Use of streptococcus pneumoniae acyl carrier protein synthase crystal structure in diagnostics, antimicrobial drug design, and biosensors

BACKGROUND OF THE INVENTION

[0002] 1. Field of the Invention

[0003] The present invention relates to the fields of protein crystallography, medical diagnostics, and pharmaceutical development. More particularly, the present invention relates to methods of purifying and crystallizing Streptococcus pneumoniae acyl carrier protein synthase (AcpS) enzyme, crystals of AcpS enzyme, the use of these crystals to determine the three-dimensional structure of AcpS enzyme, and to the three-dimensional structure of AcpS enzyme. The three-dimensional crystal structure of the AcpS enzyme can be used in medical diagnostics to produce antibodies that permit detection of Streptococcus pneumoniae both in vitro and in vivo, and therefore accurate diagnosis of infections caused by this bacterium. The three-dimensional crystal structure of AcpS can also be used in pharmaceutical discovery and development to identify and design compounds that inhibit the biochemical activity of AcpS enzyme in bacteria. The inhibitory activity of compounds identified in this way can be optimized by structure/activity studies to develop antibacterial pharmaceutical compounds for the prevention or treatment of bacterial infections in mammals.

[0004] 2. Description of Related Art

[0005] Bacterial Drug Resistance

[0006] The emerging resistance of bacteria to antibiotics is a frightening clinical problem (Cohen, 1992; Neu, 1992; Davies, 1994; Spratt, 1994a). A number of common pathogenic bacterial species such as Streptococcus pneumoniae, Staphylococcus aureus, Enterococcus, Shigella dysenteriae, and Mycobacterium tuberculosis have developed resistance to almost all of the antibiotics, including β-lactams and quinolones, two of the largest and most important classes of antibiotics that have been widely prescribed for upper respiratory tract infections (Cohen, 1992; Neu, 1992; Davies, 1994; Spratt, 1994b; Tomasz and Munoz, 1995; Thomson and Sanders, 1998; Ahamed et al., 1999). The β-lactam and quinolone antibiotics are known to target the biosynthesis of bacterial cell walls and DNA replication, respectively (Neu, 1992; Davies, 1994; Spratt, 1994b; Tomasz and Munoz, 1995 Thomson and Sanders, 1998).

[0007] Bacterial Acyl Carrier Protein Synthases

[0008] The biosynthesis of fatty acids is known to be required for the growth of bacteria as fatty acids are essential components of bacterial membrane lipids and lipopoly-saccharides (Cronan and Rock, 1996; Rock and Cronan, 1996). The fatty acid biosynthetic pathway in bacteria is well characterized (Cronan and Rock, 1996; Rock and Cronan, 1996). Bacteria utilize the type II, or dissociated fatty acid synthase system, for fatty acid synthesis (Cronan and Rock, 1996; Rock and Cronan, 1996). The type II fatty acid synthase system consists of individual enzymes that are encoded by separate genes (Cronan and Rock, 1996; Rock and Cronan, 1996). On the other hand, the type I fatty acid synthase system, almost exclusively present in eukaryotes, is characterized by the presence of a multifunctional protein that possesses all the catalytic activities required for fatty acid synthesis (S. Smith, 1994). In both systems, fatty acids are synthesized by using a repeated cycle of condensation, reduction, dehydration, and reduction reactions (Cronan and Rock, 1996; Rock and Cronan, 1996; S. Smith, 1994). In these reactions, holo-acyl carrier protein (holo-ACP) plays an essential role as an acyl carrier for fatty acid precursors, growing acyl intermediates, and nascent fatty acid products (Cronan and Rock, 1996; Rock and Cronan, 1996; S. Smith, 1994; Elovson and Vagelos, 1968; Lambalot and Walsh, 1995).

[0009] ACP is a small acidic protein in bacteria (Cronan and Rock, 1996; Rock and Cronan, 1996) or a small domain of the type I fatty acid synthase in eukaryotes (S. Smith, 1994). ACP in E. coli is encoded by the acpP gene (Cronan and Rock, 1996; Rock and Cronan, 1996). The newly synthesized ACP, or apo-ACP, is not functional in fatty acid synthesis. The conversion of apo-ACP to holo-ACP, by ACP synthase (AcpS) is required for its functionality (Cronan and Rock, 1996; Rock and Cronan, 1996; Elovson and Vagelos, 1968; Lambalot and Walsh, 1995). The enzymatic step of the reaction that converts apo-acyl carrier protein (apo-ACP) to holo-ACP (Elovson and Vagelos, 1968; Lam et al., 1992; Lambalot and Walsh, 1995; Lambalot et al., 1996; McAllister et al., 2000) is catalyzed by ACP synthase (AcpS), encoded by the acpS gene. This reaction involves the transfer of the 4′-phosphopantetheine group of Coenzyme A (CoA) onto a serine residue of apo-ACP, thereby converting apo-ACP to holo-ACP (Elovson and Vagelos, 1968; Lam et al., 1992; Lambalot and Walsh, 1995; Lambalot et al., 1996). The resulting holo-ACP mediates the transfer of fatty acid intermediates during the biosynthesis of fatty acids and lipids via the covalent attachment of carboxyl groups of fatty acid intermediates to the thiol of the 4′-phosphopantetheine prosthetic group of holo-ACP (Elovson and Vagelos, 1968; Lam et al., 1992; Magnuson et al., 1993; Lambalot and Walsh, 1995; Lambalot et al., 1996). This reaction is therefore required for the biosynthesis of all bacterial fatty acids, lipid A, which is an essential component of bacterial lipopolysacchrides, and the membrane lipids, which are also derived exclusively from acyl intermediates of fatty acids (Magnuson et al., 1993). The essential nature of this reaction has been well established genetically in E. coli and S. pneumoniae (Lam et al., 1992; Takiff et al., 1992; McAllister et al., 2000). Consistent with its important role in fatty acid biosynthesis, AcpS is widely present in Mycoplasma, as well as gram-negative and gram-positive bacteria. Homologues of AcpS and ACP have been identified in many bacterial genomes sequenced to date (Blattner et al., 1997; Cole et al., 1998; Himmelreich et al., 1996; Kalman et al., 1999); Kuns et al., 1997; Tomb et al., 1997). Thus, AcpS appears to be an attractive antibacterial target for discovery of novel antimicrobial agents.

[0010]

E. coli
AcpS has been well studied (Majerus et al., 1965; Elovson and Vagelos, 1968; Lambalot and Walsh, 1995; Lambalot et al., 1996; Gehring et al., 1997; Flugel et al., 2000). The acpS gene from E. coli forms an operon with the upstream gene, pdxJ, whose function is required for vitamin B6 biosynthesis (Lam et al., 1992; Takiff et al., 1992). The acpS gene was originally identified as dpj (downstream of pdxJ) whose function, although unknown, was required for the growth of E. coli (Lam et al., 1992; Takiff et al., 1992). Later, the landmark biochemical study by Lambalot and Walsh (1995) led to the identification of Dpj as AcpS. E. coli AcpS is a small, highly basic protein of approximately 14 kDa (Lambalot and Walsh, 1995). The E. coli enzyme has been purified and characterized (Lambalot and Walsh, 1995). The enzyme exhibits a broad substrate specificity, and can utilize a variety of AcpS, which are required for many diverse aspects of cellular metabolism (Majerus et al., 1965; Crosby et al., 1995; Lambalot and Walsh, 1995; Lambalot et al., 1996; Carreas et al., 1997; Gehring et al., 1997; Tropf et al., 1998; Kutchma et al., 1999; Zhou et al, 1999; Flugel et al., 2000). Purified AcpS also exhibits activity with a number of CoA derivatives (Gehring et al., 1997). These results indicate that AcpS may be able to participate in other metabolism besides fatty acid biosynthesis in the cell. Purified AcpS also exhibits activity with a number of CoA derivatives (Gehring et al., 1997). Finally, AcpS is a very low abundance protein in E. coli (Elovson and Vagelos, 1968; Lamabolt and Walsh, 1995). In contrast, ACP is a very abundant protein that has been estimated to be present at 25,000-60,000 molecules per cell (Cronan and Rock, 1996; Rock and Cronan, 1996; Jackowski and Rock, 1984; Vallari and Jackowshi, 1988). The majority of AcpS present in the cell are found to be holo-AcpS (Cronan and Rock, 1996; Rock and Cronan, 1996; Jackowski and Rock, 1983; Heath and Rock, 1996).

[0011] Although E. coli AcpS is well studied, the reaction mechanism of AcpS remains unknown. In addition, only the AcpS from E. coli, a rod-shaped, Gram-negative bacterium, has been thoroughly characterized to date. It still remains to be determined whether AcpS from Gram-positive bacteria plays the same physiological role. Finally, AcpS appears to possess all the features necessary for a good antibacterial target, such as its essential nature, widespread existence in bacteria, and unique catalytic position in an important biosynthetic pathway (fatty acid biosynthesis). Thus, AcpS appears to be a valuable antibacterial target for identifying novel antimicrobial agents.

[0012] Recently, AcpS from Streptococcus pneumoniae has been purified and characterized (McAllister et al., 2000). The S. pneumoniae enzyme exhibits biochemical properties similar to those of the E. coli AcpS. The acpS gene has also been shown to be essential for the growth of S. pneumoniae (McAllister et al., 2000).

[0013] The crystal structure of Bacillus subtilis AcpS has recently been described by Parris et al. (2000).

[0014] The pressing need for new antibacterial compounds can desirably be met by methods that do not rely on serendipity and/or systematic screening of large numbers of natural and synthetic compounds. One such method relies on structure-based drug design using computer modeling and the three-dimensional crystal structure of bacterial target proteins to identify and optimize antimicrobial drug candidates. The three-dimensional structure of AcpS has heretofore remained unknown as no crystals thereof have been produced that permitted the required crystallographic data to be obtained. Therefore, there is a need in the art for such crystals, for the determination of the three-dimensional structure of such crystals, and for structure-based drug design and diagnostics based on such crystallographic data.

SUMMARY OF THE INVENTION

[0015] Accordingly, in order to exploit bacterial cellular components that can serve as diagnostic agents and antibacterial targets for identifying novel antibiotics that can be used to combat the current crisis of antibiotic resistance, the present inventors have focused their attention on AcpS. The present invention includes among its various aspects crystals of AcpS enzyme, use of such AcpS crystals to determine the three-dimensional structure of AcpS enzyme, the three-dimensional crystal structure of AcpS enzyme, methods of drug discovery/design and diagnostics based on the three-dimensional crystal structure AcpS enzyme, use of crystals of AcpS in biosensors and other applications, and methods of purifying and crystallizing AcpS enzyme. As a first step toward structure-based drug design, the present invention provides the crystal structures of S. pneumoniae AcpS and the AcpS/3′,5′-ADP complex at 2.0 and 1.9 Å resolution, respectively.

[0016] More specifically, in a first aspect, the present invention provides a composition comprising a crystal of isolated Streptococcus pneumoniae AcpS. Such crystal effectively diffracts X-rays, and permits the determination of the atomic coordinates of the AcpS to a resolution of 2.0 Å or greater. As used herein, the term “greater” refers to resolution of the atomic coordinates to a value lower than 2.0 Å.

[0017] More particularly, the present invention provides a composition comprising a crystal of Streptococcus pneumoniae AcpS having the amino acid sequence shown in SEQ ID NO: 1 wherein methionine is substituted with selenomethioinine, wherein said AcpS is a homotrimer, wherein each protomer comprises the following structural motifs: (a) a three-stranded anti-parallel β-sheet formed by strands β1, β5, and β4; (b) a long α-helix that packs diagonally against said β-sheet, together with α-helices α1 α2, α3, and α4 of an anti-parallel four helical bundle; and (c) a long, extended loop with a two-strand anti-parallel β-sheet comprising strands β2 and β3, wherein said structural motifs (a), (b), and (c) are organized such that said long helix α4 runs through said homotrimer, and is surrounded by the remainder of said structural motifs, as shown in FIGS. 8(B) and 8(C). When the AcpS is in native form, i.e., the active site is unoccupied, the crystal belongs to orthorhombic space group P212121, with unit cell dimensions of a=49.8 Å, b=59.6 Å, and c=114.7 Å, or monoclinic space group C2, with unit cell dimensions of a=120.2 Å, b=62.3 Å, c=51.7 Å, and β=98.7°. Such crystals can have the atomic coordinates shown in Tables 3 and 4. When the AcpS is complexed with 3′,5′-adenosine diphosphate, the crystal belongs to monoclinic space group C2, with unit cell dimensions of a=120.2 Å, b=62.3 Å, c=51.7 Å, and β=98.7°, and the crystal can have the atomic coordinates shown in Table 5.

[0018] In another aspect, the present invention provides an enzyme active site crystal structure comprising the 3′,5′-adenosine diphosphate binding site shown in FIG. 9. More particularly, the enzyme comprises isolated, properly folded Streptococcus pneumoniae AcpS, or a fragment or protein fusion product thereof comprising the active site. Also encompassed by the present invention are active site crystal structures that are variants or homologs of the AcpS binding pocket having a root mean square deviation from the amino acid residues comprising the AcpS active site shown in FIG. 9 in the range of from about 1 to about 3 Å, more preferably from about 1 to about 2 Å, and most preferably of about 1.15 Å. Such active sites can form binding complexes with an ACP, a CoA, an apo-ACP, an acetyl-CoA, a desulfo-CoA, an acetoacetyl-CoA, a malonyl-CoA, or a dephospho-CoA.

[0019] In a further aspect, the present invention provides a method of isolating Streptococcus pneumoniae AcpS, comprising:

[0020] (a) growing Streptococcus pneumoniae in a medium lacking methionine but containing L-selenomethionine;

[0021] (b) preparing a cell extract of the Streptococcus pneumoniae;

[0022] (c) centrifuging the cell extract to produce a supernatant fraction, and collecting this supernatant fraction;

[0023] (d) chromatographing the supernatant fraction on a cation exchange column in buffer containing dithiothreitol or β-mercaptoethanol, and collecting fractions containing the Streptococcus pneumoniae AcpS; and

[0024] (e) chromatographing the fractions of step (d) on a gel filtration column in buffer containing dithiothreitol or β-mercaptoethanol, and collecting fractions containing the Streptococcus pneumoniae AcpS comprising L-selenomethionine.

[0025] An additional step in this method can comprise chromatographing the fractions of step (e) on an anion exchange column in buffer containing dithiothreitol or β-mercapto-ethanol, and collecting fractions containing Streptococcus pneumoniae AcpS.

[0026] In yet another aspect, the present invention provides isolated Streptococcus pneumoniae acyl carrier protein synthase produced by the foregoing method.

[0027] In another aspect, the present invention provides a method of producing a crystal of Streptococcus pneumoniae AcpS that diffracts X-rays, comprising:

[0028] (a) providing Streptococcus pneumoniae AcpS isolated according to the foregoing method;

[0029] (b) concentrating the AcpS to 8 mg/ml in a solution containing 10 mM MgCl2, 14 mM KCl, and 20 mM Tris-HCl at pH 7.1;

[0030] (c) equilibrating a 4 μl drop of the AcpS in a solution comprising a mixture of 1:1, v/v, protein solution/reservoir solution over a 500 μl reservoir solution comprising 8-15% polyethyleneglycol 4000, 200 mM ammonium sulfate, and 100 mM citrate buffer at pH 4.5; and

[0031] (d) growing a crystal of AcpS by vapor diffusion at 294K for 4 to 5 days or longer.

[0032] In another aspect, the present invention provides a crystal of Streptococcus pneumoniae AcpS produced by the foregoing method.

[0033] In a further aspect, the present invention provides a co-crystal of Streptococcus pneumoniae AcpS with a compound, produced by either including such compound in the protein solution/reservoir solution during crystallization, or by contacting a crystal of AcpS and a solution, such as protein or reservoir solution, comprising such compound (“soaking” the crystal in a solution of compound), and incubating the resulting mixture to permit the compound to diffuse into the crystal, thereby producing a complex between AcpS and the compound. The compound can be 3′,5′-adenosine diphosphate. Whatever compound is employed, a three-dimensional structure of the resulting acyl carrier protein synthase/compound crystal complex can then be determined.

[0034] In another aspect, the present invention provides a co-crystal of AcpS produced by the foregoing or similar method.

[0035] In yet other aspects, the present invention provides the use of a three-dimensional crystal or co-crystal structure of AcpS in medical diagnostics, biosensors, and pharmaceutical drug discovery and design. The latter enables methods of treating Streptococcal infections utilizing compounds that block the biochemical activity of Streptococcus pneumoniae AcpS enzyme, by, for example, determining a three-dimensional structure of AcpS enzyme from Streptococcus pneumoniae, utilizing such three-dimensional structure to identify/develop a compound that binds to and inhibits the enzyme, and contacting, either in vitro or in vivo, such compound and Streptococcal cells containing the enzyme, thereby inhibiting the biochemical activity of the enzyme and treating or preventing Streptococcal infections.

[0036] Further scope of the applicability of the present invention will become apparent from the detailed description provided below. However, it should be understood that the detailed description and specific examples, while indicating preferred embodiments of the present invention, are given by way of illustration only since various changes and modifications within the spirit and scope of the invention will become apparent to those skilled in the art from this detailed description.

BRIEF DESCRIPTION OF THE DRAWINGS AND TABLES

[0037] The file of this patent contains at least one drawing and one table executed in color. Copies of this patent with color drawing(s) and tables will be provided by the Patent and Trademark Office upon request and payment of the necessary fee.

[0038] The above and other aspects, features, and advantages of the present invention will be better understood from the following detailed description taken in conjunction with the accompanying drawings, all of which are given by way of illustration only, and are not limitative of the present invention, in which:

[0039]
FIGS. 1A and 1B show SDS-PAGE analysis of purified S. pneumoniae AcpS and apo-ACP, respectively, expressed in E. coli, and purified as described in Example 1. The purified AcpS is analyzed by SDS-PAGE (16% Tricine gels) and stained with Coomassie Blue R-250. FIG. 1A: Each lane contains 5 μg of protein. Lane M: prestained molecular weight markers. Lane 1: Crude extract of E. coli containing overexpressed S. pneumoniae AcpS. Lane 2: pooled fractions from 15S Source S column; Lane 3: pooled fractions from S-100 Sepharose column. FIG. 1B: Each lane contains 10 μg of protein. Lane M: prestained molecular weight markers. Lane 1: Crude extract of E. coli containing overexpressed S. pneumoniae ACP. Lane 2: pooled fractions from Source 15Q column; Lane 3: pooled fractions from S-100 Sepharose column.

[0040]
FIG. 2 shows analysis of the native structure of S. pneumoniae AcpS and apo-ACP by gel filtration column chromatography. Both AcpS and apo-ACP are purified as described in Example 1. Purified AcpS (27 μM) and apo-ACP (100 μM) are subjected to gel filtration column (S-75 Sephadex) chromatography, and their molecular weights are determined as described in Example 1. Panel A shows gel filtration column chromatograph. Peak A contains both AcpS and apo-ACP, and has an elution volume of 10.5 ml with an estimated molecular weight of 53 kDa. Peak B contains only AcpS, and has an elution volume of 11.5 ml, with an estimated molecular weight of 38 kDa. The arrow C points to the area where apo-ACP elutes. Since apo-ACP does not absorb at 280 nm, there is no apparent protein peak observed. Panel B shows SDS-PAGE analysis of the column fractions. All relevant fractions collected from Panel A are subjected to SDS-PAGE analysis. The gels are stained with SYPRO Orange, and analyzed using a FluorImager.

[0041]
FIG. 3 shows analysis of the S. pneumoniae AcpS and apo-ACP native structures by cross-linking. AcpS and apo-ACP are purified as described in Example 1. Purified AcpS (163 μM) and apo-ACP (94 μM) are treated without or with 19.5 and 9.4 mM sulfo-EGS, respectively. The resulting AcpS (Panel A) and apo-ACP (Panel B) preparations are analyzed by SDS-PAGE (16% tricine gels). Panel A: Lane 1: the pre-stained molecular weight marker; lane 2: AcpS untreated with sulfo-EGS; and lane 3: AcpS treated with sulfo-EGS. Panel B: Lane 1, the pre-stained molecular weight marker; lane 2: apo-ACP untreated with sulfo-EGS; lane 3: apo-ACP treated with sulfo-EGS.

[0042]
FIG. 4 shows a kinetic analysis of the effect of apo-ACP concentrations on the AcpS activity of S. pneumoniae. AcpS activity is measured using the HPLC method under conditions where the CoA concentration is fixed at 20 μM and the apo-ACP concentration is varied from 0.5 to 100 μM. A: the substrate (apo-ACP) saturation curve of AcpS. B and C: the double reciprocal plots of the initial velocities of the enzyme versus the various apo-ACP concentrations (<5 μM and >15 μM, respectively).

[0043]
FIG. 5 shows a kinetic analysis of the effect of CoA concentrations on the AcpS activity of S. pneumoniae. AcpS activity is measured by the HPLC method under conditions where the CoA concentrations are varied (2.5-600 μM) and the apo-ACP concentration is fixed (2 μM). A: the substrate (CoA) saturation curve of AcpS. B: the double reciprocal plot of the initial velocities of AcpS versus CoA concentrations.

[0044]
FIG. 6 shows an analysis of the mechanism of the AcpS catalyzed reaction.

[0045] AcpS activity is measured using HPLC methods. A: double-reciprocal plots of the initial velocities of AcpS versus the various CoA concentrations (2.5 -30 μM) and the fixed apo-ACP concentrations (0.25 (&Circlesolid;),0.35 (▪), 0.5 (▴), and 0.6 μM (♦)). B: double-reciprocal plots of the initial velocities of AcpS versus the various apo-ACP concentrations (0.25-0.6 μM) and the fixed CoA concentrations (2.5 (&Circlesolid;) , 5.0 (▪), 10 (▴), and 20 μM (♦)).

[0046]
FIG. 7 shows an analysis of the inhibition kinetics of 3′,5′-ADP with respect to apo-ACP and CoA. AcpS activity is measured in the absence (&Circlesolid;) or presence of 3′,5′-ADP (5 (▪) and 10 μM (▴)). A and B: the double-reciprocal plots of the initial 2 5 velocities of AcpS versus the various CoA concentrations and the fixed apo-ACP concentration, and the various apo-ACP concentrations and the fixed CoA concentrations, respectively. C and D: Dixon plots of A and B, respectively. The CoA concentrations used in panel C are 10 (&Circlesolid;) and 40 (▪) μM.

[0047]
FIG. 8A is a color stereoview showing a ribbon diagram of the AcpS homotrimer, viewed along a non-crystallographic 3-fold axis.

[0048]
FIG. 8B is a color ribbon diagram of the Cα backbone of one Streptococcus pneumoniae AcpS monomer structure.

[0049]
FIG. 8C is a color topology (Richardson) diagram of AcpS. β-strands are represented as arrows, while α helices are rectangles. The secondary structure elements are defined as follows: β1, Ile4-Glu13; α1, Leu14-Arg23; α2, Phe27-Val31; α3, Ala34-Ser42; α4, Gly45-Met66; α5, Ile70-Leu73; β2, Glu79-Asn82; β3, Pro88-Gln92; β4, Lys98-His105; β5, Phe109-Glu117.

[0050]
FIG. 9 is a color stereoview of the 3′,5′-ADP fragment of CoA bound to the active site of S. pneumoniae AcpS. The omitted electron density map corresponding to the ligand is contoured at the 1 σ level at 1.9 Å resolution.

[0051]
FIG. 10 shows a color superposition of apo-AcpS from S. pneumoniae (shown in blue) on the surfactin synthetase activating enzyme Sfp (4′-phosphopantetheinyl transferase) from Bacillus subtilis complexed with CoA (shown in red). One protomer of AcpS is superimposed on the N-terminal domain of Sfp, and a second AcpS protomer is superimposed on the C-terminal domain of Sfp. The third protomer of the AcpS trimer does not have a counterpart in the Sfp structure. A sulfate ion is found in the AcpS binding site that corresponds to the position of the α-phosphate of CoA in the Sfp molecule.

[0052] Table 1A shows sequence alignment of bacterial AcpS genes from different species. The most conserved regions are shown in grey. Secondary structural elements observed in the S. pneumoniae AcpS crystal structure are indicated above the sequence pile-up.

[0053] Table 1B shows structural alignment of two Streptococcus pneumoniae AcpS monomer molecules with two domains of Bacillus subtilis Sfp. The N-terminal half of Sfp from Metl to ProlO3 corresponds to one protomer of the AcpS trimer (shown in blue), and has a 22% sequence identity. The C-terminal half of Sfp from Ile104 to Pro209 corresponds to a second AcpS protomer (shown in green) and has 25% sequence identity. The remaining C-terminal portion from Asp210 to Leu224 has no counterpart in the AcpS structure. The three amino acid residues involved in Mg2+ binding are marked by an asterisk (*). The regions involved in CoA binding are marked by plus (+) signs.

[0054] Table 2 (1 page) summarizes the crystallographic data disclosed herein.

[0055] Table 3 (51 pages) shows the atomic coordinates for AcpS native 1.

[0056] Table 4 (52 pages) shows the atomic coordinates for AcpS native 2.

[0057] Table 5 (53 pages) shows the atomic coordinates for AcpS/3′,5′-ADP complex.

[0058] The tables herein are presented after the Abstract of the Disclosure.

DETAILED DESCRIPTION OF THE INVENTION

[0059] The following detailed description of the invention is provided to aid those skilled in the in art in practicing the present invention. Even so, the following detailed description should not be construed to unduly limit the present invention as modifications and variations in the embodiments discussed herein can be made by those of ordinary skill in the art without departing from the spirit or scope of the present inventive discovery.

[0060] The contents of each of the references cited herein are herein incorporated by reference in their entirety.

[0061] The present invention provides novel Streptococcus pneumoniae AcpS crystal structures, including their active sites, use of these crystal structures to produce antibodies to epitopes of this protein for in vitro and in vivo diagnostic purposes, and methods of using these crystal structures and active sites to identify or design AcpS inhibitor compounds for use as antibacterials in the treatment of bacterial infections. Among its many aspects, the present invention provides a method for inhibiting AcpS by administering compounds having certain structural, physical, and spatial characteristics that permit interaction, e.g., binding, of such compounds with specific amino acid residues within acyl carrier protein synthases, particularly the active sites of these enzymes. Such compounds may bind to all or only a portion of an active site, and may be competitive or non-competitive inhibitors of these enzymes.

[0062] As used herein, the term “crystal” includes an ordered protein array having a regular structure of a constituent chemical species, e.g., such as an AcpS protein or portion thereof. In one embodiment, a crystal of the present invention comprises a solid three-dimensional AcpS protein aggregate in which planar surfaces intersect at definite angles. In another embodiment, a crystal of the invention comprises an ordered two dimensional packing of AcpS proteins, such as, e.g., in a monolayer.

[0063] As used herein, the term “active site” refers to the general region of an enzyme molecule containing the catalytic residues identified with the binding of substrate(s) (and prosthetic group(s), if any), and reaction of substrate(s) by the making and breaking of bonds. “Catalytic residues” include any of the amino acid residues in an enzyme that are directly involved in making or breaking covalent bonds while the enzyme is acting on a substrate. It includes those amino acid residues that are, in the enzyme-substrate complex, either contact amino acids, i.e., those that at some point are within only one bond distance of some point on the substrate molecule (which may include both catalytic residues and specificity residues), or auxiliary amino acids, i.e., those that are not in such intimate physical contact with the substrate, but which nonetheless play a definite role in the action of the enzyme. The active site generally takes up a relatively small part of the total volume of an enzyme molecule. Most of the amino acids residues in an enzyme are not in contact with the substrate. The active site is a three-dimensional entity, often a cleft or crevice, formed by groups that come from different parts of the linear amino acid sequence. Residues far apart in the linear sequence may interact more strongly than adjacent residues in the amino acid sequence. Substrates are bound to enzymes by multiple weak attractions, including electrostatic bonds, hydrogen bonds, van der Waals forces, and hydrophobic interactions. The enzyme and substrate should have complementary shapes. Finally, the specificity of binding depends on the precisely defined arrangement of atoms in the active site, and the shapes of the active sites of some enzymes are markedly modified by the binding of substrate. Thus, the active sites of these enzymes have shapes that are complementary to that of the substrate only after the substrate is bound, a process of dynamic recognition called “induced fit.”

[0064] Inhibitors of acyl carrier protein synthases are predicted to interact with (bind) these proteins in the region comprising the 3′,5′-adenosine diphosphate binding site, shown in FIG. 9.

[0065] As used herein, including the appended claims, singular forms of words such as “a,” “an,” and “the” include, e.g., their corresponding plural referents unless the context clearly dictates otherwise. Thus, for example, reference to “a crystal” includes, e.g., one or more crystals, reference to “an AcpS crystal” includes, e.g., one or more of such crystals; reference to a binding event includes one or more such events; reference to bind a crystal includes binding one or more such crystals; and reference to “a method” includes, e.g., reference to equivalent steps and methods known to a person of ordinary skill in the art, and so forth.

[0066] With respect to antibodies for diagnostic purposes, the crystal structures disclosed herein facilitate the production of such antibodies. Knowledge of the three-dimensional structure of AcpS provides information as to various epitopes on the enzyme surface. Using this knowledge, one can synthesize peptides comprising such epitopes, and produce antibodies that specifically bind thereto by methods well known in the art. Antibodies produced in response to these peptides can then be used to detect the presence of Streptococcus pneumoniae both in vitro and in vivo, thereby providing useful diagnostic means for detecting the presence of this pathogen.

[0067] Structure-Based Drug Design

[0068] The use of protein crystal structures to design candidate antimicrobial compounds can be accomplished by structure-based drug design. In one embodiment of this method, the three-dimensional structure of a protein or protein fragment, such as a peptide, is determined, and potential antagonists (or agonists, if desired) are designed with the aid of computer modeling (Bugg et al.,1993; West et al., 1995). Once the crystal structure of the target, e.g., Streptococcus pneumoniae AcpS is determined, computer modeling is conducted (using programs such as DOCK or Multiple Copy Simultaneous Search (MCSS)) to construct candidate inhibitor compounds based on the crystal structure. These compounds are chemically synthesized, or obtained from previously existing drug libraries, and their binding to the AcpS target and/or their biological activity, i.e., inhibitory activity, against AcpS is assayed. Compounds that bind and/or that inhibit the enzymatic activity of AcpS are thereby identified as drug candidates. In a further refinement of this method, those compounds exhibiting binding and/or activity can be associated or complexed with the crystal for further X-ray diffraction analysis to map their interactions with the crystal structure. This can be accomplished by growing a supplemental crystal of AcpS in the presence of one such compound to produce a crystal containing a complex formed between the AcpS protein and the drug candidate. A crystal is chosen that effectively diffracts X-rays, allowing the determination of the atomic coordinates of the protein-ligand complex to a resolution greater than about 10 Å, preferably to a resolution greater than about 5 Å, more preferably to a resolution greater than about 3 Å, more preferably to a resolution greater than about 2.0 Å, and most preferably to a resolution of about 1.9 Å. The three-dimensional structure of the supplemental crystal is determined by molecular replacement analysis, and a drug is selected by performing rational drug design with the three-dimensional structure determined using the supplemental crystal. Such selecting is preferably performed in conjunction with computer modeling.

[0069] From the resulting inhibitor-target crystal structure, one of ordinary skill in the art can construct further improved candidate compounds.

[0070] The steps set forth in the preceding paragraphs can be repeated and refined as desired until a drug candidate having the desired potency is identified.

[0071] Protein Expression

[0072] As would be apparent to those of ordinary skill in the art, conventional molecular biological, microbiological, and recombinant DNA techniques are available that permit expression of amounts of AcpS protein sufficient for the types of studies described herein using genomic DNA, cDNA, synthetic DNA, etc. coding on expression therefor. Such techniques are fully explained in the literature, e.g., Sambrook et al., 1989 and Ausubel et al., 1987. Note also in this regard U.S. Pat. Nos. 6,020,162 and 6,087,478.

[0073] Preparation of Protein Crystals

[0074] Crystals of AcpS can be grown by a number of techniques, including batch crystallization, vapor diffusion (either by sitting drop, hanging drop, or sandwich), microdialysis, membrane crystallization, or any other conventional method of protein crystallization. Seeding of crystals is sometimes required in order to obtain X-ray quality crystals. Standard micro- and/or macro-seeding of crystals can therefore be employed. As described below, the hanging drop method can be used to obtain the crystals disclosed herein.

[0075] X-ray Diffraction

[0076] Once a crystal of the present invention is grown, X-ray diffraction data can be collected. Crystals can be characterized, for example, by using X-rays produced in a conventional source (such as a sealed tube or a rotating anode), or using a synchrotron source. Methods of characterization include, but are not limited to, precision photography, oscillation photography, and diffractometer data collection. Heavy atom derivatives, such as produced using Hg, Pb, Au, U, Pt, I, Os, etc., can be performed using Fuji imaging plates. Alternatively, AcpS can be synthesized with selenium-methionine (Se-Met) in place of methionine, and the Se-Met multiwavelength anomalous dispersion data (Hendrickson, 1991) can be collected on CHESS F2, using reverse-beam geometry to record Friedel pairs at four X-ray wavelengths, corresponding to two remote points above and below the Se absorption edge (λ1 and λ4) and the absorption edge inflection point (λ2) and peak (λ3). Selenium sites can be located using SHELXS-90 in Patterson search mode (G. M. Sheldrick). Experimental phases (αMAD) can be estimated via a multiple isomorphous replacement/anomalous scattering strategy using MLPHARE (Z. Otwinowski, Southwestern University of Texas, Dallas) with three of the wavelengths treated as derivatives and one (λ2) treated as the parent for example. In either case, data can be processed using HKL, DENZO, and SCALEPACK (Otwinowski and Minor, 1997).

[0077] In addition, X-PLOR (Brünger, 1992; X-PLOR v. 3.1 Manual, New Haven, Yale University) or Heavy (T. Terwilliger, Los Alamos National Laboratory) can be utilized for bulk solvent correction and B-factor scaling. After density modification and non-crystallographic averaging, the protein is built into an electron density map using the program O (Jones et al., 1991). Model building interspersed with positional and simulated annealing refinement (Brünger, 1992, supra) can permit the unambiguous trace and sequence assignment of the AcpS protein.

[0078] Protein-Structure Based Design of Agonists and Antagonists of AcpS

[0079] Once the three-dimensional structure of a crystal comprising the AcpS protein, or fragment or fusion protein derivative thereof comprising an active site, is determined, a potential ligand (antagonist or agonist) can be examined via the use of computer modeling using a docking program such as RAM, DOCK, or AUTODOCK (Dunbrack et al., 1997). This procedure can include computer fitting of potential ligands to AcpS to ascertain how well the shape and the chemical structure of the potential ligand will complement or interfere with the enzyme (Bugg et al., 1993; West et al., 1995). Computer programs can also be employed to estimate the attraction, repulsion, and steric hindrance of the ligand to the AcpS binding site. Generally the tighter the fit (e.g., the lower the steric hindrance, and/or the greater the attractive force) the more potent the potential drug will be since these properties are consistent with a tighter binding constant. Furthermore, the greater the specificity in the design of a potential drug, the more likely that the drug will not interfere with other properties of the AcpS protein or other proteins in host cells. This will minimize potential side-effects due to unwanted interactions with other proteins.

[0080] Initially, a potential ligand could be obtained by screening, for example, a random peptide library produced by recombinant bacteriophage (Scott et al., 1990; Cwirla et al., 1990; Devlin et al., 1990) or a chemical library. A ligand selected in this manner could be then be systematically modified by computer modeling programs until one or more promising potential ligands are identified. Such analysis has been shown to be effective in the development of HIV protease inhibitors (Lam et al., 1994; Wlodawer et al., 1993; Appelt, 1993; Erickson, 1993).

[0081] Such computer modeling allows the selection of a finite number of rational chemical modifications, as opposed to the countless number of essentially random chemical modifications that could be made, and of which any one might lead to a useful drug. Each chemical modification requires additional chemical steps, which while being reasonable for the synthesis of a finite number of compounds, quickly becomes overwhelming if all possible modifications needed to be synthesized. Thus, through the use of the three-dimensional structure disclosed herein in combination with computer modeling, a large number of these compounds can be rapidly screened on the computer monitor screen, and a few likely candidates can be determined without the laborious synthesis of untold numbers of compounds.

[0082] Once a potential ligand (agonist or antagonist) is identified, it can either be selected from a library of chemicals as are commercially available from most large chemical companies including Eli Lilly and Company, or alternatively, the potential ligand can be synthesized de novo. As noted above, the de novo synthesis of one or even a relatively small group of specific compounds is reasonable in the art of drug design. The prospective drug can be placed into any standard binding assay described below to test its effect on the AcpS protein.

[0083] When a suitable drug is identified, a supplemental crystal can be grown which comprises a protein-ligand complex formed between the AcpS protein and the drug.

[0084] Preferably, the crystal effectively diffracts X-rays, allowing the determination of the atomic coordinates of the protein-ligand complex to a resolution of greater than about 5.0 Å, more preferably greater than about 3.0 Å, and even more preferably greater than about 2.0 Å. The three-dimensional structure of the supplemental crystal can be determined by molecular replacement analysis. Molecular replacement involves using a known three-dimensional structure as a search model to determine the structure of a closely related molecule or protein-ligand complex in a new crystal form. The measured X-ray diffraction properties of the new crystal are compared with the search model structure to compute the position and orientation of the protein in the new crystal. Computer programs that can be used for this purpose include X-PLOR and AMORE (J. Navaza, 1994). Once the position and orientation are known, an electron density map can be calculated using the search model to provide X-ray phases. Thereafter, the electron density is inspected for structural differences, and the search model is modified to conform to the new structure. Using this approach, it will be possible to use the claimed structure of the AcpS protein to solve the three-dimensional structures of any such AcpS protein. Other computer programs that can be used to solve the structures of such AcpS crystals include QUANTA, CHARMM. INSIGHT, SYBYL, MACROMODE, and ICM.

[0085] For all of the drug screening assays described herein, further refinements to the structure of the drug will generally be necessary and can be made by the successive iterations of any and/or all of the steps provided by the particular drug screening assay.

[0086] Binding and Other Assays for Drug Screening

[0087] Once identified by computer modeling techniques, candidate compounds can be tested for biological activity using standard techniques. For example, such compounds can be used in assays to assess inhibition of AcpS enzymatic activity, or binding assays using conventional formats to screen inhibitors. Examples of such assays include enzyme-linked immunosorbent assays (ELISA) or fluorescence quench assays. Such compounds can also be tested in in vitro assays designed to assess growth inhibition or killing of the microorganism harboring such enzymes, or in vivo in infected hosts.

[0088] It should be noted that the present invention encompasses the use of analogs and derivatives that have the same or substantially similar enzymatic activity as that of the Streptococcus pneumoniae AcpS protein exemplified herein. Such derivatives and analogs include, but are not limited to, AcpS proteins containing amino acid additions, substitutions, or deletions that result in proteins functionally equivalent to the Streptococcus pneumoniae AcpS protein disclosed herein.

[0089] AcpS Peptide, Polvpeptide, and Protein Variants

[0090] The present invention encompasses AcpS having the amino acid sequence shown in SEQ ID NO: 1, as well as fragments of this protein containing an active site, fusions of AcpS with other proteins, fusions of fragments of this protein containing an active site, as well as amino acid variants of any of these sequences that retain AcpS enzymatic activity.

[0091] The peptides, polypeptides, and proteins of the present invention, or variants thereof, can comprise any number of contiguous amino acid residues. The subsequence of contiguous amino acids derived from the protein sequence disclosed herein can be at least about 20, at least about 30, at least about 40, at least about 50, at least about 60, at least about 70, at least about 80, or at least about 90 amino acids in length. Furthermore, the number of contiguous amino acid residues in such subsequences can be any integer selected from the group consisting of from 1 to 20, such as 2, 3, 4, or 5.

[0092] In a further aspect, the present invention encompasses an isolated AcpS peptide, polypeptide, or protein comprising an amino acid sequence having at least about 80% sequence identity, preferably at least about 81% sequence identity, more preferably at least about 82% sequence identity, yet more preferably at least about 83% sequence identity, yet more preferably at least about 84% sequence identity, yet more preferably at least about 85% sequence identity, yet more preferably at least about 86% sequence identity, yet more preferably at least about 87% sequence identity, yet more preferably at least about 88% sequence identity, yet more preferably at least about 89% sequence identity, yet more preferably at least about 90% sequence identity, yet more preferably at least about 91% sequence identity, yet more preferably at least about 92% sequence identity, yet more preferably at least about 93% sequence identity, yet more preferably at least about 94% sequence identity, yet more preferably at least about 95% sequence identity, yet more preferably at least about 96% sequence identity, yet more preferably at least about 97% sequence identity, yet more preferably at least about 98% sequence identity, and even yet more preferably at least about 99% sequence identity, to the corresponding region of the AcpS protein of the present invention (SEQ ID NO: 1).

[0093] In a further aspect, the present invention relates to an isolated peptide, polypeptide, or protein comprising an amino acid sequence scoring at least about 80% positives, preferably at least about 81% positives, more preferably at least about 82% positives, yet more preferably at least about 83% positive, yet more preferably at least about 84% positives, yet more preferably at least about 85% positives, yet more preferably at least about 86% positives, yet more preferably at least about 87% positives, yet more preferably at least about 88% positives, yet morepreferably at least about 89% positives, yet more preferably at least about 90% positives, yet more preferably at least about 91% positives, yet more preferably at least about 92% positives, yet more preferably at least about 93% positives, yet more preferably at least about 94% positives, yet more preferably at least about 95% positives, yet more preferably at least about 96% positives, yet more preferably at least about 97% positives, yet more preferably at least about 98% positives, yet more preferably at least about 99% positives, when compared with the amino acid sequence of corresponding residues shown in SEQ ID NO:1.

[0094] The present invention encompasses biochemically active variants of the AcpS protein disclosed herein. Biochemical activity includes, for example, AcpS enzymatic activity. Such biochemically active peptides, polypeptides, and proteins have activity that is at least about 20%, 30%, or 40%, preferably at least about 50%, 60%, or 70%, and most preferably at least about 80%, 90%, or 95%-100% of that of the corresponding native (non-synthetic) AcpS protein. Furthermore, the ligand binding specificity of such variant AcpS molecules is substantially similar to that of the corresponding native (non-synthetic) protein. Typically, the ligand binding specificity will be at least about 30%, 40%, or 50% that of the corresponding native (non-synthetic) protein, and more preferably at least about 60%, 70%, 80%, or 90%-100% thereof. Methods of assaying and quantifying measures of biochemical activity and ligand binding by AcpS are described herein; others are well known to those of skill in the art.

[0095] The term “amino acid” is used herein in its broadest sense, and includes naturally occurring amino acids as well as non-naturally occurring amino acids, including amino acid analogs and derivatives. The latter includes molecules containing an amino acid moiety. One skilled in the art will recognize, in view of this broad definition, that reference herein to an amino acid includes, for example, naturally occurring proteogenic L-amino acids; D-amino acids; chemically modified amino acids such as amino acid analogs and derivatives; naturally occurring non-proteogenic amino acids such as norleucine, β-alanine, ornithine, etc.; and chemically synthesized compounds having properties known in the art to be characteristic of amino acids. As used herein, the term “proteogenic” indicates that the amino acid can be incorporated into a peptide, polypeptide, or protein in a cell through a metabolic pathway.

[0096] In addition to using D-amino acids, those of ordinary skill in the art are aware that modifications in the amino acid sequence of a peptide, polypeptide, or protein can result in equivalent, or possibly improved, second generation peptides, etc., that display equivalent or superior functional characteristics when compared to the original amino acid sequences. Alterations in the AcpS peptides, polypeptides, or proteins of the present invention can include one or more amino acid insertions, deletions, substitutions, truncations, fusions, shuffling of subunit sequences, and the like, either from natural mutations or human manipulation, provided that the sequences produced by such modifications have substantially the same (or improved or reduced, as may be desirable) activity(ies) as the naturally occurring counterpart sequences disclosed herein.

[0097] One factor that can be considered in making such changes is the hydropathic index of amino acids. The importance of the hydropathic amino acid index in conferring interactive biological function on a protein has been discussed by Kyte and Doolittle (1982). It is accepted that the relative hydropathic character of amino acids contributes to the secondary structure of the resultant protein. This, in turn, affects the interaction of the protein with molecules such as enzymes, substrates, receptors, ligands, DNA, antibodies, antigens, etc. Based on its hydrophobicity and charge characteristics, each amino acid has been assigned a hydropathic index as follows: isoleucine (+4.5); valine (+4.2); leucine (+3.8); phenylalanine (+2.8); cysteine/cystine (+2.5); methionine (+1.9); alanine (+1.8); glycine (−0.4); threonine (−0.7); serine (−0.8); tryptophan (−0.9); tyrosine (−1.3); proline (−1.6); histidine (−3.2); glutamate/glutamine/aspartate/asparagine (−3.5); lysine (−3.9); and arginine (−4.5).

[0098] As is known in the art, certain amino acids in a peptide, polypeptide, or protein can be substituted for other amino acids having a similar hydropathic index or score and produce a resultant peptide, etc., having similar biological activity, i.e., which still retains biological functionality. In making such changes, it is preferable that amino acids having hydropathic indices within ±2 are substituted for one another. More preferred substitutions are those wherein the no acids have hydropathic indices within ±1. Most preferred substitutions are those wherein the amino acids have hydropathic indices within ±0.5.

[0099] Like amino acids can also be substituted on the basis of hydrophilicity. U.S. Pat. No. 4,554,101 discloses that the greatest local average hydrophilicity of a protein, as governed by the hydrophilicity of its adjacent amino acids, correlates with a biological property of the protein. The following hydrophilicity values have been assigned to amino acids: arginine/lysine (+3.0); aspartate/glutamate (+3.0±1); serine (+0.3); asparagine/glutamine (+0.2); glycine (0); threonine (−0.4); proline (−0.5±1); alanine/histidine (−0.5); cysteine (−1.0); methionine (−1.3); valine (−1.5); leucine/isoleucine (−1.8); tyrosine (−2.3); phenylalanine (−2.5); and tryptophan (−3.4). Thus, one amino acid in a peptide, polypeptide, or protein can be substituted by another amino acid having a similar hydrophilicity score and still produce a resultant peptide, etc., having similar biological activity, i.e., still retaining correct biological function. In making such changes, amino acids having hydropathic indices within ±2 are preferably substituted for one another, those within ±1 are more preferred, and those within ±0.5 are most preferred.

[0100] As outlined above, amino acid substitutions in the AcpS molecules of the present invention can be based on the relative similarity of the amino acid side-chain substituents, for example, their hydrophobicity, hydrophilicity, charge, size, etc. Exemplary substitutions that take various of the foregoing characteristics into consideration in order to produce conservative amino acid changes resulting in silent changes within the present peptides, etc., can be selected from other members of the class to which the naturally occurring amino acid belongs. Amino acids can be divided into the following four groups: (1) acidic amino acids; (2) basic amino acids; (3) neutral polar amino acids; and (4) neutral non-polar amino acids. Representative amino acids within these various groups include, but are not limited to: (1) acidic (negatively charged) amino acids such as aspartic acid and glutamic acid; (2) basic (positively charged) amino acids such as arginine, histidine, and lysine; (3) neutral polar amino acids such as glycine, serine, threonine, cysteine, cystine, tyrosine, asparagine, and glutamine; and (4) neutral non-polar amino acids such as alanine, leucine, isoleucine, valine, proline, phenylalanine, tryptophan, and methionine.

[0101] Particularly preferred conserved amino acid substitutions are:

[0102] (a) Lys for His or for Arg, or vice versa, such that a positive charge is maintained;

[0103] (b) Glu for Asp, or vice versa, such that a negative charge is maintained;

[0104] (c) Ser for Thr, or vice versa, such that a free —OH group is maintained;

[0105] (d) Gln for Asn, or vice versa, such that a free —NH2 group is maintained;

[0106] (e) Ile for Leu or for Val, or vice versa, as roughly equivalent hydrophobic amino acids; and

[0107] (f) Phe for Tyr, or vice versa, as roughly equivalent aromatic amino acids.

[0108] Non-conservative amino acid substitutions can also be introduced if they do not substantially affect either the ligand binding or enzymatic properties of the AcpS protein. Such non-conservative amino acid substitutions can occur in regions of the protein not involved in drug candidate binding, but can also be tolerated in regions involved in such binding if they do not significantly affect such binding, i.e., binding of the ligand occurs substantially the same as in the wild-type Streptococcus pneumoniae AcpS protein. It should be noted that changes that are not expected to be advantageous can also be useful if these result in the production of functional sequences. Since small peptides, etc., can be easily produced by conventional solid phase synthetic techniques, the present invention includes peptides, etc., such as those discussed herein, containing the amino acid modifications discussed above, alone or in various combinations. To the extent that such modifications can be made while substantially retaining the activity of the peptide, etc., they are included within the scope of the present invention. The utility of such modified peptides, etc., can be determined without undue experimentation by, for example, the methods described herein.

[0109] While biologically functional equivalents of the present AcpS molecules can have any number of conservative or non-conservative amino acid changes that do not significantly affect their activity(ies), or that increase or decrease activity as desired, 40, 30, 20, 10, 5, or 3 changes, such as 1-30 changes or any range or individual value therein, may be preferred. In particular, 10 or fewer amino acid changes may be preferred. More preferably, seven or fewer amino acid changes may be preferred; more preferably, five or fewer amino acid changes may be preferred; most preferably, three or fewer amino acid changes may be preferred. The encoding nucleotide sequences (gene, plasmid DNA, cDNA, synthetic DNA, or mRNA, for example) will thus have corresponding base substitutions, permitting them to code on expression for the biologically functional equivalent forms of the AcpS molecules. In any case, the AcpS peptides, polypeptides, or proteins exhibit the same or similar biological or immunological activity(ies) as that(those) of the AcpS molecule specifically dislcosed herein, or increased or reduced activity, if desired.

[0110] The activity(ies) of the variant AcpS molecules can be determined by the methods described herein or as are known in the art. Variant AcpS molecules biologically functionally equivalent to those specifically disclosed herein have activity(ies) differing from those of the presently disclosed molecules by about ±50% or less, preferably by about ±40% or less, more preferably by about ±30% or less, more preferably by about ±20% or less, more preferably by about ±10% or less, and even more preferably by about ±5% or less, when assayed by the methods disclosed herein, or as are known in the art.

[0111] Amino acids in an AcpS molecule of the present invention that are essential for activity can be identified by methods known in the art, such as site-directed mutagenesis or alanine-scanning mutagenesis (Cunningham and Wells, 1989). The latter procedure introduces single alanine mutations at every residue in the molecule. The resulting mutant molecules are then tested for biological activity. Sites that are critical for ligand binding can also be identified by structural analysis such as crystallization, nuclear magnetic resonance, or photoaffinity labeling (Smith et al., 1992, and de Vos et al., 1992).

[0112] Methods of Drug Discovery/Design Using the Three-Dimensional Structure of Crystallized AcpS

[0113] The three-dimensional crystal structures and atomic coordinates disclosed herein can be used to model an AcpS. These atomic coordinates can be used to computationally design a chemical compound that binds to the active site of an AcpS, and inhibit the enzymatic activity thereof. Such chemical compounds can be used to treat or prevent a Streptococcus pneumoniae infection in a mammal in need thereof.

[0114] Numerous methods can be employed to discover/design compounds that bind to AcpS, inhibit its activity, and that can therefore exhibit effective antibacterial activity. It should be noted that in all the methods described herein, one can employ the atomic coordinates of the entire AcpS protein, or just those of an active site.

[0115] For example, one method of drug design comprises employing the structural coordinates of a crystal of Streptococcus pneumoniae AcpS to computationally evaluate the ability of a chemical compound to interact with, e.g., bind to an active site of, the AcpS. Such chemical compound can be a competitive, non-competitive, uncompetitive, or mixed inhibitor that binds to, or inhibits the enzymatic activity of, AcpS. For example, the compound can be a competitive inhibitor that binds to the catalytic active site of AcpS.

[0116] Another method comprises employing the structural coordinates of a crystal of Streptococcus pneumoniae AcpS to identify an intermediate in a biochemical reaction between AcpS and a compound that is a substrate or inhibitor of this enzyme.

[0117] Another method of designing a candidate compound that binds to or inhibits Streptococcus pneumoniae AcpS comprises:

[0118] (a) providing the three-dimensional structure of a crystal of Streptococcus pneumoniae AcpS defined by the atomic coordinates shown in Tables 3 and 4, wherein the atomic coordinates include the active site of the synthase; and

[0119] (b) designing a candidate compound based upon the three-dimensional crystal structure of the active site of the enzyme.

[0120] Another method of designing a compound useful for inhibiting Streptococcus pneumoniae AcpS comprises:

[0121] (a) obtaining a crystal of Streptococcus penumoniae AcpS;

[0122] (b) evaluating the three-dimensional structure of the crystal;

[0123] (c) synthesizing or obtaining from a pre-existing chemical or computer library a potential inhibitor compound based on the three-dimensional crystal structure of the crystal;

[0124] (d) contacting the Streptococcus pneumoniae AcpS and the potential inhibitor compound; and

[0125] e) assaying the Streptococcus pneumoniae AcpS for activity, wherein a decrease in activity of the AcpS in the presence of the compound compared to the activity of the AcpS in the absence of the compound identifies the compound as an inhibitor of Streptococcus pneumoniae AcpS.

[0126] Another method of identifying a compound that binds to and inhibits the enzymatic activity of Streptococcus pneumoniae AcpS or any other AcpS comprising the same or similar active site coordinates (active site configuration) as those of Streptococcus pneumoniae AcpS comprises:

[0127] (a) introducing into a suitable computer program, e.g., a docking program, an algorithm for structure-based ligand design/optimization, etc., information defining the conformation of the catalytic active site of Streptococcus pneumoniae AcpS, wherein the program displays the three-dimensional structure of the catalytic active site;

[0128] (b) creating a three-dimensional representation of the active site cavity of the Streptococcus pneumoniae AcpS in the computer program;

[0129] (c) displaying and superimposing a model of the compound on the three-dimensional representation of the active site cavity of the AcpS;

[0130] (d) assessing whether the compound model fits spatially into the active site;

[0131] (e) incorporating the compound in a biological or biochemical activity assay for an AcpS comprising the active site; and

[0132] (f) determining whether the compound inhibits AcpS activity in the assay.

[0133] In another method, the coordinates in Tables 3 and 4 can be used to identify the active site of AcpS, and the obtained information can then be used for visual analysis/inspection of enzyme/inhibitor interactions to identify a compound that inhibits the function of AcpS.

[0134] Another method of identifying an inhibitor of AcpS activity comprises docking a computer representation of a first compound structure with a computer representation of the structure of the cavity formed by the active site of an AcpS, thereby forming a complex between the first compound and the AcpS. The method can further comprise:

[0135] (a) removing the computer representation of the first compound from the active site, and docking a computer representation of a second compound selected from a computer data base with the computer representation of the active site, thereby forming a second complex comprising the second compound and the AcpS active site;

[0136] (b) determining a conformation of the second complex of step (a) with a favorable geometric fit and favorable complementary interactions; and

[0137] (c) identifying a compound that best fits the active site as a potential modulator of the AcpS activity.

[0138] This method can further comprise:

[0139] (a) modifying the computer representation of the first compound by deleting one or more chemical groups from the first compound, or by adding one or more chemical groups to the first compound, thereby forming a second complex;

[0140] (b) determining a conformation of the second complex of step (a) with a favorable geometric fit and favorable complementary interactions; and

[0141] (c) identifying a compound that best fits said active site as a potential modulator of the AcpS activity.

[0142] This method can further comprise:

[0143] (a) removing the computer representation of the first compound complexed with the AcpS active site; and

[0144] (b) searching a database for a second compound structurally similar to the first compound using a compound searching computer program, or replacing portions of the first compound with chemical structures from a database using a compound construction computer program.

[0145] Furthermore, structural information on the interaction of a compound with AcpS can be used to place another compound in the active site, or to perform a virtual screen of a computer library of compounds to identify a lead compound by structure-based drug design.

[0146] The foregoing methods can further comprise:

[0147] (a) incorporating the second compound in a biological or biochemical activity assay for an AcpS comprising the active site; and

[0148] (b) determining whether the second compound inhibits the AcpS enzymatic activity in the assay.

[0149] Another method of identifying an inhibitor that competitively binds to the active site of Streptococcus pneumoniae AcpS or other acyl carrier protein synthase having the same or similar active site atomic coordinates comprises:

[0150] (a) providing the atomic coordinates of the active site to a computerized modeling system;

[0151] (b) identifying a compound that binds to the active site; and

[0152] (c) screening the compound identified in step (b) for AcpS inhibitory activity.

[0153] Another method of the present invention encompasses solving a crystal structure by using the structural coordinates of Streptococcus pneumoniae AcpS, or a portion thereof, as disclosed herein to solve a crystal form of a mutant, homologue, or co-complex of this AcpS by molecular rearrangement.

[0154] Yet other methods of the present invention relate to determining the three-dimensional structure of AcpS enzymes of unknown structure by using information derived from the three-dimensional structure of AcpS as disclosed herein. One such method comprises:

[0155] (a) aligning a computer representation of the amino acid sequence of Streptococcus pneumoniae AcpS with a computer representation of the amino acid sequence of another acyl carrier protein synthase by matching homologous regions of amino acid sequences of these representations;

[0156] (b) transferring computer representations of the amino acid sequence in said other acyl carrier protein synthase to computer representations of corresponding amino acid sequences in the three-dimensional structure of Streptococcus pneumoniae AcpS; and

[0157] (c) determining a low energy conformation of the other acyl carrier protein synthase structure resulting from step (b).

[0158] Another such method of determining the three-dimensional structure of an acyl carrier protein synthase of unknown structure comprises:

[0159] (a) determining the secondary structure of Streptococcus pneumoniae AcpS having the structural atomic coordinates set forth in Tables 3 and 4 using NMR data; and

[0160] (b) simplifying the assignment of through-space interactions of amino acids.

[0161] Another method encompassed by the present invention is one for designing a ligand that binds to the active site domain of AcpS. Such method can be computer-based, and can comprise:

[0162] (a) providing a model of the crystal structure of the active site domain of Streptococcus pneumoniae AcpS;

[0163] (b) analyzing the model to design a ligand that binds to the active site domain; and

[0164] (c) determining the effect of the ligand on the active site.

[0165] Such an effect might be a conformational change in the active site, covalent bond formation, etc. This method can further comprise modifying the ligand to improve the binding affinity to AcpS, selectivity to AcpS, or both, of the ligand.

[0166] Also encompassed by the present invention are antibacterial compounds that modulate AcpS activity, by, for example, binding to and/or inhibiting AcpS, discovered or designed by any of the foregoing methods. Non-limiting examples of such compounds include a compound selected from a computer database, a compound constructed from chemical groups selected from a computer database, a chemically synthesized compound, a naturally occurring compound, a peptide, peptidomimetic, or a natural product molecule that binds in the active site of Streptococcus pneumoniae AcpS.

[0167] Such compounds can be used in methods of preventing or treating a Streptococcus pneumoniae infection, or other infection caused by a microorganism having an AcpS enzyme, by administering to a patient in need thereof a pharmaceutically effective amount of such compound.

[0168] In addition to the foregoing applications of AcpS crystals, the present invention also encompasses the use of such crystals for a variety of other purposes, such as those discussed below.

[0169] AcpS Crystalline Compositions

[0170] Enzymes can be employed in a variety functions, such as, for example, as catalysts in large and/or laboratory scale economical production of fine and specialty chemicals (Jones, J. B., Tetrahedron 42: 3351-3403 (1986)), and as tools for the synthesis of organic compounds (Wong, C. H., Science 244: 1145-1152 (1989); Chemtracts-Org. Chem. 3: 91-111 (1990); Klibanov, A. M., Ace. Chem. Res. 23: 114-120 (1990)).

[0171] In the clinical area, enzymes can be used in extracorporeal therapy, such as hemodialysis and hemofiltration, where the enzymes selectively remove waste and toxic materials (Klein, M. and Langer, R., Trends in Biotechnology 4: 179-185 (1986)). Enzymes are used in these areas because they function efficiently as catalysts for a broad range of reaction types, at modest temperatures, with substrate specificity, and with stereoselectivity. Nonetheless, there are disadvantages associated with the use of soluble enzyme catalysts that limit their use in industrial and laboratory chemical processes (Akiyama et. al., Chemtech 627-634 (1988)).

[0172] Enzymes are expensive and relatively unstable compared to most industrial and laboratory catalysts, even when used in aqueous media where they normally function. Many of the more economically interesting chemical reactions carried out in common practice are incompatible with aqueous media, where, for example, substrates and products are often insoluble or unstable, and where hydrolysis can compete significantly. In addition, the recovery of soluble enzyme catalyst from product and unreacted substrate often requires the application of complicated and expensive separation technology. Finally, enzymes are difficult to store in a manner that retains their activity and functional integrity, for commercially reasonable periods of time (months to years) without resorting to refrigeration (4° C. to −80° C. to liquid N2 temperatures), or to maintenance in aqueous solvents of suitable ionic strength, pH, etc. The use of crystallized enzymatic proteins can avoid such limitations and is beneficial in medical, clinical, research, and industrial applications. For instance, the slow dissolution rate of protein crystals has been utilized to achieve sustained release of medications, such as crystalline formulations of insulin, interferon-alpha, and pancreatic enzymes. (see, e.g., Matsuda, et al. 1989 J. Biol. Chem. 264, 13381; Peseta, et al., in Annual Review of Biochemistry, Vol. 56, edited by Richardson, et al.; Annual Reviews: Palo Alto, 1989; p. 727; Brange, J. in The Galenics of Insulin. Berlin: Springer, 1987; Reichert, et al., Metal-interferon-alpha crystals. U.S. Pat. No. 5,441,734, 1995; Long, et al., Crystal Growth 1996, 168, 233; and reference to the Cross-Linked Enzyme Crystal formulations (CLEC®) of Altus Biologics Inc. USA).

[0173] Accordingly, the present invention encompasses crystal compositions of AcpS.

[0174] Such crystals can be produced as described herein or made according to any method in the art such as, e.g., those described in McPherson, et al. 2000 Annu Rev Biophys Biomol Struct.;29:361-410; McPherson, A 1998. Crystallization of Biological Macromolecules, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.; Gilliland, G. L. 1988. A biological macromolecule crystallization database: a basis for a crystallization strategy. J. Cryst. Growth 90: 51-59; Chernov A. A. 1998 Acta Crystallogr A. Nov 1;54(Pt 6 Pt 1):859-872; McPherson 1985 Methods Enzymol. 114:112; and Gilliland 1988 J. Crystal Growth 90: 51-59, which include a comprehensive list of suitable conditions in reviews of the crystallization literature. Such an AcpS crystal will be useful as a composition in medical, clinical, research, industrial and pharmaceutical applications as described herein.

[0175] In another particular embodiment, a crystal composition of the present invention is modified by creating an immobilized AcpS crystal of the invention, such as, for example, by linking AcpS crystals to each other and/or to a solid substrate (using any number of linking reagents and linking methods or linking means known in the art. For example, such as those described in U.S. Pat. No. 6,004,768; U.S. Pat. No. 6,042,824; WO 01/1638A2; Weygand, et al 2000 J. Mater Chem. 10:141-148; Pum, et al 2000 Nanotechnology 11: 100-107; and Ullman, 1991 An Introduction to Ultrathin Organic Films: From Langmuir-Blodgett to Self Assembly, Academic Press). Immobilized enzyme crystals retain their catalytic activity and have improved characteristics such as greater stability and resistance to degradation (see, e.g., S. J.. Bayne et al., “Enzymatically Active, Cross-Linked Pig Heart Lactate Dehydrogenase Crystals”, Carlsberg Res. Comm., 41, pp. 211-216 (1976); A. Dyer et al., “A Thermal Investigation of the Stability of Crystalline Cross-Linked Carboxypeptidase A”, Thermochimica Acta, 8, pp. 455-464 (1974); J. V Hupkes, “Practical Process Conditions for the Use of Immobilized Glucose Isomerase,” Starch, 30, pp. 24-28 (1978); P.J. Kasvinsky et al., “Activity of Glycogen Phosphorylase in the Crystalline State”, J. Biol. Chem., 251, pp. 6852-6859 (1976); and H. Mrsten et al., “Catalytic Activity of Non-Cross-Linked Microcrystals of Aspartate Aminotransferase in Poly (ethylene glycol)”, Biochem. J., 211, pp. 427-434 (1983)). Such immobilized AcpS crystals are also useful as a composition in medical, clinical, research, industrial and pharmaceutical applications as described herein.

[0176] In a more particular embodiment, an immobilized crystal composition of the invention is produced by linking an AcpS crystal with a bifunctional linking reagent, such as, for example, glutaraldehyde. This results in the stabilization of the crystal lattice contacts between the individual enzyme catalyst molecules constituting the crystal. As a result, the crystals are immobilized and function at elevated temperatures, extremes of pH and in harsh aqueous, organic, or near-anhydrous media, including combinations of such conditions. Therefore, in one embodiment, an immobilized crystal composition of the invention functions in environments incompatible with the functional integrity of corresponding uncrystallized, unimmobilized, and/or its corresponding enzyme in the native state.

[0177] In still further embodiments, immobilization of an AcpS crystal further encompasses without limitation, an AcpS crystal of the invention being: caged (such as, e.g., Schnur, J. M. 1993. Lipid tubules: A paradigm for molecularly engineered structures. Science 262: 1669-1676; Schnur, et al. 1994. Biologically engineered microstructures—controlled-release applications. J. Controlled Release 28 (1-3)(Jan.): 3-13); encapsulated (such as, e.g., in foams, fluids, gels, polymers or membranes see, e.g., WO 00/18972AD; WO 98/23734); tethered (such as, e.g., by an antibody or antibody binding fragment); coupled; bound to bacterial S-layers in predictable and geometrically well defined ways (see, e.g., Pum & Sleytr 1999 Trends in Biotechnology 17:8-11 and the references cited therein); coated (such as, e.g., with nanoparticles or polyelectrolyte molecules); electrostatically bound; layered; (such as, e.g., in 2D crystal arrangements); formed by placing AcpS proteins beneath lipid monolayers then subsequently stabilized into a durable geometric arrangement; covalently, or non-covalently bonded using any method in the art (such as, e.g., WO 00/77281 Al; U.S. Pat. No. 5,091,187; U.S. Pat. No. 5,716,709; McPherson, A 1998. Crystallization of Biological Macromolecules, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y. or; Gilliland, G. L. 1988. A biological macromolecule crystallization database: a basis for a crystallization strategy. J. Cryst. Growth 90: 51-59; Sára, et al. 1996 in Crystalline Bacterial Cell Surface Proteins (Sleytr, et al. Eds), pp. 133-159, R. G. Landesall).

[0178] Immobilized AcpS crystals can be lyophilized, producing AcpS compositions which can be stored at non-refrigerated (room) temperatures for extended periods of time, and which can be reconstituted in aqueous, organic, or mixed aqueous organic solvents of choice, without the formation of amorphous suspensions and with minimal risk of denaturation. The lyophilization of such resulting compositions provides a means of improving storage, handling, and manipulation properties of AcpS crystals of the invention. Use of the term “AcpS crystal” herein encompasses both immobilized and unimmobilized forms as described herein unless the context would clearly dictate otherwise to one skilled in the art to which it applies.

[0179] Using such crystal compositions, the present invention also encompasses methods of making selected products with them. For example, in the research and pharmaceutical area, AcpS crystals can be used in the preparation of acyl-carrier proteins (ACP) or ACP analogs or ACP derivatives such as, for example, ACP analogs with modified phosphopantetheines (see, e.g., Gehring, et al., 1997 “Ability of Streptomyces Acyl Carrier Proteins and Coenzyme A Analogs to Serve as Substrates in vitro for E. coli holo-ACP Synthase” in Chemistry and Biology 4:17). ACP analogs can be used to probe mechanistic questions in enzymes involved in the biosynthesis of fatty acids and they can also be used for commercial or pharmaceutical applications, such as, e.g., to facilitate the production of polyketides and polyketide derivatives, which have been shown to have many useful functions (for example, e.g., the polyketide antibiotic erythromycin A is used against Gram-positive bacterial infections, particularly against penicillin-resistant infections. Another polyketide, Amphotericin-B, is used primarily as an antifungal agent. The tetracyclines are broad-spectrum antibiotic polyketides that have activity against both Gram-positive and Gram-negative bacteria. Another important polyketide is doxorubicin (also known as Adriamycin), which is a widely used antitumor agent, particularly against solid tumors. Further, another interesting composition is the polyketide derivative lovastatin, a compound that has found wide use as a cholesterol reducing agent under the trade name of Mevacor®). Due to the broad substrate specificity of the AcpS enzyme, AcpS crystals themselves can also be used in the production of pharmaceutical reagents such as the above mentioned polyketides (see, e.g., Suo, et al. 2001 Proc Natl Acad Sci U S A 98(1):99-104). Accordingly, AcpS crystalline compositions are useful in the manufacture or catalysis of selected products such as for research, pharmaceutical, or industrial applications.

[0180] AcpS Crystalline Compositions for Use in Microelectronics

[0181] In still another embodiment, an AcpS crystal of the invention can be used, for example, as a fabrication material in the process, manufacture, and/or production of a microelectronic device. In one embodiment, AcpS protein crystals are employed using saturated solutions in the formation of a two-dimensional (2D) crystalline array on a solid support (such as, e.g., a silicon wafer). In 2D-nucleation growth, a 2D island is first nucleated on a flat crystal face. The 2d crystal island is a collection of molecules that are usually a single growth layer in height. Such an application of a crystal of the invention is useful as, for example, a nanometre-thick resist in semiconductor technologies and as a template for the formation of regularly arranged nanoparticles for applications in molecular electronics (see, e.g., Share, et al. Gradient composite replicas from protein crystal layer templates produced by pulsed laser deposition. PTB-Berichete, F-39, pp. 8-16; “Biologically Derived Nanometer-Scale Patterning on Chemically Modified Silicon Surfaces,” B. W. Holland, K. Douglas, N. A. Clark, Mat. Res. Soc. Symp. Proc. 330, 121 (1994); “Transfer of Biologically-Derived Nanometer-Scale Patterns to Smooth Substrates,” K. Douglas, G. Devaud, N. A. Clark, Science 257, 642 (1992); Abstract Y13.14 Laser Seeding for Biomolecular Crystallization Bancel, et al., from the 1998 March Meeting of The American Physical Society Los Angeles, Calif. showing a novel seeding technique in which a laser beam is used to select and transfer microscopic seed crystals in a growth solution; Allara, D. L. 1996. Nanoscale structures engineered by molecular self-assembly of functionalized monolayers. In Nanofabrication and Biosystems. Ed. H. C. Hoch, L. W. Jelinski, and H. G. Craighead. New York: Cambridge University Press, U.S. Pat. No. 5,597,457; WO 01/16328 for the application of proteins to a substrate. Additional references can be found in the work of Whitesides and colleagues which is described and referenced in WO 97/06468 and in the following patents: WO9954786 (A1) Elastomeric mask and use in fabrication of devices, including pixelated electroluminescent displays; WO9629629 (A2, A3), Microcontact printing on surfaces and derivative articles; W09707429 (A1), Self-assembled monolayer directed patterning of surfaces; WO9858967 (A1), Self-assembling peptide surfaces for cell patterning and interactions; U.S. Pat. No. 6,197,515, Molecular recognition at surfaces derivatized with self-assembled monolayers; U.S. Pat. No. 6,180,239, Microcontact printing on surfaces and derivative articles; U.S. Pat. No. 5,976,826, Device containing cytophilic islands that adhere cells separated by cytophobic regions; U.S. Pat. No. 5,900,160, Methods of etching articles via microcontact printing; U.S. Pat. No. 5,512,131, Formation of microstamped patterns on surfaces and derivative articles; U.S. Pat. No. 5,620,850, Molecular recognition at surfaces derivatized with self-assembled monolayers; U.S. Pat. No. 5,776,748, Method of formation of microstamped patterns on plates for adhesion of cells and other biological materials, devices and uses therefor.).

[0182] One advantage of using an AcpS crystal in microfabrication and in microlithography is that it permits the design and realization of smaller transistors that can be fabricated on a computer chip. Reduction in transistor size permits greater numbers of transistors in a defined area and thus faster data processing times that use less energy. Such reductions in transistor size support “Moore's Law,” which describes a predictable and continuing trend in the development of memory chip performance so that each new computer memory chip contains roughly twice as much capacity as its predecessor. Use of AcpS crystals in microchip fabrication provides another method for realizing “Moore's Law.”

[0183] Methods of fabricating microchips using proteins such as the AcpS crystals of the invention can be accomplished without undue experimentation using any known method in the art of protein engineering and microlithography. For example, one technique used in micro- and nanoelectronic applications is a microlithographic procedure using deep ultraviolet (DUV) laser irradiation for transferring (sub) micrometer patterns on a substrate to pattern 2D protein layers on silicon wafers (see, e.g., Pum, et al. 1996 Colloids Surf. B: Biointerfaces 8, 157-162; Pum, D. et al. 1997 Microelectron. Eng. 35, 297-300; and Calvert, J. M. 1993 J. Vaccine Sci. Technol. B 11, 2155-2163 and Pum & Sleytr 1999 Trends in Biotechnology 17:8-11). Typically, patterns are formed on 2D layers by bringing a chromium mask (on quartz glass) into direct contact with the 2D protein crystal layer on a silicon wafer. Upon irradiation with ArF pulses (DUV emitted after excitation of argon-fluoride gas in an excimer laser; wavelength 193 nm, dose ˜100 mJ per squared cm, pulse duration ˜8 nsec), the protein layer is completely removed in the exposed areas (i.e. without the mask) but retains its structural and functional integrity in the unexposed regions (i.e. masked areas). The masked or unexposed regions can subsequently be used to selectively bind other biologically functional molecules (here, for example, such as AcpS to form an AcpS/apo-ACP binding complex) or to be reinforced for subsequent reactive ion etching using any techniques in the art. Different etching rates between exposed and unexposed regions are necessary for reactive-ion etching and can obtained by reinforcing the protein layer (here, the AcpS layer) with silicon, a procedure known as silylation (see, e.g., Shaw, et al. 1989 J. Vaccine Sci. Technol. B 7, 1709). Using similar techniques, crystal protein layers are currently being produced for use as novel high-performance resists with thickness in the 10 nm range (see, e.g., Pum & Sleytr 1998 in Biological Molecules In Nanotechnology: The Convergence of Biolechnology, Polymer Chemistry and Materials Science, IBC Library Series pp.139-143 Southborough: International Business Communication, Inc.; Pum, et al. 1996 Colloids Surf. B: Biointerfaces 8, 157-162; WO 01/16328 Pum, et al. 1997 Microelectron. Eng. 35, 297-300).

[0184] Using these and similar techniques, one of skill in the art could use an AcpS crystal of the invention to serve as a fabrication mask and/or a template for improvements in silicon nano- and micro-fabrication technology. This is especially true in light of the recent successes in immobilizing biological nanoparticles (e.g., enzymes, antibodies, etc.) on these surfaces, leading to functional devices that can be employed as sensors, nanoelectrodes, prosthetic devices, or nanomachines.

[0185] AcpS Crystalline Compositions for Use in Biosensors

[0186] In another embodiment, a crystal composition of the invention is employed as a biomaterial for use in a biosensor. Biosensors use biomaterials, such as, e.g., an AcpS crystal of the application, to detect various substances of clinical, industrial, and other interest (see, e.g., Hall, E., Biosensors, Open University Press (1990)).

[0187] Biomaterials, such as those comprising a crystal of the invention (fabricated as described herein), can be integrated with a solid support using any number of strategies such as, e.g., those previously described herein and the following:

[0188] (1) by incorporation in organic or inorganic polymers that are associated with the solid matrices (see, e.g., Cosnier, S. (1997) Electropolymerization of amphiphilic monomers for designing amperometric biosensors. Electroanal. 9, 894-902; Kranz, C. et al. (1998) Controlled electrochemical preparation of amperometric biosensors based on conducting polymer multilayers. Electroanal. 10, 546-552; Willner, I. et al. (1992) Bioelectrocatalyzed reduction of nitrate utilizing polythiophene bipyridinium enzyme-electrodes. Bioelectrochem. Bioenerg. 29, 2945; Heller, A. (1992) Electrical connection of enzyme redox centers to electrodes. J. Phys. Chem. 96, 3579-3587; Gregg, B. A. and Heller, A. (1990) Cross-linked redox gels containing glucose-oxidase for amperometric biosensor applications. Anal. Chem. 62, 258-263; Gregg, B. A. and Heller, A. (1991) Redox polymer-films containing enzymes. 1. A redox-conducting epoxy cement—synthesis, characterization and electrocatalytic oxidation of hydroquinone. J. Phys. Chem. 95, 5970-5975; Gregg, B. A. and Heller, A. (1991) Redox polymer-films containing enzymes. 2. Glucose-oxidase containing enzyme electrodes. J. Phys. Chem. 95, 5976-5980; Walcarius, A. (1998) Analytical applications of silica-modified electrodes—a comprehensive review. Electroanal. 10, 1217-1235; Tsionsky, M. et al. (1994) Sol-gel-derived ceramic carbon composite electrodes—introduction and scope of applications. Anal. Chem. 66, 1747-1753);

[0189] (2) by the generation of physical blend composites between a biomaterial and an electronic element material (see, e.g., Wang, J. and Naser, N. (1994) Improved performance of carbon-paste amperometric biosensors through the incorporation of fumed silica. Electroanal. 6, 571-575; Hale, P. D. et al. (1991) Amperometric glucose biosensors based on redox polymer-mediated electron-transfer. Anal. Chem. 63, 677-682; Hale, P. D. et al. (1989) A new class of amperometric biosensor incorporating a polymeric electron-transfer mediator. J. Am. Chem. Soc. 111, 3482-3484; Kaku, T. et al. (1994) Amperometric glucose sensors based on immobilized glucose oxidase polyquinone system. Anal. Chem. 66, 1231-1235) e.g. redox enzymes in carbon paste blends); or

[0190] (3) by the incorporation of biomaterials in membrane assemblies organized on the transducers (Kinnear, K. T. and Monbouquette, H. G. (1993) Direct electron-transfer to Escherichia coli fumarate reductase in self-assembled alkanethiol monolayers on gold electrodes. Langmuir 2255-2257).

[0191] The functionalization of solid supports with monolayers, multilayers of controlled thickness, or thin film assemblies of biomaterials, reveals several attractive features for bioelectronic devices such as biosensors. Besides the fundamental feasibilities to structurally control, manipulate and address biomaterials such as protein crystals in 2D or thin 3D crystal arrays, these configurations exhibit practical advantages because they lack diffusional barriers, and biological processes that occur on the surface are rapidly translated to electronic outputs of a biosensor. The chemistry of surface modification of solid interfaces for use with monolayer and multilayer arrays has been addressed in several comprehensive review articles (see, e.g., Langmuir 2255-2257; Albery, W. J. and Hillman, A. R. (1982). Modified electrodes. Annu. Rep. Prog. Chem. Sect. C 78, 377-437; Murray, R. W. (1984) Chemically modified electrodes. In Electroanalytical Chemistry (Vol. 13) (Bard, A. J., ed.), pp. 191-368, Marcel Dekker, New York; Wrighton, M. S. (1986) Surface functionalization of electrodes with molecular reagents. Science 231, 32-37; Finklea, H. O. (1966) Electrochemistry of organized monolayers of thiols and related molecules on electrodes. In Electroanalytical Chemistry (Vol. 19) (Bard, A. J. and Rubinstein, I., eds), pp. 109-335, Marcel Dekker, New York; Zhong, C. J. and Porter, M. D. (1995) Designing interfaces at the molecular level. Anal. Chem. 67, 709A-715A.

[0192] For example, functionalized thiolate monolayers associated with gold electrodes have been used as base interfaces for the covalent linkage of biomaterials, for example, enzymes (Shoham, B. et al. (1995) A bilirubin biosensor based on a multilayer network enzyme electrode. Biosens. Bioelectron. 10, 341-352; Riklin, A. and Willner, I. (1995) Glucose and acetylcholine sensing multilayer enzyme electrodes of controlled enzyme layer thickness. Anal. Chem. 67, 4118-4126) or antibodies (Cohen, Y. et al. (1996) Modified monolayer electrodes for electrochemical and piezoelectric analysis of substrate-receptor interactions; novel immunosensor electrodes. J. Electroanal. Chem. 417, 65-75). Alternatively, functionalized siloxane films immobilized onto oxide solid supports can be used to assemble biomaterials on the oxide surfaces (Zou, C. F. and Wrighton, M. S. (1990) Synthesis of octamethylferrocene derivatives via reaction of (octamethylferrocenyl)methyl carbocation with nucleophiles and application to functionalization of surfaces. J. Am. Chem. Soc. 112, 7578-7584; Murray, R. W. (1980) Chemical modified electrodes. Acc. Chem. Res. 13, 135-141; Abruña, H. D. (1998) Coordination chemistry in 2 dimensions - chemically modified electrodes. Coord. Chem. Rev. 86, 135-189).

[0193] Using such teachings and knowledge in the art, one of ordinary skill could use a crystal composition of the invention as a biomaterial of a biosensor, for use in detecting and/or quantitating an analyte of interest, such as an analyte in a fluid, such as, for example a biological sample (e.g., a bodily fluid, such as, e.g., blood, urine, lavage, sputum, etc.), chemical and laboratory reaction media, organic media, water, culture media, foodstuffs, and beverages. In some instances, the fluid in question can be a gas.

[0194] In one particular embodiment, an AcpS crystal is used as a biomaterial in a biosensor and brought into contact with a fluid to detect an analyte. The analyte can be measured directly (such as, e.g., blood glucose level) or indirectly (e.g., such as by detecting or quantitating a substance which is a reactant (product or substrate) in a reaction in which the analyte of interest participates. In either case, the crystal composition is able to interact with the analyte or a substance that is a reactant in a reaction (such as, e.g., an analyte-binding partner that forms a binding complex with an AcpS crystal composition) in which the analyte also participates. The interaction of a crystal form of the enzyme of the invention with an analyte results in a detectable change such as, e.g., any of the following non-limiting examples: a change in pH; a colormetric change; a production of reaction product; a weight change; a change in an interference pattern (such as an interference pattern produced by a reflected wave, such as, e.g., a wave of light, a photon, a sound wave, a pressure wave, etc.); the production of light; a piezoelectric effect; a change in conductivity (such as, e.g., conductivity of: heat, light, ionic, electric, gravimetric, etc.); a change in heat; a change in electrical potential. Any such change detected and/or quantitated by any appropriate detecting means such as, e.g., without limitation: a pH electrode, a light or a heat sensing device, a means for measuring an interference pattern (e.g., such as a means for analyzing an interference pattern produced by coherent light), a means for measuring a fluctuation in weight; a means for measuring an enzymatic assay; a gravimetric detecting means; a means for measuring electrical charge; and/or a means for detecting a formation of an enzyme/binding partner complex is also encompassed herein. Any means useful for detecting a change resulting from an enzyme interaction with an analyte can be used and is encompassed by the present application. Typically a biosensor of the present invention comprises a crystal AcpS composition and a retaining means for the crystal which allows contact between the crystal(s) and an analyte of interest or a substance in a sample (e.g., such as a biological, organic, or inorganic sample) to produce a detectable change, such as, e.g., a change which is a reaction in which the analyte of interest participates.

[0195] In a more particular embodiment, a biosensor of the invention comprises amperometric detection of binding of an analyte, such as a binding agent, to a crystal composition of the invention (such as, e.g., a biomaterial comprising a 2D crystalline protein formation or a thin 3D crystal array). In this embodiment, the biosensor surface is an electrode, and the biomaterial is sufficiently closely packed and ordered (such as, e.g., in thin layer) to form an effective barrier to a current (across the biomaterial) mediated by, for example, a redox ion species in an aqueous solution in contact with the biomaterial layer. Binding of a binding agent to the biomaterial, e.g., the 2D crystalline protein formation or a or thin 3D crystal array, is sufficient to affect current flow (such as, e.g., current flow mediated by a redox species) so that binding to a crystal causes a shape change (such as, e.g., through cracking of the crystal and/or by shifting the order of the crystal packing), which subsequently permits a change in current flow across or through the biomaterial. In one such embodiment, a chamber in an apparatus is adapted to contain an aqueous solution of redox species in contact with a layer of a crystal of the invention, and the detector includes a circuit for measuring ion-mediated current across the layer in response to a binding event occurring between an AcpS crystal composition and an anaylate to form a binding complex with said crystal. The triggering event in such a biosensor is the binding of an anaylate to the AcpS crystal. Without being bound by theory, this binding can perturb the ordered structure of the biomaterial layer (or a sufficient number of individual crystals) to permit movement of redox species through the biomaterial to produce a detectable current or current change. In one example, the biosensor detects a binding event as an increase or decrease in current across an electrode, i.e., between working and counter electrodes. By analogy to a transistor, the redox solution serves as a “source,” the biomaterial layer as a “gate,” and the underlying electrode as the “drain.” Current in the biosensor “transistor” is initiated by applying a threshold voltage to the gate. In this embodiment, current is initiated by a stimulus to the monolayer “gate,” i.e., by binding to a crystal.

[0196] One extant example of an amperometric biosensor uses glucose oxidase modified with a ferrocene conductor. The modified enzyme is self-assembled onto a porous gold-black electrode to detect glucose in solution by exploiting an electron transfer pathway of the enzyme as a sensor (Aizawa, et al., 1996. Molecular assembly technology for biosensors. In Nanofabrication and Biosystems: Integrating Materials Science, Engineering And Biology. Ed. Hoch, et al., New York: Cambridge University Press).

[0197] In another embodiment, a biosensor is designed for gravimetric detection of binding of a binding agent to a crystal of the invention. In such an embodiment, the biosensor surface is a piezoelectric AcpS crystal.

[0198] The detector functions by generating a surface acoustic wave in the crystal and then detecting a shift in wave frequency, velocity, or resonance frequency of a surface acoustic wave produced in response to a binding event occurring between the crystal and an anaylate forming a binding complex with said crystal. Surface acoustic waves are generated in the crystal or crystal layer by any oscillator means. Not being bound by theory, but, according to currently accepted piezoelectric principles, the change in mass of the biomaterial resulting from binding of an AcpS crystal alters the frequency, resonance frequency, and/or wavelength of the surface acoustic waves, and at least one of these wave characteristics is measured by a detector means. The oscillator and detector collectively form a detector means for detecting binding of a binding agent to an AcpS crystal on the biosensor surface. Details of associated detector means in gravimetric biosensors are given, for example, in U.S. Pat. Nos. 5,478,756 and 4,789,804, and in PCT application WO 96/02830.

[0199] In still another embodiment, a biosensor encompassed herein is designed for optical surface plasmon resonance (SPR) detection of binding of a binding agent to a crystal composition of the invention. In this embodiment, the biosensor surface is a transparent dielectric substrate coated with a thin metal layer on which a 2D crystal layer or thin 3D crystal composition layer of the invention is formed so that the substrate and metal layer form a plasmon resonance interface. The detector functions to excite surface plasmons at a plasmon resonance angle which is dependent on the optical properties of the metal film and attached biomaterial layer, and to detect a shift in plasmon resonance angle in response to a binding event occurring between a crystal composition and an anaylate to form a binding complex.

[0200] Typical elements of a surface plasmon resonance (SPR) biosensor comprise: an open-top chamber in the biosensor which contains a waveguide composed of a dielectric film and a thin evaporated metal film constructed to support surface plasmon waves at the dielectric/metal film interface. The waveguide surface forms a biosensor surface having a crystal layer (such as, e.g., a crystalline 2D layer of AcpS or other finally deposited crystalline AcpS biomaterial). A light source directing a divergent light beam onto the biosensor surface through a lens. At some region along the length of the biosensor surface, the beam angle strikes the surface at an absorption angle at which absorption from the evanescent wave by surface plasmons occurs. The absorption angle will shift with changes in the composition of the biomaterial near the interface, that is, in response to binding events occurring at the crystal surface. The intensity of reflected light from each region along the biosensor surface is monitored by a photosensor whose photosensing grid is matched to specific detector surface regions, and which is operatively connected to an analyzer means. The light source and photosensor in this embodiment are referred to herein as biosensor means. In operation, the SPR absorption angle on the surface of the biomaterial is measured before and after addition of an analyte, with the measured shift in angle being proportional to the extent of binding of an analyte to form an AcpS/binding partner complex.

[0201] In an additional embodiment, a biosensor encompassed by the invention employs optical detection of binding of a binding agent to a crystal of the invention. The optical detector functions by irradiating a biomaterial surface of the biosensor with a light beam (such as, e.g., coherent light) and then detecting a change in the optical properties of the biomaterial. In one example, the detecting means uses ellipsometry (an optical physical measurement technique which can be used to measure small changes of refraction index at surfaces with high sensitivity, by measuring changes in elliptisity of polarized light, such as those caused by the presence of analyte biomolecules on the surface of a biomaterial of the invention) to detect binding.

[0202] Such biosensor applications can be used herein with a crystal composition of the present invention. More specifically, crystallized AcpS can be used in a biosensor application as described to detect the presence of a pathogen, such as e.g., but without limitation, the a bacterial or fungal agent that can cause a disease, disorder, condition, syndrome, or symptom such as, e.g., the following agents: Gram-Negative and Gram-positive bacteria and bacterial families and fungi such as: Actinomycetales (e.g., Corynebacterium, Mycobacterium, Norcardia), Cryptococcus neoformans, Aspergillosis, Bacillaceae (e.g., Anthrax, Clostridium), Bacteroidaceae, Blastomycosis, Bordetella, Borrelia (e.g., Borrelia burgdorferi), Brucellosis, Candidiasis, Campylobacter,Coccidioidomycosis, Cryptococcosis, Dermiatocycoses, E. coli (e.g., Enterotoxigenic E. coli and Enterohemorrhagic E. coli), Enterobacteriaceae (Klebsiella, Salmonella (e.g., Salmonella typhi, and Salmonella paratyphi), Serratia, Yersinia), Erysipelothrix, Helicobacter, Legionellosis, Leptospirosis, Listeria, Mycoplasmatales, Mycobacterium leprae, Vibrio cholerae, Neisseriaceae (e.g., Acinetobacter, Gonorrhea, Menigococcal), Meisseria meningitidis, Pasteurellacea Infections (e.g., Actinobacillus, Heamophilus (e.g., Heamophilus influenza type B), Pasteurella), Pseudomonas, Rickettsiaceae, Chlamydiaceae, Syphilis, Shigella spp., Staphylococcal, Meningiococcal, Pneumococcal and Streptococcal (e.g., S. typhimurium, Streptococcus pneumoniae and Group B Streptococcus).

[0203] For example, it has been shown that during infections AcpS proteins are specifically upregulated (e.g., the fadB gene of S. typhimurium (which encodes AcpS I) was identified in a screen for genes expressed during infection using in vivo expression technology (Mahan, et al. 1995 Proc Natl Acad Sci USA 92:669-673; and Mahan, et al. 1993 Infect Agents Dis 2:263-268) and the fadF gene also of S. typhimurium (which encodes AcpS II) was induced after the bacteria was phagocytosised by macrophages (DiRusso, et al. 1999 Progress in Lipid Research 38:129-197)). Accordingly, biological samples comprising an infectious agent and/or constituents thereof could be applied to a biosensor on a microchip for analytical, quantitative, and/or qualitative chemical analysis. Such “lab-on-a-chip” functions can be used for example, to determine the presence or level (compared to a control) of CoA and/or apo-ACP in a sample thus indicating the presence of an infectious agent. In another embodiment, AcpS crystals are used in a biosensor to determine binding agents that can modify an AcpS activity, for example, such as by acting as an agonist or antagonist.

[0204] Further embodiments of the present invention include computer-readable media encoded with data representing the atomic coordinates of the three-dimensional structure of Streptococcus pneumoniae AcpS, or computer-readable media having stored thereon a model comprising the three-dimensional structure of the catalytic active site domain of Streptococcus pneumoniae AcpS. As used herein, the term “computer-readable medium” refers to any medium that can be read and accessed directly by a computer. Such media include, but are not limited to, magnetic storage media, such as floppy discs, hard disc storage media, and magnetic tape; optical storage media, such as optical discs or CD-ROMs; electrical storage media, such as RAM and ROM; and hybrids of these categories, such as magnetic/optical storage media. Those of ordinary skill in the art 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 an amino acid or nucleotide sequence and/or atomic coordinates of the present invention.

[0205] Other features of the present invention will become apparent from the following examples, which are for illustrative purposes only, and which are not intended to limit the invention in any way.

EXAMPLE 1

Cloning of the S. pneumoniae acpS and acpP Genes; Expression and Purification of ACPS and ACPP

[0206] To understand better the function of AcpS in Streptococcus pneumoniae, a sphere-shaped, Gram-positive bacterium and major human pathogen of the upper respiratory tract, and to explore AcpS as an antibacterial target, the acpS and acpP genes of S. pneumoniae are cloned and expressed, and the gene products characterized. As disclosed below, the results disclosed herein demonstrate that S. pneumoniae AcpS shares many biochemical properties with E. coli AcpS. In addition, the results suggest that AcpS proceeds by an ordered reaction mechanism with the initial formation of the enzyme-apo-ACP intermediate from apo-ACP, followed by the transfer of 4′-phosphopantetheine from CoA to the apo-ACP of the complex. Finally, both acpS and acpP form complex operons with the genes whose functions are not required for fatty acid biosynthesis.

[0207] AcpS, an enzyme essential for bacterial fatty acid synthesis, catalyzes the transfer of 4′-phosphopantetheine from CoA to apo-ACP to form holo-ACP along with the production of 3′,5′-ADP, and is an attractive target for the development of antibacterial drugs. The structure of AcpS reveals an α/β fold, and demonstrates that the trimeric structure of the enzyme appears to be essential for the AcpS activity. These results represent the first structural determination of the interaction between the AcpS enzyme and its product, 3′,5′-ADP. These data provide a starting point for structure-based drug design efforts that should identify novel AcpS inhibitors with potent antibacterial activity.

[0208] To solve the structure of the S. pneumoniae AcpS, the protein is purified to homogeneity from an E. coli expression host using a three-step purification method (McAllister et al., 2000). The purified AcpS is crystallized as described below. Crystals of AcpS are obtained after 4-5 days at room temperature. Data are collected from these crystals, and the structure of AcpS is then solved by the multiple anomalous dispersion method (Hendrickson et al., 1991) (MAD) using selenomethionine-substituted protein and exploiting non-crystallographic 3-fold averaging.

[0209] Materials

[0210] Unless specified otherwise, all fine chemicals are from Sigma Chemical Company (St. Louis, Mo.). All fast protein liquid chromatography (FPLC) resins and columns used for protein purification, and strains and reagents for construction, expression, and purification of GST-fused proteins, are obtained from Amersham Pharmacia Biotech (Piscataway, N.J.). Luria Bertani (LB) broth medium is purchased from Bio101, Inc. (Vista, Calif.). All polyacrylamide gels and reagents are purchased from Novex (San Diego, Calif.). SYPRO Orange and Bradford protein assay reagents are purchased from BIO-RAD (Hercules, Calif.), and Sulfo-EGS (ethylene glycolbis(succinimidylsuccinate)) is obtained from Pierce (Rockford, Ill.). 3H-CoA (specific activity, 1.5 Ci/mmol) is custom-synthesized by NEN Life Science Products (Boston, Mass.).

Cloning and Expression of the acpS and acpP Genes of S. pneumoniae (hex-) R6

[0211] The acpS and acpP genes are cloned from S. pneumoniae by PCR using the same reagents, plasmids, and cell lines used for cloning and expression as described in Zhao et al., 1999. The sequences of the S. pneumoniae acpS gene and AcpS protein are disclosed in U.S. Pat. No. 6,060,282, issued May 9, 2000 (note also GenBank accession number AF276617). The acpS gene, 369 bp long, encodes a protein consisting of 122 amino acid residues, with a predicted molecular weight of 13.7 kDa (accession number AF276617). As disclosed in this patent, the deduced amino acid sequence of the S. pneumoniae AcpS protein consists of 122 amino acids, as follows (SEQ ID NO:1):

1Met Arg Met Ile Val Gly His Gly Ile Asp Ile Glu Glu Leu Ala SerIle Glu Ser Ala Val Thr Arg His Glu Gly Phe Ala Lys Arg Val LeuThr Ala Gln Glu Met Glu Arg Phe Thr Ser Leu Lys Gly Arg Arg GlnIle Glu Tyr Leu Ala Gly Arg Trp Ser Ala Lys Glu Ala Phe Ser LysAla Met Gly Thr Gly Ile Ser Lys Leu Gly Phe Gln Asp Leu Glu ValLeu Asn Asn Glu Arg Gly Ala Pro Tyr Phe Ser Gln Ala Pro Phe SerGly Lys Ile Trp Leu Ser Ile Ser His Thr Asp Gln Phe Val Thr AlaSer Val Ile Leu Glu Glu Asn His Glu Ser

[0212] It is not known if the AcpS protein as naturally produced by S. pneumoniae begins with Met Arg or Met Ile. For the purpose of the studies herein, a primer corresponding to the second Met start codon at the N-terminus of the foregoing sequence is designed and used for cloning the S. pneumoniae acpS gene. Thus, the acpS coding sequence used for expression of the protein herein produces an AcpS protein lacking the first two amino acid residues (Met Arg) of the foregoing sequence. Specifically, the following PCR primers are designed and used to amplify the acpS gene for cloning into E. coli expression systems. The 5′ PCR primer (5′-CGCGGATCCCATATGATAGTTGGACACGGAATTG -3′; SEQ ID NO:2) is designed at the second ATG start codon of acpS, and contains BamHI and NdeI sites for cloning purposes. The 3′ PCR primer (5′-CGCGGATCCCTAGCTTTCATGAATTTCCTCC -3′; SEQ ID NO:3) is designed at the stop codon of acpS, and contains a BamHI site after the stop codon. Using these primers, acpS is PCR amplified from S. pneumoniae for 25 cycles under the conditions described in Zhao et al., 1999. Five PCR reaction products are combined, and a portion of the pooled PCR products is digested with BamHI. The BamHI-digested PCR fragment is cloned into pCZA342, a low copy number plasmid (Baltz et al., 1997) that is digested with BamHI and dephosphorylated with calf intestinal alkaline phosphatase. acpS from several pCZA342 clones is sequenced, and a clone containing the consensus acpS gene sequence is used for constructing expression systems. This pCZA342 clone is digested with NdeI and BamHI. The NdeI-BamHI DNA fragment containing acpS is subcloned into pET-11a (Novagen). The resulting construct is designated as pRBP-19. The pCZA342 clone is also digested with BamHI, and the BamHI fragment of acpS is subcloned into pGEX-2T, resulting in pRBP-20.

[0213] To clone the acpP gene, the following PCR primers are used for amplification. 5′ PCR primer:

[0214] 5′-CGCGGATCCCATATGACAGAAAAAGAAATTTTTGACCGTATTG -3′ (SEQ ID NO:4); 3′ PCR primer:

[0215] 5′-CGCGGATCCGAATTCCTATTTTCCTTGAATGATTTTAACCACATC-3′ (SEQ ID NO:5). Using these primers, acpP is PCR amplified from S. pneumoniae as described above. The PCR products are digested with BamHI. The BamHI-digested PCR fragment is cloned into pCZA342. The pCZA342 clone is digested with NdeI and BamHI. The NdeI-BamHI DNA fragment containing acpP is subcloned into pET-11a (Novagen), resulting in pRBP-16.

[0216] Purification of AcPS and ACP of S. pneumoniae

[0217] LY128 (E. coli BL21 (pLysS)/pRBP-19) is first grown at 35° C. overnight in LB broth medium supplemented with 100 μg/ml ampicillin. The overnight culture (40 ml) is then inoculated into 1000 ml of LB medium supplemented with ampicillin, and grown at 33° C. with shaking at 250 rpm until an OD590 of 0.5-0.6 is reached. The culture is induced with 1 mM isopropyl-1-thio-β-D-galactopyranoside (IPTG) for 3 hr. Cells are harvested by centrifugation at 4500×g at 4° C. for 8 min, washed twice in phosphate buffered saline (PBS), resuspended in 50 mM citrate phosphate pH 6.0, and disrupted by passing twice through a French pressure cell. The resulting cell extract is centrifuged at 160,000×g for 40 min at 4° C. The supernatant fraction is collected and applied to a 15S Source S cation exchange column (2.5×8 cm) equilibrated with 50 mM citrate phosphate, pH 6.0 (buffer A). The column is washed with buffer A, and eluted with a linear gradient of 0-1.0M KCl in buffer A. Fractions (7 ml each) are collected. The presence of AcpS in the fractions is detected by SDS-PAGE analysis (16% tricine gels) (Laemmli, 1970). The fractions containing AcpS are pooled, and applied to an S-100 Sepharose preparative gel filtration fast protein liquid chromatography column (5.0×60 cm) equilibrated with 50 mM Tris-HCl, pH 7.0, 100 mM KCl. The fractions containing AcpS are collected, adjusted with glycerol to a final concentration of 15% (v/v), and stored in small aliquots at −70° C. Protein concentration is determined using a protein assay kit (Bio-Rad), with BSA as a standard (Bradford, 1976).

[0218] LY135 (E. coli XL1 Blue (mRF′)/pRBP-20) is grown, induced, harvested, disrupted, and centrifuged as above. The supernatant fraction is applied to a glutathione Sepharose 4B column (10 ml) equilibrated with 100 ml of PBS. The column is washed with 100 ml of PBS, and the GST-AcpS fusion protein is eluted with 10 mM glutathione in PBS. Fractions are analyzed by SDS-PAGE (12% glycine) and those fractions containing GST-AcpS are pooled, dialyzed against 50 mM Tris-HCl, pH 7.0 (4 liters), adjusted with glycerol to the final concentration of 15% (v/v), and stored at −70° C. as described above.

[0219] LY140 (E. coli BL21 (pLysS)/pRBP-16) is grown, induced, harvested, and disrupted as described above. The resulting cell extract is also centrifuged as described above. The supernatant fraction is collected and applied to a 15S Source Q-column (2.5×8 cm) equilibrated with 50 mM Tris-HCl, pH 8.0, 100 mM KCI (buffer C). The column is washed with 100 ml of buffer C, and eluted with a linear gradient of 0.0-1.0M KCl in buffer C. Fractions (7 ml each) are collected, and the presence of apo-ACP in the fractions is detected by SDS-PAGE as described above (16% tricine gels). The fractions containing apo-ACP are pooled and applied to an S-100 Sepharose gel filtration column (5×60 cm) equilibrated with 50 mM Tris-HCl, pH 7.0, 100 mM KCl. The column is eluted with the same buffer. Fractions (10 ml each) containing apo-ACP are collected, analyzed by electrospray mass spectrometry, and stored at −70° C. as described above.

[0220] As shown in FIG. 1, AcpS is highly expressed in E. coli, and exhibits the predicted molecular weight of approximately 13,000 daltons. The overexpressed AcpS is purified to apparent homogeneity in two steps using Source S-cation-exchange and gel filtration column chromatography (FIG. 1).

[0221] To confirm the purified protein as AcpS, N-terminal sequencing and mass spectrometric analyses are performed. The first 9 amino acid residues of AcpS purified as described above are determined to be MIVGHGIDI (SEQ ID NO:6), a sequence that is identical to the predicted amino acid sequence for the protein encoded by the cloned acpS gene. This encoded protein is predicted to have a molecular weight of 13,388. Consistent with this predicted value, mass spectrometric analysis shows that purified AcpS has a molecular weight of 13,390. Thus, the purified protein is S. pneumoniae AcpS.

[0222] Analysis of AcpS by Gel Filtration Column Chromatography

[0223] To determine the native structure of AcpS, a purified AcpS preparation (375 μg) is applied to an S-75 Superdex gel filtration column (HR 1.0×30 cm), equilibrated with 50 mM Tris-HCl, pH 7.0, 50 mM KCl, 10 mM MgCl2. The column is calibrated with protein molecular weight standards (Sigma). The effect of detergent or salt on the native structure of AcpS is analyzed by treating AcpS with 6 mM 3-cholamidopropyl-dimethylammonio-1-propane sulfonate/615 (CHAPS) or 50-500 mM KCl before and during column chromatography.

[0224] Sedimentation centrifugation analysis of AcpS is carried out using an XLA 10 ultracentrifuge (Beckman Instruments, Fullerton, Calif.). A purified AcpS preparation (adjusted to 0.2 and 0.4 mg/ml) is centrifuged at 16,000 rpm for 24 hr at 22° C. The absorbance at 280 nm as a function of radius after the system reaches equilibrium is analyzed using XL-A/XL-1, a non-linear least squares fit data analysis program. The partial specific volume of AcpS is calculated to be 0.721 ml/g based on its amino acid sequence. The molecular weight of AcpS is determined using a global fit of the two data sets collected with 0.2 and 0.4 mg/ml samples.

[0225] Cross-linking experiments are performed as follows. Purified AcpS and apo-ACP preparations (1 ml each) are dialyzed against 2 liters of 20 mM potassium phosphate buffer, pH 7.0, at 4° C. for 18 h. The dialyzed AcpS (163 μM) and apo-ACP (94 μM) preparations are mixed without or with 19.5 and 9.4 mM sulfo-EGS, respectively, and the mixtures are incubated at room temperature for 30 min. The reactions are stopped by the addition of 50 mM Tris-base, followed by incubation at room temperature for 30 min.

[0226] The resulting AcpS and apo-ACP preparations treated without or with the cross-linker (10 μl) are mixed with an equal volume of tricine sample buffer, and analyzed by SDS-PAGE (16% tricine gels).

[0227] To determine whether AcpS binds directly to apo-ACP or CoA in the absence of the other substrate, a purified AcpS preparation (27 μM) is first mixed with 10 mM MgCl2, and then either 100 μM apo-ACP or 50 μM CoA. The mixture is incubated at room temperature for 30 min and subjected to gel filtration column chromatography (S-75 Superdex) under the conditions described above. The fractions containing the AcpS-apo-ACP complex and unbound apo-ACP are analyzed by SDS-PAGE (16% tricine gels), SYPRO Orange staining, and mass spectrometry.

[0228] Enzyme Assay And Kinetics

[0229] Unless otherwise indicated, reaction mixtures contain 50 mM Tris-HCl, pH 7.0, 10 mM MgCl2, 2.5-50 μM CoA, 0.25-6.0 μM purified apo-ACP of S. pneumoniae, and 3.7 nM purified AcpS of S. pneumoniae, and are incubated at 37° C. for 9 min. Reactions are stopped by the addition of 50 mM EDTA. The formation of holo-ACP is determined by an HPLC or a trichloroacetic acid (TCA) precipitation method (see below). An HPLC-based assay is adapted from the method described previously (Lambalot and Walsh, 1997). This assay monitors the conversion of apo-ACP to holo-ACP. Reaction mixtures (100 μl each) are injected into an analytical HPLC column (Vydac protein C4 reverse-phase; P. J. Cobert Associates, Inc., St. Louis, Mo.) equilibrated with 45% acetonitrile in 0.1% trifluoroacetic acid. The column is eluted with an 8 ml linear gradient of 45-80% acetonitrile. The column elution profiles are monitored at 220 nm. Under these conditions, holo-ACP migrates faster than apo-ACP. The amount of holo-ACP formed is estimated by comparing the peak area of the holo-ACP formed with those of both apo- and holo-ACP.

[0230] AcpS activity is also assayed by using a TCA precipitation method (Lambalot and Walsh, 1995). This method measures the incorporation of the 3H-labeled 4′-phospho-pantotheine group from [3H]CoA into apo-ACP. Reaction conditions are the same as those described for the HPLC assay, except that [3H]COA (specific activity, 1.5 Ci/mmol, NEN Life Science Products, Boston, Mass.) is used alone or in combination with CoA. Reactions are stopped by the addition of 0.9 ml of cold 10% TCA followed by 37 μg of bovine serum albumin (BSA). Precipitated protein is collected by centrifugation (a microfuge at 14,000 rpm) for 5 min and washed twice with ice-cold 10% TCA. The protein collected is resuspended in 150 μl of 1M Tris base and 0.1% Triton X-100. The resulting suspension (100 μl) is mixed with 2.5 ml of Ready Protein+scintillation fluid (Beckman, Fullerton, Calif.), and counted using an LS 60001C scintillation counter (Beckman).

[0231] To examine the substrate specificity of AcpS, a variety of CoA derivatives (acetyl-CoA, malonyl-CoA, acetoacetyl-CoA, desulfo-CoA, and dephospho-CoA) are tested. All reaction mixtures contain 1.5 μM apo-ACP, 20 μM CoA or CoA derivative, and 19 nM AcpS, and the formation of holo-ACP is determined by the HPLC method.

[0232] For the determination of Km and Vmax (kcat) of AcpS for apo-ACP, reaction mixtures (in quadruplicate) contain 20 μM CoA, 0.25 to 100 μM apo-ACP, and 3.7 nM. AcpS. The formation of holo-ACP is measured by the HPLC method or the TCA precipitation method. To determine Km for CoA, the reaction conditions are the same as those described above except that the concentration of apo-ACP is 2.0 μM, and the concentrations of CoA were 5 to 600 μM.

[0233] To analyze the kinetic mechanisms of AcpS, AcpS activity is measured at different concentrations of both substrates. Reaction mixtures (in triplicate) contain 2.5-40 μM CoA, 0.25-2.0 μM apo-ACP, and 3.7 nM AcpS. The formation of holo-ACP is analyzed by the HPLC assay.

[0234] To evaluate the inhibition of AcpS activity by 3′,5′-ADP with respect to CoA, reaction mixtures contain 1-60 μM 3′,5′-ADP, 2.5-60 μM CoA, 1.0 μM apo-ACP, and 3.7 nM AcpS. To evaluate the inhibition of AcpS activity by 3′,5′-ADP with respect to apo-ACP, reaction mixtures contain 1-60 μM 3′,5′-ADP, 0.5-6.0 μM apo-ACP, 20 μM CoA, and 3.7 nM AcpS. The formation of holo-ACP is analyzed by the HPLC method.

[0235] Identification and Organization of the acpS and acpP Genes of S. pneumoniae

[0236] To understand the function of AcpS in the biosynthesis of fatty acids in S. pneumoniae, cloning and expression of the acpS and acpP gene that encodes a substrate of AcpS are carried out. Both genes are identified from an S. pneumoniae data base (Baltz et al., 1998) using the E. coli acpS and acpP gene sequences as queries in the BLAST program (Altschul et al., 1990). The acpS gene, 369 bp long, encodes a protein consisting of 122 amino acid residues (SEQ ID NO: 1) with a predicted molecular mass of 13.7 kDa (GenBank™ accession number AF276617). The acpS gene appears to be organized into an operon with genes in the order aroG-aroF-acpS-alr-recG as there are long non-coding regions located upstream of aroG and downstream of recg. Thus, the acpS operon appears to consist of the genes that are required in aromatic amino acid biosynthesis (aroF and aroG encoding 3-deoxy-D-arabino-heptulosonate 7-phosphate synthases), cell wall biosynthesis (alr encoding D-alanine racemase), and DNA recombination (recG). In this regard, the genomic organization of acpS in S. pneumoniae is quite different from that of acpS in E. coli since acps in E. coli consists of an operon with its upstream pdxj gene that is required for vitamin B6 biosynthesis (Lam et al., 1992; Takiff et al., 1992).

[0237] The acpp gene, 234 bp long, encodes a protein consisting of 77 amino acid residues, with a predicted molecular weight of 8.7 kDa (GenBank™ accession number AF276618). The acpP gene appears to consist of an operon with the genes in the order hisC-unknown-plsX-acp. There are very long non-coding regions located in the upstream of hisC and downstream of acpP. Like the acpS operon, the genes in the acpp operon are also involved in different aspects of cellular metabolism such as histidine biosynthesis (his C encoding histidinol phosphate aminotransferase), lipid biosynthesis (plsx, required for the phenotype of plsB that encodes glycerol 3-phosphate acyltransferase, an enzyme required for lipid biosynthesis), and possibly others (unknown function gene). It is known that the acpP genes in Bacillus subtilis, E. coli, Pseudomonas aeruginosa, and Vibrio harveyi are organized into operons with other fatty acid biosynthetic genes (Kutchma et al., 1999; Morbidoni et al., 1996; Rawlings and Cronan, 1992; Shen and Byers, 1996). Thus, the operon organization of the acpp gene in S. pneumoniae is also different from those of the acpp genes in E. coli and other organisms (Kutchma et al., 1999; Morbidoni et al., 1996; Rawlings and Cronan, 1992; Shen and Byers, 1996). Finally, it is known that plsx and acpp, along with other fatty acid biosynthetic genes, are also located in the same operon in B. subtilis, E. coli, P. aeruginosa, and V. harveyi (Kutchma et al., 1999; Morbidoni et al., 1996; Rawlings and Cronan, 1992; Shen and Byers, 1996). This suggests that a genetic reorganization event might have occurred during evolution, which resulted in the formation of the complex operons that currently exist in organisms such as S. pneumoniae.

[0238] The subunits of S. pneumoniae AcpS and apo-ACP exhibit molecular weights virtually identical to those of E. coli AcpS and apo-ACP, respectively. Both proteins also share 38% identities with their counterparts in E. coli. The pI value of S. pneumoniae AcpS is estimated to be 6.5, which is much lower than 9.98, the pI value of E. coli AcpS (Lam et al., 1992; Takiff et al., 1992). Therefore, S. pneumoniae AcpS is significantly less basic than E. coli AcpS. Like other AcpS (Cronan and Rock, 1996; Rock and Cronan, 1996; Kutchma et al., 1999; Morbidoni et al., 1996; Rawlings and Cronan, 1992; Shen and Byers, 1996), S. pneumoniae apo-ACP is very acidic with a pI value of only 3.4.

[0239] Whether the S. pneumoniae acpS gene complements E. coli mutant strain HT253, which is defective in the production of AcpS (Takiff et al., 1992), is also investigated. HT253 contains a mini-TnlO insertion in the pdxJ gene, which is upstream of and forms an operon with acpS (Lam et al., 1992; Takiff et al., 1992). The mini-Tn10 carries two divergent tetracycline-inducible promoters (Takiff et al., 1992). In the absence of tetracycline, HT253 cannot grow on LB plates because the mini-TnlO insertion in pdxj blocks the transcription of the acpS gene. Thus, the growth of HT253 is tetracycline-dependent. When the acpS gene (pRBP123, acpS carried on pGEX-2T) is introduced into HT253, this mutant strain is able to grow on LB medium without the supplementation of tetracycline and IPTG. Apparently, the basal level expression of acpS without IPTG induction is sufficient for the complementation of HT253. This result clearly shows that the S. pneumoniae acpS gene complements the E. coli mutant deficient in the production of AcpS. Attempts to inactivate the acpS gene of S. pneumoniae through genetic insertional mutagenesis have failed (Baltz et al., 1997; P. Treadway, unpublished results), indicating that acpS is essential for growth. Since recG and air, down stream of acpS, are not essential genes (Kullik et al., 1998; Lloyd et al., 1996), we conclude that the acpS gene is essential for the growth of S. pneumoniae. Taken together, these results establish the identity of the gene as acpS, and that the function of acpS is essential for the growth of bacterial cells.

[0240] Expression, Puirifcation, and Identification of the AcpS and ACP of S. pneumoniae

[0241] The acpS and acpP genes identified are cloned into expression vectors and expressed in E. coli as described above. Both AcpS and apo-ACP are highly expressed in E. coli, and exhibit the molecular weights predicted (FIG. 1). The overexpressed AcpS is purified to apparent homogeneity in two steps (FIG. 1A) using Source S-cation-exchange and gel filtration column chromatography. The overexpressed S. pneumoniae apo-ACP is also purified to apparent homogeneity (FIG. 1B) in two steps using Source Q-anion exchange and gel filtration column chromatography.

[0242] To confirm the purified proteins as AcpS and ACP, the proteins can be subjected to N-terminal sequencing and mass spectrometric analyses. The first 9 amino acid residues of purified AcpS are determined to be MIVGHGIDI (SEQ ID NO:6), a sequence that is identical to the predicted amino acid sequence for the protein encoded by the cloned acpS gene (compare SEQ ID NO: 1). This encoded protein is predicted to have a molecular weight of 13,388. Consistent with this predicted value, mass spectrometric analysis shows that purified AcpS has a molecular weight of 13,390. Thus, the purified protein is S. pneumoniae AcpS.

[0243] N-terminal sequencing analysis also shows that purified apo-ACP exhibits the predicted amino acid sequence (data not shown). When subjected to mass spectrometric analysis, purified apo-ACP is found to exhibit two peaks. The major peak has a molecular mass of 8,834 Da (about 80% of the total protein), while the minor peak has a molecular mass of 8,861 Da (20%) that is 26 Da larger than that of the major species. The predicted molecular weight for S. pneumoniae apo-ACP is 8,706, in agreement with the results of mass spectrometric analysis. Mass spectrometric analysis further shows that both apo-AcpS are converted to holo-ACP upon their reaction with AcpS, since the molecular weights of both AcpS increase by 341 Da, corresponding to the molecular weight of the 4′-phospho-pantetheine group (data not shown). Finally, mass spectrometric analysis shows that holo-ACP is not detectable in the apo-ACP preparations (data not shown).

[0244] The mobilities of apo-ACP and holo-ACP can be examined by native gel electrophoresis followed by staining with SYPRO Orange. Holo-ACP migrates more slowly than apo-ACP (data not shown). The complete conversion of apo-ACP to holo-ACP is confirmed by the fact that the molecular weight of ACP increases from 8,834 Da (apo-ACP) to 9,174 Da (holo-ACP) upon treatment of apo-ACP with AcpS, CoA, and Mg+2. Thus, unlike E. coli holo-ACP (5), S. pneumoniae holo-ACP migrates more slowly than apo-ACP.

[0245] Determination of the Native Structures of S. pneumoniae ACβS and ACP

[0246] The molecular weight of native AcpS can be determined by subjecting a purified AcpS preparation to gel filtration column chromatography analysis. AcpS is eluted in the fractions corresponding to a molecular weight of 38 kDa (FIG. 2A, peak B). This result suggests that AcpS is a homotrimer with a predicted molecular mass of 41 kDa (GenBank™ accession number AF276617). To confirm this further, a purified AcpS preparation is subjected to sedimentation analysis. This analysis shows that purified AcpS has a molecular mass of 39 kDa, which is consistent with the gel filtration analysis. Finally, when a purified AcpS preparation is subjected to cross-linking followed by SDS-PAGE analysis, two protein bands are observed (FIG. 3). The two bands have molecular masses of 10.4 and 28.2 kDa, respectively, corresponding to the monomeric and trimeric forms of AcpS (FIG. 3, lane 2). Taken together, these results demonstrate that the AcpS of S. pneumoniae is a trimeric enzyme. The trimeric structure of AcpS appears to be stable as AcpS retains its native structure in the presence of 6 mM CHAPS or 50-500 mM KCl during gel filtration column chromatography (data not shown).

[0247] When apo-ACP is subjected to gel filtration column chromatography, it elutes in the fractions corresponding to a molecular mass of 17 kDa, indicating that apo-ACP may exist as a dimer (FIG. 2A). apo-ACP has been shown to behave abnormally on gel filtration columns due to its molecular asymmetry in shape (Cooper et al., 1987; Rock and Cronan, 1979). To examine further whether apo-ACP is a dimer, purified apo-ACP is subjected to cross-linking followed by SDS-PAGE analysis. Only one protein band is observed, having a molecular mass of 5.6 kDa (FIG. 3B). This result demonstrates that apo-ACP is a monomeric protein. The result of the gel filtration column analysis is consistent with the previously reported anomalous behavior of apo-ACP on gel filtration columns (Cooper et al., 1987; Rock and Cronan, 1979).

EXAMPLE 2

Kinetic Characterization of S. pneumoniae AcpS

[0248] To elucidate the reaction mechanism of AcpS, its substrate specificity and kinetics are examined. When assayed by the HPLC method, purified AcpS of S. pneumoniae exhibits optimal activity at 45-50° C. and pH 6.5, and is stable at 22-65° C. AcpS is able to utilize a number of CoA derivatives as substrates, and exhibits the following relative activities: 100 (CoA), 91 (acetyl-CoA), 76 (desulfo-CoA), 65 (acetoacetyl-CoA), 12 (malonyl-CoA), and 0 (dephospho-CoA). Thus, like E. coli AcpS and Bacillus subtilis Sfp protein, S. pneumoniae AcpS utilizes different CoA derivatives as substrates (Gehring et al., 1997; Quadri et al., 1998).

[0249]

S. pneumoniae
AcpS appears to exhibit Michaelis-Menten kinetics when assayed at various CoA concentrations and apo-ACP concentrations lower than 10 μM (FIG. 4A). AcpS activity increases in a dose-dependent manner at apo-ACP concentrations of 0.5-5 μM (FIG. 4A). When the concentration of apo-ACP approaches 10 μM, AcpS activity decreases (FIG. 4A). This result is consistent with the observation that apo-ACP is inhibitory to AcpS at higher concentrations (Elovson and Vagelos, 1968; Lambalot and Walsh, 1995; Flugel et al., 2000; Gehring et al., 1997). However, a further increase of apo-ACP concentrations (>10 μM) is accompanied by a significant increase in AcpS activity (FIG. 4A). As a result, two separate substrate saturation curves are obtained at low and high concentrations of apo-ACP (FIG. 4, B and C). Double reciprocal plot analyses indicate that AcpS has Km (for apo-ACP) values of 0.5±0.08 and 109±6.8 μM, and Vmax values of 2439±243 (kcat=1.7±0.17 s-1) and 13659±1290 (kcat=9.3±0.9 s-1) nmol/min/mg at the low and high concentrations of apo-ACP, respectively. Thus, at higher apo-ACP concentrations, the affinity of AcpS for apo-ACP is significantly decreased (approximately 200-fold), but its catalytic activity is significantly increased (5-fold). Together, these results indicate that the S. pneumoniae AcpS may be allosterically regulated by its substrate, apo-ACP.

[0250] When a fixed apo-ACP concentration and various CoA concentrations are used, a hyperbolic substrate saturation curve is obtained for AcpS (FIG. 5A). The apparent Km and Vmax values of AcpS are determined to be 11.5±0.9 μM (for CoA) and 3976±73 nmol/min/mg (kcat=2.7±0.05 s-1), respectively (FIG. 5B). The kcat values determined for AcpS at low apo-ACP concentrations are thus in good agreement (1.7 versus 2.7 s−1).

[0251] Since the TCA precipitation method has been often used for the assay of AcpS activity (Elovson and Vagelos, 1968; Lambalot and Walsh, 1995; Flugel et al., 2000), we also characterize the kinetic properties of the enzyme using this assay method. This assay utilizes [3H]CoA as a substrate for AcpS. The apparent Km values of the enzyme for apo-ACP and CoA are determined to be 1.3±0.7 and 7.1±0.4 μM, respectively. The Vmax (kcat) values determined are 4179±182 (2.8±0.04 s−1) nmol/min/mg. Thus, the kinetic parameters determined by the TCA precipitation method are in general agreement with those obtained by the UPLC method. However, we did notice that the TCA precipitation method tends to generate variations significantly higher than those of the HPLC method, especially when apo-ACP is below 1 μM.

[0252] Although E. coli AcpS has been extensively studied (Elovson and Vagelos, 1968; Lambalot and Walsh, 1995; Flugel et al., 2000; Lambalot et al., 1996), the kinetic mechanism of this enzyme is unknown. To elucidate further the kinetic mechanism of S. pneumoniae AcpS, double reciprocal plots of the initial velocities of the enzyme at fixed concentrations of one substrate versus various concentrations of the other substrate (Copeland, 1996) are analyzed. This analysis yields Km and Vmax values that are similar to those determined before (data not shown). As shown in FIG. 6A, the double reciprocal plots of the initial velocities of AcpS obtained at the various CoA and fixed apo-ACP concentrations yields an intersecting pattern. The same pattern is obtained when various concentrations of apo-ACP and fixed concentrations of CoA are used (FIG. 6B). Taken together, these results suggest that AcpS proceeds by a random or compulsory ordered bi bi type, but not a ping-pong (double displacement) type, of reaction mechanism (Copeland, 1996).

[0253] To differentiate these two possible reaction mechanisms, the kinetics of product inhibition are analyzed. AcpS activity is examined in the presence of 3′,5′-ADP. As shown in FIG. 7A, when various CoA concentrations are used, the double reciprocal plots yield a simple competitive pattern with a Ki of 6.0 μM (FIG. 7C). However, when various apo-ACP concentrations are used, the double reciprocal plots yield a linear-mixed pattern with a Ki of 2.5 μM (FIG. 7, A and D). Since the patterns of inhibition with respect to CoA and apo-ACP are competitive and mixed, respectively, these results suggest that apo-ACP is probably the first substrate to bind to the enzyme, which is followed by CoA (Copeland, 1996).

EXAMPLE 3

Binding of apo-ACP and CoA to AcpS

[0254] The order of substrate binding to AcpS can be analyzed by determining the binding of CoA and apo-ACP to purified AcpS by gel filtration column chromatography, mass spectrometry, or filter binding assays. If CoA binds to AcpS first and forms an enzyme-substrate complex that is required for the next reaction with apo-ACP, then a stable enzyme-substrate complex should be detectable. When a mixture of CoA and purified AcpS incubated at room temperature for 30 min is subjected to gel filtration column chromatographic and mass spectrometric analyses, the CoA is not detectable in the fractions containing purified AcpS (data not shown). Thus, CoA does not appear to bind to AcpS in the absence of apo-ACP. To examine further the binding of CoA to AcpS, a mixture of purified AcpS and [3H]CoA incubated under the same conditions is subjected to a filter binding assay. Under these conditions, [3H]CoA does not appear to bind to AcpS as the radioactivity of [3H]CoA is not detectable after washing (data not shown). Consistent with the foregoing evidence, CoA does not appear to bind to AcpS in the absence of apo-ACP.

[0255] Whether apo-ACP binds to AcpS in the absence of CoA, a mixture of AcpS and apo-ACP (apo-ACP/AcpS=5:1) can be subjected to gel filtration column chromatography and analysis of the column fractions by SDS-PAGE. Two protein peaks are observed (FIG. 2A). The leading peak (peak A) has a molecular mass of approximately 53 kDa as judged by gel filtration analysis (FIG. 2A). Since AcpS exists as a trimer with a molecular mass of approximately 41 kDa, this leading peak probably represents a complex between apo-ACP and AcpS (FIG. 2A). Consistent with the formation of the AcpS-apo-ACP complex, the presence of apo-ACP is also detected in the fractions containing purified AcpS (FIG. 2B). Together, these results demonstrate that apo-ACP can bind to AcpS in the absence of CoA. In summary, the analysis of the initial velocities of AcpS obtained at fixed concentrations of one substrate and various concentrations of another reveals that catalysis by AcpS probably proceeds by a random or ordered compulsory bi bi reaction mechanism because an intersecting pattern was obtained regardless of which substrate (CoA or apo-ACP) was the fixed one or the varied one (Copeland, 1996) (FIG. 6). The inhibition kinetics of 3′,5′-ADP, one of the reaction products, indicates that AcpS catalysis appears to proceed by an ordered reaction mechanism, with the initial formation of an AcpS-apo-ACP intermediate and the subsequent transfer of 4′-phosphopantetheine from CoA onto apo-ACP. The mode of inhibition by 3′,5′-ADP with respect to CoA is competitive when apo-ACP is the fixed substrate and CoA is the varied substrate (FIG. 7). The competitive inhibition with respect to CoA indicates that CoA only binds to the enzyme-apo-ACP intermediate. The mode of inhibition by 3′,5′-ADP with respect to apo-ACP is mixed, i.e., a combination of competitive and noncompetitive inhibition when apo-ACP is the varied substrate and CoA is the fixed substrate (FIG. 7B). The mixed type of inhibition by 3′,5′-ADP with respect to apo-ACP suggests that 3′,5′-ADP binds to the free enzyme and the enzyme-apo-ACP intermediate. Thus, inhibition is competitive with respect to apo-ACP when 3′,5′-ADP binds to the free enzyme, and noncompetitive with respect to apo-ACP when 3′,5′-ADP binds to the enzyme-apo-ACP intermediate. This proposed reaction mechanism for AcpS is consistent with the results of the substrate-binding experiments. Under the conditions tested, apo-ACP binds tightly to AcpS in the absence of CoA, but CoA fails to bind in the absence of apo-ACP. Taken together, these results suggest that the reaction mechanism of AcpS is ordered rather than random, and that the formation of the enzyme-apo-ACP intermediate occurs prior to the transfer of 4′-phosphopantethine from CoA onto apo-ACP.

EXAMPLE 4

Crystallization of AcpS; Data Collection, Structure Solution, and Refinement

[0256] Production and Purification of Selenomethionine-Containing AcpS

[0257] Selenomethionine is incorporated into AcpS using the method of Doublie, 1997, which is based on inhibition of the methionine biosynthetic pathway. One ml of E. coli BL21 (pLysS) cells containing pETI la that carries the acpS gene of S. pneumoniae from an overnight culture in LB medium is centrifuged, and resuspended in 1 ml of M9 minimal medium (Sambrook et al., 1989) supplemented with 100 μg/ml ampicillin and 4 g/L glucose. This 1 ml suspension is added to 1 liter of the same medium pre-warmed at 33° C. Cells are grown at 33° C. with shaking at 250 rpm to an optical density of 0.5-0.6 at 590 nm (mid-log phase) before addition of amino acids as follows: lysine, phenylalanine, and threonine at 100 mg/L; isoleucine, leucine, and valine at 50 mg/L; and L-selenomethionine at 60 mg/L. Expression is induced with 1 mM IPTG 15 min after adding amino acids, and continued for 18 hours. The cells are harvested, and AcpS is purified as described above, the only modifications being the addition of 1 mM dithiothreitol (DTT) to the purification buffers to prevent oxidation of the seleno-methionine groups, and Mono Q chromatography.

[0258] The fractions from the gel filtration FPLC step containing AcpS (verified by 16% Tricine SDS-PAGE) are pooled and applied directly to a Mono Q ion exchange FPLC column (1 ml bed volume) (Pharmacia) equilibrated in 50 mM Tris-HCl, pH 7.0. The column is washed for 10 bed volumes (10 mls) in this buffer, and then a 0M to 1M KCl gradient is applied. The column is run at 1.0 ml/min, detection is at 280 nm, and 1 ml fractions are collected. The fractions are analyzed by 16% tricine SDS-PAGE. Fractions containing AcpS are pooled, dialyzed against 50 mM Tris-HCl, pH 7.0, 140 mM KCl, 10 mM MgCl2, analyzed for protein concentration using Bradford Protein assay (BioRad Laboratories) and bovine serum albumin as a standard. The resulting protein solution is then used for crystallography.

[0259] Crystallization of AcpS

[0260] Diffraction-quality crystals are grown by the vapor diffusion technique at 294K. The protein is concentrated using a Centricon filter (molecular weight cutoff=10 kDa) to 8 mg/ml in a solution of 10 mM MgCl2, 14 mM KCl, and 20 mM Tris-HCl buffer at pH 7.1. A 4 μl (1:1, v/v, protein/reservoir solution) drop is equilibrated in a 500 μl solution containing 8-15% PEG 4000, 200 mM ammonium sulfate, and 100 mM citrate buffer at pH 4.5. Crystals of AcpS are obtained after 4 to 5 days at room temperature. Crystals belong to orthorhombic space group P212121 (unit cell parameters a=49.8 Å, b=59.6 Å, c=114.7 Å) (Native 1; Tables 2 and 3). Crystallization conditions similar to those described above also yield crystals that belong to monoclinic space group C2 (unit cell parameters a=120.2 Å, b=62.3 Å, c=51.7 Å, β=98.7°) for apo-AcpS (Native 2; Tables 2 and 4) and 3′,5′-ADP complex (Tables 2 and 5). Both crystal forms have a homotrimeric molecule per asymmetric unit, with a Vm value (Matthews, 1968) of 2.08 Å3/Da, which corresponds to a solvent content of approximately 41% in both cases. CoA, in 2-3 fold of excess of the protein, is used as a starting material for co-crystallization in the 3′,5′-ADP complex.

[0261] Data Collection, Structure Solution, and Refinement

[0262] The diffraction data are collected using a MarCCD detector on IMCA (Industrial Macromolecular Crystallography Association) beam line ID-17 at the APS (Advanced Photon Source, Argonne National Laboratories) at 100K, using 15-20% glycerol as a cryoprotectant. The diffraction data are reduced using DENZO (HKL2000) (Otwinowski and Minor 1997), and the intensities are scaled with SCALEPACK (Collaborative Computing Project, No. 4, 1994). Most calculations are performed with the CCP4 suite of programs (Collaborative Computing Project, No. 4, 1994). Multiple anomalous dispersion (MAD) data at three wavelengths around the selenium K-shell edge are collected from a single crystal (selenomethionine-substituted protein) belonging to the P212121 space group at 2.8 Å resolution using the inverse beam strategy (Hendrickson et al., 1991). Location of the Se sites and phasing are performed using SOLVE (Terwilliger and Berendzen, 1999), resulting in a figure of merit of 0.64 for the data in the resolution range 20-2.8 Å. Experimental phases are subsequently modified by the application of solvent flattening and 3-fold NCS averaging using the program DM (Collaborative Computing Project, No. 4, 1994). The experimental map allows tracing of 115 amino acid residues, excluding the three-residue loop corresponding to residues Gly69-Lys73, and the four C-terminal residues for each monomer molecule of the homotrimer. This model is refined against data between 20 and 2.4 Å using a maximum likelihood algorithm as incorporated in the program CNX2000 (Badger et al., 1999) (Rwork=0.236, Rfree=0.293) (Brünger, 1992). Subsequently, the coordinates of the trimer are used as a search model in molecular replacement (AmoRe) (Navaza, 1994) for the C2 space group crystals. This structure is refined to an Rwork of 0.208 (Rfree=0.247) against the data in the resolution range of 20-2.0 Å. The AcpS/3′,5′-ADP complex structure is refined to an Rwork of 24.1% (Rfree=27.1%) for the 20-1.9 Å resolution range. The program suite QUANTA 98 (Molecular Simulation Inc., San Diego, Calif.) is used for visual inspection and manual corrections between rounds of refinement. An analysis of the geometry shows that all parameters are within the values expected for a model at this resolution. All residues are found in the most favorable and additionally allowed regions of a Ramachandran plot for all three crystal structures. The last four residues in each AcpS protomer and residues Gly69-Lys7l of a disordered surface loop for one of the subunits are not defined in the electron density even after crystallographic refinement, and for this reason are not included in the final model. The overall average temperature factor of the structures are in good agreement with that calculated from the Wilson plot.

[0263] Coordinates are deposited in the PDB under entry codes 1FTE, 1FTF, and 1FTH.

EXAMPLE 5

Overall Structure of Apo-AcpS

[0264] Data are collected from crystals and the structure of AcpS solved by the multiple anomalous dispersion method (MAD) (Hendrickson et al., 1991) using selenomethionine-substituted protein and exploiting non-crystallographic 3-fold averaging. The atomic coordinates of native AcpS (Native 1 and Native 2) are shown in Tables 3 and 4, respectively. The crystallographic data collection statistics and refinement parameters are summarized in Table 2.

[0265] The structure of AcpS reveals that it assembles as a tightly packed homotrimer. The overall view of the AcpS molecule is shown in FIG. 8A. The AcpS monomer has an elongated elliptical shape with approximate dimensions of 30×35×45 Å (FIG. 8B). The Richardson topology diagram of secondary structural elements is shown in FIG. 8C. The location of these secondary structure elements within the protein sequence is given in Table lA. The AcpS structure has an α/β fold. A topology search using the SCOP program (Murzin et al 1995) does not reveal any significant similarity with AcpS. The AcpS protomer is characterized primarily by three structural motifs. The first is a classical three-stranded anti-parallel β-sheet formed by strands β1, β5, and β4. A long α-helix packs diagonally against the β-sheet together with α-helixes α1, α2, α3, and α4 of the anti-parallel four helical bundle, which represents the second structural motif. The third feature consists of a long extended loop with a two-strand anti-parallel β-sheet β2 and β3). These structural motifs are organized in such a way that the long helix α4 runs through the whole structure and is surrounded by the other structural elements.

[0266] The side chains of each helix in the four-helical bundle are arranged so that hydrophobic side chains are buried between the helices and form a hydrophobic core comprised of Ile 17, Ala 20, Val 21 (α1); Phe 27, Ala 28, Val 31, Leu 32 (α2); Met 37, Phe 40 (α3); Ile 49, Leu 52, Trp 56 (α4). Side chains of the residues Phe 75 and Ile 70 (α5) also participate in the formation of this hydrophobic cluster. Another hydrophobic cluster is formed by the long α-helix α4, and the three- and two-stranded β-sheets, which contain side chains of the residues Phe 62, Met 66 (α4); Phe 90 (β3); Phe 95, Ile99 (β4).

[0267] The final refined structure of AcpS contains 115 out of 122 amino acids. No electron density is observed for the first two N-terminal and final four C-terminal amino acids. The three protomers are related by a non-crystallographic 3-fold pseudo symmetry axis. The three-stranded anti-parallel β-sheets of each AcpS protomer are arranged together in a barrel-like structure in the homotrimer molecule, forming a long, mostly hydrophobic tunnel that runs through the whole structure. The active sites are formed at the intermolecular interface of the homotrimer (FIG. 8B) such that two protomers contribute to the formation of each active site. An active site pocket is formed by residues of helix α4, 1-strands β4 and β5, and loop β2-β3 of one protomer, and the opposite side of helix α4, β-stranded β5 and loop α4-α5 of the second protomer molecule. Since the AcpS active site is created by the interface between two monomers, which are oriented by their homotrimer architecture, the trimeric structure of AcpS appears to be essential for activity. This is consistent with the results of dynamic light scattering (Protein Solution Inc., Charlottesville, Va.), gel filtration column chromatography, and sedimentation analysis of the purified AcpS, which demonstrate that AcpS is a homotrimer (note Example 1 and McAllister et al., 2000). Finally, the native structure reveals that only two out of three active sites are occupied by sulfate ions that are present during the crystallization of AcpS. The sulfate ions are found to be present in the vicinity of His105, Asp10, and Lys64, which corresponds to the α-phosphate of CoA (see below).

EXAMPLE 5

Co-Crystallization of Purified AcpS with Coenzyme A; Overall Structure of the AcpS/3′,5′-ADP Complex

[0268] To help identify the potential active site of AcpS for a structure-based design effort, purified AcpS is co-crystallized with CoA, a substrate of AcpS. Surprisingly, however, the purified AcpS is co-crystallized with 3′,5′-ADP, a product of the AcpS reaction. The fact that only the 3′,5′-ADP moiety exhibits a well defined electron density clearly demonstrates that 3′,5′-ADP, rather than CoA, co-crystallizes with AcpS. Consistent with the native structure of AcpS, the structure of the AcpS/3′,5′-ADP complex shows that AcpS is a trimeric enzyme. In addition, only two out of three active sites are occupied by 3′,5′-ADP in this case, rather than sulfate ions as in the case of the native structure, thus indicating that the binding of the 3′,5′-ADP molecules to AcpS competes with that of the sulfate ions. These results are also in good agreement with those of gel filtration and SDS-PAGE analysis (supra, and McAllister et al., 2000) which demonstrate that ACP is bound to AcpS in a 2:3 ratio. Finally, similar to that of the native structure, the unoccupied active site of the complex structure also exhibits no defined electron density for residues Ile70-Leu73 of the α4-α5 loop. Thus, the complex structure of AcpS suggests that the active form of the enzyme is trimeric.

[0269] The atomic coordinates of the AcpS/3′,5′-ADP complex are shown in Table 5; the active site of the AcpS/3′,5′-ADP complex is shown in FIG. 9. The 3′,5′-ADP binding site is characterized by the following structural elements. The adenine base fits in between loop β2-β3 (Gly86, Ala87, and Pro88) and loop α4-α5 (Lys64, Gly67, and Thr68) from another protomer of the AcpS trimer. An amino group of the adenine ring is in a favorable position to form a hydrogen bond with a carbonyl oxygen of Arg85 and Thr68. The ribose moiety is bound to the adenine ring with an anti-glycosidic torsion angle. The ribose is present in a 3′-endo conformation with the axial orientation of the 2′-hydroxyl and the equatorial orientation of the 3′-phosphate group. The 3′-phosphate portion of the ligand has an interaction with loop β2-β3, α4, and β4, all of which belong to the first protomer. The 3′-phosphate is surrounded by a negatively charged cluster formed by Arg39, Arg47, and Arg55. The 5′ α-phosphate is packed against β1 and α4 of the second protomer, and has hydrogen bonds with Lys64, Ser104, and His105.

[0270] In summary, AcpS, which catalyzes the transfer of 4′-phosphopantetheine from CoA to apo-ACP to form holo-ACP along with the production of 3′,5′-ADP, is an attractive target for the development of antibacterial drugs. The structure of AcpS reveals an α/β fold, and demonstrates that the trimeric structure of the enzyme appears to be essential for the AcpS activity. These results represent the first structural determination of the interaction between the AcpS enzyme and its product, 3′,5′-ADP. These data provide a starting point for structure-based diagnostics, and drug design efforts that will enable identification of novel AcpS inhibitors with potent antibacterial activity useful in treating bacterial infections.

[0271] The invention being thus described, it is obvious that the same can be varied in many ways. Such variations are not to be regarded as a departure from the spirit and scope of the present invention, and all such modifications as would be obvious to one skilled in the art are intended to be included within the scope of the following claims.

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[0334] Parris K. D., Lin L., Tam A., Mathew R., Hixon J., Stahl M, Fritz C. C., Seehra J. Somers W. S. (2000) Structure with Folding and Design, 8:883-895.

[0335] Quadri, L. E. N., Weinreb, P. H., Lie, M., Nakano, M. M., Zuber, P., and Walsh, C. T. (1998). Biochemistry 37, 1585-1595.

[0336] Rawlings, M., and Cronan, J. E., Jr. (1992) J. Biol. Chem. 267, 5751-5754.

[0337] Reuter K., Mofid M. R., Marahiel M. A., Ficner R. (1999) The EMBO J. 23, 6823-6831.

[0338] Rock, C. O., and Cronan, J. E., Jr. (1979) J. Biol. Chem. 254, 9778-9785.

[0339] Rock, C. O., and Cronan, J. E., Jr. (1996) Bioch. Biophys. Acta. 1302, 1-16.

[0340] Sambrook et al. (1989) Molecular Cloning, A Laboratory Manual, Second Edition, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.

[0341] Scott et al. (1990) Science 249:386-390.

[0342] Shen, Z., and Byers, D. M. (1996) J. Bacteriol. 178, 571-573.

[0343] Smith, et al. (1992) J. Mol. Biol. 224:899-904 (1992).

[0344] Smith, S. (1994) FASEB 8, 1248-1259.

[0345] Spratt, B. G. (1994a) Science 264, 388-393.

[0346] Spratt B. G. (1994b) “Resistance to β-lactam antibiotics” in Ghuysen J. M. and Hakenbeck R., eds., Bacterial Cell Wall, Elsevier, Amsterdam, The Netherlands, pp. 517-534.

[0347] Takiff, J. E., T. Baker, T. Copeland, S-M. Chen, D. L. Court. (1992) J. Bacteriol. 174, 1544-1553.

[0348] Terwilliger, T C & Berendzen, J. (1999) Acta Crystallogr. D 55, 849-861.

[0349] Thomson, K. S., Sanders, C. C. (1998) Antimicrob. Agents. Chemother. 42, 179-187.

[0350] Tomasz, A., Munoz, R. (1995) Microb. Drug. Resis. 1, 103-109.

[0351] Tomb, J. -F., White, O.,l Kerlavage, A. R., et al. (1997) Nature 388, 539-547.

[0352] Tropf, S., Revill, W. P., Bibb, M. J., Howood, D. A., and Schweizer, M. (1998) Chem. Biol. 5:135-146.

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[0355] West et al. (1995) TIPS 16:67-74.

[0356] Wlodawer et al. (1993) Ann. Rev. Biochem. 62:543-585.

[0357] Zhao, G., Meier, T. I., Peery, R. B., Matsushima, P., and Skatrud, P. L. (1999) Microbiology 145:791-800.

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2TABLE 1A

[0359]

3

TABLE 1B

[0360]

4

TABLE 2

Crystallographic data

Inflection, L1
Peak, L2
Remote, L3
Native 1

&
Native 2

&
3′5′-ADP

Data collection

Energy, eV
12,655.75
12,659.28
12,700.00
12,398.00
12,398.00
12,398.00

Wavelength λ, Å
0.979537
0.979400
0.976259
1.00000
1.00000
1.00000

Number of observations
210,097
205,948
211,823
336,325
423,425
304,946

Number of reflections
54,462
55,080
54,821
59,335
126,451
162,841

Number of unique reflections
8,450
8,508
8,398
14,842
20,366
29,541

Average redundancy
6.4
6.5
6.5
4.0
6.2
5.5

Completeness, %

All reflections

a
95/90
95/88
94/88
96/84
94/89
100/99

Reflections with I > 3σ
94/85
94/86
94/84
81/57
79/53
80/44

<I/σ> overall
40/14
41/19
40/18
25.6/4.5
26.5/3.0
31.1/3.8

*Rmerge, %
5.6/9.2
5.2/8.8
4.7/8.4
4.9/23.0
6.0/30.1
5.3/26.8

Resolution, Å
2.8
2.8
2.8
2.4
2.0
1.9

Refinement

Protein/Water

2,696/128
2,730/125
2,717/177

Deviation form ideal geometry

bond length, Å/bond angles, °

0.007/1.169
0.005/1.057
0.010/1.146

dihedrals/imprpers, °

25.956/0.588
23.123/0.610
22.247/0.770

Ramachandran plot statistics

Residues in most favorite/allowed regions, %

92.0/8.0
91.2/9.0
92.4/7.6

†Rwork/¶Rfree, %

23.6/29.3
20.8/24.7
24.1/27.1

a
Data after slash sign correspond to outer shell

*Rmerge = Σ|I − <I>|/ΣI, where I is the intensity of an individual measurement, and <I> is the mean intensity of this reflection

¶
Rfree is the cross-validation R-value calculated for 5% of the reflections omitted from the refinement.

†Rwork = Σ|Fo − Fc|/Σ|Fo|, where |Fo| and |Fc| are the observed and calculated structure factor amplitudes respectively.

&
Space group for these data sets is monoclinic C2, the rest of the data sets belong to orthorombic P212121 space group. Both of them contain one homotrimer per the asymmetric unit

[0361]

5

TABLE 3

REMARK coordinates from restrained individual B-factor refinement

REMARK refinement resolution: 500.0-2.40 A

REMARK starting
r = 0.2339 free_r = 0.2899

REMARK final
r = 0.2336 free_r = 0.2950

REMARK B rmsd for bonded mainchain atoms = 0.775
target = 1.5

REMARK B rmsd for bonded sidechain atoms = 0.798
target = 2.0

REMARK B rmsd for angle mainchain atoms = 1.417
target = 2.0

REMARK B rmsd for angle sidechain atoms = 1.333
target = 2.5

REMARK wa = 3.19192

REMARK rweight = 0.44902

REMARK target = mlf steps = 30

REMARK sg = P2(1)2(1)2(l) a = 49.824 b = 59.561 c = 113.738 alpha = 90

beta = 90 gamma = 90

REMARK parameter file 1: CNX_TOPPAR:protein_rep.param

REMARK parameter file 2: CNX_TOPPAR:water_rep.param

REMARK parameter file 3: CNX_TOPPAR:ion.param

REMARK parameter file 4: so4/so4.param

REMARK molecular structure file: generate.psf

REMARK input coordinates: minimize.pdb

REMARK reflection file = x-ray_data.cv

REMARK ncs = none

REMARK B-correction resolution: 6.0-2.40

REMARK initial B-factor correction applied to fobs:

REMARK B11 = 5.613 B22 = 4.955 B33 = −10.569

REMARK B12 = 0.000 B13 = 0.000 B23 = 0.000

REMARK B-factor correction applied to coordinate array B: 0.171

REMARK bulk solvent: (Mask) density level = 0.356315 e/A{circumflex over ( )}3, B-factor = 44.7059 A{circumflex over ( )}2

REMARK reflections with |Fobs|/sigma_F < 0.0 rejected

REMARK reflections with |Fobs| > 10000 * rms(Fobs) rejected

REMARK theoretical total number of refl. in resol. range:
13818
(100.0%)

REMARK number of unobserved reflections (no entry or |F| = 0):
537
( 3.9%)

REMARK number of reflections rejected:
0
( 0.0%)

REMARK total number of reflections used:
13281
( 96.1%)

REMARK number of reflections in working set:
12603
( 91.2%)

REMARK number of reflections in test set:
678
( 4.9%)

REMARK FILENAME = “acps_native 1.pdb”

REMARK Written by CNX VERSION: 2000

ATOM
1
CB
MET
A1003
6.910
33.184
39.062
1.00
31.51
C

ATOM
2
CG
MET
A1003
5.553
33.663
38.598
1.00
33.32
C

ATOM
3
SD
MET
A1003
4.818
34.801
39.816
1.00
36.27
S

ATOM
4
CE
MET
A1003
5.820
36.290
39.557
1.00
35.34
C

ATOM
5
C
MET
A1003
7.655
32.931
36.686
1.00
29.56
C

ATOM
6
O
MET
A1003
8.286
33.972
36.449
1.00
29.16
O

ATOM
7
N
MET
A1003
9.076
32.131
38.552
1.00
30.78
N

ATOM
8
CA
MET
A1003
7.675
32.305
38.074
1.00
30.32
C

ATOM
9
N
ILE
A1004
6.935
22.292
35.768
1.00
28.43
N

ATOM
10
CA
ILE
A1004
6.826
32.791
34.401
1.00
27.65
C

ATOM
11
CB
ILE
A1004
6.307
31.701
33.452
1.00
28.01
C

ATOM
12
CG2
ILE
A1004
6.103
32.287
32.051
1.00
27.49
C

ATOM
13
CG1
ILE
A1004
7.294
30.525
33.430
1.00
27.59
C

ATOM
14
CD1
ILE
A1004
6.890
29.404
32.482
1.00
28.22
C

ATOM
15
C
ILE
A1004
5.885
33.992
34.322
1.00
26.94
C

ATOM
16
O
ILE
A1004
4.741
33.920
34.765
1.00
26.43
O

ATOM
17
N
VAL
A1005
6.380
35.088
33.750
1.00
25.94
N

ATOM
18
CA
VAL
A1005
5.595
36.306
33.617
1.00
25.33
C

ATOM
19
CB
VAL
A1005
6.211
37.446
34.445
1.00
25.03
C

ATOM
20
CG1
VAL
A1005
6.389
36.995
35.882
1.00
25.00
C

ATOM
21
CG2
VAL
A1005
7.535
37.878
33.846
1.00
24.19
C

ATOM
22
C
VAL
A1005
5.432
36.796
32.173
1.00
25.45
C

ATOM
23
O
VAL
A1005
4.982
37.920
31.949
1.00
25.63
O

ATOM
24
N
GLY
A1006
5.794
35.964
31.197
1.00
25.11
N

ATOM
25
CA
GLY
A1006
5.659
36.371
29.809
1.00
24.32
C

ATOM
26
C
GLY
A1006
6.306
35.452
28.786
1.00
23.99
C

ATOM
27
O
GLY
A1006
7.413
34.947
28.996
1.00
24.03
O

ATOM
28
N
HIS
A1007
5.613
35.232
27.671
1.00
23.11
N

ATOM
29
CA
HIS
A1007
6.132
34.386
26.603
1.00
22.22
C

ATOM
30
CB
HIS
A1007
5.633
32.943
26.789
1.00
22.37
C

ATOM
31
CG
HIS
A1007
6.046
32.010
25.693
1.00
22.55
C

ATOM
32
CD2
HIS
A1007
5.331
31.123
24.961
1.00
22.89
C

ATOM
33
ND1
HIS
A1007
7.342
31.933
25.226
1.00
22.71
N

ATOM
34
CE1
HIS
A1007
7.405
31.044
24.251
1.00
22.72
C

ATOM
35
NE2
HIS
A1007
6.198
30.537
24.070
1.00
22.98
N

ATOM
36
C
HIS
A1007
5.718
34.925
25.234
1.00
21.79
C

ATOM
37
O
HIS
A1007
4.553
35.230
25.007
1.00
21.69
O

ATOM
38
N
GLY
A1005
6.682
35.054
24.325
1.00
21.62
N

ATOM
39
CA
GLY
A1008
6.380
35.549
22.994
1.00
20.43
C

ATOM
40
C
GLY
A1005
7.237
34.888
21.932
1.00
20.87
C

ATOM
41
O
GLY
A1008
8.396
34.554
22.171
1.00
20.58
O

ATOM
42
N
ILE
A1009
6.655
34.663
20.760
1.00
20.92
N

ATOM
43
CA
ILE
A1009
7.389
34.077
19.652
1.00
21.06
C

ATOM
44
CB
ILE
A1009
6.911
32.638
19.304
1.00
21.27
C

ATOM
45
CG2
ILE
A1009
7.140
31.699
20.485
1.00
21.48
C

ATOM
46
CG1
ILE
A1009
5.438
32.654
18.892
1.00
21.01
C

ATOM
47
CD1
ILE
A1009
4.967
31.340
18.285
1.00
20.98
C

ATOM
48
C
ILE
A1009
7.184
34.951
18.420
1.00
21.74
C

ATOM
49
O
ILE
A1009
6.345
35.846
18.404
1.00
20.69
O

ATOM
50
N
ASP
A1010
7.971
34.687
17.388
1.00
22.85
N

ATOM
51
CA
ASP
A1010
7.857
35.416
16.147
1.00
23.91
C

ATOM
52
CB
ASP
A1010
8.456
36.813
16.273
1.00
23.93
C

ATOM
53
CG
ASP
A1010
8.300
37.622
14.998
1.00
24.40
C

ATOM
54
OD1
ASP
A1010
9.104
37.423
14.050
1.00
24.86
O

ATOM
55
OD2
ASP
A1010
7.357
38.442
14.939
1.00
24.36
O

ATOM
56
C
ASP
A1010
8.553
34.658
15.041
1.00
24.83
C

ATOM
57
O
ASP
A1010
9.586
34.037
15.262
1.00
25.16
O

ATOM
58
N
ILE
A1011
7.959
34.687
13.852
1.00
25.82
N

ATOM
59
CA
ILE
A1011
8.541
34.021
12.697
1.00
27.04
C

ATOM
60
CB
ILE
A1011
7.713
32.780
12.258
1.00
26.91
C

ATOM
61
CG2
ILE
A1011
6.274
33.168
11.940
1.00
26.65
C

ATOM
62
CG1
ILE
A1011
8.378
32.126
11.048
1.00
27.05
C

ATOM
63
CD1
ILE
A1011
7.818
30.757
10.708
1.00
27.44
C

ATOM
64
C
ILE
A1011
8.586
35.051
11.580
1.00
27.96
C

ATOM
65
O
ILE
A1011
7.652
35.832
11.404
1.00
28.18
O

ATOM
66
N
GLU
A1012
9.688
35.070
10.845
1.00
28.86
N

ATOM
67
CA
GLU
A1012
9.841
36.023
9.762
1.00
30.03
C

ATOM
68
CB
GLU
A1012
10.772
37.161
10.186
1.00
31.54
C

ATOM
69
CG
GLU
A1012
10.071
38.292
10.895
1.00
33.83
C

ATOM
70
CD
GLU
A1012
9.006
38.913
10.026
1.00
35.22
C

ATOM
71
OE1
GLU
A1012
9.352
39.404
8.927
1.00
36.13
O

ATOM
72
OE2
GLU
A1012
7.825
38.903
10.438
1.00
36.10
O

ATOM
73
C
GLU
A1012
10.375
35.414
8.487
1.00
29.94
C

ATOM
74
O
GLU
A1012
11.219
34.526
8.513
1.00
29.44
O

ATOM
75
N
GLU
A1013
9.864
35.901
7.367
1.00
30.50
N

ATOM
76
CA
GLU
A1013
10.331
35.444
6.069
1.00
30.96
C

ATOM
77
CE
GLU
A1013
9.236
35.587
5.012
1.00
31.74
C

ATOM
78
CG
GLD
A1013
9.629
34.951
3.693
1.00
33.86
C

ATOM
79
CD
GLU
A1013
8.621
35.179
2.582
1.00
35.01
C

ATOM
80
OE1
GLU
A1013
8.792
34.550
1.515
1.00
36.28
O

ATOM
81
OE2
GLU
A1013
7.675
35.980
2.762
1.00
35.21
O

ATOM
82
C
GLU
A1013
11.498
36.372
5.735
1.00
30.42
C

ATOM
83
O
GLU
A1013
11.348
37.594
5.750
1.00
30.06
O

ATOM
84
N
LEU
A1014
12.662
35.800
5.457
1.00
30.14
N

ATOM
85
CA
LEU
A1014
13.824
36.617
5.140
1.00
30.32
C

ATOM
86
CB
LEU
A1014
15.022
35.722
4.814
1.00
30.23
C

ATOM
87
CG
LEU
A1014
15.552
34.904
6.000
1.00
30.34
C

ATOM
88
CD1
LEU
A1014
16.618
33.929
5.533
1.00
30.59
C

ATOM
89
CD2
LEU
A1014
16.117
35.835
7.053
1.00
30.41
C

ATOM
90
C
LEU
A1014
13.526
37.563
3.977
1.00
30.65
C

ATOM
91
O
LEU
A1014
13.877
38.743
4.023
1.00
30.37
O

ATOM
92
N
ALA
A1015
12.857
37.048
2.949
1.00
30.96
N

ATOM
93
CA
ALA
A1015
12.519
37.855
1.784
1.00
31.57
C

ATOM
94
CB
ALA
A1015
11.683
37.038
0.798
1.00
30.98
C

ATOM
95
C
ALA
A1015
11.780
39.131
2.183
1.00
31.93
C

ATOM
96
O
ALA
A1015
11.947
40.170
1.544
1.00
31.75
O

ATOM
97
N
SER
A1016
10.972
39.055
3.240
1.00
32.40
N

ATOM
98
CA
SER
A1016
10.227
40.224
3.714
1.00
33.29
C

ATOM
99
CB
SER
A1016
9.264
39.844
4.847
1.00
33.61
C

ATOM
100
OG
SER
A1016
8.316
38.883
4.428
1.00
34.88
O

ATOM
101
C
SER
A1016
11.194
41.279
4.235
1.00
33.73
C

ATOM
102
O
SER
A1016
11.059
42.464
3.937
1.00
33.37
O

ATOM
103
N
ILE
A1017
12.156
40.828
5.035
1.00
34.48
N

ATOM
104
CA
ILE
A1017
13.167
41.698
5.615
1.00
35.17
C

ATOM
105
CB
ILE
A1017
14.041
40.922
6.641
1.00
34.97
C

ATOM
106
CG2
ILE
A1017
15.151
41.814
7.173
1.00
34.62
C

ATOM
107
CG1
ILE
A1017
13.172
40.436
7.805
1.00
35.03
C

ATOM
108
CD1
ILE
A1017
12.550
41.555
8.623
1.00
34.83
C

ATOM
109
C
ILE
A1017
14.064
42.266
4.516
1.00
35.70
C

ATOM
110
O
ILE
A1017
14.435
43.439
4.555
1.00
35.49
O

ATOM
111
N
GLU
A1018
14.414
41.431
3.542
1.00
36.59
N

ATOM
112
CA
GLU
A1018
15.260
41.872
2.439
1.00
38.02
C

ATOM
113
CB
GLU
A1018
15.595
40.703
1.508
1.00
39.36
C

ATOM
114
CG
GLU
A1018
16.768
40.993
0.578
1.00
42.30
C

ATOM
115
CD
GLU
A1018
16.928
39.967
−0.532
1.00
44.15
C

ATOM
116
OE1
GLU
A1018
16.923
38.748
−0.239
1.00
45.23
O

ATOM
117
OE2
GLU
A1018
17.069
40.387
−1.703
1.00
45.34
O

ATOM
118
C
GLU
A1018
14.480
42.925
1.658
1.00
38.06
C

ATOM
119
O
GLU
A1018
15.026
43.936
1.212
1.00
37.81
O

ATOM
120
N
SER
A1019
13.187
42.668
1.509
1.00
37.94
N

ATOM
121
CA
SER
A1019
12.297
43.561
0.799
1.00
37.74
C

ATOM
122
CB
SER
A1019
10.921
42.906
0.680
1.00
37.89
C

ATOM
123
OG
SER
A1019
9.994
43.764
0.044
1.00
38.96
O

ATOM
124
C
SER
A1019
12.182
44.916
1.505
1.00
37.72
C

ATOM
125
O
SER
A1019
12.074
45.957
0.850
1.00
37.89
O

ATOM
126
N
ALA
A1020
12.207
44.902
2.836
1.00
37.14
N

ATOM
127
CA
ALA
A1020
12.097
46.129
3.615
1.00
37.01
C

ATOM
128
CB
ALA
A1020
11.773
45.800
5.063
1.00
36.69
C

ATOM
129
C
ALA
A1020
13.369
46.973
3.542
1.00
37.03
C

ATOM
130
O
ALA
A1020
13.309
48.201
3.538
1.00
36.27
O

ATOM
131
N
VAL
A1021
14.519
46.309
3.497
1.00
37.47
N

ATOM
132
CA
VAL
A1021
15.797
47.007
3.415
1.00
38.34
C

ATOM
133
CB
VAL
A1021
16.979
46.047
3.651
1.00
37.99
C

ATOM
134
CG1
VAL
A1021
18.282
46.740
3.316
1.00
38.47
C

ATOM
135
CG2
VAL
A1021
16.990
45.585
5.093
1.00
38.14
C

ATOM
136
C
VAL
A1021
15.937
47.605
2.025
1.00
38.86
C

ATOM
137
O
VAL
A1021
16.345
48.749
1.855
1.00
38.89
O

ATOM
138
N
THR
A1022
15.586
46.810
1.029
1.00
39.74
N

ATOM
139
CA
THR
A1022
15.670
47.244
−0.350
1.00
40.51
C

ATOM
140
CB
THR
A1022
15.220
46.117
−1.300
1.00
40.54
C

ATOM
141
OG1
THR
A1022
15.975
44.930
−1.019
1.00
40.47
O

ATOM
142
CG2
THR
A1022
15.442
46.525
−2.753
1.00
41.07
C

ATOM
143
C
THR
A1022
14.795
48.472
−0.579
1.00
40.85
C

ATOM
144
O
THR
A1022
15.227
49.433
−1.204
1.00
41.01
O

ATOM
145
N
ARG
A1023
13.577
48.442
−0.048
1.00
41.28
N

ATOM
146
CA
ARG
A1023
12.626
49.541
−0.215
1.00
41.51
C

ATOM
147
CB
ARG
A1023
11.198
49.003
−0.083
1.00
41.55
C

ATOM
148
CG
ARG
A1023
10.804
48.042
−1.201
1.00
42.10
C

ATOM
149
CD
ARG
A1023
9.460
47.375
−0.938
1.00
42.16
C

ATOM
150
NE
ARG
A1023
8.439
48.328
−0.514
0.05
42.12
N

ATOM
151
CZ
ARG
A1023
7.158
48.021
−0.344
0.05
42.14
C

ATOM
152
NH1
ARG
A1023
6.734
46.785
−0.567
0.05
42.17
N

ATOM
153
NH2
ARG
A1023
6.300
48.947
0.061
0.05
42.16
N

ATOM
154
C
ARG
A1023
12.798
50.747
0.710
1.00
41.61
C

ATOM
155
O
ARG
A1023
12.396
51.851
0.363
1.00
41.34
O

ATOM
156
N
HIS
A1024
13.395
50.544
1.878
1.00
42.27
N

ATOM
157
CA
HIS
A1024
13.583
51.636
2.835
1.00
42.70
C

ATOM
158
CB
HIS
A1024
12.658
51.445
4.040
0.05
42.61
C

ATOM
159
CG
HIS
A1024
11.202
51.471
3.693
0.05
42.54
C

ATOM
160
CD2
HIS
A1024
10.233
50.537
3.841
0.05
42.53
C

ATOM
161
ND1
HIS
A1024
10.592
52.567
3.121
0.05
42.51
N

ATOM
162
CE1
HIS
A1024
9.311
52.307
2.932
0.05
42.49
C

ATOM
163
NE2
HIS
A1024
9.067
51.081
3.360
0.05
42.48
N

ATOM
164
C
HIS
A1024
15.028
51.727
3.307
1.00
43.14
C

ATOM
165
O
HIS
A1024
15.483
50.930
4.131
1.00
43.24
O

ATOM
166
N
GLU
A1025
15.732
52.722
2.782
1.00
43.47
N

ATOM
167
CA
GLU
A1025
17.139
52.963
3.089
1.00
43.74
C

ATOM
168
CB
GLU
A1025
17.596
54.249
2.393
1.00
44.50
C

ATOM
169
CG
GLU
A1025
17.396
54.230
0.888
1.00
45.87
C

ATOM
170
CD
GLU
A1025
18.031
55.420
0.208
1.00
46.86
C

ATOM
171
OE1
GLU
A1025
19.267
55.571
0.320
1.00
47.25
O

ATOM
172
OE2
GLU
A1025
17.294
56.201
−0.434
1.00
47.49
O

ATOM
173
C
GLU
A1025
17.539
53.030
4.565
1.00
43.28
C

ATOM
174
O
GLU
A1025
18.655
52.645
4.912
1.00
43.56
O

ATOM
175
N
GLY
A1026
16.649
53.523
5.424
1.00
42.64
N

ATOM
176
CA
GLY
A1026
16.972
53.631
6.838
1.00
41.75
C

ATOM
177
C
GLY
A1026
16.244
52.645
7.731
1.00
41.40
C

ATOM
178
O
GLY
A1026
16.091
52.877
8.931
1.00
41.35
O

ATOM
179
N
PHE
A1027
15.801
51.537
7.144
1.00
40.74
N

ATOM
180
CA
PHE
A1027
15.077
50.500
7.871
1.00
39.69
C

ATOM
181
CB
PHE
A1027
14.695
49.376
6.906
1.00
39.76
C

ATOM
182
CG
PHE
A1027
13.976
48.233
7.558
1.00
40.05
C

ATOM
183
CD1
PHE
A1027
12.654
48.369
7.978
1.00
40.03
C

ATOM
184
CD2
PHE
A1027
14.618
47.012
7.748
1.00
39.83
C

ATOM
185
CE1
PHE
A1027
11.982
47.301
8.576
1.00
39.93
C

ATOM
186
CE2
PHE
A1027
13.955
45.944
8.344
1.00
39.71
C

ATOM
187
CZ
PHE
A1027
12.636
46.089
8.757
1.00
39.70
C

ATOM
188
C
PHE
A1027
15.900
49.920
9.020
1.00
39.08
C

ATOM
189
O
PHE
A1027
15.470
49.929
10.175
1.00
38.67
O

ATOM
190
N
ALA
A1028
17.080
49.409
8.682
1.00
38.48
N

ATOM
191
CA
ALA
A1028
17.980
48.811
9.656
1.00
38.36
C

ATOM
192
CB
ALA
A1028
19.242
48.321
8.960
1.00
37.96
C

ATOM
193
C
ALA
A1028
18.349
49.784
10.764
1.00
38.25
C

ATOM
194
O
ALA
A1028
18.533
49.384
11.907
1.00
38.15
O

ATOM
195
N
LYS
A1029
18.456
51.061
10.418
1.00
38.38
N

ATOM
196
CA
LYS
A1029
18.823
52.094
11.380
1.00
38.44
C

ATOM
197
CB
LYS
A1029
19.154
53.391
10.636
1.00
39.34
C

ATOM
198
CG
LYS
A1029
19.997
54.393
11.411
1.00
40.55
C

ATOM
199
CD
LYS
A1029
19.248
55.005
12.591
1.00
41.77
C

ATOM
200
CE
LYS
A1029
20.043
56.146
13.215
1.00
41.81
C

ATOM
201
NZ
LYS
A1029
20.282
57.218
12.208
1.00
42.20
N

ATOM
202
C
LYS
A1029
17.703
52.331
12.386
1.00
37.98
C

ATOM
203
O
LYS
A1029
17.948
52.731
13.522
1.00
38.26
O

ATOM
204
N
ARG
A1030
16.470
52.084
11.969
1.00
37.55
N

ATOM
205
CA
ARG
A1030
15.330
52.267
12.856
1.00
37.18
C

ATOM
206
CB
ARG
A1030
14.050
52.489
12.040
1.00
38.15
C

ATOM
207
CG
ARG
A1030
13.833
53.934
11.573
1.00
39.87
C

ATOM
208
CD
ARG
A1030
12.449
54.110
10.937
1.00
40.62
C

ATOM
209
NE
ARG
A1030
12.383
53.532
9.598
1.00
41.54
N

ATOM
210
CZ
ARG
A1030
12.825
54.142
8.500
1.00
42.11
C

ATOM
211
NH1
ARG
A1030
13.359
55.355
8.577
1.00
41.94
N

ATOM
212
NH2
ARG
A1030
12.747
53.533
7.323
1.00
42.66
N

ATOM
213
C
ARG
A1030
15.145
51.064
13.780
1.00
36.44
C

ATOM
214
O
ARG
A1030
14.650
51.202
14.900
1.00
36.62
O

ATOM
215
N
VAL
A1031
15.560
49.889
13.313
1.00
35.30
N

ATOM
216
CA
VAL
A1031
15.417
48.655
14.080
1.00
34.12
C

ATOM
217
CB
VAL
A1031
15.160
47.458
13.145
1.00
34.29
C

ATOM
218
CG1
VAL
A1031
14.965
46.190
13.963
1.00
34.93
C

ATOM
219
CG2
VAL
A1031
13.949
47.723
12.279
1.00
34.77
C

ATOM
220
C
VAL
A1031
16.615
48.300
14.960
1.00
33.18
C

ATOM
221
O
VAL
A1031
16.447
47.763
16.057
1.00
33.04
O

ATOM
222
N
LEU
A1032
17.818
48.595
14.482
1.00
31.96
N

ATOM
223
CA
LEU
A1032
19.026
48.264
15.226
1.00
31.28
C

ATOM
224
CB
LEU
A1032
20.081
47.692
14.274
1.00
30.83
C

ATOM
225
CG
LEU
A1032
19.665
46.475
13.438
1.00
30.70
C

ATOM
226
CD1
LEU
A1032
20.852
46.007
12.608
1.00
30.16
C

ATOM
227
CD2
LEU
A1032
19.172
45.351
14.349
1.00
30.17
C

ATOM
228
C
LEU
A1032
19.634
49.422
16.005
1.00
30.91
C

ATOM
229
O
LEU
A1032
19.534
50.578
15.602
1.00
31.10
O

ATOM
230
N
THR
A1033
20.262
49.095
17.129
1.00
30.41
N

ATOM
231
CA
THR
A1033
20.918
50.094
17.960
1.00
29.93
C

ATOM
232
CB
THR
A1033
21.113
49.605
19.410
1.00
29.26
C

ATOM
233
OG1
THR
A1033
22.084
48.552
19.438
1.00
28.24
O

ATOM
234
CG2
THR
A1033
19.800
49.097
19.980
1.00
29.31
C

ATOM
235
C
THR
A1033
22.291
50.334
17.339
1.00
30.14
C

ATOM
236
O
THR
A1033
22.678
49.633
16.405
1.00
29.45
O

ATOM
237
N
ALA
A1034
23.018
51.321
17.856
1.00
30.49
N

ATOM
238
CA
ALA
A1034
24.344
5L638
17.339
1.00
31.05
C

ATOM
239
CB
ALA
A1034
24.987
52.734
18.177
1.00
30.92
C

ATOM
240
C
ALA
A1034
25.211
50.388
17.356
1.00
31.28
C

ATOM
241
O
ALA
A1034
25.837
50.047
16.357
1.00
31.20
O

ATOM
242
N
LEU
A1035
25.241
49.706
18.495
1.00
31.90
N

ATOM
243
CA
LEU
A1035
26.030
48.487
18.619
1.00
32.66
C

ATOM
244
CB
LEU
A1035
25.878
47.907
20.031
1.00
32.74
C

ATOM
245
CG
LEU
A1035
26.464
48.733
21.195
1.00
32.90
C

ATOM
246
CD1
LEU
A1035
26.003
48.158
22.529
1.00
32.38
C

ATOM
247
CD2
LEU
A1035
27.985
48.737
21.121
1.00
32.56
C

ATOM
248
C
LEU
A1035
25.612
47.454
17.556
1.00
33.36
C

ATOM
249
O
LEU
A1035
26.442
46.992
16.769
1.00
33.53
O

ATOM
250
N
GLU
A1036
24.328
47.104
17.526
1.00
33.64
N

ATOM
251
CA
GLU
A1036
23.822
46.140
16.555
1.00
34.14
C

ATOM
252
CB
GLU
A1036
22.299
46.014
16.682
1.00
33.87
C

ATOM
253
CG
GLU
A1036
21.818
45.217
17.890
1.00
33.65
C

ATOM
254
CD
GLU
A1036
20.341
45.462
18.216
1.00
33.37
C

ATOM
255
OE1
GLU
A1036
19.726
44.613
18.895
1.00
32.88
O

ATOM
256
OE2
GLU
A1036
19.797
46.509
17.808
1.00
33.01
O

ATOM
257
C
GLU
A1036
24.188
46.573
15.137
1.00
34.85
C

ATOM
258
O
GLU
A1036
24.526
45.752
14.284
1.00
34.59
O

ATOM
259
N
MET
A1037
24.120
47.875
14.893
1.00
35.84
N

ATOM
260
CA
MET
A1037
24.436
48.433
13.585
1.00
37.02
C

ATOM
261
CB
MET
A1037
24.172
49.936
13.605
1.00
37.11
C

ATOM
262
CG
MET
A1037
23.656
50.510
12.294
1.00
38.16
C

ATOM
263
SD
MET
A1037
22.148
49.717
11.685
1.00
38.53
S

ATOM
264
CE
MET
A1037
22.507
49.661
9.949
1.00
38.71
C

ATOM
265
C
MET
A1037
25.899
48.141
13.215
1.00
37.76
C

ATOM
266
O
MET
A1037
26.227
47.928
12.044
1.00
37.71
O

ATOM
267
N
GLU
A1038
26.774
48.117
14.217
1.00
38.51
N

ATOM
268
CA
GLU
A1038
28.183
47.835
13.977
1.00
39.30
C

ATOM
269
CB
GLU
A1038
28.989
47.966
15.275
1.00
40.38
C

ATOM
270
CG
GLU
A1038
28.963
49.369
15.880
1.00
41.32
C

ATOM
271
CD
GLU
A1038
29.874
49.513
17.086
1.00
42.00
C

ATOM
272
OE1
GLU
A1038
29.789
50.553
17.771
1.00
42.33
O

ATOM
273
OE2
GLU
A1038
30.677
48.592
17.349
1.00
42.44
O

ATOM
274
C
GLU
A1038
28.349
46.436
13.395
1.00
39.50
C

ATOM
275
O
GLU
A1038
28.932
46.272
12.327
1.00
40.05
O

ATOM
276
N
ARG
A1039
27.837
45.423
14.087
1.00
39.36
N

ATOM
277
CA
ARG
A1039
27.945
44.063
13.577
1.00
39.25
C

ATOM
278
CB
ARG
A1039
27.347
43.053
14.563
1.00
39.62
C

ATOM
279
CG
ARG
A1039
27.395
41.632
14.025
1.00
40.25
C

ATOM
280
CD
ARG
A1039
27.177
40.585
15.089
1.00
40.85
C

ATOM
281
NE
ARG
A1039
27.251
39.243
14.516
1.00
41.68
N

ATOM
282
CZ
ARG
A1039
28.314
38.756
13.879
1.00
42.00
C

ATOM
283
NH1
ARG
A1039
28.289
37.523
13.387
1.00
42.01
N

ATOM
284
NH2
ARG
A1039
29.408
39.496
13.735
1.00
41.92
N

ATOM
285
C
ARG
A1039
27.241
43.938
12.228
1.00
39.03
C

ATOM
286
O
ARG
A1039
27.774
43.347
11.291
1.00
38.64
O

ATOM
287
N
PHE
A1040
26.040
44.502
12.136
1.00
39.10
N

ATOM
288
CA
PHE
A1040
25.255
44.464
10.901
1.00
39.18
C

ATOM
289
CB
PHE
A1040
24.030
45.369
11.036
1.00
38.05
C

ATOM
290
CG
PHE
A1040
23.268
45.560
9.754
1.00
37.43
C

ATOM
291
CD1
PHE
A1040
22.443
44.557
9.258
1.00
37.16
C

ATOM
292
CD2
PHE
A1040
23.365
46.752
9.045
1.00
37.16
C

ATOM
293
CE1
PHE
A1040
21.722
44.742
8.074
1.00
36.76
C

ATOM
294
CE2
PHE
A1040
22.649
46.946
7.863
1.00
36.76
C

ATOM
295
CZ
PHE
A1040
21.825
45.936
7.379
1.00
36.61
C

ATOM
296
C
PHE
A1040
26.063
44.910
9.682
1.00
39.84
C

ATOM
297
O
PHE
A1040
26.157
44.190
8.682
1.00
39.67
O

ATOM
298
N
THR
A1041
26.643
46.104
9.774
1.00
40.57
N

ATOM
299
CA
THR
A1041
27.415
46.668
8.676
1.00
41.24
C

ATOM
300
CB
THR
A1041
27.726
48.138
8.938
1.00
41.14
C

ATOM
301
OG1
THR
A1041
28.364
48.272
10.212
1.00
41.93
O

ATOM
302
CG2
THR
A1041
26.446
48.948
8.933
1.00
40.95
C

ATOM
303
C
THR
A1041
28.708
45.931
8.353
1.00
41.72
C

ATOM
304
O
THR
A1041
29.251
46.080
7.259
1.00
41.99
O

ATOM
305
N
SER
A1042
29.198
45.133
9.297
1.00
42.15
N

ATOM
306
CA
SER
A1042
30.419
44.367
9.078
1.00
42.65
C

ATOM
307
CB
SER
A1042
31.106
44.057
10.407
1.00
42.64
C

ATOM
308
OG
SER
A1042
30.642
42.828
10.934
1.00
43.03
O

ATOM
309
C
SER
A1042
30.066
43.050
8.381
1.00
43.22
C

ATOM
310
O
SER
A1042
30.937
42.218
8.118
1.00
43.14
O

ATOM
311
N
LEU
A1043
28.781
42.869
8.095
1.00
43.80
N

ATOM
312
CA
LEU
A1043
28.298
41.660
7.439
1.00
44.32
C

ATOM
313
CB
LEU
A1043
27.151
41.040
8.247
1.00
43.98
C

ATOM
314
CG
LEU
A1043
27.491
40.512
9.642
1.00
43.88
C

ATOM
315
CD1
LEU
A1043
26.219
40.165
10.388
1.00
43.76
C

ATOM
316
CD2
LEU
A1043
28.383
39.294
9.521
1.00
44.03
C

ATOM
317
C
LEU
A1043
27.821
41.973
6.026
1.00
44.90
C

ATOM
318
O
LEU
A1043
27.448
43.110
5.722
1.00
44.88
O

ATOM
319
N
LYS
A1044
27.827
40.950
5.174
1.00
45.38
N

ATOM
320
CA
LYS
A1044
27.412
41.088
3.782
1.00
45.95
C

ATOM
321
CB
LYS
A1044
28.556
40.673
2.856
1.00
46.91
C

ATOM
322
CG
LYS
A1044
28.976
39.209
3.060
1.00
47.97
C

ATOM
323
CD
LYS
A1044
29.803
38.669
1.896
1.00
48.98
C

ATOM
324
CE
LYS
A1044
30.319
37.260
2.187
1.00
49.35
C

ATOM
325
NZ
LYS
A1044
29.216
36.313
2.505
1.00
49.24
N

ATOM
326
C
LYS
A1044
26.202
40.217
3.457
1.00
45.75
C

ATOM
327
O
LYS
A1044
25.779
39.391
4.266
1.00
46.06
O

ATOM
328
N
GLY
A1045
25.674
40.416
2.252
1.00
45.39
N

ATOM
329
CA
GLY
A1045
24.538
39.663
1.743
1.00
44.96
C

ATOM
330
C
GLY
A1045
23.577
38.960
2.685
1.00
44.52
C

ATOM
331
O
GLY
A1045
23.147
39.520
3.692
1.00
44.43
O

ATOM
332
N
ARG
A1046
23.231
37.726
2.333
1.00
44.21
N

ATOM
333
CA
ARG
A1046
22.297
36.917
3.112
1.00
43.89
C

ATOM
334
CB
ARG
A1046
22.304
35.474
2.589
1.00
44.58
C

ATOM
335
CG
ARG
A1046
21.962
35.399
1.099
1.00
46.46
C

ATOM
336
CD
ARG
A1046
21.891
33.977
0.547
1.00
47.97
C

ATOM
337
NE
ARG
A1046
20.698
33.253
0.979
1.00
49.25
N

ATOM
338
CZ
ARG
A1046
20.360
32.043
0.538
1.00
49.83
C

ATOM
339
NH1
ARG
A1046
19.257
31.454
0.983
1.00
49.98
N

ATOM
340
NH2
ARG
A1046
21.123
31.420
−0.352
1.00
49.87
N

ATOM
341
C
ARG
A1046
22.572
36.951
4.609
1.00
43.05
C

ATOM
342
O
ARG
A1046
21.657
37.167
5.402
1.00
42.92
O

ATOM
343
N
ARG
A1047
23.830
36.751
4.994
1.00
42.04
N

ATOM
344
CA
ARG
A1047
24.212
36.775
6.401
1.00
40.92
C

ATOM
345
CB
ARG
A1047
25.726
36.592
6.553
1.00
41.86
C

ATOM
346
CG
ARG
A1047
26.196
35.146
6.581
1.00
43.21
C

ATOM
347
CD
ARG
A1047
27.613
35.070
7.134
1.00
44.61
C

ATOM
348
NE
ARG
A1047
28.023
33.709
7.475
1.00
45.70
N

ATOM
349
CZ
ARG
A1047
28.346
32.773
6.588
1.00
46.26
C

ATOM
350
NH1
ARG
A1047
28.705
31.565
7.004
1.00
46.85
N

ATOM
351
NH2
ARG
A1047
28.318
33.042
5.289
1.00
46.67
N

ATOM
352
C
ARG
A1047
23.800
38.082
7.074
1.00
39.44
C

ATOM
353
O
ARG
A1047
23.397
38.100
8.236
1.00
38.89
O

ATOM
354
N
GLN
A1048
23.914
39.178
6.338
1.00
37.81
N

ATOM
355
CA
GLN
A1048
23.550
40.475
6.871
1.00
36.41
C

ATOM
356
CB
GLN
A1048
24.011
41.576
5.920
1.00
36.74
C

ATOM
357
CG
GLN
A1048
24.106
42.940
6.565
1.00
37.57
C

ATOM
358
CD
GLN
A1048
24.476
44.024
5.578
1.00
38.09
C

ATOM
359
OE1
GLN
A1048
24.860
45.132
5.965
1.00
38.67
O

ATOM
360
NE2
CLN
A1048
24.351
43.717
4.295
1.00
38.03
N

ATOM
361
C
GLN
A1048
22.037
40.561
7.074
1.00
35.21
C

ATOM
362
O
GLN
A1048
21.567
41.201
8.015
1.00
34.68
O

ATOM
363
N
ILE
A1049
21.279
39.919
6.189
1.00
33.75
N

ATOM
364
CA
ILE
A1049
19.826
39.934
6.295
1.00
32.76
C

ATOM
365
CB
ILE
A1049
19.146
39.436
4.987
1.00
32.88
C

ATOM
366
CG2
ILE
A1049
17.628
39.437
5.153
1.00
32.63
C

ATOM
367
CG1
ILE
A1049
19.536
40.333
3.808
1.00
32.63
C

ATOM
368
CD1
ILE
A1049
19.070
41.776
3.930
1.00
32.59
C

ATOM
369
C
ILE
A1049
19.366
39.062
7.466
1.00
31.99
C

ATOM
370
O
ILE
A1049
18.480
39.456
8.223
1.00
31.76
O

ATOM
371
N
GLU
A1050
19.964
37.883
7.611
1.00
31.37
N

ATOM
372
CA
GLU
A1050
19.610
36.982
8.707
1.00
31.34
C

ATOM
373
CB
GLU
A1050
20.362
35.648
8.591
1.00
32.61
C

ATOM
374
CG
GLU
A1050
20.706
34.980
9.944
1.00
36.11
C

ATOM
375
CD
GLU
A1050
19.482
34.642
10.819
1.00
37.78
C

ATOM
376
OE1
GLU
A1050
19.674
34.340
12.024
1.00
39.05
O

ATOM
377
OE2
GLU
A1050
18.339
34.671
10.311
1.00
38.44
O

ATOM
378
C
GLU
A1050
19.929
37.642
10.047
1.00
30.27
C

ATOM
379
O
GLU
A1050
19.172
37.494
11.014
1.00
30.09
O

ATOM
380
N
TYR
A1051
21.041
38.372
10.107
1.00
28.49
N

ATOM
381
CA
TYR
A1051
21.398
39.040
11.343
1.00
27.23
C

ATOM
382
CB
TYR
A1051
22.747
39.750
11.244
1.00
26.82
C

ATOM
383
CG
TYR
A1051
23.032
40.565
12.484
1.00
26.72
C

ATOM
384
CD1
TYR
A1051
22.657
41.906
12.569
1.00
26.89
C

ATOM
385
CE1
TYR
A1051
22.830
42.627
13.750
1.00
26.37
C

ATOM
386
CD2
TYR
A1051
23.590
39.970
13.612
1.00
26.66
C

ATOM
387
CE2
TYR
A1051
23.761
40.676
14.786
1.00
26.28
C

ATOM
388
CZ
TYR
A1051
23.381
42.000
14.852
1.00
26.29
C

ATOM
389
OH
TYR
A1051
23.554
42.688
16.031
1.00
26.92
O

ATOM
390
C
TYR
A1051
20.332
40.069
11.670
1.00
26.31
C

ATOM
391
O
TYR
A1051
19.893
40.189
12.811
1.00
25.81
O

ATOM
392
N
LEU
A1052
19.927
40.812
10.650
1.00
25.22
N

ATOM
393
CA
LEU
A1052
18.923
41.845
10.809
1.00
24.40
C

ATOM
394
CB
LEU
A1052
18.854
42.685
9.532
1.00
24.44
C

ATOM
395
CG
LEU
A1052
17.719
43.703
9.465
1.00
25.24
C

ATOM
396
CD1
LEU
A1052
17.904
44.780
10.533
1.00
24.85
C

ATOM
397
CD2
LEU
A1052
17.692
44.314
8.081
1.00
25.55
C

ATOM
398
C
LEU
A1052
17.551
41.242
11.126
1.00
23.78
C

ATOM
399
O
LEU
A1052
16.808
41.771
11.957
1.00
23.28
O

ATOM
400
N
ALA
A1053
17.227
40.134
10.459
1.00
22.87
N

ATOM
401
CA
ALA
A1053
15.948
39.459
10.655
1.00
22.13
C

ATOM
402
CB
ALA
A1053
15.780
38.354
9.619
1.00
21.79
C

ATOM
403
C
ALA
A1053
15.858
38.875
12.066
1.00
21.81
C

ATOM
404
O
ALA
A1053
14.841
39.022
12.748
1.00
21.24
O

ATOM
405
N
GLY
A1054
16.932
38.215
12.497
1.00
21.35
N

ATOM
406
CA
GLY
A1054
16.953
37.624
13.819
1.00
20.95
C

ATOM
407
C
GLY
A1054
16.707
38.649
14.910
1.00
20.80
C

ATOM
408
O
GLY
A1054
15.890
38.428
15.803
1.00
20.64
O

ATOM
409
N
ARG
A1055
17.419
39.769
14.845
1.00
20.73
N

ATOM
410
CA
ARG
A1055
17.255
40.822
15.843
1.00
21.15
C

ATOM
411
CB
ARG
A1055
18.254
41.959
15.586
1.00
20.76
C

ATOM
412
CG
ARG
A1055
19.514
41.893
16.444
1.00
20.45
C

ATOM
413
CD
ARG
A1055
20.238
40.562
16.281
1.00
20.93
C

ATOM
414
NE
ARG
A1055
21.323
40.413
17.249
1.00
20.92
N

ATOM
415
CZ
ARG
A1055
22.109
39.344
17.337
1.00
21.08
C

ATOM
416
NH1
ARG
A1055
21.937
38.314
16.515
1.00
21.54
N

ATOM
417
NH2
ARG
A1055
23.073
39.308
18.246
1.00
20.48
N

ATOM
418
C
ARG
A1055
15.822
41.355
15.834
1.00
20.82
C

ATOM
419
O
ARG
A1055
15.235
41.597
16.884
1.00
19.96
O

ATOM
420
N
TRP
A1056
15.272
41.535
14.638
1.00
21.33
N

ATOM
421
CA
TRP
A1056
13.907
42.018
14.481
1.00
21.83
C

ATOM
422
CB
TRP
A1056
13.597
42.252
12.995
1.00
23.26
C

ATOM
423
CG
TRP
A1056
12.117
42.342
12.688
1.00
25.60
C

ATOM
424
CD2
TRP
A1056
11.384
43.518
12.326
1.00
26.69
C

ATOM
425
CE2
TRP
A1056
10.026
43.140
12.186
1.00
27.05
C

ATOM
426
CE3
TRP
A1056
11.741
44.852
12.106
1.00
27.71
C

ATOM
427
CD1
TRP
A1056
11.199
41.324
12.745
1.00
26.25
C

ATOM
428
NE1
TRP
A1056
9.942
41.798
12.448
1.00
27.38
N

ATOM
429
CZ2
TRP
A1056
9.025
44.048
11.839
1.00
28.05
C

ATOM
430
CZ3
TRP
A1056
10.741
45.763
11.757
1.00
29.41
C

ATOM
431
CH2
TRP
A1056
9.397
45.353
11.628
1.00
28.81
C

ATOM
432
C
TRP
A1056
12.956
40.973
15.059
1.00
21.40
C

ATOM
433
O
TRP
A1056
11.999
41.299
15.754
1.00
21.32
O

ATOM
434
N
SER
A1057
13.233
39.714
14.752
1.00
20.70
N

ATOM
435
CA
SER
A1057
12.429
38.605
15.231
1.00
20.76
C

ATOM
436
CB
SER
A1057
12.956
37.293
14.632
1.00
21.29
C

ATOM
437
OG
SER
A1057
12.032
36.234
14.815
1.00
23.54
O

ATOM
438
C
SER
A1057
12.498
38.559
16.760
1.00
20.11
C

ATOM
439
O
SER
A1057
11.484
38.361
17.438
1.00
19.93
O

ATOM
440
N
ALA
A1058
13,693
38.750
17.303
1.00
19.35
N

ATOM
441
CA
ALA
A1058
13.881
38.727
18.751
1.00
18.89
C

ATOM
442
CB
ALA
A1058
15.373
38.780
19.098
1.00
18.02
C

ATOM
443
C
ALA
A1058
13.139
39.865
19.448
1.00
18.51
C

ATOM
444
O
ALA
A1058
12.502
39.657
20.482
1.00
17.31
O

ATOM
445
N
LYS
A1059
13.213
41.062
18.875
1.00
19.01
N

ATOM
446
CA
LYS
A1059
12.560
42.230
19.470
1.00
20.07
C

ATOM
447
CB
LYS
A1059
13.026
43.513
18.771
1.00
19.92
C

ATOM
448
CG
LYS
A1059
14.539
43.671
18.811
1.00
20.81
C

ATOM
449
CD
LYS
A1059
15.003
45.101
18.534
1.00
21.35
C

ATOM
450
CE
LYS
A1059
16.530
45.190
18.538
1.00
21.30
C

ATOM
451
NZ
LYS
A1059
17.028
46.597
18.453
1.00
21.29
N

ATOM
452
C
LYS
A1059
11.045
42.112
19.420
1.00
20.60
C

ATOM
453
O
LYS
A1059
10.341
42.601
20.309
1.00
19.75
O

ATOM
454
N
GLU
A1060
10.550
41.448
18.381
1.00
21.44
N

ATOM
455
CA
GLU
A1060
9.118
41.246
18.234
1.00
22.69
C

ATOM
456
CB
GLU
A1060
8.783
40.742
16.832
1.00
24.22
C

ATOM
457
CG
GLU
A1060
7.303
40.761
16.521
1.00
27.42
C

ATOM
458
CD
GLU
A1060
6.730
42.169
16.542
1.00
29.59
C

ATOM
459
OE1
GLU
A1060
7.314
43.053
15.866
1.00
29.73
O

ATOM
460
OE2
GLU
A1060
5.700
42.386
17.229
1.00
30.63
O

ATOM
461
C
GLU
A1060
8.651
40.220
19.263
1.00
22.63
C

ATOM
462
O
GLU
A1060
7.631
40.418
19.932
1.00
22.87
O

ATOM
463
N
ALA
A1061
9.395
39.125
19.391
1.00
22.05
N

ATOM
464
CA
ALA
A1061
9.012
38.091
20.346
1.00
22.06
C

ATOM
465
CB
ALA
A1061
9.967
36.899
20.266
1.00
21.94
C

ATOM
466
C
ALA
A1061
8.997
38.663
21.755
1.00
22.04
C

ATOM
467
O
ALA
A1061
8.106
38.359
22.539
1.00
21.13
O

ATOM
468
N
PHE
A1062
9.978
39.506
22.063
1.00
22.38
N

ATOM
469
CA
PHE
A1062
10.055
40.119
23.380
1.00
23.29
C

ATOM
470
CB
PHE
A1062
11.348
40.918
23.532
1.00
22.75
C

ATOM
471
CG
PHE
A1062
11.440
41.648
24.833
1.00
22.71
C

ATOM
472
CD1
PHE
A1062
10.804
42.876
25.003
1.00
22.28
C

ATOM
473
CD2
PHE
A1062
12.107
41.080
25.914
1.00
22.60
C

ATOM
474
CE1
PHE
A1062
10.828
43.529
26.232
1.00
22.88
C

ATOM
475
CE2
PHE
A1062
12.138
41.722
27.154
1.00
22.54
C

ATOM
476
CZ
PHE
A1062
11.497
42.951
27.314
1.00
22.78
C

ATOM
477
C
PHE
A1062
8.865
41.030
23.667
1.00
24.27
C

ATOM
478
O
PHE
A1062
8.302
41.002
24.765
1.00
24.37
O

ATOM
479
N
SER
A1063
8.498
41.843
22.681
1.00
25.39
N

ATOM
480
CA
SER
A1063
7.373
42.751
22.818
1.00
26.79
C

ATOM
481
CB
SER
A1063
7.196
43.580
21.542
1.00
27.55
C

ATOM
482
OG
SER
A1063
8.184
44.598
21.464
1.00
28.80
O

ATOM
483
C
SER
A1063
6.108
41.965
23.094
1.00
27.26
C

ATOM
484
O
SER
A1063
5.271
42.366
23.897
1.00
27.47
O

ATOM
485
N
LYS
A1064
5.963
40.840
22.421
1.00
28.03
N

ATOM
486
CA
LYS
A1064
4.793
40.018
22.637
1.00
29.08
C

ATOM
487
CB
LYS
A1064
4.725
38.936
21.566
1.00
28.90
C

ATOM
488
CG
LYS
A1064
4.426
39.521
20.195
1.00
30.31
C

ATOM
489
CD
LYS
A1064
4.605
38.519
19.075
1.00
31.26
C

ATOM
490
CE
LYS
A1064
3.733
37.309
19.269
1.00
32.24
C

ATOM
491
NZ
LYS
A1064
3.887
36.361
18.141
1.00
33.56
N

ATOM
492
C
LYS
A1064
4.866
39.428
24.043
1.00
29.71
C

ATOM
493
O
LYS
A1064
3.886
39.467
24.788
1.00
29.61
O

ATOM
494
N
ALA
A1065
6.043
38.926
24.413
1.00
30.48
N

ATOM
495
CA
ALA
A1065
6.263
38.341
25.732
1.00
31.56
C

ATOM
496
CB
ALA
A1065
7.739
38.022
25.917
1.00
31.00
C

ATOM
497
C
ALA
A1065
5.780
39.269
26.851
1.00
32.65
C

ATOM
498
O
ALA
A1065
5.300
38.807
27.882
1.00
31.64
O

ATOM
499
N
MET
A1066
5.922
40.574
26.646
1.00
34.63
N

ATOM
500
CA
MET
A1066
5.479
41.557
27.630
1.00
37.05
C

ATOM
501
CB
MET
A1066
6.245
42.874
27.458
1.00
37.61
C

ATOM
502
CG
MET
A1066
7.710
42.808
27.867
1.00
39.52
C

ATOM
503
SD
MET
A1066
8.007
43.039
29.649
1.00
41.34
S

ATOM
504
CE
MET
A1066
8.983
44.550
29.647
1.00
40.03
C

ATOM
505
C
MET
A1066
3.985
41.798
27.435
1.00
38.24
C

ATOM
506
O
MET
A1066
3.313
42.364
28.295
1.00
38.31
O

ATOM
507
N
GLY
A1067
3.473
41.353
26.293
1.00
39.97
N

ATOM
508
CA
GLY
A1067
2.065
41.524
25.996
1.00
42.23
C

ATOM
509
C
GLY
A1067
1.716
42.953
25.623
1.00
43.61
C

ATOM
510
O
GLY
A1067
1.055
43.658
26.383
1.00
44.09
O

ATOM
511
N
THR
A1068
2.167
43.387
24,452
1.00
44.84
N

ATOM
512
CA
THR
A1068
1.889
44.739
23.985
1.00
46.14
C

ATOM
513
CB
THR
A1068
3.165
45.419
23.444
1.00
45.80
C

ATOM
514
OG1
THR
A1068
3.639
44.703
22.297
1.00
45.63
O

ATOM
515
CG2
THR
A1068
4.249
45.434
24.500
1.00
45.44
C

ATOM
516
C
THR
A1068
0.854
44.654
22.868
1.00
47.39
C

ATOM
517
O
THR
A1068
0.473
45.661
22.270
1.00
47.66
O

ATOM
518
N
GLY
A1069
0.409
43.432
22.592
1.00
48.83
N

ATOM
519
CA
GLY
A1069
0.585
43.211
21.555
1.00
50.40
C

ATOM
520
C
GLY
A1069
0.073
43.511
20.162
1.00
51.38
C

ATOM
521
O
GLY
A1069
0.661
42.716
19.569
1.00
51.45
O

ATOM
522
N
ILE
A1070
0.473
44.665
19.637
1.00
52.38
N

ATOM
523
CA
ILE
A1070
0.061
45.102
18.308
1.00
53.00
C

ATOM
524
CB
ILE
A1070
1.285
45.483
17.444
1.00
53.24
C

ATOM
525
CG2
ILE
A1070
2.148
44.245
17.194
1.00
53.03
C

ATOM
526
CG1
ILE
A1070
2.102
46.575
18.145
1.00
53.21
C

ATOM
527
CD1
ILE
A1070
3.310
47.043
17.350
1.00
53.51
C

ATOM
528
C
ILE
A1070
0.850
46.316
18.471
1.00
53.30
C

ATOM
529
O
ILE
A1070
1.800
46.506
17.705
1.00
53.48
O

ATOM
530
N
SER
A1071
0.544
47.137
19.473
1.00
53.35
N

ATOM
531
CA
SER
A1071
1.344
48.321
19.771
1.00
53.45
C

ATOM
532
CB
SER
A1071
0.643
49.183
20.816
1.00
53.58
C

ATOM
533
OG
SER
A1071
0.577
48.494
22.058
1.00
54.00
O

ATOM
534
C
SER
A1071
2.631
47.765
20.360
1.00
53.38
C

ATOM
535
O
SER
A1071
2.596
46.720
21.019
1.00
53.61
O

ATOM
536
N
LYS
A1072
3.763
48.431
20.138
1.00
52.81
N

ATOM
537
CA
LYS
A1072
5.019
47.908
20.680
1.00
52.05
C

ATOM
538
CB
LYS
A1072
5.857
47.243
19.575
1.00
52.53
C

ATOM
539
CG
LYS
A1072
5.068
46.578
18.459
1.00
53.49
C

ATOM
540
CD
LYS
A1072
4.079
45.535
18.964
1.00
54.32
C

ATOM
541
CE
LYS
A1072
4.750
44.344
19.619
1.00
54.90
C

ATOM
542
NZ
LYS
A1072
3.722
43.377
20.117
1.00
55.42
N

ATOM
543
C
LYS
A1072
5.897
48.936
21.383
1.00
51.05
C

ATOM
544
O
LYS
A1072
5.587
50.127
21.442
1.00
50.60
O

ATOM
545
N
LEU
A1073
7.002
48.435
21.923
1.00
50.01
N

ATOM
546
CA
LEU
A1073
7.989
49.254
22.599
1.00
48.81
C

ATOM
547
CB
LEU
A1073
8.785
48.409
23.601
1.00
49.31
C

ATOM
548
CG
LEU
A1073
8.166
48.084
24.969
1.00
49.63
C

ATOM
549
CD1
LEU
A1073
6.806
47,433
24.812
1.00
49.83
C

ATOM
550
CD2
LEU
A1073
9.099
47.160
25.720
1.00
50.04
C

ATOM
551
C
LEU
A1073
8.930
49.779
21.521
1.00
47.79
C

ATOM
552
O
LEU
A1073
8.923
49.294
20.383
1.00
47.71
O

ATOM
553
N
GLY
A1074
9.733
50.776
21.869
1.00
46.44
N

ATOM
554
CA
GLY
A1074
10.670
51.301
20.896
1.00
44.58
C

ATOM
555
C
GLY
A1074
11.722
50.244
20.621
1.00
43.12
C

ATOM
556
O
GLY
A1074
12.315
49.697
21.553
1.00
43.10
O

ATOM
557
N
PHE
A1075
11.949
49.934
19.351
1.00
41.71
N

ATOM
558
CA
PHE
A1075
12.949
48.937
19.006
1.00
40.26
C

ATOM
559
CB
PHE
A1075
12.870
48.613
17.514
1.00
41.07
C

ATOM
560
CG
PHE
A1075
11.958
47.459
17.207
1.00
42.00
C

ATOM
561
CD1
PHE
A1075
10.930
47.112
18.096
1.00
42.62
C

ATOM
562
CD2
PHE
A1075
12.124
46.707
16.048
1.00
42.28
C

ATOM
563
CE1
PHE
A1075
10.081
46.026
17.835
1.00
42.81
C

ATOM
564
CE2
PHE
A1075
11.281
45.617
15.771
1.00
42.42
C

ATOM
565
CZ
PHE
A1075
10.261
45.276
16.666
1.00
42.86
C

ATOM
566
C
PHE
A1075
14.346
49.388
19.413
1.00
38.94
C

ATOM
567
O
PHE
A1075
15.257
48.569
19.552
1.00
38.45
O

ATOM
568
N
GLN
A1076
14.503
50.692
19.623
1.00
37.14
N

ATOM
569
CA
GLN
A1076
15.779
51.244
20.051
1.00
35.77
C

ATOM
570
CB
GLN
A1076
15.864
52.739
19.720
1.00
35.98
C

ATOM
571
CG
GLN
A1076
16.064
53.046
18.240
1.00
35.74
C

ATOM
572
CD
GLN
A1076
17.323
52.418
17.683
1.00
35.92
C

ATOM
573
OE1
GLN
A1076
18.429
52.672
18.169
1.00
36.68
O

ATOM
574
NE2
GLN
A1076
17.166
51.592
16.659
1.00
35.79
N

ATOM
575
C
GLN
A1076
15.927
51.043
21.556
1.00
34.84
C

ATOM
576
O
GLN
A1076
17.000
51.249
22.116
1.00
34.87
O

ATOM
577
N
ASP
A1077
14.840
50.638
22.202
1.00
33.69
N

ATOM
578
CA
ASP
A1077
14.838
50.395
23.641
1.00
32.88
C

ATOM
579
CB
ASP
A1077
13.466
50.738
24.229
1.00
34.04
C

ATOM
580
CG
ASP
A1077
13.183
52.230
24.220
1.00
35.48
C

ATOM
581
OD1
ASP
A1077
13.877
52.971
24.953
1.00
36.31
O

ATOM
582
OD2
ASP
A1077
12.269
52.659
23.477
1.00
36.39
O

ATOM
583
C
ASP
A1077
15.170
48.935
23.943
1.00
31.37
C

ATOM
584
O
ASP
A1077
15.205
48.517
25.103
1.00
30.93
O

ATOM
585
N
LEU
A1078
15.408
48.165
22.889
1.00
29.66
N

ATOM
586
CA
LEU
A1078
15.724
46.753
23.026
1.00
28.12
C

ATOM
587
CB
LEU
A1078
14.605
45.907
22.410
1.00
28.40
C

ATOM
588
CG
LEU
A1078
13.211
46.138
22.999
1.00
28.65
C

ATOM
589
CD1
LEU
A1078
12.175
45.297
22.250
1.00
28.42
C

ATOM
590
CD2
LEU
A1078
13.232
45.784
24.485
1.00
28.42
C

ATOM
591
C
LEU
A1078
17.029
46.469
22.317
1.00
26.77
C

ATOM
592
O
LEU
A1078
17.256
46.963
21.219
1.00
26.91
O

ATOM
593
N
GLU
A1079
17.892
45.683
22.944
1.00
25.48
N

ATOM
594
CA
GLU
A1079
19.166
45.352
22.330
1.00
24.50
C

ATOM
595
CB
GLU
A1079
20.287
46.202
22.921
1.00
24.22
C

ATOM
596
CG
GLU
A1079
21.561
46.128
22.114
1.00
23.64
C

ATOM
597
CD
GLU
A1079
22.638
47.051
22.635
1.00
24.07
C

ATOM
598
QE1
GLU
A1079
23.079
46.862
23.791
1.00
23.41
O

ATOM
599
OE2
GLU
A1079
23.044
47.967
21.883
1.00
24.29
O

ATOM
600
C
GLU
A1079
19.512
43.885
22.488
1.00
23.86
C

ATOM
601
O
GLU
A1079
19.341
43.305
23.560
1.00
23.77
O

ATOM
602
N
VAL
A1080
20.003
43.291
21.408
1.00
23.09
N

ATOM
603
CA
VAL
A1080
20.377
41.888
21.411
1.00
22.78
C

ATOM
604
CB
VAL
A1080
19.413
41.032
20.529
1.00
22.41
C

ATOM
605
CG1
VAL
A1080
20.005
39.649
20.284
1.00
21.10
C

ATOM
606
CG2
VAL
A1080
18.059
40.893
21.224
1.00
21.12
C

ATOM
607
C
VAL
A1080
21.800
41.707
20.909
1.00
23.31
C

ATOM
608
O
VAL
A1080
22.102
41.942
19.737
1.00
23.36
O

ATOM
609
N
LEU
A1081
22.673
41.292
21.818
1.00
23.52
N

ATOM
610
CA
LEU
A1081
24.066
41.056
21.488
1.00
23.32
C

ATOM
611
CB
LEU
A1081
24.968
41.910
22.391
1.00
22.81
C

ATOM
612
CG
LEU
A1081
24.725
43.426
22.313
1.00
22.95
C

ATOM
613
CD1
LEU
A1081
25.680
44.170
23.239
1.00
22.31
C

ATOM
614
CD2
LEU
A1081
24.919
43.902
20.874
1.00
23.08
C

ATOM
615
C
LEU
A1081
24.347
39.576
21.709
1.00
23.58
C

ATOM
616
O
LEU
A1081
23.436
38.786
21.981
1.00
22.36
O

ATOM
617
N
ASN
A1082
25.614
39.204
21.582
1.00
24.47
N

ATOM
618
CA
ASN
A1082
26.018
37.826
21.802
1.00
25.10
C

ATOM
619
CB
ASN
A1082
26.745
37.301
20.564
1.00
25.30
C

ATOM
620
CG
ASN
A1082
25.798
37.072
19.406
1.00
25.42
C

ATOM
621
OD1
ASN
A1082
24.863
36.277
19.514
1.00
26.33
O

ATOM
622
ND2
ASN
A1082
26.023
37.769
18.299
1.00
25.02
N

ATOM
623
C
ASN
A1082
26.897
37.774
23.042
1.00
25.09
C

ATOM
624
O
ASN
A1082
27.802
38.586
23.197
1.00
24.45
O

ATOM
625
N
ASN
A1083
26.614
36.825
23.932
1.00
26.16
N

ATOM
626
CA
ASN
A1083
27.365
36.697
25.180
1.00
26.89
C

ATOM
627
CB
ASN
A1083
26.484
36.048
26.264
1.00
26.14
C

ATOM
628
CG
ASN
A1083
26.094
34.600
25.952
1.00
25.65
C

ATOM
629
OD1
ASN
A1083
25.289
34.006
26.668
1.00
25.06
O

ATOM
630
ND2
ASN
A1083
26.665
34.032
24.900
1.00
25.04
N

ATOM
631
C
ASN
A1083
28.691
35.953
25.044
1.00
27.81
C

ATOM
632
O
ASN
A1083
29.098
35.595
23.939
1.00
27.57
O

ATOM
633
N
GLU
A1084
29.373
35.729
26.162
1.00
29.55
N

ATOM
634
CA
GLU
A1084
30.656
35.041
26.102
1.00
31.72
C

ATOM
635
CB
GLU
A1084
31.382
35.091
27.465
1.00
32.66
C

ATOM
636
CG
GLU
A1084
30.618
34.574
28.685
1.00
34.91
C

ATOM
637
CD
GLU
A1084
31.407
34.752
29.998
1.00
36.48
C

ATOM
638
OE1
GLU
A1084
32.421
34.051
30.192
1.00
37.32
O

ATOM
639
OE2
GLU
A1084
31.022
35.601
30.841
1.00
37.46
O

ATOM
640
C
GLU
A1084
30.532
33.603
25.584
1.00
32.13
C

ATOM
641
O
GLU
A1084
31.522
33.007
25.186
1.00
32.93
O

ATOM
642
N
ARG
A1085
29.322
33.052
25.578
1.00
32.33
N

ATOM
643
CA
ARG
A1085
29.118
31.703
25.061
1.00
32.71
C

ATOM
644
CB
ARG
A1085
28.057
30.950
25.866
1.00
34.65
C

ATOM
645
CG
ARG
A1085
28.525
30.506
27.238
1.00
37.26
C

ATOM
646
CD
ARG
A1085
29.588
29.432
27.112
1.00
39.70
C

ATOM
647
NE
ARG
A1085
30.430
29.337
28.303
1.00
42.39
N

ATOM
648
CZ
ARG
A1085
31.329
28.375
28.501
1.00
43.44
C

ATOM
649
NH1
ARG
A1085
32.062
28.363
29.611
1.00
44.05
N

ATOM
650
NH2
ARG
A1085
31.482
27.415
27.593
1.00
43.73
N

ATOM
651
C
ARG
A1085
28.682
31.788
23.606
1.00
31.86
C

ATOM
652
O
ARG
A1085
28.369
30.775
22.983
1.00
32.12
O

ATOM
653
N
GLY
A1086
28.664
33.006
23.070
1.00
30.59
N

ATOM
654
CA
GLY
A1086
28.275
33.206
21.687
1.00
29.15
C

ATOM
655
C
GLY
A1086
26.779
33.208
21.427
1.00
28.22
C

ATOM
656
O
GLY
A1086
26.347
33.336
20.287
1.00
28.76
O

ATOM
657
N
ALA
A1087
25.980
33.079
22.476
1.00
26.78
N

ATOM
658
CA
ALA
A1087
24.536
33.052
22.313
1.00
25.40
C

ATOM
659
CB
ALA
A1087
23.907
32.162
23.378
1.00
24.76
C

ATOM
660
C
ALA
A1087
23.936
34.448
22.390
1.00
24.84
C

ATOM
661
O
ALA
A1087
24.417
35.304
23.142
1.00
24.29
O

ATOM
662
N
PRO
A1088
22.886
34.703
21.591
1.00
23.94
N

ATOM
663
CD
PRO
A1088
22.363
33.864
20.496
1.00
23.58
C

ATOM
664
CA
PRO
A1088
22.234
36.009
21.601
1.00
23.19
C

ATOM
665
CB
PRO
A1088
21.303
35.944
20.388
1.00
23.32
C

ATOM
666
CG
PRO
A1088
21.019
34.482
20.239
1.00
23.28
C

ATOM
667
C
PRO
A1088
21.483
36.232
22.911
1.00
22.65
C

ATOM
668
O
PRO
A1088
20.908
35.304
23.475
1.00
22.59
O

ATOM
669
N
TYR
A1089
21.518
37.464
23.407
1.00
22.22
N

ATOM
670
CA
TYR
A1089
20.824
37.808
24.645
1.00
21.73
C

ATOM
671
CB
TYR
A1089
21.720
37.537
25.866
1.00
21.31
C

ATOM
672
CG
TYR
A1089
22.843
38.540
26.058
1.00
20.82
C

ATOM
673
CD1
TYR
A1089
22.795
39.475
27.095
1.00
20.39
C

ATOM
674
CE1
TYR
A1089
23.791
40.428
27.253
1.00
20.46
C

ATOM
675
CD2
TYR
A1089
23.931
38.582
25.177
1.00
20.50
C

ATOM
676
CE2
TYR
A1089
24.942
39.535
25.323
1.00
20.31
C

ATOM
677
CZ
TYR
A1089
24.865
40.458
26.363
1.00
21.12
C

ATOM
678
OH
TYR
A1089
25.844
41.421
26.507
1.00
20.91
O

ATOM
679
C
TYR
A1089
20.459
39.278
24.598
1.00
21.43
C

ATOM
680
O
TYR
A1089
20.986
40.045
23.782
1.00
21.20
O

ATOM
681
N
PHE
A1090
19.541
39.670
25.469
1.00
21.81
N

ATOM
682
CA
PHE
A1090
19.134
41.058
25.534
1.00
21.85
C

ATOM
683
CB
PHE
A1090
17.694
41.182
26.041
1.00
20.99
C

ATOM
684
CG
PHE
A1090
16.651
40.841
25.006
1.00
20.79
C

ATOM
685
CD1
PHE
A1090
16.294
39.519
24.755
1.00
20.19
C

ATOM
686
CD2
PHE
A1090
16.052
41.849
24.247
1.00
20.29
C

ATOM
687
CE1
PHE
A1090
15.364
39.207
23.760
1.00
19.79
C

ATOM
688
CE2
PHE
A1090
15.122
41.543
23.252
1.00
20.00
C

ATOM
689
CZ
PHE
A1090
14.778
40.221
23.007
1.00
19.21
C

ATOM
690
C
PHE
A1090
20.087
41.794
26.467
1.00
22.39
C

ATOM
691
O
PHE
A1090
20.197
41.460
27.643
1.00
22.82
O

ATOM
692
N
SER
A1091
20.791
42.780
25.922
1.00
23.17
N

ATOM
693
CA
SER
A1091
21.725
43.590
26.697
1.00
24.38
C

ATOM
694
CB
SER
A1091
22.879
44.048
25.805
1.00
24.43
C

ATOM
695
OG
SER
A1091
22.405
44.352
24.504
1.00
25.11
O

ATOM
696
C
SER
A1091
20.979
44.805
27.248
1.00
24.91
C

ATOM
697
O
SER
A1091
21.420
45.443
28.204
1.00
24.93
O

ATOM
698
N
GLN
A1092
19.854
45.124
26.618
1.00
25.07
N

ATOM
699
CA
GLN
A1092
19.023
46.235
27.046
1.00
26.14
C

ATOM
700
CB
GLN
A1092
19.357
47.517
26.258
1.00
27.41
C

ATOM
701
CG
GLN
A1092
20.779
48.089
26.463
1.00
29.10
C

ATOM
702
CD
GLN
A1092
21.096
48.475
27.918
1.00
31.36
C

ATOM
703
QE1
GLN
A1092
20.273
49.093
28.607
1.00
32.18
O

ATOM
704
NE2
GLN
A1092
22.306
48.127
28.380
1.00
31.33
N

ATOM
705
C
GLN
A1092
17.556
45.850
26.841
1.00
25.78
C

ATOM
706
O
GLN
A1092
17.148
45.443
25.753
1.00
25.27
O

ATOM
707
N
ALA
A1093
16.777
45.961
27.909
1.00
25.60
N

ATOM
708
CA
ALA
A1093
15.357
45.630
27.870
1.00
25.62
C

ATOM
709
CB
ALA
A1093
15.171
44.110
27.867
1.00
24.75
C

ATOM
710
C
ALA
A1093
14.677
46.238
29.090
1.00
25.61
C

ATOM
711
O
ALA
A1093
15.220
46.209
30.186
1.00
25.48
O

ATOM
712
N
PRO
A1094
13.474
46.796
28.916
1.00
26.29
N

ATOM
713
CD
PRO
A1094
12.668
46.878
27.682
1.00
26.31
C

ATOM
714
CA
PRO
A1094
12.758
47.400
30.046
1.00
26.85
C

ATOM
715
CB
PRO
A1094
11.622
48.147
29.358
1.00
26.71
C

ATOM
716
CG
PRO
A1094
11.292
47.223
28.222
1.00
26.01
C

ATOM
717
C
PRO
A1094
12.241
46.343
31.024
1.00
27.25
C

ATOM
718
O
PRO
A1094
11.182
46.511
31.631
1.00
28.16
O

ATOM
719
N
PHE
A1095
12.980
45.248
31.167
1.00
26.92
N

ATOM
720
CA
PHE
A1095
12.571
44.181
32.069
1.00
26.96
C

ATOM
721
CB
PHE
A1095
12.234
42.918
31.279
1.00
26.69
C

ATOM
722
CG
PHE
A1095
11.729
41.782
32.127
1.00
26.67
C

ATOM
723
CD1
PHE
A1095
12.396
40.553
32.137
1.00
26.30
C

ATOM
724
CD2
PHE
A1095
10.567
41.920
32.879
1.00
25.87
C

ATOM
725
CE1
PHE
A1095
11.911
39.481
32.878
1.00
25.90
C

ATOM
726
CE2
PHE
A1095
10.074
40.853
33.624
1.00
25.69
C

ATOM
727
CZ
PHE
A1095
10.746
39.628
33.625
1.00
26.13
C

ATOM
728
C
PHE
A1095
13.685
43.891
33.055
1.00
26.99
C

ATOM
729
O
PHE
A1095
14.854
43.835
32.680
1.00
27.34
O

ATOM
730
N
SER
A1096
13.319
43.687
34.314
1.00
26.53
N

ATOM
731
CA
SER
A1096
14.308
43.436
35.340
1.00
26.73
C

ATOM
732
CB
SER
A1096
13.973
44.263
36.596
1.00
27.70
C

ATOM
733
OG
SER
A1096
12.642
44.023
37.052
1.00
29.18
O

ATOM
734
C
SER
A1096
14.500
41.968
35.715
1.00
26.21
C

ATOM
735
O
SER
A1096
15.426
41.639
36.464
1.00
26.51
O

ATOM
736
N
GLY
A1097
13.648
41.088
35.198
1.00
25.26
N

ATOM
737
CA
GLY
A1097
13.773
39.679
35.521
1.00
24.11
C

ATOM
738
C
GLY
A1097
14.633
38.918
34.529
1.00
24.17
C

ATOM
739
O
GLY
A1097
15.383
39.512
33.758
1.00
24.01
O

ATOM
740
N
LYS
A1098
14.526
37.594
34.552
1.00
23.74
N

ATOM
741
CA
LYS
A1098
15.281
36.745
33.643
1.00
23.42
C

ATOM
742
CB
LYS
A1098
15.360
35.309
34.172
1.00
24.51
C

ATOM
743
CG
LYS
A1098
16.177
35.141
35.444
1.00
26.65
C

ATOM
744
CD
LYS
A1098
16.236
33.682
35.898
1.00
28.23
C

ATOM
745
CE
LYS
A1098
17.224
33.510
37.058
1.00
30.02
C

ATOM
746
NZ
LYS
A1098
17.270
32.108
37.594
1.00
30.95
N

ATOM
747
C
LYS
A1098
14.602
36.730
32.287
1.00
22.48
C

ATOM
748
O
LYS
A1098
13.374
36.671
32.192
1.00
22.17
O

ATOM
749
N
ILE
A1099
15.419
36.782
31.241
1.00
21.41
N

ATOM
750
CA
ILE
A1099
14.941
36.761
29.876
1.00
20.15
C

ATOM
751
CB
ILE
A1099
15.333
38.039
29.134
1.00
19.84
C

ATOM
752
CG2
ILE
A1099
14.804
37.989
27.713
1.00
20.13
C

ATOM
753
CG1
ILE
A1099
14.791
39.263
29.873
1.00
19.76
C

ATOM
754
CD1
ILE
A1099
15.218
40.583
29.262
1.00
18.64
C

ATOM
755
C
ILE
A1099
15.576
35.581
29.148
1.00
19.81
C

ATOM
756
O
ILE
A1099
16.791
35.528
28.972
1.00
20.43
O

ATOM
757
N
TRP
A1100
14.761
34.623
28.740
1.00
19.20
N

ATOM
758
CA
TRP
A1100
15.277
33.480
28.005
1.00
18.42
C

ATOM
759
CB
TRP
A1100
14.653
32.193
28.530
1.00
17.66
C

ATOM
760
CG
TRP
A1100
14.970
31.962
29.973
1.00
17.80
C

ATOM
761
CD2
TRP
A1100
16.150
31.351
30.501
1.00
17.39
C

ATOM
762
CE2
TRP
A1100
16.038
31.375
31.914
1.00
17.58
C

ATOM
763
CE3
TRP
A1100
17.294
30.787
29.921
1.00
17.40
C

ATOM
764
CD1
TRP
A1100
14.210
32.323
31.055
1.00
17.92
C

ATOM
765
NE1
TRP
A1100
14.844
31.972
32.222
1.00
17.09
N

ATOM
766
CZ2
TRP
A1100
17.030
30.851
32.759
1.00
16.77
C

ATOM
767
CZ3
TRP
A1100
18.283
30.268
30.763
1.00
17.50
C

ATOM
768
CH2
TRP
A1100
18.138
30.307
32.167
1.00
17.07
C

ATOM
769
C
TRP
A1100
14.946
33.700
26.526
1.00
17.86
C

ATOM
770
O
TRP
A1100
13.791
33.866
26.143
1.00
18.05
O

ATOM
771
N
LEU
A1100
15.987
33.725
25.707
1.00
17.46
N

ATOM
772
CA
LEU
A1100
15.852
33.967
24.290
1.00
16.38
C

ATOM
773
CB
LEU
A1100
16.469
35.325
23.955
1.00
15.64
C

ATOM
774
CG
LEU
A1100
16.715
35.601
22.468
1.00
15.15
C

ATOM
775
CD1
LEU
A1100
15.379
35.873
21.762
1.00
13.79
C

ATOM
776
CD2
LEU
A1100
17.669
36.775
22.317
1.00
14.27
C

ATOM
777
C
LEU
A1100
16.520
32.916
23.429
1.00
16.47
C

ATOM
778
O
LEU
A1100
17.624
32.474
23.720
1.00
16.38
O

ATOM
779
N
SER
A1102
15.847
32.520
22.356
1.00
17.12
N

ATOM
780
CA
SER
A1102
16.429
31.565
21.432
1.00
17.39
C

ATOM
781
CB
SER
A1102
15.962
30.140
21.722
1.00
16.65
C

ATOM
782
OG
SER
A1102
16.736
29.217
20.966
1.00
15.28
O

ATOM
783
C
SER
A1102
16.052
31.965
20.011
1.00
18.55
C

ATOM
784
O
SER
A1102
14.902
32.319
19.727
1.00
18.33
O

ATOM
785
N
ILE
A1103
17.043
31.930
19.127
1.00
19.20
N

ATOM
786
CA
ILE
A1103
16.836
32.286
17.740
1.00
20.42
C

ATOM
787
CB
ILE
A1103
17.588
33.578
17.386
1.00
20.38
C

ATOM
788
CG2
ILE
A1103
17.216
34.026
15.981
1.00
19.83
C

ATOM
789
CG1
ILE
A1103
17.240
34.675
18.399
1.00
20.72
C

ATOM
790
CD1
ILE
A1103
17.996
35.980
18.172
1.00
20.84
C

ATOM
791
C
ILE
A1103
17.347
31.169
16.843
1.00
21.44
C

ATOM
792
O
ILE
A1103
18.373
30.551
17.121
1.00
21.72
O

ATOM
793
N
SER
A1104
16.625
30.916
15.764
1.00
21.94
N

ATOM
794
CA
SER
A1104
17.015
29.884
14.823
1.00
22.99
C

ATOM
795
CB
SER
A1104
16.334
28.556
15.185
1.00
22.73
C

ATOM
796
OG
SER
A1104
16.618
27.550
14.229
1.00
21.97
O

ATOM
797
C
SER
A1104
16.607
30.322
13.421
1.00
23.89
C

ATOM
798
O
SER
A1104
15.698
31.139
13.246
1.00
24.13
O

ATOM
799
N
HIS
A1100
17.283
29.787
12.417
1.00
25.15
N

ATOM
800
CA
HIS
A1100
16.943
30.144
11.049
1.00
26.29
C

ATOM
801
CB
HIS
A1100
17.665
31.429
10.633
1.00
26.35
C

ATOM
802
CG
HIS
A1100
19.153
31.290
10.559
1.00
27.08
C

ATOM
803
CD2
HIS
A1100
19.960
30.889
9.549
1.00
27.02
C

ATOM
804
ND1
HIS
A1100
19.980
31.551
11.630
1.00
27.58
N

ATOM
805
CE1
HIS
A1100
21.234
31.317
11.283
1.00
27.17
C

ATOM
806
NE2
HIS
A1100
21.249
30.914
10.025
1.00
27.22
N

ATOM
807
C
HIS
A1100
17.276
29.060
10.042
1.00
26.76
C

ATOM
808
O
HIS
A1100
18.031
28.129
10.318
1.00
26.55
O

ATOM
809
N
THR
A1106
16.670
29.197
8.874
1.00
27.49
N

ATOM
810
CA
THR
A1106
16.901
28.309
7.751
1.00
28.62
C

ATOM
811
CB
THR
A1106
15.595
27.643
7.273
1.00
28.44
C

ATOM
812
OG1
THR
A1106
14.721
28.635
6.712
1.00
27.15
O

ATOM
813
CG2
THR
A1106
14.901
26.954
8.447
1.00
28.62
C

ATOM
814
C
THR
A1106
17.381
29.299
6.698
1.00
29.33
C

ATOM
815
O
THR
A1106
17.685
30.442
7.027
1.00
29.14
O

ATOM
816
N
ASP
A1107
17.446
28.880
5.444
1.00
30.59
N

ATOM
817
CA
ASP
A1107
17.878
29.789
4.392
1.00
31.74
C

ATOM
818
CB
ASP
A1107
18.324
28.992
3.160
1.00
33.44
C

ATOM
819
CG
ASP
A1107
19.499
28.054
3.454
1.00
35.18
C

ATOM
820
OD1
ASP
A1107
19.827
27.214
2.582
1.00
36.15
O

ATOM
821
OD2
ASP
A1107
20.099
28.153
4.548
1.00
35.79
O

ATOM
822
C
ASP
A1107
16.720
30.722
4.020
1.00
31.63
C

ATOM
823
O
ASP
A1107
16.913
31.724
3.334
1.00
31.90
O

ATOM
824
N
GLN
A1100
15.518
30.401
4.494
1.00
31.41
N

ATOM
825
CA
GLN
A1108
14.336
31.201
4.175
1.00
30.98
C

ATOM
826
CB
GLN
A1108
13.340
30.345
3.399
1.00
32.64
C

ATOM
827
CG
GLN
A1108
13.860
29.898
2.038
1.00
34.63
C

ATOM
828
CD
GLN
A1108
12.917
28.945
1.346
1.00
35.98
C

ATOM
829
OE1
GLN
A1108
12.698
27.819
1.807
1.00
36.85
O

ATOM
830
NE2
GLN
A1108
12.340
29.391
0.231
1.00
36.81
N

ATOM
831
C
GLN
A1108
13.616
31.862
5.338
1.00
29.94
C

ATOM
832
O
GLN
A1100
12.985
32.899
5.158
1.00
29.44
O

ATOM
833
N
PHE
A1109
13.700
31.269
6.529
1.00
29.06
N

ATOM
834
CA
PHE
A1109
13.024
31.838
7.692
1.00
27.73
C

ATOM
835
CB
PHE
A1109
11.762
31.036
8.037
1.00
27.57
C

ATOM
836
CG
PHE
A1109
10.744
31.005
6.941
1.00
27.23
C

ATOM
837
CD1
PHE
A1109
10.788
30.017
5.962
1.00
27.53
C

ATOM
838
CD2
PHE
A1109
9.749
31.976
6.871
1.00
27.16
C

ATOM
839
CE1
PHE
A1109
9.852
30.000
4.921
1.00
27.28
C

ATOM
840
CE2
PHE
A1109
8.810
31.970
5.838
1.00
26.77
C

ATOM
841
CZ
PHE
A1109
8.861
30.981
4.861
1.00
26.97
C

ATOM
842
C
PHE
A1109
13.868
31.932
8.950
1.00
26.95
C

ATOM
843
O
PHE
A1109
14.877
31.243
9.102
1.00
27.19
O

ATOM
844
N
VAL
A1110
13.431
32.803
9.852
1.00
25.89
N

ATOM
845
CA
VAL
A1110
14.080
32.992
11.138
1.00
25.13
C

ATOM
846
CB
VAL
A1110
14.844
34.347
11.197
1.00
25.40
C

ATOM
847
CG1
VAL
A1110
13.874
35.510
11.081
1.00
25.64
C

ATOM
848
CG2
VAL
A1110
15.623
34.449
12.499
1.00
25.77
C

ATOM
849
C
VAL
A1110
12.956
32.973
12.184
1.00
24.39
C

ATOM
850
O
VAL
A1110
11.863
33.500
11.936
1.00
24.17
O

ATOM
851
N
THR
A1111
13.206
32.344
13.332
1.00
23.30
N

ATOM
852
CA
THR
A1111
12.208
32.289
14.404
1.00
22.55
C

ATOM
853
CB
THR
A1111
11.610
30.888
14.562
1.00
22.93
C

ATOM
854
OG1
THR
A1111
12.670
29.954
14.786
1.00
24.79
O

ATOM
855
CG2
THR
A1111
10.839
30.479
13.323
1.00
23.61
C

ATOM
856
C
THR
A1111
12.830
32.664
15.746
1.00
21.62
C

ATOM
857
O
THR
A1111
13.999
32.377
16.002
1.00
21.64
O

ATOM
858
N
ALA
A1112
12.041
33.299
16.605
1.00
20.37
N

ATOM
859
CA
ALA
A1112
12.522
33.688
17.922
1.00
19.66
C

ATOM
860
CB
ALA
A1112
12.800
35.202
17.970
1.00
19.55
C

ATOM
861
C
ALA
A1112
11.516
33.311
19.004
1.00
19.07
C

ATOM
862
O
ALA
A1112
10.302
33.410
18.814
1.00
19.29
O

ATOM
863
N
SER
A1113
12.034
32.872
20.139
1.00
17.99
N

ATOM
864
CA
SER
A1113
11.195
32.506
21.263
1.00
17.22
C

ATOM
865
CB
SER
A1113
11.174
30;989
21.457
1.00
16.88
C

ATOM
866
OG
SER
A1113
10.313
30.614
22.521
1.00
16.26
O

ATOM
867
C
SER
A1113
11.782
33.180
22.487
1.00
17.09
C

ATOM
868
O
SER
A1113
12.995
33.112
22.733
1.00
16.32
O

ATOM
869
N
VAL
A1114
10.906
33.831
23.245
1.00
17.10
N

ATOM
870
CA
VAL
A1114
11.289
34.548
24.451
1.00
16.74
C

ATOM
871
CB
VAL
A1114
11.164
36.081
24.243
1.00
16.29
C

ATOM
872
CG1
VAL
A1114
11.205
36.814
25.592
1.00
15.10
C

ATOM
873
CG2
VAL
A1114
12.298
36.574
23.329
1.00
16.31
C

ATOM
874
C
VAL
A1114
10.422
34.149
25.635
1.00
17.36
C

ATOM
875
O
VAL
A1114
9.190
34.114
25.544
1.00
16.90
O

ATOM
876
N
ILE
A1115
11.073
33.834
26.747
1.00
17.78
N

ATOM
877
CA
ILE
A1115
10.354
33.478
27.957
1.00
18.59
C

ATOM
878
CB
ILE
A1115
10.632
32.020
28.395
1.00
17.89
C

ATOM
879
CG2
ILE
A1115
9.806
31.691
29.641
1.00
17.73
C

ATOM
880
CG1
ILE
A1115
10.247
31.053
27.272
1.00
18.13
C

ATOM
881
CD1
ILE
A1115
10.654
29.599
27.521
1.00
17.22
C

ATOM
882
C
ILE
A1115
10.830
34.431
29.049
1.00
19.32
C

ATOM
883
O
ILE
A1115
12.025
34.538
29.304
1.00
19.25
O

ATOM
884
N
LEU
A1116
9.895
35.137
29.670
1.00
20.62
N

ATOM
885
CA
LEU
A1116
10.239
36.066
30.736
1.00
22.56
C

ATOM
886
CB
LEU
A1116
9.408
37.341
30.617
1.00
22.06
C

ATOM
887
CG
LEU
A1116
9.547
38.064
29.272
1.00
22.11
C

ATOM
888
CD1
LEU
A1116
8.540
39.207
29.187
1.00
21.22
C

ATOM
889
CD2
LEU
A1116
10.969
38.578
29.113
1.00
21.72
C

ATOM
890
C
LEU
A1116
9.984
35.379
32.069
1.00
24.06
C

ATOM
891
O
LEU
A1116
8.936
34.765
32.275
1.00
23.78
O

ATOM
892
N
GLU
A1117
10.953
35.486
32.970
1.00
25.93
N

ATOM
893
CA
GLU
A1117
10.857
34.843
34.267
1.00
28.06
C

ATOM
894
CB
GLU
A1117
11.604
33.502
34.204
1.00
28.05
C

ATOM
895
CG
GLU
A1117
11.800
32.793
35.536
1.00
28.32
C

ATOM
896
CD
GLU
A1117
12.626
31.512
35.405
1.00
28.66
C

ATOM
897
OE1
GLU
A1117
13.711
31.567
34.777
1.00
28.33
O

ATOM
898
OE2
GLU
A1117
12.196
30.458
35.936
1.00
28.07
O

ATOM
899
C
GLU
A1117
11.413
35.699
35.404
1.00
29.70
C

ATOM
900
O
GLU
A1117
12.242
36.583
35.190
1.00
29.81
O

ATOM
901
N
GLU
A1118
10.928
35.441
36.615
1.00
31.64
N

ATOM
902
CA
GLU
A1118
11.416
36.141
37.794
1.00
33.73
C

ATOM
903
CB
GLU
A1118
10.860
37.567
37.862
1.00
35.16
C

ATOM
904
CG
GLU
A1118
9.358
37.670
37.941
1.00
37.05
C

ATOM
905
CD
GLU
A1118
8.900
39.113
38.056
1.00
38.65
C

ATOM
906
OE1
GLU
A1118
9.476
39.973
37.348
1.00
38.82
O

ATOM
907
OE2
GLU
A1118
7.961
39.385
38.848
1.00
39.77
O

ATOM
908
C
GLU
A1118
11.043
35.365
39.048
1.00
34.16
C

ATOM
909
O
GLU
A1118
9.912
34.845
39.107
1.00
34.38
O

ATOM
910
OXT
GLU
A1118
11.894
35.280
39.956
1.00
35.21
O

TER
911

GLU
A1118

ATOM
912
CB
MET
B2003
5.244
24.216
39.082
1.00
30.13
C

ATOM
913
CG
MET
B2003
5.229
22.763
38.655
1.00
32.03
C

ATOM
914
SD
MET
B2003
4.499
21.640
39.877
1.00
34.60
S

ATOM
915
CE
MET
B2003
5.729
20.323
39.875
1.00
32.91
C

ATOM
916
C
MET
B2003
5.364
24.946
36.697
1.00
27.68
C

ATOM
917
O
MET
B2003
4.190
25.254
36.454
1.00
27.76
O

ATOM
918
N
MET
B2003
5.824
26.555
38.533
1.00
28.66
N

ATOM
919
CA
MET
B2003
5.954
25.143
38.090
1.00
28.51
C

ATOM
920
N
ILE
B2004
6.184
24.439
35.782
1.00
26.12
N

ATOM
921
CA
ILE
B2004
5.730
24.192
34.423
1.00
24.36
C

ATOM
922
CB
ILE
B2004
6.907
24.200
33.423
1.00
23.97
C

ATOM
923
CG2
ILE
B2004
6.445
23.691
32.062
1.00
22.87
C

ATOM
924
CG1
ILE
B2004
7.465
25.624
33.300
1.00
23.67
C

ATOM
925
CD1
ILE
B2004
8.670
25.746
32.379
1.00
23.02
C

ATOM
926
C
ILE
B2004
5.035
22.841
34.376
1.00
23.70
C

ATOM
927
O
ILE
B2004
5.537
21.854
34.917
1.00
23.27
O

ATOM
928
N
VAL
B2005
3.866
22.793
33.748
1.00
22.71
N

ATOM
929
CA
VAL
B2005
3.151
21.530
33.660
1.00
22.27
C

ATOM
930
CB
VAL
B2005
1.853
21.564
34.494
1.00
21.83
C

ATOM
931
CG1
VAL
B2005
2.204
21.793
35.959
1.00
21.47
C

ATOM
932
CG2
VAL
B2005
0.920
22.653
33.994
1.00
21.79
C

ATOM
933
C
VAL
B2005
2.847
21.133
32.228
1.00
22.00
C

ATOM
934
O
VAL
B2005
2.130
20.163
31.995
1.00
22.54
O

ATOM
935
N
GLY
B2006
3.417
21.880
31.278
1.00
21.53
N

ATOM
936
CA
GLY
B2006
3.225
21.594
29.867
1.00
20.47
C

ATOM
937
C
GLY
B2006
3.802
22.634
28.914
1.00
19.98
C

ATOM
938
O
GLY
B2006
3.873
23.820
29.237
1.00
20.12
O

ATOM
939
N
HIS
B2007
4.235
22.175
27.741
1.00
19.33
N

ATOM
940
CA
HIS
B2007
4.789
23.031
26.686
1.00
18.80
C

ATOM
941
CB
HIS
B2007
6.301
23.191
26.832
1.00
18.37
C

ATOM
942
CG
HIS
B2007
6.945
23.945
25.708
1.00
18.59
C

ATOM
943
CD2
HIS
B2007
8.088
23.712
25.015
1.00
19.30
C

ATOM
944
ND1
HIS
B2007
6.447
25.138
25.226
1.00
18.65
N

ATOM
945
CE1
HIS
B2007
7.254
25.607
24.289
1.00
18.01
C

ATOM
946
NE2
HIS
B2007
8.259
24.763
24.143
1.00
18.26
N

ATOM
947
C
HIS
B2007
4.482
22.387
25.342
1.00
18.69
C

ATOM
948
O
HIS
B2007
4.731
21.197
25.146
1.00
17.82
O

ATOM
949
N
GLY
B2008
3.925
23.174
24.425
1.00
19.16
N

ATOM
950
CA
GLY
B2008
3.599
22.655
23.110
1.00
18.31
C

ATOM
951
C
GLY
B2008
3.703
23.724
22.043
1.00
18.66
C

ATOM
952
O
GLY
B2008
3.378
24.890
22.297
1.00
18.62
O

ATOM
953
N
ILE
B2009
4.175
23.336
20.858
1.00
18.12
N

ATOM
954
CA
ILE
B2009
4.282
24.257
19.736
1.00
18.56
C

ATOM
955
CB
ILE
B2009
5.747
24.562
19.351
1.00
18.23
C

ATOM
956
CG2
ILE
B2009
6.471
25.174
20.538
1.00
17.94
C

ATOM
957
CG1
ILE
B2009
6.440
23.285
18.847
1.00
17.91
C

ATOM
958
CD1
ILE
B2009
7.819
23.525
18.220
1.00
16.62
C

ATOM
959
C
ILE
B2009
3.601
23.657
18.513
1.00
19.50
C

ATOM
960
O
ILE
B2009
3.286
22.470
18.472
1.00
18.95
O

ATOM
961
N
ASP
B2010
3.356
24.492
17.518
1.00
20.39
N

ATOM
962
CA
ASP
B2010
2.751
24.015
16.298
1.00
21.57
C

ATOM
963
CB
ASP
B2010
1.251
23.773
16.481
1.00
22.40
C

ATOM
964
CG
ASP
B2010
0.635
22.980
15.317
1.00
23.74
C

ATOM
965
OD1
ASP
B2010
0.223
23.595
14.308
1.00
23.88
O

ATOM
966
OD2
ASP
B2010
0.576
21.731
15.415
1.00
24.74
O

ATOM
967
C
ASP
B2010
2.979
25.019
15.200
1.00
22.11
C

ATOM
968
O
ASP
B2010
3.032
26.224
15.443
1.00
22.03
O

ATOM
969
N
ILE
B2011
3.145
24.502
13.991
1.00
23.00
N

ATOM
970
CA
ILE
B2011
3.335
25.336
12.824
1.00
24.24
C

ATOM
971
CB
ILE
B2011
4.818
25.320
12.339
1.00
24.43
C

ATOM
972
CG2
ILE
B2011
5.258
23.905
11.972
1.00
24.62
C

ATOM
973
CG1
ILE
B2011
4.970
26.244
11.133
1.00
25.18
C

ATOM
974
CD1
ILE
B2011
6.404
26.433
10.684
1.00
26.49
C

ATOM
975
C
ILE
B2011
2.398
24.818
11.732
1.00
25.03
C

ATOM
976
O
ILE
B2011
2.257
23.609
11.532
1.00
24.85
O

ATOM
977
N
GLU
B2011
1.733
25.740
11.050
1.00
26.14
N

ATOM
978
CA
GLU
B2011
0.813
25.377
9.979
1.00
27.22
C

ATOM
979
CB
GLU
B2011
0.636
25.692
10.369
1.00
28.06
C

ATOM
980
CG
GLU
B2012
1.179
24.920
11.549
1.00
30.35
C

ATOM
981
CD
GLU
B2011
1.237
23.427
11.301
1.00
31.85
C

ATOM
982
OE1
GLU
B2011
1.472
23.026
10.133
1.00
32.85
O

ATOM
983
OE2
GLU
B2011
1.065
22.660
12.278
1.00
31.85
O

ATOM
984
C
GLU
B2011
1.130
26.138
8.704
1.00
27.07
C

ATOM
985
O
GLU
B2012
1.558
27.294
8.738
1.00
26.78
O

ATOM
986
N
GLU
B2013
0.914
25.471
7.579
1.00
27.58
N

ATOM
987
CA
GLU
B2013
1.115
26.080
6.272
1.00
27.80
C

ATOM
988
CB
GLU
B2013
1.533
25.018
5.253
1.00
28.06
C

ATOM
989
CG
GLU
B2013
1.806
25.553
3.851
1.00
29.06
C

ATOM
990
CD
GLU
B2013
2.105
24.447
2.858
0.05
28.78
C

ATOM
991
OE1
GLU
B2013
3.074
23.691
3.081
0.05
28.87
O

ATOM
992
OE2
GLU
B2013
1.370
24.335
1.856
0.05
28.90
O

ATOM
993
C
GLU
B2013
−0.268
26.626
5.939
1.00
27.67
C

ATOM
994
O
GLU
B2013
−1.250
25.894
5.982
1.00
27.29
O

ATOM
995
N
LEU
B2014
−0.350
27.916
5.644
1.00
28.07
N

ATOM
996
CA
LEU
B2014
−1.629
28.542
5.330
1.00
28.65
C

ATOM
997
CB
LEU
B2014
−1.426
30.023
4.986
1.00
28.56
C

ATOM
998
CG
LEU
B2014
−1.332
31.022
6.147
1.00
28.97
C

ATOM
999
CD1
LEU
B2014
−2.677
31.113
6.840
1.00
28.76
C

ATOM
1000
CD2
LEU
B2014
−0.260
30.593
7.139
1.00
28.89
C

ATOM
1001
C
LEU
B2014
−2.356
27.847
4.189
1.00
28.89
C

ATOM
1002
O
LEU
B2014
−3.584
27.758
4.189
1.00
28.92
O

ATOM
1003
N
ALA
B2015
−1.588
27.346
3.228
1.00
29.40
N

ATOM
1004
CA
ALA
B2015
−2.137
26.665
2.058
1.00
29.93
C

ATOM
1005
CB
ALA
B2015
−0.999
26.206
1.146
1.00
29.23
C

ATOM
1006
C
ALA
B2015
−3.033
25.483
2.401
1.00
30.15
C

ATOM
1007
O
ALA
B2015
−4.062
25.278
1.760
1.00
30.32
O

ATOM
1008
N
SER
D2016
−2.648
24.703
3.403
1.00
30.53
N

ATOM
1009
CA
SER
B2016
−3.445
23.544
3.776
1.00
31.47
C

ATOM
1010
CB
SER
B2016
−2.625
22.583
4.640
1.00
31.89
C

ATOM
1011
OG
SER
B2016
−2.229
23.193
5.846
1.00
33.02
O

ATOM
1012
C
SER
B2016
−4.735
23.946
4.487
1.00
31.84
C

ATOM
1013
O
SER
B2016
−5.741
23.243
4.391
1.00
31.71
O

ATOM
1014
N
ILE
B2017
−4.716
25.068
5.201
1.00
32.07
N

ATOM
1015
CA
ILE
B2017
−5.932
25.527
5.861
1.00
32.52
C

ATOM
1016
CB
ILE
B2017
−5.651
26.688
6.843
1.00
32.37
C

ATOM
1017
CG2
ILE
B2017
−6.973
27.246
7.385
1.00
32.53
C

ATOM
1018
CG1
ILE
B2017
−4.759
26.203
7.996
1.00
32.12
C

ATOM
1019
CD1
ILE
B2017
−5.399
25.165
8.894
1.00
31.06
C

ATOM
1020
C
ILE
B2017
−6.862
26.015
4.748
1.00
33.04
C

ATOM
1021
O
ILE
B2017
−8.084
25.862
4.821
1.00
32.69
O

ATOM
1022
N
GLU
B2018
−6.263
26.597
3.711
1.00
33.86
N

ATOM
1023
CA
GLU
B2018
−7.006
27.095
2.554
1.00
34.86
C

ATOM
1024
CB
GLU
B2018
−6.042
27.669
1.504
1.00
36.31
C

ATOM
1025
CG
GLU
B2018
−5.544
29.080
1.764
1.00
38.14
C

ATOM
1026
CD
GLU
B2018
−6.554
30.137
1.359
1.00
39.70
C

ATOM
1027
OE1
GLU
B2018
−7.673
29.764
0.937
1.00
40.41
O

ATOM
1028
OE2
GLU
B2018
−6.231
31.341
1.464
1.00
40.25
O

ATOM
1029
C
GLU
B2018
−7.782
25.947
1.918
1.00
34.57
C

ATOM
1030
O
GLU
B2018
−8.964
26.076
1.612
1.00
34.08
O

ATOM
1031
N
SER
B2019
−7.094
24.828
1.711
1.00
34.49
N

ATOM
1032
CA
SER
B2019
−7.705
23.650
1.103
1.00
34.60
C

ATOM
1033
CB
SER
B2019
−6.639
22.610
0.793
1.00
34.46
C

ATOM
1034
OG
SER
B2019
−5.712
23.150
−0.125
1.00
35.85
O

ATOM
1035
C
SER
B2019
−8.761
23.039
1.996
1.00
34.54
C

ATOM
1036
O
SER
B2019
−9.827
22.646
1.523
1.00
34.67
O

ATOM
1037
N
ALA
B2020
−8.463
22.965
3.290
1.00
34.29
N

ATOM
1038
CA
ALA
B2020
−9.395
22.402
4.251
1.00
34.25
C

ATOM
1039
CB
ALA
B2020
−8.811
22.471
5.650
1.00
33.91
C

ATOM
1040
C
ALA
B2020
−10.703
23.175
4.180
1.00
34.65
C

ATOM
1041
O
ALA
B2020
−11.778
22.579
4.133
1.00
34.60
O

ATOM
1042
N
VAL
B2021
−10.604
24.502
4.151
1.00
35.08
N

ATOM
1043
CA
VAL
B2021
−11.784
25.359
4.073
1.00
35.39
C

ATOM
1044
CB
VAL
B2021
−11.411
26.855
4.220
1.00
35.27
C

ATOM
1045
CG1
VAL
B2021
−12.608
27.732
3.884
1.00
34.79
C

ATOM
1046
CG2
VAL
B2021
−10.951
27.136
5.637
1.00
35.33
C

ATOM
1047
C
VAL
B2021
−12.526
25.174
2.756
1.00
36.00
C

ATOM
1048
O
VAL
B2021
−13.746
24.985
2.749
1.00
35.93
O

ATOM
1049
N
THR
B2022
−11.795
25.237
1.644
1.00
36.68
N

ATOM
1050
CA
THR
B2022
−12.401
25.072
0.326
1.00
37.80
C

ATOM
1051
CB
THR
B2022
−11.351
25.211
−0.813
1.00
38.05
C

ATOM
1052
OG1
THR
B2022
−10.830
26.549
−0.839
1.00
37.71
O

ATOM
1053
CG2
THR
B2022
−11.988
24.898
−2.166
1.00
37.87
C

ATOM
1054
C
THR
B2022
−13.064
23.701
0.210
1.00
38.58
C

ATOM
1055
O
THR
B2022
−14.204
23.584
−0.234
1.00
38.63
O

ATOM
1056
N
ARG
B2023
−12.348
22.666
0.629
1.00
39.65
N

ATOM
1057
CA
ARG
B2023
−12.864
21.306
0.563
1.00
41.03
C

ATOM
1058
CB
ARG
B2023
−11.828
20.317
1.106
1.00
41.66
C

ATOM
1059
CG
ARG
B2023
−11.891
18.939
0.452
1.00
43.04
C

ATOM
1060
CD
ARG
B2023
−13.312
18.416
0.395
1.00
43.90
C

ATOM
1061
NE
ARG
B2023
−13.406
17.090
−0.202
1.00
44.75
N

ATOM
1062
CZ
ARG
B2023
−14.524
16.371
−0.231
1.00
45.34
C

ATOM
1063
NH1
ARG
B2023
−15.638
16.862
0.302
1.00
45.03
N

ATOM
1064
NH2
ARG
B2023
−14.527
15.157
−0.773
1.00
45.61
N

ATOM
1065
C
ARG
B2023
−14.165
21.138
1.343
1.00
41.52
C

ATOM
1066
O
ARG
B2023
−15.180
20.712
0.787
1.00
41.49
O

ATOM
1067
N
HIS
B2024
−14.120
21.467
2.631
1.00
41.94
N

ATOM
1068
CA
HIS
B2024
−15.274
21.343
3.511
1.00
42.45
C

ATOM
1069
CB
HIS
B2024
−14.931
20.424
4.678
1.00
43.39
C

ATOM
1070
CG
HIS
B2024
−14.516
19.050
4.255
1.00
44.50
C

ATOM
1071
CD2
HIS
B2024
−13.294
18.468
4.191
1.00
44.72
C

ATOM
1072
ND1
HIS
B2024
−15.411
18.115
3.777
1.00
45.05
N

ATOM
1073
CE1
HIS
B2024
−14.758
17.018
3.436
1.00
45.22
C

ATOM
1074
NE2
HIS
B2024
−13.473
17.206
3.677
1.00
45.24
N

ATOM
1075
C
HIS
B2024
−15.713
22.697
4.040
1.00
42.58
C

ATOM
1076
O
HIS
B2024
−14.934
23.412
4.672
1.00
42.87
O

ATOM
1077
N
GLU
B2025
−16.967
23.050
3.781
1.00
42.39
N

ATOM
1078
CA
GLU
B2025
−17.490
24.326
4.242
1.00
41.91
C

ATOM
1079
CB
GLU
B2025
−18.732
24.732
3.437
1.00
43.59
C

ATOM
1080
CG
GLU
B2025
−18.797
26.229
3.153
1.00
45.80
C

ATOM
1081
CD
GLU
B2025
−20.117
26.675
2.544
1.00
47.26
C

ATOM
1082
OE1
GLU
B2025
−20.610
26.003
1.603
1.00
47.52
O

ATOM
1083
OE2
GLU
B2025
−20.653
27.710
3.006
1.00
48.07
O

ATOM
1084
C
GLU
B2025
−17.848
24.211
5.712
1.00
40.39
C

ATOM
1085
O
GLU
B2025
−18.172
25.203
6.356
1.00
40.62
O

ATOM
1086
N
GLY
B2026
−17.789
22.993
6.238
1.00
38.87
N

ATOM
1087
CA
GLY
B2026
−18.105
22.788
7.638
1.00
36.84
C

ATOM
1088
C
GLY
B2026
−16.865
22.836
8.507
1.00
35.50
C

ATOM
1089
O
GLY
B2026
−16.954
22.961
9.732
1.00
35.89
O

ATOM
1090
N
PHE
B2027
−15.706
22.746
7.866
1.00
33.86
N

ATOM
1091
CA
PHE
B2027
−14.416
22.752
8.549
1.00
32.08
C

ATOM
1092
CB
PHE
B2027
−13.293
22.958
7.532
1.00
31.28
C

ATOM
1093
CG
PHE
B2027
−11.926
22.896
8.128
1.00
29.92
C

ATOM
1094
CD1
PHE
B2027
−11.396
21.682
8.555
1.00
28.97
C

ATOM
1095
CD2
PHE
B2027
−11.176
24.054
8.293
1.00
29.17
C

ATOM
1096
CE1
PHE
B2027
−10.143
21.623
9.135
1.00
28.66
C

ATOM
1097
CE2
PHE
B2027
−9.918
24.006
8.875
1.00
28.77
C

ATOM
1098
CZ
PHE
B2027
−9.399
22.790
9.298
1.00
28.68
C

ATOM
1099
C
PHE
B2027
−14.294
23.801
9.651
1.00
31.46
C

ATOM
1100
O
PHE
B2027
−14.059
23.465
10.815
1.00
31.23
O

ATOM
1101
N
ALA
B2028
−14.454
25.067
9.278
1.00
30.51
N

ATOM
1102
CA
ALA
B2028
−14.360
26.169
10.228
1.00
30.25
C

ATOM
1103
CB
ALA
B2028
−14.624
27.487
9.517
1.00
30.53
C

ATOM
1104
C
ALA
B2028
−15.305
26.030
11.421
1.00
30.13
C

ATOM
1105
O
ALA
B2028
−14.926
26.308
12.561
1.00
29.80
O

ATOM
1106
N
LYS
B2029
−16.533
25.600
11.160
1.00
30.02
N

ATOM
1107
CA
LYS
B2029
−17.520
25.448
12.225
1.00
30.10
C

ATOM
1108
CB
LYS
B2029
−18.882
25.053
11.637
1.00
30.49
C

ATOM
1109
CG
LYS
B2029
−19.552
26.148
10.821
1.00
31.20
C

ATOM
1110
CD
LYS
B2029
−20.765
25.618
10.074
0.05
30.87
C

ATOM
1111
CE
LYS
B2029
−21.354
26.675
9.153
0.05
30.89
C

ATOM
1112
NZ
LYS
B2029
−22.504
26.150
8.365
0.05
30.76
N

ATOM
1113
C
LYS
B2029
−17.099
24.408
13.248
1.00
29.50
C

ATOM
1114
O
LYS
B2029
−17.467
24.491
14.420
1.00
29.99
O

ATOM
1115
N
ARG
B2030
−16.326
23.428
12.798
1.00
28.70
N

ATOM
1116
CA
ARG
B2030
−15.877
22.348
13.667
1.00
27.83
C

ATOM
1117
CB
ARG
B2030
−15.616
21.093
12.822
1.00
27.88
C

ATOM
1118
CG
ARG
B2030
−16.867
20.503
12.193
0.05
27.87
C

ATOM
1119
CD
ARG
B2030
−16.543
19.293
11.332
0.05
27.87
C

ATOM
1120
NE
ARG
B2030
−15.748
19.648
10.160
0.05
27.89
N

ATOM
1121
CZ
ARG
B2030
−15.379
18.785
9.218
0.05
27.88
C

ATOM
1122
NH1
ARG
B2030
−15.732
17.510
9.309
0.05
27.89
N

ATOM
1123
NH2
ARG
B2030
−14.658
19.196
8.184
0.05
27.87
N

ATOM
1124
C
ARG
B2030
−14.631
22.698
14.477
1.00
26.83
C

ATOM
1125
O
ARG
B2030
−14.391
22.134
15.541
1.00
26.57
O

ATOM
1126
N
VAL
B2031
−13.854
23.644
13.965
1.00
25.79
N

ATOM
1127
CA
VAL
B2031
−12.610
24.073
14.596
1.00
24.76
C

ATOM
1128
CB
VAL
B2031
−11.565
24.442
13.505
1.00
24.82
C

ATOM
1129
CG1
VAL
B2031
−10.365
25.139
14.121
1.00
24.72
C

ATOM
1130
CG2
VAL
B2031
−11.125
23.184
12.779
1.00
24.93
C

ATOM
1131
C
VAL
B2031
−12.806
25.263
15.523
1.00
23.81
C

ATOM
1132
O
VAL
B2031
−12.166
25.365
16.568
1.00
22.82
O

ATOM
1133
N
LEU
B2032
−13.709
26.149
15.127
1.00
23.54
N

ATOM
1134
CA
LEU
B2032
−13.997
27.361
15.873
1.00
23.22
C

ATOM
1135
CB
LEU
B2032
−14.157
28.528
14.893
1.00
22.85
C

ATOM
1136
CG
LEU
B2032
−12.924
28.789
14.022
1.00
22.24
C

ATOM
1137
CD1
LEU
B2032
−13.210
29.906
13.026
1.00
22.1.1
C

ATOM
1138
CD2
LEU
B2032
−11.747
29.152
14.918
1.00
22.17
C

ATOM
1139
C
LEU
B2032
−15.233
27.256
16.744
1.00
23.32
C

ATOM
1140
O
LEU
B2032
−16.122
26.454
16.482
1.00
23.42
O

ATOM
1141
N
THR
B2033
−15.263
28.060
17.803
1.00
23.69
N

ATOM
1142
CA
THR
B2033
−16.404
28.105
18.713
1.00
23.81
C

ATOM
1143
CB
THR
B2033
−16.002
28.538
20.129
1.00
23.49
C

ATOM
1144
OG1
THR
B2033
−15.442
29.858
20.074
1.00
23.22
O

ATOM
1145
CG2
THR
B2033
−15.004
27.571
20.726
1.00
22.82
C

ATOM
1146
C
THR
B2033
−17.312
29.191
18.162
1.00
24.17
C

ATOM
1147
O
THR
B2033
−16.915
29.930
17.264
1.00
24.05
O

ATOM
1148
N
ALA
B2034
−18.516
29.302
18.709
1.00
24.73
N

ATOM
1149
CA
ALA
B2034
−19.456
30.322
18.246
1.00
25.88
C

ATOM
1150
CB
ALA
B2034
−20.704
30.326
19.127
1.00
25.52
C

ATOM
1151
C
ALA
B2034
−18.793
31.704
18.245
1.00
26.34
C

ATOM
1152
O
ALA
B2034
−18.815
32.409
17.231
1.00
26.66
O

ATOM
1153
N
LEU
B2035
−18.194
32.083
19.374
1.00
27.02
N

ATOM
1154
CA
LEU
B2035
−17.518
33.375
19.477
1.00
27.85
C

ATOM
1155
CB
LEU
B2035
−16.868
33.549
20.852
1.00
28.57
C

ATOM
1156
CG
LEU
B2035
−17.760
33.942
22.028
1.00
29.51
C

ATOM
1157
CD1
LEU
B2035
−16.879
34.241
23.246
1.00
29.47
C

ATOM
1158
CD2
LEU
B2035
−18.596
35.181
21.648
1.00
29.85
C

ATOM
1159
C
LEU
B2035
−16.445
33.516
18.405
1.00
28.07
C

ATOM
1160
O
LEU
B2035
−16.395
34.516
11.687
1.00
28.48
O

ATOM
1161
N
GLU
B2036
−15.578
32.518
18.308
1.00
27.90
N

ATOM
1162
CA
GLU
B2036
−14.518
32.542
17.310
1.00
27.73
C

ATOM
1163
CB
GLU
B2036
−13.666
31.270
17.414
1.00
26.50
C

ATOM
1164
CG
GLU
B2036
−12.568
31.339
18.474
1.00
25.25
C

ATOM
1165
CD
GLU
B2036
−11.969
29.976
18.799
1.00
24.47
C

ATOM
1166
OE1
GLU
B2036
−10.797
29.925
19.226
1.00
23.46
O

ATOM
1167
OE2
GLU
B2036
−12.676
28.957
18.636
1.00
24.23
O

ATOM
1166
C
GLU
B2036
−15.073
32.686
15.895
1.00
28.15
C

ATOM
1169
O
GLU
B2036
−14.507
33.403
15.083
1.00
28.18
O

ATOM
1170
N
MET
B2037
−16.169
31.990
15.604
1.00
29.30
N

ATOM
1171
CA
MET
B2037
−16.800
32.038
14.283
1.00
30.55
C

ATOM
1172
CB
MET
B2037
−17.984
31.069
14.211
1.00
30.95
C

ATOM
1173
CG
MET
B2037
−17.607
29.662
13.809
1.00
31.93
C

ATOM
1174
SD
MET
B2037
−16.851
29.650
12.173
1.00
33.36
S

ATOM
1175
CE
MET
B2037
−18.331
29.638
11.166
1.00
32.65
C

ATOM
1176
C
MET
B2037
−17.286
33.436
13.934
1.00
31.15
C

ATOM
1177
O
MET
B2037
−17.206
33.854
12.785
1.00
30.76
O

ATOM
1178
N
GLU
B2038
−17.789
34.153
14.934
1.00
32.42
N

ATOM
1179
CA
GLU
B2038
−18.278
35.513
14.730
1.00
33.88
C

ATOM
1180
CB
GLU
B2038
−18.841
36.062
16.044
1.00
35.07
C

ATOM
1181
CG
GLU
B2038
−19.432
37.455
15.931
1.00
37.91
C

ATOM
1182
CD
GLU
B2038
−20.528
37.714
16.955
1.00
39.72
C

ATOM
1183
OE1
GLU
B2038
−21.587
37.050
16.864
1.00
40.71
O

ATOM
1184
OE2
GLU
B2038
−20.333
38.576
17.846
1.00
40.42
O

ATOM
1185
C
GLU
B2038
−17.163
36.418
14.198
1.00
34.07
C

ATOM
1186
O
GLU
B2038
−17.406
37.320
13.397
1.00
33.98
O

ATOM
1187
N
ARG
B2039
−15.936
36.181
14.649
1.00
34.44
N

ATOM
1188
CA
ARG
B2039
−14.810
36.972
14.179
1.00
35.18
C

ATOM
1189
CB
ARG
B2039
−13.630
36.856
15.153
1.00
35.30
C

ATOM
1190
CG
ARG
B2039
−12.370
37.601
14.720
1.00
35.26
C

ATOM
1191
CD
ARG
B2039
−12.590
39.099
14.608
0.05
35.23
C

ATOM
1192
NE
ARG
B2039
−11.358
39.788
14.235
0.05
35.24
N

ATOM
1193
CZ
ARG
B2039
−11.260
41.099
14.040
0.05
35.24
C

ATOM
1194
NH1
ARG
B2039
−10.095
41.634
13.703
0.05
35.27
N

ATOM
1195
NH2
ARG
B2039
−12.325
41.875
14.182
0.05
35.27
N

ATOM
1196
C
ARG
B2039
−14.418
36.445
12.797
1.00
35.34
C

ATOM
1197
O
ARG
B2039
−14.167
37.217
11.868
1.00
35.66
O

ATOM
1198
N
PHE
B2040
−14.382
35.123
12.673
1.00
35.29
N

ATOM
1199
CA
PHE
B2040
−14.042
34.473
11.414
1.00
35.77
C

ATOM
1200
CB
PHE
B2040
−14.241
32.961
11.545
1.00
34.55
C

ATOM
1201
CG
PHE
B2040
−13.996
32.201
10.271
1.00
33.98
C

ATOM
1202
CD1
PHE
B2040
−12.716
32.122
9.725
1.00
33.52
C

ATOM
1203
CD2
PHE
B2040
−15.045
31.564
9.614
1.00
33.68
C

ATOM
1204
CE1
PHE
B2040
−12.488
31.420
8.548
1.00
33.41
C

ATOM
1205
CE2
PHE
B2040
−14.828
30.861
8.435
1.00
33.27
C

ATOM
1206
CZ
PHE
B2040
−13.549
30.787
7.899
1.00
33.46
C

ATOM
1207
C
PHE
B2040
−14.916
34.997
10.268
1.00
36.68
C

ATOM
1208
O
PHE
B2040
−14.445
35.199
9.144
1.00
36.38
O

ATOM
1209
N
THR
B2041
−16.191
35.221
10.561
1.00
37.87
N

ATOM
1210
CA
THR
B2041
−17.121
35.692
9.546
1.00
39.25
C

ATOM
1211
CB
THR
B2041
−18.580
35.450
9.981
1.00
39.24
C

ATOM
1212
OG1
THR
B2041
−18.811
34.041
10.115
1.00
39.45
O

ATOM
1213
CG2
THR
B2041
−19.540
36.001
8.943
1.00
40.16
C

ATOM
1214
C
THR
B2041
−16.947
37.159
9.159
1.00
39.72
C

ATOM
1215
O
THR
B2041
−17.496
37.598
8.157
1.00
40.46
O

ATOM
1216
N
SER
B2042
−16.175
37.915
9.930
1.00
40.14
N

ATOM
1217
CA
SER
B2042
−15.970
39.327
9.609
1.00
40.54
C

ATOM
1218
CB
SER
B2042
−16.159
40.184
10.8S8
1.00
40.81
C

ATOM
1219
OG
SER
B2042
−17.449
39.989
11.399
1.00
42.55
O

ATOM
1220
C
SER
B2O42
−14.588
39.596
9.033
1.00
40.43
C

ATOM
1221
O
SER
B2042
−14.039
40.686
9.218
1.00
40.73
O

ATOM
1222
N
LEU
B2043
−14.031
38.615
6.327
1.00
39.91
N

ATOM
1223
CA
LEU
B2043
−12.698
38.764
7.758
1.00
39.34
C

ATOM
1224
CB
LEU
B2043
−11.663
38.115
8.683
1.00
38.78
C

ATOM
1225
CG
LEU
B2043
−11.484
38.654
10.105
1.00
38.39
C

ATOM
1226
CD1
LEU
B2043
−10.642
37.666
10.913
1.00
37.70
C

ATOM
1227
CD2
LEU
B2043
−10.822
40.035
10.075
1.00
37.83
C

ATOM
1228
C
LEU
B2043
−12.555
38.165
6.360
1.00
39.45
C

ATOM
1229
O
LEU
B2043
−11.502
38.317
5.732
1.00
39.47
O

ATOM
1230
N
LYS
B2044
−13.594
37.478
5.884
1.00
38.98
N

ATOM
1231
CA
LYS
B2044
−13.569
36.850
4.556
1.00
38.77
C

ATOM
1232
CB
LYS
B2044
−14.875
37.145
3.807
1.00
39.18
C

ATOM
1233
CG
LYS
B2044
−14.988
36.486
2.442
0.05
38.97
C

ATOM
1234
CD
LYS
B2044
−15.072
34.973
2.556
0.05
38.99
C

ATOM
1235
CE
LYS
B2044
−15.263
34.332
1.191
0.05
38.96
C

ATOM
1236
NZ
LYS
B2044
−15.382
32.851
1.284
0.05
38.96
N

ATOM
1237
C
LYS
B2044
−12.383
37.340
3.720
1.00
38.31
C

ATOM
1238
O
LYS
B2044
−12.253
38.538
3.458
1.00
38.14
O

ATOM
1239
N
GLY
B2045
−11.522
36.412
3.310
1.00
37.92
N

ATOM
1240
CA
GLY
B2045
−10.351
36.767
2.521
1.00
36.95
C

ATOM
1241
C
GLY
B2045
−9.108
36.124
3.108
1.00
36.64
C

ATOM
1242
O
GLY
B2045
−9.207
35.141
3.845
1.00
37.08
O

ATOM
1243
N
ARG
B2046
−7.935
36.665
2.607
1.00
35.68
N

ATOM
1244
CA
ARG
B2046
−6.703
36.084
3.332
1.00
35.35
C

ATOM
1245
CB
ARG
B2046
−5.476
36.804
2.750
1.00
35.15
C

ATOM
1246
CG
ARG
B2046
−4.150
36.148
3.087
0.05
35.14
C

ATOM
1247
CD
ARG
B2046
−4.081
34.743
2.515
0.05
35.11
C

ATOM
1248
NE
ARG
B2046
−2.811
34.090
2.811
0.05
35.11
N

ATOM
1249
CZ
ARG
B2046
−2.504
32.853
2.436
0.05
35.09
C

ATOM
1250
NH1
ARG
B2046
−1.323
32.338
2.748
0.05
35.09
N

ATOM
1251
NH2
ARG
B2046
−3.377
32.130
1.748
0.05
35.07
N

ATOM
1252
C
ARG
B2046
−6.661
36.147
4.859
1.00
34.86
C

ATOM
1253
O
ARG
B2046
−6.273
35.184
5.522
1.00
34.07
O

ATOM
1254
N
ARG
B2047
−7.068
37.289
5.407
1.00
34.76
N

ATOM
1255
CA
ARG
B2047
−7.074
37.503
6.852
1.00
35.00
C

ATOM
1256
CB
ARG
B2047
−7.559
38.918
7.156
1.00
35.75
C

ATOM
1257
CG
ARG
B2047
−6.762
39.984
6.434
1.00
37.57
C

ATOM
1258
CD
ARG
B2047
−7.345
41.342
6.697
1.00
39.01
C

ATOM
1259
NE
ARG
B2047
−8.743
41.398
6.289
1.00
40.76
N

ATOM
1260
CZ
ARG
B2047
−9.663
42.124
6.915
1.00
41.64
C

ATOM
1261
NH1
ARG
B2047
−9.322
42.852
7.974
1.00
41.91
N

ATOM
1262
NH2
ARG
B2047
−10.924
42.110
6.497
1.00
42.15
N

ATOM
1263
C
ARG
B2047
−7.959
36.483
7.566
1.00
34.24
C

ATOM
1264
O
ARG
B2047
−7.681
36;070
8.692
1.00
34.10
O

ATOM
1265
N
GLN
B2048
−9.030
36.085
6.900
1.00
33.32
N

ATOM
1266
CA
GLN
B2048
−9.944
35.112
7.460
1.00
32.27
C

ATOM
1267
CB
GLN
B2048
−11.138
34.961
6.531
1.00
32.92
C

ATOM
1268
CG
GLN
B2048
−12.281
34.193
7.115
1.00
33.21
C

ATOM
1269
CD
GLN
B2048
−13.323
33.871
6.077
1.00
33.65
C

ATOM
1270
OE1
GLN
B2048
−13.016
33.274
5.044
1.00
34.07
O

ATOM
1271
NE2
GLN
B2048
−14.567
34.258
6.343
1.00
33.98
N

ATOM
1272
C
GLN
B2048
−9.224
33.772
7.620
1.00
31.20
C

ATOM
1273
O
GLN
B2048
−9.402
33.075
8.615
1.00
30.73
O

ATOM
1274
N
ILE
B2049
−8.405
33.419
6.634
1.00
29.96
N

ATOM
1275
CA
ILE
B2049
−7.661
32.170
6.682
1.00
28.94
C

ATOM
1276
CB
ILE
B2049
−7.007
31.856
5.313
1.00
28.51
C

ATOM
1277
CG2
ILE
B2049
−6.069
30.658
5.438
1.00
27.59
C

ATOM
1278
CG1
ILE
B2049
−8.096
31.573
4.267
1.00
28.47
C

ATOM
1279
CD1
ILE
B2049
−8.950
30.333
4.553
1.00
27.80
C

ATOM
1280
C
ILE
B2049
−6.574
32.198
7.759
1.00
28.73
C

ATOM
1281
O
ILE
B2049
−6.353
31.206
8.463
1.00
28.34
O

ATOM
1282
N
GLU
B2050
−5.896
33.336
7.879
1.00
28.38
N

ATOM
1283
CA
GLU
B2050
−4.833
33.494
8.859
1.00
28.07
C

ATOM
1284
CB
GLU
B2050
−4.151
34.848
8.665
1.00
29.65
C

ATOM
1285
CG
GLU
B2050
−3.799
35.103
7.200
1.00
32.92
C

ATOM
1286
CD
GLU
B2050
−2.865
36.279
6.995
1.00
34.62
C

ATOM
1287
OE1
GLU
B2050
−3.232
37.416
7.392
1.00
35.24
O

ATOM
1288
OE2
GLU
B2050
−1.762
36.055
6.430
1.00
35.19
O

ATOM
1289
C
GLU
B2050
−5.416
33.374
10.260
1.00
26.78
C

ATOM
1290
O
GLU
B2050
−4.812
32.768
11.150
1.00
26.09
O

ATOM
1291
N
TYR
B2051
−6.600
33.944
10.453
1.00
25.41
N

ATOM
1292
CA
TYR
B2051
−7.251
33.868
11.749
1.00
24.34
C

ATOM
1293
CB
TYR
B2051
−8.535
34.703
11.741
1.00
23.37
C

ATOM
1294
CG
TYR
B2051
−9.316
34.618
13.024
1.00
22.77
C

ATOM
1295
CD1
TYR
B2051
−10.347
33.695
13.169
1.00
22.86
C

ATOM
1296
CE1
TYR
B2051
−11.026
33.559
14.369
1.00
23.29
C

ATOM
1297
CD2
TYR
B2051
−8.984
35.413
14.116
1.00
22.81
C

ATOM
1298
CE2
TYR
B2051
−9.657
35.284
15.332
1.00
23.14
C

ATOM
1299
CZ
TYR
B2051
−10.677
34.350
15.450
1.00
23.43
C

ATOM
1300
OH
TYR
B2051
−11.332
34.186
16.649
1.00
23.03
O

ATOM
1301
C
TYR
B2051
−7.550
32.400
12.086
1.00
24.05
C

ATOM
1302
O
TYR
B2051
−7.176
31.910
13.154
1.00
24.52
O

ATOM
1303
N
LEU
B2052
−8.211
31.700
11.170
1.00
23.25
N

ATOM
1304
CA
LEU
B2052
−8.541
30.291
11.364
1.00
22.91
C

ATOM
1305
CB
LEU
B2052
−9.274
29.748
10.133
1.00
22.55
C

ATOM
1306
CG
LEU
B2052
−9.598
28.247
10.086
1.00
22.85
C

ATOM
1307
CD1
LEU
B2052
−10.345
27.814
11.343
1.00
21.95
C

ATOM
1308
CD2
LEU
B2052
−10.436
27.957
8.835
1.00
22.89
C

ATOM
1309
C
LEU
B2052
−7.284
29.457
11.622
1.00
22.68
C

ATOM
1310
O
LEU
B2052
−7.232
28.681
12.571
1.00
22.94
O

ATOM
1311
N
ALA
B2053
−6.285
29.612
10.761
1.00
22.31
N

ATOM
1312
CA
ALA
B2053
−5.024
28.897
10.884
1.00
21.99
C

ATOM
1313
CB
ALA
B2053
−4.072
29.332
9.774
1.00
21.32
C

ATOM
1314
C
ALA
B2053
−4.397
29.180
12.244
1.00
22.13
C

ATOM
1315
O
ALA
B2053
−3.805
28.295
12.868
1.00
21.87
O

ATOM
1316
N
GLY
B2054
−4.532
30.427
12.688
1.00
21.95
N

ATOM
1317
CA
GLY
B2054
−3.981
30.829
13.963
1.00
21.46
C

ATOM
1318
C
GLY
B2054
−4.654
30.111
15.107
1.00
21.35
C

ATOM
1319
O
GLY
B2054
−3.986
29.678
16.049
1.00
21.19
O

ATOM
1320
N
ARG
B2055
−5.914
29.976
15.040
1.00
20.89
N

ATOM
1321
CA
ARG
B2055
−6.681
29.290
16.114
1.00
20.89
C

ATOM
1322
CB
ARG
B2055
−8.191
29.543
16.034
1.00
20.27
C

ATOM
1323
CG
ARG
B2055
−8.685
30.688
16.934
1.00
19.89
C

ATOM
1324
CD
ARG
B2055
−7.926
31.986
16.664
1.00
20.08
C

ATOM
1325
NE
ARG
B2055
−8.265
33.046
17.609
1.00
19.79
N

ATOM
1326
CZ
ARG
B2055
−7.634
34.216
17.668
1.00
20.91
C

ATOM
1327
NH1
ARG
B2055
−6.626
34.473
16.832
1.00
20.64
N

ATOM
1328
NH2
ARG
B2055
−8.009
35.135
18.555
1.00
20.13
N

ATOM
1329
C
ARG
B2055
−6.383
27.796
16.086
1.00
20.73
C

ATOM
1330
O
ARG
B2055
−6.239
27.169
17.136
1.00
20.29
O

ATOM
1331
N
TRP
B2056
−6.273
27.235
14.884
1.00
20.69
N

ATOM
1332
CA
TRP
B2056
−5.976
25.817
14.742
1.00
20.72
C

ATOM
1333
CB
TRP
B2056
−5.992
25.408
13.262
1.00
21.90
C

ATOM
1334
CG
TRP
B2056
−5.402
24.051
13.020
1.00
23.77
C

ATOM
1335
CD2
TRP
B2056
−6.116
22.814
12.903
1.00
24.30
C

ATOM
1336
CE2
TRP
B2056
−5.151
21.780
12.814
1.00
24.91
C

ATOM
1337
CE3
TRP
B2056
−7.473
22.478
12.869
1.00
24.91
C

ATOM
1338
CD1
TRP
B2056
−4.065
23.727
12.983
1.00
23.97
C

ATOM
1339
NE1
TRP
B2056
−3.912
22.365
12.864
1.00
24.86
N

ATOM
1340
CZ2
TRP
B2056
−5.505
20.429
12.697
1.00
25.50
C

ATOM
1341
CZ3
TRP
B2056
−7.829
21.131
12.751
1.00
26.26
C

ATOM
1342
CH2
TRP
B2056
−6.843
20.122
12.667
1.00
26.22
C

ATOM
1343
C
TRP
B2056
−4.603
25.547
15.348
1.00
20.41
C

ATOM
1344
O
TRP
B2056
−4.409
24.582
16.093
1.00
20.04
O

ATOM
1345
N
SER
B2057
−3.654
26.415
15.025
1.00
19.64
N

ATOM
1346
CA
SER
B2057
−2.298
26.282
15.533
1.00
19.83
C

ATOM
1347
CB
SER
B2057
−1.395
27.339
14.898
1.00
20.26
C

ATOM
1348
OG
SER
B2057
−0.057
27.136
15.303
1.00
22.97
O

ATOM
1349
C
SER
B2057
−2.239
26.402
17.062
1.00
18.86
C

ATOM
1350
O
SER
B2057
−1.548
25.636
17.725
1.00
18.27
O

ATOM
1351
N
ALA
B2058
−2.968
27.367
17.613
1.00
18.16
N

ATOM
1352
CA
ALA
B2058
−2.996
27.566
19.058
1.00
17.01
C

ATOM
1353
CB
ALA
B2058
−3.767
28.826
19.388
1.00
16.89
C

ATOM
1354
C
ALA
B2058
−3.623
26.365
19.781
1.00
16.76
C

ATOM
1355
O
ALA
B2058
−3.087
25.890
20.783
1.00
15.81
O

ATOM
1356
N
LYS
B2059
−4.755
25.884
19.272
1.00
16.40
N

ATOM
1357
CA
LYS
B2059
−5.446
24.746
19.883
1.00
17.29
C

ATOM
1358
CB
LYS
B2059
−6.815
24.547
19.217
1.00
16.13
C

ATOM
1359
CG
LYS
B2059
−7.751
25.730
19.498
1.00
15.32
C

ATOM
1360
CD
LYS
B2059
−9.168
25.536
18.996
1.00
14.90
C

ATOM
1361
CE
LYS
B2059
−10.011
26.783
19.319
1.00
13.82
C

ATOM
1362
NZ
LYS
B2059
−11.432
26.637
18.937
1.00
11.65
N

ATOM
1363
C
LYS
B2059
−4.620
23.464
19.826
1.00
17.91
C

ATOM
1364
O
LYS
B2059
−4.640
22.656
20.748
1.00
16.96
O

ATOM
1365
N
GLU
B2060
−3.879
23.293
18.738
1.00
19.43
N

ATOM
1366
CA
GLU
B2060
−3.043
22.123
18.585
1.00
20.86
C

ATOM
1367
CB
GLU
B2060
−2.516
22.046
17.146
1.00
22.77
C

ATOM
1368
CG
GLU
B2060
−1.964
20.691
16.759
1.00
26.37
C

ATOM
1369
CD
GLU
B2060
−2.982
19.574
16.959
1.00
29.21
C

ATOM
1370
OE1
GLU
B2060
−4.047
19.602
16.287
1.00
29.92
O

ATOM
1371
OE2
GLU
B2060
−2.720
18.670
17.795
1.00
30.31
O

ATOM
1372
C
GLU
B2060
−1.889
22.256
19.593
1.00
20.86
C

ATOM
1373
O
GLU
B2060
−1.556
21.302
20.307
1.00
20.96
O

ATOM
1374
N
ALA
B2061
−1.299
23.447
19.661
1.00
20.25
N

ATOM
1375
CA
ALA
B2061
−0.191
23,697
20.580
1.00
20.38
C

ATOM
1376
CB
ALA
B2061
0.348
25.139
20.411
1.00
19.50
C

ATOM
1377
C
ALA
B2061
−0.655
23.464
22.015
1.00
20.28
C

ATOM
1378
O
ALA
B2061
0.103
22.952
22.841
1.00
20.05
O

ATOM
1379
N
PHE
B2062
−1.896
23.832
22.313
1.00
20.49
N

ATOM
1380
CA
PHE
B2062
−2.419
23.620
23.659
1.00
21.41
C

ATOM
1381
CB
PHE
B2062
−3.738
24.382
23.880
1.00
21.26
C

ATOM
1382
CG
PHE
B2062
−4.350
24.142
25.242
1.00
21.63
C

ATOM
1383
CD1
PHE
B2062
−5.134
23.015
25.481
1.00
21.14
C

ATOM
1384
CD2
PHE
B2062
−4.092
25.009
26.297
1.00
21.77
C

ATOM
1385
CE1
PHE
B2062
−5.646
22.756
26.745
1.00
21.47
C

ATOM
1386
CE2
PHE
B2062
−4.603
24.757
27.576
1.00
22.09
C

ATOM
1387
CZ
PHE
B2062
−5.382
23.627
27.799
1.00
21.52
C

ATOM
1388
C
PHE
B2062
−2.630
22.133
23.938
1.00
22.03
C

ATOM
1389
O
PHE
B2062
−2.303
21.655
25.022
1.00
22.28
O

ATOM
1390
N
SER
B2063
−3.183
21.406
22.970
1.00
22.94
N

ATOM
1391
CA
SER
B2063
−3.403
19.972
23.135
1.00
24.34
C

ATOM
1392
CB
SER
B2063
−4.120
19.379
21.921
1.00
24.96
C

ATOM
1393
OG
SER
B2063
−5.510
19.618
21.995
1.00
26.96
O

ATOM
1394
C
SER
B2063
−2.089
19.231
23.338
1.00
24.82
C

ATOM
1395
O
SER
B2063
−2.053
18.192
23.989
1.00
24.78
O

ATOM
1396
N
LYS
B2064
−1.010
19.754
22.778
1.00
24.97
N

ATOM
1397
CA
LYS
B2064
0.266
19.091
22.952
1.00
26.19
C

ATOM
1398
CB
LYS
B2064
1.201
19.454
21.802
1.00
25.92
C

ATOM
1399
CG
LYS
B2064
0.723
18.846
20.496
1.00
26.10
C

ATOM
1400
CD
LYS
B2064
1.437
19.406
19.293
1.00
26.40
C

ATOM
1401
CE
LYS
B2064
2.890
19.016
19.272
1.00
25.79
C

ATOM
1402
NZ
LYS
B2064
3.444
19.339
17.935
1.00
26.57
N

ATOM
1403
C
LYS
B2064
0.860
19.447
24.312
1.00
27.18
C

ATOM
1404
O
LYS
B2064
1.443
18.593
24.978
1.00
27.11
O

ATOM
1405
N
ALA
B2065
0.680
20.696
24.734
1.00
28.10
N

ATOM
1406
CA
ALA
B2065
1.175
21.142
26.030
1.00
29.62
C

ATOM
1407
CB
ALA
B2065
0.851
22.617
26.241
1.00
29.09
C

ATOM
1408
C
ALA
B2065
0.520
20.309
27.128
1.00
30.86
C

ATOM
1409
O
ALA
B2065
1.121
20.062
28.170
1.00
30.13
O

ATOM
1410
N
MET
B2066
−0.721
19.890
26.892
1.00
32.95
N

ATOM
1411
CA
MET
B2066
−1.449
19.079
27.866
1.00
35.41
C

ATOM
1412
CB
MET
B2066
−2.957
19.167
27.626
1.00
35.78
C

ATOM
1413
CG
MET
B2066
−3.588
20.479
28.047
1.00
36.88
C

ATOM
1414
SD
MET
B2066
−3.734
20.673
29.828
1.00
38.18
S

ATOM
1415
CE
MET
B2066
−5.497
20.288
30.048
1.00
38.92
C

ATOM
1416
C
MET
B2066
−1.010
17.621
27.783
1.00
36.81
C

ATOM
1417
O
MET
B2066
−1.414
16.797
28.595
1.00
36.82
O

ATOM
1418
N
GLY
B2067
−0.178
17.311
26.798
1.00
38.52
N

ATOM
1419
CA
GLY
B2067
−0.292
15.950
26.644
1.00
41.07
C

ATOM
1420
C
GLY
B2067
−0.794
14.998
26.187
1.00
42.84
C

ATOM
1421
O
GLY
B2067
−1.321
14.214
26.979
1.00
43.50
O

ATOM
1422
N
THR
B2068
−1.140
15.077
24.908
1.00
44.30
N

ATOM
1423
CA
THR
B2068
−2.152
14.206
24.322
1.00
45.93
C

ATOM
1424
CB
THP
B2068
−3.410
14.994
23.903
1.00
45.92
C

ATOM
1425
OG1
THR
B2068
−3.075
15.921
22.861
1.00
46.12
O

ATOM
1426
CG2
THR
B2068
−3.972
15.758
25.093
1.00
46.09
C

ATOM
1427
C
THP
B2068
−1.501
13.593
23.088
1.00
47.07
C

ATOM
1428
O
THR
B2068
−2.151
12.918
22.287
1.00
47.09
O

ATOM
1429
N
GLY
B2069
−0.202
13.862
22.957
1.00
48.53
N

ATOM
1430
CA
GLY
B2069
0.599
13.356
21.853
1.00
49.83
C

ATOM
1431
C
GLY
B2069
−0.085
13.307
20.503
1.00
50.67
C

ATOM
1432
O
GLY
B2069
−0.047
14.274
19.741
1.00
51.10
O

ATOM
1433
N
ILE
B2070
−0.699
12.166
20.208
1.00
51.17
N

ATOM
1434
CA
ILE
B2070
−1.405
11.948
18.952
1.00
51.53
C

ATOM
1435
CB
ILE
B2070
−1.574
10.427
18.668
1.00
51.94
C

ATOM
1436
CG2
ILE
B2070
−0.221
9.804
18.341
1.00
51.87
C

ATOM
1437
CG1
ILE
B2070
−2.217
9.737
19.882
1.00
52.15
C

ATOM
1438
CD1
ILE
B2070
−2.470
8.249
19.712
1.00
52.43
C

ATOM
1439
C
ILE
B2070
−2.792
12.590
18.979
1.00
51.42
C

ATOM
1440
O
ILE
B2070
−3.074
13.534
18.232
1.00
51.57
O

ATOM
1441
N
SER
B2071
−3.653
12.068
19.847
1.00
51.02
N

ATOM
1442
CA
SER
B2071
−5.013
12.566
19.967
1.00
50.61
C

ATOM
1443
CB
SER
B2071
−5.803
11.680
20.938
1.00
50.61
C

ATOM
1444
OG
SER
B2071
−5.007
11.299
22.044
1.00
50.73
O

ATOM
1445
C
SER
B2071
−5.064
14.030
20.404
1.00
50.07
C

ATOM
1446
O
SER
B2071
−4.042
14.625
20.771
1.00
49.91
O

ATOM
1447
N
LYS
B2072
−6.258
14.612
20.340
1.00
49.03
N

ATOM
1448
CA
LYS
B2072
−6.440
16.004
20.728
1.00
47.71
C

ATOM
1449
CB
LYS
B2072
−6.637
16.898
19.495
1.00
48.58
C

ATOM
1450
CG
LYS
B2072
−5.733
16.397
18.312
1.00
49.59
C

ATOM
1451
CD
LYS
B2072
−6.215
17.358
17.087
1.00
50.30
C

ATOM
1452
CE
LYS
B2072
−5.500
16.909
15.820
1.00
50.97
C

ATOM
1453
NZ
LYS
B2072
−6.051
17.588
14.610
1.00
51.33
N

ATOM
1454
C
LYS
B2072
−7.670
16.146
21.610
1.00
46.22
C

ATOM
1455
O
LYS
B2072
−8.484
15.229
21.742
1.00
46.03
O

ATOM
1456
N
LEU
B2073
−7.787
17.322
22.208
1.00
44.70
N

ATOM
1457
CA
LEU
B2073
−8.915
17.658
23.048
1.00
42.68
C

ATOM
1458
CB
LEU
B2073
−8.540
18.812
23.975
1.00
42.47
C

ATOM
1459
CG
LEU
B2073
−7.416
18.504
24.959
1.00
42.08
C

ATOM
1460
CD1
LEU
B2073
−6.916
19.781
25.594
1.00
42.04
C

ATOM
1461
CD2
LEU
B2073
−7.925
17.543
26.010
1.00
42.14
C

ATOM
1462
C
LEU
B2073
−9.999
18.116
22.083
1.00
41.35
C

ATOM
1463
O
LEU
B2073
−9.750
18.273
20.881
1.00
41.21
O

ATOM
1464
N
GLY
B2074
−11.203
18.312
22.595
1.00
39.49
N

ATOM
1465
CA
GLY
B2074
−12.252
18.791
21.727
1.00
37.51
C

ATOM
1466
C
GLY
B2074
−11.852
20.211
21.364
1.00
35.85
C

ATOM
1467
O
GLY
B2074
−11.493
20.998
22.240
1.00
35.43
O

ATOM
1468
N
PHE
B2075
−11.878
20.548
20.082
1.00
33.89
N

ATOM
1469
CA
PHE
B2075
−11.524
21.900
19.704
1.00
32.41
C

ATOM
1470
CB
PHE
B2075
−11.287
21.990
18.194
1.00
32.43
C

ATOM
1471
CG
PHE
B2075
−9.846
21.778
17.802
1.00
32.87
C

ATOM
1472
CD1
PHE
B2075
−8.952
21.151
18.682
1.00
33.28
C

ATOM
1473
CD2
PHE
B2075
−9.379
22.191
16.557
1.00
33.06
C

ATOM
1474
CE1
PHE
B2075
−7.616
20.941
18.326
1.00
33.27
C

ATOM
1475
CE2
PHE
B2075
−8.047
21.987
16.187
1.00
33.20
C

ATOM
1476
CZ
PHE
B2075
−7.163
21.360
17.071
1.00
33.45
C

ATOM
1477
C
PHE
B2075
−12.597
22.877
20.163
1.00
31.04
C

ATOM
1478
O
PHE
B2075
−12.340
24.072
20.277
1.00
30.78
O

ATOM
1479
N
GLN
B2076
−13.787
22.357
20.462 1.00
29.52
N

ATOM
1480
CA
GLN
B2076
−14.897
23.185
20.929 1.00
28.06
C

ATOM
1481
CB
GLN
B2076
−16.226
22.493
20.630 1.00
27.83
C

ATOM
1482
CG
GLN
B2076
−16.489
22.365
19.144 1.00
27.93
C

ATOM
1483
CD
GLN
B2076
−16.666
23.716
18.479 1.00
28.25
C

ATOM
1484
OE1
GLN
B2076
−16.170
23.950
17.376
1.00
28.52
O

ATOM
1485
NE2
GLN
B2076
−17.387
24.613
19.145
1.00
27.92
N

ATOM
1486
C
GLN
B2076
−14.765
23.476
22.423
1.00
27.11
C

ATOM
1487
O
GLN
B2076
−15.536
24.241
23.000
1.00
26.54
O

ATOM
1488
N
ASP
B2077
−13.768
22.860
23.037
1.00
26.23
N

ATOM
1489
CA
ASP
B2077
−13.505
23.059
24.447
1.00
26.09
C

ATOM
1490
CB
ASP
B2077
−13.173
21.721
25.108
1.00
27.19
C

ATOM
1491
CG
ASP
B2077
−14.401
20.856
25.292
1.00
28.36
C

ATOM
1492
OD1
ASP
B2077
−15.304
21.276
26.043
1.00
29.34
O

ATOM
1493
OD2
ASP
B2077
−14.469
19.767
24.686
1.00
29.83
O

ATOM
1494
C
ASP
B2077
−12.354
24.041
24.614
1.00
24.96
C

ATOM
1495
O
ASP
B2077
−11.917
24.328
25.730
1.00
24.58
O

ATOM
1496
N
LEU
B2078
−11.870
24.553
23.490
1.00
23.44
N

ATOM
1497
CA
LEU
B2078
−10.783
25.507
23.502
1.00
22.63
C

ATOM
1498
CB
LEU
B2078
−9.534
24.900
22.868
1.00
22.62
C

ATOM
1499
CG
LEU
B2078
−8.989
23.599
23.468
1.00
22.75
C

ATOM
1500
CD1
LEU
B2078
−7.933
23.010
22.543
1.00
22.77
C

ATOM
1501
CD2
LEU
B2078
−8.401
23.870
24.841
1.00
22.96
C

ATOM
1502
C
LEU
B2078
−11.200
26.741
22.726
1.00
22.37
C

ATOM
1503
O
LEU
B2078
−11.709
26.642
21.611
1.00
21.73
O

ATOM
1504
N
GLU
B2079
−11.001
27.908
23.324
1.00
21.99
N

ATOM
1505
CA
GLU
B2079
−11.342
29.145
22.648
1.00
21.60
C

ATOM
1506
CB
GLU
B2079
−12.624
29.740
23.214
1.00
21.69
C

ATOM
1507
CG
GLU
B2079
−13.132
30.922
22.421
1.00
22.30
C

ATOM
1508
CD
GLU
B2079
−14.459
31.412
22.937
1.00
23.08
C

ATOM
1509
OE1
GLU
B2079
−14.499
31.893
24.089
1.00
24.19
O

ATOM
1510
OE2
GLU
B2079
−15.462
31.311
22.201
1.00
22.86
O

ATOM
1511
C
GLU
B2079
−10.216
30.144
22.792
1.00
21.14
C

ATOM
1512
O
GLU
B2079
−9.606
30.265
23.862
1.00
21.43
O

ATOM
1513
N
VAL

B2080
−9.940
30.852
21.705
1.00
20.42
N

ATOM
1514
CA
VAL
B2080
−8.892
31.850
21.691
1.00
20.15
C

ATOM
1515
CB
VAL
B2080
−7.728
31.418
20.780
1.00
19.96
C

ATOM
1516
CG1
VAL
B2080
−6.662
32.517
20.735
1.00
19.66
C

ATOM
1517
CG2
VAL
B2080
−7.127
30.123
21.297
1.00
19.86
C

ATOM
1518
C
VAL
B2080
−9.436
33.187
21.211
1.00
20.63
C

ATOM
1519
O
VAL
B2080
−9.899
33.820
20.075
1.00
20.55
O

ATOM
1520
N
LEU
B2081
−9.379
34.178
22.089
1.00
20.91
N

ATOM
1521
CA
LEU
B2081
−9,852
35.515
21.767
1.00
21.71
C

ATOM
1522
CB
LEU
B2081
−10.913
35.953
22.779
1.00
21.41
C

ATOM
1523
CG
LEU
B2081
−12.150
35.049
22.846
1.00
21.70
C

ATOM
1524
COl
LEU
B2081
−13.145
35.618
23.864
1.00
20.86
C

ATOM
1525
CG2
LEU
B2081
−12.788
34.947
21.451
1.00
20.91
C

ATOM
1526
C
LEU
B2081
−8.690
36.488
21.802
1.00
21.95
C

ATOM
1527
O
LEU
B2081
−7.592
36.135
22.255
1.00
22.11
O

ATOM
1528
N
ASN
B2082
−8.927
37.700
21.302
1.00
22.09
N

ATOM
1529
CA
ASN
B2082
−7.912
38.754
21.334
1.00
22.53
C

ATOM
1530
CB
ASN
B2082
−7.809
39.483
19.992
1.00
23.53
C

ATOM
1531
CG
ASN
B2082
−7.347
38.588
18.882
1.00
24.84
C

ATOM
1532
001
ASN
B2082
−6.350
37.880
19.016
1.00
25.69
O

ATOM
1533
ND2
ASN
B2082
−8.066
38.613
17.766
1.00
26.27
N

ATOM
1534
C
ASM B2082
−8.345
39.754
22.402
1.00
22.18
C

ATOM
1535
O
ASN
B2082
−9.528
40.069
22.514
1.00
21.35
O

ATOM
1536
N
ASN
B2083
−7.391
40.244
23.186
1.00
22.35
N

ATOM
1537
CA
ASN
B2083
−7.699
41.215
24.227
1.00
22.53
C

ATOM
1538
CB
ASN
B2083
−6.711
41.092
25.391
1.00
21.65
C

ATOM
1539
CG
ASN
B2083
−5.267
41.394
24.995
1.00
21.91
C

ATOM
1540
ODi
ASN
B2083
−4.338
41.115
25.762
1.00
22.04
O

ATOM
1541
ND2
ASN
B2083
−5.068
41.963
23.808
1.00
20.96
N

ATOM
1542
C
ASN
B2083
−7.679
42.632
23.663
1.00
23.31
C

ATOM
1543
O
ASN
B2083
−7.344
42.834
22.493
1.00
23.42
O

ATOM
1544
N
GLU
B2084
−8.037
43.605
24.498
1.00
23.94
N

ATOM
1545
CA
GLU
B2084
−8.062
45.012
24.098
1.00
24.84
C

ATOM
1546
CB
GLU
B2084
−8.089
45.924
25.336
1.0026.09
C

ATOM
1547
CG
GLU
B2084
−9.171
45.622
26.355
1.00
28.21
C

ATOM
1548
CD
OLU B2084
−8.992
44.259
27.014
1.00
30.57
C

ATOM
1549
OE1
GLU
B2084
−7.892
44.001
27.565
1.00
31.38
O

ATOM
1550
OE2
GLU
B2084
−9.952
43.448
26.984
1.00
31.36
O

ATOM
1551
C
GLU
B2084
−6.871
45.421
23.223
1.00
24.40
C

ATOM
1552
O
GLU
B2084
−7.033
46.197
22.292
1.00
24.89
O

ATOM
1553
N
ARG
B2085
−5.683
44.905
23.530
1.00
24.24
N

ATOM
1554
CA
ARG
B2085
−4.464
45.245
22.782
1.00
24.07
C

ATOM
1555
CB
ARG
B2085
−3.237
45.139
23.688
1.00
24.81
C

ATOM
1556
CG
ARG
B2085
−3.375
45.824
25.022
1.00
26.63
C

ATOM
1557
CD
ARG
B2085
−2.090
45.727
25.844
1.00
27.63
C

ATOM
1558
NE
ARG
B2085
−2.124
46.668
26.962
1.00
28.81
N

ATOM
1559
CZ
ARG
B2095
−2.915
46.532
28.016
1.00
29.08
C

ATOM
1560
NH1
ARG
B2085
−3.725
45.489
28.090
1.00
30.38
N

ATOM
1561
NH2
ARG
B2085
−2.915
47.441
28.984
1.00
29.49
N

ATOM
1562
C
ARG
B2085
−4.201
44.386
21.548
1.00
23.45
C

ATOM
1563
O
ARG
B2085
−3.231
44.616
20.839
1.00
23.48
O

ATOM
1564
N
GLY
B2086
−5.043
43.388
21.304
1.00
22.86
N

ATOM
1565
CA
GLY
B2086
−4.845
42.531
20.148
1.00
22.18
C

ATOM
1566
C
GLY
B2086
−4.106
41.231
20.442
1.00
22.02
C

ATOM
1567
O
GLY
B2086
−3.935
40.391
19.557
1.00
22.97
O

ATOM
1568
N
ALA
B2087
−3.658
41.053
21.677
1.00
20.91
N

ATOM
1569
CA
ALA
B2087
−2.948
39.836
22.038
1.00
19.91
C

ATOM
1570
CB
ALA
B2087
−2.196
40.028
23.362
1.00
19.31
C

ATOM
1571
C
ALA
B2087
−3.940
38.675
22.161
1.00
19.35
C

ATOM
1572
O
ALA
B2087
−5.013
38.816
22.757
1.00
18.31
O

ATOM
1573
N
PRO
B2088
−3.598
37.520
21.566
1.00
19.16
N

ATOM
1574
CB
PRO
B2088
−2.449
37.311
20.656
1.00
19.16
C

ATOM
1575
CA
PRO
B2088
−4.450
36.331
21.611
1.00
18.85
C

ATOM
1576
CB
PRO
B2088
−3.968
35.529
20.408
1.00
19.28
C

ATOM
1577
CG
PRO
B2088
−2.478
35.817
20.403
1.00
18.72
C

ATOM
1578
C
PRO
B2088
−4.229
35.597
22.934
1.00
18.76
C

ATOM
1579
O
PRO
B2088
−3.098
35.484
23.404
1.00
18.99
O

ATOM
1580
N
TYR
B2089
−5.310
35.108
23.533
1.00
18.27
N

ATOM
1581
CA
TYR
B2089
−5.230
34.394
24.804
1.00
17.56
C

ATOM
1582
CB
TYR
B2089
−5.394
35.379
25.960
1.00
15.80
C

ATOM
1583
CG
TYR
B2089
−6.792
35.933
26.103
1.00
14.62
C

ATOM
1584
CD1
TYR
B2089
−7.684
35.402
27.036
1.00
14.04
C

ATOM
1585
CE1
TYR
B2089
−8.983
35.916
27.160
1.00
13.45
C

ATOM
1586
CD2
TYR
B2089
−7.231
36.991
25.294
1.00
13.76
C

ATOM
1587
CE2
TYR
B2089
−8.507
37.499
25.405
1.00
12.48
C

ATOM
1588
CZ
TYR
B2089
−9.381
36.964
26.336
1.00
13.07
C

ATOM
1589
OH
TYR
B2089
−10.649
37.475
26.433
1.00
12.87
O

ATOM
1590
C
TYR
B2089
−6.333
33.349
24.865
1.00
18.14
C

ATOM
1591
O
TYR
B2089
−7.302
33.433
24.118
1.00
18.32
O

ATOM
1592
N
PHE
B2090
−6.196
32.360
25.741
1.00
18.75
N

ATOM
1593
CA
PHE
B2090
−7.242
31.350
25.853
1.00
19.41
C

ATOM
1594
CB
PHE
B2090
−6.686
30.012
26.353
1.00
18.52
C

ATOM
1595
CG
PHE
B2090
−6.044
29.187
25.282
1.00
18.19
C

ATOM
1596
CD1
PHE
B2090
−4.716
29.402
24.912
1.00
17.08
C

ATOM
1597
CD2
PHE
B2090
6.769
28.182
24.638
1.00
17.63
C

ATOM
1598
CE1
PHE
B2090
−4.119
28.626
23.920
1.00
16.47
C

ATOM
1599
CE2
PHE
B2090
−6.177
27.400
23.640
1.00
16.79
C

ATOM
1600
CZ
PHE
B2090
−4.847
27.625
23.284
1.00
16.73
C

ATOM
1601
C
PHE
B2090
−8.334
31.806
26.802
1.00
20.35
C

ATOM
1602
O
PHE
B2090
−8.092
31.963
27.997
1.00
20.62
O

ATOM
1603
N
SER
B2091
−9.535
32.010
26.271
1.00
21.43
N

ATOM
1604
CA
SER
B2091
−10.664
32.430
27.096
1.00
22.72
C

ATOM
1605
CB
SER
B2091
−11.635
33.293
26.278
1.00
22.59
C

ATOM
1606
OG
SER
B2091
−12.173
32.566
25.187
1.00
24.06
O

ATOM
1607
C
SER
B2091
−11.385
31.194
27.651
1.00
23.50
C

ATOM
1608
O
SER
B2091
−12.133
31.289
28.623
1.00
23.39
O

ATOM
1609
N
GLN
B2092
−11.154
30.041
27.024
1.00
24.05
N

ATOM
1610
CA
GLN
B2092
−11.757
28.784
27.458
1.00
25.18
C

ATOM
1611
CB
GLN
B2092
−12.970
28.420
26.591
1.00
26.15
C

ATOM
1612
CG
GLN
B2092
−14.194
29.321
26.733
1.00
28.02
C

ATOM
1613
CD
GLN
B2092
−14.848
29.241
28.105
1.00
29.69
C

ATOM
1614
OE1
GLN
B2092
−14.974
28.159
28.687
1.00
30.83
O

ATOM
1615
NE2
GLN
B2092
−15.283
30.389
28.622
1.00
30.35
N

ATOM
1616
C
GLN
92092
−10.725
27.661
27.354
1.00
25.31
C

ATOM
1617
O
GLN
92092
−10.029
27.541
26.343
1.00
25.18
O

ATOM
1618
N
ALA
B2093
−10.631
26.838
28.395
1.00
25.61
N

ATOM
1619
CA
ALA
B2093
−9.680
25.733
28.394
1.00
26.50
C

ATOM
1620
CB
ALA
22093
−8.243
26.278
28.384
1.00
25.87
C

ATOM
1621
C
ALA
22093
−9.876
24.805
29.587
1.00
27.03
C

ATOM
1622
O
ALA
B2093
−10.200
25.252
30.687
1.00
27.16
O

ATOM
1623
N
PRO

B2094
−9.671
23.492
29.382
1.00
27.79
N

ATOM
1624
CD
PRO

B2094
−9.377
22.840
28.090
1.00
27.87
C

ATOM
1625
CA
PRO

B2094
−9.824
22.497
30.452
1.00
28.17
C

ATOM
1626
CB
PRO

B2094
−9.970
21.191
29.681
1.00
27.97
C

ATOM
1627
CG
PRO

B2094
−9.068
21.408
28.501
1.00
27.75
C

ATOM
1628
C
PRO

B2094
−8.611
22.489
31.384
1.00
28.93
C

ATOM
1629
O
PRO

B2094
−8.149
21.429
31.819
1.00
29.42
O

ATOM
1630
N
PHE
B2095
−8.099
23.676
31.690
1.00
29.04
N

ATOM
1631
CA
PHE
B2095
−6.929
23.812
32.551
1.00
28.93
C

ATOM
1632
CB
PHE
B2095
−5.704
24.150
31.689
1.00
28.61
C

ATOM
1633
CG
PHE
B2095
−4.416
24.266
32.460
1.00
28.08
C

ATOM
1634
CD1
PHE
B2095
−3.697
25.457
32.454
1.00
27.74
C

ATOM
1635
CG2
PHE
B2095
−3.918
23.185
33.187
1.00
27.48
C

ATOM
1636
CBl
PHE
B2095
−2.503
25.574
33.158
1.00
27.44
C

ATOM
1637
CB2
PHE
B2095
−2.730
23.292
33.893
1.00
27.21
C

ATOM
1638
CZ
PHE
B2095
−2.018
24.492
33.880
1.00
27.64
C

ATOM
1639
C
PHE
B2095
−7.220
24.934
33.544
1.00
29.17
C

ATOM
1640
O
PHE
B2095
−7.922
25.893
33.211
1.00
29.61
O

ATOM
1641
N
SER
B2096
−6.690
24.821
34.758
1.00
28.80
N

ATOM
1642
CA
SER
B2096
−6.931
25.837
35.771
1.00
28.67
C

ATOM
1643
CB
SER
B2096
−7.374
25.177
37.078
1.00
29.60
C

ATOM
1644
OG
SER
B2096
−8.489
24.328
36.859
1.00
31.74
O

ATOM
1645
C
SER
B2096
−5.719
26.716
36.038
1.00
27.69
C

ATOM
1646
O
SER
B2096
−5.828
27.746
36.700
1.00
27.77
O

ATOM
1647
N
GLY
B2097
−4.563
26.318
35.526
1.00
26.80
N

ATOM
1648
CA
GLY
B2097
−3.370
27.115
35.752
1.00
25.56
C

ATOM
1649
C
GLY
B2097
−3.246
28.268
34.771
1.00
24.43
C

ATOM
1650
O
GLY
B2097
−4.224
28.686
34.155
1.00
23.36
O

ATOM
1651
N
LYS
B2098
−2.032
28.786
34.629
1.00
23.85
N

ATOM
1652
CA
LYS
B2098
−1.786
29.886
33.707
1.00
23.16
C

ATOM
1653
CB
LYS
B2098
−0.656
30.789
34.212
1.00
24.15
C

ATOM
1654
CG
LYS
B2098
−1.025
31.639
35.408
1.00
25.14
C

ATOM
1655
CD
LYS
B2098
0.036
32.693
35.659
1.00
26.88
C

ATOM
1656
CE
LYS
B2098
−0.288
33.524
36.895
1.00
27.83
C

ATOM
1657
NZ
LYS
B2098
−0.224
32.680
38.126
1.00
28.96
N

ATOM
1658
C
LYS
B2098
−1.406
29.332
32.353
1.00
21.88
C

ATOM
1659
O
LYS
B2098
−0.604
28.402
32.261
1.00
21.71
O

ATOM
1660
N
ILE
B2099
−1.997
29.905
31.310
1.00
20.39
N

ATOM
1661
CA
ILE
B2099
−1.723
29.494
29.941
1.00
19.37
C

ATOM
1662
CB
ILE
B2099
−3.027
29.186
29.165
1.00
19.23
C

ATOM
1663
CG2
ILE
B2099
−2.695
28.629
27.779
1.00
18.49
C

ATOM
1664
CG1
ILE
B2099
−3.878
28.182
29.950
1.00
18.74
C

ATOM
1665
CD1
ILE
B2099
−5.199
27.892
29.299
1.00
18.23
C

ATOM
1666
C
ILE
B2099
−0.997
30.621
29.221
1.00
18.65
C

ATOM
1667
O
ILE
B2099
−1.570
31.683
28.973
1.00
18.86
O

ATOM
1668
N
TRP
B2100
0.273
30.401
28.907
1.00
17.78
N

ATOM
1669
CA
TRP
B2100
1.043
31.407
28.195
1.00
17.08
C

ATOM
1670
CB
TRP
B2100
2.477
31.487
28.735
1.00
15.80
C

ATOM
1671
CG
TRP
B2100
2.533
31.922
30.180
1.00
15.68
C

ATOM
1672
CD2
TRP
B2100
2.423
33.264
30.679
1.00
15.05
C

ATOM
1673
CE2
TRP
B2100
2.466
33.189
32.093
1.00
15.31
C

ATOM
1674
CE3
TRP
B2100
2.289
34.522
30.070
1.00
15.15
C

ATOM
1675
CD1
TRP
B2100
2.636
31.111
31.284
1.00
15.45
C

ATOM
1676
NE1
TRP
B2100
2.595
31.868
32.432
1.00
15.26
N

ATOM
1677
CZ2
TRP
B2100
2.384
34.328
32.912
1.00
15.02
C

ATOM
1678
CZ3
TRP
B2100
2.204
35.658
30.883
1.00
15.47
C

ATOM
1679
CH2
TRP
B2100
2.253
35.548
32.291
1.00
15.54
C

ATOM
1680
C
TRP
B2100
1.027
31.028
26.723
1.00
17.16
C

ATOM
1681
O
TRP
B2100
1.627
30.041
26.311
1.00
17.52
O

ATOM
1682
N
LEU
B2101
0.314
31.821
25.937
1.00
17.56
N

ATOM
1683
CA
LEU
B2101
0.180
31.575
24.508
1.00
17.56
C

ATOM
1684
CB
LEU
B2101
−1.304
31.454
24.137
1.00
17.63
C

ATOM
1685
CG
LEU
B2101
−1.641
31.497
22.635
1.00
18.34
C

ATOM
1686
CD1
LEU
B2101
−1.241
30.157
21.964
1.00
17.98
C

ATOM
1687
CD2
LEU
B2101
−3.132
31.768
22.444
1.00
17.63
C

ATOM
1688
C
LEU
B2101
0.789
32.685
23.681
1.00
17.40
C

ATOM
1689
O
LEU
B2101
0.770
33.849
24.075
1.00
17.23
O

ATOM
1690
N
SER
B2102
1.332
32.312
22.529
1.00
17.67
N

ATOM
1691
CA
SER
B2102
1.892
33.274
21.602
1.00
17.46
C

ATOM
1692
CB
SER
B2102
3.366
33.551
21.892
1.00
17.36
C

ATOM
1693
OG
SER
B2102
3.797
34.687
21.150
1.00
17.27
O

ATOM
1694
C
SER
B2102
1.731
32.739
20.185
1.00
17.83
C

ATOM
1695
O
SER
B2102
1.984
31.563
19.919
1.00
17.13
O

ATOM
1696
N
ILE
B2103
1.286
33.616
19.288
1.00
18.64
N

ATOM
1697
CA
ILE
B2103
1.084
33.270
17.888
1.00
19.37
C

ATOM
1698
CB
ILE
B2103
−0.429
33.275
17.515
1.00
19.72
C

ATOM
1699
CG2
ILE
B2103
−0.625
32.778
16.079
1.00
19.83
C

ATOM
1700
CG1
ILE
B2103
−1.213
32.382
18.480
1.00
20.18
C

ATOM
1701
CD1
ILE
B2103
−2.722
32.470
18.314
1.00
20.28
C

ATOM
1702
C
ILE
B2103
1.813
34.299
17.014
1.00
19.77
C

ATOM
1703
O
ILE
B2103
1.857
35.489
17.330
1.00
18.81
O

ATOM
1704
N
SER
B2104
2.396
33.818
15.925
1.00
20.35
N

ATOM
1705
CA
SER
B2104
3.096
34.673
14.974
1.00
21.48
C

ATOM
1706
CB
SER
B2104
4.603
34.675
15.268
1.00
21.45
C

ATOM
1707
OG
SER
B2104
5.328
35.484
14.351
1.00
21.11
O

ATOM
1708
C
SER
B2104
2.826
34.069
13.598
1.00
22.45
C

ATOM
1709
O
SER
B2104
2.492
32.884
13.488
1.00
22.26
O

ATOM
1710
N
HIS
B2105
2.949
34.872
12.549
1.00
23.91
N

ATOM
1711
CA
HIS
B2105
2.725
34.348
11.207
1.00
25.44
C

ATOM
1712
CB
HIS
B2105
1.235
34.372
10.867
1.00
26.52
C

ATOM
1713
CG
HIS
B2105
0.682
35.754
10.693
1.00
27.10
C

ATOM
1714
CD2
HIS
B2105
0.353
36.451
9.577
1.00
27.93
C

ATOM
1715
ND1
HIS
B2105
0.427
36.594
11.755
1.00
27.73
N

ATOM
1716
CE1
HIS
B2105
−0.036
37.747
11.302
1.00
27.61
C

ATOM
1717
NE2
HIS
B2105
−0.091
37.686
9.984
1.00
27.60
N

ATOM
1718
C
HIS
B2105
3.467
35.117
10.123
1.00
25.84
C

ATOM
1719
O
HIS
B2105
3.836
36.274
10.303
1.00
25.76
O

ATOM
1720
N
THR
B2106
3.688
34.444
9.001
1.00
26.43
N

ATOM
1721
CA
THR
B2106
4.314
35.051
7.834
1.00
27.12
C

ATOM
1722
CB
THR
B2106
5.546
34.261
7.341
1.00
27.09
C

ATOM
1723
OG1
THR
B2106
5.137
32.968
6.888
1.00
26.88
O

ATOM
1724
CG2
THR
B2106
6.576
34.120
8.452
1.00
27.18
C

ATOM
1725
C
THR
B2106
3.213
34.953
6.777
1.00
27.59
C

ATOM
1726
O
THR
B2106
2.059
34.688
7.116
1.00
28.11
O

ATOM
1727
N
ASP
B2107
3.553
35.148
5.508
1.00
27.85
N

ATOM
1728
CA
ASP
B2107
2.554
35.068
4.449
1.00
28.22
C

ATOM
1729
CB
ASP
B2107
3.085
35.722
3.170
0.05
28.14
C

ATOM
1730
CG
ASP
B2107
3.275
37.220
3.316
0.05
28.09
C

ATOM
1731
OD1
ASP
B2107
2.276
37.926
3.569
0.05
28.04
O

ATOM
1732
OD2
ASP
B2107
4.422
37.693
3.177
0.05
28.08
O

ATOM
1733
C
ASP
B2107
2.116
33.632
4.138
1.00
28.63
C

ATOM
1734
O
ASP
B2107
0.995
33.408
3.684
1.00
28.77
O

ATOM
1735
N
GLN
B2108
2.988
32.662
4.392
1.00
28.69
N

ATOM
1736
CA
GLN
B2108
2.663
31.272
4.093
1.00
29.21
C

ATOM
1737
CB
GLN
B2108
3.753
30.666
3.201
1.00
30.96
C

ATOM
1738
CG
GLN
B2108
4.217
31.565
2.059
1.00
32.72
C

ATOM
1739
CD
GLN
B2108
5.386
30.967
1.282
1.00
34.31
C

ATOM
1740
OE1
GLN
B2108
5.195
30.201
0.328
1.00
34.84
O

ATOM
1741
NE2
GLN
B2108
6.605
31.306
1.699
1.00
34.53
N

ATOM
1742
C
GLN
B2108
2.482
30.366
5.308
1.00
28.68
C

ATOM
1743
O
GLN
B2108
1.819
29.337
5.215
1.00
28.89
O

ATOM
1744
N
PHE
B2109
3.068
30.741
6.441
1.00
27.66
N

ATOM
1745
CA
PHE
B2109
2.985
29.916
7.641
1.00
26.50
C

ATOM
1746
CB
PHE
B2109
4.347
29.287
7.953
1.00
26.61
C

ATOM
1747
CG
PHE
B2109
4.860
28.387
6.875
1.00
27.11
C

ATOM
1748
CD1
PHE
B2109
5.577
28.907
5.799
1.00
27.30
C

ATOM
1749
CD2
PHE
B2109
4.599
27.020
6.913
1.00
26.71
C

ATOM
1750
CE1
PHE
B2109
6.026
28.073
4.773
1.00
27.50
C

ATOM
1751
CE2
PHE
B2109
5.045
26.180
5.893
1.00
27.16
C

ATOM
1752
CZ
PHE
B2109
5.757
26.706
4.823
1.00
27.50
C

ATOM
1753
C
PHE
B2109
2.524
30.648
8.883
1.00
25.59
C

ATOM
1754
O
PHE
B2109
2.625
31.872
8.967
1.00
25.67
O

ATOM
1755
N
VAL
B2110
2.016
29.881
9.843
1.00
24.04
N

ATOM
1756
CA
VAL
B2110
1.580
30.435
11.114
1.00
23.42
C

ATOM
1757
CB
VAL
B2110
0.045
30.435
11.267
1.00
23.14
C

ATOM
1758
CG1
VAL
B2110
−0.498
29.016
11.276
1.00
23.49
C

ATOM
1759
CG2
VAL
B2110
−0.327
31.151
12.535
1.00
23.40
C

ATOM
1760
C
VAL
B2110
2.201
29.562
12.188
1.00
22.98
C

ATOM
1761
O
VAL
B2110
2.371
28.364
11.996
1.00
23.38
O

ATOM
1762
N
THR
B2111
2.555
30.161
13.314
1.00
22.66
N

ATOM
1763
CA
THR
B2111
3.175
29.402
14.390
1.00
22.51
C

ATOM
1764
CB
THR
B2111
4.674
29.721
14.459
1.00
23.02
C

ATOM
1765
OG1
THR
B2111
5.310
28.830
15.373
1.00
25.57
O

ATOM
1766
CG2
THR
B2111
4.891
31.148
14.928
1.00
23.27
C

ATOM
1767
C
THR
B2111
2.531
29.714
15.735
1.00
21.17
C

ATOM
1768
O
THR
B2111
2.013
30.807
15.939
1.00
21.65
O

ATOM
1769
N
ALA
B2112
2.565
28.748
16.649
1.00
19.97
N

ATOM
1770
CA
ALA
B2112
1.986
28.928
17.985
1.00
18.49
C

ATOM
1771
CB
ALA
B2112
0.549
28.422
18.009
1.00
16.81
C

ATOM
1772
C
ALA
B2112
2.805
28.227
19.073
1.00
17.74
C

ATOM
1773
O
ALA
B2112
3.375
27.168
18.857
1.00
16.72
O

ATOM
1774
N
SER
B2113
2.860
28.834
20.251
1.00
17.84
N

ATOM
1775
CA
SER
B2213
3.597
28.250
21.365
1.00
17.93
C

ATOM
1776
CB
SER
B2113
4.985
28.893
21.495
1.00
17.90
C

ATOM
1777
OG
SER
B2113
5.742
28.263
22.512
1.00
17.60
O

ATOM
1778
C
SER
B2113
2.805
28.439
22.653
1.00
17.35
C

ATOM
1779
O
SER
B2113
2.262
29.510
22.905
1.00
17.22
O

ATOM
1780
N
VAL
B2114
2.749
27.382
23.452
1.00
16.89
N

ATOM
1781
CA
VAL
B2114
2.020
27.383
24.708
1.00
16.75
C

ATOM
1782
CB
VAL
B2114
0.718
26.533
24.612
1.00
16.63
C

ATOM
1783
CG1
VAL
B2114
0.112
26.347
25.999
1.00
16.16
C

ATOM
1784
CG2
VAL
B2114
−0.298
27.205
23.675
1.00
16.25
C

ATOM
1785
C
VAL
B2114
2.862
26.799
25.835
1.00
17.45
C

ATOM
1786
O
VAL
B2114
3.503
25.750
25.680
1.00
16.99
O

ATOM
1787
N
ILE
B2115
2.863
27.497
26.966
1.00
17.80
N

ATOM
1788
CA
ILE
B2115
3.566
27.037
28.156
1.00
18.72
C

ATOM
1789
CB
ILE
B2115
4.689
28.008
28.602
1.00
18.37
C

ATOM
1790
CG2
ILE
B2115
5.385
27.452
29.846
1.00
18.27
C

ATOM
1791
CG1
ILE
B2115
5.708
28.205
27.480
1.00
18.40
C

ATOM
1792
CD1
ILE
B2115
6.745
29.289
27.786
1.00
17.55
C

ATOM
1793
C
ILE
B2115
2.515
27.000
29.260
1.00
19.25
C

ATOM
1794
O
ILE
B2115
1.858
28.004
29.524
1.00
19.38
O

ATOM
1795
N
LEU
B2116
2.336
25.846
29.884
1.00
20.55
N

ATOM
1796
CA
LEU
B2116
1.374
25.735
30.968
1.00
22.30
C

ATOM
1797
CB
LEU
B2116
0.628
24.404
30.902
1.00
21.86
C

ATOM
1798
CG
LEU
B2116
−0.147
24.159
29.603
1.00
22.00
C

ATOM
1799
CD1
LEU
B2116
−0.976
22.893
29.732
1.00
21.49
C

ATOM
1800
CD2
LEU
B2116
−1.050
25.359
29.303
1.00
21.93
C

ATOM
1801
C
LEU
B2116
2.123
25.864
32.290
1.00
24.11
C

ATOM
1802
O
LEU
B2116
3.209
25.299
32.472
1.00
23.89
O

ATOM
1803
N
GLU
B2117
1.544
26.621
33.210
1.00
26.00
N

ATOM
1804
CA
GLU
B2117
2.177
26.840
34.493
1.00
28.60
C

ATOM
1805
CB
GLU
B2117
2.746
28.258
34.531
1.00
28.59
C

ATOM
1806
CG
GLU
B2117
3.418
28.627
35.829
1.00
30.48
C

ATOM
1807
CD
GLU
B2117
4.079
29.997
35.771
1.00
31.11
C

ATOM
1808
OE1
GLU
B2117
3.395
30.972
35.385
1.00
31.07
O

ATOM
1809
OE2
GLU
B2117
5.281
30.092
36.115
1.00
31.14
O

ATOM
1810
C
GLU
B2117
1.217
26.601
35.659
1.00
30.07
C

ATOM
1811
O
GLU
B2117
0.029
26.938
35.595
1.00
29.34
O

ATOM
1812
N
GLU
B2118
1.742
26.006
36.726
1.00
32.11
N

ATOM
1813
CA
GLU
B2118
0.926
25.712
37.889
1.00
34.40
C

ATOM
1814
CB
GLU
B2118
0.997
24.223
38.212
1.00
35.62
C

ATOM
1815
CG
GLU
B2118
−0.294
23.679
38.772
1.00
37.98
C

ATOM
1816
CD
GLU
B2118
−1.458
23.905
37.825
1.00
39.13
C

ATOM
1817
OE1
GLU
B2118
−1.403
23.398
36.682
1.00
39.94
O

ATOM
1818
OE2
GLU
B2118
−2.422
24.596
38.222
1.00
40.32
O

ATOM
1819
C
GLU
B2118
1.387 26.515
39.090
1.00
35.21
C

ATOM
1820
O
GLU
B2118
2.611
26.552
39.343
1.00
35.67
O

ATOM
1821
OXT
GLU
B2118
0.507
27.088
39.767
1.00
36.45
O

TER
1822

GLU
B2118

ATOM
1823
CB
MET
C3003
14.254
28.191
38.580
1.00
31.28
C

ATOM
1824
CG
MET
C3003
15.448
27.262
38.618
1.00
32.93
C

ATOM
1825
SD
MET
C3003
16.870
27.987
39.434
1.00
35.68
S

ATOM
1826
CE
MET
C3003
16.438
27.672
41.140
1.00
34.95
C

ATOM
1827
C
MET
C3003
13.519
27.087
36.482
1.00
29.25
C

ATOM
1828
O
MET
C3003
13.901
25.920
36.332
1.00
28.76
O

ATOM
1829
N
MET
C3003
12.435
26.519
38.666
1.00
30.53
N

ATOM
1830
CA
MET
C3003
13.052
27.596
37.845
1.00
30.20
C

ATOM
1831
N
ILE
C3004
13.491
27.976
35.493
1.00
28.16
N

ATOM
1832
CA
ILE
C3004
13.945
27.636
34.149
1.00
27.31
C

ATOM
1833
CB
ILE
C3004
13.377
28.604
33.084
1.00
27.05
C

ATOM
1834
CG2
ILE
C3004
14.103
28.413
31.761
1.00
26.26
C

ATOM
1835
CG1
ILE
C3004
11.876
28.372
32.919
1.00
26.90
C

ATOM
1836
CD1
ILE
C3004
11.203
29.374
31.996
1.00
27.09
C

ATOM
1837
C
ILE
C3004
15.452
27.775
34.170
1.00
26.61
C

ATOM
1838
O
ILE
C3004
15.970
28.755
34.685
1.00
26.80
O

ATOM
1839
N
VAL
C3005
16.153
26.794
33.617
1.00
26.02
N

ATOM
1840
CA
VAL
C3005
17.611
26.822
33.581
1.00
25.10
C

ATOM
1841
CB
VAL
C3005
18.221
25.644
34.396
1.00
25.36
C

ATOM
1842
CG1
VAL
C3005
17.820
25.766
35.869
1.00
25.11
C

ATOM
1843
CG2
VAL
C3005
17.755
24.306
33.833
1.00
24.57
C

ATOM
1844
C
VAL
C3005
18.124
26.747
32.152
1.00
24.50
C

ATOM
1845
O
VAL
C3005
19.327
26.640
31.928
1.00
25.44
O

ATOM
1846
N
GLY
C3006
17.212
26.805
31.186
1.00
23.63
N

ATOM
1847
CA
GLY
C3006
17.612
26.736
29.791
1.00
22.31
C

ATOM
1848
C
GLY
C3006
16.446
26.762
28.820
1.00
21.49
C

ATOM
1849
O
GLY
C3006
15.332
26.348
29.156
1.00
21.47
O

ATOM
1850
N
HIS
C3007
16.700
27.254
27.609
1.00
20.33
N

ATOM
1851
CA
HIS
C3007
15.664
27.336
26.582
1.00
19.44
C

ATOM
1852
GB
HIS
C3007
14.806
28.591
26.785
1.00
18.31
C

ATOM
1853
CG
HIS
C3007
13.749
28.777
25.741
1.00
18.22
C

ATOM
1854
CD2
HIS
C3007
13.411
29.857
24.997
1.00
18.17
C

ATOM
1855
ND1
HIS
C3007
12.871
27.778
25.384
1.00
18.32
N

ATOM
1856
CE1
HIS
C3007
12.036
28.233
24.467
1.00
18.15
C

ATOM
1857
NE2
HIS
C3007
12.342
29.492
24.215
1.00
18.03
N

ATOM
1858
C
HIS
C3007
16.288
27.357
25.196
1.00
18.96
C

ATOM
1859
O
HIS
C3007
17.200
28.125
24.940
1.00
19.65
O

ATOM
1860
N
GLY
C3008
15.795
26.504
24.307
1.00
18.27
N

ATOM
1861
CA
GLY
C3008
16.340
26.468
22.965
1.00
17.73
C

ATOM
1862
C
GLY
C3008
15.307
26.061
21.932
1.00
17.73
C

ATOM
1863
O
GLY
C3008
14.398
25.274
22.215
1.00
16.98
O

ATOM
1864
N
ILE
C3009
15.426
26.620
20.735
1.00
17.47
N

ATOM
1865
CA
ILE
C3009
14.512
26.281
19.658
1.00
18.23
C

ATOM
1866
CB
ILE
C3009
13.483
27.414
19.340
1.00
17.95
C

ATOM
1867
CG2
ILE
C3009
12.743
27.836
20.604
1.00
17.06
C

ATOM
1868
CG1
ILE
C3009
14.192
28.608
18.683
1.00
17.87
C

ATOM
1869
CD1
ILE
C3009
13.233
29.653
18.104
1.00
18.30
C

ATOM
1870
C
ILE
C3009
15.327
26.029
18.406
1.00
19.18
C

ATOM
1871
O
ILE
C3009
16.516
26.345
18.345
1.00
18.80
O

ATOM
1872
N
ASP
C3010
14.682
25.439
17.413
1.00
20.69
N

ATOM
1873
CA
ASP
C3010
15.330
25.188
16.144
1.00
22.71
C

ATOM
1874
CB
ASP
C3010
16.251
23.974
16.216
1.00
23.72
C

ATOM
1875
CG
ASP
C3010
16.949
23.710
14.899
1.00
24.96
C

ATOM
1876
OD1
ASP
C3010
17.840
24.501
14.528
1.00
26.04
O

ATOM
1877
OD2
ASP
C3010
16.598
22.724
14.219
1.00
26.67
O

ATOM
1878
C
ASP
C3010
14.307
24.963
15.045
1.00
23.50
C

ATOM
1879
O
ASP
C3010
13.239
24.407
15.278
1.00
23.37
O

ATOM
1880
N
ILE
C3011
14.645
25.428
13.851
1.00
24.39
N

ATOM
1881
CA
ILE
C3011
13.796
25.259
12.695
1.00
25.77
C

ATOM
1882
CB
ILE
C3011
13.178
26.600
12.239
1.00
25.68
C

ATOM
1883
CG2
ILE
C3011
14.270
27.609
11.941
1.00
24.95
C

ATOM
1884
CG1
ILE
C3011
12.274
26.364
11.022
1.00
25.90
O

ATOM
1885
CD1
ILE
C3011
11.308
27.501
10.737
1.00
25.60
O

ATOM
1886
C
ILE
C3011
14.701
24.681
11.616
1.00
27.06
O

ATOM
1887
O
ILE
C3011
15.856
25.091
11.476
1.00
27.35
O

ATOM
1888
N
GLU
C3012
14.182
23.700
10.885
1.00
28.16
N

ATOM
1889
CA
GLU
C3012
14.937
23.048
9.829
1.00
29.36
C

ATOM
1890
CB
GLU
C3012
15.410
21.664
10.278
1.00
30.33
C

ATOM
1891
CG
GLU
C3012
16.347
21.633
11.467
1.00
31.58
C

ATOM
1892
CD
GLU
C3012
17.722
22.207
11.164
1.00
32.87
C

ATOM
1893
OE1
GLU
C3012
18.082
22.322
9.965
1.00
32.65
O

ATOM
1894
OE2
GLU
C3012
18.447
22.529
12.138
1.00
32.87
O

ATOM
1895
C
GLU
C3012
14.097
22.872
8.580
1.00
29.90
O

ATOM
1896
O
GLU
C3012
12.906
22.548
8.647
1.00
29.35
O

ATOM
1897
N
GLU
C3013
14.729
23.095
7.435
1.00
31.00
N

ATOM
1898
CA
GLU
C3013
14.067
22.913
6.153
1.00
32.07
C

ATOM
1899
CB
GLU
C3013
14.782
23.722
5.075
1.00
33.32
C

ATOM
1900
CG
GLU
C3013
14.202
23.564
3.684
1.00
35.05
C

ATOM
1901
CD
GLU
C3013
15.142
24.089
2.614
1.00
36.48
C

ATOM
1902
OE1
GLU
C3013
15.645
25.228
2.761
1.00
36.82
O

ATOM
1903
OE2
GLU
C3013
15.376
23.365
1.622
1.00
37.39
O

ATOM
1904
C
GLU
C3013
14.206
21.418
5.873
1.00
31.77
C

ATOM
1905
O
GLU
C3013
15.306
20.877
5.914
1.00
31.08
O

ATOM
1906
N
LEU
C3014
13.098
20.750
5.614
1.00
32.39
N

ATOM
1907
CA
LEU
C3014
13.130
19.318
5.360
1.00
33.65
C

ATOM
1908
CB
LEU
C3014
11.718
18.794
5.080
1.00
33.57
C

ATOM
1909
CG
LEU
C3014
10.813
18.685
6.313
1.00
34.16
C

ATOM
1910
CD1
LEU
C3014
9.416
18.252
5.906
1.00
34.65
C

ATOM
1911
CD2
LEU
C3014
11.404
17.680
7.280
1.00
34.38
C

ATOM
1912
C
LEU
C3014
14.069
18.946
4.220
1.00
34.37
C

ATOM
1913
O
LEU
C3014
14.736
17.913
4.271
1.00
34.47
O

ATOM
1914
N
ALA
C3015
14.128
19.801
3.204
1.00
35.44
N

ATOM
1915
CA
ALA
C3015
14.982
19.572
2.047
1.00
36.79
C

ATOM
1916
CB
ALA
C3015
14.749
20.655
1.011
1.00
36.53
C

ATOM
1917
C
ALA
C3015
16.457
19.511
2.418
1.00
37.84
C

ATOM
1918
O
ALA
C3015
17.215
18.737
1.831
1.00
38.53
O

ATOM
1919
N
SER
C3016
16.868
20.322
3.391
1.00
39.07
N

ATOM
1920
CA
SER
C3016
18.258
20.349
3.838
1.00
40.09
C

ATOM
1921
CB
SER
C3016
18.473
21.478
4.847
1.00
40.11
C

ATOM
1922
OG
SER
C3016
18.172
22.734
4.271
1.00
41.50
O

ATOM
1923
C
SER
C3016
18.628
19.026
4.481
1.00
40.95
C

ATOM
1924
O
SER
C3016
19.757
18.552
4.340
1.00
41.12
O

ATOM
1925
N
ILE
C3017
17.683
18.428
5.197
1.00
41.82
N

ATOM
1926
CA
ILE
C3017
17.951
17.158
5.849
1.00
43.16
C

ATOM
1927
CB
ILE
C3017
16.799
16.768
6.795
1.00
42.90
C

ATOM
1928
CG2
ILE
C3017
17.170
15.527
7.598
1.00
42.32
C

ATOM
1929
CG1
ILE
C3017
16.518
17.924
7.759
1.00
43.05
C

ATOM
1930
CD1
ILE
C3017
17.709
18.332
8.597
1.00
42.53
C

ATOM
1931
C
ILE
C3017
18.165
16.076
4.789
1.00
44.24
C

ATOM
1932
O
ILE
C3017
19.033
15.215
4.941
1.00
44.09
O

ATOM
1933
N
GLU
C3018
17.383
16.128
3.713
1.00
45.44
N

ATOM
1934
CA
GLU
C3018
17.530
15.158
2.637
1.00
47.05
C

ATOM
1935
CB
GLU
C3018
16.516
15.411
1.524
1.00
47.54
C

ATOM
1936
CG
GLU
C3018
15.158
14.805
1.755
1.00
48.25
C

ATOM
1937
CD
GLU
C3018
14.383
14.664
0.463
1.00
48.87
C

ATOM
1938
QEl
GLU
C3018
14.159
15.686
−0.220
1.00
49.40
O

ATOM
1939
022
GLU
C3018
14.005
13.525
0.126
1.00
49.49
O

ATOM
1940
C
GLU
C3018
18.929
15.261
2.048
1.00
47.90
C

ATOM
1941
O
GLU
C3018
19.696
14.299
2.083
1.00
47.96
O

ATOM
1942
N
SER
C3019
19.248
16.429
1.495
1.00
48.89
N

ATOM
1943
CA
SER
C3019
20.560
16.658
0.905
1.00
49.72
C

ATOM
1944
CB
SER
C3019
20.815
18.152
0.713
1.00
49.87
C

ATOM
1945
OG
SER
C3019
19.977
18.685
−0.295
1.00
50.04
O

ATOM
1946
C
SER
C3019
21.614
16.078
1.825
1.00
50.34
C

ATOM
1947
O
SER
C3019
22.506
15.362
1.380
1.00
50.79
O

ATOM
1948
N
ALA
C3020
21.504
16.380
3.114
1.00
50.84
N

ATOM
1949
CA
ALA
C3020
22.461
15.860
4.083
1.00
51.57
C

ATOM
1950
CB
ALA
C3020
22.054
16.266
5.491
1.00
51.45
C

ATOM
1951
C
ALA
C3020
22.511
14.338
3.960
1.00
52.20
C

ATOM
1952
O
ALA
C3020
23.585
13.752
3.811
1.00
52.03
O

ATOM
1953
N
VAL
C3021
21.337
13.711
4.013
1.00
53.10
N

ATOM
1954
CA
VAL
C3021
21.212
12.259
3.897
1.00
53.96
C

ATOM
1955
CB
VAL
C3021
19.730
11.818
3.969
1.00
53.97
C

ATOM
1956
CG1
VAL
C3021
19.609
10.329
3.671
1.00
54.14
C

ATOM
1957
CG2
VAL
C3021
19.165
12.124
5.340
1.00
53.98
C

ATOM
1958
C
VAL
C3021
21.788
11.793
2.566
1.00
54.57
C

ATOM
1959
O
VAL
C3021
22.424
10.740
2.481
1.00
54.43
O

ATOM
1960
N
THR
C3022
21.553
12.591
1.530
1.00
55.21
N

ATOM
1961
CA
THR
C3022
22.041
12.293
0.194
1.00
55.84
C

ATOM
1962
CB
THR
C3022
21.456
13.283
−0.831
1.00
55.80
C

ATOM
1963
OG1
THR
C3022
20.034
13.124
−0.878
1.00
55.98
O

ATOM
1964
CG2
THR
C3022
22.036
13.036
−2.214
1.00
55.79
C

ATOM
1965
C
THR
C3022
23.566
12.355
0.155
1.00
56.35
C

ATOM
1966
O
THR
C3022
24.213
11.386
−0.230
1.00
56.58
O

ATOM
1967
N
ARG
C3023
24.135
13.489
0.557
1.00
56.81
N

ATOM
1968
CA
ARG
C3023
25.586
13.650
0.567
1.00
57.20
C

ATOM
1969
CB
ARG
C3023
25.966
15.015
1.151
1.00
57.25
C

ATOM
1970
CG
ARG
C3023
27.463
15.289
1.151
1.00
57.60
C

ATOM
1971
CD
ARG
C3023
27.782
16.762
1.388
1.00
57.64
C

ATOM
1972
NE
ARG
C3023
27.410
17.222
2.722
0.05
57.76
N

ATOM
1973
CZ
ARG
C3023
27.609
18.460
3.163
0.05
57.81
C

ATOM
1974
NH1
ARG
C3023
28.176
19.364
2.374
0.05
57.84
N

ATOM
1975
NH2
ARG
C3023
27.245
18.796
4.393
0.05
57−.82
N

ATOM
1976
C
ARG
C3023
26.203
12.522
1.390
1.00
57.47
C

ATOM
1977
O
ARG
C3023
26.328
11.402
0.903
1.00
57.73
O

ATOM
1978
N
HIS
C3024
26.592
12.806
2.630
1.00
57.66
N

ATOM
1979
CA
HIS
C3024
27.168
11.773
3.486
1.00
57.79
C

ATOM
1980
CB
HIS
C3024
27.968
12.404
4.627
0.05
57.91
C

ATOM
1981
CG
HIS
C3024
29.442
12.449
4.375
0.05
58.00
C

ATOM
1982
CG2
HIS
C3024
30.301
13.491
4.278
0.05
58.04
C

ATOM
1983
ND1
HIS
C3024
30.198
11.312
4.187
0.05
58.04
N

ATOM
1984
CBl
HIS
C3024
31.459
11.651
3.986
0.05
58.06
C

ATOM
1985
NE2
HIS
C3024
31.549
12.968
4.036
0.05
58.07
N

ATOM
1986
C
HIS
C3024
26.069
10.873
4.054
1.00
57.96
C

ATOM
1987
O
HIS
C3024
25.413
11.223
5.038
1.00
58.10
O

ATOM
1988
N
GLU
C3025
25.874
9.710
3.435
1.00
57.92
N

ATOM
1989
CA
GLTJ C3025
24.846
8.773
3.879
1.00
57.71
C

ATOM
1990
CB
GLU
C3025
24.824
7.535
2.976
1.00
58.27
C

ATOM
1991
CG
GLU
C3025
25.979
6.571
3.189
1.00
59.11
C

ATOM
1992
CD
GLU
C3025
25.784
5.259
2.446
1.00
59.59
C

ATOM
1993
OE1
GLU
C3025
24.749
4.592
2.673
1.00
59.65
O

ATOM
1994
OE2
GLU
C3025
26.665
4.893
1.637
1.00
59.98
O

ATOM
1995
C
GLU
C3025
25.029
8.341
5.336
1.00
57.11
C

ATOM
1996
O
GLU
C3025
24.089
7.857
5.974
1.00
57.33
O

ATOM
1997
N
GLY
C3026
26.238
8.508
5.861
1.00
56.15
N

ATOM
1998
CA
GLY
C3026
26.486
8.136
7.242
1.00
55.03
C

ATOM
1999
C
GLY
C3026
25.890
9.170
8.177
1.00
54.19
C

ATOM
2000
O
GLY
C3026
26.023
9.081
9.398
1.00
54.12
O

ATOM
2001
N
PHF
C3027
25.227
10.160
7.589
1.00
53.18
N

ATOM
2002
CA
PHE
C3027
24.601
11.238
8.343
1.00
52.05
C

ATOM
2003
CB
PHE
C3027
23.817
12.142
7.386
1.00
52.10
C

ATOM
2004
CG
PHE
C3027
23.129
13.289
8.059
1.00
52.03
C

ATOM
2005
CD1
PHE
C3027
23.859
14.233
8.768
1.00
51.96
C

ATOM
2006
CG2
PHE
C3027
21.743
13.427
7.984
1.00
52.34
C

ATOM
2007
CBl
PHE
C3027
23.221
15.304
9.398
1.00
52.41
C

ATOM
2008
CB2
PHE
C3027
21.092
14.492
8.609
1.00
52.33
C

ATOM
2009
CZ
PHE
C3027
21.833
15.434
9.319
1.00
52.40
C

ATOM
2010
C
PHE
C3027
23.676
10.720
9.443
1.00
51.01
C

ATOM
2011
O
PHE
C3027
23.914
10.957
10.628
1.00
51.01
O

ATOM
2012
N
ALA
C3028
22.631
10.002
9.042
1.00
49.81
N

ATOM
2013
CA
ALA
C3028
21.648
9.463
9.979
1.00
48.74
C

ATOM
2014
CB
ALA
C3028
20.608
8.645
9.231
1.00
48.50
C

ATOM
2015
C
ALA
C3028
22.240
8.630
11.104
1.00
48.04
C

ATOM
2016
O
ALA
C3028
21.865
8.802
12.266
1.00
47.95
O

ATOM
2017
N
LYS
C3029
23.156
7.726
10.767
1.00
47.14
N

ATOM
2018
CA
LYS
C3029
23.765
6.874
11.779
1.00
46.13
C

ATOM
2019
CB
LYS
C3029
24.681
5.833
11.126
1.00
46.10
C

ATOM
2020
CG
LYS
C3029
25.918
6.410
10.460
0.05
46.12
C

ATOM
2021
CD
LYS
C3029
26.810
5.310
9.907
0.05
46.11
C

ATOM
2022
CB
LYS
C3029
28.065
5.884
9.269
0.05
46.11
C

ATOM
2023
NZ
LYS
C3029
28.873
6.675
10.238
0.05
46.11
N

ATOM
2024
G
LYS
C3029
24.548
7.709
12.789
1.00
45.54
C

ATOM
2025
O
LYS
C3029
24.739
7.299
13.936
1.00
45.54
O

ATOM
2026
N
ARG
C3030
24.997
8.883
12.361
1.00
44.50
N

ATOM
2027
CA
ARG
C3030
25.747
9.770
13.243
1.00
43.62
C

ATOM
2028
CB
ARG
C3030
26.703
10.650
12.425
1.00
43.71
C

ATOM
2029
CG
ARG
C3030
28.071
10.019
12.194
0.05
43.64
C

ATOM
2030
CD
ARG
C3030
28.410
9.914
10.717
0.05
43.63
C

ATOM
2031
NE
ARG
C3030
28.407
11.214
10.051
0.05
43.58
N

ATOM
2032
CZ
ARG
C3030
28.653
11.389
8.756
0.05
43.55
C

ATOM
2033
NH1
ARG
C3030
28.923
10.347
7.983
0.05
43.53
N

ATOM
2034
NH2
ARG
C3030
28.626
12.608
8.234
0.05
43.55
N

ATOM
2035
C
ARG
C3030
24.819
10.651
14.071
1.00
42.89
C

ATOM
2036
O
ARG
C3030
25.183
11.099
15.158
1.00
42.93
O

ATOM
2037
N
VAL
C3031
23.616
10.885
13.556
1.00
41.77
N

ATOM
2038
CA
VAL
C3031
22.637
11.724
14.237
1.00
40.54
C

ATOM
2039
CB
VAL
C3031
21.761
12.464
13.213
1.00
40.55
C

ATOM
2040
CG1
VAL
C3031
20.717
13.298
13.926
1.00
40.68
C

ATOM
2041
CG2
VAL
C3031
22.631
13.339
12.328
1.00
40.57
C

ATOM
2042
C
VAL
C3031
21.727
10.941
15.180
1.00
39.76
C

ATOM
2043
O
VAL
C3031
21.373
11.418
16.256
1.00
39.22
O

ATOM
2044
N
LEU
C3032
21.353
9.736
14.771
1.00
39.10
N

ATOM
2045
CA
LEU
C3032
20.470
8.905
15.572
1.00
38.53
C

ATOM
2046
CB
LEU
C3032
19.453
8.223
14.656
1.00
38.36
C

ATOM
2047
CG
LEU
C3032
18.612
9.150
13.767
1.00
38.42
C

ATOM
2048
CD1
LEU
C3032
17.671
8.308
12.912
1.00
38.50
C

ATOM
2049
CG2
LEU
C3032
17.819
10.131
14.622
1.00
37.90
C

ATOM
2050
C
LEU
C3032
21.217
7.848
16.378
1.00
38.18
C

ATOM
2051
O
LEU
C3032
22.395
7.585
16.134
1.00
38.41
O

ATOM
2052
N
THR
C3033
20.530
7.263
17.356
1.00
37.76
N

ATOM
2053
CA
THR
C3033
21.105
6.193
18.166
1.00
37.32
C

ATOM
2054
CB
THR
C3033
20.636
6.248
19.638
1.00
37.17
C

ATOM
2055
OCi
THR
C3033
19.233
5.967
19.704
1.00
37.15
O

ATOM
2056
CG2
THR
C3033
20.900
7.612
20.236
1.00
37.54
C

ATOM
2057
C
THR
C3033
20.546
4.918
17.537
1.00
37.05
C

ATOM
2058
O
THR
C3033
19.725
4.992
16.623
1.00
36.86
O

ATOM
2059
N
ALA
C3034
20.976
3.759
18.026
1.00
37.00
N

ATOM
2060
CA
ALA
C3034
20.502
2.481
17.495
1.00
36.98
C

ATOM
2061
CB
ALA
C3034
21.121
1.324
18.279
1.00
36.85
C

ATOM
2062
C
ALA
C3034
18.978
2.384
17.538
1.00
36.93
C

ATOM
2063
O
ALA
C3034
18.331
2.154
16.516
1.00
36.95
O

ATOM
2064
N
LEU
C3035
18.401
2.553
18.721
1.00
37.04
N

ATOM
2065
CA
LEU
C3035
16.951
2.480
18.844
1.00
37.28
C

ATOM
2066
CB
LEU
C3035
16.522
2.844
20.271
1.00
37.10
C

ATOM
2067
CG
LEU
C3035
15.183
2.291
20.770
0.05
37.08
C

ATOM
2068
CD1
LEU
C3035
14.994
2.675
22.229
0.05
37.00
C

ATOM
2069
CG2
LEU
C3035
14.040
2.822
19.922
0.05
37.02
C

ATOM
2070
C
LEU
C3035
16.322
3.442
17.828
1.00
37.52
C

ATOM
2071
O
LEU
C3035
15.418
3.065
17.084
1.00
37.65
O

ATOM
2072
N
GLU
C3036
16.814
4.678
17.790
1.00
37.89
N

ATOM
2073
CA
GLU
C3036
16.299
5.679
16.854
1.00
38.14
C

ATOM
2074
CB
GLU
C3036
17.007
7.031
17.063
1.00
37.82
C

ATOM
2075
CG
GLU
C3036
16.486
7.857
18.244
1.00
37.71
C

ATOM
2076
CD
GLU
C3036
17.305
9.128
18.490
1.00
37.80
C

ATOM
2077
OEl
GLU
C3036
16.865
9.989
19.283
1.00
37.10
O

ATOM
2078
OE2
GLU
C3036
18.397
9.265
17.896
1.00
37.62
O

ATOM
2079
C
GLU
C3036
16.462
5.232
15.398
1.00
38.18
C

ATOM
2080
O
GLU
C3036
15.629
5.551
14.553
1.00
38.25
O

ATOM
2081
N
MET
C3037
17.533
4.499
15.104
1.00
38.56
N

ATOM
2082
CA
MET
C3037
17.769
4.022
13.743
1.00
39.53
C

ATOM
2083
CB
MET
C3037
19.196
3.495
13.591
1.00
40.21
C

ATOM
2084
CG
MET
C3037
20.230
4.576
13.312
1.00
41.61
C

ATOM
2085
SD
MET
C3037
19.932
5.428
11.726
1.00
43.58
S

ATOM
2086
CB
MET
C3037
20.794
4.327
10.578
1.00
42.57
C

ATOM
2087
C
MET
C3037
16.782
2.935
13.337
1.00
39.68
C

ATOM
2088
O
MET
C3037
16.356
2.881
12.186
1.00
39.73
O

ATOM
2089
N
GLU
C3038
16.421
2.072
14.284
1.00
39.82
N

ATOM
2090
CA
GLU
C3038
15.473
0.995
14.012
1.00
39.88
C

ATOM
2091
CB
GLU
C3038
15.205
0.190
15.289
1.00
39.75
C

ATOM
2092
CG
GLU
C3038
16.451
−0.428
15.905
0.05
39.71
C

ATOM
2093
CD
GLU
C3038
16.163
−1.139
17.213
0.05
39.67
C

ATOM
2094
OE1
GLU
C3038
15.344
−2.083
17.210
0.05
39.64
O

ATOM
2095
OE2
GLU
C3038
16.755
−0.755
18.243
0.05
39.61
O

ATOM
2096
C
GLU
C3038
14.175
1.609
13.500
1.00
40.09
C

ATOM
2097
O
GLU
C3038
13.556
1.105
12.559
1.00
40.19
O

ATOM
2098
N
ARG
C3039
13.774
2.709
14.126
1.00
40.05
N

ATOM
2099
CA
ARG
C3039
12.560
3.418
13.744
1.00
40.26
C

ATOM
2100
CB
ARG
C3039
12.230
4.466
14.811
1.00
40.88
C

ATOM
2101
CG
ARG
C3039
11.106
5.425
14.468
1.00
41.43
C

ATOM
2102
CD
ARG
C3039
9.756
4.739
14.377
1.00
42.67
C

ATOM
2103
NE
ARG
C3039
8.673
5.723
14.425
1.00
43.58
N

ATOM
2104
CZ
ARG
C3039
7.394
5.459
14.169
1.00
43.85
C

ATOM
2105
NH1
ARG
C3039
7.007
4.231
13.838
1.00
43.59
N

ATOM
2106
NH2
ARG
C3039
6.498
6.435
14.234
1.00
44.15
N

ATOM
2107
C
ARG
C3039
12.755
4.090
12.384
1.00
39.98
C

ATOM
2108
O
ARG
C3039
11.891
4.009
11.506
1.00
39.45
O

ATOM
2109
N
PHE
C3040
13.901
4.745
12.216
1.00
40.04
N

ATOM
2110
CA
PHE
C3040
14.218
5.440
10.968
1.00
40.26
C

ATOM
2111
CB
PHE
C3040
15.603
6.074
11.061
1.00
40.27
C

ATOM
2112
CG
PHE
C3040
16.022
6.804
9.814
1.00
40.95
C

ATOM
2113
CD1
PHE
C3040
15.431
8.015
9.466
1.00
41.11
C

ATOM
2114
CG2
PHE
C3040
17.013
6.282
8.989
1.00
41.10
C

ATOM
2115
CBl
PHE
C3040
15.822
8.699
8.315
1.00
41.43
C

ATOM
2116
CB2
PHE
C3040
17.412
6.956
7.835
1.00
41.44
C

ATOM
2117
CZ
PHE
C3040
16.815
8.169
7.497
1.00
41.61
C

ATOM
2118
C
PHE
C3040
14.181
4.507
9.756
1.00
40.43
C

ATOM
2119
O
PHE
C3040
13.467
4.757
8.784
1.00
39.60
O

ATOM
2120
N
THR
C3041
14.956
3.429
9.833
1.00
40.82
N

ATOM
2121
CA
THR
C3041
15.043
2.459
8.749
1.00
41.42
C

ATOM
2122
CB
THR
C3041
16.154
1.435
9.018
1.00
41.55
C

ATOM
2123
OG1
THR
C3041
15.782
0.597
10.121
1.00
42.56
O

ATOM
2124
CG2
THR
C3041
17.450
2.149
9.351
1.00
41.22
C

SLAYER

ATOM
2125
C
THR
C3041
13.749
1.702
8.463
1.00
41.42
C

ATOM
2126
O
THR
C3041
13.630
1.072
7.415
1.00
41.80
O

ATOM
2127
N
SER
C3042
12.783
1.757
9.377
1.00
41.30
N

ATOM
2128
CA
SER
C3042
11.521
1.059
9.152
1.00
41.35
C

ATOM
2129
CB
SER
C3042
10.998
0.445
10.454
1.00
41.25
C

ATOM
2130
OG
SER
C3042
10.501
1.442
11.324
1.00
42.03
O

ATOM
2131
C
SER
C3042
10.469
1.996
6.569
1.00
41.30
C

ATOM
2132
0
SER
C3042
9.334
1.589
8.311
1.00
41.45
O

ATOM
2133
N
LEU
C3043
10.850
3.255
8.373
1.00
41.13
N

ATOM
2134
CA
LEU
C3043
9.956
4.262
7.808
1.00
40.94
C

ATOM
2135
CB
LEU
C3043
10.026
5.566
8.618
1.00
40.70
C

ATOM
2136
CG
LEU
C3043
9.382
5.618
10.012
1.00
40.56
C

ATOM
2137
COl
LEU
C3043
9.835
6.871
10.735
1.00
40.07
C

ATOM
2138
CG2
LEU
C3043
7.859
5.586
9.891
1.00
40.06
.
C

ATOM
2139
C
LEU
C3043
10.398
4.528
6.375
1.00
41.07
C

ATOM
2140
0
LEU
C3043
11.494
4.128
5.978
1.00
40.93
O

ATOM
2141
N
LYS
C3044
9.550
5.203
5.604
1.00
41.26
N

ATOM
2142
CA
LYS
C3044
9.871
5.513
4.214
1.00
41.42
C

ATOM
2143
CB
LYS
C3044
9.481
4.346
3.307
1.00
42.49
C

ATOM
2144
CG
LYS
C3044
1.982
4.199
3.107
1.00
43.64
C

ATOM
2145
CD
LYS
C3044
7.678
3.191
2.012
1.00
45.17
C

ATOM
2146
CB
LYS
C3044
6.206
3.228
1.616
1.00
45.99
C

ATOM
2147
NZ
LYS
C3044
5.900
2.249
0.535
1.00
47.05
N

ATOM
2148
G
LYS
C3044
9.147
6.768
3.739
1.00
40.92
C

ATOM
2149
0
LYS
C3044
8.191
7.219
4.365
1.00
40.90
O

ATOM
2150
N
GLY
C3045
9.605
7.820
2.621
1.00
40.22
N

ATOM
2151
CA
GLY
C3045
8.986
8.510
2.072
1.00
39.26
C

ATOM
2152
C
GLY
C3045
9.182
9.736
2.937
1.00
38.68
C

ATOM
2153
0
GLY
C3045
10.142
9.829
3.694
1.00
38.24
0

ATOM
2154
N
ARG
C3046
8.260
10.683
2.818
1.00
38.56
N

ATOM
2155
CA
ARG
C3046
8.318
11.921
3.589
1.00
38.49
C

ATOM
2156
CB
ARG
C3046
7.107
12.793
3.251
1.00
38.44
C

ATOM
2157
CG
ARG
C3046
7.104
14.158
3.912
0.05
38.46
C

ATOM
2158
CD
ARG
C3046
5.887
14.963
3.483
0.05
38.40
C

ATOM
2159
NE
ARG
C3046
5.874
15.200
2.042
0.05
38.36
N

ATOM
2160
CZ
ARG
C3046
4.887
15.809
1.393
0.05
38.32
C

ATOM
2161
NH1
ARG
C3046
4.963
15.982
0.081
0.05
38.29
N

ATOM
2162
NH2
ARG
C3046
3.822
16.241
2.055
0.05
38.31
N

ATOM
2163
C
ARG
C3046
8.372
11.647
5.093
1.00
38.25
C

ATOM
2164
0
ARG
C3046
9.027
12.365
5.830
1.00
38.13
O

ATOM
2165
N
ARG
C3047
7.696
10.595
5.538
1.00
38.32
N

ATOM
2166
CA
ARG
C3047
7.673
10.234
6.953
1.00
38.52
C

ATOM
2167
CB
ARG
C3047
6.727
9.051
7.169
1.00
39.67
C

ATOM
2168
CG
ARG
C3047
5.251
9.432
7.225
1.00
41.67
C

ATOM
2169
CD
ARG
C3047
4.369
8.277
6.767
1.00
43.70
C

ATOM
2170
NE
ARG
C3047
3.141
8.152
7.550
1.00
45.24
N

ATOM
2171
CZ
ARG
C3047
3.112
7.824
8.840
1.00
46.12
C

ATOM
2172
NH1
ARG
C3047
4.248
7.589
9.495
1.00
46.08
N

ATOM
2173
NH2
ARG
C3047
1.947
7.722
9.474
1.00
45.94
N

ATOM
2174
C
ARG
C3047
9.042
9.906
7.554
1.00
38.04
C

ATOM
2175
0
ARG
C3047
9.287
−10.174
8.731
1.00
37.75
O

ATOM
2176
N
GLN
C3048
9.931
9.820
6.757
1.00
37.49
N

ATOM
2177
CA
GLN
C3048
11.258
8.966
7.251
1.00
36.91
C

ATOM
2178
CB
GLN
C3048
11.912
7.919
6.349
1.00
36.94
C

ATOM
2179
CG
GLN
C3048
13.283
7.496
6.849
1.00
37.10
C

ATOM
2180
CD
GLN
C3048
14.092
6.744
5.813
1.00
37.40
C

ATOM
2181
OE1
GLN
C3048
14.233
7.196
4.680
1.00
37.42
O

ATOM
2182
NE2
GLN
C3048
14.643
5.600
6.202
1.00
37.18
N

ATOM
2183
C
GLN
C3048
12.186
10.176
7.367
1.00
36.61
C

ATOM
2184
0
GLN
C3048
12.971
10.284
8.315
1.00
36.44
O

ATOM
2185
N
ILE
C3049
12.101
11.082
6.403
1.00
35.91
N

ATOM
2186
CA
ILE
U3049
12.932
12.271
6.429
1.00
35.80
C

ATOM
2187
CB
ILE
U3049
12.906
12.991
5.054
1.00
36.41
C

ATOM
2188
CG2
ILE
U3049
11.482
13.209
4.607
1.00
37.11
C

ATOM
2189
001
ILE
U3049
13.678
14.307
5.136
1.00
36.64
C

ATOM
2190
CD1
ILE
U3049
15.150
14.108
5.433
1.00
37.22
C

ATOM
2191
C
ILE
U3049
12.436
13.201
7.542
1.00
35.41
C

ATOM
2192
0
ILE
U3049
13.231
13.824
8.254
1.00
35.47
O

ATOM
2193
N
GLU
C3050
11.119
13.280
7.707
1.00
34.48
N

ATOM
2194
CA
GLU
C3050
10.546
14.118
8.756
1.00
33.55
C

ATOM
2195
CB
GLU
C3050
9.023
14.074
8.699
1.00
34.18
C

ATOM
2196
CO
GLU
C3050
8.471
14.609
7.410
1.00
36.22
C

ATOM
2197
CD
GLU
C3050
7.005
14.309
7.242
1.00
37.41
C

ATOM
2198
OE1
GLU
C3050
6.543
13.291
7.807
1.00
38.55
O

ATOM
2199
OE2
GLU
C3050
6.318
15.078
6.531
1.00
37.87
O

ATOM
2200
C
GLU
C3050
11.018
13.620
10.116
1.00
32.30
C

ATOM
2201
0
GLU
C3050
11.275
14.412
11.023
1.00
31.96
O

ATOM
2202
N
TYR
C3051
11.130
12.303
10.251
1.00
30.44
N

ATOM
2203
CA
TYR
C3051
11.574
11.715
11.501
1.00
29.38
C

ATOM
2204
CB
TYR
C3051
11.438
10.191
11.433
1.00
28.33
C

ATOM
2205
CG
TYR
C3051
11.936
9.478
12.675
1.00
27.96
C

ATOM
2206
CD1
TYR
C3051
13.234
8.964
12.741
1.00
27.15
C

ATOM
2207
CE1
TYR
C3051
13.712
8.371
13.904
1.00
26.96
C

ATOM
2208
CG2
TYR
C3051
11.127
9.373
13.809
1.00
27.47
C

ATOM
2209
CB2
TYR
C3051
11.593
8.788
14.967
1.00
27.13
C

ATOM
2210
CZ
TYR
03051
12.885
8.290
15.014
1.00
27.21
C

ATOM
2211
OH
TYR
C3051
13.344
7.735
16.187
1.00
27.00
O

ATOM
2212
C
TYR
03051
13.019
12.117
11.818
1.00
29.01
C

ATOM
2213
0
TYR
C3051
13.342
12.486
12.946
1.00
28.83
0

ATOM
2214
N
LEU
C3052
13.886
12.063
10.812
1.00
28.73
N

ATOM
2215
CA
LEU
C3052
15.287
12.417
11.009
1.00
28.07
C

ATOM
2216
CB
LEU
C3052
16.105
12.059
9.761
1.00
27.77
C

ATOM
2217
CO
LEU
C3052
17.603
12.372
9.816
1.00
28.06
C

ATOM
2218
CD1
LEU
C3052
18.267
11.639
10.972
1.00
28.26
C

ATOM
2219
CG2
LEU
C3052
18.241
11.957
8.516
1.00
28.46
C

ATOM
2220
C
LEU
C3052
15.419
13.909
11.311
1.00
27.59
C

ATOM
2221
O
LEU
C3052
16.156
14.309
12.217
1.00
26.99
O

ATOM
2222
N
ALA
C3053
14.704
14.727
10.544
1.00
27.06
N

ATOM
2223
CA
ALA
C3053
14.743
16.168
10.738
1.00
26.76
C

ATOM
2224
GB
ALA
03053
13.898
16.852
9.691
1.00
26.56
C

ATOM
2225
C
ALA
03053
14.223
16.489
12.134
1.00
26.71
C

ATOM
2226
O
ALA
C3053
14.802
17.298
12.854
1.00
26.43
O

ATOM
2227
N
GLY
C3054
13.130
15.831
12.510
1.00
26.77
N

ATOM
2228
CA
GLY
C3054
12.541
16.043
13.815
1.00
26.67
C

ATOM
2229
C
GLY
C3054
13.512
15.753
14.934
1.00
26.53
C

ATOM
2230
0
GLY
C3054
13.611
16.521
15.882
1.00
26.44
O

ATOM
2231
N
ARG
C3055
14.231
14.643
14.836
1.00
26.68
N

ATOM
2232
CA
ARG
C3055
15.198
−14.290
15.870
1.00
26.82
C

ATOM
2233
GB
ARG
C3055
15.705
12.868
15.666
1.00
26.65
C

ATOM
2234
GO
ARG
C3055
14.968
11.843
16.498
1.00
26.91
C

ATOM
2235
CD
ARG
C3055
13.458
11.922
16.298
1.00
27.49
C

ATOM
2236
NE
ARG
C3055
12.759
11.110
17.292
1.00
27.69
N

ATOM
2237
CZ
ARG
03055
11.442
11.086
17.454
1.00
27.76
C

ATOM
2238
NH1
ARG
C3055
10.662
11.831
16.685
1.00
27.51
N

ATOM
2239
NH2
ARG
03055
10.906
10.324
18.398
1.00
28.13
N

ATOM
2240
C
ARG
C3055
16.360
15.260
15.869
1.00
26.96
C

ATOM
2241
0
ARG
C3055
16.834
15.667
16.928
1.00
26.54
O

ATOM
2242
N
TRP
C3056
16.816
15.631
14.676
1.00
27.71
N

ATOM
2243
CA
TRP
C3056
17.917
16.575
14.556
1.00
28.70
C

ATOM
2244
CB
TRP
C3056
18.247
16.837
13.082
1.00
30.14
C

ATOM
2245
CG
TRP
C3056
19.074
18.069
12.881
1.00
32.25
C

ATOM
2246
CG2
TRP
C3056
20.495
18.129
12.703
1.00
33.03
C

ATOM
2247
CB2
TRP
C3056
20.854
19.497
12.662
1.00
33.33
C

ATOM
2248
CB3
TRP
C3056
21.500
17.163
12.579
1.00
33.56
C

ATOM
2249
COl
TRP
C3056
18.639
19.370
12.930
1.00
32.92
C

ATOM
2250
NEl
TRP
C3056
19.704
20.230
12.803
1.00
33.50
N

ATOM
2251
CZ2
TRP
C3056
22.175
19.920
12.505
1.00
33.41
C

ATOM
2252
CZ3
TRP
C3056
22.818
17.587
12.422
1.00
33.92
C

ATOM
2253
CH2
TRP
C3056
23.141
18.954
12.367
1.00
33.82
C

ATOM
2254
C
TRFKC3OS6
17.498
17.875
15.230
1.00
28.10
C

ATOM
2255
0
TRP
C3056
18.144
18.357
16.163
1.00
27.48
O

ATOM
2256
N
SER
C3057
16.397
18.429
14.749
1.00
27.65
N

ATOM
2257
CA
SER
C3057
15.868
19.667
15.288
1.00
27.54
C

ATOM
2258
CB
SER
C3057
14.513
19.959
14.654
1.00
27.86
C

ATOM
2259
OG
SER
C3057
14.233
21.344
14.718
1.00
29.93
O

ATOM
2260
C
SER
C3057
15.731
19.622
16.812
1.00
26.85
C

ATOM
2261
0
SER
C3057
16.059
20.588
17.503
1.00
27.24
O

ATOM
2262
N
ALA
C3058
15.257
18.501
17.340
1.00
25.77
N

ATOM
2263
CA
ALA
C3058
15.080
18.369
18.780
1.00
25.50
C

ATOM
2264
CB
ALA
C3058
14.334
17.077
19.094
1.00
25.02
C

ATOM
2265
C
ALA
C3058
16.411
18.409
19.546
1.00
25.26
C

ATOM
2266
0
ALA
C3058
16.513
19.024
20.607
1.00
24.25
O

ATOM
2267
N
LYS
C3059
17.430
17.752
19.000
1.00
25.32
N

ATOM
2268
CA
LYS
C3059
18.736
17.704
19.646
1.00
25.14
C

ATOM
2269
CB
LYS
C3059
19.568
16.577
19.035
1.00
24.87
C

ATOM
2270
CG
LYS
C3059
18.928
15.218
19.254
1.00
24.63
C

ATOM
2271
CD
LYS
C3059
19.667
14.091
18.570
1.00
24.80
C

ATOM
2272
CB
LYS
C3059
18.998
12.746
18.869
1.00
24.92
C

ATOM
2273
NZ
LYS
C3059
19.674
11.614
18.185
1.00
24.83
N

ATOM
2274
G
LYS
C3059
19.466
19.033
19.547
1.00
25.56
C

ATOM
2275
0
LYS
C3059
20.262
19.388
20.415
1.00
25.33
O

ATOM
2276
N
GLU
C3060
19.183
19.784
18.493
1.00
26.00
N

ATOM
2277
CA
GLU
C3060
19.818
21.076
18.326
1.00
26.76
C

ATOM
2278
CB
GLU
C3060
19.568
21.618
16.919
1.00
28.10
C

ATOM
2279
CG
GLU
C3060
20.545
22.717
16.530
1.00
31.38
C

ATOM
2280
CD
GLU
C3060
22.005
22.278
16.691
1.00
33.19
C

ATOM
2281
OEI
GLU
C3060
22.444
21.369
15.947
1.00
33.60
O

ATOM
2282
OE2
GLU
C3060
22.709
22.839
17.569
1.00
34.17
O

ATOM
2283
C
GLU
C3060
19.243
22.023
19.377
1.00
26.31
C

ATOM
2284
0
GLU
C3060
19.985
22.698
20.089
1.00
25.94
O

ATOM
2285
N
ALA
C3061
17.914
22.048
19.477
1.00
25.95
N

ATOM
2286
CA
ALA
C3061
17.221
22.899
20.442
1.00
25.01
C

ATOM
2287
CB
ALA
C3061
15.712
22.700
20.342
1.00
24.05
C

ATOM
2288
C
ALA
C3061
17.696
22.562
21.846
1.00
24.62
C

ATOM
2289
0
ALA
C3061
17.925
23.457
22.663
1.00
24.28
O

ATOM
2290
N
PE−LE C3062
17.837
21.271
22.129
1.00
24.17
N

ATOM
2291
CA
PHE
C3062
18.301
20.850
23.440
1.00
24.63
C

ATOM
2292
CB
PHE
C3062
18.224
19.321
23.605
1.00
24.68
C

ATOM
2293
CG
PHE
C3062
18.875
18.828
24.871
1.00
24.04
C

ATOM
2294
CD1
PHE
C3062
20.238
18.538
24.900
1.00
24.34
C

ATOM
2295
CG2
PHE
C3062
18.152
18.756
26.053
1.00
23.91
C

ATOM
2296
CBl
PHE
C3062
20.872
18.189
26.093
1.00
24.30
C

ATOM
2297
CB2
PHE
C3062
18.774
18.411
27.255
1.00
24.14
C

ATOM
2298
CZ
PHE
C3062
20.139
18.128
27.274
1.00
24.07
C

ATOM
2299
C
PHE
C3062
19.732
21.316
23.701
1.00
24.85
C

ATOM
2300
0
PHE
C3062
20.054
21.744
24.804
.1.00
24.51
O

ATOM
2301
N
SER
C3063
20.589
21.219
22.689
1.00
25.44
N

ATOM
2302
CA
SER
C3063
21.976
21.650
22.933
1.00
26.48
C

ATOM
2303
CB
SER
C3063
22.777
21.312
21.576
1.00
26.81
C

ATOM
2304
OG
SER
C3063
22.872
19.910
21.403
1.00
28.20
O

ATOM
2305
C
SER
C3063
22.059
23.149
23.082
1.00
26.77
C

ATOM
2306
0
SER
C3063
22.891
23.614
23.859
1.00
26.78
O

ATOM
2307
N
LYS
C3064
21.194
23.902
22.416
1.00
26.78
N

ATOM
2308
CA
LYS
C3064
21.188
25.342
22.565
1.00
27.25
C

ATOM
2309
CB
LYS
C3064
20.379
25.973
21.431
1.00
26.90
C

ATOM
2310
CG
LYS
C3064
20.971
25.696
20.059
1.00
26.47
C

ATOM
2311
CD
LYS
C3064
20.066
26.159
18.938
1.00
26.20
C

ATOM
2312
CB
LYS
C3064
19.799
27.664
18.988
1.00
26.50
C

ATOM
2313
NZ
LYS
C3064
18.996
28.088
17.806
1.00
26.49
N

ATOM
2314
G
LYS
C3064
20.616
25.718
23.923
1.00
28.08
C

ATOM
2315
0
LYS
C3064
20.987
26.738
24.500
1.00
27.79
O

ATOM
2316
N
ALA
C3065
19.717
24.882
24.433
1.00
29.11
N

ATOM
2317
CA
ALA
C3065
19.111
25.124
25.735
1.00
30.40
C

ATOM
2318
CB
ALA
C3065
17.957
24.163
25.968
1.00
29.37
C

ATOM
2319
C
ALA
C3065
20.179
24.932
26.804
1.00
31.79
C

ATOM
2320
O
ALA
C3065
20.228
25.668
27.786
1.00
31.85
O

ATOM
2321
N
MET
C3066
21.035
23.939
26.595
1.00
33.85
N

ATOM
2322
CA
MET
C3066
22.114
23.628
27.524
1.00
36.16
C

ATOM
2323
CB
MET
C3066
22.666
22.232
27.242
1.00
36.40
C

ATOM
2324
CG
MET
C3066
21.804
21.097
27.752
1.00
37.31
C

ATOM
2325
SD
MET
C3066
21.824
20.993
29.551
1.00
38.61
S

ATOM
2326
CB
MET
C3066
23.502
20.468
29.811
1.00
38.12
C

ATOM
2327
C
MET
C3066
23.247
24.638
27.413
1.00
37.57
C

ATOM
2328
0
MET
C3066
23.958
24.893
28.379
1.00
37.83
O

ATOM
2329
N
GLY
C3067
23.411
25.209
26.226
1.00
39.17
N

ATOM
2330
CA
GLY
C3067
24.470
26.177
26.024
1.00
41.14
C

ATOM
2331
C
GLY
C3067
25.772
25.475
25.697
1.00
42.59
C

ATOM
2332
0
GLY
C3067
26.831
25.822
26.226
1.00
42.74
O

ATOM
2333
N
THR
C3068
25.687
24.476
24.825
1.00
43.64
N

ATOM
2334
CA
THR
C3068
26.853
23.710
24.418
1.00
44.94
C

ATOM
2335
CB
THR
C3068
26.723
22.243
24.877
1.00
45.62
C

ATOM
2336
OGi
THR
C3068
27.927
21.529
24.559
1.00
46.68
O

ATOM
2337
CG2
THR
C3068
25.539
21.572
24.188
1.00
45.83
C

ATOM
2338
C
THR
C3068
26.994
23.755
22.898
1.00
45.32
C

ATOM
2339
0
THR
C3068
26.027
24.200
22.242
1.00
45.93
O

ATOM
2340
OXT
THR
C3068
28.057
23.348
22.377
1.00
45.68
O

TER
2341
THR

C3068

ATOM
2342
C
GLY
C3074
25.582
13.730
21.033
1.00
50.05
C

ATOM
2343
0
GLY
C3074
24.831
13.333
21.925
1.00
50.04
O

ATOM
2344
N
GLY
C3074
27.008
15.502
22.091
1.00
50.49
N

ATOM
2345
CA
GLY
C3074
26.990
14.201
21.354
1.00
50.33
C

ATOM
2346
N
PHE
C3075
25.218
13.780
19.755
1.00
49.73
N

ATOM
2347
CA
PHE
C3075
23.894
13.345
19.328
1.00
49.39
C

ATOM
2348
CB
PHE
C3075
23.740
13.548
17.818
1.00
49.61
C

ATOM
2349
CG
PHE
C3075
23.196
14.902
17.447
1.00
50.02
C

ATOM
2350
COl
PHE
C3075
23.555
16.036
18.178
1.00
50.35
C

ATOM
2351
CG2
PHE
C3075
22.316
15.045
16.382
1.00
50.13
C

ATOM
2352
CBl
PHE
C3075
23.040
17.294
17.854
1.00
50.43
C

ATOM
2353
CB2
PHE
C3075
21.794
16.297
16.047
1.00
50.56
C

ATOM
2354
CZ
PHE
C3075
22.156
17.424
16.784
1.00
50.60
C

ATOM
2355
C
PHE
C3075
23.644
11.894
19.710
1.00
48.79
C

ATOM
2356
O
PHE
C3075
22.530
11.528
20.073
1.00
48.53
O

ATOM
2357
N
GLN
C3076
24.694
11.082
19.642
1.00
48.39
N

ATOM
2358
CA
GLN
C3076
24.602
9.671
19.998
1.00
47.89
C

ATOM
2359
CB
GLN
C3076
25.905
8.944
19.643
1.00
48.47
C

ATOM
2360
CG
GLN
C3076
26.287
9.049
18.175
1.00
49.29
C

ATOM
2361
CD
GLN
C3076
25.242
8.441
17.260
1.00
49.81
C

ATOM
2362
OE1
GLN
C3076
25.206
8.731
16.065
1.00
50.75
O

ATOM
2363
NE2
GLN
C3076
24.391
7.584
17.815
1.00
49.76
N

ATOM
2364
C
GLN
C3076
24.351
9.560
21.492
1.00
47.10
C

ATOM
2365
0
GLN
C3076
24.003
8.493
22.000
1.00
47.45
O

ATOM
2366
N
ASP
C3077
24.533
10.676
22.190
1.00
45.97
N

ATOM
2367
CA
ASP
C3077
24.331
10.727
23.631
1.00
44.90
C

ATOM
2368
CB
ASP
C3077
25.397
11.612
24.271
1.00
46.44
C

ATOM
2369
CG
ASP
C3077
26.800
11.083
24.036
1.00
47.82
C

ATOM
2370
001
ASP
C3077
27.081
9.951
24.499
1.00
48.20
O

ATOM
2371
002
ASP
C3077
27.610
11.794
23.388
1.00
48.48
O

ATOM
2372
C
ASP
C3077
22.950
11.252
23.975
1.00
43.23
C

ATOM
2373
0
ASP
C3077
22.557
11.280
25.140
1.00
43.47
O

ATOM
2374
N
LEU
C3078
22.219
11.675
22.950
1.00
41.15
N

ATOM
2375
CA
LEU
C3078
20.869
12.193
23.129
1.00
38.63
C

ATOM
2376
CB
LELJ C3078
20.754
13.610
22.558
1.00
38.12
C

ATOM
2377
CG
LEU
C3078
21.787
14.645
23.005
1.00
37.91
C

ATOM
2378
COl
LEU
C3078
21.511
15.974
22.313
1.00
37.65
C

ATOM
2379
CG2
LEU
C3078
21.735
14.801
24.508
1.00
37.75
C

ATOM
2380
C
LEU
C3078
19.921
11.272
22.376
1.00
36.97
C

ATOM
2381
0
LEU
C3078
20.225
10.833
21.269
1.00
36.76
O

ATOM
2382
N
GLU
C3079
18.778
10.974
22.979
1.00
34.99
N

ATOM
2383
CA
GLU
C3079
17.793
10.112
22.338
1.00
33.02
C

ATOM
2384
CB
GLU
C3079
17.937
8.676
22.842
1.00
33.31
C

ATOM
2385
CO
GLU
C3079
16.818
7.753
22.412
1.00
34.12
C

ATOM
2386
CD
GLU
C3079
17.129
6.298
22.691
1.00
34.85
C

ATOM
2387
OE1
GLU
C3079
17.897
5.701
21.908
1.00
34.18
O

ATOM
2388
OE2
GLU
C3079
16.616
5.754
23.699
1.00
35.70
O

ATOM
2389
C
GLU
C3079
16.365
10.598
22.566
1.00
31.51
C

ATOM
2390
0
GLU
C3079
15.955
10.880
23.695
1.00
31.00
O

ATOM
2391
N
VAL
C3080
15.618
10.707
21.474
1.00
29.65
N

ATOM
2392
CA
VAL
C3080
14.237
11.135
21.542
1.00
28.33
C

ATOM
2393
CB
VAL
C3080
13.987
12.401
20.698
1.00
28.04
C

ATOM
2394
CG1
VAL
C3080
12.497
12.701
20.643
1.00
27.55
C

ATOM
2395
CG2
VAL
C3080
14.739
13.576
21.289
1.00
27.56
C

ATOM
2396
C
VAL
C3080
13.373
10.014
21.007
1.00
28.05
C

ATOM
2397
0
VAL
C3080
13.518
9.600
19.858
1.00
27.43
O

ATOM
2398
N
LEU
C3081
12.482
9.513
21.853
1.00
27.62
N

ATOM
2399
CA
LEU
C3081
11.578
8.445
21.455
1.00
27.82
C

ATOM
2400
CB
LEU
C3081
11.724
7.235
22.391
1.00
27.48
C

ATOM
2401
CG
LEU
C3081
13.107
6.575
22.533
1.00
27.65
C

ATOM
2402
CD1
LEU
C3081
13.069
5.544
23.648
1.00
26.80
C

ATOM
2403
CG2
LEU
C3081
13.534
5.928
21.223
1.00
26.81
C

ATOM
2404
C
LEU
C3081
10.160
9.000
21.528
1.00
27.94
C

ATOM
2405
0
LEU
C3081
9.965
10.194
21.744
1.00
27.66
O

ATOM
2406
N
ASN
C3082
9.177
8.128
21.340
1.00
28.22
N

ATOM
2407
CA
ASN
C3082
7.775
8.523
21.400
1.00
28.52
C

ATOM
2408
CB
ASN
C3082
7.111
8.355
20.024
1.00
28.54
C

ATOM
2409
CO
ASN
C3082
7.584
9.382
19.021
1.00
28.73
C

ATOM
2410
001
ASN
C3082
7.295
10.569
19.148
1.00
29.62
O

ATOM
2411
ND2
ASN
C3082
8.321
8.932
18.020
1.00
29.32
N

ATOM
2412
C
ASN
C3082
7.053
7.647
22.422
1.00
28.28
C

ATOM
2413
O
ASN
C3082
7.199
6.421
22.407
1.00
28.06
O

ATOM
2414
N
ASN
C3083
6.280
8.274
23.308
1.00
27.85
N

ATOM
2415
CA
ASN
C3083
5.537
7.520
24.304
1.00
27.66
C

ATOM
2416
CB
ASM C3083
5.183
8.398
25.515
1.00
27.64
C

ATOM
2417
CG
ASN
C3083
4.203
9.527
25.189
1.00
27.67
C

ATOM
2418
ODi
ASN
C3083
3.949
10.384
26.033
1.00
28.51
O

ATOM
2419
ND2
ASN
C3083
3.648
9.527
23.986
1.00
27.19
N

ATOM
2420
C
ASN
C3083
4.287
6.942
23.664
1.00
27.84
C

ATOM
2421
0
ASN
C3083
3.988
7.233
22.501
1.00
27.10
O

ATOM
2422
N
GLU
C3084
3.564
6.120
24.419
1.00
28.22
N

ATOM
2423
CA
GLU
C3084
2.354
5.483
23.910
1.00
28.64
C

ATOM
2424
CB
GLU
C3084
1.655
4.679
25.018
1.00
29.96
C

ATOM
2425
CG
GLU
C3084
1.146
5.509
26.187
1.00
31.56
C

ATOM
2426
CD
GLU
C3084
2.225
5.820
27.210
1.00
33.17
C

ATOM
2427
OE1
GLU
C3084
3.404
5.994
26.821
1.00
33.53
O

ATOM
2428
OE2
GLU
C3084
1.888
5.903
28.411
1.00
34.64
O

ATOM
2429
C
GLU
C3084
1.367
6.471
23.291
1.00
28.20
C

ATOM
2430
0
GLU
C3084
0.559
6.092
22.446
1.00
28.01
O

ATOM
2431
N
ARG
C3085
1.435
7.734
23.702
1.00
27.98
N

ATOM
2432
CA
ARG
C3085
0.526
8.745
23.165
1.00
27.80
C

ATOM
2433
CB
ARG
C3085
0.270
9.847
24.201
1.00
28.19
C

ATOM
2434
CG
ARG
C3085
−0.474
9.355
25.427
1.00
29.28
C

ATOM
2435
CD
ARG
C3085
−1.296
10.454
26.109
1.00
30.50
C

ATOM
2436
NE
ARG
C3085
−2.245
9.862
27.052
1.00
31.26
N

ATOM
2437
CZ
ARG
C3085
−1.872
9.221
28.153
1.00
32.48
C

ATOM
2438
N
111
ARG
C3085
−0.581
9.110
28.437
1.00
33.70
N

ATOM
2439
NH2
ARG
C3085
−2.770
8.663
28.954
1.00
33.05
N

ATOM
2440
C
ARG
C3085
1.021
9.369
21.863
1.00
27.34
C

ATOM
2441
0
ARG
C3085
0.310
10.158
21.244
1.00
27.35
O

ATOM
2442
N
CL? C3086
2.237
9.016
21.454
1.00
26.82
N

ATOM
2443
CA
GLY
C3086
2.788
9.545
20.218
1.00
25.87
C

ATOM
2444
C
GLY
C3086
3.607
10.808
20.384
1.00
25.74
C

ATOM
2445
0
GLY
C3086
4.109
11.370
19.401
1.00
25.82
O

ATOM
2446
N
ALA
C3087
3.753
11.254
21.626
1.00
24.95
N

ATOM
2447
CA
ALA
C3087
4.508
12.461
21.920
1.00
24.57
C

ATOM
2448
CB
ALA
C3087
3.933
13.147
23.155
1.00
24.64
C

ATOM
2449
C
ALA
C3087
5.991
12.183
22.130
1.00
24.46
C

ATOM
2450
0
ALA
C3087
6.372
11.277
22.878
1.00
24.54
O

ATOM
2451
N
PRO

C3088
6.851
12.964
21.461
1.00
24.09
N

ATOM
2452
CD
PRO

C3088
6.501
14.011
20.482
1.00
23.71
C

ATOM
2453
CA
PRO

C3088
8.306
12.815
21.572
1.00
23.76
C

ATOM
2454
CB
PRO

C3088
8.825
13.714
20.451
1.00
23.93
C

ATOM
2455
CG
PRO

C3088
7.781
14.816
20.403
1.00
23.82
C

ATOM
2456
C
PRO

C3088
8.799
13.249
22.952
1.00
23.43
C

ATOM
2457
0
PRO

C3088
8.162
14.066
23.610
1.00
23.03
O

ATOM
2458
N
TYR
C3089
9.925
12.692
23.391
1.00
23.74
N

ATOM
2459
CA
TYR
C3089
10.496
13.028
24.698
1.00
24.43
C

ATOM
2460
CB
TYR
C3089
9.671
−12.400
25.834
1.00
24.30
C

ATOM
2461
CG
TYR
C3089
9.843
10.904
25.973
1.00
24.64
C

ATOM
2462
COl
TYR
C3089
10.832
10.363
26.804
1.00
24.62
C

ATOM
2463
CE1
TYR
C3089
11.008
8.978
26.911
1.00
24.92
C

ATOM
2464
CG2
TYR
C3089
9.033
10.027
25.256
1.00
24.84
C

ATOM
2465
CB2
TYR
C3089
9.199
8.643
25.352
1.00
25.43
C

ATOM
2466
CZ
TYR
C3089
10.187
8.125
26.178
1.00
25.32
C

ATOM
2467
OH
TYR
C3089
10.353
6.761
26.236
1.00
25.52
O

ATOM
2468
C
TYR
C3089
11.925
12.521
24.772
1.00
24.85
C

ATOM
2469
0
TYR
C3089
12.279
11.552
24.103
1.00
25.10
O

ATOM
2470
N
PHE
C3090
12.750
13.171
25.584
1.00
25.52
N

ATOM
2471
CA
PHE
C3090
14.135
12.742
25.714
1.00
26.19
C

ATOM
2472
GB
PHE
C3090
15.038
13.901
26.156
1.00
26.18
C

ATOM
2473
CG
PHE
C3090
15.387
14.852
25.051
1.00
26.76
C

ATOM
2474
CD1
PHE
C3090
14.541
15.912
24.725
1.00
27.13
C

ATOM
2475
CG2
PHE
C3090
16.554
14.675
24.311
1.00
27.22
C

ATOM
2476
CBl
PHE
C3090
14.851
16.792
23.675
1.00
27.19
C

ATOM
2477
CB2
PHE
C3090
16.882
15.548
23.253
1.00
27.68
C

ATOM
2478
CZ
PHE
C3090
16.025
16.608
22.936
1.00
27.50
C

ATOM
2479
C
PHE
C3090
14.277
11.595
26.693
1.00
26.31
C

ATOM
2480
0
PHE
C3090
14.076
11.767
27.895
1.00
27.02
O

ATOM
2481
N
SER
C3091
14.616
10.423
26.169
1.00
26.64
N

ATOM
2482
CA
SER
C3091
14.818
9.237
26.994
1.00
27.16
C

ATOM
2483
GB
SER
C3091
14.549
7.964
26.185
1.00
26.45
C

ATOM
2484
OG
SER
C3091
15.280
7.970
24.974
1.00
27.09
O

ATOM
2485
C
SER
C3091
16.256
9.235
27.513
1.00
27.57
C

ATOM
2486
0
SER
C3091
16.594
8.485
28.424
1.00
27.76
O

ATOM
2487
N
GLN
C3092
17.095
10.086
26.928
1.00
28.18
N

ATOM
2488
CA
GLN
C3092
18.490
10.199
27.340
1.00
29.06
C

ATOM
2489
GB
GLN
C3092
19.355
9.181
26.595
1.00
30.20
C

ATOM
2490
CG
GLN
C3092
20.843
9.363
26.840
1.00
31.72
C

ATOM
2491
CD
GLN
C3092
21.280
8.873
28.211
1.00
32.79
C

ATOM
2492
OE1
GLN
C3092
21.336
7.667
28.461
1.00
33.66
O

ATOM
2493
NE2
GLN
C3092
21.590
9.805
29.105
1.00
33.12
N

ATOM
2494
C
GLN
C3092
19.021
11.601
27.069
1.00
28.89
C

ATOM
2495
0
GLN
C3092
18.889
12.118
25.954
1.00
29.04
O

ATOM
2496
N
ALA
C3093
19.630
12.207
28.088
1.00
28.63
N

ATOM
2497
CA
ALA
C3093
20.179
13.556
27.963
1.00
28.35
C

ATOM
2498
GB
ALA
C3093
19.040
14.565
27.805
1.00
28.23
C

ATOM
2499
C
ALA
C3093
21.047
13.945
29.159
1.00
28.01
C

ATOM
2500
0
ALA
C3093
20.721
13.635
30.307
1.00
28.15
O

ATOM
2501
N
PRO

C3094
22.167
14.640
28.905
1.00
27.81
N

ATOM
2502
CD
PRO

C3094
22.702
15.035
27.590
1.00
27.69
C

ATOM
2503
CA
PRO

C3094
23.066
15.067
29.984
1.00
27.41
C

ATOM
2504
GB
PRO

C3094
24.271
15.625
29.226
1.00
27.35
C

ATOM
2505
CG
PRO

C3094
23.658
16.148
27.960
1.00
27.34
C

ATOM
2506
C
PRO

C3094
22.409
16.108
30.883
1.00
27.24
C

ATOM
2507
0
PRO

C3094
22.992
17.150
31.172
1.00
27.73
O

ATOM
2508
N
PHE
C3095
21.195
15.820
31.330
1.00
26.89
N

ATOM
2509
CA
PHE
. C3095
20.457
16.740
32.182
1.00
26.88
C

ATOM
2510
GB
PHE
C3095
19.603
17.680
31.314
1.00
26.34
C

ATOM
2511
CO
PHE
C3095
18.986
18.820
32.081
1.00
25.69
C

ATOM
2512
COl
PHE
C3095
19.789
19.707
32.796
1.00
24.82
C

ATOM
2513
CG2
PHE
C3095
17.606
18.973
32.133
1.00
24.80
C

ATOM
2514
GEl
PHE
C3095
19.224
20.722
33.556
1.00
24.83
C

ATOM
2515
CB2
PHE
C3095
17.031
19.985
32.890
1.00
24.99
C

ATOM
2516
CZ
PHE
C3095
17.841
20.862
33.605
1.00
24.98
C

ATOM
2517
C
PHE
G3095
19.569
15.927
33.115
1.00
27.25
C

ATOM
2518
0
PHE
C3095
18.924
14.983
32.684
1.00
28.50
O

ATOM
2519
N
SER
C3096
19.525
16.284
34.390
1.00
27.37
N

ATOM
2520
CA
SER
C3096
18.710
15.530
35.332
1.00
27.95
C

ATOM
2521
GB
SER
C3096
19.542
15.174
36.565
1.00
28.67
C

ATOM
2522
00
SER
C3096
20.425
16.230
36.883
1.00
30.49
O

ATOM
2523
C
SER
C3096
17.403
16.202
35.754
1.00
27.66
C

ATOM
2524
0
SER
C3096
16.663
15.665
36.577
1.00
27.25
O

ATOM
2525
N
GLY
C3097
17.117
17.372
35.192
1.00
26.91
N

ATOM
2526
CA
GLY
C3097
15.874
18.045
35.521
1.00
26.05
C

ATOM
2527
C
GLY
C3097
14.839
17.654
34.488
1.00
25.55
C

ATOM
2528
0
GLY
C3097
15.047
16.696
33.745
1.00
25.35
O

ATOM
2529
N
LYS
C3098
13.729
18.384
34.428
1.00
25.19
N

ATOM
2530
CA
LYS
C3098
12.690
18.086
33.452
1.00
24.30
C

ATOM
2531
CB
LYS
C3098
11.820
18.543
33.945
1.00
24.76
C

ATOM
2532
CG
LYS
C3098
10.863
17.934
35.237
1.00
25.27
C

ATOM
2533
CD
LYS
C3098
9.397
18.241
35.459
1.00
26.28
C

ATOM
2534
CB
LYS
C3098
8.973
17.880
36.860
1.00
26.82
C

ATOM
2535
NZ
LYS
C3098
9.334
16.468
37.155
1.00
28.61
N

ATOM
2536
G
LYS
C3098
12.978
18.774
32.119
1.00
23.93
C

ATOM
2537
0
LYS
C3098
13.330
19.954
32.077
1.00
23.38
O

ATOM
2538
N
ILE
C3099
12.821
18.019
31.034
1.00
23.34
N

ATOM
2539
CA
ILE
C3099
13.033
18.536
29.690
1.00
22.75
C

ATOM
2540
CB
ILE
C3099
13.960
17.613
28.874
1.00
22.58
C

ATOM
2541
CG2
ILE
C3099
14.345
18.292
27.558
1.00
22.52
C

ATOM
2542
CG1
ILE
C3099
15.219
17.291
29.688
1.00
22.55
C

ATOM
2543
COl
ILE
C3099
16.199
16.357
28.985
1.00
22.28
C

ATOM
2544
C
ILE
C3099
11.676
18.617
28.990
1.00
22.48
C

ATOM
2545
0
ILE
C3099
11.054
17.591
28.699
1.00
22.47
O

ATOM
2546
N
TRP
C3100
11.205
19.835
28.743
1.00
21.77
N

ATOM
2547
CA
TRP
C3100
9.926
20.008
28.071
1.00
20.54
C

ATOM
2548
CB
TRP
C3100
9.180
21.228
28.600
1.00
19.83
C

ATOM
2549
CG
TRP
C3100
8.900
21.139
30.066
1.00
19.91
C

ATOM
2550
CG2
TRP
C3100
7.806
20.455
30.694
1.00
19.80
C

ATOM
2551
CB2
TRP
C3100
7.968
20.605
32.091
1.00
19.84
C

ATOM
2552
CB3
TRP
C3100
6.704
19.727
30.211
1.00
19.87
C

ATOM
2553
COl
TRP
C3100
9.660
21.660
31.081
1.00
19.93
C

ATOM
2554
NEl
TRP
C3100
9.106
21.343
32.296
1.00
19.91
N

ATOM
2555
CZ2
TRP
C3100
7.069
20.058
33.015
1.00
19.27
C

ATOM
2556
CZ3
TRP
C3100
5.808
19.181
31.128
1.00
19.78
C

ATOM
2557
CH2
TRP
C3100
6.000
19.352
32.520
1.00
20.41
C

ATOM
2558
C
TRP
C3100
10.239
20.174
26.611
1.00
20.42
C

ATOM
2559
0
TRP
C3100
10.831
21.174
26.195
1.00
21.30
O

ATOM
2560
N
LEU
C3101
9.845
19.173
25.838
1.00
19.69
N

ATOM
2561
CA
LEU
C3101
10.097
19.143
24.416
1.00
19.35
C

ATOM
2562
CB
LEU
C3101
10.903
17.891
24.072
1.00
18.36
C

ATOM
2563
CG
LEU
C3101
10.885
17.499
22.592
1.00
18.24
C

ATOM
2564
CD1
LEU
C3101
11.677
18.536
21.786
1.00
16.55
C

ATOM
2565
CG2
LEU
C3101
11.466
16.097
22.414
1.00
17.56
C

ATOM
2566
CLEt) C3101
8.831
19.145
23.587
1.00
19.41
C

ATOM
2567
0
LEU
C3101
7.846
18.493
23.929
1.00
19.45
O

ATOM
2568
N
SER
C3102
8.860
19.885
22.490
1.00
19.43
N

ATOM
2569
CA
SER
C3102
7.722
19.899
21.596
1.00
19.85
C

ATOM
2570
CB
SER
C3102
6.793
21.082
21.873
1.00
19.85
C

ATOM
2571
OG
SER
C3102
5.550
20.887
21.212
1.00
19.01
O

ATOM
2572
C
SER
C3102
8.269
19.972
20.190
1.00
20.13
C

ATOM
2573
0
SER
C3102
9.272
20.637
19.939
1.00
19.67
O

ATOM
2574
N
ILE
C3103
7.624
19.251
19.282
1.00
21.04
N

ATOM
2575
CA
ILE
C3103
8.037
19.231
17.889
1.00
22.10
C

ATOM
2576
CB
ILE
C3103
8.735
17.906
17.523
1.00
21.92
C

ATOM
2577
CG2
ILE
C3103
9.127
17.922
16.059
1.00
21.89
C

ATOM
2578
CG1
ILE
C3103
9.963
17.681
18.405
1.00
22.24
C

ATOM
2579
CD1
ILE
C3103
10.695
16.376
18.094
1.00
22.36
C

ATOM
2580
C
ILE
C3103
6.804
19.346
17.010
1.00
23.17
C

ATOM
2581
0
ILE
C3103
5.753
18.805
17.338
1.00
23.73
O

ATOM
2582
N
SER
C3104
6.932
20.051
15.896
1.00
23.79
N

ATOM
2583
CA
SER
C3104
5.829
20.186
14.965
1.00
24.82
C

ATOM
2584
CB
SER
C3104
4.989
21.419
15.294
1.00
24.69
C

ATOM
2585
OG
SER
C3104
3.905
21.546
14.390
1.00
24.65
O

ATOM
2586
C
SER
c3104
6.428
20.295
13.567
1.00
25.82
C

ATOM
2587
0
SER
C3104
7.577
20.690
13.403
1.00
25.83
O

ATOM
2588
N
HIS
C3105
5.646
19.929
12.560
1.00
27.14
N.

ATOM
2589
CA
HIS
C3105
6.140
19.996
11.200
1.00
28.67
C

ATOM
2590
CB
HIS
C3105
6.841
18.686
10.819
1.00
30.20
C

ATOM
2591
CG
HIS
C3105
5.901
17.542
10.584
1.00
31.48
C

ATOM
2592
CG2
HIS
C3105
5.474
16.961
9.437
1.00
32.52
C

ATOM
2593
ND1
HIS
C3105
5.252
16.887
11.607
1.00
33.00
N

ATOM
2594
CBl
HIS
C3105
4.465
15.952
11.103
1.00
33.08
C

ATOM
2595
NE2
HIS
C3105
4.580
15.977
9.787
1.00
33.14
N

ATOM
2596
C
HIS
C3105
5.046
20.253
10.187
1.00
29.03
C

ATOM
2597
0
HIS
C3105
3.862
20.082
10.468
1.00
28.87
O

ATOM
2598
N
THR
C3106
5.478
20.682
9.009
1.00
29.70
N

ATOM
2599
CA
THR
C3106
4.609
20.918
7.871
1.00
30.87
C

ATOM
2600
CB
THR
C3106
4.542
22.416
7.492
1.00
30.95
C

ATOM
2601
OGi
THR
C3106
5.853
22.895
7.185
1.00
31.53
O

ATOM
2602
CG2
THR
C3106
3.970
23.231
8.631
1.00
31.66
C

ATOM
2603
C
THR
C3106
5.310
20.118
6.758
1.00
31.46
C

ATOM
2604
0
THR
C3106
6.288
19.411
7.032
1.00
31.17
O

ATOM
2605
N
ASP
C3107
4.834
20.223
5.521
1.00
32.04
N

ATOM
2606
CA
ASP
C3107
5.444
19.475
4.423
1.00
32.74
C

ATOM
2607
CD
ASP
C3107
4.584
19.570
3.151
1.00
33.89
C

ATOM
2608
CG
ASP
C3107
3.252
18.836
3.276
1.00
35.29
C

ATOM
2609
ODi
ASP
C3107
3.059
18.077
4.257
1.00
35.09
O

ATOM
2610
002
ASP
C3107
2.396
19.017
2.379
1.00
35.84
O

ATOM
2611
C
ASP
C3107
6.861
19.942
4.096
1.00
32.51
C

ATOM
2612
0
ASP
C3107
7.680
19.158
3.609
1.00
32.63
O

ATOM
2613
NGL~I C3108
7.152
21.210
4.371
1.00
31.99
N

ATOM
2614
CA
GLN
C3108
8.467
21.768
4.068
1.00
31.59
C

ATOM
2615
CR
GLN
C3108
8.310
23.119
3.362
1.00
32.00
C

ATOM
2616
CG
GLN
C3108
7.482
23.077
2.086
1.00
32.40

ATOM
2617
CD
GLN
C3108
7.294
24.452
1.469
0.05
32.28
C

ATOM
2618
OE1
GLN
C3108
6.650
24.597
0.430
0.05
32.30
O

ATOM
2619
NE2
GLN
C3108
7.856
25.469
2.110
0.05
32.28
N

ATOM
2620
C
GLN
C3108
9.391
21.957
5.272
1.00
30.94
C

ATOM
2621
0
GLN
C3108
10.610
21.833
5.145
1.00
30.85
O

ATOM
2622
N
PHE
. C3109
8.822
22.258
6.436
1.00
30.12
N

ATOM
2623
CA
PHE
C3109
9.648
22.489
7.610
1.00
29.07
C

ATOM
2624
CB
PHE
C3109
9.652
23.980
7.953
1.00
29.62
C

ATOM
2625
CG
PHE
C3109
10.111
24.857
6.827
1.00
30.64
C

ATOM
2626
COl
PHE
C3109
9.215
25.275
5.845
1.00
31.09
C

ATOM
2627
CG2
PHE
C3109
11.440
25.259
6.738
1.00
30.59
C

ATOM
2628
CBl
PHE
C3109
9.636
26.084
4.788
1.00
31.21
C

ATOM
2629
CB2
PHE
C3109
11.870
26.066
5.688
1.00
30.89
C

ATOM
2630
CZ
PHE
C3109
10.964
26.480
4.709
1.00
31.08
C

ATOM
2631
C
PHE
C3109
9.292
21.716
8.860
1.00
28.01
C

ATOM
2632
0
PHE
C3109
8.252
21.065
8.936
1.00
28.14
O

ATOM
2633
N
VAL
C3110
10.192
21.798
9.838
1.00
26.84
N

ATOM
2634
CA
VAL
C3110
10.019
21.175
11.140
1.00
25.60
C

ATOM
2635
CB
VAL
C3110
10.766
19.822
11.250
1.00
25.63
C

ATOM
2636
CG1
VAL
C3110
12.268
20.035
11.191
1.00
25.54
C

ATOM
2637
CG2
VAL
C3110
10.387
19.133
12.554
1.00
25.58
C

ATOM
2638
C
VAL
C3110
10.580
22.139
12.187
1.00
24.84
C

ATOM
2639
0
VAL
C3110
11.596
22.798
11.957
1.00
24.75
O

ATOM
2640
N
THR
C3111
9.911
22.239
13.328
1.00
23.62
N

ATOM
2641
CA
THR
C3111
10.377
23.120
14.395
1.00
23.00
C

ATOM
2642
CB
THR
C3111
9.451
24.332
14.583
1.00
23.10
C

ATOM
2643
OGi
THR
C3111
8.138
23.871
14.924
1.00
24.21
O

ATOM
2644
CG2
THR
C3111
9.369
25.145
13.306
1.00
23.43
C

ATOM
2645
C
THR
C3111
10.424
22.363
15.712
1.00
22.01
C

ATOM
2646
0
THR
C3111
9.616
21.466
15.951
1.00
22.10
O

ATOM
2647
N
ALA
C3122
11.382
22.726
16.554
1.00
21.05
N

ATOM
2648
CA
ALA
C3112
11.532
22.110
17.859
1.00
20.79
C

ATOM
2649
CB
ALA
C3112
12.710
21.135
17.846
1.00
20.00
C

ATOM
2650
C
ALA
C3112
11.741
23.194
18.927
1.00
20.81
C

ATOM
2651
0
ALA
C3112
12.367
24.216
18.672
1.00
20.76
O

ATOM
2652
N
SER
C3113
11.199
22.968
20.118
1.00
20.90
N

ATOM
2653
CA
SER
C3113
11.346
23.909
21.215
1.00
20.61
C

ATOM
2654
CB
SER
C3113
10.061
24.721
21.413
1.00
20.72
C

ATOM
2655
OG
SER
C3113
10.176
25.598
22.526
1.00
20.34
O

ATOM
2656
C
SER
C3113
11.653
23.128
22.477
1.00
20.63
C

ATOM
2657
0
SER
C3113
11.013
22.119
22.759
1.00
20.86
O

ATOM
2658
N
VAL
C3114
12.633
23.599
23.237
1.00
20.54
N

ATOM
2659
CA
VAL
C3114
13.019
22.938
24.463
1.00
20.40
C

ATOM
2660
CB
VAL
C3114
14.349
22.188
24.288
1.00
20.41
C

ATOM
2661
COl
VAL
C3114
14.872
21.743
25.647
1.00
19.44
C

ATOM
2662
CG2
VAL
C3114
14.148
20.976
23.357
1.00
20.11
C

ATOM
2663
C
VAL
C3114
13.159
23.883
25.644
1.00
20.99
C

ATOM
2664
0
VAL
C3114
13.804
24.938
25.552
1.00
20.99
O

ATOM
2665
N
ILE
C3115
12.543
23.494
26.756
1.00
21.35
N

ATOM
2666
CA
ILE
C3115
12.626
24.269
27.980
1.00
22.44
C

ATOM
2667
CB
ILE
C3115
11.250
24.816
28.428
1.00
22.27
C

ATOM
2668
CG2
ILE
C3115
11.440
25.821
29.562
1.00
22.27
C

ATOM
2669
CG1
ILE
C3115
10.553
25.529
27.262
1.00
22.90
C

ATOM
2670
COl
ILE
C3115
9.141
25.990
27.562
1.00
22.49
C

ATOM
2671
C
ILE
C3115
13.167
23.360
29.077
1.00
23.09
C

ATOM
2672
0
ILE
C3115
12.570
22.331
29.388
1.00
23.11
O

ATOM
2673
N
LEU
C3116
14.311
23.730
29.640
1.00
23.90
N

ATOM
2674
CA
LEU
C3116
14.912
22.959
30.720
1.00
25.63
C

ATOM
2675
CB
LEU
C3116
16.434
23.051
30.667
1.00
24.96
C

ATOM
2676
CG
LEU
C3116
17.007
22.497
29.366
1.00
24.50
C

ATOM
2677
COl
LEU
C3116
18.508
22.663
29.350
1.00
23.62
C

ATOM
2678
CG2
LEU
C3116
16.596
21.029
29.236
1.00
24.58
C

ATOM
2679
C
LEU
C3116
14.418
23.524
32.036
1.00
27.20
C

ATOM
2680
0
LEU
C3116
14.412
24.743
32.236
1.00
27.34
O

ATOM
2681
N
GLU
C3117
13.998
22.636
32.930
1.00
28.70
N

ATOM
2682
CA
GLU
C3117
13.490
23.061
34.226
1.00
30.61
C

ATOM
2683
CB
GLU
C3117
11.957
22.951
34.249
1.00
30.11
C

ATOM
2684
CG
GLU
C3117
11.322
23.257
35.592
1.00
30.29
C

ATOM
2685
CD
GLU
C3117
9.808
23.100
35.585
1.00
30.63
C

ATOM
2686
QEl
GLU
C3117
9.313
22.085
35.043
1.00
30.65
O

ATOM
2687
OE2
GLU
C3117
9.114
23.985
36.133
1.00
30.59
O

ATOM
2688
C
GLU
C3117
14.089
22.241
35.357
1.00
31.98
C

ATOM
2689
0
GLU
C3117
14.353
21.052
35.205
1.00
32.46
O

ATOM
2690
N
GLU
C3118
14.321
22.900
36.485
1.00
33.79
N

ATOM
2691
CA
GLU
C3118
24.863
22.257
37.674
1.00
35.41
C

ATOM
2692
CB
GLU
C3118
16.264
22.779
37.990
1.00
36.58
C

ATOM
2693
CG
GLU
C3118
17.396
21.983
37.366
1.00
38.74
C

ATOM
2694
CD
GLU
C3118
17.335
20.507
37.733
1.00
40.59
C

ATOM
2695
OE1
GLU
C3118
16.936
20.189
38.881
1.00
41.34
O

ATOM
2696
OE2
GLU
C3118
17.700
19.669
36.877
1.00
41.36
O

ATOM
2697
C
GLU
C3118
13.940
22.578
38.837
1.00
36.11
C

ATOM
2698
O
GLU
C3118
13.351
21.632
39.403
1.00
37.15
O

ATOM
2699
OXT
GLU
C3118
13.813
23.778
39.156
1.00
36.00
O

TER
2700

GLU
C3118

ATOM
2701
O
HOH
W 1
8.576
28.003
19.046
1.00
26.06
O

ATOM
2702
O
HOH
W 2
11.001
13.668
14.737
1.00
16.99
O

ATOM
2703
O
HOH
W 3
−5.347
33.382
14.724
1.00
27.55
O

ATOM
2704
O
HOH
W 4
19.615
31.388
19.825
1.00
18.58
O

ATOM
2705
O
HOH
W 5
−11.216
36.113
18.617
1.00
38.18
O

ATOM
2706
O
HOH
W 6
0.159
37.746
18.293
1.00
26.61
O

ATOM
2707
O
HOH
W 7
1.276
36.190
20.543
1.00
28.54
O

ATOM
2708
O
HOH
W 8
12.334
34.067
2.484
1.00
24.27
O

ATOM
2709
O
HOH
W 9
0.255
6.277
33.704
1.00
25.24
O

ATOM
2710
O
HOH
W 1O
18.182
37.167
27.027
1.00
23.05
O

ATOM
2711
O
HOH
W 11
−4.577
31.410
31.511
1.00
38.36
O

ATOM
2712
O
HOH
W 12
−1.511
45.557
32.920
1.00
53.67
O

ATOM
2713
O
HOH
W 13
18.448
25.653
12.095
1.00
26.48
O

ATOM
2714
O
HOH
W 14
3.912
2.648
29.570
1.00
20.27
O

ATOM
2715
O
HOH
W 15
−11.595
44.974
29.760
1.00
29.90
O

ATOM
2716
O
HOH
W 16
25.183
18.367
31.463
1.00
31.92
O

ATOM
2717
O
HOH
W 17
1.272
28.443
2.735
1.00
24.74
O

ATOM
2718
O
HOH
W 18
19.674
51.864
7.542
1.00
32.28
O

ATOM
2719
O
HOH
W 19
7.406
44.679
0.671
1.00
37.76
O

ATOM
2720
O
HOH
W 20
9.102
25.639
41.587
1.00
37.75
O

ATOM
2721
O
HOH
W 21
−2.117
42.358
29.367
1.00
23.51
O

ATOM
2722
O
HOH
W 22
12.144
15.091
31.453
1.00
40.21
O

ATOM
2723
O
HOH
W 23
20.216
37.895
14.318
1.00
23.27
O

ATOM
2724
O
HOH
W 24
15.409
30.644
36.448
1.00
34.67
O

ATOM
2725
O
HOH
W 25
8.888
28.186
21.855
1.00
19.15
O

ATOM
2726
O
HOH
W 26
−6.604
42.281
29.309
1.00
52.83
O

ATOM
2727
O
HOH
W 27
20.104
53.238
15.360
1.00
42.16
O

ATOM
2728
O
HOH
W 28
24.519
36.311
10.567
1.00
45.76
O

ATOM
2729
O
HOH
W 29
17.712
23.831
7.356
1.00
49.27
O

ATOM
2730
O
HOH
W 30
−6.885
28.651
32.939
1.00
45.10
O

ATOM
2731
O
HOH
W 31
−4.869
16.926
12.390
1.00
39.22
O

ATOM
2732
O
HOH
W 32
20.935
28.085
34.073
1.00
42.57
O

ATOM
2733
O
HOH
W 33
21.868
15.456
38.834
1.00
28.55
O

ATOM
2734
O
HOH
W 34
30.171
27.602
20.593
1.00
34.40
O

ATOM
2735
O
HOH
W 35
20.651
33.038
6.426
1.00
38.43
O

ATOM
2736
O
HOH
W 36
10.238
19.208
1.078
1.00
45.56
O

ATOM
2737
O
HOH
W 37
13.283
54.499
28.613
1.00
29.72
O

ATOM
2738
O
HOH
W 38
−11.211
32.999
2.256
1.00
31.79
O

ATOM
2739
O
HOH
W 39
9.887
29.798
36.670
1.00
39.85
O

ATOM
2740
O
HOH
W 40
18.546
10.765
31.009
1.00
38.20
O

ATOM
2741
O
HOH
W 41
24.510
24.190
30.902
1.00
36.49
O

ATOM
2742
O
HOH
W 42
30.384
38.300
20.406
1.00
44.88
O

ATOM
2743
O
HOH
W 43
18.885
28.685
22.975
1.00
28.61
O

ATOM
2744
O
HOH
W 44
2.917
33.308
36.961
1.00
38.63
O

ATOM
2745
O
HOH
W 45
20.025
.37.807
29.500
1.00
35.61
O

ATOM
2746
O
HOH
W 46
8.253
16.151
27.102
1.00
45.55
O

ATOM
2747
O
HOH
W 47
7.572
21.032
36.495
1.00
16.73
O

ATOM
2748
O
HOH
W 48
19.451
28.611
27.413
1.00
35.89
O

ATOM
2749
O
HOH
W 49
11.476
8.815
36.574
1.00
25.09
O

ATOM
2750
O
HOH
W 50
14.236
27.513
3.754
1.00
34.47
O

ATOM
2751
O
HOH
W 51
5.103
9.140
28.941
1.00
41.40
O

ATOM
2752
O
HOH
W 52
34.054
32.834
25.976
1.00
45.36
O

ATOM
2753
O
HOH
W 53
12.068
21.222
2.790
1.00
39.74
O

ATOM
2754
O
HOH
W 54
2.919
30.077
39.125
1.00
41.17
O

ATOM
2755
O
HOH
W 55
27.605
12.175
17.892
1.00
50.62
O

ATOM
2756
O
HOH
W 56
−12.868
26.916
30.495
1.00
43.36
O

ATOM
2757
O
HOH
W 57
9.027
13.611
36.816
1.00
43.33
O

ATOM
2758
O
HOH
W 58
7.507
37.992
7.686
1.00
29.16
O

ATOM
2759
O
HOH
W 59
18.024
26.076
4.943
1.00
45.92
O

ATOM
2760
O
HOH
W 60
21.889
53.044
19.501
1.00
41.90
O

ATOM
2761
O
HOH
W 61
34.566
32.372
30.692
1.00
50.00
O

ATOM
2762
O
HOH
W 62
5.289
23.268
4.539
1.00
26.10
O

ATOM
2763
O
HOH
W 63
21.724
28.905
29.036
1.00
54.44
O

ATOM
2764
O
HOH
W 64
7.000
28.471
37.399
1.00
36.37
O

ATOM
2765
O
HOH
W 65
31.382
30.725
21.632
1.00
32.29
O

ATOM
2766
O
HOH
W 66
28.182
46.827
4.332
1.00
48.39
O

ATOM
2767
O
HOH
W 67
7.410
9.794
14.247
1.00
49.84
O

ATOM
2768
O
HOH
W 68
31.517
25.424
22.117
1.00
43.26
O

ATOM
2769
O
HOH
W 69
−5.301
33.373
34.239
1.00
34.98
O

ATOM
2770
O
HOH
W 70
36.871
33.074
30.281
1.00
41.21
O

ATOM
2771
O
HOH
W 71
24.903
41.702
17.966
1.00
33.98
O

ATOM
2772
O
HOH
W 72
17.963
38.386
31.211
1.00
35.46
O

ATOM
2773
O
HOH
W 73
20.723
48.845
4.797
1.00
50.12
O

ATOM
2774
O
HOH
W 74
−8.379
30.159
31.227
1.00
58.73
O

ATOM
2775
O
HOH
W 75
−1.343
19.609
10.013
1.00
53.09
O

ATOM
2776
O
HOH
W 76
15.642
12.801
31.165
1.00
65.31
O

ATOM
2777
O
HOH
W 77
−14.605
25.461
6.171
1.00
36.87
O

ATOM
2778
O
HOH
W 78
8.718
39.594
0.632
1.00
44.46
O

ATOM
2779
O
HOH
W 79
22.426
26.766
11.895
1.00
39.57
O

ATOM
2780
O
HOH
W 80
1.403
12.128
29.940
1.00
41.04
O

ATOM
2781
O
HOH
W 81
9.724
26.576
37.441
1.00
52.28
O

ATOM
2782
O
HOH
W 82
−20.852
35.093
18.162
1.00
32.23
O

ATOM
2783
O
HOH
W 83
−22.727
33.513
17.160
1.00
46.00
O

ATOM
2784
O
HOH
W 84
−9.764
38.910
4.301
1.00
38.92
O

ATOM
2785
O
HOH
W 85
4.067
40.345
32.364
1.00
54.10
O

ATOM
2786
O
HOH
W 86
8.783
44.044
3.423
1.00
45.06
O

ATOM
2787
O
HOH
W 87
19.259
34.587
26.113
1.00
34.60
O

ATOM
2788
O
HOH
W 88
19.168
34.051
31.232
1.00
40.61
O

ATOM
2789
O
HOH
W 89
−17.637
26.480
8.650
1.00
35.76
O

ATOM
2790
O
HOH
W 90
5.883
33.114
4.115
1.00
36.72
O

ATOM
2791
O
HOH
W 91
5.401
9.271
3.439
1.00
23.12
O

ATOM
2792
O
HOH
W 92
16.578
55.625
9.782
1.00
34.03
O

ATOM
2793
O
HOH
W 93
−6.649
22.603
36.177
1.00
49.27
O

ATOM
2794
O
HOH
W 94
12.263
32.477
39.013
1.00
44.31
O

ATOM
2795
O
HOH
W 95
11.064
51.183
10.359
1.00
46.81
O

ATOM
2796
O
HOH
W 96
−16.103
28.570
5.999
1.00
45.48
O

ATOM
2797
O
HOH
W 97
19.096
56.580
8.669
1.00
48.52
O

ATOM
2798
O
HOH
W 98
−0.441
38.083
25.842
1.00
30.49
O

ATOM
2799
O
HOH
W 99
18.821
50.159
23.847
1.00
35.93
O

ATOM
2800
O
HOH
W 100
21.593
29.439
22.517
1.00
46.08
O

ATOM
2801
O
HOH
W 101
24.154
31.033
26.613
1.00
41.03
O

ATOM
2802
O
HOH
W 102
18.634
43.303
30.404
1.00
40.85
O

ATOM
2803
O
HOH
W 103
19.981
32.247
35.107
1.00
36.43
O

ATOM
2804
O
HOH
W 104
−10.088
29.062
1.003
1.00
36.43
O

ATOM
2805
O
HOH
W 105
−18.529
19.631
5.334
1.00
38.77
O

ATOM
2806
O
HOH
W 106
−20.984
28.385
15.095
1.00
40.22
O

ATOM
2807
O
HOH
W 107
−19.013
26.762
15.815
1.00
32.06
O

ATOM
2808
O
HOH
W 108
−14.266
19.001
19.100
1.00
41.92
O

ATOM
2809
O
HOH
W 109
7.301
10.6941
1.123
1.00
37.73
O

ATOM
2810
O
HOH
W 110
24.398
18.549
24.386
1.00
37.13
O

ATOM
2811
O
HOH
W 111
2.259
41.877
17.603
1.00
33.35
O

ATOM
2812
O
HOH
W 112
22.143
19.952
8.110
1.00
46.84
O

ATOM
2813
O
HOH
W 113
−4.490
20.867
8.897
1.00
50.63
O

ATOM
2814
O
HOH
W 114
0.274
4.462
29.620
1.00
46.55
O

ATOM
2815
O
HOH
W 115
9.966
5.205
19.879
1.00
29.38
O

ATOM
2816
O
HOH
W 116
11.609
14.420
39.214
1.00
45.17
O

ATOM
2817
O
HOH
W 117
21.720
11.206
36.139
1.00
23.23
O

ATOM
2818
O
HOH
W 118
21.825
46.932
3.417
1.00
42.90
O

ATOM
2819
O
HOH
W 119
0.067
30.700
1.199
1.00
54.52
O

ATOM
2820
O
HOH
W 120
10.218
22.583
38.806
1.00
43.46
O

ATOM
2821
O
HOH
W 121
0.686
27.966
42.608
1.00
42.57
O

ATOM
2822
O
HOH
W 122
23.786
35.976
16.687
1.00
27.98
O

ATOM
2823
O
HOH
W 123
25.685
36.926
14.983
1.00
35.19
O

ATOM
2824
O
HOH
W 124
5.593
17.615
20.205
1.00
22.22
O

ATOM
2825
O
HOH
W 125
−3.621
36.444
16.059
1.00
38.53
O

ATOM
2826
O
HOH
W 126
−6.822
38.370
14.785
1.00
35.77
O

ATOM
2827
O
HOH
W 127
8.658
28.063
15.129
1.00
32.14
O

ATOM
2828
O
HOH
W 128
−4.302
30.987
36.514
1.00
38.06
O

ATOM
2829
O
HOH
W 129
−1.650
29.068
38.757
1.00
30.65
O

TER
2830

HOH
W 129

END

[0362]

6

TABLE 4

REMARK coordinates from restrained individual B-factor refinement

REMARK refinement resolution: 500.0 − 2.05 A

REMARK starting r = 0.2078 free_r = 0.2459

REMARK final r = 0.2076 free_r = 0.2466

REMARK B rmsd for bonded mainchain atoms = 1.338 target = 1.5

REMARK B rmsd for bonded sidechain atoms = 2.017 target = 2.0

REMARK B rmsd for angle mainchain atoms = 2.137 target = 2.0

REMARK B rmsd for angle sidechain atoms = 3.077 target = 2.5

REMARK wa = 1.98578

REMARK rweight = 0.12477

REMARK target = mlf · steps = 30

REMARK sg = C2 a = 116.043 b = 59.291 c = 49.629

alpha = 90 beta = 98.768 gamma = 90

REMARK parameter file 1 CNX_TOPPAR:protein_rep.param

REMARK parameter file 2 CNX_TOPPAR:water_rep.param

REMARK parameter file 3 CNX_TOPPAR:ion.param

REMARK molecular structure file: generate.psf

REMARK input coordinates: minimize.pdb

REMARK reflection file = ../data/x-ray_data.cv

REMARK ncs = none

REMARK B-correction resolution: 6.0 − 2.05

REMARK initial B-factor correction applied to fobs:

REMARK B11 = 0.091 B22 = −2.051 B33 = 1.959

REMARK B12 = 0.000 B13 = 0.271 B23 = 0.000

REMARK B-factor correction applied to coordinate array B: −0.022

REMARK bulk solvent: (Mask) density level = 0.368883 e/A{circumflex over ( )}3, B-factor = 52.2583 A{circumflex over ( )}2

REMARK reflections with |Fobs|/sigma_F < 0.0 rejected

REMARK reflections with |Fobs| > 10000 * rms (Fobs) rejected

REMARK theoretical total number of refl. in resol. range:
21048
(100.0%)

REMARK number of unobserved reflections (no entry or |F| = 0):
1611
(7.7%)

REMARK number of reflections rejected:
0
(0.0%)

REMARK total number of reflections used:
19437
(92.3%)

REMARK number of reflections in working set:
18494
(87.9%)

REMARK number of reflections in test set:
943
(4.5%)

REMARK FILENAME = “acps_native 2.pdb”:

created by user: rx83663

REMARK Written by CNX VERSION: 2000

ATOM
1
CB
MET
A1003
36.109
5.413
19.351
1.00
32.48
C

ATOM
2
CG
MET
A1003
35.473
5.856
20.649
1.00
37.79
C

ATOM
3
SD
MET
A1003
36.607
6.848
21.649
1.00
45.89
S

ATOM
4
CE
MET
A1003
36.791
8.314
20.599
1.00
43.10
C

ATOM
5
C
MET
A1003
33.900
5.073
18.225
1.00
27.65
C

ATOM
6
O
MET
A1003
33.795
6.027
17.463
1.00
25.93
O

ATOM
7
N
MET
A1003
35.971
4.133
17.240
1.00
28.87
N

ATOM
8
CA
MET
A1003
35.262
4.452
18.515
1.00
29.37
C

ATOM
9
N
ILE
A1004
32.860
4.513
18.832
1.00
27.12
N

ATOM
10
CA
ILE
A1004
31.500
5.005
18.649
1.00
25.95
C

ATOM
11
CB
ILE
A1004
30.463
3.928
19.020
1.00
25.43
C

ATOM
12
CG2
ILE
A1004
29.048
4.516
18.954
1.00
24.89
C

ATOM
13
CG1
ILE
A1004
30.604
2.730
18.076
1.00
24.55
C

ATOM
14
CD1
ILE
A1004
29.619
1.616
18.347
1.00
26.14
C

ATOM
15
C
ILE
A1004
31.289
6.214
19.546
1.00
27.18
C

ATOM
16
O
ILE
A1004
31.700
6.212
20.703
1.00
27.39
O

ATOM
17
N
VAL
A1005
30.655
7.251
19.018
1.00
24.87
N

ATOM
18
CA
VAL
A1005
30.420
8.439
19.818
1.00
25.40
C

ATOM
19
CB
VAL
A1005
31.326
9.589
19.346
1.00
26.42
C

ATOM
20
CG1
VAL
A1005
32.781
9.240
19.648
1.00
26.20
C

ATOM
21
CG2
VAL
A1005
31.153
9.818
17.860
1.00
27.65
C

ATOM
22
C
VAL
A1005
28.955
8.857
19.794
1.00
24.30
C

ATOM
23
O
VAL
A1005
28.592
9.964
20.195
1.00
23.88
O

ATOM
24
N
GLY
A1006
28.102
7.952
19.331
1.00
23.00
N

ATOM
25
CA
GLY
A1006
26.687
8.261
19.290
1.00
19.45
C

ATOM
26
C
GLY
A1006
25.887
7.300
18.443
1.00
18.59
C

ATOM
27
O
GLY
A1006
26.396
6.730
17.480
1.00
16.47
O

ATOM
28
N
HIS
A1007
24.621
7.130
18.809
1.00
16.39
N

ATOM
29
CA
HIS
A1007
23.720
6.249
18.092
1.00
15.38
C

ATOM
30
CB
HIS
A1007
23.825
4.818
18.636
1.00
17.15
C

ATOM
31
CG
HIS
A1007
22.877
3.853
17.993
1.00
18.41
C

ATOM
32
CD2
HIS
A1007
22.075
2.902
18.528
1.00
17.85
C

ATOM
33
ND1
HIS
A1007
22.690
3.789
16.628
1.00
17.93
N

ATOM
34
CE1
HIS
A1007
21.811
2.841
16.351
1.00
19.72
C

ATOM
35
NE2
HIS
A1007
21.423
2.288
17.486
1.00
18.78
N

ATOM
36
C
HIS
A1007
22.302
6.768
18.262
1.00
16.54
C

ATOM
37
O
HIS
A1007
21.883
7.113
19.364
1.00
15.23
O

ATOM
38
N
GLY
A1008
21.568
6.844
17.162
1.00
13.65
N

ATOM
39
CA
GLY
A1008
20.204
7.303
17.250
1.00
14.59
C

ATOM
40
C
GLY
A1008
19.364
6.591
16.220
1.00
16.81
C

ATOM
41
O
GLY
A1008
19.864
6.208
15.154
1.00
14.95
O

ATOM
42
N
ILE
A1009
18.089
6.394
16.538
1.00
16.05
N

ATOM
43
CA
ILE
A1009
17.186
5.750
15.603
1.00
16.53
C

ATOM
44
CB
ILE
A1009
16.841
4.297
16.012
1.00
16.37
C

ATOM
45
CG2
ILE
A1009
18.087
3.436
15.974
1.00
15.97
C

ATOM
46
CG1
ILE
A1009
16.168
4.284
17.393
1.00
14.54
C

ATOM
47
CD1
ILE
A1009
15.697
2.907
17.831
1.00
15.26
C

ATOM
48
C
ILE
A1009
15.898
6.541
15.578
1.00
18.21
C

ATOM
49
O
ILE
A1009
15.681
7.423
16.408
1.00
18.91
O

ATOM
50
N
ASP
A1010
15.041
6.218
14.623
1.00
19.48
N

ATOM
51
CA
ASP
A1010
13.759
6.880
14.520
1.00
20.47
C

ATOM
52
CB
ASP
A1010
13.930
8.295
13.969
1.00
21.20
C

ATOM
53
CG
ASP
A1010
12.614
9.013
13.813
1.00
24.68
C

ATOM
54
OD1
ASP
A1010
12.002
8.901
12.725
1.00
25.58
O

ATOM
55
OD2
ASP
A1010
12.182
9.675
14.785
1.00
21.51
O

ATOM
56
C
ASP
A1010
12.822
6.094
13.630
1.00
22.13
C

ATOM
57
O
ASP
A1010
13.249
5.485
12.641
1.00
21.63
O

ATOM
58
N
ILE
A1011
11.548
6.074
14.011
1.00
20.69
N

ATOM
59
CA
ILE
A1011
10.525
5.403
13.226
1.00
22.73
C

ATOM
60
CB
ILE
A1011
10.019
4.103
13.903
1.00
22.88
C

ATOM
61
CG2
ILE
A1011
9.505
4.398
15.320
1.00
23.25
C

ATOM
62
CG1
ILE
A1011
8.922
3.476
13.033
1.00
24.40
C

ATOM
63
CD1
ILE
A1011
8.496
2.096
13.466
1.00
25.25
C

ATOM
64
C
ILE
A1011
9.394
6.412
13.094
1.00
23.63
C

ATOM
65
O
ILE
A1011
9.016
7.061
14.071
1.00
23.36
O

ATOM
66
N
GLU
A1012
8.869
6.549
11.882
1.00
25.11
N

ATOM
67
CA
GLU
A1012
7.810
7.514
11.602
1.00
24.91
C

ATOM
68
CB
GLU
A1012
8.421
8.737
10.916
1.00
25.40
C

ATOM
69
CG
GLU
A1012
7.413
9.773
10.433
1.00
29.98
C

ATOM
70
CD
GLU
A1012
6.857
10.631
11.552
1.00
32.43
C

ATOM
71
OE1
GLU
A1012
5.954
11.447
11.274
1.00
36.73
O

ATOM
72
OE2
GLU
A1012
7.319
10.497
12.704
1.00
35.01
O

ATOM
73
C
GLU
A1012
6.705
6.952
10.716
1.00
24.25
C

ATOM
74
O
GLU
A1012
6.975
6.186
9.789
1.00
22.71
O

ATOM
75
N
GLU
A1013
5.462
7.331
11.006
1.00
24.75
N

ATOM
76
CA
GLU
A1013
4.326
6.895
10.195
1.00
25.26
C

ATOM
77
CB
GLU
A1013
3.006
7.010
10.956
1.00
27.28
C

ATOM
78
CG
GLU
A1013
2.782
6.015
12.056
1.00
32.89
C

ATOM
79
CD
GLU
A1013
1.337
6.025
12.512
1.00
36.18
C

ATOM
80
OE1
GLU
A1013
0.451
5.792
11.661
1.00
38.66
O

ATOM
81
OE2
GLU
A1013
1.083
6.270
13.709
1.00
39.09
O

ATOM
82
C
GLU
A1013
4.253
7.848
9.013
1.00
24.28
C

ATOM
83
O
GLU
A1013
4.254
9.062
9.197
1.00
24.07
O

ATOM
84
N
LEU
A1014
4.179
7.308
7.805
1.00
23.86
N

ATOM
85
CA
LEU
A1014
4.103
8.149
6.615
1.00
24.45
C

ATOM
86
CB
LEU
A1014
4.150
7.274
5.362
1.00
25.54
C

ATOM
87
CG
LEU
A1014
5.402
6.397
5.287
1.00
28.12
C

ATOM
88
CD1
LEU
A1014
5.266
5.386
4.162
1.00
28.37
C

ATOM
89
CD2
LEU
A1014
6.627
7.284
5.082
1.00
29.49
C

ATOM
90
C
LEU
A1014
2.838
9.010
6.611
1.00
23.06
C

ATOM
91
O
LEU
A1014
2.838
10.126
6.083
1.00
22.31
O

ATOM
92
N
ALA
A1015
1.768
8.490
7.210
1.00
22.30
N

ATOM
93
CA
ALA
A1015
0.489
9.202
7.284
1.00
21.59
C

ATOM
94
CB
ALA
A1015
−0.529
8.372
8.068
1.00
20.65
C

ATOM
95
C
ALA
A1015
0.664
10.568
7.938
1.00
21.21
C

ATOM
96
O
ALA
A1015
0.101
11.562
7.483
1.00
19.58
O

ATOM
97
N
SER
A1016
1.442
10.605
9.017
1.00
21.38
N

ATOM
98
CA
SER
A1016
1.711
11.848
9.728
1.00
22.18
C

ATOM
99
CB
SER
A1016
2.587
11.569
10.951
1.00
22.67
C

ATOM
100
OG
SER
A1016
2.034
10.523
11.733
1.00
29.64
O

ATOM
101
C
SER
A1016
2.428
12.825
8.800
1.00
22.03
C

ATOM
102
O
SER
A1016
2.134
14.020
8.786
1.00
24.58
O

ATOM
103
N
ILE
A1017
3.382
12.319
8.027
1.00
21.56
N

ATOM
104
CA
ILE
A1017
4.112
13.177
7.104
1.00
22.10
C

ATOM
105
CB
ILE
A1017
5.336
12.454
6.523
1.00
22.24
C

ATOM
106
CG2
ILE
A1017
5.975
13.312
5.432
1.00
21.89
C

ATOM
107
CG1
ILE
A1017
6.342
12.174
7.641
1.00
22.58
C

ATOM
108
CD1
ILE
A1017
6.904
13.440
8.287
1.00
24.27
C

ATOM
109
C
ILE
A1017
3.207
13.633
5.957
1.00
22.93
C

ATOM
110
O
ILE
A1017
3.244
14.793
5.549
1.00
23.54
O

ATOM
111
N
GLU
A1018
2.388
12.726
5.440
1.00
23.95
N

ATOM
112
CA
GLU
A1018
1.494
13.096
4.348
1.00
26.57
C

ATOM
113
CB
GLU
A1018
0.794
11.862
3.775
1.00
29.38
C

ATOM
114
CG
GLU
A1018
−0.244
12.197
2.709
1.00
33.05
C

ATOM
115
CD
GLU
A1018
−0.655
10.987
1.900
1.00
36.21
C

ATOM
116
OE1
GLU
A1018
−0.803
9.897
2.495
1.00
38.49
O

ATOM
117
OE2
GLU
A1018
−0.840
11.131
0.672
1.00
38.02
O

ATOM
118
C
GLU
A1018
0.466
14.116
4.819
1.00
25.75
C

ATOM
119
O
GLU
A1018
0.115
15.032
4.082
1.00
25.64
O

ATOM
120
N
SER
A1019
−0.011
13.960
6.052
1.00
27.25
N

ATOM
121
CA
SER
A1019
−0.980
14.893
6.615
1.00
27.84
C

ATOM
122
CB
SER
A1019
−1.436
14.425
8.000
1.00
28.92
C

ATOM
123
OG
SER
A1019
−2.107
13.176
7.929
1.00
31.15
O

ATOM
124
C
SER
A1019
−0.338
16.275
6.734
1.00
28.62
C

ATOM
125
O
SER
A1019
−0.956
17.289
6.400
1.00
27.65
O

ATOM
126
N
ALA
A1020
0.907
16.302
7.209
1.00
28.27
N

ATOM
127
CA
ALA
A1020
1.650
17.545
7.374
1.00
30.56
C

ATOM
128
CB
ALA
A1020
3.020
17.267
8.005
1.00
30.65
C

ATOM
129
C
ALA
A1020
1.823
18.267
6.045
1.00
31.87
C

ATOM
130
O
ALA
A1020
1.686
19.487
5.976
1.00
32.82
O

ATOM
131
N
VAL
A1021
2.127
17.513
4.992
1.00
33.76
N

ATOM
132
CA
VAL
A1021
2.304
18.099
3.666
1.00
34.05
C

ATOM
133
CB
VAL
A1021
2.830
17.057
2.656
1.00
34.30
C

ATOM
134
CG1
VAL
A1021
2.878
17.660
1.263
1.00
31.58
C

ATOM
135
CG2
VAL
A1021
4.213
16.577
3.073
1.00
33.12
C

ATOM
136
C
VAL
A1021
0.969
18.635
3.150
1.00
35.65
C

ATOM
137
O
VAL
A1021
0.891
19.754
2.643
1.00
34.17
O

ATOM
138
N
THR
A1022
−0.081
17.829
3.294
1.00
36.17
N

ATOM
139
CA
THR
A1022
−1.418
18.209
2.842
1.00
37.29
C

ATOM
140
CB
THR
A1022
−2.433
17.074
3.096
1.00
35.53
C

ATOM
141
OG1
THR
A1022
−2.107
15.955
2.265
1.00
34.37
O

ATOM
142
CG2
THR
A1022
−3.845
17.530
2.776
1.00
35.58
C

ATOM
143
C
THR
A1022
−1.933
19.482
3.504
1.00
39.32
C

ATOM
144
O
THR
A1022
−2.672
20.250
2.885
1.00
38.90
O

ATOM
145
N
ARG
A1023
−1.544
19.702
4.758
1.00
42.46
N

ATOM
146
CA
ARG
A1023
−1.977
20.885
5.496
1.00
46.07
C

ATOM
147
CB
ARG
A1023
−1.684
20.727
6.991
1.00
48.22
C

ATOM
148
CG
ARG
A1023
−2.327
19.534
7.664
1.00
51.97
C

ATOM
149
CD
ARG
A1023
−1.900
19.477
9.125
1.00
55.95
C

ATOM
150
NE
ARG
A1023
−2.234
18.208
9.770
1.00
59.02
N

ATOM
151
CZ
ARG
A1023
−1.958
17.922
11.039
1.00
61.01
C

ATOM
152
NH1
ARG
A1023
−1.344
18.818
11.804
1.00
61.80
N

ATOM
153
NH2
ARG
A1023
−2.292
16.741
11.546
1.00
61.79
N

ATOM
154
C
ARG
A1023
−1.275
22.147
4.999
1.00
47.81
C

ATOM
155
O
ARG
A1023
−1.801
22.888
4.166
1.00
47.51
O

ATOM
156
N
HIS
A1024
−0.077
22.381
5.526
1.00
49.48
N

ATOM
157
CA
HIS
A1024
0.714
23.553
5.171
1.00
49.99
C

ATOM
158
CB
HIS
A1024
1.238
24.226
6.441
1.00
51.40
C

ATOM
159
CG
HIS
A1024
1.367
23.295
7.608
1.00
53.33
C

ATOM
160
CD2
HIS
A1024
2.447
22.670
8.136
1.00
53.80
C

ATOM
161
ND1
HIS
A1024
0.284
22.885
8.357
1.00
54.21
N

ATOM
162
CE1
HIS
A1024
0.691
22.048
9.295
1.00
54.57
C

ATOM
163
NE2
HIS
A1024
1.999
21.900
9.183
1.00
54.28
N

ATOM
164
C
HIS
A1024
1.877
23.218
4.249
1.00
49.79
C

ATOM
165
O
HIS
A1024
2.655
22.296
4.513
1.00
49.42
O

ATOM
166
N
GLU
A1025
1.987
23.983
3.167
1.00
49.05
N

ATOM
167
CA
GLU
A1025
3.043
23.796
2.179
1.00
48.04
C

ATOM
168
CB
GLU
A1025
2.813
24.722
0.984
1.00
50.62
C

ATOM
169
CG
GLU
A1025
3.876
24.605
−0.092
1.00
54.70
C

ATOM
170
CD
GLU
A1025
4.200
25.938
−0.735
1.00
56.22
C

ATOM
171
OE1
GLU
A1025
3.295
26.547
−1.343
1.00
58.24
O

ATOM
172
OE2
GLU
A1025
5.365
26.377
−0.627
1.00
58.15
O

ATOM
173
C
GLU
A1025
4.418
24.081
2.768
1.00
45.80
C

ATOM
174
O
GLU
A1025
5.433
23.604
2.258
1.00
46.85
O

ATOM
175
N
GLY
A1026
4.447
24.859
3.845
1.00
43.70
N

ATOM
176
CA
GLY
A1026
5.709
25.202
4.474
1.00
39.18
C

ATOM
177
C
GLY
A1026
6.425
24.069
5.192
1.00
37.08
C

ATOM
178
O
GLY
A1026
7.572
24.235
5.608
1.00
36.56
O

ATOM
179
N
PHE
A1027
5.771
22.920
5.337
1.00
33.78
N

ATOM
180
CA
PHE
A1027
6.390
21.791
6.028
1.00
31.60
C

ATOM
181
CB
PHE
A1027
5.397
20.637
6.179
1.00
30.22
C

ATOM
182
CG
PHE
A1027
5.951
19.469
6.951
1.00
30.68
C

ATOM
183
CD1
PHE
A1027
6.224
19.586
8.312
1.00
29.31
C

ATOM
184
CD2
PHE
A1027
6.230
18.266
6.313
1.00
29.88
C

ATOM
185
CE1
PHE
A1027
6.768
18.523
9.027
1.00
31.21
C

ATOM
186
CE2
PHE
A1027
6.775
17.194
7.020
1.00
30.83
C

ATOM
187
CZ
PHE
A1027
7.045
17.326
8.383
1.00
29.69
C

ATOM
188
C
PHE
A1027
7.653
21.266
5.345
1.00
29.93
C

ATOM
189
O
PHE
A1027
8.741
21.329
5.908
1.00
30.55
O

ATOM
190
N
ALA
A1028
7.504
20.739
4.135
1.00
29.11
N

ATOM
191
CA
ALA
A1028
8.637
20.196
3.400
1.00
28.78
C

ATOM
192
CB
ALA
A1028
8.213
19.836
1.986
1.00
28.60
C

ATOM
193
C
ALA
A1028
9.779
21.204
3.371
1.00
29.38
C

ATOM
194
O
ALA
A1028
10.940
20.850
3.579
1.00
28.07
O

ATOM
195
N
LYS
A1029
9.424
22.463
3.127
1.00
30.57
N

ATOM
196
CA
LYS
A1029
10.372
23.574
3.062
1.00
32.15
C

ATOM
197
CB
LYS
A1029
9.608
24.867
2.765
1.00
34.73
C

ATOM
198
CG
LYS
A1029
10.076
25.630
1.535
1.00
38.51
C

ATOM
199
CD
LYS
A1029
11.365
26.404
1.799
1.00
41.30
C

ATOM
200
CE
LYS
A1029
11.653
27.390
0.669
1.00
41.77
C

ATOM
201
NZ
LYS
A1029
12.865
28.214
0.927
1.00
43.68
N

ATOM
202
C
LYS
A1029
11.173
23.729
4.357
1.00
31.51
C

ATOM
203
O
LYS
A1029
12.362
24.043
4.326
1.00
31.47
O

ATOM
204
N
ARG
A1030
10.521
23.512
5.495
1.00
31.52
N

ATOM
205
CA
ARG
A1030
11.195
23.626
6.787
1.00
32.17
C

ATOM
206
CB
ARG
A1030
10.188
23.625
7.949
1.00
34.49
C

ATOM
207
CG
ARG
A1030
9.287
24.838
8.058
1.00
38.44
C

ATOM
208
CD
ARG
A1030
8.775
25.030
9.497
1.00
41.54
C

ATOM
209
NE
ARG
A1030
8.304
23.796
10.134
1.00
44.99
N

ATOM
210
CZ
ARG
A1030
9.084
22.932
10.786
1.00
47.20
C

ATOM
211
NH1
ARG
A1030
10.388
23.157
10.898
1.00
48.13
N

ATOM
212
NH2
ARG
A1030
8.562
21.841
11.337
1.00
47.12
N

ATOM
213
C
ARG
A1030
12.145
22.460
7.013
1.00
30.09
C

ATOM
214
O
ARG
A1030
13.248
22.631
7.530
1.00
29.93
O

ATOM
215
N
VAL
A1031
11.696
21.272
6.628
1.00
27.81
N

ATOM
216
CA
VAL
A1031
12.460
20.050
6.819
1.00
25.50
C

ATOM
217
CB
VAL
A1031
11.531
18.806
6.723
1.00
24.73
C

ATOM
218
CG1
VAL
A1031
12.355
17.518
6.871
1.00
24.35
C

ATOM
219
CG2
VAL
A1031
10.465
18.874
7.798
1.00
23.33
C

ATOM
220
C
VAL
A1031
13.621
19.835
5.861
1.00
25.01
C

ATOM
221
O
VAL
A1031
14.664
19.307
6.252
1.00
25.89
O

ATOM
222
N
LEU
A1032
13.451
20.253
4.617
1.00
24.38
N

ATOM
223
CA
LEU
A1032
14.472
20.027
3.604
1.00
25.25
C

ATOM
224
CB
LEU
A1032
13.818
19.409
2.370
1.00
25.23
C

ATOM
225
CG
LEU
A1032
12.870
18.230
2.597
1.00
23.47
C

ATOM
226
CD1
LEU
A1032
12.275
17.806
1.266
1.00
23.54
C

ATOM
227
CD2
LEU
A1032
13.624
17.072
3.239
1.00
23.54
C

ATOM
228
C
LEU
A1032
15.271
21.243
3.169
1.00
25.67
C

ATOM
229
O
LEU
A1032
14.778
22.371
3.184
1.00
25.62
O

ATOM
230
N
THR
A1033
16.516
20.997
2.776
1.00
26.32
N

ATOM
231
CA
THR
A1033
17.387
22.057
2.289
1.00
27.40
C

ATOM
232
CB
THR
A1033
18.862
21.628
2.283
1.00
27.76
C

ATOM
233
OG1
THR
A1033
19.015
20.490
1.425
1.00
26.35
O

ATOM
234
CG2
THR
A1033
19.331
21.271
3.691
1.00
28.10
C

ATOM
235
C
THR
A1033
16.963
22.275
0.844
1.00
27.65
C

ATOM
236
O
THR
A1033
16.071
21.588
0.350
1.00
27.78
O

ATOM
237
N
ALA
A1034
17.612
23.215
0.166
1.00
27.93
N

ATOM
238
CA
ALA
A1034
17.294
23.502
−1.225
1.00
28.06
C

ATOM
239
CB
ALA
A1034
18.089
24.717
−1.695
1.00
29.35
C

ATOM
240
C
ALA
A1034
17.594
22.296
−2.119
1.00
27.67
C

ATOM
241
O
ALA
A1034
16.791
21.940
−2.981
1.00
28.26
O

ATOM
242
N
LEU
A1035
18.752
21.675
−1.918
1.00
27.21
N

ATOM
243
CA
LEU
A1035
19.131
20.510
−2.711
1.00
29.21
C

ATOM
244
CB
LEU
A1035
20.531
20.015
−2.318
1.00
28.90
C

ATOM
245
CG
LEU
A1035
21.743
20.903
−2.634
1.00
32.48
C

ATOM
246
CD1
LEU
A1035
22.960
20.382
−1.877
1.00
31.19
C

ATOM
247
CD2
LEU
A1035
22.017
20.924
−4.137
1.00
32.53
C

ATOM
248
C
LEU
A1035
18.111
19.388
−2.514
1.00
27.97
C

ATOM
249
O
LEU
A1035
17.674
18.758
−3.475
1.00
28.70
O

ATOM
250
N
GLU
A1036
17.731
19.143
−1.267
1.00
27.27
N

ATOM
251
CA
GLU
A1036
16.757
18.100
−0.980
1.00
27.49
C

ATOM
252
CB
GLU
A1036
16.599
17.938
0.532
1.00
27.41
C

ATOM
253
CG
GLU
A1036
17.760
17.195
1.186
1.00
24.80
C

ATOM
254
CD
GLU
A1036
17.720
17.252
2.703
1.00
26.22
C

ATOM
255
OE1
GLU
A1036
18.225
16.306
3.345
1.00
25.82
O

ATOM
256
OE2
GLU
A1036
17.201
18.248
3.256
1.00
26.57
O

ATOM
257
C
GLU
A1036
15.413
18.416
−1.634
1.00
27.55
C

ATOM
258
O
GLU
A1036
14.740
17.522
−2.138
1.00
25.83
O

ATOM
259
N
MET
A1037
15.031
19.691
−1.640
1.00
28.35
N

ATOM
260
CA
MET
A1037
13.765
20.099
−2.247
1.00
29.92
C

ATOM
261
CB
MET
A1037
13.529
21.599
−2.069
1.00
30.37
C

ATOM
262
CG
MET
A1037
12.985
22.000
−0.714
1.00
33.04
C

ATOM
263
SD
MET
A1037
11.412
21.198
−0.336
1.00
35.56
S

ATOM
264
CE
MET
A1037
10.356
21.852
−1.624
1.00
33.04
C

ATOM
265
C
MET
A1037
13.758
19.779
−3.731
1.00
31.19
C

ATOM
266
O
MET
A1037
12.711
19.461
−4.306
1.00
30.89
O

ATOM
267
N
GLU
A1038
14.928
19.881
−4.352
1.00
31.50
N

ATOM
268
CA
GLU
A1038
15.049
19.600
−5.774
1.00
33.14
C

ATOM
269
CB
GLU
A1038
16.499
19.777
−6.233
1.00
34.77
C

ATOM
270
CG
GLU
A1038
17.005
21.208
−6.093
1.00
39.68
C

ATOM
271
CD
GLU
A1038
18.411
21.400
−6.639
1.00
41.20
C

ATOM
272
OE1
GLU
A1038
18.981
22.492
−6.434
1.00
44.15
O

ATOM
273
OE2
GLU
A1038
18.943
20.467
−7.276
1.00
42.51
O

ATOM
274
C
GLU
A1038
14.570
18.186
−6.066
1.00
31.14
C

ATOM
275
O
GLU
A1038
13.773
17.974
−6.976
1.00
31.21
O

ATOM
276
N
ARG
A1039
15.039
17.215
−5.290
1.00
29.70
N

ATOM
277
CA
ARG
A1039
14.606
15.844
−5.521
1.00
28.01
C

ATOM
278
CB
ARG
A1039
15.499
14.846
−4.778
1.00
29.96
C

ATOM
279
CG
ARG
A1039
15.061
13.406
−5.005
1.00
30.43
C

ATOM
280
CD
ARG
A1039
16.213
12.420
−4.969
1.00
30.42
C

ATOM
281
NE
ARG
A1039
15.723
11.046
−5.085
1.00
31.83
N

ATOM
282
CZ
ARG
A1039
15.203
10.509
−6.188
1.00
32.36
C

ATOM
283
NH1
ARG
A1039
15.098
11.214
−7.310
1.00
30.37
N

ATOM
284
NH2
ARG
A1039
14.764
9.258
−6.161
1.00
32.43
N

ATOM
285
C
ARG
A1039
13.158
15.671
−5.086
1.00
26.14
C

ATOM
286
O
ARG
A1039
12.367
15.046
−5.785
1.00
25.25
O

ATOM
287
N
PHE
A1040
12.808
16.233
−3.934
1.00
24.86
N

ATOM
288
CA
PHE
A1040
11.441
16.132
−3.430
1.00
26.03
C

ATOM
289
CB
PHE
A1040
11.273
17.007
−2.178
1.00
25.44
C

ATOM
290
CG
PHE
A1040
9.861
17.056
−1.657
1.00
26.41
C

ATOM
291
CD1
PHE
A1040
9.298
15.953
−1.027
1.00
25.83
C

ATOM
292
CD2
PHE
A1040
9.080
18.194
−1.838
1.00
26.12
C

ATOM
293
CE1
PHE
A1040
7.977
15.977
−0.585
1.00
24.52
C

ATOM
294
CE2
PHE
A1040
7.752
18.232
−1.399
1.00
26.23
C

ATOM
295
CZ
PHE
A1040
7.202
17.119
−0.772
1.00
23.77
C

ATOM
296
C
PHE
A1040
10.412
16.548
−4.488
1.00
26.70
C

ATOM
297
O
PHE
A1040
9.438
15.837
−4.731
1.00
29.10
O

ATOM
298
N
THR
A1041
10.635
17.691
−5.126
1.00
28.25
N

ATOM
299
CA
THR
A1041
9.705
18.195
−6.136
1.00
30.17
C

ATOM
300
CB
THR
A1041
9.935
19.700
−6.391
1.00
31.11
C

ATOM
301
OG1
THR
A1041
11.255
19.911
−6.904
1.00
32.37
O

ATOM
302
CG2
THR
A1041
9.781
20.478
−5.099
1.00
29.66
C

ATOM
303
C
THR
A1041
9.751
17.456
−7.474
1.00
31.98
C

ATOM
304
O
THR
A1041
8.863
17.627
−8.311
1.00
32.84
O

ATOM
305
N
SER
A1042
10.781
16.637
−7.673
1.00
31.91
N

ATOM
306
CA
SER
A1042
10.933
15.869
−8.909
1.00
32.77
C

ATOM
307
CB
SER
A1042
12.416
15.609
−9.192
1.00
33.18
C

ATOM
308
OG
SER
A1042
13.106
16.820
−9.448
1.00
38.29
O

ATOM
309
C
SER
A1042
10.215
14.529
−8.831
1.00
32.24
C

ATOM
310
O
SER
A1042
10.071
13.834
−9.840
1.00
32.01
O

ATOM
311
N
LEU
A1043
9.766
14.175
−7.630
1.00
29.92
N

ATOM
312
CA
LEU
A1043
9.101
12.901
−7.394
1.00
28.48
C

ATOM
313
CB
LEU
A1043
9.541
12.332
−6.043
1.00
23.86
C

ATOM
314
CG
LEU
A1043
11.050
12.097
−5.928
1.00
22.34
C

ATOM
315
CD1
LEU
A1043
11.391
11.610
−4.538
1.00
16.25
C

ATOM
316
CD2
LEU
A1043
11.493
11.073
−6.977
1.00
20.12
C

ATOM
317
C
LEU
A1043
7.587
12.967
−7.454
1.00
30.04
C

ATOM
318
O
LEU
A1043
6.995
14.045
−7.415
1.00
29.66
O

ATOM
319
N
LYS
A1044
6.970
11.793
−7.524
1.00
30.79
N

ATOM
320
CA
LYS
A1044
5.525
11.679
−7.633
1.00
32.89
C

ATOM
321
CB
LYS
A1044
5.167
11.102
−9.008
1.00
36.71
C

ATOM
322
CG
LYS
A1044
5.598
11.946
−10.199
1.00
40.80
C

ATOM
323
CD
LYS
A1044
4.583
13.041
−10.500
1.00
45.23
C

ATOM
324
CE
LYS
A1044
4.793
13.615
−11.897
1.00
47.01
C

ATOM
325
NZ
LYS
A1044
3.591
14.354
−12.387
1.00
48.79
N

ATOM
326
C
LYS
A1044
4.883
10.801
−6.564
1.00
31.67
C

ATOM
327
O
LYS
A1044
5.512
9.894
−6.017
1.00
31.18
O

ATOM
328
N
GLY
A1045
3.611
11.080
−6.299
1.00
30.41
N

ATOM
329
CA
GLY
A1045
2.834
10.321
−5.337
1.00
31.09
C

ATOM
330
C
GLY
A1045
3.518
9.841
−4.074
1.00
31.50
C

ATOM
331
O
GLY
A1045
4.098
10.631
−3.329
1.00
32.31
O

ATOM
332
N
ARG
A1046
3.435
8.534
−3.841
1.00
31.79
N

ATOM
333
CA
ARG
A1046
4.009
7.904
−2.659
1.00
34.20
C

ATOM
334
CB
ARG
A1046
3.791
6.386
−2.717
1.00
37.24
C

ATOM
335
CG
ARG
A1046
2.420
5.971
−3.239
1.00
43.96
C

ATOM
336
CD
ARG
A1046
2.301
4.457
−3.386
1.00
48.00
C

ATOM
337
NE
ARG
A1046
1.885
3.810
−2.144
1.00
52.29
N

ATOM
338
CZ
ARG
A1046
1.793
2.493
−1.980
1.00
53.80
C

ATOM
339
NH1
ARG
A1046
1.399
1.995
−0.815
1.00
54.77
N

ATOM
340
NH2
ARG
A1046
2.106
1.673
−2.975
1.00
56.31
N

ATOM
341
C
ARG
A1046
5.499
8.194
−2.516
1.00
32.21
C

ATOM
342
O
ARG
A1046
5.972
8.529
−1.433
1.00
32.82
O

ATOM
343
N
ARG
A1047
6.234
8.060
−3.614
1.00
31.05
N

ATOM
344
CA
ARG
A1047
7.670
8.292
−3.605
1.00
30.41
C

ATOM
345
CB
ARG
A1047
8.235
8.126
−5.015
1.00
32.83
C

ATOM
346
CG
ARG
A1047
9.252
7.013
−5.123
1.00
37.44
C

ATOM
347
CD
ARG
A1047
8.909
6.055
−6.246
1.00
40.57
C

ATOM
348
NE
ARG
A1047
9.734
4.854
−6.183
1.00
45.77
N

ATOM
349
CZ
ARG
A1047
9.635
3.835
−7.028
1.00
47.39
C

ATOM
350
NH1
ARG
A1047
10.428
2.780
−6.896
1.00
49.29
N

ATOM
351
NH2
ARG
A1047
8.743
3.873
−8.008
1.00
48.96
N

ATOM
352
C
ARG
A1047
8.040
9.668
−3.062
1.00
28.90
C

ATOM
353
O
ARG
A1047
9.006
9.808
−2.307
1.00
27.20
O

ATOM
354
N
GLN
A1048
7.268
10.680
−3.444
1.00
26.75
N

ATOM
355
CA
GLN
A1048
7.522
12.042
−2.993
1.00
25.72
C

ATOM
356
CB
GLN
A1048
6.552
13.014
−3.679
1.00
26.20
C

ATOM
357
CG
GLN
A1048
6.972
14.472
−3.555
1.00
26.13
C

ATOM
358
CD
GLN
A1048
6.169
15.400
−4.449
1.00
25.31
C

ATOM
359
OE1
GLN
A1048
6.618
16.495
−4.773
1.00
27.04
O

ATOM
360
NE2
GLN
A1048
4.977
14.970
−4.843
1.00
24.57
N

ATOM
361
C
GLN
A1048
7.390
12.162
−1.475
1.00
23.82
C

ATOM
362
O
GLN
A1048
8.225
12.783
−0.819
1.00
23.93
O

ATOM
363
N
ILE
A1049
6.340
11.568
−0.919
1.00
23.76
N

ATOM
364
CA
ILE
A1049
6.126
11.615
0.523
1.00
23.77
C

ATOM
365
CB
ILE
A1049
4.733
11.084
0.900
1.00
25.38
C

ATOM
366
CG2
ILE
A1049
4.598
11.001
2.401
1.00
25.87
C

ATOM
367
CG1
ILE
A1049
3.657
11.999
0.315
1.00
26.78
C

ATOM
368
CD1
ILE
A1049
3.787
13.453
0.751
1.00
30.33
C

ATOM
369
C
ILE
A1049
7.181
10.776
1.228
1.00
22.10
C

ATOM
370
O
ILE
A1049
7.673
11.150
2.283
1.00
21.61
O

ATOM
371
N
GLU
A1050
7.525
9.642
0.631
1.00
22.60
N

ATOM
372
CA
GLU
A1050
8.532
8.755
1.200
1.00
23.30
C

ATOM
373
CB
GLU
A1050
8.667
7.478
0.363
1.00
23.16
C

ATOM
374
CG
GLU
A1050
9.889
6.659
0.739
1.00
28.58
C

ATOM
375
CD
GLU
A1050
9.978
6.445
2.234
1.00
29.28
C

ATOM
376
OE1
GLU
A1050
11.108
6.330
2.760
1.00
30.35
O

ATOM
377
OE2
GLU
A1050
8.909
6.394
2.882
1.00
30.91
O

ATOM
378
C
GLU
A1050
9.885
9.454
1.279
1.00
22.26
C

ATOM
379
O
GLU
A1050
10.627
9.288
2.253
1.00
23.12
O

ATOM
380
N
TYR
A1051
10.209
10.245
0.262
1.00
22.07
N

ATOM
381
CA
TYR
A1051
11.478
10.948
0.262
1.00
21.63
C

ATOM
382
CB
TYR
A1051
11.686
11.704
−1.054
1.00
20.34
C

ATOM
383
CG
TYR
A1051
12.992
12.472
−1.082
1.00
20.50
C

ATOM
384
CD1
TYR
A1051
13.055
13.801
−0.659
1.00
20.43
C

ATOM
385
CE1
TYR
A1051
14.269
14.490
−0.621
1.00
20.01
C

ATOM
386
CD2
TYR
A1051
14.179
11.849
−1.475
1.00
20.86
C

ATOM
387
CE2
TYR
A1051
15.400
12.531
−1.441
1.00
21.25
C

ATOM
388
CZ
TYR
A1051
15.432
13.852
−1.010
1.00
19.89
C

ATOM
389
OH
TYR
A1051
16.630
14.525
−0.959
1.00
20.04
O

ATOM
390
C
TYR
A1051
11.557
11.920
1.434
1.00
21.88
C

ATOM
391
O
TYR
A1051
12.557
11.963
2.152
1.00
20.59
O

ATOM
392
N
LEU
A1052
10.499
12.702
1.621
1.00
21.63
N

ATOM
393
CA
LEU
A1052
10.452
13.671
2.706
1.00
21.68
C

ATOM
394
CB
LEU
A1052
9.179
14.513
2.590
1.00
20.47
C

ATOM
395
CG
LEU
A1052
8.808
15.418
3.765
1.00
22.03
C

ATOM
396
CD1
LEU
A1052
9.962
16.348
4.120
1.00
21.80
C

ATOM
397
CD2
LEU
A1052
7.566
16.209
3.381
1.00
20.67
C

ATOM
398
C
LEU
A1052
10.504
12.964
4.055
1.00
20.98
C

ATOM
399
O
LEU
A1052
11.314
13.306
4.919
1.00
21.63
O

ATOM
400
N
ALA
A1053
9.639
11.971
4.223
1.00
19.65
N

ATOM
401
CA
ALA
A1053
9.578
11.190
5.457
1.00
18.20
C

ATOM
402
CB
ALA
A1053
8.567
10.054
5.299
1.00
18.13
C

ATOM
403
C
ALA
A1053
10.952
10.614
5.818
1.00
17.32
C

ATOM
404
O
ALA
A1053
11.356
10.642
6.982
1.00
15.65
O

ATOM
405
N
GLY
A1054
11.660
10.092
4.816
1.00
16.84
N

ATOM
406
CA
GLY
A1054
12.978
9.516
5.049
1.00
16.81
C

ATOM
407
C
GLY
A1054
13.981
10.540
5.542
1.00
16.80
C

ATOM
408
O
GLY
A1054
14.788
10.270
6.439
1.00
16.69
O

ATOM
409
N
ARG
A1055
13.946
11.728
4.952
1.00
18.02
N

ATOM
410
CA
ARG
A1055
14.866
12.772
5.364
1.00
18.20
C

ATOM
411
CB
ARG
A1055
14.811
13.928
4.371
1.00
19.98
C

ATOM
412
CG
ARG
A1055
15.908
13.873
3.303
1.00
19.89
C

ATOM
413
CD
ARG
A1055
15.963
12.534
2.565
1.00
21.10
C

ATOM
414
NE
ARG
A1055
17.109
12.487
1.652
1.00
21.61
N

ATOM
415
CZ
ARG
A1055
17.449
11.426
0.925
1.00
21.69
C

ATOM
416
NH1
ARG
A1055
16.730
10.311
0.999
1.00
20.97
N

ATOM
417
NH2
ARG
A1055
18.508
11.481
0.122
1.00
17.88
N

ATOM
418
C
ARG
A1055
14.534
13.243
6.781
1.00
18.74
C

ATOM
419
O
ARG
A1055
15.433
13.506
7.585
1.00
16.13
O

ATOM
420
N
TRP
A1056
13.243
13.324
7.086
1.00
17.18
N

ATOM
421
CA
TRP
A1056
12.793
13.732
8.412
1.00
19.43
C

ATOM
422
CB
TRP
A1056
11.267
13.703
8.468
1.00
21.99
C

ATOM
423
CG
TRP
A1056
10.694
14.264
9.713
1.00
26.53
C

ATOM
424
CD2
TRP
A1056
10.311
13.533
10.877
1.00
28.20
C

ATOM
425
CE2
TRP
A1056
9.816
14.468
11.813
1.00
28.53
C

ATOM
426
CE3
TRP
A1056
10.333
12.177
11.222
1.00
29.04
C

ATOM
427
CD1
TRP
A1056
10.431
15.581
9.978
1.00
26.38
C

ATOM
428
NE1
TRP
A1056
9.905
15.708
11.237
1.00
29.97
N

ATOM
429
CZ2
TRP
A1056
9.347
14.090
13.073
1.00
30.15
C

ATOM
430
CZ3
TRP
A1056
9.868
11.801
12.476
1.00
31.30
C

ATOM
431
CH2
TRP
A1056
9.379
12.755
13.386
1.00
31.45
C

ATOM
432
C
TRP
A1056
13.343
12.710
9.412
1.00
18.72
C

ATOM
433
O
TRP
A1056
13.992
13.063
10.397
1.00
16.51
O

ATOM
434
N
SER
A1057
13.084
11.435
9.137
1.00
17.50
N

ATOM
435
CA
SER
A1057
13.532
10.352
10.011
1.00
19.23
C

ATOM
436
CB
SER
A1057
13.053
9.009
9.448
1.00
21.41
C

ATOM
437
OG
SER
A1057
13.243
7.971
10.388
1.00
25.06
O

ATOM
438
C
SER
A1057
15.053
10.320
10.201
1.00
19.01
C

ATOM
439
O
SER
A1057
15.549
10.120
11.317
1.00
19.71
O

ATOM
440
N
ALA
A1058
15.789
10.511
9.111
1.00
16.54
N

ATOM
441
CA
ALA
A1058
17.243
10.495
9.162
1.00
16.02
C

ATOM
442
CB
ALA
A1058
17.798
10.607
7.757
1.00
15.16
C

ATOM
443
C
ALA
A1058
17.790
11.616
10.035
1.00
15.70
C

ATOM
444
O
ALA
A1058
18.707
11.411
10.836
1.00
16.78
O

ATOM
445
N
LYS
A1059
17.221
12.805
9.884
1.00
16.69
N

ATOM
446
CA
LYS
A1059
17.664
13.957
10.648
1.00
18.17
C

ATOM
447
CB
LYS
A1059
17.079
15.240
10.042
1.00
18.92
C

ATOM
448
CG
LYS
A1059
17.536
15.450
8.588
1.00
19.75
C

ATOM
449
CD
LYS
A1059
17.059
16.773
8.003
1.00
19.99
C

ATOM
450
CE
LYS
A1059
17.531
16.933
6.549
1.00
19.86
C

ATOM
451
NZ
LYS
A1059
17.304
18.322
6.031
1.00
20.25
N

ATOM
452
C
LYS
A1059
17.302
13.818
12.116
1.00
19.11
C

ATOM
453
O
LYS
A1059
18.067
14.222
12.995
1.00
18.56
O

ATOM
454
N
GLU
A1060
16.143
13.225
12.374
1.00
18.52
N

ATOM
455
CA
GLU
A1060
15.679
12.998
13.736
1.00
21.84
C

ATOM
456
CB
GLU
A1060
14.247
12.448
13.704
1.00
26.26
C

ATOM
457
CG
GLU
A1060
13.428
12.722
14.952
1.00
33.87
C

ATOM
458
CD
GLU
A1060
13.083
14.192
15.130
1.00
35.47
C

ATOM
459
OE1
GLU
A1060
12.298
14.733
14.322
1.00
38.74
O

ATOM
460
OE2
GLU
A1060
13.601
14.811
16.082
1.00
39.14
O

ATOM
461
O
GLU
A1060
16.631
11.982
14.390
1.00
21.03
C

ATOM
462
O
GLU
A1060
17.045
12.149
15.544
1.00
18.91
O

ATOM
463
N
ALA
A1061
16.991
10.943
13.635
1.00
18.55
N

ATOM
464
CA
ALA
A1061
17.898
9.910
14.131
1.00
18.39
C

ATOM
465
CB
ALA
A1061
18.017
8.777
13.113
1.00
15.08
C

ATOM
466
C
ALA
A1061
19.283
10.490
14.429
1.00
18.00
C

ATOM
467
O
ALA
A1061
19.905
10.151
15.436
1.00
17.16
O

ATOM
468
N
PHE
A1062
19.768
11.352
13.542
1.00
18.20
N

ATOM
469
CA
PHE
A1062
21.069
11.970
13.741
1.00
20.25
C

ATOM
470
CB
PHE
A1062
21.433
12.855
12.546
1.00
20.89
C

ATOM
471
CG
PHE
A1062
22.721
13.605
12.730
1.00
23.32
C

ATOM
472
CD1
PHE
A1062
22.761
14.776
13.489
1.00
24.72
C

ATOM
473
CD2
PHE
A1062
23.908
13.112
12.194
1.00
23.55
C

ATOM
474
CE1
PHE
A1062
23.973
15.443
13.717
1.00
24.71
C

ATOM
475
CE2
PHE
A1062
25.119
13.766
12.414
1.00
23.92
C

ATOM
476
CZ
PHE
A1062
25.150
14.934
13.179
1.00
25.42
C

ATOM
477
C
PHE
A1062
21.090
12.800
15.026
1.00
21.33
C

ATOM
478
O
PHE
A1062
22.035
12.726
15.809
1.00
20.18
O

ATOM
479
N
SER
A1063
20.045
13.593
15.244
1.00
22.52
N

ATOM
480
CA
SER
A1063
19.973
14.420
16.445
1.00
24.40
C

ATOM
481
CB
SER
A1063
18.679
15.230
16.447
1.00
25.96
C

ATOM
482
OG
SER
A1063
18.670
16.112
15.338
1.00
30.50
O

ATOM
483
C
SER
A1063
20.060
13.562
17.704
1.00
24.30
C

ATOM
484
O
SER
A1063
20.714
13.938
18.682
1.00
23.77
O

ATOM
485
N
LYS
A1064
19.407
12.406
17.678
1.00
22.33
N

ATOM
486
CA
LYS
A1064
19.451
11.513
18.823
1.00
23.04
C

ATOM
487
CB
LYS
A1064
18.405
10.406
18.684
1.00
23.38
C

ATOM
488
CG
LYS
A1064
16.971
10.881
18.903
1.00
25.10
C

ATOM
489
CD
LYS
A1064
15.986
9.734
18.726
1.00
28.41
C

ATOM
490
CE
LYS
A1064
14.548
10.194
18.924
1.00
32.98
C

ATOM
491
NZ
LYS
A1064
13.566
9.195
18.410
1.00
35.52
N

ATOM
492
C
LYS
A1064
20.845
10.907
18.949
1.00
22.52
C

ATOM
493
O
LYS
A1064
21.285
10.572
20.047
1.00
21.41
O

ATOM
494
N
ALA
A1065
21.539
10.774
17.820
1.00
21.47
N

ATOM
495
CA
ALA
A1065
22.885
10.220
17.826
1.00
22.53
C

ATOM
496
CB
ALA
A1065
23.379
9.980
16.399
1.00
20.33
C

ATOM
497
C
ALA
A1065
23.796
11.207
18.537
1.00
24.41
C

ATOM
498
O
ALA
A1065
24.751
10.811
19.201
1.00
24.00
O

ATOM
499
N
MET
A1066
23.499
12.496
18.390
1.00
28.05
N

ATOM
500
CA
MET
A1066
24.283
13.530
19.049
1.00
32.04
C

ATOM
501
CB
MET
A1066
24.167
14.859
18.309
1.00
34.23
C

ATOM
502
CG
MET
A1066
24.913
14.895
16.997
1.00
40.28
C

ATOM
503
SD
MET
A1066
25.423
16.574
16.602
1.00
48.25
S

ATOM
504
CE
MET
A1066
27.174
16.492
17.024
1.00
46.99
C

ATOM
505
C
MET
A1066
23.826
13.716
20.493
1.00
33.24
C

ATOM
506
O
MET
A1066
24.456
14.443
21.254
1.00
33.60
O

ATOM
507
N
GLY
A1067
22.720
13.069
20.856
1.00
33.56
N

ATOM
508
CA
GLY
A1067
22.217
13.159
22.216
1.00
34.99
C

ATOM
509
C
GLY
A1067
21.311
14.339
22.519
1.00
36.72
C

ATOM
510
O
GLY
A1067
21.237
14.787
23.666
1.00
34.92
O

ATOM
511
N
THR
A1068
20.616
14.845
21.504
1.00
38.07
N

ATOM
512
CA
THR
A1068
19.716
15.975
21.699
1.00
39.81
C

ATOM
513
CB
THR
A1068
20.455
17.316
21.504
1.00
40.69
C

ATOM
514
OG1
THR
A1068
19.535
18.400
21.687
1.00
42.07
O

ATOM
515
CG2
THR
A1068
21.062
17.396
20.114
1.00
40.32
C

ATOM
516
C
THR
A1068
18.520
15.922
20.752
1.00
40.62
C

ATOM
517
O
THR
A1068
18.293
14.915
20.077
1.00
41.29
O

ATOM
518
N
GLY
A1069
17.753
17.007
20.716
1.00
40.61
N

ATOM
519
CA
GLY
A1069
16.586
17.061
19.856
1.00
40.92
C

ATOM
520
C
GLY
A1069
16.835
17.849
18.587
1.00
40.96
C

ATOM
521
O
GLY
A1069
17.705
18.722
18.547
1.00
41.30
O

ATOM
522
N
ILE
A1070
16.065
17.545
17.547
1.00
40.13
N

ATOM
523
CA
ILE
A1070
16.207
18.224
16.266
1.00
40.90
C

ATOM
524
CB
ILE
A1070
15.288
17.591
15.200
1.00
40.70
C

ATOM
525
CG2
ILE
A1070
13.828
17.774
15.593
1.00
40.55
C

ATOM
526
CG1
ILE
A1070
15.557
18.227
13.835
1.00
41.43
C

ATOM
527
CD1
ILE
A1070
16.980
18.055
13.352
1.00
39.85
C

ATOM
528
C
ILE
A1070
15.876
19.712
16.387
1.00
41.49
C

ATOM
529
O
ILE
A1070
16.354
20.533
15.598
1.00
41.31
O

ATOM
530
N
SER
A1071
15.058
20.054
17.379
1.00
41.78
N

ATOM
531
CA
SER
A1071
14.672
21.442
17.594
1.00
42.83
C

ATOM
532
CB
SER
A1071
13.546
21.531
18.633
1.00
43.42
C

ATOM
533
OG
SER
A1071
13.938
20.980
19.877
1.00
44.55
O

ATOM
534
C
SER
A1071
15.856
22.295
18.039
1.00
43.32
C

ATOM
535
O
SER
A1071
15.792
23.523
17.984
1.00
44.46
O

ATOM
536
N
LYS
A1072
16.938
21.648
18.472
1.00
42.56
N

ATOM
537
CA
LYS
A1072
18.123
22.377
18.911
1.00
41.56
C

ATOM
538
CB
LYS
A1072
18.744
21.706
20.141
1.00
41.25
C

ATOM
539
CG
LYS
A1072
19.600
20.489
19.844
0.05
41.20
C

ATOM
540
CD
LYS
A1072
21.069
20.860
19.724
0.05
41.09
C

ATOM
541
CE
LYS
A1072
21.602
21.414
21.037
0.05
41.02
C

ATOM
542
NZ
LYS
A1072
21.470
20.437
22.152
0.05
40.94
N

ATOM
543
C
LYS
A1072
19.139
22.462
17.777
1.00
41.40
C

ATOM
544
O
LYS
A1072
19.840
23.462
17.643
1.00
41.76
O

ATOM
545
N
LEU
A1073
19.220
21.413
16.960
1.00
40.37
N

ATOM
546
CA
LEU
A1073
20.142
21.411
15.829
1.00
38.42
C

ATOM
547
CB
LEU
A1073
20.439
19.985
15.339
1.00
39.84
C

ATOM
548
CG
LEU
A1073
21.489
19.100
16.015
1.00
40.56
C

ATOM
549
CD1
LEU
A1073
22.585
19.956
16.635
1.00
41.19
C

ATOM
550
CD2
LEU
A1073
20.820
18.243
17.064
1.00
42.23
C

ATOM
551
C
LEU
A1073
19.556
22.198
14.664
1.00
36.59
C

ATOM
552
O
LEU
A1073
20.205
23.091
14.123
1.00
36.83
O

ATOM
553
N
GLY
A1074
18.326
21.849
14.285
1.00
34.67
N

ATOM
554
CA
GLY
A1074
17.653
22.500
13.172
1.00
31.12
C

ATOM
555
C
GLY
A1074
17.746
21.631
11.927
1.00
29.81
C

ATOM
556
O
GLY
A1074
18.830
21.176
11.576
1.00
29.20
O

ATOM
557
N
PHE
A1075
16.619
21.396
11.260
1.00
29.29
N

ATOM
558
CA
PHE
A1075
16.595
20.565
10.051
1.00
29.15
C

ATOM
559
CB
PHE
A1075
15.163
20.442
9.502
1.00
28.80
C

ATOM
560
CG
PHE
A1075
14.244
19.610
10.353
1.00
29.16
C

ATOM
561
CD1
PHE
A1075
13.306
20.212
11.183
1.00
29.51
C

ATOM
562
CD2
PHE
A1075
14.309
18.221
10.315
1.00
28.39
C

ATOM
563
CE1
PHE
A1075
12.440
19.443
11.964
1.00
28.84
C

ATOM
564
CE2
PHE
A1075
13.451
17.445
11.089
1.00
30.94
C

ATOM
565
CZ
PHE
A1075
12.514
18.059
11.916
1.00
29.27
C

ATOM
566
C
PHE
A1075
17.500
21.072
8.922
1.00
29.25
C

ATOM
567
O
PHE
A1075
18.096
20.275
8.193
1.00
27.78
O

ATOM
568
N
GLN
A1076
17.589
22.393
8.772
1.00
29.64
N

ATOM
569
CA
GLN
A1076
18.397
23.008
7.717
1.00
29.73
C

ATOM
570
CB
GLN
A1076
18.046
24.497
7.593
1.00
31.55
C

ATOM
571
CG
GLN
A1076
16.585
24.746
7.253
1.00
31.77
C

ATOM
572
CD
GLN
A1076
16.202
24.181
5.895
1.00
32.15
C

ATOM
573
OE1
GLN
A1076
15.044
23.849
5.652
1.00
34.09
O

ATOM
574
NE2
GLN
A1076
17.174
24.084
5.002
1.00
32.35
N

ATOM
575
C
GLN
A1076
19.888
22.845
7.975
1.00
31.01
C

ATOM
576
O
GLN
A1076
20.724
23.105
7.099
1.00
30.59
O

ATOM
577
N
ASP
A1077
20.211
22.401
9.183
1.00
30.30
N

ATOM
578
CA
ASP
A1077
21.592
22.182
9.588
1.00
30.99
C

ATOM
579
CB
ASP
A1077
21.684
22.266
11.111
1.00
34.42
C

ATOM
580
CG
ASP
A1077
22.894
23.034
11.578
1.00
38.94
C

ATOM
581
OD1
ASP
A1077
24.025
22.549
11.358
1.00
40.63
O

ATOM
582
OD2
ASP
A1077
22.710
24.127
12.162
1.00
41.18
O

ATOM
583
C
ASP
A1077
22.066
20.803
9.114
1.00
28.98
C

ATOM
584
O
ASP
A1077
23.247
20.470
9.198
1.00
27.03
O

ATOM
585
N
LEU
A1078
21.134
19.998
8.622
1.00
26.47
N

ATOM
586
CA
LEU
A1078
21.472
18.665
8.155
1.00
25.11
C

ATOM
587
CB
LEU
A1078
20.782
17.614
9.029
1.00
25.83
C

ATOM
588
CG
LEU
A1078
21.066
17.667
10.529
1.00
25.61
C

ATOM
589
CD1
LEU
A1078
20.075
16.787
11.291
1.00
26.16
C

ATOM
590
CD2
LEU
A1078
22.494
17.227
10.775
1.00
26.52
C

ATOM
591
C
LEU
A1078
21.015
18.495
6.723
1.00
24.62
C

ATOM
592
O
LEU
A1078
20.052
19.125
6.296
1.00
25.13
O

ATOM
593
N
GLU
A1079
21.710
17.648
5.975
1.00
23.38
N

ATOM
594
CA
GLU
A1079
21.312
17.388
4.603
1.00
22.76
C

ATOM
595
CB
GLU
A1079
22.008
18.338
3.639
1.00
24.57
C

ATOM
596
CG
GLU
A1079
21.425
18.299
2.241
1.00
25.55
C

ATOM
597
CD
GLU
A1079
22.219
19.146
1.274
1.00
28.95
C

ATOM
598
OE1
GLU
A1079
23.415
18.844
1.074
1.00
28.46
O

ATOM
599
OE2
GLU
A1079
21.652
20.114
0.722
1.00
31.06
O

ATOM
600
C
GLU
A1079
21.639
15.958
4.220
1.00
21.67
C

ATOM
601
O
GLU
A1079
22.747
15.476
4.458
1.00
21.79
O

ATOM
602
N
VAL
A1080
20.667
15.283
3.626
1.00
18.92
N

ATOM
603
CA
VAL
A1080
20.861
13.904
3.208
1.00
19.27
C

ATOM
604
CB
VAL
A1080
19.836
12.967
3.881
1.00
18.84
C

ATOM
605
CG1
VAL
A1080
20.181
11.504
3.578
1.00
18.64
C

ATOM
606
CG2
VAL
A1080
19.801
13.230
5.368
1.00
18.66
C

ATOM
607
C
VAL
A1080
20.690
13.798
1.696
1.00
19.85
C

ATOM
608
O
VAL
A1080
19.596
14.003
1.169
1.00
19.06
O

ATOM
609
N
LEU
A1081
21.780
13.497
1.003
1.00
19.76
N

ATOM
610
CA
LEU
A1081
21.742
13.332
−0.442
1.00
20.15
C

ATOM
611
CB
LEU
A1081
22.808
14.210
−1.111
1.00
19.63
C

ATOM
612
CG
LEU
A1081
22.640
15.717
−0.878
1.00
19.82
C

ATOM
613
CD1
LEU
A1081
23.817
16.488
−1.475
1.00
19.43
C

ATOM
614
CD2
LEU
A1081
21.326
16.171
−1.485
1.00
18.80
C

ATOM
615
C
LEU
A1081
22.037
11.861
−0.696
1.00
20.78
C

ATOM
616
O
LEU
A1081
22.097
11.067
0.242
1.00
19.52
O

ATOM
617
N
ASN
A1082
22.224
11.495
−1.957
1.00
21.64
N

ATOM
618
CA
ASN
A1082
22.521
10.110
−2.301
1.00
22.51
C

ATOM
619
CB
ASN
A1082
21.430
9.574
−3.230
1.00
21.83
C

ATOM
620
CG
ASN
A1082
20.134
9.281
−2.485
1.00
24.97
C

ATOM
621
OD1
ASN
A1082
19.930
8.174
−1.973
1.00
26.72
O

ATOM
622
ND2
ASN
A1082
19.264
10.275
−2.402
1.00
23.64
N

ATOM
623
C
ASN
A1082
23.897
10.029
−2.954
1.00
22.59
C

ATOM
624
O
ASN
A1082
24.196
10.786
−3.876
1.00
23.10
O

ATOM
625
N
ASN
A1083
24.738
9.118
−2.472
1.00
21.81
N

ATOM
626
CA
ASN
A1083
26.079
8.998
−3.021
1.00
24.05
C

ATOM
627
CB
ASN
A1083
27.011
8.298
−2.018
1.00
21.32
C

ATOM
628
CG
ASN
A1083
26.634
6.849
−1.748
1.00
23.86
C

ATOM
629
OD1
ASN
A1083
27.083
6.269
−0.752
1.00
23.67
O

ATOM
630
ND2
ASN
A1083
25.835
6.249
−2.631
1.00
20.56
N

ATOM
631
C
ASN
A1083
26.112
8.315
−4.385
1.00
26.50
C

ATOM
632
O
ASN
A1083
25.065
7.986
−4.951
1.00
25.00
O

ATOM
633
N
GLU
A1084
27.313
8.118
−4.921
1.00
28.34
N

ATOM
634
CA
GLU
A1084
27.447
7.514
−6.237
1.00
32.10
C

ATOM
635
CB
GLU
A1084
28.907
7.561
−6.700
1.00
32.77
C

ATOM
636
CG
GLU
A1084
29.885
6.749
−5.877
1.00
35.30
C

ATOM
637
CD
GLU
A1084
31.327
7.041
−6.263
1.00
38.54
C

ATOM
638
OE1
GLU
A1084
31.628
7.058
−7.478
1.00
39.35
O

ATOM
639
OE2
GLU
A1084
32.160
7.252
−5.356
1.00
40.56
O

ATOM
640
C
GLU
A1084
26.906
6.092
−6.307
1.00
32.37
C

ATOM
641
O
GLU
A1084
26.582
5.610
−7.386
1.00
34.17
O

ATOM
642
N
ARG
A1085
26.811
5.426
−5.158
1.00
31.86
N

ATOM
643
CA
ARG
A1085
26.278
4.069
−5.111
1.00
29.86
C

ATOM
644
CB
ARG
A1085
26.967
3.259
−4.009
1.00
30.40
C

ATOM
645
CG
ARG
A1085
28.442
2.992
−4.269
0.05
30.17
C

ATOM
646
CD
ARG
A1085
28.668
2.173
−5.540
0.05
30.07
C

ATOM
647
NE
ARG
A1085
28.539
0.730
−5.333
0.05
30.12
N

ATOM
648
CZ
ARG
A1085
27.396
0.089
−5.107
0.05
30.07
C

ATOM
649
NH1
ARG
A1085
26.249
0.751
−5.054
0.05
30.16
N

ATOM
650
NH2
ARG
A1085
27.401
−1.226
−4.938
0.05
30.04
N

ATOM
651
C
ARG
A1085
24.768
4.117
−4.860
1.00
28.84
C

ATOM
652
O
ARG
A1085
24.121
3.084
−4.683
1.00
28.73
O

ATOM
653
N
GLY
A1086
24.222
5.329
−4.842
1.00
26.09
N

ATOM
654
CA
GLY
A1086
22.797
5.514
−4.635
1.00
24.49
C

ATOM
655
C
GLY
A1086
22.286
5.493
−3.202
1.00
23.98
C

ATOM
656
O
GLY
A1086
21.090
5.649
−2.975
1.00
25.43
O

ATOM
657
N
ALA
A1087
23.172
5.306
−2.233
1.00
21.90
N

ATOM
658
CA
ALA
A1087
22.755
5.259
−0.836
1.00
21.27
C

ATOM
659
CB
ALA
A1087
23.704
4.379
−0.042
1.00
21.23
C

ATOM
660
C
ALA
A1087
22.689
6.653
−0.205
1.00
21.63
C

ATOM
661
O
ALA
A1087
23.508
7.529
−0.499
1.00
19.21
O

ATOM
662
N
PRO
A1088
21.700
6.872
0.668
1.00
20.00
N

ATOM
663
CD
PRO
A1088
20.666
5.919
1.105
1.00
20.94
C

ATOM
664
CA
PRO
A1088
21.544
8.164
1.335
1.00
20.18
C

ATOM
665
CB
PRO
A1088
20.212
8.013
2.064
1.00
20.85
C

ATOM
666
CG
PRO
A1088
20.183
6.545
2.390
1.00
22.84
C

ATOM
667
C
PRO
A1088
22.714
8.380
2.281
1.00
19.50
C

ATOM
668
O
PRO
A1088
23.220
7.431
2.887
1.00
17.61
O

ATOM
669
N
TYR
A1089
23.164
9.621
2.395
1.00
18.16
N

ATOM
670
CA
TYR
A1089
24.281
9.913
3.279
1.00
19.12
C

ATOM
671
CB
TYR
A1089
25.611
9.642
2.557
1.00
20.66
C

ATOM
672
CG
TYR
A1089
25.977
10.698
1.534
1.00
23.33
C

ATOM
673
CD1
TYR
A1089
26.869
11.724
1.853
1.00
22.08
C

ATOM
674
CE1
TYR
A1089
27.211
12.699
0.916
1.00
22.82
C

ATOM
675
CD2
TYR
A1089
25.426
10.673
0.249
1.00
22.30
C

ATOM
676
CE2
TYR
A1089
25.752
11.642
−0.692
1.00
23.44
C

ATOM
677
CZ
TYR
A1089
26.649
12.655
−0.354
1.00
25.15
C

ATOM
678
OH
TYR
A1089
26.987
13.614
−1.288
1.00
24.63
O

ATOM
679
C
TYR
A1089
24.205
11.363
3.699
1.00
17.64
C

ATOM
680
O
TYR
A1089
23.578
12.178
3.023
1.00
16.44
O

ATOM
681
N
PHE
A1090
24.824
11.691
4.825
1.00
17.81
N

ATOM
682
CA
PHE
A1090
24.801
13.070
5.277
1.00
17.81
C

ATOM
683
CB
PHE
A1090
25.019
13.159
6.791
1.00
17.48
C

ATOM
684
CG
PHE
A1090
23.777
12.873
7.595
1.00
17.01
C

ATOM
685
CD1
PHE
A1090
23.434
11.568
7.938
1.00
17.02
C

ATOM
686
CD2
PHE
A1090
22.919
13.910
7.962
1.00
16.23
C

ATOM
687
CE1
PHE
A1090
22.247
11.293
8.632
1.00
17.95
C

ATOM
688
CE2
PHE
A1090
21.732
13.647
8.656
1.00
17.65
C

ATOM
689
CZ
PHE
A1090
21.397
12.333
8.989
1.00
16.73
C

ATOM
690
C
PHE
A1090
25.852
13.892
4.547
1.00
20.29
C

ATOM
691
O
PHE
A1090
27.054
13.713
4.749
1.00
19.58
O

ATOM
692
N
SER
A1091
25.384
14.767
3.665
1.00
21.20
N

ATOM
693
CA
SER
A1091
26.266
15.646
2.921
1.00
23.08
C

ATOM
694
CB
SER
A1091
25.592
16.086
1.618
1.00
24.12
C

ATOM
695
OG
SER
A1091
24.281
16.567
1.852
1.00
24.36
O

ATOM
696
C
SER
A1091
26.580
16.856
3.806
1.00
24.80
C

ATOM
697
O
SER
A1091
27.613
17.507
3.642
1.00
25.24
O

ATOM
698
N
GLN
A1092
25.685
17.141
4.752
1.00
24.80
N

ATOM
699
CA
GLN
A1092
25.853
18.254
5.688
1.00
24.09
C

ATOM
700
CB
GLN
A1092
24.970
19.448
5.296
1.00
26.54
C

ATOM
701
CG
GLN
A1092
25.294
20.132
3.971
1.00
30.86
C

ATOM
702
CD
GLN
A1092
26.711
20.678
3.907
1.00
34.83
C

ATOM
703
OE1
GLN
A1092
27.257
21.147
4.910
1.00
37.27
O

ATOM
704
NE2
GLN
A1092
27.308
20.637
2.717
1.00
34.99
N

ATOM
705
C
GLN
A1092
25.453
17.803
7.096
1.00
23.97
C

ATOM
706
O
GLN
A1092
24.343
17.295
7.300
1.00
22.36
O

ATOM
707
N
ALA
A1093
26.356
17.989
8.057
1.00
20.55
N

ATOM
708
CA
ALA
A1093
26.097
17.621
9.447
1.00
21.00
C

ATOM
709
CB
ALA
A1093
25.948
16.101
9.580
1.00
17.57
C

ATOM
710
C
ALA
A1093
27.235
18.114
10.336
1.00
22.11
C

ATOM
711
O
ALA
A1093
28.392
18.120
9.920
1.00
23.23
O

ATOM
712
N
PRO
A1094
26.918
18.536
11.573
1.00
23.31
N

ATOM
713
CD
PRO
A1094
25.550
18.680
12.111
1.00
23.07
C

ATOM
714
CA
PRO
A1094
27.907
19.034
12.533
1.00
24.58
C

ATOM
715
CB
PRO
A1094
27.053
19.820
13.521
1.00
24.45
C

ATOM
716
CG
PRO
A1094
25.798
18.997
13.575
1.00
24.77
C

ATOM
717
C
PRO
A1094
28.687
17.909
13.219
1.00
26.12
C

ATOM
718
O
PRO
A1094
28.675
17.791
14.445
1.00
27.56
O

ATOM
719
N
PHE
A1095
29.353
17.079
12.423
1.00
26.05
N

ATOM
720
CA
PHE
A1095
30.139
15.975
12.957
1.00
26.02
C

ATOM
721
CB
PHE
A1095
29.279
14.710
13.090
1.00
27.36
C

ATOM
722
CG
PHE
A1095
30.016
13.544
13.674
1.00
26.42
C

ATOM
723
CD1
PHE
A1095
30.208
12.385
12.931
1.00
26.59
C

ATOM
724
CD2
PHE
A1095
30.571
13.625
14.950
1.00
27.10
C

ATOM
725
CE1
PHE
A1095
30.946
11.324
13.446
1.00
26.29
C

ATOM
726
CE2
PHE
A1095
31.312
12.574
15.475
1.00
25.68
C

ATOM
727
CZ
PHE
A1095
31.502
11.417
14.720
1.00
27.52
C

ATOM
728
C
PHE
A1095
31.305
15.727
12.012
1.00
26.40
C

ATOM
729
O
PHE
A1095
31.122
15.681
10.792
1.00
25.80
O

ATOM
730
N
SER
A1096
32.498
15.560
12.577
1.00
26.14
N

ATOM
731
CA
SER
A1096
33.705
15.357
11.781
1.00
29.05
C

ATOM
732
CB
SER
A1096
34.909
15.969
12.500
1.00
30.71
C

ATOM
733
OG
SER
A1096
34.768
17.373
12.603
1.00
37.13
O

ATOM
734
C
SER
A1096
34.039
13.919
11.413
1.00
28.85
C

ATOM
735
O
SER
A1096
34.702
13.678
10.407
1.00
29.54
O

ATOM
736
N
GLY
A1097
33.595
12.968
12.229
1.00
28.58
N

ATOM
737
CA
GLY
A1097
33.888
11.573
11.957
1.00
27.16
C

ATOM
738
C
GLY
A1097
32.991
10.948
10.907
1.00
26.54
C

ATOM
739
O
GLY
A1097
32.406
11.648
10.077
1.00
27.09
O

ATOM
740
N
LYS
A1098
32.888
9.624
10.931
1.00
24.94
N

ATOM
741
CA
LYS
A1098
32.045
8.930
9.973
1.00
25.69
C

ATOM
742
CB
LYS
A1098
32.587
7.535
9.644
1.00
29.36
C

ATOM
743
CG
LYS
A1098
33.687
7.015
10.547
1.00
33.98
C

ATOM
744
CD
LYS
A1098
35.051
7.532
10.120
1.00
37.43
C

ATOM
745
CE
LYS
A1098
36.164
6.583
10.568
1.00
39.11
C

ATOM
746
NZ
LYS
A1098
36.119
6.320
12.033
1.00
41.00
N

ATOM
747
C
LYS
A1098
30.625
8.796
10.492
1.00
24.62
C

ATOM
748
O
LYS
A1098
30.393
8.494
11.668
1.00
22.63
O

ATOM
749
N
ILE
A1099
29.677
9.033
9.600
1.00
22.17
N

ATOM
750
CA
ILE
A1099
28.273
8.932
9.941
1.00
21.57
C

ATOM
751
CB
ILE
A1099
27.514
10.193
9.523
1.00
19.45
C

ATOM
752
CG2
ILE
A1099
26.039
10.056
9.905
1.00
18.01
C

ATOM
753
CG1
ILE
A1099
28.155
11.419
10.177
1.00
20.05
C

ATOM
754
CD1
ILE
A1099
27.677
12.738
9.613
1.00
19.45
C

ATOM
755
C
ILE
A1099
27.695
7.748
9.184
1.00
21.84
C

ATOM
756
O
ILE
A1099
27.597
7.775
7.958
1.00
24.63
O

ATOM
757
N
TRP
A1100
27.334
6.699
9.907
1.00
20.85
N

ATOM
758
CA
TRP
A1100
26.760
5.532
9.270
1.00
19.86
C

ATOM
759
CB
TRP
A1100
27.172
4.260
10.009
1.00
18.86
C

ATOM
760
CG
TRP
A1100
28.652
4.007
9.945
1.00
19.33
C

ATOM
761
CD2
TRP
A1100
29.370
3.395
8.864
1.00
20.59
C

ATOM
762
CE2
TRP
A1100
30.743
3.416
9.209
1.00
20.05
C

ATOM
763
CE3
TRP
A1100
28.987
2.835
7.634
1.00
19.76
C

ATOM
764
CD1
TRP
A1100
29.590
4.362
10.873
1.00
19.35
C

ATOM
765
NE1
TRP
A1100
30.846
4.010
10.439
1.00
18.87
N

ATOM
766
CZ2
TRP
A1100
31.739
2.895
8.369
1.00
19.48
C

ATOM
767
CZ3
TRP
A1100
29.978
2.317
6.796
1.00
22.42
C

ATOM
768
CH2
TRP
A1100
31.343
2.354
7.172
1.00
20.56
C

ATOM
769
C
TRP
A1100
25.251
5.718
9.294
1.00
20.31
C

ATOM
770
O
TRP
A1100
24.633
5.795
10.357
1.00
20.18
O

ATOM
771
N
LEU
A1101
24.663
5.829
8.113
1.00
18.06
N

ATOM
772
CA
LEU
A1101
23.229
6.023
8.019
1.00
17.46
C

ATOM
773
CB
LEU
A1101
22.915
7.399
7.409
1.00
15.91
C

ATOM
774
CG
LEU
A1101
21.475
7.611
6.919
1.00
15.54
C

ATOM
775
CD1
LEU
A1101
20.510
7.621
8.101
1.00
14.01
C

ATOM
776
CD2
LEU
A1101
21.380
8.931
6.150
1.00
12.69
C

ATOM
777
C
LEU
A1101
22.561
4.945
7.190
1.00
17.42
C

ATOM
778
O
LEU
A1101
23.124
4.436
6.218
1.00
15.25
O

ATOM
779
N
SER
A1102
21.353
4.582
7.600
1.00
17.54
N

ATOM
780
CA
SER
A1102
20.581
3.607
6.865
1.00
15.75
C

ATOM
781
CB
SER
A1102
20.832
2.189
7.364
1.00
16.41
C

ATOM
782
OG
SER
A1102
20.242
1.258
6.469
1.00
14.51
O

ATOM
783
C
SER
A1102
19.129
3.980
7.063
1.00
17.48
C

ATOM
784
O
SER
A1102
18.711
4.322
8.173
1.00
16.20
O

ATOM
785
N
ILE
A1103
18.376
3.940
5.968
1.00
17.02
N

ATOM
786
CA
ILE
A1103
16.963
4.274
5.979
1.00
17.85
C

ATOM
787
CB
ILE
A1103
16.691
5.576
5.194
1.00
19.00
C

ATOM
788
CG2
ILE
A1103
15.207
5.948
5.278
1.00
18.57
C

ATOM
789
CG1
ILE
A1103
17.554
6.706
5.754
1.00
18.22
C

ATOM
790
CD1
ILE
A1103
17.414
8.014
4.999
1.00
20.97
C

ATOM
791
C
ILE
A1103
16.239
3.130
5.291
1.00
17.46
C

ATOM
792
O
ILE
A1103
16.769
2.510
4.368
1.00
17.27
O

ATOM
793
N
SER
A1104
15.033
2.845
5.751
1.00
14.92
N

ATOM
794
CA
SER
A1104
14.240
1.772
5.175
1.00
17.06
C

ATOM
795
CB
SER
A1104
14.566
0.447
5.876
1.00
15.94
C

ATOM
796
OG
SER
A1104
13.790
−0.613
5.342
1.00
15.77
O

ATOM
797
C
SER
A1104
12.779
2.155
5.384
1.00
17.20
C

ATOM
798
O
SER
A1104
12.453
2.859
6.333
1.00
15.90
O

ATOM
799
N
HIS
A1105
11.902
1.699
4.502
1.00
18.52
N

ATOM
800
CA
HIS
A1105
10.494
2.048
4.619
1.00
20.22
C

ATOM
801
CB
HIS
A1105
10.199
3.316
3.813
1.00
23.50
C

ATOM
802
CG
HIS
A1105
10.358
3.127
2.334
1.00
25.77
C

ATOM
803
CD2
HIS
A1105
9.487
2.690
1.392
1.00
26.90
C

ATOM
804
ND1
HIS
A1105
11.563
3.301
1.687
1.00
26.39
N

ATOM
805
CE1
HIS
A1105
11.428
2.977
0.412
1.00
27.48
C

ATOM
806
NE2
HIS
A1105
10.177
2.601
0.208
1.00
27.67
N

ATOM
807
C
HIS
A1105
9.597
0.953
4.079
1.00
21.15
C

ATOM
808
O
HIS
A1105
10.054
0.040
3.392
1.00
21.16
O

ATOM
809
N
THR
A1106
8.313
1.067
4.402
1.00
21.46
N

ATOM
810
CA
THR
A1106
7.290
0.160
3.911
1.00
22.28
C

ATOM
811
CB
THR
A1106
6.646
−0.682
5.032
1.00
21.51
C

ATOM
812
OG1
THR
A1106
5.891
0.169
5.904
1.00
19.68
O

ATOM
813
CG2
THR
A1106
7.716
−1.415
5.827
1.00
21.79
C

ATOM
814
C
THR
A1106
6.263
1.161
3.386
1.00
24.40
C

ATOM
815
O
THR
A1106
6.560
2.356
3.309
1.00
22.60
O

ATOM
816
N
ASP
A1107
5.070
0.698
3.032
1.00
25.68
N

ATOM
817
CA
ASP
A1107
4.050
1.612
2.534
1.00
28.90
C

ATOM
818
CB
ASP
A1107
2.952
0.845
1.787
1.00
34.46
C

ATOM
819
CG
ASP
A1107
3.479
0.098
0.574
1.00
40.33
C

ATOM
820
OD1
ASP
A1107
4.229
0.704
−0.225
1.00
43.51
O

ATOM
821
OD2
ASP
A1107
3.134
−1.093
0.413
1.00
43.99
O

ATOM
822
C
ASP
A1107
3.420
2.385
3.691
1.00
28.81
C

ATOM
823
O
ASP
A1107
2.613
3.285
3.470
1.00
29.78
O

ATOM
824
N
GLN
A1108
3.801
2.049
4.921
1.00
25.83
N

ATOM
825
CA
GLN
A1108
3.228
2.710
6.086
1.00
24.71
C

ATOM
826
CB
GLN
A1108
2.384
1.710
6.867
1.00
27.32
C

ATOM
827
CG
GLN
A1108
1.328
1.026
6.030
1.00
32.60
C

ATOM
828
CD
GLN
A1108
0.951
−0.324
6.583
1.00
35.93
C

ATOM
829
OE1
GLN
A1108
1.085
−1.344
5.902
1.00
37.52
O

ATOM
830
NE2
GLN
A1108
0.481
−0.346
7.829
1.00
36.07
N

ATOM
831
C
GLN
A1108
4.224
3.356
7.038
1.00
24.10
C

ATOM
832
O
GLN
A1108
3.879
4.305
7.742
1.00
23.70
O

ATOM
833
N
PHE
A1109
5.448
2.840
7.082
1.00
22.72
N

ATOM
834
CA
PHE
A1109
6.452
3.389
7.983
1.00
21.31
C

ATOM
835
CB
PHE
A1109
6.719
2.446
9.164
1.00
22.89
C

ATOM
836
CG
PHE
A1109
5.518
2.151
10.004
1.00
25.18
C

ATOM
837
CD1
PHE
A1109
4.746
1.018
9.763
1.00
26.55
C

ATOM
838
CD2
PHE
A1109
5.155
3.003
11.044
1.00
26.19
C

ATOM
839
CE1
PHE
A1109
3.626
0.734
10.549
1.00
26.78
C

ATOM
840
CE2
PHE
A1109
4.037
2.729
11.834
1.00
26.65
C

ATOM
841
CZ
PHE
A1109
3.273
1.591
11.584
1.00
25.88
C

ATOM
842
C
PHE
A1109
7.785
3.630
7.318
1.00
20.22
C

ATOM
843
O
PHE
A1109
8.096
3.053
6.275
1.00
19.27
O

ATOM
844
N
VAL
A1110
8.573
4.489
7.951
1.00
18.43
N

ATOM
845
CA
VAL
A1110
9.925
4.781
7.507
1.00
19.10
C

ATOM
846
CB
VAL
A1110
10.049
6.191
6.846
1.00
19.04
C

ATOM
847
CG1
VAL
A1110
9.654
7.277
7.820
1.00
19.30
C

ATOM
848
CG2
VAL
A1110
11.474
6.412
6.359
1.00
23.53
C

ATOM
849
C
VAL
A1110
10.744
4.718
8.797
1.00
19.12
C

ATOM
850
O
VAL
A1110
10.287
5.169
9.854
1.00
17.72
O

ATOM
851
N
THR
A1111
11.925
4.115
8.720
1.00
18.67
N

ATOM
852
CA
THR
A1111
12.805
3.992
9.875
1.00
20.42
C

ATOM
853
CB
THR
A1111
12.897
2.525
10.397
1.00
22.98
C

ATOM
854
OG1
THR
A1111
13.363
1.670
9.345
1.00
25.86
O

ATOM
855
CG2
THR
A1111
11.548
2.029
10.874
1.00
24.99
C

ATOM
856
C
THR
A1111
14.200
4.421
9.456
1.00
20.11
C

ATOM
857
O
THR
A1111
14.575
4.287
8.291
1.00
20.53
O

ATOM
858
N
ALA
A1112
14.962
4.946
10.404
1.00
17.15
N

ATOM
859
CA
ALA
A1112
16.321
5.370
10.119
1.00
18.28
C

ATOM
860
CB
ALA
A1112
16.357
6.858
9.791
1.00
16.81
C

ATOM
861
C
ALA
A1112
17.190
5.080
11.328
1.00
18.04
C

ATOM
862
O
ALA
A1112
16.721
5.142
12.464
1.00
17.37
O

ATOM
863
N
SER
A1113
18.454
4.755
11.075
1.00
17.48
N

ATOM
864
CA
SER
A1113
19.401
4.479
12.146
1.00
17.23
C

ATOM
865
CB
SER
A1113
19.635
2.967
12.283
1.00
15.09
C

ATOM
866
OG
SER
A1113
20.666
2.686
13.224
1.00
16.24
O

ATOM
867
C
SER
A1113
20.718
5.187
11.844
1.00
17.94
C

ATOM
868
O
SER
A1113
21.209
5.158
10.712
1.00
18.05
O

ATOM
869
N
VAL
A1114
21.285
5.832
12.857
1.00
18.42
N

ATOM
870
CA
VAL
A1114
22.546
6.543
12.683
1.00
17.97
C

ATOM
871
CB
VAL
A1114
22.350
8.082
12.783
1.00
17.35
C

ATOM
872
CG1
VAL
A1114
23.708
8.784
12.874
1.00
15.58
C

ATOM
873
CG2
VAL
A1114
21.571
8.592
11.571
1.00
16.65
C

ATOM
874
C
VAL
A1114
23.565
6.130
13.735
1.00
18.00
C

ATOM
875
O
VAL
A1114
23.241
6.023
14.926
1.00
17.56
O

ATOM
876
N
ILE
A1115
24.793
5.885
13.286
1.00
17.57
N

ATOM
877
CA
ILE
A1115
25.885
5.536
14.181
1.00
15.61
C

ATOM
878
CB
ILE
A1115
26.416
4.109
13.951
1.00
17.48
C

ATOM
879
CG2
ILE
A1115
27.514
3.806
14.965
1.00
14.97
C

ATOM
880
CG1
ILE
A1115
25.287
3.086
14.082
1.00
16.92
C

ATOM
881
CD1
ILE
A1115
25.695
1.685
13.638
1.00
16.69
C

ATOM
882
C
ILE
A1115
27.019
6.499
13.860
1.00
17.74
C

ATOM
883
O
ILE
A1115
27.470
6.573
12.714
1.00
16.21
O

ATOM
884
N
LEU
A1116
27.470
7.246
14.864
1.00
17.78
N

ATOM
885
CA
LEU
A1116
28.562
8.188
14.668
1.00
19.32
C

ATOM
886
CB
LEU
A1116
28.333
9.442
15.510
1.00
20.38
C

ATOM
887
CG
LEU
A1116
26.963
10.095
15.322
1.00
20.47
C

ATOM
888
CD1
LEU
A1116
26.877
11.326
16.205
1.00
22.94
C

ATOM
889
CD2
LEU
A1116
26.751
10.462
13.860
1.00
18.60
C

ATOM
890
C
LEU
A1116
29.851
7.490
15.093
1.00
21.10
C

ATOM
891
O
LEU
A1116
29.909
6.870
16.156
1.00
19.16
O

ATOM
892
N
GLU
A1117
30.880
7.590
14.259
1.00
22.54
N

ATOM
893
CA
GLU
A1117
32.141
6.934
14.554
1.00
25.40
C

ATOM
894
CB
GLU
A1117
32.323
5.743
13.616
1.00
25.16
C

ATOM
895
CG
GLU
A1117
33.629
5.000
13.817
1.00
27.61
C

ATOM
896
CD
GLU
A1117
33.720
3.772
12.950
1.00
27.04
C

ATOM
897
OE1
GLU
A1117
33.391
3.875
11.750
1.00
27.90
O

ATOM
898
OE2
GLU
A1117
34.126
2.712
13.465
1.00
27.49
O

ATOM
899
C
GLU
A1117
33.358
7.852
14.464
1.00
27.82
C

ATOM
900
O
GLU
A1117
33.425
8.742
13.616
1.00
26.44
O

ATOM
901
N
GLU
A1118
34.328
7.605
15.339
1.00
31.38
N

ATOM
902
CA
GLU
A1118
35.549
8.396
15.387
1.00
35.38
C

ATOM
903
CB
GLU
A1118
35.632
9.122
16.732
1.00
38.96
C

ATOM
904
CG
GLU
A1118
36.450
10.397
16.711
1.00
44.28
C

ATOM
905
CD
GLU
A1118
35.953
11.381
15.671
1.00
46.94
C

ATOM
906
OE1
GLU
A1118
36.206
11.153
14.469
1.00
47.99
O

ATOM
907
OE2
GLU
A1118
35.302
12.377
16.054
1.00
49.20
O

ATOM
908
C
GLU
A1118
36.756
7.482
15.210
1.00
36.85
C

ATOM
909
O
GLU
A1118
37.586
7.767
14.319
1.00
39.18
O

ATOM
910
OXT
GLU
A1118
36.858
6.488
15.967
1.00
37.85
O

TER
911

GLU
A1118

ATOM
912
CB
MET
B2003
36.089
−4.001
20.131
1.00
36.93
C

ATOM
913
CG
MET
B2003
35.997
−4.450
21.581
1.00
42.07
C

ATOM
914
SD
MET
B2003
37.062
−5.865
21.964
1.00
49.34
S

ATOM
915
CE
MET
B2003
36.267
−7.158
21.006
1.00
46.76
C

ATOM
916
C
MET
B2003
33.796
−3.017
20.233
1.00
31.67
C

ATOM
917
O
MET
B2003
33.469
−2.921
21.422
1.00
28.54
O

ATOM
918
N
MET
B2003
35.809
−1.560
20.439
1.00
33.64
N

ATOM
919
CA
MET
B2003
35.239
−2.773
19.791
1.00
33.04
C

ATOM
920
N
ILE
B2004
32.938
−3.327
19.264
1.00
29.22
N

ATOM
921
CA
ILE
B2004
31.537
−3.604
19.538
1.00
26.95
C

ATOM
922
CB
ILE
B2004
30.694
−3.586
18.236
1.00
27.19
C

ATOM
923
CG2
ILE
B2004
29.273
−4.070
18.528
1.00
26.67
C

ATOM
924
CG1
ILE
B2004
30.692
−2.175
17.642
1.00
27.75
C

ATOM
925
CD1
ILE
B2004
29.965
−2.048
16.307
1.00
28.82
C

ATOM
926
C
ILE
B2004
31.452
−4.986
20.165
1.00
25.64
C

ATOM
927
O
ILE
B2004
32.092
−5.924
19.693
1.00
26.78
O

ATOM
928
N
VAL
B2005
30.681
−5.114
21.240
1.00
23.42
N

ATOM
929
CA
VAL
B2005
30.534
−6.406
21.904
1.00
22.67
C

ATOM
930
CB
VAL
B2005
31.099
−6.379
23.344
1.00
23.16
C

ATOM
931
CG1
VAL
B2005
32.615
−6.311
23.305
1.00
22.80
C

ATOM
932
CG2
VAL
B2005
30.552
−5.197
24.096
1.00
23.38
C

ATOM
933
C
VAL
B2005
29.086
−6.878
21.948
1.00
21.18
C

ATOM
934
O
VAL
B2005
28.772
−7.884
22.577
1.00
23.33
O

ATOM
935
N
GLY
B2006
28.200
−6.155
21.275
1.00
19.21
N

ATOM
936
CA
GLY
B2006
26.811
−6.568
21.260
1.00
17.80
C

ATOM
937
C
GLY
B2006
25.896
−5.584
20.567
1.00
17.03
C

ATOM
938
O
GLY
B2006
26.161
−4.387
20.553
1.00
16.68
O

ATOM
939
N
HIS
B2007
24.813
−6.093
19.989
1.00
16.35
N

ATOM
940
CA
HIS
B2007
23.846
−5.237
19.323
1.00
16.88
C

ATOM
941
CB
HIS
B2007
24.216
−5.042
17.847
1.00
17.35
C

ATOM
942
CG
HIS
B2007
23.254
−4.170
17.097
1.00
18.35
C

ATOM
943
CD2
HIS
B2007
22.786
−4.239
15.827
1.00
17.84
C

ATOM
944
ND1
HIS
B2007
22.668
−3.058
17.660
1.00
18.04
N

ATOM
945
CE1
HIS
B2007
21.880
−2.479
16.769
1.00
19.69
C

ATOM
946
NE2
HIS
B2007
21.934
−3.176
15.648
1.00
16.84
N

ATOM
947
C
HIS
B2007
22.447
−5.831
19.444
1.00
17.26
C

ATOM
948
O
HIS
B2007
22.238
−7.027
19.213
1.00
14.74
O

ATOM
949
N
GLY
B2008
21.490
−4.990
19.819
1.00
16.95
N

ATOM
950
CA
GLY
B2008
20.129
−5.464
19.962
1.00
17.68
C

ATOM
951
C
GLY
B2008
19.095
−4.401
19.661
1.00
18.32
C

ATOM
952
O
GLY
B2008
19.321
−3.212
19.901
1.00
19.75
O

ATOM
953
N
ILE
B2009
17.964
−4.830
19.112
1.00
17.31
N

ATOM
954
CA
ILE
B2009
16.868
−3.917
18.821
1.00
18.07
C

ATOM
955
CB
ILE
B2009
16.727
−3.598
17.306
1.00
16.33
C

ATOM
956
CG2
ILE
B2009
18.025
−2.990
16.777
1.00
16.15
C

ATOM
957
CG1
ILE
B2009
16.361
−4.856
16.519
1.00
19.06
C

ATOM
958
CD1
ILE
B2009
16.014
−4.559
15.060
1.00
16.01
C

ATOM
959
C
ILE
B2009
15.607
−4.607
19.312
1.00
17.52
C

ATOM
960
O
ILE
B2009
15.576
−5.827
19.448
1.00
17.73
O

ATOM
961
N
ASP
B2010
14.580
−3.825
19.607
1.00
18.54
N

ATOM
962
CA
ASP
B2010
13.327
−4.384
20.089
1.00
20.76
C

ATOM
963
CB
ASP
B2010
13.401
−4.663
21.598
1.00
21.38
C

ATOM
964
CG
ASP
B2010
12.157
−5.372
22.127
1.00
22.62
C

ATOM
965
OD1
ASP
B2010
11.403
−4.762
22.915
1.00
22.62
O

ATOM
966
OD2
ASP
B2010
11.932
−6.544
21.756
1.00
23.17
O

ATOM
967
C
ASP
B2010
12.198
−3.416
19.814
1.00
21.83
C

ATOM
968
O
ASP
B2010
12.378
−2.200
19.912
1.00
21.02
O

ATOM
969
N
ILE
B2011
11.039
−3.966
19.464
1.00
21.90
N

ATOM
970
CA
ILE
B2011
9.848
−3.163
19.189
1.00
25.52
C

ATOM
971
CB
ILE
B2011
9.346
−3.346
17.752
1.00
27.88
C

ATOM
972
CG2
ILE
B2011
8.410
−2.194
17.388
1.00
30.28
C

ATOM
973
CG1
ILE
B2011
10.518
−3.410
16.783
1.00
29.66
C

ATOM
974
CD1
ILE
B2011
10.131
−3.937
15.420
1.00
31.53
C

ATOM
975
C
ILE
B2011
8.738
−3.670
20.102
1.00
24.08
C

ATOM
976
O
ILE
B2011
8.561
−4.874
20.258
1.00
22.40
O

ATOM
977
N
GLU
B2012
8.002
−2.757
20.718
1.00
24.39
N

ATOM
978
CA
GLU
B2012
6.911
−3.156
21.598
1.00
24.77
C

ATOM
979
CB
GLU
B2012
7.269
−2.868
23.056
1.00
25.42
C

ATOM
980
CG
GLU
B2012
8.482
−3.637
23.554
1.00
28.89
C

ATOM
981
CD
GLU
B2012
8.233
−5.139
23.652
1.00
31.05
C

ATOM
982
OE1
GLU
B2012
9.224
−5.895
23.721
1.00
31.07
O

ATOM
983
OE2
GLU
B2012
7.053
−5.560
23.671
1.00
30.63
O

ATOM
984
C
GLU
B2012
5.655
−2.387
21.208
1.00
24.28
C

ATOM
985
O
GLU
B2012
5.732
−1.235
20.786
1.00
24.45
O

ATOM
986
N
GLU
B2013
4.507
−3.043
21.328
1.00
22.06
N

ATOM
987
CA
GLU
B2013
3.223
−2.431
21.008
1.00
21.01
C

ATOM
988
CB
GLU
B2013
2.241
−3.508
20.545
1.00
21.98
C

ATOM
989
CG
GLU
B2013
0.857
−3.010
20.179
0.05
20.80
C

ATOM
990
CD
GLU
B2013
−0.106
−4.152
19.921
0.05
20.56
C

ATOM
991
OE1
GLU
B2013
0.231
−5.039
19.109
0.05
20.26
O

ATOM
992
OE2
GLU
B2013
−1.196
−4.166
20.529
0.05
20.00
O

ATOM
993
C
GLU
B2013
2.719
−1.793
22.292
1.00
20.42
C

ATOM
994
O
GLU
B2013
2.644
−2.457
23.326
1.00
19.82
O

ATOM
995
N
LEU
B2014
2.383
−0.512
22.244
1.00
20.95
N

ATOM
996
CA
LEU
B2014
1.906
0.149
23.452
1.00
25.05
C

ATOM
997
CB
LEU
B2014
1.530
1.604
23.162
1.00
26.46
C

ATOM
998
CG
LEU
B2014
2.610
2.478
22.521
1.00
29.15
C

ATOM
999
CD1
LEU
B2014
2.171
3.929
22.610
1.00
32.28
C

ATOM
1000
CD2
LEU
B2014
3.945
2.294
23.225
1.00
28.39
C

ATOM
1001
C
LEU
B2014
0.708
−0.582
24.053
1.00
25.52
C

ATOM
1002
O
LEU
B2014
0.635
−0.773
25.266
1.00
25.48
O

ATOM
1003
N
ALA
B2015
−0.220
−1.001
23.196
1.00
26.92
N

ATOM
1004
CA
ALA
B2015
−1.425
−1.697
23.637
1.00
28.21
C

ATOM
1005
CB
ALA
B2015
−2.267
−2.088
22.426
1.00
29.71
C

ATOM
1006
C
ALA
B2015
−1.144
−2.932
24.490
1.00
29.10
C

ATOM
1007
O
ALA
B2015
−1.864
−3.208
25.450
1.00
29.79
O

ATOM
1008
N
SER
B2016
−0.106
−3.681
24.135
1.00
29.36
N

ATOM
1009
CA
SER
B2016
0.246
−4.885
24.875
1.00
30.31
C

ATOM
1010
CB
SER
B2016
1.357
−5.633
24.147
1.00
32.28
C

ATOM
1011
OG
SER
B2016
1.032
−5.782
22.779
1.00
33.64
O

ATOM
1012
C
SER
B2016
0.705
−4.508
26.275
1.00
30.37
C

ATOM
1013
O
SER
B2016
0.369
−5.170
27.260
1.00
29.37
O

ATOM
1014
N
ILE
B2017
1.476
−3.431
26.353
1.00
30.04
N

ATOM
1015
CA
ILE
B2017
1.979
−2.955
27.625
1.00
30.17
C

ATOM
1016
CB
ILE
B2017
2.907
−1.741
27.420
1.00
29.67
C

ATOM
1017
CG2
ILE
B2017
3.323
−1.153
28.765
1.00
31.54
C

ATOM
1018
CG1
ILE
B2017
4.141
−2.178
26.630
1.00
29.63
C

ATOM
1019
CD1
ILE
B2017
4.883
−3.368
27.246
1.00
29.53
C

ATOM
1020
C
ILE
B2017
0.814
−2.585
28.537
1.00
30.53
C

ATOM
1021
O
ILE
B2017
0.736
−3.051
29.673
1.00
29.90
O

ATOM
1022
N
GLU
B2018
−0.100
−1.762
28.034
1.00
31.91
N

ATOM
1023
CA
GLU
B2018
−1.252
−1.363
28.831
1.00
34.92
C

ATOM
1024
CB
GLU
B2018
−2.113
−0.355
28.064
1.00
37.97
C

ATOM
1025
CG
GLU
B2018
−1.895
−0.370
26.565
1.00
42.86
C

ATOM
1026
CD
GLU
B2018
−2.698
0.700
25.844
1.00
45.97
C

ATOM
1027
OE1
GLU
B2018
−3.945
0.608
25.843
1.00
47.86
O

ATOM
1028
OE2
GLU
B2018
−2.084
1.633
25.279
1.00
47.02
O

ATOM
1029
C
GLU
B2018
−2.085
−2.573
29.247
1.00
34.56
C

ATOM
1030
O
GLU
B2018
−2.490
−2.678
30.404
1.00
35.89
O

ATOM
1031
N
SER
B2019
−2.349
−3.488
28.321
1.00
33.29
N

ATOM
1032
CA
SER
B2019
−3.117
−4.674
28.681
1.00
33.75
C

ATOM
1033
CB
SER
B2019
−3.270
−5.623
27.490
1.00
32.73
C

ATOM
1034
OG
SER
B2019
−4.314
−5.203
26.635
1.00
36.89
O

ATOM
1035
C
SER
B2019
−2.416
−5.402
29.822
1.00
33.12
C

ATOM
1036
O
SER
B2019
−3.066
−5.963
30.698
1.00
32.83
O

ATOM
1037
N
ALA
B2020
−1.087
−5.398
29.808
1.00
33.22
N

ATOM
1038
CA
ALA
B2020
−0.329
−6.055
30.869
1.00
35.36
C

ATOM
1039
CB
ALA
B2020
1.157
−6.105
30.510
1.00
34.87
C

ATOM
1040
C
ALA
B2020
−0.537
−5.295
32.179
1.00
36.08
C

ATOM
1041
O
ALA
B2020
−0.669
−5.898
33.241
1.00
34.70
O

ATOM
1042
N
VAL
B2021
−0.570
−3.968
32.097
1.00
38.89
N

ATOM
1043
CA
VAL
B2021
−0.783
−3.133
33.277
1.00
42.15
C

ATOM
1044
CB
VAL
B2021
−0.672
−1.627
32.931
1.00
42.05
C

ATOM
1045
CG1
VAL
B2021
−1.060
−0.775
34.138
1.00
42.48
C

ATOM
1046
CG2
VAL
B2021
0.746
−1.298
32.504
1.00
42.42
C

ATOM
1047
C
VAL
B2021
−2.176
−3.410
33.841
1.00
44.98
C

ATOM
1048
O
VAL
B2021
−2.491
−3.029
34.967
1.00
45.67
O

ATOM
1049
N
THR
B2022
−3.001
−4.085
33.047
1.00
47.50
N

ATOM
1050
CA
THR
B2022
−4.359
−4.420
33.451
1.00
50.10
C

ATOM
1051
CB
THR
B2022
−5.323
−4.368
32.236
1.00
51.16
C

ATOM
1052
OG1
THR
B2022
−5.501
−3.007
31.824
1.00
53.24
O

ATOM
1053
CG2
THR
B2022
−6.677
−4.957
32.592
1.00
52.95
C

ATOM
1054
C
THR
B2022
−4.454
−5.799
34.109
1.00
50.81
C

ATOM
1055
O
THR
B2022
−4.937
−5.918
35.232
1.00
51.36
O

ATOM
1056
N
ARG
B2023
−3.988
−6.836
33.421
1.00
51.25
N

ATOM
1057
CA
ARG
B2023
−4.064
−8.187
33.968
1.00
52.22
C

ATOM
1058
CB
ARG
B2023
−3.746
−9.220
32.883
1.00
52.29
C

ATOM
1059
CG
ARG
B2023
−4.157
−10.644
33.242
0.05
51.97
C

ATOM
1060
CD
ARG
B2023
−5.531
−10.663
33.905
0.05
51.83
C

ATOM
1061
NE
ARG
B2023
−6.183
−11.966
33.828
0.05
51.66
N

ATOM
1062
CZ
ARG
B2023
−6.697
−12.474
32.713
0.05
51.57
C

ATOM
1063
NH1
ARG
B2023
−6.634
−11.789
31.579
0.05
51.47
N

ATOM
1064
NH2
ARG
B2023
−7.284
−13.663
32.730
0.05
51.49
N

ATOM
1065
C
ARG
B2023
−3.157
−8.405
35.173
1.00
53.22
C

ATOM
1066
O
ARG
B2023
−3.256
−9.424
35.859
1.00
53.07
O

ATOM
1067
N
HIS
B2024
−2.274
−7.447
35.432
1.00
53.34
N

ATOM
1068
CA
HIS
B2024
−1.365
−7.544
36.564
1.00
53.62
C

ATOM
1069
CB
HIS
B2024
−0.042
−8.176
36.127
1.00
54.97
C

ATOM
1070
CG
HIS
B2024
−0.208
−9.477
35.403
1.00
56.91
C

ATOM
1071
CD2
HIS
B2024
−0.006
−10.755
35.805
1.00
57.80
C

ATOM
1072
ND1
HIS
B2024
−0.660
−9.552
34.103
1.00
57.75
N

ATOM
1073
CE1
HIS
B2024
−0.729
−10.820
33.735
1.00
58.06
C

ATOM
1074
NE2
HIS
B2024
−0.338
−11.570
34.750
1.00
57.59
N

ATOM
1075
C
HIS
B2024
−1.127
−6.157
37.148
1.00
53.35
C

ATOM
1076
O
HIS
B2024
−0.312
−5.385
36.644
1.00
53.29
O

ATOM
1077
N
GLU
B2025
−1.861
−5.854
38.214
1.00
52.80
N

ATOM
1078
CA
GLU
B2025
−1.785
−4.569
38.905
1.00
51.46
C

ATOM
1079
CB
GLU
B2025
−2.618
−4.637
40.188
1.00
54.49
C

ATOM
1080
CG
GLU
B2025
−4.095
−4.920
39.949
1.00
56.85
C

ATOM
1081
CD
GLU
B2025
−4.798
−5.434
41.190
1.00
58.84
C

ATOM
1082
OE1
GLU
B2025
−4.520
−6.584
41.595
1.00
60.08
O

ATOM
1083
OE2
GLU
B2025
−5.624
−4.690
41.763
1.00
59.42
O

ATOM
1084
C
GLU
B2025
−0.364
−4.122
39.247
1.00
48.83
C

ATOM
1085
O
GLU
B2025
−0.058
−2.931
39.211
1.00
48.34
O

ATOM
1086
N
GLY
B2026
0.497
−5.074
39.588
1.00
45.49
N

ATOM
1087
CA
GLY
B2026
1.864
−4.729
39.932
1.00
40.95
C

ATOM
1088
C
GLY
B2026
2.826
−4.920
38.774
1.00
37.63
C

ATOM
1089
O
GLY
B2026
4.027
−5.077
38.978
1.00
37.06
O

ATOM
1090
N
PHE
B2027
2.301
−4.902
37.554
1.00
33.22
N

ATOM
1091
CA
PHE
B2027
3.135
−5.083
36.374
1.00
30.35
C

ATOM
1092
CB
PHE
B2027
2.287
−4.995
35.105
1.00
29.47
C

ATOM
1093
CG
PHE
B2027
3.079
−5.162
33.840
1.00
28.37
C

ATOM
1094
CD1
PHE
B2027
3.501
−6.421
33.431
1.00
28.75
C

ATOM
1095
CD2
PHE
B2027
3.432
−4.055
33.076
1.00
26.82
C

ATOM
1096
CE1
PHE
B2027
4.264
−6.575
32.277
1.00
27.85
C

ATOM
1097
CE2
PHE
B2027
4.195
−4.199
31.919
1.00
27.50
C

ATOM
1098
CZ
PHE
B2027
4.611
−5.458
31.520
1.00
28.11
C

ATOM
1099
C
PHE
B2027
4.245
−4.038
36.303
1.00
28.35
C

ATOM
1100
O
PHE
B2027
5.419
−4.378
36.179
1.00
27.55
O

ATOM
1101
N
ALA
B2028
3.863
−2.768
36.376
1.00
26.54
N

ATOM
1102
CA
ALA
B2028
4.820
−1.674
36.306
1.00
26.97
C

ATOM
1103
CB
ALA
B2028
4.103
−0.340
36.503
1.00
26.06
C

ATOM
1104
C
ALA
B2028
5.938
−1.815
37.329
1.00
27.20
C

ATOM
1105
O
ALA
B2028
7.112
−1.697
36.998
1.00
26.33
O

ATOM
1106
N
LYS
B2029
5.555
−2.075
38.572
1.00
28.14
N

ATOM
1107
CA
LYS
B2029
6.496
−2.213
39.673
1.00
30.24
C

ATOM
1108
CB
LYS
B2029
5.738
−2.543
40.965
1.00
33.94
C

ATOM
1109
CG
LYS
B2029
6.597
−2.502
42.215
1.00
39.10
C

ATOM
1110
CD
LYS
B2029
7.038
−1.082
42.540
1.00
42.39
C

ATOM
1111
CE
LYS
B2029
8.108
−1.070
43.629
1.00
45.14
C

ATOM
1112
NZ
LYS
B2029
7.712
−1.858
44.836
1.00
46.16
N

ATOM
1113
C
LYS
B2029
7.567
−3.264
39.437
1.00
28.56
C

ATOM
1114
O
LYS
B2029
8.696
−3.114
39.902
1.00
28.42
O

ATOM
1115
N
ARG
B2030
7.219
−4.325
38.717
1.00
26.96
N

ATOM
1116
CA
ARG
B2030
8.171
−5.397
38.452
1.00
25.76
C

ATOM
1117
CB
ARG
B2030
7.430
−6.708
38.180
1.00
27.87
C

ATOM
1118
CG
ARG
B2030
6.318
−7.007
39.174
0.05
26.73
C

ATOM
1119
CD
ARG
B2030
6.358
−8.451
39.652
0.05
26.68
C

ATOM
1120
NE
ARG
B2030
6.295
−9.416
38.557
0.05
26.45
N

ATOM
1121
CZ
ARG
B2030
5.263
−9.553
37.730
0.05
26.36
C

ATOM
1122
NH1
ARG
B2030
4.191
−8.783
37.862
0.05
26.22
N

ATOM
1123
NH2
ARG
B2030
5.301
−10.469
36.771
0.05
26.29
N

ATOM
1124
C
ARG
B2030
9.069
−5.076
37.266
1.00
24.16
C

ATOM
1125
O
ARG
B2030
10.200
−5.551
37.187
1.00
22.83
O

ATOM
1126
N
VAL
B2031
8.559
−4.270
36.341
1.00
22.75
N

ATOM
1127
CA
VAL
B2031
9.319
−3.903
35.158
1.00
22.54
C

ATOM
1128
CB
VAL
B2031
8.371
−3.536
33.984
1.00
23.94
C

ATOM
1129
CG1
VAL
B2031
9.156
−2.884
32.855
1.00
24.54
C

ATOM
1130
CG2
VAL
B2031
7.677
−4.794
33.467
1.00
24.38
C

ATOM
1131
C
VAL
B2031
10.264
−2.739
35.409
1.00
21.20
C

ATOM
1132
O
VAL
B2031
11.364
−2.699
34.858
1.00
21.89
O

ATOM
1133
N
LEU
B2032
9.837
−1.805
36.252
1.00
20.43
N

ATOM
1134
CA
LEU
B2032
10.623
−0.607
36.552
1.00
21.46
C

ATOM
1135
CB
LEU
B2032
9.722
0.624
36.459
1.00
21.16
C

ATOM
1136
CG
LEU
B2032
8.902
0.814
35.180
1.00
22.44
C

ATOM
1137
CD1
LEU
B2032
7.913
1.951
35.383
1.00
25.05
C

ATOM
1138
CD2
LEU
B2032
9.822
1.107
34.003
1.00
23.51
C

ATOM
1139
C
LEU
B2032
11.289
−0.613
37.928
1.00
20.88
C

ATOM
1140
O
LEU
B2032
10.758
−1.188
38.875
1.00
24.06
O

ATOM
1141
N
THR
B2033
12.451
0.027
38.035
1.00
20.86
N

ATOM
1142
CA
THR
B2033
13.147
0.117
39.317
1.00
20.81
C

ATOM
1143
CB
THR
B2033
14.602
0.569
39.160
1.00
20.39
C

ATOM
1144
OG1
THR
B2033
14.623
1.853
38.521
1.00
21.21
O

ATOM
1145
CG2
THR
B2033
15.394
−0.443
38.341
1.00
20.57
C

ATOM
1146
C
THR
B2033
12.432
1.189
40.119
1.00
21.74
C

ATOM
1147
O
THR
B2033
11.479
1.806
39.635
1.00
22.52
O

ATOM
1148
N
ALA
B2034
12.893
1.427
41.339
1.00
22.64
N

ATOM
1149
CA
ALA
B2034
12.267
2.441
42.177
1.00
24.18
C

ATOM
1150
CB
ALA
B2034
12.939
2.479
43.541
1.00
24.55
C

ATOM
1151
C
ALA
B2034
12.371
3.806
41.502
1.00
25.08
C

ATOM
1152
O
ALA
B2034
11.393
4.555
41.437
1.00
24.57
O

ATOM
1153
N
LEU
B2035
13.558
4.119
40.989
1.00
25.67
N

ATOM
1154
CA
LEU
B2035
13.786
5.403
40.337
1.00
27.37
C

ATOM
1155
CB
LEU
B2035
15.274
5.576
40.025
1.00
30.75
C

ATOM
1156
CG
LEU
B2035
15.792
7.017
40.016
1.00
34.25
C

ATOM
1157
CD1
LEU
B2035
15.529
7.681
41.373
1.00
34.25
C

ATOM
1158
CD2
LEU
B2035
17.286
7.010
39.715
1.00
36.03
C

ATOM
1159
C
LEU
B2035
12.948
5.550
39.066
1.00
26.19
C

ATOM
1160
O
LEU
B2035
12.424
6.625
38.789
1.00
25.81
O

ATOM
1161
N
GLU
B2036
12.829
4.479
38.288
1.00
24.86
N

ATOM
1162
CA
GLU
B2036
12.010
4.523
37.074
1.00
24.94
C

ATOM
1163
CB
GLU
B2036
12.218
3.256
36.238
1.00
24.20
C

ATOM
1164
CG
GLU
B2036
13.521
3.220
35.439
1.00
22.34
C

ATOM
1165
CD
GLU
B2036
13.823
1.834
34.878
1.00
22.43
C

ATOM
1166
OE1
GLU
B2036
14.592
1.744
33.899
1.00
20.15
O

ATOM
1167
OE2
GLU
B2036
13.302
0.834
35.425
1.00
21.31
O

ATOM
1168
C
GLU
B2036
10.528
4.645
37.461
1.00
25.14
C

ATOM
1169
O
GLU
B2036
9.740
5.261
36.746
1.00
24.49
O

ATOM
1170
N
MET
B2037
10.155
4.051
38.593
1.00
25.36
N

ATOM
1171
CA
MET
B2037
8.772
4.116
39.067
1.00
27.03
C

ATOM
1172
CB
MET
B2037
8.570
3.202
40.279
1.00
28.19
C

ATOM
1173
CG
MET
B2037
8.077
1.811
39.932
1.00
30.50
C

ATOM
1174
SD
MET
B2037
6.592
1.878
38.903
1.00
35.36
S

ATOM
1175
CE
MET
B2037
5.315
2.130
40.111
1.00
31.11
C

ATOM
1176
C
MET
B2037
8.389
5.541
39.445
1.00
27.51
C

ATOM
1177
O
MET
B2037
7.288
6.004
39.146
1.00
27.72
O

ATOM
1178
N
GLU
B2038
9.309
6.232
40.104
1.00
29.26
N

ATOM
1179
CA
GLU
B2038
9.075
7.604
40.522
1.00
30.50
C

ATOM
1180
CB
GLU
B2038
10.261
8.089
41.363
1.00
33.66
C

ATOM
1181
CG
GLU
B2038
10.100
7.747
42.852
1.00
38.27
C

ATOM
1182
CD
GLU
B2038
11.384
7.278
43.517
1.00
41.20
C

ATOM
1183
OE1
GLU
B2038
12.448
7.886
43.264
1.00
41.95
O

ATOM
1184
OE2
GLU
B2038
11.322
6.307
44.309
1.00
42.56
O

ATOM
1185
C
GLU
B2038
8.827
8.512
39.320
1.00
29.98
C

ATOM
1186
O
GLU
B2038
8.059
9.473
39.403
1.00
29.40
O

ATOM
1187
N
ARG
B2039
9.465
8.198
38.198
1.00
28.37
N

ATOM
1188
CA
ARG
B2039
9.272
8.973
36.986
1.00
28.60
C

ATOM
1189
CB
ARG
B2039
10.374
8.670
35.973
1.00
32.59
C

ATOM
1190
CG
ARG
B2039
10.103
9.236
34.589
1.00
36.59
C

ATOM
1191
CD
ARG
B2039
9.892
10.740
34.627
1.00
42.20
C

ATOM
1192
NE
ARG
B2039
9.750
11.301
33.284
1.00
46.45
N

ATOM
1193
CZ
ARG
B2039
9.599
12.597
33.025
1.00
48.88
C

ATOM
1194
NH1
ARG
B2039
9.477
13.014
31.770
1.00
48.84
N

ATOM
1195
NH2
ARG
B2039
9.570
13.478
34.018
1.00
49.51
N

ATOM
1196
C
ARG
B2039
7.926
8.585
36.397
1.00
27.40
C

ATOM
1197
O
ARG
B2039
7.107
9.439
36.047
1.00
28.21
O

ATOM
1198
N
PHE
B2040
7.717
7.280
36.291
1.00
25.73
N

ATOM
1199
CA
PHE
B2040
6.489
6.710
35.758
1.00
26.22
C

ATOM
1200
CB
PHE
B2040
6.546
5.185
35.916
1.00
24.31
C

ATOM
1201
CG
PHE
B2040
5.265
4.477
35.573
1.00
26.63
C

ATOM
1202
CD1
PHE
B2040
4.871
4.318
34.248
1.00
26.24
C

ATOM
1203
CD2
PHE
B2040
4.467
3.938
36.579
1.00
26.94
C

ATOM
1204
CE1
PHE
B2040
3.698
3.627
33.930
1.00
27.58
C

ATOM
1205
CE2
PHE
B2040
3.297
3.249
36.276
1.00
27.41
C

ATOM
1206
CZ
PHE
B2040
2.911
3.090
34.950
1.00
27.69
C

ATOM
1207
C
PHE
B2040
5.245
7.262
36.463
1.00
26.33
C

ATOM
1208
O
PHE
B2040
4.269
7.622
35.814
1.00
27.93
O

ATOM
1209
N
THR
B2041
5.287
7.324
37.792
1.00
27.19
N

ATOM
1210
CA
THR
B2041
4.151
7.805
38.575
1.00
27.42
C

ATOM
1211
CB
THR
B2041
4.328
7.485
40.078
1.00
27.34
C

ATOM
1212
OG1
THR
B2041
5.504
8.132
40.577
1.00
28.52
O

ATOM
1213
CG2
THR
B2041
4.458
5.986
40.294
1.00
28.04
C

ATOM
1214
C
THR
B2041
3.896
9.304
38.432
1.00
28.31
C

ATOM
1215
O
THR
B2041
2.840
9.796
38.840
1.00
27.03
O

ATOM
1216
N
SER
B2042
4.854
10.024
37.853
1.00
28.11
N

ATOM
1217
CA
SER
B2042
4.706
11.465
37.665
1.00
31.34
C

ATOM
1218
CB
SER
B2042
6.039
12.179
37.896
1.00
32.90
C

ATOM
1219
OG
SER
B2042
6.326
12.278
39.282
1.00
36.54
O

ATOM
1220
C
SER
B2042
4.168
11.841
36.289
1.00
31.32
C

ATOM
1221
O
SER
B2042
3.909
13.012
36.018
1.00
30.89
O

ATOM
1222
N
LEU
B2043
4.008
10.849
35.421
1.00
31.83
N

ATOM
1223
CA
LEU
B2043
3.487
11.088
34.077
1.00
31.92
C

ATOM
1224
CB
LEU
B2043
4.293
10.300
33.038
1.00
29.48
C

ATOM
1225
CG
LEU
B2043
5.785
10.603
32.912
1.00
29.62
C

ATOM
1226
CD1
LEU
B2043
6.420
9.633
31.921
1.00
29.54
C

ATOM
1227
CD2
LEU
B2043
5.985
12.035
32.462
1.00
29.33
C

ATOM
1228
C
LEU
B2043
2.039
10.623
34.058
1.00
33.01
C

ATOM
1229
O
LEU
B2043
1.569
10.030
35.026
1.00
32.48
O

ATOM
1230
N
LYS
B2044
1.337
10.877
32.957
1.00
36.01
N

ATOM
1231
CA
LYS
B2044
−0.060
10.469
32.850
1.00
38.06
C

ATOM
1232
CB
LYS
B2044
−0.967
11.586
33.375
1.00
39.86
C

ATOM
1233
CG
LYS
B2044
−2.402
11.149
33.619
1.00
43.44
C

ATOM
1234
CD
LYS
B2044
−3.295
12.317
34.013
1.00
45.82
C

ATOM
1235
CE
LYS
B2044
−4.630
11.825
34.554
1.00
46.21
C

ATOM
1236
NZ
LYS
B2044
−5.292
10.879
33.615
1.00
47.83
N

ATOM
1237
C
LYS
B2044
−0.472
10.116
31.422
1.00
38.81
C

ATOM
1238
O
LYS
B2044
0.225
10.438
30.459
1.00
39.23
O

ATOM
1239
N
GLY
B2045
−1.611
9.443
31.299
1.00
39.57
N

ATOM
1240
CA
GLY
B2045
−2.134
9.068
29.996
1.00
40.10
C

ATOM
1241
C
GLY
B2045
−1.177
8.355
29.062
1.00
40.74
C

ATOM
1242
O
GLY
B2045
−0.513
7.394
29.454
1.00
41.23
O

ATOM
1243
N
ARG
B2046
−1.115
8.832
27.820
1.00
41.17
N

ATOM
1244
CA
ARG
B2046
−0.255
8.249
26.791
1.00
41.02
C

ATOM
1245
CB
ARG
B2046
−0.396
9.015
25.472
1.00
43.31
C

ATOM
1246
CG
ARG
B2046
−1.812
9.081
24.931
1.00
47.77
C

ATOM
1247
CD
ARG
B2046
−1.882
9.873
23.627
1.00
50.51
C

ATOM
1248
NE
ARG
B2046
−3.260
10.180
23.244
1.00
52.23
N

ATOM
1249
CZ
ARG
B2046
−3.611
10.768
22.103
1.00
52.56
C

ATOM
1250
NH1
ARG
B2046
−4.890
11.012
21.844
1.00
52.50
N

ATOM
1251
NH2
ARG
B2046
−2.684
11.107
21.217
1.00
53.75
N

ATOM
1252
C
ARG
B2046
1.212
8.229
27.184
1.00
39.59
C

ATOM
1253
O
ARG
B2046
1.873
7.198
27.078
1.00
38.95
O

ATOM
1254
N
ARG
B2047
1.718
9.375
27.631
1.00
38.59
N

ATOM
1255
CA
ARG
B2047
3.117
9.492
28.022
1.00
36.93
C

ATOM
1256
CB
ARG
B2047
3.415
10.914
28.497
1.00
39.53
C

ATOM
1257
CG
ARG
B2047
3.284
11.965
27.408
1.00
43.89
C

ATOM
1258
CD
ARG
B2047
3.915
13.275
27.843
1.00
46.98
C

ATOM
1259
NE
ARG
B2047
5.322
13.091
28.189
1.00
49.81
N

ATOM
1260
CZ
ARG
B2047
6.145
14.072
28.545
1.00
50.90
C

ATOM
1261
NH1
ARG
B2047
5.708
15.324
28.603
1.00
51.65
N

ATOM
1262
NH2
ARG
B2047
7.409
13.800
28.845
1.00
52.13
N

ATOM
1263
C
ARG
B2047
3.543
8.496
29.095
1.00
34.22
C

ATOM
1264
O
ARG
B2047
4.671
8.017
29.086
1.00
33.86
O

ATOM
1265
N
GLN
B2048
2.646
8.187
30.022
1.00
31.68
N

ATOM
1266
CA
GLN
B2048
2.968
7.247
31.081
1.00
29.06
C

ATOM
1267
CB
GLN
B2048
1.844
7.212
32.121
1.00
29.98
C

ATOM
1268
CG
GLN
B2048
2.236
6.524
33.420
1.00
32.80
C

ATOM
1269
CD
GLN
B2048
1.089
6.443
34.415
1.00
34.55
C

ATOM
1270
OE1
GLN
B2048
1.297
6.158
35.596
1.00
36.97
O

ATOM
1271
NE2
GLN
B2048
−0.125
6.682
33.940
1.00
33.10
N

ATOM
1272
C
GLN
B2048
3.161
5.861
30.471
1.00
27.54
C

ATOM
1273
O
GLN
B2048
4.134
5.170
30.769
1.00
26.96
O

ATOM
1274
N
ILE
B2049
2.230
5.459
29.612
1.00
25.61
N

ATOM
1275
CA
ILE
B2049
2.318
4.159
28.961
1.00
24.60
C

ATOM
1276
CB
ILE
B2049
1.099
3.894
28.053
1.00
24.71
C

ATOM
1277
CG2
ILE
B2049
1.310
2.606
27.254
1.00
25.39
C

ATOM
1278
CG1
ILE
B2049
−0.174
3.814
28.906
1.00
25.99
C

ATOM
1279
CD1
ILE
B2049
−0.111
2.776
30.004
1.00
26.01
C

ATOM
1280
C
ILE
B2049
3.570
4.090
28.104
1.00
23.58
C

ATOM
1281
O
ILE
B2049
4.281
3.091
28.120
1.00
24.35
O

ATOM
1282
N
GLU
B2050
3.828
5.160
27.360
1.00
22.52
N

ATOM
1283
CA
GLU
B2050
4.985
5.238
26.482
1.00
23.92
C

ATOM
1284
CB
GLU
B2050
4.980
6.575
25.739
1.00
24.81
C

ATOM
1285
CG
GLU
B2050
6.216
6.842
24.901
1.00
27.69
C

ATOM
1286
CD
GLU
B2050
6.470
5.767
23.859
1.00
30.29
C

ATOM
1287
OE1
GLU
B2050
5.514
5.384
23.149
1.00
32.11
O

ATOM
1288
OE2
GLU
B2050
7.632
5.314
23.740
1.00
29.75
O

ATOM
1289
C
GLU
B2050
6.278
5.085
27.270
1.00
23.59
C

ATOM
1290
O
GLU
B2050
7.235
4.452
26.804
1.00
23.37
O

ATOM
1291
N
TYR
B2051
6.304
5.666
28.466
1.00
23.27
N

ATOM
1292
CA
TYR
B2051
7.487
5.584
29.306
1.00
23.17
C

ATOM
1293
CB
TYR
B2051
7.300
6.397
30.592
1.00
22.74
C

ATOM
1294
CG
TYR
B2051
8.520
6.367
31.492
1.00
22.74
C

ATOM
1295
CD1
TYR
B2051
8.667
5.382
32.474
1.00
21.76
C

ATOM
1296
CE1
TYR
B2051
9.818
5.317
33.263
1.00
23.29
C

ATOM
1297
CD2
TYR
B2051
9.555
7.288
31.324
1.00
21.56
C

ATOM
1298
CE2
TYR
B2051
10.708
7.230
32.106
1.00
22.47
C

ATOM
1299
CZ
TYR
B2051
10.832
6.243
33.072
1.00
24.14
C

ATOM
1300
OH
TYR
B2051
11.973
6.182
33.843
1.00
26.11
O

ATOM
1301
C
TYR
B2051
7.749
4.123
29.645
1.00
22.35
C

ATOM
1302
O
TYR
B2051
8.834
3.603
29.397
1.00
21.78
O

ATOM
1303
N
LEU
B2052
6.735
3.470
30.200
1.00
21.05
N

ATOM
1304
CA
LEU
B2052
6.820
2.069
30.581
1.00
20.91
C

ATOM
1305
CB
LEU
B2052
5.486
1.626
31.193
1.00
19.71
C

ATOM
1306
CG
LEU
B2052
5.321
0.141
31.535
1.00
20.97
C

ATOM
1307
CD1
LEU
B2052
6.463
−0.293
32.453
1.00
20.68
C

ATOM
1308
CD2
LEU
B2052
3.953
−0.092
32.206
1.00
18.56
C

ATOM
1309
C
LEU
B2052
7.176
1.164
29.394
1.00
19.19
C

ATOM
1310
O
LEU
B2052
8.055
0.305
29.502
1.00
18.65
O

ATOM
1311
N
ALA
B2053
6.501
1.365
28.264
1.00
18.96
N

ATOM
1312
CA
ALA
B2053
6.748
0.553
27.075
1.00
18.97
C

ATOM
1313
CB
ALA
B2053
5.712
0.867
26.003
1.00
19.24
C

ATOM
1314
C
ALA
B2053
8.153
0.777
26.526
1.00
19.65
C

ATOM
1315
O
ALA
B2053
8.811
−0.167
26.067
1.00
19.77
O

ATOM
1316
N
GLY
B2054
8.604
2.028
26.569
1.00
18.25
N

ATOM
1317
CA
GLY
B2054
9.930
2.355
26.084
1.00
16.89
C

ATOM
1318
C
GLY
B2054
11.004
1.748
26.970
1.00
18.42
C

ATOM
1319
O
GLY
B2054
12.072
1.344
26.488
1.00
17.94
O

ATOM
1320
N
ARG
B2055
10.731
1.692
28.270
1.00
16.40
N

ATOM
1321
CA
ARG
B2055
11.684
1.112
29.202
1.00
19.09
C

ATOM
1322
CB
ARG
B2055
11.253
−1.377
30.647
1.00
20.94
C

ATOM
1323
CG
ARG
B2055
12.060
2.478
31.329
1.00
20.89
C

ATOM
1324
CD
ARG
B2055
11.968
3.790
30.570
1.00
24.51
C

ATOM
1325
NE
ARG
B2055
12.987
4.745
31.003
1.00
25.33
N

ATOM
1326
CZ
ARG
B2055
13.239
5.897
30.388
1.00
25.95
C

ATOM
1327
NH1
ARG
B2055
12.544
6.243
29.313
1.00
23.97
N

ATOM
1328
NH2
ARG
B2055
14.194
6.700
30.843
1.00
25.82
N

ATOM
1329
C
ARG
B2055
11.774
−0.386
28.932
1.00
18.98
C

ATOM
1330
O
ARG
B2055
12.855
−0.971
28.985
1.00
18.90
O

ATOM
1331
N
TRP
B2056
10.632
−1.003
28.631
1.00
20.10
N

ATOM
1332
CA
TRP
B2056
10.613
−2.426
28.322
1.00
20.52
C

ATOM
1333
CB
TRP
B2056
9.178
−2.930
28.107
1.00
22.74
C

ATOM
1334
CG
TRP
B2056
9.118
−4.394
27.738
1.00
26.17
C

ATOM
1335
CD2
TRP
B2056
8.573
−5.459
28.527
1.00
27.99
C

ATOM
1336
CE2
TRP
B2056
8.791
−6.661
27.815
1.00
28.39
C

ATOM
1337
CE3
TRP
B2056
7.924
−5.516
29.767
1.00
27.60
C

ATOM
1338
CD1
TRP
B2056
9.623
−4.978
26.607
1.00
26.87
C

ATOM
1339
NE1
TRP
B2056
9.432
−6.337
26.648
1.00
29.27
N

ATOM
1340
CZ2
TRP
B2056
8.384
−7.906
28.301
1.00
29.62
C

ATOM
1341
CZ3
TRP
B2056
7.516
−6.760
30.253
1.00
30.44
C

ATOM
1342
CH2
TRP
B2056
7.750
−7.937
29.519
1.00
30.93
C

ATOM
1343
C
TRP
B2056
11.430
−2.659
27.056
1.00
18.69
C

ATOM
1344
O
TRP
B2056
12.265
−3.562
27.007
1.00
15.35
O

ATOM
1345
N
SER
B2057
11.190
−1.843
26.032
1.00
18.10
N

ATOM
1346
CA
SER
B2057
11.925
−1.993
24.778
1.00
19.73
C

ATOM
1347
CB
SER
B2057
11.475
−0.948
23.756
1.00
21.79
C

ATOM
1348
OG
SER
B2057
10.174
−1.245
23.273
1.00
30.44
O

ATOM
1349
C
SER
B2057
13.427
−1.857
25.009
1.00
17.21
C

ATOM
1350
O
SER
B2057
14.207
−2.679
24.539
1.00
17.96
O

ATOM
1351
N
ALA
B2058
13.821
−0.814
25.728
1.00
15.24
N

ATOM
1352
CA
ALA
B2058
15.233
−0.568
26.016
1.00
15.12
C

ATOM
1353
CB
ALA
B2058
15.387
0.718
26.819
1.00
14.34
C

ATOM
1354
C
ALA
B2058
15.879
−1.724
26.768
1.00
15.45
C

ATOM
1355
O
ALA
B2058
16.981
−2.158
26.421
1.00
14.80
O

ATOM
1356
N
LYS
B2059
15.203
−2.216
27.804
1.00
15.14
N

ATOM
1357
CA
LYS
B2059
15.748
−3.315
28.593
1.00
16.97
C

ATOM
1358
CB
LYS
B2059
14.909
−3.523
29.860
1.00
18.38
C

ATOM
1359
CG
LYS
B2059
14.958
−2.303
30.796
1.00
17.80
C

ATOM
1360
CD
LYS
B2059
14.216
−2.546
32.097
1.00
19.77
C

ATOM
1361
CE
LYS
B2059
14.345
−1.327
33.021
1.00
19.57
C

ATOM
1362
NZ
LYS
B2059
13.932
−1.624
34.417
1.00
20.44
N

ATOM
1363
C
LYS
B2059
15.857
−4.608
27.792
1.00
17.95
C

ATOM
1364
O
LYS
B2059
16.805
−5.375
27.967
1.00
16.15
O

ATOM
1365
N
GLU
B2060
14.897
−4.844
26.904
1.00
17.88
N

ATOM
1366
CA
GLU
B2060
14.923
−6.041
26.070
1.00
17.87
C

ATOM
1367
CB
GLU
B2060
13.551
−6.261
25.420
1.00
19.58
C

ATOM
1368
CG
GLU
B2060
13.519
−7.359
24.361
1.00
23.62
C

ATOM
1369
CD
GLU
B2060
13.834
−8.753
24.897
1.00
24.96
C

ATOM
1370
OE1
GLU
B2060
14.150
−8.906
26.099
1.00
27.91
O

ATOM
1371
OE2
GLU
B2060
13.764
−9.707
24.096
1.00
27.02
O

ATOM
1372
C
GLU
B2060
16.013
−5.885
24.999
1.00
17.82
C

ATOM
1373
O
GLU
B2060
16.769
−6.816
24.741
1.00
16.78
O

ATOM
1374
N
ALA
B2061
16.106
−4.700
24.396
1.00
15.53
N

ATOM
1375
CA
ALA
B2061
17.126
−4.443
23.379
1.00
15.22
C

ATOM
1376
CB
ALA
B2061
17.017
−3.010
22.868
1.00
12.83
C

ATOM
1377
C
ALA
B2061
18.514
−4.683
23.984
1.00
15.45
C

ATOM
1378
O
ALA
B2061
19.396
−5.252
23.337
1.00
15.13
O

ATOM
1379
N
PHE
B2062
18.699
−4.248
25.227
1.00
15.78
N

ATOM
1380
CA
PHE
B2062
19.965
−4.441
25.923
1.00
16.16
C

ATOM
1381
CB
PHE
B2062
19.972
−3.664
27.244
1.00
18.34
C

ATOM
1382
CG
PHE
B2062
21.173
−3.954
28.110
1.00
20.05
C

ATOM
1383
CD1
PHE
B2062
21.180
−5.055
28.972
1.00
20.65
C

ATOM
1384
CD2
PHE
B2062
22.311
−3.158
28.030
1.00
20.37
C

ATOM
1385
CE1
PHE
B2062
22.304
−5.358
29.737
1.00
20.45
C

ATOM
1386
CE2
PHE
B2062
23.450
−3.453
28.796
1.00
21.28
C

ATOM
1387
CZ
PHE
B2062
23.443
−4.552
29.647
1.00
20.21
C

ATOM
1388
C
PHE
B2062
20.210
−5.930
26.195
1.00
17.69
C

ATOM
1389
O
PHE
B2062
21.297
−6.455
25.933
1.00
17.00
O

ATOM
1390
N
SER
B2063
19.203
−6.608
26.730
1.00
18.58
N

ATOM
1391
CA
SER
B2063
19.336
−8.033
27.016
1.00
19.54
C

ATOM
1392
CB
SER
B2063
18.025
−8.584
27.565
1.00
19.74
C

ATOM
1393
OG
SER
B2063
17.710
−7.950
28.793
1.00
22.28
O

ATOM
1394
C
SER
B2063
19.733
−8.789
25.753
1.00
20.63
C

ATOM
1395
O
SER
B2063
20.574
−9.682
25.803
1.00
18.71
O

ATOM
1396
N
LYS
B2064
19.128
−8.430
24.620
1.00
19.41
N

ATOM
1397
CA
LYS
B2064
19.457
−9.088
23.362
1.00
20.24
C

ATOM
1398
CB
LYS
B2064
18.447
−8.705
22.276
1.00
21.74
C

ATOM
1399
CG
LYS
B2064
17.036
−9.246
22.553
1.00
21.35
C

ATOM
1400
CD
LYS
B2064
16.007
−8.785
21.525
1.00
21.53
C

ATOM
1401
CE
LYS
B2064
16.378
−9.233
20.116
1.00
19.60
C

ATOM
1402
NZ
LYS
B2064
15.400
−8.764
19.091
1.00
19.68
N

ATOM
1403
C
LYS
B2064
20.875
−8.709
22.946
1.00
20.67
C

ATOM
1404
O
LYS
B2064
21.573
−9.498
22.310
1.00
21.49
O

ATOM
1405
N
ALA
B2065
21.303
−7.502
23.308
1.00
17.85
N

ATOM
1406
CA
ALA
B2065
22.660
−7.059
22.995
1.00
19.57
C

ATOM
1407
CB
ALA
B2065
22.826
−5.576
23.323
1.00
15.70
C

ATOM
1408
C
ALA
B2065
23.647
−7.892
23.820
1.00
20.80
C

ATOM
1409
O
ALA
B2065
24.793
−8.096
23.414
1.00
18.12
O

ATOM
1410
N
MET
B2066
23.199
−8.359
24.985
1.00
22.49
N

ATOM
1411
CA
MET
B2066
24.039
−9.187
25.849
1.00
27.36
C

ATOM
1412
CB
MET
B2066
23.608
−9.069
27.310
1.00
27.69
C

ATOM
1413
CG
MET
B2066
23.933
−7.749
27.971
1.00
30.93
C

ATOM
1414
SD
MET
B2066
25.678
−7.548
28.342
1.00
35.00
S

ATOM
1415
CE
MET
B2066
25.840
−8.691
29.727
1.00
35.63
C

ATOM
1416
C
MET
B2066
23.927
−10.646
25.416
1.00
28.77
C

ATOM
1417
O
MET
B2066
24.570
−11.517
25.990
1.00
29.95
O

ATOM
1418
N
GLY
B2067
23.095
−10.906
24.411
1.00
30.61
N

ATOM
1419
CA
GLY
B2067
22.927
−12.266
23.924
1.00
32.14
C

ATOM
1420
C
GLY
B2067
21.816
−13.073
24.577
1.00
33.83
C

ATOM
1421
O
GLY
B2067
21.728
−14.282
24.353
1.00
35.17
O

ATOM
1422
N
THR
B2068
20.964
−12.425
25.369
1.00
33.49
N

ATOM
1423
CA
THR
B2068
19.870
−13.124
26.048
1.00
35.61
C

ATOM
1424
CB
THR
B2068
20.225
−13.393
27.528
1.00
37.06
C

ATOM
1425
OG1
THR
B2068
20.480
−12.149
28.194
1.00
37.62
O

ATOM
1426
CG2
THR
B2068
21.461
−14.274
27.622
1.00
40.72
C

ATOM
1427
C
THR
B2068
18.519
−12.396
26.008
1.00
34.51
C

ATOM
1428
O
THR
B2068
18.212
−11.679
25.054
1.00
34.74
O

ATOM
1429
N
GLY
B2069
17.715
−12.598
27.051
1.00
34.71
N

ATOM
1430
CA
GLY
B2069
16.403
−11.970
27.132
1.00
33.79
C

ATOM
1431
C
GLY
B2069
16.195
−11.248
28.452
1.00
33.36
C

ATOM
1432
O
GLY
B2069
16.823
−11.590
29.455
1.00
32.35
O

ATOM
1433
N
ILE
B2070
15.300
−10.263
28.467
1.00
33.38
N

ATOM
1434
CA
ILE
B2070
15.059
−9.487
29.680
1.00
34.29
C

ATOM
1435
CB
ILE
B2070
14.122
−8.283
29.401
1.00
33.36
C

ATOM
1436
CG2
ILE
B2070
12.761
−8.768
28.904
1.00
35.55
C

ATOM
1437
CG1
ILE
B2070
13.966
−7.446
30.672
1.00
32.13
C

ATOM
1438
CD1
ILE
B2070
15.277
−6.991
31.269
1.00
28.50
C

ATOM
1439
C
ILE
B2070
14.514
−10.295
30.856
1.00
35.39
C

ATOM
1440
O
ILE
B2070
14.868
−10.039
32.008
1.00
35.52
O

ATOM
1441
N
SER
B2071
13.666
−11.276
30.572
1.00
37.28
N

ATOM
1442
CA
SER
B2071
13.104
−12.104
31.630
1.00
39.77
C

ATOM
1443
CB
SER
B2071
12.020
−13.025
31.066
1.00
42.43
C

ATOM
1444
OG
SER
B2071
11.433
−13.795
32.102
1.00
46.76
O

ATOM
1445
C
SER
B2071
14.189
−12.947
32.299
1.00
40.07
C

ATOM
1446
O
SER
B2071
14.024
−13.402
33.428
1.00
39.81
O

ATOM
1447
N
LYS
B2072
15.299
−13.154
31.596
1.00
39.77
N

ATOM
1448
CA
LYS
B2072
16.403
−13.940
32.132
1.00
39.15
C

ATOM
1449
CB
LYS
B2072
17.115
−14.689
31.007
1.00
40.68
C

ATOM
1450
CG
LYS
B2072
16.225
−15.656
30.252
1.00
43.38
C

ATOM
1451
CD
LYS
B2072
16.996
−16.371
29.151
1.00
44.69
C

ATOM
1452
CE
LYS
B2072
16.070
−17.260
28.342
1.00
46.81
C

ATOM
1453
NZ
LYS
B2072
15.337
−18.225
29.214
1.00
47.85
N

ATOM
1454
C
LYS
B2072
17.396
−13.039
32.842
1.00
38.30
C

ATOM
1455
O
LYS
B2072
17.952
−13.401
33.879
1.00
38.50
O

ATOM
1456
N
LEU
B2073
17.613
−11.860
32.269
1.00
36.74
N

ATOM
1457
CA
LEU
B2073
18.540
−10.883
32.821
1.00
34.89
C

ATOM
1458
CB
LEU
B2073
18.817
−9.803
31.766
1.00
35.18
C

ATOM
1459
CG
LEU
B2073
20.010
−8.856
31.910
1.00
35.71
C

ATOM
1460
CD1
LEU
B2073
19.804
−7.943
33.107
1.00
37.71
C

ATOM
1461
CD2
LEU
B2073
21.296
−9.661
32.050
1.00
36.74
C

ATOM
1462
C
LEU
B2073
17.961
−10.259
34.098
1.00
34.21
C

ATOM
1463
O
LEU
B2073
18.683
−10.044
35.071
1.00
32.72
O

ATOM
1464
N
GLY
B2074
16.658
−9.982
34.090
1.00
33.08
N

ATOM
1465
CA
GLY
B2074
16.014
−9.383
35.247
1.00
32.12
C

ATOM
1466
C
GLY
B2074
15.762
−7.897
35.053
1.00
30.96
C

ATOM
1467
O
GLY
B2074
16.702
−7.127
34.871
1.00
31.73
O

ATOM
1468
N
PHE
B2075
14.497
−7.489
35.095
1.00
29.97
N

ATOM
1469
CA
PHE
B2075
14.139
−6.083
34.913
1.00
30.52
C

ATOM
1470
CB
PHE
B2075
12.620
−5.896
34.973
1.00
32.55
C

ATOM
1471
CG
PHE
B2075
11.880
−6.511
33.822
1.00
33.89
C

ATOM
1472
CD1
PHE
B2075
11.474
−7.843
33.868
1.00
35.06
C

ATOM
1473
CD2
PHE
B2075
11.578
−5.755
32.693
1.00
34.72
C

ATOM
1474
CE1
PHE
B2075
10.774
−8.412
32.806
1.00
35.34
C

ATOM
1475
CE2
PHE
B2075
10.879
−6.316
31.623
1.00
34.77
C

ATOM
1476
CZ
PHE
B2075
10.477
−7.646
31.681
1.00
34.64
C

ATOM
1477
C
PHE
B2075
14.769
−5.146
35.934
1.00
29.45
C

ATOM
1478
O
PHE
B2075
15.159
−4.025
35.599
1.00
30.37
O

ATOM
1479
N
GLN
B2076
14.867
−5.607
37.177
1.00
28.05
N

ATOM
1480
CA
GLN
B2076
15.417
−4.796
38.259
1.00
27.24
C

ATOM
1481
CB
GLN
B2076
15.043
−5.420
39.607
1.00
27.56
C

ATOM
1482
CG
GLN
B2076
13.539
−5.436
39.859
1.00
27.74
C

ATOM
1483
CD
GLN
B2076
12.929
−4.041
39.834
1.00
30.00
C

ATOM
1484
OE1
GLN
B2076
11.896
−3.807
39.193
1.00
31.13
O

ATOM
1485
NE2
GLN
B2076
13.563
−3.107
40.536
1.00
28.51
N

ATOM
1486
C
GLN
B2076
16.920
−4.538
38.198
1.00
26.61
C

ATOM
1487
O
GLN
B2076
17.430
−3.698
38.935
1.00
25.98
O

ATOM
1488
N
ASP
B2077
17.621
−5.251
37.320
1.00
26.64
N

ATOM
1489
CA
ASP
B2077
19.062
−5.084
37.160
1.00
27.59
C

ATOM
1490
CB
ASP
B2077
19.723
−6.426
36.847
1.00
32.09
C

ATOM
1491
CG
ASP
B2077
19.749
−7.352
38.041
1.00
35.66
C

ATOM
1492
OD1
ASP
B2077
18.670
−7.841
38.440
1.00
39.93
O

ATOM
1493
OD2
ASP
B2077
20.850
−7.584
38.586
1.00
40.87
O

ATOM
1494
C
ASP
B2077
19.403
−4.087
36.054
1.00
26.77
C

ATOM
1495
O
ASP
B2077
20.571
−3.825
35.779
1.00
25.66
O

ATOM
1496
N
LEU
B2078
18.375
−3.539
35.420
1.00
24.12
N

ATOM
1497
CA
LEU
B2078
18.570
−2.571
34.356
1.00
23.25
C

ATOM
1498
CB
LEU
B2078
18.058
−3.118
33.018
1.00
23.97
C

ATOM
1499
CG
LEU
B2078
18.750
−4.370
32.475
1.00
24.92
C

ATOM
1500
CD1
LEU
B2078
17.987
−4.914
31.276
1.00
23.04
C

ATOM
1501
CD2
LEU
B2078
20.180
−4.021
32.089
1.00
26.74
C

ATOM
1502
C
LEU
B2078
17.795
−1.321
34.702
1.00
23.29
C

ATOM
1503
O
LEU
B2078
16.669
−1.390
35.196
1.00
23.17
O

ATOM
1504
N
GLU
B2079
18.397
−0.173
34.446
1.00
21.42
N

ATOM
1505
CA
GLU
B2079
17.724
1.075
34.716
1.00
21.45
C

ATOM
1506
CB
GLU
B2079
18.192
1.666
36.036
1.00
22.77
C

ATOM
1507
CG
GLU
B2079
17.346
2.835
36.477
1.00
24.03
C

ATOM
1508
CD
GLU
B2079
17.726
3.340
37.848
1.00
25.73
C

ATOM
1509
OE1
GLU
B2079
18.797
3.972
37.976
1.00
26.42
O

ATOM
1510
OE2
GLU
B2079
16.950
3.099
38.798
1.00
27.63
O

ATOM
1511
C
GLU
B2079
18.014
2.055
33.600
1.00
20.55
C

ATOM
1512
O
GLU
B2079
19.167
2.241
33.203
1.00
20.96
O

ATOM
1513
N
VAL
B2080
16.954
2.666
33.095
1.00
18.00
N

ATOM
1514
CA
VAL
B2080
17.055
3.648
32.033
1.00
18.55
C

ATOM
1515
CB
VAL
B2080
16.268
3.211
30.769
1.00
16.14
C

ATOM
1516
CG1
VAL
B2080
16.429
4.262
29.686
1.00
16.12
C

ATOM
1517
CG2
VAL
B2080
16.755
1.849
30.276
1.00
14.67
C

ATOM
1518
C
VAL
B2080
16.442
4.948
32.549
1.00
19.85
C

ATOM
1519
O
VAL
B2080
15.234
5.019
32.805
1.00
19.59
O

ATOM
1520
N
LEU
B2081
17.279
5.966
32.708
1.00
20.39
N

ATOM
1521
CA
LEU
B2081
16.825
7.271
33.176
1.00
21.24
C

ATOM
1522
CB
LEU
B2081
17.644
7.716
34.394
1.00
21.31
C

ATOM
1523
CG
LEU
B2081
17.683
6.758
35.593
1.00
22.71
C

ATOM
1524
CD1
LEU
B2081
18.641
7.299
36.661
1.00
23.10
C

ATOM
1525
CD2
LEU
B2081
16.280
6.594
36.165
1.00
22.25
C

ATOM
1526
C
LEU
B2081
17.027
8.259
32.040
1.00
22.16
C

ATOM
1527
O
LEU
B2081
17.421
7.882
30.934
1.00
22.05
O

ATOM
1528
N
ASN
B2082
16.755
9.526
32.309
1.00
22.54
N

ATOM
1529
CA
ASN
B2082
16.933
10.561
31.303
1.00
24.30
C

ATOM
1530
CB
ASN
B2082
15.598
11.247
31.022
1.00
25.64
C

ATOM
1531
CG
ASN
B2082
14.657
10.371
30.207
1.00
27.22
C

ATOM
1532
OD1
ASN
B2082
14.779
10.280
28.982
1.00
28.88
O

ATOM
1533
ND2
ASN
B2082
13.729
9.710
30.883
1.00
24.27
N

ATOM
1534
C
ASN
B2082
17.945
11.555
31.840
1.00
25.00
C

ATOM
1535
O
ASN
B2082
17.860
11.958
33.001
1.00
23.46
O

ATOM
1536
N
ASN
B2083
18.913
11.939
31.010
1.00
25.22
N

ATOM
1537
CA
ASN
B2083
19.920
12.890
31.454
1.00
25.69
C

ATOM
1538
CB
ASN
B2083
21.215
12.744
30.641
1.00
25.99
C

ATOM
1539
CG
ASN
B2083
21.013
12.961
29.153
1.00
27.46
C

ATOM
1540
OD1
ASN
B2083
20.173
13.758
28.729
1.00
25.62
O

ATOM
1541
ND2
ASN
B2083
21.811
12.265
28.348
1.00
27.23
N

ATOM
1542
C
ASN
B2083
19.410
14.330
31.397
1.00
26.79
C

ATOM
1543
O
ASN
B2083
18.216
14.571
31.215
1.00
25.77
O

ATOM
1544
N
GLU
B2084
20.322
15.281
31.559
1.00
29.60
N

ATOM
1545
CA
GLU
B2084
19.982
16.701
31.563
1.00
31.78
C

ATOM
1546
CB
GLU
B2084
21.238
17.539
31.827
1.00
33.94
C

ATOM
1547
CG
GLU
B2084
22.148
16.960
32.896
1.00
39.23
C

ATOM
1548
CD
GLU
B2084
22.774
15.640
32.470
1.00
41.35
C

ATOM
1549
OE1
GLU
B2084
23.642
15.652
31.567
1.00
42.45
O

ATOM
1550
OE2
GLU
B2084
22.390
−14.588
33.030
1.00
42.21
O

ATOM
1551
C
GLU
B2084
19.351
17.153
30.253
1.00
30.81
C

ATOM
1552
O
GLU
B2084
18.472
18.013
30.242
1.00
29.26
O

ATOM
1553
N
ARG
B2085
19.808
16.573
29.148
1.00
30.86
N

ATOM
1554
CA
ARG
B2085
19.291
16.940
27.838
1.00
31.05
C

ATOM
1555
CB
ARG
B2085
20.364
16.716
26.775
1.00
33.27
C

ATOM
1556
CG
ARG
B2085
21.598
17.554
27.005
1.00
35.81
C

ATOM
1557
CD
ARG
B2085
22.636
17.335
25.928
1.00
38.24
C

ATOM
1558
NE
ARG
B2085
23.735
18.286
26.060
1.00
41.03
N

ATOM
1559
CZ
ARG
B2085
24.544
18.349
27.110
1.00
42.41
C

ATOM
1560
NH1
ARG
B2085
24.381
17.515
28.128
1.00
43.26
N

ATOM
1561
NH2
ARG
B2085
25.523
19.239
27.138
1.00
44.30
N

ATOM
1562
C
ARG
B2085
18.024
16.190
27.465
1.00
30.14
C

ATOM
1563
O
ARG
B2085
17.450
16.432
26.408
1.00
31.11
O

ATOM
1564
N
GLY
B2086
17.593
15.273
28.326
1.00
29.20
N

ATOM
1565
CA
GLY
B2086
16.371
14.530
28.057
1.00
27.93
C

ATOM
1566
C
GLY
B2086
16.531
13.222
27.304
1.00
26.69
C

ATOM
1567
O
GLY
B2086
15.541
12.581
26.952
1.00
27.22
O

ATOM
1568
N
ALA
B2087
17.770
12.818
27.056
1.00
24.98
N

ATOM
1569
CA
ALA
B2087
18.033
11.582
26.340
1.00
23.11
C

ATOM
1570
CB
ALA
B2087
19.358
11.692
25.589
1.00
24.73
C

ATOM
1571
C
ALA
B2087
18.065
10.369
27.269
1.00
22.69
C

ATOM
1572
O
ALA
B2087
18.611
10.431
28.370
1.00
22.81
O

ATOM
1573
N
PRO
B2088
17.481
9.242
26.833
1.00
22.85
N

ATOM
1574
CD
PRO
B2088
16.722
9.014
25.588
1.00
23.63
C

ATOM
1575
CA
PRO
B2088
17.485
8.039
27.674
1.00
21.17
C

ATOM
1576
CB
PRO
B2088
16.471
7.134
26.982
1.00
22.95
C

ATOM
1577
CG
PRO
B2088
16.650
7.489
25.528
1.00
24.16
C

ATOM
1578
C
PRO
B2088
18.879
7.416
27.716
1.00
20.46
C

ATOM
1579
O
PRO
B2088
19.584
7.407
26.712
1.00
18.12
O

ATOM
1580
N
TYR
B2089
19.280
6.906
28.878
1.00
19.76
N

ATOM
1581
CA
TYR
B2089
20.593
6.275
29.019
1.00
19.97
C

ATOM
1582
CB
TYR
B2089
21.660
7.337
29.324
1.00
20.30
C

ATOM
1583
CG
TYR
B2089
21.605
7.850
30.743
1.00
21.25
C

ATOM
1584
CD1
TYR
B2089
22.471
7.347
31.719
1.00
23.06
C

ATOM
1585
CE1
TYR
B2089
22.386
7.765
33.046
1.00
22.62
C

ATOM
1586
CD2
TYR
B2089
20.651
8.793
31.128
1.00
21.67
C

ATOM
1587
CE2
TYR
B2089
20.557
9.218
32.454
1.00
23.51
C

ATOM
1588
CZ
TYR
B2089
21.429
8.693
33.404
1.00
22.23
C

ATOM
1589
OH
TYR
B2089
21.327
9.078
34.715
1.00
23.91
O

ATOM
1590
C
TYR
B2089
20.547
5.246
30.148
1.00
18.84
C

ATOM
1591
O
TYR
B2089
19.738
5.356
31.066
1.00
16.92
O

ATOM
1592
N
PHE
B2090
21.408
4.237
30.076
1.00
19.96
N

ATOM
1593
CA
PHE
B2090
21.432
3.218
31.116
1.00
20.18
C

ATOM
1594
CB
PHE
B2090
22.015
1.906
30.588
1.00
18.86
C

ATOM
1595
CG
PHE
B2090
21.031
1.078
29.813
1.00
17.77
C

ATOM
1596
CD1
PHE
B2090
20.843
1.282
28.452
1.00
18.34
C

ATOM
1597
CD2
PHE
B2090
20.276
0.102
30.455
1.00
17.66
C

ATOM
1598
CE1
PHE
B2090
19.915
0.523
27.737
1.00
16.58
C

ATOM
1599
CE2
PHE
B2090
19.344
−0.666
29.751
1.00
16.83
C

ATOM
1600
CZ
PHE
B2090
19.166
−0.453
28.393
1.00
18.42
C

ATOM
1601
C
PHE
B2090
22.249
3.683
32.307
1.00
21.96
C

ATOM
1602
O
PHE
B2090
23.464
3.837
32.215
1.00
21.17
O

ATOM
1603
N
SER
B2091
21.569
3.916
33.423
1.00
21.79
N

ATOM
1604
CA
SER
B2091
22.233
4.346
34.642
1.00
23.26
C

ATOM
1605
CB
SER
B2091
21.269
5.171
35.498
1.00
24.51
C

ATOM
1606
OG
SER
B2091
20.046
4.473
35.689
1.00
27.15
O

ATOM
1607
C
SER
B2091
22.676
−3.101
35.406
1.00
24.05
C

ATOM
1608
O
SER
B2091
23.572
3.158
36.241
1.00
22.27
O

ATOM
1609
N
GLN
B2092
22.039
1.974
35.100
1.00
24.23
N

ATOM
1610
CA
GLN
B2092
22.343
0.702
35.750
1.00
26.68
C

ATOM
1611
CB
GLN
B2092
21.324
0.420
36.858
1.00
30.19
C

ATOM
1612
CG
GLN
B2092
21.738
0.888
38.236
1.00
36.96
C

ATOM
1613
CD
GLN
B2092
22.791
−0.013
38.846
1.00
41.69
C

ATOM
1614
OE1
GLN
B2092
23.923
−0.086
38.360
1.00
44.08
O

ATOM
1615
NE2
GLN
B2092
22.419
−0.719
39.914
1.00
43.86
N

ATOM
1616
C
GLN
B2092
22.318
−0.450
34.755
1.00
25.68
C

ATOM
1617
O
GLN
B2092
21.350
−0.628
34.015
1.00
25.64
O

ATOM
1618
N
ALA
B2093
23.378
−1.243
34.750
1.00
24.06
N

ATOM
1619
CA
ALA
B2093
23.451
−2.379
33.845
1.00
24.55
C

ATOM
1620
CB
ALA
B2093
23.544
−1.896
32.401
1.00
23.95
C

ATOM
1621
C
ALA
B2093
24.654
−3.240
34.182
1.00
24.42
C

ATOM
1622
O
ALA
B2093
25.669
−2.737
34.662
1.00
23.73
O

ATOM
1623
N
PRO
B2094
24.542
−4.560
33.958
1.00
24.28
N

ATOM
1624
CD
PRO
B2094
23.286
−5.266
33.634
1.00
24.45
C

ATOM
1625
CA
PRO
B2094
25.625
−5.509
34.226
1.00
24.13
C

ATOM
1626
CB
PRO
B2094
24.882
−6.827
34.404
1.00
24.53
C

ATOM
1627
CG
PRO
B2094
23.752
−6.693
33.412
1.00
25.43
C

ATOM
1628
C
PRO
B2094
26.575
−5.532
33.033
1.00
25.18
C

ATOM
1629
O
PRO
B2094
26.687
−6.538
32.330
1.00
27.39
O

ATOM
1630
N
PHE
B2095
27.237
−4.406
32.795
1.00
25.59
N

ATOM
1631
CA
PHE
B2095
28.166
−4.276
31.674
1.00
26.28
C

ATOM
1632
CB
PHE
B2095
27.394
−3.937
30.392
1.00
26.01
C

ATOM
1633
CG
PHE
B2095
28.264
−3.808
29.176
1.00
25.16
C

ATOM
1634
CD1
PHE
B2095
28.289
−2.622
28.448
1.00
23.33
C

ATOM
1635
CD2
PHE
B2095
29.070
−4.864
28.766
1.00
24.13
C

ATOM
1636
CE1
PHE
B2095
29.106
−2.488
27.333
1.00
23.09
C

ATOM
1637
CE2
PHE
B2095
29.890
−4.739
27.652
1.00
24.48
C

ATOM
1638
CZ
PHE
B2095
29.906
−3.542
26.933
1.00
21.85
C

ATOM
1639
C
PHE
B2095
29.157
−3.168
32.000
1.00
25.62
C

ATOM
1640
O
PHE
B2095
28.768
−2.080
32.413
1.00
26.70
O

ATOM
1641
N
SER
B2096
30.438
−3.441
.31.804
1.00
26.81
N

ATOM
1642
CA
SER
B2096
31.472
−2.466
32.122
1.00
27.94
C

ATOM
1643
CB
SER
B2096
32.750
−3.203
32.531
1.00
27.66
C

ATOM
1644
OG
SER
B2096
33.144
−4.111
31.518
1.00
29.62
O

ATOM
1645
C
SER
B2096
31.787
−1.469
31.007
1.00
27.71
C

ATOM
1646
O
SER
B2096
32.430
−0.452
31.249
1.00
27.75
O

ATOM
1647
N
GLY
B2097
31.325
−1.746
29.792
1.00
26.55
N

ATOM
1648
CA
GLY
B2097
31.611
−0.847
28.690
1.00
23.99
C

ATOM
1649
C
GLY
B2097
30.611
0.274
28.499
1.00
23.68
C

ATOM
1650
O
GLY
B2097
29.869
0.639
29.413
1.00
22.73
O

ATOM
1651
N
LYS
B2098
30.606
0.838
27.299
1.00
23.32
N

ATOM
1652
CA
LYS
B2098
29.682
1.912
26.975
1.00
23.52
C

ATOM
1653
CB
LYS
B2098
30.323
2.896
25.995
1.00
25.66
C

ATOM
1654
CG
LYS
B2098
31.546
3.599
26.562
1.00
29.30
C

ATOM
1655
CD
LYS
B2098
32.162
4.532
25.545
1.00
31.81
C

ATOM
1656
CE
LYS
B2098
33.364
5.247
26.128
1.00
35.72
C

ATOM
1657
NZ
LYS
B2098
33.970
6.194
25.154
1.00
38.45
N

ATOM
1658
C
LYS
B2098
28.438
1.302
26.356
1.00
21.94
C

ATOM
1659
O
LYS
B2098
28.518
0.350
25.570
1.00
20.64
O

ATOM
1660
N
ILE
B2099
27.294
1.862
26.721
1.00
20.44
N

ATOM
1661
CA
ILE
B2099
26.008
1.400
26.236
1.00
19.38
C

ATOM
1662
CB
ILE
B2099
25.109
1.012
27.421
1.00
19.92
C

ATOM
1663
CG2
ILE
B2099
23.804
0.423
26.919
1.00
20.26
C

ATOM
1664
CG1
ILE
B2099
25.839
−0.008
28.302
1.00
19.45
C

ATOM
1665
CD1
ILE
B2099
25.193
−0.230
29.663
1.00
21.98
C

ATOM
1666
C
ILE
B2099
25.352
2.529
25.444
1.00
19.88
C

ATOM
1667
O
ILE
B2099
24.950
3.546
26.011
1.00
19.12
O

ATOM
1668
N
TRP
B2100
25.267
2.352
24.129
1.00
19.02
N

ATOM
1669
CA
TRP
B2100
24.662
3.351
23.265
1.00
17.64
C

ATOM
1670
CB
TRP
B2100
25.430
3.431
21.951
1.00
19.81
C

ATOM
1671
CG
TRP
B2100
26.840
3.861
22.165
1.00
20.97
C

ATOM
1672
CD2
TRP
B2100
27.295
5.202
22.383
1.00
21.20
C

ATOM
1673
CE2
TRP
B2100
28.680
5.137
22.640
1.00
20.87
C

ATOM
1674
CE3
TRP
B2100
26.661
6.454
22.393
1.00
22.40
C

ATOM
1675
CD1
TRP
B2100
27.938
3.059
22.289
1.00
22.80
C

ATOM
1676
NE1
TRP
B2100
29.050
3.818
22.576
1.00
21.53
N

ATOM
1677
CZ2
TRP
B2100
29.448
6.279
22.901
1.00
21.01
C

ATOM
1678
CZ3
TRP
B2100
27.425
7.591
22.654
1.00
19.76
C

ATOM
1679
CH2
TRP
B2100
28.803
7.492
22.905
1.00
20.24
C

ATOM
1680
C
TRP
B2100
23.207
2.987
23.023
1.00
17.98
C

ATOM
1681
O
TRP
B2100
22.889
2.033
22.308
1.00
19.71
O

ATOM
1682
N
LEU
B2101
22.323
3.761
23.632
1.00
16.57
N

ATOM
1683
CA
LEU
B2101
20.897
3.527
23.524
1.00
15.94
C

ATOM
1684
CB
LEU
B2101
20.292
3.364
24.925
1.00
14.34
C

ATOM
1685
CG
LEU
B2101
18.756
3.387
25.013
1.00
15.83
C

ATOM
1686
CD1
LEU
B2101
18.195
2.073
24.455
1.00
11.99
C

ATOM
1687
CD2
LEU
B2101
18.324
3.555
26.467
1.00
14.03
C

ATOM
1688
C
LEU
B2101
20.142
4.632
22.810
1.00
16.46
C

ATOM
1689
O
LEU
B2101
20.464
5.807
22.937
1.00
14.73
O

ATOM
1690
N
SER
B2102
19.133
4.232
22.047
1.00
17.13
N

ATOM
1691
CA
SER
B2102
18.260
5.182
21.380
1.00
16.87
C

ATOM
1692
CB
SER
B2102
18.683
5.449
19.945
1.00
17.85
C

ATOM
1693
OG
SER
B2102
17.856
6.473
19.405
1.00
18.12
O

ATOM
1694
C
SER
B2102
16.866
4.577
21.393
1.00
15.72
C

ATOM
1695
O
SER
B2102
16.706
3.368
21.230
1.00
14.46
O

ATOM
1696
N
ILE
B2103
15.863
5.414
21.613
1.00
15.13
N

ATOM
1697
CA
ILE
B2103
14.478
4.948
21.646
1.00
17.16
C

ATOM
1698
CB
ILE
B2103
13.897
5.031
23.070
1.00
17.86
C

ATOM
1699
CG2
ILE
B2103
12.439
4.560
23.063
1.00
17.77
C

ATOM
1700
CG1
ILE
B2103
14.765
4.215
24.036
1.00
18.09
C

ATOM
1701
CD1
ILE
B2103
14.406
4.396
25.497
1.00
17.05
C

ATOM
1702
C
ILE
B2103
13.645
5.852
20.749
1.00
17.44
C

ATOM
1703
O
ILE
B2103
13.886
7.055
20.684
1.00
17.70
O

ATOM
1704
N
SER
B2104
12.675
5.275
20.053
1.00
17.76
N

ATOM
1705
CA
SER
B2104
11.803
6.065
19.187
1.00
19.81
C

ATOM
1706
CB
SER
B2104
12.355
6.117
17.759
1.00
19.27
C

ATOM
1707
OG
SER
B2104
11.570
6.964
16.930
1.00
20.56
O

ATOM
1708
C
SER
B2104
10.426
5.432
19.189
1.00
20.64
C

ATOM
1709
O
SER
B2104
10.290
4.213
19.338
1.00
22.59
O

ATOM
1710
N
HIS
B2105
9.396
6.246
19.020
1.00
20.13
N

ATOM
1711
CA
HIS
B2105
8.055
5.698
19.028
1.00
22.93
C

ATOM
1712
CB
HIS
B2105
7.456
5.812
20.432
1.00
23.19
C

ATOM
1713
CG
HIS
B2105
7.277
7.227
20.890
1.00
24.84
C

ATOM
1714
CD2
HIS
B2105
6.221
8.069
20.785
1.00
26.28
C

ATOM
1715
ND1
HIS
B2105
8.284
7.950
21.490
1.00
26.53
N

ATOM
1716
CE1
HIS
B2105
7.858
9.176
21.737
1.00
25.54
C

ATOM
1717
NE2
HIS
B2105
6.609
9.275
21.318
1.00
26.28
N

ATOM
1718
C
HIS
B2105
7.116
6.375
18.050
1.00
21.93
C

ATOM
1719
O
HIS
B2105
7.395
7.460
17.554
1.00
21.72
O

ATOM
1720
N
THR
B2106
6.016
5.687
17.769
1.00
23.48
N

ATOM
1721
CA
THR
B2106
4.941
6.183
16.919
1.00
25.16
C

ATOM
1722
CB
THR
B2106
4.605
5.242
15.755
1.00
25.21
C

ATOM
1723
OG1
THR
B2106
4.222
3.965
16.278
1.00
25.03
O

ATOM
1724
CG2
THR
B2106
5.791
5.089
14.823
1.00
25.52
C

ATOM
1725
C
THR
B2106
3.775
6.121
17.894
1.00
25.80
C

ATOM
1726
O
THR
B2106
3.978
5.862
19.081
1.00
24.98
O

ATOM
1727
N
ASP
B2107
2.559
6.329
17.406
1.00
25.90
N

ATOM
1728
CA
ASP
B2107
1.397
6.284
18.285
1.00
27.49
C

ATOM
1729
CB
ASP
B2107
0.169
6.862
17.574
0.05
26.86
C

ATOM
1730
CG
ASP
B2107
0.127
8.380
17.621
0.05
26.92
C

ATOM
1731
OD1
ASP
B2107
1.090
9.023
17.157
0.05
27.01
O

ATOM
1732
OD2
ASP
B2107
−0.874
8.930
18.125
0.05
26.97
O

ATOM
1733
C
ASP
B2107
1.085
4.877
18.788
1.00
27.36
C

ATOM
1734
O
ASP
B2107
0.493
4.717
19.854
1.00
29.78
O

ATOM
1735
N
GLN
B2108
1.482
3.858
18.032
1.00
25.07
N

ATOM
1736
CA
GLN
B2108
1.207
2.483
18.433
1.00
25.09
C

ATOM
1737
CB
GLN
B2108
0.523
1.736
17.293
1.00
26.05
C

ATOM
1738
CG
GLN
B2108
−0.728
2.395
16.780
1.00
29.37
C

ATOM
1739
CD
GLN
B2108
−1.145
1.827
15.445
1.00
31.53
C

ATOM
1740
OE1
GLN
B2108
−0.362
1.822
14.492
1.00
31.44
O

ATOM
1741
NE2
GLN
B2108
−2.379
1.345
15.363
1.00
31.86
N

ATOM
1742
C
GLN
B2108
2.412
1.658
18.876
1.00
24.58
C

ATOM
1743
O
GLN
B2108
2.251
0.710
19.650
1.00
22.64
O

ATOM
1744
N
PHE
B2109
3.606
2.000
18.386
1.00
23.20
N

ATOM
1745
CA
PHE
B2109
4.800
1.229
18.725
1.00
22.81
C

ATOM
1746
CB
PHE
B2109
5.309
0.456
17.501
1.00
24.68
C

ATOM
1747
CG
PHE
B2109
4.236
−0.250
16.721
1.00
26.08
C

ATOM
1748
CD1
PHE
B2109
3.701
0.329
15.576
1.00
26.47
C

ATOM
1749
CD2
PHE
B2109
3.783
−1.505
17.110
1.00
27.02
C

ATOM
1750
CE1
PHE
B2109
2.729
−0.336
14.825
1.00
28.36
C

ATOM
1751
CE2
PHE
B2109
2.810
−2.177
16.366
1.00
27.54
C

ATOM
1752
CZ
PHE
B2109
2.287
−1.592
15.224
1.00
28.20
C

ATOM
1753
C
PHE
B2109
5.980
2.037
19.260
1.00
21.56
C

ATOM
1754
O
PHE
B2109
6.096
3.233
19.027
1.00
22.22
O

ATOM
1755
N
VAL
B2110
6.872
1.358
19.969
1.00
21.04
N

ATOM
1756
CA
VAL
B2110
8.073
2.005
20.485
1.00
20.21
C

ATOM
1757
CB
VAL
B2110
7.982
2.279
22.006
1.00
19.74
C

ATOM
1758
CG1
VAL
B2110
7.649
1.001
22.751
1.00
21.12
C

ATOM
1759
CG2
VAL
B2110
9.307
2.861
22.504
1.00
21.25
C

ATOM
1760
C
VAL
B2110
9.230
1.063
20.197
1.00
20.24
C

ATOM
1761
O
VAL
B2110
9.160
−0.128
20.523
1.00
21.27
O

ATOM
1762
N
THR
B2111
10.276
1.580
19.557
1.00
19.29
N

ATOM
1763
CA
THR
B2111
11.440
0.763
19.235
1.00
20.44
C

ATOM
1764
CB
THR
B2111
11.759
0.788
17.725
1.00
22.75
C

ATOM
1765
OG1
THR
B2111
12.116
2.120
17.337
1.00
27.12
O

ATOM
1766
CG2
THR
B2111
10.550
0.353
16.911
1.00
26.61
C

ATOM
1767
C
THR
B2111
12.668
1.270
19.982
1.00
19.21
C

ATOM
1768
O
THR
B2111
12.780
2.455
20.278
1.00
18.06
O

ATOM
1769
N
ALA
B2112
13.581
0.353
20.280
1.00
18.16
N

ATOM
1770
CA
ALA
B2112
14.810
0.675
20.988
1.00
17.59
C

ATOM
1771
CB
ALA
B2112
14.715
0.231
22.442
1.00
14.54
C

ATOM
1772
C
ALA
B2112
15.951
−0.052
20.292
1.00
17.15
C

ATOM
1773
O
ALA
B2112
15.776
−1.163
19.788
1.00
15.26
O

ATOM
1774
N
SER
B2113
17.111
0.588
20.258
1.00
16.75
N

ATOM
1775
CA
SER
B2113
18.297
0.015
19.631
1.00
17.12
C

ATOM
1776
CB
SER
B2113
18.574
0.705
18.287
1.00
17.55
C

ATOM
1777
OG
SER
B2113
19.674
0.112
17.603
1.00
19.24
O

ATOM
1778
C
SER
B2113
19.470
0.227
20.588
1.00
16.82
C

ATOM
1779
O
SER
B2113
19.677
1.327
21.092
1.00
17.25
O

ATOM
1780
N
VAL
B2114
20.220
−0.837
20.840
1.00
16.23
N

ATOM
1781
CA
VAL
B2114
21.364
−0.778
21.736
1.00
15.71
C

ATOM
1782
CB
VAL
B2114
21.129
−1.591
23.017
1.00
13.94
C

ATOM
1783
CG1
VAL
B2114
22.451
−1.731
23.784
1.00
14.11
C

ATOM
1784
CG2
VAL
B2114
20.070
−0.923
23.877
1.00
10.51
C

ATOM
1785
C
VAL
B2114
22.617
−1.345
21.106
1.00
16.39
C

ATOM
1786
O
VAL
B2114
22.578
−2.412
20.492
1.00
16.76
O

ATOM
1787
N
ILE
B2115
23.724
−0.625
21.259
1.00
14.68
N

ATOM
1788
CA
ILE
B2115
25.014
−1.093
20.763
1.00
15.53
C

ATOM
1789
CB
ILE
B2115
25.589
−0.191
19.664
1.00
16.82
C

ATOM
1790
CG2
ILE
B2115
26.983
−0.702
19.253
1.00
14.25
C

ATOM
1791
CG1
ILE
B2115
24.649
−0.168
18.461
1.00
17.22
C

ATOM
1792
CD1
ILE
B2115
25.020
0.874
17.423
1.00
18.67
C

ATOM
1793
C
ILE
B2115
25.956
−1.039
21.956
1.00
16.88
C

ATOM
1794
O
ILE
B2115
26.080
0.006
22.614
1.00
16.02
O

ATOM
1795
N
LEU
B2116
26.603
−2.164
22.237
1.00
14.98
N

ATOM
1796
CA
LEU
B2116
27.529
−2.259
23.361
1.00
16.57
C

ATOM
1797
CB
LEU
B2116
27.365
−3.605
24.067
1.00
16.24
C

ATOM
1798
CG
LEU
B2116
25.945
−3.870
24.578
1.00
16.49
C

ATOM
1799
CD1
LEU
B2116
25.872
−5.256
25.197
1.00
15.73
C

ATOM
1800
CD2
LEU
B2116
25.563
−2.803
25.591
1.00
15.00
C

ATOM
1801
C
LEU
B2116
28.945
−2.121
22.852
1.00
17.64
C

ATOM
1802
O
LEU
B2116
29.297
−2.703
21.827
1.00
17.88
O

ATOM
1803
N
GLU
B2117
29.763
−1.373
23.584
1.00
19.16
N

ATOM
1804
CA
GLU
B2117
31.132
−1.136
23.166
1.00
22.44
C

ATOM
1805
CB
GLU
B2117
31.199
0.229
22.473
1.00
21.55
C

ATOM
1806
CG
GLU
B2117
32.570
0.672
22.003
1.00
26.09
C

ATOM
1807
CD
GLU
B2117
32.563
2.110
21.477
1.00
26.21
C

ATOM
1808
OE1
GLU
B2117
31.958
2.997
22.132
1.00
24.17
O

ATOM
1809
OE2
GLU
B2117
33.170
2.355
20.412
1.00
27.59
O

ATOM
1810
C
GLU
B2117
32.116
−1.191
24.335
1.00
24.52
C

ATOM
1811
O
GLU
B2117
31.829
−0.711
25.432
1.00
21.96
O

ATOM
1812
N
GLU
B2118
33.266
−1.806
24.084
1.00
26.38
N

ATOM
1813
CA
GLU
B2118
34.331
−1.920
25.070
1.00
31.02
C

ATOM
1814
CB
GLU
B2118
34.781
−3.373
25.209
1.00
33.06
C

ATOM
1815
CG
GLU
B2118
33.888
−4.220
26.082
1.00
38.01
C

ATOM
1816
CD
GLU
B2118
34.094
−3.939
27.552
1.00
42.42
C

ATOM
1817
OE1
GLU
B2118
33.776
−2.816
27.998
1.00
44.59
O

ATOM
1818
OE2
GLU
B2118
34.584
−4.845
28.262
1.00
45.87
O

ATOM
1819
C
GLU
B2118
35.482
−1.091
24.533
1.00
32.66
C

ATOM
1820
O
GLU
B2118
35.880
−0.108
25.197
1.00
35.23
O

ATOM
1821
OXT
GLU
B2118
35.958
−1.442
23.431
1.00
32.94
O

TER
1822

GLU
B2118

ATOM
1823
CB
MET
C3003
37.039
0.395
12.081
1.00
32.22
C

ATOM
1824
CG
MET
C3003
37.297
−0.447
10.845
1.00
36.68
C

ATOM
1825
SD
MET
C3003
38.483
0.306
9.716
1.00
46.15
S

ATOM
1826
CE
MET
C3003
37.454
1.490
8.876
1.00
42.14
C

ATOM
1827
C
MET
C3003
34.864
−0.764
12.331
1.00
25.86
C

ATOM
1828
O
MET
C3003
34.821
−1.903
11.864
1.00
26.11
O

ATOM
1829
N
MET
C3003
36.772
−1.388
13.778
1.00
27.93
N

ATOM
1830
CA
MET
C3003
36.090
−0.264
13.082
1.00
27.91
C

ATOM
1831
N
ILE
C3004
33.866
0.097
12.219
1.00
23.54
N

ATOM
1832
CA
ILE
C3004
32.655
−0.247
11.500
1.00
21.79
C

ATOM
1833
CB
ILE
C3004
31.503
0.697
11.890
1.00
22.07
C

ATOM
1834
CG2
ILE
C3004
30.259
0.377
11.063
1.00
20.08
C

ATOM
1835
CG1
ILE
C3004
31.212
0.560
13.391
1.00
21.69
C

ATOM
1836
CD1
ILE
C3004
30.181
1530
13.913
1.00
20.52
C

ATOM
1837
C
ILE
C3004
32.942
−0.109
10.005
1.00
22.42
C

ATOM
1838
O
ILE
C3004
33.595
0.843
9.578
1.00
21.61
O

ATOM
1839
N
VAL
C3005
32.483
−1.071
9.212
1.00
21.57
N

ATOM
1840
CA
VAL
C3005
32.692
−0.999
7.777
1.00
22.56
C

ATOM
1841
CB
VAL
C3005
33.600
−2.145
7.265
1.00
24.27
C

ATOM
1842
CG1
VAL
C3005
34.954
−2.087
7.975
1.00
23.54
C

ATOM
1843
CG2
VAL
C3005
32.924
−3.487
7.478
1.00
25.12
C

ATOM
1844
C
VAL
C3005
31.349
−1.036
7.049
1.00
22.07
C

ATOM
1845
O
VAL
C3005
31.297
−0.988
5.823
1.00
22.90
O

ATOM
1846
N
GLY
C3006
30.264
−1.106
7.814
1.00
19.77
N

ATOM
1847
CA
GLY
C3006
28.946
−1.124
7.207
1.00
18.90
C

ATOM
1848
C
GLY
C3006
27.840
−1.111
8.240
1.00
18.66
C

ATOM
1849
O
GLY
C3006
28.039
−1.542
9.375
1.00
19.40
O

ATOM
1850
N
HIS
C3007
26.679
−0.595
7.849
1.00
17.60
N

ATOM
1851
CA
HIS
C3007
25.517
−0.544
8.726
1.00
17.25
C

ATOM
1852
CB
HIS
C3007
25.541
0.709
9.615
1.00
17.61
C

ATOM
1853
CG
HIS
C3007
24.315
0.867
10.469
1.00
17.57
C

ATOM
1854
CD2
HIS
C3007
23.615
1.967
10.834
1.00
17.24
C

ATOM
1855
ND1
HIS
C3007
23.686
−0.203
11.072
1.00
17.16
N

ATOM
1856
CE1
HIS
C3007
22.651
0.231
11.771
1.00
17.81
C

ATOM
1857
NE2
HIS
C3007
22.585
1.545
11.644
1.00
18.60
N

ATOM
1858
C
HIS
C3007
24.264
−0.540
7.867
1.00
17.20
C

ATOM
1859
O
HIS
C3007
24.138
0.249
6.924
1.00
17.44
O

ATOM
1860
N
GLY
C3008
23.335
−1.427
8.187
1.00
16.34
N

ATOM
1861
CA
GLY
C3008
22.111
−1.484
7.416
1.00
18.39
C

ATOM
1862
C
GLY
C3008
20.925
−1.924
8.242
1.00
19.04
C

ATOM
1863
O
GLY
C3008
21.060
−2.752
9.145
1.00
19.03
O

ATOM
1864
N
ILE
C3009
19.761
−1.352
7.944
1.00
18.83
N

ATOM
1865
CA
ILE
C3009
18.542
−1.718
8.640
1.00
19.42
C

ATOM
1866
CB
ILE
C3009
18.047
−0.598
9.594
1.00
18.51
C

ATOM
1867
CG2
ILE
C3009
19.197
−0.150
10.493
1.00
20.36
C

ATOM
1868
CG1
ILE
C3009
17.505
0.585
8.797
1.00
17.23
C

ATOM
1869
CD1
ILE
C3009
16.778
1.592
9.643
1.00
13.66
C

ATOM
1870
C
ILE
C3009
17.473
−1.992
7.602
1.00
18.70
C

ATOM
1871
O
ILE
C3009
17.647
−1.685
6.427
1.00
15.95
O

ATOM
1872
N
ASP
C3010
16.369
−2.585
8.037
1.00
19.75
N

ATOM
1873
CA
ASP
C3010
15.278
−2.882
7.129
1.00
20.22
C

ATOM
1874
CB
ASP
C3010
15.550
−4.184
6.358
1.00
20.94
C

ATOM
1875
CG
ASP
C3010
14.474
−4.487
5.310
1.00
22.14
C

ATOM
1876
OD1
ASP
C3010
14.480
−3.844
4.236
1.00
22.44
O

ATOM
1877
OD2
ASP
C3010
13.617
−5.363
5.561
1.00
20.92
O

ATOM
1878
C
ASP
C3010
14.007
−3.047
7.932
1.00
21.28
C

ATOM
1879
O
ASP
C3010
14.042
−3.500
9.078
1.00
21.26
O

ATOM
1880
N
ILE
C3011
12.893
−2.646
7.333
1.00
19.66
N

ATOM
1881
CA
ILE
C3011
11.588
−2.813
7.949
1.00
20.09
C

ATOM
1882
CB
ILE
C3011
10.959
−1.476
8.400
1.00
20.39
C

ATOM
1883
CG2
ILE
C3011
10.910
−0.478
7.234
1.00
16.27
C

ATOM
1884
CG1
ILE
C3011
9.561
−1.753
8.971
1.00
20.84
C

ATOM
1885
CD1
ILE
C3011
9.081
−0.712
9.969
1.00
21.63
C

ATOM
1886
C
ILE
C3011
10.777
−3.440
6.825
1.00
21.21
C

ATOM
1887
O
ILE
C3011
10.866
−3.006
5.678
1.00
21.49
O

ATOM
1888
N
GLU
C3012
10.018
−4.481
7.140
1.00
21.79
N

ATOM
1889
CA
GLU
C3012
9.249
−5.174
6.120
1.00
23.44
C

ATOM
1890
CB
GLU
C3012
10.024
−6.415
5.656
1.00
24.63
C

ATOM
1891
CG
GLU
C3012
9.269
−7.309
4.667
1.00
27.74
C

ATOM
1892
CD
GLU
C3012
9.351
−6.812
3.237
1.00
27.70
C

ATOM
1893
OE1
GLU
C3012
9.663
−5.626
3.032
1.00
28.89
O

ATOM
1894
OE2
GLU
C3012
9.091
−7.612
2.314
1.00
31.17
O

ATOM
1895
C
GLU
C3012
7.873
−5.583
6.625
1.00
23.57
C

ATOM
1896
O
GLU
C3012
7.750
−6.258
7.647
1.00
22.12
O

ATOM
1897
N
GLU
C3013
6.840
−5.170
5.904
1.00
23.45
N

ATOM
1898
CA
GLU
C3013
5.491
−5.519
6.286
1.00
24.76
C

ATOM
1899
CB
GLU
C3013
4.479
−4.613
5.571
1.00
29.22
C

ATOM
1900
CG
GLU
C3013
3.662
−3.731
6.531
1.00
33.17
C

ATOM
1901
CD
GLU
C3013
3.915
−2.242
6.349
1.00
38.85
C

ATOM
1902
OE1
GLU
C3013
3.660
−1.719
5.238
1.00
44.44
O

ATOM
1903
OE2
GLU
C3013
4.359
−1.586
7.318
1.00
38.04
O

ATOM
1904
C
GLU
C3013
5.238
−6.993
5.963
1.00
24.30
C

ATOM
1905
O
GLU
C3013
5.643
−7.502
4.910
1.00
21.31
O

ATOM
1906
N
LEU
C3014
4.599
−7.685
6.898
1.00
22.97
N

ATOM
1907
CA
LEU
C3014
4.287
−9.092
6.712
1.00
26.19
C

ATOM
1908
CB
LEU
C3014
3.531
−9.613
7.939
1.00
28.12
C

ATOM
1909
CG
LEU
C3014
4.251
−10.630
8.829
1.00
31.98
C

ATOM
1910
CD1
LEU
C3014
5.647
−10.144
9.191
1.00
31.03
C

ATOM
1911
CD2
LEU
C3014
3.414
−10.868
10.083
1.00
33.69
C

ATOM
1912
C
LEU
C3014
3.453
−9.308
5.439
1.00
25.44
C

ATOM
1913
O
LEU
C3014
3.554
−10.345
4.793
1.00
25.78
O

ATOM
1914
N
ALA
C3015
2.644
−8.320
5.073
1.00
24.83
N

ATOM
1915
CA
ALA
C3015
1.801
−8.438
3.879
1.00
27.12
C

ATOM
1916
CB
ALA
C3015
0.915
−7.206
3.747
1.00
27.24
C

ATOM
1917
C
ALA
C3015
2.592
−8.659
2.584
1.00
27.01
C

ATOM
1918
O
ALA
C3015
2.215
−9.497
1.761
1.00
26.98
O

ATOM
1919
N
SER
C3016
3.683
−7.916
2.399
1.00
26.19
N

ATOM
1920
CA
SER
C3016
4.498
−8.062
1.192
1.00
27.18
C

ATOM
1921
CB
SER
C3016
5.706
−7.117
1.232
1.00
27.62
C

ATOM
1922
OG
SER
C3016
5.324
−5.799
1.573
1.00
28.51
O

ATOM
1923
C
SER
C3016
4.997
−9.502
1.072
1.00
27.53
C

ATOM
1924
O
SER
C3016
5.069
−10.062
−0.027
1.00
26.07
O

ATOM
1925
N
ILE
C3017
5.343
−10.094
2.212
1.00
26.80
N

ATOM
1926
CA
ILE
C3017
5.841
−11.464
2.248
1.00
25.88
C

ATOM
1927
CB
ILE
C3017
6.519
−11.771
3.613
1.00
25.28
C

ATOM
1928
CG2
ILE
C3017
6.909
−13.241
3.688
1.00
23.81
C

ATOM
1929
CG1
ILE
C3017
7.739
−10.863
3.808
1.00
24.39
C

ATOM
1930
CD1
ILE
C3017
8.815
−11.007
2.735
1.00
24.49
C

ATOM
1931
C
ILE
C3017
4.698
−12.456
2.019
1.00
26.06
C

ATOM
1932
O
ILE
C3017
4.830
−13.408
1.253
1.00
26.57
O

ATOM
1933
N
GLU
C3018
3.576
−12.235
2.690
1.00
26.59
N

ATOM
1934
CA
GLU
C3018
2.429
−13.122
2.534
1.00
28.88
C

ATOM
1935
CB
GLU
C3018
1.284
−12.645
3.427
1.00
29.66
C

ATOM
1936
CG
GLU
C3018
1.688
−12.504
4.884
1.00
32.78
C

ATOM
1937
CD
GLU
C3018
0.656
−11.783
5.722
1.00
34.19
C

ATOM
1938
OE1
GLU
C3018
−0.010
−10.865
5.190
1.00
34.18
O

ATOM
1939
OE2
GLU
C3018
0.525
−12.118
6.920
1.00
35.99
O

ATOM
1940
C
GLU
C3018
1.983
−13.163
1.067
1.00
29.36
C

ATOM
1941
O
GLU
C3018
1.763
−14.239
0.507
1.00
28.97
O

ATOM
1942
N
SER
C3019
1.867
−11.994
0.440
1.00
28.95
N

ATOM
1943
CA
SER
C3019
1.454
−11.931
−0.957
1.00
29.90
C

ATOM
1944
CB
SER
C3019
1.285
−10.476
−1.410
1.00
30.07
C

ATOM
1945
OG
SER
C3019
2.542
−9.866
−1.632
1.00
33.15
O

ATOM
1946
C
SER
C3019
2.489
−12.623
−1.837
1.00
30.43
C

ATOM
1947
O
SER
C3019
2.138
−13.362
−2.755
1.00
30.07
O

ATOM
1948
N
ALA
C3020
3.766
−12.391
−1.549
1.00
29.14
N

ATOM
1949
CA
ALA
C3020
4.842
−12.994
−2.327
1.00
30.13
C

ATOM
1950
CB
ALA
C3020
6.191
−12.465
−1.847
1.00
31.02
C

ATOM
1951
C
ALA
C3020
4.834
−14.527
−2.269
1.00
30.69
C

ATOM
1952
O
ALA
C3020
5.111
−15.198
−3.264
1.00
30.30
O

ATOM
1953
N
VAL
C3021
4.530
−15.082
−1.103
1.00
30.94
N

ATOM
1954
CA
VAL
C3021
4.501
−16.532
−0.959
1.00
33.03
C

ATOM
1955
CB
VAL
C3021
4.172
−16.950
0.489
1.00
32.04
C

ATOM
1956
CG1
VAL
C3021
3.982
−18.465
0.565
1.00
31.51
C

ATOM
1957
CG2
VAL
C3021
5.292
−16.521
1.414
1.00
31.14
C

ATOM
1958
C
VAL
C3021
3.458
−17.135
−1.896
1.00
35.03
C

ATOM
1959
O
VAL
C3021
3.736
−18.094
−2.616
1.00
36.27
O

ATOM
1960
N
THR
C3022
2.263
−16.552
−1.889
1.00
36.26
N

ATOM
1961
CA
THR
C3022
1.166
−17.019
−2.726
1.00
38.71
C

ATOM
1962
CB
THR
C3022
−0.142
−16.274
−2.371
1.00
38.89
C

ATOM
1963
OG1
THR
C3022
−0.532
−16.613
−1.034
1.00
39.61
O

ATOM
1964
CG2
THR
C3022
−1.262
−16.654
−3.336
1.00
37.67
C

ATOM
1965
C
THR
C3022
1.458
−16.836
−4.214
1.00
40.67
C

ATOM
1966
O
THR
C3022
1.325
−17.772
−5.005
1.00
40.21
O

ATOM
1967
N
ARG
C3023
1.859
−15.626
−4.587
1.00
42.70
N

ATOM
1968
CA
ARG
C3023
2.161
−15.303
−5.974
1.00
46.22
C

ATOM
1969
CB
ARG
C3023
2.861
−13.944
−6.037
1.00
46.79
C

ATOM
1970
CG
ARG
C3023
2.842
−13.278
−7.396
1.00
47.31
C

ATOM
1971
CD
ARG
C3023
3.264
−11.827
−7.269
1.00
47.58
C

ATOM
1972
NE
ARG
C3023
4.544
−11.695
−6.577
1.00
48.02
N

ATOM
1973
CZ
ARG
C3023
4.741
−10.924
−5.511
1.00
48.91
C

ATOM
1974
NH1
ARG
C3023
3.736
−10.214
−5.008
1.00
46.67
N

ATOM
1975
NH2
ARG
C3023
5.943
−10.861
−4.948
1.00
48.13
N

ATOM
1976
C
ARG
C3023
3.020
−16.391
−6.616
1.00
47.90
C

ATOM
1977
O
ARG
C3023
2.684
−16.906
−7.681
1.00
49.41
O

ATOM
1978
N
HIS
C3024
4.129
−16.737
−5.968
1.00
49.64
N

ATOM
1979
CA
HIS
C3024
5.019
−17.787
−6.458
1.00
50.08
C

ATOM
1980
CB
HIS
C3024
6.303
−17.193
−7.045
1.00
51.60
C

ATOM
1981
CG
HIS
C3024
6.100
−16.464
−8.338
1.00
53.54
C

ATOM
1982
CD2
HIS
C3024
6.507
−16.754
−9.597
1.00
53.69
C

ATOM
1983
ND1
HIS
C3024
5.397
−15.282
−8.426
1.00
54.78
N

ATOM
1984
CE1
HIS
C3024
5.379
−14.875
−9.683
1.00
53.97
C

ATOM
1985
NE2
HIS
C3024
6.045
−15.750
−10.414
1.00
53.74
N

ATOM
1986
C
HIS
C3024
5.370
−18.720
−5.304
1.00
50.32
C

ATOM
1987
O
HIS
C3024
6.030
−18.314
−4.347
1.00
50.15
O

ATOM
1988
N
GLU
C3025
4.929
−19.971
−5.394
1.00
49.54
N

ATOM
1989
CA
GLU
C3025
5.197
−20.937
−4.335
1.00
49.18
C

ATOM
1990
CB
GLU
C3025
4.507
−22.270
−4.632
1.00
52.19
C

ATOM
1991
CG
GLU
C3025
4.778
−23.331
−3.575
1.00
55.07
C

ATOM
1992
CD
GLU
C3025
4.269
−24.694
−3.972
1.00
57.92
C

ATOM
1993
OE1
GLU
C3025
3.033
−24.870
−4.053
1.00
58.55
O

ATOM
1994
OE2
GLU
C3025
5.111
−25.590
−4.206
1.00
59.67
O

ATOM
1995
C
GLU
C3025
6.685
−21.182
−4.118
1.00
46.90
C

ATOM
1996
O
GLU
C3025
7.087
−21.711
−3.084
1.00
47.27
O

ATOM
1997
N
GLY
C3026
7.502
−20.801
−5.092
1.00
44.54
N

ATOM
1998
CA
GLY
C3026
8.933
−20.997
−4.956
1.00
41.90
C

ATOM
1999
C
GLY
C3026
9.636
−19.811
−4.320
1.00
40.26
C

ATOM
2000
O
GLY
C3026
10.867
−19.768
−4.265
1.00
39.86
O

ATOM
2001
N
PHE
C3027
8.860
−18.842
−3.841
1.00
37.59
N

ATOM
2002
CA
PHE
C3027
9.434
−17.655
−3.217
1.00
35.31
C

ATOM
2003
CB
PHE
C3027
8.323
−16.715
−2.738
1.00
34.09
C

ATOM
2004
CG
PHE
C3027
8.832
−15.491
−2.031
1.00
33.77
C

ATOM
2005
CD1
PHE
C3027
9.633
−14.569
−2.700
1.00
33.43
C

ATOM
2006
CD2
PHE
C3027
8.543
−15.277
−0.687
1.00
32.68
C

ATOM
2007
CE1
PHE
C3027
10.141
−13.450
−2.042
1.00
32.28
C

ATOM
2008
CE2
PHE
C3027
9.045
−14.163
−0.016
1.00
33.06
C

ATOM
2009
CZ
PHE
C3027
9.847
−13.248
−0.696
1.00
33.30
C

ATOM
2010
C
PHE
C3027
10.331
−18.032
−2.042
1.00
34.03
C

ATOM
2011
O
PHE
C3027
11.511
−17.688
−2.019
1.00
34.88
O

ATOM
2012
N
ALA
C3028
9.767
−18.743
−1.071
1.00
33.39
N

ATOM
2013
CA
ALA
C3028
10.516
−19.159
0.109
1.00
34.32
C

ATOM
2014
CB
ALA
C3028
9.651
−20.053
0.987
1.00
33.64
C

ATOM
2015
C
ALA
C3028
11.799
−19.885
−0.263
1.00
34.75
C

ATOM
2016
O
ALA
C3028
12.873
−19.572
0.257
1.00
34.90
O

ATOM
2017
N
LYS
C3029
11.683
−20.854
−1.166
1.00
33.73
N

ATOM
2018
CA
LYS
C3029
12.831
−21.636
−1.605
1.00
32.87
C

ATOM
2019
CB
LYS
C3029
12.396
−22.671
−2.650
1.00
32.28
C

ATOM
2020
CG
LYS
C3029
11.313
−23.617
−2.157
0.05
32.40
C

ATOM
2021
CD
LYS
C3029
10.821
−24.537
−3.261
0.05
32.28
C

ATOM
2022
CE
LYS
C3029
9.721
−25.456
−2.753
0.05
32.20
C

ATOM
2023
NZ
LYS
C3029
9.160
−26.313
−3.833
0.05
32.15
N

ATOM
2024
C
LYS
C3029
13.910
−20.735
−2.181
1.00
32.70
C

ATOM
2025
O
LYS
C3029
15.100
−21.016
−2.048
1.00
33.44
O

ATOM
2026
N
ARG
C3030
13.498
−19.643
−2.814
1.00
32.85
N

ATOM
2027
CA
ARG
C3030
14.458
−18.714
−3.397
1.00
32.53
C

ATOM
2028
CB
ARG
C3030
13.796
−17.877
−4.497
0.05
32.58
C

ATOM
2029
CG
ARG
C3030
13.442
−18.670
−5.747
0.05
32.72
C

ATOM
2030
CD
ARG
C3030
13.135
−17.752
−6.922
0.05
32.87
C

ATOM
2031
NE
ARG
C3030
11.916
−16.973
−6.722
0.05
33.03
N

ATOM
2032
CZ
ARG
C3030
10.691
−17.490
−6.720
0.05
33.10
C

ATOM
2033
NH1
ARG
C3030
10.517
−18.791
−6.908
0.05
33.16
N

ATOM
2034
NH2
ARG
C3030
9.639
−16.705
−6.531
0.05
33.04
N

ATOM
2035
C
ARG
C3030
15.080
−17.794
−2.351
1.00
32.30
C

ATOM
2036
O
ARG
C3030
16.242
−17.408
−2.470
1.00
32.85
O

ATOM
2037
N
VAL
C3031
14.303
−17.455
−1.325
1.00
31.53
N

ATOM
2038
CA
VAL
C3031
14.755
−16.574
−0.245
1.00
30.10
C

ATOM
2039
CB
VAL
C3031
13.541
−15.905
0.469
1.00
30.44
C

ATOM
2040
CG1
VAL
C3031
14.007
−15.140
1.701
1.00
31.92
C

ATOM
2041
CG2
VAL
C3031
12.824
−14.967
−0.484
1.00
31.35
C

ATOM
2042
C
VAL
C3031
15.576
−17.284
0.836
1.00
29.72
C

ATOM
2043
O
VAL
C3031
16.475
−16.686
1.439
1.00
29.40
O

ATOM
2044
N
LEU
C3032
15.259
−18.554
1.076
1.00
27.31
N

ATOM
2045
CA
LEU
C3032
15.911
−19.338
2.119
1.00
25.97
C

ATOM
2046
CB
LEU
C3032
14.839
−19.917
3.047
1.00
24.74
C

ATOM
2047
CG
LEU
C3032
13.782
−18.943
3.572
1.00
22.82
C

ATOM
2048
CD1
LEU
C3032
12.717
−19.708
4.361
1.00
23.17
C

ATOM
2049
CD2
LEU
C3032
14.454
−17.893
4.452
1.00
21.55
C

ATOM
2050
C
LEU
C3032
16.793
−20.485
1.630
1.00
27.28
C

ATOM
2051
O
LEU
C3032
16.447
−21.187
0.676
1.00
28.34
O

ATOM
2052
N
THR
C3033
17.924
−20.676
2.307
1.00
26.40
N

ATOM
2053
CA
THR
C3033
18.847
−21.756
1.984
1.00
27.30
C

ATOM
2054
CB
THR
C3033
20.149
−21.662
2.795
1.00
25.69
C

ATOM
2055
OG1
THR
C3033
19.845
−21.820
4.186
1.00
26.34
O

ATOM
2056
CG2
THR
C3033
20.835
−20.323
2.574
1.00
26.77
C

ATOM
2057
C
THR
C3033
18.170
−23.062
2.385
1.00
27.70
C

ATOM
2058
O
THR
C3033
17.061
−23.061
2.920
1.00
28.12
O

ATOM
2059
N
ALA
C3034
18.853
−24.174
2.145
1.00
28.90
N

ATOM
2060
CA
ALA
C3034
18.314
−25.484
2.493
1.00
29.05
C

ATOM
2061
CB
ALA
C3034
19.283
−26.572
2.062
1.00
29.42
C

ATOM
2062
C
ALA
C3034
18.047
−25.594
3.990
1.00
28.60
C

ATOM
2063
O
ALA
C3034
16.965
−26.008
4.403
1.00
29.51
O

ATOM
2064
N
LEU
C3035
19.029
−25.218
4.805
1.00
28.04
N

ATOM
2065
CA
LEU
C3035
18.869
−25.310
6.249
1.00
27.61
C

ATOM
2066
CB
LEU
C3035
20.187
−24.964
6.952
1.00
29.31
C

ATOM
2067
CG
LEU
C3035
20.522
−25.809
8.190
1.00
31.59
C

ATOM
2068
CD1
LEU
C3035
20.472
−27.297
7.821
1.00
32.29
C

ATOM
2069
CD2
LEU
C3035
21.902
−25.438
8.727
1.00
30.00
C

ATOM
2070
C
LEU
C3035
17.740
−24.410
6.747
1.00
27.52
C

ATOM
2071
O
LEU
C3035
16.922
−24.832
7.571
1.00
26.23
O

ATOM
2072
N
GLU
C3036
17.688
−23.176
6.247
1.00
27.39
N

ATOM
2073
CA
GLU
C3036
16.636
−22.240
6.649
1.00
27.23
C

ATOM
2074
CB
GLU
C3036
16.849
−20.877
5.981
1.00
25.56
C

ATOM
2075
CG
GLU
C3036
17.834
−19.978
6.707
1.00
22.65
C

ATOM
2076
CD
GLU
C3036
18.256
−18.777
5.880
1.00
23.21
C

ATOM
2077
OE1
GLU
C3036
18.735
−17.784
6.469
1.00
22.56
O

ATOM
2078
OE2
GLU
C3036
18.124
−18.825
4.638
1.00
24.80
O

ATOM
2079
C
GLU
C3036
15.258
−22.793
6.278
1.00
28.00
C

ATOM
2080
O
GLU
C3036
14.306
−22.668
7.047
1.00
27.30
O

ATOM
2081
N
MET
C3037
15.160
−23.401
5.098
1.00
28.24
N

ATOM
2082
CA
MET
C3037
13.897
−23.979
4.641
1.00
30.24
C

ATOM
2083
CB
MET
C3037
14.051
−24.593
3.247
1.00
31.74
C

ATOM
2084
CG
MET
C3037
13.885
−23.605
2.102
1.00
32.56
C

ATOM
2085
SD
MET
C3037
12.289
−22.761
2.156
1.00
37.45
S

ATOM
2086
CE
MET
C3037
11.153
−24.108
1.753
1.00
36.07
C

ATOM
2087
C
MET
C3037
13.411
−25.049
5.608
1.00
31.16
C

ATOM
2088
O
MET
C3037
12.222
−25.124
5.920
1.00
30.55
O

ATOM
2089
N
GLU
C3038
14.336
−25.882
6.076
1.00
31.23
N

ATOM
2090
CA
GLU
C3038
13.992
−26.936
7.018
1.00
31.35
C

ATOM
2091
CB
GLU
C3038
15.257
−27.635
7.525
0.05
30.95
C

ATOM
2092
CG
GLU
C3038
15.478
−29.023
6.948
0.05
30.58
C

ATOM
2093
CD
GLU
C3038
16.721
−29.692
7.504
0.05
30.41
C

ATOM
2094
OE1
GLU
C3038
16.840
−29.795
8.744
0.05
30.03
O

ATOM
2095
OE2
GLU
C3038
17.578
−30.118
6.702
0.05
30.15
O

ATOM
2096
C
GLU
C3038
13.235
−26.330
8.191
1.00
31.53
C

ATOM
2097
O
GLU
C3038
12.255
−26.897
8.663
1.00
32.15
O

ATOM
2098
N
ARG
C3039
13.697
−25.176
8.664
1.00
32.00
N

ATOM
2099
CA
ARG
C3039
13.046
−24.496
9.781
1.00
33.21
C

ATOM
2100
CB
ARG
C3039
13.928
−23.353
10.289
1.00
34.11
C

ATOM
2101
CG
ARG
C3039
13.317
−22.548
11.434
1.00
37.68
C

ATOM
2102
CD
ARG
C3039
13.189
−23.377
12.704
1.00
39.59
C

ATOM
2103
NE
ARG
C3039
12.565
−22.626
13.791
1.00
41.92
N

ATOM
2104
CZ
ARG
C3039
12.195
−23.159
14.952
1.00
43.02
C

ATOM
2105
NH1
ARG
C3039
12.384
−24.450
15.183
1.00
43.57
N

ATOM
2106
NH2
ARG
C3039
11.625
−22.402
15.881
1.00
44.00
N

ATOM
2107
C
ARG
C3039
11.692
−23.939
9.339
1.00
32.70
C

ATOM
2108
O
ARG
C3039
10.674
−24.130
10.005
1.00
31.81
O

ATOM
2109
N
PHE
C3040
11.699
−23.240
8.210
1.00
32.86
N

ATOM
2110
CA
PHE
C3040
10.489
−22.646
7.653
1.00
33.52
C

ATOM
2111
CB
PHE
C3040
10.778
−22.128
6.242
1.00
32.08
C

ATOM
2112
CG
PHE
C3040
9.569
−21.604
5.528
1.00
32.50
C

ATOM
2113
CD1
PHE
C3040
9.012
−20.380
5.880
1.00
31.27
C

ATOM
2114
CD2
PHE
C3040
8.980
−22.340
4.503
1.00
32.76
C

ATOM
2115
CE1
PHE
C3040
7.882
−19.895
5.222
1.00
31.92
C

ATOM
2116
CE2
PHE
C3040
7.851
−21.865
3.839
1.00
33.27
C

ATOM
2117
CZ
PHE
C3040
7.301
−20.637
4.201
1.00
31.45
C

ATOM
2118
C
PHE
C3040
9.367
−23.680
7.595
1.00
33.45
C

ATOM
2119
O
PHE
C3040
8.264
−23.457
8.100
1.00
33.35
O

ATOM
2120
N
THR
C3041
9.669
−24.819
6.983
1.00
34.68
N

ATOM
2121
CA
THR
C3041
8.706
−25.898
6.828
1.00
35.57
C

ATOM
2122
CB
THR
C3041
9.286
−27.002
5.923
1.00
36.24
C

ATOM
2123
OG1
THR
C3041
9.517
−26.464
4.616
1.00
38.04
O

ATOM
2124
CG2
THR
C3041
8.324
−28.170
5.813
1.00
36.60
C

ATOM
2125
C
THR
C3041
8.232
−26.517
8.143
1.00
36.09
C

ATOM
2126
O
THR
C3041
7.084
−26.945
8.247
1.00
37.27
O

ATOM
2127
N
SER
C3042
9.100
−26.560
9.147
1.00
36.67
N

ATOM
2128
CA
SER
C3042
8.718
−27.142
10.427
1.00
37.38
C

ATOM
2129
CB
SER
C3042
9.952
−27.377
11.303
1.00
38.44
C

ATOM
2130
OG
SER
C3042
10.391
−26.172
11.904
1.00
39.31
O

ATOM
2131
C
SER
C3042
7.744
−26.230
11.157
1.00
37.81
C

ATOM
2132
O
SER
C3042
7.010
−26.671
12.042
1.00
38.07
O

ATOM
2133
N
LEU
C3043
7.740
−24.956
10.781
1.00
37.43
N

ATOM
2134
CA
LEU
C3043
6.860
−23.969
11.400
1.00
37.02
C

ATOM
2135
CB
LEU
C3043
7.549
−22.600
11.428
1.00
37.05
C

ATOM
2136
CG
LEU
C3043
8.597
−22.327
12.513
1.00
37.93
C

ATOM
2137
CD1
LEU
C3043
9.573
−23.470
12.628
1.00
39.39
C

ATOM
2138
CD2
LEU
C3043
9.328
−21.040
12.177
1.00
38.02
C

ATOM
2139
C
LEU
C3043
5.526
−23.851
10.666
1.00
37.04
C

ATOM
2140
O
LEU
C3043
5.389
−24.291
9.522
1.00
37.65
O

ATOM
2141
N
LYS
C3044
4.542
−23.250
11.325
1.00
36.12
N

ATOM
2142
CA
LYS
C3044
3.236
−23.075
10.707
1.00
35.63
C

ATOM
2143
CB
LYS
C3044
2.313
−24.246
11.072
1.00
37.63
C

ATOM
2144
CG
LYS
C3044
1.985
−24.356
12.555
1.00
40.09
C

ATOM
2145
CD
LYS
C3044
0.926
−25.432
12.813
1.00
42.38
C

ATOM
2146
CE
LYS
C3044
1.397
−26.813
12.365
1.00
42.85
C

ATOM
2147
NZ
LYS
C3044
0.339
−27.847
12.550
1.00
43.11
N

ATOM
2148
C
LYS
C3044
2.584
−21.753
11.111
1.00
33.57
C

ATOM
2149
O
LYS
C3044
2.990
−21.116
12.086
1.00
33.02
O

ATOM
2150
N
GLY
C3045
1.579
−21.345
10.339
1.00
31.64
N

ATOM
2151
CA
GLY
C3045
0.860
−20.115
10.618
1.00
29.90
C

ATOM
2152
C
GLY
C3045
1.689
−18.844
10.666
1.00
28.38
C

ATOM
2153
O
GLY
C3045
2.643
−18.676
9.915
1.00
28.13
O

ATOM
2154
N
ARG
C3046
1.299
−17.946
11.564
1.00
28.66
N

ATOM
2155
CA
ARG
C3046
1.957
−16.661
11.758
1.00
27.23
C

ATOM
2156
CB
ARG
C3046
1.279
−15.920
12.912
0.05
27.45
C

ATOM
2157
CG
ARG
C3046
−0.235
−15.860
12.769
0.05
27.80
C

ATOM
2158
CD
ARG
C3046
−0.912
−15.403
14.048
0.05
28.08
C

ATOM
2159
NE
ARG
C3046
−2.364
−15.526
13.962
0.05
28.35
N

ATOM
2160
CZ
ARG
C3046
−3.199
−15.249
14.959
0.05
28.51
C

ATOM
2161
NH1
ARG
C3046
−4.506
−15.394
14.792
0.05
28.59
N

ATOM
2162
NH2
ARG
C3046
−2.727
−14.831
16.127
0.05
28.63
N

ATOM
2163
C
ARG
C3046
3.451
−16.827
12.041
1.00
26.66
C

ATOM
2164
O
ARG
C3046
4.276
−16.065
11.537
1.00
23.83
O

ATOM
2165
N
ARG
C3047
3.797
−17.824
12.847
1.00
26.74
N

ATOM
2166
CA
ARG
C3047
5.197
−18.068
13.172
1.00
28.45
C

ATOM
2167
CB
ARG
C3047
5.330
−19.223
14.167
1.00
30.78
C

ATOM
2168
CG
ARG
C3047
4.824
−18.919
15.567
1.00
36.74
C

ATOM
2169
CD
ARG
C3047
5.548
−19.793
16.580
1.00
40.75
C

ATOM
2170
NE
ARG
C3047
6.991
−19.561
16.540
1.00
43.99
N

ATOM
2171
CZ
ARG
C3047
7.894
−20.341
17.126
1.00
45.84
C

ATOM
2172
NH1
ARG
C3047
7.508
−21.417
17.803
1.00
47.05
N

ATOM
2173
NH2
ARG
C3047
9.184
−20.046
17.036
1.00
46.26
N

ATOM
2174
C
ARG
C3047
6.004
−18.396
11.924
1.00
26.96
C

ATOM
2175
O
ARG
C3047
7.171
−18.019
11.809
1.00
27.18
O

ATOM
2176
N
GLN
C3048
5.385
−19.108
10.989
1.00
25.16
N

ATOM
2177
CA
GLN
C3048
6.080
−19.474
9.765
1.00
24.64
C

ATOM
2178
CB
GLN
C3048
5.262
−20.489
8.964
1.00
24.71
C

ATOM
2179
CG
GLN
C3048
6.087
−21.176
7.884
1.00
24.87
C

ATOM
2180
CD
GLN
C3048
5.261
−22.028
6.947
1.00
27.10
C

ATOM
2181
OE1
GLN
C3048
5.757
−23.007
6.393
1.00
28.27
O

ATOM
2182
NE2
GLN
C3048
4.000
−21.650
6.747
1.00
27.28
N

ATOM
2183
C
GLN
C3048
6.342
−18.240
8.907
1.00
23.81
C

ATOM
2184
O
GLN
C3048
7.441
−18.064
8.376
1.00
22.00
O

ATOM
2185
N
ILE
C3049
5.323
−17.394
8.767
1.00
23.83
N

ATOM
2186
CA
ILE
C3049
5.449
−16.174
7.972
1.00
22.84
C

ATOM
2187
CB
ILE
C3049
4.099
−15.428
7.889
1.00
23.39
C

ATOM
2188
CG2
ILE
C3049
4.270
−14.110
7.123
1.00
20.78
C

ATOM
2189
CG1
ILE
C3049
3.068
−16.317
7.194
1.00
25.01
C

ATOM
2190
CD1
ILE
C3049
1.637
−15.812
7.313
1.00
28.28
C

ATOM
2191
C
ILE
C3049
6.492
−15.254
8.596
1.00
22.76
C

ATOM
2192
O
ILE
C3049
7.334
−14.695
7.901
1.00
22.64
O

ATOM
2193
N
GLU
C3050
6.426
−15.119
9.917
1.00
23.06
N

ATOM
2194
CA
GLU
C3050
7.347
−14.287
10.685
1.00
23.40
C

ATOM
2195
CB
GLU
C3050
7.023
−14.436
12.169
1.00
27.99
C

ATOM
2196
CG
GLU
C3050
7.336
−13.229
13.014
1.00
34.34
C

ATOM
2197
CD
GLU
C3050
6.633
−11.997
12.501
1.00
37.30
C

ATOM
2198
OE1
GLU
C3050
7.273
−11.233
11.752
1.00
38.54
O

ATOM
2199
OE2
GLU
C3050
5.437
−11.807
12.825
1.00
38.13
O

ATOM
2200
C
GLU
C3050
8.798
−14.707
10.429
1.00
22.91
C

ATOM
2201
O
GLU
C3050
9.675
−13.863
10.212
1.00
19.78
O

ATOM
2202
N
TYR
C3051
9.042
−16.018
10.451
1.00
20.98
N

ATOM
2203
CA
TYR
C3051
10.379
−16.549
10.218
1.00
20.96
C

ATOM
2204
CB
TYR
C3051
10.376
−18.087
10.286
1.00
20.94
C

ATOM
2205
CG
TYR
C3051
11.727
−18.710
9.996
1.00
21.84
C

ATOM
2206
CD1
TYR
C3051
12.091
−19.072
8.699
1.00
21.88
C

ATOM
2207
CE1
TYR
C3051
13.365
−19.563
8.420
1.00
22.08
C

ATOM
2208
CD2
TYR
C3051
12.675
−18.864
11.011
1.00
24.22
C

ATOM
2209
CE2
TYR
C3051
13.947
−19.353
10.743
1.00
22.50
C

ATOM
2210
CZ
TYR
C3051
14.286
−19.695
9.447
1.00
23.28
C

ATOM
2211
OH
TYR
C3051
15.557
−20.142
9.181
1.00
26.17
O

ATOM
2212
C
TYR
C3051
10.893
−16.093
8.863
1.00
21.41
C

ATOM
2213
O
TYR
C3051
11.973
−15.508
8.764
1.00
20.67
O

ATOM
2214
N
LEU
C3052
10.104
−16.357
7.823
1.00
20.18
N

ATOM
2215
CA
LEU
C3052
10.468
−15.985
6.465
1.00
19.73
C

ATOM
2216
CB
LEU
C3052
9.347
−16.399
5.502
1.00
20.90
C

ATOM
2217
CG
LEU
C3052
9.488
−16.052
4.019
1.00
20.73
C

ATOM
2218
CD1
LEU
C3052
10.837
−16.537
3.484
1.00
21.92
C

ATOM
2219
CD2
LEU
C3052
8.329
−16.704
3.247
1.00
22.34
C

ATOM
2220
C
LEU
C3052
10.725
−14.487
6.365
1.00
18.62
C

ATOM
2221
O
LEU
C3052
11.745
−14.057
5.819
1.00
18.97
O

ATOM
2222
N
ALA
C3053
9.805
−13.697
6.912
1.00
18.23
N

ATOM
2223
CA
ALA
C3053
9.921
−12.238
6.888
1.00
19.28
C

ATOM
2224
CB
ALA
C3053
8.670
−11.611
7.489
1.00
19.78
C

ATOM
2225
C
ALA
C3053
11.164
−11.746
7.634
1.00
18.63
C

ATOM
2226
O
ALA
C3053
11.835
−10.815
7.191
1.00
17.69
O

ATOM
2227
N
GLY
C3054
11.464
−12.375
8.767
1.00
18.30
N

ATOM
2228
CA
GLY
C3054
12.635
−11.989
9.534
1.00
18.14
C

ATOM
2229
C
GLY
C3054
13.915
−12.303
8.776
1.00
19.55
C

ATOM
2230
O
GLY
C3054
14.888
−11.545
8.831
1.00
18.40
O

ATOM
2231
N
ARG
C3055
13.927
−13.421
8.060
1.00
18.30
N

ATOM
2232
CA
ARG
C3055
15.112
−13.783
7.298
1.00
19.48
C

ATOM
2233
CB
ARG
C3055
15.021
−15.239
6.839
1.00
20.53
C

ATOM
2234
CG
ARG
C3055
15.815
−16.213
7.709
1.00
22.48
C

ATOM
2235
CD
ARG
C3055
15.450
−16.093
9.181
1.00
26.13
C

ATOM
2236
NE
ARG
C3055
16.291
−16.945
10.019
1.00
28.05
N

ATOM
2237
CZ
ARG
C3055
16.240
−16.972
11.347
1.00
28.02
C

ATOM
2238
NH1
ARG
C3055
15.389
−16.190
11.999
1.00
28.89
N

ATOM
2239
NH2
ARG
C3055
17.034
−17.788
12.024
1.00
28.23
N

ATOM
2240
C
ARG
C3055
15.283
−12.849
6.108
1.00
20.40
C

ATOM
2241
O
ARG
C3055
16.396
−12.399
5.817
1.00
20.36
O

ATOM
2242
N
TRP
C3056
14.182
−12.547
5.424
1.00
20.72
N

ATOM
2243
CA
TRP
C3056
14.234
−11.641
4.280
1.00
22.18
C

ATOM
2244
CB
TRP
C3056
12.837
−11.486
3.655
1.00
23.99
C

ATOM
2245
CG
TRP
C3056
12.716
−10.303
2.719
1.00
29.31
C

ATOM
2246
CD2
TRP
C3056
12.723
−10.335
1.289
1.00
30.25
C

ATOM
2247
CE2
TRP
C3056
12.609
−9.001
0.840
1.00
32.03
C

ATOM
2248
CE3
TRP
C3056
12.821
−11.362
0.342
1.00
33.18
C

ATOM
2249
CD1
TRP
C3056
12.598
−8.984
3.070
1.00
30.82
C

ATOM
2250
NE1
TRP
C3056
12.532
−8.198
1.947
1.00
33.62
N

ATOM
2251
CZ2
TRP
C3056
12.582
−8.665
−0.515
1.00
34.74
C

ATOM
2252
CZ3
TRP
C3056
12.795
−11.029
−1.010
1.00
34.82
C

ATOM
2253
CH2
TRP
C3056
12.679
−9.690
−1.425
1.00
36.26
C

ATOM
2254
C
TRP
C3056
14.746
−10.284
4.760
1.00
20.86
C

ATOM
2255
O
TRP
C3056
15.608
−9.670
4.134
1.00
18.98
O

ATOM
2256
N
SER
C3057
14.206
−9.835
5.885
1.00
18.95
N

ATOM
2257
CA
SER
C3057
14.586
−8.558
6.487
1.00
19.90
C

ATOM
2258
CB
SER
C3057
13.755
−8.321
7.752
1.00
21.78
C

ATOM
2259
OG
SER
C3057
14.067
−7.076
8.342
1.00
25.39
O

ATOM
2260
C
SER
C3057
16.070
−8.506
6.841
1.00
18.84
C

ATOM
2261
O
SER
C3057
16.767
−7.545
6.514
1.00
19.51
O

ATOM
2262
N
ALA
C3058
16.550
−9.545
7.509
1.00
18.85
N

ATOM
2263
CA
ALA
C3058
17.949
−9.611
7.917
1.00
18.94
C

ATOM
2264
CB
ALA
C3058
18.182
−10.854
8.765
1.00
16.86
C

ATOM
2265
C
ALA
C3058
18.912
−9.608
6.730
1.00
19.28
C

ATOM
2266
O
ALA
C3058
19.955
−8.946
6.765
1.00
19.47
O

ATOM
2267
N
LYS
C3059
18.567
−10.349
5.683
1.00
18.93
N

ATOM
2268
CA
LYS
C3059
19.424
−10.432
4.507
1.00
19.60
C

ATOM
2269
CB
LYS
C3059
18.965
−11.575
3.604
1.00
20.15
C

ATOM
2270
CG
LYS
C3059
19.102
−12.925
4.271
1.00
17.40
C

ATOM
2271
CD
LYS
C3059
18.773
−14.069
3.331
1.00
21.58
C

ATOM
2272
CE
LYS
C3059
18.813
−15.392
4.070
1.00
19.13
C

ATOM
2273
NZ
LYS
C3059
18.667
−16.545
3.158
1.00
24.92
N

ATOM
2274
C
LYS
C3059
19.437
−9.121
3.744
1.00
21.37
C

ATOM
2275
O
LYS
C3059
20.457
−8.734
3.165
1.00
22.73
O

ATOM
2276
N
GLU
C3060
18.297
−8.440
3.745
1.00
22.26
N

ATOM
2277
CA
GLU
C3060
18.175
−7.158
3.080
1.00
22.29
C

ATOM
2278
CB
GLU
C3060
16.708
−6.716
3.076
1.00
24.97
C

ATOM
2279
CG
GLU
C3060
16.424
−5.392
2.373
1.00
32.66
C

ATOM
2280
CD
GLU
C3060
16.807
−5.410
0.901
1.00
37.10
C

ATOM
2281
OE1
GLU
C3060
16.401
−6.359
0.190
1.00
38.38
O

ATOM
2282
OE2
GLU
C3060
17.509
−4.472
0.456
1.00
38.70
O

ATOM
2283
C
GLU
C3060
19.042
−6.172
3.864
1.00
20.94
C

ATOM
2284
O
GLU
C3060
19.829
−5.429
3.285
1.00
22.93
O

ATOM
2285
N
ALA
C3061
18.907
−6.178
5.186
1.00
19.68
N

ATOM
2286
CA
ALA
C3061
19.698
−5.282
6.024
1.00
20.17
C

ATOM
2287
CB
ALA
C3061
19.373
−5.515
7.499
1.00
19.49
C

ATOM
2288
C
ALA
C3061
21.185
−5.520
5.759
1.00
19.14
C

ATOM
2289
O
ALA
C3061
21.953
−4.576
5.572
1.00
18.81
O

ATOM
2290
N
PHE
C3062
21.588
−6.786
5.723
1.00
19.90
N

ATOM
2291
CA
PHE
C3062
22.987
−7.115
5.465
1.00
19.78
C

ATOM
2292
CB
PHE
C3062
23.214
−8.624
5.570
1.00
20.80
C

ATOM
2293
CG
PHE
C3062
24.604
−9.051
5.171
1.00
21.17
C

ATOM
2294
CD1
PHE
C3062
24.896
−9.376
3.847
1.00
21.25
C

ATOM
2295
CD2
PHE
C3062
25.629
−9.074
6.109
1.00
20.45
C

ATOM
2296
CE1
PHE
C3062
26.195
−9.717
3.463
1.00
22.31
C

ATOM
2297
CE2
PHE
C3062
26.930
−9.412
5.738
1.00
21.98
C

ATOM
2298
CZ
PHE
C3062
27.211
−9.733
4.410
1.00
22.06
C

ATOM
2299
C
PHE
C3062
23.443
−6.629
4.089
1.00
21.35
C

ATOM
2300
O
PHE
C3062
24.526
−6.067
3.951
1.00
20.77
O

ATOM
2301
N
SER
C3063
22.612
−6.843
3.074
1.00
22.17
N

ATOM
2302
CA
SER
C3063
22.949
−6.434
1.717
1.00
22.74
C

ATOM
2303
CB
SER
C3063
21.851
−6.873
0.754
1.00
23.43
C

ATOM
2304
OG
SER
C3063
21.635
−8.265
0.877
1.00
28.48
O

ATOM
2305
C
SER
C3063
23.123
−4.926
1.649
1.00
22.84
C

ATOM
2306
O
SER
C3063
24.001
−4.422
0.947
1.00
21.58
O

ATOM
2307
N
LYS
C3064
22.277
−4.205
2.377
1.00
21.35
N

ATOM
2308
CA
LYS
C3064
22.370
−2.755
2.406
1.00
21.55
C

ATOM
2309
CB
LYS
C3064
21.111
−2.168
3.055
1.00
22.13
C

ATOM
2310
CG
LYS
C3064
19.841
−2.416
2.238
1.00
21.86
C

ATOM
2311
CD
LYS
C3064
18.588
−1.884
2.929
1.00
22.40
C

ATOM
2312
CE
LYS
C3064
18.653
−0.375
3.120
1.00
22.07
C

ATOM
2313
NZ
LYS
C3064
17.579
0.125
4.017
1.00
21.49
N

ATOM
2314
C
LYS
C3064
23.639
−2.341
3.168
1.00
21.95
C

ATOM
2315
O
LYS
C3064
24.295
−1.363
2.812
1.00
22.05
O

ATOM
2316
N
ALA
C3065
23.994
−3.104
4.197
1.00
20.93
N

ATOM
2317
CA
ALA
C3065
25.193
−2.818
4.983
1.00
23.70
C

ATOM
2318
CB
ALA
C3065
25.254
−3.729
6.200
1.00
22.08
C

ATOM
2319
C
ALA
C3065
26.450
−3.010
4.136
1.00
25.75
C

ATOM
2320
O
ALA
C3065
27.420
−2.278
4.297
1.00
25.29
O

ATOM
2321
N
MET
C3066
26.433
−4.008
3.255
1.00
27.80
N

ATOM
2322
CA
MET
C3066
27.569
−4.278
2.375
1.00
31.06
C

ATOM
2323
CB
MET
C3066
27.386
−5.616
1.649
1.00
30.03
C

ATOM
2324
CG
MET
C3066
27.666
−6.848
2.495
1.00
30.77
C

ATOM
2325
SD
MET
C3066
29.395
−6.944
3.059
1.00
31.09
S

ATOM
2326
CE
MET
C3066
30.192
−7.610
1.576
1.00
29.01
C

ATOM
2327
C
MET
C3066
27.683
−3.159
1.342
1.00
33.44
C

ATOM
2328
O
MET
C3066
28.778
−2.782
0.940
1.00
32.94
O

ATOM
2329
N
GLY
C3067
26.539
−2.634
0.918
1.00
36.57
N

ATOM
2330
CA
GLY
C3067
26.542
−1.565
−0.059
1.00
40.47
C

ATOM
2331
C
GLY
C3067
26.101
−2.041
−1.426
1.00
43.36
C

ATOM
2332
O
GLY
C3067
26.602
−1.573
−2.447
1.00
44.87
O

ATOM
2333
N
THR
C3068
25.161
−2.976
−1.447
0.05
44.27
N

ATOM
2334
CA
THR
C3068
24.650
−3.506
−2.701
0.05
45.40
C

ATOM
2335
CB
THR
C3068
25.521
−4.680
−3.201
0.05
45.40
C

ATOM
2336
OG1
THR
C3068
25.018
−5.147
−4.459
0.05
45.48
O

ATOM
2337
CG2
THR
C3068
25.518
−5.821
−2.193
0.05
45.43
C

ATOM
2338
C
THR
C3068
23.212
−3.973
−2.507
0.05
46.15
C

ATOM
2339
O
THR
C3068
22.452
−3.355
−1.761
0.05
46.24
O

ATOM
2340
N
GLY
C3069
22.839
−5.058
−3.175
0.05
47.05
N

ATOM
2341
CA
GLY
C3069
21.488
−5.567
−3.043
0.05
48.19
C

ATOM
2342
C
GLY
C3069
21.341
−6.984
−3.555
0.05
48.95
C

ATOM
2343
O
GLY
C3069
22.322
−7.627
−3.927
0.05
49.00
O

ATOM
2344
N
ILE
C3070
20.106
−7.471
−3.569
0.05
49.77
N

ATOM
2345
CA
ILE
C3070
19.809
−8.817
−4.038
0.05
50.58
C

ATOM
2346
CB
ILE
C3070
18.311
−9.155
−3.800
0.05
50.80
C

ATOM
2347
CG2
ILE
C3070
17.434
−8.193
−4.584
0.05
51.01
C

ATOM
2348
CG1
ILE
C3070
18.011
−10.600
−4.205
0.05
51.05
C

ATOM
2349
CD1
ILE
C3070
18.852
−11.631
−3.486
0.05
51.19
C

ATOM
2350
C
ILE
C3070
20.140
−8.927
−5.528
0.05
50.91
C

ATOM
2351
O
ILE
C3070
20.642
−7.977
−6.126
0.05
50.98
O

ATOM
2352
N
SER
C3071
19.868
−10.093
−6.108
0.05
51.31
N

ATOM
2353
CA
SER
C3071
20.112
−10.372
−7.522
0.05
51.63
C

ATOM
2354
CB
SER
C3071
19.393
−9.349
−8.411
0.05
51.73
C

ATOM
2355
OG
SER
C3071
20.018
−8.080
−8.363
0.05
51.85
O

ATOM
2356
C
SER
C3071
21.592
−10.420
−7.891
0.05
51.76
C

ATOM
2357
O
SER
C3071
21.967
−11.053
−8.878
0.05
51.87
O

ATOM
2358
N
LYS
C3072
22.433
−9.755
−7.106
0.05
51.86
N

ATOM
2359
CA
LYS
C3072
23.867
−9.751
−7.374
0.05
51.85
C

ATOM
2360
CB
LYS
C3072
24.396
−8.312
−7.449
0.05
52.23
C

ATOM
2361
CG
LYS
C3072
24.392
−7.543
−6.131
0.05
52.70
C

ATOM
2362
CD
LYS
C3072
25.580
−7.907
−5.245
0.05
53.07
C

ATOM
2363
CE
LYS
C3072
26.905
−7.581
−5.920
0.05
53.33
C

ATOM
2364
NZ
LYS
C3072
27.022
−6.134
−6.253
0.05
53.48
N

ATOM
2365
C
LYS
C3072
24.606
−10.529
−6.292
0.05
51.55
C

ATOM
2366
O
LYS
C3072
25.643
−11.140
−6.550
0.05
51.64
O

ATOM
2367
N
LEU
C3073
24.062
−10.500
−5.080
0.05
51.11
N

ATOM
2368
CA
LEU
C3073
24.660
−11.204
−3.953
0.05
50.57
C

ATOM
2369
CB
LEU
C3073
24.615
−10.328
−2.699
0.05
50.79
C

ATOM
2370
CG
LEU
C3073
25.349
−10.863
−1.467
0.05
50.92
C

ATOM
2371
CD1
LEU
C3073
26.830
−11.010
−1.783
0.05
51.03
C

ATOM
2372
CD2
LEU
C3073
25.145
−9.917
−0.294
0.05
50.94
C

ATOM
2373
C
LEU
C3073
23.893
−12.498
−3.707
0.05
50.00
C

ATOM
2374
O
LEU
C3073
24.444
−13.473
−3.198
0.05
50.02
O

ATOM
2375
N
GLY
C3074
22.616
−12.492
−4.076
1.00
49.38
N

ATOM
2376
CA
GLY
C3074
21.779
−13.663
−3.899
1.00
48.02
C

ATOM
2377
C
GLY
C3074
21.479
−13.986
−2.447
1.00
46.92
C

ATOM
2378
O
GLY
C3074
22.391
−14.150
−1.642
1.00
46.73
O

ATOM
2379
N
PHE
C3075
20.197
−14.076
−2.107
1.00
46.04
N

ATOM
2380
CA
PHE
C3075
19.804
−14.393
−0.741
1.00
45.56
C

ATOM
2381
CB
PHE
C3075
18.305
−14.137
−0.544
1.00
45.22
C

ATOM
2382
CG
PHE
C3075
17.969
−12.705
−0.211
1.00
44.58
C

ATOM
2383
CD1
PHE
C3075
18.961
−11.724
−0.187
1.00
44.91
C

ATOM
2384
CD2
PHE
C3075
16.661
−12.337
0.082
1.00
43.89
C

ATOM
2385
CE1
PHE
C3075
18.654
−10.397
0.127
1.00
45.66
C

ATOM
2386
CE2
PHE
C3075
16.340
−11.016
0.398
1.00
44.22
C

ATOM
2387
CZ
PHE
C3075
17.338
−10.042
0.420
1.00
44.74
C

ATOM
2388
C
PHE
C3075
20.147
−15.841
−0.407
1.00
45.42
C

ATOM
2389
O
PHE
C3075
20.099
−16.251
0.754
1.00
44.99
O

ATOM
2390
N
GLN
C3076
20.503
−16.607
−1.433
1.00
44.83
N

ATOM
2391
CA
GLN
C3076
20.874
−18.006
−1.256
1.00
44.38
C

ATOM
2392
CB
GLN
C3076
20.766
−18.749
−2.589
1.00
44.21
C

ATOM
2393
CG
GLN
C3076
19.360
−19.192
−2.890
1.00
45.02
C

ATOM
2394
CD
GLN
C3076
18.868
−20.206
−1.880
1.00
46.01
C

ATOM
2395
OE1
GLN
C3076
17.666
−20.367
−1.676
1.00
47.94
O

ATOM
2396
NE2
GLN
C3076
19.802
−20.906
−1.245
1.00
45.65
N

ATOM
2397
C
GLN
C3076
22.287
−18.133
−0.706
1.00
43.75
C

ATOM
2398
O
GLN
C3076
22.660
−19.165
−0.149
1.00
44.83
O

ATOM
2399
N
ASP
C3077
23.070
−17.074
−0.862
1.00
43.01
N

ATOM
2400
CA
ASP
C3077
24.442
−17.065
−0.377
1.00
41.11
C

ATOM
2401
CB
ASP
C3077
25.315
−16.254
−1.333
1.00
44.24
C

ATOM
2402
CG
ASP
C3077
25.261
−16.789
−2.756
1.00
45.88
C

ATOM
2403
OD1
ASP
C3077
25.692
−17.943
−2.974
1.00
47.04
O

ATOM
2404
OD2
ASP
C3077
24.777
−16.064
−3.652
1.00
46.86
O

ATOM
2405
C
ASP
C3077
24.493
−16.481
1.028
1.00
38.51
C

ATOM
2406
O
ASP
C3077
25.564
−16.291
1.598
1.00
39.35
O

ATOM
2407
N
LEU
C3078
23.319
−16.194
1.578
1.00
35.03
N

ATOM
2408
CA
LEU
C3078
23.199
−15.649
2.927
1.00
31.01
C

ATOM
2409
CB
LEU
C3078
22.479
−14.296
2.889
1.00
30.66
C

ATOM
2410
CG
LEU
C3078
23.280
−13.026
2.584
1.00
31.31
C

ATOM
2411
CD1
LEU
C3078
24.253
−13.251
1.440
1.00
33.52
C

ATOM
2412
CD2
LEU
C3078
22.303
−11.900
2.254
1.00
30.14
C

ATOM
2413
C
LEU
C3078
22.396
−16.632
3.778
1.00
28.65
C

ATOM
2414
O
LEU
C3078
21.391
−17.178
3.322
1.00
28.16
O

ATOM
2415
N
GLU
C3079
22.839
−16.860
5.009
1.00
25.38
N

ATOM
2416
CA
GLU
C3079
22.138
−17.779
5.895
1.00
24.35
C

ATOM
2417
CB
GLU
C3079
22.794
−19.163
5.869
1.00
24.49
C

ATOM
2418
CG
GLU
C3079
21.999
−20.224
6.616
1.00
24.73
C

ATOM
2419
CD
GLU
C3079
22.653
−21.592
6.558
1.00
26.90
C

ATOM
2420
OE1
GLU
C3079
23.770
−21.740
7.089
1.00
28.68
O

ATOM
2421
OE2
GLU
C3079
22.053
−22.523
5.979
1.00
29.27
O

ATOM
2422
C
GLU
C3079
22.098
−17.267
7.327
1.00
22.68
C

ATOM
2423
O
GLU
C3079
23.123
−16.873
7.883
1.00
22.88
O

ATOM
2424
N
VAL
C3080
20.901
−17.275
7.907
1.00
21.79
N

ATOM
2425
CA
VAL
C3080
20.678
−16.824
9.276
1.00
21.18
C

ATOM
2426
CB
VAL
C3080
19.705
−15.621
9.325
1.00
22.20
C

ATOM
2427
CG1
VAL
C3080
19.404
−15.244
10.777
1.00
20.66
C

ATOM
2428
CG2
VAL
C3080
20.311
−14.435
8.587
1.00
23.11
C

ATOM
2429
C
VAL
C3080
20.064
−17.971
10.060
1.00
20.45
C

ATOM
2430
O
VAL
C3080
18.972
−18.429
9.743
1.00
19.50
O

ATOM
2431
N
LEU
C3081
20.781
−18.441
11.072
1.00
20.00
N

ATOM
2432
CA
LEU
C3081
20.303
−19.540
11.897
1.00
21.15
C

ATOM
2433
CB
LEU
C3081
21.328
−20.686
11.905
1.00
21.34
C

ATOM
2434
CG
LEU
C3081
21.677
−21.275
10.528
1.00
22.27
C

ATOM
2435
CD1
LEU
C3081
22.713
−22.396
10.653
1.00
23.04
C

ATOM
2436
CD2
LEU
C3081
20.400
−21.802
9.884
1.00
24.47
C

ATOM
2437
C
LEU
C3081
20.107
−19.003
13.300
1.00
21.01
C

ATOM
2438
O
LEU
C3081
20.287
−17.811
13.541
1.00
20.54
O

ATOM
2439
N
ASN
C3082
19.732
−19.881
14.220
1.00
21.50
N

ATOM
2440
CA
ASN
C3082
19.530
−19.494
15.608
1.00
22.77
C

ATOM
2441
CB
ASN
C3082
18.089
−19.783
16.020
1.00
23.53
C

ATOM
2442
CG
ASN
C3082
17.099
−18.880
15.310
1.00
25.44
C

ATOM
2443
OD1
ASN
C3082
16.907
−17.731
15.698
1.00
25.60
O

ATOM
2444
ND2
ASN
C3082
16.488
−19.388
14.247
1.00
27.37
N

ATOM
2445
C
ASN
C3082
20.499
−20.258
16.499
1.00
22.68
C

ATOM
2446
O
ASN
C3082
20.629
−21.478
16.380
1.00
21.84
O

ATOM
2447
N
ASN
C3083
21.191
−19.541
17.382
1.00
23.99
N

ATOM
2448
CA
ASN
C3083
22.137
−20.187
18.282
1.00
23.34
C

ATOM
2449
CB
ASN
C3083
23.141
−19.170
18.840
1.00
24.83
C

ATOM
2450
CG
ASN
C3083
22.474
−18.019
19.575
1.00
25.31
C

ATOM
2451
OD1
ASN
C3083
21.405
−18.175
20.174
1.00
23.71
O

ATOM
2452
ND2
ASN
C3083
23.116
−16.859
19.550
1.00
26.83
N

ATOM
2453
C
ASN
C3083
21.381
−20.877
19.415
1.00
25.05
C

ATOM
2454
O
ASN
C3083
20.152
−20.876
19.432
1.00
22.22
O

ATOM
2455
N
GLU
C3084
22.108
−21.460
20.365
1.00
27.04
N

ATOM
2456
CA
GLU
C3084
21.472
−22.174
21.466
1.00
29.78
C

ATOM
2457
CB
GLU
C3084
22.517
−22.954
22.275
1.00
32.58
C

ATOM
2458
CG
GLU
C3084
23.715
−22.141
22.711
1.00
36.99
C

ATOM
2459
CD
GLU
C3084
24.857
−22.184
21.707
1.00
41.57
C

ATOM
2460
OE1
GLU
C3084
24.647
−21.812
20.529
1.00
42.03
O

ATOM
2461
OE2
GLU
C3084
25.972
−22.590
22.107
1.00
43.80
O

ATOM
2462
C
GLU
C3084
20.638
−21.294
22.396
1.00
30.13
C

ATOM
2463
O
GLU
C3084
19.766
−21.796
23.111
1.00
30.37
O

ATOM
2464
N
ARG
C3085
20.901
−19.991
22.401
1.00
28.98
N

ATOM
2465
CA
ARG
C3085
20.119
−19.088
23.238
1.00
30.28
C

ATOM
2466
CB
ARG
C3085
20.976
−17.912
23.716
1.00
31.17
C

ATOM
2467
CG
ARG
C3085
22.055
−18.340
24.705
1.00
34.80
C

ATOM
2468
CD
ARG
C3085
23.056
−17.237
24.995
1.00
37.35
C

ATOM
2469
NE
ARG
C3085
24.367
−17.801
25.310
1.00
40.35
N

ATOM
2470
CZ
ARG
C3085
24.634
−18.518
26.396
1.00
40.77
C

ATOM
2471
NH1
ARG
C3085
23.681
−18.757
27.285
1.00
42.29
N

ATOM
2472
NH2
ARG
C3085
25.852
−19.007
26.587
1.00
41.71
N

ATOM
2473
C
ARG
C3085
18.918
−18.597
22.438
1.00
29.32
C

ATOM
2474
O
ARG
C3085
18.112
−17.806
22.923
1.00
30.16
O

ATOM
2475
N
GLY
C3086
18.805
−19.086
21.207
1.00
27.92
N

ATOM
2476
CA
GLY
C3086
17.690
−18.714
20.350
1.00
26.11
C

ATOM
2477
C
GLY
C3086
17.893
−17.452
19.530
1.00
25.66
C

ATOM
2478
O
GLY
C3086
17.005
−17.044
18.782
1.00
26.33
O

ATOM
2479
N
ALA
C3087
19.061
−16.831
19.654
1.00
23.88
N

ATOM
2480
CA
ALA
C3087
19.328
−15.613
18.914
1.00
22.63
C

ATOM
2481
CB
ALA
C3087
20.408
−14.797
19.610
1.00
21.67
C

ATOM
2482
C
ALA
C3087
19.742
−15.893
17.478
1.00
22.49
C

ATOM
2483
O
ALA
C3087
20.515
−16.808
17.210
1.00
22.63
O

ATOM
2484
N
PRO
C3088
19.220
−15.098
16.532
1.00
21.73
N

ATOM
2485
CD
PRO
03088
18.185
−14.068
16.740
1.00
21.19
C

ATOM
2486
CA
PRO
C3088
19.536
−15.244
15.112
1.00
20.08
C

ATOM
2487
CB
PRO
C3088
18.434
−14.435
14.435
1.00
22.01
C

ATOM
2488
CG
PRO
C3088
18.196
−13.325
15.412
1.00
23.33
C

ATOM
2489
C
PRO
C3088
20.931
−14.689
14.822
1.00
20.77
C

ATOM
2490
O
PRO
C3088
21.360
−13.704
15.434
1.00
19.53
O

ATOM
2491
N
TYR
C3089
21.647
−15.327
13.903
1.00
18.65
N

ATOM
2492
CA
TYR
C3089
22.986
−14.869
13.548
1.00
18.94
C

ATOM
2493
CB
TYR
C3089
24.015
−15.410
14.557
1.00
19.72
C

ATOM
2494
CG
TYR
C3089
24.295
−16.891
14.434
1.00
20.97
C

ATOM
2495
CD1
TYR
C3089
25.313
−17.360
13.600
1.00
21.58
C

ATOM
2496
CE1
TYR
C3089
25.549
−18.721
13.448
1.00
21.20
C

ATOM
2497
CD2
TYR
C3089
23.521
−17.826
15.118
1.00
21.44
C

ATOM
2498
CE2
TYR
C3089
23.748
−19.193
14.974
1.00
21.49
C

ATOM
2499
CZ
TYR
C3089
24.764
−19.630
14.133
1.00
20.90
C

ATOM
2500
OH
TYR
C3089
24.980
−20.972
13.961
1.00
21.13
O

ATOM
2501
C
TYR
C3089
23.310
−15.356
12.142
1.00
19.33
C

ATOM
2502
O
TYR
C3089
22.695
−16.305
11.658
1.00
18.04
O

ATOM
2503
N
PHE
C3090
24.252
−14.694
11.476
1.00
21.68
N

ATOM
2504
CA
PHE
C3090
24.644
−15.095
10.129
1.00
22.43
C

ATOM
2505
CB
PHE
C3090
25.224
−13.921
9.343
1.00
21.81
C

ATOM
2506
CG
PHE
C3090
24.187
−13.057
8.686
1.00
22.97
C

ATOM
2507
CD1
PHE
C3090
23.627
−11.980
9.364
1.00
22.58
C

ATOM
2508
CD2
PHE
C3090
23.774
−13.317
7.382
1.00
22.20
C

ATOM
2509
CE1
PHE
C3090
22.670
−11.172
8.752
1.00
21.60
C

ATOM
2510
CE2
PHE
C3090
22.815
−12.512
6.762
1.00
21.04
C

ATOM
2511
CZ
PHE
C3090
22.267
−11.439
7.453
1.00
20.05
C

ATOM
2512
C
PHE
C3090
25.681
−16.201
10.185
1.00
23.74
C

ATOM
2513
O
PHE
C3090
26.804
−15.992
10.642
1.00
23.80
O

ATOM
2514
N
SER
C3091
25.291
−17.381
9.727
1.00
25.13
N

ATOM
2515
CA
SER
C3091
26.186
−18.522
9.707
1.00
24.76
C

ATOM
2516
CB
SER
C3091
25.378
−19.805
9.790
1.00
25.31
C

ATOM
2517
OG
SER
C3091
24.465
−19.856
8.709
1.00
25.46
O

ATOM
2518
C
SER
C3091
26.959
−18.493
8.393
1.00
25.15
C

ATOM
2519
O
SER
C3091
28.036
−19.075
8.285
1.00
24.95
O

ATOM
2520
N
GLN
C3092
26.398
−17.806
7.401
1.00
25.28
N

ATOM
2521
CA
GLN
C3092
27.012
−17.701
6.079
1.00
26.50
C

ATOM
2522
CB
GLN
C3092
26.414
−18.759
5.150
1.00
29.33
C

ATOM
2523
CG
GLN
C3092
26.948
−18.723
3.728
1.00
33.15
C

ATOM
2524
CD
GLN
C3092
28.353
−19.271
3.638
1.00
35.44
C

ATOM
2525
OE1
GLN
C3092
29.292
−18.711
4.204
1.00
36.58
O

ATOM
2526
NE2
GLN
C3092
28.503
−20.384
2.935
1.00
37.04
N

ATOM
2527
C
GLN
C3092
26.780
−16.323
5.465
1.00
25.49
C

ATOM
2528
O
GLN
C3092
25.637
−15.871
5.365
1.00
24.76
O

ATOM
2529
N
ALA
C3093
27.864
−15.674
5.042
1.00
24.56
N

ATOM
2530
CA
ALA
C3093
27.801
−14.350
4.422
1.00
24.82
C

ATOM
2531
CB
ALA
C3093
27.400
−13.302
5.451
1.00
24.36
C

ATOM
2532
C
ALA
C3093
29.152
−13.978
3.808
1.00
24.47
C

ATOM
2533
O
ALA
C3093
30.200
−14.284
4.365
1.00
24.58
O

ATOM
2534
N
PRO
C3094
29.137
−13.289
2.654
1.00
25.93
N

ATOM
2535
CD
PRO
C3094
27.920
−12.815
1.965
1.00
24.23
C

ATOM
2536
CA
PRO
C3094
30.345
−12.860
1.935
1.00
25.56
C

ATOM
2537
CB
PRO
C3094
29.788
−12.404
0.592
1.00
26.20
C

ATOM
2538
CG
PRO
C3094
28.472
−11.792
0.997
1.00
26.19
C

ATOM
2539
C
PRO
C3094
31.098
−11.744
2.658
1.00
26.12
C

ATOM
2540
O
PRO
C3094
31.403
−10.703
2.077
1.00
25.63
O

ATOM
2541
N
PHE
C3095
31.404
−11.971
3.930
1.00
26.90
N

ATOM
2542
CA
PHE
C3095
32.098
−10.977
4.739
1.00
26.88
C

ATOM
2543
CB
PHE
C3095
31.068
−10.004
5.331
1.00
26.61
C

ATOM
2544
CG
PHE
C3095
31.665
−8.923
6.179
1.00
26.50
C

ATOM
2545
CD1
PHE
C3095
31.491
−8.931
7.559
1.00
25.34
C

ATOM
2546
CD2
PHE
C3095
32.406
−7.895
5.601
1.00
26.22
C

ATOM
2547
CE1
PHE
C3095
32.043
−7.937
8.350
1.00
24.07
C

ATOM
2548
CE2
PHE
C3095
32.964
−6.895
6.384
1.00
25.18
C

ATOM
2549
CZ
PHE
C3095
32.781
−6.917
7.764
1.00
26.71
C

ATOM
2550
C
PHE
C3095
32.830
−11.726
5.841
1.00
27.07
C

ATOM
2551
O
PHE
C3095
32.234
−12.547
6.527
1.00
28.82
O

ATOM
2552
N
SER
C3096
34.119
−11.450
6.013
1.00
27.08
N

ATOM
2553
CA
SER
C3096
34.907
−12.153
7.022
1.00
26.87
C

ATOM
2554
CB
SER
C3096
36.287
−12.488
6.457
1.00
27.85
C

ATOM
2555
OG
SER
C3096
36.967
−11.315
6.073
1.00
29.01
O

ATOM
2556
C
SER
C3096
35.072
−11.446
8.364
1.00
27.60
C

ATOM
2557
O
SER
C3096
35.753
−11.957
9.251
1.00
28.27
O

ATOM
2558
N
GLY
C3097
34.466
−10.271
8.513
1.00
26.02
N

ATOM
2559
CA
GLY
C3097
34.559
−9.558
9.775
1.00
25.74
C

ATOM
2560
C
GLY
C3097
33.406
−9.991
10.664
1.00
26.75
C

ATOM
2561
O
GLY
C3097
32.796
−11.029
10.422
1.00
26.07
O

ATOM
2562
N
LYS
C3098
33.084
−9.202
11.682
1.00
25.99
N

ATOM
2563
CA
LYS
C3098
31.985
−9.559
12.572
1.00
26.80
C

ATOM
2564
CB
LYS
C3098
32.302
−9.106
13.998
1.00
28.83
C

ATOM
2565
CG
LYS
C3098
33.742
−9.410
14.383
1.00
33.82
C

ATOM
2566
CD
LYS
C3098
34.014
−9.227
15.860
1.00
37.34
C

ATOM
2567
CE
LYS
C3098
33.574
−10.444
16.652
1.00
39.78
C

ATOM
2568
NZ
LYS
C3098
33.986
−10.326
18.084
1.00
40.81
N

ATOM
2569
C
LYS
C3098
30.676
−8.944
12.095
1.00
25.06
C

ATOM
2570
O
LYS
C3098
30.633
−7.785
11.670
1.00
24.85
O

ATOM
2571
N
ILE
C3099
29.611
−9.737
12.152
1.00
22.88
N

ATOM
2572
CA
ILE
C3099
28.292
−9.286
11.730
1.00
20.01
C

ATOM
2573
CB
ILE
C3099
27.688
−10.246
10.687
1.00
19.89
C

ATOM
2574
CG2
ILE
C3099
26.373
−9.674
10.150
1.00
15.87
C

ATOM
2575
CG1
ILE
C3099
28.686
−10.474
9.548
1.00
18.98
C

ATOM
2576
CD1
ILE
C3099
28.241
−11.543
8.561
1.00
19.71
C

ATOM
2577
C
ILE
C3099
27.364
−9.243
12.941
1.00
20.05
C

ATOM
2578
O
ILE
C3099
26.967
−10.289
13.459
1.00
21.97
O

ATOM
2579
N
TRP
C3100
27.032
−8.038
13.398
1.00
18.21
N

ATOM
2580
CA
TRP
C3100
26.140
−7.880
14.541
1.00
17.20
C

ATOM
2581
CB
TRP
C3100
26.570
−6.678
15.383
1.00
17.48
C

ATOM
2582
CG
TRP
C3100
27.959
−6.851
15.948
1.00
17.00
C

ATOM
2583
CD2
TRP
C3100
28.323
−7.642
17.085
1.00
16.80
C

ATOM
2584
CE2
TRP
C3100
29.724
−7.538
17.237
1.00
18.05
C

ATOM
2585
CE3
TRP
C3100
27.599
−8.431
17.992
1.00
19.31
C

ATOM
2586
CD1
TRP
C3100
29.119
−6.316
15.465
1.00
17.86
C

ATOM
2587
NE1
TRP
C3100
30.188
−6.724
16.236
1.00
18.87
N

ATOM
2588
CZ2
TRP
C3100
30.417
−8.192
18.263
1.00
19.19
C

ATOM
2589
CZ3
TRP
C3100
28.290
−9.082
19.012
1.00
19.20
C

ATOM
2590
CH2
TRP
C3100
29.687
−8.955
19.136
1.00
17.94
C

ATOM
2591
C
TRP
C3100
24.717
−7.699
14.018
1.00
17.56
C

ATOM
2592
O
TRP
C3100
24.365
−6.656
13.461
1.00
18.14
O

ATOM
2593
N
LEU
C3101
23.916
−8.742
14.191
1.00
17.00
N

ATOM
2594
CA
LEU
C3101
22.540
−8.764
13.725
1.00
16.11
C

ATOM
2595
CB
LEU
C3101
22.321
−9.991
12.837
1.00
16.56
C

ATOM
2596
CG
LEU
C3101
20.875
−10.417
12.559
1.00
16.77
C

ATOM
2597
CD1
LEU
C3101
20.194
−9.413
11.625
1.00
15.60
C

ATOM
2598
CD2
LEU
C3101
20.883
−11.809
11.939
1.00
18.41
C

ATOM
2599
C
LEU
C3101
21.525
−8.811
14.852
1.00
16.81
C

ATOM
2600
O
LEU
C3101
21.746
−9.435
15.890
1.00
14.02
O

ATOM
2601
N
SER
C3102
20.410
−8.128
14.638
1.00
15.53
N

ATOM
2602
CA
SER
C3102
19.316
−8.151
15.588
1.00
14.91
C

ATOM
2603
CB
SER
C3102
19.424
−7.035
16.619
1.00
14.40
C

ATOM
2604
OG
SER
C3102
18.483
−7.263
17.657
1.00
15.41
O

ATOM
2605
C
SER
C3102
18.052
−7.981
14.761
1.00
14.92
C

ATOM
2606
O
SER
C3102
18.020
−7.195
13.805
1.00
14.51
O

ATOM
2607
N
ILE
C3103
17.023
−8.734
15.129
1.00
14.41
N

ATOM
2608
CA
ILE
C3103
15.744
−8.710
14.437
1.00
15.86
C

ATOM
2609
CB
ILE
C3103
15.490
−10.043
13.668
1.00
16.91
C

ATOM
2610
CG2
ILE
C3103
14.171
−9.958
12.880
1.00
18.33
C

ATOM
2611
CG1
ILE
C3103
16.665
−10.353
12.737
1.00
18.54
C

ATOM
2612
CD1
ILE
C3103
16.557
−11.729
12.042
1.00
20.00
C

ATOM
2613
C
ILE
C3103
14.657
−8.608
15.495
1.00
17.43
C

ATOM
2614
O
ILE
C3103
14.805
−9.148
16.594
1.00
17.45
O

ATOM
2615
N
SER
C3104
13.566
−7.929
15.157
1.00
18.17
N

ATOM
2616
CA
SER
C3104
12.439
−7.798
16.070
1.00
20.57
C

ATOM
2617
CB
SER
C3104
12.610
−6.583
16.986
1.00
19.79
C

ATOM
2618
OG
SER
C3104
11.596
−6.571
17.981
1.00
23.17
O

ATOM
2619
C
SER
C3104
11.188
−7.645
15.214
1.00
22.21
C

ATOM
2620
O
SER
C3104
11.269
−7.301
14.033
1.00
22.47
O

ATOM
2621
N
HIS
C3105
10.028
−7.889
15.796
1.00
23.30
N

ATOM
2622
CA
HIS
C3105
8.818
−7.784
15.009
1.00
25.44
C

ATOM
2623
CB
HIS
C3105
8.597
−9.083
14.241
1.00
27.72
C

ATOM
2624
CG
HIS
C3105
8.509
−10.287
15.125
1.00
29.50
C

ATOM
2625
CD2
HIS
C3105
7.438
−10.938
15.639
1.00
33.02
C

ATOM
2626
ND1
HIS
C3105
9.622
−10.934
15.615
1.00
32.99
N

ATOM
2627
CE1
HIS
C3105
9.242
−11.933
16.393
1.00
34.27
C

ATOM
2628
NE2
HIS
C3105
7.922
−11.956
16.424
1.00
33.98
N

ATOM
2629
C
HIS
C3105
7.565
−7.489
15.805
1.00
26.04
C

ATOM
2630
O
HIS
C3105
7.499
−7.729
17.009
1.00
23.14
O

ATOM
2631
N
THR
C3106
6.575
−6.972
15.086
1.00
28.54
N

ATOM
2632
CA
THR
C3106
5.261
−6.652
15.613
1.00
30.04
C

ATOM
2633
CB
THR
C3106
4.855
−5.209
15.300
1.00
31.60
C

ATOM
2634
OG1
THR
C3106
4.804
−5.030
13.878
1.00
31.75
O

ATOM
2635
CG2
THR
C3106
5.848
−4.231
15.905
1.00
30.63
C

ATOM
2636
C
THR
C3106
4.332
−7.576
14.840
1.00
30.05
C

ATOM
2637
O
THR
C3106
4.792
−8.451
14.101
1.00
31.00
O

ATOM
2638
N
ASP
C3107
3.031
−7.374
14.987
1.00
31.29
N

ATOM
2639
CA
ASP
C3107
2.056
−8.206
14.296
1.00
32.30
C

ATOM
2640
CB
ASP
C3107
0.674
−8.033
14.934
1.00
36.82
C

ATOM
2641
CG
ASP
C3107
0.596
−8.612
16.327
1.00
40.78
C

ATOM
2642
OD1
ASP
C3107
−0.205
−8.097
17.136
1.00
44.76
O

ATOM
2643
OD2
ASP
C3107
1.319
−9.591
16.612
1.00
44.36
O

ATOM
2644
C
ASP
C3107
1.959
−7.890
12.807
1.00
31.24
C

ATOM
2645
O
ASP
C3107
1.521
−8.729
12.026
1.00
32.84
O

ATOM
2646
N
GLN
C3108
2.374
−6.690
12.410
1.00
28.20
N

ATOM
2647
CA
GLN
C3108
2.284
−6.289
11.009
1.00
27.03
C

ATOM
2648
CB
GLN
C3108
1.590
−4.928
10.877
0.05
26.57
C

ATOM
2649
CG
GLN
C3108
0.284
−4.788
11.626
0.05
26.25
C

ATOM
2650
CD
GLN
C3108
0.486
−4.733
13.121
0.05
26.05
C

ATOM
2651
OE1
GLN
C3108
1.220
−3.887
13.631
0.05
25.96
O

ATOM
2652
NE2
GLN
C3108
−0.165
−5.636
13.834
0.05
25.84
N

ATOM
2653
C
GLN
C3108
3.607
−6.204
10.264
1.00
25.37
C

ATOM
2654
O
GLN
C3108
3.624
−6.210
9.032
1.00
24.85
O

ATOM
2655
N
PHE
C3109
4.716
−6.098
10.987
1.00
24.20
N

ATOM
2656
CA
PHE
C3109
5.996
−5.994
10.299
1.00
23.19
C

ATOM
2657
CB
PHE
C3109
6.210
−4.548
9.827
1.00
24.65
C

ATOM
2658
CG
PHE
C3109
6.268
−3.541
10.947
1.00
26.19
C

ATOM
2659
CD1
PHE
C3109
7.406
−3.421
11.738
1.00
26.36
C

ATOM
2660
CD2
PHE
C3109
5.181
−2.714
11.211
1.00
27.63
C

ATOM
2661
CE1
PHE
C3109
7.464
−2.490
12.780
1.00
26.39
C

ATOM
2662
CE2
PHE
C3109
5.225
−1.780
12.249
1.00
28.63
C

ATOM
2663
CZ
PHE
C3109
6.371
−1.669
13.036
1.00
28.60
C

ATOM
2664
C
PHE
C3109
7.191
−6.459
11.116
1.00
21.14
C

ATOM
2665
O
PHE
C3109
7.100
−6.648
12.328
1.00
19.22
O

ATOM
2666
N
VAL
C3110
8.308
−6.650
10.425
1.00
19.26
N

ATOM
2667
CA
VAL
C3110
9.550
−7.083
11.052
1.00
19.85
C

ATOM
2668
CB
VAL
C3110
10.027
−8.438
10.471
1.00
21.25
C

ATOM
2669
CG1
VAL
C3110
11.360
−8.859
11.101
1.00
23.25
C

ATOM
2670
CG2
VAL
C3110
8.980
−9.488
10.719
1.00
25.17
C

ATOM
2671
C
VAL
C3110
10.604
−6.039
10.737
1.00
19.21
C

ATOM
2672
O
VAL
C3110
10.503
−5.345
9.725
1.00
19.53
O

ATOM
2673
N
THR
C3111
11.603
−5.925
11.608
1.00
19.09
N

ATOM
2674
CA
THR
C3111
12.695
−4.984
11.409
1.00
20.72
C

ATOM
2675
CB
THR
C3111
12.608
−3.765
12.368
1.00
22.75
C

ATOM
2676
OG1
THR
C3111
12.635
−4.216
13.730
1.00
26.03
O

ATOM
2677
CG2
THR
C3111
11.322
−2.976
12.124
1.00
22.96
C

ATOM
2678
C
THR
C3111
13.993
−5.725
11.684
1.00
20.16
C

ATOM
2679
O
THR
C3111
14.024
−6.664
12.481
1.00
20.27
O

ATOM
2680
N
ALA
C3112
15.060
−5.312
11.010
1.00
19.72
N

ATOM
2681
CA
ALA
C3112
16.361
−5.935
11.201
1.00
19.77
C

ATOM
2682
CB
ALA
C3112
16.617
−6.975
10.109
1.00
18.61
C

ATOM
2683
C
ALA
C3112
17.441
−4.868
11.172
1.00
19.41
C

ATOM
2684
O
ALA
C3112
17.337
−3.885
10.442
1.00
22.32
O

ATOM
2685
N
SER
C3113
18.474
−5.062
11.980
1.00
20.21
N

ATOM
2686
CA
SER
C3113
19.579
−4.124
12.045
1.00
18.53
C

ATOM
2687
CB
SER
C3113
19.506
−3.298
13.327
1.00
19.50
C

ATOM
2688
OG
SER
C3113
20.510
−2.293
13.328
1.00
19.90
O

ATOM
2689
C
SER
C3113
20.888
−4.895
12.003
1.00
18.71
C

ATOM
2690
O
SER
C3113
21.084
−5.843
12.767
1.00
16.55
O

ATOM
2691
N
VAL
C3114
21.779
−4.472
11.107
1.00
17.09
N

ATOM
2692
CA
VAL
C3114
23.071
−5.115
10.930
1.00
17.37
C

ATOM
2693
CB
VAL
C3114
23.145
−5.842
9.563
1.00
16.61
C

ATOM
2694
CG1
VAL
C3114
24.593
−6.263
9.255
1.00
18.34
C

ATOM
2695
CG2
VAL
C3114
22.244
−7.050
9.576
1.00
16.94
C

ATOM
2696
C
VAL
C3114
24.216
−4.116
10.993
1.00
16.94
C

ATOM
2697
O
VAL
C3114
24.145
−3.043
10.408
1.00
16.28
O

ATOM
2698
N
ILE
C3115
25.265
−4.477
11.720
1.00
17.86
N

ATOM
2699
CA
ILE
C3115
26.446
−3.632
11.820
1.00
19.21
C

ATOM
2700
CB
ILE
C3115
26.667
−3.085
13.253
1.00
19.71
C

ATOM
2701
CG2
ILE
C3115
27.926
−2.217
13.287
1.00
19.20
C

ATOM
2702
CG1
ILE
C3115
25.451
−2.268
13.703
1.00
19.12
C

ATOM
2703
CD1
ILE
C3115
25.573
−1.701
15.110
1.00
20.38
C

ATOM
2704
C
ILE
C3115
27.627
−4.516
11.440
1.00
18.95
C

ATOM
2705
O
ILE
C3115
27.806
−5.589
12.007
1.00
18.31
O

ATOM
2706
N
LEU
C3116
28.409
−4.076
10.457
1.00
19.22
N

ATOM
2707
CA
LEU
C3116
29.578
−4.830
10.021
1.00
20.77
C

ATOM
2708
CB
LEU
C3116
29.696
−4.805
8.493
1.00
20.70
C

ATOM
2709
CG
LEU
C3116
28.445
−5.235
7.703
1.00
19.25
C

ATOM
2710
CD1
LEU
C3116
28.758
−5.249
6.218
1.00
21.02
C

ATOM
2711
CD2
LEU
C3116
27.996
−6.614
8.150
1.00
19.48
C

ATOM
2712
C
LEU
C3116
30.803
−4.182
10.655
1.00
21.44
C

ATOM
2713
O
LEU
C3116
30.996
−2.969
10.554
1.00
21.12
O

ATOM
2714
N
GLU
C3117
31.620
−4.994
11.314
1.00
23.48
N

ATOM
2715
CA
GLU
C3117
32.812
−4.493
11.987
1.00
26.83
C

ATOM
2716
CB
GLU
C3117
32.571
−4.457
13.504
1.00
27.48
C

ATOM
2717
CG
GLU
C3117
33.817
−4.166
14.343
1.00
30.16
C

ATOM
2718
CD
GLU
C3117
33.628
−4.470
15.826
1.00
29.66
C

ATOM
2719
OE1
GLU
C3117
33.182
−5.595
16.158
1.00
29.18
O

ATOM
2720
OE2
GLU
C3117
33.932
−3.585
16.660
1.00
29.22
O

ATOM
2721
C
GLU
C3117
34.048
−5.335
11.680
1.00
28.97
C

ATOM
2722
O
GLU
C3117
33.978
−6.563
11.578
1.00
27.81
O

ATOM
2723
N
GLU
C3118
35.178
−4.657
11.513
1.00
31.18
N

ATOM
2724
CA
GLU
C3118
36.446
−5.323
11.248
1.00
35.42
C

ATOM
2725
CB
GLU
C3118
37.015
−4.880
9.893
1.00
37.41
C

ATOM
2726
CG
GLU
C3118
36.592
−5.772
8.727
1.00
41.62
C

ATOM
2727
CD
GLU
C3118
37.041
−5.248
7.368
1.00
43.91
C

ATOM
2728
OE1
GLU
C3118
38.193
−4.776
7.253
1.00
46.07
O

ATOM
2729
OE2
GLU
C3118
36.242
−5.321
6.409
1.00
44.10
O

ATOM
2730
C
GLU
C3118
37.414
−4.963
12.369
1.00
35.74
C

ATOM
2731
O
GLU
C3118
37.417
−3.784
12.785
1.00
35.88
O

ATOM
2732
OXT
GLU
C3118
38.154
−5.858
12.821
1.00
38.35
O

TER
2733

GLU
C3118

ATOM
2734
O
HOH
W4002
24.915
17.154
36.149
1.00
24.34
O

ATOM
2735
O
HOH
W4003
1.430
5.412
7.521
1.00
22.65
O

ATOM
2736
O
HOH
W4004
15.230
−11.883
17.512
1.00
29.62
O

ATOM
2737
O
HOH
W4006
20.551
4.946
39.709
1.00
33.21
O

ATOM
2738
O
HOH
W4008
0.497
12.883
37.515
1.00
46.32
O

ATOM
2739
O
HOH
W4009
22.219
1.070
4.722
1.00
20.90
O

ATOM
2740
O
HOH
W4010
23.057
4.216
27.783
1.00
22.10
O

ATOM
2741
O
HOH
W4012
26.158
9.664
6.047
1.00
26.69
O

ATOM
2742
O
HOH
W4013
13.195
−14.652
11.137
1.00
18.24
O

ATOM
2743
O
HOH
W4014
32.126
−19.177
9.562
1.00
41.78
O

ATOM
2744
O
HOH
W4016
11.365
8.055
−2.295
1.00
29.34
O

ATOM
2745
O
HOH
W4017
16.979
7.951
22.041
1.00
23.20
O

ATOM
2746
O
HOH
W4018
20.734
17.150
36.413
1.00
25.86
O

ATOM
2747
O
HOH
W4020
−9.281
−6.387
41.928
1.00
31.95
O

ATOM
2748
O
HOH
W4021
18.869
−12.662
22.632
1.00
30.51
O

ATOM
2749
O
HOH
W4025
18.802
13.286
−2.320
1.00
31.86
O

ATOM
2750
O
HOH
W4026
26.500
16.583
31.811
1.00
52.21
O

ATOM
2751
O
HOH
W4027
6.858
−4.124
3.265
1.00
23.26
O

ATOM
2752
O
HOH
W4028
10.702
1.088
−3.405
1.00
41.81
O

ATOM
2753
O
HOH
W4029
12.811
8.598
27.541
1.00
33.12
O

ATOM
2754
O
HOH
W4031
12.749
−8.445
19.973
1.00
24.85
O

ATOM
2755
O
HOH
W4032
13.535
0.610
2.032
1.00
40.39
O

ATOM
2756
O
HOH
W4033
13.594
8.162
33.675
1.00
30.23
O

ATOM
2757
O
HOH
W4035
10.527
5.028
27.661
1.00
22.20
O

ATOM
2758
O
HOH
W4038
10.071
6.775
24.507
1.00
34.64
O

ATOM
2759
O
HOH
W4039
22.581
2.348
2.717
1.00
30.28
O

ATOM
2760
O
HOH
W4041
34.765
−18.840
6.665
1.00
52.31
O

ATOM
2761
O
HOH
W4042
19.832
10.430
22.362
1.00
30.27
O

ATOM
2762
O
HOH
W4043
25.556
−0.749
36.545
1.00
47.38
O

ATOM
2763
O
HOH
W4044
1.280
−1.711
37.119
1.00
35.25
O

ATOM
2764
O
HOH
W4045
23.055
−3.951
37.102
1.00
29.32
O

ATOM
2765
O
HOH
W4046
10.346
9.220
18.446
1.00
31.53
O

ATOM
2766
O
HOH
W4047
−3.287
0.403
31.271
1.00
53.94
O

ATOM
2767
O
HOH
W4048
4.921
−2.235
2.298
1.00
35.71
O

ATOM
2768
O
HOH
W4050
4.512
−5.663
22.584
1.00
34.27
O

ATOM
2769
O
HOH
W4051
32.165
−16.448
3.541
1.00
29.46
O

ATOM
2770
O
HOH
W4052
17.356
−10.554
17.298
1.00
20.37
O

ATOM
2771
O
HOH
W4053
23.079
8.307
36.567
1.00
27.23
O

ATOM
2772
O
HOH
W4054
22.333
9.961
24.703
1.00
41.93
O

ATOM
2773
O
HOH
W4055
19.848
3.106
3.638
1.00
23.68
O

ATOM
2774
O
HOH
W4056
14.228
9.547
2.164
1.00
13.78
O

ATOM
2775
O
HOH
W4057
−5.992
9.409
37.088
1.00
40.47
O

ATOM
2776
O
HOH
W4058
15.141
2.885
1.432
1.00
32.54
O

ATOM
2777
O
HOH
W4059
27.207
3.715
−0.205
1.00
38.02
O

ATOM
2778
O
HOH
W4060
4.520
8.617
13.683
1.00
29.66
O

ATOM
2779
O
HOH
W4061
−0.534
22.844
0.843
1.00
43.95
O

ATOM
2780
O
HOH
W4062
33.271
0.399
4.561
1.00
41.51
O

ATOM
2781
O
HOH
W4063
10.750
−9.990
18.523
1.00
37.79
O

ATOM
2782
O
HOH
W4065
35.003
2.841
10.072
1.00
34.95
O

ATOM
2783
O
HOH
W4066
15.619
13.987
20.059
1.00
51.87
O

ATOM
2784
O
HOH
W4067
30.322
−16.861
5.985
1.00
25.67
O

ATOM
2785
O
HOH
W4068
−3.928
16.855
6.776
1.00
37.28
O

ATOM
2786
O
HOH
W4069
20.489
9.067
39.451
1.00
48.83
O

ATOM
2787
O
HOH
W4070
38.865
−2.991
24.079
1.00
52.94
O

ATOM
2788
O
HOH
W4071
18.289
12.534
22.275
1.00
32.83
O

ATOM
2789
O
HOH
W4072
16.738
0.024
14.519
1.00
34.01
O

ATOM
2790
O
HOH
W4073
1.959
−19.500
14.371
1.00
40.61
O

ATOM
2791
O
HOH
W4074
1.805
−19.989
7.096
1.00
40.73
O

ATOM
2792
O
HOH
W4075
15.612
10.434
34.742
1.00
32.10
O

ATOM
2793
O
HOH
W4076
13.088
0.232
13.391
1.00
37.71
O

ATOM
2794
O
HOH
W4077
−3.125
13.706
3.280
1.00
34.62
O

ATOM
2795
O
HOH
W4078
2.257
8.002
15.256
1.00
30.49
O

ATOM
2796
O
HOH
W4079
1.805
3.820
14.707
1.00
34.86
O

ATOM
2797
O
HOH
W4080
5.391
−8.908
−2.363
1.00
35.80
O

ATOM
2798
O
HOH
W4081
13.173
18.130
19.444
1.00
42.58
O

ATOM
2799
O
HOH
W4083
3.428
25.760
7.166
1.00
47.46
O

ATOM
2800
O
HOH
W4085
19.600
0.144
14.509
1.00
27.27
O

ATOM
2801
O
HOH
W4086
17.905
−21.379
25.352
1.00
38.73
O

ATOM
2802
O
HOH
W4087
33.360
5.719
22.662
1.00
36.03
O

ATOM
2803
O
HOH
W4089
9.617
−0.859
41.147
1.00
32.45
O

ATOM
2804
O
HOH
W4090
28.109
−16.115
0.982
1.00
29.92
O

ATOM
2805
O
HOH
W4091
38.387
−10.896
9.764
1.00
47.94
O

ATOM
2806
O
HOH
W4092
5.988
24.794
8.424
1.00
43.14
O

ATOM
2807
O
HOH
W4093
−3.277
6.265
6.376
1.00
35.40
O

ATOM
2808
O
HOH
W4094
30.455
10.041
6.941
1.00
32.99
O

ATOM
2809
O
HOH
W4095
26.815
0.664
4.954
1.00
27.85
O

ATOM
2810
O
HOH
W4096
15.273
23.735
−4.277
1.00
47.73
O

ATOM
2811
O
HOH
W4099
26.449
1.509
2.656
1.00
65.15
O

ATOM
2812
O
HOH
W4100
0.838
7.963
3.230
1.00
37.27
O

ATOM
2813
O
HOH
W4101
29.381
8.723
0.899
1.00
43.02
O

ATOM
2814
O
HOH
W4102
40.660
−5.785
23.570
1.00
45.63
O

ATOM
2815
O
HOH
W4103
26.328
6.312
5.240
1.00
53.46
O

ATOM
2816
O
HOH
W4104
34.720
1.902
16.155
1.00
43.82
O

ATOM
2817
O
HOH
W4105
−7.319
−8.388
40.539
1.00
39.00
O

ATOM
2818
O
HOH
W4106
18.869
25.116
1.680
1.00
46.38
O

ATOM
2819
O
HOH
W4107
16.340
14.706
24.191
1.00
38.04
O

ATOM
2820
O
HOH
W4108
6.923
8.908
27.885
1.00
36.28
O

ATOM
2821
O
HOH
W4109
12.525
−11.624
17.355
1.00
34.51
O

ATOM
2822
O
HOH
W4110
34.314
−7.049
18.369
1.00
34.61
O

ATOM
2823
O
HOH
W4113
38.750
−2.512
27.167
1.00
57.88
O

ATOM
2824
O
HOH
W4114
18.115
3.750
1.319
1.00
31.45
O

ATOM
2825
O
HOH
W4115
27.875
1.248
31.553
1.00
55.12
O

ATOM
2826
O
HOH
W4116
7.683
−21.130
−8.639
1.00
46.38
O

ATOM
2827
O
HOH
W4117
−0.188
6.861
39.329
1.00
45.23
O

ATOM
2828
O
HOH
W4118
15.597
2.256
13.150
1.00
38.63
O

ATOM
2829
O
HOH
W4120
29.648
18.094
28.167
1.00
35.93
O

ATOM
2830
O
HOH
W4121
16.930
−20.733
11.766
1.00
37.44
O

ATOM
2831
O
HOH
W4122
7.167
−12.636
−7.617
1.00
48.07
O

ATOM
2832
O
HOH
W4123
37.628
10.036
12.640
1.00
43.48
O

ATOM
2833
O
HOH
W4124
13.082
−13.269
27.306
1.00
52.38
O

ATOM
2834
O
HOH
W4125
4.976
−26.696
6.493
1.00
47.37
O

ATOM
2835
O
HOH
W4126
2.241
−22.225
15.163
1.00
51.68
O

ATOM
2836
O
HOH
W4127
8.988
−10.057
20.455
1.00
50.47
O

ATOM
2837
O
HOH
W4128
18.719
−13.639
−6.616
1.00
49.20
O

ATOM
2838
O
HOH
W4129
21.651
22.882
0.638
1.00
46.89
O

ATOM
2839
O
HOH
W4130
27.239
3.345
29.234
1.00
25.74
O

ATOM
2840
O
HOH
W4131
9.016
−8.748
−1.209
1.00
45.62
O

ATOM
2841
O
HOH
W4132
13.082
−9.632
37.155
1.00
43.55
O

ATOM
2842
O
HOH
W4133
29.378
15.689
6.467
1.00
49.72
O

ATOM
2843
O
HOH
W4134
−7.908
−3.988
42.818
1.00
30.81
O

ATOM
2844
O
HOH
W4135
3.562
−8.297
27.665
1.00
45.56
O

ATOM
2845
O
HOH
W4136
−7.199
−0.161
28.514
1.00
24.59
O

ATOM
2846
O
HOH
W4137
31.194
6.207
6.288
1.00
42.31
O

ATOM
2847
O
HOH
W4138
19.383
8.002
23.933
1.00
35.57
O

ATOM
2848
O
HOH
W4139
−6.335
−8.439
24.417
1.00
47.50
O

ATOM
2849
O
HOH
W4140
37.800
−1.901
17.636
1.00
38.42
O

ATOM
2850
O
HOH
W4141
36.896
4.279
13.213
1.00
44.41
O

ATOM
2851
O
HOH
W4142
18.980
16.923
−5.091
1.00
32.40
O

ATOM
2852
O
HOH
W4143
6.338
17.886
−7.468
1.00
44.66
O

ATOM
2853
O
HOH
W4144
8.099
9.789
−8.452
1.00
34.29
O

ATOM
2854
O
HOH
W4145
22.400
22.185
4.929
1.00
58.51
O

ATOM
2855
O
HOH
W4146
23.417
1.724
−2.662
1.00
49.61
O

ATOM
2856
O
HOH
W4147
28.353
11.186
5.638
1.00
36.80
O

ATOM
2857
O
HOH
W4148
0.018
1.428
9.817
1.00
46.52
O

ATOM
2858
O
HOH
W4149
38.727
−0.038
26.083
1.00
50.08
O

ATOM
2859
O
HOH
W4150
24.171
−8.880
20.179
1.00
43.36
O

ATOM
2860
O
HOH
W4151
−0.768
−7.980
41.105
1.00
48.48
O

ATOM
2861
O
HOH
W4152
26.257
5.046
35.426
1.00
48.00
O

ATOM
2862
O
HOH
W4153
35.432
0.075
28.104
1.00
43.89
O

ATOM
2863
O
HOH
W4154
35.301
2.870
27.050
1.00
52.24
O

ATOM
2864
O
HOH
W4155
−4.097
3.796
17.913
1.00
44.40
O

ATOM
2865
O
HOH
W4156
29.195
0.822
3.786
1.00
40.55
O

ATOM
2866
O
HOH
W4157
15.774
−2.195
11.976
1.00
39.79
O

ATOM
2867
O
HOH
W4158
22.736
4.680
3.551
1.00
24.63
O

ATOM
2868
O
HOH
W4159
10.086
−24.038
17.929
1.00
54.44
O

ATOM
2869
O
HOH
W4161
37.774
−8.164
11.579
1.00
59.16
O

ATOM
2870
O
HOH
W4162
25.882
18.452
33.331
1.00
33.59
O

ATOM
2871
O
HOH
W4163
−0.430
0.356
12.041
1.00
45.32
O

ATOM
2872
O
HOH
W4164
−3.073
−7.128
24.073
1.00
45.12
O

ATOM
2873
O
HOH
W4165
31.655
13.815
8.848
1.00
29.05
O

ATOM
2874
O
HOH
W4166
17.133
8.014
−0.782
1.00
24.81
O

ATOM
2875
O
HOH
W4167
11.582
−12.517
13.880
1.00
37.19
O

ATOM
2876
O
HOH
W4168
15.057
−15.827
14.902
1.00
25.73
O

ATOM
2877
O
HOH
W4169
12.130
−17.876
15.236
1.00
35.36
O

ATOM
2878
O
HOH
W4170
7.663
8.075
46.234
1.00
31.45
O

ATOM
2879
O
HOH
W4171
8.858
17.412
12.301
1.00
37.47
O

TER
2880

HOH
W4171

END

[0363]

7

TABLE 5

REMARK coordinates from restrained individual B-factor refinement

REMARK refinement resolution: 500.0 − 1.90 A

REMARK starting r = 0.2427 free_r = 0.2720

REMARK final r = 0.2425 free_r = 0.2731

REMARK B rmsd for bonded mainchain atoms = 0.960 target = 1.5

REMARK B rmsd for bonded sidechain atoms = 1.085 target = 2.0

REMARK B rmsd for angle mainchain atoms = 1.688 target = 2.0

REMARK B rmsd for angle sidechain atoms = 1.768 target = 2.5

REMARK wa = 1.18715

REMARK rweight = 0.298329

REMARK target = mlf steps = 30

REMARK sg = C2 a = 120.188 b = 62.273 c = 51.673 alpha = 90

beta = 98.745 gamma = 90

REMARK parameter file 1 CNX_TOPPAR:protein_rep.param

REMARK parameter file 2 CNX_TOPPAR:water_rep.param

REMARK parameter file 3 CNX_TOPPAR:ion.param

REMARK parameter file 4 35-ADP/35-ADP.param

REMARK molecular structure file: generate.psf

REMARK input coordinates: minimize.pdb

REMARK reflection file = ../data/x-ray_data.cv

REMARK ncs = none

REMARK B-correction resolution: 6.0 − 1.90

REMARK initial B-factor correction applied to fobs:

REMARK B11 = 0.036 B22 = −2.635 B33 = 2.599

REMARK B12 = 0.000 B13 = 0.515 B23 = 0.000

REMARK B-factor correction applied to coordinate array B: 0.030

REMARK bulk solvent: (Mask) density level = 0.369861 e/A{circumflex over ( )}3, B-factor = 96.7512 A{circumflex over ( )}2

REMARK reflections with |Fobs|/sigma_F < 0.0 rejected

REMARK reflections with |Fobs| > 10000 * rms (Fobs) rejected

REMARK theoretical total number of refl. in resol. range:
29870
(100.0%)

REMARK number of unobserved reflections (no entry or |F| = 0):
330
(1.1%)

REMARK number of reflections rejected:
0
(0.0%)

REMARK total number of reflections used:
29540
(98.9%)

REMARK number of reflections in working set:
28083
(94.0%)

REMARK number of reflections in test set:
1457
(4.9%)

REMARK FILENAME = “acps 35-ADP.pdb”

REMARK Written by CNX VERSION: 2000

ATOM
1
CB
MET
A1003
37.264
5.634
20.230
1.00
26.46
C

ATOM
2
CG
MET
A1003
36.648
6.209
21.498
1.00
29.51
C

ATOM
3
SD
MET
A1003
37.784
7.312
22.398
1.00
33.70
S

ATOM
4
CE
MET
A1003
37.843
8.718
21.291
1.00
32.08
C

ATOM
5
C
MET
A1003
35.048
5.262
19.102
1.00
23.04
C

ATOM
6
O
MET
A1003
35.009
6.245
18.358
1.00
22.46
O

ATOM
7
N
MET
A1003
37.108
4.155
18.256
1.00
24.80
N

ATOM
8
CA
MET
A1003
36.389
4.622
19.479
1.00
24.32
C

ATOM
9
N
ILE
A1004
33.957
4.690
19.606
1.00
22.15
N

ATOM
10
CA
ILE
A1004
32.606
5.202
19.348
1.00
21.16
C

ATOM
11
CB
ILE
A1004
31.535
4.120
19.670
1.00
21.51
C

ATOM
12
CG2
ILE
A1004
30.122
4.710
19.558
1.00
21.66
C

ATOM
13
CG1
ILE
A1004
31.696
2.927
18.722
1.00
21.75
C

ATOM
14
CD1
ILE
A1004
30.823
1.734
19.074
1.00
22.20
C

ATOM
15
C
ILE
A1004
32.361
6.417
20.245
1.00
20.57
C

ATOM
16
O
ILE
A1004
32.773
6.416
21.407
1.00
21.36
O

ATOM
17
N
VAL
A1005
31.705
7.448
19.713
1.00
19.47
N

ATOM
18
CA
VAL
A1005
31.409
8.652
20.492
1.00
18.73
C

ATOM
19
CB
VAL
A1005
32.308
9.852
20.042
1.00
19.66
C

ATOM
20
CG1
VAL
A1005
33.779
9.530
20.319
1.00
20.39
C

ATOM
21
CG2
VAL
A1005
32.119
10.142
18.562
1.00
20.39
C

ATOM
22
C
VAL
A1005
29.924
9.085
20.502
1.00
17.55
C

ATOM
23
O
VAL
A1005
29.601
10.193
20.940
1.00
16.98
O

ATOM
24
N
GLY
A1006
29.026
8.207
20.041
1.00
16.14
N

ATOM
25
CA
GLY
A1006
27.593
8.513
20.046
1.00
14.83
C

ATOM
26
C
GLY
A1006
26.725
7.566
19.216
1.00
13.78
C

ATOM
27
O
GLY
A1006
27.223
6.982
18.257
1.00
12.47
O

ATOM
28
N
HIS
A1007
25.442
7.409
19.581
1.00
13.88
N

ATOM
29
CA
HIS
A1007
24.495
6.535
18.844
1.00
14.19
C

ATOM
30
CB
HIS
A1007
24.638
5.080
19.332
1.00
14.36
C

ATOM
31
CG
HIS
A1007
23.663
4.115
18.711
1.00
14.94
C

ATOM
32
CD2
HIS
A1007
22.904
3.137
19.266
1.00
15.52
C

ATOM
33
ND1
HIS
A1007
23.410
4.070
17.355
1.00
14.28
N

ATOM
34
CE1
HIS
A1007
22.537
3.108
17.102
1.00
15.47
C

ATOM
35
NE2
HIS
A1007
22.214
2.526
18.245
1.00
15.49
N

ATOM
36
C
HIS
A1007
23.025
7.000
18.999
1.00
13.90
C

ATOM
37
O
HIS
A1007
22.588
7.310
20.115
1.00
13.25
O

ATOM
38
N
GLY
A1008
22.276
7.053
17.888
1.00
13.72
N

ATOM
39
CA
GLY
A1008
20.870
7.476
17.931
1.00
13.61
C

ATOM
40
C
GLY
A1008
19.944
6.833
16.890
1.00
13.86
C

ATOM
41
O
GLY
A1008
20.402
6.498
15.795
1.00
13.86
O

ATOM
42
N
ILE
A1009
18.653
6.649
17.218
1.00
13.29
N

ATOM
43
CA
ILE
A1009
17.672
6.046
16.281
1.00
13.44
C

ATOM
44
CB
ILE
A1009
17.342
4.554
16.639
1.00
14.13
C

ATOM
45
CG2
ILE
A1009
18.619
3.696
16.642
1.00
13.71
C

ATOM
46
CG1
ILE
A1009
16.638
4.503
18.003
1.00
13.45
C

ATOM
47
CD1
ILE
A1009
16.175
3.134
18.434
1.00
15.16
C

ATOM
48
C
ILE
A1009
16.318
6.799
16.257
1.00
14.09
C

ATOM
49
O
ILE
A1009
16.033
7.589
17.165
1.00
12.83
O

ATOM
50
N
ASP
A1010
15.491
6.537
15.232
1.00
14.68
N

ATOM
51
CA
ASP
A1010
14.161
7.167
15.101
1.00
16.24
C

ATOM
52
CB
ASP
A1010
14.287
8.580
14.496
1.00
17.11
C

ATOM
53
CG
ASP
A1010
12.944
9.328
14.428
1.00
19.40
C

ATOM
54
OD1
ASP
A1010
12.265
9.295
13.369
1.00
19.82
O

ATOM
55
OD2
ASP
A1010
12.563
9.948
15.446
1.00
19.26
O

ATOM
56
C
ASP
A1010
13.193
6.348
14.230
1.00
16.72
C

ATOM
57
O
ASP
A1010
13.618
5.693
13.276
1.00
16.89
O

ATOM
58
N
ILE
A1011
11.900
6.387
14.570
1.00
17.01
N

ATOM
59
CA
ILE
A1011
10.850
5.706
13.796
1.00
17.33
C

ATOM
60
CB
ILE
A1011
10.410
4.353
14.447
1.00
18.10
C

ATOM
61
CG2
ILE
A1011
9.963
4.570
15.898
1.00
17.28
C

ATOM
62
CG1
ILE
A1011
9.297
3.717
13.601
1.00
18.21
C

ATOM
63
CD1
ILE
A1011
8.852
2.338
14.083
1.00
20.73
C

ATOM
64
C
ILE
A1011
9.648
6.664
13.679
1.00
18.00
C

ATOM
65
O
ILE
A1011
9.262
7.298
14.663
1.00
16.80
O

ATOM
66
N
GLU
A1012
9.060
6.760
12.481
1.00
18.22
N

ATOM
67
CA
GLU
A1012
7.951
7.690
12.220
1.00
19.38
C

ATOM
68
CB
GLU
A1012
8.537
8.972
11.609
1.00
20.91
C

ATOM
69
CG
GLU
A1012
7.537
10.036
11.186
1.00
23.69
C

ATOM
70
CD
GLU
A1012
7.065
10.909
12.336
1.00
24.81
C

ATOM
71
OE1
GLU
A1012
7.432
10.632
13.499
1.00
24.64
O

ATOM
72
OE2
GLU
A1012
6.318
11.878
12.070
1.00
27.04
O

ATOM
73
C
GLU
A1012
6.845
7.146
11.293
1.00
19.45
C

ATOM
74
O
GLU
A1012
7.119
6.397
10.358
1.00
17.84
O

ATOM
75
N
GLU
A1013
5.599
7.538
11.557
1.00
20.13
N

ATOM
76
CA
GLU
A1013
4.456
7.119
10.735
1.00
21.62
C

ATOM
77
CB
GLU
A1013
3.178
7.146
11.584
1.00
24.29
C

ATOM
78
CG
GLU
A1013
1.916
6.753
10.845
1.00
28.34
C

ATOM
79
CD
GLU
A1013
0.710
6.656
11.766
1.00
30.69
C

ATOM
80
OE1
GLU
A1013
−0.400
6.361
11.267
1.00
33.13
O

ATOM
81
OE2
GLU
A1013
0.871
6.872
12.990
1.00
33.49
O

ATOM
82
C
GLU
A1013
4.302
8.061
9.521
1.00
21.59
C

ATOM
83
O
GLU
A1013
4.247
9.280
9.682
1.00
20.05
O

ATOM
84
N
LEU
A1014
4.223
7.493
8.316
1.00
21.61
N

ATOM
85
CA
LEU
A1014
4.104
8.288
7.087
1.00
22.02
C

ATOM
86
CB
LEU
A1014
4.191
7.365
5.857
1.00
23.16
C

ATOM
87
CG
LEU
A1014
5.502
6.571
5.745
1.00
24.38
C

ATOM
88
CD1
LEU
A1014
5.454
5.622
4.551
1.00
25.08
C

ATOM
89
CD2
LEU
A1014
6.667
7.538
5.604
1.00
25.38
C

ATOM
90
C
LEU
A1014
2.841
9.158
7.006
1.00
22.02
C

ATOM
91
O
LEU
A1014
2.867
10.240
6.419
1.00
21.55
O

ATOM
92
N
ALA
A1015
1.742
8.691
7.593
1.00
22.06
N

ATOM
93
CA
ALA
A1015
0.488
9.452
7.595
1.00
22.62
C

ATOM
94
CB
ALA
A1015
−0.605
8.656
8.299
1.00
22.21
C

ATOM
95
C
ALA
A1015
0.644
10.817
8.274
1.00
22.87
C

ATOM
96
O
ALA
A1015
0.005
11.796
7.875
1.00
23.00
O

ATOM
97
N
SER
A1016
1.482
10.876
9.307
1.00
23.27
N

ATOM
98
CA
SER
A1016
1.716
12.123
10.034
1.00
23.77
C

ATOM
99
CB
SER
A1016
2.535
11.860
11.305
1.00
24.30
C

ATOM
100
OG
SER
A1016
1.890
10.919
12.145
1.00
26.09
O

ATOM
101
C
SER
A1016
2.443
13.146
9.162
1.00
23.41
C

ATOM
102
O
SER
A1016
2.173
14.348
9.249
1.00
23.19
O

ATOM
103
N
ILE
A1017
3.378
12.673
8.340
1.00
23.05
N

ATOM
104
CA
ILE
A1017
4.118
13.566
7.450
1.00
22.92
C

ATOM
105
CB
ILE
A1017
5.355
12.860
6.838
1.00
23.00
C

ATOM
106
CG2
ILE
A1017
6.107
13.823
5.918
1.00
23.26
C

ATOM
107
CG1
ILE
A1017
6.289
12.365
7.951
1.00
23.63
C

ATOM
108
CD1
ILE
A1017
6.896
13.467
8.810
1.00
22.84
C

ATOM
109
C
ILE
A1017
3.204
14.053
6.308
1.00
23.44
C

ATOM
110
O
ILE
A1017
3.276
15.218
5.896
1.00
23.11
O

ATOM
111
N
GLU
A1018
2.341
13.170
5.805
1.00
22.98
N

ATOM
112
CA
GLU
A1018
1.443
13.549
4.714
1.00
24.09
C

ATOM
113
CB
GLU
A1018
0.729
12.306
4.147
1.00
25.23
C

ATOM
114
CG
GLU
A1018
−0.252
12.592
2.997
1.00
27.75
C

ATOM
115
CD
GLU
A1018
−0.632
11.345
2.190
1.00
29.64
C

ATOM
116
OE1
GLU
A1018
−0.807
10.255
2.783
1.00
30.50
O

ATOM
117
OE2
GLU
A1018
−0.771
11.459
0.952
1.00
30.61
O

ATOM
118
C
GLU
A1018
0.427
14.612
5.150
1.00
24.15
C

ATOM
119
O
GLU
A1018
0.142
15.550
4.395
1.00
23.68
O

ATOM
120
N
SER
A1019
−0.103
14.481
6.367
1.00
23.86
N

ATOM
121
CA
SER
A1019
−1.078
15.445
6.879
1.00
24.87
C

ATOM
122
CB
SER
A1019
−1.641
14.993
8.234
1.00
24.60
C

ATOM
123
OG
SER
A1019
−2.387
13.794
8.120
1.00
26.37
O

ATOM
124
C
SER
A1019
−0.450
16.824
7.045
1.00
25.06
C

ATOM
125
O
SER
A1019
−1.077
17.836
6.741
1.00
25.39
O

ATOM
126
N
ALA
A1020
0.790
16.856
7.525
1.00
25.98
N

ATOM
127
CA
ALA
A1020
1.508
18.112
7.748
1.00
26.26
C

ATOM
128
CB
ALA
A1020
2.869
17.829
8.399
1.00
26.48
C

ATOM
129
C
ALA
A1020
1.695
18.909
6.460
1.00
26.83
C

ATOM
130
O
ALA
A1020
1.589
20.138
6.463
1.00
26.25
O

ATOM
131
N
VAL
A1021
1.974
18.210
5.364
1.00
27.31
N

ATOM
132
CA
VAL
A1021
2.166
18.855
4.064
1.00
28.77
C

ATOM
133
CB
VAL
A1021
2.767
17.868
3.029
1.00
28.35
C

ATOM
134
CG1
VAL
A1021
2.801
18.510
1.639
1.00
28.63
C

ATOM
135
CG2
VAL
A1021
4.176
17.461
3.457
1.00
28.09
C

ATOM
136
C
VAL
A1021
0.845
19.396
3.512
1.00
30.16
C

ATOM
137
O
VAL
A1021
0.775
20.541
3.054
1.00
29.31
O

ATOM
138
N
THR
A1022
−0.195
18.565
3.557
1.00
31.76
N

ATOM
139
CA
THR
A1022
−1.515
18.951
3.057
1.00
33.81
C

ATOM
140
CB
THR
A1022
−2.541
17.798
3.230
1.00
33.53
C

ATOM
141
OG1
THR
A1022
−2.119
16.663
2.466
1.00
33.79
O

ATOM
142
CG2
THR
A1022
−3.926
18.224
2.749
1.00
33.72
C

ATOM
143
C
THR
A1022
−2.032
20.183
3.790
1.00
34.97
C

ATOM
144
O
THR
A1022
−2.802
20.968
3.237
1.00
36.01
O

ATOM
145
N
ARG
A1023
−1.585
20.346
5.029
1.00
36.61
N

ATOM
146
CA
ARG
A1023
−1.988
21.462
5.876
1.00
38.01
C

ATOM
147
CB
ARG
A1023
−1.371
21.297
7.267
1.00
38.96
C

ATOM
148
CG
ARG
A1023
−2.284
21.702
8.409
1.00
40.44
C

ATOM
149
CD
ARG
A1023
−2.443
20.556
9.393
1.00
41.63
C

ATOM
150
NE
ARG
A1023
−1.184
20.219
10.053
1.00
42.83
N

ATOM
151
CZ
ARG
A1023
−1.000
19.134
10.800
1.00
43.45
C

ATOM
152
NH1
ARG
A1023
−1.997
18.277
10.981
1.00
43.85
N

ATOM
153
NH2
ARG
A1023
0.178
18.906
11.367
1.00
43.30
N

ATOM
154
C
ARG
A1023
−1.603
22.825
5.302
1.00
38.55
C

ATOM
155
O
ARG
A1023
−2.143
23.850
5.722
1.00
38.81
O

ATOM
156
N
HIS
A1024
−0.663
22.842
4.359
1.00
38.91
N

ATOM
157
CA
HIS
A1024
−0.244
24.096
3.733
1.00
38.99
C

ATOM
158
CB
HIS
A1024
−1.432
24.654
2.935
1.00
40.09
C

ATOM
159
CG
HIS
A1024
−1.184
25.993
2.315
1.00
41.43
C

ATOM
160
CD2
HIS
A1024
−1.936
27.119
2.304
1.00
41.88
C

ATOM
161
ND1
HIS
A1024
−0.058
26.276
1.573
1.00
41.78
N

ATOM
162
CE1
HIS
A1024
−0.126
27.519
1.131
1.00
42.17
C

ATOM
163
NE2
HIS
A1024
−1.257
28.053
1.560
1.00
42.70
N

ATOM
164
C
HIS
A1024
0.245
25.107
4.782
1.00
38.60
C

ATOM
165
O
HIS
A1024
−0.251
26.236
4.857
1.00
38.61
O

ATOM
166
N
GLU
A1025
1.234
24.696
5.575
1.00
37.69
N

ATOM
167
CA
GLU
A1025
1.784
25.533
6.643
1.00
36.89
C

ATOM
168
CB
GLU
A1025
1.545
24.854
7.995
1.00
37.94
C

ATOM
169
CG
GLU
A1025
2.255
23.508
8.126
1.00
39.13
C

ATOM
170
CD
GLU
A1025
2.003
22.828
9.459
1.00
40.28
C

ATOM
171
OE1
GLU
A1025
0.853
22.405
9.709
1.00
41.24
O

ATOM
172
OE2
GLU
A1025
2.959
22.716
10.258
1.00
40.84
O

ATOM
173
C
GLU
A1025
3.280
25.856
6.518
1.00
35.45
C

ATOM
174
O
GLU
A1025
3.857
26.466
7.424
1.00
35.71
O

ATOM
175
N
GLY
A1026
3.906
25.441
5.420
1.00
33.22
N

ATOM
176
CA
GLY
A1026
5.324
25.708
5.220
1.00
30.99
C

ATOM
177
C
GLY
A1026
6.265
24.668
5.819
1.00
29.44
C

ATOM
178
O
GLY
A1026
7.448
24.943
6.040
1.00
28.80
O

ATOM
179
N
PHE
A1027
5.743
23.470
6.073
1.00
27.49
N

ATOM
180
CA
PHE
A1027
6.524
22.378
6.657
1.00
26.42
C

ATOM
181
CB
PHE
A1027
5.618
21.149
6.830
1.00
26.50
C

ATOM
182
CG
PHE
A1027
6.272
19.995
7.541
1.00
26.07
C

ATOM
183
CD1
PHE
A1027
6.650
20.103
8.876
1.00
25.99
C

ATOM
184
CD2
PHE
A1027
6.499
18.790
6.873
1.00
26.17
C

ATOM
185
CE1
PHE
A1027
7.243
19.028
9.541
1.00
26.70
C

ATOM
186
CE2
PHE
A1027
7.091
17.711
7.527
1.00
26.08
C

ATOM
187
CZ
PHE
A1027
7.465
17.828
8.863
1.00
26.23
C

ATOM
188
C
PHE
A1027
7.776
21.998
5.852
1.00
25.70
C

ATOM
189
O
PHE
A1027
8.892
22.017
6.377
1.00
25.54
O

ATOM
190
N
ALA
A1028
7.598
21.656
4.579
1.00
24.86
N

ATOM
191
CA
ALA
A1028
8.726
21.260
3.737
1.00
24.85
C

ATOM
192
CB
ALA
A1028
8.232
20.919
2.333
1.00
24.87
C

ATOM
193
C
ALA
A1028
9.824
22.325
3.661
1.00
25.07
C

ATOM
194
O
ALA
A1028
11.018
22.009
3.685
1.00
24.02
O

ATOM
195
N
LYS
A1029
9.417
23.587
3.571
1.00
25.80
N

ATOM
196
CA
LYS
A1029
10.364
24.695
3.488
1.00
26.80
C

ATOM
197
CB
LYS
A1029
9.598
26.000
3.222
1.00
28.18
C

ATOM
198
CG
LYS
A1029
10.449
27.200
2.800
1.00
30.30
C

ATOM
199
CD
LYS
A1029
11.251
27.769
3.958
1.00
32.28
C

ATOM
200
CE
LYS
A1029
11.799
29.151
3.636
1.00
33.23
C

ATOM
201
NZ
LYS
A1029
10.702
30.153
3.506
1.00
34.55
N

ATOM
202
C
LYS
A1029
11.197
24.806
4.771
1.00
26.54
C

ATOM
203
O
LYS
A1029
12.344
25.244
4.738
1.00
26.39
O

ATOM
204
N
ARG
A1030
10.624
24.394
5.897
1.00
26.43
N

ATOM
205
CA
ARG
A1030
11.327
24.464
7.178
1.00
26.50
C

ATOM
206
CB
ARG
A1030
10.312
24.485
8.334
1.00
27.57
C

ATOM
207
CG
ARG
A1030
10.945
24.487
9.727
1.00
30.51
C

ATOM
208
CD
ARG
A1030
9.933
24.858
10.820
1.00
31.96
C

ATOM
209
NE
ARG
A1030
8.887
23.851
11.008
1.00
32.84
N

ATOM
210
CZ
ARG
A1030
9.033
22.740
11.723
1.00
33.04
C

ATOM
211
NH1
ARG
A1030
10.184
22.482
12.327
1.00
33.30
N

ATOM
212
NH2
ARG
A1030
8.028
21.884
11.836
1.00
33.60
N

ATOM
213
C
ARG
A1030
12.325
23.327
7.407
1.00
25.55
C

ATOM
214
O
ARG
A1030
13.402
23.539
7.976
1.00
25.72
O

ATOM
215
N
VAL
A1031
11.967
22.130
6.952
1.00
24.16
N

ATOM
216
CA
VAL
A1031
12.795
20.934
7.134
1.00
23.09
C

ATOM
217
CB
VAL
A1031
11.903
19.655
7.150
1.00
23.53
C

ATOM
218
CG1
VAL
A1031
12.765
18.398
7.339
1.00
23.93
C

ATOM
219
CG2
VAL
A1031
10.874
19.754
8.258
1.00
22.96
C

ATOM
220
C
VAL
A1031
13.932
20.684
6.134
1.00
22.57
C

ATOM
221
O
VAL
A1031
14.952
20.094
6.504
1.00
22.31
O

ATOM
222
N
LEU
A1032
13.765
21.127
4.887
1.00
21.47
N

ATOM
223
CA
LEU
A1032
14.764
20.888
3.830
1.00
21.78
C

ATOM
224
CB
LEU
A1032
14.062
20.277
2.607
1.00
21.38
C

ATOM
225
CG
LEU
A1032
13.126
19.073
2.773
1.00
20.75
C

ATOM
226
CD1
LEU
A1032
12.446
18.779
1.428
1.00
21.22
C

ATOM
227
CD2
LEU
A1032
13.912
17.851
3.249
1.00
20.06
C

ATOM
228
C
LEU
A1032
15.565
22.107
3.355
1.00
22.39
C

ATOM
229
O
LEU
A1032
15.061
23.233
3.375
1.00
22.40
O

ATOM
230
N
THR
A1033
16.806
21.875
2.917
1.00
23.26
N

ATOM
231
CA
THR
A1033
17.661
22.951
2.394
1.00
24.31
C

ATOM
232
CB
THR
A1033
19.171
22.577
2.366
1.00
24.32
C

ATOM
233
OG1
THR
A1033
19.380
21.472
1.473
1.00
24.43
O

ATOM
234
CG2
THR
A1033
19.671
22.217
3.756
1.00
23.93
C

ATOM
235
C
THR
A1033
17.255
23.215
0.945
1.00
25.20
C

ATOM
236
O
THR
A1033
16.343
22.570
0.426
1.00
24.87
O

ATOM
237
N
ALA
A1034
17.937
24.158
0.297
1.00
25.70
N

ATOM
238
CA
ALA
A1034
17.650
24.476
−1.100
1.00
26.57
C

ATOM
239
CB
ALA
A1034
18.485
25.676
−1.548
1.00
27.15
C

ATOM
240
C
ALA
A1034
17.943
23.270
−1.997
1.00
26.78
C

ATOM
241
O
ALA
A1034
17.115
22.896
−2.829
1.00
27.20
O

ATOM
242
N
LEU
A1035
19.122
22.672
−1.831
1.00
26.52
N

ATOM
243
CA
LEU
A1035
19.513
21.503
−2.623
1.00
27.27
C

ATOM
244
CB
LEU
A1035
20.943
21.063
−2.276
1.00
27.34
C

ATOM
245
CG
LEU
A1035
22.137
21.950
−2.658
1.00
28.71
C

ATOM
246
CD1
LEU
A1035
23.388
21.443
−1.953
1.00
28.34
C

ATOM
247
CD2
LEU
A1035
22.348
21.949
−4.171
1.00
29.34
C

ATOM
248
C
LEU
A1035
18.549
20.327
−2.408
1.00
26.73
C

ATOM
249
O
LEU
A1035
18.124
19.679
−3.369
1.00
26.11
O

ATOM
250
N
GLU
A1036
18.209
20.048
−1.151
1.00
26.36
N

ATOM
251
CA
GLU
A1036
17.285
18.958
−0.852
1.00
26.00
C

ATOM
252
CB
GLU
A1036
17.119
18.801
0.675
1.00
24.96
C

ATOM
253
CG
GLU
A1036
18.307
18.111
1.367
1.00
22.07
C

ATOM
254
CD
GLU
A1036
18.254
18.150
2.900
1.00
22.03
C

ATOM
255
OE1
GLU
A1036
18.819
17.229
3.540
1.00
20.25
O

ATOM
256
OE2
GLU
A1036
17.671
19.102
3.472
1.00
19.80
O

ATOM
257
C
GLU
A1036
15.934
19.228
−1.526
1.00
27.44
C

ATOM
258
O
GLU
A1036
15.296
18.314
−2.060
1.00
26.45
O

ATOM
259
N
MET
A1037
15.514
20.493
−1.525
1.00
28.51
N

ATOM
260
CA
MET
A1037
14.242
20.888
−2.132
1.00
30.20
C

ATOM
261
CB
MET
A1037
13.979
22.377
−1.877
1.00
31.18
C

ATOM
262
CG
MET
A1037
12.608
22.872
−2.324
1.00
32.64
C

ATOM
263
SD
MET
A1037
11.236
22.231
−1.342
1.00
35.22
S

ATOM
264
CE
MET
A1037
9.873
22.344
−2.511
1.00
34.31
C

ATOM
265
C
MET
A1037
14.192
20.608
−3.637
1.00
30.82
C

ATOM
266
O
MET
A1037
13.141
20.248
−4.176
1.00
31.12
O

ATOM
267
N
GLU
A1038
15.320
20.780
−4.317
1.00
31.36
N

ATOM
268
CA
GLU
A1038
15.371
20.526
−5.756
1.00
31.95
C

ATOM
269
CB
GLU
A1038
16.773
20.820
−6.296
1.00
33.04
C

ATOM
270
CG
GLU
A1038
17.111
22.300
−6.367
1.00
35.12
C

ATOM
271
CD
GLU
A1038
18.578
22.550
−6.673
1.00
36.56
C

ATOM
272
OE1
GLU
A1038
18.943
23.713
−6.941
1.00
37.89
O

ATOM
273
OE2
GLU
A1038
19.371
21.585
−6.639
1.00
37.49
O

ATOM
274
C
GLU
A1038
14.988
19.080
−6.072
1.00
31.21
C

ATOM
275
O
GLU
A1038
14.268
18.816
−7.036
1.00
30.88
O

ATOM
276
N
ARG
A1039
15.474
18.151
−5.253
1.00
29.97
N

ATOM
277
CA
ARG
A1039
15.188
16.730
−5.427
1.00
28.84
C

ATOM
278
CB
ARG
A1039
16.086
15.913
−4.483
1.00
29.69
C

ATOM
279
CG
ARG
A1039
15.853
14.402
−4.480
1.00
31.09
C

ATOM
280
CD
ARG
A1039
16.329
13.727
−5.758
1.00
32.23
C

ATOM
281
NE
ARG
A1039
16.125
12.280
−5.708
1.00
33.37
N

ATOM
282
CZ
ARG
A1039
16.076
11.492
−6.780
1.00
33.30
C

ATOM
283
NH1
ARG
A1039
16.222
12.007
−7.992
1.00
33.19
N

ATOM
284
NH2
ARG
A1039
15.852
10.191
−6.641
1.00
32.92
N

ATOM
285
C
ARG
A1039
13.709
16.442
−5.145
1.00
27.71
C

ATOM
286
O
ARG
A1039
13.059
15.705
−5.887
1.00
26.61
O

ATOM
287
N
PHE
A1040
13.189
17.041
−4.076
1.00
26.75
N

ATOM
288
CA
PHE
A1040
11.795
16.867
−3.659
1.00
26.16
C

ATOM
289
CB
PHE
A1040
11.532
17.729
−2.405
1.00
25.81
C

ATOM
290
CG
PHE
A1040
10.111
17.665
−1.886
1.00
25.91
C

ATOM
291
CD1
PHE
A1040
9.615
16.508
−1.292
1.00
25.16
C

ATOM
292
CD2
PHE
A1040
9.275
18.778
−1.979
1.00
25.61
C

ATOM
293
CE1
PHE
A1040
8.309
16.457
−0.798
1.00
25.37
C

ATOM
294
CE2
PHE
A1040
7.966
18.740
−1.490
1.00
25.17
C

ATOM
295
CZ
PHE
A1040
7.481
17.579
−0.897
1.00
25.69
C

ATOM
296
C
PHE
A1040
10.782
17.210
−4.760
1.00
25.80
C

ATOM
297
O
PHE
A1040
9.835
16.460
−4.990
1.00
25.42
O

ATOM
298
N
THR
A1041
10.984
18.332
−5.443
1.00
25.73
N

ATOM
299
CA
THR
A1041
10.053
18.759
−6.493
1.00
26.24
C

ATOM
300
CB
THR
A1041
10.257
20.259
−6.836
1.00
26.86
C

ATOM
301
OG1
THR
A1041
11.634
20.507
−7.154
1.00
26.58
O

ATOM
302
CG2
THR
A1041
9.849
21.130
−5.656
1.00
26.06
C

ATOM
303
C
THR
A1041
10.066
17.948
−7.800
1.00
26.59
C

ATOM
304
O
THR
A1041
9.149
18.071
−8.620
1.00
27.01
O

ATOM
305
N
SER
A1042
11.080
17.111
−7.996
1.00
26.31
N

ATOM
306
CA
SER
A1042
11.158
16.305
−9.222
1.00
26.03
C

ATOM
307
CB
SER
A1042
12.618
16.106
−9.631
1.00
26.30
C

ATOM
308
OG
SER
A1042
13.287
15.231
−8.737
1.00
27.19
O

ATOM
309
C
SER
A1042
10.488
14.935
−9.082
1.00
25.97
C

ATOM
310
O
SER
A1042
10.354
14.198
−10.063
1.00
25.27
O

ATOM
311
N
LEU
A1043
10.064
14.599
−7.865
1.00
25.25
N

ATOM
312
CA
LEU
A1043
9.431
13.310
−7.601
1.00
25.51
C

ATOM
313
CB
LEU
A1043
9.906
12.765
−6.245
1.00
24.11
C

ATOM
314
CG
LEU
A1043
11.425
12.571
−6.118
1.00
24.06
C

ATOM
315
CD1
LEU
A1043
11.768
12.080
−4.715
1.00
22.60
C

ATOM
316
CD2
LEU
A1043
11.914
11.571
−7.164
1.00
23.86
C

ATOM
317
C
LEU
A1043
7.907
13.389
−7.634
1.00
25.82
C

ATOM
318
O
LEU
A1043
7.333
14.475
−7.575
1.00
26.42
O

ATOM
319
N
LYS
A1044
7.256
12.233
−7.723
1.00
26.67
N

ATOM
320
CA
LYS
A1044
5.802
12.184
−7.785
1.00
27.60
C

ATOM
321
CB
LYS
A1044
5.361
11.803
−9.200
1.00
29.18
C

ATOM
322
CG
LYS
A1044
5.705
10.369
−9.562
1.00
31.06
C

ATOM
323
CD
LYS
A1044
5.359
10.045
−10.999
1.00
32.81
C

ATOM
324
CE
LYS
A1044
5.572
8.567
−11.282
1.00
33.54
C

ATOM
325
NZ
LYS
A1044
4.702
7.716
−10.419
1.00
34.84
N

ATOM
326
C
LYS
A1044
5.159
11.211
−6.795
1.00
27.94
C

ATOM
327
O
LYS
A1044
5.774
10.227
−6.367
1.00
27.61
O

ATOM
328
N
GLY
A1045
3.904
11.500
−6.464
1.00
27.68
N

ATOM
329
CA
GLY
A1045
3.124
10.671
−5.562
1.00
28.74
C

ATOM
330
C
GLY
A1045
3.741
10.224
−4.252
1.00
28.99
C

ATOM
331
O
GLY
A1045
4.282
11.024
−3.487
1.00
29.00
O

ATOM
332
N
ARG
A1046
3.643
8.925
−3.998
1.00
29.30
N

ATOM
333
CA
ARG
A1046
4.155
8.320
−2.776
1.00
30.48
C

ATOM
334
CB
ARG
A1046
3.790
6.833
−2.754
1.00
32.57
C

ATOM
335
CG
ARG
A1046
3.044
6.390
−1.513
1.00
35.84
C

ATOM
336
CD
ARG
A1046
2.680
4.922
−1.598
1.00
38.51
C

ATOM
337
NE
ARG
A1046
2.023
4.445
−0.384
1.00
41.12
N

ATOM
338
CZ
ARG
A1046
1.613
3.194
−0.204
1.00
42.33
C

ATOM
339
NH1
ARG
A1046
1.024
2.842
0.931
1.00
42.60
N

ATOM
340
NH2
ARG
A1046
1.793
2.292
−1.164
1.00
43.25
N

ATOM
341
C
ARG
A1046
5.663
8.479
−2.582
1.00
29.60
C

ATOM
342
O
ARG
A1046
6.128
8.686
−1.460
1.00
28.95
O

ATOM
343
N
ARG
A1047
6.423
8.375
−3.668
1.00
28.70
N

ATOM
344
CA
ARG
A1047
7.875
8.495
−3.585
1.00
28.01
C

ATOM
345
CD
ARG
A1047
8.512
8.167
−4.943
1.00
29.65
C

ATOM
346
CG
ARG
A1047
9.566
7.069
−4.869
1.00
32.09
C

ATOM
347
CD
ARG
A1047
9.831
6.426
−6.228
1.00
34.53
C

ATOM
348
NE
ARG
A1047
8.601
5.910
−6.825
1.00
36.57
N

ATOM
349
CZ
ARG
A1047
8.548
5.138
−7.906
1.00
37.35
C

ATOM
350
NH1
ARG
A1047
7.373
4.727
−8.368
1.00
38.05
N

ATOM
351
NH2
ARG
A1047
9.663
4.767
−8.523
1.00
38.02
N

ATOM
352
C
ARG
A1047
8.288
9.890
−3.117
1.00
26.86
C

ATOM
353
O
ARG
A1047
9.309
10.048
−2.444
1.00
25.61
O

ATOM
354
N
GLN
A1048
7.481
10.891
−3.464
1.00
25.04
N

ATOM
355
CA
GLN
A1048
7.739
12.277
−3.079
1.00
24.33
C

ATOM
356
CB
GLN
A1048
6.733
13.217
−3.779
1.00
25.19
C

ATOM
357
CG
GLN
A1048
7.138
14.694
−3.774
1.00
26.24
C

ATOM
358
CD
GLN
A1048
6.221
15.581
−4.620
1.00
26.41
C

ATOM
359
OE1
GLN
A1048
6.617
16.664
−5.047
1.00
26.86
O

ATOM
360
NE2
GLN
A1048
4.994
15.127
−4.853
1.00
27.01
N

ATOM
361
C
GLN
A1048
7.632
12.442
−1.553
1.00
23.25
C

ATOM
362
O
GLN
A1048
8.463
13.110
−0.935
1.00
23.01
O

ATOM
363
N
ILE
A1049
6.615
11.830
−0.949
1.00
22.49
N

ATOM
364
CA
ILE
A1049
6.423
11.919
0.504
1.00
22.00
C

ATOM
365
CB
ILE
A1049
5.011
11.414
0.916
1.00
23.38
C

ATOM
366
CG2
ILE
A1049
4.810
11.564
2.421
1.00
23.48
C

ATOM
367
CG1
ILE
A1049
3.928
12.197
0.161
1.00
24.39
C

ATOM
368
CD1
ILE
A1049
3.923
13.695
0.424
1.00
25.65
C

ATOM
369
C
ILE
A1049
7.496
11.118
1.274
1.00
21.25
C

ATOM
370
O
ILE
A1049
7.940
11.537
2.347
1.00
19.66
O

ATOM
371
N
GLU
A1050
7.913
9.975
0.724
1.00
20.69
N

ATOM
372
CA
GLU
A1050
8.939
9.146
1.372
1.00
20.67
C

ATOM
373
CB
GLU
A1050
9.093
7.794
0.650
1.00
22.03
C

ATOM
374
CG
GLU
A1050
10.362
7.017
1.051
1.00
23.69
C

ATOM
375
CD
GLU
A1050
10.385
6.625
2.520
1.00
24.98
C

ATOM
376
OE1
GLU
A1050
11.498
6.519
3.095
1.00
23.91
O

ATOM
377
OE2
GLU
A1050
9.292
6.409
3.097
1.00
25.89
O

ATOM
378
C
GLU
A1050
10.298
9.851
1.430
1.00
19.72
C

ATOM
379
O
GLU
A1050
11.073
9.634
2.367
1.00
19.12
O

ATOM
380
N
TYR
A1051
10.604
10.680
0.431
1.00
18.43
N

ATOM
381
CA
TYR
A1051
11.878
11.400
0.435
1.00
17.86
C

ATOM
382
CB
TYR
A1051
12.110
12.129
−0.902
1.00
18.12
C

ATOM
383
CG
TYR
A1051
13.379
12.970
−0.932
1.00
17.88
C

ATOM
384
CD1
TYR
A1051
13.372
14.307
−0.518
1.00
17.74
C

ATOM
385
CE1
TYR
A1051
14.547
15.076
−0.516
1.00
17.82
C

ATOM
386
CD2
TYR
A1051
14.592
12.419
−1.345
1.00
17.56
C

ATOM
387
CE2
TYR
A1051
15.770
13.176
−1.344
1.00
18.21
C

ATOM
388
CZ
TYR
A1051
15.740
14.501
−0.929
1.00
18.16
C

ATOM
389
OH
TYR
A1051
16.908
15.237
−0.923
1.00
18.28
O

ATOM
390
C
TYR
A1051
11.915
12.409
1.590
1.00
17.91
C

ATOM
391
O
TYR
A1051
12.927
12.525
2.290
1.00
16.53
O

ATOM
392
N
LEU
A1052
10.810
13.137
1.778
1.00
17.38
N

ATOM
393
CA
LEU
A1052
10.709
14.131
2.851
1.00
17.07
C

ATOM
394
CB
LEU
A1052
9.392
14.917
2.731
1.00
17.53
C

ATOM
395
CG
LEU
A1052
8.985
15.844
3.890
1.00
17.80
C

ATOM
396
CD1
LEU
A1052
10.096
16.844
4.191
1.00
18.32
C

ATOM
397
CD2
LEU
A1052
7.693
16.573
3.524
1.00
17.67
C

ATOM
398
C
LEU
A1052
10.784
13.448
4.219
1.00
16.62
C

ATOM
399
O
LEU
A1052
11.544
13.874
5.093
1.00
16.61
O

ATOM
400
N
ALA
A1053
10.006
12.383
4.394
1.00
15.83
N

ATOM
401
CA
ALA
A1053
9.985
11.645
5.662
1.00
15.97
C

ATOM
402
CB
ALA
A1053
8.974
10.516
5.587
1.00
15.80
C

ATOM
403
C
ALA
A1053
11.362
11.091
6.038
1.00
15.64
C

ATOM
404
O
ALA
A1053
11.750
11.129
7.208
1.00
15.53
O

ATOM
405
N
GLY
A1054
12.094
10.573
5.054
1.00
14.85
N

ATOM
406
CA
GLY
A1054
13.420
10.028
5.327
1.00
14.89
C

ATOM
407
C
GLY
A1054
14.431
11.073
5.789
1.00
14.97
C

ATOM
408
O
GLY
A1054
15.243
10.820
6.689
1.00
14.15
O

ATOM
409
N
ARG
A1055
14.403
12.250
5.169
1.00
14.68
N

ATOM
410
CA
ARG
A1055
15.327
13.313
5.553
1.00
15.29
C

ATOM
411
CB
ARG
A1055
15.257
14.462
4.533
1.00
14.70
C

ATOM
412
CG
ARG
A1055
16.364
14.420
3.438
1.00
16.14
C

ATOM
413
CD
ARG
A1055
16.452
13.082
2.658
1.00
16.61
C

ATOM
414
NE
ARG
A1055
17.610
13.039
1.745
1.00
16.90
N

ATOM
415
CZ
ARG
A1055
17.966
11.976
1.021
1.00
17.56
C

ATOM
416
NH1
ARG
A1055
17.265
10.850
1.093
1.00
16.02
N

ATOM
417
NH2
ARG
A1055
19.028
12.034
0.215
1.00
18.06
N

ATOM
418
C
ARG
A1055
15.010
13.804
6.980
1.00
15.61
C

ATOM
419
O
ARG
A1055
15.909
14.138
7.755
1.00
15.05
O

ATOM
420
N
TRP
A1056
13.731
13.826
7.333
1.00
15.92
N

ATOM
421
CA
TRP
A1056
13.324
14.252
8.676
1.00
17.44
C

ATOM
422
CB
TRP
A1056
11.791
14.409
8.706
1.00
20.42
C

ATOM
423
CG
TRP
A1056
11.151
14.202
10.044
1.00
24.52
C

ATOM
424
CD2
TRP
A1056
10.650
15.212
10.921
1.00
26.47
C

ATOM
425
CE2
TRP
A1056
10.140
14.556
12.065
1.00
27.71
C

ATOM
426
CE3
TRP
A1056
10.581
16.607
10.854
1.00
27.13
C

ATOM
427
CD1
TRP
A1056
10.931
13.005
10.673
1.00
25.93
C

ATOM
428
NE1
TRP
A1056
10.325
13.211
11.885
1.00
27.77
N

ATOM
429
CZ2
TRP
A1056
9.567
15.250
13.133
1.00
28.62
C

ATOM
430
CZ3
TRP
A1056
10.012
17.297
11.915
1.00
28.11
C

ATOM
431
CH2
TRP
A1056
9.512
16.617
13.041
1.00
29.24
C

ATOM
432
C
TRP
A1056
13.807
13.259
9.758
1.00
16.63
C

ATOM
433
O
TRP
A1056
14.339
13.661
10.813
1.00
14.62
O

ATOM
434
N
SER
A1057
13.645
11.965
9.477
1.00
15.34
N

ATOM
435
CA
SER
A1057
14.034
10.892
10.404
1.00
14.89
C

ATOM
436
CB
SER
A1057
13.509
9.549
9.864
1.00
16.31
C

ATOM
437
OG
SER
A1057
13.653
8.482
10.792
1.00
15.29
O

ATOM
438
C
SER
A1057
15.558
10.833
10.624
1.00
14.80
C

ATOM
439
O
SER
A1057
16.033
10.618
11.748
1.00
13.11
O

ATOM
440
N
ALA
A1058
16.326
11.043
9.560
1.00
13.86
N

ATOM
441
CA
ALA
A1058
17.784
11.015
9.670
1.00
14.03
C

ATOM
442
CB
ALA
A1058
18.408
11.077
8.283
1.00
14.39
C

ATOM
443
C
ALA
A1058
18.326
12.162
10.528
1.00
14.15
C

ATOM
444
O
ALA
A1058
19.253
11.972
11.326
1.00
12.67
O

ATOM
445
N
LYS
A1059
17.760
13.356
10.346
1.00
14.25
N

ATOM
446
CA
LYS
A1059
18.198
14.530
11.102
1.00
14.94
C

ATOM
447
CB
LYS
A1059
17.561
15.807
10.511
1.00
14.63
C

ATOM
448
CG
LYS
A1059
18.030
16.077
9.061
1.00
15.21
C

ATOM
449
CD
LYS
A1059
17.605
17.445
8.497
1.00
14.78
C

ATOM
450
CE
LYS
A1059
18.198
17.662
7.096
1.00
15.27
C

ATOM
451
NZ
LYS
A1059
17.780
18.955
6.460
1.00
14.73
N

ATOM
452
C
LYS
A1059
17.902
14.382
12.597
1.00
15.88
C

ATOM
453
O
LYS
A1059
18.726
14.755
13.441
1.00
15.17
O

ATOM
454
N
GLU
A1060
16.743
13.819
12.933
1.00
15.81
N

ATOM
455
CA
GLU
A1060
16.395
13.609
14.337
1.00
16.66
C

ATOM
456
CB
GLU
A1060
14.943
13.142
14.474
1.00
18.92
C

ATOM
457
CG
GLU
A1060
13.922
14.183
14.023
1.00
23.44
C

ATOM
458
CD
GLU
A1060
12.804
14.369
15.031
1.00
26.75
C

ATOM
459
OE1
GLU
A1060
12.175
13.358
15.414
1.00
29.16
O

ATOM
460
OE2
GLU
A1060
12.547
15.522
15.437
1.00
27.98
O

ATOM
461
C
GLU
A1060
17.333
12.578
14.977
1.00
15.69
C

ATOM
462
O
GLU
A1060
17.740
12.730
16.138
1.00
14.40
O

ATOM
463
N
ALA
A1061
17.689
11.541
14.219
1.00
14.51
N

ATOM
464
CA
ALA
A1061
18.586
10.500
14.727
1.00
14.88
C

ATOM
465
CB
ALA
A1061
18.658
9.312
13.730
1.00
14.28
C

ATOM
466
C
ALA
A1061
19.998
11.037
15.018
1.00
15.17
C

ATOM
467
O
ALA
A1061
20.635
10.622
16.001
1.00
14.05
O

ATOM
468
N
PHE
A1062
20.488
11.943
14.167
1.00
14.78
N

ATOM
469
CA
PHE
A1062
21.811
12.545
14.365
1.00
16.06
C

ATOM
470
CB
PHE
A1062
22.200
13.433
13.161
1.00
16.25
C

ATOM
471
CG
PHE
A1062
23.514
14.176
13.341
1.00
17.02
C

ATOM
472
CD1
PHE
A1062
23.562
15.384
14.039
1.00
17.84
C

ATOM
473
CD2
PHE
A1062
24.707
13.642
12.847
1.00
16.96
C

ATOM
474
CE1
PHE
A1062
24.783
16.049
14.247
1.00
17.77
C

ATOM
475
CE2
PHE
A1062
25.931
14.297
13.049
1.00
17.84
C

ATOM
476
CZ
PHE
A1062
25.964
15.505
13.754
1.00
18.67
C

ATOM
477
C
PHE
A1062
21.830
13.380
15.651
1.00
16.47
C

ATOM
478
O
PHE
A1062
22.792
13.326
16.422
1.00
15.43
O

ATOM
479
N
SER
A1063
20.760
14.138
15.895
1.00
17.69
N

ATOM
480
CA
SER
A1063
20.695
14.979
17.093
1.00
19.00
C

ATOM
481
CB
SER
A1063
19.446
15.881
17.067
1.00
20.22
C

ATOM
482
OG
SER
A1063
18.276
15.162
17.434
1.00
23.89
O

ATOM
483
C
SER
A1063
20.707
14.148
18.383
1.00
19.17
C

ATOM
484
O
SER
A1063
21.229
14.602
19.405
1.00
19.65
O

ATOM
485
N
LYS
A1064
20.124
12.949
18.353
1.00
18.93
N

ATOM
486
CA
LYS
A1064
20.121
12.093
19.545
1.00
19.27
C

ATOM
487
CB
LYS
A1064
19.094
10.961
19.418
1.00
19.83
C

ATOM
488
CG
LYS
A1064
17.648
11.413
19.471
1.00
21.72
C

ATOM
489
CD
LYS
A1064
16.720
10.201
19.456
1.00
23.02
C

ATOM
490
CE
LYS
A1064
15.270
10.614
19.240
1.00
24.30
C

ATOM
491
NZ
LYS
A1064
14.379
9.425
19.074
1.00
25.01
N

ATOM
492
C
LYS
A1064
21.510
11.497
19.770
1.00
19.33
C

ATOM
493
O
LYS
A1064
21.920
11.256
20.922
1.00
18.44
O

ATOM
494
N
ALA
A1065
22.230
11.254
18.674
1.00
18.91
N

ATOM
495
CA
ALA
A1065
23.588
10.716
18.757
1.00
20.48
C

ATOM
496
CB
ALA
A1065
24.110
10.348
17.359
1.00
19.55
C

ATOM
497
C
ALA
A1065
24.515
11.745
19.417
1.00
22.05
C

ATOM
498
O
ALA
A1065
25.486
11.374
20.086
1.00
22.04
O

ATOM
499
N
MET
A1066
24.224
13.032
19.224
1.00
23.48
N

ATOM
500
CA
MET
A1066
25.027
14.101
19.836
1.00
26.32
C

ATOM
501
CB
MET
A1066
24.893
15.409
19.044
1.00
27.55
C

ATOM
502
CG
MET
A1066
25.471
15.377
17.634
1.00
29.85
C

ATOM
503
SD
MET
A1066
27.227
15.839
17.541
1.00
34.49
S

ATOM
504
CE
MET
A1066
27.100
17.585
17.194
1.00
32.80
C

ATOM
505
C
MET
A1066
24.554
14.334
21.277
1.00
27.22
C

ATOM
506
O
MET
A1066
25.272
14.916
22.093
1.00
27.02
O

ATOM
507
N
GLY
A1067
23.335
13.885
21.572
1.00
28.21
N

ATOM
508
CA
GLY
A1067
22.770
14.032
22.905
1.00
29.77
C

ATOM
509
C
GLY
A1067
22.161
15.395
23.194
1.00
31.30
C

ATOM
510
O
GLY
A1067
21.943
15.746
24.356
1.00
30.88
O

ATOM
511
N
THR
A1068
21.857
16.153
22.145
1.00
32.65
N

ATOM
512
CA
THR
A1068
21.305
17.495
22.309
1.00
34.08
C

ATOM
513
CB
THR
A1068
22.128
18.520
21.510
1.00
34.54
C

ATOM
514
OG1
THR
A1068
21.950
18.280
20.109
1.00
34.50
O

ATOM
515
CG2
THR
A1068
23.613
18.400
21.849
1.00
34.68
C

ATOM
516
C
THR
A1068
19.843
17.694
21.911
1.00
35.08
C

ATOM
517
O
THR
A1068
19.199
18.637
22.380
1.00
35.34
O

ATOM
518
N
GLY
A1069
19.320
16.834
21.046
1.00
35.84
N

ATOM
519
CA
GLY
A1069
17.942
16.995
20.611
1.00
37.37
C

ATOM
520
C
GLY
A1069
17.855
18.092
19.561
1.00
38.51
C

ATOM
521
O
GLY
A1069
18.739
18.946
19.478
1.00
38.69
O

ATOM
522
N
ILE
A1070
16.801
18.088
18.752
1.00
39.34
N

ATOM
523
CA
ILE
A1070
16.688
19.108
17.722
1.00
40.39
C

ATOM
524
CB
ILE
A1070
16.453
18.482
16.329
1.00
40.56
C

ATOM
525
CG2
ILE
A1070
15.019
17.992
16.207
1.00
40.43
C

ATOM
526
CG1
ILE
A1070
16.784
19.515
15.245
1.00
40.90
C

ATOM
527
CD1
ILE
A1070
16.900
18.947
13.841
1.00
40.92
C

ATOM
528
C
ILE
A1070
15.616
20.147
18.019
1.00
41.07
C

ATOM
529
O
ILE
A1070
14.461
19.826
18.305
1.00
41.30
O

ATOM
530
N
SER
A1071
16.046
21.398
17.936
1.00
41.96
N

ATOM
531
CA
SER
A1071
15.247
22.588
18.201
1.00
42.87
C

ATOM
532
CB
SER
A1071
14.184
22.325
19.271
1.00
43.28
C

ATOM
533
OG
SER
A1071
14.779
21.937
20.496
1.00
44.51
O

ATOM
534
C
SER
A1071
16.314
23.521
18.753
1.00
43.09
C

ATOM
535
O
SER
A1071
16.254
24.741
18.585
1.00
43.47
O

ATOM
536
N
LYS
A1072
17.295
22.914
19.419
1.00
42.86
N

ATOM
537
CA
LYS
A1072
18.427
23.637
19.982
1.00
42.57
C

ATOM
538
CB
LYS
A1072
19.143
22.768
21.022
1.00
42.32
C

ATOM
539
CG
LYS
A1072
18.214
22.218
22.093
0.05
42.40
C

ATOM
540
CD
LYS
A1072
17.501
23.339
22.829
0.05
42.37
C

ATOM
541
CE
LYS
A1072
16.446
22.789
23.773
0.05
42.36
C

ATOM
542
NZ
LYS
A1072
15.708
23.878
24.472
0.05
42.34
N

ATOM
543
C
LYS
A1072
19.330
23.904
18.783
1.00
42.27
C

ATOM
544
O
LYS
A1072
20.222
24.752
18.814
1.00
42.17
O

ATOM
545
N
LEU
A1073
19.065
23.149
17.723
1.00
41.69
N

ATOM
546
CA
LEU
A1073
19.773
23.255
16.458
1.00
41.03
C

ATOM
547
CB
LEU
A1073
20.879
22.197
16.365
1.00
41.27
C

ATOM
548
CG
LEU
A1073
21.578
22.058
15.008
1.00
41.68
C

ATOM
549
CD1
LEU
A1073
23.024
21.623
15.193
1.00
41.49
C

ATOM
550
CD2
LEU
A1073
20.819
21.060
14.156
1.00
41.59
C

ATOM
551
C
LEU
A1073
18.696
23.006
15.408
1.00
39.74
C

ATOM
552
O
LEU
A1073
17.999
21.994
15.458
1.00
40.51
O

ATOM
553
N
GLY
A1074
18.550
23.937
14.473
1.00
37.90
N

ATOM
554
CA
GLY
A1074
17.532
23.795
13.452
1.00
34.96
C

ATOM
555
C
GLY
A1074
17.853
22.756
12.399
1.00
32.76
C

ATOM
556
O
GLY
A1074
18.968
22.237
12.331
1.00
31.86
O

ATOM
557
N
PHE
A1075
16.861
22.447
11.575
1.00
30.76
N

ATOM
558
CA
PHE
A1075
17.047
21.474
10.510
1.00
29.13
C

ATOM
559
CB
PHE
A1075
15.691
21.061
9.913
1.00
28.59
C

ATOM
560
CG
PHE
A1075
14.795
20.317
10.871
1.00
28.14
C

ATOM
561
CD1
PHE
A1075
14.129
20.990
11.893
1.00
28.80
C

ATOM
562
CD2
PHE
A1075
14.617
18.940
10.747
1.00
27.48
C

ATOM
563
CE1
PHE
A1075
13.294
20.301
12.780
1.00
28.53
C

ATOM
564
CE2
PHE
A1075
13.787
18.239
11.624
1.00
28.38
C

ATOM
565
CZ
PHE
A1075
13.123
18.921
12.644
1.00
28.31
C

ATOM
566
C
PHE
A1075
17.940
22.039
9.402
1.00
27.80
C

ATOM
567
O
PHE
A1075
18.556
21.280
8.655
1.00
27.44
O

ATOM
568
N
GLN
A1076
18.022
23.366
9.301
1.00
26.94
N

ATOM
569
CA
GLN
A1076
18.828
24.003
8.250
1.00
26.57
C

ATOM
570
CB
GLN
A1076
18.468
25.490
8.111
1.00
27.23
C

ATOM
571
CG
GLN
A1076
17.037
25.783
7.655
1.00
28.06
C

ATOM
572
CD
GLN
A1076
16.725
25.253
6.261
1.00
28.68
C

ATOM
573
OE1
GLN
A1076
17.504
25.432
5.321
1.00
28.59
O

ATOM
574
NE2
GLN
A1076
15.571
24.616
6.119
1.00
28.78
N

ATOM
575
C
GLN
A1076
20.341
23.880
8.435
1.00
26.18
C

ATOM
576
O
GLN
A1076
21.110
24.292
7.565
1.00
25.59
O

ATOM
577
N
ASP
A1077
20.774
23.318
9.558
1.00
25.77
N

ATOM
578
CA
ASP
A1077
22.204
23.158
9.808
1.00
25.68
C

ATOM
579
CB
ASP
A1077
22.498
23.399
11.287
1.00
28.73
C

ATOM
580
CG
ASP
A1077
23.952
23.697
11.542
1.00
30.84
C

ATOM
581
OD1
ASP
A1077
24.457
24.688
10.969
1.00
33.09
O

ATOM
582
OD2
ASP
A1077
24.590
22.947
12.309
1.00
32.53
O

ATOM
583
C
ASP
A1077
22.729
21.770
9.393
1.00
24.42
C

ATOM
584
O
ASP
A1077
23.928
21.487
9.516
1.00
23.80
O

ATOM
585
N
LEU
A1078
21.831
20.919
8.899
1.00
22.23
N

ATOM
586
CA
LEU
A1078
22.187
19.559
8.463
1.00
20.68
C

ATOM
587
CB
LEU
A1078
21.530
18.525
9.398
1.00
19.99
C

ATOM
588
CG
LEU
A1078
21.781
18.646
10.911
1.00
19.68
C

ATOM
589
CD1
LEU
A1078
20.853
17.703
11.686
1.00
19.87
C

ATOM
590
CD2
LEU
A1078
23.241
18.328
11.221
1.00
20.17
C

ATOM
591
C
LEU
A1078
21.706
19.326
7.022
1.00
20.16
C

ATOM
592
O
LEU
A1078
20.708
19.915
6.605
1.00
19.88
O

ATOM
593
N
GLU
A1079
22.408
18.474
6.265
1.00
19.89
N

ATOM
594
CA
GLU
A1079
22.021
18.165
4.875
1.00
18.83
C

ATOM
595
CB
GLU
A1079
22.690
19.153
3.905
1.00
19.73
C

ATOM
596
CG
GLU
A1079
22.172
19.085
2.459
1.00
21.03
C

ATOM
597
CD
GLU
A1079
22.914
20.028
1.510
1.00
22.47
C

ATOM
598
OE1
GLU
A1079
24.127
19.815
1.271
1.00
22.27
O

ATOM
599
OE2
GLU
A1079
22.279
20.982
1.002
1.00
23.12
O

ATOM
600
C
GLU
A1079
22.385
16.716
4.484
1.00
18.06
C

ATOM
601
O
GLU
A1079
23.492
16.242
4.778
1.00
17.37
O

ATOM
602
N
VAL
A1080
21.451
16.023
3.826
1.00
16.74
N

ATOM
603
CA
VAL
A1080
21.644
14.626
3.396
1.00
16.37
C

ATOM
604
CB
VAL
A1080
20.633
13.675
4.138
1.00
16.24
C

ATOM
605
CG1
VAL
A1080
20.859
12.217
3.738
1.00
16.31
C

ATOM
606
CG2
VAL
A1080
20.776
13.832
5.654
1.00
16.73
C

ATOM
607
C
VAL
A1080
21.454
14.439
1.868
1.00
16.11
C

ATOM
608
O
VAL
A1080
20.356
14.635
1.357
1.00
16.59
O

ATOM
609
N
LEU
A1081
22.519
14.060
1.155
1.00
16.23
N

ATOM
610
CA
LEU
A1081
22.473
13.830
−0.303
1.00
16.11
C

ATOM
611
CB
LEU
A1081
23.488
14.749
−1.017
1.00
16.03
C

ATOM
612
CG
LEU
A1081
23.400
16.265
−0.767
1.00
17.13
C

ATOM
613
CD1
LEU
A1081
24.565
16.983
−1.464
1.00
16.85
C

ATOM
614
CD2
LEU
A1081
22.064
16.798
−1.283
1.00
17.61
C

ATOM
615
C
LEU
A1081
22.790
12.350
−0.624
1.00
16.47
C

ATOM
616
O
LEU
A1081
22.881
11.530
0.285
1.00
15.85
O

ATOM
617
N
ASN
A1082
22.954
12.004
−1.906
1.00
17.23
N

ATOM
618
CA
ASN
A1082
23.266
10.615
−2.299
1.00
18.16
C

ATOM
619
CB
ASN
A1082
22.169
10.064
−3.227
1.00
19.47
C

ATOM
620
CG
ASN
A1082
20.853
9.800
−2.496
1.00
20.37
C

ATOM
621
OD1
ASN
A1082
20.701
8.793
−1.806
1.00
23.12
O

ATOM
622
ND2
ASN
A1082
19.908
10.709
−2.637
1.00
21.16
N

ATOM
623
C
ASN
A1082
24.633
10.540
−3.004
1.00
18.65
C

ATOM
624
O
ASN
A1082
24.894
11.311
−3.936
1.00
18.53
O

ATOM
625
N
ASN
A1083
25.501
9.621
−2.567
1.00
18.47
N

ATOM
626
CA
ASN
A1083
26.840
9.496
−3.160
1.00
19.58
C

ATOM
627
CB
ASN
A1083
27.823
8.831
−2.172
1.00
19.14
C

ATOM
628
CG
ASN
A1083
27.525
7.354
−1.898
1.00
19.47
C

ATOM
629
OD1
ASN
A1083
28.000
6.806
−0.896
1.00
21.52
O

ATOM
630
ND2
ASN
A1083
26.774
6.705
−2.778
1.00
18.08
N

ATOM
631
C
ASN
A1083
26.879
8.801
−4.522
1.00
21.02
C

ATOM
632
O
ASN
A1083
25.835
8.408
−5.053
1.00
20.46
O

ATOM
633
N
GLU
A1084
28.073
8.655
−5.095
1.00
22.56
N

ATOM
634
CA
GLU
A1084
28.183
8.048
−6.422
1.00
25.48
C

ATOM
635
CB
GLU
A1084
29.606
8.243
−6.993
1.00
26.01
C

ATOM
636
CG
GLU
A1084
30.704
7.346
−6.452
1.00
27.48
C

ATOM
637
CD
GLU
A1084
32.055
7.621
−7.127
1.00
28.81
C

ATOM
638
OE1
GLU
A1084
32.087
7.807
−8.365
1.00
28.44
O

ATOM
639
OE2
GLU
A1084
33.085
7.644
−6.424
1.00
29.66
O

ATOM
640
C
GLU
A1084
27.747
6.583
−6.523
1.00
26.10
C

ATOM
641
O
GLU
A1084
27.675
6.030
−7.618
1.00
26.96
O

ATOM
642
N
ARG
A1085
27.446
5.958
−5.390
1.00
26.87
N

ATOM
643
CA
ARG
A1085
26.976
4.571
−5.381
1.00
27.01
C

ATOM
644
CB
ARG
A1085
27.697
3.761
−4.302
1.00
29.89
C

ATOM
645
CG
ARG
A1085
29.210
3.670
−4.479
1.00
33.27
C

ATOM
646
CD
ARG
A1085
29.603
2.687
−5.570
1.00
35.91
C

ATOM
647
NE
ARG
A1085
31.041
2.724
−5.834
1.00
37.82
N

ATOM
648
CZ
ARG
A1085
31.696
1.814
−6.549
1.00
39.02
C

ATOM
649
NH1
ARG
A1085
33.005
1.929
−6.739
1.00
39.21
N

ATOM
650
NH2
ARG
A1085
31.043
0.782
−7.067
1.00
39.98
N

ATOM
651
C
ARG
A1085
25.467
4.573
−5.097
1.00
26.06
C

ATOM
652
O
ARG
A1085
24.830
3.515
−5.033
1.00
26.15
O

ATOM
653
N
GLY
A1086
24.911
5.768
−4.907
1.00
24.38
N

ATOM
654
CA
GLY
A1086
23.485
5.910
−4.649
1.00
22.84
C

ATOM
655
C
GLY
A1086
22.989
5.874
−3.207
1.00
21.70
C

ATOM
656
O
GLY
A1086
21.780
5.910
−2.980
1.00
21.52
O

ATOM
657
N
ALA
A1087
23.896
5.813
−2.234
1.00
20.27
N

ATOM
658
CA
ALA
A1087
23.506
5.757
−0.819
1.00
19.12
C

ATOM
659
CB
ALA
A1087
24.452
4.825
−0.065
1.00
19.31
C

ATOM
660
C
ALA
A1087
23.468
7.126
−0.123
1.00
18.28
C

ATOM
661
O
ALA
A1087
24.293
8.001
−0.400
1.00
17.46
O

ATOM
662
N
PRO
A1088
22.511
7.322
0.807
1.00
17.16
N

ATOM
663
CD
PRO
A1088
21.424
6.400
1.186
1.00
17.79
C

ATOM
664
CA
PRO
A1088
22.398
8.598
1.529
1.00
16.21
C

ATOM
665
CB
PRO
A1088
21.053
8.469
2.263
1.00
16.47
C

ATOM
666
CG
PRO
A1088
20.938
6.995
2.507
1.00
17.39
C

ATOM
667
C
PRO
A1088
23.579
8.828
2.481
1.00
15.55
C

ATOM
668
O
PRO
A1088
24.084
7.876
3.082
1.00
14.47
O

ATOM
669
N
TYR
A1089
24.018
10.085
2.597
1.00
14.68
N

ATOM
670
CA
TYR
A1089
25.148
10.453
3.466
1.00
15.17
C

ATOM
671
CB
TYR
A1089
26.478
10.205
2.728
1.00
15.96
C

ATOM
672
CG
TYR
A1089
26.834
11.280
1.707
1.00
17.14
C

ATOM
673
CD1
TYR
A1089
27.815
12.240
1.980
1.00
17.14
C

ATOM
674
CE1
TYR
A1089
28.136
13.243
1.042
1.00
17.71
C

ATOM
675
CD2
TYR
A1089
26.180
11.345
0.476
1.00
17.70
C

ATOM
676
CE2
TYR
A1089
26.490
12.342
−0.470
1.00
18.23
C

ATOM
677
CZ
TYR
A1089
27.467
13.286
−0.180
1.00
18.79
C

ATOM
678
OH
TYR
A1089
27.769
14.272
−1.110
1.00
18.83
O

ATOM
679
C
TYR
A1089
25.068
11.931
3.886
1.00
15.23
C

ATOM
680
O
TYR
A1089
24.480
12.749
3.172
1.00
14.55
O

ATOM
681
N
PHE
A1090
25.664
12.276
5.030
1.00
15.03
N

ATOM
682
CA
PHE
A1090
25.646
13.668
5.502
1.00
16.07
C

ATOM
683
CB
PHE
A1090
25.891
13.743
7.023
1.00
15.87
C

ATOM
684
CG
PHE
A1090
24.662
13.469
7.864
1.00
15.54
C

ATOM
685
CD1
PHE
A1090
24.359
12.176
8.287
1.00
14.81
C

ATOM
686
CD2
PHE
A1090
23.798
14.512
8.213
1.00
15.28
C

ATOM
687
CE1
PHE
A1090
23.207
11.920
9.048
1.00
15.40
C

ATOM
688
CE2
PHE
A1090
22.643
14.272
8.973
1.00
16.17
C

ATOM
689
CZ
PHE
A1090
22.347
12.971
9.390
1.00
15.25
C

ATOM
690
C
PHE
A1090
26.694
14.553
4.800
1.00
16.94
C

ATOM
691
O
PHE
A1090
27.898
14.378
5.005
1.00
15.67
O

ATOM
692
N
SER
A1091
26.233
15.499
3.983
1.00
18.05
N

ATOM
693
CA
SER
A1091
27.135
16.421
3.285
1.00
20.04
C

ATOM
694
CB
SER
A1091
26.528
16.864
1.949
1.00
20.26
C

ATOM
695
OG
SER
A1091
25.196
17.305
2.106
1.00
21.03
O

ATOM
696
C
SER
A1091
27.456
17.653
4.143
1.00
20.79
C

ATOM
697
O
SER
A1091
28.445
18.349
3.890
1.00
21.71
O

ATOM
698
N
GLN
A1092
26.606
17.930
5.133
1.00
20.94
N

ATOM
699
CA
GLN
A1092
26.810
19.049
6.062
1.00
21.39
C

ATOM
700
CB
GLN
A1092
25.958
20.265
5.665
1.00
23.27
C

ATOM
701
CG
GLN
A1092
26.267
20.898
4.305
1.00
25.76
C

ATOM
702
CD
GLN
A1092
27.623
21.589
4.244
1.00
27.71
C

ATOM
703
OE1
GLN
A1092
28.044
22.248
5.197
1.00
29.37
O

ATOM
704
NE2
GLN
A1092
28.301
21.461
3.106
1.00
28.25
N

ATOM
705
C
GLN
A1092
26.416
18.619
7.489
1.00
20.95
C

ATOM
706
O
GLN
A1092
25.340
18.064
7.689
1.00
20.12
O

ATOM
707
N
ALA
A1093
27.290
18.868
8.466
1.00
20.33
N

ATOM
708
CA
ALA
A1093
27.030
18.533
9.874
1.00
20.84
C

ATOM
709
CB
ALA
A1093
26.874
17.013
10.046
1.00
20.16
C

ATOM
710
C
ALA
A1093
28.179
19.041
10.757
1.00
21.48
C

ATOM
711
O
ALA
A1093
29.319
19.128
10.304
1.00
21.44
O

ATOM
712
N
PRO
A1094
27.890
19.389
12.027
1.00
22.28
N

ATOM
713
CD
PRO
A1094
26.539
19.598
12.585
1.00
22.57
C

ATOM
714
CA
PRO
A1094
28.921
19.887
12.954
1.00
22.63
C

ATOM
715
CB
PRO
A1094
28.125
20.803
13.876
1.00
22.88
C

ATOM
716
CG
PRO
A1094
26.828
20.043
14.020
1.00
23.37
C

ATOM
717
C
PRO
A1094
29.678
18.791
13.731
1.00
23.05
C

ATOM
718
O
PRO
A1094
29.571
18.700
14.959
1.00
23.97
O

ATOM
719
N
PHE
A1095
30.446
17.976
13.009
1.00
22.89
N

ATOM
720
CA
PHE
A1095
31.232
16.883
13.590
1.00
22.99
C

ATOM
721
CB
PHE
A1095
30.341
15.639
13.767
1.00
22.67
C

ATOM
722
CG
PHE
A1095
31.067
14.436
14.307
1.00
22.55
C

ATOM
723
CD1
PHE
A1095
31.374
13.360
13.474
1.00
22.34
C

ATOM
724
CD2
PHE
A1095
31.462
14.385
15.641
1.00
22.13
C

ATOM
725
CE1
PHE
A1095
32.068
12.250
13.963
1.00
22.27
C

ATOM
726
CE2
PHE
A1095
32.156
13.281
16.143
1.00
22.71
C

ATOM
727
CZ
PHE
A1095
32.461
12.209
15.300
1.00
22.51
C

ATOM
728
C
PHE
A1095
32.406
16.592
12.639
1.00
23.22
C

ATOM
729
O
PHE
A1095
32.221
16.574
11.426
1.00
23.38
O

ATOM
730
N
SER
A1096
33.602
16.353
13.183
1.00
23.37
N

ATOM
731
CA
SER
A1096
34.792
16.122
12.347
1.00
23.62
C

ATOM
732
CB
SER
A1096
35.993
16.858
12.955
1.00
24.11
C

ATOM
733
OG
SER
A1096
36.331
16.317
14.223
1.00
26.37
O

ATOM
734
C
SER
A1096
35.233
14.691
12.000
1.00
23.23
C

ATOM
735
O
SER
A1096
36.094
14.510
11.125
1.00
22.88
O

ATOM
736
N
GLY
A1097
34.670
13.686
12.669
1.00
22.73
N

ATOM
737
CA
GLY
A1097
35.043
12.304
12.391
1.00
21.96
C

ATOM
738
C
GLY
A1097
34.138
11.589
11.393
1.00
21.41
C

ATOM
739
O
GLY
A1097
33.518
12.232
10.555
1.00
21.73
O

ATOM
740
N
LYS
A1098
34.066
10.259
11.479
1.00
20.96
N

ATOM
741
CA
LYS
A1098
33.228
9.456
10.578
1.00
20.77
C

ATOM
742
CB
LYS
A1098
33.822
8.052
10.409
1.00
22.35
C

ATOM
743
CG
LYS
A1098
35.205
8.017
9.774
1.00
25.18
C

ATOM
744
CD
LYS
A1098
35.630
6.587
9.449
1.00
26.26
C

ATOM
745
CE
LYS
A1098
36.996
6.553
8.772
1.00
28.39
C

ATOM
746
NZ
LYS
A1098
37.332
5.194
8.258
1.00
28.94
N

ATOM
747
C
LYS
A1098
31.770
9.313
11.046
1.00
19.74
C

ATOM
748
O
LYS
A1098
31.517
9.064
12.224
1.00
19.90
O

ATOM
749
N
ILE
A1099
30.826
9.461
10.113
1.00
18.27
N

ATOM
750
CA
ILE
A1099
29.393
9.340
10.400
1.00
17.38
C

ATOM
751
CB
ILE
A1099
28.622
10.638
9.997
1.00
17.39
C

ATOM
752
CG2
ILE
A1099
27.124
10.465
10.284
1.00
16.62
C

ATOM
753
CG1
ILE
A1099
29.171
11.849
10.761
1.00
15.42
C

ATOM
754
CD1
ILE
A1099
28.790
13.196
10.165
1.00
15.80
C

ATOM
755
C
ILE
A1099
28.777
8.164
9.607
1.00
17.23
C

ATOM
756
O
ILE
A1099
28.697
8.226
8.381
1.00
18.55
O

ATOM
757
N
TRP
A1100
28.356
7.102
10.298
1.00
16.06
N

ATOM
758
CA
TRP
A1100
27.733
5.939
9.641
1.00
15.73
C

ATOM
759
CB
TRP
A1100
28.163
4.638
10.347
1.00
15.81
C

ATOM
760
CG
TRP
A1100
29.665
4.374
10.328
1.00
16.55
C

ATOM
761
CD2
TRP
A1100
30.415
3.750
9.274
1.00
16.48
C

ATOM
762
CE2
TRP
A1100
31.774
3.736
9.676
1.00
17.61
C

ATOM
763
CE3
TRP
A1100
30.071
3.199
8.030
1.00
17.03
C

ATOM
764
CD1
TRP
A1100
30.575
4.704
11.300
1.00
17.00
C

ATOM
765
NE1
TRP
A1100
31.844
4.322
10.916
1.00
16.91
N

ATOM
766
CZ2
TRP
A1100
32.792
3.191
8.873
1.00
17.99
C

ATOM
767
CZ3
TRP
A1100
31.083
2.654
7.230
1.00
18.05
C

ATOM
768
CH2
TRP
A1100
32.430
2.656
7.659
1.00
17.40
C

ATOM
769
C
TRP
A1100
26.190
6.079
9.705
1.00
15.39
C

ATOM
770
O
TRP
A1100
25.638
6.160
10.801
1.00
15.11
O

ATOM
771
N
LEU
A1101
25.517
6.100
8.545
1.00
14.54
N

ATOM
772
CA
LEU
A1101
24.045
6.260
8.448
1.00
14.10
C

ATOM
773
CB
LEU
A1101
23.705
7.658
7.883
1.00
14.83
C

ATOM
774
CG
LEU
A1101
22.267
7.893
7.366
1.00
15.12
C

ATOM
775
CD1
LEU
A1101
21.330
8.116
8.541
1.00
15.77
C

ATOM
776
CD2
LEU
A1101
22.216
9.105
6.427
1.00
15.58
C

ATOM
777
C
LEU
A1101
23.318
5.214
7.576
1.00
13.98
C

ATOM
778
O
LEU
A1101
23.847
4.789
6.537
1.00
13.24
O

ATOM
779
N
SER
A1102
22.109
4.808
7.996
1.00
13.49
N

ATOM
780
CA
SER
A1102
21.278
3.857
7.226
1.00
14.16
C

ATOM
781
CB
SER
A1102
21.525
2.411
7.683
1.00
14.32
C

ATOM
782
OG
SER
A1102
20.947
1.471
6.781
1.00
14.30
O

ATOM
783
C
SER
A1102
19.777
4.190
7.363
1.00
14.45
C

ATOM
784
O
SER
A1102
19.311
4.519
8.464
1.00
13.54
O

ATOM
785
N
ILE
A1103
19.029
4.089
6.254
1.00
14.69
N

ATOM
786
CA
ILE
A1103
17.575
4.387
6.231
1.00
15.31
C

ATOM
787
CB
ILE
A1103
17.282
5.709
5.454
1.00
15.58
C

ATOM
788
CG2
ILE
A1103
15.783
6.027
5.508
1.00
15.76
C

ATOM
789
CG1
ILE
A1103
18.085
6.875
6.041
1.00
15.76
C

ATOM
790
CD1
ILE
A1103
17.838
8.216
5.317
1.00
17.30
C

ATOM
791
C
ILE
A1103
16.766
3.263
5.541
1.00
15.22
C

ATOM
792
O
ILE
A1103
17.249
2.668
4.575
1.00
16.46
O

ATOM
793
N
SER
A1104
15.550
2.977
6.023
1.00
15.94
N

ATOM
794
CA
SER
A1104
14.686
1.926
5.429
1.00
17.08
C

ATOM
795
CB
SER
A1104
14.993
0.564
6.085
1.00
17.67
C

ATOM
796
OG
SER
A1104
14.251
−0.486
5.476
1.00
17.18
O

ATOM
797
C
SER
A1104
13.174
2.248
5.574
1.00
17.46
C

ATOM
798
O
SER
A1104
12.784
2.982
6.483
1.00
16.57
O

ATOM
799
N
HIS
A1105
12.323
1.699
4.698
1.00
18.34
N

ATOM
800
CA
HIS
A1105
10.877
1.989
4.776
1.00
19.13
C

ATOM
801
CB
HIS
A1105
10.572
3.300
4.041
1.00
20.61
C

ATOM
802
CG
HIS
A1105
10.702
3.188
2.551
1.00
21.51
C

ATOM
803
CD2
HIS
A1105
9.799
2.840
1.601
1.00
22.68
C

ATOM
804
ND1
HIS
A1105
11.906
3.333
1.896
1.00
23.14
N

ATOM
805
CE1
HIS
A1105
11.742
3.075
0.610
1.00
23.36
C

ATOM
806
NE2
HIS
A1105
10.473
2.772
0.405
1.00
22.97
N

ATOM
807
C
HIS
A1105
9.918
0.933
4.192
1.00
19.69
C

ATOM
808
O
HIS
A1105
10.324
0.073
3.405
1.00
19.77
O

ATOM
809
N
THR
A1106
8.640
1.034
4.577
1.00
20.07
N

ATOM
810
CA
THR
A1106
7.564
0.171
4.056
1.00
20.65
C

ATOM
811
CB
THR
A1106
6.941
−0.769
5.131
1.00
20.02
C

ATOM
812
OG1
THR
A1106
6.198
0.004
6.085
1.00
19.30
O

ATOM
813
CG2
THR
A1106
8.029
−1.578
5.852
1.00
19.90
C

ATOM
814
C
THR
A1106
6.470
1.143
3.587
1.00
22.48
C

ATOM
815
O
THR
A1106
6.720
2.347
3.476
1.00
21.87
O

ATOM
816
N
ASP
A1107
5.262
0.652
3.315
1.00
23.59
N

ATOM
817
CA
ASP
A1107
4.214
1.569
2.875
1.00
25.20
C

ATOM
818
CB
ASP
A1107
3.146
0.831
2.052
1.00
27.87
C

ATOM
819
CG
ASP
A1107
2.302
−0.116
2.886
1.00
29.94
C

ATOM
820
OD1
ASP
A1107
1.331
−0.672
2.332
1.00
32.47
O

ATOM
821
OD2
ASP
A1107
2.601
−0.314
4.086
1.00
32.30
O

ATOM
822
C
ASP
A1107
3.549
2.322
4.027
1.00
25.08
C

ATOM
823
O
ASP
A1107
2.673
3.156
3.791
1.00
25.52
O

ATOM
824
N
GLN
A1108
3.965
2.042
5.264
1.00
24.18
N

ATOM
825
CA
GLN
A1108
3.380
2.703
6.435
1.00
23.78
C

ATOM
826
CB
GLN
A1108
2.533
1.715
7.251
1.00
25.19
C

ATOM
827
CG
GLN
A1108
1.283
1.211
6.550
1.00
28.60
C

ATOM
828
CD
GLN
A1108
0.375
0.426
7.479
1.00
30.45
C

ATOM
829
OE1
GLN
A1108
0.768
−0.606
8.026
1.00
31.65
O

ATOM
830
NE2
GLN
A1108
−0.847
0.918
7.670
1.00
31.23
N

ATOM
831
C
GLN
A1108
4.361
3.391
7.390
1.00
22.77
C

ATOM
832
O
GLN
A1108
3.966
4.334
8.081
1.00
22.34
O

ATOM
833
N
PHE
A1109
5.616
2.926
7.441
1.00
21.34
N

ATOM
834
CA
PHE
A1109
6.633
3.513
8.342
1.00
20.67
C

ATOM
835
CB
PHE
A1109
6.888
2.605
9.567
1.00
21.50
C

ATOM
836
CG
PHE
A1109
5.654
2.213
10.328
1.00
22.53
C

ATOM
837
CD1
PHE
A1109
4.947
1.059
9.989
1.00
23.72
C

ATOM
838
CD2
PHE
A1109
5.212
2.978
11.403
1.00
23.05
C

ATOM
839
CE1
PHE
A1109
3.816
0.673
10.715
1.00
24.14
C

ATOM
840
CE2
PHE
A1109
4.082
2.601
12.135
1.00
24.05
C

ATOM
841
CZ
PHE
A1109
3.383
1.445
11.789
1.00
23.64
C

ATOM
842
C
PHE
A1109
8.015
3.755
7.705
1.00
19.29
C

ATOM
843
O
PHE
A1109
8.333
3.199
6.654
1.00
19.32
O

ATOM
844
N
VAL
A1110
8.830
4.582
8.368
1.00
18.27
N

ATOM
845
CA
VAL
A1110
10.218
4.864
7.955
1.00
16.90
C

ATOM
846
CB
VAL
A1110
10.368
6.279
7.299
1.00
17.79
C

ATOM
847
CG1
VAL
A1110
10.126
7.377
8.325
1.00
17.09
C

ATOM
848
CG2
VAL
A1110
11.754
6.428
6.681
1.00
17.98
C

ATOM
849
C
VAL
A1110
11.100
4.796
9.224
1.00
16.47
C

ATOM
850
O
VAL
A1110
10.655
5.214
10.300
1.00
15.21
O

ATOM
851
N
THR
A1111
12.323
4.260
9.097
1.00
15.44
N

ATOM
852
CA
THR
A1111
13.271
4.126
10.225
1.00
16.10
C

ATOM
853
CB
THR
A1111
13.369
2.646
10.736
1.00
16.89
C

ATOM
854
OG1
THR
A1111
13.775
1.775
9.667
1.00
18.14
O

ATOM
855
CG2
THR
A1111
12.038
2.180
11.274
1.00
18.11
C

ATOM
856
C
THR
A1111
14.692
4.582
9.860
1.00
15.27
C

ATOM
857
O
THR
A1111
15.082
4.502
8.690
1.00
14.78
O

ATOM
858
N
ALA
A1112
15.462
5.041
10.858
1.00
14.23
N

ATOM
859
CA
ALA
A1112
16.845
5.505
10.639
1.00
13.59
C

ATOM
860
CB
ALA
A1112
16.855
7.001
10.293
1.00
12.71
C

ATOM
861
C
ALA
A1112
17.764
5.255
11.843
1.00
12.99
C

ATOM
862
O
ALA
A1112
17.310
5.303
12.993
1.00
12.81
O

ATOM
863
N
SER
A1113
19.055
5.032
11.570
1.00
12.47
N

ATOM
864
CA
SER
A1113
20.064
4.761
12.610
1.00
13.04
C

ATOM
865
CB
SER
A1113
20.256
3.238
12.736
1.00
13.53
C

ATOM
866
OG
SER
A1113
21.244
2.893
13.698
1.00
13.09
O

ATOM
867
C
SER
A1113
21.427
5.444
12.318
1.00
13.78
C

ATOM
868
O
SER
A1113
21.901
5.419
11.180
1.00
13.46
O

ATOM
869
N
VAL
A1114
22.048
6.039
13.348
1.00
13.44
N

ATOM
870
CA
VAL
A1114
23.349
6.735
13.208
1.00
12.85
C

ATOM
871
CB
VAL
A1114
23.151
8.288
13.286
1.00
12.88
C

ATOM
872
CG1
VAL
A1114
24.496
9.005
13.384
1.00
12.82
C

ATOM
873
CG2
VAL
A1114
22.384
8.794
12.056
1.00
13.36
C

ATOM
874
C
VAL
A1114
24.393
6.328
14.278
1.00
12.70
C

ATOM
875
O
VAL
A1114
24.045
6.140
15.444
1.00
12.48
O

ATOM
876
N
ILE
A1115
25.662
6.183
13.873
1.00
13.61
N

ATOM
877
CA
ILE
A1115
26.765
5.846
14.800
1.00
13.97
C

ATOM
878
CB
ILE
A1115
27.291
4.399
14.621
1.00
14.70
C

ATOM
879
CG2
ILE
A1115
28.393
4.124
15.653
1.00
15.55
C

ATOM
880
CG1
ILE
A1115
26.163
3.377
14.800
1.00
14.56
C

ATOM
881
CD1
ILE
A1115
26.580
1.948
14.433
1.00
14.04
C

ATOM
882
C
ILE
A1115
27.940
6.786
14.502
1.00
15.39
C

ATOM
883
O
ILE
A1115
28.372
6.879
13.348
1.00
14.30
O

ATOM
884
N
LEU
A1116
28.456
7.465
15.537
1.00
15.93
N

ATOM
885
CA
LEU
A1116
29.574
8.412
15.397
1.00
16.40
C

ATOM
886
CB
LEU
A1116
29.300
9.680
16.235
1.00
16.45
C

ATOM
887
CG
LEU
A1116
27.972
10.439
16.051
1.00
15.86
C

ATOM
888
CD1
LEU
A1116
27.935
11.642
16.994
1.00
16.47
C

ATOM
889
CD2
LEU
A1116
27.816
10.888
14.601
1.00
16.74
C

ATOM
890
C
LEU
A1116
30.906
7.778
15.839
1.00
17.18
C

ATOM
891
O
LEU
A1116
30.973
7.125
16.880
1.00
15.82
O

ATOM
892
N
GLU
A1117
31.970
8.002
15.064
1.00
18.58
N

ATOM
893
CA
GLU
A1117
33.278
7.414
15.362
1.00
21.21
C

ATOM
894
CB
GLU
A1117
33.404
6.068
14.615
1.00
21.29
C

ATOM
895
CG
GLU
A1117
34.793
5.403
14.659
1.00
21.49
C

ATOM
896
CD
GLU
A1117
34.930
4.238
13.675
1.00
21.22
C

ATOM
897
OE1
GLU
A1117
34.538
4.390
12.500
1.00
20.57
O

ATOM
898
OE2
GLU
A1117
35.446
3.166
14.064
1.00
22.68
O

ATOM
899
C
GLU
A1117
34.487
8.290
15.001
1.00
23.59
C

ATOM
900
O
GLU
A1117
34.440
9.108
14.083
1.00
22.02
O

ATOM
901
N
GLU
A1118
35.576
8.115
15.740
1.00
27.34
N

ATOM
902
CA
GLU
A1118
36.801
8.839
15.429
1.00
31.25
C

ATOM
903
CB
GLU
A1118
36.859
10.184
16.157
1.00
33.00
C

ATOM
904
CG
GLU
A1118
36.747
10.131
17.651
1.00
35.45
C

ATOM
905
CD
GLU
A1118
37.042
11.480
18.269
1.00
37.44
C

ATOM
906
OE1
GLU
A1118
36.389
12.470
17.874
1.00
38.60
O

ATOM
907
OE2
GLU
A1118
37.932
11.551
19.145
1.00
39.01
O

ATOM
908
C
GLU
A1118
38.005
7.964
15.764
1.00
33.04
C

ATOM
909
O
GLU
A1118
38.074
7.358
16.835
1.00
33.37
O

ATOM
910
N
ASN
A1119
38.928
7.875
14.809
1.00
34.80
N

ATOM
911
CA
ASN
A1119
40.132
7.063
14.945
1.00
36.61
C

ATOM
912
CB
ASN
A1119
40.203
6.015
13.823
1.00
37.32
C

ATOM
913
CG
ASN
A1119
38.862
5.356
13.537
1.00
38.38
C

ATOM
914
OD1
ASN
A1119
38.258
4.731
14.409
1.00
39.30
O

ATOM
915
ND2
ASN
A1119
38.393
5.492
12.302
1.00
38.79
N

ATOM
916
C
ASN
A1119
41.354
7.972
14.845
1.00
37.29
C

ATOM
917
O
ASN
A1119
42.132
7.795
13.885
1.00
37.98
O

ATOM
918
OXT
ASN
A1119
41.513
8.857
15.710
1.00
38.37
O

TER
919

ASN
A1119

ATOM
920
CB
MET
B2003
37.510
−3.957
21.175
1.00
28.67
C

ATOM
921
CG
MET
B2003
37.230
−5.443
21.092
1.00
31.61
C

ATOM
922
SD
MET
B2003
38.381
−6.420
22.089
1.00
36.00
S

ATOM
923
CE
MET
B2003
37.478
−6.538
23.632
1.00
34.64
C

ATOM
924
C
MET
B2003
35.111
−3.318
20.851
1.00
24.52
C

ATOM
925
O
MET
B2003
34.821
−3.223
22.044
1.00
23.78
O

ATOM
926
N
MET
B2003
36.911
−1.645
20.536
1.00
26.75
N

ATOM
927
CA
MET
B2003
36.543
−3.080
20.373
1.00
26.43
C

ATOM
928
N
ILE
B2004
34.220
−3.611
19.907
1.00
23.33
N

ATOM
929
CA
ILE
B2004
32.814
−3.877
20.214
1.00
21.77
C

ATOM
930
CB
ILE
B2004
31.948
−3.818
18.923
1.00
22.25
C

ATOM
931
CG2
ILE
B2004
30.528
−4.317
19.214
1.00
21.40
C

ATOM
932
CG1
ILE
B2004
31.936
−2.387
18.370
1.00
22.04
C

ATOM
933
CD1
ILE
B2004
31.248
−2.242
17.013
1.00
23.31
C

ATOM
934
C
ILE
B2004
32.688
−5.268
20.837
1.00
21.10
C

ATOM
935
O
ILE
B2004
33.423
−6.190
20.463
1.00
21.53
O

ATOM
936
N
VAL
B2005
31.774
−5.423
21.793
1.00
19.59
N

ATOM
937
CA
VAL
B2005
31.577
−6.725
22.423
1.00
18.29
C

ATOM
938
CB
VAL
B2005
32.240
−6.783
23.834
1.00
18.82
C

ATOM
939
CG1
VAL
B2005
33.741
−6.518
23.712
1.00
18.55
C

ATOM
940
CG2
VAL
B2005
31.596
−5.776
24.778
1.00
19.42
C

ATOM
941
C
VAL
B2005
30.108
−7.189
22.520
1.00
17.17
C

ATOM
942
O
VAL
B2005
29.827
−8.180
23.193
1.00
16.88
O

ATOM
943
N
GLY
B2006
29.190
−6.493
21.838
1.00
15.24
N

ATOM
944
CA
GLY
B2006
27.776
−6.881
21.849
1.00
14.41
C

ATOM
945
C
GLY
B2006
26.800
−5.899
21.191
1.00
13.76
C

ATOM
946
O
GLY
B2006
27.067
−4.703
21.177
1.00
12.82
O

ATOM
947
N
HIS
B2007
25.667
−6.388
20.664
1.00
13.79
N

ATOM
948
CA
HIS
B2007
24.656
−5.521
20.015
1.00
13.97
C

ATOM
949
CB
HIS
B2007
25.046
−5.296
18.534
1.00
13.17
C

ATOM
950
CG
HIS
B2007
24.110
−4.400
17.767
1.00
13.29
C

ATOM
951
CD2
HIS
B2007
23.648
−4.481
16.494
1.00
13.60
C

ATOM
952
ND1
HIS
B2007
23.602
−3.224
18.281
1.00
14.70
N

ATOM
953
CE1
HIS
B2007
22.871
−2.619
17.357
1.00
15.43
C

ATOM
954
NE2
HIS
B2007
22.884
−3.360
16.262
1.00
13.92
N

ATOM
955
C
HIS
B2007
23.227
−6.108
20.104
1.00
13.36
C

ATOM
956
O
HIS
B2007
23.024
−7.293
19.817
1.00
13.30
O

ATOM
957
N
GLY
B2008
22.249
−5.286
20.504
1.00
13.56
N

ATOM
958
CA
GLY
B2008
20.870
−5.758
20.603
1.00
13.42
C

ATOM
959
C
GLY
B2008
19.760
−4.724
20.407
1.00
13.33
C

ATOM
960
O
GLY
B2008
19.921
−3.566
20.786
1.00
13.08
O

ATOM
961
N
ILE
B2009
18.630
−5.143
19.827
1.00
13.48
N

ATOM
962
CA
ILE
B2009
17.476
−4.253
19.601
1.00
13.81
C

ATOM
963
CB
ILE
B2009
17.327
−3.864
18.086
1.00
14.27
C

ATOM
964
CG2
ILE
B2009
18.651
−3.276
17.549
1.00
14.33
C

ATOM
965
CG1
ILE
B2009
16.931
−5.091
17.257
1.00
14.49
C

ATOM
966
CD1
ILE
B2009
16.666
−4.783
15.777
1.00
15.47
C

ATOM
967
C
ILE
B2009
16.155
−4.916
20.066
1.00
14.94
C

ATOM
968
O
ILE
B2009
16.090
−6.145
20.190
1.00
14.51
O

ATOM
969
N
ASP
B2010
15.115
−4.111
20.318
1.00
15.66
N

ATOM
970
CA
ASP
B2010
13.806
−4.644
20.746
1.00
17.47
C

ATOM
971
CB
ASP
B2010
13.820
−4.974
22.250
1.00
18.72
C

ATOM
972
CG
ASP
B2010
12.474
−5.527
22.757
1.00
19.74
C

ATOM
973
OD1
ASP
B2010
11.670
−4.747
23.311
1.00
21.08
O

ATOM
974
OD2
ASP
B2010
12.214
−6.740
22.593
1.00
19.62
O

ATOM
975
C
ASP
B2010
12.623
−3.709
20.447
1.00
18.58
C

ATOM
976
O
ASP
B2010
12.769
−2.483
20.472
1.00
17.47
O

ATOM
977
N
ILE
B2011
11.465
−4.304
20.148
1.00
19.97
N

ATOM
978
CA
ILE
B2011
10.224
−3.558
19.874
1.00
22.59
C

ATOM
979
CB
ILE
B2011
9.666
−3.817
18.459
1.00
23.44
C

ATOM
980
CG2
ILE
B2011
8.532
−2.831
18.167
1.00
24.17
C

ATOM
981
CG1
ILE
B2011
10.752
−3.688
17.411
1.00
23.83
C

ATOM
982
CD1
ILE
B2011
10.368
−4.350
16.110
1.00
24.58
C

ATOM
983
C
ILE
B2011
9.134
−4.066
20.833
1.00
23.70
C

ATOM
984
O
ILE
B2011
9.039
−5.271
21.078
1.00
23.87
O

ATOM
985
N
GLU
B2012
8.305
−3.166
21.359
1.00
24.36
N

ATOM
986
CA
GLU
B2012
7.232
−3.569
22.270
1.00
25.44
C

ATOM
987
CB
GLU
B2012
7.626
−3.297
23.723
1.00
26.83
C

ATOM
988
CG
GLU
B2012
6.659
−3.896
24.741
1.00
29.96
C

ATOM
989
CD
GLU
B2012
6.806
−5.408
24.892
1.00
32.18
C

ATOM
990
OE1
GLU
B2012
7.094
−6.098
23.888
1.00
33.01
O

ATOM
991
OE2
GLU
B2012
6.617
−5.908
26.024
1.00
33.41
O

ATOM
992
C
GLU
B2012
5.915
−2.848
21.952
1.00
25.77
C

ATOM
993
O
GLU
B2012
5.911
−1.677
21.585
1.00
24.25
O

ATOM
994
N
GLU
B2013
4.800
−3.563
22.089
1.00
26.07
N

ATOM
995
CA
GLU
B2013
3.483
−2.997
21.806
1.00
26.79
C

ATOM
996
CB
GLU
B2013
2.546
−4.097
21.294
1.00
27.06
C

ATOM
997
CG
GLU
B2013
3.025
−4.777
20.014
1.00
27.29
C

ATOM
998
CD
GLU
B2013
2.147
−5.943
19.607
0.05
27.19
C

ATOM
999
OE1
GLU
B2013
0.920
−5.750
19.479
0.05
27.19
O

ATOM
1000
OE2
GLU
B2013
2.684
−7.054
19.413
0.05
27.19
O

ATOM
1001
C
GLU
B2013
2.895
−2.358
23.061
1.00
27.09
C

ATOM
1002
O
GLU
B2013
2.816
−2.998
24.113
1.00
27.20
O

ATOM
1003
N
LEU
B2014
2.489
−1.096
22.952
1.00
27.74
N

ATOM
1004
CA
LEU
B2014
1.915
−0.383
24.088
1.00
28.99
C

ATOM
1005
CB
LEU
B2014
1.448
1.015
23.666
1.00
29.85
C

ATOM
1006
CG
LEU
B2014
2.499
2.064
23.293
1.00
30.49
C

ATOM
1007
CD1
LEU
B2014
1.802
3.353
22.863
1.00
31.36
C

ATOM
1008
CD2
LEU
B2014
3.408
2.332
24.477
1.00
30.66
C

ATOM
1009
C
LEU
B2014
0.742
−1.144
24.705
1.00
29.62
C

ATOM
1010
O
LEU
B2014
0.614
−1.209
25.924
1.00
28.92
O

ATOM
1011
N
ALA
B2015
−0.103
−1.723
23.855
1.00
30.68
N

ATOM
1012
CA
ALA
B2015
−1.273
−2.468
24.312
1.00
31.89
C

ATOM
1013
CB
ALA
B2015
−2.062
−2.992
23.106
1.00
31.63
C

ATOM
1014
C
ALA
B2015
−0.942
−3.624
25.256
1.00
32.68
C

ATOM
1015
O
ALA
B2015
−1.705
−3.913
26.180
1.00
32.95
O

ATOM
1016
N
SER
B2016
0.192
−4.282
25.026
1.00
32.98
N

ATOM
1017
CA
SER
B2016
0.599
−5.409
25.861
1.00
33.69
C

ATOM
1018
CB
SER
B2016
1.758
−6.157
25.205
1.00
34.30
C

ATOM
1019
OG
SER
B2016
1.360
−6.697
23.955
1.00
36.37
O

ATOM
1020
C
SER
B2016
0.993
−4.981
27.271
1.00
33.62
C

ATOM
1021
O
SER
B2016
0.707
−5.680
28.242
1.00
33.30
O

ATOM
1022
N
ILE
B2017
1.656
−3.835
27.384
1.00
33.85
N

ATOM
1023
CA
ILE
B2017
2.056
−3.339
28.694
1.00
34.29
C

ATOM
1024
CB
ILE
B2017
2.995
−2.115
28.571
1.00
34.08
C

ATOM
1025
CG2
ILE
B2017
3.350
−1.588
29.958
1.00
33.83
C

ATOM
1026
CG1
ILE
B2017
4.264
−2.501
27.800
1.00
33.75
C

ATOM
1027
CD1
ILE
B2017
5.080
−3.611
28.449
1.00
33.98
C

ATOM
1028
C
ILE
B2017
0.802
−2.932
29.474
1.00
35.14
C

ATOM
1029
O
ILE
B2017
0.714
−3.143
30.683
1.00
34.67
O

ATOM
1030
N
GLU
B2018
−0.172
−2.362
28.770
1.00
36.36
N

ATOM
1031
CA
GLU
B2018
−1.414
−1.925
29.402
1.00
37.92
C

ATOM
1032
CB
GLU
B2018
−2.292
−1.189
28.386
1.00
38.65
C

ATOM
1033
CG
GLU
B2018
−1.548
−0.122
27.599
1.00
40.03
C

ATOM
1034
CD
GLU
B2018
−2.462
0.705
26.716
1.00
41.09
C

ATOM
1035
OE1
GLU
B2018
−3.463
0.148
26.216
1.00
41.60
O

ATOM
1036
OE2
GLU
B2018
−2.172
1.907
26.510
1.00
41.15
O

ATOM
1037
C
GLU
B2018
−2.189
−3.093
30.011
1.00
38.32
C

ATOM
1038
O
GLU
B2018
−2.697
−2.993
31.129
1.00
39.05
O

ATOM
1039
N
SER
B2019
−2.281
−4.198
29.278
1.00
38.71
N

ATOM
1040
CA
SER
B2019
−2.989
−5.375
29.771
1.00
39.10
C

ATOM
1041
CB
SER
B2019
−2.996
−6.476
28.709
1.00
39.02
C

ATOM
1042
OG
SER
B2019
−3.734
−6.082
27.568
1.00
39.39
O

ATOM
1043
C
SER
B2019
−2.332
−5.903
31.044
1.00
39.56
C

ATOM
1044
O
SER
B2019
−3.013
−6.228
32.016
1.00
39.07
O

ATOM
1045
N
ALA
B2020
−1.004
−5.983
31.031
1.00
39.92
N

ATOM
1046
CA
ALA
B2020
−0.253
−6.471
32.182
1.00
40.75
C

ATOM
1047
CB
ALA
B2020
1.240
−6.474
31.866
1.00
39.96
C

ATOM
1048
C
ALA
B2020
−0.531
−5.614
33.415
1.00
41.51
C

ATOM
1049
O
ALA
B2020
−0.584
−6.122
34.535
1.00
41.34
O

ATOM
1050
N
VAL
B2021
−0.704
−4.314
33.202
1.00
42.82
N

ATOM
1051
CA
VAL
B2021
−0.985
−3.390
34.295
1.00
44.39
C

ATOM
1052
CB
VAL
B2021
−0.767
−1.922
33.855
1.00
44.31
C

ATOM
1053
CG1
VAL
B2021
−1.303
−0.971
34.913
1.00
44.07
C

ATOM
1054
CG2
VAL
B2021
0.718
−1.663
33.627
1.00
44.22
C

ATOM
1055
C
VAL
B2021
−2.424
−3.555
34.787
1.00
45.72
C

ATOM
1056
O
VAL
B2021
−2.673
−3.604
35.992
1.00
45.74
O

ATOM
1057
N
THR
B2022
−3.365
−3.642
33.851
1.00
47.27
N

ATOM
1058
CA
THR
B2022
−4.776
−3.801
34.191
1.00
48.73
C

ATOM
1059
CB
THR
B2022
−5.661
−3.833
32.919
1.00
49.02
C

ATOM
1060
OG1
THR
B2022
−5.482
−2.619
32.177
1.00
49.29
O

ATOM
1061
CG2
THR
B2022
−7.134
−3.968
33.293
1.00
49.42
C

ATOM
1062
C
THR
B2022
−4.988
−5.093
34.977
1.00
49.61
C

ATOM
1063
O
THR
B2022
−5.953
−5.225
35.733
1.00
49.90
O

ATOM
1064
N
ARG
B2023
−4.077
−6.043
34.794
1.00
50.61
N

ATOM
1065
CA
ARG
B2023
−4.152
−7.325
35.484
1.00
51.35
C

ATOM
1066
CB
ARG
B2023
−3.028
−8.245
35.009
1.00
52.09
C

ATOM
1067
CG
ARG
B2023
−3.416
−9.710
34.907
1.00
53.02
C

ATOM
1068
CD
ARG
B2023
−3.676
−10.103
33.461
1.00
54.10
C

ATOM
1069
NE
ARG
B2023
−2.492
−9.895
32.628
1.00
54.73
N

ATOM
1070
CZ
ARG
B2023
−2.419
−10.194
31.334
1.00
55.21
C

ATOM
1071
NH1
ARG
B2023
−3.465
−10.720
30.710
1.00
55.43
N

ATOM
1072
NH2
ARG
B2023
−1.296
−9.967
30.663
1.00
55.24
N

ATOM
1073
C
ARG
B2023
−4.025
−7.093
36.989
1.00
51.64
C

ATOM
1074
O
ARG
B2023
−4.448
−7.924
37.794
1.00
51.91
O

ATOM
1075
N
HIS
B2024
−3.428
−5.960
37.354
1.00
51.80
N

ATOM
1076
CA
HIS
B2024
−3.242
−5.575
38.753
1.00
51.59
C

ATOM
1077
CB
HIS
B2024
−4.586
−5.645
39.491
1.00
52.56
C

ATOM
1078
CG
HIS
B2024
−4.528
−5.165
40.908
1.00
53.50
C

ATOM
1079
CD2
HIS
B2024
−4.815
−5.791
42.074
1.00
53.85
C

ATOM
1080
ND1
HIS
B2024
−4.142
−3.886
41.245
1.00
53.73
N

ATOM
1081
CE1
HIS
B2024
−4.195
−3.743
42.557
1.00
54.11
C

ATOM
1082
NE2
HIS
B2024
−4.601
−4.885
43.084
1.00
54.34
N

ATOM
1083
C
HIS
B2024
−2.207
−6.427
39.490
1.00
50.92
C

ATOM
1084
O
HIS
B2024
−1.802
−6.100
40.607
1.00
51.09
O

ATOM
1085
N
GLU
B2025
−1.777
−7.511
38.853
1.00
49.85
N

ATOM
1086
CA
GLU
B2025
−0.805
−8.436
39.429
1.00
48.60
C

ATOM
1087
CB
GLU
B2025
−0.133
−9.231
38.309
1.00
49.70
C

ATOM
1088
CG
GLU
B2025
−1.109
−9.812
37.300
1.00
50.84
C

ATOM
1089
CD
GLU
B2025
−0.430
−10.676
36.255
1.00
51.43
C

ATOM
1090
OE1
GLU
B2025
0.084
−11.754
36.617
1.00
52.08
O

ATOM
1091
OE2
GLU
B2025
−0.408
−10.276
35.073
1.00
51.96
O

ATOM
1092
C
GLU
B2025
0.274
−7.788
40.301
1.00
47.18
C

ATOM
1093
O
GLU
B2025
0.636
−8.322
41.350
1.00
47.28
O

ATOM
1094
N
GLY
B2026
0.779
−6.638
39.864
1.00
45.23
N

ATOM
1095
CA
GLY
B2026
1.832
−5.953
40.598
1.00
42.17
C

ATOM
1096
C
GLY
B2026
3.021
−5.830
39.663
1.00
39.71
C

ATOM
1097
O
GLY
B2026
4.185
−5.914
40.066
1.00
39.77
O

ATOM
1098
N
PHE
B2027
2.695
−5.632
38.392
1.00
37.19
N

ATOM
1099
CA
PHE
B2027
3.667
−5.509
37.315
1.00
34.55
C

ATOM
1100
CB
PHE
B2027
2.922
−5.189
36.014
1.00
34.52
C

ATOM
1101
CG
PHE
B2027
3.752
−5.355
34.777
1.00
34.13
C

ATOM
1102
CD1
PHE
B2027
4.207
−6.613
34.393
1.00
34.08
C

ATOM
1103
CD2
PHE
B2027
4.067
−4.258
33.986
1.00
34.08
C

ATOM
1104
CE1
PHE
B2027
4.963
−6.776
33.237
1.00
34.11
C

ATOM
1105
CE2
PHE
B2027
4.825
−4.409
32.824
1.00
34.27
C

ATOM
1106
CZ
PHE
B2027
5.274
−5.670
32.449
1.00
34.06
C

ATOM
1107
C
PHE
B2027
4.755
−4.459
37.559
1.00
32.71
C

ATOM
1108
O
PHE
B2027
5.933
−4.794
37.676
1.00
31.86
O

ATOM
1109
N
ALA
B2028
4.352
−3.192
37.631
1.00
30.82
N

ATOM
1110
CA
ALA
B2028
5.284
−2.082
37.831
1.00
29.20
C

ATOM
1111
CB
ALA
B2028
4.506
−0.787
38.047
1.00
29.12
C

ATOM
1112
C
ALA
B2028
6.290
−2.269
38.966
1.00
28.66
C

ATOM
1113
O
ALA
B2028
7.451
−1.884
38.836
1.00
27.76
O

ATOM
1114
N
LYS
B2029
5.846
−2.853
40.075
1.00
27.74
N

ATOM
1115
CA
LYS
B2029
6.718
−3.065
41.226
1.00
27.62
C

ATOM
1116
CB
LYS
B2029
5.899
−3.552
42.423
1.00
27.96
C

ATOM
1117
CG
LYS
B2029
5.853
−2.569
43.584
1.00
28.74
C

ATOM
1118
CD
LYS
B2029
7.247
−2.299
44.131
0.05
28.50
C

ATOM
1119
CE
LYS
B2029
7.204
−1.384
45.343
0.05
28.61
C

ATOM
1120
NZ
LYS
B2029
6.454
−1.997
46.474
0.05
28.56
N

ATOM
1121
C
LYS
B2029
7.864
−4.042
40.969
1.00
27.09
C

ATOM
1122
O
LYS
B2029
8.937
−3.910
41.555
1.00
27.52
O

ATOM
1123
N
ARG
B2030
7.642
−5.022
40.099
1.00
25.99
N

ATOM
1124
CA
ARG
B2030
8.682
−6.002
39.803
1.00
24.71
C

ATOM
1125
CB
ARG
B2030
8.048
−7.358
39.465
1.00
25.36
C

ATOM
1126
CG
ARG
B2030
7.303
−7.990
40.631
0.05
25.04
C

ATOM
1127
CD
ARG
B2030
6.804
−9.384
40.291
0.05
25.09
C

ATOM
1128
NE
ARG
B2030
6.143
−10.015
41.430
0.05
25.02
N

ATOM
1129
CZ
ARG
B2030
5.651
−11.249
41.421
0.05
25.00
C

ATOM
1130
NH1
ARG
B2030
5.742
−11.996
40.329
0.05
24.97
N

ATOM
1131
NH2
ARG
B2030
5.067
−11.739
42.506
0.05
24.97
N

ATOM
1132
C
ARG
B2030
9.616
−5.566
38.674
1.00
23.43
C

ATOM
1133
O
ARG
B2030
10.763
−6.008
38.613
1.00
22.95
O

ATOM
1134
N
VAL
B2031
9.131
−4.688
37.797
1.00
22.08
N

ATOM
1135
CA
VAL
B2031
9.924
−4.202
36.665
1.00
20.91
C

ATOM
1136
CB
VAL
B2031
8.998
−3.878
35.447
1.00
21.66
C

ATOM
1137
CG1
VAL
B2031
9.804
−3.269
34.307
1.00
21.12
C

ATOM
1138
CG2
VAL
B2031
8.311
−5.152
34.961
1.00
21.59
C

ATOM
1139
C
VAL
B2031
10.806
−2.971
36.946
1.00
20.08
C

ATOM
1140
O
VAL
B2031
11.891
−2.840
36.362
1.00
18.87
O

ATOM
1141
N
LEU
B2032
10.362
−2.096
37.851
1.00
18.43
N

ATOM
1142
CA
LEU
B2032
11.093
−0.857
38.170
1.00
18.33
C

ATOM
1143
CB
LEU
B2032
10.123
0.333
38.094
1.00
18.11
C

ATOM
1144
CG
LEU
B2032
9.264
0.562
36.836
1.00
17.77
C

ATOM
1145
CD1
LEU
B2032
8.288
1.710
37.095
1.00
18.63
C

ATOM
1146
CD2
LEU
B2032
10.141
0.893
35.642
1.00
18.26
C

ATOM
1147
C
LEU
B2032
11.809
−0.804
39.537
1.00
18.11
C

ATOM
1148
O
LEU
B2032
11.313
−1.351
40.528
1.00
17.53
O

ATOM
1149
N
THR
B2033
12.964
−0.133
39.589
1.00
17.46
N

ATOM
1150
CA
THR
B2033
13.707
0.022
40.848
1.00
17.07
C

ATOM
1151
CB
THR
B2033
15.178
0.466
40.617
1.00
17.19
C

ATOM
1152
OG1
THR
B2033
15.199
1.760
39.996
1.00
17.05
O

ATOM
1153
CG2
THR
B2033
15.919
−0.544
39.733
1.00
15.96
C

ATOM
1154
C
THR
B2033
13.010
1.107
41.686
1.00
17.66
C

ATOM
1155
O
THR
B2033
12.042
1.720
41.234
1.00
17.87
O

ATOM
1156
N
ALA
B2034
13.501
1.355
42.896
1.00
17.54
N

ATOM
1157
CA
ALA
B2034
12.886
2.367
43.757
1.00
18.74
C

ATOM
1158
CB
ALA
B2034
13.565
2.369
45.123
1.00
18.99
C

ATOM
1159
C
ALA
B2034
12.925
3.771
43.145
1.00
18.65
C

ATOM
1160
O
ALA
B2034
11.930
4.503
43.188
1.00
18.77
O

ATOM
1161
N
LEU
B2035
14.066
4.148
42.572
1.00
18.26
N

ATOM
1162
CA
LEU
B2035
14.216
5.470
41.962
1.00
19.09
C

ATOM
1163
CB
LEU
B2035
15.697
5.742
41.665
1.00
20.60
C

ATOM
1164
CG
LEU
B2035
16.154
7.182
41.435
1.00
22.12
C

ATOM
1165
CD1
LEU
B2035
15.976
8.015
42.714
1.00
23.52
C

ATOM
1166
CD2
LEU
B2035
17.618
7.173
41.031
1.00
24.30
C

ATOM
1167
C
LEU
B2035
13.383
5.610
40.680
1.00
18.93
C

ATOM
1168
O
LEU
B2035
12.801
6.670
40.430
1.00
19.57
O

ATOM
1169
N
GLU
B2036
13.333
4.559
39.858
1.00
18.62
N

ATOM
1170
CA
GLU
B2036
12.533
4.604
38.626
1.00
18.35
C

ATOM
1171
CB
GLU
B2036
12.733
3.327
37.784
1.00
17.51
C

ATOM
1172
CG
GLU
B2036
14.085
3.215
37.042
1.00
15.99
C

ATOM
1173
CD
GLU
B2036
14.300
1.848
36.391
1.00
16.12
C

ATOM
1174
OE1
GLU
B2036
15.007
1.777
35.361
1.00
15.21
O

ATOM
1175
OE2
GLU
B2036
13.781
0.836
36.911
1.00
15.16
O

ATOM
1176
C
GLU
B2036
11.039
4.744
38.982
1.00
19.23
C

ATOM
1177
O
GLU
B2036
10.290
5.440
38.296
1.00
19.60
O

ATOM
1178
N
MET
B2037
10.616
4.074
40.051
1.00
19.86
N

ATOM
1179
CA
MET
B2037
9.219
4.123
40.501
1.00
21.88
C

ATOM
1180
CB
MET
B2037
9.008
3.086
41.615
1.00
22.85
C

ATOM
1181
CG
MET
B2037
7.623
3.055
42.236
1.00
25.86
C

ATOM
1182
SD
MET
B2037
6.356
2.391
41.143
1.00
28.53
S

ATOM
1183
CE
MET
B2037
6.759
0.626
41.201
1.00
27.97
C

ATOM
1184
C
MET
B2037
8.834
5.528
41.000
1.00
22.03
C

ATOM
1185
O
MET
B2037
7.716
6.006
40.772
1.00
22.35
O

ATOM
1186
N
GLU
B2038
9.759
6.187
41.687
1.00
22.54
N

ATOM
1187
CA
GLU
B2038
9.501
7.528
42.194
1.00
23.34
C

ATOM
1188
CB
GLU
B2038
10.663
7.973
43.101
1.00
23.49
C

ATOM
1189
CG
GLU
B2038
10.475
7.496
44.550
1.00
24.52
C

ATOM
1190
CD
GLU
B2038
11.772
7.284
45.326
1.00
25.50
C

ATOM
1191
OE1
GLU
B2038
12.785
7.962
45.036
1.00
25.67
O

ATOM
1192
OE2
GLU
B2038
11.765
6.439
46.251
1.00
25.94
O

ATOM
1193
C
GLU
B2038
9.252
8.513
41.046
1.00
23.18
C

ATOM
1194
O
GLU
B2038
8.512
9.482
41.200
1.00
23.42
O

ATOM
1195
N
ARG
B2039
9.854
8.250
39.888
1.00
23.18
N

ATOM
1196
CA
ARG
B2039
9.659
9.097
38.713
1.00
23.42
C

ATOM
1197
CB
ARG
B2039
10.801
8.888
37.710
1.00
24.21
C

ATOM
1198
CG
ARG
B2039
10.566
9.517
36.338
1.00
24.82
C

ATOM
1199
CD
ARG
B2039
10.414
11.027
36.415
0.05
24.52
C

ATOM
1200
NE
ARG
B2039
10.169
11.609
35.099
0.05
24.58
N

ATOM
1201
CZ
ARG
B2039
9.995
12.908
34.873
0.05
24.54
C

ATOM
1202
NH1
ARG
B2039
9.776
13.344
33.640
0.05
24.55
N

ATOM
1203
NH2
ARG
B2039
10.039
13.771
35.879
0.05
24.55
N

ATOM
1204
C
ARG
B2039
8.323
8.738
38.057
1.00
22.97
C

ATOM
1205
O
ARG
B2039
7.591
9.614
37.594
1.00
23.62
O

ATOM
1206
N
PHE
B2040
8.015
7.443
38.037
1.00
22.59
N

ATOM
1207
CA
PHE
B2040
6.777
6.914
37.456
1.00
23.04
C

ATOM
1208
CB
PHE
B2040
6.769
5.381
37.598
1.00
23.27
C

ATOM
1209
CG
PHE
B2040
5.520
4.705
37.082
1.00
24.49
C

ATOM
1210
CD1
PHE
B2040
5.270
4.604
35.716
1.00
24.75
C

ATOM
1211
CD2
PHE
B2040
4.611
4.125
37.971
1.00
24.92
C

ATOM
1212
CE1
PHE
B2040
4.135
3.930
35.240
1.00
25.22
C

ATOM
1213
CE2
PHE
B2040
3.473
3.451
37.509
1.00
24.72
C

ATOM
1214
CZ
PHE
B2040
3.236
3.353
36.139
1.00
25.48
C

ATOM
1215
C
PHE
B2040
5.529
7.506
38.126
1.00
23.15
C

ATOM
1216
O
PHE
B2040
4.558
7.841
37.448
1.00
22.73
O

ATOM
1217
N
THR
B2041
5.559
7.636
39.452
1.00
23.63
N

ATOM
1218
CA
THR
B2041
4.407
8.165
40.186
1.00
25.06
C

ATOM
1219
CB
THR
B2041
4.487
7.819
41.701
1.00
24.62
C

ATOM
1220
OG1
THR
B2041
5.710
8.322
42.250
1.00
24.25
O

ATOM
1221
CG2
THR
B2041
4.421
6.311
41.910
1.00
24.17
C

ATOM
1222
C
THR
B2041
4.156
9.669
40.050
1.00
25.84
C

ATOM
1223
O
THR
B2041
3.089
10.155
40.442
1.00
26.22
O

ATOM
1224
N
SER
B2042
5.119
10.412
39.508
1.00
27.24
N

ATOM
1225
CA
SER
B2042
4.939
11.856
39.346
1.00
28.70
C

ATOM
1226
CB
SER
B2042
6.256
12.605
39.605
1.00
29.90
C

ATOM
1227
OG
SER
B2042
7.260
12.270
38.658
1.00
31.49
O

ATOM
1228
C
SER
B2042
4.404
12.214
37.959
1.00
29.44
C

ATOM
1229
O
SER
B2042
4.245
13.392
37.632
1.00
28.96
O

ATOM
1230
N
LEU
B2043
4.127
11.192
37.151
1.00
29.93
N

ATOM
1231
CA
LEU
B2043
3.598
11.379
35.797
1.00
30.98
C

ATOM
1232
CB
LEU
B2043
4.466
10.622
34.779
1.00
30.83
C

ATOM
1233
CG
LEU
B2043
5.925
11.061
34.614
1.00
30.66
C

ATOM
1234
CD1
LEU
B2043
6.690
10.037
33.778
1.00
31.31
C

ATOM
1235
CD2
LEU
B2043
5.970
12.431
33.960
1.00
31.38
C

ATOM
1236
C
LEU
B2043
2.160
10.864
35.712
1.00
31.75
C

ATOM
1237
O
LEU
B2043
1.711
10.106
36.573
1.00
31.45
O

ATOM
1238
N
LYS
B2044
1.440
11.264
34.668
1.00
33.21
N

ATOM
1239
CA
LYS
B2044
0.059
10.820
34.497
1.00
34.53
C

ATOM
1240
CB
LYS
B2044
−0.904
11.853
35.100
1.00
35.00
C

ATOM
1241
CG
LYS
B2044
−2.362
11.415
35.118
0.05
34.86
C

ATOM
1242
CD
LYS
B2044
−3.267
12.481
35.714
0.05
34.96
C

ATOM
1243
CE
LYS
B2044
−4.718
12.025
35.718
0.05
34.95
C

ATOM
1244
NZ
LYS
B2044
−5.625
13.056
36.293
0.05
35.07
N

ATOM
1245
C
LYS
B2044
−0.311
10.580
33.035
1.00
35.45
C

ATOM
1246
O
LYS
B2044
0.422
10.960
32.121
1.00
35.43
O

ATOM
1247
N
GLY
B2045
−1.454
9.934
32.829
1.00
36.33
N

ATOM
1248
CA
GLY
B2045
−1.940
9.671
31.488
1.00
37.45
C

ATOM
1249
C
GLY
B2045
−1.031
8.869
30.579
1.00
38.02
C

ATOM
1250
O
GLY
B2045
−0.215
8.065
31.036
1.00
38.35
O

ATOM
1251
N
ARG
B2046
−1.187
9.099
29.279
1.00
38.11
N

ATOM
1252
CA
ARG
B2046
−0.414
8.409
28.250
1.00
38.00
C

ATOM
1253
CB
ARG
B2046
−0.718
9.026
26.882
1.00
38.22
C

ATOM
1254
CG
ARG
B2046
−2.203
9.241
26.635
0.05
38.32
C

ATOM
1255
CD
ARG
B2046
−2.469
9.951
25.319
0.05
38.47
C

ATOM
1256
NE
ARG
B2046
−2.193
9.103
24.164
0.05
38.58
N

ATOM
1257
CZ
ARG
B2046
−2.418
9.462
22.904
0.05
38.64
C

ATOM
1258
NH1
ARG
B2046
−2.138
8.626
21.915
0.05
38.67
N

ATOM
1259
NH2
ARG
B2046
−2.925
10.657
22.633
0.05
38.67
N

ATOM
1260
C
ARG
B2046
1.083
8.472
28.516
1.00
37.79
C

ATOM
1261
O
ARG
B2046
1.809
7.514
28.262
1.00
37.64
O

ATOM
1262
N
ARG
B2047
1.534
9.611
29.031
1.00
37.35
N

ATOM
1263
CA
ARG
B2047
2.945
9.827
29.327
1.00
36.86
C

ATOM
1264
CB
ARG
B2047
3.139
11.262
29.824
1.00
38.35
C

ATOM
1265
CG
ARG
B2047
4.529
11.834
29.622
1.00
40.01
C

ATOM
1266
CD
ARG
B2047
4.591
13.258
30.156
1.00
41.52
C

ATOM
1267
NE
ARG
B2047
5.880
13.894
29.903
1.00
43.12
N

ATOM
1268
CZ
ARG
B2047
6.276
15.030
30.471
1.00
44.06
C

ATOM
1269
NH1
ARG
B2047
7.467
15.539
30.180
1.00
44.67
N

ATOM
1270
NH2
ARG
B2047
5.486
15.654
31.336
1.00
44.50
N

ATOM
1271
C
ARG
B2047
3.460
8.826
30.368
1.00
35.56
C

ATOM
1272
O
ARG
B2047
4.631
8.454
30.354
1.00
34.93
O

ATOM
1273
N
GLN
B2048
2.578
8.388
31.263
1.00
34.21
N

ATOM
1274
CA
GLN
B2048
2.947
7.433
32.305
1.00
32.54
C

ATOM
1275
CB
GLN
B2048
1.866
7.413
33.396
1.00
33.03
C

ATOM
1276
CG
GLN
B2048
2.203
6.564
34.616
1.00
32.53
C

ATOM
1277
CD
GLN
B2048
1.203
6.741
35.751
1.00
33.31
C

ATOM
1278
OE1
GLN
B2048
0.009
6.499
35.586
1.00
32.97
O

ATOM
1279
NE2
GLN
B2048
1.694
7.164
36.914
1.00
33.17
N

ATOM
1280
C
GLN
B2048
3.161
6.021
31.740
1.00
31.47
C

ATOM
1281
O
GLN
B2048
4.119
5.340
32.106
1.00
31.22
O

ATOM
1282
N
ILE
B2049
2.269
5.589
30.852
1.00
29.87
N

ATOM
1283
CA
ILE
B2049
2.366
4.266
30.233
1.00
28.47
C

ATOM
1284
CB
ILE
B2049
1.087
3.936
29.417
1.00
28.92
C

ATOM
1285
CG2
ILE
B2049
1.263
2.627
28.667
1.00
29.21
C

ATOM
1286
CG1
ILE
B2049
−0.130
3.858
30.346
1.00
29.32
C

ATOM
1287
CD1
ILE
B2049
−0.118
2.675
31.305
1.00
28.99
C

ATOM
1288
C
ILE
B2049
3.577
4.191
29.292
1.00
27.84
C

ATOM
1289
O
ILE
B2049
4.172
3.127
29.116
1.00
27.30
O

ATOM
1290
N
GLU
B2050
3.933
5.321
28.688
1.00
26.72
N

ATOM
1291
CA
GLU
B2050
5.073
5.373
27.774
1.00
26.84
C

ATOM
1292
CB
GLU
B2050
5.060
6.692
26.985
1.00
27.77
C

ATOM
1293
CG
GLU
B2050
6.298
6.973
26.119
1.00
30.05
C

ATOM
1294
CD
GLU
B2050
6.456
6.027
24.927
1.00
31.34
C

ATOM
1295
OE1
GLU
B2050
5.443
5.718
24.262
1.00
32.49
O

ATOM
1296
OE2
GLU
B2050
7.603
5.610
24.643
1.00
31.18
O

ATOM
1297
C
GLU
B2050
6.397
5.223
28.520
1.00
25.29
C

ATOM
1298
O
GLU
B2050
7.339
4.621
27.994
1.00
24.70
O

ATOM
1299
N
TYR
B2051
6.471
5.767
29.737
1.00
23.32
N

ATOM
1300
CA
TYR
B2051
7.696
5.675
30.537
1.00
21.39
C

ATOM
1301
CB
TYR
B2051
7.576
6.526
31.821
1.00
21.45
C

ATOM
1302
CG
TYR
B2051
8.819
6.522
32.712
1.00
20.60
C

ATOM
1303
CD1
TYR
B2051
8.974
5.577
33.728
1.00
20.47
C

ATOM
1304
CE1
TYR
B2051
10.128
5.547
34.526
1.00
20.26
C

ATOM
1305
CD2
TYR
B2051
9.852
7.444
32.512
1.00
20.44
C

ATOM
1306
CE2
TYR
B2051
11.012
7.420
33.302
1.00
20.69
C

ATOM
1307
CZ
TYR
B2051
11.141
6.469
34.306
1.00
20.69
C

ATOM
1308
OH
TYR
B2051
12.277
6.449
35.094
1.00
21.32
O

ATOM
1309
C
TYR
B2051
7.978
4.212
30.885
1.00
20.75
C

ATOM
1310
O
TYR
B2051
9.085
3.718
30.658
1.00
19.49
O

ATOM
1311
N
LEU
B2052
6.968
3.520
31.413
1.00
19.18
N

ATOM
1312
CA
LEU
B2052
7.096
2.109
31.788
1.00
18.14
C

ATOM
1313
CB
LEU
B2052
5.782
1.616
32.419
1.00
18.69
C

ATOM
1314
CG
LEU
B2052
5.668
0.154
32.868
1.00
19.58
C

ATOM
1315
CD1
LEU
B2052
6.783
−0.189
33.861
1.00
19.24
C

ATOM
1316
CD2
LEU
B2052
4.299
−0.070
33.511
1.00
20.41
C

ATOM
1317
C
LEU
B2052
7.476
1.209
30.598
1.00
17.54
C

ATOM
1318
O
LEU
B2052
8.347
0.347
30.719
1.00
16.53
O

ATOM
1319
N
ALA
B2053
6.828
1.411
29.453
1.00
16.29
N

ATOM
1320
CA
ALA
B2053
7.115
0.600
28.262
1.00
16.39
C

ATOM
1321
CB
ALA
B2053
6.106
0.926
27.154
1.00
16.13
C

ATOM
1322
C
ALA
B2053
8.550
0.794
27.744
1.00
15.79
C

ATOM
1323
O
ALA
B2053
9.206
−0.169
27.325
1.00
16.28
O

ATOM
1324
N
GLY
B2054
9.034
2.033
27.771
1.00
15.48
N

ATOM
1325
CA
GLY
B2054
10.391
2.311
27.316
1.00
15.32
C

ATOM
1326
C
GLY
B2054
11.471
1.701
28.201
1.00
16.07
C

ATOM
1327
O
GLY
B2054
12.550
1.309
27.716
1.00
14.96
O

ATOM
1328
N
ARG
B2055
11.208
1.633
29.506
1.00
15.22
N

ATOM
1329
CA
ARG
B2055
12.179
1.040
30.430
1.00
16.35
C

ATOM
1330
CB
ARG
B2055
11.790
1.353
31.886
1.00
17.42
C

ATOM
1331
CG
ARG
B2055
12.545
2.543
32.514
1.00
19.58
C

ATOM
1332
CD
ARG
B2055
12.545
3.794
31.623
1.00
21.46
C

ATOM
1333
NE
ARG
B2055
13.423
4.838
32.153
1.00
21.36
N

ATOM
1334
CZ
ARG
B2055
13.695
5.986
31.534
1.00
22.03
C

ATOM
1335
NH1
ARG
B2055
13.155
6.256
30.353
1.00
22.33
N

ATOM
1336
NH2
ARG
B2055
14.520
6.865
32.094
1.00
21.30
N

ATOM
1337
C
ARG
B2055
12.261
−0.479
30.194
1.00
16.15
C

ATOM
1338
O
ARG
B2055
13.339
−1.079
30.277
1.00
15.13
O

ATOM
1339
N
TRP
B2056
11.119
−1.090
29.884
1.00
16.30
N

ATOM
1340
CA
TRP
B2056
11.055
−2.528
29.608
1.00
17.26
C

ATOM
1341
CB
TRP
B2056
9.592
−2.966
29.425
1.00
19.31
C

ATOM
1342
CG
TRP
B2056
9.393
−4.449
29.444
1.00
22.46
C

ATOM
1343
CD2
TRP
B2056
9.458
−5.335
28.325
1.00
24.24
C

ATOM
1344
CE2
TRP
B2056
9.234
−6.644
28.813
1.00
25.47
C

ATOM
1345
CE3
TRP
B2056
9.684
−5.153
26.954
1.00
25.79
C

ATOM
1346
CD1
TRP
B2056
9.139
−5.234
30.540
1.00
23.87
C

ATOM
1347
NE1
TRP
B2056
9.041
−6.552
30.167
1.00
24.64
N

ATOM
1348
CZ2
TRP
B2056
9.231
−7.763
27.979
1.00
26.38
C

ATOM
1349
CZ3
TRP
B2056
9.681
−6.270
26.122
1.00
27.06
C

ATOM
1350
CH2
TRP
B2056
9.455
−7.559
26.641
1.00
27.05
C

ATOM
1351
C
TRP
B2056
11.843
−2.850
28.327
1.00
16.16
C

ATOM
1352
O
TRP
B2056
12.642
−3.794
28.288
1.00
16.26
O

ATOM
1353
N
SER
B2057
11.608
−2.053
27.288
1.00
15.01
N

ATOM
1354
CA
SER
B2057
12.265
−2.208
25.980
1.00
14.82
C

ATOM
1355
CB
SER
B2057
11.678
−1.155
25.017
1.00
15.72
C

ATOM
1356
OG
SER
B2057
12.069
−1.352
23.670
1.00
19.47
O

ATOM
1357
C
SER
B2057
13.807
−2.052
26.087
1.00
14.21
C

ATOM
1358
O
SER
B2057
14.581
−2.816
25.471
1.00
12.39
O

ATOM
1359
N
ALA
B2058
14.246
−1.072
26.873
1.00
12.21
N

ATOM
1360
CA
ALA
B2058
15.680
−0.810
27.052
1.00
12.92
C

ATOM
1361
CB
ALA
B2058
15.878
0.516
27.800
1.00
12.17
C

ATOM
1362
C
ALA
B2058
16.398
−1.949
27.801
1.00
12.59
C

ATOM
1363
O
ALA
B2058
17.507
−2.354
27.428
1.00
11.75
O

ATOM
1364
N
LYS
B2059
15.772
−2.455
28.861
1.00
12.47
N

ATOM
1365
CA
LYS
B2059
16.368
−3.546
29.634
1.00
13.35
C

ATOM
1366
CB
LYS
B2059
15.579
−3.757
30.947
1.00
14.19
C

ATOM
1367
CG
LYS
B2059
15.656
−2.538
31.896
1.00
14.71
C

ATOM
1368
CD
LYS
B2059
14.961
−2.754
33.258
1.00
15.04
C

ATOM
1369
CE
LYS
B2059
15.045
−1.488
34.124
1.00
16.38
C

ATOM
1370
NZ
LYS
B2059
14.590
−1.651
35.545
1.00
15.99
N

ATOM
1371
C
LYS
B2059
16.459
−4.846
28.814
1.00
14.13
C

ATOM
1372
O
LYS
B2059
17.406
−5.632
28.992
1.00
13.94
O

ATOM
1373
N
GLU
B2060
15.500
−5.072
27.907
1.00
13.55
N

ATOM
1374
CA
GLU
B2060
15.535
−6.276
27.066
1.00
14.73
C

ATOM
1375
CB
GLU
B2060
14.160
−6.552
26.436
1.00
16.24
C

ATOM
1376
CG
GLU
B2060
14.173
−7.696
25.413
1.00
20.48
C

ATOM
1377
CD
GLU
B2060
14.283
−9.089
26.037
1.00
23.43
C

ATOM
1378
OE1
GLU
B2060
14.802
−9.230
27.168
1.00
26.30
O

ATOM
1379
OE2
GLU
B2060
13.860
−10.061
25.376
1.00
25.45
O

ATOM
1380
C
GLU
B2060
16.608
−6.174
25.960
1.00
13.95
C

ATOM
1381
O
GLU
B2060
17.238
−7.178
25.609
1.00
13.52
O

ATOM
1382
N
ALA
B2061
16.819
−4.971
25.418
1.00
13.22
N

ATOM
1383
CA
ALA
B2061
17.838
−4.765
24.379
1.00
13.62
C

ATOM
1384
CB
ALA
B2061
17.740
−3.332
23.801
1.00
13.16
C

ATOM
1385
C
ALA
B2061
19.241
−5.022
24.950
1.00
13.67
C

ATOM
1386
O
ALA
B2061
20.107
−5.576
24.257
1.00
14.02
O

ATOM
1387
N
PHE
B2062
19.463
−4.630
26.207
1.00
13.22
N

ATOM
1388
CA
PHE
B2062
20.760
−4.860
26.873
1.00
14.50
C

ATOM
1389
CB
PHE
B2062
20.844
−4.049
28.185
1.00
14.44
C

ATOM
1390
CG
PHE
B2062
22.074
−4.353
29.029
1.00
14.90
C

ATOM
1391
CD1
PHE
B2062
22.084
−5.445
29.908
1.00
15.30
C

ATOM
1392
CD2
PHE
B2062
23.223
−3.571
28.923
1.00
15.56
C

ATOM
1393
CE1
PHE
B2062
23.223
−5.752
30.663
1.00
15.94
C

ATOM
1394
CE2
PHE
B2062
24.375
−3.869
29.678
1.00
15.34
C

ATOM
1395
CZ
PHE
B2062
24.370
−4.961
30.545
1.00
15.50
C

ATOM
1396
C
PHE
B2062
20.969
−6.363
27.147
1.00
14.72
C

ATOM
1397
O
PHE
B2062
22.063
−6.894
26.938
1.00
14.93
O

ATOM
1398
N
SER
B2063
19.922
−7.052
27.599
1.00
14.63
N

ATOM
1399
CA
SER
B2063
20.016
−8.490
27.864
1.00
15.27
C

ATOM
1400
CB
SER
B2063
18.688
−9.021
28.415
1.00
16.20
C

ATOM
1401
OG
SER
B2063
18.406
−8.473
29.694
1.00
18.16
O

ATOM
1402
C
SER
B2063
20.379
−9.257
26.579
1.00
15.62
C

ATOM
1403
O
SER
B2063
21.187
−10.185
26.607
1.00
14.45
O

ATOM
1404
N
LYS
B2064
19.767
−8.872
25.459
1.00
15.61
N

ATOM
1405
CA
LYS
B2064
20.049
−9.514
24.175
1.00
16.52
C

ATOM
1406
CB
LYS
B2064
19.012
−9.077
23.125
1.00
16.00
C

ATOM
1407
CG
LYS
B2064
17.614
−9.664
23.369
1.00
15.31
C

ATOM
1408
CD
LYS
B2064
16.563
−9.149
22.365
1.00
17.09
C

ATOM
1409
CE
LYS
B2064
16.849
−9.635
20.935
1.00
18.35
C

ATOM
1410
NZ
LYS
B2064
15.798
−9.213
19.951
1.00
19.10
N

ATOM
1411
C
LYS
B2064
21.470
−9.195
23.694
1.00
17.20
C

ATOM
1412
O
LYS
B2064
22.113
−10.024
23.043
1.00
17.94
O

ATOM
1413
N
ALA
B2065
21.962
−7.999
24.014
1.00
18.06
N

ATOM
1414
CA
ALA
B2065
23.316
−7.605
23.623
1.00
19.56
C

ATOM
1415
CB
ALA
B2065
23.545
−6.119
23.922
1.00
20.35
C

ATOM
1416
C
ALA
B2065
24.361
−8.453
24.358
1.00
21.22
C

ATOM
1417
O
ALA
B2065
25.473
−8.657
23.859
1.00
20.91
O

ATOM
1418
N
MET
B2066
24.007
−8.940
25.545
1.00
22.79
N

ATOM
1419
CA
MET
B2066
24.924
−9.774
26.331
1.00
25.40
C

ATOM
1420
CB
MET
B2066
24.690
−9.573
27.836
1.00
25.98
C

ATOM
1421
CG
MET
B2066
25.035
−8.178
28.353
1.00
28.04
C

ATOM
1422
SD
MET
B2066
26.596
−8.065
29.288
1.00
31.65
S

ATOM
1423
CE
MET
B2066
26.043
−8.670
30.858
1.00
29.68
C

ATOM
1424
C
MET
B2066
24.761
−11.256
25.983
1.00
26.28
C

ATOM
1425
O
MET
B2066
25.539
−12.095
26.441
1.00
27.12
O

ATOM
1426
N
GLY
B2067
23.743
−11.570
25.184
1.00
26.98
N

ATOM
1427
CA
GLY
B2067
23.501
−12.943
24.772
1.00
28.85
C

ATOM
1428
C
GLY
B2067
22.447
−13.728
25.544
1.00
30.30
C

ATOM
1429
O
GLY
B2067
22.379
−14.950
25.408
1.00
30.22
O

ATOM
1430
N
THR
B2068
21.618
−13.048
26.335
1.00
31.36
N

ATOM
1431
CA
THR
B2068
20.583
−13.729
27.120
1.00
33.00
C

ATOM
1432
CB
THR
B2068
21.043
−13.892
28.595
1.00
32.89
C

ATOM
1433
OG1
THR
B2068
20.057
−14.628
29.332
1.00
33.56
O

ATOM
1434
CG2
THR
B2068
21.253
−12.528
29.248
1.00
32.58
C

ATOM
1435
C
THR
B2068
19.217
−13.023
27.083
1.00
33.93
C

ATOM
1436
O
THR
B2068
18.867
−12.381
26.091
1.00
34.69
O

ATOM
1437
N
GLY
B2069
18.446
−13.157
28.161
1.00
35.37
N

ATOM
1438
CA
GLY
B2069
17.132
−12.534
28.239
1.00
36.59
C

ATOM
1439
C
GLY
B2069
16.890
−11.870
29.586
1.00
37.70
C

ATOM
1440
O
GLY
B2069
17.525
−12.221
30.580
1.00
38.22
O

ATOM
1441
N
ILE
B2070
15.960
−10.918
29.631
1.00
38.74
N

ATOM
1442
CA
ILE
B2070
15.668
−10.195
30.869
1.00
39.48
C

ATOM
1443
CB
ILE
B2070
14.789
−8.948
30.595
1.00
39.69
C

ATOM
1444
CG2
ILE
B2070
13.430
−9.375
30.057
1.00
40.00
C

ATOM
1445
CG1
ILE
B2070
14.621
−8.132
31.880
1.00
39.65
C

ATOM
1446
CD1
ILE
B2070
15.923
−7.652
32.491
1.00
39.07
C

ATOM
1447
C
ILE
B2070
15.008
−11.043
31.960
1.00
40.17
C

ATOM
1448
O
ILE
B2070
15.155
−10.748
33.150
1.00
40.22
O

ATOM
1449
N
SER
B2071
14.283
−12.087
31.564
1.00
40.66
N

ATOM
1450
CA
SER
B2071
13.632
−12.963
32.539
1.00
41.23
C

ATOM
1451
CB
SER
B2071
12.702
−13.965
31.841
1.00
41.77
C

ATOM
1452
OG
SER
B2071
11.623
−13.319
31.185
1.00
43.00
O

ATOM
1453
C
SER
B2071
14.694
−13.729
33.324
1.00
41.05
C

ATOM
1454
O
SER
B2071
14.446
−14.202
34.435
1.00
41.50
O

ATOM
1455
N
LYS
B2072
15.883
−13.838
32.740
1.00
40.66
N

ATOM
1456
CA
LYS
B2072
16.992
−14.554
33.360
1.00
39.81
C

ATOM
1457
CB
LYS
B2072
17.754
−15.336
32.286
1.00
40.65
C

ATOM
1458
CG
LYS
B2072
16.868
−16.186
31.383
1.00
41.38
C

ATOM
1459
CD
LYS
B2072
17.686
−16.871
30.301
1.00
42.22
C

ATOM
1460
CE
LYS
B2072
16.818
−17.749
29.419
1.00
42.85
C

ATOM
1461
NZ
LYS
B2072
15.748
−16.964
28.747
1.00
43.40
N

ATOM
1462
C
LYS
B2072
17.954
−13.620
34.093
1.00
38.99
C

ATOM
1463
O
LYS
B2072
18.445
−13.947
35.174
1.00
38.73
O

ATOM
1464
N
LEU
B2073
18.214
−12.457
33.502
1.00
38.00
N

ATOM
1465
CA
LEU
B2073
19.136
−11.480
34.082
1.00
37.21
C

ATOM
1466
CB
LEU
B2073
19.514
−10.444
33.015
1.00
37.84
C

ATOM
1467
CG
LEU
B2073
20.842
−9.689
33.144
1.00
38.45
C

ATOM
1468
CD1
LEU
B2073
21.202
−9.069
31.801
1.00
38.77
C

ATOM
1469
CD2
LEU
B2073
20.738
−8.625
34.226
1.00
38.87
C

ATOM
1470
C
LEU
B2073
18.583
−10.784
35.338
1.00
36.22
C

ATOM
1471
O
LEU
B2073
19.335
−10.491
36.268
1.00
36.38
O

ATOM
1472
N
GLY
B2074
17.276
−10.527
35.366
1.00
34.86
N

ATOM
1473
CA
GLY
B2074
16.670
−9.874
36.520
1.00
32.86
C

ATOM
1474
C
GLY
B2074
16.457
−8.376
36.351
1.00
31.51
C

ATOM
1475
O
GLY
B2074
17.415
−7.625
36.168
1.00
31.09
O

ATOM
1476
N
PHE
B2075
15.204
−7.934
36.435
1.00
29.86
N

ATOM
1477
CA
PHE
B2075
14.873
−6.516
36.274
1.00
28.90
C

ATOM
1478
CB
PHE
B2075
13.348
−6.309
36.264
1.00
29.85
C

ATOM
1479
CG
PHE
B2075
12.656
−6.885
35.062
1.00
30.57
C

ATOM
1480
CD1
PHE
B2075
12.145
−8.177
35.090
1.00
31.57
C

ATOM
1481
CD2
PHE
B2075
12.502
−6.130
33.905
1.00
31.69
C

ATOM
1482
CE1
PHE
B2075
11.487
−8.714
33.980
1.00
31.82
C

ATOM
1483
CE2
PHE
B2075
11.845
−6.656
32.786
1.00
32.40
C

ATOM
1484
CZ
PHE
B2075
11.336
−7.954
32.828
1.00
32.18
C

ATOM
1485
C
PHE
B2075
15.470
−5.558
37.310
1.00
27.58
C

ATOM
1486
O
PHE
B2075
15.773
−4.409
36.983
1.00
26.85
O

ATOM
1487
N
GLN
B2076
15.626
−6.013
38.551
1.00
26.42
N

ATOM
1488
CA
GLN
B2076
16.161
−5.156
39.612
1.00
26.02
C

ATOM
1489
CB
GLN
B2076
15.829
−5.745
40.995
1.00
26.15
C

ATOM
1490
CG
GLN
B2076
14.332
−5.838
41.292
1.00
25.92
C

ATOM
1491
CD
GLN
B2076
13.641
−4.482
41.284
1.00
26.13
C

ATOM
1492
OE1
GLN
B2076
12.615
−4.300
40.624
1.00
25.80
O

ATOM
1493
NE2
GLN
B2076
14.193
−3.528
42.031
1.00
25.89
N

ATOM
1494
C
GLN
B2076
17.663
−4.892
39.524
1.00
25.52
C

ATOM
1495
O
GLN
B2076
18.195
−4.068
40.276
1.00
25.38
O

ATOM
1496
N
ASP
B2077
18.343
−5.576
38.608
1.00
25.07
N

ATOM
1497
CA
ASP
B2077
19.789
−5.407
38.448
1.00
25.24
C

ATOM
1498
CB
ASP
B2077
20.447
−6.739
38.060
1.00
28.16
C

ATOM
1499
CG
ASP
B2077
20.008
−7.895
38.945
1.00
31.24
C

ATOM
1500
OD1
ASP
B2077
19.868
−7.699
40.172
1.00
32.43
O

ATOM
1501
OD2
ASP
B2077
19.815
−9.009
38.407
1.00
34.01
O

ATOM
1502
C
ASP
B2077
20.164
−4.350
37.402
1.00
23.27
C

ATOM
1503
O
ASP
B2077
21.347
−4.096
37.173
1.00
23.32
O

ATOM
1504
N
LEU
B2078
19.160
−3.742
36.774
1.00
21.03
N

ATOM
1505
CA
LEU
B2078
19.376
−2.717
35.746
1.00
18.79
C

ATOM
1506
CB
LEU
B2078
18.923
−3.240
34.370
1.00
18.82
C

ATOM
1507
CG
LEU
B2078
19.560
−4.543
33.861
1.00
19.30
C

ATOM
1508
CD1
LEU
B2078
18.877
−5.001
32.575
1.00
19.23
C

ATOM
1509
CD2
LEU
B2078
21.040
−4.325
33.622
1.00
19.43
C

ATOM
1510
C
LEU
B2078
18.582
−1.451
36.081
1.00
18.03
C

ATOM
1511
O
LEU
B2078
17.463
−1.543
36.591
1.00
17.56
O

ATOM
1512
N
GLU
B2079
19.150
−0.276
35.792
1.00
16.76
N

ATOM
1513
CA
GLU
B2079
18.466
0.998
36.060
1.00
15.78
C

ATOM
1514
CB
GLU
B2079
18.912
1.563
37.417
1.00
16.39
C

ATOM
1515
CG
GLU
B2079
18.136
2.809
37.863
1.00
18.61
C

ATOM
1516
CD
GLU
B2079
18.567
3.319
39.237
1.00
19.54
C

ATOM
1517
OE1
GLU
B2079
19.725
3.776
39.376
1.00
18.25
O

ATOM
1518
OE2
GLU
B2079
17.743
3.257
40.180
1.00
20.67
O

ATOM
1519
C
GLU
B2079
18.729
2.029
34.944
1.00
15.93
C

ATOM
1520
O
GLU
B2079
19.884
2.233
34.543
1.00
15.32
O

ATOM
1521
N
VAL
B2080
17.659
2.666
34.452
1.00
15.15
N

ATOM
1522
CA
VAL
B2080
17.735
3.664
33.371
1.00
15.13
C

ATOM
1523
CB
VAL
B2080
16.973
3.169
32.083
1.00
14.90
C

ATOM
1524
CG1
VAL
B2080
17.063
4.228
30.963
1.00
12.93
C

ATOM
1525
CG2
VAL
B2080
17.555
1.844
31.593
1.00
14.67
C

ATOM
1526
C
VAL
B2080
17.120
5.015
33.779
1.00
16.52
C

ATOM
1527
O
VAL
B2080
15.913
5.096
34.046
1.00
16.43
O

ATOM
1528
N
LEU
B2081
17.941
6.069
33.815
1.00
17.23
N

ATOM
1529
CA
LEU
B2081
17.469
7.414
34.178
1.00
18.35
C

ATOM
1530
CB
LEU
B2081
18.248
7.944
35.398
1.00
18.31
C

ATOM
1531
CG
LEU
B2081
18.457
7.034
36.621
1.00
18.74
C

ATOM
1532
CD1
LEU
B2081
19.403
7.722
37.602
1.00
19.49
C

ATOM
1533
CD2
LEU
B2081
17.128
6.720
37.296
1.00
19.00
C

ATOM
1534
C
LEU
B2081
17.657
8.391
33.006
1.00
19.38
C

ATOM
1535
O
LEU
B2081
18.257
8.040
31.984
1.00
18.07
O

ATOM
1536
N
ASN
B2082
17.148
9.616
33.159
1.00
21.21
N

ATOM
1537
CA
ASN
B2082
17.276
10.659
32.125
1.00
23.15
C

ATOM
1538
CB
ASN
B2082
15.898
11.236
31.770
1.00
24.29
C

ATOM
1539
CG
ASN
B2082
15.110
10.351
30.816
1.00
25.10
C

ATOM
1540
OD1
ASN
B2082
15.401
10.292
29.619
1.00
26.00
O

ATOM
1541
ND2
ASN
B2082
14.109
9.657
31.343
1.00
24.28
N

ATOM
1542
C
ASN
B2082
18.171
11.785
32.654
1.00
23.63
C

ATOM
1543
O
ASN
B2082
17.988
12.228
33.785
1.00
24.09
O

ATOM
1544
N
ASN
B2083
19.137
12.260
31.864
1.00
24.20
N

ATOM
1545
CA
ASN
B2083
20.001
13.328
32.376
1.00
25.17
C

ATOM
1546
CB
ASN
B2083
21.395
13.280
31.711
1.00
25.74
C

ATOM
1547
CG
ASN
B2083
21.405
13.770
30.270
1.00
25.64
C

ATOM
1548
OD1
ASN
B2083
22.425
13.652
29.584
1.00
27.52
O

ATOM
1549
ND2
ASN
B2083
20.299
14.327
29.810
1.00
24.85
N

ATOM
1550
C
ASN
B2083
19.356
14.718
32.279
1.00
25.54
C

ATOM
1551
O
ASN
B2083
18.214
14.844
31.831
1.00
25.60
O

ATOM
1552
N
GLU
B2084
20.067
15.759
32.706
1.00
26.28
N

ATOM
1553
CA
GLU
B2084
19.490
17.105
32.688
1.00
27.23
C

ATOM
1554
CB
GLU
B2084
20.378
18.083
33.479
1.00
28.30
C

ATOM
1555
CG
GLU
B2084
21.731
18.411
32.879
1.00
29.51
C

ATOM
1556
CD
GLU
B2084
22.612
19.175
33.860
1.00
31.00
C

ATOM
1557
OE1
GLU
B2084
22.065
19.983
34.645
1.00
31.91
O

ATOM
1558
OE2
GLU
B2084
23.847
18.976
33.847
1.00
30.61
O

ATOM
1559
C
GLU
B2084
19.153
17.675
31.307
1.00
27.45
C

ATOM
1560
O
GLU
B2084
18.514
18.725
31.207
1.00
27.41
O

ATOM
1561
N
ARG
B2085
19.569
16.986
30.244
1.00
27.72
N

ATOM
1562
CA
ARG
B2085
19.259
17.429
28.885
1.00
27.29
C

ATOM
1563
CB
ARG
B2085
20.490
17.355
27.976
1.00
29.07
C

ATOM
1564
CG
ARG
B2085
21.545
18.411
28.244
1.00
30.86
C

ATOM
1565
CD
ARG
B2085
22.540
18.483
27.089
1.00
33.01
C

ATOM
1566
NE
ARG
B2085
23.592
19.471
27.319
1.00
34.52
N

ATOM
1567
CZ
ARG
B2085
24.556
19.337
28.221
1.00
34.97
C

ATOM
1568
NH1
ARG
B2085
24.608
18.252
28.982
1.00
36.01
N

ATOM
1569
NH2
ARG
B2085
25.469
20.285
28.363
1.00
35.52
N

ATOM
1570
C
ARG
B2085
18.147
16.563
28.294
1.00
26.76
C

ATOM
1571
O
ARG
B2085
17.642
16.838
27.203
1.00
26.29
O

ATOM
1572
N
GLY
B2086
17.777
15.508
29.018
1.00
25.36
N

ATOM
1573
CA
GLY
B2086
16.721
14.623
28.558
1.00
24.19
C

ATOM
1574
C
GLY
B2086
17.156
13.325
27.896
1.00
23.02
C

ATOM
1575
O
GLY
B2086
16.305
12.537
27.475
1.00
22.83
O

ATOM
1576
N
ALA
B2087
18.462
13.083
27.798
1.00
21.71
N

ATOM
1577
CA
ALA
B2087
18.938
11.848
27.172
1.00
20.63
C

ATOM
1578
CB
ALA
B2087
20.336
12.055
26.576
1.00
21.15
C

ATOM
1579
C
ALA
B2087
18.955
10.671
28.157
1.00
19.81
C

ATOM
1580
O
ALA
B2087
19.364
10.824
29.315
1.00
18.56
O

ATOM
1581
N
PRO
B2088
18.505
9.479
27.707
1.00
18.87
N

ATOM
1582
CD
PRO
B2088
17.864
9.249
26.397
1.00
19.36
C

ATOM
1583
CA
PRO
B2088
18.461
8.258
28.530
1.00
17.76
C

ATOM
1584
CB
PRO
B2088
17.442
7.390
27.790
1.00
18.59
C

ATOM
1585
CG
PRO
B2088
17.719
7.724
26.358
1.00
18.87
C

ATOM
1586
C
PRO
B2088
19.831
7.571
28.650
1.00
16.87
C

ATOM
1587
O
PRO
B2088
20.593
7.559
27.688
1.00
15.25
O

ATOM
1588
N
TYR
B2089
20.130
7.002
29.826
1.00
16.14
N

ATOM
1589
CA
TYR
B2089
21.405
6.311
30.078
1.00
16.26
C

ATOM
1590
CB
TYR
B2089
22.510
7.344
30.377
1.00
17.32
C

ATOM
1591
CG
TYR
B2089
22.461
7.951
31.774
1.00
16.96
C

ATOM
1592
CD1
TYR
B2089
23.255
7.445
32.810
1.00
18.32
C

ATOM
1593
CE1
TYR
B2089
23.217
8.007
34.098
1.00
18.36
C

ATOM
1594
CD2
TYR
B2089
21.625
9.031
32.057
1.00
17.32
C

ATOM
1595
CE2
TYR
B2089
21.580
9.595
33.332
1.00
18.67
C

ATOM
1596
CZ
TYR
B2089
22.379
9.079
34.347
1.00
18.08
C

ATOM
1597
OH
TYR
B2089
22.337
9.654
35.601
1.00
19.43
O

ATOM
1598
C
TYR
B2089
21.313
5.311
31.250
1.00
16.51
C

ATOM
1599
O
TYR
B2089
20.453
5.455
32.127
1.00
16.59
O

ATOM
1600
N
PHE
B2090
22.191
4.304
31.261
1.00
16.46
N

ATOM
1601
CA
PHE
B2090
22.207
3.292
32.338
1.00
16.71
C

ATOM
1602
CB
PHE
B2090
22.803
1.953
31.855
1.00
15.86
C

ATOM
1603
CG
PHE
B2090
21.830
1.069
31.099
1.00
16.44
C

ATOM
1604
CD1
PHE
B2090
21.652
1.216
29.724
1.00
16.03
C

ATOM
1605
CD2
PHE
B2090
21.089
0.094
31.770
1.00
16.46
C

ATOM
1606
CE1
PHE
B2090
20.748
0.407
29.022
1.00
16.54
C

ATOM
1607
CE2
PHE
B2090
20.179
−0.723
31.084
1.00
16.80
C

ATOM
1608
CZ
PHE
B2090
20.008
−0.568
29.709
1.00
16.46
C

ATOM
1609
C
PHE
B2090
23.027
3.748
33.550
1.00
17.25
C

ATOM
1610
O
PHE
B2090
24.245
3.938
33.445
1.00
16.58
O

ATOM
1611
N
SER
B2091
22.372
3.900
34.700
1.00
16.92
N

ATOM
1612
CA
SER
B2091
23.068
4.312
35.922
1.00
18.02
C

ATOM
1613
CB
SER
B2091
22.148
5.177
36.802
1.00
18.33
C

ATOM
1614
OG
SER
B2091
20.902
4.535
37.052
1.00
17.93
O

ATOM
1615
C
SER
B2091
23.592
3.105
36.729
1.00
18.66
C

ATOM
1616
O
SER
B2091
24.479
3.255
37.582
1.00
18.83
O

ATOM
1617
N
GLN
B2092
23.048
1.920
36.448
1.00
18.75
N

ATOM
1618
CA
GLN
B2092
23.438
0.675
37.116
1.00
19.69
C

ATOM
1619
CB
GLN
B2092
22.526
0.377
38.313
1.00
21.62
C

ATOM
1620
CG
GLN
B2092
22.726
1.259
39.533
1.00
25.05
C

ATOM
1621
CD
GLN
B2092
21.981
0.730
40.746
1.00
27.87
C

ATOM
1622
OE1
GLN
B2092
20.775
0.944
40.900
1.00
29.82
O

ATOM
1623
NE2
GLN
B2092
22.696
0.018
41.611
1.00
29.02
N

ATOM
1624
C
GLN
B2092
23.336
−0.512
36.151
1.00
19.36
C

ATOM
1625
O
GLN
B2092
22.316
−0.678
35.486
1.00
18.36
O

ATOM
1626
N
ALA
B2093
24.383
−1.336
36.094
1.00
18.90
N

ATOM
1627
CA
ALA
B2093
24.411
−2.514
35.221
1.00
19.53
C

ATOM
1628
CB
ALA
B2093
24.441
−2.073
33.755
1.00
19.53
C

ATOM
1629
C
ALA
B2093
25.625
−3.407
35.524
1.00
20.13
C

ATOM
1630
O
ALA
B2093
26.641
−2.928
36.024
1.00
20.09
O

ATOM
1631
N
PRO
B2094
25.527
−4.720
35.239
1.00
21.00
N

ATOM
1632
CD
PRO
B2094
24.303
−5.472
34.892
1.00
21.48
C

ATOM
1633
CA
PRO
B2094
26.653
−5.631
35.498
1.00
21.95
C

ATOM
1634
CB
PRO
B2094
25.956
−6.963
35.744
1.00
22.34
C

ATOM
1635
CG
PRO
B2094
24.808
−6.905
34.739
1.00
22.42
C

ATOM
1636
C
PRO
B2094
27.613
−5.677
34.300
1.00
22.30
C

ATOM
1637
O
PRO
B2094
27.695
−6.690
33.594
1.00
22.45
O

ATOM
1638
N
PHE
B2095
28.331
−4.572
34.083
1.00
22.56
N

ATOM
1639
CA
PHE
B2095
29.267
−4.435
32.957
1.00
23.11
C

ATOM
1640
CB
PHE
B2095
28.471
−4.089
31.688
1.00
22.75
C

ATOM
1641
CG
PHE
B2095
29.307
−3.979
30.439
1.00
22.31
C

ATOM
1642
CD1
PHE
B2095
29.484
−2.746
29.812
1.00
22.23
C

ATOM
1643
CD2
PHE
B2095
29.898
−5.107
29.876
1.00
22.30
C

ATOM
1644
CE1
PHE
B2095
30.237
−2.639
28.640
1.00
22.73
C

ATOM
1645
CE2
PHE
B2095
30.655
−5.012
28.705
1.00
22.36
C

ATOM
1646
CZ
PHE
B2095
30.825
−3.774
28.085
1.00
21.98
C

ATOM
1647
C
PHE
B2095
30.305
−3.340
33.248
1.00
23.62
C

ATOM
1648
O
PHE
B2095
29.965
−2.284
33.778
1.00
23.96
O

ATOM
1649
N
SER
B2096
31.561
−3.584
32.884
1.00
24.19
N

ATOM
1650
CA
SER
B2096
32.636
−2.623
33.143
1.00
25.11
C

ATOM
1651
CB
SER
B2096
33.927
−3.376
33.477
1.00
26.30
C

ATOM
1652
OG
SER
B2096
33.722
−4.306
34.523
1.00
28.33
O

ATOM
1653
C
SER
B2096
32.954
−1.591
32.050
1.00
24.46
C

ATOM
1654
O
SER
B2096
33.606
−0.583
32.332
1.00
25.13
O

ATOM
1655
N
GLY
B2097
32.513
−1.828
30.818
1.00
23.39
N

ATOM
1656
CA
GLY
B2097
32.818
−0.891
29.739
1.00
21.60
C

ATOM
1657
C
GLY
B2097
31.823
0.242
29.527
1.00
20.27
C

ATOM
1658
O
GLY
B2097
31.138
0.651
30.460
1.00
20.10
O

ATOM
1659
N
LYS
B2098
31.756
0.758
28.299
1.00
19.44
N

ATOM
1660
CA
LYS
B2098
30.822
1.836
27.954
1.00
17.90
C

ATOM
1661
CB
LYS
B2098
31.472
2.822
26.978
1.00
20.19
C

ATOM
1662
CG
LYS
B2098
32.604
3.651
27.561
1.00
21.96
C

ATOM
1663
CD
LYS
B2098
33.055
4.682
26.543
1.00
24.18
C

ATOM
1664
CE
LYS
B2098
34.115
5.612
27.103
1.00
25.70
C

ATOM
1665
NZ
LYS
B2098
34.538
6.626
26.087
1.00
27.22
N

ATOM
1666
C
LYS
B2098
29.561
1.256
27.309
1.00
16.51
C

ATOM
1667
O
LYS
B2098
29.647
0.298
26.543
1.00
14.73
O

ATOM
1668
N
ILE
B2099
28.401
1.844
27.621
1.00
15.59
N

ATOM
1669
CA
ILE
B2099
27.107
1.395
27.086
1.00
15.02
C

ATOM
1670
CB
ILE
B2099
26.144
0.954
28.236
1.00
15.10
C

ATOM
1671
CG2
ILE
B2099
24.823
0.429
27.647
1.00
16.11
C

ATOM
1672
CG1
ILE
B2099
26.790
−0.138
29.095
1.00
15.18
C

ATOM
1673
CD1
ILE
B2099
25.994
−0.462
30.363
1.00
16.41
C

ATOM
1674
C
ILE
B2099
26.406
2.533
26.308
1.00
14.43
C

ATOM
1675
O
ILE
B2099
26.039
3.551
26.900
1.00
14.51
O

ATOM
1676
N
TRP
B2100
26.207
2.359
25.000
1.00
13.72
N

ATOM
1677
CA
TRP
B2100
25.547
3.381
24.173
1.00
13.62
C

ATOM
1678
CB
TRP
B2100
26.342
3.558
22.864
1.00
13.58
C

ATOM
1679
CG
TRP
B2100
27.817
3.938
23.093
1.00
13.89
C

ATOM
1680
CD2
TRP
B2100
28.334
5.257
23.347
1.00
13.95
C

ATOM
1681
CE2
TRP
B2100
29.726
5.126
23.597
1.00
14.82
C

ATOM
1682
CE3
TRP
B2100
27.755
6.535
23.395
1.00
14.46
C

ATOM
1683
CD1
TRP
B2100
28.890
3.085
23.187
1.00
14.49
C

ATOM
1684
NE1
TRP
B2100
30.041
3.795
23.492
1.00
14.89
N

ATOM
1685
CZ2
TRP
B2100
30.546
6.230
23.895
1.00
15.47
C

ATOM
1686
CZ3
TRP
B2100
28.577
7.640
23.697
1.00
15.28
C

ATOM
1687
CH2
TRP
B2100
29.955
7.472
23.942
1.00
14.88
C

ATOM
1688
C
TRP
B2100
24.071
2.998
23.886
1.00
13.84
C

ATOM
1689
O
TRP
B2100
23.816
1.995
23.214
1.00
13.89
O

ATOM
1690
N
LEU
B2101
23.120
3.808
24.379
1.00
13.08
N

ATOM
1691
CA
LEU
B2101
21.657
3.557
24.239
1.00
12.41
C

ATOM
1692
CB
LEU
B2101
21.059
3.267
25.634
1.00
13.29
C

ATOM
1693
CG
LEU
B2101
19.524
3.353
25.825
1.00
12.98
C

ATOM
1694
CD1
LEU
B2101
18.889
2.043
25.355
1.00
12.28
C

ATOM
1695
CD2
LEU
B2101
19.156
3.601
27.303
1.00
12.42
C

ATOM
1696
C
LEU
B2101
20.796
4.674
23.602
1.00
11.67
C

ATOM
1697
O
LEU
B2101
21.063
5.858
23.811
1.00
11.61
O

ATOM
1698
N
SER
B2102
19.760
4.287
22.844
1.00
11.90
N

ATOM
1699
CA
SER
B2102
18.799
5.237
22.237
1.00
11.37
C

ATOM
1700
CB
SER
B2102
19.212
5.616
20.810
1.00
11.79
C

ATOM
1701
OG
SER
B2102
18.405
6.679
20.308
1.00
9.95
O

ATOM
1702
C
SER
B2102
17.371
4.634
22.219
1.00
11.48
C

ATOM
1703
O
SER
B2102
17.220
3.421
22.026
1.00
11.63
O

ATOM
1704
N
ILE
B2103
16.351
5.482
22.425
1.00
10.47
N

ATOM
1705
CA
ILE
B2103
14.912
5.096
22.465
1.00
10.97
C

ATOM
1706
CB
ILE
B2103
14.337
5.250
23.934
1.00
11.04
C

ATOM
1707
CG2
ILE
B2103
12.852
4.835
23.981
1.00
11.15
C

ATOM
1708
CG1
ILE
B2103
15.136
4.390
24.924
1.00
10.41
C

ATOM
1709
CD1
ILE
B2103
14.781
4.658
26.424
1.00
10.59
C

ATOM
1710
C
ILE
B2103
14.042
5.995
21.536
1.00
11.56
C

ATOM
1711
O
ILE
B2103
14.327
7.184
21.393
1.00
11.36
O

ATOM
1712
N
SER
B2104
12.994
5.435
20.915
1.00
13.13
N

ATOM
1713
CA
SER
B2104
12.073
6.214
20.054
1.00
14.88
C

ATOM
1714
CB
SER
B2104
12.582
6.263
18.603
1.00
15.92
C

ATOM
1715
OG
SER
B2104
11.787
7.132
17.789
1.00
16.21
O

ATOM
1716
C
SER
B2104
10.652
5.617
20.070
1.00
15.87
C

ATOM
1717
O
SER
B2104
10.485
4.418
20.297
1.00
15.32
O

ATOM
1718
N
HIS
B2105
9.623
6.429
19.822
1.00
17.79
N

ATOM
1719
CA
HIS
B2105
8.266
5.872
19.833
1.00
19.31
C

ATOM
1720
CB
HIS
B2105
7.683
5.921
21.249
1.00
21.32
C

ATOM
1721
CG
HIS
B2105
7.405
7.306
21.746
1.00
23.02
C

ATOM
1722
CD2
HIS
B2105
6.279
8.058
21.704
1.00
25.09
C

ATOM
1723
ND1
HIS
B2105
8.363
8.086
22.356
1.00
25.22
N

ATOM
1724
CE1
HIS
B2105
7.841
9.260
22.669
1.00
25.65
C

ATOM
1725
NE2
HIS
B2105
6.577
9.269
22.285
1.00
26.41
N

ATOM
1726
C
HIS
B2105
7.237
6.486
18.870
1.00
20.14
C

ATOM
1727
O
HIS
B2105
7.453
7.560
18.305
1.00
18.58
O

ATOM
1728
N
THR
B2106
6.128
5.763
18.687
1.00
20.92
N

ATOM
1729
CA
THR
B2106
5.008
6.208
17.852
1.00
23.37
C

ATOM
1730
CB
THR
B2106
4.758
5.302
16.612
1.00
23.62
C

ATOM
1731
OG1
THR
B2106
4.237
4.035
17.039
1.00
24.37
O

ATOM
1732
CG2
THR
B2106
6.043
5.092
15.820
1.00
23.72
C

ATOM
1733
C
THR
B2106
3.766
6.106
18.735
1.00
23.79
C

ATOM
1734
O
THR
B2106
3.867
5.875
19.937
1.00
24.63
O

ATOM
1735
N
ASP
B2107
2.591
6.255
18.138
1.00
24.86
N

ATOM
1736
CA
ASP
B2107
1.355
6.176
18.906
1.00
24.83
C

ATOM
1737
CB
ASP
B2107
0.189
6.691
18.059
0.05
24.72
C

ATOM
1738
CG
ASP
B2107
−0.652
7.716
18.790
0.05
24.62
C

ATOM
1739
OD1
ASP
B2107
−1.227
7.372
19.844
0.05
24.64
O

ATOM
1740
OD2
ASP
B2107
−0.738
8.867
18.312
0.05
24.51
O

ATOM
1741
C
ASP
B2107
1.043
4.763
19.403
1.00
24.92
C

ATOM
1742
O
ASP
B2107
0.368
4.598
20.421
1.00
26.07
O

ATOM
1743
N
GLN
B2108
1.535
3.745
18.701
1.00
24.68
N

ATOM
1744
CA
GLN
B2108
1.255
2.361
19.086
1.00
24.22
C

ATOM
1745
CB
GLN
B2108
0.522
1.652
17.939
1.00
25.96
C

ATOM
1746
CG
GLN
B2108
−0.753
2.352
17.462
1.00
27.90
C

ATOM
1747
CD
GLN
B2108
−1.328
1.732
16.189
1.00
29.69
C

ATOM
1748
OE1
GLN
B2108
−2.371
1.073
16.215
1.00
31.19
O

ATOM
1749
NE2
GLN
B2108
−0.641
1.940
15.069
1.00
30.55
N

ATOM
1750
C
GLN
B2108
2.450
1.489
19.517
1.00
23.66
C

ATOM
1751
O
GLN
B2108
2.246
0.490
20.216
1.00
22.94
O

ATOM
1752
N
PHE
B2109
3.672
1.854
19.115
1.00
22.58
N

ATOM
1753
CA
PHE
B2109
4.869
1.058
19.450
1.00
22.19
C

ATOM
1754
CB
PHE
B2109
5.440
0.378
18.187
1.00
23.42
C

ATOM
1755
CG
PHE
B2109
4.409
−0.256
17.287
1.00
25.28
C

ATOM
1756
CD1
PHE
B2109
3.830
0.469
16.248
1.00
26.47
C

ATOM
1757
CD2
PHE
B2109
4.038
−1.586
17.459
1.00
26.35
C

ATOM
1758
CE1
PHE
B2109
2.894
−0.123
15.386
1.00
26.84
C

ATOM
1759
CE2
PHE
B2109
3.106
−2.190
16.607
1.00
27.41
C

ATOM
1760
CZ
PHE
B2109
2.534
−1.454
15.567
1.00
27.07
C

ATOM
1761
C
PHE
B2109
6.031
1.852
20.088
1.00
20.94
C

ATOM
1762
O
PHE
B2109
6.034
3.082
20.086
1.00
20.73
O

ATOM
1763
N
VAL
B2110
7.020
1.128
20.619
1.00
20.20
N

ATOM
1764
CA
VAL
B2110
8.225
1.737
21.210
1.00
18.93
C

ATOM
1765
CB
VAL
B2110
8.115
1.867
22.761
1.00
19.35
C

ATOM
1766
CG1
VAL
B2110
7.968
0.496
23.404
1.00
21.12
C

ATOM
1767
CG2
VAL
B2110
9.339
2.595
23.316
1.00
19.95
C

ATOM
1768
C
VAL
B2110
9.423
0.846
20.845
1.00
18.01
C

ATOM
1769
O
VAL
B2110
9.295
−0.380
20.827
1.00
17.84
O

ATOM
1770
N
THR
B2111
10.576
1.450
20.548
1.00
16.67
N

ATOM
1771
CA
THR
B2111
11.768
0.678
20.170
1.00
15.96
C

ATOM
1772
CB
THR
B2111
11.950
0.693
18.628
1.00
17.10
C

ATOM
1773
OG1
THR
B2111
13.011
−0.201
18.258
1.00
21.79
O

ATOM
1774
CG2
THR
B2111
12.283
2.096
18.141
1.00
17.28
C

ATOM
1775
C
THR
B2111
13.049
1.203
20.839
1.00
14.55
C

ATOM
1776
O
THR
B2111
13.122
2.380
21.194
1.00
12.59
O

ATOM
1777
N
ALA
B2112
14.044
0.326
21.005
1.00
13.42
N

ATOM
1778
CA
ALA
B2112
15.325
0.680
21.644
1.00
12.71
C

ATOM
1779
CB
ALA
B2112
15.247
0.379
23.145
1.00
12.85
C

ATOM
1780
C
ALA
B2112
16.516
−0.078
21.024
1.00
12.80
C

ATOM
1781
O
ALA
B2112
16.348
−1.196
20.535
1.00
13.45
O

ATOM
1782
N
SER
B2113
17.709
0.527
21.060
1.00
12.54
N

ATOM
1783
CA
SER
B2113
18.937
−0.077
20.498
1.00
12.67
C

ATOM
1784
CB
SER
B2113
19.222
0.539
19.115
1.00
12.72
C

ATOM
1785
OG
SER
B2113
20.402
0.007
18.523
1.00
13.88
O

ATOM
1786
C
SER
B2113
20.152
0.142
21.443
1.00
11.86
C

ATOM
1787
O
SER
B2113
20.326
1.247
21.973
1.00
12.14
O

ATOM
1788
N
VAL
B2114
20.967
−0.905
21.636
1.00
10.76
N

ATOM
1789
CA
VAL
B2114
22.157
−0.885
22.526
1.00
11.02
C

ATOM
1790
CB
VAL
B2114
21.912
−1.748
23.810
1.00
10.07
C

ATOM
1791
CG1
VAL
B2114
23.204
−1.874
24.619
1.00
12.63
C

ATOM
1792
CG2
VAL
B2114
20.808
−1.124
24.689
1.00
11.23
C

ATOM
1793
C
VAL
B2114
23.451
−1.438
21.880
1.00
11.08
C

ATOM
1794
O
VAL
B2114
23.408
−2.477
21.204
1.00
10.49
O

ATOM
1795
N
ILE
B2115
24.584
−0.753
22.093
1.00
11.85
N

ATOM
1796
CA
ILE
B2115
25.905
−1.198
21.585
1.00
11.88
C

ATOM
1797
CB
ILE
B2115
26.485
−0.236
20.492
1.00
12.44
C

ATOM
1798
CG2
ILE
B2115
27.841
−0.756
19.999
1.00
12.78
C

ATOM
1799
CG1
ILE
B2115
25.529
−0.134
19.300
1.00
12.56
C

ATOM
1800
CD1
ILE
B2115
25.889
0.986
18.331
1.00
12.68
C

ATOM
1801
C
ILE
B2115
26.883
−1.197
22.782
1.00
12.95
C

ATOM
1802
O
ILE
B2115
26.966
−0.197
23.507
1.00
13.03
O

ATOM
1803
N
LEU
B2116
27.600
−2.306
22.994
1.00
12.77
N

ATOM
1804
CA
LEU
B2116
28.559
−2.432
24.115
1.00
14.04
C

ATOM
1805
CB
LEU
B2116
28.353
−3.785
24.830
1.00
13.62
C

ATOM
1806
CG
LEU
B2116
26.929
−4.093
25.349
1.00
14.05
C

ATOM
1807
CD1
LEU
B2116
26.866
−5.489
25.971
1.00
15.37
C

ATOM
1808
CD2
LEU
B2116
26.520
−3.055
26.384
1.00
14.15
C

ATOM
1809
C
LEU
B2116
30.020
−2.296
23.630
1.00
14.81
C

ATOM
1810
O
LEU
B2116
30.381
−2.839
22.582
1.00
14.52
O

ATOM
1811
N
GLU
B2117
30.858
−1.605
24.409
1.00
16.40
N

ATOM
1812
CA
GLU
B2117
32.255
−1.353
24.027
1.00
18.58
C

ATOM
1813
CB
GLU
B2117
32.344
0.062
23.426
1.00
18.84
C

ATOM
1814
CG
GLU
B2117
33.737
0.570
23.061
1.00
21.74
C

ATOM
1815
CD
GLU
B2117
33.703
1.977
22.450
1.00
23.34
C

ATOM
1816
OE1
GLU
B2117
33.161
2.908
23.098
1.00
22.55
O

ATOM
1817
OE2
GLU
B2117
34.221
2.153
21.322
1.00
24.09
O

ATOM
1818
C
GLU
B2117
33.247
−1.495
25.196
1.00
20.32
C

ATOM
1819
O
GLU
B2117
32.989
−1.010
26.303
1.00
18.78
O

ATOM
1820
N
GLU
B2118
34.384
−2.141
24.931
1.00
22.46
N

ATOM
1821
CA
GLU
B2118
35.413
−2.366
25.949
1.00
26.31
C

ATOM
1822
CB
GLU
B2118
35.364
−3.830
26.415
1.00
28.48
C

ATOM
1823
CG
GLU
B2118
36.185
−4.151
27.657
1.00
31.58
C

ATOM
1824
CD
GLU
B2118
35.479
−3.793
28.952
1.00
33.18
C

ATOM
1825
OE1
GLU
B2118
34.479
−4.464
29.295
1.00
34.62
O

ATOM
1826
OE2
GLU
B2118
35.925
−2.839
29.628
1.00
34.75
O

ATOM
1827
C
GLU
B2118
36.820
−2.039
25.435
1.00
27.70
C

ATOM
1828
O
GLU
B2118
36.958
−1.559
24.285
1.00
28.17
O

ATOM
1829
OXT
GLU
B2118
37.784
−2.267
26.199
1.00
29.81
O

TER
1830

GLU
B2118

ATOM
1831
CB
MET
C3003
38.407
0.566
12.507
1.00
29.11
C

ATOM
1832
CG
MET
C3003
38.953
−0.372
11.436
1.00
32.10
C

ATOM
1833
SD
MET
C3003
39.971
0.467
10.186
1.00
36.76
S

ATOM
1834
CE
MET
C3003
41.535
0.656
11.078
1.00
35.20
C

ATOM
1835
C
MET
C3003
36.229
−0.625
12.723
1.00
24.49
C

ATOM
1836
O
MET
C3003
36.251
−1.743
12.216
1.00
24.23
O

ATOM
1837
N
MET
C3003
38.104
−1.203
14.236
1.00
26.20
N

ATOM
1838
CA
MET
C3003
37.432
−0.097
13.493
1.00
26.22
C

ATOM
1839
N
ILE
C3004
35.182
0.190
12.648
1.00
22.87
N

ATOM
1840
CA
ILE
C3004
33.960
−0.165
11.933
1.00
21.52
C

ATOM
1841
CB
ILE
C3004
32.800
0.781
12.355
1.00
21.32
C

ATOM
1842
CG2
ILE
C3004
31.535
0.469
11.557
1.00
21.05
C

ATOM
1843
CG1
ILE
C3004
32.547
0.638
13.864
1.00
20.83
C

ATOM
1844
CD1
ILE
C3004
31.537
1.615
14.443
1.00
20.25
C

ATOM
1845
C
ILE
C3004
34.199
−0.043
10.422
1.00
21.57
C

ATOM
1846
O
ILE
C3004
34.938
0.848
9.979
1.00
21.16
O

ATOM
1847
N
VAL
C3005
33.610
−0.952
9.638
1.00
20.59
N

ATOM
1848
CA
VAL
C3005
33.749
−0.906
8.182
1.00
20.63
C

ATOM
1849
CB
VAL
C3005
34.642
−2.068
7.628
1.00
21.47
C

ATOM
1850
CG1
VAL
C3005
36.083
−1.890
8.090
1.00
21.00
C

ATOM
1851
CG2
VAL
C3005
34.109
−3.413
8.076
1.00
23.00
C

ATOM
1852
C
VAL
C3005
32.413
−0.901
7.422
1.00
19.52
C

ATOM
1853
O
VAL
C3005
32.411
−0.880
6.192
1.00
19.11
O

ATOM
1854
N
GLY
C3006
31.289
−0.906
8.149
1.00
18.23
N

ATOM
1855
CA
GLY
C3006
29.974
−0.880
7.508
1.00
17.17
C

ATOM
1856
C
GLY
C3006
28.797
−0.986
8.482
1.00
16.61
C

ATOM
1857
O
GLY
C3006
28.963
−1.526
9.579
1.00
16.76
O

ATOM
1858
N
HIS
C3007
27.620
−0.477
8.093
1.00
15.51
N

ATOM
1859
CA
HIS
C3007
26.400
−0.531
8.935
1.00
15.40
C

ATOM
1860
CB
HIS
C3007
26.418
0.624
9.953
1.00
15.15
C

ATOM
1861
CG
HIS
C3007
25.191
0.709
10.821
1.00
14.61
C

ATOM
1862
C02
HIS
C3007
24.430
1.772
11.180
1.00
14.84
C

ATOM
1863
ND1
HIS
C3007
24.668
−0.377
11.493
1.00
15.01
N

ATOM
1864
CE1
HIS
C3007
23.639
0.013
12.229
1.00
15.56
C

ATOM
1865
NE2
HIS
C3007
23.475
1.313
12.058
1.00
15.15
N

ATOM
1866
C
HIS
C3007
25.086
−0.476
8.115
1.00
14.78
C

ATOM
1867
O
HIS
C3007
24.933
0.372
7.228
1.00
14.49
O

ATOM
1868
N
GLY
C3008
24.145
−1.376
8.418
1.00
14.82
N

ATOM
1869
CA
GLY
C3008
22.867
−1.390
7.709
1.00
14.90
C

ATOM
1870
C
GLY
C3008
21.668
−1.918
8.495
1.00
15.74
C

ATOM
1871
O
GLY
C3008
21.835
−2.757
9.391
1.00
14.75
O

ATOM
1872
N
ILE
C3009
20.465
−1.425
8.166
1.00
15.25
N

ATOM
1873
CA
ILE
C3009
19.211
−1.847
8.823
1.00
15.66
C

ATOM
1874
CB
ILE
C3009
18.692
−0.769
9.837
1.00
14.95
C

ATOM
1875
CG2
ILE
C3009
19.789
−0.421
10.873
1.00
15.05
C

ATOM
1876
CG1
ILE
C3009
18.261
0.492
9.079
1.00
14.33
C

ATOM
1877
CD1
ILE
C3009
17.632
1.555
9.956
1.00
14.63
C

ATOM
1878
C
ILE
C3009
18.090
−2.102
7.780
1.00
16.20
C

ATOM
1879
O
ILE
C3009
18.221
−1.696
6.619
1.00
16.14
O

ATOM
1880
N
ASP
C3010
17.004
−2.762
8.204
1.00
16.80
N

ATOM
1881
CA
ASP
C3010
15.853
−3.080
7.330
1.00
17.32
C

ATOM
1882
CB
ASP
C3010
16.130
−4.365
6.527
1.00
18.68
C

ATOM
1883
CG
ASP
C3010
14.977
−4.741
5.579
1.00
18.99
C

ATOM
1884
OD1
ASP
C3010
14.852
−4.105
4.518
1.00
19.45
O

ATOM
1885
OD2
ASP
C3010
14.193
−5.667
5.896
1.00
19.42
O

ATOM
1886
C
ASP
C3010
14.549
−3.290
8.120
1.00
18.11
C

ATOM
1887
O
ASP
C3010
14.580
−3.711
9.283
1.00
17.23
O

ATOM
1888
N
ILE
C3011
13.411
−2.978
7.488
1.00
17.97
N

ATOM
1889
CA
ILE
C3011
12.082
−3.191
8.081
1.00
18.54
C

ATOM
1890
CB
ILE
C3011
11.444
−1.876
8.656
1.00
18.66
C

ATOM
1891
CG2
ILE
C3011
11.363
−0.776
7.579
1.00
19.04
C

ATOM
1892
CG1
ILE
C3011
10.048
−2.185
9.211
1.00
19.19
C

ATOM
1893
CG1
ILE
C3011
9.421
−1.049
9.999
1.00
19.08
C

ATOM
1894
C
ILE
C3011
11.207
−3.762
6.950
1.00
18.75
C

ATOM
1895
O
ILE
C3011
11.286
−3.288
5.825
1.00
18.39
O

ATOM
1896
N
GLU
C3012
10.389
−4.774
7.253
1.00
19.66
N

ATOM
1897
CA
GLU
C3012
9.544
−5.433
6.246
1.00
20.80
C

ATOM
1898
CB
GLU
C3012
10.290
−6.663
5.706
1.00
22.15
C

ATOM
1899
CG
GLU
C3012
9.468
−7.566
4.774
1.00
23.49
C

ATOM
1900
CD
GLU
C3012
9.692
−7.274
3.300
1.00
24.70
C

ATOM
1901
OE1
GLU
C3012
10.294
−6.228
2.973
1.00
24.77
O

ATOM
1902
OE2
GLU
C3012
9.258
−8.095
2.460
1.00
25.50
O

ATOM
1903
C
GLU
C3012
8.160
−5.870
6.759
1.00
21.36
C

ATOM
1904
O
GLU
C3012
8.049
−6.431
7.848
1.00
20.37
O

ATOM
1905
N
GLU
C3013
7.111
−5.614
5.971
1.00
22.03
N

ATOM
1906
CA
GLU
C3013
5.743
−6.004
6.345
1.00
23.43
C

ATOM
1907
CB
GLU
C3013
4.703
−5.207
5.534
1.00
24.60
C

ATOM
1908
CG
GLU
C3013
4.706
−3.683
5.716
1.00
26.52
C

ATOM
1909
CD
GLU
C3013
4.063
−3.212
7.018
1.00
28.49
C

ATOM
1910
OE1
GLU
C3013
3.071
−3.834
7.467
1.00
28.55
O

ATOM
1911
OE2
GLU
C3013
4.533
−2.192
7.579
1.00
28.72
O

ATOM
1912
C
GLU
C3013
5.517
−7.501
6.075
1.00
23.35
C

ATOM
1913
O
GLU
C3013
5.931
−8.012
5.032
1.00
23.44
O

ATOM
1914
N
LEU
C3014
4.855
−8.198
7.000
1.00
23.78
N

ATOM
1915
CA
LEU
C3014
4.578
−9.627
6.818
1.00
24.31
C

ATOM
1916
CB
LEU
C3014
3.922
−10.227
8.071
1.00
24.95
C

ATOM
1917
CG
LEU
C3014
4.664
−10.149
9.417
1.00
27.00
C

ATOM
1918
CD1
LEU
C3014
3.957
−11.044
10.423
1.00
27.46
C

ATOM
1919
CD2
LEU
C3014
6.118
−10.589
9.258
1.00
26.69
C

ATOM
1920
C
LEU
C3014
3.660
−9.867
5.608
1.00
24.29
C

ATOM
1921
O
LEU
C3014
3.680
−10.939
5.004
1.00
23.68
O

ATOM
1922
N
ALA
C3015
2.857
−8.868
5.262
1.00
24.50
N

ATOM
1923
CA
ALA
C3015
1.946
−8.984
4.120
1.00
24.91
C

ATOM
1924
CB
ALA
C3015
1.082
−7.732
4.016
1.00
25.04
C

ATOM
1925
C
ALA
C3015
2.691
−9.220
2.803
1.00
25.57
C

ATOM
1926
O
ALA
C3015
2.215
−9.962
1.940
1.00
25.88
O

ATOM
1927
N
SER
C3016
3.857
−8.592
2.648
1.00
25.61
N

ATOM
1928
CA
SER
C3016
4.658
−8.737
1.432
1.00
25.91
C

ATOM
1929
CB
SER
C3016
5.829
−7.742
1.441
1.00
26.86
C

ATOM
1930
OG
SER
C3016
5.385
−6.401
1.589
1.00
27.09
O

ATOM
1931
C
SER
C3016
5.204
−10.159
1.275
1.00
26.38
C

ATOM
1932
O
SER
C3016
5.276
−10.690
0.161
1.00
25.43
O

ATOM
1933
N
ILE
C3017
5.603
−10.768
2.390
1.00
26.46
N

ATOM
1934
CA
ILE
C3017
6.128
−12.131
2.365
1.00
26.86
C

ATOM
1935
CB
ILE
C3017
6.839
−12.474
3.706
1.00
26.57
C

ATOM
1936
CG2
ILE
C3017
7.306
−13.925
3.709
1.00
26.15
C

ATOM
1937
CG1
ILE
C3017
8.029
−11.526
3.923
1.00
26.30
C

ATOM
1938
CD1
ILE
C3017
9.102
−11.612
2.842
1.00
26.29
C

ATOM
1939
C
ILE
C3017
4.986
−13.129
2.121
1.00
28.01
C

ATOM
1940
O
ILE
C3017
5.160
−14.133
1.426
1.00
27.90
O

ATOM
1941
N
GLU
C3018
3.816
−12.837
2.679
1.00
28.89
N

ATOM
1942
CA
GLU
C3018
2.657
−13.713
2.530
1.00
30.68
C

ATOM
1943
CB
GLU
C3018
1.527
−13.250
3.456
1.00
31.08
C

ATOM
1944
CG
GLU
C3018
1.936
−13.180
4.919
1.00
32.50
C

ATOM
1945
CD
GLU
C3018
0.853
−12.614
5.817
1.00
33.07
C

ATOM
1946
OE1
GLU
C3018
0.161
−11.663
5.395
1.00
33.76
O

ATOM
1947
OE2
GLU
C3018
0.704
−13.108
6.955
1.00
33.50
O

ATOM
1948
C
GLU
C3018
2.144
−13.796
1.092
1.00
31.38
C

ATOM
1949
O
GLU
C3018
1.736
−14.868
0.639
1.00
31.29
O

ATOM
1950
N
SER
C3019
2.166
−12.677
0.372
1.00
32.24
N

ATOM
1951
CA
SER
C3019
1.691
−12.676
−1.008
1.00
33.36
C

ATOM
1952
CB
SER
C3019
1.420
−11.240
−1.494
1.00
33.64
C

ATOM
1953
OG
SER
C3019
2.610
−10.547
−1.838
1.00
34.47
O

ATOM
1954
C
SER
C3019
2.706
−13.364
−1.918
1.00
34.14
C

ATOM
1955
O
SER
C3019
2.331
−14.055
−2.864
1.00
34.07
O

ATOM
1956
N
ALA
C3020
3.989
−13.191
−1.611
1.00
34.65
N

ATOM
1957
CA
ALA
C3020
5.061
−13.791
−2.399
1.00
35.89
C

ATOM
1958
CB
ALA
C3020
6.415
−13.247
−1.938
1.00
35.73
C

ATOM
1959
C
ALA
C3020
5.071
−15.322
−2.347
1.00
36.89
C

ATOM
1960
O
ALA
C3020
5.451
−15.978
−3.317
1.00
36.66
O

ATOM
1961
N
VAL
C3021
4.663
−15.891
−1.217
1.00
38.20
N

ATOM
1962
CA
VAL
C3021
4.640
−17.343
−1.078
1.00
40.04
C

ATOM
1963
CB
VAL
C3021
4.270
−17.770
0.362
1.00
40.00
C

ATOM
1964
CG1
VAL
C3021
4.180
−19.285
0.445
1.00
40.22
C

ATOM
1965
CG2
VAL
C3021
5.310
−17.255
1.347
1.00
40.17
C

ATOM
1966
C
VAL
C3021
3.636
−17.969
−2.043
1.00
41.37
C

ATOM
1967
O
VAL
C3021
3.939
−18.954
−2.718
1.00
41.44
O

ATOM
1968
N
THR
C3022
2.443
−17.387
−2.105
1.00
42.72
N

ATOM
1969
CA
THR
C3022
1.382
−17.883
−2.974
1.00
44.38
C

ATOM
1970
CB
THR
C3022
0.049
−17.160
−2.683
1.00
43.84
C

ATOM
1971
OG1
THR
C3022
−0.341
−17.403
−1.326
1.00
43.59
O

ATOM
1972
CG2
THR
C3022
−1.048
−17.665
−3.612
1.00
43.81
C

ATOM
1973
C
THR
C3022
1.703
−17.738
−4.461
1.00
45.84
C

ATOM
1974
O
THR
C3022
1.725
−18.730
−5.193
1.00
45.92
O

ATOM
1975
N
ARG
C3023
1.951
−16.508
−4.906
1.00
47.48
N

ATOM
1976
CA
ARG
C3023
2.250
−16.253
−6.313
1.00
49.27
C

ATOM
1977
CB
ARG
C3023
2.771
−14.823
−6.502
1.00
49.46
C

ATOM
1978
CG
ARG
C3023
2.801
−14.390
−7.958
1.00
49.98
C

ATOM
1979
CD
ARG
C3023
2.939
−12.884
−8.125
1.00
50.04
C

ATOM
1980
NE
ARG
C3023
4.288
−12.399
−7.854
0.05
50.32
N

ATOM
1981
CZ
ARG
C3023
4.694
−11.158
−8.105
0.05
50.40
C

ATOM
1982
NH1
ARG
C3023
3.853
−10.279
−8.634
0.05
50.48
N

ATOM
1983
NH2
ARG
C3023
5.940
−10.797
−7.833
0.05
50.49
N

ATOM
1984
C
ARG
C3023
3.260
−17.259
−6.861
1.00
50.29
C

ATOM
1985
O
ARG
C3023
2.889
−18.186
−7.580
1.00
50.77
O

ATOM
1986
N
HIS
C3024
4.532
−17.074
−6.526
1.00
51.47
N

ATOM
1987
CA
HIS
C3024
5.581
−17.988
−6.970
1.00
52.39
C

ATOM
1988
CB
HIS
C3024
6.822
−17.207
−7.410
0.05
52.53
C

ATOM
1989
CG
HIS
C3024
7.108
−17.304
−8.876
0.05
52.72
C

ATOM
1990
CD2
HIS
C3024
7.177
−16.353
−9.838
0.05
52.78
C

ATOM
1991
ND1
HIS
C3024
7.367
−18.503
−9.505
0.05
52.78
N

ATOM
1992
CE1
HIS
C3024
7.583
−18.287
−10.790
0.05
52.83
C

ATOM
1993
NE2
HIS
C3024
7.474
−16.990
−11.018
0.05
52.83
N

ATOM
1994
C
HIS
C3024
5.931
−18.911
−5.806
1.00
53.02
C

ATOM
1995
O
HIS
C3024
6.822
−18.613
−5.013
1.00
52.97
O

ATOM
1996
N
GLU
C3025
5.222
−20.032
−5.712
1.00
53.71
N

ATOM
1997
CA
GLU
C3025
5.430
−20.992
−4.632
1.00
54.23
C

ATOM
1998
CB
GLU
C3025
4.308
−22.035
−4.647
1.00
55.24
C

ATOM
1999
CG
GLU
C3025
4.150
−22.772
−5.965
1.00
56.63
C

ATOM
2000
CD
GLU
C3025
2.869
−23.585
−6.024
1.00
57.48
C

ATOM
2001
OE1
GLU
C3025
2.657
−24.435
−5.131
1.00
58.10
O

ATOM
2002
OE2
GLU
C3025
2.075
−23.372
−6.966
1.00
57.87
O

ATOM
2003
C
GLU
C3025
6.796
−21.684
−4.626
1.00
53.75
C

ATOM
2004
O
GLU
C3025
6.916
−22.841
−4.227
1.00
53.95
O

ATOM
2005
N
GLY
C3026
7.820
−20.961
−5.068
1.00
53.15
N

ATOM
2006
CA
GLY
C3026
9.171
−21.492
−5.080
1.00
51.80
C

ATOM
2007
C
GLY
C3026
10.057
−20.503
−4.340
1.00
50.97
C

ATOM
2008
O
GLY
C3026
11.260
−20.712
−4.167
1.00
50.85
O

ATOM
2009
N
PHE
C3027
9.426
−19.418
−3.899
1.00
49.86
N

ATOM
2010
CA
PHE
C3027
10.077
−18.331
−3.173
1.00
48.78
C

ATOM
2011
CB
PHE
C3027
9.001
−17.419
−2.570
1.00
48.81
C

ATOM
2012
CG
PHE
C3027
9.546
−16.198
−1.884
1.00
48.66
C

ATOM
2013
CD1
PHE
C3027
10.279
−15.252
−2.593
1.00
48.61
C

ATOM
2014
CD2
PHE
C3027
9.313
−15.986
−0.527
1.00
48.69
C

ATOM
2015
CE1
PHE
C3027
10.772
−14.111
−1.962
1.00
48.58
C

ATOM
2016
CE2
PHE
C3027
9.802
−14.849
0.113
1.00
48.35
C

ATOM
2017
CZ
PHE
C3027
10.533
−13.910
−0.606
1.00
48.38
C

ATOM
2018
C
PHE
C3027
11.037
−18.795
−2.076
1.00
47.88
C

ATOM
2019
O
PHE
C3027
12.188
−18.364
−2.027
1.00
47.77
O

ATOM
2020
N
ALA
C3028
10.558
−19.676
−1.205
1.00
47.03
N

ATOM
2021
CA
ALA
C3028
11.362
−20.186
−0.097
1.00
46.36
C

ATOM
2022
CB
ALA
C3028
10.529
−21.147
0.741
1.00
46.30
C

ATOM
2023
C
ALA
C3028
12.668
−20.862
−0.519
1.00
45.98
C

ATOM
2024
O
ALA
C3028
13.735
−20.562
0.026
1.00
46.02
O

ATOM
2025
N
LYS
C3029
12.585
−21.774
−1.483
1.00
44.97
N

ATOM
2026
CA
LYS
C3029
13.762
−22.497
−1.952
1.00
44.02
C

ATOM
2027
CB
LYS
C3029
13.377
−23.478
−3.065
1.00
44.26
C

ATOM
2028
CG
LYS
C3029
12.440
−24.589
−2.621
0.05
44.27
C

ATOM
2029
CD
LYS
C3029
12.186
−25.576
−3.749
0.05
44.38
C

ATOM
2030
CE
LYS
C3029
11.290
−26.717
−3.296
0.05
44.42
C

ATOM
2031
NZ
LYS
C3029
11.066
−27.712
−4.380
0.05
44.48
N

ATOM
2032
C
LYS
C3029
14.878
−21.586
−2.444
1.00
43.30
C

ATOM
2033
O
LYS
C3029
16.055
−21.926
−2.330
1.00
43.66
O

ATOM
2034
N
ARG
C3030
14.516
−20.429
−2.988
1.00
42.33
N

ATOM
2035
CA
ARG
C3030
15.515
−19.498
−3.495
1.00
41.38
C

ATOM
2036
CB
ARG
C3030
14.933
−18.685
−4.655
1.00
41.73
C

ATOM
2037
CG
ARG
C3030
14.577
−19.527
−5.870
0.05
41.77
C

ATOM
2038
CD
ARG
C3030
14.062
−18.672
−7.016
0.05
41.90
C

ATOM
2039
NE
ARG
C3030
13.773
−19.474
−8.202
0.05
42.00
N

ATOM
2040
CZ
ARG
C3030
13.329
−18.977
−9.351
0.05
42.04
C

ATOM
2041
NH1
ARG
C3030
13.092
−19.784
−10.377
0.05
42.08
N

ATOM
2042
NH2
ARG
C3030
13.119
−17.674
−9.476
0.05
42.08
N

ATOM
2043
C
ARG
C3030
16.073
−18.551
−2.435
1.00
40.66
C

ATOM
2044
O
ARG
C3030
17.141
−17.969
−2.620
1.00
40.56
O

ATOM
2045
N
VAL
C3031
15.357
−18.402
−1.324
1.00
39.61
N

ATOM
2046
CA
VAL
C3031
15.797
−17.509
−0.252
1.00
38.51
C

ATOM
2047
CB
VAL
C3031
14.593
−16.737
0.354
1.00
38.68
C

ATOM
2048
CG1
VAL
C3031
15.046
−15.899
1.545
1.00
39.01
C

ATOM
2049
CG2
VAL
C3031
13.964
−15.843
−0.703
1.00
39.32
C

ATOM
2050
C
VAL
C3031
16.535
−18.222
0.887
1.00
37.22
C

ATOM
2051
O
VAL
C3031
17.392
−17.625
1.540
1.00
36.96
O

ATOM
2052
N
LEU
C3032
16.215
−19.494
1.109
1.00
35.97
N

ATOM
2053
CA
LEU
C3032
16.825
−20.268
2.194
1.00
35.20
C

ATOM
2054
CB
LEU
C3032
15.713
−20.865
3.062
1.00
34.43
C

ATOM
2055
CG
LEU
C3032
14.682
−19.887
3.635
1.00
34.07
C

ATOM
2056
CD1
LEU
C3032
13.508
−20.658
4.224
1.00
34.12
C

ATOM
2057
CD2
LEU
C3032
15.340
−19.010
4.694
1.00
33.54
C

ATOM
2058
C
LEU
C3032
17.774
−21.395
1.756
1.00
35.04
C

ATOM
2059
O
LEU
C3032
17.592
−21.997
0.696
1.00
34.60
O

ATOM
2060
N
THR
C3033
18.780
−21.679
2.584
1.00
34.45
N

ATOM
2061
CA
THR
C3033
19.729
−22.755
2.293
1.00
34.22
C

ATOM
2062
CB
THR
C3033
21.050
−22.619
3.096
1.00
33.96
C

ATOM
2063
OG1
THR
C3033
20.797
−22.889
4.481
1.00
33.02
O

ATOM
2064
CG2
THR
C3033
21.630
−21.222
2.953
1.00
34.21
C

ATOM
2065
C
THR
C3033
19.063
−24.063
2.720
1.00
34.16
C

ATOM
2066
O
THR
C3033
17.968
−24.052
3.279
1.00
33.78
O

ATOM
2067
N
ALA
C3034
19.729
−25.185
2.472
1.00
34.40
N

ATOM
2068
CA
ALA
C3034
19.178
−26.487
2.839
1.00
34.48
C

ATOM
2069
CB
ALA
C3034
20.103
−27.598
2.350
1.00
34.65
C

ATOM
2070
C
ALA
C3034
18.927
−26.638
4.341
1.00
34.51
C

ATOM
2071
O
ALA
C3034
17.867
−27.117
4.751
1.00
34.56
O

ATOM
2072
N
LEU
C3035
19.895
−26.233
5.162
1.00
34.52
N

ATOM
2073
CA
LEU
C3035
19.755
−26.345
6.612
1.00
34.61
C

ATOM
2074
CB
LEU
C3035
21.087
−26.047
7.308
1.00
34.52
C

ATOM
2075
CG
LEU
C3035
21.101
−26.182
8.834
0.05
34.52
C

ATOM
2076
CD1
LEU
C3035
20.741
−27.607
9.228
0.05
34.51
C

ATOM
2077
CD2
LEU
C3035
22.475
−25.814
9.369
0.05
34.53
C

ATOM
2078
C
LEU
C3035
18.675
−25.414
7.156
1.00
35.00
C

ATOM
2079
O
LEU
C3035
17.965
−25.769
8.098
1.00
35.04
O

ATOM
2080
N
GLU
C3036
18.558
−24.222
6.574
1.00
35.33
N

ATOM
2081
CA
GLU
C3036
17.537
−23.263
7.004
1.00
35.62
C

ATOM
2082
CB
GLU
C3036
17.741
−21.907
6.310
1.00
34.70
C

ATOM
2083
CG
GLU
C3036
18.809
−21.006
6.941
1.00
33.21
C

ATOM
2084
CD
GLU
C3036
19.117
−19.767
6.103
1.00
32.82
C

ATOM
2085
OE1
GLU
C3036
19.598
−18.759
6.671
1.00
31.24
O

ATOM
2086
OE2
GLU
C3036
18.893
−19.803
4.873
1.00
32.21
O

ATOM
2087
C
GLU
C3036
16.155
−23.815
6.654
1.00
36.75
C

ATOM
2088
O
GLU
C3036
15.205
−23.687
7.427
1.00
36.40
O

ATOM
2089
N
MET
C3037
16.064
−24.436
5.481
1.00
38.24
N

ATOM
2090
CA
MET
C3037
14.821
−25.018
4.981
1.00
40.09
C

ATOM
2091
CB
MET
C3037
15.064
−25.625
3.596
1.00
41.14
C

ATOM
2092
CG
MET
C3037
13.808
−26.028
2.834
1.00
43.15
C

ATOM
2093
SD
MET
C3037
12.851
−24.618
2.239
1.00
45.06
S

ATOM
2094
CE
MET
C3037
11.189
−25.242
2.400
1.00
44.92
C

ATOM
2095
C
MET
C3037
14.270
−26.089
5.926
1.00
40.63
C

ATOM
2096
O
MET
C3037
13.061
−26.171
6.151
1.00
40.94
O

ATOM
2097
N
GLU
C3038
15.159
−26.911
6.473
1.00
41.23
N

ATOM
2098
CA
GLU
C3038
14.752
−27.969
7.393
1.00
41.49
C

ATOM
2099
CB
GLU
C3038
15.982
−28.713
7.924
1.00
41.61
C

ATOM
2100
CG
GLU
C3038
16.711
−29.544
6.878
0.05
41.50
C

ATOM
2101
CD
GLU
C3038
15.889
−30.721
6.385
0.05
41.51
C

ATOM
2102
OE1
GLU
C3038
16.376
−31.459
5.503
0.05
41.48
O

ATOM
2103
OE2
GLU
C3038
14.758
−30.911
6.880
0.05
41.45
O

ATOM
2104
C
GLU
C3038
13.958
−27.391
8.559
1.00
41.78
C

ATOM
2105
O
GLU
C3038
12.984
−27.989
9.013
1.00
41.81
O

ATOM
2106
N
ARG
C3039
14.384
−26.226
9.037
1.00
42.11
N

ATOM
2107
CA
ARG
C3039
13.716
−25.550
10.146
1.00
42.69
C

ATOM
2108
CB
ARG
C3039
14.580
−24.380
10.634
1.00
43.67
C

ATOM
2109
CG
ARG
C3039
13.950
−23.514
11.722
1.00
45.06
C

ATOM
2110
CD
ARG
C3039
13.752
−24.276
13.026
1.00
46.69
C

ATOM
2111
NE
ARG
C3039
13.295
−23.394
14.099
1.00
47.90
N

ATOM
2112
CZ
ARG
C3039
12.966
−23.803
15.321
1.00
48.72
C

ATOM
2113
NH1
ARG
C3039
13.040
−25.089
15.637
1.00
49.17
N

ATOM
2114
NH2
ARG
C3039
12.563
−22.925
16.230
1.00
49.02
N

ATOM
2115
C
ARG
C3039
12.343
−25.034
9.714
1.00
42.44
C

ATOM
2116
O
ARG
C3039
11.360
−25.153
10.448
1.00
42.21
O

ATOM
2117
N
PHE
C3040
12.293
−24.467
8.512
1.00
42.44
N

ATOM
2118
CA
PHE
C3040
11.064
−23.909
7.948
1.00
42.58
C

ATOM
2119
CB
PHE
C3040
11.343
−23.394
6.529
1.00
41.84
C

ATOM
2120
CG
PHE
C3040
10.165
−22.713
5.879
1.00
41.26
C

ATOM
2121
CD1
PHE
C3040
9.621
−21.556
6.428
1.00
40.76
C

ATOM
2122
CD2
PHE
C3040
9.610
−23.223
4.708
1.00
40.96
C

ATOM
2123
CE1
PHE
C3040
8.541
−20.915
5.821
1.00
40.74
C

ATOM
2124
CE2
PHE
C3040
8.527
−22.590
4.090
1.00
40.92
C

ATOM
2125
CZ
PHE
C3040
7.992
−21.433
4.649
1.00
40.88
C

ATOM
2126
C
PHE
C3040
9.899
−24.902
7.913
1.00
43.12
C

ATOM
2127
O
PHE
C3040
8.790
−24.585
8.343
1.00
42.92
O

ATOM
2128
N
THR
C3041
10.156
−26.104
7.406
1.00
43.77
N

ATOM
2129
CA
THR
C3041
9.119
−27.126
7.303
1.00
44.43
C

ATOM
2130
CB
THR
C3041
9.569
−22.283
6.395
1.00
44.80
C

ATOM
2131
OG1
THR
C3041
10.703
−28.936
6.978
1.00
45.05
O

ATOM
2132
CG2
THR
C3041
9.935
−27.759
5.016
1.00
45.00
C

ATOM
2133
C
THR
C3041
8.676
−27.719
8.635
1.00
44.57
C

ATOM
2134
O
THR
C3041
7.611
−28.327
8.721
1.00
44.92
O

ATOM
2135
N
SER
C3042
9.488
−27.548
9.672
1.00
44.91
N

ATOM
2136
CA
SER
C3042
9.160
−28.091
10.986
1.00
44.98
C

ATOM
2137
CB
SER
C3042
10.439
−28.297
11.801
1.00
45.18
C

ATOM
2138
OG
SER
C3042
11.336
−29.151
11.110
1.00
45.91
O

ATOM
2139
C
SER
C3042
8.194
−27.212
11.770
1.00
44.99
C

ATOM
2140
O
SER
C3042
7.536
−27.683
12.699
1.00
45.11
O

ATOM
2141
N
LEU
C3043
8.112
−25.938
11.397
1.00
44.68
N

ATOM
2142
CA
LEU
C3043
7.228
−24.993
12.073
1.00
44.47
C

ATOM
2143
CB
LEU
C3043
7.882
−23.608
12.124
1.00
44.33
C

ATOM
2144
CG
LEU
C3043
9.250
−23.485
12.797
1.00
44.21
C

ATOM
2145
CD1
LEU
C3043
9.761
−22.052
12.662
1.00
44.22
C

ATOM
2146
CD2
LEU
C3043
9.139
−23.875
14.265
1.00
44.47
C

ATOM
2147
C
LEU
C3043
5.888
−24.899
11.347
1.00
44.31
C

ATOM
2148
O
LEU
C3043
5.738
−25.422
10.240
1.00
44.09
O

ATOM
2149
N
LYS
C3044
4.923
−24.221
11.965
1.00
44.27
N

ATOM
2150
CA
LYS
C3044
3.601
−24.064
11.365
1.00
44.15
C

ATOM
2151
CB
LYS
C3044
2.703
−25.234
11.777
1.00
45.11
C

ATOM
2152
CG
LYS
C3044
1.429
−25.375
10.953
1.00
46.10
C

ATOM
2153
CD
LYS
C3044
0.462
−26.398
11.547
1.00
47.10
C

ATOM
2154
CE
LYS
C3044
1.099
−27.774
11.701
1.00
47.88
C

ATOM
2155
NZ
LYS
C3044
2.155
−27.802
12.758
1.00
48.36
N

ATOM
2156
C
LYS
C3044
2.924
−22.745
11.753
1.00
43.58
C

ATOM
2157
O
LYS
C3044
3.349
−22.062
12.687
1.00
43.58
O

ATOM
2158
N
GLY
C3045
1.868
−22.397
11.022
1.00
42.72
N

ATOM
2159
CA
GLY
C3045
1.129
−21.177
11.299
1.00
41.65
C

ATOM
2160
C
GLY
C3045
1.932
−19.893
11.197
1.00
40.64
C

ATOM
2161
O
GLY
C3045
2.788
−19.749
10.323
1.00
40.57
O

ATOM
2162
N
ARG
C3046
1.644
−18.956
12.097
1.00
39.78
N

ATOM
2163
CA
ARG
C3046
2.327
−17.666
12.129
1.00
38.64
C

ATOM
2164
CB
ARG
C3046
1.752
−16.792
13.249
1.00
38.93
C

ATOM
2165
CG
ARG
C3046
2.393
−15.415
13.350
0.05
38.89
C

ATOM
2166
CD
ARG
C3046
1.769
−14.591
14.465
0.05
38.99
C

ATOM
2167
NE
ARG
C3046
0.346
−14.352
14.241
0.05
39.04
N

ATOM
2168
CZ
ARG
C3046
−0.428
−13.636
15.050
0.05
39.08
C

ATOM
2169
NH1
ARG
C3046
−1.713
−13.471
14.768
0.05
39.09
N

ATOM
2170
NH2
ARG
C3046
0.084
−13.084
16.142
0.05
39.12
N

ATOM
2171
C
ARG
C3046
3.826
−17.840
12.338
1.00
37.81
C

ATOM
2172
O
ARG
C3046
4.629
−17.130
11.735
1.00
37.34
O

ATOM
2173
N
ARG
C3047
4.195
−18.785
13.198
1.00
36.94
N

ATOM
2174
CA
ARG
C3047
5.601
−19.056
13.485
1.00
35.80
C

ATOM
2175
CB
ARG
C3047
5.727
−20.255
14.424
1.00
37.34
C

ATOM
2176
CG
ARG
C3047
5.554
−19.924
15.887
1.00
38.72
C

ATOM
2177
CD
ARG
C3047
5.695
−21.177
16.731
1.00
40.55
C

ATOM
2178
NE
ARG
C3047
6.145
−20.870
18.083
1.00
41.86
N

ATOM
2179
CZ
ARG
C3047
7.328
−20.335
18.369
1.00
42.33
C

ATOM
2180
NH1
ARG
C3047
8.181
−20.050
17.395
1.00
43.10
N

ATOM
2181
NH2
ARG
C3047
7.659
−20.087
19.629
1.00
42.88
N

ATOM
2182
C
ARG
C3047
6.408
−19.329
12.223
1.00
34.36
C

ATOM
2183
O
ARG
C3047
7.518
−18.812
12.057
1.00
33.67
O

ATOM
2184
N
GLN
C3048
5.852
−20.152
11.340
1.00
32.32
N

ATOM
2185
CA
GLN
C3048
6.522
−20.493
10.095
1.00
30.19
C

ATOM
2186
CB
GLN
C3048
5.709
−21.538
9.326
1.00
30.56
C

ATOM
2187
CG
GLN
C3048
6.346
−21.947
8.010
1.00
31.08
C

ATOM
2188
CD
GLN
C3048
5.545
−22.989
7.256
1.00
31.55
C

ATOM
2189
OE1
GLN
C3048
4.363
−22.793
6.971
1.00
32.61
O

ATOM
2190
NE2
GLN
C3048
6.189
−24.100
6.919
1.00
31.23
N

ATOM
2191
C
GLN
C3048
6.749
−19.266
9.211
1.00
28.78
C

ATOM
2192
O
GLN
C3048
7.816
−19.113
8.615
1.00
27.77
O

ATOM
2193
N
ILE
C3049
5.747
−18.396
9.124
1.00
27.16
N

ATOM
2194
CA
ILE
C3049
5.862
−17.195
8.298
1.00
26.51
C

ATOM
2195
CB
ILE
C3049
4.485
−16.521
8.086
1.00
26.30
C

ATOM
2196
CG2
ILE
C3049
4.647
−15.250
7.255
1.00
26.17
C

ATOM
2197
CG1
ILE
C3049
3.530
−17.491
7.380
1.00
26.22
C

ATOM
2198
CD1
ILE
C3049
4.023
−17.978
6.014
1.00
26.61
C

ATOM
2199
C
ILE
C3049
6.831
−16.178
8.910
1.00
25.94
C

ATOM
2200
O
ILE
C3049
7.570
−15.510
8.192
1.00
25.27
O

ATOM
2201
N
GLU
C3050
6.824
−16.069
10.236
1.00
26.02
N

ATOM
2202
CA
GLU
C3050
7.716
−15.141
10.935
1.00
25.96
C

ATOM
2203
CB
GLU
C3050
7.347
−15.075
12.423
1.00
27.39
C

ATOM
2204
CG
GLU
C3050
6.073
−14.287
12.724
1.00
29.92
C

ATOM
2205
CD
GLU
C3050
6.345
−12.853
13.175
1.00
31.52
C

ATOM
2206
OE1
GLU
C3050
7.446
−12.322
12.894
1.00
32.57
O

ATOM
2207
OE2
GLU
C3050
5.444
−12.252
13.802
1.00
31.86
O

ATOM
2208
C
GLU
C3050
9.195
−15.521
10.792
1.00
24.88
C

ATOM
2209
O
GLU
C3050
10.061
−14.650
10.815
1.00
24.17
O

ATOM
2210
N
TYR
C3051
9.481
−16.815
10.652
1.00
23.54
N

ATOM
2211
CA
TYR
C3051
10.863
−17.281
10.508
1.00
22.59
C

ATOM
2212
CB
TYR
C3051
10.941
−18.808
10.711
1.00
23.12
C

ATOM
2213
CG
TYR
C3051
12.317
−19.425
10.473
1.00
23.17
C

ATOM
2214
CD1
TYR
C3051
12.685
−19.902
9.213
1.00
23.85
C

ATOM
2215
CE1
TYR
C3051
13.954
−20.454
8.984
1.00
24.32
C

ATOM
2216
CD2
TYR
C3051
13.253
−19.515
11.504
1.00
24.30
C

ATOM
2217
CE2
TYR
C3051
14.528
−20.064
11.288
1.00
24.54
C

ATOM
2218
CZ
TYR
C3051
14.868
−20.528
10.026
1.00
24.99
C

ATOM
2219
OH
TYR
C3051
16.122
−21.050
9.803
1.00
25.78
O

ATOM
2220
C
TYR
C3051
11.419
−16.894
9.140
1.00
22.18
C

ATOM
2221
O
TYR
C3051
12.546
−16.395
9.031
1.00
20.97
O

ATOM
2222
N
LEU
C3052
10.618
−17.115
8.101
1.00
21.39
N

ATOM
2223
CA
LEU
C3052
11.016
−16.787
6.736
1.00
21.55
C

ATOM
2224
CB
LEU
C3052
9.935
−17.254
5.747
1.00
22.13
C

ATOM
2225
CG
LEU
C3052
10.124
−16.929
4.259
1.00
21.93
C

ATOM
2226
CD1
LEU
C3052
11.439
−17.515
3.755
1.00
22.55
C

ATOM
2227
CD2
LEU
C3052
8.958
−17.495
3.469
1.00
22.75
C

ATOM
2228
C
LEU
C3052
11.245
−15.284
6.574
1.00
21.31
C

ATOM
2229
O
LEU
C3052
12.196
−14.866
5.914
1.00
21.85
O

ATOM
2230
N
ALA
C3053
10.371
−14.484
7.181
1.00
20.68
N

ATOM
2231
CA
ALA
C3053
10.454
−13.025
7.102
1.00
20.75
C

ATOM
2232
CB
ALA
C3053
9.203
−12.401
7.738
1.00
20.99
C

ATOM
2233
C
ALA
C3053
11.720
−12.469
7.768
1.00
20.60
C

ATOM
2234
O
ALA
C3053
12.356
−11.552
7.237
1.00
20.36
O

ATOM
2235
N
GLY
C3054
12.073
−13.027
8.925
1.00
20.45
N

ATOM
2236
CA
GLY
C3054
13.264
−12.597
9.646
1.00
20.63
C

ATOM
2237
C
GLY
C3054
14.576
−12.928
8.945
1.00
20.53
C

ATOM
2238
O
GLY
C3054
15.550
−12.174
9.034
1.00
19.61
O

ATOM
2239
N
ARG
C3055
14.620
−14.065
8.256
1.00
20.88
N

ATOM
2240
CA
ARG
C3055
15.824
−14.457
7.527
1.00
21.09
C

ATOM
2241
CB
ARG
C3055
15.731
−15.930
7.101
1.00
21.81
C

ATOM
2242
CG
ARG
C3055
16.533
−16.895
7.988
1.00
23.24
C

ATOM
2243
CD
ARG
C3055
16.139
−16.801
9.465
1.00
23.82
C

ATOM
2244
NE
ARG
C3055
17.018
−17.600
10.325
1.00
23.91
N

ATOM
2245
CZ
ARG
C3055
16.881
−17.706
11.646
1.00
24.64
C

ATOM
2246
NH1
ARG
C3055
15.901
−17.065
12.267
1.00
23.93
N

ATOM
2247
NH2
ARG
C3055
17.719
−18.459
12.352
1.00
25.21
N

ATOM
2248
C
ARG
C3055
16.017
−13.552
6.301
1.00
21.23
C

ATOM
2249
O
ARG
C3055
17.142
−13.234
5.921
1.00
20.84
O

ATOM
2250
N
TRP
C3056
14.911
−13.132
5.694
1.00
21.62
N

ATOM
2251
CA
TRP
C3056
14.958
−12.247
4.529
1.00
22.92
C

ATOM
2252
CB
TRP
C3056
13.559
−12.121
3.910
1.00
25.18
C

ATOM
2253
CG
TRP
C3056
13.515
−11.388
2.594
1.00
27.65
C

ATOM
2254
CD2
TRP
C3056
13.357
−9.977
2.401
1.00
28.51
C

ATOM
2255
CE2
TRP
C3056
13.413
−9.736
1.009
1.00
29.11
C

ATOM
2256
CE3
TRP
C3056
13.176
−8.892
3.269
1.00
29.11
C

ATOM
2257
CD1
TRP
C3056
13.656
−11.931
1.344
1.00
28.78
C

ATOM
2258
NE1
TRP
C3056
13.596
−10.944
0.388
1.00
29.88
N

ATOM
2259
CZ2
TRP
C3056
13.296
−8.453
0.465
1.00
28.95
C

ATOM
2260
CZ3
TRP
C3056
13.060
−7.614
2.726
1.00
29.68
C

ATOM
2261
CH2
TRP
C3056
13.121
−7.409
1.336
1.00
29.31
C

ATOM
2262
C
TRP
C3056
15.453
−10.855
4.953
1.00
22.17
C

ATOM
2263
O
TRP
C3056
16.286
−10.247
4.281
1.00
22.33
O

ATOM
2264
N
SER
C3057
14.942
−10.365
6.078
1.00
21.01
N

ATOM
2265
CA
SER
C3057
15.311
−9.041
6.587
1.00
20.66
C

ATOM
2266
CB
SER
C3057
14.388
−8.663
7.751
1.00
21.23
C

ATOM
2267
OG
SER
C3057
14.569
−7.311
8.147
1.00
22.78
O

ATOM
2268
C
SER
C3057
16.786
−8.969
7.025
1.00
20.18
C

ATOM
2269
O
SER
C3057
17.464
−7.959
6.803
1.00
19.84
O

ATOM
2270
N
ALA
C3058
17.280
−10.043
7.633
1.00
18.66
N

ATOM
2271
CA
ALA
C3058
18.671
−10.090
8.085
1.00
18.83
C

ATOM
2272
CB
ALA
C3058
18.905
−11.344
8.939
1.00
17.30
C

ATOM
2273
C
ALA
C3058
19.663
−10.062
6.915
1.00
18.44
C

ATOM
2274
O
ALA
C3058
20.693
−9.381
6.980
1.00
18.07
O

ATOM
2275
N
LYS
C3059
19.359
−10.803
5.851
1.00
18.60
N

ATOM
2276
CA
LYS
C3059
20.252
−10.850
4.692
1.00
18.76
C

ATOM
2277
CB
LYS
C3059
19.848
−12.012
3.766
1.00
18.60
C

ATOM
2278
CG
LYS
C3059
19.956
−13.396
4.447
1.00
18.86
C

ATOM
2279
CD
LYS
C3059
19.739
−14.578
3.494
1.00
19.28
C

ATOM
2280
CE
LYS
C3059
19.815
−15.920
4.244
1.00
20.00
C

ATOM
2281
NZ
LYS
C3059
19.590
−17.130
3.388
1.00
20.93
N

ATOM
2282
C
LYS
C3059
20.274
−9.508
3.938
1.00
19.50
C

ATOM
2283
O
LYS
C3059
21.306
−9.117
3.388
1.00
20.13
O

ATOM
2284
N
GLU
C3060
19.142
−8.804
3.935
1.00
20.20
N

ATOM
2285
CA
GLU
C3060
19.026
−7.501
3.277
1.00
20.95
C

ATOM
2286
CB
GLU
C3060
17.550
−7.090
3.205
1.00
23.10
C

ATOM
2287
CG
GLU
C3060
17.268
−5.738
2.545
1.00
26.69
C

ATOM
2288
CD
GLU
C3060
17.579
−5.717
1.055
1.00
29.57
C

ATOM
2289
OE1
GLU
C3060
17.161
−6.660
0.341
1.00
30.70
O

ATOM
2290
OE2
GLU
C3060
18.232
−4.749
0.598
1.00
31.10
O

ATOM
2291
C
GLU
C3060
19.837
−6.432
4.030
1.00
20.53
C

ATOM
2292
O
GLU
C3060
20.455
−5.563
3.414
1.00
20.28
O

ATOM
2293
N
ALA
C3061
19.838
−6.497
5.360
1.00
19.74
N

ATOM
2294
CA
ALA
C3061
20.591
−5.531
6.165
1.00
19.24
C

ATOM
2295
CB
ALA
C3061
20.252
−5.696
7.656
1.00
19.62
C

ATOM
2296
C
ALA
C3061
22.097
−5.711
5.938
1.00
18.92
C

ATOM
2297
O
ALA
C3061
22.848
−4.732
5.885
1.00
18.37
O

ATOM
2298
N
PHE
C3062
22.530
−6.963
5.811
1.00
18.75
N

ATOM
2299
CA
PHE
C3062
23.941
−7.270
5.570
1.00
19.65
C

ATOM
2300
CB
PHE
C3062
24.190
−8.783
5.714
1.00
19.70
C

ATOM
2301
CG
PHE
C3062
25.592
−9.224
5.325
1.00
20.12
C

ATOM
2302
CD1
PHE
C3062
25.917
−9.472
3.988
1.00
20.55
C

ATOM
2303
CD2
PHE
C3062
26.577
−9.391
6.293
1.00
20.19
C

ATOM
2304
CE1
PHE
C3062
27.200
−9.883
3.622
1.00
21.03
C

ATOM
2305
CE2
PHE
C3062
27.871
−9.803
5.940
1.00
20.44
C

ATOM
2306
CZ
PHE
C3062
28.181
−10.049
4.598
1.00
20.96
C

ATOM
2307
C
PHE
C3062
24.381
−6.784
4.182
1.00
20.13
C

ATOM
2308
O
PHE
C3062
25.474
−6.231
4.037
1.00
20.04
O

ATOM
2309
N
SER
C3063
23.530
−6.981
3.174
1.00
21.29
N

ATOM
2310
CA
SER
C3063
23.840
−6.551
1.808
1.00
22.13
C

ATOM
2311
CB
SER
C3063
22.727
−6.967
0.832
1.00
22.59
C

ATOM
2312
OG
SER
C3063
22.699
−8.374
0.636
1.00
24.36
O

ATOM
2313
C
SER
C3063
24.019
−5.032
1.762
1.00
22.61
C

ATOM
2314
O
SER
C3063
24.913
−4.527
1.082
1.00
22.10
O

ATOM
2315
N
LYS
C3064
23.160
−4.309
2.477
1.00
22.80
N

ATOM
2316
CA
LYS
C3064
23.257
−2.852
2.530
1.00
24.07
C

ATOM
2317
CB
LYS
C3064
22.013
−2.261
3.210
1.00
23.92
C

ATOM
2318
CG
LYS
C3064
20.734
−2.376
2.377
1.00
23.95
C

ATOM
2319
CD
LYS
C3064
19.505
−1.886
3.138
1.00
24.12
C

ATOM
2320
CE
LYS
C3064
19.616
−0.407
3.519
1.00
24.30
C

ATOM
2321
NZ
LYS
C3064
18.388
0.060
4.209
1.00
24.43
N

ATOM
2322
C
LYS
C3064
24.519
−2.408
3.281
1.00
24.84
C

ATOM
2323
O
LYS
C3064
25.132
−1.401
2.939
1.00
24.90
O

ATOM
2324
N
ALA
C3065
24.916
−3.166
4.297
1.00
26.22
N

ATOM
2325
CA
ALA
C3065
26.101
−2.818
5.079
1.00
28.20
C

ATOM
2326
CB
ALA
C3065
26.184
−3.693
6.324
1.00
28.57
C

ATOM
2327
C
ALA
C3065
27.396
−2.943
4.277
1.00
30.15
C

ATOM
2328
O
ALA
C3065
28.346
−2.188
4.492
1.00
29.72
O

ATOM
2329
N
MET
C3066
27.435
−3.903
3.361
1.00
32.11
N

ATOM
2330
CA
MET
C3066
28.629
−4.113
2.555
1.00
35.57
C

ATOM
2331
CB
MET
C3066
28.706
−5.577
2.115
1.00
36.03
C

ATOM
2332
CG
MET
C3066
30.087
−5.993
1.635
1.00
38.01
C

ATOM
2333
SD
MET
C3066
30.589
−7.586
2.315
1.00
39.43
S

ATOM
2334
CE
MET
C3066
29.820
−8.664
1.141
1.00
38.43
C

ATOM
2335
C
MET
C3066
28.641
−3.186
1.340
1.00
37.25
C

ATOM
2336
O
MET
C3066
29.690
−2.928
0.753
1.00
37.48
O

ATOM
2337
N
GLY
C3067
27.468
−2.678
0.978
1.00
39.12
N

ATOM
2338
CA
GLY
C3067
27.372
−1.782
−0.158
1.00
41.84
C

ATOM
2339
C
GLY
C3067
27.338
−2.554
−1.458
1.00
43.68
C

ATOM
2340
O
GLY
C3067
28.251
−2.446
−2.277
1.00
44.30
O

ATOM
2341
N
THR
C3068
26.281
−3.337
−1.648
1.00
45.16
N

ATOM
2342
CA
THR
C3068
26.133
−4.140
−2.853
1.00
46.52
C

ATOM
2343
CB
THR
C3068
27.012
−5.409
−2.771
1.00
46.98
C

ATOM
2344
OG1
THR
C3068
26.723
−6.268
−3.880
1.00
47.83
O

ATOM
2345
CG2
THR
C3068
26.756
−6.154
−1.469
1.00
47.19
C

ATOM
2346
C
THR
C3068
24.679
−4.546
−3.076
1.00
47.27
C

ATOM
2347
O
THR
C3068
23.940
−4.800
−2.123
1.00
47.53
O

ATOM
2348
N
GLY
C3069
24.272
−4.597
−4.341
1.00
47.97
N

ATOM
2349
CA
GLY
C3069
22.908
−4.969
−4.668
1.00
48.41
C

ATOM
2350
C
GLY
C3069
22.848
−6.140
−5.629
1.00
48.94
C

ATOM
2351
O
GLY
C3069
22.349
−5.952
−6.758
1.00
49.17
O

ATOM
2352
OXT
GLY
C3069
23.304
−7.244
−5.257
1.00
49.26
O

TER
2353

GLY
C3069

ATOM
2354
C
GLY
C3074
23.102
−14.343
−2.448
1.00
42.87
C

ATOM
2355
O
GLY
C3074
23.918
−14.155
−1.552
1.00
43.22
O

ATOM
2356
N
GLY
C3074
23.249
−12.549
−4.163
1.00
43.05
N

ATOM
2357
CA
GLY
C3074
23.446
−14.000
−3.885
1.00
42.94
C

ATOM
2358
N
PHE
C3075
21.892
−14.845
−2.228
1.00
42.82
N

ATOM
2359
CA
PHE
C3075
21.441
−15.212
−0.890
1.00
42.97
C

ATOM
2360
CB
PHE
C3075
19.920
−15.035
−0.787
1.00
43.13
C

ATOM
2361
CG
PHE
C3075
19.484
−13.638
−0.400
1.00
43.82
C

ATOM
2362
CD1
PHE
C3075
20.299
−12.534
−0.647
1.00
43.85
C

ATOM
2363
CD2
PHE
C3075
18.243
−13.429
0.199
1.00
43.74
C

ATOM
2364
CE1
PHE
C3075
19.883
−11.243
−0.304
1.00
44.03
C

ATOM
2365
CE2
PHE
C3075
17.817
−12.144
0.545
1.00
44.13
C

ATOM
2366
CZ
PHE
C3075
18.639
−11.049
0.293
1.00
44.14
C

ATOM
2367
C
PHE
C3075
21.826
−16.639
−0.516
1.00
42.74
C

ATOM
2368
O
PHE
C3075
21.820
−17.007
0.661
1.00
42.92
O

ATOM
2369
N
GLN
C3076
22.175
−17.438
−1.518
1.00
42.00
N

ATOM
2370
CA
GLN
C3076
22.548
−18.824
−1.276
1.00
41.00
C

ATOM
2371
CB
GLN
C3076
22.537
−19.615
−2.587
1.00
41.57
C

ATOM
2372
CG
GLN
C3076
21.135
−19.865
−3.119
1.00
42.06
C

ATOM
2373
CD
GLN
C3076
20.286
−20.695
−2.171
1.00
42.45
C

ATOM
2374
OE1
GLN
C3076
19.056
−20.670
−2.243
1.00
42.81
O

ATOM
2375
NE2
GLN
C3076
20.938
−21.445
−1.284
1.00
42.52
N

ATOM
2376
C
GLN
C3076
23.892
−18.977
−0.584
1.00
40.27
C

ATOM
2377
O
GLN
C3076
24.216
−20.060
−0.103
1.00
40.25
O

ATOM
2378
N
ASP
C3077
24.682
−17.907
−0.537
1.00
38.81
N

ATOM
2379
CA
ASP
C3077
25.965
−17.981
0.148
1.00
37.42
C

ATOM
2380
CB
ASP
C3077
27.107
−17.527
−0.769
1.00
39.03
C

ATOM
2381
CG
ASP
C3077
27.008
−16.075
−1.152
1.00
40.35
C

ATOM
2382
OD1
ASP
C3077
25.897
−15.635
−1.514
1.00
41.46
O

ATOM
2383
OD2
ASP
C3077
28.048
−15.379
−1.102
1.00
40.89
O

ATOM
2384
C
ASP
C3077
25.926
−17.158
1.438
1.00
35.34
C

ATOM
2385
O
ASP
C3077
26.916
−16.556
1.848
1.00
35.66
O

ATOM
2386
N
LEU
C3078
24.751
−17.142
2.060
1.00
32.99
N

ATOM
2387
CA
LEU
C3078
24.513
−16.456
3.328
1.00
30.22
C

ATOM
2388
CB
LEU
C3078
23.775
−15.127
3.113
1.00
30.01
C

ATOM
2389
CG
LEU
C3078
24.478
−13.972
2.393
1.00
30.35
C

ATOM
2390
CD1
LEU
C3078
23.555
−12.762
2.352
1.00
29.89
C

ATOM
2391
CD2
LEU
C3078
25.768
−13.615
3.114
1.00
31.03
C

ATOM
2392
C
LEU
C3078
23.632
−17.392
4.165
1.00
27.99
C

ATOM
2393
O
LEU
C3078
22.645
−17.927
3.659
1.00
27.40
O

ATOM
2394
N
GLU
C3079
23.984
−17.589
5.435
1.00
25.61
N

ATOM
2395
CA
GLU
C3079
23.206
−18.467
6.310
1.00
24.01
C

ATOM
2396
CB
GLU
C3079
23.815
−19.876
6.284
1.00
24.83
C

ATOM
2397
CG
GLU
C3079
23.137
−20.897
7.190
1.00
25.45
C

ATOM
2398
CD
GLU
C3079
23.716
−22.290
7.022
1.00
26.01
C

ATOM
2399
OE1
GLU
C3079
23.270
−23.022
6.110
1.00
26.62
O

ATOM
2400
OE2
GLU
C3079
24.627
−22.648
7.797
1.00
25.76
O

ATOM
2401
C
GLU
C3079
23.113
−17.945
7.756
1.00
22.32
C

ATOM
2402
O
GLU
C3079
24.113
−17.500
8.335
1.00
21.78
O

ATOM
2403
N
VAL
C3080
21.905
−18.007
8.319
1.00
20.99
N

ATOM
2404
CA
VAL
C3080
21.616
−17.554
9.685
1.00
19.93
C

ATOM
2405
CB
VAL
C3080
20.634
−16.347
9.666
1.00
19.55
C

ATOM
2406
CG1
VAL
C3080
20.302
−15.911
11.099
1.00
18.41
C

ATOM
2407
CG2
VAL
C3080
21.246
−15.183
8.878
1.00
19.42
C

ATOM
2408
C
VAL
C3080
20.992
−18.667
10.550
1.00
20.28
C

ATOM
2409
O
VAL
C3080
19.888
−19.140
10.261
1.00
19.70
O

ATOM
2410
N
LEU
C3081
21.701
−19.075
11.606
1.00
20.21
N

ATOM
2411
CA
LEU
C3081
21.232
−20.121
12.521
1.00
21.05
C

ATOM
2412
CB
LEU
C3081
22.240
−21.290
12.559
1.00
21.12
C

ATOM
2413
CG
LEU
C3081
22.698
−21.950
11.246
1.00
20.96
C

ATOM
2414
CD1
LEU
C3081
23.699
−23.067
11.542
1.00
21.74
C

ATOM
2415
CD2
LEU
C3081
21.497
−22.498
10.489
1.00
20.34
C

ATOM
2416
C
LEU
C3081
21.041
−19.566
13.948
1.00
21.83
C

ATOM
2417
O
LEU
C3081
21.340
−18.399
14.211
1.00
20.95
O

ATOM
2418
N
ASN
C3082
20.546
−20.411
14.855
1.00
22.96
N

ATOM
2419
CA
ASN
C3082
20.322
−20.043
16.262
1.00
24.19
C

ATOM
2420
CB
ASN
C3082
18.857
−20.281
16.654
1.00
24.95
C

ATOM
2421
CG
ASN
C3082
17.913
−19.223
16.101
1.00
25.21
C

ATOM
2422
OD1
ASN
C3082
17.843
−18.100
16.611
1.00
26.05
O

ATOM
2423
ND2
ASN
C3082
17.184
−19.577
15.055
1.00
24.39
N

ATOM
2424
C
ASN
C3082
21.212
−20.890
17.184
1.00
24.76
C

ATOM
2425
O
ASN
C3082
21.268
−22.114
17.034
1.00
24.23
O

ATOM
2426
N
ASN
C3083
21.901
−20.258
18.133
1.00
24.88
N

ATOM
2427
CA
ASN
C3083
22.753
−21.024
19.046
1.00
26.41
C

ATOM
2428
CB
ASN
C3083
23.880
−20.147
19.619
1.00
26.57
C

ATOM
2429
CG
ASN
C3083
23.394
−19.088
20.603
1.00
27.00
C

ATOM
2430
OD1
ASN
C3083
24.185
−18.255
21.047
1.00
28.80
O

ATOM
2431
ND2
ASN
C3083
22.114
−19.115
20.952
1.00
25.26
N

ATOM
2432
C
ASN
C3083
21.922
−21.676
20.159
1.00
26.81
C

ATOM
2433
O
ASN
C3083
20.697
−21.536
20.178
1.00
26.49
O

ATOM
2434
N
GLU
C3084
22.567
−22.390
21.078
1.00
27.91
N

ATOM
2435
CA
GLU
C3084
21.815
−23.070
22.132
1.00
28.75
C

ATOM
2436
CB
GLU
C3084
22.716
−24.035
22.917
1.00
29.93
C

ATOM
2437
CG
GLU
C3084
24.064
−23.506
23.335
1.00
31.45
C

ATOM
2438
CD
GLU
C3084
24.916
−24.594
23.966
1.00
32.85
C

ATOM
2439
OE1
GLU
C3084
26.051
−24.298
24.397
1.00
33.48
O

ATOM
2440
OE2
GLU
C3084
24.445
−25.752
24.029
1.00
33.46
O

ATOM
2441
C
GLU
C3084
21.024
−22.189
23.092
1.00
28.50
C

ATOM
2442
O
GLU
C3084
20.074
−22.664
23.714
1.00
28.13
O

ATOM
2443
N
ARG
C3085
21.399
−20.917
23.215
1.00
28.57
N

ATOM
2444
CA
ARG
C3085
20.661
−20.001
24.085
1.00
28.82
C

ATOM
2445
CB
ARG
C3085
21.584
−18.929
24.670
1.00
29.93
C

ATOM
2446
CG
ARG
C3085
22.566
−19.469
25.692
1.00
31.34
C

ATOM
2447
CD
ARG
C3085
22.949
−18.409
26.713
1.00
33.11
C

ATOM
2448
NE
ARG
C3085
23.902
−18.936
27.683
1.00
33.67
N

ATOM
2449
CZ
ARG
C3085
25.167
−19.217
27.398
1.00
34.16
C

ATOM
2450
NH1
ARG
C3085
25.630
−19.014
26.171
1.00
34.21
N

ATOM
2451
NH2
ARG
C3085
25.965
−19.715
28.330
1.00
33.81
N

ATOM
2452
C
ARG
C3085
19.519
−19.332
23.318
1.00
28.44
C

ATOM
2453
O
ARG
C3085
18.663
−18.667
23.912
1.00
28.67
O

ATOM
2454
N
GLY
C3086
19.522
−19.496
21.996
1.00
27.15
N

ATOM
2455
CA
GLY
C3086
18.466
−18.928
21.170
1.00
26.89
C

ATOM
2456
C
GLY
C3086
18.800
−17.712
20.316
1.00
26.43
C

ATOM
2457
O
GLY
C3086
17.942
−17.229
19.581
1.00
26.94
O

ATOM
2458
N
ALA
C3087
20.031
−17.218
20.396
1.00
25.34
N

ATOM
2459
CA
ALA
C3087
20.432
−16.043
19.622
1.00
25.00
C

ATOM
2460
CB
ALA
C3087
21.610
−15.361
20.300
1.00
25.01
C

ATOM
2461
C
ALA
C3087
20.788
−16.355
18.163
1.00
24.71
C

ATOM
2462
O
ALA
C3087
21.385
−17.394
17.867
1.00
23.78
O

ATOM
2463
N
PRO
C3088
20.413
−15.457
17.231
1.00
23.74
N

ATOM
2464
CD
PRO
C3088
19.533
−14.291
17.448
1.00
24.91
C

ATOM
2465
CA
PRO
C3088
20.697
−15.631
15.800
1.00
23.12
C

ATOM
2466
CB
PRO
C3088
19.628
−14.762
15.136
1.00
24.34
C

ATOM
2467
CG
PRO
C3088
19.551
−13.593
16.083
1.00
24.53
C

ATOM
2468
C
PRO
C3088
22.115
−15.157
15.466
1.00
22.17
C

ATOM
2469
O
PRO
C3088
22.606
−14.198
16.070
1.00
21.42
O

ATOM
2470
N
TYR
C3089
22.765
−15.826
14.512
1.00
20.38
N

ATOM
2471
CA
TYR
C3089
24.128
−15.469
14.098
1.00
19.72
C

ATOM
2472
CB
TYR
C3089
25.149
−16.054
15.097
1.00
19.67
C

ATOM
2473
CG
TYR
C3089
25.352
−17.564
15.029
1.00
19.93
C

ATOM
2474
CD1
TYR
C3089
26.410
−18.110
14.294
1.00
21.07
C

ATOM
2475
CE1
TYR
C3089
26.594
−19.497
14.194
1.00
20.45
C

ATOM
2476
CD2
TYR
C3089
24.477
−18.446
15.672
1.00
20.53
C

ATOM
2477
CE2
TYR
C3089
24.653
−19.848
15.578
1.00
20.54
C

ATOM
2478
CZ
TYR
C3089
25.717
−20.359
14.833
1.00
20.66
C

ATOM
2479
OH
TYR
C3089
25.908
−21.725
14.713
1.00
19.20
O

ATOM
2480
C
TYR
C3089
24.428
−15.972
12.671
1.00
19.17
C

ATOM
2481
O
TYR
C3089
23.820
−16.944
12.213
1.00
17.72
O

ATOM
2482
N
PHE
C3090
25.340
−15.295
11.967
1.00
19.73
N

ATOM
2483
CA
PHE
C3090
25.729
−15.704
10.607
1.00
20.26
C

ATOM
2484
CB
PHE
C3090
26.310
−14.529
9.800
1.00
20.96
C

ATOM
2485
CG
PHE
C3090
25.274
−13.607
9.198
1.00
20.15
C

ATOM
2486
CD1
PHE
C3090
24.812
−12.499
9.902
1.00
20.78
C

ATOM
2487
CD2
PHE
C3090
24.791
−13.831
7.912
1.00
20.37
C

ATOM
2488
CE1
PHE
C3090
23.880
−11.620
9.330
1.00
20.73
C

ATOM
2489
CE2
PHE
C3090
23.860
−12.964
7.326
1.00
20.67
C

ATOM
2490
CZ
PHE
C3090
23.404
−11.853
8.040
1.00
20.35
C

ATOM
2491
C
PHE
C3090
26.788
−16.812
10.637
1.00
20.91
C

ATOM
2492
O
PHE
C3090
27.905
−16.598
11.117
1.00
20.54
O

ATOM
2493
N
SER
C3091
26.442
−17.986
10.116
1.00
21.82
N

ATOM
2494
CA
SER
C3091
27.378
−19.113
10.073
1.00
22.73
C

ATOM
2495
CB
SER
C3091
26.630
−20.435
10.290
1.00
22.96
C

ATOM
2496
OG
SER
C3091
25.613
−20.617
9.318
1.00
23.28
O

ATOM
2497
C
SER
C3091
28.137
−19.164
8.738
1.00
23.33
C

ATOM
2498
O
SER
C3091
29.114
−19.904
8.604
1.00
22.86
O

ATOM
2499
N
GLN
C3092
27.683
−18.375
7.762
1.00
23.62
N

ATOM
2500
CA
GLN
C3092
28.309
−18.319
6.436
1.00
24.85
C

ATOM
2501
CB
GLN
C3092
27.730
−19.439
5.558
1.00
25.88
C

ATOM
2502
CG
GLN
C3092
28.045
−19.357
4.064
1.00
28.11
C

ATOM
2503
CD
GLN
C3092
29.529
−19.339
3.762
1.00
29.40
C

ATOM
2504
OE1
GLN
C3092
30.298
−20.131
4.310
1.00
31.43
O

ATOM
2505
NE2
GLN
C3092
29.940
−18.441
2.874
1.00
30.15
N

ATOM
2506
C
GLN
C3092
28.107
−16.944
5.764
1.00
24.73
C

ATOM
2507
O
GLN
C3092
26.974
−16.472
5.637
1.00
24.71
O

ATOM
2508
N
ALA
C3093
29.205
−16.310
5.343
1.00
23.94
N

ATOM
2509
CA
ALA
C3093
29.160
−14.994
4.685
1.00
23.97
C

ATOM
2510
CB
ALA
C3093
28.779
−13.909
5.706
1.00
23.95
C

ATOM
2511
C
ALA
C3093
30.493
−14.618
4.009
1.00
23.83
C

ATOM
2512
O
ALA
C3093
31.556
−15.008
4.472
1.00
23.82
O

ATOM
2513
N
PRO
C3094
30.443
−13.841
2.910
1.00
24.15
N

ATOM
2514
CD
PRO
C3094
29.221
−13.410
2.203
1.00
24.15
C

ATOM
2515
CA
PRO
C3094
31.649
−13.414
2.177
1.00
24.68
C

ATOM
2516
CB
PRO
C3094
31.098
−13.058
0.801
1.00
24.26
C

ATOM
2517
CG
PRO
C3094
29.762
−12.461
1.144
1.00
24.90
C

ATOM
2518
C
PRO
C3094
32.369
−12.231
2.840
1.00
24.92
C

ATOM
2519
O
PRO
C3094
32.529
−11.165
2.239
1.00
25.65
O

ATOM
2520
N
PHE
C3095
32.810
−12.437
4.076
1.00
25.08
N

ATOM
2521
CA
PHE
C3095
33.495
−11.410
4.864
1.00
25.37
C

ATOM
2522
CB
PHE
C3095
32.444
−10.502
5.521
1.00
24.79
C

ATOM
2523
CG
PHE
C3095
33.015
−9.384
6.356
1.00
24.93
C

ATOM
2524
CD1
PHE
C3095
33.652
−8.299
5.760
1.00
24.60
C

ATOM
2525
CD2
PHE
C3095
32.883
−9.403
7.741
1.00
24.43
C

ATOM
2526
CE1
PHE
C3095
34.148
−7.247
6.536
1.00
24.72
C

ATOM
2527
CE2
PHE
C3095
33.374
−8.358
8.527
1.00
24.22
C

ATOM
2528
CZ
PHE
C3095
34.008
−7.278
7.921
1.00
24.70
C

ATOM
2529
C
PHE
C3095
34.288
−12.163
5.928
1.00
25.61
C

ATOM
2530
O
PHE
C3095
33.766
−13.101
6.537
1.00
26.06
O

ATOM
2531
N
SER
C3096
35.538
−11.773
6.164
1.00
26.42
N

ATOM
2532
CA
SER
C3096
36.343
−12.485
7.158
1.00
27.23
C

ATOM
2533
CB
SER
C3096
37.709
−12.857
6.558
1.00
27.32
C

ATOM
2534
OG
SER
C3096
38.389
−11.725
6.054
1.00
28.68
O

ATOM
2535
C
SER
C3096
36.529
−11.795
8.515
1.00
27.58
C

ATOM
2536
O
SER
C3096
37.311
−12.259
9.349
1.00
28.21
O

ATOM
2537
N
GLY
C3097
35.807
−10.700
8.745
1.00
27.18
N

ATOM
2538
CA
GLY
C3097
35.908
−10.003
10.021
1.00
26.33
C

ATOM
2539
C
GLY
C3097
34.808
−10.462
10.971
1.00
26.17
C

ATOM
2540
O
GLY
C3097
34.322
−11.584
10.845
1.00
25.72
O

ATOM
2541
N
LYS
C3098
34.408
−9.610
11.916
1.00
25.25
N

ATOM
2542
CA
LYS
C3098
33.347
−9.971
12.864
1.00
24.54
C

ATOM
2543
CB
LYS
C3098
33.759
−9.591
14.289
1.00
25.96
C

ATOM
2544
CG
LYS
C3098
35.059
−10.259
14.723
1.00
28.19
C

ATOM
2545
CD
LYS
C3098
35.079
−10.576
16.208
1.00
29.56
C

ATOM
2546
CE
LYS
C3098
35.022
−9.324
17.053
1.00
30.68
C

ATOM
2547
NZ
LYS
C3098
35.150
−9.647
18.505
1.00
32.82
N

ATOM
2548
C
LYS
C3098
32.013
−9.313
12.498
1.00
22.87
C

ATOM
2549
O
LYS
C3098
31.984
−8.155
12.082
1.00
22.97
O

ATOM
2550
N
ILE
C3099
30.919
−10.060
12.659
1.00
21.29
N

ATOM
2551
CA
ILE
C3099
29.567
−9.589
12.316
1.00
19.46
C

ATOM
2552
CB
ILE
C3099
28.918
−10.546
11.251
1.00
19.44
C

ATOM
2553
CG2
ILE
C3099
27.577
−9.987
10.769
1.00
18.38
C

ATOM
2554
CG1
ILE
C3099
29.869
−10.742
10.062
1.00
19.30
C

ATOM
2555
CD1
ILE
C3099
29.447
−11.853
9.103
1.00
19.40
C

ATOM
2556
C
ILE
C3099
28.632
−9.537
13.544
1.00
18.29
C

ATOM
2557
O
ILE
C3099
28.381
−10.568
14.165
1.00
18.68
O

ATOM
2558
N
TRP
C3100
28.109
−8.357
13.888
1.00
16.88
N

ATOM
2559
CA
TRP
C3100
27.195
−8.233
15.036
1.00
15.59
C

ATOM
2560
CB
TRP
C3100
27.643
−7.078
15.956
1.00
15.65
C

ATOM
2561
CG
TRP
C3100
29.076
−7.231
16.505
1.00
15.70
C

ATOM
2562
CD2
TRP
C3100
29.492
−8.034
17.626
1.00
15.13
C

ATOM
2563
CE2
TRP
C3100
30.901
−7.910
17.735
1.00
15.28
C

ATOM
2564
CE3
TRP
C3100
28.813
−8.846
18.547
1.00
16.40
C

ATOM
2565
CD1
TRP
C3100
30.220
−6.668
15.997
1.00
15.61
C

ATOM
2566
NE1
TRP
C3100
31.321
−7.074
16.734
1.00
15.83
N

ATOM
2567
CZ2
TRP
C3100
31.639
−8.570
18.730
1.00
15.21
C

ATOM
2568
CZ3
TRP
C3100
29.549
−9.504
19.538
1.00
15.48
C

ATOM
2569
CH2
TRP
C3100
30.950
−9.358
19.618
1.00
15.73
C

ATOM
2570
C
TRP
C3100
25.746
−8.022
14.533
1.00
15.44
C

ATOM
2571
O
TRP
C3100
25.438
−6.991
13.924
1.00
14.84
O

ATOM
2572
N
LEU
C3101
24.875
−9.003
14.800
1.00
14.06
N

ATOM
2573
CA
LEU
C3101
23.469
−9.004
14.348
1.00
13.05
C

ATOM
2574
CB
LEU
C3101
23.268
−10.161
13.357
1.00
13.07
C

ATOM
2575
CG
LEU
C3101
21.828
−10.623
13.084
1.00
12.96
C

ATOM
2576
CD1
LEU
C3101
21.208
−9.737
12.015
1.00
13.42
C

ATOM
2577
CD2
LEU
C3101
21.821
−12.083
12.624
1.00
14.82
C

ATOM
2578
C
LEU
C3101
22.382
−9.133
15.430
1.00
12.57
C

ATOM
2579
O
LEU
C3101
22.597
−9.789
16.450
1.00
11.63
O

ATOM
2580
N
SER
C3102
21.215
−8.525
15.181
1.00
12.95
N

ATOM
2581
CA
SER
C3102
20.054
−8.615
16.092
1.00
13.03
C

ATOM
2582
CB
SER
C3102
20.128
−7.536
17.187
1.00
13.35
C

ATOM
2583
OG
SER
C3102
19.148
−7.749
18.205
1.00
12.78
O

ATOM
2584
C
SER
C3102
18.736
−8.484
15.297
1.00
13.43
C

ATOM
2585
O
SER
C3102
18.687
−7.747
14.298
1.00
13.38
O

ATOM
2586
N
ILE
C3103
17.687
−9.197
15.741
1.00
13.23
N

ATOM
2587
CA
ILE
C3103
16.355
−9.215
15.082
1.00
14.65
C

ATOM
2588
CB
ILE
C3103
16.135
−10.552
14.290
1.00
15.02
C

ATOM
2589
CG2
ILE
C3103
14.776
−10.534
13.581
1.00
14.81
C

ATOM
2590
CG1
ILE
C3103
17.254
−10.764
13.267
1.00
15.40
C

ATOM
2591
CD1
ILE
C3103
17.113
−12.053
12.443
1.00
16.79
C

ATOM
2592
C
ILE
C3103
15.180
−9.123
16.087
1.00
15.28
C

ATOM
2593
O
ILE
C3103
15.239
−9.717
17.166
1.00
15.06
O

ATOM
2594
N
SER
C3104
14.109
−8.414
15.726
1.00
16.55
N

ATOM
2595
CA
SER
C3104
12.930
−8.295
16.614
1.00
17.82
C

ATOM
2596
CB
SER
C3104
13.077
−7.067
17.527
1.00
18.38
C

ATOM
2597
OG
SER
C3104
12.058
−7.028
18.524
1.00
18.13
O

ATOM
2598
C
SER
C3104
11.629
−8.186
15.793
1.00
19.18
C

ATOM
2599
O
SER
C3104
11.672
−7.850
14.608
1.00
18.60
O

ATOM
2600
N
HIS
C3105
10.475
−8.466
16.405
1.00
21.28
N

ATOM
2601
CA
HIS
C3105
9.209
−8.376
15.660
1.00
23.07
C

ATOM
2602
CB
HIS
C3105
8.964
−9.664
14.877
1.00
24.36
C

ATOM
2603
CG
HIS
C3105
8.715
−10.856
15.749
1.00
25.51
C

ATOM
2604
CD2
HIS
C3105
7.631
−11.219
16.474
1.00
26.93
C

ATOM
2605
ND1
HIS
C3105
9.673
−11.815
15.986
1.00
26.74
N

ATOM
2606
CE1
HIS
C3105
9.192
−12.721
16.820
1.00
27.20
C

ATOM
2607
NE2
HIS
C3105
7.955
−12.383
17.132
1.00
28.00
N

ATOM
2608
C
HIS
C3105
7.927
−8.081
16.452
1.00
24.09
C

ATOM
2609
O
HIS
C3105
7.913
−8.058
17.686
1.00
23.14
O

ATOM
2610
N
THR
C3106
6.851
−7.870
15.692
1.00
25.15
N

ATOM
2611
CA
THR
C3106
5.506
−7.616
16.212
1.00
26.55
C

ATOM
2612
CB
THR
C3106
5.100
−6.137
16.097
1.00
26.80
C

ATOM
2613
OG1
THR
C3106
5.097
−5.748
14.717
1.00
27.05
O

ATOM
2614
CG2
THR
C3106
6.052
−5.258
16.880
1.00
27.26
C

ATOM
2615
C
THR
C3106
4.549
−8.437
15.339
1.00
27.26
C

ATOM
2616
O
THR
C3106
4.987
−9.196
14.477
1.00
26.93
O

ATOM
2617
N
ASP
C3107
3.245
−8.287
15.539
1.00
28.56
N

ATOM
2618
CA
ASP
C3107
2.310
−9.067
14.732
1.00
30.14
C

ATOM
2619
CB
ASP
C3107
0.977
−9.243
15.474
1.00
32.49
C

ATOM
2620
CG
ASP
C3107
0.498
−7.968
16.133
1.00
34.70
C

ATOM
2621
OD1
ASP
C3107
0.406
−6.930
15.440
1.00
37.09
O

ATOM
2622
OD2
ASP
C3107
0.209
−8.003
17.348
1.00
36.52
O

ATOM
2623
C
ASP
C3107
2.065
−8.499
13.334
1.00
29.74
C

ATOM
2624
O
ASP
C3107
1.264
−9.043
12.575
1.00
30.83
O

ATOM
2625
N
GLN
C3108
2.762
−7.425
12.979
1.00
28.55
N

ATOM
2626
CA
GLN
C3108
2.578
−6.815
11.665
1.00
27.66
C

ATOM
2627
CB
GLN
C3108
1.942
−5.432
11.822
1.00
27.82
C

ATOM
2628
CG
GLN
C3108
0.557
−5.445
12.466
1.00
28.58
C

ATOM
2629
CD
GLN
C3108
0.012
−4.045
12.681
0.05
28.18
C

ATOM
2630
OE1
GLN
C3108
−1.083
−3.866
13.214
0.05
28.21
O

ATOM
2631
NE2
GLN
C3108
0.779
−3.043
12.266
0.05
28.20
N

ATOM
2632
C
GLN
C3108
3.845
−6.693
10.812
1.00
26.77
C

ATOM
2633
O
GLN
C3108
3.760
−6.652
9.582
1.00
25.82
O

ATOM
2634
N
PHE
C3109
5.015
−6.625
11.449
1.00
25.68
N

ATOM
2635
CA
PHE
C3109
6.268
−6.496
10.697
1.00
24.08
C

ATOM
2636
CB
PHE
C3109
6.441
−5.039
10.221
1.00
25.01
C

ATOM
2637
CG
PHE
C3109
6.572
−4.029
11.343
1.00
26.02
C

ATOM
2638
CD1
PHE
C3109
7.763
−3.908
12.062
1.00
26.89
C

ATOM
2639
CD2
PHE
C3109
5.505
−3.205
11.682
1.00
26.71
C

ATOM
2640
CE1
PHE
C3109
7.889
−2.977
13.105
1.00
27.26
C

ATOM
2641
CE2
PHE
C3109
5.616
−2.268
12.725
1.00
27.81
C

ATOM
2642
CZ
PHE
C3109
6.811
−2.156
13.437
1.00
27.24
C

ATOM
2643
C
PHE
C3109
7.497
−6.950
11.497
1.00
22.66
C

ATOM
2644
O
PHE
C3109
7.382
−7.267
12.681
1.00
21.87
O

ATOM
2645
N
VAL
C3110
8.658
−6.992
10.833
1.00
20.94
N

ATOM
2646
CA
VAL
C3110
9.932
−7.396
11.460
1.00
19.58
C

ATOM
2647
CB
VAL
C3110
10.402
−8.790
10.931
1.00
20.14
C

ATOM
2648
CG1
VAL
C3110
10.731
−8.705
9.443
1.00
20.40
C

ATOM
2649
CG2
VAL
C3110
11.639
−9.268
11.707
1.00
21.57
C

ATOM
2650
C
VAL
C3110
11.049
−6.374
11.162
1.00
18.29
C

ATOM
2651
O
VAL
C3110
10.982
−5.675
10.154
1.00
16.70
O

ATOM
2652
N
THR
C3111
12.065
−6.298
12.035
1.00
17.21
N

ATOM
2653
CA
THR
C3111
13.210
−5.383
11.852
1.00
16.21
C

ATOM
2654
CB
THR
C3111
13.109
−4.122
12.781
1.00
16.74
C

ATOM
2655
OG1
THR
C3111
13.100
−4.528
14.159
1.00
19.56
O

ATOM
2656
CG2
THR
C3111
11.851
−3.321
12.485
1.00
18.23
C

ATOM
2657
C
THR
C3111
14.551
−6.096
12.159
1.00
15.10
C

ATOM
2658
O
THR
C3111
14.575
−7.053
12.945
1.00
13.98
O

ATOM
2659
N
ALA
C3112
15.643
−5.638
11.532
1.00
13.72
N

ATOM
2660
CA
ALA
C3112
16.996
−6.210
11.737
1.00
14.06
C

ATOM
2661
CB
ALA
C3112
17.266
−7.324
10.712
1.00
13.98
C

ATOM
2662
C
ALA
C3112
18.092
−5.135
11.630
1.00
13.79
C

ATOM
2663
O
ALA
C3112
17.936
−4.164
10.884
1.00
14.41
O

ATOM
2664
N
SER
C3113
19.194
−5.320
12.364
1.00
13.18
N

ATOM
2665
CA
SER
C3113
20.321
−4.369
12.395
1.00
12.99
C

ATOM
2666
CB
SER
C3113
20.210
−3.510
13.665
1.00
12.64
C

ATOM
2667
OG
SER
C3113
21.209
−2.499
13.724
1.00
12.28
O

ATOM
2668
C
SER
C3113
21.690
−5.103
12.369
1.00
13.25
C

ATOM
2669
O
SER
C3113
21.875
−6.075
13.097
1.00
12.44
O

ATOM
2670
N
VAL
C3114
22.636
−4.611
11.555
1.00
13.63
N

ATOM
2671
CA
VAL
C3114
23.972
−5.230
11.374
1.00
13.14
C

ATOM
2672
CB
VAL
C3114
24.030
−5.984
9.989
1.00
12.86
C

ATOM
2673
CG1
VAL
C3114
25.467
−6.425
9.641
1.00
13.59
C

ATOM
2674
CG2
VAL
C3114
23.117
−7.194
10.016
1.00
13.11
C

ATOM
2675
C
VAL
C3114
25.161
−4.248
11.419
1.00
13.18
C

ATOM
2676
O
VAL
C3114
25.094
−3.171
10.834
1.00
11.64
O

ATOM
2677
N
ILE
C3115
26.245
−4.631
12.101
1.00
14.05
N

ATOM
2678
CA
ILE
C3115
27.463
−3.797
12.176
1.00
15.16
C

ATOM
2679
CB
ILE
C3115
27.717
−3.208
13.593
1.00
15.92
C

ATOM
2680
CG2
ILE
C3115
28.902
−2.217
13.532
1.00
16.68
C

ATOM
2681
CG1
ILE
C3115
26.482
−2.477
14.122
1.00
15.85
C

ATOM
2682
CD1
ILE
C3115
26.657
−1.949
15.549
1.00
15.56
C

ATOM
2683
C
ILE
C3115
28.699
−4.655
11.836
1.00
16.02
C

ATOM
2684
O
ILE
C3115
28.900
−5.714
12.444
1.00
14.67
O

ATOM
2685
N
LEU
C3116
29.519
−4.195
10.883
1.00
16.42
N

ATOM
2686
CA
LEU
C3116
30.741
−4.920
10.469
1.00
17.73
C

ATOM
2687
CB
LEU
C3116
30.864
−4.910
8.939
1.00
17.22
C

ATOM
2688
CG
LEU
C3116
29.646
−5.423
8.157
1.00
17.27
C

ATOM
2689
CD1
LEU
C3116
29.914
−5.349
6.660
1.00
17.70
C

ATOM
2690
CD2
LEU
C3116
29.339
−6.855
8.570
1.00
18.07
C

ATOM
2691
C
LEU
C3116
32.016
−4.322
11.099
1.00
18.48
C

ATOM
2692
O
LEU
C3116
32.185
−3.101
11.134
1.00
16.07
O

ATOM
2693
N
GLU
C3117
32.926
−5.184
11.562
1.00
20.56
N

ATOM
2694
CA
GLU
C3117
34.150
−4.718
12.227
1.00
23.53
C

ATOM
2695
CB
GLU
C3117
33.939
−4.757
13.754
1.00
24.06
C

ATOM
2696
CG
GLU
C3117
35.200
−4.587
14.608
1.00
24.76
C

ATOM
2697
CD
GLU
C3117
34.952
−4.835
16.103
1.00
25.52
C

ATOM
2698
OE1
GLU
C3117
34.507
−5.946
16.473
1.00
25.65
O

ATOM
2699
OE2
GLU
C3117
35.203
−3.917
16.913
1.00
25.88
O

ATOM
2700
C
GLU
C3117
35.429
−5.488
11.878
1.00
25.38
C

ATOM
2701
O
GLU
C3117
35.403
−6.695
11.654
1.00
25.28
O

ATOM
2702
N
GLU
C3118
36.545
−4.766
11.840
1.00
28.60
N

ATOM
2703
CA
GLU
C3118
37.857
−5.346
11.559
1.00
32.23
C

ATOM
2704
CB
GLU
C3118
38.321
−4.996
10.139
1.00
33.43
C

ATOM
2705
CG
GLU
C3118
37.520
−5.678
9.038
1.00
35.47
C

ATOM
2706
CD
GLU
C3118
38.123
−5.482
7.657
1.00
36.73
C

ATOM
2707
OE1
GLU
C3118
37.561
−6.029
6.683
1.00
37.62
O

ATOM
2708
OE2
GLU
C3118
39.156
−4.786
7.540
1.00
37.51
O

ATOM
2709
C
GLU
C3118
38.857
−4.800
12.576
1.00
33.91
C

ATOM
2710
O
GLU
C3118
39.168
−3.608
12.576
1.00
34.12
O

ATOM
2711
N
ASN
C3119
39.348
−5.678
13.444
1.00
36.07
N

ATOM
2712
CA
ASN
C3119
40.308
−5.298
14.477
1.00
37.92
C

ATOM
2713
CB
ASN
C3119
40.307
−6.343
15.597
1.00
38.97
C

ATOM
2714
CG
ASN
C3119
38.908
−6.622
16.137
1.00
39.98
C

ATOM
2715
OD1
ASN
C3119
38.271
−5.753
16.737
1.00
40.51
O

ATOM
2716
ND2
ASN
C3119
38.424
−7.841
15.919
1.00
40.65
N

ATOM
2717
C
ASN
C3119
41.713
−5.169
13.889
1.00
38.71
C

ATOM
2718
O
ASN
C3119
41.850
−5.354
12.662
1.00
39.38
O

ATOM
2719
OXT
ASN
C3119
42.661
−4.885
14.657
1.00
39.94
O

TER
2720

ASN
C3119

ATOM
2721
O
HOH
W5001
1.203
5.537
8.026
1.00
17.73
O

ATOM
2722
O
HOH
W5002
14.815
9.909
2.322
1.00
14.32
O

ATOM
2723
O
HOH
W5003
23.904
8.622
37.957
1.00
27.02
O

ATOM
2724
O
HOH
W5004
20.469
3.444
3.735
1.00
17.55
O

ATOM
2725
O
HOH
W5005
24.018
4.203
28.855
1.00
20.10
O

ATOM
2726
O
HOH
W5006
10.973
5.376
28.684
1.00
19.79
O

ATOM
2727
O
HOH
W5007
22.784
15.314
34.546
1.00
22.90
O

ATOM
2728
O
HOH
W5008
23.453
4.929
3.777
1.00
19.63
O

ATOM
2729
O
HOH
W5009
23.062
1.129
4.843
1.00
21.68
O

ATOM
2730
O
HOH
W5010
25.642
18.163
37.608
1.00
19.94
O

ATOM
2731
O
HOH
W5011
23.184
2.653
2.606
1.00
26.65
O

ATOM
2732
O
HOH
W5012
28.019
0.947
5.252
1.00
22.66
O

ATOM
2733
O
HOH
W5013
4.711
21.958
2.912
1.00
24.85
O

ATOM
2734
O
HOH
W5014
36.483
3.458
10.706
1.00
31.97
O

ATOM
2735
O
HOH
W5015
17.241
0.177
14.610
1.00
23.93
O

ATOM
2736
O
HOH
W5016
13.566
−15.296
11.672
1.00
22.95
O

ATOM
2737
O
HOH
W5017
19.479
14.186
−2.520
1.00
25.49
O

ATOM
2738
O
HOH
W5018
27.283
10.084
6.422
1.00
24.49
O

ATOM
2739
O
HOH
W5019
14.135
8.932
34.920
1.00
26.53
O

ATOM
2740
O
HOH
W5020
36.044
2.408
16.583
1.00
32.56
O

ATOM
2741
O
HOH
W5021
33.258
−17.363
3.678
1.00
19.73
O

ATOM
2742
O
HOH
W5022
15.667
−0.884
2.725
1.00
31.95
O

ATOM
2743
O
HOH
W5023
9.740
−0.876
42.696
1.00
26.45
O

ATOM
2744
O
HOH
W5024
28.298
−24.311
26.736
1.00
36.28
O

ATOM
2745
O
HOH
W5025
16.170
2.461
13.853
1.00
22.79
O

ATOM
2746
O
HOH
W5026
13.623
−1.972
15.922
1.00
33.10
O

ATOM
2747
O
HOH
W5027
35.568
−7.137
18.918
1.00
28.33
O

ATOM
2748
O
HOH
W5028
21.193
8.337
22.471
1.00
24.39
O

ATOM
2749
O
HOH
W5029
0.905
8.530
3.669
1.00
29.99
O

ATOM
2750
O
HOH
W5030
26.791
21.664
30.504
1.00
26.91
O

ATOM
2751
O
HOH
W5031
12.687
−4.279
3.191
1.00
33.49
O

ATOM
2752
O
HOH
W5032
25.981
5.485
38.408
1.00
30.01
O

ATOM
2753
O
HOH
W5033
18.351
−22.326
27.170
1.00
39.62
O

ATOM
2754
O
HOH
W5034
27.692
−22.175
28.942
1.00
33.59
O

ATOM
2755
O
HOH
W5035
7.766
9.184
29.149
1.00
37.38
O

ATOM
2756
O
HOH
W5036
27.081
7.365
5.947
1.00
37.77
O

ATOM
2757
O
HOH
W5037
26.538
19.381
35.080
1.00
37.77
O

ATOM
2758
O
HOH
W5038
−4.201
17.799
6.607
1.00
32.96
O

ATOM
2759
O
HOH
W5039
5.036
8.700
14.260
1.00
30.11
O

ATOM
2760
O
HOH
W5040
0.851
9.642
42.538
1.00
22.98
O

ATOM
2761
O
HOH
W5041
19.927
0.231
15.198
1.00
20.70
O

ATOM
2762
O
HOH
W5042
38.613
−9.206
13.685
1.00
46.18
O

ATOM
2763
O
HOH
W5043
35.672
−15.638
5.122
1.00
43.16
O

ATOM
2764
O
HOH
W5044
14.774
−8.966
39.562
1.00
27.43
O

ATOM
2765
O
HOH
W5045
−0.343
−11.294
8.886
1.00
35.83
O

ATOM
2766
O
HOH
W5046
0.384
7.133
40.132
1.00
36.11
O

ATOM
2767
O
HOH
W5047
−1.790
−16.597
10.364
1.00
51.74
O

ATOM
2768
O
HOH
W5048
17.913
8.434
22.684
1.00
19.14
O

ATOM
2769
O
HOH
W5049
26.849
7.812
30.849
1.00
32.50
O

ATOM
2770
O
HOH
W5050
31.682
10.495
7.280
1.00
43.96
O

ATOM
2771
O
HOH
W5051
33.295
7.550
31.842
1.00
42.65
O

ATOM
2772
O
HOH
W5052
26.726
22.667
9.308
1.00
42.17
O

ATOM
2773
O
HOH
W5053
16.839
2.653
43.220
1.00
32.73
O

ATOM
2774
O
HOH
W5054
28.300
3.705
0.074
1.00
31.84
O

ATOM
2775
O
HOH
W5055
21.249
10.241
40.281
1.00
40.01
O

ATOM
2776
O
HOH
W5056
18.910
0.164
43.189
1.00
35.91
O

ATOM
2777
O
HOH
W5057
14.293
25.027
1.495
1.00
30.20
O

ATOM
2778
O
HOH
W5058
15.432
−0.416
17.518
1.00
26.65
O

ATOM
2779
O
HOH
W5059
21.028
5.383
41.219
1.00
31.60
O

ATOM
2780
O
HOH
W5060
27.025
7.703
33.714
1.00
38.38
O

ATOM
2781
O
HOH
W5061
1.162
−2.470
38.136
1.00
32.76
O

ATOM
2782
O
HOH
W5062
7.118
−4.468
3.111
1.00
25.42
O

ATOM
2783
O
HOH
W5063
10.345
8.046
50.558
1.00
21.47
O

ATOM
2784
O
HOH
W5064
1.601
−6.957
7.392
1.00
19.01
O

ATOM
2785
O
HOH
W5065
8.301
8.667
48.256
1.00
31.31
O

ATOM
2786
O
HOH
W5066
13.857
7.152
1.988
1.00
29.65
O

ATOM
2787
O
HOH
W5067
−8.101
−4.494
44.898
1.00
34.47
O

ATOM
2788
O
HOH
W5068
31.896
−17.405
6.589
1.00
41.64
O

ATOM
2789
O
HOH
W5069
17.654
−25.606
27.581
1.00
27.36
O

ATOM
2790
O
HOH
W5070
23.222
14.650
26.416
1.00
26.05
O

ATOM
2791
O
HOH
W5071
7.588
−0.528
0.314
1.00
32.42
O

ATOM
2792
O
HOH
W5072
37.956
−17.275
4.444
1.00
27.98
O

ATOM
2793
O
HOH
W5073
13.506
−13.814
28.837
1.00
53.93
O

ATOM
2794
O
HOH
W5074
32.339
6.763
6.234
1.00
44.01
O

ATOM
2795
O
HOH
W5075
17.732
−21.822
12.391
1.00
27.13
O

ATOM
2796
O
HOH
W5076
2.962
14.623
32.943
1.00
35.34
O

ATOM
2797
O
HOH
W5077
18.219
−11.144
17.921
1.00
32.13
O

ATOM
2798
O
HOH
W5078
21.073
24.057
−0.096
1.00
34.29
O

ATOM
2799
O
HOH
W5079
15.379
−12.595
24.369
1.00
37.81
O

ATOM
2800
O
HOH
W5080
26.131
21.190
0.182
1.00
31.04
O

ATOM
2801
O
HOH
W5081
−7.427
−1.162
30.153
1.00
37.22
O

ATOM
2802
O
HOH
W5082
9.376
19.648
13.353
1.00
46.89
O

ATOM
2803
O
HOH
W5083
26.771
−14.783
26.158
1.00
30.66
O

ATOM
2804
O
HOH
W5085
24.158
−4.023
38.598
1.00
29.95
O

ATOM
2805
O
HOH
W5086
2.673
−2.236
40.838
1.00
36.71
O

ATOM
2806
O
HOH
W5087
14.901
15.719
31.793
1.00
66.05
O

ATOM
2807
O
HOH
W5089
0.185
6.149
5.302
1.00
45.92
O

ATOM
2808
O
HOH
W5090
−3.050
13.963
3.439
1.00
31.57
O

ATOM
2809
O
HOH
W5091
20.002
26.238
4.307
1.00
38.95
O

ATOM
2810
O
HOH
W5092
9.528
7.010
25.049
1.00
40.00
O

ATOM
2811
O
HOH
W5093
22.998
9.245
25.495
1.00
45.96
O

ATOM
2812
O
HOH
W5094
25.633
5.504
41.203
1.00
33.74
O

ATOM
2813
O
HOH
W5095
22.525
7.413
40.125
1.00
27.93
O

ATOM
2814
O
HOH
W5096
25.772
−0.812
38.637
1.00
43.16
O

ATOM
2815
O
HOH
W5097
1.675
3.923
15.398
1.00
24.93
O

ATOM
2816
O
HOH
W5098
3.426
25.166
2.688
1.00
33.60
O

ATOM
2817
O
HOH
W5099
6.716
24.079
2.431
1.00
30.61
O

ATOM
2818
O
HOH
W5100
13.776
2.826
15.316
1.00
35.09
O

ATOM
2819
O
HOH
W5101
2.840
22.627
5.321
1.00
28.88
O

ATOM
2820
O
HOH
W5102
4.306
26.695
0.803
1.00
45.75
O

ATOM
2821
O
HOH
W5103
28.312
3.533
30.225
1.00
30.56
O

ATOM
2822
O
HOH
W5104
7.296
5.105
45.493
1.00
44.55
O

ATOM
2823
O
HOH
W5105
8.727
−7.822
20.152
1.00
30.96
O

ATOM
2824
O
HOH
W5106
15.910
2.991
1.288
1.00
26.19
O

ATOM
2825
O
HOH
W5107
24.692
15.648
32.485
1.00
45.46
O

ATOM
2826
O
HOH
W5108
10.229
10.752
16.032
1.00
39.52
O

ATOM
2827
O
HOH
W5109
30.124
8.492
1.194
1.00
42.53
O

ATOM
2828
O
HOH
W5110
38.431
9.460
12.406
1.00
34.79
O

ATOM
2829
O
HOH
W5111
15.296
−0.704
44.230
1.00
30.31
O

ATOM
2830
O
HOH
W5112
22.219
−25.058
0.518
1.00
40.16
O

ATOM
2831
O
HOH
W5113
16.280
−1.757
13.031
1.00
32.98
O

ATOM
2832
O
HOH
W5114
7.672
5.118
50.500
1.00
42.44
O

ATOM
2833
O
HOH
W5116
19.588
26.165
1.692
1.00
35.11
O

ATOM
2834
O
HOH
W5117
29.689
0.468
33.170
1.00
50.63
O

ATOM
2835
O
HOH
W5118
27.638
14.621
27.167
1.00
37.33
O

ATOM
2836
O
HOH
W5119
25.674
24.122
6.832
1.00
44.26
O

ATOM
2837
O
HOH
W5120
40.801
−13.288
5.322
1.00
31.98
O

ATOM
2838
O
HOH
W5121
36.143
−1.829
16.148
1.00
41.24
O

ATOM
2839
O
HOH
W5122
3.151
5.682
48.883
1.00
34.36
O

ATOM
2840
O
HOH
W5123
32.693
14.445
9.290
1.00
34.74
O

ATOM
2841
O
HOH
W5124
28.701
6.185
34.708
1.00
49.77
O

ATOM
2842
O
HOH
W5125
26.196
1.517
−1.280
1.00
39.43
O

ATOM
2843
O
HOH
W5126
−0.033
0.726
10.398
1.00
47.62
O

ATOM
2844
O
HOH
W5127
21.383
−3.597
−1.922
1.00
51.56
O

ATOM
2845
O
HOH
W5128
13.364
12.833
27.633
1.00
52.29
O

ATOM
2846
O
HOH
W5129
21.714
12.615
35.721
1.00
33.09
O

ATOM
2847
O
HOH
W5130
8.469
6.895
52.440
1.00
45.76
O

ATOM
2848
O
HOH
W5131
26.110
4.660
30.832
1.00
35.30
O

ATOM
2849
O
HOH
W5132
19.463
−23.363
14.165
1.00
35.76
O

ATOM
2850
O
HOH
W5133
13.443
20.073
−9.252
1.00
40.04
O

ATOM
2851
O
HOH
W5134
9.131
8.743
16.901
1.00
44.35
O

ATOM
2852
O
HOH
W5135
2.141
8.144
15.984
1.00
43.82
O

ATOM
2853
O
HOH
W5136
8.533
27.824
6.026
1.00
33.71
O

ATOM
2854
O
HOH
W5137
23.489
23.402
0.284
1.00
47.94
O

ATOM
2855
O
HOH
W5138
19.996
15.564
−7.451
1.00
42.23
O

ATOM
2856
O
HOH
W5139
3.830
6.820
−6.454
1.00
43.70
O

ATOM
2857
O
HOH
W5140
15.282
15.611
18.402
1.00
41.11
O

ATOM
2858
O
HOH
W5141
17.265
26.061
11.713
1.00
39.14
O

ATOM
2859
O
HOH
W5142
23.754
1.893
−2.493
1.00
45.81
O

ATOM
2860
O
HOH
W5143
26.488
3.338
6.608
1.00
42.72
O

ATOM
2861
O
HOH
W5144
6.963
4.729
1.634
1.00
33.11
O

ATOM
2862
O
HOH
W5145
−0.293
3.358
3.517
1.00
47.82
O

ATOM
2863
O
HOH
W5146
13.304
0.010
14.071
1.00
44.49
O

ATOM
2864
O
HOH
W5147
14.485
−0.911
11.196
1.00
34.10
O

ATOM
2865
O
HOH
W5148
38.684
−3.391
16.424
1.00
42.58
O

ATOM
2866
O
HOH
W5149
−0.378
−3.887
41.179
1.00
39.92
O

ATOM
2867
O
HOH
W5150
14.999
10.060
38.087
1.00
56.40
O

ATOM
2868
O
HOH
W5151
27.440
−10.394
33.773
1.00
51.57
O

ATOM
2869
O
HOH
W5152
9.035
−7.425
0.106
1.00
46.37
O

ATOM
2870
O
HOH
W5153
5.110
−2.372
2.316
1.00
33.68
O

ATOM
2871
O
HOH
W5154
29.018
−14.387
13.400
1.00
40.14
O

ATOM
2872
O
HOH
W5155
1.676
−2.447
9.577
1.00
41.85
O

ATOM
2873
O
HOH
W5156
20.185
11.538
−6.635
1.00
37.49
O

ATOM
2874
O
HOH
W5157
15.389
−28.857
26.962
1.00
41.90
O

ATOM
2875
O
HOH
W5158
−6.106
19.784
6.635
1.00
36.72
O

ATOM
2876
O
HOH
W5159
5.517
17.184
13.233
1.00
48.23
O

ATOM
2877
O
HOH
W5160
5.076
15.020
11.985
1.00
45.45
O

ATOM
2878
O
HOH
W5161
5.445
−7.849
27.659
1.00
39.11
O

ATOM
2879
O
HOH
W5162
20.980
18.101
37.922
1.00
29.42
O

ATOM
2880
O
HOH
W5163
16.748
−29.146
3.293
1.00
42.39
O

ATOM
2881
O
HOH
W5164
30.770
4.871
31.188
1.00
43.36
O

ATOM
2882
O
HOH
W5165
3.854
−8.929
29.337
1.00
54.81
O

ATOM
2883
O
HOH
W5166
10.593
19.605
16.042
1.00
47.04
O

ATOM
2884
O
HOH
W5167
42.095
8.840
19.150
1.00
49.61
O

ATOM
2885
O
HOH
W5168
9.957
11.390
13.550
1.00
42.37
O

ATOM
2886
O
HOH
W5169
−4.606
21.333
1.399
1.00
48.40
O

ATOM
2887
O
HOH
W5170
11.695
29.342
6.480
1.00
58.15
O

ATOM
2888
O
HOH
W5171
23.099
25.128
3.657
1.00
40.99
O

ATOM
2889
O
HOH
W5172
23.505
24.766
−3.702
1.00
44.31
O

ATOM
2890
O
HOH
W5173
14.447
17.461
20.573
1.00
40.93
O

ATOM
2891
O
HOH
W5174
11.974
23.606
15.698
1.00
50.59
O

ATOM
2892
O
HOH
W5175
33.868
19.345
11.374
1.00
39.71
O

ATOM
2893
O
HOH
W5176
8.306
−9.142
31.222
1.00
42.33
O

ATOM
2894
O
HOH
W5177
12.171
14.379
29.266
1.00
52.75
O

ATOM
2895
O
HOH
W5178
29.974
−2.958
37.157
1.00
38.64
O

ATOM
2896
O
HOH
W5179
30.177
1.102
3.621
1.00
43.39
O

ATOM
2897
O
HOH
W5180
13.634
0.062
1.980
1.00
43.54
O

ATOM
2898
O
HOH
W5181
9.893
10.792
25.719
1.00
35.63
O

ATOM
2899
O
HOH
W5182
15.133
16.851
24.775
1.00
34.15
O

TER
2900

HOH
W5182

ATOM
2901
N1A
COE
E4002
19.788
−13.382
22.863
1.00
37.66
N

ATOM
2902
C2A
COE
E4002
19.629
−12.509
21.832
1.00
37.59
C

ATOM
2903
N3A
COE
E4002
18.590
−12.603
20.980
1.00
37.39
N

ATOM
2904
C4A
COE
E4002
17.686
−13.627
21.196
1.00
37.85
C

ATOM
2905
C5A
COE
E4002
17.805
−14.571
22.262
1.00
38.04
C

ATOM
2906
C6A
COE
E4002
18.900
−14.393
23.079
1.00
38.11
C

ATOM
2907
N6A
COE
E4002
19.128
−15.221
24.120
1.00
38.32
N

ATOM
2908
N7A
COE
E4002
16.749
−15.454
22.198
1.00
38.10
N

ATOM
2909
C8A
COE
E4002
15.977
−15.090
21.125
1.00
38.02
C

ATOM
2910
N9A
COE
E4002
16.529
−13.990
20.508
1.00
38.30
N

ATOM
2911
C71
COE
E4002
15.927
−13.354
19.309
1.00
38.56
C

ATOM
2912
C72
COE
E4002
15.686
−14.244
18.059
1.00
38.64
C

ATOM
2913
O72
COE
E4002
16.358
−13.703
16.916
1.00
37.72
O

ATOM
2914
C73
COE
E4002
14.168
−14.225
17.883
1.00
39.06
C

ATOM
2915
O73
COE
E4002
13.797
−14.451
16.455
1.00
38.84
O

ATOM
2916
P73
COE
E4002
14.041
−15.822
15.721
1.00
39.24
P

ATOM
2917
O7A
COE
E4002
13.165
−15.826
14.433
1.00
39.04
O

ATOM
2918
O8A
COE
E4002
15.540
−15.939
15.325
1.00
39.12
O

ATOM
2919
O9A
COE
E4002
13.637
−17.009
16.646
1.00
39.35
O

ATOM
2920
C74
COE
E4002
13.826
−12.831
18.392
1.00
39.77
C

ATOM
2921
O74
COE
E4002
14.690
−12.631
19.516
1.00
39.23
O

ATOM
2922
C75
COE
E4002
12.345
−12.657
18.817
1.00
40.70
C

ATOM
2923
O75
COE
E4002
12.121
−11.261
19.226
1.00
42.75
O

ATOM
2924
P1A
COE
E4002
10.787
−10.752
19.901
1.00
43.64
P

ATOM
2925
O3A
COE
E4002
9.754
−11.915
20.051
1.00
43.83
O

ATOM
2926
O4A
COE
E4002
10.208
−9.595
19.036
1.00
44.05
O

ATOM
2927
O5A
COE
E4002
11.200
−10.230
21.306
1.00
43.87
O

TER
2928

COE
E4002

END

[0364]

Use of streptococcus pneumoniae acyl carrier protein synthase crystal structure in diagnostics, antimicrobial drug design, and biosensors

Information

Publication Number

Date Filed

Date Published

Inventors

CPC

US Classifications

International Classifications

Abstract

Description

Claims

Parent Case Info

Provisional Applications (1)