEU D 282-34.804 56.419-38. 262 1.00 16.52 4547 CA LEU D 282-34.376 55. 258-37. 494 1.00 17. 75 4548 CB LEU D 282-35.464 54.841-36. 499 1. 00 19.64 4549 CG LEU D 282-35.210 53.515-35. 761 1.00 22.35 4550 CD1 LEU D 282-35. 759 53. 578-34. 343 1.00 23.61 4551 CD2 LEU D 282-35.848 52.370-36. 539 1.00 23. 47 1 2 3 4 5 6 7 8 9 10 4552 C LEU D 282-34.076 54.100-38. 430 1.00 19. 49 4553 O LEU D 282-34.839 53.839-39. 360 1.00 18.21 4554 N LYS D 283-32. 967 53.407-38. 183 1. 00 20.42 4555 CA LYS D 283 -32.585 52.270 -39.015 1.00 21.41 4556 CB LYS D 283 -31.062 52.082 -39.004 1.00 22.79 4557 CG LYS D 283 -30.553 51.103 -40.060 1.00 24.15 4558 CD LYS D 283-29.033 51. 018-40. 049 1.00 26.57 4559 CE LYS D 283-28.504 50.296-41. 285 1.00 28.21 4560 NZ LYS D 283-28.937 48.875-41. 334 1.00 29. 19 4561 C LYS D 283-33.262 50.988-38. 525 1.00 22. 39 4562 O LYS D 283-33.023 50. 529-37. 409 1.00 22.17 4563 N LEU D 284-34.108 50. 418-39. 374 1.00 22.88 4564 CA LEU D 284-34.828 49. 193-39. 055 1.00 24.94 4565 CB LEU D 284-35. 959 48. 994-40. 070 1.00 22.62 4566 CG LEU D 284-36.981 50. 135-40. 070 1.00 25.21 4567 CD1 LEU D 284-37. 940 49.998-41. 254 1.00 25.72 4568 CD2 LEU D 284-37. 739 50. 118-38. 751 1.00 22.78 4569 C LEU D 284-33.887 47.990-39. 076 1.00 29.06 4570 O LEU D 284-33.100 47. 828-40. 005 1.00 29. 51 4571 N LEU D 285-33. 963 47.150-38. 048 1.00 32.73 4572 CA LEU D 285-33.114 45. 967-37. 979 1.00 38.16 4573 CB LEU D 285-33.352 45.223-36. 666 1.00 39. 27 4574 CG LEU D 285-32.585 45.801-35. 476 1.00 40.86 4575 CD1 LEU D 285-33. 053 45.163-34. 180 1.00 43.33 4576 CD2 LEU D 285-31.098 45.558-35. 686 1.00 42.94 4577 C LEU D 285-33. 359 45.032-39. 164 1.00 41.92 4578 O LEU D 285-32.370 44. 593-39. 794 1.00 44.76 4579 OXT LEU D 285-34. 540 44. 748-39. 449 1.00 44.71 4580 CB VAL E 142-34.128 38.168-36. 406 1.00 49.10 4581 CG1 VAL E 142-35. 550 38. 230-36.958 1.00 48.57 4582 CG2 VAL E 142-33.837 36.785-35. 842 1.00 49.43 4583 C VAL E 142-33.320 39.956-37. 956 1. 00 46.06 4584 O VAL E 142-32.647 40.866-37. 476 1.00 45.26 1 2 3 4 5 6 7 8 9 10 4585 N VAL E 142-31.707 38. 307-37. 045 1. 00 48.97 4586 CA VAL E 142-33.106 38.509-37. 519 1.00 48.04 4587 N THR E 143-34.254 40.157-38. 879 1.00 43.73 4588 CA THR E 143-34. 568 41. 488-39. 382 1.00 41.21 4589 CB THR E 143-34.174 41.637-40. 866 1.00 41.25 4590 OG1 THR E 143-34.748 40.565-41. 623 1.00 43.91 4591 CG2 THR E 143-32.661 41.610-41. 026 1. 00 43.99 4592 C THR E 143-36.058 41.766-39. 245 1.00 37.99 4593 0 THR E 143-36. 821 40.908-38. 799 1.00 39.88 4594 N GLN E 144-36.466 42.969-39. 630 1.00 32.89 4595 CA GLN E 144-37.862 43. 363-39. 556 1.00 30. 42 4596 CB GLN E 144-37. 991 44.747-38. 913 1.00 29.96 4597 CG GLN E 144-37. 730 44.762-37. 417 1.00 29.10 4598 CD GLN E 144-37.814 46.154-36. 828 1.00 30.79 4599 OE1 GLN E 144-36.941 46. 993-37. 057 1.00 30.26 4600 NE2 GLN E 144-38.873 46. 411-36. 070 1.00 29.83 4601 C GLN E 144-38.491 43. 385-40. 941 1.00 28.42 4602 O GLN E 144-38.188 44.260-41. 758 1.00 27.17 4603 N ASP E 145-39.360 42.418-41. 207 1.00 25.61 4604 CA ASP E 145-40. 034 42.359-42. 497 1.00 26.06 4605 CB ASP E 145-40. 863 41.076-42. 621 1.00 27.25 4606 CG ASP E 145-40.008 39.819-42. 648 1.00 31.26 4607 OD1 ASP E 145-38.765 39.929-42. 552 1.00 31.87 4608 OD2 ASP E 145-40.586 38.717-42. 768 1.00 33.59 4609 C ASP E 145-40.965 43.557-42. 601 1.00 24.68 4610 O ASP E 145-41.531 43.997-41. 603 1.00 25.42 4611 N CYS E 146-41.115 44.090-43. 807 1.00 22. 27 4612 CA CYS E 146-42.009 45.213-44. 025 1.00 22. 52 4613 CB CYS E 146-41. 347 46.531-43. 600 1.00 22.86 4614 SG CYS E 146-39. 753 46. 873-44345 1.00 26.90 4615 C CYS E 146-42.442 45.272-45. 481 1.00 22.50 4616 O CYS E 146-41. 887 44.583-46. 338 1.00 22. 90 4617 N LEU-43. 449 46. 088-45. 755 1. 00 22. 10 1 2 3 4 5 6 7 8 9 10 4618 CA LEU E 147-43. 967 46. 220-47. 104 1.00 22.91 4619 CB LEU E 147-44.958 45.082-47. 383 1.00 24.24 4620 CG LEU E 147-45. 658 45.019-48. 745 1.00 26.21 4621 CD1 LEU E 147-46.081 43.589-49. 029 1.00 27.23 4622 CD2 LEU E 147-46.856 45.950-48. 758 1.00 26.21 4623 C LEU E 147-44.642 47.576-47. 231 1. 00 22.69 4624 O LEU E 147-45. 365 48.002-46. 334 1.00 22.65 4625 N GLN E 148-44. 392 48. 260-48. 343 1.00 20.78 4626 CA GLN E 148-44. 975 49.570-48. 555 1. 00 19.93 4627 CB GLN E 148-43. 915 50. 653-48. 340 1.00 20.31 4628 CG GLN E 148-44. 441 52.075-48. 423 1. 00 20. 94 4629 CD GLN E 148-43. 448 53.083-47. 856 1.00 25. 34 4630 OE1 GLN E 148-43. 347 53.258-46. 641 1.00 23.09 4631 NE2 GLN E 148-42.694 53.731-48. 737 1.00 25.79 4632 C GLN E 148-45. 591 49. 699-49. 940 1.00 19.54 4633 O GLN E 148-44.971 49. 365-50. 948 1.00 22. 18 4634 N LEU E 149-46.826 50.182-49. 964 1.00 19.41 4635 CA LEU E 149-47. 584 50. 378-51. 191 1.00 21.56 4636 CB LEU E 149-48.974 49.746-51. 051 1.00 19.96 4637 CG LEU E 149-49. 049 48.265-50. 675 1.00 21. 33 4638 CD1 LEU E 149-50. 507 47. 862-50. 491 1.00 21. 55 4639 CD2 LEU E 149-48.387 47.421-51. 760 1.00 22.00 4640 C LEU E 149-47. 744 51.873-51. 434 1.00 22.08 4641 O LEU E 149-47. 866 52.649-50. 485 1.00 23.06 4642 N ILE E 150-47.732 52.277-52. 701 1.00 21. 45 4643 CA ILE E 150-47.908 53. 680-53. 052 1.00 22.46 4644 CB ILE E 150-46.602 54. 301-53. 608 1. 00 23. 18 4645 CG2 ILE E 150-45. 545 54.358-52. 503 1.00 23.20 4646 CG1 ILE E 150-46. 097 53.485-54. 801 1.00 24.87 4647 CD1 ILE E 150-44.859 54. 070-55. 474 1.00 29.06 4648 C ILE E 150-49.006 53. 771-54. 105 1.00 23.46 4649 O ILE E 150-49.201 52. 840-54. 883 1.00 24.05 4650 N ALA E 151-49. 725 54. 887-54. 122 1.00 25.33 1 2 3 4 5 6 7 8 9 10 4651 CA ALA E 151-50.817 55.068-55. 077 1.00 27. 86 4652 CB ALA E 151-51.434 56.450-54. 904 1: 00 24.72 4653 C ALA E 151-50. 364 54.875-56. 522 1.00 30.30 4654 O ALA E 151-49.265 55.292-56. 900 1.00 30.00 4655 N ASP E 152-51.219 54.234-57. 318 1.00 32.15 4656 CA ASP E 152-50.937 53.985-58. 730 1.00 34.47 4657 CB ASP E 152-51.610 52.692-59. 195 1.00 35.44 4658 CG ASP E 152-51.183 52.285-60. 596 1.00 36.66 4659 OD1 ASP E 152-50.738 53.162-61. 367 1.00 36.51 4660 OD2 ASP E 152-51.301 51.091-60. 931 1.00 36.43 4661 C ASP E 152-51.491 55.164-59. 524 1.00 36.53 4662 O ASP E 152-52.701 55.285-59. 737 1.00 35.25 4663 N SER E 153-50.587 56.032-59. 958 1.00 38.93 4664 CA SER E 153-50.934 57.233-60. 705 1.00 42. 18 4665 CB SER E 153-49.650 57.998-61. 033 1.00 42.98 4666 OG SER E 153-49.934 59.203-61. 711 1.00 46.22 4667 C SER E 153-51.747 57.031-61. 990 1.00 43.98 4668 O SER E 153-52.517 57. 911-62. 383 1.00 44.64 4669 N GLU E 154-51.589 55. 887-62. 645 1. 00 44. 82 4670 CA GLU E 154-52.308 55.650-63. 893 1.00 47.83 4671 CB GLU E 154-51.306 55.364-65. 015 1.00 49.78 4672 CG GLU E 154-50.130 54.508-64. 600 1.00 53.65 4673 CD GLU E 154-48.949 54. 675-65. 532 1.00 56.16 4674 OE1 GLU E 154-49.080 54. 340-66. 729 1.00 59.41 4675 OE2 GLU E 154-47. 889 55.147-65. 071 1.00 57. 89 4676 C GLU E 154-53. 387 54.575-63. 870 1.00 47.23 4677 O GLU E 154-53.520 53.793-64. 812 1.00 48. 21 4678 N THR E 155-54.166 54.554-62. 795 1.00 46.19 4679 CA THR E 155-55.254 53. 598-62. 646 1.00 44. 58 4680 CB THR E 155-54.803 52. 345-61. 871 1.00 45. 26 4681 OG1 THR E 155-53. 777 51.674-62. 610 1. 00 46.23 4682 CG2 THR E 155-55.975 51.390-61. 663 1. 00 45. 79 4683 C THR E 155-56. 393 54.271-61. 888 1. 00 43. 03 1 2 3 4 5 6 7 8 9 10 4684 O THR E 155-56.166 54. 969-60. 900 1.00 42. 70 4685 N PRO E 156-57.635 54.091-62. 359 1.00 41.57 4686 CD PRO E 156-58.036 53.453-63. 624 1.00 42. 19 4687 CA PRO E 156-58.790 54.699-61. 694 1.00 40.64 4688 CB PRO E 156-59. 947 54.374-62. 641 1.00 40.51 4689 CG PRO E 156-59.275 54.230-63. 977 1.00 41.58 4690 C PRO E 156-58.998 54. 077-60. 316 1.00 39.21 4691 O PRO E 156-58.541 52.964-60. 061 1.00 37.66 4692 N THR E 157-59.678 54. 794-59. 426 1.00 38.94 4693 CA THR E 157-59. 944 54.258-58. 098 1.00 38.79 4694 CB THR E 157-60.536 55.321-57. 151 1.00 38.81 4695 OG1 THR E 157-61.725 55. 868-57. 730 1.00 39.11 4696 CG2 THR E 157-59. 530 56.436-56. 900 1.00 37.92 4697 C THR E 157-60.958 53.132-58. 262 1.00 39.33 4698 O THR E 157-61.749 53. 133-59. 204 1.00 38.63 4699 N ILE E 158-60.928 52. 173-57. 347 1.00 38.93 4700 CA ILE E 158-61.839 51. 044-57. 400 1. dO 38.36 4701 CB ILE E 158-61.150 49.772-56. 867 1.00 39.32 4702 CG2 ILE E 158-62.094 48.583-56. 950 1.00 38.22 4703 CGI ILE E 158-59.878 49.510-57. 680 1.00 38.71 4704 CDI ILE E 158-59. 007 48. 405-57. 126 1.00 41.16 4705 C ILE E 158-63.085 51. 339-56. 577 1.00 39.04 4706 O ILE E 158-62.997 51. 688 -55.397 1.00 36.74 4707 N GLN E 159-64.247 51.216-57. 211 1.00 38. 75 4708 CA GLN E 159-65. 522 51.464-56. 539 1. 00 39.97 4709 CB GLN E 159-66.467 52.217-57. 481 1.00 39.86 4710 CG GLN E 159-65.934 53. 561-57. 942 1.00 38.19 4711 CD GLN E 159-65.703 54.517-56. 788 1. 00 37.70 4712 OE1 GLN E 159-66.628 54.838-56. 040 1.00 35.97 4713 NE2 GLN E 159-64.465 54.980-56. 638 1.00 37.59 4714 C GLN E 159-66.147 50.137-56. 123 1.00 41.94 4715 O GLN E 159-66.422 49.288-56. 974 1.00 41.49 4716 N LYS E 160-66.375 49.960-54. 826 1.00 42. 81 1 2 3 4 5 6 7 8 9 10 4717 CA LYS E 160-66.955 48. 718-54. 335 1.00 44.77 4718 CB LYS E 160-65. 870 47.649-54. 227 1.00 45.40 4719 CG LYS E 160-66. 357 46.329-53. 685 1.00 47.71 4720 CD LYS E 160-65.284 45.260-53. 742 1.00 49. 68 4721 CE LYS E 160-64.898 44.932-55. 178 1.00 51. 81 4722 NZ LYS E 160-63.933 43.794-55. 250 1.00 53.71 4723 C LYS E 160-67.626 48. 896-52. 978 1.00 45.66 4724 O LYS E 160-67.123 49.592-52. 098 1.00 45.67 4725 N GLY E 161-68.774 48.253-52. 823 1.00 45.97 4726 CA GLY E 161-69.483 48. 359-51. 573 1.00 46.40 4727 C GLY E 161-69.686 49.799-51. 132 1.00 46.90 4728 O GLY E 161-69.807 50. 069-49.923 1.00 47.70 4729 N SER E 162-69.696 50.742-52. 068 1.00 46.43 4730 CA SER E 162-69.938 52.161-51. 763 1.00 46.91 4731 CB SER E 162-71.175 52. 311-50. 887 1.00 46.98 4732 OG SER E 162-72. 319 51.822-51. 548 1.00 50.07 4733 C SER E 162-68.831 53.054-51. 160 1.00 45.85 4734 O SER E 162-69.036 54.281-51. 012 1. 00 45.58 4735 N TYR E 163-67.699 52.441-50. 798 1.00 45.58 4736 CA TYR E 163-66. 560 53.165-50. 253 1.00 45.66 4737 CB TYR E 163-65.628 52. 286-49. 404 1.00 46.76 4738 CG TYR E 163-66.257 51.393-48. 294 1.00 49.86 4739 CD1 TYR E 163-66.203 50.007-48. 382 1.00 51.48 4740 CEI TYR E 163-66.611 49.178-47. 317 1.00 52. 86 4741 CD2 TYR E 163-66.747 51. 954-47. 097 1.00 51.25 4742 CE2 TYR E 163-67.151 51.149-46. 014 1.00 52.60 4743 CZ TYR E 163-67.069 49.754-46. 134 1.00 53.81 4744 OH TYR E 163-67.432 48.919-45. 102 1. 00 54. 08 4745 C TYR E 163-65.808 53. 691-51. 505 1.00 44. 42 4746 O TYR E 163-66.427 54.190-52. 456 1.00 48.12 4747 N THR E 164-64.483 53.589-51. 512 1.00 40.29 4748 CA THR E 164-63.662 53.985-52. 655 1.00 33.11 4749 CB THR E 164-63.588 55. 509-52. 827 1.00 34.53 1 2 3 4 5 6 7 8 9 10 4750 OG1 THR E 164-64.780 55.982-53. 478 1.00 34.21 4751 CG2 THR E 164-62. 380 55.872-53. 696 1.00 31.03 4752 C THR E 164-62. 282 53. 478-52. 308 1. 00 31.66 4753 O THR E 164-61.747 53.842-51. 269 1.00 28.12 4754 N PHE E 165-61.688 52.644-53. 151 1.00 28. 94 4755 CA PHE E 165-60.363 52.104-52. 843 1.00 29.15 4756 CB PHE E 165-60.395 50.561-52. 861 1.00 29.94 4757 CG PHE E 165-61.315 49.960-51. 824 1.00 31.89 4758 CD1 PHE E 165-62.688 49.861-52. 066 1.00 33.16 4759 CD2 PHE E 165-60.817 49.516-50. 596 1.00 30.58 4760 CE1 PHE E 165-63.543 49. 325-51. 108 1.00 33.95 4761 CE2 PHE E 165-61.673 48.977-49. 631 1.00 32.73 4762 CZ PHE E 165-63.034 48.884-49. 889 1.00 34.12 4763 C PHE E 165-59.271 52. 588-53. 757 1.00 28.94 4764 O PHE E 165-59. 410 52. 573-54. 977 1.00 28.37 4765 N VAL E 166-58.179 53.021-53. 142 1.00 27. 31 4766 CA VAL E 166-57. 014 53.514-53. 869 1.00 25.99 4767 CB VAL E 166-55.980 54.153-52. 891 1.00 25.82 4768 CG1 VAL E 166-54.758 54.651-53. 659 1.00 25.36 4769 CG2 VAL E 166-56.626 55. 292-52. 123 1.00 24.98 4770 C VAL E 166-56.340 52. 320-54. 545 1.00 26.37 4771 O VAL E 166-56.175 51.265-53. 924 1.00 25.54 4772 N PRO E 167-55. 970 52.452-55. 830 1.00 26.25 4773 CD PRO E 167-56. 314 53.530-56. 778 1.00 26.60 4774 CA PRO E 167-55.306 51. 337-56. 516 1.00 26.27 4775 CB PRO E 167-55.531 51. 660-57. 990 1.00 27. 31 4776 CG PRO E 167-55. 490 53.168-58. 003 1.00 27.39 4777 C PRO E 167-53.829 51. 389-56. 115 1.00 25.74 4778 O PRO E 167-53. 175 52.413-56. 293 1.00 26.21 4779 N TRP E 168-53. 306 50. 293-55. 573 1.00 26.31 4780 CA TRP E 168-51.923 50. 267-55. 104 1.00 26. 39 4781 CB TRP E 168-51.835 49. 559-53. 749 1. 00 24.92 4782 CG TRP E 168-52.664 50.174-52. 660 1.00 22.83 1 2 3 4 5 6 7 8 9 10 4783 CD2 TRP E 168 -52.492 51.469 -52.074 1.00 22.24 4784 CE2 TRP E 168 -53.481 51.609 -51.074 1.00 21.47 4785 CE3 TRP E 168-51. 625 52.541-52. 320 1.00 20.33 4786 CD1 TRP E 168-53.703 49.585-51. 995 1.00 21.92 4787 NE1 TRP E 168-54.194 50.439-51. 036 1.00 23.19 4788 CZ2 TRP E 168-53.594 52.760-50. 285 1.00 21.24 4789 CZ3 TRP E 168-51.739 53.690-51. 537 1.00 18.85 4790 CH2 TRP E 168-52.731 53. 796-50. 544 1.00 21.03 4791 C TRP E 168-50.872 49.646-56. 009 1.00 28.36 4792 O TRP E 168-51.140 48.730-56. 783 1.00 28.79 4793 N LEU E 169-49.657 50.160-55. 862 1.00 28.43 4794 CA LEU E 169-48.492 49.690-56. 591 1.00 29.60 4795 CB LEU E 169-47. 943 50.820-57. 463 1.00 32.50 4796 CG LEU E 169-47. 689 50.529-58. 944 1.00 36. 87 4797 CD1 LEU E 169-48.900 49.845-59. 565 1.00 35.43 4798 CD2 LEU E 169-47.388 51.840-59. 660 1.00 37.07 4799 C LEU E 169-47.489 49.329-55. 490 1.00 29.88 4800 O LEU E 169-47.393 50.032-54. 483 1.00 27.06 4801 N LEU E 170-46.754 48.239-55. 663 1.00 30.10 4802 CA LEU E 170-45.786 47. 835-54. 652 1.00 32.11 4803 CB LEU E 170-45.397 46. 368-54. 836 1.00 32. 34 4804 CG LEU E 170-44.388 45.835-53. 810 1.00 34. 12 4805 CD1 LEU E 170-45.041 45.773-52. 433 1.00 31.56 4806 CD2 LEU E 170-43.905 44.452-54. 229 1.00 34.51 4807 C LEU E 170-44.524 48.691-54. 692 1.00 32.85 4808 O LEU E 170-43.808 48.698-55. 691 1.00 33.31 4809 N SER E 171-44.258 49.412-53. 605 1.00 31. 72 4810 CA SER E 171-43.062 50.247-53. 515 1.00 31.27 4811 CB SER E 171-43.210 51. 271-52. 389 1.00 33.14 4812 OG SER E 171-42.085 52.129-52. 340 1.00 37.05 4813 C SER E 171-41.867 49.331-53. 244 1.00 29.73 4814 O SER E 171-40.847 49.402-53. 930 1.00 28.61 4815 N PHE E 172-41.996 48.481-52. 229 1.00 27. 92 1 2 3 4 5 6 7 8 9 10 4816 CA PHE E 172-40.956 47.513-51. 894 1.00 26. 89 4817 CB PHE E 172-39.675 48.207-51. 403 1.00 28.50 4818 CG PHE E 172-39. 843 48.968-50. 123 1.00 29.59 4819 CD1 PHE E 172-39. 937 48.302-48. 905 1.00 30.73 4820 CD2 PHE E 172-39. 935 50. 353-50. 139 1.00 29.02 4821 CE1 PHE E. 172-40.126 49.008-47. 721 1.00 32.11 4822 CE2 PHE E 172-40.123 51.066-48. 962 1.00 30.05 4823 CZ PHE E 172-40.218 50.394-47. 752 1.00 29.04 4824 C PHE E 172-41.457 46.516-50. 857 1.00 27. 26 4825 O PHE E 172-42.379 46. 800-50. 086 1. 00 24.84 4826 N LYS E 173-40. 848 45.337-50. 861 1.00 26.72 4827 CA LYS E 173-41.207 44.267-49. 948 1.00 28. 51 4828 CB LYS E 173-41.982 43.185-50. 712 1.00 30.45 4829 CG LYS E 173-42. 335 41.934-49. 921 1.00 33.79 4830 CD LYS E 173-43. 055 40.937-50. 832 1.00 36.66 4831 CE LYS E 173-43.467 39.664-50. 100 1.00 40.50 4832 NZ LYS E 173-42. 313 38.817-49. 687 1.00 42.97 4833 C LYS E 173-39.913 43. 699-49. 389 1.00 28.62 4834 O LYS E 173-38.974 43.434-50. 136 1.00 28.88 4835 N ARG E 174-39.863 43.530-48. 074 1.00 25.79 4836 CA ARG E 174-38.685 42.987-47. 412 1.00 26.87 4837 CB ARG E 174-38.046 44.068-46. 542 1.00 26.43 4838 CG ARG E 174-36.782 43.650-45. 827 1.00 28.57 4839 CD ARG E 174-36.472 44.641-44. 711 1. 00 30.40 4840 NE ARG E 174-35. 098 44.523-44. 236 1.00 30.92 4841 CZ ARG E 174-34.672 44. 995-43. 070 1.00 30.31 4842 NH1 ARG E 174-35.513 45.614-42. 251 1.00 29. 30 4843 NH2 ARG E 174-33. 401 44.849-42. 723 1.00 33.78 4844 C ARG E 174-39.120 41.809-46. 543 1.00 26.95 4845 O ARG E 174-39. 999 41.954-45. 693 1.00 25.98 4846 N GLY E 175-38.510 40.645-46. 756 1.00 26.63 4847 CA GLY E 175-38.865 39. 472-45. 972 1.00 26.98 4848 C GLY E 175-40. 090 38.750-46. 508 1. 00 27.88 1 2 3 4 5 6 7 8 9 10 4849 O GLY E 175-40.528 39.011-47. 626 1.00 29.75 4850 N SER E 176-40.659 37.850-45. 712 1.00 28.09 4851 CA SER E 176-41.825 37.095-46. 159 1.00 30.12 4852 CB SER E 176-41.437 35.629-46. 358 1.00 32.00 4853 OG SER E 176-40.969 35.065-45. 144 1.00 36.54 4854 C SER E 176-43. 053 37.161-45. 255 1.00 28.57 4855 O SER E 176-44.063 36. 520-45. 544 1.00 29.08 4856 N ALA E 177-42.980 37.926-44. 170 1.00 26. 80 4857 CA ALA E 177-44.114 38.032-43. 247 1.00 24. 28 4858 CB ALA E 177-43.681 38.732-41. 965 1.00 23.70 4859 C ALA E 177-45314 38.763-43. 844 1.00 24.50 4860 O ALA E 177-46.456 38.536-43. 431 1.00 25.67 4861 N LEU E 178-45. 054 39.634-44. 814 1.00 21.98 4862 CA LEU E 178-46.107 40. 421-45. 445 1.00 23.65 4863 CB LEU E 178-45. 974 41.889-45. 019 1.00 22.25 4864 CG LEU E 178-46.163 42.181-43. 526 1.00 21. 17 4865 CD1 LEU E 178-45.576 43.547-43. 174 1.00 21.32 4866 CD2 LEU E 178-47.648 42.122-43. 191 1.00 19.74 4867 C LEU E 178-46.058 40.336-46. 968 1.00 24.66 4868 O LEU E 178-44.986 40.394-47. 565 1.00 25.23 4869 N GLU E 179-47.231 40.204-47. 582 1. 00 25.77 4870 CA GLU E 179-47. 357 40. 118-49. 034 1.00 27.54 4871 CB GLU E 179-47.675 38.682-49. 464 1.00 30. 12 4872 CG GLU E 179-46.532 37. 692-49373 1.00 34.03 4873 CD GLU E 179-46.965 36. 288-49. 777 1.00 37.58 4874 OE1 GLU E 179-47. 779 36.169-50. 717 1.00 38.91 4875 OE2 GLU E 179-46.491 35.307-49. 166 1.00 39.45 4876 C GLU E 179-48.494 41. 012-49. 509 1.00 27. 57 4877 O GLU E 179-49.364 41.395-48. 728 1.00 26.51 4878 N GLU E 180-48.477 41. 352-50. 791 1.00 27.83 4879 CA GLU E 180-49.546 42.154-51. 366 1.00 31.55 4880 CB GLU E 180-49.010 43.208-52. 336 1.00 33.59 4881 CG GLU E 180-50. 125 43.859-53. 143 1. 00 37. 48 2 3 4 5 6 7 8 9 10 4882 CD GLU E 180-49.621 44. 821-54. 195 1.00 42.42 4883 OBI GLU E 180-48.573 44.535-54. 817 1. 00 44.12 4884 OE2 GLU E 180-50.285 45.858-54. 410 1. 00 43.63 4885 C GLU E 180-50.429 41.173-52. 130 1.00 32.66 4886 O GLU E 180-49.927 40.345-52. 888 1.00 33. 03 4887 N LYS E 181-51.736 41.261-51. 921 1.00 34.11 4888 CA LYS E 181-52.671 40.364-52. 584 1.00 35.64 4889 CB LYS E 181-52.906 39.124-51. 718 1.00 38.68 4890 CG LYS E 181-53. 870 38.110-52. 320 1.00 43.29 4891 CD LYS E 181-54. 136 36.968-51. 349 1.00 46.18 4892 CE LYS E 181-55. 118 35.958-51. 931 1. 00 48.52 4893 NZ LYS E 181-55. 406 34. 854-50. 971 1.00 50.16 4894 C LYS E 181-54. 002 41.053-52. 855 1.00 35.17 4895 O LYS E 181-54.676 41.516-51. 932 1.00 34.56 4896 N GLU E 182-54. 367 41. 125-54. 130 1.00 34.58 4897 CA GLU E 182-55.622 41. 738-54. 540 1.00 34.39 4898 CB GLU E 182-56.786 40.803-54. 185 1.00 38.63 4899 CG GLU E 182-56.668 39.419-54. 818 1.00 44.85 4900 CD GLU E 182-57. 775 38. 469-54. 389 1.00 49. 35 4901 OE1 GLU E 182-57.906 38. 204-53. 173 1.00 51.14 4902 OE2 GLU E 182-58.513 37.982-55. 271 1.00 52. 67 4903 C GLU E 182-55. 840 43.117-53. 919 1.00 31.99 4904 O GLU E 182-56.892 43. 393-53. 341 1.00 30.57 4905 N ASN E 183-54.828 43.972-54. 046 1.00 30.18 4906 CA ASN E 183-54.865 45. 342-53. 534 1. 00 27.96 4907 CB ASN E 183-56.050 46. 104-54. 135 1. 00 27.05 4908 CG ASN E 183-55. 759 47.588-54. 318 1.00 27.13 4909 OD1 ASN E 183-56.556 48.448-53. 923 1.00 26. 89 4910 ND2 ASN E 183-54.620 47.894-54. 932 1.00 23.44 4911 C ASN E 183-54. 945 45.407-52. 013 1.00 25.97 4912 O ASN E 183-55. 427 46. 392-51. 449 1.00 25. 22 4913 N LYS E 184-54. 470 44.359-51. 355 1.00 24. 96 4914 CA LYS E 184-54.486 44.304-49. 901 1. 00 25. 63 1 2 3 4 5 6 7 8 9 10 4915 CB LYS E 184-55. 627 43. 405-49. 416 1.00 27.27 4916 CG LYS E 184-57. 009 43. 942-49. 743 1. 00 29.29 4917 CD LYS E 184-58. 111 43. 080-49. 138 1.00 33.25 4918 CE LYS E 184-58.713 42. 119-50. 158 1.00 35.62 4919 NZ LYS E 184-57.742 41.090-50. 623 1.00 41.22 4920 C LYS E 184-53. 169 43. 762-49379 1.00 24. 18 4921 O LYS E 184-52.383 43. 181-50. 128 1.00 24.81 4922 N ILE E 185-52.927 43.970-48. 091 1.00 23.16 4923 CA ILE E 185-51.724 43. 464-47. 455 1.00 22.86 4924 CB ILE E 185-51. 164 44.449-46. 414 1.00 22.02 4925 CG2 ILE E 185-49.963 43. 823-45. 709 1.00 20.75 4926 CG1 ILE E 185-50.764 45.760-47. 096 1.00 22. 25 4927 CD1 ILE E 185-50.253 46.827-46. 134 1.00 23.04 4928 C ILE E 185-52.128 42.182-46. 746 1.00 23.80 4929 O ILE E 185-53.021 42.190-45. 897 1.00 25.62 4930 N LEU E 186-51.476 41. 085-47. 109 1.00 23.39 4931 CA LEU E 186-51.751 39.782-46. 523 1.00 22.97 4932 CB LEU E 186-51.736 38.699-47. 610 1.00 23. 04 4933 CG LEU E 186-51.831 37. 248-47. 122 1.00 23.68 4934 CD1 LEU E 186-53.129 37.038-46. 343 1.00 23. 56 4935 CD2 LEU E 186-51.766 36. 304-48. 315 1.00 25.21 4936 C LEU E 186-50.715 39. 441-45. 463 1.00 22.78 4937 O LEU E 186-49.514 39. 522-45. 711 1.00 23.49 4938 N VAL E 187-51.190 39. 055-44. 284 1.00 21.21 4939 CA VAL E 187-50. 316 38.680-43. 185 1. 00 22.72 4940 CB VAL E 187-50. 999 38.949-41. 830 1.00 23.21 4941 CG1 VAL E 187-50. 109 38.474-40. 682 1. 00 23. 03 4942 CG2 VAL E 187-51.288 40.444-41. 699 1.00 23.59 4943 C VAL E 187-50. 000 37. 196-43. 324 1. 00 23.63 4944 O VAL E 187-50. 903 36. 363-43. 321 1.00 21. 65 4945 N LYS E 188-48.716 36. 880-43. 458 1.00 24.57 4946 CA LYS E 188-48.261 35. 503-43. 621 1.00 26.09 4947 CB LYS E 188-47.188 35.439-44. 718 1.00 27. 36 1 2 3 4 5 6 7 8 9 10 4948 CG LYS E 188-47.683 35.850-46. 104 1.00 29.37 4949 CD LYS E 188-48.701 34.853-46. 645 1.00 33.70 4950 CE LYS E 188-48. 058 33.491-46. 879 1.00 35.18 4951 NZ LYS E 188-49.063 32.440-47. 213 1.00 39.49 4952 C LYS E 188-47. 704 34.910-42. 328 1.00 26.83 4953 O LYS E 188-47. 509 33.696-42. 227 1.00 27.01 4954 N GLU E 189-47. 455 35. 770-41. 342 1.00 25.85 4955 CA GLU E 189-46.908 35. 345-40. 053 1.00 25.40 4956 CB GLU E 189-45397 35.580-40. 014 1.00 26.93 4957 CG GLU E 189-44.585 34.688-40. 928 1.00 33.33 4958 CD GLU E 189-43.122 35.093-40. 972 1.00 36.82 4959 OE1 GLU E 189-42.569 35.451-39. 911 1.00 39. 22 4960 OE2 GLU E 189-42.525 35.044-42. 067 1.00 39.42 4961 C GLU E 189-47. 551 36. 107-38. 897 1.00 24.99 4962 O GLU E 189-47.612 37. 338-38. 912 1.00 24.41 4963 N THR E 190-48.012 35.371-37. 890 1.00 23.03 4964 CA THR E 190-48.644 35.978-36. 721 1.00 22.65 4965 CB THR E 190-49.238 34. 890-35. 801 1.00 22.94 4966 OG1 THR E 190-50.261 34.177-36. 512 1.00 23.38 4967 CG2 THR E 190-49.827 35. 512-34. 539 1.00 20.93 4968 C THR E 190-47.646 36.824-35. 925 1.00 22.74 4969 O THR E 190-46.492 36. 435-35. 749 1.00 21.04 4970 N GLY E 191-48.094 37.981-35. 446 1.00 21. 83 4971 CA GLY E 191-47.214 38.848-34. 681 1.00 19.29 4972 C GLY E 191-47. 754 40. 256-34. 534 1.00 18.42 4973 O GLY E 191-48.917 40.525-34. 854 1.00 17. 17 4974 N TYR E 192-46.902 41. 153-34. 043 1.00 17.25 4975 CA TYR E 192-47.256 42.555-33. 844 1.00 17.83 4976 CB TYR E 192-46.637 43.065-32. 540 1.00 18.33 4977 CG TYR E 192-47. 335 42. 569-31. 295 1.00 21. 44 4978 CD1 TYR E 192-48. 355 43. 315-30. 710 1.00 22.11 4979 CE1 TYR E 192-49.006 42. 874-29.562 1.00 23.20 4980 CD2 TYR E 192-46. 981 41.354-30. 701 1.00 22.66 1 2 3 4 5 6 7 8 9 10 4981 CE2 TYR E 192-47.638 40.897-29. 543 1.00 25.59 4982 CZ TYR E 192-48.649 41.672-28. 986 1. 00 23.88 4983 OH TYR E 192 -49.315 41.254-27. 860 1.00 28.22 4984 C TYR E 192-46.736 43. 380-35. 014 1.00 18.25 4985 O TYR E 192-45.588 43. 217-35. 434 1.00 18.54 4986 N PHE E 193-47.578 44. 268-35. 533 1.00 16.83 4987 CA PHE E 193-47.201 45.104-36. 669 1.00 17.30 4988 CB PHE E 193-47. 947 44.656-37. 940 1. 00 17.10 4989 CG PHE E 193-47.649 43.238-38. 364 1.00 16.90 4990 CDI PHE E 193-48.241 42.156-37. 711 1. 00 16.91 4991 CD2 PHE E 193-46.781 42.990-39. 424 1.00 15.94 4992 CEI PHE E 193-47. 955 40.838-38. 103 1. 00 17.14 4993 CE2 PHE E 193-46.487 41.682-39. 824 1.00 17.91 4994 CZ PHE E 193-47.083 40. 603-39. 165 1.00 17.49 4995 C PHE E 193-47. 504 46.584-36. 462 1. 00 16.74 4996 O PHE E 193-48.499 46.935-35. 824 1.00 16.86 4997 N PHE E 194-46.641 47.434-37. 017 1.00 17.36 4998 CA PHE E 194-46.828 48.886-36. 997 1.00 17.72 4999 CB PHE E 194-45. 484 49.625-36. 881 1.00 17.10 5000 CG PHE E 194-45. 596 51. 124-37. 041 1.00 18.81 5001 CD1 PHE E 194-46.201 51.906-36. 061 1.00 20.28 5002 CD2 PHE E 194-45.124 51.748-38. 193 1.00 18.81 5003 CE1 PHE E 194-46. 340 53.291-36. 232 1.00 20. 94 5004 CE2 PHE E 194-45. 258 53.126-38. 371 1.00 20.10 5005 CZ PHE E 194-45.868 53.897-37. 387 1.00 18.50 5006 C PHE E 194-47.436 49.114-38. 384 1. 00 17.58 5007 O PHE E 194-46.834 48. 747-39399 1. 00 17. 87 5008 N ILE E 195-48.628 49.705-38. 423 1.00 16.29 5009 CA ILE E 195-49. 351 49.928-39. 673 1.00 16.99 5010 CB ILE E 195-50.696 49.172-39. 644 1.00 17.42 5011 CG2 ILE E 195-51.364 49.229-41. 015 1.00 19.59 5012 CG1 ILE E 195-50. 455 47.716-39. 229 1.00 20.43 5013 ILS ILE E 195-51.703 47. 012-38. 721 1.00 20.93 123 4 5 6 7 8 9 10 5014 C ILE E 195-49.633 51.412-39. 878 1. 00 16.16 5015 O ILE E 195-50.066 52.092-38. 951 1.00 15.99 5016 N TYR E 196-49.413 51. 903-41. 095 1. 00 16.04 5017 CA TYR E 196-49. 620 321-41. 3 1.00 17.04 5018 CB TYR E 196-48.284 54.061-41. 257 1. 00 17.29 5019 CG TYR E 196-47. 212 53. 522-42. 181 1.00 18.27 5020 CD1 TYR E 196-47. 026 54. 053-43. 459 1.00 18.63 5021 CE1 TYR E 196-46.062 53.517-44. 331 1.00 18.51 5022 CD2 TYR E 196-46.413 52.449-41. 791 1.00 19.72 5023 CE2 TYR E 196-45. 455 51.908-42. 649 1.00 19.89 5024 CZ TYR E 196-45.285 52.444-43. 912 1.00 20.77 5025 OH TYR E'196-44. 342 51. 896-44. 753 1.00 20.31 5026 C TYR E 196-50.217 53.587-42. 775 1. 00 17.34 5027 O TYR E 196-50.083 52.779-43. 691 1. 00 21.16 5028 N GLY E 197-50.872 54.733-42. 917 1.00 18. 30 5029 CA GLY E 197-51.479 55. 089-44. 186 1.00 18.34 5030 C GLY E 197-51.785 56.571-44. 264 1. 00 19.44 5031 O GLY E 197-52.150 57. 194-43. 269 1.00 20. 96 5032 N GLN E 198-51.626 57.142-45. 451 1.00 18.10 5033 CA GLN E 198-51.898 58.557-45. 657 1.00 18.14 5034 CB GLN E 198-50.588 59. 368-45. 626 1.00 17.74 5035 CG GLN E 198-50. 773 60.857-45. 915 1.00 17.82 5036 CD GLN E 198-49.460 61.638-45. 883 1.00 20.72 5037 OE1 GLN E 198-48.819 61.764-44. 838 1.00 21.40 5038 NE2 GLN E 198-49.058 62.161-47. 036 1.00 18.04 5039 C GLN E 198-52.580 58. 756-47. 003 1. 00 16.98 5040 O GLN E 198-52.288 58.054-47. 958 1.00 18.22 5041 N VAL E 199-53.502 59.707-47. 063 1.00 16.97 5042 CA VAL E 199-54.185 60. 011-48. 302 1.00 15.87 5043 CB VAL E 199-55.621 59. 411-48. 355 1.00 16.88 5044 CG1 VAL E 199-56.297 59.812-49. 655 1.00 15.49 5045 CG2 VAL E 199-55.572 57.882-48. 229 1.00 15. 47 5046 C VAL E 199-54. 320 61. 517-48. 431 1. 00 16. 97 1 2 3 4 5 6 7 8 9 10 5047 O VAL E 199-54. 511 62. 223-47. 443 1.00 16.63 5048 N LEU E 200-54.193 62.019-49. 654 1.00 18.97 5049 CA LEU E 200-54.372 63. 465-49. 904 1.00 20.59 5050 CB LEU E 200-53. 314 63.995-50. 858 1.00 21.07 5051 CG LEU E 200-53.568 65.393-51. 457 1. 00 21. 93 5052 CD1 LEU E 200-53.786 66.412-50. 348 1.00 21.50 5053 CD2 LEU E 200-52.397 65. 819-52. 339 1.00 22.79 5054 C LEU E 200-55.738 63. 708-50. 475 1.00 22.33 5055 O LEU E 200-56.030 63.273-51. 610 1.00 21.08 5056 N TYR E 201-56.594 64.389-49. 698 1.00 24.88 5057 CA TYR E 201-57.982 64.610-50. 207 1.00 27.95 5058 CB TYR E 201-59. 028 64.523-49. 118 1.00 28.67 5059 CG TYR E 201-59.016 63.140-48. 454 1.00 29.49 5060 CD1 TYR E 201-58.198 62. 876-47. 349 1. 00 28. 36 5061 CE1 TYR E 201-58.167 61.631-46. 760 1. 00 29. 17 5062 CD2 TYR E 201-59.803 62.090-48. 939 1.00 29.45 5063 CE2 TYR E 201-59.782 60. 855-48. 369 1.00 30.22 5064 CZ TYR E 201-58.956 60. 608-47. 260 1.00 29. 48 5065 OH TYR E 201-58.891 59.356-46. 641 1.00 32.17 5066 C TYR E 201-58.035 66.042-50. 785 1.00 30. 79 5067 O TYR E 201-57.578 67. 020-50. 139 1.00 28.08 5068 N THR E 202-58. 636 66.169-51. 975 1.00 34.72 5069 CA THR E 202-58.798 67.426-52. 607 1.00 40.27 5070 CB THR E 202-57. 903 67.569-53. 840 1.00 41. 64 5071 OG1 THR E 202-58.246 66.545-54. 817 1.00 42.37 5072 CG2 THR E 202-56.434 67.323-53. 421 1.00 42.41 5073 C THR E 202-60.288 67. 499-53. 010 1.00 42.80 5074 O THR E 202-60.645 67.808-54. 137 1.00 42.86 5075 N ASP E 203-61.119 67.220-52. 008 1.00 46.14 5076 CA ASP E 203-62.545 67.178-52. 153 1. 00 47.94 5077 CB ASP E 203-63.083 65.842-51. 624 1.00 50. 58 5078 CG ASP E 203-64.413 65.473-52. 231 1.00 52.02 5079 OD1 ASP E 203-65. 351 66.269-52. 062 1.00 52.77 1 2 3 4 5 6 7 8 9 10 5080 OD2 ASP E 203-64.505 64.367-52. 820 1.00 53.14 5081 C ASP E 203-63.203 68. 326-51. 358 1.00 48.02 5082 O ASP E 203-62.731 68. 668-50. 277 1.00 46.85 5083 N LYS E 204-64.275 68.922-51. 892 1.00 49.18 5084 CA LYS E 204-64.968 70.020-51. 226 1.00 50.88 5085 CB LYS E 204-65.803 70.814-52. 235 1.00 52.89 5086 CG LYS E 204-65.009 71.551-53. 292 1.00 55.28 5087 CD LYS E 204-65.778 72.764-53. 807 1.00 57.87 5088 CE LYS E 204-67.153 72. 390-54. 341 1.00 58.64 5089 NZ LYS E 204-67.911 73.596-54. 776 1.00 59.92 5090 C LYS E 204-65.866 69.563-50. 083 1.00 50.79 5091 O LYS E 204-66.278 70.382-49. 262 1.00 50.25 5092 N THR E 205-66.177 68. 268-50. 035 1.00 52.08 5093 CA THR E 205-67.033 67.712-48. 979 1.00 52.97 5094 CB THR E 205-67.046 66. 165-49. 007 1.00 54.59 5095 OGI THR E 205-67.495 65.705-50. 290 1.00 56.21 5096 CG2 THR E 205-67.970 65.624-47. 921 1.00 54.50 5097 C THR E 205-66.556 68.150-47. 598 1.00 52.71 5098 O THR E 205-65.378 68.003-47. 270 1.00 53.30 5099 N TYR E 206-67.479 68.662-46. 788 1.00 51.37 5100 CA TYR E 206-67.160 69.150-45. 448 1.00 51.14 5101 CB TYR E 206-68.447 69.293-44. 621 1.00 54.59 5102 CG TYR E 206-69.074 67.988-44. 176 1.00 58.75 5103 CD1 TYR E 206-68.628 67. 330-43. 030 1.00 59.70 5104 CE1 TYR E 206-69.211 66.133-42. 613 1.00 62.54 5105 CD2 TYR E 206-70.121 67. 415-44. 900 1.00 60.98 5106 CE2 TYR E 206-70. 709 66. 219-44. 493 1.00 62.51 5107 CZ TYR E 206-70.251 65.585-43. 352 1.00 62. 84 5108 OH TYR E 206-70.833 64.403-42. 952 1.00 65.11 5109 C TYR E 206-66.123 68. 331-44. 669 1.00 47. 91 5110 O TYR E 206-65.410 68.885-43. 826 1.00 46.98 5111 N ALA E 207-66.038 67. 028-44. 943 1.00 42.48 5112 CA ALA E 207-65. 070 66.162-44. 261 1.00 38.50 1 2 3 4 5 6 7 8 9 10 5113 CB ALA E 207-65.573 65.808-42. 863 1. 00 38.78 5114 C ALA E 207-64.764 64. 884-45. 044 1.00 35.47 5115 O ALA E 207-65. 672 64. 212-45. 535 1.00 33.52 5116 N MET E 208-63.476 64.565-45. 153 1.00 31.30 5117 CA MET E 208-63.001 63. 376-45. 864 1.00 29.73 5118 CB MET E 208-62.250 63.778-47. 137 1.00 30.46 5119 CG MET E 208-63.090 64.515-48. 169 1.00 33.75 5120 SD MET E 208-64.413 63.489-48. 849 1.00 36.00 5121 CE MET E 208-63. 529 62. 520-50. 057 1.00 35.33 5122 C MET E 208-62.058 62.574-44. 966 1.00 28.74 5123 O MET E 208-61.410 63.130-44. 083 1.00 27.69 5124 N GLY E 209-61.976 61.269-45. 192 1.00 28.71 5125 CA GLY E 209-61.100 60. 451-44. 373 1.00 27.51 5126 C GLY E 209-61. 028 59.020-44. 857 1.00 26.87 5127 O GLY E 209-61. 777 58. 624-45. 754 1.00 28.58 5128 N HIS E 210-60.117 58.244-44. 278 1.00 24.07 5129 CA HIS E 210-59.971 56.850-44. 661 1.00 20.60 5130 CB HIS E 210-58.718 56.636-45. 523 1.00 19.45 5131 CG HIS E 210-57. 443 57.103-44. 886 1.00 20. 49 5132 CD2 HIS E 210-56.502 56.431-44. 179 1.00 18.82 5133 ND1 HIS E 210-57.008 58. 409-44. 959 1. 00 22.14 5134 CE1 HIS E 210-55.851 58. 521-44. 328 1.00 20. 87 5135 NE2 HIS E 210-55. 523 57. 335-43. 846 1.00 21. 10 5136 C HIS E 210-59.926 55. 933-43. 450 1.00 21. 54 5137 O HIS E 210-59.694 56. 374-42. 317 1.00 19.07 5138 N LEU E 211-60.160 54.652-43. 706 1.00 21.27 5139 CA LEU E 211-60.164 53.639-42. 664 1.00 20.69 5140 CB LEU E 211-61. 536 52.953-42. 592 1.00 22.97 5141 CG LEU E 211-62. 812 53.803-42. 624 1.00 23. 33 5142 CD1 LEU E 211-64.022 52.897-42. 844 1.00 24.24 5143 CD2 LEU E 211-62.949 54. 583-41. 332 1.00 22.97 5144 C LEU E 211-59.128 52.579-42. 990 1.00 20.44 5145 0LEU E 211-59. 034 52.129-44. 130 1. 00 21. 60 1 2 3 4 5 6 7 8 9 10 5146 N ILE E 212-58. 338 52.195-41. 994 1.00 20.02 5147 CA ILE E 212-57. 370 51. 125-42. 170 1.00 21.24 5148 CB ILE E 212-56. 061 51. 403-41399 1.00 23.17 5149 CG2 ILE E 212-55. 185 50.161-41. 405 1.00 23.10 5150 CG1 ILE E 212-55. 323 52.578-42. 054 1.00 23. 37 5151 CD1 ILE E 212-54.062 53. 025-41. 317 1.00 30.66 5152 C ILE E 212-58. 136 49. 967-41. 546 1.00 21.47 5153 O ILE E 212-58.353 49.941-40. 332 1.00 20.32 5154 N GLN E 213-58.565 49. 031-42. 387 1.00 21.71 5155 CA GLN E 213-59. 376 47.900-41. 944 1.00 22.25 5156 CB GLN E 213-60.603 47.757-42. 851 1.00 23.13 5157 CG GLN E 213-61. 434 49. 014-43. 020 1. 00 26. 21 5158 CD GLN E 213-62.561 48. 809-44. 014 1.00 26.69 5159 OE1 GLN E 213-62.337 48.375-45. 141 1.00 29.16 5160 NE2 GLN E 213-63.779 49. 119-43. 600 1.00 29.89 5161 C GLN E 213-58.673 46.560-41. 903 1.00 20. 34 5162 O GLN E 213-57. 735 46. 307-42. 657 1.00 20.93 5163 N ARG E 214-59. 166 45.698-41. 022 1.00 19.91 5164 CA ARG E 214-58.636 44. 355-40. 844 1.00 20.37 5165 CB ARG E 214-58.227 44.147-39. 382 1. 00 21.51 5166 CG ARG E 214-57.752 42. 737-39. 044 1. 00 22.86 5167 CD ARG E 214-57. 744 42. 511-37. 537 1. 00 23. 37 5168 NE ARG E 214 57. 198 41. 206-37. 175 1.00 24.81 5169 CZ ARG E 214-57.168 40.719-35. 936 1.00 27.73 5170 NH1 ARG E 214-57.657 41.428-34. 923 1.00 27.13 5171 NH2 ARG E 214-56.647 39.521-35. 706 1.00 26.44 5172 C ARG E 214-59.710 43.328-41. 218 1.00 21.44 5173 O ARG E 214-60.817 43.353-40. 675 1.00 20.50 5174 N LYS E 215-59388 42.452-42. 165 1.00 21.08 5175 CA LYS E 215-60.305 41.392-42. 580 1.00 22.93 5176 CB LYS E 215-60.182 41.116-44. 084 1.00 26.50 5177 CG LYS E 215-61.189 40.102-44. 624 1.00 31.14 5178 CD LYS E 215-62.621 40. 579-44. 400 1.00 36.23 1 2 3 4 5 6 7 8 9 10 5179 CE LYS E 215-63.646 39.630-45. 018 1.00 39.29 5180 NZ LYS E 215-65.046 40.121-44. 813 1.00 41.25 5181 C LYS E 215-59.825 40.196-41. 777 1.00 21.61 5182 O LYS E 215-58.807 39.578-42. 104 1.00 20.07 5183 N LYS E 216-60.549 39. 898-40. 705 1.00 21.43 5184 CA LYS E 216-60. 204 38.810-39. 798 1. 00 23.20 5185 CB LYS E 216-61.050 38.938-38. 527 1.00 22. 47 5186 CG LYS E 216-60.809 40. 242-37. 775 1.00 25.02 5187 CD LYS E 216-62.065 40.725-37. 060 1.00 26. 30 5188 CE LYS E 216-62.497 39. 765-35. 971 1.00 27.42 5189 NZ LYS E 216-63.798 40.182-35. 371 1.00 28.25 5190 C LYS E 216-60. 368 37.417-40. 396 1.00 24.50 5191 O LYS E 216-61.333 37.156-41. 112 1.00 25.15 5192 N VAL E 217-59.419 36. 530-40. 099 1.00 24. 39 5193 CA VAL E 217-59. 470 35. 158-40. 597 1.00 27.52 5194 CB VAL E 217-58.035 34.566-40. 781 1.00 27.08 5195 CG1 VAL E 217-57. 366 34. 356-39. 435 1.00 26.33 5196 CG2 VAL E 217-58.101 33.264-41. 555 1.00 28.67 5197 C VAL E 217-60.282 34.282-39. 630 1.00 28.26 5198 O VAL E 217-60.734 33. 196-39. 995 1.00 29. 57 5199 N HIS E 218-60. 459 34.770-38. 400 1.00 27. 84 5200 CA HIS E 218-61.229 34. 085-37. 353 1.00 28.03 5201 CB HIS E 218-60. 331 33.704-36. 170 1.00 31.22 5202 CG HIS E 218-59.184 32.812-36. 527 1.00 36. 32 5203 CD2 HIS E 218-59. 075 31.809-37. 431 1.00 39.04 5204 ND1 HIS E 218-57.967 32.885-35. 887 1. 00 39. 32 5205 CE1 HIS E 218-57.156 31. 966-36. 380 1.00 40. 27 5206 NE2 HIS E 218-57.803 31. 299-37. 317 1.00 40. 04 5207 C HIS E 218-62.286 35.063-36. 837 1.00 27.35 5208 O HIS E 218-61.947 36.180-36. 438 1.00 25.34 5209 N VAL E 219-63.554 34.651-36. 835 1.00 23.45 5210 CA VAL E 219-64.642 35.501-36. 361 1.00 22.04 5211 CB VAL E 219-65.510 36. 004-37. 540 1.00 23.38 1 2 3 4 5 6 7 8 9 10 5212 CG1 VAL E 219-66. 543 37. 006-37. 045 1. 00 24. 47 5213 CG2 VAL E 219-64.631 36.636-38. 606 1.00 25.53 5214 C VAL E 219-65. 534 34. 698-35. 404 1.00 24.11 5215 O VAL E 219-65.924 33.573-35. 718 1.00 20.47 5216 N PHE E 220-65.850 35.268-34. 241 1.00 22.57 5217 CA PHE E 220-66.693 34.571-33. 266 1.00 25. 28 5218 CB PHE E 220-65.845 34.061-32. 090 1.00 25. 87 5219 CG PHE E 220-64.677 33.210-32. 508 1.00 26.24 5220 CD1 PHE E 220-63.410 33.765-32. 643 1.00 26.36 5221 CD2 PHE E 220-64.851 31.858-32. 794 1.00 25.77 5222 CE1 PHE E 220-62.334 32. 987-33. 074 1. 00 28.15 5223 CE2 PHE E 220-63.785 31.075-33. 226 1.00 25. 32 5224 CZ PHE E 220-62.524 31.637-33. 361 1.00 26.98 5225 C PHE E 220-67. 843 35.417-32. 713 1.00 25.57 5226 O PHE E 220-67.796 36. 648-32. 727 1.00 25.49 5227 N GLY E 221-68.879 34. 743-32. 225 1.00 25.43 5228 CA GLY E 221-70.015 35.444-31. 655 1.00 25.89 5229 C GLY E 221-70.652 36.445-32. 596 1.00 26.58 5230 O GLY E 221-70. 939 36.117-33. 746 1.00 25.16 5231 N ASP E 222-70.870 37.669-32. 118 1.00 27.02 5232 CA ASP E 222-71.495 38.696-32. 945 1.00 31.00 5233 CB ASP E 222-72.546 39.467-32. 145 1.00 35.07 5234 CG ASP E 222-73.487 38.556-31. 395 1.00 38.80 5235 OD1 ASP E 222-73. 312 38.424-30. 165 1.00 42. 23 5236 OD2 ASP E 222-74.386 37.967-32. 036 1. 00 38.89 5237 C ASP E 222-70.514 39. 690-33. 549 1.00 31. 74 5238 O ASP E 222-70.932 40.682-34. 147 1.00 32.21 - 5239 N GLU E 223-69.218 39. 441-33394 1.00 31.58 5240 CA GLU E 223-68.225 40. 346-33. 959 1.00 31.68 5241 CB GLU E 223-66.831 40. 022-33. 409 1.00 30.51 5242 CG GLU E 223-66.725 40. 243-31. 897 1.00 32. 64 5243 CD GLU E 223-65.292 40. 316-31. 402 1. 00 35. 30 5244 OEl GLU E 223-64. 526 39. 358-31. 645 1.00 34.99 1 2 3 4 5 6 7'8'9 10 5245 OE2 GLU E 223-64.931 41. 336-30. 768 1. 00 35. 65 5246 C GLU E 223-68.249 40.265-35. 485 1.00 31.69 5247 O GLU E 223-68. 727 39.285-36. 061 1.00 30.32 5248 N LEU E 224-67.741 41.304-36. 136 1.00 31.57 5249 CA LEU E 224-67.734 41.366-37. 592 1.00 29.87 5250 CB LEU E 224-67.893 42.817-38. 049 1.00 32.90 5251 CG LEU E 224-68. 996 43. 614-37349 1.00 35.74 5252 CD1 LEU E 224-68.988 45.042-37. 866 1.00 36.60 5253 CD2 LEU E 224-70.346 42.957-37. 584 1.00 35.81 5254 C LEU E 224-66.468 40.795-38. 210 1.00 27. 56 5255 O LEU E 224-65. 446 40.654-37. 542 1.00 26.41 5256 N SER E 225-66.557 40. 481-39. 499 1.00 25.73 5257 CA SER E 225-65.443 39.945-40. 264 1.00 26.43 5258 CB SER E 225-65.980 39.225-41. 503 1.00 28.27 5259 OG SER E 225-64.930 38.809-42. 353 1.00 34. 36 5260 C SER E 225-64.507 41.084-40. 688 1. 00 25. 73 5261 O SER E 225-63.287 40.979-40. 576 1.00 24.06 5262 N LEU E 226-65.092 42.174-41. 175 1.00 25.91 5263 CA LEU E 226-64. 311 43. 329-41.611 1.00 26.78 5264 CB LEU E 226-64.849 43.852-42. 945 1.00 28.69 5265 CG LEU E 226-63.876 44. 524-43. 927 1.00 31. 40 5266 CD1 LEU E 226-64.670 45. 387-44. 898 1.00 29. 96 5267 CD2 LEU E 226-62.866 45.376-43. 183 1.00 32.32 5268 C LEU E 226-64.435 44. 415-40. 547 1.00 26.21 5269 O LEU E 226-65.536 44.899-40. 287 1.00 25.27 5270 N VAL E 227-63. 317 44.792-39. 927 1.00 25.84 5271 CA VAL E 227-63. 342 45.819-38. 891 1.00 23.17 5272 CB VAL E 227-63.160 45.191-37. 492 1.00 25.28 5273 CG1 VAL E 227-64. 176 44.067-37. 293 1.00 26.45 5274 CG2 VAL E 227-61.739 44. 663-37. 334 1.00 26.65 5275 C VAL E 227-62.296 46. 932-39. 054 1.00 23.65 5276 O VAL E 227-61.247 46.730-39. 656 1.00 20.89 5277 N THR E 228-62. 597 48. 098-38. 488 1.00 21. 91 1 2 3 4 5 6 7 8 9 10 5278 CA THR E 228-61.700 49.249-38. 557 1.00 21.98 5279 CB THR E 228-62.492 50.576-38. 505 1.00 22.44 5280 OGI THR E 228-63. 371 50.653-39. 634 1.00 22.11 5281 CG2 THR E 228-61.541 51.776-38. 526 1.00 20.27 5282 C THR E 228-60.697 49. 253-37. 400 1.00 21.57 5283 O THR E 228-61.086 49. 198-36. 230 1.00 20.70 5284 N LEU E 229-59. 409 49. 316-37. 730 1.00 19.01 5285 CA LEU E 229-58. 363 49.363-36. 708 1.00 19.14 5286 CB LEU E 229-57.069 48.719-37. 218 1.00 20.43 5287 CG LEU E 229-57.012 47. 204-37. 407 1.00 21. 37 5288 CD1 LEU E 229-55.651 46.833-37. 996 1.00 20.91 5289 CD2 LEU E 229-57.222 46.495-36. 070 1.00 20.95 5290 C LEU E 229-58.082 50.814-36. 325 1.00 19.40 5291 O LEU E 229-58.108 51.169-35. 148 1.00 20.42 5292 N PHE E 230-57.809 51.649-37. 325 1.00 18.51 5293 CA PHE E 230-57. 529 53. 067-37. 097 1.00 20.49 5294 CB PHE E 230-56.012 53. 348-37. 095 1.00 21.09 5295 CG PHE E 230-55.206 52.370-36. 297 1.00 23.83 5296 CD1 PHE E 230-54. 470 51.377-36. 936 1. 00 25. 67 5297 CD2 PHE E 230-55.183 52. 437-34. 904 1.00 26.07 5298 CE1 PHE E 230-53.724 50.454-36. 196 1.00 28.35 5299 CE2 PHE E 230-54. 443 51. 520-34.151 1.00 25.25 5300 CZ PHE E 230-53.710 50. 528-34. 799 1.00 27. 92 5301 C PHE E 230-58. 145 53.859-38. 244 1.00 19.44 5302 O PHE E 230-58.-328 53. 321-39. 336 1.00 18.29 5303 N ARG E 231-58.470 55. 125-37. 999 1.00 18.50 5304 CA ARG E 231-59.021 55.974-39. 051 1.00 18.73 5305 CB ARG E 231-60. 560 55.931-39. 068 1.00 20.66 5306 CG ARG E 231-61. 282 56.550-37. 888 1.00 19.67 5307 CD ARG E 231-62.803 56. 303-38. 025 1.00 21.38 5308 NE ARG E 231-63.571 56.786-36. 876 1.00 22.56 5309 CZ ARG E 231-64.069 58.016-36. 762 1.00 23.28 5310 NH1 ARG E 231-63. 888 58. 904-37. 730 1.00 23.82 1 2 3 4 5 6 7 8 9 10 5311 NH2 ARG E 231-64.752 58.360-35. 678 1.00 22.23 5312 C ARG E 231-58.529 57.418-38. 926 1.00 20.13 5313 O ARG E 231-58.093 57.847-37. 856 1.00 18.97 5314 N CYS E 232-58.610 58.146-40. 038 1.00 20.15 5315 CA CYS E 232-58.159 59. 531-40. 137 1.00 23.11 5316 C CYS E 232-59.291 60.372-40. 748 1.00 22.13 5317 O CYS E 232-60.031 59.876-41. 592 1.00 21.52 5318 CB CYS E 232-56.931 59.586-41. 069 1.00 23.34 5319 SG CYS E 232-55.948 61. 109-40. 943 1.00 35.95 5320 N ILE E 233-59. 440 61.625-40. 326 1.00 21.24 5321 CA ILE E 233-60.477 62.479-40. 915 1.00 22.14 5322 CB ILE E 233-61.850 62.302-40. 205 1.00 23.77 5323 CG2 ILE E 233-61.819 62.910-38. 817 1. 00 22. 85 5324 CG1 ILE E 233-62. 951 62.971-41. 033 1.00 24.34 5325 CD1 ILE E 233-64.366 62. 611-40. 577 1.00 26.31 5326 C ILE E 233-60.074 63. 952-40. 903 1.00 21.60 5327 O ILE E 233-59. 439 64.426-39. 961 1.00 20.16 5328 N GLN E 234-60.445 64.666-41. 964 1.00 21. 00 5329 CA GLN E 234-60. 112 66.082-42. 116 1.00 21. 96 5330 CB GLN E 234-58.911 66. 228-43. 063 1.00 20.43 5331 CG GLN E 234-57. 588 65.734-42. 504 1.00 20.43 5332 CD GLN E 234-56.964 66.739-41. 563 1.00 20.66 5333 OE1 GLN E 234-56.478 67.785-41. 993 1.00 22.12 5334 NE2 GLN E 234-56.989 66.438-40. 271 1.00 18.32 5335 C GLN E 234-61.264 66.910-42. 695 1.00 22. 34 5336 0 GLN E 234-61.888 66.495-43. 667 1.00 22. 26 5337 N ASN E 235-61.545 68.067-42. 098 1.00 23.20 5338 CA ASN E 235-62.578 68.959-42. 631 1.00 24. 82 5339 CB ASN E 235-62.890 70.110-41. 665 1.00 24. 31 5340 CG ASN E 235-63.837 69.709-40. 551 1. 00 26.02 5341 ODE ASN E 235-64.955 69.247-40. 802 1.00 27.72 5342 ND2 ASN E 235-63.402 69. 896-39. 310 1.00 22.99 5343 C ASN E 235-61.952 69. 544-43. 892 1.00 26.42 1 2 3 4 5 6 7 8 9 10 5344 O ASN E 235-60.730 69. 737-43. 944 LOO 25.14 5345 N MET E 236-62.775 69.832-44. 899 1.00 25.95 5346 CA MET E 236-62. 283 70.391-46. 156 1.00 26.80 5347 CB MET E 236-62.621 69. 452-47. 317 1.00 26.80 5348 CG MET E 236-62.212 67.993-47. 106 1.00 25.51 5349 SD MET E 236-60.428 67.757-46. 937 1.00 25.25 5350 CE MET E 236-59.873 68.306-48. 508 1.00 23.59 5351 C MET E 236-62.909 71.766-46. 416 1.00 30.02 5352 O MET E 236-64.075 72.001-46. 083 1.00 29.77 5353 N PRO E 237-62. 137 72.696-47. 008 1.00 31.66 5354 CD PRO E 237-60.699 72. 591-47. 317 1.00 31.11 5355 CA PRO E 237-62.630 74. 045-47. 305 1.00 34.73 5356 CB PRO E 237-61. 342 74.851-47. 441 1.00 33.58 5357 CG PRO E 237-60.438 73.868-48. 107 1.00 33.04 5358 C PRO E 237-63. 482 74.100-48. 573 1.00 36.63 5359 O PRO E 237-63.513 73.149-49. 356 1.00 36.25 5360 N GLU E 238-64.157 75.228-48. 769 1.00 40.02 5361 CA GLU E 238-65.021 75.430-49. 928 1. 00 43.92 5362 CB GLU E 238-65.932 76.640-49. 696 1.00 46.73 5363 CG GLU E 238-66. 939 76.459-48. 567 1.00 52.12 5364 CD GLU E 238-67.998 75.419-48. 887 1.00 55.65 5365 OE1 GLU E 238-68.748 75.614-49. 870 1.00 57.97 5366 OE2 GLU E 238-68.084 74.406-48. 158 1.00 57.24 5367 C GLU E 238-64.240 75.627-51. 223 1.00 44.02 5368 O GLU E 238-64. 756 75. 363-52. 311 1.00 46.07 5369 N THR E 239-63.000 76. 089-51.114 1.00 43.32 5370 CA THR E 239-62.188 76. 314-52. 303 1.00 42.81 5371 CB THR E 239-62.086 77.820-52. 623 1.00 43.95 5372 OG1 THR E 239-61. 484 78.506-51. 518 1.00 45. 97 5373 CG2 THR E 239-63.468 78.402-52. 884 1.00 44. 29 5374 C THR E 239-60.780 75.744-52. 191 1.00 41. 26 5375 O THR E 239-60.192 75.712-51. 109 1. 00 40.53 5376 N LEU E 240-60.253 75.294-53. 326 1.00 39.30 1 2 3 4 5 6 7 8 9 10 5377 CA LEU E 240-58.912 74. 724-53. 404 1.00 38.43 5378 CB LEU E 240-57.869 75. 847-53. 373 1. 00 38. 97 5379 CG LEU E 240-57.992 76. 905-54. 477 1.00 40.83 5380 CD1 LEU E 240-57. 034 78.058-54. 209 1.00 40.37 5381 CD2 LEU E 240-57. 707 76.265-55. 828 1.00 41.06 5382 C LEU E 240-58.630 73.720-52. 283 1.00 37.49 5383 O LEU E 240-57.645 73.849-51. 553 1.00 36.88 5384 N PRO E 241-59. 494 72.702-52. 132 1.00 36.07 5385 CD PRO E 241-60.698 72.376-52. 919 1.00 35.32 5386 CA PRO E 241-59.273 71.709-51. 076 1.00 34.11 5387 CB PRO E 241-60.532 70.841-51. 148 1.00 34.47 5388 CG PRO E 241-60.906 70.909-52. 597 1.00 36. 17 5389 C PRO E 241-57. 990 70.914-51. 301 1.00 33. 03 5390 O PRO E 241-57.714 70.462-52. 416 1.00 31.47 5391 N ASN E 242-57.204 70.753-50. 239 1.00 31. 55 5392 CA ASN E 242-55.948 70. 021-50. 328 1.00 31. 26 5393 CB ASN E 242-54.912 70.848-51. 101 1.00 34.21 5394 CG ASN E 242-54.113 70.016-52. 083 1.00 37. 31 5395 OD1 ASN E 242-54.622 69.601-53. 123 1.00 41.79 5396 ND2 ASN E 242-52.856 69.759-51. 752 1.00 41.29 5397 C ASN E 242-55.416 69.711-48. 928 1.00 30.14 5398 O ASN E 242-54.551 70.423-48. 412 1.00 28.76 5399 N ASN E 243-55.948 68. 656-48. 316 1. 00 26.81 5400 CA ASN E 243-55. 528 68.234-46. 983 1.00 24.72 5401 CB ASN E 243-56.681 68.335-45. 980 1.00 25.55 5402 CG ASN E 243-56.919 69.745-45. 486 1.00 26.81 5403 OD1 ASN E 243-55. 984 70.450-45. 106 1.00 23. 30 5404 ND2 ASN E 243-58.186 70.155-45. 458 1.00 26.18 5405 C ASN E 243-55.071 66. 784-47. 005 1. 00 23.31 5406 O ASN E 243-55.803 65. 910-47. 475 1.00 23.47 5407 N SER E 244-53.864 66.522-46. 515 1.00 20. 54 5408 CA SER E 244-53. 390 65.146-46. 453 1. 00 20. 47 5409 CB SER E 244-51. 863 65.068-46. 626 1. 00 20. 26 1 2 3 4 5 6 7 8 9 10 5410 OG SER E 244-51.161 65.723-45. 581 1.00 21.06 5411 C SER E 244-53. 820 64. 668-45. 060 1. 00 20. 91 5412 O SER E 244-53. 962 65. 479-44. 137 1.00 19.85 5413 N CYS E 245-54.051 63.369-44. 918 1.00 20.46 5414 CA CYS E 245-54. 494 62. 800-43. 644 1.00 22.55 5415 C CYS E 245-53. 653 61. 568-43. 328 1.00 20.79 5416 O CYS E 245-53. 677 60.607-44. 084 1.00 20. 35 5417 CB CYS E 245-55.969 62. 374-43. 742 1.00 26.22 5418 SG CYS E 245-56.869 62.449-42. 163 1.00 33.40 5419 N TYR E 246-52.915 61.599-42. 221 1.00 19.67 5420 CA TYR E 246-52. 072 60.469-41. 829 1.00 18.28 5421 CB TYR E 246-50.598 60.910-41. 737 1.00 17.72 5422 CG TYR E 246-49.628 59.852-41. 216 1.00 15.37 5423 CD1 TYR E 246-49.596 59.495-39. 861 1.00 15.88 5424 CE1 TYR E 246-48.694 58. 533-39. 383 1.00 14.14 5425 CD2 TYR E 246-48.734 59.218-42. 077 1.00 15.71 5426 CE2 TYR E 246-47. 827 58. 253-41. 606 1.00 15.55 5427 CZ TYR E 246-47.813 57. 919-40. 264 1.00 15.40 5428 OH TYR E 246-46.917 56. 975-39. 797 1.00 17.22 5429 C TYR E 246-52.486 59. 864-40. 494 1.00 18. 63 5430 O TYR E 246-52.902 60. 575-39. 575 1.00 18. 64 5431 N SER E 247-52.376 58.544-40. 396 1. 00 17.23 5432 CA SER E 247-52.661 57. 854-39. 149 1.00 17.08 5433 CB SER E 247-54.160 57.584-38. 982 1.00 18.50 5434 OG SER E 247-54.429 57.151-37. 651 1.00 19.43 5435 C SER E 247-51.880 56.543-39. 131 1.00 16.25 5436 O SER E 247-51.607 55. 959-40. 182 1.00 15. 78 5437 N ALA E 248-51.511 56. 098-37. 935 1.00 15. 65 5438 CA ALA E 248-50. 755 54.862-37. 765 1.00 16. 98 5439 CB ALA E 248-49. 257 55. 124-37. 995 1.00 15.29 5440 C ALA E 248-50. 974 54.298-36. 366 1. 00 17.30 5441 0 ALA E 248-51. 304 55. 032-35.424 1.00 16. 60 5442 N GLY E 249-50.781 52. 993-36. 223 1.00 16. 87 1 2 3 4 5 6 7 8 9 10 5443 CA GLY E 249-50.958 52.377-34. 921 1.00 17.25 5444 C GLY E 249-50. 368 50. 986-34. 905 1.00 17.84 5445 O GLY E 249-49.844 50.526-35. 922 1.00 15.97 5446 N ILE E 250-50. 455 50. 315-33. 760 1.00 16.79 5447 CA ILE E 250-49.919 48. 964-33. 628 1.00 16.73 5448 CB ILE E 250-48. 907 48.870-32. 457 1.00 16.29 5449 CG2 ILE E 250-48.462 47.411-32. 278 1.00 16.10 5450 CG1 ILE E 250-47.697 49.781-32. 728 1.00 16.74 5451 CDI ILE E 250-46.685 49.837-31. 572 1.00 19.08 5452 C ILE E 250-51. 031 47. 940 -33.387 1.00 18.68 5453 O ILE E 250-51.943 48.171-32. 591 1.00 17.15 5454 N ALA E 251-50.958 46.809-34. 080 1.00 17.50 5455 CA ALA E 251-51.957 45. 765-33. 898 1. 00 18. 77 5456 CB ALA E 251-53. 063 45. 895-34. 957 1.00 18.29 5457 C ALA E 251-51.343 44.375 -33. 963 1.00 18.91 5458 O ALA E 251-50. 366 44.140-34. 685 1.00 18.37 5459 N LYS E 252-51.912 43. 461-33. 185 1.00 20.11 5460 CA LYS E 252-51.476 42. 069-33. 176 1.00 21.05 5461 CB LYS E 252-51.821 41.422-31. 832 1.00 24.52 5462 CG LYS E 252-51.582 39.919-31. 751 1.00 30.34 5463 CD LYS E 252-50. 108 39.586-31. 719 1.00 35.48 5464 CE LYS E 252-49.887 38.097-31. 484 1.00 38.48 5465 NZ LYS E 252-50.483 37. 656-30. 193 1.00 42.53 5466 C LYS E 252-52. 312 41.435-34. 283 1.00 21.27 5467 O LYS E 252-53. 539 41.455-34. 213 1.00 22.19 5468 N LEU E 253-51.661 40. 889-35. 305 1.00 19.66 5469 CA LEU E 253-52.385 40. 283-36. 416 1.00 20.74 5470 CB LEU E 253-52.047 41.012-37. 725 1. 00 19.27 5471 CG LEU E 253-52.292 42. 534-37. 774 1.00 20.68 5472 CD1 LEU E 253-51. 765 43. 092-39. 088 1.00 19.66 5473 CD2 LEU E 253-53. 780 42.841-37. 615 1.00 20.74 5474 C LEU E 253-52.050 38.797-36. 549 1.00 22.56 5475 O LEU E 253-50.968 38.358-36. 158 1.00 23. 50 1 2 3 4 5 6 7 8 9 10 5476 N GLU E 254-52.983 38.024-37. 096 1.00 24. 01 5477 CA GLU E 254-52.765 36.594-37. 269 1.00 26.00 5478 CB GLU E 254-53. 944 35.808-36. 665 1.00 31.48 5479 CG GLU E 254-54.144 36.083-35. 180 1.00 42.41 5480 CD GLU E 254-55. 244 35. 241-34. 568 1.00 48.92 5481 OE1 GLU E 254-55. 949 34.529-35. 320 1. 00 52.62 5482 OE2 GLU E 254-55.410 35.293-33. 329 1. 00 53.98 5483 C GLU E 254-52.579 36.196-38. 721 1.00 23.61 5484 O GLU E 254-53.122 36.842-39. 627 1.00 21.77 5485 N GLU E 255-51. 814 35.128-38. 943 1.00 23.70 5486 CA GLU E 255-51. 577 34. 612-40. 289 1.00 24.44 5487 CB GLU E 255-50. 829 33.273-40. 206 1.00 27.24 5488 CG GLU E 255-50. 459 32.679-41. 563 1.00 33. 74 5489 CD GLU E 255-49. 685 31.377-41. 460 1. 00 38.53 5490 OE1 GLU E 255-49.469 30. 903-40. 330 1.00 40.21 5491 OE2 GLU E 255-49.290 30.828-42. 514 1.00 42.57 5492 C GLU E 255-52.929 34.431-40. 967 1.00 23.55 5493 0 GLU E 255-53.830 33. 812-40. 394 1.00 23.74 5494 N GLY E 256-53.067 34.971-42. 177 1. 00 22.40 5495 CA GLY E 256-54. 340 34.856-42. 872 1.00 21.39 5496 C GLY E 256-55.132 36. 153-42. 884 1. 00 20.60 5497 0 GLY E 256-55.962 36. 365-43. 769 1.00 18.98 5498 N ASP E 257-54. 905 37. 013-41. 892 1.00 19.82 5499 CA ASP E 257-55. 597 38.301-41. 842 1. 00 21. 56 5500 CB ASP E 257-55.242 39.100-40. 571 1. 00 22.20 5501 CG ASP E 257-55.915 38.571-39. 311 1.00 25.18 5502 OD1 ASP E 257-56. 863 37. 765-39.415 1.00 23.12 5503 OD2 ASP E 257-55. 493 38.986-38. 203 1.00 25.23 5504 C ASP E 257-55.148 39.133-43. 041 1.00 21.21 5505 |O ASP E 257-54.078 38.899-43. 598 1. 00 22.38 5506 N GLU E 258-55.968 40.101-43. 429 1.00 21.48 5507 CA GLU E 258-55. 633 40.990-44. 529 1. 00 23.36 5508 CB GLU E 258-56. 467 40.662-45. 768 1.00 25.44 1 2 3 4 5 6 7 8 9 10 5509 CG GLU E 258-56.239 39. 271-46. 317 1.00 31.82 5510 CD GLU E 258-56.922 39.063-47. 656 1. 00 36.82 5511 OE1 GLU E 258-58.160 39.233-47. 727 1.00 37.10 5512 OE2 GLU E 258-56.216 38.734-48. 635 1.00 41.12 5513 C GLU E 258-55.922 42.419-44. 086 1.00 22.67 5514 O GLU E 258-56.794 42. 647-43.245 1. 00 22.80 5515 N LEU E 259-55.180 43. 374-44. 640 1. 00 21.66 5516 CA LEU E 259-55.378 44. 787-44. 318 1.00 20.75 5517 CB LEU E 259-54.103 45.387-43. 712 1.00 21.78 5518 CG LEU E 259-53.538 44.768-42. 428 1.00 22.56 5519 CD1 LEU E 259-52.169 45.369-42. 114 1. 00 20.55 5520 CD2 LEU E 259-54. 507 45.003-41. 285 1.00 22.98 5521 C LEU E 259-55.727 45. 554-45. 593 1.00 21.13 5522 O LEU E 259-55.190 45.267-46. 660 1.00 21. 60 5523 N GLN E 260-56.632 46.519-45. 481 1.00 20.87 5524 CA GLN E 260-57.015 47.339-46. 621 1.00 22.49 5525 CB GLN E 260-58.246 46.754-47. 336 1.00 24.06 5526 CG GLN E 260-59. 495 46.599-46. 478 1.00 24.85 5527 CD GLN E 260-60.646 45.961-47. 254 1.00 27.51 5528 OE1 GLN E 260-60.445 44.992-47. 982 1.00 28. 39 5529 NE2 GLN E 260-61.852 46. 498-47. 093 1.00 25.87 5530 C GLN E 260-57. 305 48.759-46. 157 1.00 20.83 5531 O GLN E 260-57.663 48.978-45. 001 1.00 20.82 5532 N LEU E 261-57.125 49. 722-47. 057 1. 00 20.59 5533 CA LEU E 261-57. 373 51.127-46. 742 1.00 22. 12 5534 CB LEU E 261-56.148 51.980-47. 109 1.00 22.24 5535 CG LEU E 261-56.175 53.461-46. 700 1.00 24.78 5536 CD1 LEU E 261-54.746 53.982-46. 549 1.00 24.36 5537 CD2 LEU E 261-56.946 54.267-47. 727 1.00 23.15 5538 C LEU E 261-58.595 51. 566-47. 537 1.00 22.53 5539 O LEU E 261-58.575 51.577-48. 768 1.00 24.14 5540 N ALA E 262-59.654 51.939-46. 824 1.00 23. 28 5541 CA ALA E 262-60.903 52. 325-47. 457 1.00 22. 64 1 2 3 4 5 6 7 8 9 10 5542 CB ALA E 262-62.004 51. 343-47. 034 1.00 23.66 5543 C ALA E 262-61.367 53. 745-47. 184 1.00 23.61 5544 O ALA E 262-61.196 54.265-46. 086 1.00 24.57 5545 N ILE E 263-61.968 54.359-48. 198 1.00 22.35 5546 CA ILE E 263-62.517 55.706-48. 083 1.00 24.19 5547 CB ILE E 263-62.019 56.619-49. 227 1.00 22.80 5548 CG2 ILE E 263-62.659 58.002-49. 103 1. 00 21. 45 5549 CG I ILE E 263-60.488 56. 725-49. 169 1.00 22.62 5550 CD1 ILE E 263-59.877 57. 531-50. 300 1.00 23.50 5551 C ILE E 263-64.033 55.514-48. 188 1.00 26.54 5552 O ILE E 263-64.547 55.161-49. 250 1.00 26.25 5553 N PRO E 264-64.762 55.730-47. 082 1.00 28.73 5554 CD PRO E 264-64.248 56.187-45. 776 1.00 29.56 5555 CA PRO E 264-66.222 55. 570-47. 037 1.00 31.45 5556 CB PRO E 264-66.514 55. 572-45. 540 1.00 31.38 5557 CG PRO E 264-65.520 56. 573-45. 035 1.00 31. 24 5558 C PRO E 264-67.038 56.619-47. 787 1.00 32.77 5559 O PRO E 264-67.872 57.304-47. 200 1.00 33.93 5560 N ARG E 265-66.796 56.734-49. 085 1.00 34.77 5561 CA ARG E 265-67.521 57.682-49. 920 1.00 37.13 5562 CB ARG E 265-66.958 59. 096-49. 757 1.00 41.03 5563 CG ARG E 265-67.819 60.159-50. 417 1.00 45.73 5564 CD ARG E 265-67.262 61.559-50. 229 1.00 50.01 5565 NE ARG E 265-68. 317 62. 560-50. 367 1.00 54.84 5566 CZ ARG E 265-69.088 62. 979-49. 366 1.00 57. 20 5567 NH1 ARG E 265-68.923 62.493-48. 142 1.00 58. 09 5568 NH2 ARG E 265-70. 037 63.876-49. 589 1.00 58. 14 5569 C ARG E 265-67.388 57.251-51. 372 1.00 37. 30 5570 O ARG E 265-66.314 56.833-51. 803 1.00 35.42 5571 N GLU E 266-68.482 57.346-52. 123 1.00 37.81 5572 CA GLU E 266-68. 468 56. 968-53. 530 1.00 37.81 5573 CB GLU E 266-69.899 56. 809-54. 050 1.00 41.03 5574 CG GLU E 266-70. 673 55. 661-53. 425 1.00 45.52 1 2 3 4 5 6 7 8 9 10 5575 CD GLU E 266-72.093 55. 571-53. 957 1.00 49.54 5576 OE1 GLU E 266-72.260 55. 494-55. 192 1.00 50.86 5577 OE2 GLU E 266-73. 042 55. 575-53. 143 1.00 51.45 5578 C GLU E 266-67.741 58. 028-54353 1.00 36.24 5579 O GLU E 266-67.911 59. 226-54. 125 1.00 35.94 5580 N ASN'E 267-66.931 57. 573-55. 305 1.00 34.82 5581 CA ASN E 267-66. 171 58.461-56. 177 1.00 35.28 5582 CB ASN E 267-67.096 59.108-57. 208 1.00 36.49 5583 CG ASN E 267-67.807 58.088-58. 064 1.00 38.12 5584 OD1 ASN E 267-67.169 57.283-58. 744 1.00 37.77 5585 ND2 ASN E 267-69.137 58.109-58. 032 1.00 38.62 5586 C ASN E 267-65.423 59.550-55. 423 1. 00 34.54 5587 O ASN E 267-65.524 60.731-55. 762 1.00 34.48 5588 N ALA E 268-64.667 59. 150-54. 405 1.00 32.87 5589 CA ALA E 268-63. 896 60.099-53. 607 1. 00 31.38 5590 CB ALA E 268-63.266 59. 382-52. 417 1.00 30.51 5591 C ALA E 268-62.811 60.760-54. 461 1.00 30.50 5592 O ALA E 268-62.124 60. 088-55. 234 1.00 30.00 5593 N GLN E 269-62.667 62. 075-54. 320 1.00 30.49 5594 CA GLN E 269-61.667 62. 826-55. 072 1.00 31.20 5595 CB GLN E 269-62.187 64. 235-55. 370 1.00 34.27 5596 CG GLN E 269-63.439 64.239-56. 231 1.00 37.74 5597 CD GLN E 269-63.206 63. 582-57. 577 1. 00 39.16 5598 OEIL GLN E 269-62.542 64.148-58. 447 1.00 40.68 5599 NE2 GLN E 269-63. 737 62.373-57. 751 1.00 38.73 5600 C GLN E 269-60.367 62.904-54. 278 1.00 30.58 5601 O GLN E 269-60. 306 63. 553-53. 233 1.00 28.39 5602 N ILE E 270-59.332 62.244-54. 785 1.00 29.73 5603 CA ILE E 270-58.043 62.215-54. 110 1.00 30.80 5604 CB ILE E 270-57.877 60. 906-53. 299 1.00 31.47 5605 CG2 ILE E 270-58.998 60.774-52. 272 1.00 29. 06 5606 CG1 ILE E 270-57. 892 59.705-54. 253 1.00 31.86 5607 CD1 ILE E 270-57. 616 58. 375-53. 580 1.00 34.39 1 2 3 4 5 6 7 8 9 10 5608 C ILE E 270-56.873 62. 303-55. 084 1.00 31.11 5609 O ILE E 270-57. 045 62.200-56. 302 1. 00 30.94 5610 N SER E 271-55. 680 62.489-54. 532 1.00 30.56 5611 CA SER E 271-54.464 62.562-55. 329 1.00 30.00 5612 CB SER E 271-53. 493 63. 581-54. 733 1.00 30.64 5613 OG SER E 271-52.243 63. 522-55. 395 1.00 31.44 5614 C SER E 271-53. 817 61. 181-55. 328 1.00 29.94 5615 O SER E 271-53. 769 60. 507-54. 301 1.00 29.16 5616 N LEU E 272 -53.318 60.760-56. 482 1.00 28.67 5617 CA LEU E 272-52.689 59.456-56. 598 1.00 28. 64 5618 CB LEU E 272-53. 269 58.699-57. 791 1.00 29. 22 5619 CG LEU E 272-54.764 58. 387-57. 685 1.00 29.64 5620 CD1 LEU E 272-55.232 57.649-58. 933 1.00 32.32 5621 CD2 LEU E 272-55.024 57.545-56. 443 1. 00 29.78 5622 C LEU E 272-51.175 59.539-56. 711 1. 00 29.71 5623 O LEU E 272-50.531 58.660-57. 289 1.00 30.01 5624 N ASP E 273-50.600 60.596-56. 144 1.00 30.48 5625 CA ASP E 273-49. 147 60.774-56. 154 1.00 31.04 5626 CB ASP E 273-48.786 62. 230-55. 843 1.00 35.80 5627 CG ASP E 273-47. 303 62.517-56. 003 1.00 42.87 5628 OD1 ASP E 273-46.494 61.560-55. 938 1.00 45.88 5629 OD2 ASP E 273-46.949 63.704-56. 187 1.00 47.96 5630 C ASP E 273-48.580 59. 846-55. 090 1.00 28.27 5631 O ASP E 273-49. 011 59.884-53. 931 1.00 26.97 5632 N GLY E 274-47.591 59.051-55. 488 1.00 26.61 5633 CA GLY E 274-46.978 58.108-54. 566 1.00 26.80 5634 C GLY E 274-46.354 58.665-53. 298 1. 00 27.55 5635 O GLY E 274-46.239 57. 941-52. 303 1.00 26.27 5636 N ASP E 275-45.956 59. 936-53. 307 1.00 25.68 5637 CA ASP E 275 -45.347 60.512-52. 117 1.00 25.07 5638 CB ASP E 275-44.271 61.546-52. 489 1.00 26. 30 5639 CG ASP E 275-44.806 62. 703-53. 315 1.00 29.08 5640 OD1 ASP E 275-46.017 62. 994-53. 262 1.00 28.43 1 2 3 4 5 6 7 8 9 10 5641 OD2 ASP E 275-43.990 63.342-54. 013 1. 00 31. 91 5642 C ASP E 275-46.324 61.133-51. 123 1.00 23. 00 5643 O ASP E 275-45.909 61.593-50. 059 1.00 21.60 5644 N VAL E 276-47.613 61.139-51. 449 1.00 20.96 5645 CA VAL E 276-48.595 61.717-50. 541 1.00 20.34 5646 CB VAL E 276-49.158 63.051-51. 106 1.00 21.73 5647 CGI VAL E 276-50.187 62.783-52. 204 1.00 22.18 5648 CG2 VAL E 276-49. 742 63.881-49. 976 1.00 22.78 5649 C VAL E 276-49.738 60.757-50. 188 1.00 19.60 5650 O VAL E 276-50.447 60.965-49. 204 1.00 17.93 5651 N THR E 277-49.904 59. 702-50. 982 1.00 19.23 5652 CA THR E 277-50.939 58.693-50. 728 1.00 20.20 5653 CB THR E 277-52.032 58.712-51. 826 1.00 20.09 5654 OG1 THR E 277-52.728 59.960-51. 767 1.00 18.35 5655 CG2 THR E 277-53.042 57.581-51. 611 1.00 20.83 5656 C THR E 277-50.212 57.359-50. 717 1.00 18.48 5657 O THR E 277-49.741 56.892-51. 752 1.00 19.64 5658 N PHE E 278-50.092 56.763-49. 533 1.00 17.40 5659 CA PHE E 278-49. 364 55.508-49. 384 1.00 17.59 5660 CB PHE E 278-47.854 55.785-49. 246 1.00 17.11 5661 CG PHE E 278-47.509 56.772-48. 155 1.00 18. 68 5662 CD1 PHE E 278-47.348 56. 351-46. 840 1.00 16.85 5663 CD2 PHE E 278-47.344 58.127-48. 451 1.00 17.16 5664 CE1 PHE E 278-47.041 57.267-45. 830 1.00 18.93 5665 CE2 PHE E 278-47.038 59.052-47. 451 1.00 16.48 5666 CZ PHE E 278-46.880 58.623-46. 141 1.00 18.17 5667 C PHE E 278-49. 878 54.682-48. 211 1.00 17.24 5668 O PHE E 278-50.633 55. 176-47. 381 1.00 17.77 5669 N PHE E 279-49.437 53.431-48. 130 1.00 18. 77 5670 CA PHE E 279-49.949 52.509-47. 118 1.00 18.98 5671 CB PHE E 279-51.277 51.965-47. 692 1. 00 20.16 5672 CG PHE E 279-51.957 50.905-46. 866 1.00 20.57 5673 CD1 PHE E 279-52.071 51.016-45. 487 1.00 19. 42 123 4 5 6 7 8 9 10 5674 CD2 PHE E 279-52.571 49. 823-47. 505 1.00 23.00 5675 CE1 PHE E 279-52.775 50.060-44. 748 1.00 20.69 5676 CE2 PHE E 279-53. 280 48.861-46. 774 1.00 21.63 5677 CZ PHE E 279-53.385 48. 987-45.396 1.00 20.17 5678 C PHE E 279-48.902 51.419-46. 886 1.00 19.05 5679 O PHE E 279-48. 351 50.871-47. 839 1.00 19.25 5680 N GLY E 280-48.603 51.121-45. 625 1.00 18.84 5681 CA GLY E 280-47.602 50. 103-45349 1.00 18. 35 5682 C GLY E 280-47.672 49. 471-43. 975 1.00 17.87 5683 O GLY E 280-48.443 49.902-43. 118 1.00 17.15 5684 N ALA E 281-46.861 48.438-43. 763 1.00 19. 10 5685 CA ALA E 281-46.823 47.745-42. 482 1.00 19.77 5686 CB ALA E 281-47.852 46.614-42. 453 1.00 20.72 5687 C ALA E 281-45. 431 47.199-42. 216 1.00 19.52 5688 O ALA E 281-44.699 46.838-43. 143 1.00 19.48 5689 N LEU E 282-45.078 47.143-40. 938 1.00 19.98 5690 CA LEU E 282-43.767 46.672-40. 501 1.00 21.08 5691 CB LEU E 282-42.937 47.879-40. 062 1.00 24.10 5692 CG LEU E 282-41.693 47.682-39. 202 1.00 27.27 5693 CD1 LEU E 282-40. 559 47. 110-40. 044 1.00 26.11 5694 CD2 LEU E 282-41.294 49.031-38. 614 1.00 29.28 5695 C LEU E 282-43. 926 45. 697-39. 337 1.00 21. 13 5696 O LEU E 282-44.665 45. 974-38. 393 1.00 18. 79 5697 N LYS E 283-43.239 44.557-39. 402 1.00 20.50 5698 CA LYS E 283-43.331 43. 571-38. 328 1.00 22. 02 5699 CB LYS E 283-43. 018 42.163-38. 850 1.00 22. 37 5700 CG LYS E 283-43. 374 41. 047-37. 864 1.00 22. 42 5701 CD LYS E 283-43. 055 39.666-38. 437 1.00 24. 44 5702 CE LYS E 283-43.643 38.541-37. 588 1.00 27.30 5703 NZ LYS E 283-43.109 38.524-36. 198 1. 00 26. 74 5704 C LYS E 283-42.364 43. 932-37. 202 1.00 24.22 5705 O LYS E 283-41.160 44.075-37. 419 1.00 25.41 5706 N LEU E 284-42.897 44.082-35. 996 1.00 22.51 1 2 3 4 5 6 7 8 9 10 5707 CA LEU E 284-42.082 44.443-34. 844 1.00 26. 21 5708 CB LEU E 284-42.973 45.061-33. 765 1.00 22. 34 5709 CG LEU E 284-43. 780 46.265-34. 270 1.00 23.34 5710 CD1 LEU E 284-44.714 46.761-33. 185 1.00 23.99 5711 CD2 LEU E 284-42.817 47. 365-34. 709 1. 00 22.72 5712 C LEU E 284-41.354 43.225-34. 284 1.00 29.97 5713 O LEU E 284-41.932 42.143-34. 179 1.00 31.53 5714 N LEU E 285-40.084 43394-33. 937 1. 00 33. 03 5715 CA LEU E 285-39. 319 42.289-33. 376 1.00 37.50 5716 CB LEU E 285-37.837 42.656-33. 271 1.00 37.77 5717 CG LEU E 285-37. 047 42.449-34. 566 1.00 40.46 5718 CD1 LEU E 285-35.619 42. 939-34. 395 1.00 41.30 5719 CD2 LEU E 285-37.062 40.967-34. 931 1.00 41.03 5720 C LEU E 285-39.869 41. 930-32. 003 1.00 38.98 5721 O LEU E 285-40.130 40.730-31. 768 1.00 41.85 5722 OXT LEU E 285-40. 034 42.856-31. 181 1.00 41. 70 5723 CB VAL F 142-33.702 40.776-29. 187 1.00 46.74 5724 CG1 VAL F 142-32.364 40.573-28. 494 1.00 47.93 5725 CG2 VAL F 142-33.601 40. 378-30. 653 1.00 46.79 5726 C VAL F 142-36.158 40.329-29. 027 1.00 43. 38 5727 O VAL F 142-36.562 39.883-30. 101 1.00 43.17 5728 N VAL F 142-34. 539 38.474-28. 655 1.00 46.03 5729 CA VAL F 142-34.789 39.935-28. 480 1.00 45.42 5730 N THR F 143-36.868 41.167-28. 280 1.00 41.75 5731 CA THR F 143-38.198 41.610-28. 678 1. 00 39. 21 5732 CB THR F 143-39.276 40.671-28. 096 1.00 41.23 5733 OG1 THR F 143-40. 579 41.199-28. 370 1.00 44.93 5734 CG2 THR F 143-39.098 40.525-26. 593 1.00 43. 20 5735 C THR F 143-38.460 43.037-28. 203 1.00 36.74 5736 O THR F 143-37.848 43.500-27. 241 1.00 38.13 5737 N GLN F 144-39. 366 43.730-28. 886 1.00 31.99 5738 CA GLN F 144-39. 705 45.107-28. 539 1.00 28.95 5739 CB GLN F 144-39.882 45.946-29. 802 1. 00 29.55 1 2 3 4 5 6 7 8 9 10 5740 CG GLN F 144-38.614 46.184-30. 583 1.00 30.58 5741 CD GLN F 144-38.870 46.962-31. 850 1.00 32.70 5742 OE1 GLN F 144-39. 501 46.462-32. 785 1.00 32.01 5743 NE2 GLN F 144-38. 391 48.197-31. 890 1.00 34.89 5744 C GLN F 144-40.987 45.195-27. 724 1.00 26.78 5745 O GLN F 144-42.074 44.932-28. 240 1.00 23.79 5746 N ASP F 145-40.857 45.567-26. 455 1.00 23.57 5747 CA ASP F 145-42. 020 45.710-25. 595 1. 00 22.87 5748 CB ASP F 145 -41.594 45.896 -24.133 1.00 23.14 5749 CB ASP F 145 -40.949 44.651 -23.543 1.00 27.10 5750 CB ASP F 145 -40.874 43.622 -24.252 1.00 26.86 5751 OD2 ASP F 145-40. 521 44.704-22. 367 1.00 26.82 5752 C ASP F 145 -42.796 46.939 -26.056 1.00 21.81 5753 O ASP F 145 -42.218 47.882 -26.607 1.00 19.38 5754 N CYS F 146-44.107 46.921-25. 846 1.00 19.97 5755 CA CYS F 146-44. 947 48.047-26. 223 1.00 18.98 5756 CB CYS F 146-45. 135 48.114-27. 750 1.00 21.00 5757 SG CYS F 146-45.358 46.537-28. 633 1.00 24.90 5758 C CYS F 146-46.293 47.988-25. 516 1.00 19.47 5759 0 CYS F 146-46.698 46.940-25. 007 1.00 19.01 5760 N LEU F 147-46.972 49.128-25. 471 1.00 18.41 5761 CA LEU F 147-48.268 49.226-24. 816 1.00 19.69 5762 CB LEU F 147-48.076 49. 611-23. 340 1.00 20.25 5763 CG LEU F 147-49. 302 49.642-22. 421 1.00 22. 58 5764 CD1 LEU F 147-48.872 49.398-20. 985 1.00 21.69 5765 CD2 LEU F 147-50.022 50.986-22. 556 1.00 24.74 5766 C LEU F 147-49.105 50.267-25. 555 1.00 19. 35 5767 O LEU F 147-48.608 51. 338-25. 917 1.00 18. 24 5768 N GLN F 148-50.367 49.938-25. 801 1.00 16.40 5769 CA GLN F 148-51.262 50.842-26. 512 1. 00 15.08 5770 CB GLN F 148-51.532 50.296-27. 919 1.00 15.73 5771 CG GLN F 148-52.443 51.159-28. 786 1.00 16. 01 5772 CD GLN F 148-52.457 50.694-30. 231 1.00 20. 35 1 2 3 4 5 6 7 8 9 10 5773 OE1 GLN F 148-51.657 51.153-31. 052 1. 00 18.66 5774 NE2 GLN F 148-53. 361 49. 761-30. 547 1.00 18.17 5775 C GLN F 148-52.574 51.028-25. 755 1.00 16.51 5776 O GLN F 148-53. 123 50.068-25. 201 1.00 16.95 5777 N LEU F 149-53. 067 52.266-25. 750 1.00 16.52 5778 CA LEU F 149-54. 308 52.635-25. 073 1.00 17.09 5779 CB LEU F 149-54.029 53.701-23. 994 1.00 14.95 5780 CG LEU F 149-53. 056 53.363-22. 851 1.00 16.47 5781 CD1 LEU F 149-52.823 54.603-21. 980 1.00 17.28 5782 CD2 LEU F 149-53.614 52.227-22. 008 1.00 17.38 5783 C LEU F 149-55. 292 53.202-26. 093 1.00 19.62 5784 O LEU F 149-54.895 53.920-27. 011 1.00 19.30 5785 N ILE F 150-56.573 52.874-25. 942 1.00 17. 79 5786 CA ILE F 150-57. 599 53. 382-26. 847 1.00 17. 75 5787 CB ILE F 150-58.212 52. 247-27.716 1.00 19. 33 5788 CG2 ILE F 150-57. 182 51.755-28. 722 1.00 19. 19 5789 CG1 ILE F 150-58.690 51.095-26. 827 1.00 20. 96 5790 CD1 ILE F 150-59. 377 49.971-27. 597 1.00 25. 31 5791 C ILE F 150-58.688 54.062-26. 019 1.00 18.22 5792 O ILE F 150-58.904 53.708-24. 863 1.00 19.24 5793 N ALA F 151-59. 360 55.047-26. 605 1.00 17.73 5794 CA ALA F 151-60.404 55.783-25. 897 1.00 19.41 5795 CB ALA F 151-60.983 56.859-26. 801 1.00 18.85 5796 C ALA F 151-61. 525 54. 877-25. 379 1.00 22.64 5797 O ALA F 151-61.852 53.861-25. 996 1.00 19.98 5798 N ASP F 152-62.100 55.258-24. 242 1.00 24.16 5799 CA ASP F 152-63. 187 54.502-23. 613 1. 00 28.01 5800 CB ASP F 152-62.850 54.245-22. 143 1.00 28.99 5801 CG ASP F 152-63.906 53.409-21. 431 1.00 31. 85 5802 OD1 ASP F 152-64.887 52.985-22. 077 1.00 33.18 5803 OD2 ASP F 152-63.746 53.176-20. 217 1.00 33.15 5804 C ASP F 152-64.483 55.305-23. 725 1.00 28.73 5805 O ASP F 152-64. 713 56.248-22. 969 1. 00 28. 28 1 2 3 4 5 6 7 8 9 10 5806 N SER F 153-65. 328 54.925-24. 677 1. 00 31. 39 5807 CA SER F 153-66.589 55.625-24. 916 1.00 34.53 5808 CB SER F 153-67. 238 55.094-26. 199 1. 00 36.49 5809 OG SER F 153-67.340 53.678-26. 168 1.00 39.33 5810 C SER F 153-67.606 55. 570-23. 773 1.00 35. 59 5811 O SER F 153-68.524 56.388-23. 722 1.00 35.86 5812 N GLU F 154-67.443 54.621-22. 858 1.00 37.77 5813 CA GLU F 154-68.375 54.480-21. 738 1.00 41.08 5814 CB GLU F 154-68.530 53. 001-21. 370 1.00 42.56 5815 CG GLU F 154-69.020 52.134-22. 519 1.00 48.21 5816 CD GLU F 154-70. 383 52.562-23. 038 1.00 51.41 5817 OE1 GLU F 154-70.818 52.021-24. 078 1.00 53. 64 5818 OE2 GLU F 154-71.024 53.432-22. 405 1.00 54.19 5819 C GLU F 154-67.964 55. 263-20. 494 1.00 40.83 5820 O GLU F 154-68.521 55.060-19. 414 1.00 41.50 5821 N THR F 155-66.997 56. 160-20. 649 1.00 39.38 5822 CA THR F 155-66.510 56.954-19. 528 1.00 36.97 5823 CB THR F 155-65.134 56.438-19. 061 1.00 38.28 5824 OG1 THR F 155-65.243 55.057-18. 693 1.00 38.36 5825 CG2 THR F 155-64.630 57.241-17. 871 1.00 38. 97 5826 C THR F 155-66. 373 58.421-19. 913 1.00 35.76 5827 O THR F 155-65.906 58.742-21. 004 1.00 35.32 5828 N PRO F 156-66.786 59.335-19. 021 1.00 34.63 5829 CD PRO F 156-67.460 59.121-17. 726 1. 00 35.26 5830 CA PRO F 156-66.676 60. 765-19. 327 1.00 34.02 5831 CB PRO F 156-67.546 61.412-18. 253 1.00 34.64 5832 CG PRO F 156-67.362 60.489-17. 081 1.00 36. 89 5833 C PRO F 156-65.221 61.237-19. 263 1.00 32.35 5834 O PRO F 156-64.406 60.657-18. 545 1.00 29.43 5835 N THR F 157-64.894 62. 279-20. 021 1.00 32.62 5836 CA THR F 157-63.532 62.805-20. 009 1. 00 32. 01 5837 CB THR F 157-63.359 63.991-20. 983 1. 00 31. 97 5838 OG1 THR F 157-64.281 65. 033-20.639 1.00 34.44 1 2 3 4 5 6 7 8 9 10 5839 CG2 THR F 157-63.605 63.547-22. 419 1.00 30.62 5840 C THR F 157-63.199 63. 283-18. 598 1.00 32. 35 5841 O THR F 157-64.086 63. 660-17. 826 1.00 32.16 5842 N ILE F 158-61. 917 63. 255-18. 263 1.00 30.46 5843 CA ILE F 158-61.462 63. 682-16. 952 1.00 30.76 5844 CB ILE F 158-60.284 62. 799-16. 482 1. 00 30. 94 5845 CG2 ILE F 158-59.761 63. 273-15. 132 1.00 29.14 5846 CG1 ILE F 158-60.751 61. 344-16. 393 1.00 32.49 5847 CD1 ILE F 158-59.643 60. 347-16. 138 1.00 35.95 5848 C ILE F 158-61.034 65.146-17. 009 1.00 31.51 5849 O ILE F 158-60.245 65. 538-17. 867 1.00 30.45 5850 N GLN F 159-61. 578 65. 955-16. 105 1.00 30.49 5851 CA GLN F 159-61.245 67. 371-16. 050 1.00 32.69 5852 CB GLN F 159-62.515 68.208-15. 872 1.00 32.87 5853 CG GLN F 159-63.530 68. 048-16. 991 1.00 32.49 5854 CD GLN F 159-63.034 68.609-18. 307 1.00 31.76 5855 OE1 GLN F 159-62.638 69. 773-18. 385 1.00 31.48 5856 NE2 GLN F 159-63.059 67.787-19. 352 1.00 30.45 5857 C GLN F 159-60. 305 67.613-14. 877 1.00 34.60 5858 O GLN F 159-60.678 67.404-13. 724 1.00 34.21 5859 N LYS F 160-59.083 68. 045-15. 173 1.00 36.03 5860 CA LYS F 160-58.103 68. 308-14. 127 1.00 38. 17 5861 CB LYS F 160-57. 314 67.035-13. 795 1.00 38.92 5862 CG LYS F 160-56.194 67. 272-12. 791 1. 00 43. 34 5863 CD LYS F 160-55. 364 66. 024-12. 524 1.00 46.85 5864 CE LYS F 160-56.143 64. 978-11. 736 1.00 49.58 5865 NZ LYS F 160-55.280 63. 821-11. 354 1.00 52.18 5866 C LYS F 160-57.128 69.416-14. 506 1.00 38.92 5867 O LYS F 160-56.563 69. 417-15. 602 1.00 38.76 5868 N GLY F 161-56. 934 70.358-13. 587 1.00 39.39 5869 CA GLY F 161-56.015 71.456-13. 825 1.00 39.64 5870 C GLY F 161-56.275 72. 243-15. 095 1.00 40.02 5871 O GLY F 161-55. 333 72.626-15. 791 1. 00 41. 81 1 2 3 4 5 6 7 8 9 10 5872 N SER F 162 -57.547 72.483 -15.399 1.00 38.22 5873 CA SER F 162-57. 945 73.240-16. 584 1.00 37.68 5874 CB SER F 162-57.239 74.598-16. 604 1.00 40.05 5875 OG SER F 162-57. 562 75.348-15. 445 1.00 43.88 5876 C SER F 162-57. 704 72.514-17. 909 1.00 35. 15 5877 O SER F 162-57.898 73.089-18. 983 1.00 33.78 5878 N TYR F 163-57.278 71.257-17. 828 1.00 32.28 5879 CA TYR F 163-57. 041 70.444-19. 019 1.00 30. 64 5880 CB TYR F 163-55.657 69.780-18. 967 1.00 34.02 5881 CG TYR F 163-54. 474 70.680-19. 267 1.00 39.23 5882 CD1 TYR F 163-53.199 70.137-19. 424 1.00 40.48 5883 CE1 TYR F 163-52.097 70.941-19. 699 1.00 41.91 5884 CD2 TYR F 163-54.619 72.063-19. 392 1.00 41.12 5885 CE2 TYR F 163-53.516 72.882-19. 669 1.00 42.97 5886 CZ TYR F 163-52.258 72. 310-19. 820 1.00 43.05 5887 OH TYR F 163-51.159 73.099-20. 094 1.00 44.03 5888 C TYR F 163-58.095 69.342-19. 098 1.00 28.08 5889 O TYR F 163-58. 767 69.042-18. 111 1.00 27.13 5890 N THR F 164-58.226 68.739-20. 276 1. 00 24. 80 5891 CA THR F 164-59.163 67.643-20. 493 1.00 22.76 5892 CB THR F 164-60.085 67.912-21. 705 1.00 23.15 5893 OG1 THR F 164-60.988 68.988-21. 400 1.00 23.41 5894 CG2 THR F 164-60.879 66.658-22. 062 1.00 22.36 5895 C THR F 164-58.342 66. 384-20. 773 1.00 22.66 5896 O THR F 164-57. 470 66.387-21. 643 1.00 21. 50 5897 N PHE F 165-58.619 65. 315-20. 035 1.00 21.05 5898 CA PHE F 165-57. 900 64.063-20. 220 1.00 21.17 5899 CB PHE F 165-57.204 63.649-18. 920 1.00 21.55 5900 CG PHE F 165-56.066 64.556-18. 521 1.00 24.70 5901 CD1 PHE F 165-56.288 65.660-17. 701 1.00 25.22 5902 CD2 PHE F 165-54.769 64. 306-18. 974 1.00 23.75 5903 CE1 PHE F 165-55. 231 66.509-17. 335 1.00 27.50 5904 CE2 PHE F 165-53.706 65. 145-18. 616 1 00 26 11 1 2 3 4 5 6 7 8 9 10 5905 CZ PHE F 165-53. 937 66. 248-17. 792 1.00 25.82 5906 C PHE F 165-58.793 62.924-20. 706 1.00 22.24 5907 O PHE F 165-59. 802 62.585-20. 078 1.00 21.84 5908 N VAL F 166-58.407 62.343-21. 835 1.00 21.65 5909 CA VAL F 166-59. 133 61.229-22. 426 1.00 21.40 5910 CB VAL F 166-58.511 60.816-23. 791 1.00 21.21 5911 CG1 VAL F 166-59.291 59.649-24. 398 1.00 20.40 5912 CG2 VAL F 166-58.498 62.001-24. 743 1.00 20.46 5913 C VAL F 166-59. 057 60.023-21. 493 1.00 22.51 5914 O VAL F 166-57. 990 59.708-20. 968 1.00 22.14 5915 N PRO F 167-60.197 59.354-21. 247 1.00 21.59 5916 CD PRO F 167-61.566 59. 748-21. 635 1.00 23.67 5917 CA PRO F 167-60.211 58. 175-20. 376 1.00 20.83 5918 CB PRO F 167-61.675 58. 080-19. 949 1.00 21.33 5919 CG PRO F 167-62.403 58. 555-21. 169 1. 00 22. 16 5920 C PRO F 167-59. 763 56.997-21. 248 1.00 20.25 5921 O PRO F 167-60.340 56.751-22. 308 1.00 21.87 5922 N TRP F 168-58.732 56.282-20. 812 1.00 19.83 5923 CA TRP F 168-58.192 55.175-21. 601 1.00 21.57 5924 CB TRP F 168-56.655 55.219-21. 600 1.00 18. 75 5925 CG TRP F 168-56.045 56.493-22. 133 1.00 17.31 5926 CD2 TRP F 168-56.156 57.009-23. 468 1.00 17. 16 5927 CE2 TRP F 168-55.408 58.213-23. 509 1.00 16.70 5928 CE3 TRP F 168-56.787 56.564-24. 640 1.00 17. 26 5929 CD1 TRP F 168-55. 279 57. 381-21. 439 1.00 17.36 5930 NE1 TRP F 168-54.896 58.419-22. 257 1. 00 15. 39 5931 CZ2 TRP F 168-55. 306 58.990-24. 670 1.00 15.44 5932 CZ3 TRP F 168-56.683 57. 337-25. 797 1.00 17.28 5933 CH2 TRP F 168-55. 937 58.530-25. 805 1.00 16. 14 5934 C TRP F 168-58.603 53.767-21. 182 1.00 23.01 5935 O TRP F 168-58.944 53.507-20. 030 1.00 24.08 5936 N LEU F 169-58.534 52.864-22. 152 1.00 23.55 5937 CA LEU F 169-58.823 51. 453-21. 959 1.00 23. 96 1 2 3 4 5 6 7 8 9 10 5938 CB LEU F 169-60.076 51.072-22. 753 1.00 28. 78 5939 CG LEU F 169-60.738 49.712-22. 538 1.00 35.94 5940 CD1 LEU F 169-62.175 49.778-23. 057 1.00 36.66 5941 CD2 LEU F 169-59.948 48.613-23. 251 1.00 38.33 5942 C LEU F 169-57.582 50.776-22. 542 1.00 22.82 5943 O LEU F 169-57.010 51.273-23. 510 1.00 19.39 5944 N LEU F 170-57.152 49.662-21. 966 1.00 20. 86 5945 CA LEU F 170-55. 970 48.985-22. 485 1.00 22.39 5946 CB LEU F 170-55.421 47.988-21. 461 1.00 20.67 5947 CG LEU F 170-54.110 47. 312-21. 885 1.00 21.29 5948 CD1 LEU F 170-52. 972 48. 348-21. 903 1.00 20. 16 5949 CD2 LEU F 170-53.780 46.186-20. 924 1.00 21.09 5950 C LEU F 170-56.242 48.248-23. 795 1.00 22.92 5951 O LEU F 170-57. 177 47.454-23. 891 1.00 22.40 5952 N SER F 171-55. 432 48.533-24. 810 1.00 19.62 5953 CA SER F 171-55.562 47.859-26. 094 1.00 18. 67 5954 CB SER F 171-55. 004 48.744-27. 214 1.00 17. 87 5955 OG SER F 171-54. 970 48.061-28. 453 1.00 19.04 5956 C SER F 171-54.742 46.576-25. 951 1.00 20.76 5957 O SER F 171-55.225 45.477-26. 236 1.00 20.67 5958 N PHE F 172-53.498 46.727-25. 494 1.00 19.21 5959 CA PHE F 172-52.605 45.593-25. 261 1.00 19.84 5960 CB PHE F 172-52. 205 44.909-26. 584 1.00 19.86 5961 CG PHE F 172-51.216 45.698-27. 411 1.00 20.38 5962 CD1 PHE F 172-49.856 45.684-27. 103 1. 00 19.70 5963 CD2 PHE F 172-51.647 46.468-28. 486 1.00 18.55 5964 CE1 PHE F 172-48. 943 46.435-27. 850 1.00 21.22 5965 CE2 PHE F 172-50. 737 47. 224-29. 241 1.00 16.90 5966 CZ PHE F 172-49.388 47.203-28. 923 1.00 18.08 5967 C PHE F 172-51.341 46.030-24. 528 1. 00 20.34 5968 O PHE F 172-50. 944 47.200-24. 571 1.00 19.35 5969 N LYS F 173-50.725 45.076-23. 844 1. 00 20. 13 5970 CA LYS F 173-49.472 45.298-23. 137 1. 00 21. 85 1 2 3 4 5 6 7 8 9 10 5971 CB LYS F 173-49.686 45. 317-21. 620 1.00 22.82 5972 CG LYS F 173-48. 386 45.329-20. 811 1.00 24. 68 5973 CD LYS F 173-48.666 45.509-19. 326 1.00 24.74 5974 CE LYS F 173-47. 432 45.242-18. 485 1. 00 26.36 5975 NZ LYS F 173-47.002 43.819-18. 588 1.00 28.22 5976 C LYS F 173-48.581 44.124-23. 527 1.00 22.56 5977 O LYS F 173-48.884 42.974-23. 215 1.00 23.07 5978 N ARG F 174-47.498 44.418-24. 235 1.00 23.06 5979 CA ARG F 174-46.564 43.388-24. 677 1.00 22.61 5980 CB ARG F 174-46.314 43.526-26. 180 1.00 21.96 5981 CG ARG F 174-45. 506 42.391-26. 787 1.00 23.90 5982 CD ARG F 174-44.894 42.802-28. 118 1.00 23.94 5983 NE ARG F 174-44.301 41.662-28. 810 1.00 26.46 5984 CZ ARG F 174-43. 417 41.757-29. 799 1.00 24.98 5985 NH1 ARG F 174-43. 005 42.947-30. 219 1.00 23.42 5986 NH2 ARG F 174-42.954 40. 656-30. 379 1.00 27. 06 5987 C ARG F 174-45.247 43.552-23. 921 1.00 23. 07 5988 0 ARG F 174-44. 592 44.589-24. 028 1.00 20.83 5989 N GLY F 175-44.858 42.535-23. 158 1. 00 21.98 5990 CA GLY F 175-43.615 42.633-22. 411 1.00 23.55 5991 C GLY F 175-43.781 43. 349-21. 082 1.00 23.62 5992 0 GLY F 175-44. 900 43.552-20. 609 1.00 25.71 5993 N SER F 176-42.671 43.766-20. 483 1.00 23.76 5994 CA SER F 176-42.733 44.416-19. 178 1. 00 23. 92 5995 CB SER F 176-42.056 43.512-18. 146 1.00 25.68 5996 OG SER F 176-40.713 43.267-18. 521 1.00 30.56 5997 C SER F 176-42.149 45.823-19. 058 1. 00 23.40 5998 0 SER F 176-42.238 46.430-17. 994 1.00 23.45 5999 N ALA F 177-41.553 46.345-20. 127 1.00 21.84 6000 CA ALA F 177-40.964 47.684-20. 065 1.00 21.80 6001 CB ALA F 177-40.188 47.979-21. 349 1.00 21.42 6002 C ALA F 177-41.986 48. 795-19. 816 1.00 22.26 6003 O ALA F 177 -41. 633 49. 853-19. 292 1. 00 21. 34 1 2 3 4 5 6 7 8 9 10 6004 N LEU F 178-43.245 48.551-20. 181 1. 00 20.25 6005 CA LEU F 178-44.301 49.548-20. 014 1.00 21.24 6006 CB LEU F 178-44.686 50. 123-21. 381 1.00 20. 54 6007 CG LEU F 178-43.576 50.892-22. 107 1.00 21.25 6008 CD1 LEU F 178-43.845 50.926-23. 604 1.00 20.34 6009 CD2 LEU F 178-43.474 52.305-21. 521 1.00 19.45 6010 C LEU F 178-45.558 49.015-19. 326 1.00 23.07 6011 O LEU F 178-45.976 47.874-19. 556 1.00 21.59 6012 N GLU F 179-46.161 49.863-18. 497 1.00 22.32 6013 CA GLU F 179-47. 377 49. 524-17. 765 1.00 23.76 6014 CB GLU F 179-47.044 49.227-16. 298 1.00 26. 37 6015 CG GLU F 179-46.438 47.861-16. 026 1.00 30.47 6016 CD GLU F 179-45.991 47.701-14. 578 1.00 32.97 6017 OE1 GLU F 179-46.597 48. 340-13. 686 1.00 33. 36 6018 OE2 GLU F 179-45.040 46.929-14. 331 1. 00 31. 90 6019 C GLU F 179-48. 370 50.681-17. 802 1.00 25.10 6020 O GLU F 179-47.999 51.827-18. 068 1.00 23.25 6021 N GLU F 180-49.637 50.377-17. 541 1.00 23. 73 6022 CA GLU F 180-50.657 51.415-17. 483 1.00 26.79 6023 CB GLU F 180-51.976 50.949-18. 105 1.00 30.22 6024 CG GLU F 180-53.151 51.879-17. 790 1.00 33.51 6025 CD GLU F 180-54.467 51.399-18. 384 1.00 37. 18 6026 OE1 GLU F 180-54.681 50.168-18. 448 1. 00 38. 85 6027 OE2 GLU F 180-55.296 52.254-18. 772 1.00 39.51 6028 C GLU F 180-50.870 51.704-16. 003 1.00 27.58 6029 O GLU F 180-50.948 50.776-15. 191 1.00 26.69 6030 N LYS F 181-50. 953 52.984-15. 651 1. 00 26. 27 6031 CA LYS F 181-51.152 53.373-14. 261 1.00 27.07 6032 CB LYS F 181-49.810 53.452-13. 526 1.00 28.84 6033 CG LYS F 181-49.948 53. 932-12. 087 1.00 33.11 6034 CD LYS F 181-48. 608 54. 009-11. 374 1.00 36.86 6035 CE LYS F 181-48.785 54.454-9. 925 1.00 38.60 6036 NZ LYS F 181-47.480 54.608-9. 213 1.00 39. 92 1 2 3 4 5 6 7 8 9 10 6037 C LYS F 181-51. 862 54. 710-14. 126 1.00 25.98 6038 O LYS F 181-51.343 55.738-14. 552 1.00 24.77 6039 N GLU F 182-53. 048 54. 683-13. 527 1. 00 25. 48 6040 CA GLU F 182-53. 837 55. 890-13. 309 1.00 26.31 6041 CB GLU F 182-53. 173 56. 758-12. 237 1.00 29.45 6042 CG GLU F 182-53.171 56.128-10. 857 1.00 37.15 6043 CD GLU F 182-52. 399 56.951-9. 837 1.00 42. 45 6044 OBI GLU F 182-52.477 56.625-8. 633 1.00 45. 87 6045 OE2 GLU F 182-51.710 57. 918-10. 236 1.00 45.74 6046 C GLU F 182-54. 033 56. 705-14. 582 1.00 24.74 6047 O GLU F 182-53.801 57.912-14. 595 1.00 24.51 6048 N ASN F 183-54.458 56. 031-15. 645 1.00 22.03 6049 CA ASN F 183-54. 713 56. 659-16. 935 1.00 21.43 6050 CB ASN F 183-55. 738 57. 790-16. 782 1.00 22. 34 6051 CG ASN F 183-56.547 58. 013-18. 045 1.00 25.24 6052 OD1 ASN F 183-56.710 59.147-18. 509 1.00 27. 14 6053 ND2 ASN F 183-57.065 56. 923-18. 610 1.00 23.08 6054 C ASN F 183-53. 450 57. 208-17. 610 1.00 19.95 6055 O ASN F 183-53. 542 58.072-18. 483 1.00 18.72 6056 N LYS F 184-52.285 56. 702-17. 208 1.00 17.42 6057 CA LYS F 184-51.005 57. 127-17. 781 1.00 18.64 6058 CB LYS F 184-50.257 58. 037-16. 795 1.00 19.47 6059 CG LYS F 184-50. 934 59384-16. 546 1.00 22.33 6060 CD LYS F 184-50. 304 60. 123-15. 367 1.00 25. 51 6061 CE LYS F 184-50. 678 59. 459-14. 048 1.00 29.66 6062 NZ LYS F 184-50. 127 60. 190-12. 877 1.00 35.34 6063 C LYS F 184-50.129 55. 913-18. 106 1.00 19.21 6064 0 LYS F 184-50. 407 54. 801-17. 659 1.00 19. 55 6065 N ILE F 185-49.076 56. 124-18. 891 1. 00 17.94 6066 CA ILE F 185-48.165 55. 035-19. 229 1.00 18.67 6067 CB ILE F 185-47. 733 55.087-20. 712 1.00 17.92 6068 CG2 ILE F 185-46. 782 53.922-21. 019 1.00 18.68 6069 CG 1 ILE F 185-48. 970 54. 996-21. 616 1.00 18.24 1 2 3 4 5 6 7 8 9 10 6070 CD1 ILE F 185-48.663 55.096-23. 098 1.00 17.90 6071 C ILE F 185-46.923 55.136-18. 344 1.00 18. 91 6072 O ILE F 185-46.191 56.123-18. 402 1.00 20.60 6073 N LEU F 186-46.705 54. 114-17. 521 1.00 19.62 6074 CA LEU F 186-45. 565 54. 060-16. 606 1.00 21.20 6075 CB LEU F 186-45.967 53337-15314 1.00 22.99 6076 CG LEU F 186-44.876 53.075-14. 266 @ 00 25.36 6077 CD1 LEU F 186-44. 334 54.392-13. 741 1. 00 23.55 6078 CD2 LEU F 186-45. 452 52. 245-13. 119 1.00 25.43 6079 C LEU F 186-44. 365 53.347-17. 235 1.00 21.81 6080 O LEU F 186-44. 495 52. 249-17. 772 1.00 20.52 6081 N VAL F 187-43. 197 53.980-17. 162 1.00 20.46 6082 CA VAL F 187-41.972 53. 411-17. 714 1.00 19.66 6083 CB VAL F 187-41.017 54.535-18. 176 1.00 19.78 6084 CG1 VAL F 187-39.764 53. 941-18. 791 1.00 17. 88 6085 CG2 VAL F 187-41.739 55. 448-19. 178 1.00 17.25 6086 C VAL F 187-41.283 52. 556-16. 648 1.00 21.05 6087 O VAL F 187-40.964 53. 047-15. 563 1.00 20.79 6088 N LYS F 188-41.055 51. 282-16. 961 1.00 21.12 6089 CA LYS F 188-40.423 50. 354-16. 024 1.00 22.55 6090 CB LYS F 188-41.184 49.022-16. 010 1.00 22.03 6091 CG LYS F 188-42.659 49. 142-15. 642 1.00 25.12 6092 CD LYS F 188-42. 847 49. 635-14. 211 1.00 25.91 6093 CE LYS F 188-42.237 48. 663-13. 209 1.00 30.54 6094 NZ LYS F 188-42. 411 49.134-11. 801 1.00 35.02 6095 C LYS F 188-38.959 50. 086-16. 373 1.00 24.07 6096 O LYS F 188-38.213 49. 525-15. 571 1.00 25.09 6097 N GLU F 189-38.556 50. 480-17. 574 1.00 23.05 6098 CA GLU F 189-37. 189 50. 264-18. 028 1.00 24.08 6099 CB GLU F 189-37.127 49. 043-18. 959 1.00 24.80 6100 CG GLU F 189-37. 229 47. 692-18. 255 1.00 30.20 6101 CD GLU F 189-37395 46. 529-19. 231 1.00 32.04 6102 OBI GLU F 189-36.733 46. 535-20.291 1.00 33.21 1 2 3 4 5 6 7 8 9 10 6103 OE2 GLU F 189-38.181 45.604-18. 931 1.00 33.01 6104 C GLU F 189-36.661 51.487-18. 763 1.00 23.17 6105 O GLU F 189-37.316 52.008-19. 668 1.00 24.48 6106 N THR F 190-35. 473 51.938-18. 380 1. 00 22.37 6107 CA THR F 190-34.852 53.097-19. 014 1.00 21.36 6108 CB THR F 190-33. 595 53.540-18. 227 1.00 20.81 6109 OG1 THR F 190-34. 000 54.042-16. 948 1.00 21.40 6110 CG2 THR F 190-32.833 54.629-18. 979 1.00 20.86 6111 C THR F 190-34.460 52.775-20. 453 1.00 22.09 6112 O THR F 190-33.998 51.668-20. 746 1.00 23.65 6113 N GLY F 191-34.650 53.737-21. 353 1.00 20.50 6114 CA GLY F 191-34.295 53.510-22. 744 1.00 20.84 6115 C GLY F 191-34.911 54.494-23. 723 1.00 19.81 6116 O GLY F 191-35. 454 55.533-23. 332 1.00 19.76 6117 N TYR F 192-34.818 54.161-25. 004 1.00 17.94 6118 CA TYR F 192-35. 365 54.992-26. 071 1.00 19.16 6119 CB TYR F 192-34.401 55.000-27. 258 1.00 22.11 6120 CG TYR F 192-33.254 55.972-27. 083 1.00 25.68 6121 CD1 TYR F 192-33395 57.309-27. 447 1.00 26.93 6122 CE1 TYR F 192-32.359 58.219-27. 271 1.00 29.86 6123 CD2 TYR F 192-32.035 55.562-26. 533 1.00 28.31 6124 CE2 TYR F 192-30.983 56. 471-26. 350 1.00 28.90 6125 CZ TYR F 192-31.159 57.797-26. 723 1.00 30.61 6126 OH TYR F 192-30.150 58. 713-26. 540 1.00 32.56 6127 C TYR F 192-36.729 54.445-26. 496 1.00 19.20 6128 O TYR F 192-36.873 53.241-26. 700 1.00 17. 66 6129 N PHE F 193-37.719 55.331-26. 626 1.00 17. 38 6130 CA PHE F 193-39.078 54.925-26. 996 1.00 17.34 6131 CB PHE F 193-40.028 55.065-25. 795 1.00 16.61 6132 CG PHE F 193-39. 709 54.159-24. 646 1.00 17.56 6133 CD1 PHE F 193-38.632 54.425-23. 806 1.00 17.81 6134 CD2 PHE F 193-40. 490 53. 036-24. 399 1.00 16.77 6135 CE1 PHE F 193-38. 335 53.578-22. 735 1. 00 17. 78 1 2 3 4 5 6 7 8 9 10 6136 CE2 PHE F 193-40.202 52.183-23. 331 1.00 18.24 6137 CZ PHE F 193-39. 125 52.456-22. 496 1.00 18.80 6138 C PHE F 193-39. 717 55.710-28. 141 1.00 17.41 6139 O PHE F 193-39.548 56.929-28. 247 1.00 16.83 6140 N PHE F 194-40.460 55.005-28. 992 1. 00 14.46 6141 CA PHE F 194-41.206 55.661-30. 063 1.00 14.72 6142 CB PHE F 194-41.380 54.739-31. 274 1.00 15. 57 6143 CG PHE F 194-42. 297 55. 299-32. 337 1.00 18.91 6144 CD 1 PHE F 194-41. 920 56. 408-33. 086 1.00 20.24 6145 CD2 PHE F 194-43. 546 54.724-32. 575 1.00 19.61 6146 CE1 PHE F 194-42.765 56.936-34. 067 1.00 21.94 6147 CE2 PHE F 194-44. 398 55. 244-33. 554 1.00 20.97 6148 CZ PHE F 194-44. 007 56.355-34. 297 1.00 20.58 6149 C PHE F 194-42.567 55.902-29. 401 1.00 14. 57 6150 O PHE F 194-43.181 54.963-28. 896 1.00 16.02 6151 N ILE F 195-43. 035 57. 147-29. 400 1.00 14.48 6152 CA ILE F 195-44.301 57.486-28. 746 1.00 14.66 6153 CB ILE F 195-44. 049 58.437-27. 563 1.00 15.02 6154 CG2 ILE F 195-45. 339 58.656-26. 782 1.00 18.06 6155 CG1 ILE F 195-42.975 57. 847-26. 643 1.00 15. 33 6156 CD1 ILE F 195-42. 394 58.861-25. 656 1. 00 18. 07 6157 C ILE F 195-45.255 58.161-29. 730 1. 00 15. 02 6158 O ILE F 195-44.848 59.046-30. 483 1.00 13.61 6159 N TYR F 196-46.524 57.752-29. 705 1.00 15.13 6160 CA TYR F 196-47.523 58.298-30. 624 1.00 13. 13 6161 CB TYR F 196-47.674 57. 350-31.819 1.00 11.85 6162 CG TYR F 196-48.113 55.946-31. 437 1. 00 14.77 6163 CD1 TYR F 196-49. 461 55.580-31. 461 1.00 15.79 6164 CE1 TYR F 196-49.869 54.286-31. 098 1. 00 16. 41 6165 CD2 TYR F 196-47. 180 54.988-31. 038 1.00 15. 14 6166 CE2 TYR F 196-47. 577 53.691-30. 668 1.00 15.81 6167 CZ TYR F 196-48.923 53. 352-30. 703 1. 00 17.56 6168 OH TYR F 196-49. 323 52.079-30. 341 1. 00 19.82 1 2 3 4 5 6 7 8 9 10 6169 C TYR F 196-48.890 58.540-29. 978 1.00 14.17 6170 O TYR F 196-49.249 57.892-28. 989 1.00 15. 48 6171 N GLY F 197-49.647 59.479-30. 541 1.00 14.65 6172 CA GLY F 197-50.966 59. 787-30. 014 1.00 15.45 6173 C GLY F 197-51. 845 60.497-31. 032 1.00 17.77 6174 O GLY F 197-51. 357 61.312-31. 819 1.00 16.53 6175 N GLN F 198-53.141 60.183-31. 025 1. 00 16. 03 6176 CA GLN F 198-54. 091 60.810-31. 943 1.00 14.57 6177 CB GLN F 198-54. 344 59.899-33. 148 1.00 16. 34 6178 CG GLN F 198 -55.371 60.446-34. 131 1.00 15.72 6179 CD GLN F 198-55.569 59. 557 -35.338 1.00 18. 78 6180 OE1 GLN F 198-54.647 59.347-36. 122 1.00 21. 18 6181 NE2 GLN F 198-56.786 59. 034-35. 501 1.00 18.24 6182 C GLN F 198-55. 413 61.097-31. 228 1.00 14.95 6183 O GLN F 198-55.822 60. 348-30. 346 1.00 13. 36 6184 N VAL F 199-56.064 62.194-31. 601 1.00 15. 74 6185 CA VAL F 199 -57.349 62.576-31. 016 1.00 15. 60 6186 CB VAL F 199-57.186 63.678-29. 924 1.00 16.58 6187 CG1 VAL F 199-58.555 64.081-29. 367 1.00 17.10 6188 CG2 VAL F 199-56.286 63. 179-28.794 1.00 17.13 6189 C VAL F 199-58.230 63.149-32. 125 1.00 17.53 6190 O VAL F 199-57.729 63.830-33. 018 1. 00 16. 18 6191 N LEU F 200-59.531 62.854-32. 085 1.00 17.14 6192 CA LEU F 200-60.461 63.411-33. 069 1.00 18. 16 6193 CB LEU F 200-61. 471 62.362-33. 566 1.00 19. 10 6194 CG LEU F 200-62.680 62.928-34. 348 1.00 18. 98 6195 CD1 LEU F 200-62.198 63.868-35. 448 1.00 18.83 6196 CD2 LEU F 200-63.511 61. 784-34. 939 1.00 18.88 6197 C LEU F 200-61.207 64.544-32. 376 1.00 19. 35 6198 O LEU F 200-61.924 64.314-31. 399 1.00 16. 32 6199 N TYR F 201-61.022 65.766-32. 870 1.00 19.79 6200 CA TYR F 201-61.676 66.928-32. 283 1. 00 22.61 6201 CB TYR F 201-60.736 68.142-32. 314 1.00 24.00 1 2 3 4 5 6 7 8 9 10 6202 CG TYR F 201-59. 466 67.915-31. 520 1.00 25.41 6203 CD1 TYR F 201-58.315 67.415-32. 132 1.00 26.99 6204 CE1 TYR F 201-57.165 67.125-31. 385 1.00 23.62 6205 CD2 TYR F 201-59.441 68.127-30. 141 1.00 25.21 6206 CE2 TYR F 201-58.304 67. 840-29. 387 1.00 27.13 6207 CZ TYR F 201-57.170 67. 336-30. 017 1.00 24.33 6208 OH TYR F 201-56.062 67. 017-29. 264 1. 00 27.55 6209 C TYR F 201-62.981 67. 254-32. 997 1.00 24.18 6210 O TYR F 201-63.064 67. 194-34. 222 1.00 22.55 6211 N THR F 202-64.000 67. 582-32. 211 1.00 26.55 6212 CA THR F 202-65.319 67.919-32. 738 1.00 30.94 6213 CB THR F 202-66.329 66.792-32. 432 1.00 30. 38 6214 OG1 THR F 202-66.410 66.591-31. 015 1.00 29.13 6215 CG2 THR F 202-65.883 65. 483-33. 090 1.00 30.27 6216 C THR F 202-65.792 69.218-32. 085 1.00 34.02 6217 O THR F 202-66.983 69.417-31. 852 1.00 36.03 6218 N ASP F 203-64.832 70.094-31. 802 1.00 37. 30 6219 CA ASP F 203-65.072 71. 383-31. 157 1.00 40.10 6220 CB ASP F 203-63.986 71.608-30. 096 1.00 42.73 6221 CG ASP F 203-64.445 72.491-28. 955 1.00 44.01 6222 OD1 ASP F 203-64.902 73.622-29. 217 1.00 47.08 6223 OD2 ASP F 203-64. 335 72.052-27. 790 1.00 44.05 6224 C ASP F 203-65.020 72.499-32. 210 1.00 41.95 6225 O ASP F 203-64.245 72.423-33. 164 1.00 39.00 6226 N LYS F 204-65. 841 73.532-32. 034 1.00 44.60 6227 CA LYS F 204-65.879 74.649-32. 979 1.00 48.18 6228 CB LYS F 204-67.239 75. 354-32. 912 1.00 51.02 6229 CG LYS F 204-68.401 74. 531-33. 455 1.00 56. 14 6230 CD LYS F 204-69. 729 75.260-33. 279 1.00 59. 20 6231 CE LYS F 204-69.730 76. 603-33. 995 1.00 61.74 6232 NZ LYS F 204-70. 993 77.362-33. 764 1. 00 64. 32 6233 C LYS F 204-64. 766 75.677-32. 759 1.00 47.99 6234 O LYS F 204-64. 559 76. 557-33. 595 1. 00 48. 17 1 2 3 4 5 6 7 8 9 10 6235 N THR F 205-64.054 75.560-31. 638 1.00 48.84 6236 CA THR F 205-62.957 76.475-31. 307 1.00 50.12 6237 CB THR F 205-62. 183 75.995-30. 060 1.00 51. 58 6238 OG1 THR F 205-63.082 75.896-28. 949 1.00 52.90 6239 CG2 THR F 205-61.063 76.975-29. 716 1.00 52.29 6240 C THR F 205-61.971 76.600-32. 467 1.00 49. 11 6241 O THR F 205-61.538 75.595-33. 036 1.00 48.81 6242 N TYR F 206-61.608 77.837-32. 794 1.00 47.49 6243 CA TYR F 206-60.700 78. 120-33. 903 1.00 47.00 6244 CB TYR F 206-60.227 79.582-33. 836 1.00 51. 40 6245 CG TYR F 206-59.135 79.863-32. 827 1.00 55. 70 6246 CD1 TYR F 206-57.789 79.733-33. 171 1.00 57.00 6247 CE1 TYR F 206-56.780 80.004-32. 249 1.00 60. 25 6248 CD2 TYR F 206-59. 447 80.268-31. 530 1.00 58. 48 6249 CE2 TYR F 206-58.446 80.540-30. 598 1.00 60.61 6250 CZ TYR F 206-57. 115 80.407-30. 966 1.00 61.56 6251 OH TYR F 206-56.121 80. 684-30. 054 1.00 62.97 6252 C TYR F 206-59.496 77.182-34. 032 1.00 42. 89 6253 O TYR F 206-59.001 76.973-35. 141 1.00 41. 94 6254 N ALA F 207-59.029 76.622-32. 914 1.00 38.42 6255 CA ALA F 207-57. 889 75.698-32. 936 1.00 34.20 6256 CB ALA F 207-56.577 76.482-32. 980 1.00 35. 01 6257 C ALA F 207-57.887 74. 740-31. 742 1. 00 31.35 6258 O ALA F 207-58.060 75.159-30. 600 1.00 30.71 6259 N MET F 208-57.681 73.456-32. 023 1.00 28.46 6260 CA MET F 208-57. 659 72.411-30. 998 1.00 27.62 6261 CB MET F 208-58.907 71.529-31. 131 1.00 28.36 6262 CG MET F 208-60.230 72. 257-30. 947 1.00 30.46 6263 SD MET F 208-60.453 72.803-29. 253 1.00 34. 47 6264 CE MET F 208-60. 776 71.253-28. 435 1.00 34.60 6265 C MET F 208-56.418 71.521-31. 156 1.00 25.57 6266 O MET F 208-55. 936 71. 320-32. 269 1.00 24.23 6267 N GLY F 209-55.921 70. 974-30. 050 1.00 24. 50 1 2 3 4 5 6 7 8 9 10 6268 CA GLY F 209-54.761 70. 099-30. 130 1.00 23. 94 6269 C GLY F 209-54.463 69. 378-28. 832 1.00 23.09 6270 O GLY F 209-55.131 69.606-27. 822 1.00 23.61 6271 N HIS F 210-53. 471 68.492-28. 849 1.00 20.04 6272 CA HIS F 210-53. 104 67.777-27. 636 1.00 18. 66 6273 CB HIS F 210-53.659 66.342-27. 637 1.00 18.55 6274 CG HIS F 210-53. 216 65.508-28. 799 1.00 18. 35 6275 CD2 HIS F 210-52.249 64.565-28. 900 1. 00 17.55 6276 ND1 HIS F 210-53.809 65.583-30. 041 1.00 20.02 6277 CE1 HIS F 210-53. 227 64.721-30. 855 1.00 18.69 6278 NE2 HIS F 210-52.278 64. 090-30. 187 1.00 17.83 6279 HIS F 210-51.595 67.758-27. 434 1.00 19.01 6280 O HIS F 210-50.830 68.007-28. 368 1. 00 16.53 6281 N LEU F 211-51. 190 67.468-26. 201 1.00 16. 88 6282 CA LEU F 211-49.791 67. 422-25. 803 1.00 19.05 6283 CB LEU F 211-49. 530 68.431-24. 674 1.00 20.23 6284 CG LEU F 211-49.756 69.935-24. 872 1.00 26.52 6285 CD1 LEU F 211-51.121 70. 177-25.454 1.00 30.36 6286 CD2 LEU F 211-49.631 70.661-23. 535 1.00 26. 60 6287 C LEU F 211-49.423 66.041-25. 278 1.00 18.47 6288 O LEU F 211-50.123 65.495-24. 427 1.00 17.81 6289 N ILE F 212-48.337 65.472-25. 795 1. 00 17.03 6290 CA ILE F 212-47. 849 64.186-25. 302 1.00 15.78 6291 CB ILE F 212-47.233 63.329-26. 425 1.00 18.86 6292 CG2 ILE F 212-46.489 62.140-25. 817 1.00 18. 59 6293 CGl ILE F 212-48.341 62.867-27. 378 1. 00 20. 51 6294 CD1 ILE F 212-47.847 62.141-28. 611 1.00 23.95 6295 C ILE F 212-46.778 64. 642-24.323 1.00 17. 88 6296 O ILE F 212-45. 754 65.216-24. 720 1. 00 15. 72 6297 N GLN F 213-47. 021 64.401-23. 040 1.00 16.99 6298 CA GLN F 213-46.120 64.877-22. 008 1. 00 16.62 6299 CB GLN F 213-46.890 65.823-21. 075 1.00 17.12 6300 CG GLN F 213-47. 674 66. 896-21.823 1.00 15.68 1 2 3 4 5 6 7 8 9 10 6301 CD GLN F 213-48.386 67.856-20. 896 1.00 20.57 6302 OE1 GLN F 213-49.255 67.457-20. 116 1.00 18. 96 6303 NE2 GLN F 213-48. 021 69.136-20. 973 1.00 19.13 6304 C GLN F 213-45.427 63.815-21. 187 1.00 17.87 6305 O GLN F 213-45. 937 62.705-21. 011 1.00 16.91 6306 N ARG F 214-44.254 64.187-20. 682 1.00 16.67 6307 CA ARG F 214-43. 434 63. 318-19. 851 1.00 18.07 6308 CB ARG F 214-42.010 63.229-20. 425 1.00 20.34 6309 CG ARG F 214-41. 005 62.482-19. 540 1.00 18.37 6310 CD ARG F 214-39.552 62.772-19. 961 1.00 21.19 6311 NE ARG F 214-38.586 61.969-19. 208 1.00 22.06 6312 CZ ARG F 214-37.273 62.193-19. 174 1.00 22.71 6313 NH1 ARG F 214-36. 744 63.204-19. 848 1.00 21.19 6314 NH2 ARG F 214-36.484 61.391-18. 470 1.00 22.95 6315 C ARG F 214-43.358 63.894-18. 442 1.00 19.63 6316 O ARG F 214-42.948 65.045-18. 255 1.00 17.95 6317 N LYS F 215-43.780 63.103-17. 459 1.00 19.27 6318 CA LYS F 215-43.701 63.508-16. 063 1.00 21.20 6319 CB LYS F 215-44.899 62.980-15. 265 1.00 24.33 6320 CG LYS F 215-44.834 63.326-13. 779 1.00 30.07 6321 CD LYS F 215-46.138 63.015-13. 047 1.00 36.24 6322 CE LYS F 215-47.278 63.909-13. 529 1.00 38.01 6323 NZ LYS F 215-48.489 63.767-12. 679 1.00 42.00 6324 C LYS F 215-42.405 62.872-15. 560 1.00 20.74 6325 O LYS F 215-42.336 61.657-15. 358 1.00 20.11 6326 N LYS F 216-41.375 63. 696-15. 393 1.00 19.64 6327 CA LYS F 216-40.064 63.233-14. 948 1.00 19.76 6328 CB LYS F 216-39. 054 64.383-15. 030 1.00 20.02 6329 CG LYS F 216-38.894 64.951-16. 435 1.00 21. 50 6330 CD LYS F 216-37. 909 66.103-16. 461 1.00 27.76 6331 CE LYS F 216-36.556 65.648-15. 938 1.00 29.92 6332 NZ LYS F 216-35.463 66. 560-16. 312 1.00 32.78 6333 C LYS F 216-40. 095 62.681-13. 527 1. 00 20. 17 1 2 3 4 5 6 7 8 9 10 6334 O LYS F 216-40. 534 63. 362-12. 599 1.00 18. 91 6335 N VAL F 217-37.851 59. 577-12. 724 1.00 35. 33 6336 CA VAL F 217-38. 722 60.563-12. 084 1.00 33.48 6337 CB VAL F 217-39.699 59.839-11. 120 1.00 36.34 6338 CG1 VAL F 217-38.916 59. 032-10. 092 1. 00 36.14 6339 CG2 VAL F 217-40.636 60. 845-10. 451 1.00 41.27 6340 C VAL F 217-37.855 61.594-11. 333 1.00 30.17 6341 O VAL F 217-38.076 61. 883-10. 156 1.00 27. 30 6342 N HIS F 218-36.884 62. 165-12. 042 1.00 26.59 6343 CA HIS F 218-35. 945 63.116-11. 445 1.00 25.59 6344 CB HIS F 218-34. 532 62. 538-11. 541 1.00 27.06 6345 CG HIS F 218-34. 417 61. 133-11. 040 1.00 27.90 6346 CD2 HIS F 218-34.931 60. 527-9. 943 1.00 29.11 6347 ND 1 HIS F 218-33. 675 60. 173-11. 690 1.00 29.96 6348 CE1 HIS F 218-33. 734 59.037-11. 020 1.00 29.53 6349 NE2 HIS F 218-34.489 59. 225-9. 954 1.00 28.96 6350 C HIS F 218-35. 946 64. 514-12. 068 1.00 24.92 6351 O HIS F 218-36.123 64. 669-13. 275 1.00 21.78 6352 N VAL F 219-35. 724 65. 527-11. 233 1.00 24.24 6353 CA VAL F 219-35. 684 66. 917-11. 684 1.00 23.44 6354 CB VAL F 219-37.016 67.647-11. 367 1.00 25.03 6355 CG1 VAL F 219-38.158 67.002-12. 135 1.00 29.93 6356 CG2 VAL F 219-37. 305 67.585-9. 884 1.00 26.13 6357 C VAL F 219-34. 530 67. 650-10. 995 1.00 22.90 6358 O. VAL F 219-34.261 67.421-9. 818 1.00 20.80 6359 N PHE F 220-33.849 68.525-11. 732 1.00 21. 89 6360 CA PHE F 220-32. 722 69. 277-11. 181 1.00 22.03 6361 CB PHE F 220-31.387 68.731-11. 701 1.00 20.29 6362 CG PHE F 220-31.135 67. 288-11. 365 1.00 21.08 6363 CD1 PHE F 220-31.740 66. 273-12. 098 1.00 21.29 6364 CD2 PHE F 220-30.286 66. 943-10. 318 1.00 18.74 6365 CE1 PHE F 220-31.504 64.931-11. 797 1.00 20.51 6366 CE2 PHE F 220-30.041 65. 606-10. 007 1.00 20. 22 1 2 3 4 5 6 7 8 9 10 6367 CZ PHE F 220-30.652 64.595-10. 749 1.00 20.78 6368 C PHE F 220-32.787 70.759-11. 539 1.00 23.51 6369 O PHE F 220-33.338 71.140-12. 573 1. 00 22.82 6370 N GLY F 221-32.200 71.582-10. 675 1.00 24.03 6371 CA GLY F 221-32.153 73.014-10. 900 1.00 23.77 6372 C GLY F 221-33. 447 73.655-11. 352 1.00 25.33 6373 O GLY F 221-34. 487 73.500-10. 705 1. 00 25. 08 6374 N ASP F 222-33.384 74.384-12. 463 1.00 23.88 6375 CA ASP F 222-34.562 75.067-12. 979 1.00 24.62 6376 CB ASP F 222-34.172 76.470-13. 483 1.00 25.57 6377 CG ASP F 222-33.273 76.436-14. 714 1.00 26.80 6378 OD1 ASP F 222-32.620 75.401-14. 962 1.00 27.50 6379 OD2 ASP F 222-33.210 77.461-15. 429 1.00 29.04 6380 C ASP F 222-35.320 74.286-14. 060 1.00 24.40 6381 O ASP F 222-36.098 74.866-14. 818 1.00 25.23 6382 N GLU F 223-35. 099 72.974-14. 125 1.00 23.89 6383 CA GLU F 223-35.802 72.124-15. 097 1.00 24.00 6384 CB GLU F 223-35. 305 70.673-15. 043 1.00 24.43 6385 CG GLU F 223-33.877 70. 387-15. 478 1. 00 25.70 6386 CD GLU F 223-33.556 68.890-15. 409 1.00 26.80 6387 OBI GLU F 223-34.125 68.192-14. 540 1.00 24.92 6388 OE2 GLU F 223-32.729 68.410-16. 214 1.00 28.88 6389 C GLU F 223-37.283 72.079-14. 729 1.00 24.08 6390 O GLU F 223-37.642 72.233-13. 565 1.00 23.52 6391 N LEU F 224-38.144 71. 858-15. 715 1.00 25.71 6392 CA LEU F 224-39. 572 71.720-15. 436 1.00 25.08 6393 CB LEU F 224-40.416 72.163-16. 633 1.00 29.37 6394 CG LEU F 224-40.423 73.640-17. 021 1.00 33.49 6395 CD1 LEU F 224-41 : 486 73.869-18. 087 1.00 36. 43 6396 CD2 LEU F 224-40.719 74.493-15. 802 1.00 36.55 6397 C LEU F 224-39. 768 70. 225-15. 208 1.00 23.96 6398 O LEU F 224-39.105 69.415-15. 859 1.00 20.69 6399 N SER F 225-40.659 69. 850-14. 293 1. 00 22. 10 1 2 3 4 5 6 7 8 9 10 6400 CA SER F 225-40.898 68.430-14. 031 1.00 24.01 6401 CB SER F 225-41.508 68.230-12. 637 1.00 26.23 6402 OG SER F 225-42. 779 68.849-12. 545 1.00 33.43 6403 C SER F 225-41.818 67.821-15. 095 1.00 23.41 6404 O SER F 225-41.827 66.608-15. 294 1.00 22.86 6405 N LEU F 226-42.584 68.669-15. 776 1.00 21.01 6406 CA LEU F 226-43. 490 68. 209-16. 829 1.00 22.71 6407 CB LEU F 226-44. 918 68.704-16. 571 1.00 23.09 6408 CG LEU F 226-46.002 68.218-17. 543 1.00 24.08 6409 CD1 LEU F 226-46.195 66.710-17. 401 1.00 23.27 6410 CD2 LEU F 226-47.310 68.943-17. 244 1.00 25.35 6411 C LEU F 226-42.998 68.733-18. 175 1.00 21.03 6412 O LEU F 226-43. 000 69.940-18. 432 1.00 24.17 6413 N VAL F 227-42.572 67.813-19. 030 1.00 20.00 6414 CA VAL F 227-42.049 68. 161-20. 346 1.00 20.65 6415 CB VAL F 227-40. 707 67.413-20. 618 1.00 22.04 6416 CG1 VAL F 227-40.200 67.722-22. 031 1.00 22.69 6417 CG2 VAL F 227-39.671 67.803-19. 571 1.00 21.53 6418 C VAL F 227-43. 010 67.788-21. 466 1. 00 19. 99 6419 O VAL F 227-43.510 66.665-21. 510 1.00 19. 72 6420 N THR F 228-43.277 68.731-22. 363 1.00 17.71 6421 CA THR F 228-44.128 68.444-23. 510 1.00 17.88 6422 CB THR F 228-44.873 69.694-24. 021 1.00 18.10 6423 OG1 THR F 228-45. 795 70.144-23. 017 1.00 19.79 6424 CG2 THR F 228-45.648 69.361-25. 300 1.00 19.41 6425 C THR F 228-43.171 67.964-24. 598 1.00 17.78 6426 O THR F 228-42. 368 68.742-25. 112 1. 00 14. 98 6427 N LEU F 229-43.255 66.681-24. 930 1.00 16.16 6428 CA LEU F 229-42. 387 66.087-25. 935 1.00 15.95 6429 CB LEU F 229-42.357 64.566-25. 760 1.00 17.29 6430 CG LEU F 229-41.801 64.077-24. 423 1.00 18.61 6431 CD1 LEU F 229-42.059 62.583-24. 272 1.00 17. 41 6432 CD2 LEU F 229-40.301 64. 385-24. 359 1.00 19. 06 1 2 3 4 5 6 7 8 9 10 6433 C LEU F 229-42.808 66.427-27. 355 1. 00 17.70 6434 O LEU F 229-42.000 66.917-28. 147 1.00 16.77 6435 N PHE F 230-44.071 66.155-27. 677 1.00 14.92 6436 CA PHE F 230-44.609 66.417-29. 003 1.00 16.47 6437 CB PHE F 230-44.654 65.117-29. 826 1.00 16.99 6438 CG PHE F 230-43.412 64.262-29. 691 1.00 19.47 6439 CD1 PHE F 230-43.412 63.131-28. 876 1.00 20.28 6440 CD2 PHE F 230-42.225 64.631-30. 324 1.00 20.35 6441 CE1 PHE F 230-42.246 62.381-28. 690 1.00 21.59 6442 CE2 PHE F 230-41.048 63.885-30. 143 1.00 20.81 6443 CZ PHE F 230-41.063 62.763-29. 322 1.00 20.58 6444 C PHE F 230-46.023 66.976-28. 850 1.00 17.46 6445 O PHE F 230-46.733 66.615-27. 915 1.00 15. 51 6446 N ARG F 231-46.419 67.866-29. 753 1.00 16.81 6447 CA ARG F 231-47.764 68.437-29. 705 1.00 19.77 6448 CB ARG F 231-47.734 69.864-29. 149 1.00 23.47 6449 CG ARG F 231-46.783 70.784-29. 865 1.00 30.47 6450 CD ARG F 231-46.741 72.175-29. 225 1.00 35.40 6451 NE ARG F 231-47.755 73.055-29. 774 1.00 39.75 6452 CZ ARG F 231-47.543 74.338-30. 018 1.00 39.60 6453 NH1 ARG F 231-46.374 74.897-29. 767 1.00 40. 28 6454 NH2 ARG F 231-48.513 75.060-30. 526 1.00 45.14 6455 C ARG F 231 -48.359 68.436 -31.099 1.00 19.61 6456 O ARG F 231 -47.643 68.418 -31.105 1.00 18.82 6457 N CYS F 232-49.682 68.476-31. 142 1.00 17.27 6458 CA CYS F 232-50.437 68. 432-32. 388 1.00 20.52 6459 C CYS F 232-51.444 69.580-32. 336 1.00 19.48 6460 O CYS F 232-51.965 69.876-31. 268 1.00 18.73 6461 CB CYS F 232-51.184 67.077-32. 460 1.00 23.18 6462 SG CYS F 232-51.616 66.561-34. 139 1.00 33.81 6463 N ILE F 233-51.725 70.228-33. 464 1.00 17. 85 6464 CA ILE F 233-52.726 71. 304-33. 455 1.00 20.17 6465 CB ILE F 233-52.118 72.673-33. 042 1. 00 22. 76 1 2 3 4 5 6 7 8 9 10 6466 CG2 ILE F 233-51.147 73.166-34. 105 1.00 21.59 6467 CG 1 ILE F 233-53.242 73.697-32. 843 1.00 22.31 6468 CD 1 ILE F 233-52. 793 74.989-32. 178 1.00 25.69 6469 C ILE F 233-53. 450 71. 447-34. 790 1.00 19.23 6470 O ILE F 233-52.843 71.318-35. 849 1.00 19.00 6471 N GLN F 234-54. 759 71.699-34. 727 1.00 20.76 6472 CA GLN F 234-55.582 71.840-35. 927 1.00 21. 65 6473 CB GLN F 234-56.369 70.548-36. 183 1.00 22.95 6474 CG GLN F 234-55.532 69.327-36. 534 1.00 24.47 6475 CD GLN F 234-55.173 69. 277-38. 006 1.00 25.73 6476 OEIL GLN F 234-56.031 69.033-38. 856 1.00 24.01 6477 NE2 GLN F 234-53. 897 69.514-38. 317 1. 00 23. 49 6478 C GLN F 234-56.598 72.979-35. 818 1. 00 22. 71 6479 O GLN F 234-57.254 73.130-34. 787 1.00 21.36 6480 N ASN F 235-56.725 73.776-36. 879 1.00 23.21 6481 CA ASN F 235-57.729 74.838-36. 899 1.00 24.17 6482 CB ASN F 235-57.502 75.811-38. 067 1.00 22.45 6483 CG ASN F 235-56.448 76.864-37. 767 1.00 22.31 6484 OD1 ASN F 235-56.561 77.626-36. 805 1.00 25.11 6485 ND2 ASN F 235-55.424 76.917-38. 600 1.00 17.62 6486 C ASN F 235-59. 055 74.097-37. 124 1.00 24.06 6487 O ASN F 235-59. 093 73.108-37. 861 1.00 22.14 6488 N MET F 236-60.128 74.571-36. 496 1.00 24.61 6489 CA MET F 236-61.447 73.942-36. 634 1.00 25.75 6490 CB MET F 236-62.014 73.585-35. 256 1.00 25. 36 6491 CG MET F 236-61.080 72. 794-34. 350 1. 00 24.13 6492 SD MET F 236-60.620 71.191-35. 041 1.00 24.81 6493 CE MET F 236-62.250 70.391-35. 123 1.00 23.24 6494 C MET F 236-62.425 74. 896-37. 330 1.00 28.48 6495 O MET F 236-62.413 76.105-37. 069 1.00 27.63 6496 N PRO F 237-63.294 74.364-38. 214 1.00 30.22 6497 CD PRO F 237-63. 435 72.955-38. 624 1.00 29.12 6498 CA PRO F 237-64. 265 75.206-38. 922 1.00 32. 62 1 2 3 4 5 6 7 8 9 10 6499 CB PRO F 237-64. 692 74. 325-40. 085 1.00 31. 05 6500 CG PRO F 237-64.730 72.971-39. 431 1.00 31.87 6501 C PRO F 237-65.439 75.569-38. 022 1.00 36. 09 6502 O PRO F 237-65. 531 75.110-36. 882 1.00 35.54 6503 N GLU F 238-66.340 76. 390-38. 545 1.00 39.92 6504 CA GLU F 238-67.505 76.818-37. 788 1.00 43.88 6505 CB GLU F 238-68.012 78.150-38. 345 1.00 48. 06 6506 CG GLU F 238-66.983 79.274-38. 254 1.00 53.93 6507 CD GLU F 238-67.309 80.451-39. 159 1.00 57.29 6508 OE1 GLU F 238-66.562 81.456-39. 124 1.00 59.39 6509 OE2 GLU F 238-68.306 80.372-39. 910 1.00 60.34 6510 C GLU F 238-68.616 75.772-37. 834 1.00 43.62 6511 O GLU F 238-69. 374 75.623-36. 876 1.00 44.71 6512 N THR F 239-68.690 75.034-38. 938 1.00 42.71 6513 CA THR F 239-69.724 74.017-39. 115 1.00 42.49 6514 CB THR F 239-70. 499 74. 246-40. 435 1. 00 43. 04 6515 OG1 THR F 239-70. 973 75.597-40. 487 1.00 45.61 6516 CG2 THR F 239-71.689 73. 302-40. 527 1.00 45. 18 6517 C THR F 239-69. 192 72.584-39. 129 1.00 40. 49 6518 O THR F 239-68.180 72. 292-39. 770 1.00 39.97 6519 N LEU F 240-69.897 71.699-38. 429 1.00 38.33 6520 CA LEU F 240-69.544 70.283-38. 347 1.00 37.08 6521 CB LEU F 240-70.078 69. 542-39. 577 1.00 37. 32 6522 CG LEU F 240 -71.540 69.074 -39.536 1.00 40.52 6523 CD1 LEU F 240 -72.450 70.209 -39.123 1.00 41.09 6524 CD2 LEU F 240-71.933 68.535-40. 902 1.00 40.32 6525 C LEU F 240-68.048 70. 007-38. 196 1.00 35.25 6526 O LEU F 240-67.429 69.399-39. 071 1.00 34.27 6527 N PRO F 241-67. 452 70. 439-37. 073 1.00 34. 39 6528 CD PRO F 241-68.084 71. 141-35. 945 1.00 33.53 6529 CA PRO F 241-66.020 70.227-36. 822 1.00 33.75 6530 CB PRO F 241-65.797 70. 911-35. 471 1.00 33.16 6531 CG PRO F 241-66.930 71. 905-35. 375 1.00 35.81 1 2 3 4 5 6 7 8 9 10 6532 C PRO F 241-65.704 68. 728-36. 755 1.00 32.10 6533 O PRO F 241-66.425 67.965-36. 112 1.00 30.40 6534 N ASN F 242-64. 630 68.308-37. 414 1.00 30. 60 6535 CA ASN F 242-64.245 66. 899-37. 407 1.00 30.03 6536 CB ASN F 242-65.230 66.078-38. 252 1.00 34.25 6537 CG ASN F 242-65.823 64.907-37. 485 1.00 38.01 6538 OD1 ASN F 242-66.598 65.092-36. 548 1.00 42.79 6539 ND2 ASN F 242-65.453 63.697-37. 876 1.00 40.25 6540 C ASN F 242-62.834 66. 714-37. 957 1.00 25.82 6541 O ASN F 242-62.668 66.269-39. 085 1.00 26.20 6542 N ASN F 243-61.826 67.061-37. 159 1.00 23. 28 6543 CA ASN F 243-60.423 66. 933-37. 570 1.00 21.13 6544 CB ASN F 243-59.716 68. 302-37. 560 1.00 21.58 6545 CG ASN F 243-60.056 69.166-38. 765 1.00 21.39 6546 OD1 ASN F 243-60.054 68.698-39. 902 1.00 23.55 6547 ND2 ASN F 243-60.317 70.450-38. 520 1.00 20.44 6548 C ASN F 243-59.648 66.023-36. 619 1.00 19.46 6549 O ASN F 243-59.625 66.275-35. 416 1.00 20.04 6550 N SER F 244-59.021 64.966-37. 131 1.00 17.65 6551 CA SER F 244-58.216 64.130-36. 245 1.00 18.26 6552 CB SER F 244-58.181 62.663-36. 704 1.00 16.74 6553 OG SER F 244-57.587 62. 505-37. 979 1.00 18. 04 6554 C SER F 244-56.812 64.736-36. 287 1.00 19. 14 6555 O SER F 244-56.439 65. 359-37. 279 1.00 19.66 6556 N CYS F 245-56.054 64.576-35. 207 1.00 20.79 6557 CA CYS F 245-54.698 65.124-35. 122 1.00 21.97 6558 C CYS F 245-53. 747 64.045-34. 611 1.00 20.04 6559 O CYS F 245-53.956 63.503-33. 531 1.00 20. 94 6560 CB CYS F 245-54. 670 66. 318-34. 154 1.00 25. 86 6561 SG CYS F 245-53. 360 67.525-34. 531 1.00 33.29 6562 N TYR F 246-52.709 63.741-35. 387 1.00 18.77 6563 CA TYR F 246-51.725 62.719-35. 016 1.00 17.06 6564 CB TYR F 246-51.723 61.586-36. 060 1.00 15.47 123 4 5 6 7 8 9 10 6565 CG TYR F 246-50.673 60.494-35. 857 1.00 15. 97 6566 CD1 TYR F 246-49.320 60.705-36. 182 1.00 14.27 6567 CE1 TYR F 246-48. 362 59. 692-36.002 1.00 11. 88 6568 CD2 TYR F 246-51.033 59. 246-35. 346 1.00 14.32 6569 CE2 TYR F 246-50. 087 58.233-35. 158 1. 00 14. 12 6570 CZ TYR F 246-48.756 58.460-35. 488 1.00 15.03 6571 OH TYR F 246-47.838 57. 449-35. 307 1.00 13.61 6572 C TYR F 246-50.314 63.297-34. 916 1.00 17.66 6573 O TYR F 246-49. 928 64. 166-35. 707 1.00 15.73 6574 N SER F 247-49. 551 62. 800-33. 946 1.00 17.37 6575 CA SER F 247-48.158 63. 208-33. 779 1.00 18.10 6576 CB SER F 247-48.037 64.490-32. 948 1.00 20. 50 6577 OG SER F 247-46.712 65. 005-33. 050 1.00 20.83 6578 C SER F 247-47. 398 62.078-33. 102 1.00 16.82 6579 O SER F 247-47. 966 61. 319-32. 310 1.00 13. 37 6580 N ALA F 248-46.117 61.954-33. 432 1.00 15.64 6581 CA ALA F 248-45.277 60. 906-32. 860 1.00 14. 09 6582 CB ALA F 248-45. 515 59. 584-33. 597 1.00 13.10 6583 C ALA F 248-43.806 61.288-32. 954 1.00 15.02 6584 O ALA F 248-43.418 62. 096-33. 797 1.00 15.06 6585 N GLY F 249-42.996 60.699-32. 084 1.00 15.82 6586 CA GLY F 249-41.572 60.982-32. 090 1.00 17.64 6587 C GLY F 249-40.822 60.025-31. 186 1.00 16.58 6588 O GLY F 249-41.414 59.104-30. 619 1. 00 17.85 6589 N ILE F 250-39.520 60.247-31. 040 1.00 15.41 6590 CA ILE F 250-38.695 59. 393-30. 197 1.00 14.60 6591 CB ILE F 250-37.484 58.834-30. 983 1.00 15.87 6592 CG2 ILE F 250-36.594 57. 995-30. 057 1.00 14.83 6593 CG1 ILE F 250-37. 979 57.984-32. 159 1.00 16.47 6594 CD1 ILE F 250-36.858 57.455-33. 056 1.00 19.17 6595 C ILE F 250-38.185 60. 175-28. 993 1.00 15.62 6596 O ILE F 250-37.796 61.336-29. 121 1.00 15.34 6597 N ALA F 251-38. 196 59. 542-27. 823 1. 00 15.37 1 2 3 4 5 6 7 8 9 10 6598 CA ALA F 251-37.719 60.201-26. 611 1.00 17. 54 6599 CB ALA F 251-38.899 60.792-25. 830 1.00 19.20 6600 C ALA F 251-36.942 59.247-25. 719 1.00 17.45 6601 O ALA F 251-37.135 58.032-25. 768 1.00 16. 94 6602 N LYS F 252-36.053 59. 811-24. 908 1.00 19.06 6603 CA LYS F 252-35.259 59.032-23. 965 1.00 19.52 6604 CB LYS F 252-33.858 59.645-23. 808 1.00 20.24 6605 CG LYS F 252-33.015 59.019-22. 699 1.00 23.73 6606 CD LYS F 252-32.746 57.542-22. 960 1.00 26.36 6607 CE LYS F 252-32.011 56.888-21. 791 1.00 28.97 6608 NZ LYS F 252-30.649 57.452-21. 571 1.00 29.02 6609 C LYS F 252-36.020 59.118-22. 649 1.00 19.59 6610 O LYS F 252-36.224 60.214-22. 118 1.00 23.20 6611 N LEU F 253-36.447 57.971-22. 129 1.00 17.43 6612 CA LEU F 253-37.216 57.930-20. 891 1.00 19.84 6613 CB LEU F 253-38.582 57.282-21. 143 1.00 19.67 6614 CG LEU F 253-39.423 57.936-22. 245 1.00 20.03 6615 CD1 LEU F 253-40. 707 57. 128-22. 450 1.00 20.86 6616 CD2 LEU F 253-39.738 59.390-21. 870 1.00 19.39 6617 C LEU F 253-36.497 57.181-19. 781 1.00 19.22 6618 O LEU F 253-35. 711 56.276-20. 035 1.00 18.08 6619 N GLU F 254-36.797 57.559-18. 545 1.00 19.07 6620 CA GLU F 254-36.167 56.952-17. 384 1.00 22.10 6621 CB GLU F 254-35.591 58. 056-16. 488 1.00 22.93 6622 CG GLU F 254-35. 009 57.570-15. 175 1.00 31.12 6623 CD GLU F 254-33.586 57.063-15. 313 1.00 35.63 6624 OE1 GLU F 254-33.072 56.474-14. 341 1.00 39.32 6625 GLU F 254-32.977 57. 263-16. 389 1.00 37.42 6626 C GLU F 254-37.153 56.098-16. 587 1.00 21. 58 6627 O GLU F 254-38.326 56.439-16. 472 1.00 22.15 6628 N GLU F 255-36.674 54. 986-16. 041 1.00 21.99 6629 CA GLU F 255-37. 526 54.120-15. 232 1.00 22.69 6630 CB GLU F 255-36. 688 53.028-14. 567 1. 00 26. 06 1 2 3 4 5 6 7 8 9 10 6631 CG GLU F 255-37.520 51.990-13. 825 1.00 33. 35 6632 CD GLU F 255-36.671 50.981-13. 072 1.00 37.78 6633 OE1 GLU F 255-35.628 50. 556-13. 616 1.00 38.62 6634 OE2 GLU F 255-37.058 50.602-11. 942 1.00 40.26 6635 C GLU F 255-38.175 55.000-14. 156 1.00 23. 39 6636 O GLU F 255-37. 480 55.730-13. 442 1.00 21.77 6637 N GLY F 256-39.502 54.941-14. 048 1.00 21.80 6638 CA GLY F 256-40.201 55.764-13. 071 1.00 20.56 6639 C GLY F 256-40.965 56.915-13. 712 1.00 21.91 6640 O GLY F 256-41. 889 57.470-13. 111 1.00 23.73 6641 N ASP F 257-40.572 57.291-14. 927 1.00 20. 79 6642 CA ASP F 257-41.244 58.370-15. 659 1.00 20.36 6643 CB ASP F 257-40.514 58.682-16. 972 1.00 21.55 6644 CG ASP F 257-39.239 59.494-16. 785 1.00 24.32 6645 OD1 ASP F 257-38.531 59.683-17. 800 1.00 25.03 6646 OD2 ASP F 257-38.940 59.952-15. 660 1.00 23. 49 6647 C ASP F 257-42.654 57.911-16. 034 1.00 21.27 6648 O ASP F 257-42.923 56. 713-16.092 1.00 20.45 6649 N GLU F 258-43. 545 58.864-16. 294 1.00 20. 32 6650 CA GLU F 258-44. 905 58.551-16. 722 1.00 21.41 6651 CB GLU F 258-45.928 58.841-15. 617 1.00 24.03 6652 CG GLU F 258-45. 722 58.029-14. 354 1.00 30.02 6653 CD GLU F 258-46.901 58.115-13. 408 1.00 33. 98 6654 OE1 GLU F 258-47.388 59.237-13. 158 1.00 35.67 6655 OE2 GLU F 258-47. 335 57.055-12. 908 1.00 38.31 6656 C GLU F 258-45.228 59.415-17. 935 1.00 21.42 6657 O GLU F 258-44.760 60.553-18. 036 1.00 22.90 6658 N LEU F 259-46.014 58.872-18. 858 1.00 18.60 6659 CA LEU F 259-46.414 59.607-20. 054 1.00 17.95 6660 CB LEU F 259-46.075 58.809-21. 317 1.00 19.02 6661 CG LEU F 259-44.625 58. 385-21. 553 1.00 19.60 6662 CD1 LEU F 259-44.569 57.506-22. 790 1.00 20.42 6663 CD2 LEU F 259-43.728 59.618-21. 718 1.00 20. 02 1 2 3 4 5 6 7 8 9 10 6664 C LEU F 259-47.924 59. 844-20. 014 1.00 18.67 6665 O LEU F 259-48. 684 58.966-19. 594 1.00 18.40 6666 N GLN F 260-48. 355 61.025-20. 448 1.00 17.26 6667 CA GLN F 260-49.780 61.339-20. 485 1.00 17.64 6668 CB GLN F 260-50. 197 62. 148-19. 241 1.00 17.41 6669 CG GLN F 260-49.562 63. 540-19. 109 1.00 18.91 6670 CD GLN F 260-50.026 64. 279-17. 855 1.00 20.17 6671 OE1 GLN F 260-50. 240 63. 668-16. 806 1.00 21.98 6672 NE2 GLN F 260-50. 165 65.597-17. 955 1.00 18.69 6673 C GLN F 260-50.101 62.123-21. 750 1.00 18.55 6674 O GLN F 260-49.222 62.760-22. 339 1.00 16.20 6675 N LEU F 261-51.357 62.047-22. 180 1.00 16.80 6676 CA LEU F 261-51.816 62.777-23. 355 1.00 17.60 6677 CB LEU F 261-52.461 61.819-24. 367 1.00 14.38 6678 CG LEU F 261-52.762 62.399-25. 757 1.00 14.77 6679 CD 1 LEU F 261-52.741 61.291-26. 785 1.00 15.67 6680 CD2 LEU F 261-54. 119 63.120-25. 749 1.00 14.61 6681 C LEU F 261-52.831 63.786-22. 826 1.00 20.25 6682 O LEU F 261-53.887 63. 402-22. 320 1.00 19.06 6683 N ALA F 262-52.501 65.073-22. 933 1.00 19.75 6684 CA ALA F 262-53.361 66.139-22. 424 1.00 21.14 6685 CB ALA F 262-52.609 66. 918-21. 339 1.00 20. 28 6686 C ALA F 262-53.880 67.117-23. 472 1.00 21.84 6687 O ALA F 262-53.173 67.449-24. 423 1.00 22.26 6688 N ILE F 263-55. 119 67.576-23. 283 1.00 20.59 6689 CA ILE F 263-55. 747 68.558-24. 172 1.00 20. 48 6690 CB ILE F 263-57.159 68.090-24. 613 1.00 22.16 6691 CG2 ILE F 263-57.821 69.146-25. 505 1.00 20.92 6692 CG1 ILE F 263-57.038 66.770-25. 384 1.00 21.99 6693 CD1 ILE F 263-58.362 66.094-25. 673 1.00 23. 64 6694 C ILE F 263-55.834 69. 848-23. 342 1.00 22. 00 6695 O ILE F 263-56.594 69.928-22. 372 1.00 20.52 6696 N PRO F 264-55. 045 70.874-23. 711 1.00 22.75 1 2 3 4 5 6 7 8 9 10 6697 CD PRO F 264 -54.191 70.922 -24.915 1.00 22.76 6698 CA PRO F 264'-55. 007 72.157-23. 003 1.00 24.87 6699 CB PRO F 264-53. 748 72.809-23. 567 1.00 25. 58 6700 CG PRO F 264-53.806 72.396-24. 999 1.00 23.89 6701 C PRO F 264-56.244 73.043-23. 140 1.00 27.74 6702 O PRO F 264-56.146 74.206-23. 543 1.00 26.40 6703 N ARG F 265-57. 403 72.491-22. 790 1.00 27.61 6704 CA ARG F 265-58.657 73.233-22. 854 1.00 29.17 6705 CB ARG F 265-59.173 73.283-24. 289 1.00 33.44 6706 CG ARG F 265.-60. 502 74.003-24. 434 1.00 39.54 6707 CD ARG F 265-60.997 73.973-25. 869 1.00 44. 90 6708 NE ARG F 265-62. 342 74.528-25. 999 1.00 50.69 6709 CZ ARG F 265-62.665 75. 791-25.731 1. 00 53.25 6710 NH1 ARG F 265-61.738 76. 644-25. 316 1.00 55.11 6711 NH2 ARG F 265-63.918 76.203-25. 877 1.00 54.80 6712 C ARG F 265-59.693 72.568-21. 954 1.00 29. 32 6713 O ARG F 265-59.801 71.341-21. 921 1.00 27. 44 6714 N GLU F 266-60.444 73.379-21. 216 1.00 28. 30 6715 CA GLU F 266-61.473 72.858-20. 325 1.00 28. 77 6716 CB GLU F 266-61.941 73. 954-19.359 1.00 31.95 6717 CG GLU F 266-60.934 74.292-18. 265 1.00 37.39 6718 CD GLU F 266-61. 374 75. 457-17. 386 1.00 42.38 6719 OE1 GLU F 266-60.716 75. 697-16. 348 1.00 44.38 6720 OE2 GLU F 266-62. 367 76.139-17. 732 1.00 43.57 6721 C GLU F 266-62.664 72.324-21. 118 1.00 27.10 6722 O GLU F 266-63.093 72.936-22. 096 1. 00 26.67 6723 N ASN F 267-63. 178 71.170-20. 702 1.00 27. 33 6724 CA ASN F 267-64.336 70.556-21. 353 1.00 27.48 6725 CB ASN F 267-65.600 71.336-20. 976 1.00 28. 98 6726 CG ASN F 267-65.812 71.400-19. 475 1.00 29.97 6727 OD1 ASN F 267-65.857 70.371-18. 804 1.00 34. 86 6728 ND2 ASN F 267-65. 937 72. 610-18. 941 1.00 32.06 6729 C ASN F 267-64.227 70. 469-22. 872 1.00 27.27 1 2 3 4 5 6 7 8 9 10 6730 O ASN F 267-65.168 70.802-23. 590 1.00 25.42 6731 N ALA F 268-63.082 70.008-23. 366 1.00 26.43 6732 CA ALA F 268-62. 880 69.888-24. 804 1.00 25.40 6733 CB ALA F 268-61.428 69.505-25. 097 1.00 25.52 6734 C ALA F 268-63.831 68.840-25. 382 1.00 25.94 6735 O ALA F 268-64.086 67.811-24. 761 1.00 26.13 6736 N GLN F 269-64.363 69.109-26. 568 1. 00 26.06 6737 CA GLN F 269-65.279 68.172-27. 205 1.00 27.59 6738 CB GLN F 269-66.429 68.928-27. 880 1.00 29.07 6739 CG GLN F 269-67.281 69.744-26. 895 1. 00 31.22 6740 CD GLN F 269-67.878 68.894-25. 771 1.00 33.82 6741 OE1 GLN F 269-68.666 67.978-26. 017 1.00 34.21 6742 NE2 GLN F 269-67.501 69.198-24. 531 1.00 33.66 6743 C GLN F 269-64.522 67. 314-28. 213 1.00 25. 38 6744 0 GLN F 269-64.001 67.814-29. 210 1. 00 24.36 6745 N ILE F 270-64.459 66.018-27. 927 1.00 24.10 6746 CA ILE F 270-63.750 65.072-28. 777 1.00 24.80 6747 CB ILE F 270-62. 389 64.696-28. 152 1.00 24.66 6748 CG2 ILE F 270-61.508 65.939-28. 023 1.00 23.50 6749 CG1 ILE F 270-62.622 64.069-26. 773 1. 00 26.09 6750 CD1 ILE F 270-61. 380 63.491-26. 133 1. 00 28.93 6751 C ILE F 270-64.542 63.780-28. 950 1.00 26.16 6752 O ILE F 270-65.531 63.544-28. 255 1.00 25.71 6753 N SER F 271-64.094 62.948-29. 884 1.00 24.77 6754 CA SER F 271-64.720 61.659-30. 131 1. 00 24.53 6755 CB SER F 271-64.638 61.303-31. 615 1.00 24. 36 6756 OG SER F 271-65.051 59.966-31. 841 1.00 25.86 6757 C SER F 271-63.970 60.610-29. 313 1.00 25.84 6758 O SER F 271-62.735 60.612-29. 270 1. 00 25. 27 6759 N LEU F 272-64.714 59. 719-28. 664 1.00 23. 29 6760 CA LEU F 272-64.107 58.672-27. 860 1.00 23. 77 6761 CB LEU F 272-64.775 58.605-26. 481 1.00 22.71 6762 CG LEU F 272-64.604 59.846-25. 588 1. 00 26. 57 1 2 3 4 5 6 7 8 9 10 6763 CDI LEU F 272-65. 332 59. 631-24. 264 1.00 25.50 6764 CD2 LEU F 272-63.112 60.108-25. 335 1.00 24.06 6765 C LEU F 272-64.132 57.292-28. 534 1.00 23.59 6766 O LEU F 272-64.141 56.268-27. 854 1.00 25.23 6767 N ASP F 273-64.145 57.264-29. 866 1.00 23.74 6768 CA ASP F 273-64.115 55.993-30. 592 1.00 24.06 6769 CB ASP F 273-64.475 56.165-32. 075 1.00 26.23 6770 CG ASP F 273-65.910 56.607-32. 298 1.00 32.45 6771 ODI ASP F 273-66.770 56.350-31. 429 1.00 35.25 6772 OD2 ASP F 273-66.179 57.198-33. 366 1. 00 35.15 6773 C ASP F 273-62.677 55.472-30. 512 1.00 23.57 6774 O ASP F 273-61.731 56. 212-30. 795 1.00 22.65 6775 N GLY F 274-62.521 54. 200-30. 154 1. 00 22. 02 6776 CA GLY-F 274-61.200 53. 605-30. 034 1.00 20.68 6777 C GLY F 274-60.392 53. 525-31. 319 1.00 21.24 6778 O GLY F 274-59. 179 53. 309-31. 277 1.00 21.00 6779 N ASP F 275-61.045 53.695-32. 464 1.00 18.99 6780 CA ASP F 275-60. 324 53. 641-33. 724 1. 00 18. 58 6781 CB ASP F 275-61. 204 53.062-34. 842 1. 00 19. 62 6782 CG ASP F 275-62. 447 53. 894-35. 115 1.00 23.46 6783 ODE ASP F 275-62.570 55.014-34. 576 1.00 25.42 6784 OD2 ASP F 275-63. 309 53.421-35. 887 1.00 27.04 6785 C ASP F 275-59. 790 55.003-34. 159 1.00 17.10 6786 O ASP F 275-59. 077 55.088-35. 150 1.00 16.99 6787 N VAL F 276-60.114 56. 064-33. 423 1.00 16.40 6788 CA VAL F 276-59.643 57. 392-33. 816 1.00 17. 33 6789 CB VAL F 276-60.807 58. 234-34. 396 1.00 17.71 6790 CG1 VAL F 276-61.729 58.695-33. 285 1.00 16.88 6791 CG2 VAL F 276-60.257 59. 404-35. 196 1.00 19.03 6792 C VAL F 276-58.921 58.198-32. 723 1.00 17.13 6793 O VAL F 276-58.217 59. 159-33. 025 1.00 17.63 6794 N THR F 277-59. 090 57.805-31. 464 1.00 16.69 6795 CA THR F 277-58.433 58.477-30. 346 1.00 15.30 1 2 3 4 5 6 7 8 9 10 6796 CB THR F 277-59.466 59.164-29. 420 1.00 14.65 6797 OG1 THR F 277-60.183 60.152-30. 173 1.00 16.55 6798 CG2 THR F 277-58.774 59.847-28. 245 1.00 14. 21 6799 C THR F 277-57.682 57.386-29. 596 1.00 15. 68 6800 O THR F 277-58.295 56.529-28. 957 1.00 14.85 6801 N PHE F 278-56. 353 57.406-29. 713 1.00 15.80 6802 CA PHE F 278-55. 497 56. 399-29. 096 1.00 14.12 6803 CB PHE F 278-55.383 55. 180-30. 030 1.00 14.73 6804 CG PHE F 278-54.985 55.515-31. 440 1.00 16.70 6805 CD1 PHE F 278-53. 643 55.628-31. 792 1.00 18.14 6806 CD2 PHE F 278-55. 954 55.707-32. 428 1. 00 18. 22 6807 CE1 PHE F 278-53.268 55.928-33. 103 1.00 17.50 6808 CE2 PHE F 278-55. 590 56. 008-33. 740 1.00 17. 61 6809 CZ PHE F 278-54.241 56. 117-34. 079 1.00 17.12 6810 C PHE F 278-54.116 56.966-28. 724 1.00 16.03 6811 O PHE F 278-53. 747 58.061-29. 161 1.00 14.60 6812 N PHE F 279-53.352 56.198-27. 952 1.00 15.83 6812 N PHE F 279 -@@.@@@ @@.@@@ -27.9@2 1.00 15.83 6813 CA PHE F 279 -52.068 56.650 -27.412 1.00 15.82 6814 CB PHE F 279 -52.428 57.439 -26.135 1.00 14.45 6815 CG PHE F 279-51.264 57.910-25. 296 1.00 17.02 6816 CD1 PHE F 279-50.123 58.469-25. 870 1.00 18.04 6817 CD2 PHE F 279-51. 378 57.900-23. 900 1.00 16.49 6818 CE1 PHE F 279-49.116 59.020-25. 067 1.00 17.23 6819 CE2 PHE F 279-50. 378 58.450-23. 085 1.00 18. 87 6820 CZ PHE F 279-49. 244 59.013-23. 672 1.00 16.38 6821 C PHE F 279-51.192 55.420-27. 111 1.00 16.90 6822 O PHE F 279-51.667 54.456-26. 508 1.00 15.81 6823 N GLY F 280-49.929 55.442-27. 538 1.00 15.11 6824 CA GLY F 280-49.064 54.301-27. 279 1.00 14.61 6825 C GLY F 280-47.565 54.573-27. 266 1.00 16.82 6826 O GLY F 280-47.113 55.669-27. 616 1. 00 15. 12 6827 N ALA F 281-46.793 53.571-26. 849 1. 00 15. 74 6828 CA ALA F 281-45. 338 53.684-26. 795 1. 00 17. 23 1 2 3 4 5 6 7 8 9 10 6829 CB ALA F 281-44.895 54.214-25. 427 1.00 16.52 6830 C ALA F 281-44.693 52.326-27. 070 1.00 17.64 6831 O ALA F 281-45.266 51.271-26. 764 1.00 15. 94 6832 N LEU F 282-43.492 52.364-27. 639 1.00 16.94 6833 CA LEU F 282-42.757 51.156-27. 990 1.00 17.96 6834 CB LEU F 282-42.962 50.877-29. 478 1.00 21.09 6835 CG LEU F 282-42.034 49.889-30. 177 1.00 23.87 6836 CD1 LEU F 282-42.494 48.464-29. 962 1.00 26.36 6837 CD2 LEU F 282-42. 051 50.203-31. 655 1.00 29.70 6838 C LEU F 282-41.264 51. 318-27. 693 1.00 18. 77 6839 O LEU F 282-40.643 52.292-28. 123 1.00 18.33 6840 N LYS F 283-40. 689 50.363-26. 970 1.00 18.82 6841 CA LYS F 283-39.272 50.430-26. 634 1. 00 20.72 6842 CB LYS F 283-38.951 49.566-25. 406 1.00 22.42 6843 CG LYS F 283-37. 505 49.754-24. 934 1.00 21.99 6844 CD LYS F 283-37.175 48.993-23. 665 1.00 27.55 6845 CE LYS F 283-35.741 49.296-23. 243 1.00 28. 39 6846 NZ LYS F 283-35. 339 48.554-22. 029 1.00 37.37 6847 C LYS F 283-38.410 49.979-27. 805 1.00 21. 88 6848 O LYS F 283-38.524 48.848-28. 279 1.00 21.81 6849 N LEU F 284-37.542 50.873-28. 262 1.00 21.54 6850 CA LEU F 284-36.658 50.591-29. 384 1.00 23.94 6851 CB LEU F 284-36.197 51. 912-30. 003 1.00 22.89 6852 CG LEU F 284-37.310 52.858-30. 471 1.00 21.96 6853 CD1 LEU F 284-36.719 54.202-30. 865 1.00 22.68 6854 CD2 LEU F 284-38.054 52.229-31. 639 1.00 21. 39 6854 CD2 LEU F 284 -38.054 52.229 -31.639 1.00 21.39 6855 C LEU F 284 -35.437 49.763 -28.971 1.00 27.72 6856 O LEU F 284 -34.835 49.998 -27.921 1.00 27.67 6857 N LEU F 285-35. 074 48.790-29. 801 1.00 30.51 6858 CA LEU F 285-33. 918 47.945-29. 522 1.00 34. 18 6859 CB LEU F 285-33. 933 46. 716-30. 433 1.00 35.51 6860 CG LEU F 285-34.931 45. 646-29.988 1. 00 37.83 6861 CD1 LEU F 285-35.146 44. 616-31.091 1. 00 37.41 2 3 4 5 6 7 8 9 10 6862 CD2 LEU F 285-34. 403 44.989-28. 721 1.00 37.06 6863 C LEU F 285-32.619 48.723-29. 711 1.00 36.06 6864 O LEU F 285-31. 725 48.613-28. 846 1.00 38.88 6865 OXT LEU F 285-32.507 49.432-30. 729 1.00 38.77 6867 MG MG G 1-22.921 88. 053 2.601 1.00 28.06 6866 MG MG G 2-23.584 91.124 3.232 1.00 33.53 6869 OH2 TIP G 3-24.009 89.831 1.107 1.00 22.42 6868 OH2 TIP G 4-21.236 89.953 3.332 1.00 24. 30 6870 OH2 TIP G 5-24.511 89.232 4.571 1.00 24.54 6871 OH2 TIP G 6-26.069 92.174 2.963 1.00 33.08 7075 OH2 TIP G 7-22.569 93.079 2.040 1.00 23.43 6873 OH2 TIP G 8-23.130 92.326 5.420 1.00 23.63 6874 OH2 TIP G 9-25.793 93.108 5.718 1.00 38.91 6875 OH2 TIP G 10-24.770 94.254 1.295 1.00 41.06 6876 OH2 TIP G 11-21.990 94.700 3.958 1. 00 40.10 6877 OH2 TIP G 12-27.271 94.164 7.755 1.00 27.72 6878 OH2 TIP G 13-19.846 96.395 4.491 1.00 31.89 6879 OH2 TIP G 14-17.701 98.077 3.256 1.00 46.66 6880 OH2 TIP G 15-26.638 95.875-0. 396 1.00 29.64 6881 OH2 TIP G 16-29.139 96. 379-1. 472 1.00 43.92 6882 OH2 TIP G 17-28.402 98.434 4.341 1.00 45.43 6883 OH2 TIP G 18-23.591 98.965 7.457 1.00 47.07 6884 OH2 TIP G 19-27.138 97.241 7.180 1.00 53.08 6885 OH2 TIP G 20-25.944 98.354 9.901 1.00 46.12 6886 OH2 TIP G 21-25.138 60.304 18.474 1.00 50.73 6887 OH2 TIP G 22-29.612 99.181 1.291 1.00 51.79 6888 MG MG H 1-58.402 72.484-41. 756 1. 00 32.64 6889 MG MG H 2-56.384 70. 077-41. 130 1.00 28.82 6890 OH2 TIP H 3-58.854 69.843-41. 994 1.00 23.49 6891 OH2 TIP H 4-56.239 71.944-42. 921 1.00 18.29 6892 OH2 TIP H 5-57. 160 71.971-39. 586 1. 00 19.86 6893 OH2 TIP H 6-59. 484 72. 769-43. 992 1. 00 24.11 6894 OH2 TIP H 7-57.778 74.915-41. 553 1.00 20.48 1 2 3 4 5 6 7 8 9 10 6895 OH2 TIP H 8-60.645 72.856-40. 631 1. 00 21.91 6896 OH2 TIP H 9-58. 651 75. 484-44. 505 1.00 38.42 6897 OH2 TIP H 10-59. 943 75. 445-40. 101 1. 00 32.35 6898 OH2 TIP H 11-62.276 73.197-42. 874 1.00 41.25 6899 OH2 TIP H 12-60.569 77.896-38. 424 1.00 38.51 6900 OH2 TIP H 13-64.391 77.352-46. 803 1.00 48.45 6901 OH2 TIP H 14-58.560 77.056-46. 625 1.00 30.37 6902 OH2 TIP H 15-59.361 80. 054-37. 152 1.00 42.47 6903 OH2 TIP H 16-61.085 81. 001-43. 309 1.00 46. 30 6904 OH2 TIP H 17-50.253 64. 049-43. 618 1.00 22.10 6905 Cl CIT 1 888-32.153 60. 756-15. 651 1.00 20.00 6906 O1 CIT I 888-31.314 60. 398-16. 269 1.00 20.00 6907 02 CIT I 888-32.318 60. 676-14. 474 1.00 20.00 6908 C2 CIT I 888-33. 401 61. 402-16. 316 1.00 20.00 6909 C3 CIT I 888-33. 447 62. 938-16. 577 1.00 20.00 6910 07 CIT I 888-34. 819 63. 421-16. 675 1.00 20.00 6911 C4 CIT I 888-32.869 63. 665-15. 340 1.00 20. 00 6912 C5 CIT I 888-32.292 65. 014-15. 693 1.00 20.00 6913 03 CIT I 888-30. 970 65. 027-15. 812 1.00 20.00 6914 04 CIT I 888-32.915 66. 009-15. 951 1.00 20.00 6915 C6 CIT I 888-32.693 63. 268-17.841 1.00 20.00 6916 05 CIT I 888-33. 351, 63. 697-18. 840 1.00 20.00 6917 06 CIT I 888-31.439 63. 040-17. 828 1.00 20.00 6918 Cl DIO K 1-16.257 80.857-22. 628 1.00 41.37 6919 C2 DIO K 1-17.536 79.712-21. 055 1.00 41.00 6920 Cl'DIO K 1-17.490 81. 183-23. 388 1.00 42.65 6921 C2'DIO K 1-18. 751 79. 804-21. 957 1.00 39.56 6922 01 DIO K 1-16.720 80.883-21. 280 1.00 42.80 6923 01'DIO K 1-18. 291 79.986-23. 309 1.00 41. 54 7044 OH2 TIP U 7-17. 346 81.696-0. 104 1.00 19.49 7045 OH2 TIP U 17-28.005 65.690-22. 192 1.00 18.70 7046 OH2 TIP U 28-17. 104 78. 182-17377 1.00 22.67 7047 OH2 TIP U 32-28.902 66. 894-13. 811 1.00 24.14 1 2 3 4 5 6 7 8 9 10 7048 OH2 TIP U 46-11. 424 63. 382-14. 935 1.00 24.39 7049 OH2 TIP U 51-9. 517 58. 832-10. 376 1.00 27.04 7050 OH2 TIP U 54-21.423 58. 230-10. 957 1. 00 24.53 7051 OH2 TIP U 56-15.471 91.801-16. 315 1.00 33.51 7052 OH2 TIP U 59-36.500 72.706-26. 688 1. 00 28. 49 7053 OH2 TIP U 62-27.962 60.985-17. 954 1.00 31.79 7054 OH2 TIP U 68-20.752 57.018-20. 434 1.00 29. 18 7055 OH2 TIP U 71-28.827 63. 464-17. 117 1.00 26.28 7056 OH2 TIP U 77-4. 687 75. 366-18. 022 1.00 32. 86 7057 OH2 TIP U 85-15. 915 72.500-3. 012 1.00 25.11 7058 OH2 TIP U 96-44. 375 71.468-20. 754 1.00 28. 64 7059 OH2 TIP U 97-10.042 90.068-0. 976 1.00 31.21 7060 OH2 TIP U 100-11. 847 87.969-23. 545 1.00 50.27 7061 OH2 TIP U 103-8.572 68.346-20. 094 1.00 35.91 7062 OH2 TIP U 106-14. 582 57. 752-11. 220 1.00 30.45 7063 OH2 TIP U 109-30. 534 59. 952-18. 292 1.00 34. 09 7064 OH2 TIP U 123-7.491 81. 301-19. 193 1.00 34.11 7065 OH2 TIP U 135-18.125 83.535-15. 034 1.00 33.65 7066 OH2 TIP U 137-31.276 77.100-23. 401 1.00 34.66 7067 OH2 TIP U 141-10. 283 73. 391-25. 339 1.00 33.61 7068 OH2 TIP U 144-13.175 96.278-3. 280 1. 00 46. 08 7069 OH2 TIP U 158-5.111 85. 927-2.502 1.00 37.63 7070 OH2 TIP U 170-12. 375 64.728-25. 752 1.00 42.08 7071 OH2 TIP U 179-28.528 81.747-18. 447 1. 00 33.52 7072 OH2 TIP U 185-18. 060 65.640-26. 786 1.00 50.82 7073 OH2 TIP U 188-7.847 89.954-9. 830 1. 00 45. 64 7074 OH2 TIP U 191-26.063 91. 141-10. 657 1.00 58.23 6872 OH2 TIP U 194-16.441 80. 957-16. 770 1.00 26.13 7076 OH2 TIP U 201-34.032 71. 242-19. 547 1.00 32.24 7077 OH2 TIP U 210-20.035 67.562-26. 482 1.00 33.83 7078 OH2 TIP U 230-16. 840 57.234-9. 681 1.00 48.56 7079 OH2 TIP U 266-32.375 86.226-7. 056 1.00 38.60 7080 OH2 TIP U 268-25. 879 62.475-29. 357 1. 00 44. 05 2 3 4 5 6 7 8 9 10 7081 OH2 TIP U 272-5. 030 60. 908-13. 579 1.00 45.20 7082 OH2 TIP U 274-10. 985 61.426-20. 842 1.00 43.06 7083 OH2 TIP U 277-14. 604 89.077-24. 340 1. 00 39. 14 7084 OH2 TIP U 282-17. 996 63.565-24. 815 1.00 49.48 7085 OH2 TIP U 295-20.741 55. 591-16. 678 1.00 45.83 7086 OH2 TIP U 357-9.615 78.553-20. 735 1.00 47.84 7087 OH2 TIP U 358-30. 372 58. 203-12. 727 1.00 47.14 7088 OH2 TIP U 364-13.792 53. 416-10. 181 1. 00 51.77 7089 OH2 TIP U 365-8.168 61.253-20. 335 1.00 46. 30 7090 OH2 TIP U 385-5. 143 59.098-8. 527 1.00 50.96 7091 OH2 TIP U 390-10. 107 75.943-22. 390 1.00 44.52 7092 OH2 TIP U 405-31.088 81. 178-14. 517 1.00 47.57 7093 OH2 TIP U 414-23.954 89. 127-11. 201 1.00 49.73 7094 OH2 TIP U 421-13. 048 91.758-20. 682 1.00 49.00 7095 OH2 TIP U 437-14. 892 101.647-2. 212 1.00 43.38 7096 OH2 TIP U 457-12.788 56. 595-15. 640 1.00 52.29 7097 OH2 TIP U 465-11.658 93. 344-8. 783 1.00 54. 96 7098 OH2 TIP U 473-14. 206 56. 939-13. 640 1.00 58.87 7099 OH2 TIP U 480-26. 857 55.486-19. 550 1.00 56.51 7100 OH2 TIP U 484-4. 054 86.631-8. 756 1.00 53.28 7101 OH2 TIP U 508-22.448 55. 547-11. 947 1.00 50. 15 7102 OH2 TIP U 514-6.508 71.179-19. 784 1.00 46.98 7103 OH2 TIP U 517-24.268 56.981-21. 472 1.00 48.87 7104 OH2 TIP U 521-11. 018 68.865-24. 415 1.00 50.66 7105 OH2 TIP U 526-2.161 74. 805-14. 912 1.00 45. 24 7106 OH2 TIP U 545-9.710 56. 176-15. 817 1.00 53.84 7107 OH2 TIP U 549-3. 575 72. 551-19. 036 1.00 50.60 7108 OH2 TIP U 551-0.706 79. 084-17. 862 1.00 47.45 7109 OH2 TIP U 579-4.969 90. 947-17. 434 1.00 55. 72 7110 OH2 TIP U 584-13. 420 97.422-6. 334 1.00 57. 36 7111 OH2 TIP U 588-1.644 70.155-16. 612 1.00 53. 39 7112 OH2 TIP U 594-7. 737 66.016-22. 022 1.00 47.78 7113 OH2 TIP U 614-27. 188 79.649-35. 207 1.00 59. 41 1 2 3 4 5 6 7 8 9 10 7114 OH2 TIP V 1-19. 599 71. 812-0. 059 1. 00 15. 55 7115 OH2 TIP V 3-24.820 80.390-1. 534 1.00 21.90 7116 OH2 TIP V 30-30.556 56. 626-0. 886 1.00 29. 19 7117 OH2 TIP V 43-21. 301 63.707 13.952 1.00 31.29 7118 OH2 TIP V 61-37. 864 72.223 5.600 1.00 28.06 7119 OH2 TIP V 64-30.729 72. 369-7. 558 1.00 29.63 7120 OH2 TIP V 74-20. 890 55.723 5.885 1.00 26. 82 7121 OH2 TIP V 83-28.778 71.785 19.165 1. 00 39.57 7122 OH2 TIP V 84-35. 744 59.997 14.079 1.00 32.51 7123 OH2 TIP V 91-23.555 70. 696-1. 859 1.00 34.54 7124 OH2 TIP V 93-41.364 64.993-4. 236 1.00 28.98 7125 OH2 TIP V 115-34.561 52.581 1.045 1.00 40.92 7126 OH2 TIP V 120-40. 307 81. 970-4. 882 1.00 45.35 7127 OH2 TIP V 125-36.061 63.454 25.923 1.00 40.49 7128 OH2 TIP V 136-39. 047 71. 932-9. 421 1.00 46.75 7129 OH2 TIP V 139-36.808 75.601 6.192 1.00 33. 38 7130 OH2 TIP V 147-27.562 50. 302 9.999 1.00 35.21 7131 OH2 TIP V 151-42.855 81.871 4.904 1.00 39. 72 7132 OH2 TIP V 155-29.958 58.219 17.223 1.00 30.83 7133 OH2 TIP V 162-38.871 53.203 5.271 1.00 46.21 7134 OH2 TIP V 165 -42.306 64.060 2.066 1.00 41.24 7135 OH2 TIP V 186 -25.563 71.992 18.126 1.00 47.08 7136 OH2 TIP V 193-36.765 69.691 6.220 1.00 22.06 7137 OH2 TIP V 206-39.712 74.250-8. 120 1.00 52.93 713.8 OH2 TIP V 229-25.856 54. 380-4. 967 1.00 33.93 7139 OH2 TIP V 237-37.308 56.774 12. 334 1.00 38.23 7140 OH2 TIP V 254-35.653 91. 383-2. 606 1.00 38.52 7141 OH2 TIP V 267-38.034 76. 598-9. 403 1.00 50.93 7142 OH2 TIP V 271-34.894 77. 239-10. 355 1.00 44. 66 7143 OH2 TIP V 276-43.826 70. 053-1.589 1.00 37. 04 7144 OH2 TIP V 279-33.438 84.256 11.655 1.00 52.39 7145 OH2 TIP V 291-37.960 57. 896-0. 444 1.00 45.12 7146 OH2 TIP V 322-25. 599 65.100 16.928 1.00 43. 61 1 2 3 4 5 6 7 8 9 10 7147 OH2 TIP V 325-26.107 55. 352-10. 483 1.00 50.71 7148 OH2 TIP V 332-20.544 71.035 12.906 1. 00 41. 23 7149 OH2 TIP V 341-37. 951 60.145 16.009 1.00 51.66 7150 OH2 TIP V 351-23.859 53.722-0. 131 1.00 46.78 7151 OH2 TIP V 367-35.362 84.138-6. 572 1.00 45.24 7152 OH2 TIP V 370-31.145 92.146-4. 661 1. 00 58.09 7153 OH2 TIP V 378-36.560 96.691-1. 033 1.00 43.48 7154 OH2 TIP V 394-26.648 50.876-2. 869 1.00 45.31 7155 OH2 TIP V 399-45.146 86.974 10.800 1.00 47.25 7156 OH2 TIP V 407-39.103 64. 103-8. 580 1.00 53. 42 7157 OH2 TIP V 429-48.421 75.637 7.713 1.00 48.45 7158 OH2 TIP V 441-21.763 54.715 0.933 1.00 43.79 7159 OH2 TIP V 447-32.786 47.162 10.257 1.00 52.39 7160 OH2 TIP V 455-36.932 59.482 26.857 1.00 48. 56 7161 OH2 TIP V 461-23.964 63.505 15.083 1.00 50.31 7162 OH2 TIP V 466-43.635 60.757 3.367 1.00 50.00 7163 OH2 TIP V 474-31.825 60.851 34.311 1. 00 52.50 7164 OH2 TIP V 486-41.568 72. 742-9. 553 1.00 56.59 7165 OH2 TIP V 493-43.914 79.443 12.081 1.00 47.04 7166 OH2 TIP V 505-45. 364 80.578 1. 337 1.00 48.71 7167 OH2 TIP V 506-39. 932 57.124 3.387 1.00 50.10 7168 OH2 TIP V 523-42.348 67.216 0.889 1.00 48.87 7169 OH2 TIP V 542-47.006 75.567 15.902 1.00 54. 98 7170 OH2 TIP V 548-45.901 78.164 14.251 1.00 51.77 7171 OH2 TIP V 556-47.715 73.998 2.699 1.00 49.67 7172 OH2 TIP V 568-18.184 60.464 17.643 1. 00 55. 14 7173 OH2 TIP V 583-25.330 51. 609 1.089 1.00 58.23 7174 OH2 TIP V 600-47. 777 83.406 12.083 1.00 51.67 7175 OH2 TIP V 602-35.682 67.140 26.038 1.00 57.62 7176 OH2 TIP V 616-39.515 89.983-0. 272 1. 00 53. 84 7177 OH2 TIP W 4-5. 955 75.440 12.154 1.00 21.84 7178 OH2 TIP W 10-6.978 77.605 13.537 1.00 23.50 7179 OH2 TIP W 12-8. 301 59.847 9.271 1.00 23.16 123 4 5 6 7 8 9 10 7180 OH2 TIP W 34 4.582 69.027 0.017 1. 00 26. 73 7181 OH2 TIP W 40 0. 538 87.696 16.370 1.00 33.75 7182 OH2 TIP W 42-21.987 79.810 5. 756 1.00 24. 62 7183 OH2 TIP W 58-9. 503 86.752 18.671 1.00 31. 99 7184 OH2 TIP W 67 0.003 74.064-2. 882 1.00 27.25 7185 OH2 TIP W 69-7. 009 59.878-2. 530 1.00 27.20 7186 OH2 TIP W 79-5. 730 62.829 15.678 1.00 30.62 7187 OH2 TIP W 86-8.448 80.874 12.409 1.00 22.54 7188 OH2 TIP W 95-1.092 84.704 3.899 1.00 44.99 7189 OH2 TIP W 101-0.222 81. 901-0. 393 1.00 33.29 7190 OH2 TIP W 105 4.182 70.034 6.660 1.00 27.25 7191 OH2 TIP W 110-7.811 76.877-5. 189 1.00 31. 78 7192 OH2 TIP W 126 1.624 58.000 1.651 1.00 32.22 7193 OH2 TIP W 134-18.651 82.100 20.970 1.00 40.78 7194 OH2 TIP W 143-3.721 84.334 0.828 1.00 43.46 7195 OH2 TIP W 156-25.921 83.910 15.933 1.00 52.93 7196 OH2 TIP W 182-1.283 79. 785-2. 851 1.00 35.46 7197 OH2 TIP W 196 7.477 74.056-3. 923 1.00 24.82 7198 OH2 TIP W 203-2.456 87.928 15.911 1.00 31.90 7199 OH2 TIP W 221-13.817 59. 721 16.426 1.00 34.63 7200 OH2 TIP W 222-18.461 70.582 4.144 1.00 33.64 7201 OH2 TIP W 22. 8-12. 503 55.179 6.815 1.00 35.29 7202 OH2 TIP W 234-0.956 81.780 3.009 1.00 42.98 7203 OH2 TIP W 238 11.783 79.498-1. 770 1.00 35.74 7204 OH2 TIP W 249-8. 390 73.426 21.787 1.00 42.87 7205 OH2 TIP W 255-22.882 90.832 16.401 1.00 42.05 7206 OH2 TIP W 263-26.568 76.664 18.070 1. 00 48. 36 7207 OH2 TIP W 264 0.351 68.387-4. 619 1.00 50.55 7208 OH2 TIP W 275-4.285 69.795 18.478 1.00 40.82 7209 OH2 TIP W 278 8.955 79.882 2.620 1. 00 44.01 7210 OH2 TIP W 283-2.117 83.449 21.667 1.00 38.10 7211 OH2 TIP W 289-19.662 74.946 20.749 1.00 45.30 7212 OH2 TIP W 290 3.923 85.135 16.748 1.00 45. 90 2 3 4-5 6 7 8 9 10 7213 OH2 TIP W 292-4.179 93.099 12. 428 1.00 43.21 7214 OH2 TIP W 299-2.921 57.583 11.405 1.00 41.51 7215 OH2 TIP W 302 3.768 88.945 13.090 1.00 46.72 7216 OH2 TIP W 309-24.058 96.418 16.924 1.00 46.81 7217 OH2 TIP W 317 4.032 73.800-5. 438 1.00 40.51 7218 OH2 TIP W 318 3.438 71.556-4. 602 1.00 51.80 7219 OH2 TIP W 319 8.020 73.194 5.163 1.00 49.81 7220 OH2 TIP W 321 5.857 80.454 3.899 1.00 41.51 7221 OH2 TIP W 326-13. 056 81.630 24.418 1.00 45.54 7222 OH2 TIP W 338-17. 362 73. 369 23.948 1.00 47.63 7223 OH2 TIP W 343-4. 034 57.597-2. 201 1.00 43.48 7224 OH2 TIP W 354 10.536 82. 828-1. 854 1.00 56.28 7225 OH2 TIP W 366-15. 383 67.041 20.840 1.00 44.16 7226 OH2 TIP W 380-5.712 79.486 23. 370 1.00 40.13 7227 OH2 TIP W 387-27.466 94.598 10.799 1.00 46.04 7228 OH2 TIP W 389 1.030 87.211 19. 356 1.00 55.06 7229 OH2 TIP W 406-7.926 97.431 8.832 1. 00 51. 72 7230 OH2 TIP W 408-23.461 85. 542 17.040 1.00 48. 31 7231 OH2 TIP W 415-9.424 56.620 2.876 1.00 39.73 7232 OH2 TIP W 417-19.333 68.265 14.350 1.00 42.52 7233 OH2 TIP W 428 2.163 75.576 9.802 1.00 46.17 7234 OH2 TIP W 431-6.653 85.438 22.224 1.00 42.41 7235 OH2 TIP W 434 0.528 58.116 14.577 1.00 53.91 7236 OH2 TIP W 446-4. 144 95.502 15.011 1.00 50. 35 7237 OH2 TIP W 456 5.655 62.738 1.055 1.00 42.25 7238 OH2 TIP W 467-9.221 56.449 14.022 1.00 52. 07 7239 OH2 TIP W 478 7.034 70.440 7.566 1.00 48.84 7240 OH2 TIP W 488-6. 729 54.929 2.817 1.00 52.02 7241 OH2 TIP W 496-16. 896 64. 305 19.788 1. 00 49.09 7242 OH2 TIP W 502 10.376 83. 019-10. 207 1.00 52.82 7243 OH2 TIP W 503 2.102 77.633 13.729 1.00 59. 02 7244 OH2 TIP W 507 1.564 61.134 13.585 1.00 43.33 7245 OH2 TIP W 515-9. 465 67.390 20.561 1. 00 36. 14 1 2 3 4 5 6 7 8 9 10 1 2 3 4 5 6 7 8 9 10 7246 OH2 TIP W 530 -1.059 67.655 18.997 1.00 49.20 7247 OH2 TIP W 537 5.076 66.798 8.771 1.00 42.11 7248 OH2 TIP W 559-23. 570 82.820 17.869 1.00 55.67 7249 OH2 TIP W 561-4. 122 87. 304 3.580 1.00 54.80 7250 OH2 TIP W 564 6.737 71.159-4. 618 1.00 55.63 7251 OH2 TIP W 598 6.952 82. 903-4. 940 1.00 48.21 7252 OH2 TIP X 14-33.385 69. 740-43. 555 1.00 19.94 7253 OH2 TIP X 18-31.860 48.289-42. 328 1. 00 21.58 7254 OH2 TIP X 24-34.896 72.205-43. 041 1.00 27.45 7255 OH2 TIP X 26-49.341 66.979-36. 598 1.00 18.72 7256 OH2 TIP X 36-37.551 53.835-50. 741 1.00 29.00 7257 OH2 TIP X 47-27.047 57. 070-35. 726 1.00 26.15 7258 OH2 TIP X 48-23.822 63.880-36. 103 1.00 26.79 7259 OH2 TIP X 50-29.581 47.176-38. 952 1.00 54.90 7260 OH2 TIP X 66-39.651 67.060-29. 949 1.00 28.63 7261 OH2 TIP X 70-28. 131 69. 218-28. 874 1.00 29.42 7262 OH2 TIP X 82-35.630 57.079-53. 486 1.00 35.56 7263 OH2 TIP X 87-28.399 52.267-31. 438 1.00 34.75 7264 OH2 TIP X 89-39.318 82.018-43. 141 1.00 29.27 7265 OH2 TIP X 94-23. 227 50.442-45. 926 1.00 29.03 7266 OH2 TIP X 98-41.465 80.156-33. 164 1.00 41.97 7267 OH2 TIP X 99 -30.706 48.700 -37.046 1.00 38.93 7268 OH2 TIP X 107 -35.463 83.931 -43.119 1.00 41.16 7269 OH2 TIP X 113-21.230 57.524-37. 516 1.00 37.93 7270 OH2 TIP X 114-25.723 71.127-39. 317 1.00 33.47 7271 OH2 TIP X 117-36.952 45.267-50. 858 1. 00 35. 97 7272 OH2 TIP X 122-27.145 70.913-33. 109 1.00 33.79 7273 OH2 TIP X 131-26.045 62.772-50. 829 1.00 36.77 7274 OH2 TIP X 149-29.478 75.639-35. 706 1.00 41. 07 7275 OH2 TIP X 154-39.914 55. 295-49. 707 1.00 36.92 7276 OH2 TIP X 160-42.432 60.059-35. 469 1.00 30.39 7277 OH2 TIP X 175-22.354 70.204-40. 498 1.00 39.22 7278 OH2 TIP X 176-23. 382 54.019-51. 401 1.00 42. 78 1 23 4 56 7 8 9 10 7279 OH2 TIP X 177-24. 710 55. 955-29. 329 1.00 44. 05 7280 OH2 TIP X 189-27.813 46. 860-43. 037 1.00 54.62 7281 OH2 TIP X 198-35. 685 75.144-29. 921 1.00 27.30 7282 OH2 TIP X 202-28.589 49.840-36. 154 1.00 41.89 7283 OH2 TIP X 212-26.640 50.094-52. 521 1.00 41.28 7284 OH2 TIP X 217-55. 376 76.671-48. 048 1.00 37.35 7285 OH2 TIP X 225-37. 953 73. 400-43. 940 1.00 29.74 7286 OH2 TIP X 236-19. 303 61.636-41. 812 1.00 32.08 7287 OH2 TIP X 239-27.849 56. 766-53. 856 1.00 39.36 7288 OH2 TIP X 244-41. 269 73.716-27. 824 1.00 34. 34 7289 OH2 TIP X 246-49. 696 76. 946-31. 374 1.00 39.23 7290 OH2 TIP X 258-41.848 67.256-54. 927 1.00 43.11 7291 OH2 TIP X 261-34. 155 76.953-28. 410 1.00 37.98 7292 OH2 TIP X 262-38.251 74.827-28. 325 1. 00 45.09 7293 OH2 TIP X 269-39. 363 64.037-56. 689 1.00 37.78 7294 OH2 TIP X 296-30.831 83.167-48. 098 1.00 50. 32 7295 OH2 TIP X 298-45. 394 73.781-26. 066 1.00 49.52 7296 OH2 TIP X 305-27.443 45. 958-34. 749 1.00 48.35 7297 OH2 TIP X 306-24. 769 51. 064-33. 238 1. 00 39.87 7298 OH2 TIP X 311-45.674 75. 306-48. 295 1.00 40. 02 7299 OH2 TIP X 313-27.486 71.806-35. 608 1. 00 49. 30 7300 OH2 TIP X 316-25. 793 ; 70. 245-30. 483 1.00 43.02 7301 OH2 TIP X 320-30.192 80.815-39. 685 1.00 48.52 7302 OH2 TIP X 323-37.548 70. 171-54. 934 1.00 42.53 7303 OH2 TIP X 331-22.544 62.155-49. 032 1. 00 38.93 7304 OH2 TIP X 345-24.236 69.557-38. 060 1.00 54.21 7305 OH2 TIP X 348-35. 457 55.104-51. 610 1.00 56. 00 7306 OH2 TIP X 353-31.407 51.263-24. 789 1.00 46.27 7307 OH2 TIP X 356-36.028 85.121-50. 245 1.00 59.53 7308 OH2 TIP X 369-51.450 78. 393-29. 927 1.00 58.86 7309 OH2 TIP X 372-26. 017 49.494-37. 325 1.00 49. 86 7310 OH2 TIP X 377-51.734 82. 206-35. 906 1.00 44.24 7311 OH2 TIP X 382-50.865 69. 297-53.601 1. 00 45.76 1 2 3 4 5 6 7 8 9 10 7312 OH2 TIP X 384-21.668 64.808-40. 285 1.00 44.69 7313 OH2 TIP X 391-27.949 73.712-38. 850 1.00 50.50 7314 OH2 TIP X 401-29. 710 52.222-20. 254 1.00 51.25 7315 OH2 TIP X 409-45.128 81. 560-35. 774 1.00 49.05 7316 OH2 TIP X 413-31. 045 76.837-29. 323 1.00 43.82 7317 OH2 TIP X 419-33. 779 42.610-47. 792 1.00 51.67 7318 OH2 TIP X 426-30.801 82.911-41. 985 1.00 47.51 7319 OH2 TIP X 439-28.196 76.491-37. 667 1.00 53.10 7320 OH2 TIP X 463-28.378 77.722-32. 106 1.00 52.01 7321 OH2 TIP X 469-19. 848 54. 258-42. 519 1.00 50.57 7322 OH2 TIP X 482-31.614 80.924-56. 879 1.00 53.86 7323 OH2 TIP X 489-23.861 59.359-29. 874 1.00 52.96 7324 OH2 TIP X 497-45.060 65.506-55. 768 1. 00 47.59 7325 OH2 TIP X 513-27.032 72.853-46. 455 1.00 55.75 7326 OH2 TIP X 524-41.910 71.833-55. 123 1.00 49. 32 7327 OH2 TIP X 527-47.111 83.985-38. 291 1.00 52.45 7328 OH2 TIP X 538-47. 543 76.865-50. 192 1. 00 49.14 7329 OH2 TIP X 552-21.192 62.950-36. 124 1.00 49.65 7330 OH2 TIP X 555-40.135 79.636-30. 469 1.00 53.38 7331 OH2 TIP X 565-25.285 74.158-48. 608 1.00 57. 58 7332 OH2 TIP X 571-29.648 70. 849-50. 590 1.00 57.77 7333 OH2 TIP X 586-48. 388 79.453-33. 127 1.00 56.44 7334 OH2 TIP X 590-33.141 62.036 32.658 0.00 1.00 7335 OH2 TIP X 591-32.933 45.202-49. 786 1.00 49.76 7336 OH2 TIP X 595-38.019 52.850-53. 325 1. 00 49.42 7337 OH2 TIP X 611-22.774 64. 372-47. 890 1. 00 53.20 7338 OH2 TIP X 615-22.964 67.547-36. 895 1.00 53.25 7339 OH2 TIP Y 2-45.808 57. 444-37331 1.00 16.41 7340 OH2 TIP Y 15-43. 990 40.571-34. 224 1.00 22.68 7341 OH2 TIP Y 23-58.151 36.757-37. 176 1.00 31.70 7342 OH2 TIP Y 25-64.135 37. 659-33. 586 1.00 26.66 7343 OH2 TIP Y 27-42.636 40.911-45. 891 1.00 24.79 7344 OH2 TIP Y 33-60.130 30.526-40. 642 1.00 25.41 1 2 3 4 5 6 7 8 9 10 7345 OH2 TIP Y 35-39. 475 40.248-39. 341 1.00 25. 15 7346 OH2 TIP Y 44-64.945 72.674-43. 368 1.00 27.24 7347 OH2 TIP Y 49-56. 388 48.568-49. 801 1.00 26. 37 7348 OH2 TIP Y 55-59.463 43.675-34. 481 1.00 26.84 7349 OH2 TIP Y 57-39.270 44.691-53. 218 1.00 29.97 7350 OH2 TIP Y 65-58.508 37. 526-44. 028 1.00 25.59 7351 OH2 TIP Y 78-58. 072 71. 472-55. 000 1.00 32.81 7352 OH2 TIP Y 81-65.367 48.358-37. 588 1.00 31.36 7353 OH2 TIP Y 88-57.381 50.619-51. 262 1.00 26.90 7354 OH2 TIP Y 92-66.497 43. 547-30. 099 1.00 31.43 7355 OH2 TIP Y 111-64.844 49.116-41. 245 1.00 33.93 7356 OH2 TIP Y 118-67.166 37. 043-30. 004 1.00 36.04 7357 OH2 TIP Y 119-54.011 31.951-38. 085 1.00 37.86 7358 OH2 TIP Y 121-67.745 42.229-42. 000 1.00 38. 23 7359 OH2 TIP Y 124-50.789 47.715-62. 894 1.00 51.93 7360 OH2 TIP Y 127-59. 084 53. 794-50. 386 1.00 28.91 7361 OH2 TIP Y 129-71.162 37.511-36. 017 1.00 31.52 7362 OH2 TIP Y 130-47.738 32.479-38. 051 1.00 30.52 7363 OH2 TIP Y 132-66.479 43. 322-34. 609 1.00 31.62 7364 OH2 TIP Y 145-56. 481 34. 711-45.924 1.00 34.92 7365 OH2 TIP Y 150-36.592 41.456-43. 181 1.00 33. 35 7366 OH2 TIP Y 153-61.723 75.573-55. 606 1.00 42.64 7367 OH2 TIP Y 167-65.191 52.764-38. 523 1.00 37.90 7368 OH2 TIP Y 187-36.284 40.736-48. 792 1.00 41.18 7369 OH2 TIP Y 215-62.812 58. 142-57. 053 1.00 31.17 7370 OH2 TIP Y 220-60.821 46.241-34. 803 1.00 37.63 7371 OH2 TIP Y 227-39.885 41.267-36. 669 1.00 42.09 7372 OH2 TIP Y 241-70.654 43.522-33. 572 1.00 41. 35 7373 OH2 TIP Y 248-50.282 52.448-68. 271 1.00 40.45 7374 OH2 TIP Y 281-45.209 55.693-41. 607 1.00 41.29 7375 OH2 TIP Y 293-50.408 41.781-56. 516 1.00 47.83 7376 OH2 TIP Y 310-55. 731 40.217-32. 931 1.00 53.52 7377 OH2 TIP Y 328-64.479 60.079-46. 509 1.00 41.96 1 2 3 4 5 6 7 8 9 10 7378 OH2 TIP Y 329-40.132 37.018-40. 659 1. 00 51. 40 7379 OH2 TIP Y 330-47.023 31.623-44. 138 1.00 52.41 7380 OH2 TIP Y 333-46.303 40.380-52. 431 1.00 41.99 7381 OH2 TIP Y 347-58.985 50.426-61. 195 1.00 41. 19 7382 OH2 TIP Y 350-71.060 58.834-50. 857 1. 00 43. 76 7383 OH2 TIP Y 352-66.832 61.960-46. 648 1.00 45.11 7384 OH2 TIP Y 360-53.002 46.421-56. 583 1.00 44. 40 7385 OH2 TIP Y 375-32.439 43.675-45. 192 1.00 52.29 7386 OH2 TIP Y 379-52.486 43.407-55. 602 1.00 51.62 7387 OH2 TIP Y 383-69.233 44.913-42. 779 1.00 53.05 7388 OH2 TIP Y 392-35.054 40. 133-45. 449 1.00 47. 06 7389 OH2 TIP Y 395-37. 177 37.566-43. 035 1.00 43. 86 7390 OH2 TIP Y 396-47.212 55.979-59. 067 1.00 58.65 7391 OH2 TIP Y 402-73.678 40.755-27. 354 1.00 55.67 7392 OH2 TIP Y 404-58.754 77.175-49. 316 1.00 46.90 7393 OH2 TIP Y 410-51.489 29.638-38. 071 1.00 54.06 7394 OH2 TIP Y 411-51.056 31.711-35. 244 1.00 43.38 7395 OH2 TIP Y 420-63.567 36.523-42. 291 1.00 46.21 7396 OH2 TIP Y 425-59.474 38.027-35. 409 1.00 54.67 7397 OH2 TIP Y 432-67.776 44.195-32. 492 1.00 49. 13 7398 OH2 TIP Y 433-60.707 35.871-45. 133 1.00 49. 33 7399 OH2 TIP Y 436-42.192 34. 568-37. 316 1.00 55.20 7400 OH2 TIP Y 440-44.021 60.656-56. 440 1.00 53.01 7401 OH2 TIP Y 444-40. 035 42.327-54. 102 1.00 52. 84 7402 OH2 TIP Y 449-69.359 39.722-40. 449 1. 00 45. 44 7403 OH2 TIP Y 454-42.406 54.590-51. 506 1.00 48.94 7404 OH2 TIP Y 468-47.006 59. 056-58.409 1.00 49.36 7405 OH2 TIP Y 479-63.388 33.419-40. 963 1.00 44.18 7406 OH2 TIP Y 491-53.237 39.109-55. 884 1.00 46.71 7407 OH2 TIP Y 495-52.226 49.154-59. 730 1.00 46.08 7408 OH2 TIP Y 500-59.269 33.882-45. 895 1.00 55.01 7409 OH2 TIP Y 531-63.282 55.156-60. 362 1.00 46.25 7410 OH2 TIP Y 535-69.668 50. 849-55.132 1.00 45. 84 2 3 4 5 6 7 8 9 10 7411 OH2 TIP Y 536-47.982 28.460-42. 352 1.00 51. 61 7412 OH2 TIP Y 541-67.186 51.130-42. 036 1.00 52.40 7413 OH2 TIP Y 546-68.115 53.087-54. 368 1. 00 45.63 7414 OH2 TIP Y 569-70. 975 60.015-56. 736 1.00 50.69 7415 OH2 TIP Y 570-50.171 50.980-66. 029 1.00 51.77 7416 OH2 TIP Y 581-68. 453 71. 944-49. 263 1.00 54.83 7417 OH2 TIP Y 593-44. 486 58.193-56. 545 1.00 55.59 7418 OH2 TIP Y 601-40.606 39. 074-35. 599 1.00 48.91 7419 OH2 TIP Z 5-38.200 45.717-25. 261 1.00 26.93 7420 OH2 TIP Z 8-53.051 60.239-20. 443 1.00 20.95 7421 OH2 TIP Z 9-44. 560 46.623-21. 912 1.00 23.18 7422 OH2 TIP Z 11-55.546 61.351-21. 108 1. 00 21.80 7423 OH2 TIP Z 13-36.658 61.636-14. 882 1. 00 19. 55 7424 OH2 TIP Z 19-67.882 64.243-30. 528 1.00 47.82 7425 OH2 TIP Z 20-42.004 42.061-26. 174 1.00 28.04 7426 OH2 TIP Z 21-54.983 61.740-37. 865 1.00 22.15 7427 OH2 TIP Z 37-56.415 64.235-23. 200 1.00 24.13 7428 OH2 TIP Z 38-36.767 62.676-23. 496 1.00 26.52 7429 OH2 TIP Z 41-63.236 65.052-14. 109 1.00 34. 35 7430 OH2 TIP Z 45-52.475 42.837-23. 296 1.00 25.15 7431 OH2 TIP Z 52-37.782 64.758-21. 883 1. 00 28. 25 7432 OH2 TIP Z 53-33.174 68.578-18. 772 1.00 30.13 7433 OH2 TIP Z 60-64.623 67. 048-22. 343 1.00 23.79 7434 OH2 TIP Z 72-35.635 67.460-18. 647 1.00 27.87 7435 OH2 TIP Z 73-50. 263 47.517-16. 918 1.00 28.11 7436 OH2 TIP Z 75-66.020 74.913-20. 105 1.00 41. 24 7437 OH2 TIP Z 76-37.426 69.353-17. 960 1.00 33.85 7438 OH2 TIP Z 80-31.415 78.034-17. 302 1.00 33.39 7439 OH2 TIP Z 102-48.740 55. 181-34. 338 1.00 27.67 7440 OH2 TIP Z 108-34.239 50.613-16. 133 1.00 35.13 7441 OH2 TIP Z 112-43.751 45.443-15. 996 1.00 37.66 7442 OH2 TIP Z 116-34. 322 51.399-25. 778 1. 00 23.68 7443 OH2 TIP Z 128-43.017 56.766-10. 752 1.00 33.58 1 2 3 4 5 6 7 8 9 10 7444 OH2 TIP Z 133-58.226 48.744-19. 539 1.00 33. 68 7445 OH2 TIP Z 138-30.205 68.855-15. 483 1. 00 31.12 7446 OH2 TIP Z 140-41. 706 71.983-12. 392 1.00 39.86 7447 OH2 TIP Z 146-57.911 54.895-17. 012 1.00 37.69 7448 OH2 TIP Z 148-45. 614 48.722-11. 159 1.00 40.26 7449 OH2 TIP Z 152-64.954 52.558-29. 543 1. 00 43.30 7450 OH2 TIP Z 157-46.272 39.966-23. 017 1.00 45.94 7451 OH2 TIP Z 161-67.597 59.753-28. 850 1.00 35.80 7452 OH2 TIP Z 163-61.339 54.330-18. 744 1.00 44.04 7453 OH2 TIP Z 164-59.989 71.400-14. 357 1.00 45.04 7454 OH2 TIP Z 166-67.364 72.057-42. 470 1. 00 55. 53 7455 OH2 TIP Z 168-32.701 49.582-19. 280 1.00 51.49 7456 OH2 TIP Z 169-48.765 71.730-19. 699 1.00 34.28 7457 OH2 TIP Z 171-36.605 46.835-27. 049 1.00 43.61 7458 OH2 TIP Z 172-68.374 59.599-22. 440 1.00 44.45 7459 OH2 TIP Z 174-68.271 73.051-30. 563 1.00 43.27 7460 OH2 TIP Z 178-45.019 43.195-16. 629 1.00 41.33 7461 OH2 TIP Z 181-48.780 49.774-13. 091 1.00 44.80 7462 OH2 TIP Z 184-30. 479 56.969-17. 264 1.00 59.20 7463 OH2 TIP Z 192-40.482 41.275-20. 596 1.00 48.61 7464 OH2 TIP Z 205-34.116 60.659-19. 990 1.00 28.72 7465 OH2 TIP Z 208-37. 003 72.578-11. 079 1.00 29.56 7466 OH2 TIP Z 211-57.216 51.605-32. 309 1.00 32.22 7467 OH2 TIP Z 218-60.630 70.860-16. 845 1.00 40.79 7468 OH2 TIP Z 219-51.111 72.137-29. 131 1. 00 51. 45 7469 OH2 TIP Z 224-68.983 67.562-35. 168 1.00 46.32 7470 OH2 TIP Z 233-28.948 58. 387-23. 906 1.00 38.76 7471 OH2 TIP Z 235-53. 880 52.078-12. 269 1. 00 39.79 7472 OH2 TIP Z 240-43. 034 39.716-24. 661 1.00 45.76 7473 OH2 TIP Z 243-66.073 61.075-37. 416 1.00 32.44 7474 OH2 TIP Z 245-39. 549 41.502-23. 322 1.00 44.21 7475 OH2 TIP Z 247-36.708 72.215-18. 736 1.00 36.71 7476 OH2 TIP Z 250-32. 735 58.234-19. 028 1.00 42. 12 1 2 3 4 5 6 7 8 9 10 7477 OH2 TIP Z 252-66.573 65. 324-18. 467 1.00 38.53 7478 OH2 TIP Z 253-64.563 53.681-27. 006 1.00 48.26 7479 OH2 TIP Z 256-36.203 45. 302-23. 600 1.00 55.07 7480 OH2 TIP Z 284-48.162 41.477-20. 799 1.00 47. 28 7481 OH2 TIP Z 286-45. 659 56. 395-10. 523 1.00 54.00 7482 OH2 TIP Z 294-67.328 62.950-21. 732 1.00 38. 57 7483 OH2 TIP Z 297-51.867 74.409-28. 316 1.00 52.55 7484 OH2 TIP Z 301-34.098 47.501-25. 634 1.00 50.36 7485 OH2 TIP Z 303-29.461 55.113-19. 453 1.00 55.67 7486 OH2 TIP Z 324-46. 813 73.168-23. 574 1. 00 48. 84 7487 OH2 TIP Z 327-60.134 76.287-21. 449 1.00 40.59 7488 OH2 TIP Z 335-45. 453 68. 629-12. 885 1. 00 42.17 7489 OH2 TIP Z 336-52.267 42. 372-20. 362 1.00 50.25 7490 OH2 TIP Z 337-63. 393 51.423-26. 444 1. 00 47. 11 7491 OH2 TIP Z 344-43.588 71.202-14. 708 1.00 37.79 7492 OH2 TIP Z 346-57. 178 72.204-27. 481 1.00 38. 34 7493 OH2 TIP Z 374-48.739 45. 365-15. 118 1.00 48.05 7494 OH2 TIP Z 376-62.900 80.034-30. 466 1.00 49.47 7495 OH2 TIP Z 381-65.758 51.476-24. 695 1.00 49.06 7496 OH2 TIP Z 393-64.269 59. 744-16. 034 1.00 50. 13 7497 OH2 TIP Z 397-55. 399 53. 278-15. 266 1.00 42.46 7498 OH2 TIP Z 418-68.431 61.422-31. 127 1.00 56.79 7499 OH2 TIP Z 422-27.543 58.108-27. 480 1.00 48.83 7500 OH2 TIP Z 423-40.463 65. 358-10. 535 1.00 38.87 7501 OH2 TIP Z 438-54.834 50. 956-14. 559 1.00 53.86 7502 OH2 TIP Z 445-58.889 50.360-17. 762 1.00 58.16 7503 OH2 TIP Z 451-67.608 68.165-18. 136 1.00 44.19 7504 OH2 TIP Z 460-46.317 78.109-31. 722 1.00 46.26 7505 OH2 TIP Z 464-31.207 54.770-15. 409 1.00 52.76 7506 OH2 TIP Z 481-62.855 79.166-39. 877 1. 00 54.55 7507 OH2 TIP Z 483-46.534 51. 307-9. 660 1.00 49. 26 7508 OH2 TIP Z 494-51.325 62. 604-12. 405 1.00 49.04 7509 OH2 TIP Z 499-65.213 62.852-15. 041 1.00 47. 36 1 2 3 4 5 6 7 8 9 10 7510 OH2 TIP Z 509-64.491 67. 215-12. 208 1.00 50.08 7511 OH2 TIP Z 516-37.914 44.240-22. 059 1.00 51.15 7512 OH2 TIP Z 528-65.807 54.861-35. 629 1.00 45.88 7513 OH2 TIP Z 534-35.488 48.131-14. 876 1.00 52.69 7514 OH2 TIP Z 550-69.472 56.535-32. 418 1. 00 52.53 7515 OH2 TIP Z 557-52. 548 46. 803-17. 747 1.00 52.66 7516 OH2 TIP Z 572-48.863 76.498-27. 131 1.00 55. 29 7517 OH2 TIP Z 575-51.910 43. 997-18. 355 1.00 54.09 7518 OH2 TIP Z 590-62.735 78. 055-19. 574 1.00 55.25 7519 OH2 TIP Z 604-67.529 62. 794-34. 955 1. 00 46.32 7520 OH2 TIP Z 606-58.457 70. 015-11. 076 1.00 54.41 7521 OH2 TIP Z 617-68. 369 57. 932-34. 937 1. 00 51. 47 [0208] Table 2 provides the atomic coordinates of the three-dimensional structure of hNeutokine-alpha. Specifically, the above coordinates comprise the residues 141-285 of hNeutrokine-alpha in crystal form. Moreover, the entire set of coordinates listed in Table 2 comprise the hNeutrokine-alpha protein in crystalline form as a dimer of trimers. The coordinates listed in Table 2 further comprise The following provides a description of the columns listed in above Table 2. The coordinates listed in Table 2 are used in a standard PDB file format, a described in http://www. rcsb. org/pdb/docs/format/pdbguide2. 2/guide2. 2 frame. html. The set of atomic coordinates of Table 2, or equivalent thereof, has been deposited into and is available from the Protein Data Bank: I. D. No.: 1 KXG. (H. M. Berman, et al., The Protein Data Bank. Nucleic Acids Research, 28 pp. 235-242 (2000)).

[0209] Column 1 indicates the atom number of each atom listed in coordinates of human Neutrokine-alpha. The atoms are numbered numerically from 1-7521.

[0210] Column 2 indicates the atom name, according to standard nomenclature for Protein Data Bank files. The following Table 3 provides the standard information regarding the atom names in column 2 of Table 2.

Table 3. Atom types. Atom Name Type of Atom C Carbonyl carbon of peptide bond N Nitrogen of peptide bond O Oxygen of peptide bond CA Alpha carbon CB Beta carbon CG Gamma carbon CD Delta carbon CE Epsilon carbon NA Alpha nitrogen NB Beta nitrogen NG Gamma nitrogen ND Delta nitrogen DE Epsilon nitrogen OA Alpha oxygen OB Beta oxygen OD Delta oxygen OE Epsilon oxygen OH Tyrosine hydroxyl oxygen OH2 Oxygen of water molecule OXT Terminal oxygen of peptide chain MG Magnesium ion [0211] In addition, when the residue type is CIT (see column 3, infra), the atom names Cl, C2, C3, C4, C5, C6, 01, 02,03, 04, 05, 06, and 07 refer to non- hydrogen atoms that comprise a citrate molecule. When the residue type is DIO (see column 3, infra), the atom names Cl, C2, C1', C2', 01, and 01'refer to the non-hydrogen atoms comprise that a dioxane molecule.

[0212] Column 3 indicates the residue type according to standard nomenclature for Protein Data Bank files. Additionally, MG indicates a magnesium ion; CIT indicates a citrate molecule; TIP indicates a water molecule; DIO indicates a dioxane molecule.

[0213] Column 4 indicates the fragment identification. The letter A indicates protein subunit A. The letter B indicates protein subunit B. The letter C indicates protein subunit C. The letter D indicates protein subunit D. The letter E indicates protein subunit E. The letter F indicates protein subunit F. One trimer of hNeutrokine-alpha comprises subunits A, B, and C; a second trimer comprises subunits D, E, and F. As described above, each trimer comprises three monomers, or subunits. As is apparent, each monomer of hNeutrokine-alpha is represented by one of subunits A-F. The letters G and H indicate Magnesium or Water atoms. The letter I indicates citrate atoms. The letter K indicates dioxane atoms. The letter U, V, W, X, Y and Z indicate water atoms.

[0214] Column 5 indicates the residue number of a particular atom. For atoms part of the protein, the residue number is number of the amino acid residue to which the atom belongs, wherein the number of the amino acid residue is numbered according to standard numbering of Neutrokine-alpha peptide numbering.

[0215] Column 6 indicates the x-coordinate in three dimensional space. Column 7 indicates the y-coordinate in three dimensional space. Column 8 indicates the z-coordinate in three dimensional space. The units of each coordinate is angstroms.

[0216] Column 9 indicates the occupancy. For all atoms in Table 1, the occupancy value is 1. Column 10 specifies the temperature factor.

Table 4 Full Length Amino Acid Sequence of Human Neutrokine-alpha 61 ltwsfyqva alqgdlaslr aelqghhaek lpagagapka gleeapavta glkifeppap 121 gegnssqnsr nkravqgpee tvtqdclqli adsetptiqk gsytfvpwll sfkrgsalee 181 kenkilvket gyffiygqvl ytdktyamgh liqrkkvhvf gdelslvtlf rciqnmpetl 241 pnnscysagi akleegdelq laiprenaqi sldgdvtffg alkll Table 5 Amino Acid Sequence of Soluble Human Neutrokine-alpha 141 tvtqdclqli adsetptiqk gsytfvpwll sfkrgsalee 181 kenkilvket gyffiygqvl ytdktyamgh liqrkkvhvf gdelslvtlf rciqnmpetl 241 pnnscysagi akleegdelq laiprenaqi sldgdvtffg alkll TABLE 6. Energy-minimized Structure of Neutrokine-alpha monomer.

1 N VAL E 142 2.070-28. 495-18.257 1.00 0.00 2 CA VAL E 142 0.713-28. 363-18.753 1.00 0.00 3 C VAL E 142 0.452-26. 957-19.217 1.00 0.00 4 O VAL E 142 1.178-26. 042-18. 861 1.00 0.00 5 CB VAL E 142-0.298-28. 771-17.660 1.00 0.00 6 CG1 VAL E 142-1.739-28. 727-18.205 1.00 0.00 7 CG2 VAL E 142 0.008-30. 197-17.163 1.00 0.00 8 N THR E 143-0.608-26. 791-20.031 1.00 0.00 9 CA THR E 143-0.942-25. 454-20.486 1. 00 0.00 10 C THR E 143-2.427-25. 239-20.400 1.00 0.00 11 O THR E 143-3.163-26. 143-20.041 1.00 0.00 12 CB THR E 143-0.451-25. 216-21.928 1.00 0.00 13 OG1 THR E 143-1.007-26. 198-22.810 1.00 0.00 14 CG2 THR E 143 1.085-25. 286-21.977 1.00 0.00 15 N GLN E 144-2.863-24. 011-20.734 1.00 0.00 16 CA GLN E 144-4.279-23. 714-20.640 1.00 0.00 17 C GLN E 144-4.871-23. 691-22.017 1.00 0.00 18 O GLN E 144-4.582-22. 791-22.790 1.00 0.00 19 CB GLN E 144-4.460-22. 346-19.956 1.00 0.00 20 CG GLN E 144-3.696-22. 334-18.617 1.00 0.00 21 CD GLN E 144-3.859-20. 993-17.959 1.00 0.00 22 OE1 GLN E 144-2.904-20. 238-17.881 1.00 0.00 23 NE2 GLN E 144-5.079-20. 693-17.475 1.00 0.00 24 N ASP E 145-5.714-24. 696-22.320 1.00 0.00 25 CA ASP E 145-6.343-24. 711-23.628 1.00 0.00 26 C ASP E 145-7.271-23. 540-23.772 1.00 0. 00 27 O ASP E 145-7.804-23. 060-22. 785 1.00 0.00 28 CB ASP E 145-7.126-26. 019-23.854 1.00 0.00 29 CG ASP E 145-6.221-27. 217-23.937 1.00 0.00 30 OD1 ASP E 145-4.975-27. 039-24.011 1.00 0.00 31 OD2 ASP E 145-6.761-28. 355-23.922 1.00 0.00 32 N CYS E 146-7.452-23. 073-25.021 1.00 0.00 33 CA CYS E 146-8.322-21. 929-25.217 1.00 0.00 34 C CYS E 146-8.802-21. 859-26.639 1.00 0.00 35 O CYS E 146-8.309-22. 575-27.496 1.00 0.00 36 CB CYS E 146-7.623-20. 619-24. 800 1.00 0.00 37 SG CYS E 146-6.083-20. 415-25.749 1.00 0.00 38 N LEU E 147-9.784-20. 971-26.876 1.00 0.00 39 CA LEU E 147-'10. 280-20.820-28. 228 1.00 0.00 40 C LEU E 147-10.839-19. 436-28.394 1.00 0.00 41 O LEU E 147-11. 443-18.901-27. 477 1.00 0.00 42 CB LEU E 147-11.341-21. 903-28.516 1.00 0.00 43 CG LEU E 147-11.620-22. 025-30.029 1.00 0.00 44 CD1 LEU E 147-12. 272-23. 389-30.325 1.00 0.00 45 CD2 LEU E 147-12.552-20. 887-30.494 1.00 0.00 46 N GLN E 148-10.620-18. 852-29.586 1.00 0.00 47 CA GLN E 148-11.133-17. 517-29.809 1.00 0.00 48 C GLN E 148-11.894-17. 461-31.102 1.00 0.00 49 O GLN E 148-11.538-18. 134-32.057 1.00 0.00 50 CB GLN E 148-9.962-16. 519-29.804 1.00 0.00 51 CG GLN E 148-10.501-15. 078-29.736 1.00 0.00 52 CD GLN E 148-9.421-14. 159-29.229 1.00 0.00 53 OE1 GLN E 148-8.925-13. 338-29.983 1.00 0.00 54 NE2 GLN E 148-9.056-14. 287-27.940 1.00 0.00 55 N LEU E 149-12. 963-16. 644-31.104 1.00 0.00 56 CA LEU E 149-13.738-16. 500-32.320 1.00 0.00 57 C LEU E 149-13.939-15. 044-32.620 1.00 0.00 58 O LEU E 149-13.784-14. 203-31.749 1.00 0.00 59 CB LEU E 149-15. 101-17.208-32. 210 1.00 0.00 60 CG LEU E 149-14.908-18. 731-32.070 1.00 0.00 61 CD1 LEU E 149-16. 288-19.393-31. 896 1.00 0.00 62 CD2 LEU E 149-14.201-19. 314-33.310 1.00 0.00 63 N ILE E 150-14.282-14. 756-33.888 1.00 0.00 64 CA ILE E 150-14. 435-13.365-34. 277 1.00 0.00 65 C ILE E 150-15.553-13. 210-35.267 1.00 0.00 66 O ILE E 150-15.952-14. 173-35. 903 1.00 0.00 67 CB ILE E 150-13.117-12. 803-34.847 1.00 0. 00 68 CG1 ILE E 150-12.577-13. 747-35.941 1.00 0.00 69 CG2 ILE E 150-12.081-12. 657-33.715 1.00 0.00 70 CD1 ILE E 150-11.330-13. 131-36.602 1.00 0.00 71 N ALA E 151-16.071-11. 971-35.376 1.00 0.00 72 CA ALA E 151-17.203-11. 764-36.261 1.00 0.00 73 C ALA E 151-16.833-11. 979-37.701 1.00 0.00 74 O ALA E 151-15.767-11. 567-38.130 1.00 0.00 75 CB ALA E 151-17.805-10. 361-36.066 1.00 0.00 76 N ASP E 152-17.739-12. 647-38. 439 1.00 0.00 77 CA ASP E 152-17.485-12. 868-39.850 1.00 0.00 78 C ASP E 152-18. 037-11. 685-40. 591 1.00 0.00 79 0 ASP E 152-19.234-11. 613-40.822 1.00 0.00 80 CB ASP E 152-18.189-14. 160-40.314 1.00 0.00 81 CG ASP E 152-17. 671-14. 592-41.657 1.00 0.00 82 OD1 ASP E 152-17.517-13. 720-42.555 1.00 0.00 83 OD2 ASP E 152-17.408-15. 813-41.821 1.00 0.00 84 N SER E 153-17.136-10. 757-40.966 1.00 0.00 85 CA SER E 153-17.578-9. 568-41. 675 1.00 0.00 86 C SER E 153-18.321-9. 941-42.929 1.00 0.00 87 0 SER E 153-19.424-9. 460-43.139 1.00 0.00 88 CB SER E 153-16. 342-8. 714-42.024 1.00 0.00 89 OG SER E 153-15.393-9. 479-42.776 1.00 0.00 90 N GLU E 154-17.710-10. 812-43.757 1.00 0.00 91 CA GLU E 154-18.376-11. 173-44.996 1.00 0.00 92 C GLU E 154-19.366-12. 294-44.810 1.00 0.00 93 O GLU E 154-19.411-13. 215-45.612 1.00 0.00 94 CB GLU E 154-17.361-11. 460-46.120 1.00 0.00 95 CG GLU E 154-16.407-12. 594-45.698 1.00 0.00 96 CD GLU E 154-15.170-12. 536-46.546 1.00 0.00 97 OE1 GLU E 154-15.231-13. 004-47.714 1.00 0.00 98 OE2 GLU E 154-14.132-12. 033-46.040 1.00 0.00 99 N THR E 155-20.179-12. 201-43.739 1.00 0.00 100 CA THR E 155-21.214-13. 201-43.539 1.00 0.00 101 C THR E 155-22.367-12. 582-42.799 1.00 0.00 102 O THR E 155-22. 134-11.908-41. 809 1.00 0.00 103 CB THR E 155-20.684-14. 448-42.799 1.00 0.00 104 OG1 THR E 155-19.753-15. 138-43. 638 1.00 0. 00.

105 CG2 THR E 155-21.843-15. 415-42.497 1.00 0.00 106 N PRO E 156-23.615-12. 798-43.270 1.00 0.00 107 CA PRO E 156-24.759-12. 233-42. 586 1.00 0.00 108 C PRO E 156-25. 000-12.924-41. 274 1.00 0.00 109 O PRO E 156-24.432-13. 975-41.023 1.00 0.00 110 CB PRO E 156-25.913-12. 557-43. 556 1.00 0.00 111 CG PRO E 156-25.356-13. 499-44. 648 1.00 0.00 112 CD PRO E 156-23.829-13. 593-44. 462 1.00 0.00 113 N THR E 157-25.849-12. 310-40. 426 1.00 0.00 114 CA THR E 157-26.111-12. 921-39.133 1.00 0.00 115 C THR E 157-27.070-14. 070-39.258 1.00 0.00 116 O THR E 157-27.729-14. 215-40.275 1.00 0.00 117 CB THR E 157-26. 648-11. 882-38.128 1.00 0.00 118 OG1 THR E 157-27.823-11. 249-38.647 1.00 0.00 119 CG2 THR E 157-25.566-10. 826-37.847 1.00 0.00 120 N ILE E 158-27.131-14. 895-38.197 1.00 0.00 121 CA ILE E 158-28.007-16. 051-38.252 1.00 0.00 122 C ILE E 158-29.269-15. 770-37.487 1.00 0.00 123 0 ILE E 158-29. 247-15.686-36. 269 1.00 0.00 124 CB ILE E 158-27.269-17. 268-37.658 1.00 0.00 125 CG1 ILE E 158-25.948-17. 498-38.421 1.00 0.00 126 CG2 ILE E 158-28.164-18. 516-37.772 1.00 0.00 127 CD1 ILE E 158-25. 112-18. 581-37.714 1.00 0.00 128 N GLN E 159-30.386-15. 635-38.223 1.00 0.00 129 CA GLN E 159-31.645-15. 429-37.536 1.00 0.00 130 C GLN E 159-32.208-16. 756-37.113 1.00 0.00 131 O GLN E 159-32.444-17. 611-37.951 1.00 0.00 132 CB GLN E 159-32.638-14. 679-38.446 1.00 0.00 133 CG GLN E 159-32. 096-13. 281-38.806 1.00 0.00 134 CD GLN E 159-31.751-12. 520-37.556 1.00 0.00 135 OE1 GLN E 159-32.601-12. 328-36.702 1.00 0.00 136 NE2 GLN E 159-30.483-12. 088-37.443 1.00 0.00 137 N LYS E 160-32.422-16. 924-35.795 1.00 0.00 138 CA LYS E 160-32.993-18. 174-35.332 1.00 0.00 139 C LYS E 160-33.609-18. 004-33.971 1.00 0.00 140 O LYS E 160-32.975-17. 449-33.088 1.00 0.00 141 CB LYS E 160-31.914-19. 272-35.302 1.00 0.00 142 CG LYS E 160-32.575-20. 628-34.987 1.00 0.00 143 CD LYS E 160-31.526-21. 755-34.994 1.00 0.00 144 CE LYS E 160-31.121-22. 097-36.440 1.00 0.00 145 NZ LYS E 160-30.340-23. 344-36.460 1.00 0.00 146 N GLY E 161-34.860-18. 492-33.836 1.00 0.00 147 CA GLY E 161-35.564-18. 372-32.571 1.00 0.00 148 C GLY E 161-35.782-16. 933-32.199 1.00 0.00 149 O GLY E 161-35.798-16. 614-31.021 1.00 0.00 150 N SER E 162-35.938-16. 064-33.219 1.00 0.00 151 CA SER E 162-36. 067-14.642-32. 948 1.00 0.00 152 C SER E 162-34.797-14. 081-32.363 1.00 0.00 153 O SER E 162-34. 833-13.113-31. 620 1.00 0.00 154 CB SER E 162-37. 306-14.323-32. 088 1.00 0.00 155 OG SER E 162-38.486-14. 837-32.713 1.00 0.00 156 N TYR E 163-33.659-14. 715-32.710 1.00 0.00 157 CA TYR E 163-32.388-14. 210-32.227 1.00 0.00 158 C TYR E 163-31.498-13. 898-33.393 1.00 0.00 159 O TYR E 163-31.669-14. 443-34.473 1.00 0.00 160 CB TYR E 163-31.660-15. 260-31.368 1.00 0.00 161 CG TYR E 163-32.306-15. 392-29.995 1.00 0.00 162 CD1 TYR E 163-33.255-16. 390, -29.761 1.00 0.00 163 CD2 TYR E 163-31.939-14. 518-28.969 1.00 0.00 164 CE1 TYR E 163-33.830-16. 520-28.494 1.00 0.00 165 CE2 TYR E 163-32.512-14. 653-27.701 1.00 0.00 166 CZ TYR E 163-33.457-15. 653-27.463 1.00 0.00 167 OH TYR E 163-34.026-15. 787-26.201 1.00 0.00 168 N THR E 164-30.527-13. 002-33.145 1.00 0.00 169 CA THR E 164-29.539-12. 747-34.173 1.00 0.00 170 C THR E 164-28.247-13. 363-33.719 1.00 0.00 171 O THR E 164-27. 796-13.098-32. 615 1.00 0.00 172 CB THR E 164-29.396-11. 233-34.417 1.00 0.00 173 OG1 THR E 164-30.651-10. 713-34.871 1.00 0.00 174 CG2 THR E 164-28.328-10. 977-35.495 1.00 0.00 175 N PHE E 165-27.658-14. 207-34.585 1.00 0.00 176 CA PHE E 165-26.421-14. 850-34.184 1.00 0.00 177 C PHE E 165-25.269-14. 344-35.001 1.00 0.00 178 O PHE E 165-25.424-14. 054-36.177 1.00 0.00 179 CB PHE E 165-26.546-16. 381-34. 280 1.00 0.00 180 CG PHE E 165-27.538-16. 870-33.229 1.00 0.00 181 CD1 PHE E 165-28. 904-16. 936-33. 518 1.00 0.00 182 CD2 PHE E 165-27.073-17. 254-31.968 1.00 0.00 183 CE1 PHE E 165-29.804-17. 382-32.547 1.00 0.00 184 CE2 PHE E 165-27.971-17. 703-30.996 1.00 0.00 185 CZ PHE E 165-29.336-17. 766-31.287 1.00 0.00 186 N VAL E 166-24.097-14. 226-34.349 1.00 0.00 187 CA VAL E 166-22.950-13. 700-35.066 1.00 0.00 188 C VAL E 166-22.260-14. 798-35.824 1.00 0.00 189 O VAL E 166-21.907-15. 800-35.223 1.00 0.00 190 CB VAL E 166-21.966-13. 017-34.093 1.00 0.00 191 CG1 VAL E 166-20.731-12. 496-34.853 1.00 0.00 192 CG2 VAL E 166-22. 668-11. 846-33.377 1.00 0.00 193 N PRO E 167-22.047-14. 617-37.145 1.00 0.00 194 CA PRO E 167-21.292-15. 600-37.893 1.00 0.00 195 C PRO E 167-19.890-15. 580-37.356 1.00 0.00 196 O PRO E 167-19.190-14. 592-37.508 1.00 0.00 197 CB PRO E 167-21.329-15. 017-39.320 1.00 0.00 198 CG PRO E 167-21.962-13. 610-39.240 1.00 0.00 199 CD PRO E 167-22.518-13. 423-37.816 1.00 0.00 200 N TRP E 168-19.482-16. 680-36.702 1.00 0.00 201 CA TRP E 168-18.171-16. 656-36.081 1.00 0.00 202 C TRP E 168-17.073-17. 106-36. 999 1. 00 0.00 203 O TRP E 168-17. 321-17. 635-38. 072 1.00 0.00 204 CB TRP E 168-18.179-17. 516-34.806 1.00 0.00 205 CG TRP E 168-18. 954-16.783-33. 754 1.00 0.00 206 CD1 TRP E 168-20.089-17. 186-33.157 1.00 0.00 207 CD2 TRP E 168-18.596-15. 442-33.177 1.00 0.00 208 NE1 TRP E 168-20.487-16. 282-32.298 1.00 0.00 209 CE2 TRP E 168-19.637-15. 236-32.283 1.00 0.00 210 CE3 TRP E 168-17.562-14. 531-33.368 1.00 0.00 211 CZ2 TRP E 168-19.710-14. 074-31.520 1.00 0.00 212 CZ3 TRP E 168-17. 635-13.364-32. 604 1.00 0.00 213 CH2 TRP E 168-18.681-13. 138-31.693 1.00 0.00 214 N LEU E 169-15.833-16. 878-36.532 1.00 0.00 215 CA LEU E 169-14. 686-17. 317-37.302 1.00 0.00 216 C LEU E 169-13. 606-17. 686-36. 328 1.00 0.00 217 O LEU E 169-13.400-16. 971-35.361 1.00 0.00 218 CB LEU E 169-14.189-16. 187-38. 224 1.00 0.00 219 CG LEU E 169-15.183-15. 960-39.380 1.00 0.00 220 CD1 LEU E 169-14.764-14. 723-40.198 1.00 0.00 221 CD2 LEU E 169-15.229-17. 198-40.300 1.00 0.00 222 N LEU E 170-12.923-18. 821-36. 571 1.00 0.00 223 CA LEU E 170-11.932-19. 252-35.605 1.00 0.00 224 C LEU E 170-10.737-18. 341-35.619 1.00 0.00 225 O LEU E 170-9.909-18. 428-36.511 1.00 0.00 226 CB LEU E 170-11.518-20. 718-35.843 1.00 0.00 227 CG LEU E 170-10.521-21. 166-34.752 1.00 0.00 228 CD1 LEU E 170-11.186-21. 080-33.366 1.00 0.00 229 CD2 LEU E 170-10.082-22. 619-35.013 1.00 0.00 230 N SER E 171-10. 661-17. 474-34.590 1.00 0.00 231 CA SER E 171-9.478-16. 649-34.436 1.00 0.00 232 C SER E 171-8.303-17. 556-34.198 1.00 0.00 233 O SER E 171-7.320-17. 475-34.917 1.00 0.00 234 CB SER E 171-9.682-15. 730-33.218 1.00 0.00 235 OG SER E 171-8.526-14. 907-33.032 1.00 0.00 236 N PHE E 172-8.432-18. 435-33.184 1.00 0.00 237 CA PHE E 172-7.375-19. 400-32.947 1.00 0.00 238 C PHE E 172-7.833-20. 470-31. 996 1.00 0.00 239 O PHE E 172-8. 882-20.353-31. 381 1.00 0.00 240 CB PHE E 172-6.081-18. 732-32.439 1.00 0.00 241 CG PHE E 172-6.331-17. 994-31. 126 1.00 0.00 242 CD1 PHE E 172-6.211-18. 673-29.910 1.00 0.00 243 CD2 PHE E 172-6.676-16. 639-31. 139 1.00 0.00 244 CE1 PHE E 172-6.420-17. 994-28.706 1.00 0.00 245 CE2 PHE E 172-6.870-15. 955-29.936 1.00 0.00 246 CZ PHE E 172-6.749-16. 636-28.721 1.00 0. 00 247 N LYS E 173-7.011-21. 529-31.885 1.00 0.00 248 CA LYS E 173-7.358-22. 599-30.972 1.00 0.00 249 C LYS E 173-6.124-23. 068-30.252 1.00 0.00 250 O LYS E 173-5.021-22. 915-30.754 1.00 0.00 251 CB LYS E 173-8.036-23. 750-31.741 1.00 0.00 252 CG LYS E 173-8.545-24. 830-30.765 1.00 0.00 253 CD LYS E 173-9.117-26. 002-31.581 1.00 0.00 254 CE LYS E 173-9.395-27. 195-30.648 1.00 0.00 255 NZ LYS E 173-9.820-28. 354-31.447 1.00 0.00 256 N ARG E 174-6.328-23. 632-29.047 1.00 0.00 257 CA ARG E 174-5.180-24. 057-28.270 1.00 0.00 258 C ARG E 174-5.564-25. 256-27. 453 1.00 0.00 259 O ARG E 174-6.513-25. 195-26.688 1.00 0.00 260 CB ARG E 174-4.694-22. 905-27.372 1.00 0.00 261 CG ARG E 174-3.308-23. 238-26.786 1.00 0.00 262 CD ARG E 174-2.778-22. 028-25.993 1.00 0.00 263 NE ARG E 174-1.477-22. 347-25.434 1.00 0.00 264 CZ ARG E 174-1.194-22. 107-24.185 1.00 0. 00 265 NH1 ARG E 174-2.060-21. 559-23.383 1.00 0.00 266 NH2 ARG E 174-0.019-22. 424-23.728 1.00 0.00 267 N GLY E 175-4.816-26. 360-27.634 1.00 0.00 268 CA GLY E 175-5.163-27. 572-26.914 1.00 0.00 269 C GLY E 175-6.343-28. 257-27.544 1.00 0.00 270 O GLY E 175-6. 609-28. 070-28.721 1.00 0.00 271 N SER E 176-7. 056-29.065-26. 736 1.00 0.00 272 CA SER E 176-8.187-29. 791-27.288 1.00 0.00 273 C SER E 176-9.361-29. 758-26. 350 1.00 0.00 274 O SER E 176-10.367-30. 393-26.626 1.00 0.00 275 CB SER E 176-7.770-31. 244-27.581 1.00 0.00 276 OG SER E 176-7.335-31. 875-26.372 1.00 0.00 277 N ALA E 177-9.227-29. 012-25.235 1.00 0.00 278 CA ALA E 177-10. 327-28. 921-24.289 1.00 0.00 279 C ALA E 177-11.499-28. 239-24.934 1.00 0.00 280 O ALA E 177-12.628-28. 645-24.711 1.00 0.00 281 CB ALA E 177-9.862-28. 102-23.072 1.00 0.00 282 N LEU E 178-11.225-27. 201-25.746 1.00 0.00 283 CA LEU E 178-12.331-26. 522-26.397 1.00 0.00 284 C LEU E 178-12.357-26. 822-27.870 1.00 0.00 285 O LEU E 178-11.412-27. 385-28.400 1.00 0.00 286 CB LEU E 178-12.218-25. 003-26.163 1.00 0.00 287 CG LEU E 178-12. 280-24. 703-24.651 1.00 0.00 288 CD1 LEU E 178-12.047-23. 199-24.407 1.00 0.00 289 CD2 LEU E 178-13.654-25. 115-24.082 1.00 0.00 290 N GLU E 179-13.474-26. 436-28.518 1.00 0.00 291 CA GLU E 179-13.594-26. 683-29.943 1.00 0.00 292 C GLU E 179-14.691-25. 837-30.526 1.00 0.00 293 O GLU E 179-15.538-25. 341-29.800 1.00 0.00 294 CB GLU E 179-13.933-28. 165-30.192 1.00 0.00 295 CG GLU E 179-12.650-28. 946-30.538 1.00 0.00 296 CD GLU E 179-12.941-30. 416-30.632 1.00 0.00 297 OE1 GLU E 179-13.850-30. 797-31.418 1.00 0.00 298 OE2 GLU E 179-12.257-31. 197-29.918 1.00 0.00 299 N GLU E 180-14. 675-25.671-31. 862 1.00 0.00 300 CA GLU E 180-15.775-24. 960-32.486 1.00 0.00 301 C GLU E 180-16.721-25. 961-33.090 1.00 0.00 302 O GLU E 180-16.290-27. 019-33.522 1.00 0.00 303 CB GLU E 180-15.263-23. 966-33.545 1.00 0.00 304 CG GLU E 180-16.419-23. 075-34.043 1.00 0.00 305 CD GLU E 180-15.910-21. 983-34.943 1.00 0.00 306 OE1 GLU E 180-15. 018-22. 264-35.788 1.00 0.00 307 OE2 GLU E 180-16.400-20. 831-34.800 1.00 0.00 308 N LYS E 181-18.027-25. 627-33.107 1.00 0.00 309 CA LYS E 181-18.981-26. 577-33.645 1.00 0.00 310 C LYS E 181-20.299-25. 906-33.892 1.00 0.00 311 O LYS E 181-20.996-25. 563-32.950 1.00 0.00 312 CB LYS E 181-19.167-27. 757-32.673 1.00 0.00 313 CG LYS E 181-20.057-28. 824-33.343 1.00 0.00 314 CD LYS E 181-20.403-29. 929-32.331 1.00 0.00 315 CE LYS E 181-21.354-30. 944-32.994 1.00 0.00 316 NZ LYS E 181-21.619-32. 050-32.061 1.00 0.00 317 N GLU E 182-20.632-25. 741-35.189 1.00 0.00 318 CA GLU E 182-21.923-25. 172-35.541 1.00 0.00 319 C GLU E 182-22.076-23. 798-34.950 1.00 0.00 320 0 GLU E 182-23.076-23. 503-34.315 1.00 0.00 321 CB GLU E 182-23. 065-26. 128-35.143 1.00 0.00 322 CG GLU E 182-22.802-27. 518-35.756 1.00 0.00 323 CD GLU E 182-23.869-28. 480-35.321 1.00 0.00 324 OE1 GLU E 182-23.828-28. 914-34.139 1.00 0.00 325 OE2 GLU E 182-24.742-28. 811-36.166 1.00 0.00 326 N ASN E 183-21. 043-22.957-35. 164 1.00 0.00 327 CA ASN E 183-21.067-21. 618-34.598 1.00 0.00 328 C ASN E 183-21.194-21. 651-33.098 1.00 0.00 329 O ASN E 183-21.924-20. 857-32.526 1.00 0.00 330 CB ASN E 183-22.176-20. 779-35.258 1.00 0.00 331 CG ASN E 183-21.805-19. 325-35.240 1.00 0.00 332 OD1 ASN E 183-22.502-18. 528-34.633 1.00 0.00 333 ND2 ASN E 183-20.698-18. 970-35.914 1.00 0.00 334 N LYS E 184-20.466-22. 595-32. 467 1.00 0.00 335 CA LYS E 184-20.547-22. 708-31.022 1.00 0.00 336 C LYS E 184-19.254-23. 210-30.443 1.00 0.00 337 O LYS E 184-18.359-23. 620-31.166 1.00 0.00 338 CB LYS E 184-21.676-23. 677-30.625 1.00 0.00 339 CG LYS E 184-23.054-23. 032-30.869 1.00 0.00 340 CD LYS E 184-24.155-23. 967-30.333 1.00 0.00 341 CE LYS E 184-24.154-25. 300-31.108 1.00 0.00 342 NZ LYS E 184-24.616-25. 085-32.488 1.00 0.00 343 N ILE E 185-19.165-23. 169-29.100 1.00 0.00 344 CA ILE E 185-17.954-23. 652-28.461 1.00 0.00 345 C ILE E 185-18.260-24. 948-27.768 1.00 0.00 346 O ILE E 185-18.942-24. 951-26.755 1.00 0.00 347 CB ILE E 185-17.424-22. 600-27.466 1.00 0.00 348 CG1 ILE E 185-17.186-21. 267-28.204 1.00 0.00 349 CG2 ILE E 185-16.092-23. 096-26.869 1.00 0.00 350 CD1 ILE E 185-16.797-20. 166-27.199 1.00 0.00 351 N LEU E 186-17.738-26. 055-28.330 1.00 0.00 352 CA LEU E 186-17.976-27. 341-27.700 1.00 0.00 353 C LEU E 186-17. 029-27.579-26. 556 1.00 0.00 354 O LEU E 186-15.851-27. 270-26.651 1.00 0.00 355 CB LEU E 186-17.860-28. 472-28.740 1.00 0.00 356 CG LEU E 186-18. 142-29.840-28. 089 1.00 0.00 357 CD1 LEU E 186-19.575-29. 880-27.520 1.00 0.00 358 CD2 LEU E 186-17.978-30. 947-29.149 1.00 0.00 359 N VAL E 187-17.573-28. 141-25.460 1.00 0.00 360 CA VAL E 187-16.726-28. 437-24.319 1.00 0.00 361 C VAL E 187-16.244-29. 854-24.446 1.00 0.00 362 O VAL E 187-16.993-30. 779-24.173 1.00 0.00 363 CB VAL E 187-17.514-28. 258-23.004 1.00 0.00 364 CG1 VAL E 187-16. 569-28. 466-21. 805 1.00 0.00 365 CG2 VAL E 187-18. 100-26. 836-22. 933 1.00 0.00 366 N LYS E 188-14.973-29. 998-24.864 1.00 0.00 367 CA LYS E 188-14.406-31. 328-24.991 1.00 0.00 368 C LYS E 188-13.964-31. 849-23.651 1.00 0.00 369 O LYS E 188-13.939-33. 054-23.458 1.00 0.00 370 CB LYS E 188-13.207-31. 282-25.961 1.00 0.00 371 CG LYS E 188-13.630-30. 637-27.297 1.00 0.00 372 CD LYS E 188-14.825-31. 395-27.910 1.00 0.00 373 CE LYS E 188-14.371-32. 769-28.443 1.00 0.00 374 NZ LYS E 188-14. 166-33.708-27. 330 1.00 0.00 375 N GLU E 189-13.625-30. 940-22.716 1.00 0.00 376 CA GLU E 189-13.189-31. 402-21.411 1.00 0.00 377 C GLU E 189-13.898-30. 659-20.315 1.00 0.00 378 0 GLU E 189-14.115-29. 463-20.426 1.00 0.00 379 CB GLU E 189-11.665-31. 232-21.273 1.00 0.00 380 CG GLU E 189-10.941-32. 153-22.275 1.00 0.00 381 CD GLU E 189-9.532-31. 682-22. 496 1.00 0. 00 382 OE1 GLU E 189-8.819-31. 438-21.485 1.00 0.00 383 OE2 GLU E 189-9.133-31. 549-23.683 1.00 0.00 384 N THR E 190-14.261-31. 395-19.247 1.00 0.00 385 CA THR E 190-14.913-30. 737-18.129 1.00 0.00 386 C THR E 190-13.910-29. 937-17.340 1.00 0.00 387 O THR E 190-12.717-30. 171-17.452 1.00 0.00 388 CB THR E 190-15.602-31. 786-17.232 1.00 0.00 389 OG1 THR E 190-16.441-32. 636-18.020 1.00 0.00 390 CG2 THR E 190-16.455-31. 091-16.154 1.00 0.00 391 N GLY E 191-14.406-28. 974-16.542 1.00 0.00 392 CA GLY E 191-13.488-28. 170-15.755 1.00 0.00 393 C GLY E 191-13.925-26. 732-15.728 1.00 0.00 394 O GLY E 191-14.977-26. 396-16.247 1.00 0.00 395 N TYR E 192-13. 094-25.872-15. 110 1.00 0.00 396 CA TYR E 192-13.448-24. 465-15.080 1.00 0.00 397 C TYR E 192-13.010-23. 773-16.340 1.00 0.00 398 O TYR E 192-12.107-24. 235-17.021 1.00 0.00 399 CB TYR E 192-12.830-23. 767-13. 855 1.00 0.00 400 CG TYR E 192-13.561-24. 219-12.597 1.00 0.00 401 CD1 TYR E 192-14.518-23. 385-12.013 1.00 0.00 402 CD2 TYR E 192-13.274-25. 464-12.032 1.00 0.00 403 CE1 TYR E 192-15.186-23. 797-10.857 1.00 0.00 404 CE2 TYR E 192-13.946-25. 874-10.878 1.00 0.00 405 CZ TYR E 192-14.900-25. 041-10. 288 1.00 0.00 406 OH TYR E 192-15.561-25. 448-9.135 1.00 0.00 407 N PHE E 193-13.679-22. 646-16.646 1.00 0.00 408 CA PHE E 193-13.327-21. 932-17.858 1.00 0.00 409 C PHE E 193-13.613-20. 466-17.710 1.00 0.00 410 O PHE E 193-14.603-20. 086-17.105 1.00 0.00 411 CB PHE E 193-14.157-22. 443-19.051 1.00 0.00 412 CG PHE E 193-13.794-23. 879-19.415 1.00 0.00 413 CD1 PHE E 193-14.497-24. 956-18.867 1.00 0.00 414 CD2 PHE E 193-12.747-24. 108-20.311 1.00 0.00 415 CE1 PHE E 193-14.125-26. 265-19.190 1.00 0.00 416 CE2 PHE E 193-12.396-25. 415-20.654 1.00 0.00 417 CZ PHE E 193-13.087-26. 495-20.097 1.00 0.00 418 N PHE E 194-12. 718-19.645-18. 289 1.00 0.00 419 CA PHE E 194-12.993-18. 224-18.317 1.00 0.00 420 C PHE E 194-13.657-17. 928-19.630 1.00 0.00 421 O PHE E 194-13. 110-18.254-20. 672 1.00 0.00 422 CB PHE E 194-11.699-17. 399-18.169 1.00 0.00 423 CG PHE E 194-12.020-15. 921-18.384 1.00 0.00 424 CD1 PHE E 194-12. 674-15.194-17. 386 1.00 0.00 425 CD2 PHE E 194-11.672-15. 298-19.586 1.00 0.00 426 CE1 PHE E 194-12.994-13. 850-17.594 1.00 0.00 427 CE2 PHE E 194-11. 989-13.953-19. 796 1.00 0.00 428 CZ PHE E 194-12. 647-13.230-18. 797 1.00 0.00 429 N ILE E 195-14.850-17. 309-19.571 1.00 0.00 430 CA ILE E 195-15.531-17. 001-20.815 1.00 0.00 431 C ILE E 195-15. 650-15.512-20. 998 1.00 0.00 432 O ILE E 195-15.512-14. 763-20.043 1.00 0.00 433 CB ILE E 195-16. 903-17.701-20. 865 1.00 0.00 434 CG1 ILE E 195-16.714-19. 204-20.573 1.00 0.00 435 CG2 ILE E 195-17.542-17. 519-22.258 1.00 0.00 436 CD1 ILE E 195-18.084-19. 891-20.418 1.00 0.00 437 N TYR E 196-15.893-15. 089-22.254 1.00 0.00 438 CA TYR E 196-15.976-13. 664-22.518 1.00 0.00 439 C TYR E 196-16.542-13. 421-23.891 1.00 0.00 440 O TYR E 196-16. 619-14.338-24. 694 1.00 0.00 441 CB TYR E 196-14.590-13. 001-22.392 1.00 0.00 442 CG TYR E 196-13.591-13. 696-23.313 1.00 0.00 443 CD1 TYR E 196-13.438-13. 260-24.632 1.00 0.00 444 CD2 TYR E 196-12.835-14. 771-22.838 1.00 0.00 445 CE1 TYR E 196-12. 529-13.902-25. 477 1.00 0.00 446 CE2 TYR E 196-11.920-15. 406-23.682 1.00 0.00 447 CZ TYR E 196-11.771-14. 975-25.003 1.00 0.00 448 OH TYR E 196-10.869-15. 615-25. 845 1.00 0.00 449 N GLY E 197-16.943-12. 162-24. 151 1.00 0.00 450 CA GLY E 197-17.513-11. 855-25.449 1.00 0.00 451 C GLY E 197-17. 768-10. 379-25.569 1.00 0.00 452 0 GLY E 197-18.014-9. 716-24.573 1.00 0.00 453 N GLN E 198-17.712-9. 867-26.813 1.00 0.00 454 CA GLN E 198-17.999-8. 458-27.000 1.00 0.00 455 C GLN E 198-18.765-8. 227-28.272 1.00 0.00 456 0 GLN E 198-18.592-8. 956-29.236 1.00 0.00 457 CB GLN E 198-16.677-7. 673-27.023 1.00 0.00 458 CG GLN E 198-16. 938-6.199-26. 656 1.00 0.00 459 CD GLN E 198-15.637-5. 437-26.626 1.00 0.00 460 OE1 GLN E 198-15.240-4. 967-25.571 1.00 0.00 461 NE2 GLN E 198-14.968-5. 298-27.786 1.00 0.00 462 N VAL E 199-19.631-7. 195-28.259 1.00 0.00 463 CA VAL E 199-20.442-6. 942-29.436 1.00 0.00 464 C VAL E 199-20.609-5. 462-29.631 1.00 0.00 465 0 VAL E 199-20.844-4. 739-28.676 1.00 0.00 466 CB VAL E 199-21.828-7. 607-29.307 1.00 0.00 467 CG1 VAL E 199-22.618-7. 413-30. 617 1.00 0.00 468 CG2 VAL E 199-21.698-9. 113-29.010 1.00 0.00 469 N LEU E 200-20.479-5. 017-30.895 1.00 0.00 470 CA LEU E 200-20.657-3. 601-31.156 1.00 0.00 471 C LEU E 200-22.035-3. 371-31.709 1.00 0.00 472 0 LEU E 200-22.284-3. 657-32.870 1.00 0.00 473 CB LEU E 200-19. 583-3.113-32. 148 1.00 0.00 474 CG LEU E 200-19. 806-1. 623-32. 479 1.00 0.00 475 CD1 LEU E 200-19.740-0. 766-31.198 1.00 0.00 476 CD2 LEU E 200-18.723-1. 157-33.469 1.00 0.00 477 N TYR E 201-22.930-2. 835-30.858 1.00 0.00 478 CA TYR E 201-24.264-2. 537-31.346 1.00 0.00 479 C TYR E 201-24.273-1. 251-32.124 1.00 0.00 480 0 TYR E 201-23.403-0. 416-31.931 1.00 0.00 481 CB TYR E 201-25.289-2. 541-30.197 1.00 0.00 482 CG TYR E 201-25.287-3. 942-29.598 1.00 0.00 483 CD1 TYR E 201-24.378-4. 253-28.584 1.00 0.00 484 CD2 TYR E 201-26.176-4. 911-30.070 1.00 0.00 485 CE1 TYR E 201-24.273-5. 569-28.128 1.00 0.00 486 CE2 TYR E 201-26.071-6. 226-29.609 1.00 0.00 487 CZ-TYR E 201-25. 084-6. 565-28. 678 1.00 0.00 488 OH TYRE 201-24.904-7. 892-28.307 1.00 0.00 489 N THR E 202-25.259-1. 110-33. 031 1.00 0.00 490 CA THR E 202-25.255 0.057-33. 896 1.00 0.00 491 C THR E 202-26.649 0.575-34. 122 1.00 0.00 492 O THR E 202-26.806 1.614-34. 744 1.00 0.00 493 CB THR E 202-24.576-0. 292-35.237 1.00 0.00 494 OG1 THR E 202-25.198-1. 446-35. 815 1.00 0.00 495 CG2 THR E 202-23.079-0. 577-35.019 1.00 0.00 496 N ASP E 203-27.673-0. 136-33.612 1.00 0.00 497 CA ASP E 203-29.015 0.405-33. 734 1.00 0.00 498 C ASP E 203-29.280 1.402-32. 638 1.00 0.00 499 O ASP E 203-28.627 1.362-31. 608 1.00 0.00 500 CB ASP E 203-30.080-0. 705-33.796 1.00 0.00 501 CG ASP E 203-29.945-1. 648-32.636 1.00 0.00 502 OD1 ASP E 203-29.119-2. 596-32.732 1.00 0.00 503 OD2 ASP E 203-30.679-1. 447-31.632 1.00 0.00 504 N LYS E 204-30.235 2.320-32. 884 1.00 0.00 505 CA LYS E 204-30.396 3.439-31. 974 1.00 0.00 506 C LYS E 204-31.577 3.313-31. 045 1.00 0.00 507 O LYS E 204-32.213 2.274-30. 974 1.00 0.00 508 CB LYS E 204-30.550 4.684-32. 871 1.00 0.00 509 CG LYS E 204-31.885 4.639-33. 641 1.00 0.00 510 CD LYS E 204-31.956 5.828-34. 615 1.00 0.00 511 CE LYS E 204-33.426 6.098-34. 985 1.00 0.00 512 NZ LYS E 204-33.533 7.434-35. 588 1.00 0.00 513 N THR E 205-31.849 4.434-30. 343 1.00 0.00 514 CA THR E 205-33.048 4.538-29. 530 1.00 0.00 515 C THR E 205-33.008 3.765-28. 246 1.00 0.00 516 O THR E 205-32.982 4.388-27. 196 1.00 0.00 517 CB THR E 205-34.381 4.444-30. 297 2. 00 0.00 518 OG1 THR E 205 -34. 706 3.087-30. 619 1.00 0.00 519 CG2 THR E 205-34.324 5.324-31. 561 1.00 0.00 520 N TYR E 206-33.009 2.419-28. 303 1.00 0.00 521 CA TYR E 206-33.028 1.693-27. 045 1.00 0.00 522 C TYR E 206-31.862 0. 755-26. 886 1.00 0.00 523 O TYR E 206-31.080 0.574-27. 805 1.00 0.00 524 CB TYR E 206-34.385 0.992-26. 835 1.00 0.00 525 CG TYR E 206-34.620 0.700-25. 355 1.00 0.00 526 CD1 TYR E 206-35.375-0. 414-24.976 1.00 0.00 527 CD2 TYR E 206-34.076 1.541-24. 380 1.00 0.00 528 CE1 TYR E 206-35.561-0. 697-23.620 1.00 0.00 529 CE2 TYR E 206-34.240 1. 238-23. 027 1.00 0.00 530 CZ TYR E 206-34.984 0.119-22. 643 1.00 0.00 531 OH TYR E 206-35.150-0. 179-21.294 1.00 0.00 532 N ALA E 207-31.754 0.170-25. 677 1.00 0.00 533 CA ALA E 207-30.587-0. 634-25.363 1.00 0.00 534 C ALA E 207-30.445-1. 867-26.211 1.00 0.00 535 O ALA E 207-31.375-2. 273-26.889 1.00 0.00 536 CB ALA E 207-30.612-1. 024-23.875 1.00 0.00 537 N MET E 208-29.234-2. 453-26.146 1.00 0.00 538 CA MET E 208-28.962-3. 663-26.900 1.00 0.00 539 C MET E 208-27.993-4. 509-26.118 1.00 0.00 540 0 MET E 208-27.399-4. 029-25.165 1.00 0.00 541 CB MET E 208-28.329-3. 313-28.262 1.00 0.00 542 CG MET E 208-29.362-2. 643-29. 189 1.00 0.00 543 SD MET E 208-30.524-3. 927-29. 742 1.00 0.00 544 CE MET E 208-29.390-4. 895-30.784 1.00 0.00 545 N GLY E 209-27.829-5. 785-26. 515 1.00 0.00 546 CA GLY E 209-26.909-6. 626-25.769 1.00 0.00 547 C GLY E 209-26.924-8. 046-26.257 1.00 0.00 548 0 GLY E 209-27.546-8. 354-27. 263 1.00 0.00 549 N HIS E 210-26.210-8. 914-25.516 1.00 0.00 550 CA HIS E 210-26.110-10. 294-25.955 1.00 0.00 551 C HIS E 210-26.063-11. 235-24.784 1.00 0.00 552 0 HIS E 210-25.992-10. 802-23.645 1.00 0.00 553 CB HIS E 210-24.878-10. 487-26.861 1.00 0.00 554 CG HIS E 210-23.629-9. 981-26.196 1.00 0.00 555 ND1 HIS E 210-23.369-8. 698-26.092 1.00 0.00 556 CD2 HIS E 210-22.672-10. 755-25.650 1.00 0.00 557 CE1 HIS E 210-22.236-8. 581-25.476 1.00 0.00 558 NE2 HIS E 210-21.786-9. 722-25.195 1.00 0.00 559 N LEU E 211-26.111-12. 546-25.089 1.00 0.00 560 CA LEU E 211-26.131-13. 519-24.011 1.00 0.00 561 C LEU E 211-25.126-14. 607-24.265 1.00 0.00 562 O LEU E 211-24.978-15. 061-25.389 1.00 0.00 563 CB LEU E 211-27.529-14. 159-23.894 1.00 0.00 564 CG LEU E 211-28.629-13. 080-23.896 1.00 0.00 565 CD1 LEU E 211-30.004-13. 757-24.050 1.00 0.00 566 CD2 LEU E 211-28.590-12. 280-22.579 1.00 0.00 567 N ILE E 212-24.426-15. 032-23.198 1.00 0.00 568 CA ILE E 212'23. 501-16.138-23. 362 1.00 0.00 569 C ILE E 212-24. 137-17.349-22. 743 1.00 0.00 570 O ILE E 212-23.910-17. 647-21.580 1.00 0.00 571 CB ILE E 212-22.125-15. 772-22.767 1.00 0.00 572 CG1 ILE E 212-21.527-14. 611-23.589 1.00 0.00 573 CG2 ILE E 212-21.188-16. 997-22.816 1.00 0.00 574 CD1 ILE E 212-20.135-14. 217-23.059 1.00 0.00 575 N GLN E 213-24. 952-18.034-23. 566 1.00 0.00 576 CA GLN E 213-25.683-19. 176-23.054 1.00 0.00 577 C GLN E 213-24. 838-20.412-22. 897 1.00 0.00 578 O GLN E 213-23.672-20. 441-23.261 1.00 0.00 579 CB GLN E 213-26.856-19. 474-24.005 1.00 0.00 580 CG GLN E 213-27.919-18. 365-23.876 1.00 0.00 581 CD GLN E 213-28.714-18. 251-25.148 1.00 0.00 582 OE1 GLN E 213-28.170-18. 388-26.231 1.00 0.00 583 NE2 GLN E 213-30.029-18. 000-25.020 1.00 0.00 584 N ARG E 214-25.476-21. 457-22.337 1.00 0.00 585 CA ARG E 214-24.779-22. 715-22.159 1.00 0.00 586 C ARG E 214-25.730-23. 834-22.472 1.00 0.00 587 O ARG E 214-26.697-24. 032-21.753 1.00 0.00 588 CB ARG E 214-24.309-22. 812-20.696 1.00 0.00 589 CG ARG E 214-23.699-24. 203-20.434 1.00 0.00 590 CD ARG E 214-23.278-24. 326-18.956 1.00 0.00 591 NE ARG E 214-22.947-25. 705-18.635 1.00 0.00 592 CZ ARG E 214-23.386-26. 277-17.549 1.00 0.00 593 NH1 ARG E 214-24.134-25. 639-16.697 1.00 0.00 594 NH2 ARG E 214-23.073-27. 515-17.305 1.00 0.00 595 N LYS E 215-25.434-24. 575-23.557 1.00 0.00 596 CA LYS E 215-26.271-25. 713-23.871 1.00 0.00 597 C LYS E 215-25.888-26. 842-22.960 1.00 0.00 598 O LYS E 215-24.897-27. 517-23.194 1.00 0.00 599 CB LYS E 215-26.082-26. 098-25.350 1.00 0.00 600 CG LYS E 215-27.207-27. 065-25.774 1.00 0.00 601 CD LYS E 215-28. 573-26. 384-25.579 1.00 0.00 602 CE LYS E 215-29.697-27. 375-25.932 1.00 0.00 603 NZ LYS E 215-31.004-26. 760-25.650 1.00 0.00 604 N LYS E 216-26.703-27. 029-21.905 1.00 0.00 605 CA LYS E 216-26.393-28. 065-20.936 1.00 0.00 606 C LYS E 216-26.470-29. 434-21.552 1.00 0.00 607 O LYS E 216-27.401-29. 731-22.283 1.00 0.00 608 CB LYS E 216-27.383-27. 994-19.760 1.00 0.00 609 CG LYS E 216-27.203-26. 667-18.998 1.00 0.00 610 CD LYS E 216-28.478-26. 355-18.189 1.00 0.00 611 CE LYS E 216-28.727-27. 458-17.142 1.00 0.00 612 NZ LYS E 216-29.942-27. 145-16.378 1.00 0.00 613 N VAL E 217-25. 463-30. 271-21.237 1.00 0.00 614 CA VAL E 217-25.514-31. 646-21.699 1.00 0.00 615 C VAL E 217-26.502-32. 394-20.846 1.00 0.00 616 O VAL E 217-27.341-33. 105-21.376 1.00 0.00 617 CB VAL E 217-24.101-32. 268-21.641 1.00 0.00 618 CG1 VAL E 217-23.570-32. 309-20.196 1.00 0.00 619 CG2 VAL E 217-24.123-33. 704-22.201 1.00 0.00 620 N HIS E 218-26. 406-32. 207-19.515 1.00 0.00 621 CA HIS E 218-27. 368-32. 853-18.643 1.00 0.00 622 C HIS E 218-28.385-31. 851-18.174 1.00 0.00 623 O HIS E 218-28.073-30. 678-18.036 1.00 0.00 624 CB HIS E 218-26.658-33. 480-17.427 1.00 0.00 625 CG HIS E 218-25.457-34. 278-17.851 1.00 0.00 626 ND1 HIS E 218-24. 336-34. 250-17. 165 1.00 0.00 627 CD2 HIS E 218-25.389-35. 076-18.933 1.00 0.00 628 CE1 HIS E 218-23.495-35. 025-17.770 1.00 0. 00 629 NE2 HIS E 218-24.034-35. 528-18.789 1.00 0.00 630 N VAL E 219-29.616-32. 341-17.936 1.00 0.00 631 CA VAL E 219-30.646-31. 457-17.423 1.00 0.00 632 C VAL E 219-31.539-32. 247-16.506 1.00 0.00 633 O VAL E 219-31.746-33. 430-16.726 1.00 0.00 634 CB VAL E 219-31.460-30. 789-18.551 1.00 0.00 635 CG1 VAL E 219-32.457-29. 784-17.940 1.00 0.00 636 CG2 VAL E 219-30.533-30. 047-19.534 1.00 0.00 637 N PHE E 220-32.060-31. 590-15.453 1.00 0.00 638 CA PHE E 220-32.865-32. 333-14.499 1.00 0.00 639 C PHE E 220-33.940-31. 467-13.905 1.00 0.00 640 O PHE E 220-33.863-30. 251-13.994 1.00 0.00 641 CB PHE E 220-31.985-32. 888-13.362 1.00 0.00 642 CG PHE E 220-30.833-33. 709-13.934 1.00 0.00 643 CD1 PHE E 220-29.610-33. 098-14.230 1.00 0.00 644 CD2 PHE E 220-31.006-35. 075-14.168 1.00 0.00 645 CE1 PHE E 220-28.579-33. 844-14.809 1.00 0.00 646 CE2 PHE E 220-29.972-35. 824-14.735 1.00 0.00 647 CZ PHE E 220-28.761-35. 206-15.062 1.00 0.00 648 N GLY E 221-34.945-32. 133-13.300 1.00 0.00 649 CA GLY E 221-36. 032-31.403-12. 670 1.00 0.00 650 C GLY E 221-36.731-30. 513-13.657 1.00 0.00 651 O GLY E 221-37.012-30. 942-14.765 1.00 0.00 652 N ASP E 222-37.001-29. 257-13.253 1.00 0.00 653 CA ASP E 222-37.626-28. 341-14.194 1.00 0.00 654 C ASP E 222-36.604-27. 386-14.751 1.00 0.00 655 O ASP E 222-36.929-26. 261-15.099 1.00 0.00 656 CB ASP E 222-38.779-27. 591-13.498 1.00 0.00 657 CG ASP E 222-39.689-28. 561-12.800 1.00 0.00 658 OD1 ASP E 222-39.504-28. 770-11.571 1.00 0.00 659 OD2 ASP E 222-40.602-29. 106-13.476 1.00 0.00 660 N GLU E 223-35.340-27. 846-14.825 1.00 0.00 661 CA GLU E 223-34.302-26. 964-15.327 1.00 0.00 662 C GLU E 223-34.325-26. 917-16. 827 1.00 0.00 663 O GLU E 223-34.894-27. 792-17.460 1.00 0.00 664 CB GLU E 223-32.918-27. 418-14. 830 1.00 0. 00 665 CG GLU E 223-32.865-27. 317-13.294 1.00 0.00 666 CD GLU E 223-31.467-26. 987-12.859 1.00 0.00 667 OE1 GLU E 223-30.595-27. 894-12.931 1.00 0.00 668 OE2 GLU E 223-31.239-25. 823-12.434 1.00 0.00 669 N LEU E 224-33.700-25. 868-17.391 1.00 0.00 670 CA LEU E 224-33.696-25. 756-18.838 1.00 0.00 671 C LEU E 224-32. 442-26. 339-19.425 1.00 0.00 672 O LEU E 224-31.459-26. 516-18.725 1.00 0.00 673 CB LEU E 224-33.829-24. 280-19.260 1.00 0.00 674 CG LEU E 224-35.049-23. 631-18.577 1.00 0.00 675 CD1 LEU E 224-35.125-22. 142-18.963 1.00 0.00 676 CD2 LEU E 224-36.351-24. 343-19.000 1.00 0.00 677 N SER E 225-32.484-26. 638-20.737 1.00 0.00 678 CA SER E 225-31.278-27. 130-21.379 1.00 0.00 679 C SER E 225-30.385-25. 958-21.679 1.00 0.00 680 O SER E 225-29.295-25. 875-21.134 1.00 0.00 681 CB SER E 225-31.635-27. 885-22.674 1.00 0.00 682 OG SER E 225-30.462-28. 513-23.199 1.00 0.00 683 N LEU E 226-30.865-25. 044-22.545 1.00 0.00 684 CA LEU E 226-30.085-23. 846-22.782 1.00 0.00 685 C LEU E 226-30.339-22. 872-21.665 1.00 0.00 686 O LEU E 226-31.452-22. 783-21.169 1.00 0.00 687 CB LEU E 226-30.446-23. 209-24.138 1.00 0.00 688 CG LEU E 226-29.515-22. 012-24.429 1.00 0.00 689 CD1 LEU E 226-28.072-22. 508-24.635 1.00 0.00 690 CD2 LEU E 226-29.999-21. 276-25.692 1.00 0.00 691 N VAL E 227-29.270-22. 150-21.273 1.00 0.00 692 CA VAL E 227-29.412-21. 202-20.181 1.00 0.00 693 C VAL E 227-28.423-20. 080-20.345 1.00 0.00 694 O VAL E 227-27.425-20. 251-21.025 1.00 0.00 695 CB VAL E 227-29.190-21. 910-18.827 1.00 0.00 696 CG1 VAL E 227-30.347-22. 879-18.505 1.00 0.00 697 CG2 VAL E 227-27.847-22. 671-18.837 1.00 0.00 698 N THR E 228-28. 693-18.912-19. 730 1.00 0.00 699 CA THR E 228-27. 735-17.828-19. 867 1.00 0. 00.

700 C THR E 228-26. 761-17. 841-18.723 1.00 0.00 701 O THR E 228-27. 171-17.836-17. 574 1.00 0.00 702 CB THR E 228-28.446-16. 466-19.973 1.00 0.00 703 OG1 THR E 228-29.341-16. 477-21.090 1.00 0.00 704 CG2 THR E 228-27.395-15. 360-20.184 1.00 0.00 705 N LEU E 229-25.456-17. 856-19.057 1.00 0.00 706 CA LEU E 229-24.453-17. 806-18.007 1.00 0.00 707 C LEU E 229-24. 330-16. 371-17.589 1.00 0.00 708 O LEU E 229-24.545-16. 056-16.430 1.00 0.00 709 CB LEU E 229-23.112-18. 313-18.571 1.00 0.00 710 CG LEU E 229-23.262-19. 769-19.052 1.00 0.00 711 CD1 LEU E 229-21.961-20. 209-19.752 1.00 0.00 712 CD2 LEU E 229-23.563-20. 692-17.853 1.00 0.00 713 N PHE E 230-24.006-15. 492-18.556 1.00 0.00 714 CA PHE E 230-24.001-14. 076-18.233 1.00 0.00 715 C PHE E 230-24.348-13. 257-19.443 1.00 0.00 716 O PHE E 230-24.434-13. 799-20.533 1.00 0.00 717 CB PHE E 230-22.671-13. 624-17.596 1.00 0.00 718 CG PHE E 230-21.462-13. 955-18.473 1.00 0.00 719 CD1 PHE E 230-20.930-12. 997-19.341 1.00 0.00 720 CD2 PHE E 230-20.874-15. 222-18.401 1.00 0.00 721 CE1 PHE E 230-19.800-13. 293-20.110 1.00 0.00 722 CE2 PHE E 230-19.746-15. 523-19.169 1.00 0.00 723 CZ PHE E 230-19.195-14. 548-20.005 1.00 0.00 724 N ARG E 231-24.561-11. 941-19.258 1.00 0.00 725 CA ARG E 231-25.031-11. 151-20.384 1.00 0.00 726 C ARG E 231-24.566-9. 727-20.277 1.00 0.00 727 O ARG E 231-23.881-9. 381-19.328 1.00 0.00 728 CB ARG E 231-26.572-11. 187-20.399 1.00 0.00 729 CG ARG E 231-27.136-10. 812-19.012 1.00 0.00 730 CD ARG E 231-28.675-10. 753-19.074 1.00 0.00 731 NE ARG E 231-29.202-10. 266-17.810 1.00 0.00 732 CZ ARG E 231-29.755-9. 091-17.712 1.00 0.00 733 NH1ARGE 231-29. 890-8.320-18. 751 1.00 0.00 734 NH2 ARG E 231-30.175-8. 673-16.555 1.00 0.00 735 N CYS E 232-24.953-8. 908-21.276 1.00 0.00 736 CA CYS E 232-24.508-7. 526-21.275 1.00 0.00 737 C CYS E 232-25.519-6. 656-21.963 1.00 0.00 738 0 CYS E 232-26.326-7. 148-22.738 1.00 0.00 739 CB CYS E 232-23.123-7. 382-21.934 1.00 0.00 740 SG CYS E 232-22.046-6. 567-20. 720 1.00 0.00 741 N ILE E 233-25.478-5. 343-21.663 1.00 0.00 742 CA ILE E 233-26. 447-4.457-22. 285 1.00 0.00 743 C ILE E 233-26. 019-3.017-22. 248 1.00 0.00 744 0 ILE E 233-25.223-2. 623-21.411 1.00 0.00 745 CB ILE E 233-27.856-4. 651-21.685 1.00 0.00 746 CG1 ILE E 233-28.910-3. 921-22.540 1.00 0.00 747 CG2 ILE E 233-27.894-4. 133-20.233 1.00 0.00 748 CD1 ILE E 233-30.321-4. 406-22.159 1.00 0.00 749 N GLN E 234-26.577-2. 237-23.194 1.00 0.00 750 CA GLN E 234-26.233-0. 827-23. 266 1.00 0.00 751 C GLN E 234-27.329-0. 101-23.991 1.00 0.00 752 0 GLN E 234-27.687-0. 514-25.082 1.00 0.00 753 CB GLN E 234-24.967-0. 658-24.130 1.00 0.00 754 CG GLN E 234-23.720-1. 224-23.427 1.00 0.00 755 CD GLN E 234-23.192-0. 203-22.454 1.00 0.00 756 OE1 GLN E 234-22.152 0.386-22. 703 1.00 0.00 757 NE2 GLN E 234-23.909 0.004-21. 332 1.00 0.00 758 N ASN E 235-27.861 0.985-23. 393 1.00 0.00 759 CA ASN E 235-28. 902 1.728-24. 089 1.00 0.00 760 C ASN E 235-28.322 2. 339-25. 332 1.00 0.00 761 0 ASN E 235-27.120 2.554-25. 376 1.00 0.00 762 CB ASN E 235-29.535 2.825-23. 205 1.00 0.00 763 CG ASN E 235-30. 013 2.240-21. 903 1.00 0.00 764 OD1 ASN E 235-31.133 1.761-21. 822 1.00 0.00 765 ND2 ASN E 235-29.158 2. 285-20. 864 1.00 0.00 766 N MET E 236-29. 166 2.601-26. 350 1.00 0.00 767 CA MET E 236-28.623 3.173-27. 571 1.00 0.00 768 C MET E 236-29.089 4.585-27. 804 1.00 0.00 769 0 MET E 236-30.208 4.912-27. 443 1.00 0.00 770 CB MET E 236-28.859 2.261-28. 790 1.00 0.00 771 CG MET E 236-28.235 0.874-28. 530 1.00 0.00 772 SD MET E 236-26. 436 1.014-28. 282 1.00 0.00 773 CE MET E 236-25.967 1.404-29. 993 1.00 0.00 774 N PRO E 237-28.225 5.440-28. 393 1.00 0.00 775 CA PRO E 237-28.590 6.825-28. 603 1.00 0.00 776 C PRO E 237-29.550 6.954-29. 749 1.00 0.00 777 O PRO E 237-29.668 6.046-30. 556 1.00 0.00 778 CB PRO E 237-27.242 7.454-29. 012 1.00 0.00 779 CG PRO E 237-26. 282 6.293-29. 355 1.00 0.00 780 CD PRO E 237-26.910 4.996-28. 806 1.00 0.00 781 N GLU E 238-30.242 8.107-29. 810 1.00 0.00 782 CA GLU E 238-31.158 8.325-30. 914 1.00 0.00 783 C GLU E 238-30.391 8.447-32. 199 1.00 0.00 784 O GLU E 238-30.904 8.048-33. 232 1.00 0.00 785 CB GLU E 238-31.928 9.637-30. 677 1.00 0.00 786 CG GLU E 238-32.943 9.451-29. 534 1.00 0.00 787 CD GLU E 238-33.915 8.353-29. 859 1.00 0.00 788 OE1 GLU E 238-34.654 8.490-30. 871 1.00 0.00 789 OE2 GLU E 238-33.942 7.349-29. 099 1.00 0.00 790 N THR E 239-29.159 8.989-32. 135 1.00 0.00 791 CA THR E 239-28.390 9.109-33. 360 1.00 0.00 792 C THR E 239-27.008 8.547-33. 189 1.00 0.00 793 O THR E 239-26. 466 8.567-32. 095 1.00 0.00 794 CB THR E 239-28.315 10.571-33. 840 1.00 0.00 795 OG1 THR E 239-27.721 11.383-32. 820 1.00 0.00 796 CG2 THR E 239-29.730 11.094-34. 132 1.00 0.00 797 N LEU E 240-26.451 8.038-34. 305 1.00 0.00 798 CA LEU E 240-25.097 7. 510-34. 275 1.00 0.00 799 C LEU E 240-24.898 6.496-33. 174 1.00 0.00 800 O LEU E 240-23.986 6.664-32. 379 1.00 0.00 801 CB LEU E 240-24.093 8.679-34. 199 1.00 0.00 802 CG LEU E 240-24.358 9.673-35. 347 1.00 0.00 803 CD1 LEU E 240-23.549 10.962-35. 115 1.00 0.00 804 CD2 LEU E 240-23.961 9.040-36. 696 1.00 0.00 805 N PRO E 241-25.736 5.436-33. 103 1.00 0.00 806 CA PRO E 241-25.576 4.443-32. 062 1.00 0.00 807 C PRO E 241-24.302 3. 682-32. 284 1.00 0.00 808 O PRO E 241-24.062 3.169-33. 366 1.00 0.00 809 CB PRO E 241-26.792 3.521-32. 276 1.00 0.00 810 CG PRO E 241-27.582 4.066-33. 487 1.00 0.00 811 CD PRO E 241-26.805 5.266-34. 063 1.00 0.00 812 N ASN E 242-23.469 3.632-31. 228 1.00 0.00 813 CA ASN E 242-22.172 3.006-31. 395 1.00 0.00 814 C ASN E 242-21. 644 2.618-30. 046 1.00 0.00 815 O ASN E 242-20. 808 3.308-29. 485 1.00 0.00 816 CB ASN E 242-21. 236 3.991-32. 125 1.00 0.00 817 CG ASN E 242-20. 431 3.272-33. 174 1.00 0.00 818 OD1 ASN E 242-19. 245 3.523-33. 311 1.00 0.00 819 ND2 ASN E 242-21. 075 2.364-33. 932 1.00 0.00 820 N ASN E 243-22. 154 1.482-29. 531 1.00 0.00 821 CA ASN E 243-21. 739 1.059-28. 206 1.00 0.00 822 C ASN E 243 -21. 292-0.375-28. 206 1.00 0.00 823 O ASN E 243 -22. 032-1.251-28. 628 1.00 0.00 824 CB ASN E 243-22. 945 1.206-27. 261 1.00 0.00 825 CG ASN E 243 -23. 064 2. 611-26. 743 1.00 0.00 826 OD1 ASN E 243 -22. 084 3.334-26. 656 1.00 0.00 827 ND2 ASN E 243 -24. 301 3.007-26. 393 1.00 0.00 828 N SER E 244 -20. 057-0.605-27. 717 1.00 0.00 829 CA SER E 244 -19. 590-1.975-27. 605 1.00 0.00 830 C SER E 244 -20 173-2.566-26. 352 1.00 0.00 831 O SER E 244 -20. 776-1.838-25. 579 1.00 0.00 832 CB SER E 244 -18. 049-2.028-27. 574 1.00 0.00 833 OG SER E 244 -17. 532-1.140-26. 577 1.00 0.00 834 N CYS E 245-19. 996-3.890-26. 166 1.00 0.00 835 CA CYS E 245-20. 591-4.531-25. 007 1.00 0.00 836 C CYS E 245-19. 752-5.719-24. 620 1.00 0.00 837 O CYS E 245-19. 854-6.779-25. 219 1.00 0.00 838 CB CYS E 245-22. 041-4.939-25. 332 1.00 0.00 839 SG CYS E 245-23. 033-4.653-23. 835 1.00 0.00 840 N TYR E 246 -18. 904-5.526-23. 592 1.00 0.00 841 CA TYR E 246 -18. 047-6.619-23. 172 1.00 0.00 842 C TYR E 246 -18. 519-7.223-21. 879 1.00 0.00 843 O TYR E 246 -18. 997-6.519-21. 004 1.00 0.00 844 CB TYR E 246 -16. 598-6.110-23. 044 1.00 0.00 845 CG TYR E 246-15. 684-7.213-22. 522 1.00 0.00 846 CD1 TYR E 246-15. 493-7.374-21. 146 1.00 0.00 847 CD2 TYR E 246-15. 043-8.063-23. 427 1.00 0.00 848 CE1 TYR E 246 -14. 679-8.407-20. 674 1.00 0.00 849 CE2 TYR E 246-14.220-9. 087-22.952 1.00 0.00 850 CZ TYR E 246-14.042-9. 263-21.578 1.00 0.00 851 OH TYR E 246-13. 230-10.289-21. 109 1.00 0.00 852 N SER E 247-18.365-8. 557-21.774 1.00 0.00 853 CA SER E 247-18.715-9. 215-20.529 1.00 0.00 854 C SER E 247-17.935-10. 496-20.407 1.00 0.00 855 O SER E 247-17.451-11. 014-21.402 1.00 0.00 856 CB SER E 247-20.229-9. 491-20.452 1.00 0.00 857 OG SER E 247-20. 581-9. 902-19.127 1.00 0.00 858 N ALA E 248-17.805-11. 002-19.166 1.00 0.00 859 CA ALA E 248-17.025-12. 213-18.977 1.00 0.00 860 C ALA E 248-17.304-12. 827-17.632 1.00 0.00 861 0 ALA E 248-17.952-12. 211-16.800 1.00 0.00 862 CB ALA E 248-15.524-11. 900-19.117 1.00 0.00 863 N GLY E 249-16.806-14. 062-17.429 1.00 0.00 864 CA GLY E 249-17.040-14. 710-16.154 1.00 0.00 865 C GLY E 249-16.499-16. 113-16.157 1.00 0.00 866 O GLY E 249-16.216-16. 663-17.209 1.00 0.00 867 N ILE E 250-16'. 360-16.694-14. 950 1.00 0.00 868 CA ILE E 250-15.874-18. 061-14.881 1.00 0.00 869 C ILE E 250-17.019-19. 024-14.719 1.00 0.00 870 O ILE E 250-18.068-18. 655-14.215 1.00 0.00 871 CB ILE E 250-14.874-18. 221-13.719 1.00 0.00 872 CG1 ILE E 250-13.755-17. 167-13.840 1.00 0.00 873 CG2 ILE E 250-14.260-19. 637-13.738 1.00 0.00 874 CD1 ILE E 250-12.881-17. 177-12.571 1.00 0.00 875 N ALA E 251-16.799-20. 277-15.162 1.00 0.00 876 CA ALA E 251-17.842-21. 273-15.000 1.00 0.00 877 C ALA E 251-17.295-22. 655-15.223 1.00 0.00 878 O ALA E 251-16.449-22. 853-16.080 1.00 0.00 879 CB ALA E 251-19.013-21. 014-15.964 1.00 0.00 880 N LYS E 252-17.793-23. 618-14.425 1.00 0.00 881 CA LYS E 252-17.327-24. 980-14.589 1.00 0.00 882 C LYS E 252-18.193-25. 662-15.610 1.00 0.00 883 O LYS E 252-19.368-25. 883-15.360 1.00 0.00 884 CB LYS E 252-17.424-25. 692-13.227 1.00 0.00 885 CG LYS E 252-16. 719-27.060-13. 301 1.00 0.00 886 CD LYS E 252-16.938-27. 811-11.978 1.00 0.00 887 CE LYS E 252-16.399-29. 248-12.106 1.00 0.00 888 NZ LYS E 252-16.782-30. 013-10.909 1.00 0.00 889 N LEU E 253-17. 597-25.990-16. 771 1.00 0.00 890 CA LEU E 253-18.383-26. 645-17.801 1.00 0.00 891 C LEU E 253-18. 089-28.117-17. 863 1.00 0.00 892 0 LEU E 253-17.008-28. 544-17.490 1.00 0. 00 893 CB LEU E 253-18.106-26. 002-19.171 1.00 0.00 894 CG LEU E 253-18.472-24. 507-19.126 1.00 0.00 895 CD1 LEU E 253-18. 050-23. 844-20.451 1.00 0.00 896 CD2 LEU E. 253-19. 989-24.328-18. 902 1.00 0.00 897 N GLU E 254-19.081-28. 891-18.340 1.00 0.00 898 CA GLU E 254-18.873-30. 323-18. 471 1.00 0.00 899 C GLU E 254-18.609-30. 673-19.906 1.00 0.00 900 O GLU E 254-18.878-29. 877-20.791 1.00 0.00 901 CB GLU E 254-20.131-31. 096-18.033 1.00 0.00 902 CG GLU E 254-20.483-30. 763-16.570 1.00 0.00 903 CD GLU E 254-21.436-31. 799-16.048 1.00 0.00 904 OE1 GLU E 254-22.548-31. 931-16.627 1.00 0.00 905 OE2 GLU E 254-21.072-32. 485-15.056 1.00 0.00 906 N GLU E 255-18.083-31. 893-20.126 1.00 0.00 907 CA GLU E 255-17.876-32. 330-21.494 1.00 0.00 908 C GLU E 255-19.207-32. 500-22.173 1.00 0.00 909 0 GLU E 255-20.177-32. 863-21.526 1.00 0.00 910 CB GLU E 255-17.115-33. 667-21.479 1.00 0.00 911 CG GLU E 255-16.627-34. 020-22.897 1.00 0.00 912 CD GLU E 255-15.958-35. 365-22.889 1.00 0.00 913 OE1 GLU E 255-15.039-35. 573-22.050 1.00 0.00 914 OE2 GLU E 255-16.353-36. 222-23.723 1.00 0.00 915 N GLY E 256-19.243-32. 213-23.488 1.00 0.00 916 CA GLY E 256-20.513-32. 288-24.186 1.00 0.00 917 C GLY E 256-21.244-30. 976-24.116 1.00 0.00 918 0 GLY E 256-22.113-30. 741-24.940 1.00 0.00 919 N ASP E 257-20. 897-30.116-23. 137 1.00 0.00 920 CA ASP E 257-21. 572-28.830-23. 055 1.00 0.00 921 C ASP E 257-21.231-27. 959-24.231 1.00 0.00 922 0 ASP E 257-20.271-28. 226-24.937 1.00 0.00 923 CB ASP E 257-21.196-28. 094-21.755 1.00 0.00 924 CG ASP E 257-21.949-28. 631-20.570 1.00 0.00 925 OD1 ASP E 257-23.004-29. 291-20.768 1.00 0.00 926 OD2 ASP E 257-21.478-28. 402-19.426 1.00 0.00 927 N GLU E 258-22.039-26. 902-24.437 1.00 0.00 928 CA GLU E 258-21.756-26. 005-25.543 1.00 0.00 929 C GLU E 258-21.968-24. 578-25.129 1.00 0.00 930 O GLU E 258-22.597-24. 315-24.116 1.00 0.00 931 CB GLU E 258-22.639-26. 336-26.761 1.00 0.00 932 CG GLU E 258-22. 225-27.694-27. 360 1.00 0.00 933 CD GLU E 258-22.835-27. 849-28.723 1.00 0.00 934 OE1 GLU E 258-24.092-27. 834-28.816 1.00 0.00 935 OE2 GLU E 258-22.059-27. 988-29.706 1.00 0.00 936 N LEU E 259-21.419-23. 652-25.937 1.00 0.00 937 CA LEU E 259-21.587-22. 249-25. 611 1.00 0.00 938 C LEU E 259-21.977-21. 472-26. 834 1.00 0.00 939 O LEU E 259-21.717-21. 902-27.947 1.00 0.00 940 CB LEU E 259-20.292-21. 674-25.010 1.00 0.00 941 CG LEU E 259-19.949-22. 393-23.691 1.00 0.00 942 CD1 LEU E 259-18.583-21. 888-23.190 1.00 0.00 943 CD2 LEU E 259-21.024-22. 099-22.625 1.00 0.00 944 N GLN E 260-22.622-20. 312-26.611 1.00 0.00 945 CA GLN E 260-23.029-19. 510-27.749 1.00 0.00 946 C GLN E 260-23.353-18. 101-27.342 1.00 0.00 947 O GLN E 260-23.750-17. 854-26.214 1.00 0.00 948 CB GLN E 260-24.200-20. 157-28.516 1.00 0.00 949 CG GLN E 260-25.466-20. 182-27.636 1.00 0.00 950 CD GLN E 260-26.568-20. 985-28.279 1.00 0.00 951 OE1 GLN E 260-26.354-21. 663-29.272 1.00 0.00 952 NE2 GLN E 260-27.777-20. 904-27.698 1.00 0.00 953 N LEU E 261-23. 168-17.172-28. 296 1.00 0.00 954 CA LEU E 261-23. 503-15. 792-28.008 1.00 0.00 955 C LEU E 261-24.704-15. 425-28.833 1.00 0.00 956 0 LEU E 261-24.611-15. 353-30.049 1.00 0.00 957 CB LEU E 261-22.285-14. 916-28.362 1.00 0.00 958 CG LEU E 261-22.409-13. 525-27.706 1.00 0.00 959 CD1 LEU E 261-21.054-12. 796-27.793 1.00 0.00 960 CD2 LEU E 261-23.499-12. 694-28.415 1.00 0.00 961 N ALA E 262-25.846-15. 193-28.159 1.00 0.00 962 CA ALA E 262-27.038-14. 856-28.915 1.00 0.00 963 C ALA E 262-27.487-13. 448-28.644 1.00 0.00 964 O ALA E 262-27.237-12. 908-27.578 1.00 0.00 965 CB ALA E 262-28.170-15. 834-28.554 1.00 0.00 966 N ILE E 263-28.170-12. 855-29. 641 1.00 0.00 967 CA ILE E 263-28.754-11. 550-29.404 1.00 0.00 968 C ILE E 263-30.248-11. 718-29.383 1.00 0.00 969 0 ILE E 263-30.802-12. 153-30.380 1.00 0.00 970 CB ILE E 263-28.300-10. 533-30.470 1.00 0.00 971 CG1 ILE E 263-26.774-10. 336-30.368 1.00 0.00 972 CG2 ILE E 263-29.013-9. 188-30.229 1.00 0.00 973 CD1 ILE E 263-26. 283-9. 396-31.486 1.00 0.00 974 N PRO E 264-30.900-11. 387-28.247 1.00 0.00 975 CA PRO E 264-32.336-11. 544-28.149 1.00 0.00 976 C PRO E 264-33.031-10. 481-28.955 1.00 0.00 977 O PRO E 264-33.638-9. 573-28.409 1.00 0.00 978 CB PRO E 264-32.572-11. 363-26.636 1.00 0.00 979 CG PRO E 264-31.266-10. 818-26.018 1.00 0.00 980 CD PRO E 264-30.168-10. 894-27.099 1.00 0.00 981 N ARG E 265-32.934-10. 619-30.291 1.00 0.00 982 CA ARG E 265-33.590-9. 666-31. 163 1.00 0.00 983 C ARG E 265-33.524-10. 164-32.578 1.00 0.00 984 O ARG E 265-32.623-10. 913-32.922 1.00 0.00 985 CB ARG E 265-32.917-8. 284-31.059 1.00 0.00 986 CG ARG E 265-33.743-7. 234-31.828 1.00 0.00 987 CD ARG E 265-33.346-5. 815-31.378 1.00 0.00 988 NE ARG E 265-34.150-4. 841-32.094 1.00 0.00 989 CZ ARG E 265-35.245-4. 355-31.581 1.00 0.00 990 NH1 ARG E 265-35.665-4. 723-30.407 1.00 0.00 991 NH2 ARG E 265-35.934-3. 484-32.257 1.00 0.00 992 N GLU E 266-34.500-9. 745-33.405 1.00 0.00 993 CA GLU E 266-34.472-10. 187-34.785 1.00 0.00 994 C GLU E 266-33.782-9. 156-35.626 1.00 0.00 995 O GLU E 266-34.137-7. 989-35.573 1.00 0.00 996 CB GLU E 266-35.903-10. 422-35.296 1.00 0.00 997 CG GLU E 266-36.494-11. 672-34.616 1.00 0.00 998 CD GLU E 266-37.958-11. 775-34.933 1.00 0.00 999 OE1 GLU E 266-38.293-12. 024-36.122 1.00 0.00 1000 OE2 GLU E 266-38. 778-11.613-33. 991 1.00 0.00 1001 N ASN E 267-32. 780-9. 613-36. 404 1.00 0.00 1002 CA ASN E 267-32. 064-8.704-37. 284 1.00 0.00 1003 C ASN E 267-31.417-7. 599-36.495 1.00 0.00 1004 O ASN E 267-31.638-6. 431-36.775 1.00 0.00 1005 CB ASN E 267-32.980-8. 175-38. 407 1.00 0.00 1006 CG ASN E 267-33.761-9. 306-39.015 1.00 0.00 1007 OD1 ASN E 267-33. 186-10. 162-39. 668 1.00 0.00 1008 ND2 ASN E 267-35. 088-9.314-38. 800 1.00 0.00 1009 N ALA E 268-30.608-7. 988-35.488 1.00 0.00 1010 CA ALA E 268-29.961-6. 980-34.664 1.00 0.00 1011 C ALA E 268-28.924-6. 222-35.445 1.00 0.00 1012 O ALA E 268-28. 296-6. 784-36.329 1.00 0.00 1013 CB ALA E 268-29.324-7. 624-33.417 1.00 0.00 1014 N GLN E 269-28. 760-4.925-35. 120 1.00 0.00 1015 CA GLN E 269-27. 779-4.140-35. 848 1.00 0.00 1016 C GLN E 269-26. 488-4.106-35. 087 1.00 0.00 1017 O GLN E 269-26. 427-3.524-34. 016 1.00 0.00 1018 CB GLN E 269-28.309-2. 715-36.101 1.00 0.00 1019 CG GLN E 269-29.582-2. 754-36.970 1. 00 0.00 1020 CD GLN E 269-29.332-3. 451-38.283 1.00 0.00 1021 OE1 GLN E 269-29. 187-2.793-39. 300 1.00 0.00 1022. NE2 GLN E 269-29.294-4. 797-38.271 1.00 0.00 1023 N ILE E 270-25.451-4. 746-35.661 1.00 0.00 1024 CA ILE E 270-24.169-4. 785-34.977 1.00 0.00 1025 C ILE E 270-23. 032-4.762-35. 963 1.00 0.00 1026 O ILE E 270-23.238-4. 906-37. 158 1.00 0.00 1027 CB ILE E 270-24.049-6. 049-34.096 1.00 0.00 1028 CG1 ILE E 270-24.281-7. 308-34.954 1.00 0.00 1029 CG2 ILE E 270-25.076-6. 013-32.948 1.00 0.00 1030 CD1 ILE E 270-23. 907-8.573-34. 158 1.00 0. 00' 1031 N SER E 271 -21. 807-4.579-35. 434 1.00 0.00 1032 CA SER E 271 -20. 649-4.617-36. 305 1.00 0.00 1033 C SER E 271 -20. 134-6.026-36. 408 1.00 0.00 1034 O SER E 271-20. 186-6.764-35. 437 1.00 0.00 1035 CB SER E 271 -19. 550-3.699-35. 738 1.00 0.00 1036 OG SER E 271-18. 401-3.735-36. 587 1.00 0.00 1037 N LEU E 272-19. 631-6.399-37. 600 1.00 0.00 1038 CA LEU E 272-19. 020-7.711-37. 713 1.00 0.00 1039 C LEU E 272-17. 524-7.576-37. 676 1.00 0.00 1040 O LEU E 272-16. 819-8.331-38. 328 1.00 0.00 1041 CB LEU E 272-19. 505-8.466-38. 965 1.00 0.00 1042 CG LEU E 272-20. 954-8.949-38. 758 1.00 0.00 1043 CD1 LEU E 272-21. 445-9.624-40. 051 1.00 0.00 1044 CD2 LEU E 272-21. 015-9.960-37. 594 1.00 0.00 1045 N ASP E 273-17. 041-6.587-36. 898 1.00 0.00 1046 CA ASP E 273-15. 605-6.411-36. 797 1.00 0.00 1047 C ASP E 273-15. 024-7.453-35. 879 1.00 0.00 1048 O ASP E 273-15. 704-7.913-34. 974 1.00 0. 00 1049 CB ASP E 273 -15. 253-5.002-36. 293 1.00 0.00 1050 CG ASP E 273 -14. 040-4.490-37. 013 1.00 0.00 1051 OD1 ASP E 273-12. 929-5.034-36. 771 1.00 0.00 1052 OD2 ASP E 273-14. 193-3.534-37. 820 1.00 0.00 1053 N GLY E 274 -13. 755-7.832-36. 131 1.00 0.00 1054 CA GLY E 274 -13. 148-8. 849-35. 294 1.00 0.00 1055 C GLY E 274-12. 684-8. 245-33.998 1.00 0.00 1056 O GLY E 274 -12. 970-8.780-32. 938 1.00 0.00 1057 N ASP E 275 -11. 959-7.112-34. 098 1.00 0.00 1058 CA ASP E 275 -11. 448-6.489-32. 887 1.00 0.00 1059 C ASP E 275-12. 549-6.034-31. 970 1.00 0.00 1060 O ASP E 275 -12. 324-5.960-30. 772 1.00 0.00 1061 CB ASP E 275 -10. 554-5.292-33. 260 1.00 0.00 1062 CG ASP E 275 -11. 171-4.394-34. 296 1.00 0.00 1063 OD1 ASP E 275-12. 373-4.037-34. 161 1.00 0.00 1064 OD2 ASP E 275 -10. 444-4.046-35. 263 1.00 0.00 1065 N VAL E 276-13.740-5. 733-32.528 1.00 0.00 1066 CA VAL E 276-14. 821-5.284-31. 668 1.00 0.00 1067 C VAL E 276 -15. 721-6.427-31. 283 1.00 0.00 1068 O VAL E 276 -16. 030-6.586-30. 112 1.00 0.00 1069 CB VAL E 276-15. 580-4.134-32. 364 1.00 0.00 1070 CG1 VAL E 276-16. 442-4.637-33. 541 1.00 0.00 1071 CG2 VAL E 276-16. 463-3.405-31. 336 1.00 0.00 1072 N THR E 277-16. 143-7.230-32. 279 1.00 0.00 1073 CA THR E 277-17. 047-8.322-31. 963 1.00 0.00 1074 C THR E 277 -16. 302-9.626-31. 942 1.00 0.00 1075 0 THR E 277-15. 700-10.005-32. 934 1.00 0.00 1076 CB THR E 277-18. 212-8.348-32. 971 1.00 0.00 1077 OG1 THR E 277-18. 863-7.075-32. 956 1.00 0.00 1078 CG2 THR E 277-19. 233-9.425-32. 559 1.00 0.00 1079 N PHE E 278-16. 354-10.310-30. 783 1.00 0.00 1080 CA PHE E 278-15. 628-11.563-30. 666 1.00 0.00 1081 C PHE E 278-16. 191-12.406-29. 555 1.00 0.00 1082 0 PHE E 278-17. 050-11.951-28. 815 1.00 0.00 1083 CB PHE E 278-14. 120-11.310-30. 463 1.00 0.00 1084 CG PHE E 278-13. 890-10.246-29. 392 1.00 0.00 1085 CD1 PHE E 278-13. 785-10.616-28. 048 1.00 0.00 1086 CD2 PHE E 278-13. 784-8.900-29. 756 1.00 0.00 1087 CE1 PHE E 278-13. 563-9.643-27. 070 1.00 0.00 1088 CE2 PHE E 278-13. 562-7.927-28. 778 1.00 0.00 1089 CZ PHE E 278-13. 449-8.299-27. 436 1.00 0.00 1090 N PHE E 279-15. 701-13.656-29. 449 1.00 0.00 1091 CA PHE E 279-16. 257-14.556-28. 455 1.00 0.00 1092 C PHE E 279-15. 295-15.693-28. 241 1.00 0.00 1093 0 PHE E 279-15. 007-16. 424-29.175 1.00 0.00 1094 CB PHE E 279-17. 615-15.065-28. 984 1.00 0.00 1095 CG PHE E 279-18. 238-16.106-28. 056 1.00 0.00 1096 CD1 PHE E 279-18. 292-15.884-26. 678 1.00 0.00 1097 CD2 PHE E 279-18. 763-17.285-28. 593 1.00 0.00 1098 CE1 PHE E 279-18. 894-16.826-25. 839 1.00 0.00 1099 CE2 PHE E 279-19. 378-18.222-27. 757 1.00 0.00 1100 CZ PHE E 279-19. 426-18.000-26. 378 1.00 0.00 1101 N GLY E 280-14.795-15. 837-26.997 1.00 0.00 1102 CA GLY E 280-13.839-16. 902-26.755. 1.00 0.00 1103 C GLY E 280-13.851-17. 355-25.322 1.00 0.00 1104 O GLY E 280-14.609-16. 843-24.513 1.00 0.00 1105 N ALA E 281-12.980-18. 338-25.024 1.00 0.00 1106 CA ALA E 281-12.925-18. 858-23. 669 1.00 0.00 1107 C ALA E 281-11.573-19. 458-23.383 1.00 0.00 1108 O ALA E 281-10.723-19. 512-24.258 1.00 0.00 1109 CB ALA E 281-14.028-19. 913-23.470 1.00 0.00 1110 N LEU E 282-11. 382-19. 911-22.129 1.00 0.00 1111 CA LEU E 282-10.091-20. 459-21.757 1.00 0.00 1112 C LEU E 282-10. 264-21. 459-20.647 1.00 0.00 1113 O LEU E 282-11.040-21. 230-19.733 1.00 0.00 1114 CB LEU E 282-9.172-19. 303-21.309 1.00 0.00 1115 CG LEU E 282-7.876-19. 820-20.649 1.00 0.00 1116 CD1 LEU E 282-6.977-20. 500-21.698 1.00 0.00 1117 CD2 LEU E 282-7.120-18. 637-20.014 1.00 0.00 1118 N LYS E 283-9.529-22. 582-20.736 1.00 0.00 1119 CA LYS E 283-9.608-23. 547-19.659 1.00 0.00 1120 C LYS E 283-8.699-23. 123-18.542 1.00 0.00 1121 O LYS E 283-7.539-22. 823-18.779 1.00 0.00 1122 CB LYS E 283-9.234-24. 953-20.159 1.00 0.00 1123 CG LYS E 283-9.763-25. 996-19.155 1.00 0.00 1124 CD LYS E 283-9.667-27. 401-19.771 1.00 0.00 1125 CE LYS E 283-10.378-28. 417-18.856 1.00 0.00 1126 NZ LYS E 283-9. 655-28.537-17. 579 1.00 0.00 1127 N LEU E 284-9.250-23. 090-17.315 1.00 0.00 1128 CA LEU E 284-8.430-22. 668-16.194 1.00 0.00 1129 C LEU E 284-7.623-23. 818-15.665 1.00 0.00 1130 O LEU E 284-8.058-24. 956-15.741 1.00 0.00 1131 CB LEU E 284-9.313-22. 072-15.081 1.00 0.00 1132 CG LEU E 284-10.177-20. 927-15.647 1.00 0.00 1133 CD1 LEU E 284-11.154-20. 435-14.564 1.00 0.00 1134 CD2 LEU E 284-9.284-19. 760-16.113 1.00 0.00 1135 N LEU E 285-6.426-23. 505-15.132 1.00 0.00 1136 CA LEU E 285-5.604-24. 568-14.577 1.00 0.00 1137 C LEU E 285-6.126-24. 949-13.223 1.00 0.00 1138 O LEU E 285-6.291-26. 115-12.896 1.00 0.00 1139 CB LEU E 285-4.148-24. 079-14.465 1.00 0.00 1140 CG LEU E 285-3.485-24. 108-15.855 1.00 0.00 1141 CD1 LEU E 285-2.079-23. 484-15.767 1.00 0.00 1142 CD2 LEU E 285-3.366-25. 559-16.361 1.00 0.00 1143 OXT LEU E 285-6.409-23. 944-12.402 1.00 0.00 [0217] Having now fully described this invention, it will be understood to those of ordinary skill in the art that the same can be performed within a wide and equivalent range of conditions, formulations, and other parameters without affecting the scope of the invention or any embodiment thereof. All patents and publications cited herein are fully incorporated by reference herein in their entirety.