Peptide mutant of human ERAB or HADH2, its X-ray crystal structure, and materials and method for identification of inhibitors thereof

TECHNICAL FIELD OF THE INVENTION

[0002] The present invention relates to the three-dimensional crystal structure of human ERAB or HADH2 with NAD+ cofactor and its use in the design and development of inhibitors thereof.

BACKGROUND OF THE INVENTION

[0003] Endoplasmic reticulum-associated amyloid β-peptide-binding protein (ERAB), a member of the short-chain dehydrogenase/reductase (SDR) family of enzymes, has been implicated in the development of Alzheimer's disease (AD). As the name suggests, ERAB, also known as L-3-hydroxyacyl-CoA dehydrogenase Type II (HADH2), is a dehydrogenase enzyme capable of binding amyloid-β (Aβ) peptide. Inhibition of ERAB or HADH2 finds therapeutic utility in the treatment of AD and research and diagnostic utility in the delineation of the role of the enzyme in both normal cellular function and in AD pathogenesis.

[0004] AD is a progressive neurodegenerative disease of the brain resulting in diminished cognitive abilities, dementia, and ultimately death. A strong link has been established between the development of AD and the accumulation of Aβ in the brain [Storey et al., Neuropathology And Applied Neurobiology, Vol. 25, pp. 81-97 (1999); Selkoe, Annual Review of Neuroscience, Vol. 17, pp. 489-517 (1994); Small et al., J. Neurochemistry, Vol. 73, pp. 443-9 (1999)]. Aβ is a proteolytic fragment of the integral membrane glycoprotein, amyloid-β precursor protein (APP) [Kang et al., Nature, Vol. 325, pp. 733-736 (1987)]. Aβ is also the principal component of the extracellular plaques that are diagnostic of AD and species of the peptide have been shown to be engaged by intracellular targets [Yan et al., Nature, Vol. 389, pp. 689-95 (1997)]. Although aggregated Aβ appears to be toxic to neuronal cells in culture, the mechanisms of Aβ neurotoxicity in vivo are not completely understood.

[0005] Aβ accumulates both inside and outside nerve cells [Wilson et al., Journal of Neuropathology And Experimental Neurology, Vol. 58, pp. 787-94 (1999)]. There is evidence that the interaction of Aβ with intracellular proteins could lead to cytotoxic events prior to the formation of extracellular plaques. ERAB or HADH2, an intracellular protein, has been found to bind Aβ in the yeast two-hybrid system [Yan et al., Nature, Vol. 389, pp. 689-95 (1997)]. HADH2, a protein identical to ERAB, has been independently identified as an L-3-hydroxyacyl-CoA dehydrogenase with an apparent role in the mitochondrial fatty acid β-oxidation pathway [He et al., Journal of Biochemistry, Vol. 273. No. 17, pp. 10741-10746 (1998)].

[0006] ERAB or HADH2 is reported to be an NAD+ dependent dehydrogenase which catalyzes the reversible oxidation of L-3-hydroxyacyl-CoA. The human short chain L-3-hydroxyacyl-CoA dehydrogenase gene is organized into six exons and five introns and maps to chromosone Xp 11.2 [He et al. (1998), supra]. Sequence comparisons show that ERAB or HADH2 belongs to the SDR family of enzymes.

[0007] ERAB or HADH2 has been cloned, expressed, purified, and characterized from human brain [He et al. (1998), supra]. ERAB or HADH2 messenger RNA (mRNA) is expressed ubiquitously in normal human tissues. Its expression is highest in liver and heart but ERAB or HADH2 mRNA is also expressed in normal brain. In normal brain, ERAB or HADH2 antigen is present at low levels, being predominantly localized in neurons. However, in neurons affected in AD, ERAB or HADH2 is reported to be overexpressed relative to non-AD age-matched controls, especially near deposits of Aβ [Yan et al., Nature, Vol. 389, pp. 689-95 (1997); U.S. Pat. No. 6,268,479].

[0008] A variety of experimental evidence suggests that ERAB or HADH2 interacts with the Aβ peptide and can mediate its cytotoxic effects [Yan et al. (1997), supra]. For example, ERAB or HADH2, normally found in the endoplasmic reticulum and mitochondria, has been shown to become redistributed to the plasma membrane fraction of cells in the presence of Aβ peptide [Yan et al.(1997), supra]. Likewise, it has been shown that the cytotoxic effects of Aβ on neuroblastoma cells in cultures, can be blocked by anti-ERAB or HADH2 antibodies. Cells which overexpress ERAB or HADH2 and Aβ show elevated markers of cytotoxicity and cell stress compared to mock transfected controls; conversely, cells overexpressing catalytically inactive mutants of ERAB or HADH2 were no more sensitive than controls which overexpressed Aβ alone [Yan et al., Journal of Biochemistry, Vol. 274, pp. 2145-56 (1999)].

[0009] These observations support the theory that ERAB or HADH2 mediates the intraneuronal toxicity of Aβ by acting on inappropriate substrates, possibly generating toxic aldehydes [Yan et al., Journal of Biochemistry, Vol. 274, pp. 2145-56 (1999)]. It has also been suggested that ERAB or HADH2 could contribute to Aβ-associated pathogenesis of AD by reducing neuroprotective estrogen levels in the brain, based on the finding that the enzyme can also utilize estrogen as a substrate [Yan et al., Journal of Biochemistry, Vol. 274, pp. 2145-56 (1999); He et al., Journal of Biochemistry, Vol. 274, pp. 15014-9 (1999)]. Although the two proposed roles for ERAB or HADH2 in AD are quite distinct, enzymatic activity of the protein is a prerequisite in either case.

[0010] Several attempts have been made to elucidate the three-dimensional structure of proteins to design candidate drugs. For example, Davis et al., Prevention of Chemotherapy-Induced Alopecia in Rats by CDK Inhibitors (2001) Science 291:134-137; Zhu et al., Structural Analysis of the Lymphocyte-Specific Kinase Lck in Complex with Non-selective and Src Family selective Kinase Inhibitors (1999) Structure 7: 651-661; and Ymaguchi et al., Structural Basis for Activation of Human Lymphocyte Kinase Lck Upon Tyrosine Phosphorylation (1996) Nature 384: 484-489. U.S. Pat. Nos. 5,322,933, 5,556,778, 5,616,555, 5,872,011 and 6,020,162 disclose the three-dimensional structure of proteins, protein-ligand complex, or enzyme-cofactor complex.

SUMMARY OF THE INVENTION

[0011] The present invention relates to an isolated, purified polynucleotide that encodes a mutant ERAB or HADH2 peptide, wherein the mutant peptide is engineered to avoid cysteine oxidation. It further relates to an isolated, purified polypeptide comprising a mutant ERAB or HADH2 peptide, which is engineered to avoid cysteine oxidation. According to one embodiment, the polypeptide has an amino acid other than cysteine at one or all of positions 5, 58, and/or 214 of SEQ ID NO: 2, and particularly the polypeptide has an amino acid sequence selected from the group consisting of SEQ ID NO: 2, SEQ ID NO: 4, SEQ ID NO: 6, SEQ ID NO: 20, and SEQ ID NO: 23 and functional variants thereof.

[0012] The present invention further relates to a crystalline mutant ERAB or HADH2 peptide. For one embodiment of the invention, the crystalline peptide diffracts x-rays at a resolution value of≦3 Å, and preferably≦2 Å.

[0013] The present invention further relates to a crystal of a mutant ERAB or HADH2 peptide:ligand:NAD+ complex comprising a mutant ERAB or HADH2 peptide:ligand:NAD+.

[0014] The present invention still further relates to a mutant ERAB or HADH2 peptide comprising a fold, wherein the fold comprises: a core β-sheet of seven strands sandwiched between two sets of three α-helices; and first and second insert domains, relative to other members of the short-chain dehydrogenase/reductase (SDR) family, the first insert domain forming a β hairpin that extends the surface of the ERAB or HADH2 peptide on one side of a substrate-binding cleft, and the second insert domain extending a loop between an α-helix comprising residues 123-136 and a β-sheet comprising residues 148-153 of SEQ ID NO: 2.

[0015] The present invention relates to an expression vector comprising a ploynucleotide that encodes a mutant ERAB or HADH2 peptide; transcriptional regulatory sequences functional in the host cell operably linked to the polynucleotide; and a selectable marker, as well as to a host cell stably transfected and transformed with such polynucleotide.

[0016] The present invention further relates to a method for identifying a candidate compound for its ability to interact with the human ERAB or HADH2 peptide comprising:

[0017] (a) expressing an isolated polynucleotide sequence which encodes a mutant ERAB or HADH2 peptide in a host cell capable of producing the peptide;

[0018] (b) exposing the mutant ERAB or HADH2 peptide to the candidate compound; and

[0019] (c) evaluating the interaction of the mutant ERAB or HADH2 peptide with the candidate compound.

[0020] The present invention further relates to a process of drug design for compounds which interact with ERAB or HADH2 comprising:

[0021] (a) crystallizing a mutant ERAB or HADH2 peptide;

[0022] (b) resolving the x-ray crystallography of the peptide;

[0023] (c) applying the data generated from resolving the x-ray crystallography of the peptide to a computer algorithm which generates a model of the peptide suitable for use in designing molecules that will act as agonists or antagonists to the peptide; and

[0024] (d) applying an interative process whereby various molecular structures are applied to the computer-generated model to identify potential agonists or antagonists of the peptide.

[0025] The present invention also relates to a method of assessing compounds which are agonists or antagonists of the activity of the human ERAB or HADH2 enzyme comprising:

[0026] (a) crystallizing a mutant ERAB or HADH2 peptide; obtaining crystallography coordinates for the crystallized peptide;

[0027] (b) applying the crystallography coordinates for the peptide to a computer algorithm such that the algorithm generates a model of the peptide, the model suitable for use in designing molecules that will act as agonists or antagonists to the peptide; and

[0028] (c) applying an iterative process whereby various molecular structures are applied to the computer-generated model to identify potential agonists or antagonists to the peptide.

[0029] The invention further relates to a method of identifying a compound that associates with ERAB or HADH2 comprising the step of using the structure coordinates of Table II to computationally analyze a molecular structure to evaluate a chemical compound for associating with the substrate-binding site of ERAB or HADH2 and identifying those chemical entities that associate with the substrate-binding site, wherein the step of computationally analyzing the molecular structure comprises:

[0030] (a) using a machine readable data storage medium comprising a data storage material encoded with machine readable data wherein the data comprises crystal coordinates of mutant ERAB or HADH2 peptide molecule or complex of the peptide;

[0031] (b) employing a working memory for string instructions for processing the machine readable data,

[0032] (c) using a central processor unit (CPU) coupled to the working memory and the machine readable data for performing a Fourier transformation of the machine readable data and for processing such data into crystal coordinates of three-dimensional molecule or complex of the peptide, and

[0033] (d) displaying a display coupled to the CPU for displaying the crystal coordinates of the three-dimensional moleculer or complex.

[0034] Other aspects, features, and advantages of the invention will be become apparent upon consideration of the detailed description below in conjunction with the appended figures.

BRIEF DESCRIPTION OF THE DRAWINGS

[0035] The file of this patent contains at least one drawing executed in color. Copies of this patent with color drawing(s) will be provided by the Patent and Trademark Office upon request and payment of the necessary fee.

[0036]
FIGS. 1A and 1B depict the three-dimensional structure of the ERAB or HADH2 monomer. FIG. 1A shows the stereo Cα trace of the ERAB or HADH2 monomer. Every tenth residue is numbered. The bound NAD-inhibitor adduct is also shown. FIG. 1B is a ribbon diagram of the ERAB or HADH2 monomer, with the NAD-inhibitor adduct shown in ball-and-stick representation. The ribbon is white at the amino terminus and becomes darker blue moving toward the carboxy terminus. Alpha-carbon positions of residues in the insertion regions of ERAB or HADH2 are shown as yellow spheres.

[0037]
FIG. 2 shows the sequence alignment of wild-type ERAB or HADH2 and representative members of the SDR family. The wild-type ERAB or HADH2 sequence is aligned with five related members of the SDR family: E. coli 7α-hydroxysteroid dehydrogenase (7α-HSD), Streptomyces hydrogenans 3α-20β-hydroxysteroid dehydrogenase (3α-20β-HSD), human 17β-hydrodroxysteroid dehydrogenase (17β-HSD), human 15-hydroxyprostaglandin dehydrogenase (15-PGD; P15428) (Ensor et al., Journal of Biochemistry, Vol. 265, pp. 14888-91 (1990)) and a human protein of unknown function, GenBank accession number CAA20237.1. 7α-HSD (1fmc) and 3α-20β-HSD (1hdc) are two proteins with known structures that are closely related to ERAB or HADH2; 17β-HSD (1fdt) is a similar human protein of known structure. A gapped sequence alignment for comparison is derived using Gapped BLAST [Altschul et al., Nucleic Acids Research, Vol. 25, pp. 3389-3402 (1997)] to search NCBI's GenBank database. Results indicate that 15-PGD is a human protein sequence similar to ERAB or HADH2; CAA20237.1 is a human nucleotide sequence that is similar when translated to its corresponding protein sequence. The alignment of ERAB or HADH2 to 17β-HSD, 7α-HSD, and 3α-20β-HSD was derived from a structural superposition using the tools in Insight II [available through Molecular Simulations Inc. (1999)] coupled with visual inspection. The sequences of 15-PGD and translated CAA20237.1 were aligned to the resulting profile using CLUSTALW [Thompson et al., Nucleic Acids Research, Vol. 22, pp. 4673-4680 (1994)]. Every tenth residue in ERAB or HADH2 is labeled. The secondary structure elements of ERAB or HADH2, as identified by PROCHECK (Laskowski et al., Journal of Applied Crystallography, Vol. 26, pp. 283-291 (1993)), are underlined and labeled above the sequences. Residues that are identical (&Circlesolid;) or similar (∘) in all six proteins are marked beneath the sequences. The first six residues of ERAB or HADH2, which are disordered in the crystal structure, are not shown. The final 53 residues of 17β-HSD are also not shown.

[0038]
FIG. 3 is a ribbon representation of the ERAB or HADH2 tetramer. The tetramer is viewed down one of three mutually perpendicular two-fold axes. Individual monomers are shown in red, green, blue and yellow. The bound NAD+ and NAD-inhibitor adduct molecules are shown in ball-and-stick representation.

[0039]
FIG. 4A shows the structural formula and binding enantiomer of Compound I. FIG. 4B is a stereoview of the electron density for the NAD-Compound I adduct. FIG. 4C depicts the proposed reaction scheme occurring between the NAD+ and Compound I. FIG. 4D is a schematic LIGPLOT (Wallace et al., Protein England Vol. 8, pp. 127 -134 (1995)) view of ERAB or HADH2-Compound I interactions. Compound I, the C4N atom (see Table III) of NAD+, and the enzyme side-chains that form hydrogen bonds to the ligand are shown in ball-and-stick representation.

[0040]
FIG. 5 is a plot of integrated-binding data obtained for a calorimetric titration of wild-type ERAB or HADH2 into Compound I in the presence and absence of cofactor. Wild-type ERAB or HADH2 (415 μM) was titrated into 20 μM inhibitor in the presence and absence of 20 μM cofactor at 15° C. The closed symbols represent the integrated-data points for 10 μL injections of ERAB or HADH2 into inhibitor in the absence of cofactor (♦); in the presence of NAD+ (&Circlesolid;); and in the presence of NADH (▪). The open symbols represent the integrated data points for the corresponding control titrations of ERAB or HADH2 into buffer (Δ); in the presence of NAD+ (∘); and in the presence of NADH (□). Lines connecting the data points have been added for visual clarity.

SEQUENCE LISTINGS

[0041] SEQ ID NO. 1—Full-length mutant ERAB or HADH2 C214R (nucleotide sequence—786 base pairs)

[0042] SEQ ID NO. 2—Full-length mutant ERAB or HADH2 C214R (peptide sequence—261 AA)

[0043] SEQ ID NO. 3—Full-length mutant ERAB or HADH2 C5V (nucleotide sequence—786 base pairs)

[0044] SEQ ID NO. 4—Full-length mutant ERAB or HADH2 C5V (peptide sequence—261 AA)

[0045] SEQ ID NO. 5—Full-length mutant ERAB or HADH2 C58V (nucleotide sequence—786 base pairs)

[0046] SEQ ID NO. 6—Full-length mutant ERAB or HADH2 C58V (peptide sequence—261 AA)

[0047] SEQ ID NO. 7—DNA sequence of wild-type ERAB or HADH2 (nucleotide sequence—786 base pairs)

[0048] SEQ ID NO. 8—Peptide sequence of wild-type ERAB or HADH2 (peptide sequence—261 AA)

[0049] SEQ ID NO. 9—PCR primer

[0050] SEQ ID NO. 10—PCR primer

[0051] SEQ ID NO. 11—Oligonucleotide for C5V

[0052] SEQ ID NO. 12—Oligonucleotide for C58V

[0053] SEQ ID NO. 13—Oligonucleotide for C214R

[0054] SEQ ID NO. 14—Peptide sequence of 7α-HDS

[0055] SEQ ID NO. 15—Peptide sequence of 3α20β-HDS

[0056] SEQ ID NO. 16—Peptide sequence of 17β-HDS

[0057] SEQ ID NO. 17—Peptide sequence of CAA20237.1

[0058] SEQ ID NO. 18—Peptide sequence of 15- PGD

[0059] SEQ ID NO. 19—Full-length mutant ERAB or HADH2 C214A (nucleotide sequence—786 base pairs)

[0060] SEQ ID NO. 20—Full-length mutant ERAB or HADH2 C214A (peptide sequence—261 AA)

[0061] SEQ ID NO. 21—Oligonucleotide for ERAB or HADH2 C214A

[0062] SEQ ID NO. 22—Full-length mutant ERAB or HADH2 C214S (nucleotide sequence—786 base pairs)

[0063] SEQ ID NO. 23—Full-length mutant ERAB or HADH2 C214S (peptide sequence—261 AA)

[0064] SEQ ID NO. 24—Oligonucleotide for ERAB or HADH2 C214S

DETAILED DESCRIPTION OF THE INVENTION

[0065] ERAB or HADH2 is a member of the short-chain dehydrogenase/reductase (SDR) family of enzymes. We have facilitated overexpression of several mutants of the enzyme in E. coli. The mutants having advantageous physical characteristics as compared to the wild-type ERAB or HADH2. The mutant ERAB or HADH2 peptides of the present invention have sufficient activity, stability and solubility so as to allow for peptide crystallization and subsequent x-ray crystallography characterization. Such properties facilitate the resolution of the three-dimensional crystal structure of human ERAB or HADH2 as well as the characterization of several structural features of ERAB or HADH2 responsible for interactions associated with high-affinity binding of substrates to ERAB or HADH2. Such interactions include the formation of a covalent linkage between the bound substrate and the NAD+ cofactor.

[0066] We have determined the crystal structure of human ERAB or HADH2 with NAD+ and an inhibitory small molecule bound thereto. The inhibitor occupies the substrate-binding site and forms a covalent adduct with the NAD+ cofactor. The crystal structure provides a basis for the design of ERAB or HADH2 inhibitors with potential application in the treatment of Alzheimer's disease. Crystals of ERAB or HADH2 with bound NAD+ and Compound I were obtained using the C214R mutant of the enzyme. This mutant was produced to avoid potential problems with cysteine oxidation in the protein, with arginine selected as the replacement amino acid because of its occurrence at this position in other mammalian ERAB or HADH2 sequences [He et al. (1998), supra]. Enzymatic activity of the C214R mutant protein is comparable to that of the wild-type protein. The crystal structure of the ERAB or HADH2:NAD+:Compound I complex was determined at 2.0 Å using molecular replacement techniques. The search model for molecular replacement was our 1.9 Å resolution structure of the mutant ERAB or HADH2:NAD+ complex. The structure was refined to an R factor of 0.215 for all data to 2.0 Å resolution. Data collection, structure determination, and refinement statistics are summarized in Table I. The resolution of the ERAB or HADH2 crystal structure allows for efficient design and development of inhibitors or modulators of human ERAB or HADH2. Inhibition of ERAB or HADH2 finds therapeutic utility in the treatment of AD. In addition to any therapeutic application, ERAB or HADH2 inhibitors can facilitate the delineation of the role of the enzyme in both normal cellular function and in Aβ pathogenesis.

[0067] The invention encompasses both the mutant peptides per se and salts thereof. The peptide may be synthetically or naturally produced. The invention further relates to an isolated, purified polynucleotide which encodes an enzymatically active peptide mutant of ERAB or HADH2 in the active conformation. The polynucleotide may be natural or recombinant.

[0068] The invention provides an expression vector for producing an enzymatically active mutant of human ERAB or HADH2 peptide in a host cell. The invention further relates to a host cell stably transformed and transfected with a polynucleotide encoding an enzymatically active peptide mutant of ERAB or HADH2, or fragment thereof, or an active functional analog thereof, in a manner allowing the expression of the enzymatically active peptide mutant of ERAB or HADH2 in the active conformation.

[0069] According to the present invention, an inhibitor (Compound I) of ERAB or HADH2 and the crystal structure of the ERAB or HADH2:NAD+:inhibitor complex are provided. The availability of a potent specific inhibitor of ERAB or HADH2 can facilitate the detailed analysis of the role of this enzyme in AD pathogenesis and may ultimately provide a new therapeutic approach for treatment of the disease. The crystal structure of the enzyme:inhibitor:cofactor complex provides a basis for the design of additional inhibitors and for elucidating the nature of the interactions between ERAB or HADH2 and the amyloid-β peptide.

[0070] The molecular structure of the x-ray crystallography data may be used to model the binding of candidate compounds in order to screen candidate compounds. In accordance with the invention, there is also provided several structural features unique to ERAB or HADH2 as compared to other members of the short-chain dehydrogenase/reductase (SDR) family. Some of these features are responsible for the high-affinity binding of an inhibitor compound to the ERAB or HADH2 substrate-binding site, including the formation of a covalent linkage between inhibitor and the NAD+ cofactor.

[0071] Potential inhibitors or modulators of the human ERAB or HADH2 may be identified according to the method of the present invention. Potential therapeutic compounds for the treatment of various disease conditions associated with the ERAB or HADH2, for example neurodegenerative diseases and cancers may be designed and screened according to the present invention. In the designing and screening processes, the DNA sequence or variants thereof encoding the mutant ERAB or HADH2 peptide is expressed, and may be assayed for interaction of the enzyme with the candidate compound by exposing the enzyme to the candidate compound and evaluating the interaction of the enzyme with the candidate compound. The designing and synthesis as well as screening may be automated, for example, utilizing robotic techniques.

[0072] Three-dimensional molecular structure of ERAB or HADH2 of the present invention may be used to model the binding of candidate compounds to the ERAB or HADH2 binding site, facilitating screening candidate compounds. The x-ray crystallographic coordinates disclosed herein, allow for the generation of three-dimensional models of the catalytic region and binding site of the human ERAB or HADH2. Design of inhibitors generally involves the generation of molecules via the use of computer programs, which build and link fragments or atoms into a site based upon steric and electrostatic complementary, without reference to substrate analog structures. The drug design process begins after the structure of the target (human ERAB or HADH2) is solved to at least a resolution of 3 Å, more preferably 2.5 Å, even more preferably 2 Å. Refinement of the structure to a resolution of 2 Å or better with fixed water molecules in place provides more optimal conditions to undertake drug design.

[0073] In one preferred embodiment, the method of screening utilized the steps of (a) computer-generating a virtual-binding cavity, the binding cavity defined by the binding sites; (b) computer-generating a compound structure that spatially conforms to the binding cavity; and (c) testing to see whether said compound binds to at least one of the stated-binding sites.

[0074] The invention also has utility in the iterative drug design process. The process screens potential inhibitors or modulators of the ERAB or HADH2 enzyme by determining their ability to bind to and inhibit or modulate the ERAB or HADH2. The x-ray crystallographic coordinates disclosed herein allow advantageously generation of three-dimensional models of the enzymatically active site and the drug-binding site of the ERAB or HADH2 protein. De novo design comprises of the generation of molecules via the use of computer programs which build and link fragments or atoms into a site based upon steric and electrostatic complementarily, without reference to substrate analog structures. The determination of the structure of the target (human ERAB or HADH2) is solved to at least a resolution of 3 Å, more preferably 2.5 Å, even more preferably 2 Å. Refinement of the structure to a resolution of 2 Å or better with fixed water molecules in place provides more optimal conditions to undertake drug design.

[0075] In one preferred embodiment, the method for identifying potential inhibitors utilizes the steps of (a) designing a potential inhibitor or modulator for ERAB or HADH2 that will interact with amino acids in the ERAB or HADH2 substrate-binding site based on the crystal coordinates of the mutant ERAB or HADH2 peptide:ligand:NAD+ complex set forth in Table II; and (b) synthesizing the potential inhibitor or modulator and assaying it to determine whether it inhibits or modulates the activity of ERAB or HADH2.

[0076] Rapidly screening methods to assay those compounds that inhibit or modulate the ERAB or HADH2 enzyme or core structure for further ERAB or HADH2 inhibitor design may be used. The high throughput-screening assay is capable of being fully automated on robotic workstations. The assay may employ radioactivity or other materials useful for detection.

[0077] A computer processor may be used for analyzing a molecular structure comprising by using a machine-readable data storage medium comprising a data storage material encoded with machine-readable data. The data comprises crystal coordinates of mutant ERAB or HADH2 peptide molecule or its molecular complex. In this method, a CPU coupled to a working memory and the machine readable data may be used to perform a Fourier transformation of the machine readable data and to process such data into crystal coordinates of three-dimensional molecule or complex of said peptide. The x-ray coordinate data may be processed into three-dimensional graphical display using a computer-based method. The machine-readable data storage medium may include CD-ROM, magneto-optic disk, or other storage media.

[0078] The terms as used herein are explained below. Also, as used herein, the terms “comprising” and “including” are used in the conventional, non-limiting sense.

[0079] A. Peptides, Proteins and Antibodies

[0080] The present invention provides isolated peptide and protein molecules that consist of, consist essentially of or are comprised of the amino acid sequences of the mutant peptides encoded by the nucleic acid sequences disclosed in the SEQ ID NO: 1, SEQ ID NO: 3, SEQ ID NO: 5, SEQ ID NO: 19 and SEQ ID NO: 22 as well as all obvious variants of these peptides that the within the art to make and use. Some of these variants are described in detail below.

[0081] The invention also includes a modified, enzymatically active ERAB or HADH2 peptide comprising a fold, wherein said fold comprises: a core β-sheet of seven strands sandwiched between two sets of three α-helices; and first and second insert domains, relative to other members of the SDR family, the first insert domain forming a β hairpin that extends the surface of said ERAB or HADH2 peptide on one side of a substrate-binding cleft, and the second insert domain extending a loop between an α-helix comprising residues 123-136 and a β-sheet comprising residues 148-153 of SEQ ID NO: 2. The invention provides a peptide having an amino acid sequence comprising amino acids 90 to 261 of SEQ ID NO. 2 or an active or functional variant thereof.

[0082] As used herein, a peptide is said to be “isolated” or “purified” when it is substantially free of homologous cellular material or free of chemical precursors or other chemicals. The peptides of the present invention can be purified to homogeneity or other degrees of purity. The level of purification will be based on the intended use. The critical feature is that the preparation allows for the desired function of the peptide, even if in the presence of considerable amounts of other components.

[0083] In some uses, “substantially free of cellular material” includes preparations of the peptide having less than 30% (by dry weight) other proteins (i.e., contaminating protein), preferably less than 20% other proteins, more preferably less than 10% other proteins, or most preferably less than 5% other proteins. When the peptide is recombinantly produced, it can also be substantially free of culture medium, i.e., culture medium represents less than 20% of the volume of the protein preparation.

[0084] The language “substantially free of chemical precursors or other chemicals” includes preparations of the peptide in which it is separated from chemical precursors or other chemicals that are involved in its synthesis. In one embodiment, the language “substantially free of chemical precursors or other chemicals” includes preparations of the mutant peptide having less than 30% (by dry weight) chemical precursors or other chemicals, preferably less than 20% chemical precursors or other chemicals, more preferably less than 10% chemical precursors or other chemicals, or most preferably less than 5% chemical precursors or other chemicals.

[0085] The isolated mutant peptide described herein can be purified from cells that naturally express it, purified from cells that have been altered to express it (recombination), or synthesized using known protein synthesis methods. For example, a nucleic acid molecule encoding the mutant peptide is cloned into an expression vector, the expression vector introduced into a host cell and the peptide expressed in the host cell. The peptide can then be isolated from the cells by an appropriate purification scheme using standard peptide/protein purification techniques. Many of these techniques are described in detail below.

[0086] As mentioned above, the present invention also provides and enables obvious variants of the amino acid sequence of the peptides of the present invention, such as naturally occurring mature forms of the peptides, allelic/sequence variants of the peptides, non-naturally occurring recombinantly derived variants of the peptides, and orthologs and paralogs of the peptides. Such variants can be generated using techniques that are known by those skilled in the fields of recombinant nucleic acid technology and protein biochemistry.

[0087] Such variants can readily be identified/made using molecular techniques and the sequence information disclosed herein. Further, such variants can readily be distinguished from other peptides based on sequence and/or structural homology to the peptides of the present invention. The degree of homology/identity present will be based primarily on whether the peptide is a functional variant or non-functional variant, the amount of divergence present in the paralog family and the evolutionary distance between the orthologs.

[0088] To determine the percent identity of two amino acid sequences or two nucleic acid sequences, the sequences are aligned for optimal comparison purposes (e.g., gaps can be introduced in one or both of a first and a second amino acid or nucleic acid sequence for optimal alignment and non-homologous sequences can be disregarded for comparison purposes). The length of a reference sequence aligned for comparison purposes is at least 30%, preferably 40%, more preferably 50%, even more preferably 60% or more of the length of the reference sequence. In a preferred embodiement, the length of a reference sequence aligned for comparison purposes is at least 70%, preferably 80%, more preferably 90% or more of the length of the reference sequence. The amino acid residues or nucleotides at corresponding amino acid positions or nucleotide positions are then compared. When a position in the first sequence is occupied by the same amino acid residue or nucleotide as the corresponding position in the second sequence, then the molecules are identical at that position (as used herein amino acid or nucleic acid ‘identity’ is equivalent to amino acid or nucleic acid ‘homology’). The percent identity between the two sequences is a function of the number of identical positions shared by the sequences, taking into account the number of gaps, and the length of each gap, which need to be introduced for optimal alignment of the two sequences.

[0089] The comparison of sequences and determination of percent identity and similarity between two sequences can be accomplished using a mathematical algorithm. (See, e.g., Computational Molecular Biology, Lesk, A. M., ed., Oxford University Press, New York, 1988; Biocomputing: Informatics and Genome Projects, Smith, D. W., ed., Academic Press, New York, 1993; Computer Analysis of Sequence Data, Part 1, Griffin, A. M., and Griffin, H. G., eds., Humana Press, New Jersey, 1994; Sequence Analysis in Molecular Biology, von Heinje, G., Academic Press, 1987; and Sequence Analysis Primer, Gribskov, M. and Devereux, J., eds., M Stockton Press, New York, 1991). In a preferred embodiment, the percent identity between two amino acid sequences is determined using the Needleman and Wunsch (J. Mol. Biol (48):444-453 (1970)) algorithm which has been incorporated into commercially available computer programs, such as GAP in the GCG software package, using either a Blossom 62 matrix or a PAM250 matrix, and a gap weight of 16, 14, 12, 10, 8, 6, or 4 and a length weight of 1, 2, 3, 4, 5, or 6. In yet another preferred embodiment, the percent identity between two nucleotide sequences can be determined using the commercially available computer programs including the GAP program in the GCG software package (Devereux, J., et al., Nucleic Acids Res. 12(1):387 (1984)), the NWS gap DNA CMP matrix and a gap weight of 40, 50, 60, 70, or 80 and a length weight of 1, 2, 3, 4, 5, or 6. In another embodiment, the percent identity between two amino acid or nucleotide sequences is determined using the algorithm of E. Meyers and W. Miller (CABIOS, 4:11-17 (1989)) which has been incorporated into commercially available computer programs, such as ALIGN (version 2.0), using a PAM120 weight residue table, a gap length penalty of 12 and a gap penalty of 4.

[0090] The nucleic acid and protein sequences of the present invention can further be used as a “query sequence” to perform a search against sequence databases to, for example, identify other family members or related sequences. Such searches can be performed using commercially available search engines, such as the NBLAST and XBLAST programs (version 2.0) of Altschul, et al. (J. Mol. Biol. 215:403-10 (1990)). BLAST nucleotide searches can be performed with the NBLAST program, score=100, wordlength=12 to obtain nucleotide sequences homologous to the nucleic acid molecules of the invention. BLAST protein searches can be performed with the XBLAST program, score=50, wordlength=3 to obtain amino acid sequences homologous to the proteins of the invention. To obtain gapped alignments for comparison purposes, Gapped BLAST can be utilized as described in Altschul et al. (Nucleic Acids Res. 25(17):3389-3402 (1997)). When utilizing BLAST programs, the default parameters of the respective programs (e.g., XBLAST and NBLAST) can be used.

[0091] Full-length clones comprising one of the peptides of the present invention can readily be identified as having complete sequence identity to one of the mutant peptides of human ERAB or HADH2 of the present invention as well as being encoded by the same genetic locus as the mutant peptide provided herein.

[0092] Allelic variants of a peptide can readily be identified as having a high degree (significant) of sequence homology/identity to at least a portion of the peptide as well as being encoded by the same genetic locus as the mutant peptide provided herein. As used herein, two proteins (or a region of the proteins) have significant homology when the amino acid sequences are typically at least 70%, preferably 75%, more preferably 80% or 85%, and typically at least 90%, more preferably 95% or more homologous. A significantly homologous amino acid sequence, according to the present invention, will be encoded by a nucleic acid sequence that will hybridize to a peptide encoding nucleic acid molecule under stringent conditions as described below.

[0093] Paralogs of a peptide can readily be identified as having some degree of significant sequence homology/identity to at least a portion of the mutant peptide as well as being encoded by a gene from human, and as having similar activity or function. Two proteins will typically be considered paralogs when the amino acid sequences are typically at least 70%, preferably 80%, more preferably at least 90%, most preferably 95% or more homologous through a given region or domain. Such paralogs will be encoded by a nucleic acid sequence that will hybridize to a mutant peptide encoding nucleic acid molecule under stringent conditions as described in the section “B. Nucleic Acids and Polynucleotides” below.

[0094] Orthologs of a mutant peptide can readily be identified as having some degree of significant sequence homology/identity to at least a portion of the mutant peptide as well as being encoded by a gene from another organism. Preferred orthologs will be isolated from mammals other than human, for the development of human therapeutic targets and agents, or other invertebrates, particularly insects of economical/agriculture importance, e.g. members of the Lepidopteran and Coleopteran orders, for the development of insecticides and insecticidal targets. Such orthologs will be encoded by a nucleic acid sequence that will hybridize to a mutant peptide encoding nucleic acid molecule under moderate to highly stringent conditions, as more fully described below, depending on the degree of relatedness of the two organisms yielding the proteins.

[0095] Non-naturally occurring variants of the mutant peptides of the present invention can readily be generated using recombinant techniques. Such variants include, but are not limited to deletions, additions and substitutions in the amino acid sequence of the mutant peptide. For example, one class of substitutions involves conserved amino acid changes. Such substitutions are those that substitute a given amino acid in a peptide by another amino acid of like characteristics. Typically seen as conservative substitutions are the replacements, one for another, among the aliphatic amino acids Ala, Val, Leu, and Ile; interchange of the hydroxyl residues Ser and Thr; exchange of the acidic residues Asp and Glu; substitution between the amide residues Asn and Gln; exchange of the basic residues Lys and Arg; and replacements among the aromatic residues Phe, Tyr. Guidance concerning which amino acid changes are likely to be phenotypically silent are found in Bowie et al., Science 247:1306-1310 (1990).

[0096] Variants of the mutant peptide can be fully functional or can lack function in one or more activities. Fully functional variants typically contain only conservative variation or variation in non-critical residues or in non-critical regions. Functional variants can also contain substitution of similar amino acids, which result in no change or an insignificant change in function. Alternatively, such substitutions may positively or negatively affect function to some degree.

[0097] Non-functional variants typically contain one or more non-conservative amino acid substitutions, deletions, insertions, inversions, or truncation or a substitution, insertion, inversion, or deletion in a critical residue or critical region.

[0098] Amino acids that are essential for function can be identified by methods known in the art, such as site-directed mutagenesis or alanine-scanning mutagenesis (Cunningham et al., Science 244:1081-1085 (1989)). The latter procedure introduces single alanine mutations at every residue in the molecule. The resulting mutant molecules are then tested for biological activity such as receptor binding or in vitro proliferative activity. Sites that are critical for binding can also be determined by structural analysis such as x-ray crystallography, nuclear magnetic resonance or photoaffinity labeling (Smith et al., J. Mol. Biol. 224:899-904 (1992); de Vos et al. Science 255:306-312 (1992)). Accordingly, the polypeptides also encompass derivatives or analogs in which a substituted amino acid residue is not one encoded by the genetic code; in which a substituent group is included, in which the mature polypeptide is fused with another compound, such as a compound to increase the half-life of the polypeptide (for example, polyethylene glycol), or in which the additional amino acids are fused to the mature polypeptide, such as a leader or secretory sequence or a sequence for purification of the mature polypeptide or a pro-protein sequence.

[0099] “Polypeptide” refers to any peptide or protein comprising two or more amino acids joined to each other by peptide bonds or modified peptide bonds, i.e., peptide isosteres. “Polypeptide” refers to both short chains, commonly referred to as peptides, oligopeptides or oligomers, and to longer chains, generally referred to as proteins. The terms “peptide”, “polypeptide” and “protein” are used interchangeably herein. Polypeptides may contain amino acids other than the 20 naturally occurring amino acids. Further, many amino acids, including the terminal amino acids, may be modified by natural processes, such as processing and other post-translational modifications, or by chemical modification techniques well known in the art. Common modifications that occur naturally in polypeptides are described in basic texts, detailed monographs, and the research literature, and they are well known to those of skill in the art. Generally known modifications include, but are not limited to, acetylation, acylation, ADP-ribosylation, amidation, covalent attachment of flavin, covalent attachment of a heme moiety, covalent attachment of a nucleotide or nucleotide derivative, covalent attachment of a lipid or lipid derivative, covalent attachment of phosphotidylinositol, cross-linking, cyclization, disulfide bond formation, demethylation, formation of covalent crosslinks, formation of cystine, formation of pyroglutamate, formylation, gamma carboxylation, glycosylation, GPI anchor formation, hydroxylation, iodination, methylation, myristoylation, oxidation, proteolytic processing, phosphorylation, phenylation, racemization, selenoylation, sulfation, transfer-RNA mediated addition of amino acids to proteins such as arginylation, and ubiquitination. Several particularly common modifications, glycosylation, lipid attachment, sulfation, gamma-carboxylation of glutamic acid residues, hydroxylation and ADP-ribosylation, for instance, are described in most basic texts, such as Creighton, Proteins—Structure and Molecular Properties, 2nd Ed., W. H. Freeman and Company, New York (1993). Many reviews are available on this subject, such as Wold, Posttranslational Covalent Modification of Proteins, B. C. Johnson, Ed., Academic Press, New York 1-12 (1983); Seifter et al. (Meth. Enzymol. 182:626-646 (1990)) and Rattan et al. (Ann. N.Y. Acad. Sci. 663:48-62 (1992)).

[0100] The present invention further provides for fragments of the mutant peptides, in addition to proteins and peptides that comprises and consist of such fragments.

[0101] As used herein, a fragment comprises at least 8 or more contiguous amino acid residues from the mutant peptide of ERAB or HADH2. Such fragments can be chosen based on the ability to retain one or more of the biological activities of the ERAB or HADH2 or could be chosen for the ability to perform a function, e.g. act as an immunogen. Particularly important fragments are biologically active fragments, peptides which are, for example about 8 or more amino acids in length. Such fragments will typically comprise a domain or motif of the mutant peptide, e.g., active site. Further, possible fragments include, but are not limited to, domain or motif containing fragments, soluble peptide fragments, and fragments containing immunogenic structures. Predicted domains and functional sites are readily identifiable by computer programs well-known and readily available to those of skill in the art (e.g., by PROSITE analysis).

[0102] The peptides of the present invention can be attached to heterologous sequences to form chimeric or fusion proteins. Such chimeric and fusion proteins comprise a peptide operatively linked to a heterologous protein having an amino acid sequence not substantially homologous to the mutant peptide of ERAB or HADH2. “Operatively linked” indicates that the peptide and the heterologous protein are fused in-frame. The heterologous protein can be fused to the N-terminus or C-terminus of the mutant peptide of ERAB or HADH2. The two peptides linked in a fusion peptide are typically derived from two independent sources, and therefore a fusion peptide comprises two linked peptides not normally found linked in nature. The two peptides may be from the same or different genome.

[0103] In some uses, the fusion protein does not affect the activity of the peptide per se. For example, the fusion protein can include, but is not limited to, enzymatic fusion proteins, for example beta-galactosidase fusions, yeast two-hybrid GAL fusions, poly-His fusions, MYC-tagged, HI-tagged and Ig fusions. Such fusion proteins, particularly poly-His fusions, can facilitate the purification of recombinant peptide. In certain host cells (e.g., mammalian host cells), expression and/or secretion of a protein can be increased by using a heterologous signal sequence.

[0104] A chimeric or fusion protein can be produced by standard recombinant DNA techniques. For example, DNA fragments coding for the different protein sequences are ligated together in-frame in accordance with conventional techniques. In another embodiment, the fusion gene can be synthesized by conventional techniques including automated DNA synthesizers. Alternatively, PCR amplification of gene fragments can be carried out using anchor primers which give rise to complementary overhangs between two consecutive gene fragments which can subsequently be annealed and re-amplified to generate a chimeric gene sequence [see Ausubel et al., Current Protocols in Molecular Biology (1992)]. Moreover, many expression vectors are commercially available that already encode a fusion moiety (e.g., a GST protein). A mutant ERAB or HADH2 peptide-encoding nucleic acid can be cloned into such an expression vector such that the fusion moiety is linked in-frame to the mutant peptide.

[0105] B. Nucleic Acids and Polynucleotides

[0106] The present invention provides isolated nucleic acid molecules that encode the functional, active mutant peptides of ERAB or HADH2 of the present invention. Such nucleic acid molecules will consist of, consist essentially of, or comprise a nucleotide sequence that encodes one of the peptides of the present invention, an allelic variant thereof, or an ortholog or paralog thereof.

[0107] As used herein, an “isolated” nucleic acid molecule is one that is separated from other nucleic acid present in the natural source of the nucleic acid. Preferably, an “isolated” nucleic acid is free of sequences which naturally flank the nucleic acid (i.e., sequences located at the 5′ and 3′ ends of the nucleic acid) in the genomic DNA or cDNA of the organism from which the nucleic acid is derived. However, there can be some flanking nucleotide sequences, for example up to about 5KB, particularly contiguous peptide encoding sequences and peptide encoding sequences within the same gene but separated by introns in the genomic sequence. The important point is that the nucleic acid is isolated from remote and unimportant flanking sequences such that it can be subjected to the specific manipulations described herein such as recombinant expression, preparation of probes and primers, and other uses specific to the nucleic acid sequences.

[0108] Moreover, an “isolated” nucleic acid molecule, such as a cDNA molecule, can be substantially free of other cellular material, or culture medium when produced by recombinant techniques, or chemical precursors or other chemicals when chemically synthesized. However, the nucleic acid molecule can be fused to other coding or regulatory sequences and still be considered isolated.

[0109] For example, recombinant DNA molecules contained in a vector are considered isolated. Further examples of isolated DNA molecules include recombinant DNA molecules maintained in heterologous host cells or purified (partially or substantially) DNA molecules in solution. Isolated RNA molecules include in vivo or in vitro RNA transcripts of the isolated DNA molecules of the present invention. Isolated nucleic acid molecules according to the present invention further include such molecules produced synthetically.

[0110] Full-length genes may be cloned from known sequence using any one of a number of methods known in the art. For example, a method which employs XL-PCR (Perkin-Elmer, Foster City, Calif.) to amplify long pieces of DNA may be used. Other methods for obtaining full-length sequences are known in the art.

[0111] The isolated nucleic acid molecules can encode the active protein plus additional amino or carboxyl-terminal amino acids, or amino acids interior to the mature peptide (when the mature form has more than one peptide chain, for instance). Such sequences may play a role in processing of a protein from precursor to an active form, facilitate protein trafficking, prolong or shorten protein half-life or facilitate manipulation of a protein for assay or production, among other things. As generally is the case in situ, the additional amino acids may be processed away from the mature protein by cellular enzymes. As mentioned above, the isolated nucleic acid molecules include, but are not limited to, the sequence encoding the active mutant peptide of ERAB or HADH2 alone or in combination with coding sequences, such as a leader or secretory sequence (e.g., a pre-pro or pro-protein sequence), the sequence encoding the active mutant peptide, with or without the additional coding sequences, plus additional non-coding sequences, for example introns and non-coding 5′ and 3′ sequences such as transcribed but non-translated sequences that play a role in transcription, including mRNA processing (including splicing and polyadenylation signals), ribosome binding sites and sequences important for stability of MRNA. In addition, the nucleic acid molecule may be fused to a marker sequence encoding, for example, a peptide that facilitates purification.

[0112] Isolated nucleic acid molecules can be in the form of RNA, such as mRNA, or in the form of DNA, including cDNA and genomic DNA, obtained by cloning or produced by chemical synthetic techniques or by a combination thereof. The nucleic acid, especially DNA, can be double-stranded or single-stranded. Single-stranded nucleic acid can be the coding strand (sense strand) or the non-coding strand (antisense strand).

[0113] The invention further provides nucleic acid molecules that encode fragments of the peptides of the present invention and that encode obvious variants of the peptides of the present invention that are described herein. Such nucleic acid molecules may be naturally occurring, such as allelic variants (same locus), paralogs (different locus), and orthologs (different organism), or may be constructed by recombinant DNA methods or by chemical synthesis. Such non-naturally occurring variants may be made by mutagenesis techniques, including those applied to nucleic acid molecules, cells, or organisms. Accordingly, as discussed above, the variants can contain nucleotide substitutions, deletions, inversions and insertions. Variation can occur in either or both the coding and non-coding regions. The variations can produce both conservative and non-conservative amino acid substitutions.

[0114] A fragment comprises a contiguous nucleotide sequence greater than 12 or more nucleotides. Further, a fragment could be at least 30, preferably 40, more preferably 50, even more preferably 100, most preferably 250 or 500 nucleotides in length. The length of the fragment will be based on its intended use. For example, the fragment can encode epitope bearing regions of the peptide, or can be useful as DNA probes and primers. Such fragments can be isolated using the known nucleotide sequence to synthesize an oligonucleotide probe. A labeled probe can then be used to screen a cDNA library, genomic DNA library, or MRNA to isolate nucleic acid corresponding to the coding region. Further, primers can be used in PCR reactions to clone specific regions of gene.

[0115] A probe/primer typically comprises a substantially purified oligonucleotide or oligonucleotide pair. The oligonucleotide typically comprises a region of nucleotide sequence that hybridizes under stringent conditions to at least 12, preferably 20, more preferably 25, even more preferably 40, most preferably 50 or more consecutive nucleotides.

[0116] Orthologs, homologs, and allelic variants can be identified using methods known in the art. As described above, these variants comprise a nucleotide sequence encoding a peptide that is typically 60%, preferably 70%, more preferably 80%, even more preferably 85%, and typically at least 90%, preferably 95% or more homologous to the nucleotide sequence provided in SEQ ID NO: 1, SEQ ID NO: 3, SEQ ID NO: 5, SEQ ID NO: 19 or SEQ ID NO: 22, or a fragment of these sequences. Such nucleic acid molecules can readily be identified as being able to hybridize under moderate to highly stringent conditions, to the nucleotide sequences shown in SEQ ID NO: 1, SEQ ID NO: 3, SEQ ID NO: 5, SEQ ID NO: 19 or SEQ ID NO: 22, or a fragment thereof.

[0117] As used herein, the term “hybridizes under stringent conditions” is intended to describe conditions for hybridization and washing under which nucleotide sequences encoding a peptide at least 50%, preferably 55% or more homologous to each other typically remain hybridized to each other. The conditions can be such that sequences at least 65%, preferably 70%, more preferably 75% or more homologous to each other typically remain hybridized to each other. Standard hybridization conditions from moderate to highly stringent conditions are known to those skilled in the art (See e.g., Current Protocols in Molecular Biology, John Wiley & Sons, N.Y. (1989), 6.3.1-6.3.6). Moderate hybridization conditions are defined as equivalent to hybridization in 2×sodium chloride/sodium citrate (SSC) at 30° C., followed by one or more washes in 1×SSC, 0.1% SDS at 50-60° C. Highly stringent conditions are defined as equivalent to hybridization in 6×sodium chloride/sodium citrate (SSC) at 45° C., followed by one or more washes in 0.2×SSC, 0.1% SDS at 50-65° C.

[0118] The nucleic acid molecules of the present invention are useful for probes, primers, chemical intermediates, and in biological assays. The nucleic acid molecules are useful as a hybridization probe for cDNA and genomic DNA to isolate full-length cDNA and genomic clones encoding the peptide described herein and to isolate cDNA and genomic clones that correspond to variants (alleles, orthologs, etc.) producing the same or related peptides described herein.

[0119] The probe can correspond to any sequence along the entire length of the nucleic acid molecules provided in the SEQ ID NO: 1, SEQ ID NO: 3. SEQ ID NO: 5, SEQ ID NO: 19 or SEQ ID NO: 22. Accordingly, it could be derived from 5′ noncoding regions, the coding region, and 3′ noncoding regions.

[0120] The nucleic acid molecules are also useful as primers for PCR to amplify any given region of a nucleic acid molecule and are useful to synthesize antisense molecules of desired length and sequence.

[0121] The nucleic acid molecules are also useful for constructing recombinant vectors. Such vectors include expression vectors that express a portion of, or all of, the peptide sequences. Vectors also include insertion vectors, used to integrate into another nucleic acid molecule sequence, such as into the cellular genome, to alter in situ expression of a gene and/or gene product. For example, an endogenous coding sequence can be replaced via homologous recombination with all or part of the coding region containing one or more specifically introduced mutations.

[0122] The nucleic acid molecules are also useful for expressing antigenic portions of the proteins; for determining the chromosomal positions of the nucleic acid molecules by means of in situ hybridization methods; for designing ribozymes corresponding to all, or a part, of the mRNA produced from the nucleic acid molecules described herein; for constructing host cells expressing a part, or all, of the nucleic acid molecules and peptides; for constructing transgenic animals expressing all, or a part, of the nucleic acid molecules and peptides; and for making vectors that express part, or all, of the peptides.

[0123] The nucleic acid molecules are also useful as hybridization probes for determining the presence, level, form and distribution of nucleic acid expression. Accordingly, the probes can be used to detect the presence of, or to determine levels of, a specific nucleic acid molecule in cells, tissues, and in organisms. The nucleic acid whose level is determined can be DNA or RNA. Accordingly, probes corresponding to the peptides described herein can be used to assess expression and/or gene copy number in a given cell, tissue, or organism. These uses are relevant for diagnosis of disorders involving an increase or decrease in protein expression relative to normal results.

[0124] In vitro techniques for detection of mRNA include Northern hybridizations and in situ hybridizations. In vitro techniques for detecting DNA include Southern hybridizations and in situ hybridization.

[0125] Probes can be used as a part of a diagnostic test kit for identifying cells or tissues that express a protein.

[0126] C. Vectors and Host Cells

[0127] The invention also provides vectors containing the nucleic acid molecules described herein. The term “vector” refers to a vehicle, preferably a nucleic acid molecule, that can transport the nucleic acid molecules. When the vector is a nucleic acid molecule, the nucleic acid molecules are covalently linked to the vector nucleic acid. With this aspect of the invention, the vector includes a plasmid, single or double stranded phage, a single or double stranded RNA or DNA viral vector, or artificial chromosome, such as a BAC, PAC, YAC, OR MAC. Various expression vectors can be used to express polynucleotide encoding the mutant peptide of human ERAB or HADH2.

[0128] A vector can be maintained in the host cell as an extrachromosomal element where it replicates and produces additional copies of the nucleic acid molecules. Alternatively, the vector may integrate into the host cell genome and produce additional copies of the nucleic acid molecules when the host cell replicates.

[0129] The invention provides vectors for the maintenance (cloning vectors) or vectors for expression (expression vectors) of the nucleic acid molecules. The vectors can function in prokaryotic or eukaryotic cells or in both (shuttle vectors).

[0130] Expression vectors contain cis-acting regulatory regions that are operably linked in the vector to the nucleic acid molecules such that transcription of the nucleic acid molecules is allowed in a host cell. The nucleic acid molecules can be introduced into the host cell with a separate nucleic acid molecule capable of affecting transcription. Thus, the second nucleic acid molecule may provide a trans-acting factor interacting with the cis-regulatory control region to allow transcription of the nucleic acid molecules from the vector. Alternatively, a trans-acting factor may be supplied by the host cell. Finally, a trans-acting factor can be produced from the vector itself. It is understood, however, that in some embodiments, transcription and/or translation of the nucleic acid molecules can occur in a cell-free system.

[0131] The regulatory sequences to which the nucleic acid molecules described herein can be operably linked include promoters for directing mRNA transcription. These include, but are not limited to, the left promoter from bacteriophage λ, the lac, TRP, and TAC promoters from E. coli, the early and late promoters from SV40, the CMV immediate early promoter, the adenovirus early and late promoters, and retrovirus long-terminal repeats (LTR).

[0132] In addition to control regions that promote transcription, expression vectors may also include regions that modulate transcription, such as repressor binding sites and enhancers. Examples include the SV40 enhancer, the cytomegalovirus immediate early enhancer, polyoma enhancer, adenovirus enhancers, and retrovirus LTR enhancers.

[0133] In addition to containing sites for transcription initiation and control, expression vectors can also contain sequences necessary for transcription termination and, in the transcribed region a ribosome-binding site for translation. Other regulatory control elements for expression include initiation and termination codons as well as polyadenylation signals. The person of ordinary skill in the art would be aware of the numerous regulatory sequences that are useful in expression vectors. Such regulatory sequences are described, for example, in Sambrook et al., (Molecular Cloning: A Laboratory Manual. 2nd. ed., Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y., (1989)).

[0134] A variety of expression vectors can be used to express a nucleic acid molecule. Such vectors include chromosomal, episomal, and virus-derived vectors, for example vectors derived from bacterial plasmids, from bacteriophage, from yeast episomes, from yeast chromosomal elements, including yeast artificial chromosomes, from viruses such as baculoviruses, papovaviruses such as SV40, Vaccinia viruses, adenoviruses, poxviruses, pseudorabies viruses, and retroviruses. Vectors may also be derived from combinations of these sources such as those derived from plasmid and bacteriophage genetic elements, e.g., cosmids and phagemids. Appropriate cloning and expression vectors for prokaryotic and eukaryotic hosts are described in Sambrook et al., Molecular Cloning: A Laboratory Manual. 2nd. ed., Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y., (1989).

[0135] The regulatory sequence may provide constitutive expression in one or more host cells (i.e. tissue specific) or may provide for inducible expression in one or more cell types such as by temperature, nutrient additive, or exogenous factor such as a hormone or other ligand. A variety of vectors providing for constitutive and inducible expression in prokaryotic and eukaryotic hosts are known to those of ordinary skill in the art.

[0136] The nucleic acid molecules can be inserted into the vector nucleic acid by well-known methodology. Generally, the DNA sequence that will ultimately be expressed is joined to an expression vector by cleaving the DNA sequence and the expression vector with one or more restriction enzymes and then ligating the fragments together. Procedures for restriction enzyme digestion and ligation are known to those of ordinary skill in the art.

[0137] The vector containing the appropriate nucleic acid molecule can be introduced into an appropriate host cell for propagation or expression using well-known techniques. Bacterial cells include, but are not limited to, E. coli, Streptomyces, and Salmonella typhimurium. Eukaryotic cells include, but are not limited to, yeast, insect cells such as Drosophila, animal cells such as COS and CHO cells, and plant cells.

[0138] It may be desirable to express a peptide of the present invention as a fusion protein. Accordingly, the invention provides fusion vectors that allow for the production of such peptides. Fusion vectors can increase the expression of a recombinant protein, increase the solubility of the recombinant protein, and aid in the purification of the protein by acting for example as a ligand for affinity purification. A proteolytic cleavage site may be introduced at the junction of the fusion moiety so that the desired peptide can ultimately be separated from the fusion moiety. Proteolytic enzymes include, but are not limited to, factor Xa, thrombin, and enterokinase. Typical fusion expression vectors include pGEX (Smith et al., (1988) Gene 67:31-40), pMAL (New England Biolabs, Beverly, Mass.) and pRIT5 (Pharmacia, Piscataway, N.J.) which fuse glutathione S-transferase (GST), maltose E binding protein, or protein A, respectively, to the target recombinant protein. Examples of suitable inducible non-fusion E. coli expression vectors include pTrc (Amann et al., (1988) Gene 69:301-315) and pET 11d (Studier et al., (1990) Gene Expression Technology: Methods in Enzymology 185:60-89).

[0139] Recombinant protein expression can be maximized in a host bacteria by providing a genetic background wherein the host cell has an impaired capacity to proteolytically cleave the recombinant protein. (Gottesman, S., Gene Expression Technology: Methods in Enzymology 185, Academic Press, San Diego, Calif. (1990) 119-128). Alternatively, the sequence of the nucleic acid molecule of interest can be altered to provide preferential codon usage for a specific host cell, for example E. coli. (Wada et al., (1992) Nucleic Acids Res. 20:2111-2118).

[0140] The nucleic acid molecules can also be expressed by expression vectors that are operative in yeast. Examples of vectors for expression in yeast e.g., S. cerevisiae include pYepSec1 (Baldari, et al., (1987) EMBO J. 6:229-234), pMFa (Kurjan et al., (1982) Cell 30:933-943), pJRY88 (Schultz et al., (1987) Gene 54:113-123), and pYES2 (Invitrogen Corporation, San Diego, Calif.).

[0141] The nucleic acid molecules can also be expressed in insect cells using, for example, baculovirus expression vectors. Baculovirus vectors available for expression of proteins in cultured insect cells (e.g., Sf 9 cells) include the pAc series (Smith et al., (1983) Mol. Cell Biol. 3:2156-2165) and the pVL series (Lucklow et al., (1989) Virology 170:31-39).

[0142] In certain embodiments of the invention, the nucleic acid molecules described herein are expressed in mammalian cells using mammalian expression vectors. Examples of mammalian expression vectors include pCDM8 (Seed, B. (1987) Nature 329:840) and pMT2PC (Kaufman et al., (1987) EMBO J. 6:187-195).

[0143] The expression vectors listed herein are provided by way of example only of the well-known vectors available to those of ordinary skill in the art that would be useful to express the nucleic acid molecules. Preferred vectors include the pET28a (Novagen, Madison, Wis.), pAcSG2 (Pharmingen, San Diego, Calif.), and pFastBac (Life Technologies, Gaithersburg, Md.). The person of ordinary skill in the art would be aware of other vectors suitable for maintenance propagation or expression of the nucleic acid molecules described herein. These are found for example in Sambrook, J., Fritsh, E. F., and Maniatis, T. Molecular Cloning: A Laboratory Manual 2nd, ed., Cold Spring Harbor Laboratory, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y., 1989.

[0144] The invention also encompasses vectors in which the nucleic acid sequences described herein are cloned into the vector in reverse orientation, but operably linked to a regulatory sequence that permits transcription of antisense RNA. Thus, an antisense transcript can be produced to all, or to a portion, of the nucleic acid molecule sequences described herein, including both coding and non-coding regions. Expression of this antisense RNA is subject to each of the parameters described above in relation to expression of the sense RNA (regulatory sequences, constitutive or inducible expression, tissue-specific expression).

[0145] The invention also relates to recombinant host cells containing the vectors described herein. Host cells therefore include prokaryotic cells, lower eukaryotic cells such as yeast, other eukaryotic cells such as insect cells, and higher eukaryotic cells such as mammalian cells. Preferred host cells of the instant invention include E. coli and Sf9.

[0146] The recombinant host cells are prepared by introducing the vector constructs described herein into the cells by techniques readily available to the person of ordinary skill in the art. These include, but are not limited to, calcium phosphate transfection, DEAE-dextran-mediated transfection, cationic lipid-mediated transfection, electroporation, transduction, infection, lipofection, and other techniques, such as those found in Sambrook et al. (Molecular Cloning: A Laboratory Manual. 2nd, ed., Cold Spring Harbor Laboratory, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y., 1989).

[0147] Host cells can contain more than one vector. Thus, different nucleotide sequences can be introduced on different vectors of the same cell. Similarly, the nucleic acid molecules can be introduced either alone or with other nucleic acid molecules that are not related to the nucleic acid molecules such as those providing trans-acting factors for expression vectors. When more than one vector is introduced into a cell, the vectors can be introduced independently, co-introduced or joined to the nucleic acid molecule vector.

[0148] In the case of bacteriophage and viral vectors, these can be introduced into cells as packaged or encapsulated virus by standard procedures for infection and transduction. Viral vectors can be replication-competent or replication-defective. In the case in which viral replication is defective, replication will occur in host cells providing functions that complement the defects.

[0149] Vectors generally include selectable markers that enable the selection of the subpopulation of cells that contain the recombinant vector constructs. The marker can be contained in the same vector that contains the nucleic acid molecules described herein or may be on a separate vector. Markers include tetracycline or ampicillin-resistance genes for prokaryotic host cells and dihydrofolate reductase or neomycin resistance for eukaryotic host cells. However, any marker that provides selection for a phenotypic trait will be effective.

[0150] While the active proteins can be produced in bacteria, yeast, mammalian cells, and other cells under the control of the appropriate regulatory sequences, cell- free transcription and translation systems can also be used to produce these proteins using RNA derived from the DNA constructs described herein.

[0151] Where secretion of the peptide is desired, appropriate secretion signals are incorporated into the vector. The signal sequence can be endogenous to the peptides or heterologous to these peptides.

[0152] It is also understood that depending upon the host cell in recombinant production of the peptides described herein, the peptides can have various glycosylation patterns, depending upon the cell, or maybe non-glycosylated as when produced in bacteria. In addition, the peptides may include an initial modified methionine in some cases as a result of a host-mediated process.

[0153] The recombinant host cells expressing the peptides described herein have a variety of uses. First, the cells are useful for producing a peptide or protein that can be further purified to produce desired amounts of protein or fragments. Thus, host cells containing expression vectors are useful for peptide production.

[0154] Host cells are also useful for conducting cell-based assays involving the ERAB or HADH2 protein/peptide, or its fragments. Thus, a recombinant host cell expressing a native protein is useful for assaying compounds that stimulate or inhibit protein function.

[0155] Host cells are also useful for identifying ERAB or HAHD2 protein mutants in which these functions are affected. If the mutants naturally occur and give rise to a pathology, host cells containing the mutations are useful to assay compounds that have a desired effect on the mutant protein (for example, stimulating or inhibiting function) which may not be indicated by their effect on the native protein.

EXAMPLES

[0156] A. Synthesis of an ERAB or HADH2 Inhibitor (Compound I)

[0157] The structure of Compound I as a single enantiomer is shown in FIG. 4A. Compound I was synthesized using two reaction schemes. The abbreviations employed in the Schemes have the following meaning unless otherwise indicated: Me: methyl; Et: ethyl; Ac: acetyl; Boc: butyloxycarbonyl; EtoAc: ethyl acetate; TFA: trifluoroacetic acid; DCC: dicyclohexylcarbodimide; rt: room temperature; HATU: [O-(7-azabenzotriazol-1-yl)-1,1,3,3-tetra-triethyl-uronium hexafluorophsphate; DMAP: N,N-dimethyl-4-aminopyridine; and DMF: dimethylformamide.

[0158] 1. Preparation of 1-azepan-1-yl-2-phenyl-2-(4-thioxo-1,4-dihydro-pyrazolo[3,4-d]pyrimidin-5-yl)-ethanone (Compound I) According to Scheme 1.

[0159] 1-a. General Description of Scheme 1.

[0160] 2-Chloro-2-phenyl-acetyl chloride (1) and hexamethyleneimine (2) are reacted in dichloromethane in the presence of triethylamine to afford the intermediate (3). This intermediate (3) is then carried forward and reacted with commercially available 4-mercapto-1H-pyrazolo[3,4-d] pyrimidine (4) to afford a mixture of products Compound I and 14. The two products are separated via column chromatography to yield 1-azepan-1-yl-2-phenyl-2-(4-thioxo-1,4-dihydro-pyrazolo[3,4-d]pyrimidin-5-yl)-ethanone (Compound I) as the minor and 14 major products respectively. The desired Compound I is further purified via preparatory HPLC to yield the product in>95% purity. Compound I, made according to Scheme 1, when tested against ERAB as described below, exhibited an IC50=88 nM.

[0161] 1-b. Experimental Section to Scheme 1.

[0162] 2-Chloro-2-phenyl-acetyl chloride (1) (2.50 ml, 15.75 mmol) was dissolved in CH2Cl2 (50 ml), the mixture was cooled to 0° C., hexamethyleneimine (2) (1.76 ml, 15.75 mmol) was added dropwise, followed by triethylamine (2.19 ml, 15.75 mmol). The resulting mixture containing intermediate (3) was stirred at 0° C. for 15 min followed by warming to room temperature and stirring an additional 60 min. The mixture (3) was then concentrated on a rotary evaporator, the residual oil was taken up in dimethylformamide (DMF) (50 ml), triethylamine (2.19 ml, 15.75 mmol) was added, followed by addition of 4-mercapto-1H-pyrazolo[3,4-d]pyrimidine (4) (2.33 g, 15.44 mmol) in one portion as a solid. The reaction product was warmed to 80° C. and stirred for approximately 17 h. The reaction product was cooled to room temperature, diluted with water, and extracted with EtOAc (3×30 ml), and the combined organics were washed with brine, dried over anhyd. Na2SO4, filtered and concentrated to obtain crude products (Compound I and 14). The crude products were purified on silica gel eluting with 30-40-80% ethyl acetate/hexane to yield two products. 3.55 g of the product (14) with the lower Rf was isolated as a white solid. The desired compound (0.266 g) with higher Rf was obtained as a tan solid. This product was further purified by preparatory HPLC (5-95% CH3CN/H2O, 10 min, followed by 95% CH3CN/H2O, 0.1% trifluoroacetic acid (TFA), 10 min)). The desired HPLC fractions were combined, diluted with brine (30 ml), 50% aqueous NaHCO3 solution (30 ml) was added, and the aqueous layer extracted with EtOAc (3×30 ml), combined organics washed with brine, dried over anhyd. Na2SO4, filtered and concentrated to yield (0.178 g, 0.484 mmol)>95% purity of Compound I. mp: 201-202° C.; Rf=0.60 (EtOAc:Hexanes=6:4). 1H-NMR; (DMSO-d6) δ14.18 (s, 1H), 8.27 (s, 1H), 8.17 (s, 1H), 7.95 (s, 1H), 7.52-7.54 (m, 3H), 7.39-7.41 (m, 2H), 3.19-3.74 (m, 4H), 1.34-1.90 (m, 8H). Anal. Calcd for C19H21N5OS.0.2 TFA.0.4 H2O: C, 62.10; H, 5.76; N, 19.06. Found: C, 58.59; H, 5.53; N, 17.84; MALDI HRMS Calcd for C19H21N5OS (M+H)=368.1545, observed (M+H)=368.1535; HPLC: 10% CH3CN/H2O (0.1% TFA)-90% CH3CN/H2O (0.1%TFA): Retention time=13.80 min.

[0163] 2. Preparation of 1-azepan-1-yl-2-phenyl-2-(4-thioxo-1,4-dihydro-pyrazolo[3,4-d]pyrimidin-5-yl)-ethanone (Compound I) according to Scheme 2.

[0164] added dropwise, followed by triethylamine (2.19 ml, 15.75 mmol). The resulting mixture containing intermediate (3) was stirred at 0° C. for 15 min followed by warming to room temperature and stirring an additional 60 min. The mixture (3) was then concentrated on a rotary evaporator, the residual oil was taken up in dimethylformamide (DMF) (50 ml), triethylamine (2.19 ml, 15.75 mmol) was added, followed by addition of 4-mercapto-1H-pyrazolo[3,4-d] pyrimidine (4) (2.33 g, 15.44 mmol) in one portion as a solid. The reaction product was warmed to 80° C. and stirred for approximately 17 h. The reaction product was cooled to room temperature, diluted with water, and extracted with EtOAc (3×30 ml), and the combined organics were washed with brine, dried over anhyd. Na2SO4, filtered and concentrated to obtain crude products (Compound I and 14). The crude products were purified on silica gel eluting with 30-40-80% ethyl acetate/hexane to yield two products. 3.55 g of the product (14) with the lower Rf was isolated as a white solid. The desired compound (0.266 g) with higher Rf was obtained as a tan solid. This product was further purified by preparatory HPLC (5-95% CH3CN/H2O, 10 min, followed by 95% CH3CN/H2O, 0.1% trifluoroacetic acid (TFA), 10 min)). The desired HPLC fractions were combined, diluted with brine (30 ml), 50% aqueous NaHCO3 solution (30 ml) was added, and the aqueous layer extracted with EtOAc (3×30 ml), combined organics washed with brine, dried over anhyd. Na2SO4, filtered and concentrated to yield (0.178 g, 0.484 mmol)>95% purity of Compound I. mp: 201-202° C.; Rf=0.60 (EtOAc:Hexanes=6:4). 1H-NMR; (DMSO-d6) δ14.18 (s, 1H), 8.27 (s, 1H), 8.17 (s, 1H), 7.95 (s, 1H), 7.52-7.54 (m, 3H), 7.39-7.41 (m, 2H), 3.19-3.74 (m, 4H), 1.34-1.90 (m, 8H). Anal. Calcd for C19H21N5OS.0.2 TFA.0.4 H2O: C, 62.10; H, 5.76; N, 19.06. Found: C, 58.59; H, 5.53; N, 17.84; MALDI HRMS Calcd for C19H21N5OS (M+H)=368.1545, observed (M+H)=368.1535; HPLC: 10% CH3CN/H2O (0.1%TFA)-90% CH3CN/H2O (0.1% TFA): Retention time=13.80 min.

[0165] 2. Preparation of 1-azepan-1-yl-2-phenyl-2-(4-thioxo-1,4-dihydro-pyrazolo[3,4-d]pyrimidin-5-yl)-ethanone (Compound I) according to Scheme 2.

[0166] 2-a. General Description of Scheme 2.

[0167] Boc-L-α-phenylglycine (5) and cyclohexanol are reacted in dichloromethane in the presence of dicyclohexylcarbodiimide (DCC) and catalytic amount of N,N-dimethyl-4-aminopyridine (DMAP) to give 6 (R=Boc) in almost quantitative yield. Treatment of 6 with trifluoroacetic acid (TFA) yields 7 (R=H) in 98% yield. 7 is then coupled to alpha-cyanoacetic acid (8) using O-(7-azabenzotriazol-1-yl)-1,1,3,3-tetra-triethyl-uronium hexafluorophosphate (HATU) as the coupling agent to afford (2-cyano-acetylamino)-phenyl-acetic acid cyclohexyl ester (9). The reaction of 9 with triethyl orthoformate in acetic anhydride and catalytic anhydrous ZnCl2 gives an intermediate which upon reaction with hydrazine in 1,4-dioxane at 105° C. affords 10 in 51% yield. The [(5-amino-1H-pyrazol-4-carbonyl)-amino]-phenyl-acetic acid cyclohexyl ester (10) is then treated with formamide at 180-100° C. to give the desired cyclized product (11). Compound 11 is treated with Lawesson's reagent under inert gas atmosphere to afford compound 12. Hydrolysis of compound 12 affords the carboxylic acid 13, which is then coupled to hexamethyeneimine using the coupling reagent HATU to afford Compound I.

[0168] 2-b. Experimental Section to Scheme 2.

[0169] Step 1: tert-Butoxycarbonylamino-phenyl-acetic Acid Cyclohexyl Ester (6).

[0170] To an ice-cold suspension of Boc-L-α-phenylglycine (5) (14.14 g, 40.35 mmol) and DMAP (0.5 g, 4.04 mmol) and cyclohexanol (5.12 ml, 48.42 mmol) in 60 ml of CH2Cl2 was slowly added DCC (9.16 g, 44.4 mmol). The resulting mixture was stirred at 0° C. to room temperature and monitored by TLC. Upon completion the reaction was filtered and the precipitate was washed with CH2Cl2 to remove most of the N,N′-dicyclohexylurea. The filtrate was then partitioned between CH2Cl2 and satd. NaHCO3 and the layers separated. The aqueous phase was extracted with CH2Cl2 (2×200 ml), and the combined organics were washed with H2O (150 ml), brine (150 ml) and dried over anhyd. Na2SO4, filtered, and concentrated under reduced pressure. The resulting yellowish oil was chromatographed on silica gel using Hexane:EtOAc=2:1 as the elutant to yield compound 6 (13.37 g, 39.95 mmol, 99% yield) as a viscous yellow oil. TLC; Rf=0.7 (EtOAc:Hexanes=6:4). 1H-NMR; (CDCl3) δ1.27-1.83 (m, 10H), 1.47 (s, 9H) 4.78-4.83 (m, 1H), 5.31-5.33 (d, 1H, J=8 Hz), 5.61-5.63 (br, s, 1H, NH), 7.32-7.41 (m, 5H). MS Calcd for C19H27NO4 (M+H)=334, observed (M+H)=334; HPLC: 30% CH3CN/H2O (0.1% TFA) to 90% CH3CN/H2O (0.1% TFA)/20 min: Retention time=14.61 min.

[0171] Step 2: Amino-phenyl-acetic Acid Cyclohexyl Ester (7).

[0172] To a solution of 6 (13.27 g, 39.79 mmol) in 50 ml of CH2Cl2 at 0° C. was added TFA (30 ml, 385.1 mmol) dropwise. The resulting yellowish mixture was stirred at 0° C. to room temperature overnight. The reaction was then concentrated under reduced pressure and the resulting yellow oil was partitioned between CH2Cl2 (300 ml) and satd. NaHCO3 (150 ml) and the layers separated. The aqueous phase was extracted with CH2Cl2 (2×150 ml) and the combined organics were washed with H2O (150 ml), brine (150 ml) and dried over anhyd. Na2SO4, filtered and concentrated under reduced pressure to yield compound 7 (9.05 g, 38.99 mmol, 98% yield) as a yellow oil. TLC; Rf=0.7 (CH2Cl2:MeOH=9:1).1H-NMR (CDCl3) δ1.25-2.03 (m, 10H), 4.62 (s, 1H), 4.81-4.85 (m, 1H), 7.30-7.43 (m, 5H). MS Calcd for C14H19NO2 (M+H)=334, observed (M+H)=334; HPLC: 5% CH3CN/H2O (0.1% TFA) to 90% CH3CN/H2O (0.1% TFA)/20min. Retention time=7.52 min.

[0173] Step 3: (2-Cyano-acetylamino)-phenyl-acetic Acid Cyclohexyl Ester (9).

[0174] To a solution of 7 (9.01 g, 38.63 mmol), α-cyanoacetic acid (8) (3.58 g, 42.05 mmol) and triethylamine (12 ml, 84.1 mmol) in 60 ml of DMF at 0° C. was added HATU (24 g, 63.1 mmol). The yellow solution was stirred at 0° C. to room temperature overnight. The reaction was then partitioned between EtOAc (300 ml) and H2O (150 ml) and the layers separated. The organic phase was washed with satd. NaHCO3 (150 ml), H2O (150 ml), 0.5 N HCl (150 ml), brine (150 ml), and dried over anhyd. Na2SO4, filtered and concentrated under reduced pressure. The resulting yellow oil was chromatographed on silica gel using hexane:EtOAc=1:1 as the elutant to yield compound 9 (6.57 g, 21.88 mmol, 57% yield) as a white solid. mp: 114-116° C.; TLC; Rf=0.8 (EtOAc:Hexanes=1:1). 1H-NMR; (CDCl3) δ1.28-1.85 (m, 10H), 3.45 (s, 2H), 4.87-5.00 (m, 1H), 5.54-5.56 (d, 1H, J=7 Hz), 7.10-7.29 (br, s, 1H, NH), 7.29-7.39 (s, 5H). MS Calcd for C17H20N2O3 (M+Na)=323, observed (M+Na)=323, observed (M+Na)=323; HPLC:30% CH3CN/H2O (0.1% TFA) to 90% CH3CN/H2O (0.1% TFA)/20min. Retention time=9.67 min.

[0175] Step 4: (5Amino-1H-pyrazol-4-carbonyl)-aminol-phenyl-acetic Acid Cyclohexyl Ester (10)

[0176] A round-bottom flask was charged with compound 9 (2.3 g, 7.67 mmol), triethyl orthoformate (9.0 ml, 53.7 mmol), acetic anhydride (4.5 ml, 46.02 mmol), and anhyd. ZnCl2 (1.05 g, 7.67 mmol), and then heated to reflux at 130° C. for 4 h, most preferably 105° C. for 4 h. The yellow reaction mixture was concentrated under vacuum and azeotroped with toluene (3×15 ml). The resulting was titrated with CH2Cl2 (100 ml) filtered and washed with CH2Cl2 (150 ml). The filtrate was then concentrated under vacuum to yield crude residue as yellow grease. The crude residue was treated with hydrazine hydrate (0.56 ml, 11.51 mmol) in 10 ml of 1,4-dioxane and then refluxed at 105° C. overnight. The reaction was cooled to room temperature and concentrated under vacuum. The residue was partitioned between EtOAc (250 ml) and satd. NaHCO3, brine (2×100 ml), dried over anhyd. Na2SO4, filtered and concentrated under vacuum to afford the crude product as a yellow grease. The crude product was chromatographed using silica gel and eluted with CH2Cl2:MeOH=9:1 to afford compound 10 (1.343 g, 3.92 mmol, 51% yield) as a white solid. mp: 92-94° C.; TLC; Rf=0.4 (CH2Cl2:MeOH=9:1). 1H-NMR; (CDCl3/CD3OD) δ1.14-1.37 (m, 4H), 1.38-1.41 (m, 2H), 1.52-1.54 (m, 2H); 1.67-1.71 (m, 2H), 4.68-4.72 (m,1H), 5.53 (s, 1H), 7.29-7.30 (m, 5H), 7.79 (s, 1H). MS Calcd for C18H22N4O3 (M+H)=343, observed (M+H)=343; 5% CH3CN/H2O (0.1% TFA) to 90% CH3CN/H2O (0.1% TFA)/20min. Retention time=9.24 min.

[0177] Step 5: (4-Oxo-1,4-dihydro-pyrazolo[3,4-d]pyrimidin-5-yl)-phenyl-acetic Acid Cyclohexyl Ester (11).

[0178] Compound 10 (1.244 g, 3.63 mmol) in 8 ml of formamide was heated to 180° C. for 4 h and then at 100° C. overnight, most preferably 145° overnight. The cooled reaction was filtered and the white precipitate product (11) was washed with and dried in a vacuum oven over P2O5. Additionally, the filtrate was concentrated under reduced pressure and the residue was partitioned between EtOAc (250 ml) and satd. NaHCO3 (2×100 ml), wash with brine (100 ml), dried over anhyd. Na2SO4, filtered and concentrated under vacuum to afford the crude product as a yellow grease, which was then chromatographed using silica gel and eluted with CH2Cl2:EtOAc (1:1) to afford an additional 0.341 g, 0.97 mmol, and 27% of compound 11 as a white solid. mp: 176-180° C.; TLC; Rf=0.5 (CH2Cl2:EtOAc=1:1). 1H-NMR; (CDCl3) δ1.24-1.91 (m, 10H), 4.98-5.03 (m, 1H), 6.84 (s, 1H), 7.29-7.30 (m, 2H), 7.36-7.49 (m, 3H), 7.91 (s, 1H), 8.23 (s, 1H). MS Calcd for C19H20N4O3 (M+H)=353, observed (M+H)=353; HPLC:5% CH3CN/H2O (0.1% TFA) to 90% CH3CN/H2O (0.1% TFA)/20min. Retention time=12.9 min.

[0179] Step 6: 2-Phenyl-(4-thioxo-1,4-dihydro-pyrazolo[3,4-d]pyrimidin-5-yl)-acetic Acid Cyclohexyl Ester (12).

[0180] A solution of compound 11 (0.326 g, 0.93 mmol) in 5 ml of xylene was purged with argon for 20 minutes, to which was then added Lawesson's reagent (0.375 g, 0.93 mmol) and the resulting mixture heated at 145° C. for 2 h under argon. The yellow reaction mixture was concentrated under vacuum and partitioned between EtOAc (100 ml) and satd. NaHCO3, washed with brine (2×50 ml), dried over anhyd. Na2SO4, filtered and concentrated under vacuum. The crude product was chromatographed using silica gel and eluted with CH2Cl2:EtOAc (1:1) to afford 0.316 g, 0.86 mmol, 92% yield of product 12 as a off white solid. mp: 170-173° C.; TLC: Rf=0.8 (CH2Cl2:EtOAc=1:1). 1H-NMR (CDCl3) δ1.30-1.93 (m, 10H), 5.03 (m, 1H), 7.41-7.49 (m, 5H), 7.98 (s, 1H), 8.04 (s, 1H), 8.38 (s, 1H), 10.55 (br, s, 1H, NH). MS Calcd for C19H20N4O2S (M+H)=368, observed (M+H)=369; HPLC:5% CH3CN/H2O (0.1% TFA) to 90% CH3CN/H2O (0.1% TFA)/20min. Retention time=14.6 min.

[0181] Step 7: 2-Phenyl-(4-thioxo-1,4-dihydro-pyrazolo[3,4-d]pyrimidin-5-yl)acetic Acid (13).

[0182] To a solution of 2-phenyl-(4-thioxo-1,4-dihydro-pyrazolo[3,4-d]pyrimidin-5-yl)acetic acid cyclohexyl ester (12), 0.467 g, 1.27 mmol, in 10 ml of methanol was added to 2N KOH aqueous solution (1.3 ml, 2.53 mmol) at 0° C. The resulting mixture of yellow solution was stirred at 0° C. to room temperature overnight. The reaction mixture was concentrated by vacuum to remove most of methanol and water was added. The pH was adjusted to 4.0 with aqueous 10% citric acid solution. The product was extracted with EtOAc (2×75 ml). The combined organic layer was washed with water, brine and dried over anhyd. Na2SO4, then concentrated by vacuum to afford compound 13 (0.354 g, 1.19 mmol, 97% yield) as an off-white solid. mp: 95-98° C.; TLC; Rf=0.1 (CH2Cl2:MeOH=9:1). 1H-NMR; (CD3OD) δ3.23 (s, 1H), 7.50 (s, 5H), 8.08 (s, 1H), 8.09 (s, 1H), 8.34 (s, 1H, NH). MS Calcd for C13H10N4O2S (M+H)=287, observed (M+H)=287; HPLC:5% CH3CN/H2O (0.1% TFA) to 90% CH3CN/H2O (0.1% TFA) to 90% CH3CN/H2O (0.1% TFA)/20min. Retention time=3.9 min.

[0183] Step 8: 1-Azepan-1-yl-2-phenyl-2-(4-thioxo-1,4-dihydro-1,4-dihrdropyrazolo [3,4-d]pyrimidin-5-yl)-ethanone (Compound I).

[0184] To a solution of 2-phenyl-(4-thioxo-1,4-dihydro-pyrazolo[3,4-d]pyrimidin-5-yl)acetic Acid (13), 0.064 g, 0.22 mmol, and hexamethyleneimine (0.023 g, 0.23 mmol) with 4-methylmorpholine (50 μl, 0.44 mol) in 3 ml of DMF at 0° C. was added HATU [O-(7-azabenzotriazol-1-yl)-1,1,3,3-tetra-triethyl-uronium hexafluorophosphate] (0.125 g, 0.33 mol). The resulting mixture of yellow solution was stirred at 0° C. to room temperature for overnight. The yellow reaction mixture was partitioned between EtOAc (100 ml) and brine, satd. NaHCO3, brine (3×50 ml). The organic layer dried over anhyd. Na2SO4, filtered and concentrated under vacuum. The crude product was chomatographed using silica gel and eluted with CH2Cl2:EtOAc (1:1) to afford Compound I (0.043 g, 0.12 mmol, 53% yield) as a yellowish solid. The Compound I obtained via the above procedure appears to be a different crystalline form from that obtained via Scheme 1. This may account for the different melting points. Co-injection of Compound I obtained via step 8, Scheme 2 and that from Scheme 1 gave a single peak via HPLC. mp:>230° C. TLC; Rf=0.7 (CH2Cl2:EtOAc=1:1). 1H-NMR; (CDCl3) δ1.60-2.08 (m, 8H), 3.37-3.84 (m, 4H), 7.44-7.49 (m, 5H), 8.09 (s, 1H), 8.36 (s, 1H), 8.41 (s, 1H), 10.65 (s, br, 1H, NH). MS Calcd for C19H21N5OS (M+H)=368, observed (M+H)=368; HPLC:5% CH3CN/H2O (0.1% TFA) to 90% CH3CN/H2O (0.1% TFA)/20min. Retention time=11.66 min.

[0185] B. Cloning, Overexpression, and Purification of Wild Type and Mutant Peptides of ERAB or HADH2.

[0186] The coding sequence for full length wild-type ERAB or HADH2 [SEQ ID NO: 7, Yan et al., (1997), supra; He et al., (1998), supra] was amplified by PCR [Mullis et al., Cold Spring Harbor Symposium Quantum Biology, Vol. 51, pp. 263 -273 (1986); Saiki et al., Science, Vol. 239, pp. 487-491 (1988)] from a Marathon-Ready human lung cDNA library and the Advantage™ cDNA PCR kit, both from Clontech (Palo Alto, Calif.), using the manufacturer's instructions. The forward primer was 5′-GGGCACACCATGGCAGCAGCGTGTCGGAGCGTGAAGG-3′ (SEQ ID NO: 9) and the reverse primer was 5 ′-AGCTTTCGGCCGTTAAGGCTGCATACGAATAGCCCCATCC-3′ (SEQ ID NO: 10).

[0187] The amplified DNA was digested with the restriction enzymes NcoI and Eagl, ligated into the E. coli plasmid pMGH4 [Kan et al., Journal of Protein Chemistry, Vol. 11, pp. 467-473 (1992); Schoner et al., Proceedings of National Academy of Science, USA, Vol. 83, pp. 8506-8510 (1986)], sequence verified, and compared to the sequences in GENBANK Accession numbers AF035555 and U96132.

[0188] Mutations were introduced by oligonucleotide site-directed mutagenesis [Kunkel, Proceedings of National Academy of Science, USA, Vol. 82, pp. 488-492 (1985)] using the Muta-Gene in vitro Mutagenesis Kit (obtained from Bio-rad, Hercules, Calif.). The ssDNA uracil template (minus strand) was created in E. coli strain CJ236 supplied in the kit using the pMGH4-ERAB or HADH2 construct. All DNA modification and restriction enzymes were purchased from New England Biolabs and oligonucleotides were purchased from Genosys Biotechnology.

[0189] The following oligonucleotides were used for mutagenesis:

1C5V5′-CCATGGCAGCAGCTGTTCGGAGCGTGAAGG-3′(SEQ ID NO:11)C58V5′-GAAGTTAGGAAACAACGTTGTTTTCGCCCCAGCC-3′(SEQ ID NO:12)C214R5′-CCAGAGAAAGTGCGTAACTTCTTAGCCAGCCAAG-3′(SEQ ID NO:13)C124A5′-CCAGAGAAAGTAGCAAACTTCCTCGCCAGCCAAG-3′(SEQ ID NO:21)C214S5′-CCAGAGAAAGTGTCTAACTTCTTAGCCAGCCAAG-3′(SEQ ID NO:24)

[0190] All mutants were sequence-verified through the region of the mutations and tested for expression in a spontaneous mutant of E. coli strain B121 (DE3) (obtained from Novagen, Madison, Wis.) [See Miroux et al., Journal of Molecular Biology, Vol. 260, pp. 289-298 (1996)].

[0191] Wild-type and mutant proteins were purified in the same manner. The final purification protocol was modified from published reports [Furuta et al., Biochemistry Biophysics Acta, Vol. 1350, pp. 317-324 (1997)]. All procedures were carried out at 4° C. Cell paste was resuspended in half volume 50 mM Tris-HCl pH 7.5, 1 mM EDTA, 10 mM β-mercaptoethanol (BME). The cells were disrupted by micro-fluidization. Cleared supernatant was passed through a Q-Sepharose Fast Flow column. Unbound enzyme was collected in the flow through. This was loaded directly onto a Blue Sepharose Fast Flow column equilibrated in 20 mM Tris-HCl pH 7.5, 10 mM BME, 0.01% NaN3. ERAB or HADH2 was eluted with a salt gradient increasing to 1 M NaCl over 10 column volumes. Peak fractions were concentrated for size exclusion. The pool was fractionated on a 500 ml Superdex 200 column equilibrated in 20 mM Tris-HCl pH 7.5, 200 mM NaCl, 5-10 mM BME, 0.01% NaN3. The peak eluted as a tetramer. The peak fractions were concentrated to 20-25 mg/ml and stored in aliquots at −20° C. All chromatography media were from Pharmacia Biotech.

[0192] C. Isothermal Titration Calorimetry

[0193] Titrations described herein were performed with an MCS microcalorimeter (obtained from MicroCal, Inc., Northampton, Miss.).

[0194] For the inhibitor binding experiments, the titrations were performed in 25 mM MOPS (pH 7.5), 125 mM NaCl, 10% glycerol, 2.0% DMSO, 0.5 mM TCEP (Tri(2-carboxyethyl)phosphine), 0.1 mM EDTA at 15° C. The syringe contained 415 μM wild-type ERAB or HADH2 and the cell contained either 20 μM inhibitor, 20 μM cofactor, or 20 μM each of inhibitor and cofactor. After a preliminary 20 μL injection, 12 injections of 10.0 μL each were made at 4 minute intervals. Dilution control titrations of buffer into buffer, protein into buffer, and buffer into inhibitor, cofactor and inhibitor/cofactor mixture were also performed. For the cofactor binding experiments, the titrations were performed in 50 mM MOPS (3-(N-morpholino) propanesulfonic acid, pH 7.5), 250 mM NaCl, 10% glycerol, 2.0% DMSO, 10 mM TCEP at 15° C.

[0195] For the NADH titration, the syringe contained 700 μM cofactor and the cell contained 35 μM wild type ERAB or HADH2. For the NAD+ titration, the syringe contained 2.68 mM cofactor and the cell contained 127 μM wild-type ERAB or HADH2.

[0196] The IC50 value for Compound I was determined spectrophotometrically by monitoring the reduction of NADH to NAD+ with acetoacetyl-CoA as substrate. Enzyme (2.5 nM) was preincubated with inhibitor for 400 seconds at 30° C. in the presence of 36 uM NADH, 25 mM MOPS, pH 7.5, 250 mM NaCl, 2% (v/v) DMSO, and 2.5 mM TCEP. The reaction was initiated by addition of substrate (38 μM). Reduction of NADH was monitored at 340 λ. The IC50 value was determined by non-linear regression analysis using KaleidaGraph (obtained from Synergy Software, Reading, Pa.).

[0197] Compound I made according to Scheme 2 was found to have an average IC50 of 92±5 nM against ERAB or HADH2 (for a racemic mixture of the compound). The experimental data and co-crystal structure of the compound indicates that Compound I inhibits the ERAB or HADH2 via an interaction with NAD+, which is the natural co-factor for ERAB or HADH2. This interaction with NAD+ enables Compound I to bind ERAB or HADH2, approximately 1000-fold more potently than in the absence of NAD+. Further, the tertiary structure analysis of the crystallized ERAB or HADH2:inhibitor complex shows that the inhibitor binds in the active site cavity of the enzyme and reacts with the NAD+ cofactor to form a covalent adduct (FIG. 4C). The conformation and binding interactions of the inhibitor appear identical in the three ERAB or HADH2 monomers to which it binds in the crystal.

[0198] Referring to FIGS. 4A and 4C, the N2 nitrogen of the inhibitor is covalently linked to the reactive C4 carbon on the nicotinamide ring of the NAD+. Adduct formation does not alter the conformation of the bound NAD+ cofactor beyond movement of the C4 atom out of the plane of the nicotinamide ring. Consistent with the observed covalent binding, experiments using isothermal titration calorimetry demonstrate that the inhibitor binds weakly to ERAB or HADH2 in the absence of cofactor or in the presence of NADH (FIG. 5). No binding was detected when ERAB or HADH2 was titrated into either inhibitor or NAD+ alone. A reaction was detected, however, when ERAB or HADH2 was titrated into an equimolar mixture of inhibitor and NAD+. The data display the characteristics of a tight-binding curve involving one mole of ERAB or HADH2 per mole of inhibitor/NAD+ mixture. The results obtained when ERAB or HADH2 was titrated into an equimolar mixture of inhibitor and NADH, on the other hand, are comparable to the results obtained when the protein was titrated into NADH alone. Similar results were observed using the C214R mutant of ERAB or HADH2. This observed reaction cannot simply be attributed to NAD+ binding to ERAB or HADH2, as the Kd for NAD+ was independently determined to be on the order of 500 uM. Therefore, a high cooperative binding of NAD+ and inhibitor must account for the observed reaction. No significant cooperativity was observed for NADH binding in the presence of inhibitor. The formation of a covalent adduct apparently occurs because the inhibitor closely mimics the reaction stereochemistry of the substrate. A proposed mechanism for the reaction of Compound I with NAD+ is shown in FIG. 4C.

[0199] Despite a lack of structural similarity between Compound I and either of the ERAB or HADH2 substrates (wild-type or mutant ), the inhibitor is in intimate contact with the protein within the substrate-binding cleft. A schematic representation of the protein-ligand interactions is shown in FIG. 4D. The inhibitor contacts nine protein residues, primarily through hydrophobic interactions. Two hydrogen bonds are formed between Compound I and ERAB or HADH2, one between the OH of Tyr 168 and N1 of Compound I and the other between Nε of Gln 165 and the carbonyl oxygen of Compound I. As mentioned previously, human 17β-hydroxysteroid dehydrogenase is a human protein closely related to ERAB or HADH2 whose structure has been reported (Ghosh et al., Structure, Vol. 3, pp. 503-513 (1995)). Likewise, 15-PGD and CAA20237.1, identified using the BLAST search engine (Altschul et al., Nucleic Acids Research, Vol. 25, pp. 3389-3402 (1997)), are two reported human sequences closely related to ERAB or HADH2 (see FIG. 2). At most three of the nine residues that interact with the inhibitor are found in any of these three related proteins. This uniqueness suggests that a high level of specificity may be attainable for ERAB or HADH2 inhibitors. Consistent with this, Compound I showed no detectable inhibition of two closely related members of the SDR family, E. coli 17β-hydroxysteroid dehydrogenase and Streptomycetes hydrogenans 3α-20β- hydroxysteroid dehydrogenase, at concentrations as high as 100 μM.

[0200] D. Crystallographic Analysis

[0201] The C214R mutant of ERAB or HADH2, made by the mutagenesis process described above, was engineered to avoid cysteine oxidation in the protein, with arginine selected as the replacement amino acid because of its occurrence at this position in other mammalian ERAB or HADH2 sequences (He et al., Journal of Biochemistry Vol. 273, pp. 10741-10746 (1998)). The C214R mutant of ERAB or HADH2 was concentrated to 20 mg/ml for crystallization. Five mM β-NAD and 5 mM Compound I were combined; and the precipitate removed by centrifugation. Initial thin plates were observed in Hampton Crystal Screen condition 40 (20% isopropanol, 20% PEG 4000, pH 5.6). The final conditions for crystal growth were 20% MME PEG 2000, 0.1 M Na citrate pH 6.0, 4% isopropanol. Nuclei were introduced to the drops by streak seeding [Stura et al., Journal of Crystal Growth, Vol. 110, pp. 270-282 (1991)]. Single, thick plates grew over five days. Isopropanol, Tris, EDTA, glycerol and sodium citrate were all purchased from Fisher Scientific (Pittsburgh, Pa.). NaCl, β-mercaptoethanol, acetyl CoA, β-NAD+ and MME PEG 2000 were from Sigma. PEG 400 was from BDH Laboratory Supplies (Poole, England). Crystal Screen and VDX plates were purchased from Hampton Research (Laguna Niguel, Calif.).

[0202] The results from the crystallographic analysis are shown in Table I below. Crystal coordinates are set forth in Table II.

2TABLE IData Collection, Molecular Replacement, and Refinement StatisticsCrystal InformationSpace groupC2Unit cell parametersa = 122.0 Å, b = 80.8 Å,c = 110.0 Å, β = 105.6°Estimated solvent content 50%Data CollectionResolution30.0-2.0 ÅTotal observations221,823Unique reflections (completeness) 69,169 (99.4%)Rsym 0.066Molecular ReplacementProgramEPMRData resolution range15.0-4.0 ÅSolution correlation coefficient/R-factor 0.682/0.361RefinementResolution range25.0-2.0 ÅNumber of reflections 68595Final R-factor (R-free) 0.215 (0.263)Number of non-hydrogen atomsProtein 7224NAD 176Compound I 78Water 282Rms deviations from ideal geometryBond lengths 0.005 ÅBond angles 1.5°Residues within most favored 91.9%regions of Ramachandran plot

[0203]

3

TABLE II

Crystal coordinates of the ERAB or the HADH22:Compound I complex

ATOM
1
CB
SER A
7
51.735
12.841
30.482
1.000
22.48

ATOM
2
C
SER A
7
53.935
12.748
29.330
1.000
44.59

ATOM
3
O
SER A
7
53.965
12.623
28.111
1.000
43.24

ATOM
4
N
SER A
7
52.577
14.801
29.231
1.000
59.99

ATOM
5
CA
SER A
7
52.952
13.663
30.055
1.000
50.69

ATOM
6
N
VAL A
8
54.749
12.075
30.131
1.000
39.56

ATOM
7
CA
VAL A
8
55.600
11.010
29.608
1.000
36.12

ATOM
8
CB
VAL A
8
56.868
10.859
30.460
1.000
38.89

ATOM
9
CG1
VAL A
8
57.743
12.106
30.341
1.000
32.22

ATOM
10
CG2
VAL A
8
56.501
10.596
31.916
1.000
29.19

ATOM
11
C
VAL A
8
54.816
9.703
29.573
1.000
31.85

ATOM
12
O
VAL A
8
55.319
8.694
29.085
1.000
33.39

ATOM
13
N
LYS A
9
53.585
9.748
30.085
1.000
39.60

ATOM
14
CA
LYS A
9
52.728
8.572
30.162
1.000
29.90

ATOM
15
CB
LYS A
9
51.315
8.942
30.592
1.000
28.88

ATOM
16
C
LYS A
9
52.675
7.826
28.833
1.000
31.95

ATOM
17
O
LYS A
9
52.345
8.403
27.798
1.000
32.99

ATOM
18
N
GLY A
10
53.024
6.543
28.880
1.000
33.00

ATOM
19
CA
GLY A
10
53.013
5.713
27.696
1.000
32.38

ATOM
20
C
GLY A
10
54.267
5.765
26.855
1.000
33.35

ATOM
21
O
GLY A
10
54.439
4.954
25.937
1.000
38.54

ATOM
22
N
LEU A
11
55.173
6.706
27.127
1.000
29.52

ATOM
23
CA
LEU A
11
56.388
6.795
26.319
1.000
36.56

ATOM
24
CB
LEU A
11
57.087
8.136
26.562
1.000
27.30

ATOM
25
CG
LEU A
11
56.273
9.399
26.270
1.000
34.09

ATOM
26
CD1
LEU A
11
57.138
10.635
26.489
1.000
37.47

ATOM
27
CD2
LEU A
11
55.701
9.388
24.860
1.000
30.46

ATOM
28
C
LEU A
11
57.340
5.641
26.619
1.000
25.91

ATOM
29
O
LEU A
11
57.359
5.140
27.744
1.000
25.89

ATOM
30
N
VAL A
12
58.113
5.236
25.611
1.000
24.21

ATOM
31
CA
VAL A
12
59.120
4.198
25.754
1.000
24.85

ATOM
32
CB
VAL A
12
59.025
3.133
26.644
1.000
27.51

ATOM
33
CG1
VAL A
12
60.027
2.022
24.931
1.000
23.67

ATOM
34
CG2
VAL A
12
57.620
2.569
24.502
1.000
27.54

ATOM
35
C
VAL A
12
60.533
4.781
25.713
1.000
29.72

ATOM
36
O
VAL A
12
60.961
5.327
24.691
1.000
28.03

ATOM
37
N
ALA A
13
61.284
4.665
26.808
1.000
27.51

ATOM
38
CA
ALA A
13
62.633
5.221
26.840
1.000
25.01

ATOM
39
CB
ALA A
13
62.764
6.230
27.972
1.000
23.55

ATOM
40
C
ALA A
13
63.709
4.156
26.996
1.000
26.59

ATOM
41
O
ALA A
13
53.678
3.310
27.887
1.000
29.37

ATOM
42
N
VAL A
14
64.702
4.209
26.111
1.000
22.79

ATOM
43
CA
VAL A
14
65.894
3.371
26.286
1.000
23.38

ATOM
44
CB
VAL A
14
66.418
2.828
24.955
1.000
24.29

ATOM
45
CG1
VAL A
14
67.737
2.093
25.113
1.000
22.79

ATOM
46
CG2
VAL A
14
65.376
1.889
24.355
1.000
24.04

ATOM
47
C
VAL A
14
66.940
4.213
27.012
1.000
27.20

ATOM
48
O
VAL A
14
67.350
5.258
26.513
1.000
25.93

ATOM
49
N
ILE A
15
67.326
3.763
28.196
1.000
24.90

ATOM
50
CA
ILE A
15
68.260
4.512
29.039
1.000
22.39

ATOM
51
CB
ILE A
15
67.608
4.791
30.408
1.000
25.05

ATOM
52
CG2
ILE A
15
68.514
5.626
31.295
1.000
24.50

ATOM
53
CG1
ILE A
15
66.225
5.437
30.298
1.000
26.19

ATOM
54
CD1
ILE A
15
65.483
5.627
31.601
1.000
29.49

ATOM
55
C
ILE A
15
69.566
3.752
29.192
1.000
23.74

ATOM
56
O
ILE A
15
69.630
2.729
29.877
1.000
22.94

ATOM
57
N
THR A
16
70.629
4.224
28.535
1.000
23.34

ATOM
58
CA
THR A
16
71.921
3.555
28.681
1.000
22.89

ATOM
59
CB
THR A
16
72.884
3.870
27.258
1.000
21.08

ATOM
60
OG1
THR A
16
73.546
5.110
27.809
1.000
22.39

ATOM
61
CG2
THR A
16
72.116
4.034
26.222
1.000
18.21

ATOM
62
C
THR A
16
72.563
3.962
30.006
1.000
18.37

ATOM
63
O
THR A
16
72.328
5.085
30.456
1.000
22.95

ATOM
64
N
GLY A
17
73.338
3.053
30.591
1.000
22.86

ATOM
65
CA
GLY A
17
73.856
3.305
31.939
1.000
22.89

ATOM
66
C
GLY A
17
72.716
3.236
32.947
1.000
26.28

ATOM
67
O
GLY A
17
72.844
3.705
37.080
1.000
24.11

ATOM
68
N
GLY A
17
71.589
2.647
32.543
1.000
24.25

ATOM
69
CA
GLY A
17
70.398
2.613
33.367
1.000
22.22

ATOM
70
C
GLY A
17
70.476
1.749
34.607
1.000
23.39

ATOM
71
O
GLY A
17
69.530
1.757
35.401
1.000
25.11

ATOM
72
N
ALA A
19
71.533
0.981
34.851
1.000
22.33

ATOM
73
CA
ALA A
19
71.533
0.130
36.042
1.000
23.45

ATOM
74
CB
ALA A
19
72.441
−1.094
35.839
1.000
20.63

ATOM
75
C
ALA A
19
72.023
0.898
37.269
1.000
29.15

ATOM
76
O
ALA A
19
71.941
0.421
38.399
1.000
28.79

ATOM
77
N
SER A
20
72.534
2.110
37.069
1.000
25.73

ATOM
78
CA
SER A
20
73.135
2.829
38.192
1.000
24.12

ATOM
79
CB
SER A
20
74.627
2.487
38.237
1.000
25.36

ATOM
80
OG
SER A
20
75.308
3.189
39.253
1.000
28.39

ATOM
81
C
SER A
20
72.923
4.333
38.087
1.000
27.60

ATOM
82
O
SER A
20
72.555
4.843
37.025
1.000
25.39

ATOM
83
N
GLY A
21
73.151
5.015
39.199
1.000
25.28

ATOM
84
CA
GLY A
21
73.234
6.445
39.322
1.000
23.93

ATOM
85
C
GLY A
21
72.214
7.255
38.556
1.000
27.30

ATOM
86
O
GLY A
21
71.002
7.148
38.761
1.000
21.90

ATOM
87
N
LEU A
22
72.670
8.121
37.652
1.000
23.35

ATOM
88
CA
LEU A
22
71.727
9.032
36.990
1.000
22.33

ATOM
89
CB
LEU A
22
72.489
10.123
36.238
1.000
22.48

ATOM
90
CG
LEU A
22
73.530
10.891
37.065
1.000
20.02

ATOM
91
CD1
LEU A
22
74.242
11.934
36.220
1.000
17.51

ATOM
92
CD2
LEU A
22
72.873
11.552
38.269
1.000
19.27

ATOM
93
C
LEU A
22
70.776
8.278
36.072
1.000
21.31

ATOM
94
O
LEU A
22
69.584
8.600
36.033
1.000
25.91

ATOM
95
N
GLY A
23
71.281
7.281
35.346
1.000
23.21

ATOM
96
CA
GLY A
23
70.440
6.507
34.447
1.000
25.79

ATOM
97
C
GLY A
23
69.358
5.770
35.216
1.000
26.66

ATOM
98
O
GLY A
23
68.186
5.751
34.825
1.000
23.79

ATOM
99
N
LEU A
24
69.752
5.161
36.337
1.000
21.40

ATOM
100
CA
LEU A
24
68.777
4.449
37.166
1.000
20.59

ATOM
101
CB
LEU A
24
69.496
3.755
38.319
1.000
21.40

ATOM
102
CG
LEU A
24
68.626
3.074
39.371
1.000
23.90

ATOM
103
CD1
LEU A
24
67.775
1.976
38.757
1.000
22.46

ATOM
104
CD2
LEU A
24
69.525
2.526
40.475
1.000
25.95

ATOM
105
C
LEU A
24
67.690
5.366
37.705
1.000
22.12

ATOM
106
O
LEU A
24
66.516
5.001
37.707
1.000
25.08

ATOM
107
N
ALA A
25
68.066
6.552
37.171
1.000
23.29

ATOM
108
CA
ALA A
25
67.095
7.482
38.735
1.000
21.28

ATOM
109
CB
ALA A
25
67.803
8.645
39.410
1.000
21.52

ATOM
110
C
ALA A
25
66.146
7.995
37.657
1.000
25.16

ATOM
111
O
ALA A
25
64.967
8.241
37.885
1.000
26.05

ATOM
112
N
THR A
26
66.688
8.160
36.448
1.000
25.64

ATOM
113
CA
THR A
26
65.845
8.558
35.321
1.000
23.48

ATOM
114
CB
THR A
26
66.719
8.816
34.085
1.000
25.74

ATOM
115
OG1
THR A
26
67.686
9.832
34.416
1.000
22.48

ATOM
116
CG2
THR A
26
65.892
9.364
32.937
1.000
17.61

ATOM
117
C
THR A
26
64.794
7.490
35.055
1.000
21.52

ATOM
118
O
THR A
26
63.610
7.767
34.864
1.000
26.28

ATOM
119
N
ALA A
27
65.226
6.236
35.064
1.000
20.21

ATOM
120
CA
ALA A
27
64.316
5.109
34.921
1.000
25.18

ATOM
121
CB
ALA A
27
65.121
3.818
34.862
1.000
25.77

ATOM
122
C
ALA A
27
63.300
5.079
36.056
1.000
28.07

ATOM
123
O
ALA A
27
62.098
4.897
35.838
1.000
26.17

ATOM
124
N
GLU A
28
63.759
5.262
37.299
1.000
25.77

ATOM
125
CA
GLU A
28
62.793
5.280
38.403
1.000
26.24

ATOM
126
CB
GLU A
28
63.509
5.474
39.747
1.000
26.43

ATOM
127
CG
GLU A
28
64.155
4.190
40.239
1.000
29.26

ATOM
128
CD
GLU A
28
65.322
4.364
41.176
1.000
35.43

ATOM
129
OE1
GLU A
28
65.845
3.327
41.641
1.000
39.79

ATOM
130
OE2
GLU A
28
65.725
5.511
41.457
1.000
40.51

ATOM
131
C
GLU A
28
61.736
6.353
38.200
1.000
29.60

ATOM
132
O
GLU A
28
60.527
6.105
38.265
1.000
24.84

ATOM
133
N
ARG A
29
62.157
8.589
37.935
1.000
24.83

ATOM
134
CA
ARG A
29
61.176
8.661
37.772
1.000
26.33

ATOM
135
CB
ARG A
29
61.908
9.991
37.560
1.000
23.24

ATOM
136
CG
ARG A
29
61.039
11.130
37.078
1.000
24.21

ATOM
137
CD
ARG A
29
61.639
12.485
37.398
1.000
25.40

ATOM
138
NE
ARG A
29
60.559
13.482
37.422
1.000
27.67

ATOM
139
CZ
ARG A
29
60.014
13.892
38.559
1.000
30.21

ATOM
140
NH1
ARG A
29
59.042
14.791
38.527
1.000
31.45

ATOM
141
NH2
ARG A
29
60.441
13.409
39.718
1.000
29.38

ATOM
142
C
ARG A
29
60.210
8.405
36.620
1.000
29.14

ATOM
143
O
ARG A
29
58.992
8.557
36.761
1.000
31.80

ATOM
144
N
LEU A
30
60.749
8.024
35.461
1.000
25.02

ATOM
145
CA
LEU A
30
59.880
7.864
34.295
1.000
27.73

ATOM
146
CB
LEU A
30
60.700
7.667
33.017
1.000
26.81

ATOM
147
CG
LEU A
30
61.602
8.837
32.602
1.000
25.95

ATOM
148
CD1
LEU A
30
62.296
8.530
31.280
1.000
18.00

ATOM
149
CD2
LEU A
30
60.832
10.141
32.501
1.000
25.79

ATOM
150
C
LEU A
30
58.910
6.705
34.504
1.000
32.32

ATOM
151
O
LEU A
30
57.707
6.857
34.261
1.000
32.24

ATOM
152
N
VAL A
31
59.420
5.555
34.951
1.000
26.53

ATOM
153
CA
VAL A
31
58.504
4.438
35.202
1.000
30.92

ATOM
154
CB
VAL A
31
59.228
3.177
35.690
1.000
33.99

ATOM
155
CG1
VAL A
31
58.227
2.141
36.183
1.000
41.79

ATOM
156
CG2
VAL A
31
60.092
2.582
34.586
1.000
28.28

ATOM
157
C
VAL A
31
57.465
4.884
36.228
1.000
32.60

ATOM
158
O
VAL A
31
56.271
4.603
36.133
1.000
35.28

ATOM
159
N
GLY A
32
57.937
5.637
37.219
1.000
26.54

ATOM
160
CA
GLY A
32
57.041
6.213
38.209
1.000
28.51

ATOM
161
C
GLY A
32
56.043
7.178
37.602
1.000
35.42

ATOM
162
O
GLY A
32
54.960
7.376
38.160
1.000
31.39

ATOM
163
N
GLN A
33
56.387
7.791
36.470
1.000
36.54

ATOM
164
CA
GLN A
33
55.470
8.735
35.835
1.000
35.97

ATOM
165
CB
GLN A
33
56.251
9.946
35.304
1.000
39.48

ATOM
166
CG
GLN A
33
56.931
10.759
36.395
1.000
44.03

ATOM
167
CD
GLN A
33
55.975
11.701
37.105
1.000
48.53

ATOM
168
OE1
GLN A
33
55.142
12.349
36.469
1.000
57.31

ATOM
169
NE2
GLN A
33
56.073
11.773
38.426
1.000
58.52

ATOM
170
C
GLN A
33
54.666
8.107
37.708
1.000
33.10

ATOM
171
O
GLN A
33
54.151
8.809
33.835
1.000
32.11

ATOM
172
N
GLY A
34
54.548
6.786
34.698
1.000
30.58

ATOM
173
CA
GLY A
34
53.759
6.081
33.712
1.000
30.35

ATOM
174
C
GLY A
34
54.465
5.672
32.444
1.000
33.61

ATOM
175
O
GLY A
34
53.842
5.118
31.529
1.000
32.81

ATOM
176
N
ALA A
35
55.769
5.914
32.316
1.000
29.29

ATOM
177
CA
ALA A
35
56.477
5.513
31.103
1.000
24.74

ATOM
178
CB
ALA A
35
57.603
6.507
30.811
1.000
25.46

ATOM
179
C
ALA A
35
57.043
4.110
31.214
1.000
25.25

ATOM
180
O
ALA A
35
57.104
3.509
32.287
1.000
29.96

ATOM
181
N
SER A
36
57.502
3.540
30.094
1.000
27.78

ATOM
182
CA
SER A
36
58.197
2.255
30.188
1.000
29.92

ATOM
183
CB
SER A
36
57.665
1.248
29.173
1.000
29.14

ATOM
184
OG
SER A
36
56.246
1.180
29.229
1.000
34.85

ATOM
185
C
SER A
36
59.693
2.474
29.987
1.000
34.68

ATOM
186
O
SER A
36
60.112
3.339
29.199
1.000
29.89

ATOM
187
N
ALA A
37
60.520
1.704
30.699
1.000
69.94

ATOM
188
CA
ALA A
37
61.956
1.937
30.534
1.000
29.90

ATOM
189
CB
ALA A
37
62.525
2.620
31.769
1.000
27.09

ATOM
190
C
ALA A
37
62.702
0.647
30.219
1.000
26.26

ATOM
191
O
ALA A
37
62.390
−0.426
30.728
1.000
32.04

ATOM
192
N
VAL A
38
63.695
0.788
29.354
1.000
23.68

ATOM
193
CA
VAL A
38
64.637
−0.263
29.023
1.000
22.95

ATOM
194
CB
VAL A
38
64.811
−0.441
27.504
1.000
25.74

ATOM
195
CG1
VAL A
38
65.856
−1.513
27.223
1.000
24.56

ATOM
196
CG2
VAL A
38
63.491
−0.774
26.830
1.000
32.06

ATOM
197
C
VAL A
38
65.997
0.093
29.617
1.000
28.45

ATOM
198
O
VAL A
38
66.594
1.082
29.173
1.000
26.25

ATOM
199
N
LEU A
39
66.491
−0.659
30.600
1.000
27.75

ATOM
200
CA
LEU A
39
67.800
−0.311
31.164
1.000
25.11

ATOM
201
CB
LEU A
39
67.947
−0.783
32.608
1.000
24.71

ATOM
202
CG
LEU A
39
66.802
−0.447
33.563
1.000
22.78

ATOM
203
CD1
LEU A
39
67.098
−0.949
34.969
1.000
22.70

ATOM
204
CD2
LEU A
39
66.523
1.047
33.573
1.000
21.30

ATOM
205
C
LEU A
39
68.904
−0.910
30.305
1.000
25.85

ATOM
206
O
LEU A
39
69.165
−2.113
30.378
1.000
29.36

ATOM
207
N
LEU A
40
69.548
−0.085
29.480
1.000
24.69

ATOM
208
CA
LEU A
40
70.644
−0.615
28.655
1.000
22.81

ATOM
209
CB
LEU A
40
70.642
0.066
27.298
1.000
19.59

ATOM
210
CG
LEU A
40
71.463
−0.528
26.158
1.000
25.17

ATOM
211
CD1
LEU A
40
70.956
−0.022
24.814
1.000
27.01

ATOM
212
CD2
LEU A
40
72.940
−0.191
26.275
1.000
26.56

ATOM
213
C
LEU A
40
71.962
−0.442
29.410
1.000
26.53

ATOM
214
O
LEU A
40
72.434
0.664
29.672
1.000
25.35

ATOM
215
N
ASP A
41
72.575
−1.561
29.783
1.000
28.32

ATOM
216
CA
ASP A
41
73.804
−1.500
30.579
1.000
27.97

ATOM
217
CB
ASP A
41
73.454
−1.175
32.031
1.000
21.96

ATOM
218
CG
ASP A
41
74.535
−0.431
32.778
1.000
27.64

ATOM
219
OD1
ASP A
41
75.708
−0.851
32.693
1.000
27.85

ATOM
220
OD2
ASP A
41
74.235
0.571
33.459
1.000
25.29

ATOM
221
C
ASP A
41
74.559
−2.815
30.443
1.000
28.71

ATOM
222
O
ASP A
41
74.000
−3.774
29.901
1.000
26.54

ATOM
223
N
LEU A
42
72.795
−2.879
30.910
1.000
26.54

ATOM
224
CA
LEU A
42
76.641
−4.055
30.732
1.000
28.04

ATOM
225
CB
LEU A
42
78.055
−3.751
31.262
1.000
27.78

ATOM
226
CG
LEU A
42
78.868
−2.727
30.459
1.000
29.86

ATOM
227
CD1
LEU A
42
80.180
−2.423
31.172
1.000
26.34

ATOM
228
CD2
LEU A
42
79.126
−3.212
29.043
1.000
18.86

ATOM
229
C
LEU A
42
76.098
−5.293
31.423
1.000
26.58

ATOM
230
O
LEU A
42
75.344
−5.204
32.392
1.000
23.94

ATOM
231
N
PRO A
43
76.468
−6.473
30.947
1.000
30.41

ATOM
232
CD
PRO A
43
77.291
−6.725
29.753
1.000
31.03

ATOM
233
CA
PRO A
43
76.042
−7.716
31.593
1.000
32.05

ATOM
234
CB
PRO A
43
76.767
−8.808
30.796
1.000
29.32

ATOM
235
CB
PRO A
43
77.035
−8.184
29.469
1.000
32.03

ATOM
236
C
PRO A
43
76.484
−7.799
33.046
1.000
33.41

ATOM
237
O
PRO A
43
75.756
−8.304
33.911
1.000
37.54

ATOM
238
N
ASN A
44
77.685
−7.316
33.356
1.000
31.95

ATOM
239
CA
ASN A
44
78.146
−7.453
34.744
1.000
40.41

ATOM
240
CB
ASN A
44
79.668
−7.347
34.827
1.000
49.11

ATOM
241
CG
ASN A
44
80.196
−6.236
33.938
1.000
49.11

ATOM
242
OD1
ASN A
44
80.617
−6.491
32.805
1.000
69.12

ATOM
243
ND2
ASN A
44
80.167
−5.006
34.446
1.000
62.20

ATOM
244
C
ASN A
44
77.490
−6.415
35.636
1.000
38.34

ATOM
245
O
ASN A
44
77.624
−6.435
36.861
1.000
41.33

ATOM
246
N
SER A
45
76.741
−5.475
35.053
1.000
35.28

ATOM
247
CA
SER A
45
76.052
−4.530
35.939
1.000
32.87

ATOM
248
CB
SER A
45
75.622
−3.278
35.188
1.000
31.87

ATOM
249
OG
SER A
45
74.642
−3.582
34.212
1.000
29.60

ATOM
250
C
SER A
45
74.863
−5.241
36.578
1.000
37.42

ATOM
251
O
SER A
45
74.533
−6.370
36.209
1.000
64.40

ATOM
252
N
GLY A
46
74.217
−4.587
37.537
1.000
34.25

ATOM
253
CA
GLY A
46
73.055
−5.178
38.181
1.000
31.85

ATOM
254
C
GLY A
46
71.759
−4.755
37.526
1.000
30.67

ATOM
255
O
GLY A
46
70.729
−4.609
38.193
1.000
33.01

ATOM
256
N
GLY A
47
71.756
−4.541
36.209
1.000
29.41

ATOM
257
CA
GLY A
47
70.527
−4.137
35.549
1.000
30.70

ATOM
258
C
GLY A
47
69.377
−5.097
35.791
1.000
33.15

ATOM
259
O
GLY A
47
68.247
−4.677
36.065
1.000
31.89

ATOM
260
N
GLU A
48
69.659
−6.397
35.698
1.000
32.03

ATOM
261
CA
GLU A
48
68.588
−7.391
35.804
1.000
31.42

ATOM
262
CB
GLU A
48
69.127
−8.815
35.682
1.000
37.80

ATOM
263
CG
GLU A
48
68.132
−9.893
35.337
1.000
47.30

ATOM
264
CD
GLU A
48
66.763
−9.448
34.885
1.000
58.32

ATOM
265
OE1
GLU A
48
65.804
−9.621
35.670
1.000
65.85

ATOM
266
OE2
GLU A
48
66.612
−8.930
33.758
1.000
70.00

ATOM
267
C
GLU A
48
67.846
−7.239
37.118
1.000
30.92

ATOM
268
O
GLU A
48
66.617
−7.218
37.178
1.000
36.04

ATOM
269
N
ALA A
49
68.606
−7.117
38.205
1.000
31.19

ATOM
270
CA
ALA A
49
67.948
−6.896
39.494
1.000
31.65

ATOM
271
CB
ALA A
49
68.978
−7.001
40.610
1.000
31.46

ATOM
272
C
ALA A
49
67.228
−5.537
39.519
1.000
30.98

ATOM
273
O
ALA A
49
66.139
−5.435
40.085
1.000
27.23

ATOM
274
N
GLN A
50
67.816
−4.515
38.920
1.000
29.45

ATOM
275
CA
GLN A
50
67.152
−3.211
38.984
1.000
26.50

ATOM
276
CB
GLN A
50
68.110
−2.104
38.549
1.000
26.43

ATOM
277
CG
GLN A
50
69.247
−1.827
39.512
1.000
26.86

ATOM
278
CD
GLN A
50
68.821
−1.263
40.853
1.000
31.76

ATOM
279
OE1
GLN A
50
69.636
−1.155
41.777
1.000
48.35

ATOM
280
NE2
GLN A
50
67.557
−0.892
41.009
1.000
25.67

ATOM
281
C
GLN A
50
65.893
−3.202
38.123
1.000
26.83

ATOM
282
O
GLN A
50
64.914
−2.541
38.469
1.000
28.11

ATOM
283
N
ALA A
51
65.919
−3.926
37.003
1.000
26.24

ATOM
284
CA
ALA A
51
64.730
−4.022
36.163
1.000
29.19

ATOM
285
CB
ALA A
51
65.064
−4.714
34.851
1.000
29.30

ATOM
286
C
ALA A
51
63.604
−4.759
36.880
1.000
31.69

ATOM
287
O
ALA A
51
62.434
−4.410
36.725
1.000
29.70

ATOM
288
CB
LYS A
52
63.436
−7.768
39.045
1.000
39.33

ATOM
289
C
LYS A
52
62.289
−5.597
39.496
1.000
32.07

ATOM
290
O
LYS A
52
61.074
−5.564
39.705
1.000
31.48

ATOM
291
N
LYS A
52
63.934
−5.779
37.666
1.000
31.15

ATOM
292
CA
LYS A
53
62.895
−6.487
38.421
1.000
33.63

ATOM
293
N
LYS A
53
63.132
−4.849
40.206
1.000
31.94

ATOM
294
CA
LYS A
53
62.646
−3.936
41.231
1.000
33.54

ATOM
295
CB
LYS A
53
63.805
−3.177
41.871
1.000
35.96

ATOM
296
CG
LYS A
53
64.746
−3.962
42.758
1.000
43.20

ATOM
297
CD
LYS A
53
65.258
−3.055
43.877
1.000
49.44

ATOM
298
CE
LYS A
53
64.198
−2.022
44.244
1.000
50.60

ATOM
299
NZ
LYS A
53
64.784
−0.830
44.919
1.000
60.33

ATOM
300
C
LYS A
53
61.671
−2.908
40.672
1.000
36.81

ATOM
301
O
LYS A
53
60.745
−2.481
41.369
1.000
40.69

ATOM
302
N
LEU A
54
61.855
−2.468
39.423
1.000
35.85

ATOM
303
CA
LEU A
54
61.021
−1.353
38.960
1.000
32.59

ATOM
304
CB
LEU A
54
61.779
−0.549
37.886
1.000
28.86

ATOM
305
CG
LEU A
54
62.665
0.555
38.491
1.000
30.10

ATOM
306
CD1
LEU A
54
63.603
1.152
37.459
1.000
29.65

ATOM
307
CD2
LEU A
54
61.779
1.617
39.126
1.000
29.77

ATOM
308
C
LEU A
54
59.660
−1.797
38.457
1.000
31.24

ATOM
309
O
LEU A
54
58.766
−0.954
38.352
1.000
39.12

ATOM
310
N
GLY A
55
59.484
−3.081
38.163
1.000
34.66

ATOM
311
CA
GLY A
55
59.174
−3.601
37.829
1.000
29.84

ATOM
312
C
GLY A
55
58.004
−4.016
36.387
1.000
30.24

ATOM
313
O
GLY A
55
58.972
−4.176
35.645
1.000
27.18

ATOM
314
N
ASN A
56
56.747
−4.198
35.985
1.000
32.93

ATOM
315
CA
ASN A
56
56.409
−4.664
34.650
1.000
38.74

ATOM
316
CB
ASN A
56
54.896
−4.906
34.554
1.000
45.27

ATOM
317
CG
ASN A
56
54.472
−6.105
35.376
1.000
52.39

ATOM
318
OD1
ASN A
56
53.386
−6.091
35.948
1.000
62.55

ATOM
319
ND2
ASN A
56
55.334
−7.116
35.417
1.000
51.01

ATOM
320
C
ASN A
56
56.802
−3.691
33.548
1.000
36.08

ATOM
321
O
ASN A
56
56.989
−4.108
32.400
1.000
37.33

ATOM
322
N
ASN A
57
56.905
−2.405
33.885
1.000
35.54

ATOM
323
CA
ASN A
57
57.123
−1.426
32.816
1.000
34.82

ATOM
324
CB
ASN A
57
56.314
−0.156
33.089
1.000
33.64

ATOM
325
CG
ASN A
57
54.817
−0.410
33.105
1.000
38.38

ATOM
326
OD1
ASN A
57
54.099
0.174
33.917
1.000
46.58

ATOM
327
ND2
ASN A
57
54.352
−1.283
32.219
1.000
39.66

ATOM
328
C
ASN A
57
58.601
−1.096
32.641
1.000
35.06

ATOM
329
O
ASN A
57
58.952
−0.061
32.068
1.000
29.66

ATOM
330
N
CYS A
58
59.463
−1.981
33.132
1.000
32.26

ATOM
331
CA
CYS A
58
60.908
−1.788
33.018
1.000
31.63

ATOM
332
CB
CYS A
58
61.453
−1.136
34.299
1.000
30.13

ATOM
333
SG
CYS A
58
63.247
−0.942
34.332
1.000
30.84

ATOM
334
C
CYS A
58
61.686
−3.094
32.749
1.000
28.19

ATOM
335
O
CYS A
58
61.469
−4.089
33.455
1.000
31.62

ATOM
336
N
VAL A
59
62.479
−3.139
31.716
1.000
29.67

ATOM
337
CA
VAL A
59
63.231
−4.367
31.450
1.000
27.92

ATOM
338
CB
VAL A
59
62.717
−5.090
30.193
1.000
34.40

ATOM
339
CG1
VAL A
59
61.194
−5.189
30.205
1.000
35.21

ATOM
340
CG2
VAL A
59
63.186
−4.379
28.931
1.000
33.09

ATOM
341
C
VAL A
59
64.720
−4.068
31.305
1.000
30.47

ATOM
342
O
VAL A
59
65.109
−2.914
31.099
1.000
30.32

ATOM
343
N
PHE A
60
65.540
−5.106
31.414
1.000
28.13

ATOM
344
CA
PHE A
60
66.984
−4.984
31.257
1.000
27.53

ATOM
345
CB
PHE A
60
67.699
−5.719
32.386
1.000
26.77

ATOM
346
CG
PHE A
60
69.197
−5.879
32.228
1.000
29.40

ATOM
347
CD1
PHE A
60
70.027
−4.793
32.017
1.000
30.82

ATOM
348
CD2
PHE A
60
69.775
−7.134
32.295
1.000
30.46

ATOM
349
CE1
PHE A
60
71.391
−4.955
31.880
1.000
28.83

ATOM
350
CE2
PHE A
60
71.144
−7.301
32.157
1.000
28.61

ATOM
351
CZ
PHE A
60
71.963
−6.211
31.948
1.000
26.40

ATOM
352
C
PHE A
60
67.430
−5.520
29.900
1.000
31.03

ATOM
353
O
PHE A
60
67.112
−6.641
29.507
1.000
28.03

ATOM
354
N
ALA A
61
68.183
−4.708
29.165
1.000
29.19

ATOM
355
CA
ALA A
61
68.787
−5.142
27.909
1.000
25.43

ATOM
356
CB
ALA A
61
68.346
−4.273
26.748
1.000
28.07

ATOM
357
C
ALA A
61
70.306
−5.101
28.044
1.000
28.34

ATOM
358
O
ALA A
61
70.876
−4.007
28.104
1.000
32.03

ATOM
359
N
PRO A
62
70.940
−6.263
28.112
1.000
30.23

ATOM
360
CD
PRO A
62
70.344
−7.605
28.031
1.000
27.38

ATOM
361
CA
PRO A
62
72.397
−6.292
28.287
1.000
29.81

ATOM
362
CB
PRO A
62
72.692
−7.775
28.525
1.000
28.87

ATOM
363
CG
PRO A
62
71.543
−8.503
27.920
1.000
28.71

ATOM
364
C
PRO A
62
73.114
−5.792
27.042
1.000
29.91

ATOM
365
O
PRO A
62
72.857
−6.253
25.926
1.000
31.43

ATOM
366
N
ALA A
63
74.026
−4.836
27.200
1.000
23.31

ATOM
367
CA
ALA A
63
74.725
−4.334
26.017
1.000
27.56

ATOM
368
CB
ALA A
63
73.754
−3.643
25.064
1.000
24.43

ATOM
369
C
ALA A
63
75.845
−3.363
26.369
1.000
23.71

ATOM
370
O
ALA A
63
75.730
−2.283
27.305
1.000
27.32

ATOM
371
N
ASP A
64
76.910
−3.416
25.594
1.000
24.90

ATOM
372
CA
ASP A
64
78.039
−2.504
25.601
1.000
27.05

ATOM
373
CB
ASP A
64
79.335
−3.280
25.359
1.000
24.11

ATOM
374
CG
ASP A
64
80.575
−2.425
25.459
1.000
27.69

ATOM
375
OD1
ASP A
64
81.672
−2.969
25.700
1.000
32.95

ATOM
376
OD2
ASP A
64
80.481
−1.188
25.299
1.000
29.28

ATOM
377
C
ASP A
64
77.816
−1.455
24.513
1.000
26.63

ATOM
378
O
ASP A
64
77.662
−1.864
23.353
1.000
23.13

ATOM
379
N
VAL A
65
77.773
−0.175
24.870
1.000
28.62

ATOM
380
CA
VAL A
65
77.445
0.878
23.913
1.000
25.22

ATOM
381
CB
VAL A
65
77.169
2.252
24.562
1.000
22.72

ATOM
382
CG1
VAL A
65
75.934
2.199
25.445
1.000
19.07

ATOM
383
CG2
VAL A
65
78.382
2.737
25.354
1.000
22.83

ATOM
384
C
VAL A
65
78.545
1.085
22.882
1.000
22.70

ATOM
385
O
VAL A
65
78.316
1.783
21.891
1.000
26.47

ATOM
386
N
THR A
66
79.731
0.513
23.074
1.000
21.37

ATOM
387
CA
THR A
66
80.742
0.660
22.027
1.000
23.63

ATOM
388
CB
THR A
66
82.175
0.536
22.567
1.000
26.03

ATOM
389
OG1
THR A
66
82.330
−0.756
23.182
1.000
28.93

ATOM
390
CG1
THR A
66
82.437
1.562
23.658
1.000
26.52

ATOM
391
C
THR A
66
80.567
−0.391
20.934
1.000
27.05

ATOM
392
O
THR A
66
81.322
−0.413
19.966
1.000
27.67

ATOM
393
N
SER A
67
79.588
−1.273
21.068
1.000
28.37

ATOM
394
CA
SER A
67
79.390
−2.367
20.128
1.000
27.49

ATOM
395
CB
SER A
67
79.300
−3.686
20.904
1.000
23.12

ATOM
396
OG
SER A
67
78.456
−4.607
20.235
1.000
28.63

ATOM
397
C
SER A
67
78.143
−2.202
19.266
1.000
27.54

ATOM
398
O
SER A
67
77.027
−2.082
19.789
1.000
28.72

ATOM
399
N
GLU A
68
78.325
−2.214
17.942
1.000
27.74

ATOM
400
CA
GLU A
68
77.192
−2.102
17.028
1.000
29.78

ATOM
401
CB
GLU A
68
77.652
−2.183
15.560
1.000
30.35

ATOM
402
CG
GLU A
68
76.501
−1.980
14.588
1.000
33.75

ATOM
403
CD
GLU A
68
76.933
−1.791
13.150
1.000
37.21

ATOM
404
OE1
GLU A
68
77.152
−0.638
12.731
1.000
36.37

ATOM
405
OE2
GLU A
68
77.055
−2.805
12.432
1.000
44.18

ATOM
406
C
GLU A
68
76.153
−3.186
17.271
1.000
27.83

ATOM
407
O
GLU A
68
74.964
−2.915
17.443
1.000
26.11

ATOM
408
CB
LYS A
69
76.372
−6.876
17.184
1.000
34.15

ATOM
409
C
LYS A
69
74.896
−5.512
18.692
1.000
29.20

ATOM
410
O
LYS A
69
73.680
−5.745
18.740
1.000
28.05

ATOM
411
N
LYS A
69
76.601
−4.442
17.264
1.000
24.54

ATOM
412
CA
LYS A
69
75.653
−5.551
17.369
1.000
27.59

ATOM
413
N
ASP A
70
75.589
−5.223
19.791
1.000
26.28

ATOM
414
CA
ASP A
70
74.905
−5.189
21.085
1.000
28.59

ATOM
415
CB
ASP A
70
75.891
−4.867
22.211
1.000
30.01

ATOM
416
CG
ASP A
70
76.714
−6.064
22.626
1.000
30.41

ATOM
417
OD1
ASP A
70
76.556
−7.136
22.014
1.000
32.46

ATOM
418
OD2
ASP A
70
77.520
−5.919
23.568
1.000
31.67

ATOM
419
C
ASP A
70
73.785
−4.161
21.118
1.000
25.48

ATOM
420
O
ASP A
70
72.673
−4.412
21.582
1.000
28.32

ATOM
421
N
VAL A
71
74.102
−2.962
20.614
1.000
27.50

ATOM
422
CA
VAL A
71
73.073
−1.917
20.648
1.000
25.54

ATOM
423
CB
VAL A
71
73.667
−0.550
20.280
1.000
25.70

ATOM
424
CG1
VAL A
71
72.592
0.519
20.166
1.000
23.17

ATOM
425
CG2
VAL A
71
74.711
−0.143
21.315
1.000
27.59

ATOM
426
C
VAL A
71
71.932
−2.316
19.723
1.000
25.05

ATOM
427
O
VAL A
71
70.750
−2.147
20.019
1.000
26.83

ATOM
428
N
GLN A
72
72.293
−2.883
18.574
1.000
24.81

ATOM
429
CA
GLN A
72
71.261
−3.431
17.693
1.000
29.31

ATOM
430
CB
GLN A
72
71.918
−4.055
16.465
1.000
28.74

ATOM
431
CG
GLN A
72
72.472
−3.031
15.482
1.000
30.16

ATOM
432
CD
GLN A
72
73.120
−3.697
14.283
1.000
36.36

ATOM
433
OE1
GLN A
72
73.821
−4.699
14.442
1.000
43.12

ATOM
434
NE2
GLN A
72
72.895
−3.153
13.093
1.000
40.74

ATOM
435
C
GLN A
72
70.418
−4.454
18.439
1.000
26.93

ATOM
436
O
GLN A
72
69.191
−4.448
18.377
1.000
30.79

ATOM
437
N
THR A
73
71.069
−5.359
19.173
1.000
26.15

ATOM
438
CA
THR A
73
70.306
−6.375
19.901
1.000
30.40

ATOM
439
CB
THR A
73
71.227
−7.417
20.561
1.000
37.27

ATOM
440
OG1
THR A
73
72.116
−7.998
19.599
1.000
36.22

ATOM
441
OG2
THR A
73
70.393
−8.571
21.103
1.000
35.78

ATOM
442
C
THR A
73
69.410
−5.755
20.963
1.000
32.05

ATOM
443
O
THR A
73
68.253
−6.130
21.181
1.000
36.06

ATOM
444
N
ALA A
74
69.935
−4.759
21.681
1.000
27.56

ATOM
445
CA
ALA A
74
69.125
−4.130
22.719
1.000
23.23

ATOM
446
CB
ALA A
74
70.014
−3.240
23.579
1.000
27.20

ATOM
447
C
ALA A
74
67.975
−3.327
22.143
1.000
27.14

ATOM
448
O
ALA A
74
66.920
−3.170
22.769
1.000
32.32

ATOM
449
N
LEU A
75
68.124
−2.755
20.943
1.000
27.14

ATOM
450
CA
LEU A
75
67.004
−1.940
20.453
1.000
27.09

ATOM
451
CB
LEU A
75
67.496
−1.012
19.342
1.000
27.14

ATOM
452
CG
LEU A
75
68.362
0.157
19.824
1.000
26.32

ATOM
453
CD1
LEU A
75
68.833
1.022
18.667
1.000
27.27

ATOM
454
CD2
LEU A
75
67.602
1.004
20.836
1.000
23.37

ATOM
455
C
LEU A
75
65.856
−2.839
20.007
1.000
26.19

ATOM
456
O
LEU A
75
64.673
−2.555
20.198
1.000
26.12

ATOM
457
N
ALA A
76
66.226
−3.955
19.394
1.000
28.48

ATOM
458
CA
ALA A
76
65.291
−4.987
18.974
1.000
32.72

ATOM
459
CB
ALA A
76
66.033
−6.067
18.194
1.000
30.42

ATOM
460
C
ALA A
76
64.584
−5.562
20.191
1.000
36.42

ATOM
461
O
ALA A
76
63.386
−5.845
20.160
1.000
35.82

ATOM
462
N
LEU A
77
65.323
−5.733
21.287
1.000
34.58

ATOM
463
CA
LEU A
77
64.675
−6.174
22.526
1.000
30.05

ATOM
464
CB
LEU A
77
65.706
−6.374
23.623
1.000
32.29

ATOM
465
CG
LEU A
77
65.256
−6.961
24.965
1.000
35.67

ATOM
466
CD1
LEU A
77
66.370
−7.768
25.618
1.000
39.63

ATOM
467
CD2
LEU A
77
64.799
−5.868
25.922
1.000
31.59

ATOM
468
C
LEU A
77
63.621
−5.149
22.927
1.000
32.17

ATOM
469
O
LEU A
77
62.499
−5.499
23.299
1.000
35.79

ATOM
470
N
ALA A
78
64.007
−3.875
22.853
1.000
29.62

ATOM
471
CA
ALA A
78
63.101
−2.822
23.307
1.000
32.17

ATOM
472
CB
ALA A
78
63.822
−1.483
23.336
1.000
32.12

ATOM
473
C
ALA A
78
61.849
−2.748
22.447
1.000
30.46

ATOM
474
O
ALA A
78
60.731
−2.575
22.946
1.000
30.23

ATOM
475
N
LYS A
79
62.013
−2.876
21.133
1.000
33.18

ATOM
476
CA
LYS A
79
60.833
−2.810
20.266
1.000
36.74

ATOM
477
CB
LYS A
79
61.245
−2.779
18.804
1.000
33.27

ATOM
478
C
LYS A
79
59.908
−3.987
20.553
1.000
38.51

ATOM
479
O
LYS A
79
58.725
−3.833
20.865
1.000
37.04

ATOM
480
N
GLY A
80
60.457
−5.196
20.455
1.000
38.59

ATOM
481
CA
GLY A
80
59.683
−6.401
20.700
1.000
40.57

ATOM
482
C
GLY A
80
58.971
−6.362
22.035
1.000
42.68

ATOM
483
O
GLY A
80
57.842
−6.835
22.193
1.000
43.09

ATOM
484
N
LYS A
81
59.614
−5.779
23.052
1.000
37.05

ATOM
485
CA
LYS A
81
58.951
−5.799
24.356
1.000
34.36

ATOM
486
CB
LYS A
81
59.988
−5.738
25.482
1.000
39.39

ATOM
487
CG
LYS A
81
59.370
−5.571
26.863
1.000
47.54

ATOM
488
CD
LYS A
81
58.961
−6.918
27.443
1.000
53.39

ATOM
489
CE
LYS A
81
57.911
−6.741
28.529
1.000
57.33

ATOM
490
NZ
LYS A
81
57.931
−7.873
29.500
1.000
62.03

ATOM
491
C
LYS A
81
57.947
−4.670
24.506
1.000
35.60

ATOM
492
O
LYS A
81
56.870
−4.863
25.069
1.000
33.46

ATOM
493
N
PHE A
82
58.271
−3.472
24.015
1.000
32.89

ATOM
494
CA
PHE A
82
57.382
−2.357
24.335
1.000
31.56

ATOM
495
CB
PHE A
82
58.129
−1.303
25.161
1.000
34.84

ATOM
496
CG
PHE A
82
58.418
−1.752
26.585
1.000
33.59

ATOM
497
CD1
PHE A
82
57.406
−2.221
27.406
1.000
31.18

ATOM
498
CD2
PHE A
82
59.712
−1.693
27.081
1.000
30.71

ATOM
499
CE1
PHE A
82
57.690
−2.623
28.698
1.000
34.47

ATOM
500
CE2
PHE A
82
60.002
−2.097
28.371
1.000
30.31

ATOM
501
CZ
PHE A
82
58.987
−2.563
29.185
1.000
33.43

ATOM
502
C
PHE A
82
56.760
−1.710
23.107
1.000
33.34

ATOM
503
O
PHE A
82
55.969
−0.783
23.304
1.000
35.24

ATOM
504
N
GLY A
83
57.098
−2.188
21.916
1.000
35.59

ATOM
505
CA
GLY A
83
56.424
−1.757
20.707
1.000
37.30

ATOM
506
C
GLY A
83
57.132
−0.690
19.906
1.000
40.28

ATOM
507
O
GLY A
83
57.141
−0.747
18.668
1.000
38.84

ATOM
508
N
ARG A
84
57.724
0.292
20.573
1.000
36.22

ATOM
509
CA
ARG A
84
58.472
1.354
19.917
1.000
33.53

ATOM
510
CB
ARG A
84
57.523
2.420
19.371
1.000
28.51

ATOM
511
CG
ARG A
84
56.638
3.117
20.390
1.000
34.98

ATOM
512
CD
ARG A
84
56.394
4.574
20.015
1.000
44.46

ATOM
513
NE
ARG A
84
55.513
4.720
18.871
1.000
52.06

ATOM
514
CZ
ARG A
84
55.176
5.811
18.208
1.000
56.54

ATOM
515
NH1
ARG A
84
54.338
5.706
17.176
1.000
63.82

ATOM
516
NH2
ARG A
84
55.641
7.015
18.527
1.000
33.88

ATOM
517
C
ARG A
84
59.483
7.015
20.882
1.000
34.32

ATOM
518
O
ARG A
84
59.515
1.588
22.052
1.000
37.33

ATOM
519
N
VAL A
85
60.264
2.925
20.388
1.000
28.25

ATOM
520
CA
VAL A
85
61.157
3.768
21.179
1.000
26.10

ATOM
521
CB
VAL A
85
62.635
3.482
20.862
1.000
28.04

ATOM
522
CG1
VAL A
85
63.551
4.419
21.629
1.000
28.94

ATOM
523
CG2
VAL A
85
62.983
2.037
21.191
1.000
24.86

ATOM
524
C
VAL A
85
60.849
5.242
20.922
1.000
26.87

ATOM
525
O
VAL A
85
60.849
5.696
19.775
1.000
28.91

ATOM
526
N
ASP A
86
60.565
5.994
21.974
1.000
27.02

ATOM
527
CA
ASP A
86
60.191
7.394
21.880
1.000
25.13

ATOM
528
CB
ASP A
86
58.914
7.687
22.679
1.000
26.20

ATOM
529
CG
ASP A
86
57.755
6.817
22.227
1.000
32.00

ATOM
530
OD1
ASP A
86
57.283
5.983
23.028
1.000
31.29

ATOM
531
OD2
ASP A
86
57.330
6.991
21.070
1.000
32.98

ATOM
532
C
ASP A
86
61.287
8.298
22.434
1.000
27.98

ATOM
533
O
ASP A
86
61.426
9.448
22.029
1.000
23.19

ATOM
534
N
VAL A
87
62.044
7.759
23.386
1.000
21.53

ATOM
535
CA
VAL A
87
63.071
8.542
24.056
1.000
20.22

ATOM
536
CB
VAL A
87
62.603
8.986
25.458
1.000
26.46

ATOM
537
CG1
VAL A
87
63.720
9.700
26.207
1.000
24.62

ATOM
538
CG2
VAL A
87
61.388
9.895
25.352
1.000
25.17

ATOM
539
C
VAL A
87
64.351
7.740
24.198
1.000
23.75

ATOM
540
O
VAL A
87
64.311
6.537
24.472
1.000
26.72

ATOM
541
N
ALA A
88
65.488
8.400
24.013
1.000
22.89

ATOM
542
CA
ALA A
88
66.760
7.766
24.350
1.000
21.75

ATOM
543
CB
ALA A
88
67.562
7.361
23.128
1.000
20.27

ATOM
544
C
ALA A
88
67.554
8.732
25.234
1.000
24.86

ATOM
545
O
ALA A
88
67.614
9.931
24.941
1.000
25.52

ATOM
546
N
VAL A
89
68.133
8.190
26.290
1.000
22.71

ATOM
547
CA
VAL A
89
68.941
8.943
27.242
1.000
21.03

ATOM
548
CB
VAL A
89
68.273
9.059
28.619
1.000
26.69

ATOM
549
CG1
VAL A
89
69.077
9.959
29.552
1.000
22.65

ATOM
550
CG2
VAL A
89
66.854
9.602
28.502
1.000
19.47

ATOM
551
C
VAL A
89
70.291
8.249
27.383
1.000
20.81

ATOM
552
O
VAL A
89
70.347
7.096
27.818
1.000
22.03

ATOM
553
N
ASN A
90
71.367
8.939
27.005
1.000
19.58

ATOM
554
CA
ASN A
90
72.695
8.336
27.105
1.000
21.95

ATOM
555
CB
ASN A
90
73.590
8.778
25.940
1.000
20.86

ATOM
556
CG
ASN A
90
73.116
8.208
24.611
1.000
24.64

ATOM
557
OD1
ASN A
90
72.514
8.903
23.785
1.000
25.87

ATOM
558
ND2
ASN A
90
73.396
6.930
24.405
1.000
19.47

ATOM
559
C
ASN A
90
73.346
8.680
28.440
1.000
25.33

ATOM
560
O
ASN A
90
73.842
9.790
28.609
1.000
24.77

ATOM
561
N
CYS A
91
73.353
7.734
29.377
1.000
22.76

ATOM
562
CA
CYS A
91
74.035
7.962
30.646
1.000
24.30

ATOM
563
CB
CYS A
91
73.078
7.785
31.830
1.000
21.56

ATOM
564
SG
CYS A
91
71.780
9.046
31.900
1.000
26.30

ATOM
565
C
CYS A
91
75.244
7.045
30.818
1.000
26.70

ATOM
566
O
CYS A
91
76.075
7.325
31.693
1.000
23.50

ATOM
567
N
ALA A
92
75.370
5.987
30.014
1.000
24.53

ATOM
568
CA
ALA A
92
76.584
5.164
30.095
1.000
25.46

ATOM
569
CB
ALA A
92
76.617
4.053
29.056
1.000
17.19

ATOM
570
C
ALA A
92
77.828
6.029
29.938
1.000
29.08

ATOM
571
O
ALA A
92
77.960
6.832
29.012
1.000
21.74

ATOM
572
N
GLY A
93
78.761
5.870
30.863
1.000
26.43

ATOM
573
CA
GLY A
93
79.968
6.688
30.863
1.000
21.76

ATOM
574
C
GLY A
93
80.973
6.213
31.898
1.000
26.37

ATOM
575
O
GLY A
93
80.618
5.566
32.884
1.000
21.56

ATOM
576
N
ILE A
94
82.241
6.549
31.675
1.000
22.95

ATOM
577
CA
ILE A
94
83.284
6.187
32.626
1.000
23.39

ATOM
578
CB
ILE A
94
84.202
5.061
32.107
1.000
23.77

ATOM
579
CG2
ILE A
94
83.443
3.739
32.043
1.000
23.99

ATOM
580
CG1
ILE A
94
84.872
5.403
30.774
1.000
26.25

ATOM
581
CD1
ILE A
94
85.890
4.373
30.312
1.000
27.52

ATOM
582
C
ILE A
94
84.136
7.411
32.952
1.000
25.18

ATOM
583
O
ILE A
94
84.147
8.392
32.212
1.000
20.18

ATOM
584
N
ALA A
95
84.841
7.327
34.071
1.000
30.99

ATOM
585
CA
ALA A
95
85.701
8.409
34.529
1.000
31.12

ATOM
586
CB
ALA A
95
85.203
8.956
35.861
1.000
25.55

ATOM
587
C
ALA A
95
87.133
7.924
34.689
1.000
30.69

ATOM
588
O
ALA A
95
87.340
6.756
35.011
1.000
26.55

ATOM
589
N
VAL A
96
88.101
8.803
34.473
1.000
26.73

ATOM
590
CA
VAL A
96
89.465
8.504
37.874
1.000
25.75

ATOM
591
CB
VAL A
96
90.383
7.900
33.795
1.000
35.08

ATOM
592
CG1
VAL A
96
89.750
6.702
33.103
1.000
52.12

ATOM
593
CG2
VAL A
96
90.760
8.960
32.768
1.000
41.24

ATOM
594
C
VAL A
96
90.096
9.811
35.353
1.000
24.96

ATOM
595
O
VAL A
96
89.705
10.888
34.903
1.000
24.58

ATOM
596
N
ALA A
97
91.063
9.688
36.254
1.000
22.38

ATOM
597
CA
ALA A
97
91.802
10.883
36.648
1.000
21.56

ATOM
598
CB
ALA A
97
91.603
11.239
38.105
1.000
29.25

ATOM
599
C
ALA A
97
93.265
10.618
36.313
1.000
25.19

ATOM
600
O
ALA A
97
93.879
9.717
36.875
1.000
28.39

ATOM
601
N
SER A
98
93.804
11.403
35.382
1.000
21.29

ATOM
602
CA
SER A
98
95.185
11.135
34.382
1.000
25.00

ATOM
603
CB
SER A
98
95.202
9.932
34.031
1.000
24.99

ATOM
604
OG
SER A
98
96.526
9.479
33.788
1.000
24.22

ATOM
605
C
SER A
98
95.751
12.391
34.346
1.000
26.54

ATOM
606
O
SER A
98
95.142
12.938
34.847
1.000
22.14

ATOM
607
N
LYS A
99
96.886
12.866
34.841
1.000
20.88

ATOM
608
CA
LYS A
99
97.482
14.073
34.285
1.000
25.15

ATOM
609
CB
LYS A
99
98.556
14.615
35.230
1.000
24.83

ATOM
610
CG
LYS A
99
97.977
15.198
36.515
1.000
25.85

ATOM
611
CD
LYS A
99
99.074
15.324
37.563
1.000
31.66

ATOM
612
CE
LYS A
99
98.556
15.983
38.833
1.000
36.77

ATOM
613
NZ
LYS A
99
99.590
16.860
39.449
1.000
50.56

ATOM
614
C
LYS A
99
98.080
13.823
32.905
1.000
26.15

ATOM
615
O
LYS A
99
98.577
12.729
32.630
1.000
22.84

ATOM
616
N
THR A
100
98.038
14.837
32.044
1.000
20.67

ATOM
617
CA
THR A
100
98.657
14.728
30.723
1.000
18.37

ATOM
618
CB
THR A
100
98.611
16.080
29.989
1.000
22.10

ATOM
619
OG1
THR A
100
97.253
16.349
29.621
1.000
23.52

ATOM
620
CG2
THR A
100
99.413
16.049
28.694
1.000
21.67

ATOM
621
C
THR A
100
100.108
14.269
30.845
1.000
22.79

ATOM
622
O
THR A
100
100.536
13.330
30.171
1.000
21.78

ATOM
623
N
TYR A
101
100.821
14.958
31.731
1.000
22.60

ATOM
624
CA
TYR A
101
102.201
14.670
32.073
1.000
24.11

ATOM
625
CB
TYR A
101
103.177
15.281
31.065
1.000
21.94

ATOM
626
CG
TYR A
101
104.619
14.943
31.362
1.000
26.06

ATOM
627
CD1
TYR A
101
105.517
15.952
31.675
1.000
27.69

ATOM
628
CE1
TYR A
101
106.835
15.651
31.950
1.000
30.87

ATOM
629
CD2
TYR A
101
105.074
13.633
31.332
1.000
28.68

ATOM
630
CE2
TYR A
101
106.393
13.319
31.602
1.000
33.41

ATOM
631
CZ
TYR A
101
107.265
14.338
31.912
1.000
32.89

ATOM
632
OH
TYR A
101
108.590
14.059
32.183
1.000
29.23

ATOM
633
C
TYR A
101
102.517
15.222
33.462
1.000
25.97

ATOM
634
O
TYR A
101
102.057
16.312
33.799
1.000
30.11

ATOM
635
N
ASN A
102
103.280
14.468
34.240
1.000
27.66

ATOM
636
CA
ASN A
102
103.722
14.888
35.565
1.000
27.66

ATOM
637
CB
ASN A
102
103.050
14.019
36.632
1.000
31.17

ATOM
638
CG
ASN A
102
103.342
14.473
38.047
1.000
34.75

ATOM
639
OD1
ASN A
102
104.386
15.056
38.326
1.000
35.20

ATOM
640
ND2
ASN A
102
102.405
14.196
38.944
1.000
24.47

ATOM
641
C
ASN A
102
105.239
14.800
35.674
1.000
24.25

ATOM
642
O
ASN A
102
105.793
13.706
35.784
1.000
27.18

ATOM
643
N
LEU A
103
105.917
15.938
35.639
1.000
27.28

ATOM
644
CA
LEU A
103
107.377
15.978
35.641
1.000
30.32

ATOM
645
CB
LEU A
103
107.862
17.419
35.527
1.000
29.30

ATOM
646
CG
LEU A
103
109.359
17.699
35.508
1.000
31.61

ATOM
647
CD1
LEU A
103
110.065
16.887
34.426
1.000
34.65

ATOM
648
CD2
LEU A
103
109.639
19.177
35.284
1.000
27.84

ATOM
649
C
LEU A
103
107.952
15.312
36.888
1.000
36.01

ATOM
650
O
LEU A
103
108.817
14.448
36.800
1.000
38.35

ATOM
651
N
LYS A
104
107.451
15.715
38.052
1.000
40.99

ATOM
652
CA
LYS A
104
107.983
15.240
39.324
1.000
42.00

ATOM
653
CB
LYS A
104
107.336
15.999
40.472
1.000
49.59

ATOM
654
C
LYS A
104
107.803
13.738
39.480
1.000
38.56

ATOM
655
O
LYS A
104
108.705
13.052
39.970
1.000
44.22

ATOM
656
N
LYS A
105
106.657
13.212
39.067
1.000
33.35

ATOM
657
CA
LYS A
105
106.386
11.785
39.147
1.000
33.59

ATOM
658
CB
LYS A
105
104.884
11.507
39.226
1.000
42.15

ATOM
659
CG
LYS A
105
104.271
11.477
40.612
1.000
51.74

ATOM
660
CD
LYS A
105
103.136
10.461
40.692
1.000
61.56

ATOM
661
CE
LYS A
105
103.327
9.347
39.675
1.000
67.86

ATOM
662
NZ
LYS A
105
103.163
7.990
40.272
1.000
70.57

ATOM
663
C
LYS A
105
106.933
11.030
37.938
1.000
31.13

ATOM
664
O
LYS A
105
106.964
9.801
37.943
1.000
31.14

ATOM
665
N
GLY A
106
107.340
11.761
36.902
1.000
26.45

ATOM
666
CA
GLY A
106
107.796
11.094
35.685
1.000
24.64

ATOM
667
C
GLY A
106
106.701
10.239
35.083
1.000
27.43

ATOM
668
O
GLY A
106
106.886
9.081
34.715
1.000
32.86

ATOM
669
N
GLN A
107
105.502
10.813
34.985
1.000
31.11

ATOM
670
CA
GLN A
107
104.374
10.038
34.477
1.000
31.27

ATOM
671
CB
GLN A
107
103.362
9.742
35.574
1.000
28.80

ATOM
672
C
GLN A
107
103.696
10.751
33.303
1.000
28.71

ATOM
673
O
GLN A
107
103.435
11.948
33.346
1.000
24.27

ATOM
674
N
THR A
108
103.430
9.961
32.274
1.000
27.64

ATOM
675
CA
THR A
108
102.755
10.383
31.062
1.000
38.26

ATOM
676
CB
THR A
108
103.610
10.129
29.808
1.000
27.09

ATOM
677
OG1
THR A
108
104.883
10.783
29.912
1.000
25.29

ATOM
678
CG2
THR A
108
102.922
10.733
28.587
1.000
25.91

ATOM
679
C
THR A
108
101.428
9.637
30.923
1.000
24.77

ATOM
680
O
THR A
108
101.378
8.417
31.067
1.000
23.98

ATOM
681
N
HIS A
109
100.355
10.364
30.653
1.000
24.32

ATOM
682
CA
HIS A
109
99.051
9.760
30.368
1.000
22.88

ATOM
683
CB
HIS A
109
98.089
10.835
29.870
1.000
23.80

ATOM
684
CG
HIS A
109
96.630
10.563
30.566
1.000
21.82

ATOM
685
CD2
HIS A
109
95.644
11.296
30.566
1.000
22.92

ATOM
686
ND1
HIS A
109
96.003
9.467
29.439
1.000
21.44

ATOM
687
CE1
HIS A
109
94.699
9.521
29.691
1.000
21.06

ATOM
688
NE2
HIS A
109
94.463
10.622
30.380
1.000
21.74

ATOM
689
C
HIS A
109
99.205
8.654
29.341
1.000
21.10

ATOM
690
O
HIS A
109
99.885
8.840
28.325
1.000
25.00

ATOM
691
N
THR A
110
98.632
7.478
29.588
1.000
20.94

ATOM
692
CA
THR A
110
98.750
6.454
28.546
1.000
21.31

ATOM
693
CB
THR A
110
98.515
5.040
29.088
1.000
24.24

ATOM
694
OG1
THR A
110
97.114
4.885
29.372
1.000
24.99

ATOM
695
CG2
THR A
110
99.305
4.818
30.376
1.000
20.99

ATOM
696
C
THR A
110
97.739
6.708
27.427
1.000
24.56

ATOM
697
O
THR A
110
96.963
7.326
27.615
1.000
27.87

ATOM
698
N
LEU A
111
98.072
6.217
26.237
1.000
26.90

ATOM
699
CA
LEU A
111
97.172
6.378
25.099
1.000
23.81

ATOM
700
CB
LEU A
111
97.883
5.931
23.820
1.000
24.39

ATOM
701
CG
LEU A
111
97.223
6.387
22.516
1.000
26.14

ATOM
702
CD1
LEU A
111
97.221
7.908
22.457
1.000
23.83

ATOM
703
CD2
LEU A
111
97.923
5.788
21.308
1.000
26.57

ATOM
704
C
LEU A
111
95.900
5.582
25.310
1.000
25.30

ATOM
705
O
LEU A
111
94.786
5.995
24.987
1.000
26.74

ATOM
706
N
GLU A
112
96.019
4.371
25.856
1.000
25.49

ATOM
707
CA
GLU A
112
94.818
3.548
25.972
1.000
31.39

ATOM
708
CB
GLU A
112
95.191
2.092
26.246
1.000
42.44

ATOM
709
CG
GLU A
112
95.339
1.235
25.003
1.000
59.05

ATOM
710
CD
GLU A
112
94.763
1.797
25.003
1.000
63.34

ATOM
711
OE1
GLU A
112
93.684
1.315
23.296
1.000
56.32

ATOM
712
OE2
GLU A
112
95.377
2.706
23.110
1.000
40.30

ATOM
713
C
GLU A
112
93.874
4.076
27.044
1.000
29.79

ATOM
714
O
GLU A
112
92.670
3.798
26.999
1.000
25.74

ATOM
715
N
ASP A
113
94.368
4.833
28.020
1.000
27.16

ATOM
716
CA
ASP A
113
93.433
5.446
28.969
1.000
24.71

ATOM
717
CB
ASP A
113
94.133
6.035
30.187
1.000
29.48

ATOM
718
CG
ASP A
113
94.281
5.075
31.345
1.000
29.48

ATOM
719
OD1
ASP A
113
93.602
4.030
31.393
1.000
29.16

ATOM
720
OD2
ASP A
113
95.103
5.363
32.235
1.000
28.92

ATOM
721
C
ASP A
113
92.648
6.540
28.253
1.000
23.27

ATOM
722
O
ASP A
113
91.454
6.730
28.487
1.000
26.21

ATOM
723
N
PHE A
114
93.313
7.279
27.365
1.000
21.26

ATOM
724
CA
PHE A
114
92.614
8.328
26.610
1.000
21.70

ATOM
725
CB
PHE A
114
93.609
9.168
25.808
1.000
21.14

ATOM
726
CG
PHE A
114
93.010
10.429
25.212
1.000
22.14

ATOM
727
CD1
PHE A
114
92.544
10.432
23.907
1.000
23.21

ATOM
728
CD2
PHE A
114
92.918
11.590
25.965
1.000
19.80

ATOM
729
CE1
PHE A
114
91.993
11.579
23.354
1.000
21.77

ATOM
730
CE2
PHE A
114
92.375
12.736
25.417
1.000
22.25

ATOM
731
CZ
PHE A
114
91.910
12.732
24.117
1.000
18.82

ATOM
732
C
PHE A
114
91.582
7.719
25.669
1.000
21.96

ATOM
733
O
PHE A
114
90.462
8.204
25.526
1.000
23.38

ATOM
734
N
GLN A
115
91.989
6.632
25.021
1.000
23.07

ATOM
735
CA
GLN A
115
91.174
5.965
24.017
1.000
25.81

ATOM
736
CB
GLN A
115
92.006
4.911
23.278
1.000
26.74

ATOM
737
CG
GLN A
115
91.332
4.324
22.045
1.000
30.43

ATOM
738
CD
GLN A
115
91.298
5.316
20.896
1.000
32.36

ATOM
739
OE1
GLN A
115
91.328
5.858
20.509
1.000
34.25

ATOM
740
NE2
GLN A
115
90.114
5.565
20.352
1.000
30.37

ATOM
741
C
GLN A
115
89.948
5.307
24.629
1.000
24.71

ATOM
742
O
GLN A
115
88.834
5.443
24.119
1.000
27.44

ATOM
743
N
ARG A
116
90.149
4.577
25.726
1.000
20.08

ATOM
744
CA
ARG A
116
89.030
3.888
26.368
1.000
23.81

ATOM
745
CB
ARG A
116
89.519
3.077
27.562
1.000
25.84

ATOM
746
C
ARG A
116
87.944
4.868
26.808
1.000
21.73

ATOM
747
O
ARG A
116
86.752
4.589
26.705
1.000
22.10

ATOM
748
N
VAL A
117
88.376
6.027
27.297
1.000
22.33

ATOM
749
CA
VAL A
117
87.449
7.054
27.770
1.000
21.83

ATOM
750
CB
VAL A
117
88.220
8.132
28.550
1.000
21.56

ATOM
751
CG1
VAL A
117
87.409
9.401
28.744
1.000
19.07

ATOM
752
CG2
VAL A
117
88.648
7.572
29.907
1.000
26.74

ATOM
753
C
VAL A
117
86.673
7.663
26.612
1.000
22.89

ATOM
754
O
VAL A
117
85.461
7.877
26.721
1.000
25.91

ATOM
755
N
LEU A
118
87.377
7.927
25.516
1.000
19.69

ATOM
756
CA
LEU A
118
86.764
8.413
24.290
1.000
22.74

ATOM
757
CB
LEU A
118
87.803
8.612
23.187
1.000
24.33

ATOM
758
CG
LEU A
118
88.570
9.921
23.065
1.000
36.03

ATOM
759
CD1
LEU A
118
89.032
10.111
23.527
1.000
33.40

ATOM
760
CD2
LEU A
118
87.757
11.119
23.527
1.000
37.38

ATOM
761
C
LEU A
118
85.746
7.406
23.760
1.000
22.78

ATOM
762
O
LEU A
118
84.604
7.710
23.436
1.000
24.98

ATOM
763
N
ASP A
119
86.218
6.164
23.658
1.000
22.45

ATOM
764
CA
ASP A
119
85.406
5.118
23.056
1.000
22.07

ATOM
765
CB
ASP A
119
86.197
3.806
23.000
1.000
22.13

ATOM
766
CG
ASP A
119
87.190
3.829
21.848
1.000
25.42

ATOM
767
OD1
ASP A
119
87.869
2.807
21.639
1.000
36.77

ATOM
768
OD2
ASP A
119
87.287
4.870
21.172
1.000
26.49

ATOM
769
C
ASP A
119
84.094
4.920
23.796
1.000
27.63

ATOM
770
O
ASP A
119
83.030
4.908
23.177
1.000
24.16

ATOM
771
N
VAL A
120
84.143
4.769
25.119
1.000
24.76

ATOM
772
CA
VAL A
120
82.887
4.553
25.842
1.000
22.84

ATOM
773
CB
VAL A
120
83.139
4.070
27.282
1.000
22.77

ATOM
774
CG1
VAL A
120
81.837
3.978
28.060
1.000
21.91

ATOM
775
CG2
VAL A
120
83.836
2.719
27.288
1.000
25.70

ATOM
776
C
VAL A
120
82.027
5.809
25.873
1.000
18.91

ATOM
777
O
VAL A
120
80.851
5.772
25.508
1.000
24.20

ATOM
778
N
ASN A
121
82.591
6.929
26.299
1.000
16.61

ATOM
779
CA
ASN A
121
81.133
8.133
26.575
1.000
18.33

ATOM
780
CB
ASN A
121
82.687
9.131
27.370
1.000
21.37

ATOM
781
CG
ASN A
121
82.845
8.766
28.830
1.000
25.63

ATOM
782
OD1
ASN A
121
82.362
7.733
29.286
1.000
24.93

ATOM
783
ND2
ASN A
121
83.530
9.649
29.554
1.000
20.70

ATOM
784
C
ASN A
121
81.327
8.853
25.325
1.000
19.73

ATOM
785
O
ASN A
121
80.194
9.344
25.345
1.000
20.54

ATOM
786
N
LEU A
122
82.173
8.935
24.309
1.000
21.10

ATOM
787
CA
LEU A
122
81.869
9.718
23.115
1.000
18.45

ATOM
788
CB
LEU A
122
83.085
10.545
22.703
1.000
19.01

ATOM
789
CG
LEU A
122
82.961
11.441
21.473
1.000
21.55

ATOM
790
CD1
LEU A
122
81.614
12.151
21.431
1.000
19.41

ATOM
791
CD2
LEU A
122
84.086
12.461
21.448
1.000
15.87

ATOM
792
C
LEU A
122
81.422
8.826
21.968
1.000
22.39

ATOM
793
O
LEU A
122
80.294
8.948
21.478
1.000
26.80

ATOM
794
N
MET A
123
82.287
7.917
21.519
1.000
20.44

ATOM
795
CA
MET A
123
81.888
7.004
20.445
1.000
21.80

ATOM
796
CB
MET A
123
83.060
6.098
20.072
1.000
21.27

ATOM
797
CG
MET A
123
82.766
5.105
18.953
1.000
25.44

ATOM
798
SD
MET A
123
82.185
3.504
19.564
1.000
31.17

ATOM
799
CE
MET A
123
83.722
2.836
20.210
1.000
23.57

ATOM
800
C
MET A
123
80.668
6.186
20.853
1.000
26.48

ATOM
801
O
MET A
123
79.736
5.992
20.064
1.000
25.13

ATOM
802
N
GLY A
124
80.656
5.705
22.094
1.000
22.35

ATOM
803
CA
GLY A
124
79.550
4.901
22.591
1.000
23.21

ATOM
804
C
GLY A
124
78.229
5.642
22.491
1.000
27.27

ATOM
805
O
GLY A
124
77.207
5.078
22.095
1.000
23.57

ATOM
806
N
THR A
125
78.256
6.925
22.860
1.000
22.28

ATOM
807
CA
THR A
125
77.045
7.739
22.795
1.000
19.72

ATOM
808
CB
THR A
125
77.255
9.070
23.532
1.000
19.88

ATOM
809
OG1
THR A
125
77.070
8.852
24.945
1.000
22.47

ATOM
810
CG2
THR A
125
76.220
10.106
23.132
1.000
18.39

ATOM
811
C
THR A
125
76.625
7.967
21.343
1.000
22.09

ATOM
812
O
THR A
125
75.439
7.913
21.004
1.000
22.22

ATOM
813
N
PHE A
126
77.573
8.233
20.443
1.000
21.93

ATOM
814
CA
PHE A
126
77.185
8.425
19.041
1.000
23.53

ATOM
815
CB
PHE A
126
78.343
8.986
18.210
1.000
18.23

ATOM
816
CG
PHE A
126
77.956
9.204
16.748
1.000
26.47

ATOM
817
CD1
PHE A
126
77.173
10.285
16.374
1.000
23.71

ATOM
818
CD2
PHE A
126
78.369
8.314
15.770
1.000
28.65

ATOM
819
CE1
PHE A
126
76.824
10.480
15.052
1.000
20.77

ATOM
820
CE2
PHE A
126
78.048
8.518
14.439
1.000
25.27

ATOM
821
CZ
PHE A
126
77.273
9.604
14.708
1.000
21.02

ATOM
822
C
PHE A
126
76.694
7.114
18.432
1.000
21.88

ATOM
823
O
PHE A
126
75.783
7.138
17.606
1.000
21.58

ATOM
824
N
ASN A
127
77.261
5.979
18.820
1.000
21.02

ATOM
825
CA
ASN A
127
76.759
4.686
18.354
1.000
24.14

ATOM
826
CB
ASN A
127
77.568
3.521
18.926
1.000
22.79

ATOM
827
CG
ASN A
127
77.317
2.205
18.218
1.000
28.53

ATOM
828
OD1
ASN A
127
77.052
2.133
17.017
1.000
29.14

ATOM
829
ND2
ASN A
127
77.406
1.109
18.966
1.000
23.91

ATOM
830
C
ASN A
127
75.295
4.488
18.729
1.000
25.90

ATOM
831
O
ASN A
127
74.490
4.051
17.904
1.000
28.86

ATOM
832
N
VAL A
128
74.942
4.799
19.979
1.000
24.12

ATOM
833
CA
VAL A
128
73.540
4.664
20.384
1.000
23.40

ATOM
834
CB
VAL A
128
73.350
4.890
21.893
1.000
24.92

ATOM
835
CG1
VAL A
128
71.874
4.993
22.246
1.000
20.34

ATOM
836
CG2
VAL A
128
74.007
3.759
22.670
1.000
22.63

ATOM
837
C
VAL A
128
72.672
5.641
19.595
1.000
25.23

ATOM
838
O
VAL A
128
71.566
5.294
19.159
1.000
26.49

ATOM
839
N
ILE A
129
73.189
6.861
19.429
1.000
20.97

ATOM
840
CA
ILE A
129
72.408
7.892
18.747
1.000
21.24

ATOM
841
CB
ILE A
129
73.136
9.249
18.751
1.000
20.96

ATOM
842
CG2
ILE A
129
72.554
10.167
17.682
1.000
17.73

ATOM
843
CG1
ILE A
129
73.138
9.927
20.124
1.000
17.73

ATOM
844
CD1
ILE A
129
73.850
11.258
20.195
1.000
19.83

ATOM
845
C
ILE A
129
72.092
7.495
17.314
1.000
23.42

ATOM
846
O
ILE A
129
70.950
7.589
16.864
1.000
24.98

ATOM
847
N
ARG A
130
73.100
7.041
16.577
1.000
22.21

ATOM
848
CA
ARG A
130
72.896
6.800
15.146
1.000
23.59

ATOM
849
CB
ARG A
130
74.246
6.567
14.467
1.000
21.91

ATOM
850
CG
ARG A
130
74.743
5.138
14.544
1.000
20.59

ATOM
851
CD
ARG A
130
76.260
5.024
14.349
1.000
20.58

ATOM
852
CZ
ARG A
130
76.675
3.671
14.727
1.000
25.06

ATOM
853
NE
ARG A
130
76.637
2.621
13.913
1.000
26.85

ATOM
854
NH1
ARG A
130
77.028
1.433
14.360
1.000
23.90

ATOM
855
NH2
ARG A
130
76.220
2.741
12.659
1.000
20.62

ATOM
856
C
ARG A
130
71.944
5.632
14.904
1.000
28.92

ATOM
857
O
ARG A
130
71.179
5.628
13.932
1.000
23.14

ATOM
858
N
LEU A
131
71.989
4.638
15.783
1.000
25.17

ATOM
859
CA
LEU A
131
71.155
3.452
15.636
1.000
26.41

ATOM
860
CB
LEU A
131
71.766
2.270
16.394
1.000
25.84

ATOM
861
CG
LEU A
131
73.124
1.753
15.921
1.000
28.03

ATOM
862
CD1
LEU A
131
73.678
0.706
16.878
1.000
31.36

ATOM
863
CD2
LEU A
131
73.010
1.186
14.512
1.000
32.31

ATOM
864
C
LEU A
131
69.730
3.723
16.110
1.000
28.46

ATOM
865
O
LEU A
131
68.749
3.359
15.463
1.000
24.94

ATOM
866
N
VAL A
132
69.582
4.386
17.257
1.000
22.13

ATOM
867
CA
VAL A
132
68.250
4.675
17.733
1.000
18.99

ATOM
868
CB
VAL A
132
68.258
5.172
19.228
1.000
22.45

ATOM
869
CG1
VAL A
132
68.598
6.653
19.308
1.000
22.79

ATOM
870
CG2
VAL A
132
66.902
4.903
19.873
1.000
23.15

ATOM
871
C
VAL A
132
67.548
5.705
16.896
1.000
23.29

ATOM
872
O
VAL A
132
66.314
5.691
16.833
1.000
28.24

ATOM
873
N
ALA A
133
68.292
6.586
16.229
1.000
20.41

ATOM
874
CA
ALA A
133
67.650
7.522
15.304
1.000
23.10

ATOM
875
CB
ALA A
133
68.671
8.475
14.697
1.000
21.23

ATOM
876
C
ALA A
133
66.891
6.777
14.209
1.000
24.68

ATOM
877
O
ALA A
133
68.772
7.133
13.844
1.000
23.73

ATOM
878
N
GLY A
134
67.494
5.719
13.666
1.000
27.05

ATOM
879
CA
GLY A
134
66.830
4.933
12.634
1.000
31.03

ATOM
880
C
GLY A
134
65.602
4.225
13.168
1.000
34.82

ATOM
881
O
GLY A
134
64.647
3.969
12.436
1.000
33.45

ATOM
882
N
GLU A
135
65.593
3.877
14.455
1.000
32.85

ATOM
883
CA
GLU A
135
64.406
3.276
15.056
1.000
28.48

ATOM
884
CB
GLU A
135
64.737
2.662
16.414
1.000
27.36

ATOM
885
CG
GLU A
135
65.749
1.534
16.374
1.000
30.53

ATOM
886
CD
GLU A
135
65.173
0.289
15.721
1.000
35.24

ATOM
887
OE1
GLU A
135
65.894
−0.377
14.955
1.000
46.65

ATOM
888
OE1
GLU A
135
63.990
−0.011
15.987
1.000
45.16

ATOM
889
C
GLU A
135
63.300
4.312
15.218
1.000
28.72

ATOM
890
O
GLU A
135
62.128
4.062
14.943
1.000
30.55

ATOM
891
N
MET A
136
63.662
5.510
15.681
1.000
22.47

ATOM
892
CA
MET A
136
62.637
6.534
15.868
1.000
22.92

ATOM
893
CB
MET A
136
63.185
7.726
16.656
1.000
25.85

ATOM
894
CG
MET A
136
63.669
7.411
18.066
1.000
28.30

ATOM
895
SD
MET A
136
64.718
8.715
18.754
1.000
25.89

ATOM
896
CE
MET A
136
64.988
8.067
20.408
1.000
23.78

ATOM
897
C
MET A
136
62.095
6.992
14.519
1.000
21.98

ATOM
898
O
MET A
136
60.937
7.374
14.392
1.000
28.43

ATOM
899
N
GLY A
137
62.925
6.971
13.477
1.000
24.89

ATOM
900
CA
GLY A
137
62.492
7.463
12.174
1.000
28.70

ATOM
901
C
GLY A
137
61.344
6.642
11.616
1.000
33.98

ATOM
902
O
GLY A
137
60.627
7.094
10.717
1.000
35.20

ATOM
903
N
GLN A
138
61.158
5.439
12.134
1.000
28.41

ATOM
904
CA
GLN A
138
60.034
4.585
11.795
1.000
29.57

ATOM
905
CB
GLN A
138
60.413
3.124
12.014
1.000
33.29

ATOM
906
C
GLN A
138
58.798
4.942
12.606
1.000
33.23

ATOM
907
O
GLN A
138
57.700
4.431
12.349
1.000
36.19

ATOM
908
N
ASN A
139
58.901
5.817
13.613
1.000
30.84

ATOM
909
CA
ASN A
139
57.673
6.225
14.290
1.000
29.71

ATOM
910
CB
ASN A
139
57.951
6.918
15.616
1.000
30.72

ATOM
911
CG
ASN A
139
58.539
6.044
16.695
1.000
34.82

ATOM
912
OD1
ASN A
139
58.309
4.840
16.748
1.000
33.24

ATOM
913
ND2
ASN A
139
59.316
6.643
17.599
1.000
27.65

ATOM
914
C
ASN A
139
56.873
7.178
13.405
1.000
32.55

ATOM
915
O
ASN A
139
57.442
7.999
12.686
1.000
31.43

ATOM
916
N
GLU A
140
55.545
7.095
13.455
1.000
32.34

ATOM
917
CA
GLU A
140
54.765
8.130
12.765
1.000
33.47

ATOM
918
CB
GLU A
140
53.338
7.698
12.521
1.000
37.78

ATOM
919
C
GLU A
140
54.829
9.390
13.622
1.000
33.02

ATOM
920
O
GLU A
140
54.685
9.297
14.848
1.000
31.57

ATOM
921
N
PRO A
141
55.053
10.552
13.029
1.000
31.82

ATOM
922
CD
PRO A
141
55.197
10.833
11.595
1.000
30.12

ATOM
923
CA
PRO A
141
55.180
11.763
13.850
1.000
30.60

ATOM
924
CB
PRO A
141
55.411
12.868
12.821
1.000
32.30

ATOM
925
CG
PRO A
141
55.887
12.174
11.595
1.000
31.21

ATOM
926
C
PRO A
141
53.892
12.026
14.618
1.000
37.04

ATOM
927
O
PRO A
141
52.792
11.743
14.141
1.000
38.85

ATOM
928
N
ASP A
142
54.021
12.576
15.821
1.000
32.62

ATOM
929
CA
ASP A
142
52.834
13.005
16.551
1.000
30.09

ATOM
930
CB
ASP A
142
53.157
13.277
18.011
1.000
33.63

ATOM
931
CG
ASP A
142
54.244
14.306
18.230
1.000
34.93

ATOM
932
OD1
ASP A
142
54.390
15.234
17.410
1.000
25.78

ATOM
933
OD2
ASP A
142
54.970
14.201
19.245
1.000
35.97

ATOM
934
C
ASP A
142
52.264
14.255
15.881
1.000
35.02

ATOM
935
O
ASP A
142
52.772
14.699
14.848
1.000
29.85

ATOM
936
N
GLN A
143
51.224
14.806
16.494
1.000
33.99

ATOM
937
CA
GLN A
143
50.579
16.007
15.990
1.000
38.09

ATOM
938
CB
GLN A
143
49.401
16.380
16.884
1.000
38.12

ATOM
939
C
GLN A
143
51.547
17.178
15.890
1.000
40.07

ATOM
940
O
GLN A
143
51.283
18.129
15.148
1.000
37.88

ATOM
941
N
GLY A
144
52.656
17.131
16.625
1.000
34.69

ATOM
942
CA
GLY A
144
53.618
18.218
16.584
1.000
30.50

ATOM
943
C
GLY A
144
54.788
17.941
15.657
1.000
30.57

ATOM
944
O
GLY A
144
55.778
18.668
15.666
1.000
30.79

ATOM
945
N
GLY A
145
54.672
16.890
14.857
1.000
28.63

ATOM
946
CA
GLY A
145
55.684
16.503
13.902
1.000
26.20

ATOM
947
C
GLY A
145
56.793
15.676
14.508
1.000
26.99

ATOM
948
O
GLY A
145
57.758
15.304
13.841
1.000
25.11

ATOM
949
N
GLN A
146
56.698
15.370
15.797
1.000
26.86

ATOM
950
CA
GLN A
146
57.832
14.756
16.482
1.000
26.54

ATOM
951
CB
GLN A
146
57.877
15.283
17.926
1.000
26.88

ATOM
952
CG
GLN A
146
59.203
14.976
18.615
1.000
31.74

ATOM
953
CD
GLN A
146
59.200
15.449
20.057
1.000
29.31

ATOM
954
OE1
GLN A
146
59.518
16.613
20.289
1.000
27.82

ATOM
955
NE2
GLN A
146
58.846
14.565
20.986
1.000
26.30

ATOM
956
C
GLN A
146
57.794
13.239
16.479
1.000
27.53

ATOM
957
O
GLN A
146
56.743
12.629
16.690
1.000
29.32

ATOM
958
N
ARG A
147
58.957
12.634
16.643
1.000
22.43

ATOM
959
CA
ARG A
147
59.134
11.200
16.208
1.000
20.85

ATOM
960
CB
ARG A
147
59.862
10.761
14.937
1.000
22.13

ATOM
961
CG
ARG A
147
59.043
10.766
13.663
1.000
23.35

ATOM
962
CD
ARG A
147
59.897
10.222
12.520
1.000
26.83

ATOM
963
NE
ARG A
147
59.101
10.004
11.309
1.000
28.18

ATOM
964
CZ
ARG A
147
59.049
10.883
10.313
1.000
32.45

ATOM
965
NH1
ARG A
147
58.306
10.621
9.246
1.000
37.01

ATOM
966
NH2
ARG A
147
59.736
12.015
10.385
1.000
28.29

ATOM
967
C
ARG A
147
59.968
10.684
17.380
1.000
27.24

ATOM
968
O
ARG A
147
59.901
9.498
17.710
1.000
25.10

ATOM
969
N
GLY A
148
60.776
11.548
17.994
1.000
25.61

ATOM
970
CA
GLY A
148
61.684
11.059
19.019
1.000
24.15

ATOM
971
C
GLY A
148
62.366
12.198
19.761
1.000
25.59

ATOM
972
O
GLY A
148
62.322
13.322
19.276
1.000
22.65

ATOM
973
N
VAL A
149
62.915
11.884
20.929
1.000
23.40

ATOM
974
CA
VAL A
149
63.767
12.768
21.704
1.000
22.36

ATOM
975
CB
VAL A
149
63.054
13.362
22.930
1.000
22.74

ATOM
976
CG1
VAL A
149
63.922
14.438
23.584
1.000
25.25

ATOM
977
CG2
VAL A
149
61.703
13.937
22.539
1.000
29.65

ATOM
978
C
VAL A
149
65.016
12.010
22.150
1.000
22.55

ATOM
979
O
VAL A
149
64.954
10.907
22.666
1.000
20.35

ATOM
980
N
ILE A
150
66.183
12.602
21.951
1.000
24.00

ATOM
981
CA
ILE A
150
67.442
12.020
22.398
1.000
22.32

ATOM
982
CB
ILE A
150
68.377
11.695
21.220
1.000
24.31

ATOM
983
CG2
ILE A
150
69.729
11.203
21.721
1.000
22.61

ATOM
984
CG1
ILE A
150
67.770
10.709
20.223
1.000
21.68

ATOM
985
CD1
ILE A
150
68.649
10.447
19.019
1.000
23.99

ATOM
986
C
ILE A
150
68.127
12.991
23.356
1.000
23.92

ATOM
987
O
ILE A
150
68.657
14.172
23.041
1.000
23.96

ATOM
988
N
ILE A
151
68.538
12.488
24.512
1.000
20.89

ATOM
989
CA
ILE A
151
69.131
13.304
25.564
1.000
18.19

ATOM
990
CB
ILE A
151
68.303
13.414
26.786
1.000
19.91

ATOM
991
CG2
ILE A
151
68.801
14.266
27.888
1.000
15.01

ATOM
992
CG1
ILE A
151
66.808
13.944
26.428
1.000
23.45

ATOM
993
CD1
ILE A
151
65.805
13.843
27.556
1.000
24.66

ATOM
994
C
ILE A
151
70.462
12.689
25.972
1.000
21.60

ATOM
995
O
ILE A
151
70.484
11.519
26.366
1.000
22.74

ATOM
996
N
ASN A
152
71.524
13.476
25.847
1.000
20.63

ATOM
997
CA
ASN A
152
72.867
12.980
26.113
1.000
18.99

ATOM
998
CB
ASN A
152
73.836
13.384
24.992
1.000
19.22

ATOM
999
CG
ASN A
152
73.211
13.074
23.637
1.000
20.09

ATOM
1000
OD1
ASN A
152
72.912
13.977
22.856
1.000
33.18

ATOM
1001
ND2
ASN A
152
73.017
11.795
23.386
1.000
15.75

ATOM
1002
C
ASN A
152
73.395
13.517
27.437
1.000
22.55

ATOM
1003
O
ASN A
152
72.860
14.512
27.943
1.000
21.43

ATOM
1004
N
THR A
153
74.438
12.854
27.944
1.000
21.33

ATOM
1005
CA
THR A
153
75.076
13.367
29.150
1.000
19.67

ATOM
1006
CB
THR A
153
75.042
12.363
30.311
1.000
20.60

ATOM
1007
OG1
THR A
153
73.730
11.801
30.437
1.000
20.29

ATOM
1008
CG2
THR A
153
75.315
13.093
31.620
1.000
20.24

ATOM
1009
C
THR A
153
76.520
13.771
28.857
1.000
20.09

ATOM
1010
O
THR A
153
77.336
12.925
28.497
1.000
20.49

ATOM
1011
N
ALA A
154
76.797
15.058
29.012
1.000
17.99

ATOM
1012
CA
ALA A
154
78.157
15.580
28.941
1.000
21.71

ATOM
1013
CB
ALA A
154
78.230
16.698
28.183
1.000
15.72

ATOM
1014
C
ALA A
154
78.678
15.745
30.366
1.000
18.97

ATOM
1015
O
ALA A
154
78.650
14.795
31.141
1.000
21.19

ATOM
1016
N
SER A
155
79.124
16.935
30.721
1.000
22.57

ATOM
1017
CA
SER A
155
79.663
17.252
32.041
1.000
19.46

ATOM
1018
CB
SER A
155
80.837
16.336
32.389
1.000
20.68

ATOM
1019
OG
SER A
155
81.569
16.832
33.512
1.000
19.92

ATOM
1020
C
SER A
155
80.132
18.969
32.066
1.000
19.44

ATOM
1021
O
SER A
155
80.451
19.246
31.008
1.000
18.95

ATOM
1022
N
VAL A
156
80.226
19.329
33.240
1.000
17.21

ATOM
1023
CA
VAL A
156
80.827
20.659
33.282
1.000
16.12

ATOM
1024
CB
VAL A
156
80.606
21.359
34.638
1.000
22.05

ATOM
1025
CG1
VAL A
156
79.111
21.526
34.908
1.000
23.71

ATOM
1026
CG2
VAL A
156
81.286
20.596
35.758
1.000
23.52

ATOM
1027
C
VAL A
156
82.320
20.593
32.977
1.000
15.83

ATOM
1028
O
VAL A
156
82.948
21.638
32.780
1.000
18.99

ATOM
1029
N
ALA A
157
82.900
19.397
32.941
1.000
17.17

ATOM
1030
CA
ALA A
157
84.294
19.227
35.522
1.000
17.12

ATOM
1031
CB
ALA A
157
84.783
17.824
32.831
1.000
14.53

ATOM
1032
C
ALA A
157
84.460
19.540
31.038
1.000
21.86

ATOM
1033
O
ALA A
157
85.573
19.705
30.542
1.000
22.45

ATOM
1034
N
ALA A
158
83.369
19.638
30.292
1.000
21.67

ATOM
1035
CA
ALA A
158
83.424
20.098
28.902
1.000
21.61

ATOM
1036
CB
ALA A
158
82.081
19.902
28.225
1.000
18.71

ATOM
1037
C
ALA A
158
83.835
21.561
28.856
1.000
21.63

ATOM
1038
O
ALA A
158
84.331
22.076
27.858
1.000
21.79

ATOM
1039
N
PHE A
159
83.621
22.268
22.969
1.000
18.53

ATOM
1040
CA
PHE A
159
83.861
23.702
30.013
1.000
21.39

ATOM
1041
CB
PHE A
159
82.558
24.436
30.386
1.000
22.21

ATOM
1042
CG
PHE A
159
81.370
24.032
29.536
1.000
23.73

ATOM
1043
CD1
PHE A
159
80.333
23.289
30.067
1.000
23.69

ATOM
1044
CD2
PHE A
159
81.317
24.402
28.204
1.000
24.10

ATOM
1045
CE1
PHE A
159
79.251
22.908
29.283
1.000
23.62

ATOM
1046
CE2
PHE A
159
80.237
24.032
27.419
1.000
26.19

ATOM
1047
CZ
PHE A
159
79.204
23.293
27.960
1.000
22.24

ATOM
1048
C
PHE A
159
84.949
21.110
30.997
1.000
24.75

ATOM
1049
O
PHE A
159
85.636
25.110
30.780
1.000
22.24

ATOM
1050
N
GLU A
160
85.118
23.285
32.097
1.000
22.83

ATOM
1051
CA
GLU A
160
86.123
23.705
33.102
1.000
24.53

ATOM
1052
CB
GLU A
160
85.536
24.348
34.355
1.000
26.40

ATOM
1053
CG
GLU A
160
84.785
25.647
34.193
1.000
31.12

ATOM
1054
CD
GLU A
160
83.296
25.519
34.442
1.000
34.00

ATOM
1055
OE1
GLU A
160
82.527
26.110
33.652
1.000
30.58

ATOM
1056
OE2
GLU A
160
82.858
24.845
35.397
1.000
25.33

ATOM
1057
C
GLU A
160
86.865
22.434
33.526
1.000
22.82

ATOM
1058
O
GLU A
160
86.876
22.118
34.722
1.000
22.77

ATOM
1059
N
GLY A
161
87.450
21.730
32.560
1.000
17.77

ATOM
1060
CA
GLY A
161
88.190
20.511
32.844
1.000
20.11

ATOM
1061
C
GLY A
161
89.207
20.771
33.988
1.000
22.40

ATOM
1062
O
GLY A
161
89.925
21.771
33.954
1.000
19.29

ATOM
1063
N
GLN A
162
89.250
19.898
34.986
1.000
21.52

ATOM
1064
CA
GLN A
162
90.173
20.050
36.106
1.000
24.64

ATOM
1065
CB
GLN A
162
89.554
19.454
37.375
1.000
21.82

ATOM
1066
CG
GLN A
162
88.342
20.197
37.909
1.000
23.34

ATOM
1067
CD
GLN A
162
88.026
19.778
39.341
1.000
25.33

ATOM
1068
OE1
GLN A
162
87.431
18.723
39.550
1.000
25.69

ATOM
1069
NE2
GLN A
162
88.428
20.600
40.306
1.000
21.01

ATOM
1070
C
GLN A
162
91.495
19.343
35.833
1.000
24.73

ATOM
1071
O
GLN A
162
91.586
18.564
34.881
1.000
21.61

ATOM
1072
N
VAL A
163
92.483
19.598
36.690
1.000
22.60

ATOM
1073
CA
VAL A
163
93.739
18.841
36.572
1.000
22.73

ATOM
1074
CB
VAL A
163
94.752
19.204
37.667
1.000
20.09

ATOM
1075
CG1
VAL A
163
95.932
18.237
37.643
1.000
22.25

ATOM
1076
CG2
VAL A
163
95.233
20.641
37.504
1.000
14.78

ATOM
1077
C
VAL A
163
93.436
17.350
36.637
1.000
23.33

ATOM
1078
O
VAL A
163
92.734
16.916
37.552
1.000
26.46

ATOM
1079
N
GLY A
164
93.925
16.560
35.692
1.000
20.35

ATOM
1080
CA
GLY A
164
93.645
15.138
35.560
1.000
19.48

ATOM
1081
C
GLY A
164
92.459
14.754
34.783
1.000
23.54

ATOM
1082
O
GLY A
164
92.222
13.560
34.572
1.000
22.45

ATOM
1083
N
GLN A
165
91.689
15.709
34.263
1.000
21.33

ATOM
1084
CA
GLN A
165
90.485
15.381
33.506
1.000
22.94

ATOM
1085
CB
GLN A
165
89.313
16.245
33.986
1.000
22.47

ATOM
1086
CG
GLN A
165
88.735
15.870
35.337
1.000
26.75

ATOM
1087
CD
GLN A
165
87.425
16.603
35.591
1.000
28.68

ATOM
1088
OE1
GLN A
165
87.305
17.805
35.337
1.000
24.50

ATOM
1089
NE2
GLN A
165
86.442
15.866
36.091
1.000
28.31

ATOM
1090
C
GLN A
165
90.598
15.595
32.002
1.000
25.31

ATOM
1091
O
GLN A
165
89.564
31.325
31.325
1.000
24.16

ATOM
1092
N
ALA A
166
91.795
15.645
31.432
1.000
20.17

ATOM
1093
CA
ALA A
166
91.934
15.880
29.992
1.000
19.87

ATOM
1094
CB
ALA A
166
93.411
15.881
29.620
1.000
21.17

ATOM
1095
C
ALA A
166
91.166
14.870
29.156
1.000
22.80

ATOM
1096
O
ALA A
166
90.404
15.240
28.254
1.000
23.88

ATOM
1097
N
ALA A
167
91.325
13.572
29.410
1.000
20.76

ATOM
1098
CA
ALA A
167
90.598
12.576
28.619
1.000
18.57

ATOM
1099
CB
ALA A
167
91.081
11.188
28.998
1.000
20.24

ATOM
1100
C
ALA A
167
89.093
12.682
28.810
1.000
22.84

ATOM
1101
O
ALA A
167
88.305
12.642
27.866
1.000
21.97

ATOM
1102
N
TYR A
168
88.644
12.808
30.059
1.000
19.71

ATOM
1103
CA
TYR A
168
87.244
12.964
30.346
1.000
18.72

ATOM
1104
CB
TYR A
168
86.990
13.100
31.854
1.000
19.50

ATOM
1105
CG
TYR A
168
85.552
12.961
32.315
1.000
17.69

ATOM
1106
CD1
TYR A
168
84.865
11.762
32.189
1.000
19.32

ATOM
1107
CE1
TYR A
168
83.554
11.634
32.611
1.000
19.30

ATOM
1108
CD2
TYR A
168
84.887
14.038
32.890
1.000
16.32

ATOM
1109
CE2
TYR A
168
83.574
13.929
33.324
1.000
18.41

ATOM
1110
CZ
TYR A
168
82.919
12.724
33.181
1.000
22.12

ATOM
1111
OH
TYR A
168
81.616
12.584
33.603
1.000
21.21

ATOM
1112
C
TYR A
168
86.651
14.186
29.630
1.000
21.33

ATOM
1113
O
TYR A
168
85.593
14.116
29.009
1.000
21.12

ATOM
1114
N
SER A
169
87.367
15.294
29.741
1.000
18.05

ATOM
1115
CA
SER A
169
86.938
16.572
29.194
1.000
17.88

ATOM
1116
CB
SER A
169
87.876
17.706
29.606
1.000
19.40

ATOM
1117
OG
SER A
169
87.889
17.932
31.008
1.000
20.81

ATOM
1118
C
SER A
169
86.848
16.499
27.667
1.000
22.37

ATOM
1119
O
SER A
169
85.950
17.101
27.079
1.000
22.30

ATOM
1120
N
ALA A
170
87.787
15.770
27.080
1.000
21.43

ATOM
1121
CA
ALA A
170
87.820
15.524
25.643
1.000
20.27

ATOM
1122
CB
ALA A
170
89.051
14.700
25.279
1.000
17.19

ATOM
1123
C
ALA A
170
86.552
14.801
25.203
1.000
23.52

ATOM
1124
O
ALA A
170
85.894
15.162
24.229
1.000
21.45

ATOM
1125
N
SER A
171
86.204
13.754
25.947
1.000
18.86

ATOM
1126
CA
SER A
171
85.032
12.950
25.622
1.000
17.10

ATOM
1127
CB
SER A
171
85.051
11.681
26.473
1.000
18.30

ATOM
1128
OG
SER A
171
84.557
11.914
27.786
1.000
22.04

ATOM
1129
C
SER A
171
83.740
13.735
25.811
1.000
22.12

ATOM
1130
O
SER A
171
82.803
13.603
25.015
1.000
23.65

ATOM
1131
N
LYS A
172
83.668
14.564
26.858
1.000
17.81

ATOM
1132
CA
LYS A
172
82.442
15.323
27.110
1.000
20.04

ATOM
1133
CB
LYS A
172
82.330
15.703
28.592
1.000
18.29

ATOM
1134
CG
LYS A
172
82.267
14.485
29.505
1.000
17.34

ATOM
1135
CD
LYS A
172
81.143
13.533
29.128
1.000
21.47

ATOM
1136
CE
LYS A
172
80.971
12.469
30.211
1.000
19.97

ATOM
1137
NZ
LYS A
172
79.740
11.651
30.012
1.000
16.10

ATOM
1138
C
LYS A
172
82.365
16.563
26.232
1.000
21.83

ATOM
1139
O
LYS A
172
81.282
16.962
25.804
1.000
20.78

ATOM
1140
N
GLY A
173
83.501
17.189
25.934
1.000
20.14

ATOM
1141
CA
GLY A
173
83.504
18.311
25.002
1.000
19.14

ATOM
1142
C
GLY A
173
83.042
17.843
23.623
1.000
22.28

ATOM
1143
O
GLY A
173
82.382
18.601
22.905
1.000
20.41

ATOM
1144
N
GLY A
174
83.399
16.599
23.295
1.000
18.15

ATOM
1145
CA
GLY A
174
82.918
15.952
22.083
1.000
19.24

ATOM
1146
C
GLY A
174
81.397
15.897
22.049
1.000
23.10

ATOM
1147
O
GLY A
174
80.746
16.228
21.053
1.000
18.74

ATOM
1148
N
ILE A
175
80.801
15.470
23.165
1.000
23.71

ATOM
1149
CA
ILE A
175
79.344
15.374
23.240
1.000
18.13

ATOM
1150
CB
ILE A
175
78.859
14.808
24.585
1.000
22.59

ATOM
1151
CG2
ILE A
175
77.333
14.772
24.601
1.000
19.28

ATOM
1152
CG1
ILE A
175
79.439
13.444
24.954
1.000
21.35

ATOM
1153
CD1
ILE A
175
78.870
12.312
24.142
1.000
29.59

ATOM
1154
C
ILE A
175
78.710
16.741
23.050
1.000
20.98

ATOM
1155
O
ILE A
175
77.720
16.959
22.343
1.000
22.66

ATOM
1156
N
VAL A
176
79.321
17.723
23.727
1.000
14.93

ATOM
1157
CA
VAL A
176
78.799
19.079
23.568
1.000
13.95

ATOM
1158
CB
VAL A
176
79.535
20.078
24.467
1.000
20.03

ATOM
1159
CG1
VAL A
176
79.154
21.504
24.109
1.000
18.47

ATOM
1160
CG2
VAL A
176
79.229
19.794
25.936
1.000
18.79

ATOM
1161
C
VAL A
176
78.897
19.488
22.105
1.000
19.79

ATOM
1162
O
VAL A
176
77.916
19.919
21.505
1.000
20.43

ATOM
1163
N
GLY A
177
80.074
19.348
21.490
1.000
20.46

ATOM
1164
CA
GLY A
177
80.236
19.823
20.125
1.000
20.42

ATOM
1165
C
GLY A
177
79.334
19.148
19.115
1.000
23.30

ATOM
1166
O
GLY A
177
78.913
19.781
18.138
1.000
22.67

ATOM
1167
N
MET A
178
78.997
17.869
19.277
1.000
19.64

ATOM
1168
CA
MET A
178
78.174
17.239
18.244
1.000
18.59

ATOM
1169
CB
MET A
178
78.527
15.754
18.109
1.000
18.46

ATOM
1170
CG
MET A
178
78.124
14.883
19.283
1.000
21.01

ATOM
1171
SD
MET A
178
78.675
13.176
19.081
1.000
24.29

ATOM
1172
CE
MET A
178
77.901
12.383
20.486
1.000
18.63

ATOM
1173
C
MET A
178
76.677
17.381
18.498
1.000
21.98

ATOM
1174
O
MET A
178
75.854
16.917
17.703
1.000
22.55

ATOM
1175
N
THR A
179
76.303
18.020
19.601
1.000
18.53

ATOM
1176
CA
THR A
179
74.882
18.192
19.915
1.000
18.51

ATOM
1177
CB
THR A
179
74.719
18.925
21.266
1.000
19.84

ATOM
1178
OG1
THR A
179
75.155
18.062
22.331
1.000
18.46

ATOM
1179
CG2
THR A
179
73.261
19.271
21.537
1.000
15.79

ATOM
1180
C
THR A
179
74.148
18.940
18.813
1.000
23.20

ATOM
1181
O
THR A
179
73.114
18.480
18.315
1.000
21.33

ATOM
1182
N
LEU A
180
74.649
20.099
18.396
1.000
21.40

ATOM
1183
CA
LEU A
180
73.940
20.900
17.400
1.000
20.22

ATOM
1184
CB
LEU A
180
74.563
22.297
17.303
1.000
17.06

ATOM
1185
CG
LEU A
180
73.884
23.245
16.308
1.000
23.58

ATOM
1186
CD1
LEU A
180
72.454
23.531
16.740
1.000
24.53

ATOM
1187
CD2
LEU A
180
74.683
24.531
16.158
1.000
21.92

ATOM
1188
C
LEU A
180
73.906
20.253
16.020
1.000
18.83

ATOM
1189
O
LEU A
180
72.827
20.176
15.421
1.000
22.66

ATOM
1190
N
PRO A
181
75.022
19.807
15.460
1.000
20.32

ATOM
1191
CD
PRO A
181
76.403
19.915
15.952
1.000
19.33

ATOM
1192
CA
PRO A
181
74.976
19.137
14.148
1.000
20.68

ATOM
1193
CB
PRO A
181
76.411
18.645
13.926
1.000
22.44

ATOM
1194
CG
PRO A
181
77.074
18.748
15.264
1.000
20.59

ATOM
1195
C
PRO A
181
74.034
17.943
14.120
1.000
27.41

ATOM
1196
O
PRO A
181
73.304
17.744
13.139
1.000
22.18

ATOM
1197
N
ILE A
182
74.023
17.111
15.168
1.000
20.68

ATOM
1198
CA
ILE A
182
73.095
15.976
15.144
1.000
18.87

ATOM
1199
CB
ILE A
182
73.354
14.981
16.283
1.000
18.97

ATOM
1200
CG2
ILE A
182
72.317
13.868
16.266
1.000
19.51

ATOM
1201
CG1
ILE A
182
74.760
14.380
16.254
1.000
19.27

ATOM
1202
CD1
ILE A
182
75.128
13.520
17.437
1.000
20.55

ATOM
1203
C
ILE A
182
74.660
16.499
15.170
1.000
23.55

ATOM
1204
O
ILE A
182
70.825
16.022
14.398
1.000
23.85

ATOM
1205
N
ALA A
183
71.390
17.490
16.026
1.000
19.15

ATOM
1206
CA
ALA A
183
70.071
18.126
16.012
1.000
20.67

ATOM
1207
CB
ALA A
183
70.005
19.247
17.039
1.000
20.13

ATOM
1208
C
ALA A
183
69.758
18.656
14.611
1.000
25.01

ATOM
1209
O
ALA A
183
68.653
18.519
14.087
1.000
21.56

ATOM
1210
N
ARG A
184
70.739
19.287
13.962
1.000
21.73

ATOM
1211
CA
ARG A
184
70.485
19.799
12.610
1.000
21.73

ATOM
1212
CB
ARG A
184
71.642
20.679
12.134
1.000
17.36

ATOM
1213
CG
ARG A
184
71.779
21.973
12.907
1.000
16.93

ATOM
1214
CD
ARG A
184
73.039
22.748
12.567
1.000
17.35

ATOM
1215
NE
ARG A
184
72.915
24.175
12.842
1.000
21.03

ATOM
1216
CZ
ARG A
184
73.838
25.093
12.581
1.000
20.96

ATOM
1217
NH1
ARG A
184
73.645
23.374
12.864
1.000
18.08

ATOM
1218
NH2
ARG A
184
75.000
24.762
12.025
1.000
20.87

ATOM
1219
C
ARG A
184
70.038
18.626
11.667
1.000
21.16

ATOM
1220
O
ARG A
184
69.317
18.667
10.841
1.000
21.06

ATOM
1221
N
ASP A
185
71.030
17.564
11.799
1.000
16.34

ATOM
1222
CA
ASP A
185
70.844
16.368
10.987
1.000
19.85

ATOM
1223
CB
ASP A
185
71.782
15.251
11.432
1.000
21.41

ATOM
1224
CG
ASP A
185
73.175
15.269
10.850
1.000
24.87

ATOM
1225
OD1
ASP A
185
73.959
14.367
11.247
1.000
21.48

ATOM
1226
OD2
ASP A
185
73.527
16.130
10.020
1.000
18.18

ATOM
1227
C
ASP A
185
69.419
15.818
11.060
1.000
26.43

ATOM
1228
O
ASP A
185
68.808
15.496
10.036
1.000
20.25

ATOM
1229
N
LEU A
186
69.893
15.689
12.282
1.000
20.78

ATOM
1230
CA
LEU A
186
67.630
14.992
12.483
1.000
20.72

ATOM
1231
CB
LEU A
186
67.689
14.210
13.806
1.000
20.73

ATOM
1232
CG
LEU A
186
68.918
13.319
13.997
1.000
22.47

ATOM
1233
CD1
LEU A
186
68.781
12.514
15.282
1.000
20.41

ATOM
1234
CD2
LEU A
186
69.120
12.401
12.799
1.000
19.86

ATOM
1235
C
LEU A
186
66.411
15.900
12.496
1.000
22.45

ATOM
1236
O
LEU A
186
65.263
15.440
12.554
1.000
24.25

ATOM
1237
N
ALA A
187
66.624
17.210
12.453
1.000
15.94

ATOM
1238
CA
ALA A
187
65.484
18.127
12.463
1.000
18.11

ATOM
1239
CB
ALA A
187
65.992
19.563
12.429
1.000
15.41

ATOM
1240
C
ALA A
187
64.490
17.852
11.344
1.000
24.07

ATOM
1241
O
ALA A
187
63.275
17.911
11.601
1.000
24.26

ATOM
1242
N
PRO A
188
64.865
17.560
10.109
1.000
27.53

ATOM
1243
CD
PRO A
188
66.210
17.517
9.510
1.000
30.77

ATOM
1244
CA
PRO A
188
63.843
17.246
9.097
1.000
28.68

ATOM
1245
CB
PRO A
188
64.660
16.872
7.848
1.000
28.47

ATOM
1246
CG
PRO A
188
65.927
17.649
8.036
1.000
32.25

ATOM
1247
C
PRO A
188
62.971
16.066
9.471
1.000
32.36

ATOM
1248
O
PRO A
188
61.897
15.882
8.886
1.000
30.80

ATOM
1249
N
ILE A
189
63.381
15.222
10.423
1.000
27.68

ATOM
1250
CA
ILE A
189
62.466
14.100
10.677
1.000
27.31

ATOM
1251
CB
ILE A
189
63.133
12.746
10.415
1.000
31.22

ATOM
1252
CG2
ILE A
189
63.458
12.582
8.932
1.000
36.22

ATOM
1253
CG1
ILE A
189
64.389
12.443
11.227
1.000
27.19

ATOM
1254
CD1
ILE A
189
64.885
11.011
11.005
1.000
28.72

ATOM
1255
C
ILE A
189
61.890
14.171
12.088
1.000
23.39

ATOM
1256
O
ILE A
189
61.367
13.198
12.633
1.000
25.26

ATOM
1257
N
GLY A
190
61.973
15.530
12.696
1.000
18.90

ATOM
1258
CA
GLY A
190
61.345
15.608
13.970
1.000
20.72

ATOM
1259
C
GLY A
190
61.925
14.880
15.159
1.000
23.61

ATOM
1260
O
GLY A
190
61.202
14.431
16.052
1.000
25.17

ATOM
1261
N
ILE A
191
63.248
14.742
15.202
1.000
20.22

ATOM
1262
CA
ILE A
191
63.887
14.146
16.375
1.000
20.80

ATOM
1263
CB
ILE A
191
64.762
12.938
16.021
1.000
20.20

ATOM
1264
CG2
ILE A
191
62.535
12.457
17.243
1.000
23.67

ATOM
1265
CG1
ILE A
191
63.978
11.784
15.393
1.000
21.41

ATOM
1266
CD1
ILE A
191
64.857
10.645
14.911
1.000
20.93

ATOM
1267
C
ILE A
191
64.730
15.216
17.070
1.000
23.22

ATOM
1268
O
ILE A
191
65.691
15.702
16.474
1.000
23.95

ATOM
1269
N
ARG A
192
64.342
15.563
18.298
1.000
20.33

ATOM
1270
CA
ARG A
192
65.063
16.567
19.069
1.000
19.85

ATOM
1271
CB
ARG A
192
64.185
17.172
20.169
1.000
20.25

ATOM
1272
CG
ARG A
192
63.053
18.031
19.641
1.000
21.19

ATOM
1273
CD
ARG A
192
62.285
18.757
20.720
1.000
20.91

ATOM
1274
NE
ARG A
192
61.452
17.886
21.554
1.000
21.19

ATOM
1275
CZ
ARG A
192
61.635
17.793
22.871
1.000
23.70

ATOM
1276
NH1
ARG A
192
62.597
18.494
23.462
1.000
20.82

ATOM
1277
NH2
ARG A
192
60.869
17.000
23.606
1.000
22.23

ATOM
1278
C
ARG A
192
66.308
15.944
19.699
1.000
19.83

ATOM
1279
O
ARG A
192
66.281
14.761
20.052
1.000
21.50

ATOM
1280
N
VAL A
193
67.352
16.752
19.827
1.000
20.77

ATOM
1281
CA
VAL A
193
68.585
16.282
20.464
1.000
21.10

ATOM
1282
CB
VAL A
193
69.706
16.014
19.449
1.000
21.95

ATOM
1283
CG1
VAL A
193
70.938
15.439
20.132
1.000
21.45

ATOM
1284
CG2
VAL A
193
69.225
15.065
18.356
1.000
18.83

ATOM
1285
C
VAL A
193
69.024
17.321
21.493
1.000
21.27

ATOM
1286
O
VAL A
193
69.264
18.476
21.157
1.000
18.26

ATOM
1287
N
MET A
194
69.099
16.893
22.746
1.000
20.77

ATOM
1288
CA
MET A
194
69.458
17.762
23.856
1.000
20.59

ATOM
1289
CB
MET A
194
68.226
18.038
27.719
1.000
21.73

ATOM
1290
CG
MET A
194
67.235
19.025
24.121
1.000
20.14

ATOM
1291
SD
MET A
194
67.834
20.721
24.138
1.000
21.56

ATOM
1292
CE
MET A
194
68.099
20.980
25.905
1.000
16.72

ATOM
1293
C
MET A
194
70.561
17.137
24.706
1.000
24.88

ATOM
1294
O
MET A
194
70.762
15.918
24.723
1.000
20.06

ATOM
1295
N
THR A
195
71.293
17.991
25.431
1.000
23.18

ATOM
1296
CA
THR A
195
72.360
17.453
26.281
1.000
21.06

ATOM
1297
CB
THR A
195
73.726
17.690
25.615
1.000
20.20

ATOM
1298
OG1
THR A
195
73.807
16.866
24.440
1.000
20.09

ATOM
1299
CG2
THR A
195
74.865
17.267
26.259
1.000
20.65

ATOM
1300
C
THR A
195
72.320
18.078
27.668
1.000
19.09

ATOM
1301
O
THR A
195
72.095
19.281
27.817
1.000
22.65

ATOM
1302
N
ILE A
196
72.531
17.260
28.695
1.000
21.42

ATOM
1303
CA
ILE A
196
72.642
17.775
30.054
1.000
21.21

ATOM
1304
CB
ILE A
196
71.775
16.991
31.058
1.000
22.86

ATOM
1305
CG2
ILE A
196
72.088
17.388
32.496
1.000
13.56

ATOM
1306
CG1
ILE A
196
70.270
17.101
30.786
1.000
18.56

ATOM
1307
CD1
ILE A
196
69.434
15.969
31.334
1.000
21.74

ATOM
1308
C
ILE A
196
74.109
17.727
30.487
1.000
19.78

ATOM
1309
O
ILE A
196
74.770
16.720
30.243
1.000
20.85

ATOM
1310
N
ALA A
197
74.586
18.798
31.107
1.000
17.33

ATOM
1311
CA
ALA A
197
75.910
18.819
31.706
1.000
20.74

ATOM
1312
CB
ALA A
197
76.703
20.032
31.236
1.000
15.79

ATOM
1313
C
ALA A
197
75.807
18.823
33.232
1.000
17.73

ATOM
1314
O
ALA A
197
75.684
19.885
33.844
1.000
20.44

ATOM
1315
N
PRO A
198
78.851
17.663
33.859
1.000
15.54

ATOM
1316
CD
PRO A
198
75.908
16.311
33.281
1.000
14.44

ATOM
1317
CA
PRO A
198
75.815
17.630
35.325
1.000
18.78

ATOM
1318
CB
PRO A
198
75.661
16.145
35.650
1.000
18.65

ATOM
1319
CG
PRO A
198
75.273
15.478
34.368
1.000
16.32

ATOM
1320
C
PRO A
198
77.101
18.178
35.939
1.000
21.23

ATOM
1321
O
PRO A
198
78.200
18.050
35.387
1.000
21.65

ATOM
1322
N
GLY A
199
76.973
18.801
37.111
1.000
16.71

ATOM
1323
CA
GLY A
199
78.144
19.282
37.831
1.000
20.34

ATOM
1324
C
GLY A
199
78.720
18.158
38.681
1.000
25.67

ATOM
1325
O
GLY A
199
79.558
17.382
38.215
1.000
29.26

ATOM
1326
N
LEU A
200
78.276
18.047
39.936
1.000
24.30

ATOM
1327
CA
LEU A
200
78.728
16.935
40.779
1.000
24.04

ATOM
1328
CB
LEU A
200
79.670
17.423
41.874
1.000
28.95

ATOM
1329
CG
LEU A
200
80.780
19.398
41.494
1.000
27.68

ATOM
1330
CD1
LEU A
200
81.456
18.959
42.741
1.000
23.71

ATOM
1331
CD2
LEU A
200
81.833
17.748
40.608
1.000
26.72

ATOM
1332
C
LEU A
200
77.516
16.224
41.373
1.000
21.56

ATOM
1333
O
LEU A
200
76.691
16.873
42.026
1.000
24.91

ATOM
1334
N
PHE A
201
77.391
14.922
41.160
1.000
18.56

ATOM
1335
CA
PHE A
201
76.258
14.175
41.696
1.000
22.51

ATOM
1336
CB
PHE A
201
75.324
13.676
40.585
1.000
18.39

ATOM
1337
CG
PHE A
201
74.333
14.750
40.151
1.000
22.13

ATOM
1338
CD1
PHE A
201
74.766
15.884
39.486
1.000
21.16

ATOM
1339
CD2
PHE A
201
72.985
14.614
40.415
1.000
21.94

ATOM
1340
CE1
PHE A
201
73.870
16.865
39.098
1.000
20.75

ATOM
1341
CE2
PHE A
201
72.083
15.594
40.036
1.000
22.20

ATOM
1342
CZ
PHE A
201
72.523
16.726
39.375
1.000
18.43

ATOM
1343
C
PHE A
201
76.711
12.983
42.543
1.000
24.36

ATOM
1344
O
PHE A
201
77.745
13.372
42.294
1.000
23.72

ATOM
1345
N
GLY A
202
75.903
12.676
43.555
1.000
26.29

ATOM
1346
CA
GLY A
202
76.191
11.573
44.455
1.000
27.80

ATOM
1347
C
GLY A
202
75.787
10.233
43.872
1.000
26.77

ATOM
1348
O
GLY A
202
74.706
9.721
44.164
1.000
32.55

ATOM
1349
N
THR A
203
76.647
9.654
43.043
1.000
25.13

ATOM
1350
CA
THR A
203
76.404
8.380
42.392
1.000
25.12

ATOM
1351
CB
THR A
203
76.257
8.557
40.862
1.000
28.49

ATOM
1352
OG1
THR A
203
77.560
8.874
40.347
1.000
23.32

ATOM
1353
CG2
THR A
203
75.287
9.679
40.553
1.000
27.37

ATOM
1354
C
THR A
203
77.565
7.429
42.650
1.000
27.93

ATOM
1355
O
THR A
203
78.614
7.903
43.107
1.000
25.79

ATOM
1356
N
PRO A
204
77.425
6.138
42.369
1.000
27.07

ATOM
1357
CD
PRO A
204
76.190
5.445
41.943
1.000
29.16

ATOM
1358
CA
PRO A
204
78.546
5.201
42.502
1.000
29.50

ATOM
1359
CB
PRO A
204
77.974
3.880
41.969
1.000
27.25

ATOM
1360
CG
PRO A
204
76.505
3.996
42.214
1.000
27.48

ATOM
1361
C
PRO A
204
79.773
5.592
41.687
1.000
25.78

ATOM
1362
O
PRO A
204
80.857
5.062
41.939
1.000
32.08

ATOM
1363
N
LEU A
205
79.645
6.483
40.716
1.000
37.07

ATOM
1364
CA
LEU A
205
80.788
6.983
39.963
1.000
31.42

ATOM
1365
CB
LEU A
205
80.346
8.062
38.969
1.000
28.18

ATOM
1366
CG
LEU A
205
81.354
8.485
37.900
1.000
35.16

ATOM
1367
CD1
LEU A
205
81.596
7.353
36.911
1.000
31.93

ATOM
1368
CD2
LEU A
205
80.884
9.746
37.187
1.000
31.91

ATOM
1369
C
LEU A
205
81.856
7.554
40.889
1.000
27.98

ATOM
1370
O
LEU A
205
83.042
7.313
40.676
1.000
34.06

ATOM
1371
N
LEU A
206
81.465
8.320
41.904
1.000
21.36

ATOM
1372
CA
LEU A
206
82.421
9.023
42.750
1.000
18.23

ATOM
1373
CB
LEU A
206
81.777
10.282
43.351
1.000
19.00

ATOM
1374
CG
LEU A
206
81.166
11.282
42.373
1.000
29.73

ATOM
1375
CD1
LEU A
206
80.600
12.484
43.114
1.000
26.59

ATOM
1376
CD2
LEU A
206
82.196
11.722
41.344
1.000
45.64

ATOM
1377
C
LEU A
206
82.959
8.185
43.903
1.000
25.48

ATOM
1378
O
LEU A
206
83.768
8.675
44.699
1.000
29.01

ATOM
1379
N
THR A
207
82.518
6.943
44.017
1.000
27.24

ATOM
1380
CA
THR A
207
82.834
6.112
45.176
1.000
24.16

ATOM
1381
CB
THR A
207
82.002
4.814
45.180
1.000
31.81

ATOM
1382
OG1
THR A
207
80.604
5.121
45.103
1.000
33.01

ATOM
1383
CG2
THR A
207
82.189
4.062
46.492
1.000
39.64

ATOM
1384
C
THR A
207
84.317
5.774
45.241
1.000
27.40

ATOM
1385
O
THR A
207
84.893
5.719
46.330
1.000
34.76

ATOM
1386
N
SER A
208
84.932
5.557
44.085
1.000
31.07

ATOM
1387
CA
SER A
208
86.362
5.291
44.002
1.000
37.59

ATOM
1388
CB
SER A
208
86.794
5.170
42.536
1.000
40.21

ATOM
1389
OG
SER A
208
85.664
4.850
41.732
1.000
64.46

ATOM
1390
C
SER A
208
87.164
6.379
44.711
1.000
39.66

ATOM
1391
O
SER A
208
88.177
6.088
45.351
1.000
59.11

ATOM
1392
N
LEU A
209
86.710
7.622
44.608
1.000
28.44

ATOM
1393
CA
LEU A
209
87.362
8.752
45.254
1.000
35.84

ATOM
1394
CB
LEU A
209
86.632
10.056
44.879
1.000
36.73

ATOM
1395
CG
LEU A
209
86.694
10.394
43.380
1.000
35.96

ATOM
1396
CD1
LEU A
209
85.999
11.711
43.072
1.000
20.66

ATOM
1397
CD2
LEU A
209
88.146
10.411
42.921
1.000
33.37

ATOM
1398
C
LEU A
209
87.414
8.605
46.770
1.000
34.49

ATOM
1399
O
LEU A
209
86.475
8.101
47.383
1.000
32.58

ATOM
1400
N
PRO A
210
88.512
9.043
47.374
1.000
29.27

ATOM
1401
CD
PRO A
210
89.765
9.458
46.720
1.000
27.98

ATOM
1402
CA
PRO A
210
88.602
9.147
48.831
1.000
29.98

ATOM
1403
CB
PRO A
210
89.947
9.846
49.069
1.000
27.49

ATOM
1404
CG
PRO A
210
90.746
9.460
47.866
1.000
25.08

ATOM
1405
C
PRO A
210
87.479
10.015
49.389
1.000
31.11

ATOM
1406
O
PRO A
210
87.131
11.047
48.810
1.000
31.99

ATOM
1407
N
GLU A
211
86.929
9.576
50.514
1.000
27.60

ATOM
1408
CA
GLU A
211
85.816
10.265
51.145
1.000
26.18

ATOM
1409
CB
GLU A
211
85.562
9.614
52.509
1.000
40.32

ATOM
1410
CG
GLU A
211
84.354
9.696
52.509
1.000
43.94

ATOM
1411
CD
GLU A
211
84.054
8.131
53.884
1.000
42.42

ATOM
1412
OE1
GLU A
211
83.181
8.700
54.573
1.000
30.45

ATOM
1413
OE2
GLU A
211
84.705
7.119
54.222
1.000
31.95

ATOM
1414
C
GLU A
211
86.092
11.748
51.308
1.000
24.00

ATOM
1415
O
GLU A
211
85.265
12.615
51.031
1.000
24.47

ATOM
1416
N
LYS A
212
87.308
12.033
21.770
1.000
22.33

ATOM
1417
CA
LYS A
212
87.768
13.405
51.947
1.000
29.30

ATOM
1418
CB
LYS A
212
89.228
13.403
52.387
1.000
40.01

ATOM
1419
C
LYS A
212
87.595
14.237
50.680
1.000
23.78

ATOM
1420
O
LYS A
212
87.161
15.389
50.730
1.000
24.76

ATOM
1421
N
VAL A
213
87.925
13.677
49.521
1.000
24.58

ATOM
1422
CA
VAL A
213
87.769
14.435
48.278
1.000
26.36

ATOM
1423
CB
VAL A
213
88.451
13.686
47.120
1.000
35.53

ATOM
1424
CG1
VAL A
213
88.325
14.449
45.808
1.000
27.07

ATOM
1425
CG2
VAL A
213
89.916
13.443
47.469
1.000
38.54

ATOM
1426
C
VAL A
213
86.297
14.679
47.965
1.000
24.27

ATOM
1427
O
VAL A
213
85.865
15.790
47.657
1.000
23.99

ATOM
1428
N
ARG A
214
85.503
13.619
48.050
1.000
23.64

ATOM
1429
CA
ARG A
214
84.062
13.735
47.858
1.000
23.89

ATOM
1430
CB
ARG A
214
83.387
12.395
48.152
1.000
28.02

ATOM
1431
CG
ARG A
214
83.291
11.484
46.938
1.000
31.88

ATOM
1432
CD
ARG A
214
86.728
10.064
47.279
1.000
35.66

ATOM
1433
NE
ARG A
214
82.744
9.415
48.130
1.000
37.47

ATOM
1434
CZ
ARG A
214
82.895
8.303
48.828
1.000
44.73

ATOM
1435
NH1
ARG A
214
84.031
7.613
48.828
1.000
37.28

ATOM
1436
NH2
ARG A
214
81.860
7.878
49.548
1.000
67.12

ATOM
1437
C
ARG A
214
83.477
14.826
48.743
1.000
30.95

ATOM
1438
O
ARG A
214
82.709
15.670
48.281
1.000
33.19

ATOM
1439
N
ASN A
215
83.837
14.840
50.028
1.000
28.66

ATOM
1440
CA
ASN A
215
83.308
15.887
50.902
1.000
27.53

ATOM
1441
CB
ASN A
215
83.684
15.663
52.369
1.000
32.68

ATOM
1442
CG
ASN A
215
83.258
14.304
52.883
1.000
31.08

ATOM
1443
OD1
ASN A
215
82.446
13.619
52.262
1.000
37.63

ATOM
1444
ND2
ASN A
215
86.810
13.898
54.017
1.000
43.42

ATOM
1445
C
ASN A
215
83.810
17.258
50.469
1.000
18.44

ATOM
1446
O
ASN A
215
83.057
18.231
50.485
1.000
30.03

ATOM
1447
N
PHE A
216
85.081
17.340
50.084
1.000
22.51

ATOM
1448
CA
PHE A
216
85.609
18.441
49.675
1.000
25.01

ATOM
1449
CB
PHE A
216
87.113
18.554
49.401
1.000
26.17

ATOM
1450
CG
PHE A
216
87.636
19.848
48.788
1.000
30.92

ATOM
1451
CD1
PHE A
216
87.820
20.969
49.576
1.000
26.31

ATOM
1452
CD2
PHE A
216
87.929
19.922
47.439
1.000
38.31

ATOM
1453
CE1
PHE A
216
88.284
22.150
49.036
1.000
28.91

ATOM
1454
CE2
PHE A
216
88.397
21.102
46.888
1.000
42.22

ATOM
1455
CZ
PHE A
216
88.574
22.216
47.685
1.000
36.56

ATOM
1456
C
PHE A
216
84.876
19.173
48.442
1.000
31.65

ATOM
1457
O
PHE A
216
84.487
20.342
48.442
1.000
27.79

ATOM
1458
N
LEU A
217
84.688
18.320
47.439
1.000
31.39

ATOM
1459
CA
LEU A
217
83.933
18.685
46.238
1.000
32.23

ATOM
1460
CB
LEU A
217
83.887
17.516
45.255
1.000
32.50

ATOM
1461
CG
LEU A
217
85.207
16.990
44.682
1.000
29.24

ATOM
1462
CD1
LEU A
217
84.907
15.797
43.765
1.000
17.82

ATOM
1463
CD2
LEU A
217
85.962
18.082
43.943
1.000
29.21

ATOM
1464
C
LEU A
217
82.524
19.136
46.611
1.000
31.73

ATOM
1465
O
LEU A
217
81.996
20.132
46.107
1.000
23.72

ATOM
1466
N
ALA A
218
81.886
18.401
47.526
1.000
29.13

ATOM
1467
CA
ALA A
218
80.555
18.785
47.981
1.000
28.01

ATOM
1468
CB
ALA A
218
80.007
17.826
49.035
1.000
24.11

ATOM
1469
C
ALA A
218
80.565
20.188
48.568
1.000
24.33

ATOM
1470
O
ALA A
218
79.656
20.984
48.355
1.000
24.23

ATOM
1471
N
SER A
219
81.616
20.490
49.328
1.000
25.40

ATOM
1472
CA
SER A
219
81.633
21.782
50.012
1.000
26.17

ATOM
1473
CB
SER A
219
82.801
21.841
51.007
1.000
23.46

ATOM
1474
OG
SER A
219
84.035
21.883
50.304
1.000
28.86

ATOM
1475
C
SER A
219
81.731
22.929
49.026
1.000
28.77

ATOM
1476
O
SER A
219
81.470
24.075
49.387
1.000
29.20

ATOM
1477
N
GLN A
220
82.102
22.651
47.777
1.000
31.06

ATOM
1478
CA
GLN A
220
82.336
23.755
46.850
1.000
28.95

ATOM
1479
CB
GLN A
220
83.511
23.370
45.940
1.000
35.57

ATOM
1480
CG
GLN A
220
84.805
23.152
46.713
1.000
46.25

ATOM
1481
CD
GLN A
220
85.559
24.459
46.910
1.000
54.85

ATOM
1482
OE1
GLN A
220
85.311
25.169
47.883
1.000
67.11

ATOM
1483
NE2
GLN A
220
86.465
27.766
45.989
1.000
58.88

ATOM
1484
C
GLN A
220
81.139
24.144
46.005
1.000
27.97

ATOM
1485
O
GLN A
220
81.188
25.140
45.266
1.000
25.50

ATOM
1486
N
VAL A
221
80.038
23.397
46.066
1.000
24.23

ATOM
1487
CA
VAL A
221
78.877
23.801
45.257
1.000
19.71

ATOM
1488
CB
VAL A
221
77.881
22.645
45.135
1.000
20.16

ATOM
1489
CG1
VAL A
221
76.729
23.008
44.204
1.000
16.09

ATOM
1490
CG2
VAL A
221
78.595
21.382
44.657
1.000
17.00

ATOM
1491
C
VAL A
221
78.226
25.016
45.896
1.000
24.47

ATOM
1492
O
VAL A
221
77.763
24.933
47.041
1.000
25.19

ATOM
1493
N
PRO A
222
78.187
26.160
45.232
1.000
25.80

ATOM
1494
CD
PRO A
222
78.681
26.411
43.859
1.000
24.80

ATOM
1495
CA
PRO A
222
77.651
27.382
45.848
1.000
22.49

ATOM
1496
CB
PRO A
222
77.602
28.367
44.666
1.000
18.73

ATOM
1497
CG
PRO A
222
78.785
27.924
43.841
1.000
22.15

ATOM
1498
C
PRO A
222
76.272
27.231
46.462
1.000
27.78

ATOM
1499
O
PRO A
222
76.075
27.491
47.650
1.000
24.62

ATOM
1500
N
PHE A
223
75.253
29.829
45.714
1.000
24.56

ATOM
1501
CA
PHE A
223
73.945
26.652
46.334
1.000
20.97

ATOM
1502
CB
PHE A
223
73.215
27.947
46.693
1.000
20.13

ATOM
1503
CG
PHE A
223
71.883
27.618
47.370
1.000
25.97

ATOM
1504
CD1
PHE A
223
71.850
27.192
48.687
1.000
28.70

ATOM
1505
CD2
PHE A
223
70.668
27.728
46.689
1.000
22.64

ATOM
1506
CE1
PHE A
223
70.654
26.880
49.320
1.000
25.50

ATOM
1507
CE2
PHE A
223
69.488
27.424
47.313
1.000
25.33

ATOM
1508
CZ
PHE A
223
69.464
26.993
48.629
1.000
22.68

ATOM
1509
C
PHE A
223
73.057
25.813
45.415
1.000
26.48

ATOM
1510
O
PHE A
223
72.918
26.178
44.248
1.000
24.24

ATOM
1511
N
PRO A
224
72.466
24.733
45.911
1.000
28.80

ATOM
1512
CD
PRO A
224
71.556
23.870
45.133
1.000
28.23

ATOM
1513
CA
PRO A
224
72.625
24.268
47.290
1.000
29.22

ATOM
1514
CB
PRO A
224
71.509
23.232
47.436
1.000
31.63

ATOM
1515
CG
PRO A
224
71.279
22.721
46.058
1.000
29.47

ATOM
1516
C
PRO A
224
73.982
23.602
47.531
1.000
28.36

ATOM
1517
O
PRO A
224
74.550
22.999
46.621
1.000
22.58

ATOM
1518
N
SER A
225
74.484
23.778
48.751
1.000
25.87

ATOM
1519
CA
SER A
225
75.832
23.351
49.090
1.000
29.25

ATOM
1520
CB
SER A
225
76.367
24.152
50.283
1.000
37.81

ATOM
1521
OG
SER A
225
76.577
25.493
49.874
1.000
56.13

ATOM
1522
C
SER A
225
75.883
21.863
49.385
1.000
29.47

ATOM
1523
O
SER A
225
75.952
21.398
50.516
1.000
28.64

ATOM
1524
N
ARG A
226
75.850
21.105
48.293
1.000
23.34

ATOM
1525
CA
ARG A
226
75.876
19.658
48.378
1.000
21.20

ATOM
1526
CB
ARG A
226
74.594
19.134
49.026
1.000
20.65

ATOM
1527
CG
ARG A
226
73.340
19.637
48.306
1.000
20.10

ATOM
1528
CD
ARG A
226
72.203
18.633
48.397
1.000
23.97

ATOM
1529
NE
ARG A
226
70.932
19.239
47.978
1.000
23.27

ATOM
1530
CZ
ARG A
226
70.369
19.014
46.796
1.000
27.29

ATOM
1531
NH1
ARG A
226
69.219
19.600
46.488
1.000
20.66

ATOM
1532
NH2
ARG A
226
70.943
18.206
45.908
1.000
22.51

ATOM
1533
C
ARG A
226
76.007
19.003
46.972
1.000
24.78

ATOM
1534
O
ARG A
226
75.759
19.779
45.986
1.000
24.98

ATOM
1535
N
LEU A
227
76.368
17.812
46.899
1.000
21.08

ATOM
1536
CA
LEU A
227
76.314
17.125
45.617
1.000
25.85

ATOM
1537
CB
LEU A
227
76.849
15.701
45.778
1.000
25.37

ATOM
1538
CG
LEU A
227
78.246
15.581
46.398
1.000
24.53

ATOM
1539
CD1
LEU A
227
78.615
14.112
46.539
1.000
23.43

ATOM
1540
CD2
LEU A
227
79.254
16.352
45.562
1.000
19.26

ATOM
1541
C
LEU A
227
74.885
17.114
45.105
1.000
25.75

ATOM
1542
O
LEU A
227
73.932
17.166
45.890
1.000
21.27

ATOM
1543
N
GLY A
228
74.697
17.041
43.786
1.000
23.15

ATOM
1544
CA
GLY A
228
73.327
16.959
43.294
1.000
19.97

ATOM
1545
C
GLY A
228
72.747
15.590
43.606
1.000
21.85

ATOM
1546
O
GLY A
228
73.477
14.604
43.695
1.000
22.71

ATOM
1547
N
ASP A
229
71.423
15.532
43.766
1.000
23.70

ATOM
1548
CA
ASP A
229
70.781
14.228
43.962
1.000
21.75

ATOM
1549
CB
ASP A
229
69.594
14.376
44.909
1.000
25.58

ATOM
1550
CG
ASP A
229
69.011
13.036
45.317
1.000
37.77

ATOM
1551
OD1
ASP A
229
68.989
12.691
46.522
1.000
52.48

ATOM
1552
OD2
ASP A
229
68.565
12.322
44.393
1.000
37.02

ATOM
1553
C
ASP A
229
70.362
13.661
42.618
1.000
18.38

ATOM
1554
O
ASP A
229
69.795
14.402
41.817
1.000
21.95

ATOM
1555
N
PRO A
230
70.630
12.396
42.353
1.000
24.18

ATOM
1556
CD
PRO A
230
71.242
11.395
43.258
1.000
23.15

ATOM
1557
CA
PRO A
230
70.332
11.833
41.027
1.000
23.50

ATOM
1558
CB
PRO A
230
70.618
10.340
41.234
1.000
24.52

ATOM
1559
CG
PRO A
230
71.705
10.352
42.273
1.000
23.78

ATOM
1560
C
PRO A
230
68.895
12.054
40.589
1.000
26.53

ATOM
1561
O
PRO A
230
68.602
12.084
39.387
1.000
25.38

ATOM
1562
N
ALA A
231
67.961
12.207
41.528
1.000
26.35

ATOM
1563
CA
ALA A
231
66.579
12.467
41.116
1.000
26.18

ATOM
1564
CB
ALA A
231
65.608
12.325
42.280
1.000
21.25

ATOM
1565
C
ALA A
231
66.449
13.855
40.495
1.000
26.64

ATOM
1566
O
ALA A
231
65.546
14.075
39.478
1.000
26.06

ATOM
1567
N
GLU A
232
67.322
14.786
40.857
1.000
22.42

ATOM
1568
CA
GLU A
232
67.304
16.120
40.250
1.000
23.24

ATOM
1569
CB
GLU A
232
68.224
17.072
41.030
1.000
23.89

ATOM
1570
CG
GLU A
232
67.618
17.531
42.345
1.000
22.94

ATOM
1571
CD
GLU A
232
68.572
18.110
43.357
1.000
22.44

ATOM
1572
OE1
GLU A
232
69.783
17.800
43.363
1.000
22.54

ATOM
1573
OE2
GLU A
232
68.106
18.906
44.206
1.000
22.99

ATOM
1574
C
GLU A
232
67.677
16.041
38.772
1.000
21.16

ATOM
1575
O
GLU A
232
67.133
16.772
37.943
1.000
23.00

ATOM
1576
N
TYR A
233
68.600
15.162
37.418
1.000
18.83

ATOM
1577
CA
TYR A
233
68.921
14.913
37.015
1.000
21.13

ATOM
1578
CB
TYR A
233
70.096
13.937
36.893
1.000
19.96

ATOM
1579
CG
TYR A
233
70.437
13.521
35.475
1.000
21.89

ATOM
1580
CD1
TYR A
233
71.301
14.274
34.688
1.000
19.55

ATOM
1581
CE1
TYR A
233
71.606
13.877
33.393
1.000
18.37

ATOM
1582
CD2
TYR A
233
69.307
12.366
34.909
1.000
19.47

ATOM
1583
CE2
TYR A
233
70.197
11.970
33.624
1.000
22.32

ATOM
1584
CZ
TYR A
233
71.056
12.740
32.864
1.000
21.80

ATOM
1585
OH
TYR A
233
71.345
12.329
31.579
1.000
22.58

ATOM
1586
C
TYR A
233
67.693
14.366
36.285
1.000
27.74

ATOM
1587
O
TYR A
233
67.365
14.803
35.181
1.000
27.25

ATOM
1588
N
ALA A
234
67.043
13.382
36.903
1.000
23.68

ATOM
1589
CA
ALA A
234
65.851
12.738
36.377
1.000
20.29

ATOM
1590
CB
ALA A
234
62.349
11.677
37.349
1.000
23.40

ATOM
1591
C
ALA A
234
64.740
13.744
36.094
1.000
20.45

ATOM
1592
O
ALA A
234
64.060
13.659
35.066
1.000
25.13

ATOM
1593
N
HIS A
235
64.545
14.693
37.004
1.000
19.46

ATOM
1594
CA
HIS A
235
63.560
15.746
36.801
1.000
20.05

ATOM
1595
CB
HIS A
235
63.490
16.680
38.008
1.000
20.64

ATOM
1596
CG
HIS A
235
62.661
17.910
37.798
1.000
23.05

ATOM
1597
CD2
HIS A
235
62.979
19.150
37.361
1.000
21.17

ATOM
1598
ND1
HIS A
235
61.306
17.954
38.072
1.000
28.32

ATOM
1599
CE1
HIS A
235
60.826
19.155
37.806
1.000
22.48

ATOM
1600
NE2
HIS A
235
61.825
19.898
37.370
1.000
27.72

ATOM
1601
C
HIS A
235
63.890
16.550
35.549
1.000
24.63

ATOM
1602
O
HIS A
235
62.975
16.892
37.798
1.000
24.01

ATOM
1603
N
LEU A
236
65.167
16.867
35.324
1.000
24.45

ATOM
1604
CA
LEU A
236
65.509
17.681
34.160
1.000
22.07

ATOM
1605
CB
LEU A
236
66.950
18.181
34.211
1.000
20.78

ATOM
1606
CG
LEU A
236
67.404
19.047
33.026
1.000
18.62

ATOM
1607
CD1
LEU A
236
66.248
20.196
32.799
1.000
16.03

ATOM
1608
CD2
LEU A
236
68.809
19.579
33.252
1.000
16.04

ATOM
1609
C
LEU A
236
65.266
16.903
32.866
1.000
21.70

ATOM
1610
O
LEU A
236
64.772
17.483
31.900
1.000
20.42

ATOM
1611
N
VAL A
237
65.582
15.617
32.841
1.000
21.20

ATOM
1612
CA
VAL A
237
65.283
14.783
31.675
1.000
21.16

ATOM
1613
CB
VAL A
237
65.172
13.318
31.863
1.000
23.98

ATOM
1614
CG1
VAL A
237
65.154
12.454
30.730
1.000
23.53

ATOM
1615
CG2
VAL A
237
67.225
13.178
31.928
1.000
21.01

ATOM
1616
C
VAL A
237
63.789
14.818
31.361
1.000
24.81

ATOM
1617
O
VAL A
237
63.371
14.951
30.208
1.000
23.68

ATOM
1618
N
GLN A
238
62.942
14.701
32.383
1.000
22.85

ATOM
1619
CA
GLN A
238
61.503
14.737
32.105
1.000
23.14

ATOM
1620
CB
GLN A
238
60.680
14.420
33.355
1.000
27.65

ATOM
1621
CG
GLN A
238
59.175
14.510
33.117
1.000
34.44

ATOM
1622
CD
GLN A
238
58.382
14.022
34.313
1.000
45.36

ATOM
1623
OE1
GLN A
238
58.910
13.369
35.216
1.000
44.78

ATOM
1624
NE2
GLN A
238
57.091
14.335
34.341
1.000
41.18

ATOM
1625
C
GLN A
238
61.074
16.092
31.546
1.000
20.15

ATOM
1626
O
GLN A
238
60.265
16.158
30.626
1.000
28.26

ATOM
1627
N
ALA A
239
31.625
17.165
32.104
1.000
16.27

ATOM
1628
CA
ALA A
239
61.311
18.514
31.669
1.000
17.56

ATOM
1629
CB
ALA A
239
62.049
19.520
32.536
1.000
21.61

ATOM
1630
C
ALA A
239
61.664
18.722
30.198
1.000
22.67

ATOM
1631
O
ALA A
239
60.942
19.377
29.457
1.000
23.10

ATOM
1632
N
ILE A
240
62.790
18.165
29.781
1.000
20.80

ATOM
1633
CA
ILE A
240
63.216
18.205
28.386
1.000
25.50

ATOM
1634
CB
ILE A
240
64.683
17.734
28.278
1.000
23.55

ATOM
1635
CG2
ILE A
240
65.037
17.338
26.860
1.000
20.26

ATOM
1636
CG1
ILE A
240
62.683
18.769
28.827
1.000
17.72

ATOM
1637
CD1
ILE A
240
67.703
18.186
28.998
1.000
19.57

ATOM
1638
C
ILE A
240
62.314
17.348
27.511
1.000
26.46

ATOM
1639
O
ILE A
240
62.916
17.735
26.411
1.000
21.98

ATOM
1640
N
ILE A
241
61.969
16.155
27.992
1.000
21.35

ATOM
1641
CA
ILE A
241
61.046
15.306
27.238
1.000
26.98

ATOM
1642
CB
ILE A
241
60.734
13.972
27.940
1.000
27.84

ATOM
1643
CG2
ILE A
241
59.573
13.265
27.244
1.000
23.88

ATOM
1644
CG1
ILE A
241
61.926
13.023
28.066
1.000
22.84

ATOM
1645
CD1
ILE A
241
61.693
11.863
29.011
1.000
20.80

ATOM
1646
C
ILE A
241
59.739
16.056
26.990
1.000
27.61

ATOM
1647
O
ILE A
241
59.144
16.033
25.913
1.000
24.04

ATOM
1648
N
GLU A
242
29.286
16.746
28.036
1.000
21.41

ATOM
1649
CA
GLU A
242
57.969
17.364
27.977
1.000
23.08

ATOM
1650
CB
GLU A
242
57.499
17.647
29.408
1.000
22.57

ATOM
1651
CG
GLU A
242
57.170
16.396
30.206
1.000
25.70

ATOM
1652
CD
GLU A
242
56.396
16.747
31.475
1.000
31.32

ATOM
1653
OE1
GLU A
242
55.646
15.891
31.987
1.000
41.56

ATOM
1654
OE2
GLU A
242
56.553
17.892
31.951
1.000
38.20

ATOM
1655
C
GLU A
242
57.936
18.649
27.170
1.000
27.56

ATOM
1656
O
GLU A
242
56.914
18.945
26.552
1.000
27.92

ATOM
1657
N
ASN A
243
59.015
19.426
27.170
1.000
22.75

ATOM
1658
CA
ASN A
243
59.011
20.717
26.485
1.000
24.21

ATOM
1659
CB
ASN A
243
59.999
21.671
27.156
1.000
21.86

ATOM
1660
CG
ASN A
243
59.811
23.108
26.172
1.000
23.53

ATOM
1661
OD1
ASN A
243
89.775
23.431
25.522
1.000
22.67

ATOM
1662
ND2
ASN A
243
59.700
23.988
27.689
1.000
19.20

ATOM
1663
C
ASN A
243
59.356
20.565
25.009
1.000
27.29

ATOM
1664
O
ASN A
243
60.489
20.231
24.654
1.000
24.50

ATOM
1665
N
PRO A
244
58.382
20.804
21.138
1.000
27.24

ATOM
1666
CD
PRO A
244
57.005
21.238
24.434
1.000
24.08

ATOM
1667
CA
PRO A
244
58.603
20.626
22.700
1.000
22.73

ATOM
1668
CB
PRO A
244
57.222
20.911
22.084
1.000
23.36

ATOM
1669
CG
PRO A
244
56.269
20.716
23.222
1.000
26.47

ATOM
1670
C
PRO A
244
59.603
21.596
22.100
1.000
21.55

ATOM
1671
O
PRO A
244
60.085
21.321
20.988
1.000
24.58

ATOM
1672
N
PHE A
245
59.941
22.717
22.735
1.000
21.03

ATOM
1673
CA
PHE A
245
60.793
23.659
21.993
1.000
19.57

ATOM
1674
CB
PHE A
245
60.283
25.086
22.178
1.000
22.58

ATOM
1675
CG
PHE A
245
60.458
26.021
20.995
1.000
18.83

ATOM
1676
CD1
PHE A
245
61.118
27.224
21.130
1.000
17.04

ATOM
1677
CD2
PHE A
245
59.957
25.695
19.742
1.000
18.90

ATOM
1678
CE1
PHE A
245
61.281
28.103
20.068
1.000
19.82

ATOM
1679
CE2
PHE A
245
60.103
26.548
18.663
1.000
16.29

ATOM
1680
CZ
PHE A
245
60.797
27.749
18.832
1.000
18.24

ATOM
1681
C
PHE A
245
62.263
23.549
22.388
1.000
25.70

ATOM
1682
O
PHE A
245
63.087
24.304
21.873
1.000
19.98

ATOM
1683
N
LEU A
246
62.630
22.635
23.279
1.000
23.56

ATOM
1684
CA
LEU A
246
64.026
22.477
23.685
1.000
22.39

ATOM
1685
CB
LEU A
246
64.141
21.902
25.102
1.000
21.56

ATOM
1686
CG
LEU A
246
63.840
22.873
26.249
1.000
23.45

ATOM
1687
CD1
LEU A
246
63.735
22.128
27.570
1.000
23.33

ATOM
1688
CD2
LEU A
246
64.900
23.962
26.334
1.000
20.46

ATOM
1689
C
LEU A
246
64.782
21.575
22.715
1.000
20.66

ATOM
1690
O
LEU A
246
64.517
20.378
22.630
1.000
21.20

ATOM
1691
N
ASN A
247
65.735
22.145
21.985
1.000
20.82

ATOM
1692
CA
ASN A
247
66.483
21.349
21.010
1.000
21.25

ATOM
1693
CB
ASN A
247
65.671
21.292
19.718
1.000
21.44

ATOM
1694
CG
ASN A
247
66.084
20.187
18.770
1.000
27.16

ATOM
1695
OD1
ASN A
247
66.899
19.328
19.096
1.000
20.56

ATOM
1696
ND2
ASN A
247
65.498
20.210
17.569
1.000
22.46

ATOM
1697
C
ASN A
247
67.862
21.932
20.741
1.000
19.13

ATOM
1698
O
ASN A
247
68.019
23.151
20.747
1.000
18.86

ATOM
1699
N
GLY A
248
68.861
21.095
20.493
1.000
19.82

ATOM
1700
CA
GLY A
248
70.191
21.529
20.123
1.000
20.18

ATOM
1701
C
GLY A
248
70.947
22.319
21.161
1.000
21.65

ATOM
1702
O
GLY A
248
71.837
23.111
20.846
1.000
18.31

ATOM
1703
N
GLU A
249
70.617
22.123
22.436
1.000
19.76

ATOM
1704
CA
GLU A
249
71.193
22.933
23.512
1.000
15.34

ATOM
1705
CB
GLU A
249
70.093
23.812
24.096
1.000
17.49

ATOM
1706
CG
GLU A
249
70.339
24.393
25.479
1.000
18.34

ATOM
1707
CD
GLU A
249
71.417
25.457
25.495
1.000
20.71

ATOM
1708
OE1
GLU A
249
71.291
26.430
26.270
1.000
24.53

ATOM
1709
OE2
GLU A
249
72.399
25.321
24.737
1.000
20.71

ATOM
1710
C
GLU A
249
71.827
22.049
24.576
1.000
20.26

ATOM
1711
O
GLU A
249
71.485
20.874
24.713
1.000
18.20

ATOM
1712
N
VAL A
250
72.758
22.628
25.324
1.000
20.14

ATOM
1713
CA
VAL A
250
73.423
21.963
26.444
1.000
15.45

ATOM
1714
CB
VAL A
250
74.950
21.971
26.285
1.000
23.58

ATOM
1715
CG1
VAL A
250
75.633
21.356
27.501
1.000
21.33

ATOM
1716
CG2
VAL A
250
75.346
21.233
25.011
1.000
20.50

ATOM
1717
C
VAL A
250
73.029
22.660
27.744
1.000
19.05

ATOM
1718
O
VAL A
250
73.131
23.892
27.823
1.000
18.90

ATOM
1719
N
ILE A
251
72.577
21.905
28.746
1.000
17.48

ATOM
1720
CA
ILE A
251
72.115
22.552
29.977
1.000
19.87

ATOM
1721
CB
ILE A
251
70.639
22.211
30.259
1.000
19.82

ATOM
1722
CG2
ILE A
251
70.190
22.867
31.567
1.000
18.96

ATOM
1723
CG1
ILE A
251
69.670
22.552
29.127
1.000
16.79

ATOM
1724
CD1
ILE A
251
68.244
22.113
29.385
1.000
18.75

ATOM
1725
C
ILE A
251
72.953
22.143
31.183
1.000
18.61

ATOM
1726
O
ILE A
251
73.009
20.947
31.501
1.000
20.95

ATOM
1727
N
ARG A
252
73.594
23.118
31.822
1.000
20.09

ATOM
1728
CA
ARG A
252
74.390
22.869
33.018
1.000
20.43

ATOM
1729
CB
ARG A
252
76.386
24.034
33.378
1.000
20.29

ATOM
1730
CG
ARG A
252
76.386
24.442
32.411
1.000
22.69

ATOM
1731
CD
ARG A
252
77.182
25.646
32.914
1.000
21.00

ATOM
1732
NE
ARG A
252
77.981
25.296
34.708
1.000
19.89

ATOM
1733
CZ
ARG A
252
79.304
25.251
34.157
1.000
21.01

ATOM
1734
NH1
ARG A
252
79.896
24.909
35.293
1.000
16.77

ATOM
1735
NH2
ARG A
252
80.069
25.543
33.114
1.000
20.53

ATOM
1736
C
ARG A
252
73.453
22.609
34.008
1.000
19.55

ATOM
1737
O
ARG A
252
72.587
23.437
34.488
1.000
15.60

ATOM
1738
N
LEU A
253
73.623
21.494
34.897
1.000
19.36

ATOM
1739
CA
LEU A
253
72.859
21.189
36.109
1.000
18.74

ATOM
1740
CB
LEU A
253
71.984
19.960
35.898
1.000
17.63

ATOM
1741
CG
LEU A
253
71.116
19.524
37.089
1.000
20.75

ATOM
1742
CD1
LEU A
253
70.028
20.566
37.333
1.000
14.44

ATOM
1743
CD2
LEU A
253
70.514
18.148
36.872
1.000
14.92

ATOM
1744
C
LEU A
253
73.854
20.999
37.247
1.000
21.59

ATOM
1745
O
LEU A
253
74.367
19.906
37.465
1.000
19.92

ATOM
1746
N
ASP A
254
74.167
22.074
38.791
1.000
19.66

ATOM
1747
CA
ASP A
254
75.366
22.050
38.791
1.000
19.66

ATOM
1748
CB
ASP A
254
76.544
22.469
37.883
1.000
15.11

ATOM
1749
CG
ASP A
254
76.311
23.832
37.262
1.000
21.56

ATOM
1750
OD1
ASP A
254
75.534
24.535
37.673
1.000
18.87

ATOM
1751
OD2
ASP A
254
77.085
24.205
35.351
1.000
22.35

ATOM
1752
C
ASP A
254
75.369
22.971
39.994
1.000
20.87

ATOM
1753
O
ASP A
254
76.442
23.142
40.582
1.000
23.02

ATOM
1754
N
GLY A
255
74.248
23.582
40.371
1.000
21.44

ATOM
1755
CA
GLY A
255
74.249
24.391
41.590
1.000
17.40

ATOM
1756
C
GLY A
255
75.152
25.600
41.497
1.000
24.03

ATOM
1757
O
GLY A
255
75.619
26.088
42.529
1.000
20.64

ATOM
1758
N
ALA A
256
75.377
26.065
40.270
1.000
23.32

ATOM
1759
CA
ALA A
256
76.148
27.265
39.372
1.000
21.34

ATOM
1760
CB
ALA A
256
75.654
28.440
40.814
1.000
18.73

ATOM
1761
C
ALA A
256
77.646
27.063
40.179
1.000
19.93

ATOM
1762
O
ALA A
256
78.420
28.029
40.229
1.000
19.19

ATOM
1763
N
ILE A
257
78.106
25.815
40.309
1.000
17.99

ATOM
1764
CA
ILE A
257
79.550
25.652
40.528
1.000
19.13

ATOM
1765
CB
ILE A
257
79.893
24.238
41.020
1.000
18.18

ATOM
1766
CG2
ILE A
257
79.829
23.235
39.875
1.000
23.53

ATOM
1767
CG1
ILE A
257
81.250
24.126
41.723
1.000
18.23

ATOM
1768
CD1
ILE A
257
81.531
22.750
42.290
1.000
16.33

ATOM
1769
C
ILE A
257
80.337
25.944
39.250
1.000
24.61

ATOM
1770
O
ILE A
257
79.827
25.788
38.139
1.000
17.90

ATOM
1771
N
ARG A
258
81.583
26.366
39.421
1.000
21.54

ATOM
1772
CA
ARG A
258
82.544
26.437
38.321
1.000
18.05

ATOM
1773
CB
ARG A
258
82.840
27.868
37.900
1.000
17.08

ATOM
1774
CG
ARG A
258
81.674
28.634
37.604
1.000
18.32

ATOM
1775
CD
ARG A
258
81.189
27.958
36.030
1.000
21.14

ATOM
1776
NE
ARG A
258
80.078
28.673
35.403
1.000
21.78

ATOM
1777
CZ
ARG A
258
78.799
28.476
35.694
1.000
22.43

ATOM
1778
NH1
ARG A
258
77.865
29.176
35.066
1.000
18.08

ATOM
1779
NH2
ARG A
258
78.461
27.578
36.615
1.000
18.74

ATOM
1780
C
ARG A
258
83.813
25.725
38.774
1.000
21.78

ATOM
1781
O
ARG A
258
84.418
26.130
39.766
1.000
21.81

ATOM
1782
N
MET A
259
84.246
24.671
38.100
1.000
21.16

ATOM
1783
CA
MET A
259
85.366
23.892
38.637
1.000
23.09

ATOM
1784
CB
MET A
259
85.406
22.519
37.953
1.000
23.03

ATOM
1785
CG
MET A
259
84.099
21.752
38.058
1.000
26.30

ATOM
1786
SD
MET A
259
83.442
21.712
39.743
1.000
27.07

ATOM
1787
CE
MET A
259
84.624
20.636
40.546
1.000
26.15

ATOM
1788
C
MET A
259
86.723
24.554
38.505
1.000
29.45

ATOM
1789
O
MET A
259
87.113
25.112
37.473
1.000
28.26

ATOM
1790
N
GLN A
260
27.445
24.505
39.594
1.000
29.83

ATOM
1791
CA
GLN A
260
88.838
24.069
39.623
1.000
25.68

ATOM
1792
CB
GLN A
260
89.054
28.670
41.014
1.000
30.10

ATOM
1793
CG
GLN A
260
88.941
27.172
41.032
1.000
43.43

ATOM
1794
CD
GLN A
260
89.302
27.235
39.784
1.000
50.49

ATOM
1795
OE1
GLN A
260
90.325
28.634
39.755
1.000
40.10

ATOM
1796
NE2
GLN A
260
88.520
27.897
38.714
1.000
67.81

ATOM
1797
C
GLN A
260
89.862
24.012
39.243
1.000
24.65

ATOM
1798
O
GLN A
260
89.449
22.852
39.076
1.000
22.12

ATOM
1799
N
PRO A
261
91.136
24.340
39.072
1.000
22.80

ATOM
1800
CD
PRO A
261
91.766
25.666
39.162
1.000
26.19

ATOM
1801
CA
PRO A
261
92.121
23.308
38.708
1.000
22.38

ATOM
1802
CB
PRO A
261
93.465
24.021
35.882
1.000
23.53

ATOM
1803
CG
PRO A
261
93.140
25.448
35.596
1.000
27.38

ATOM
1804
C
PRO A
261
92.074
22.109
39.643
1.000
23.33

ATOM
1805
OT1
PRO A
261
92.038
22.366
40.861
1.000
26.80

ATOM
1806
OT2
PRO A
261
92.043
20.977
39.140
1.000
24.26

ATOM
1807
PN
LIG A
262
79.866
8.049
36.850
1.000
21.10

ATOM
1808
O1N
LIG A
262
77.161
9.214
37.816
1.000
19.63

ATOM
1809
O2N
LIG A
262
78.412
7.604
36.951
1.000
20.28

ATOM
1810
O3P
LIG A
262
77.863
6.917
37.203
1.000
23.34

ATOM
1811
O5M
LIG A
262
77.188
8.537
35.356
1.000
26.86

ATOM
1812
C5M
LIG A
262
76.146
8.614
34.334
1.000
23.59

ATOM
1813
C4M
LIG A
262
76.601
9..638
33.328
1.000
23.45

ATOM
1814
O4M
LIG A
262
76.662
10.947
33.848
1.000
26.65

ATOM
1815
C3M
LIG A
262
78.028
9.344
32.697
1.000
24.43

ATOM
1816
O3M
LIG A
262
78.068
9.688
31.290
1.000
32.36

ATOM
1817
C2M
LIG A
262
78.922
10.273
33.544
1.000
19.91

ATOM
1818
O2M
LIG A
262
80.125
10.601
32.794
1.000
18.63

ATOM
1819
C1M
LIG A
262
77.987
11.498
33.713
1.000
19.38

ATOM
1820
N1N
LIG A
262
78.345
12.467
34.776
1.000
15.56

ATOM
1821
C6N
LIG A
262
78.804
13.791
34.353
1.000
11.07

ATOM
1822
C5N
LIG A
262
79.102
14.736
35.267
1.000
22.79

ATOM
1823
C4N
LIG A
262
79.372
14.335
36.735
1.000
20.14

ATOM
1824
C3N
LIG A
262
78.582
13.044
37.131
1.000
15.94

ATOM
1825
C2N
LIG A
262
78.264
12.124
36.205
1.000
19.61

ATOM
1826
C7N
LIG A
262
78.486
12.780
38.627
1.000
18.21

ATOM
1827
O7N
LIG A
262
78.848
13.651
39.435
1.000
24.82

ATOM
1828
N7N
LIG A
262
78.006
11.610
38.987
1.000
18.62

ATOM
1829
PA
LIG A
262
77.561
5.422
37.391
1.000
28.11

ATOM
1830
O1A
LIG A
262
78.894
4.662
37.439
1.000
22.53

ATOM
1831
O2A
LIG A
262
76.764
5.153
38.682
1.000
33.29

ATOM
1832
O5B
LIG A
262
76.695
4.845
36.178
1.000
28.65

ATOM
1833
C5B
LIG A
262
77.355
4.504
34.932
1.000
32.11

ATOM
1834
C4B
LIG A
262
76.714
3.251
34.284
1.000
27.97

ATOM
1835
O4B
LIG A
262
77.188
3.143
32.914
1.000
32.15

ATOM
1836
C3B
LIG A
262
77.031
1.916
35.013
1.000
25.46

ATOM
1837
O3B
LIG A
262
75.811
1.148
35.157
1.000
32.29

ATOM
1838
C2B
LIG A
262
77.960
1.198
34.001
1.000
26.52

ATOM
1839
O2B
LIG A
262
77.862
−0.237
34.126
1.000
31.44

ATOM
1840
C1B
LIG A
262
77.427
1.738
32.649
1.000
33.69

ATOM
1841
N9A
LIG A
262
78.396
1.552
31.519
1.000
27.56

ATOM
1842
C4A
LIG A
262
78.161
1.003
30.254
1.000
22.23

ATOM
1843
N3A
LIG A
262
76.989
0.455
29.579
1.000
25.87

ATOM
1844
C2A
LIG A
262
77.176
0.033
28.351
1.000
26.73

ATOM
1845
N1A
LIG A
262
78.279
0.037
27.632
1.000
27.79

ATOM
1846
C6A
LIG A
262
79.396
0.518
28.154
1.000
27.44

ATOM
1847
C5A
LIG A
262
79.411
1.038
29.510
1.000
22.37

ATOM
1848
N7A
LIG A
262
80.444
1.588
30.265
1.000
23.23

ATOM
1849
C8A
LIG A
262
79.747
1.856
31.414
1.000
20.75

ATOM
1850
N6A
LIG A
262
80.554
0.221
27.558
1.000
28.05

ATOM
1851
C
LIG A
262
86.532
12.596
38.895
1.000
36.33

ATOM
1852
C1
LIG A
262
87.716
13.547
38.393
1.000
43.35

ATOM
1853
N
LIG A
262
88.747
13.908
39.257
1.000
45.45

ATOM
1854
O
LIG A
262
87.661
13.937
37.206
1.000
50.12

ATOM
1855
C2
LIG A
262
88.763
13.383
40.662
1.000
45.14

ATOM
1856
C3
LIG A
262
88.417
14.342
41.834
1.000
39.71

ATOM
1857
C4
LIG A
262
89.819
14.827
38.761
1.000
44.30

ATOM
1858
C5
LIG A
262
89.602
16.294
39.221
1.000
48.68

ATOM
1859
C6
LIG A
262
89.419
16.470
40.739
1.000
52.16

ATOM
1860
C7
LIG A
262
88.192
15.801
41.385
1.000
48.56

ATOM
1861
C8
LIG A
262
86.919
11.070
38.927
1.000
37.05

ATOM
1862
C9
LIG A
262
86.039
10.178
39.567
1.000
40.45

ATOM
1863
C10
LIG A
262
86.308
8.812
39.624
1.000
35.05

ATOM
1864
C11
LIG A
262
87.482
8.325
39.053
1.000
33.43

ATOM
1865
C12
LIG A
262
88.359
9.191
38.406
1.000
34.29

ATOM
1866
C13
LIG A
262
88.092
10.560
38.358
1.000
32.93

ATOM
1867
C15
LIG A
262
84.992
12.198
37.018
1.000
31.80

ATOM
1868
N1
LIG A
262
83.945
12.171
6.253
1.000
35.97

ATOM
1869
C16
LIG A
262
82.786
12.926
36.676
1.000
26.22

ATOM
1870
C17
LIG A
262
82.816
13.642
37.893
1.000
27.12

ATOM
1871
C18
LIG A
262
84.093
13.620
38.766
1.000
30.03

ATOM
1872
N2
LIG A
262
85.193
12.803
38.165
1.000
35.96

ATOM
1873
S
LIG A
262
84.095
14.537
40.290
1.000
29.89

ATOM
1874
C19
LIG A
262
81.624
14.284
38.089
1.000
27.34

ATOM
1875
N3
LIG A
262
80.834
13.998
36.974
1.000
26.99

ATOM
1876
N4
LIG A
262
81.533
13.152
36.151
1.000
21.47

ATOM
1877
CB
SER B
7
111.935
37.270
18.577
1.000
66.13

ATOM
1878
C
SER B
7
110.628
35.164
18.813
1.000
46.22

ATOM
1879
O
SER B
7
110.939
34.462
19.779
1.000
51.08

ATOM
1880
N
SER B
7
110.142
37.116
20.244
1.000
60.83

ATOM
1881
CA
SER B
7
110.571
36.681
18.917
1.000
52.01

ATOM
1882
N
VAL B
8
110.333
34.638
17.623
1.000
39.96

ATOM
1883
CA
VAL B
8
110.396
33.185
17.459
1.000
36.17

ATOM
1884
CB
VAL B
8
109.250
32.662
16.582
1.000
37.32

ATOM
1885
CG1
VAL B
8
107.898
33.067
17.159
1.000
31.50

ATOM
1886
CG2
VAL B
8
109.400
33.182
15.161
1.000
28.98

ATOM
1887
C
VAL B
8
111.745
32.781
16.869
1.000
30.70

ATOM
1888
O
VAL B
8
112.019
31.602
16.641
1.000
35.02

ATOM
1889
N
LYS B
9
112.596
33.767
16.617
1.000
27.16

ATOM
1890
CA
LYS B
9
113.944
33.473
16.135
1.000
30.39

ATOM
1891
CB
LYS B
9
114.753
34.756
15.991
1.000
29.44

ATOM
1892
C
LYS B
9
114.635
32.490
17.073
1.000
32.76

ATOM
1893
O
LYS B
9
114.688
32.689
18.289
1.000
35.63

ATOM
1894
N
GLY B
10
115.160
31.399
16.527
1.000
33.78

ATOM
1895
CA
GLY B
10
115.891
30.436
17.329
1.000
33.33

ATOM
1896
C
GLY B
10
115.042
29.382
17.990
1.000
32.26

ATOM
1897
O
GLY B
10
115.570
28.369
18.453
1.000
38.86

ATOM
1898
N
LEU B
11
113.729
29.580
18.047
1.000
28.07

ATOM
1899
CA
LEU B
11
112.840
28.565
18.607
1.000
23.95

ATOM
1900
CB
LEU B
11
111.455
29.191
18.812
1.000
26.82

ATOM
1901
CG
LEU B
11
111.409
30.356
19.811
1.000
33.74

ATOM
1902
CD1
LEU B
11
110.025
30.980
19.884
1.000
39.05

ATOM
1903
CD2
LEu B
11
111.848
29.890
21.194
1.000
29.81

ATOM
1904
C
LEU B
11
112.747
27.342
17.707
1.000
23.70

ATOM
1905
o
LEU B
11
112.922
27.452
16.490
1.000
26.55

ATOM
1906
N
VAL B
12
112.476
26.173
18.268
1.000
22.02

ATOM
1907
CA
VAL B
12
112.260
24.944
17.510
1.000
24.81

ATOM
1908
CB
VAL B
12
113.162
23.803
18.016
1.000
26.08

ATOM
1909
CG1
VAL B
12
112.893
22.513
17.258
1.000
24.44

ATOM
1910
CG2
VAL B
12
114.632
24.197
17.897
1.000
26.10

ATOM
1911
C
VAL B
12
110.804
24.489
17.581
1.000
28.66

ATOM
1912
O
VAL B
12
110.278
24.226
18.666
1.000
26.85

ATOM
1913
N
ALA B
13
110.140
24.380
16.440
1.000
26.46

ATOM
1914
CA
ALA B
13
108.743
23.981
16.366
1.000
26.62

ATOM
1915
CB
ALA B
13
107.929
25.058
15.643
1.000
22.29

ATOM
1916
C
ALA B
13
108.521
22.657
15.653
1.000
25.93

ATOM
1917
O
ALA B
13
109.050
22.444
14.556
1.000
27.28

ATOM
1918
N
VAL B
14
107.735
21.790
16.277
1.000
17.65

ATOM
1919
CA
VAL B
14
107.277
20.556
15.655
1.000
20.86

ATOM
1920
CB
VAL B
14
107.358
19.366
16.617
1.000
22.80

ATOM
1921
CG1
VAL B
14
106.621
18.133
16.114
1.000
19.92

ATOM
1922
CG2
VAL B
14
108.824
19.012
16.861
1.000
22.22

ATOM
1923
C
VAL B
14
105.849
20.790
15.160
1.000
27.03

ATOM
1924
O
VAL B
14
104.970
21.108
15.963
1.000
25.82

ATOM
1925
N
ILE B
15
105.610
20.658
13.868
1.000
26.11

ATOM
1926
CA
ILE B
15
104.313
20.975
13.264
1.000
24.37

ATOM
1927
CB
ILE B
15
104.478
22.167
12.296
1.000
26.30

ATOM
1928
CG2
ILE B
15
103.173
22.574
11.630
1.000
22.89

ATOM
1929
CG1
ILE B
15
105.139
23.381
12.966
1.000
25.67

ATOM
1930
CD1
ILE B
15
105.607
24.422
11.979
1.000
30.46

ATOM
1931
C
ILE B
15
103.704
19.784
12.549
1.000
23.69

ATOM
1932
O
ILE B
15
104.196
19.329
11.517
1.000
22.43

ATOM
1933
N
THR B
16
102.611
19.249
13.089
1.000
22.07

ATOM
1934
CA
THR B
16
101.905
18.147
12.451
1.000
22.03

ATOM
1935
CB
THR B
16
101.071
17.349
13.471
1.000
21.22

ATOM
1936
OG1
THR B
16
99.840
18.027
13.733
1.000
23.42

ATOM
1937
CG2
THR B
16
101.799
17.252
14.806
1.000
16.43

ATOM
1938
C
THR B
16
101.012
18.664
11.324
1.000
17.32

ATOM
1939
O
THR B
16
100.520
19.792
11.351
1.000
22.26

ATOM
1940
N
GLY B
17
100.795
17.843
10.306
1.000
20.98

ATOM
1941
CA
GLY B
17
100.165
18.276
9.067
1.000
21.27

ATOM
1942
C
GLY B
17
101.035
19.294
8.350
1.000
25.39

ATOM
1943
O
GLY B
17
100.598
20.121
7.545
1.000
22.63

ATOM
1944
N
GLY B
18
102.337
19.254
8.646
1.000
23.37

ATOM
1945
CA
GLY B
18
103.254
20.254
8.127
1.000
20.34

ATOM
1946
C
GLY B
18
103.480
20.154
6.629
1.000
21.06

ATOM
1947
O
GLY B
18
104.077
21.066
6.057
1.000
22.45

ATOM
1948
N
ALA B
19
103.026
19.092
5.966
1.000
21.71

ATOM
1949
CA
ALA B
19
103.241
18.974
4.525
1.000
23.71

ATOM
1950
CB
ALA B
19
103.100
17.520
4.099
1.000
21.03

ATOM
1951
C
ALA B
19
102.286
19.849
3.726
1.000
29.96

ATOM
1952
O
ALA B
19
102.472
20.117
2.538
1.000
27.73

ATOM
1953
N
SER B
20
101.225
20.333
4.367
1.000
23.76

ATOM
1954
CA
SER B
20
100.184
21.004
3.590
1.000
22.85

ATOM
1955
CB
SER B
20
99.207
19.923
3.103
1.000
26.71

ATOM
1956
OG
SER B
20
98.093
20.470
2.425
1.000
31.44

ATOM
1957
C
SER B
20
99.454
22.065
4.395
1.000
29.26

ATOM
1958
O
SER B
20
99.625
22.195
5.609
1.000
27.20

ATOM
1959
N
GLY B
21
98.634
22.827
3.687
1.000
26.85

ATOM
1960
CA
GLY B
21
97.667
23.751
4.207
1.000
22.83

ATOM
1961
C
GLY B
21
98.094
24.570
5.391
1.000
26.72

ATOM
1962
O
GLY B
21
99.054
25.337
5.312
1.000
19.24

ATOM
1963
N
LEU B
22
97.365
24.441
6.509
1.000
22.57

ATOM
1964
CA
LEU B
22
97.659
25.336
7.627
1.000
22.91

ATOM
1965
CB
LEU B
22
96.548
25.233
8.679
1.000
24.42

ATOM
1966
CG
LEU B
22
95.151
25.647
8.208
1.000
20.85

ATOM
1967
CD1
LEU B
22
94.133
25.482
9.327
1.000
15.35

ATOM
1968
CD2
LEU B
22
95.161
27.077
7.699
1.000
20.68

ATOM
1969
C
LEU B
22
99.028
25.041
8.237
1.000
19.89

ATOM
1970
O
LEU B
22
99.782
25.970
8.539
1.000
25.67

ATOM
1971
N
GLY B
23
99.359
23.766
8.424
1.000
22.60

ATOM
1972
CA
GLY B
23
100.651
23.436
9.030
1.000
27.37

ATOM
1973
C
GLY B
23
101.807
23.934
8.185
1.000
25.30

ATOM
1974
O
GLY B
23
102.762
24.548
8.660
1.000
21.48

ATOM
1975
N
LEU B
24
101.703
23.677
6.878
1.000
23.68

ATOM
1976
CA
LEU B
24
102.735
24.155
5.959
1.000
20.25

ATOM
1977
CB
LEU B
24
102.420
23.731
4.528
1.000
21.69

ATOM
1978
CG
LEU B
24
103.390
24.209
3.444
1.000
23.32

ATOM
1979
CD1
LEU B
24
104.833
23.871
3.784
1.000
23.41

ATOM
1980
CD2
LEU B
24
103.000
23.591
2.103
1.000
25.33

ATOM
1981
C
LEU B
24
102.892
25.663
6.030
1.000
20.67

ATOM
1982
O
LEU B
24
104.013
26.176
6.115
1.000
24.35

ATOM
1983
N
ALA B
25
101.772
26.390
6.006
1.000
24.78

ATOM
1984
CA
ALA B
25
101.832
27.851
6.098
1.000
20.17

ATOM
1985
CB
ALA B
25
100.444
28.459
6.025
1.000
18.79

ATOM
1986
C
ALA B
25
102.528
28.289
7.381
1.000
24.83

ATOM
1987
O
ALA B
25
103.263
29.274
7.409
1.000
27.08

ATOM
1988
N
THR B
26
102.283
27.539
8.455
1.000
23.74

ATOM
1989
CA
THR B
26
102.908
27.892
9.733
1.000
23.95

ATOM
1990
CB
THR B
26
102.271
27.065
10.862
1.000
27.15

ATOM
1991
OG1
THR B
26
100.870
27.390
10.918
1.000
20.96

ATOM
1992
CG2
THR B
26
102.862
27.405
12.213
1.000
14.50

ATOM
1993
C
THR B
26
104.415
27.688
9.653
1.000
21.31

ATOM
1994
O
THR B
26
105.202
28.552
10.040
1.000
23.66

ATOM
1995
N
ALA B
27
104.825
26.540
9.126
1.000
19.96

ATOM
1996
CA
ALA B
27
106.248
26.260
8.935
1.000
25.17

ATOM
1997
CB
ALA B
27
106.418
24.912
8.249
1.000
25.01

ATOM
1998
C
ALA B
27
106.931
27.354
8.126
1.000
26.74

ATOM
1999
O
ALA B
27
107.949
27.905
8.542
1.000
27.61

ATOM
2000
N
GLU B
28
106.372
27.679
6.963
1.000
24.69

ATOM
2001
CA
GLU B
28
106.950
28.704
6.105
1.000
25.04

ATOM
2002
CB
GLU B
28
106.027
28.975
4.911
1.000
26.62

ATOM
2003
CG
GLU B
28
106.168
27.956
3.796
1.000
29.46

ATOM
2004
CD
GLU B
28
105.090
28.019
2.739
1.000
34.48

ATOM
2005
OE1
GLU B
28
105.230
27.290
1.733
1.000
37.01

ATOM
2006
OE2
GLU B
28
104.104
28.772
2.894
1.000
38.70

ATOM
2007
C
GLU B
28
107.196
29.999
6.861
1.000
28.38

ATOM
2008
O
GLU B
28
108.280
30.567
6.830
1.000
22.48

ATOM
2009
N
ARG B
29
106.170
30.468
7.572
1.000
26.36

ATOM
2010
CA
ARG B
29
106.300
31.722
8.295
1.000
27.51

ATOM
2011
CB
ARG B
29
104.930
32.181
8.837
1.000
22.39

ATOM
2012
CG
ARG B
29
105.045
33.565
9.447
1.000
23.62

ATOM
2013
CD
ARG B
29
103.721
34.034
10.040
1.000
26.86

ATOM
2014
NE
ARG B
29
103.902
35.402
10.544
1.000
28.00

ATOM
2015
CZ
ARG B
29
103.723
36.469
9.770
1.000
30.37

ATOM
2016
NE1
ARG B
29
103.907
37.674
10.276
1.000
29.53

ATOM
2017
NH2
ARG B
29
103.359
36.297
8.506
1.000
28.65

ATOM
2018
C
ARG B
29
107.291
31.618
9.444
1.000
28.71

ATOM
2019
Oo
ARG B
29
108.116
32.510
9.652
1.000
29.86

ATOM
2020
N
LEU B
30
107.236
30.533
10.224
1.000
24.31

ATOM
2021
CA
LEU B
30
108.179
30.478
11.349
1.000
26.41

ATOM
2022
CB
LEU B
30
107.813
29.347
12.302
1.000
23.96

ATOM
2023
CG
LEU B
30
106.436
29.430
12.973
1.000
23.79

ATOM
2024
CD1
LEU B
30
106.267
28.268
13.944
1.000
17.95

ATOM
2025
CD2
LEU B
30
106.228
30.765
13.668
1.000
24.22

ATOM
2026
C
LEU B
30
109.616
30.343
10.853
1.000
31.93

ATOM
2027
O
LEU B
30
110.527
31.003
11.357
1.000
30.60

ATOM
2028
N
VAL B
31
109.840
29.485
9.858
1.000
26.74

ATOM
2029
CA
VAL B
31
111.190
29.383
9.287
1.000
31.33

ATOM
2030
CB
VAL B
31
111.255
28.275
8.221
1.000
34.12

ATOM
2031
CG1
VAL B
31
112.445
28.443
7.291
1.000
40.80

ATOM
2032
CG2
VAL B
31
111.305
26.915
8.908
1.000
27.68

ATOM
2033
C
VAL B
31
111.609
30.722
8.705
1.000
32.48

ATOM
2034
O
VAL B
31
112.725
31.203
8.897
1.000
33.88

ATOM
2035
N
GLY B
32
110.692
31.370
7.982
1.000
24.58

ATOM
2036
CA
GLY B
32
110.995
32.685
7.451
1.000
26.48

ATOM
2037
C
GLY B
32
111.368
33.677
8.531
1.000
33.49

ATOM
2038
O
GLY B
32
112.062
34.657
8.266
1.000
31.55

ATOM
2039
N
GLN B
33
110.918
33.443
9.760
1.000
37.11

ATOM
2040
CA
GLN B
33
111.183
34.351
10.868
1.000
35.69

ATOM
2041
CB
GLN B
33
109.978
34.440
11.811
1.000
41.00

ATOM
2042
CG
GLN B
33
108.656
34.800
11.155
1.000
43.78

ATOM
2043
CD
GLN B
33
108.409
36.287
11.106
1.000
45.96

ATOM
2044
OE1
GLN B
33
108.660
36.975
12.095
1.000
56.75

ATOM
2045
NE2
GLN B
33
107.927
36.777
9.972
1.000
58.65

ATOM
2046
C
GLN B
33
112.390
33.917
11.688
1.000
33.13

ATOM
2047
O
GLN B
33
112.636
34.505
12.745
1.000
32.32

ATOM
2048
N
GLY B
34
113.148
32.913
11.256
1.000
30.65

ATOM
2049
CA
GLY B
34
114.338
32.544
12.011
1.000
30.69

ATOM
2050
C
GLY B
34
114.173
31.350
12.916
1.000
33.53

ATOM
2051
O
GLY B
34
115.124
30.941
13.593
1.000
34.90

ATOM
2052
N
ALA B
35
112.994
30.732
12.972
1.000
28.17

ATOM
2053
CA
ALA B
35
112.817
29.534
13.781
1.000
24.02

ATOM
2054
CB
ALA B
35
111.343
29.442
14.168
1.000
27.36

ATOM
2055
C
ALA B
35
113.262
28.268
13.064
1.000
24.80

ATOM
2056
O
ALA B
35
113.543
28.284
11.863
1.000
29.10

ATOM
2057
N
SER B
36
113.339
27.139
13.766
1.000
21.95

ATOM
2058
CA
SER B
36
113.601
25.861
13.109
1.000
31.07

ATOM
2059
CB
SER B
36
114.705
25.069
13.814
1.000
28.05

ATOM
2060
OG
SER B
36
115.900
25.829
13.875
1.000
35.09

ATOM
2061
C
SER B
36
112.323
25.037
13.067
1.000
33.10

ATOM
2062
O
SER B
36
111.495
25.123
13.982
1.000
29.14

ATOM
2063
N
ALA B
37
112.102
24.227
12.030
1.000
28.97

ATOM
2064
CA
ALA B
37
110.812
23.522
12.032
1.000
28.78

ATOM
2065
CB
ALA B
37
109.801
24.213
11.123
1.000
28.35

ATOM
2066
C
ALA B
37
110.956
22.066
11.632
1.000
28.14

ATOM
2067
O
ALA B
37
111.725
21.696
10.746
1.000
31.18

ATOM
2068
N
VAL B
38
110.170
21.241
12.323
1.000
2S.45

ATOM
2069
CA
VAL B
38
110.026
19.846
11.961
1.000
22.16

ATOM
2070
CB
VAL B
38
110.207
18.872
13.132
1.000
25.04

ATOM
2071
CD1
VAL B
38
110.049
17.452
12.602
1.000
24.40

ATOM
2072
CG2
VAL B
38
111.554
19.045
13.807
1.000
33.39

ATOM
2073
C
VAL B
38
108.629
19.628
11.377
1.000
27.42

ATOM
2074
O
VAL B
38
107.645
19.860
12.081
1.000
28.93

ATOM
2075
N
LEU B
39
108.584
19.205
10.125
1.000
26.52

ATOM
2076
CA
LEU B
39
107.331
18.890
9.462
1.000
25.31

ATOM
2077
CB
LEU B
39
107.440
19.084
7.947
1.000
22.95

ATOM
2078
CG
LEU B
39
108.057
20.391
7.464
1.000
21.80

ATOM
2079
CD1
LEU B
39
107.904
20.508
5.951
1.000
22.36

ATOM
2080
CD2
LEU B
39
107.425
21.579
8.178
1.000
22.97

ATOM
2081
C
LEU B
39
106.914
17.455
9.749
1.000
25.46

ATOM
2082
O
LEU B
39
107.489
16.500
9.232
1.000
26.63

ATOM
2083
N
LEU B
40
105.897
17.315
10.591
1.000
23.83

ATOM
2084
CA
LEU B
40
105.426
15.985
10.972
1.000
21.42

ATOM
2085
CB
LEU B
40
105.097
15.966
12.470
1.000
18.48

ATOM
2086
CG
LEU B
40
105.036
14.599
13.150
1.000
25.45

ATOM
2087
CD1
LEU B
40
105.258
14.749
14.649
1.000
26.21

ATOM
2088
CD2
LEU B
40
103.719
13.884
12.872
1.000
26.04

ATOM
2089
C
LEU B
40
104.218
15.623
10.120
1.000
28.34

ATOM
2090
O
LEU B
40
103.156
16.248
10.223
1.000
25.37

ATOM
2091
N
ASP B
41
104.353
14.609
9.267
1.000
28.65

ATOM
2092
CA
ASP B
41
103.254
14.287
8.354
1.000
26.00

ATOM
2093
CB
ASP B
41
103.214
15.303
7.213
1.000
20.92

ATOM
2094
CG
ASP B
41
101.812
15.531
6.671
1.000
29.64

ATOM
2095
OD1
ASP B
41
101.105
14.524
6.429
1.000
27.42

ATOM
2096
OD2
ASP B
41
101.405
16.703
6.478
1.000
26.42

ATOM
2097
C
ASP B
41
103.396
12.858
7.850
1.000
29.93

ATOM
2098
O
ASP B
41
104.359
12.163
8.188
1.000
26.42

ATOM
2099
N
LEU B
42
102.437
12.392
7.051
1.000
28.41

ATOM
2100
CA
LEU B
42
102.481
11.005
6.581
1.000
27.15

ATOM
2101
CB
LEU B
42
101.108
10.576
6.063
1.000
27.77

ATOM
2102
CG
LEU B
42
99.985
10.577
7.115
1.000
29.61

ATOM
2103
CD1
LEU B
42
98.614
10.414
6.481
1.000
27.21

ATOM
2104
CD2
LEU B
42
100.221
9.488
8.154
1.000
19.92

ATOM
2105
C
LEU B
42
103.574
10.841
5.531
1.000
25.47

ATOM
2106
O
LEU B
42
103.937
11.779
4.822
1.000
22.04

ATOM
2107
N
PRO B
43
104.122
9.639
5.436
1.000
29.99

ATOM
2108
CD
PRO B
43
103.694
8.435
6.176
1.000
32.56

ATOM
2109
CA
PRO B
43
105.242
9.382
4.537
1.000
31.41

ATOM
2110
CB
PRO B
43
105.524
7.885
4.706
1.000
29.49

ATOM
2111
CG
PRO B
43
104.804
7.459
5.934
1.000
32.19

ATOM
2112
C
PRO B
43
104.892
9.640
3.079
1.000
32.37

ATOM
2113
O
PRO B
43
105.741
10.056
2.290
1.000
40.08

ATOM
2114
N
ASN B
44
103.649
9.379
2.688
1.000
32.25

ATOM
2115
CA
ASN B
44
103.351
9.437
1.251
1.000
42.24

ATOM
2116
CB
ASN B
44
102.182
8.494
0.942
1.000
51.15

ATOM
2117
CG
ASN B
44
101.098
8.594
2.004
1.000
57.16

ATOM
2118
OD1
ASN B
44
101.059
7.778
2.927
1.000
69.55

ATOM
2119
ND2
ASN B
44
100.233
9.594
1.871
1.000
64.33

ATOM
2120
C
ASN B
44
103.050
10.848
0.782
1.000
38.90

ATOM
2121
O
ASN B
44
102.817
11.126
−0.391
1.000
43.08

ATOM
2122
N
SER B
45
103.044
11.795
1.706
1.000
38.17

ATOM
2123
CA
SER B
45
102.784
13.191
1.397
1.000
32.01

ATOM
2124
CB
SER B
45
102.407
13.904
2.699
1.000
32.03

ATOM
2125
OG
SER B
45
103.500
13.896
3.615
1.000
31.99

ATOM
2126
C
SER B
45
104.006
13.834
0.765
1.000
37.39

ATOM
2127
O
SER B
45
105.029
13.173
0.571
1.000
64.10

ATOM
2128
N
GLY B
46
103.940
15.127
0.453
1.000
31.91

ATOM
2129
CA
GLY B
46
105.100
15.848
−0.037
1.000
32.05

ATOM
2130
C
GLY B
46
105.862
16.554
1.068
1.000
29.66

ATOM
2131
O
GLY B
46
106.422
17.629
0.865
1.000
28.80

ATOM
2132
N
GLY B
47
105.917
15.984
2.274
1.000
27.32

ATOM
2133
CA
GLY B
47
106.644
16.681
3.330
1.000
30.59

ATOM
2134
C
GLY B
47
108.119
16.856
3.032
1.000
33.46

ATOM
2135
O
GLY B
47
108.684
17.915
3.326
1.000
29.47

ATOM
2136
N
GLD B
48
108.764
15.832
2.466
1.000
29.78

ATOM
2137
CA
GLU B
48
110.212
15.914
2.232
1.000
32.49

ATOM
2138
CB
GLU B
48
110.744
14.610
1.647
1.000
36.34

ATOM
2139
CG
GLU B
48
112.256
14.551
1.507
1.000
46.76

ATOM
2140
CD
GLU B
48
112.991
14.939
2.774
1.000
58.39

ATOM
2141
OE1
GLU B
48
113.372
16.117
2.956
1.000
65.04

ATOM
2142
OE2
GLU B
48
113.207
14.028
3.606
1.000
69.75

ATOM
2143
C
GLU B
48
110.524
17.101
1.331
1.000
29.02

ATOM
2144
0
GLU B
48
111.404
17.915
1.607
1.000
34.13

ATOM
2145
N
ALA B
49
109.785
17.216
0.234
1.000
26.82

ATOM
2146
CA
ALA B
49
110.004
18.341
−0.673
1.000
30.63

ATOM
2147
CB
ALA B
49
109.092
18.199
−1.886
1.000
29.53

ATOM
2148
C
ALA B
49
109.794
19.675
0.022
1.000
29.76

ATOM
2149
O
ALA B
49
110.547
20.635
−0.182
1.000
23.29

ATOM
2150
N
GLN B
50
108.761
19.788
0.867
1.000
27.24

ATOM
2151
CA
GLN B
50
108.548
21.102
1.495
1.000
25.56

ATOM
2152
CB
GLN B
50
107.198
21.202
2.190
1.000
23.47

ATOM
2153
CG
GLN B
50
105.977
20.906
1.343
1.000
24.08

ATOM
2154
CD
GLN B
50
105.804
21.782
0.126
1.000
29.27

ATOM
2155
OE1
GLN B
50
105.277
21.374
−0.913
1.000
47.91

ATOM
2156
NE2
GLN B
50
106.246
23.030
0.225
1.000
26.60

ATOM
2157
C
GLN B
50
109.685
21.407
2.470
1.000
24.41

ATOM
2158
O
GLN B
50
110.136
22.545
2.584
1.000
24.06

ATOM
2159
N
ALA B
51
110.164
20.382
3.167
1.000
26.27

ATOM
2160
CA
ALA B
51
111.284
20.572
4.092
1.000
28.44

ATOM
2161
CB
ALA B
51
111.492
19.317
4.921
1.000
27.41

ATOM
2162
C
ALA B
51
112.549
20.947
3.328
1.000
31.71

ATOM
2163
O
ALA B
51
113.313
21.838
3.699
1.000
26.46

ATOM
2164
N
LYS B
52
112.792
20.260
2.206
1.000
31.97

ATOM
2165
CA
LYS B
52
113.941
20.629
1.370
1.000
32.72

ATOM
2166
CB
LYS B
52
114.046
19.675
0.190
1.000
37.57

ATOM
2167
CG
LYS B
52
114.741
20.219
−1.041
1.000
48.41

ATOM
2168
CD
LY5 B
52
113.843
20.066
−2.266
1.000
61.11

ATOM
2169
CE
LY5 B
52
112.614
20.953
−2.133
1.000
65.36

ATOM
2170
NZ
LY5 B
52
111.536
20.598
−3.095
1.000
32.81

ATOM
2171
C
LY5 B
52
113.812
22.074
0.919
1.000
31.76

ATOM
2172
O
LY5 B
52
114.749
22.872
1.011
1.000
30.51

ATOM
2173
N
LY5 B
53
112.625
22.447
0.436
1.000
30.99

ATOM
2174
CA
LY5 B
53
112.430
23.823
−0.007
1.000
34.36

ATOM
2175
CB
LY5 B
53
111.017
24.015
−0.558
1.000
35.38

ATOM
2176
C
LY5 B
53
112.670
24.835
1.104
1.000
35.83

ATOM
2177
O
LY5 B
53
113.099
25.966
0.863
1.000
37.38

ATOM
2178
N
LEU B
54
112.376
24.467
2.355
1.000
34.60

ATOM
2179
CA
LEU B
54
112.414
25.524
3.378
1.000
32.04

ATOM
2180
CB
LEU B
54
111.386
25.206
4.469
1.000
27.56

ATOM
2181
CG
LEU B
54
109.951
25.622
4.092
1.000
29.64

ATOM
2182
CD1
LEU B
54
108.940
25.049
5.072
1.000
26.83

ATOM
2183
CD2
LEU B
54
109.854
27.139
4.005
1.000
28.08

ATOM
2184
C
LEU B
54
113.803
25.751
3.946
1.000
30.99

ATOM
2185
O
LEU B
54
114.035
26.722
4.670
1.000
36.53

ATOM
2186
N
GLY B
55
114.760
24.889
3.613
1.000
35.24

ATOM
2187
CA
GLY B
55
116.145
25.129
3.970
1.000
28.30

ATOM
2188
C
GLY B
55
116.658
24.251
5.088
1.000
28.98

ATOM
2189
O
GLY B
55
115.983
23.344
5.577
1.000
26.51

ATOM
2190
N
A5N B
56
117.886
24.525
5.500
1.000
31.16

ATOM
2191
CA
A5N B
56
118.579
23.765
6.527
1.000
37.68

ATOM
2192
CB
A5N B
56
120.017
24.285
6.673
1.000
45.44

ATOM
2193
CG
A5N B
56
120.802
24.041
5.394
1.000
53.62

ATOM
2194
OD1
A5N B
56
121.666
24.836
5.028
1.000
63.23

ATOM
2195
ND2
A5N B
56
120.488
22.943
4.713
1.000
51.47

ATOM
2196
C
A5N B
56
117.884
23.822
7.876
1.000
35.34

ATOM
2197
O
A5N B
56
118.077
22.918
8.695
1.000
36.61

ATOM
2198
N
A5N B
57
117.080
24.852
8.124
1.000
35.84

ATOM
2199
CA
A5N B
57
116.390
24.941
9.415
1.000
33.51

ATOM
2200
CB
A5N B
57
116.150
26.402
9.776
1.000
34.67

ATOM
2201
CG
A5N B
57
117.396
27.188
10.107
1.000
37.48

ATOM
2202
OD1
A5N B
57
117.464
28.386
9.831
1.000
44.60

ATOM
2203
ND2
A5N B
57
118.378
26.525
10.702
1.000
40.04

ATOM
2204
C
A5N B
57
115.062
24.188
9.411
1.000
34.71

ATOM
2205
O
A5N B
57
114.259
24.325
10.339
1.000
30.75

ATOM
2206
N
CY5 B
58
114.815
23.385
8.381
1.000
29.69

ATOM
2207
CA
CY5 B
58
113.570
22.626
8.314
1.000
31.12

ATOM
2208
CB
CY5 B
58
112.554
23.328
7.403
1.000
28.69

ATOM
2209
5G
CY5 B
58
110.969
22.451
7.263
1.000
28.53

ATOM
2210
C
CYS B
58
113.803
21.196
7.842
1.000
29.28

ATOM
2211
O
CYS B
58
114.439
20.961
6.813
1.000
32.21

ATOM
2212
N
VAL B
59
113.295
20.221
8.587
1.000
26.05

ATOM
2213
CA
VAL B
59
113.388
18.827
8.185
1.000
27.33

ATOM
2214
CB
VAL B
59
114.370
18.032
9.068
1.000
35.06

ATOM
2215
CG1
VAL B
59
115.723
18.727
9.136
1.000
33.58

ATOM
2216
CG2
VAL B
59
113.819
17.829
10.473
1.000
34.14

ATOM
2217
C
VAL B
59
112.021
18.148
8.226
1.000
27.96

ATOM
2218
O
VAL B
59
111.077
18.615
8.868
1.000
29.69

ATOM
2219
N
PHE B
60
111.910
17.034
7.523
1.000
26.97

ATOM
2220
CA
PHE B
60
110.708
16.227
7.457
1.000
26.91

ATOM
2221
CB
PEE B
60
110.427
15.790
6.020
1.000
25.25

ATOM
2222
CG
PHE B
60
109.323
14.749
5.896
1.000
29.29

ATOM
2223
CD1
PHE B
60
108.032
15.040
6.313
1.000
29.86

ATOM
2224
CD2
PHE B
60
109.578
13.496
5.370
1.000
28.92

ATOM
2225
CE1
PHE B
60
107.038
14.090
6.198
1.000
27.49

ATOM
2226
CE2
PHE B
60
108.586
12.541
5.248
1.000
26.44

ATOM
2227
CZ
PHE B
60
107.300
12.839
5.667
1.000
25.34

ATOM
2228
C
PHE B
60
110.830
14.998
8.353
1.000
30.94

ATOM
2229
O
PHE B
60
111.820
14.270
8.314
1.000
25.53

ATOM
2230
N
ALA B
61
109.800
14.783
9.167
1.000
28.55

ATOM
2231
CA
ALA B
61
109.720
13.601
10.013
1.000
25.87

ATOM
2232
CB
ALA B
61
109.776
13.997
11.480
1.000
26.71

ATOM
2233
C
ALA B
61
108.444
12.838
9.687
1.000
27.90

ATOM
2234
O
ALA B
61
107.358
13.292
10.060
1.000
32.37

ATOM
2235
N
PRO B
62
108.554
11.718
8.984
1.000
30.44

ATOM
2236
CD
PRO B
62
109.781
11.150
8.400
1.000
27.89

ATOM
2237
CA
PRO B
62
107.376
10.900
8.679
1.000
29.03

ATOM
2238
CB
PRO B
62
107.922
9.757
7.816
1.000
28.20

ATOM
2239
CG
PRO B
62
109.385
9.732
8.097
1.000
28.71

ATOM
2240
C
PRO B
62
106.750
10.325
9.944
1.000
29.30

ATOM
2241
O
PRO B
62
107.417
9.731
10.789
1.000
30.53

ATOM
2242
N
ALA B
63
105.439
10.485
10.095
1.000
27.18

ATOM
2243
CA
ALA B
63
104.766
9.913
11.259
1.000
27.63

ATOM
2244
CB
ALA B
63
105.180
10.646
12.524
1.000
23.24

ATOM
2245
C
ALA B
63
103.249
9.974
11.099
1.000
23.37

ATOM
2246
O
ALA B
63
102.722
10.929
10.526
1.000
27.56

ATOM
2247
N
ASP B
64
102.583
8.953
11.609
1.000
24.35

ATOM
2248
CA
ASP B
64
101.133
8.963
11.799
1.000
26.55

ATOM
2249
CB
ASP B
64
100.551
7.597
11.478
1.000
24.92

ATOM
2250
CG
ASP B
64
99.045
7.527
11.597
1.000
25.45

ATOM
2251
OD1
ASP B
64
98.476
6.566
11.044
1.000
32.77

ATOM
2252
OD2
ASP B
64
98.418
8.396
12.227
1.000
28.70

ATOM
2253
C
ASP B
64
100.836
9.364
13.243
1.000
26.22

ATOM
2254
O
ASP B
64
101.328
8.686
14.153
1.000
22.25

ATOM
2255
N
VAL B
65
100.072
10.435
13.456
1.000
29.99

ATOM
2256
CA
VAL B
65
99.881
10.939
14.821
1.000
24.56

ATOM
2257
CB
VAL B
65
99.246
12.340
14.882
1.000
24.64

ATOM
2258
CG1
VAL B
65
100.144
13.380
14.212
1.000
20.71

ATOM
2259
CG2
VAL B
65
97.855
12.336
14.260
1.000
19.79

ATOM
2260
C
VAL B
65
99.029
9.988
15.655
1.000
21.85

ATOM
2261
O
VAL B
65
98.984
10.127
16.883
1.000
27.56

ATOM
2262
N
TSR B
66
98.358
9.029
15.024
1.000
18.06

ATOM
2263
CA
TSR B
66
97.587
8.071
15.806
1.000
23.90

ATOM
2264
CB
TSR B
66
96.458
7.415
14.988
1.000
27.89

ATOM
2265
OD1
TSR B 66
97.053
6.676
13.911
1.000
30.40

ATOM
2266
CG2
TSR B 66
95.531
8.457
14.387
1.000
26.02

ATOM
2267
C
TSR B
66
98.477
6.956
16.354
1.000
25.80

ATOM
2268
O
TSR B
66
97.994
6.069
17.052
1.000
28.04

ATOM
2269
N
SER B
67
99.765
6.987
16.043
1.000
26.27

ATOM
2270
CA
SER B
67
100.658
5.901
16.457
1.000
28.10

ATOM
2271
CB
SER B
67
101.309
5.256
15.229
1.000
22.33

ATOM
2272
OG
SER B
67
102.655
4.885
15.432
1.000
26.97

ATOM
2273
CB
SER B
67
101.718
6.397
17.438
1.000
25.97

ATOM
2274
O
SER B
67
102.509
7.2881
7.137
1.000
28.64

ATOM
2275
N
GLU B
68
101.742
5.8121
8.628
1.000
25.20

ATOM
2276
CA
GLU B
68
102.668
6.2401
9.678
1.000
28.93

ATOM
2277
CB
GLU B
68
102.418
5.401
20.920
1.000
29.49

ATOM
2278
CG
GLU B
68
103.467
5.385
22.009
1.000
32.30

ATOM
2279
CD
GLU B
68
102.977
4.561
23.196
1.000
38.17

ATOM
2280
OE1
GLU B 68
102.637
5.171
24.237
1.000
35.47

ATOM
2281
OE2
GLU B 68
102.917
3.315
23.091
1.000
44.60

ATOM
2282
C
GLU B
68
104.110
6.125
19.201
1.000
26.61

ATOM
2283
O
GLU B
68
104.899
7.061
19.313
1.000
23.88

ATOM
2284
N
LYS B
69
104.437
4.958
18.662
1.000
24.43

ATOM
2285
CA
LYS B
69
105.780
4.698
18.156
1.000
27.96

ATOM
2286
CB
LYS B
69
105.851
3.281
17.595
1.000
34.89

ATOM
2287
C
LYS B
69
106.202
5.708
17.100
1.000
27.55

ATOM
2288
O
LYS B
69
107.302
6.264
17.148
1.000
26.09

ATOM
2289
N
ASP B
70
105.324
5.973
16.128
1.000
26.32

ATOM
2290
CA
ASP B
70
105.666
6.951
15.094
1.000
25.61

ATOM
2291
CB
ASP B
70
104.521
7.076
14.090
1.000
29.36

ATOM
2292
CG
ASP B
70
104.475
5.972
13.052
1.000
32.02

ATOM
2293
OD1
ASP B
70
105.238
4.989
13.156
1.000
28.74

ATOM
2294
OD2
ASP B
70
103.655
6.078
12.105
1.000
31.35

ATOM
2295
C
ASP B
70
105.969
8.310
15.703
1.000
25.58

ATOM
2296
O
ASP B
70
106.940
8.988
15.360
1.000
25.97

ATOM
2297
N
VAL B
71
105.114
8.758
16.635
1.000
27.46

ATOM
2298
CA
VAL B
71
105.340
10.110
17.172
1.000
23.79

ATOM
2299
CB
VAL B
71
104.121
10.602
17.966
1.000
23.68

ATOM
2300
CD1
VAL B
71
104.423
11.915
18.668
1.000
22.16

ATOM
2301
CG2
VAL B
71
102.929
10.759
17.030
1.000
27.40

ATOM
2302
C
VAL B
71
106.598
10.124
18.025
1.000
23.50

ATOM
2303
O
VAL B
71
107.373
11.079
18.014
1.000
25.44

ATOM
2304
N
GLN B
72
106.808
9.037
18.777
1.000
22.76

ATOM
2305
CA
GLN B
72
108.078
8.961
19.507
1.000
28.52

ATOM
2306
CB
GLN B
72
108.135
7.661
20.313
1.000
28.51

ATOM
2307
CG
GLN B
72
107.370
7.770
21.621
1.000
29.69

ATOM
2308
CD
GLN B
72
107.251
6.451
22.355
1.000
35.53

ATOM
2309
OE1
GLN B
72
106.976
5.411
21.762
1.000
42.43

ATOM
2310
NE2
GLN B
72
107.450
6.507
23.669
1.000
42.60

ATOM
2311
C
GLN B
72
109.238
9.055
18.532
1.000
27.07

ATOM
2312
O
GLN B
72
110.206
9.781
18.738
1.000
30.00

ATOM
2313
N
THR B
73
109.126
8.301
17.432
1.000
23.90

ATOM
2314
CA
THR B
73
110.180
8.335
16.419
1.000
30.39

ATOM
2315
CB
THR B
73
109.809
7.402
15.245
1.000
37.28

ATOM
2316
OG1
THR B
73
109.774
6.051
15.729
1.000
35.29

ATOM
2317
CG2
THR B
73
110.846
7.464
14.138
1.000
35.54

ATOM
2318
C
THR B
73
110.426
9.744
15.905
1.000
31.92

ATOM
2319
O
THR B
73
111.559
10.226
15.830
1.000
33.51

ATOM
2320
N
ALA B
74
109.341
10.436
15.545
1.000
27.80

ATOM
2321
CA
ALA B
74
109.484
11.799
15.050
1.000
22.69

ATOM
2322
CB
ALA B
74
108.134
12.322
14.574
1.000
23.30

ATOM
2323
C
ALA B
74
110.074
12.723
16.102
1.000
26.52

ATOM
2324
O
ALA B
74
110.869
13.610
15.783
1.000
29.72

ATOM
2325
N
LEU B
75
109.701
12.558
17.374
1.000
25.95

ATOM
2326
CA
LEU B
75
110.234
13.504
18.364
1.000
25.51

ATOM
2327
CB
LEU B
75
109.399
13.416
19.648
1.000
26.48

ATOM
2328
CG
LEU B
75
107.994
14.018
19.562
1.000
24.78

ATOM
2329
CD1
LEU B
75
107.305
13.969
20.919
1.000
28.37

ATOM
2330
CD2
LEU B
75
108.043
15.449
19.050
1.000
24.31

ATOM
2331
C
LEU B
75
111.705
13.245
18.648
1.000
22.87

ATOM
2332
O
LEU B
75
112.509
14.147
18.887
1.000
22.28

ATOM
2333
N
ALA B
76
112.089
11.972
18.627
1.000
27.27

ATOM
2334
CA
ALA B
76
113.506
11.626
18.780
1.000
33.68

ATOM
2335
CB
ALA B
76
113.673
10.117
18.844
1.000
30.02

ATOM
2336
C
ALA B
76
114.318
12.238
17.643
1.000
34.38

ATOM
2337
O
ALA B
76
115.423
12.735
17.830
1.000
32.44

ATOM
2338
N
LEU B
77
113.746
12.211
16.439
1.000
35.72

ATOM
2339
CA
LEU B
77
114.406
12.813
15.279
1.000
29.98

ATOM
2340
CB
LEU B
77
113.597
12.512
14.022
1.000
32.18

ATOM
2341
CG
LEU B
77
114.232
12.800
12.666
1.000
35.08

ATOM
2342
CD1
LEU B
77
113.659
11.860
11.611
1.000
41.62

ATOM
2343
CD2
LEU B
77
114.033
14.245
12.241
1.000
32.26

ATOM
2344
C
LEU B
77
114.574
14.310
15.481
1.000
31.25

ATOM
2345
O
LEU B
77
115.606
14.894
15.149
1.000
31.59

ATOM
2346
N
ALA B
78
113.541
14.968
16.013
1.000
29.31

ATOM
2347
CA
ALA B
78
113.645
16.414
16.212
1.000
29.75

ATOM
2348
CB
ALA B
78
112.313
17.019
16.619
1.000
30.45

ATOM
2349
C
ALA B
78
114.710
16.745
17.249
1.000
28.71

ATOM
2350
O
ALA B
78
115.502
17.670
17.063
1.000
27.61

ATOM
2351
N
LYS B
79
114.745
16.003
18.357
1.000
33.16

ATOM
2352
CA
LYS B
79
115.778
16.335
19.354
1.000
38.43

ATOM
2353
CB
LYS B
79
115.625
15.513
20.619
1.000
31.00

ATOM
2354
C
LYS B
79
117.164
16.157
18.731
1.000
38.50

ATOM
2355
O
LYS B
79
118.019
17.042
18.730
1.000
37.36

ATOM
2356
N
GLY B
80
117.376
14.975
18.163
1.000
38.28

ATOM
2357
CA
GLY B
80
118.617
14.652
17.482
1.000
40.37

ATOM
2358
C
GLY B
80
118.986
15.682
16.440
1.000
41.82

ATOM
2359
O
GLY B
80
120.160
15.985
16.233
1.000
43.44

ATOM
2360
N
LYS B
81
117.993
16.265
15.757
1.000
38.61

ATOM
2361
CA
LYS B
81
118.386
17.243
14.741
1.000
34.19

ATOM
2362
CB
LYS B
81
117.372
17.249
13.592
1.000
39.19

ATOM
2363
CG
LYS B
81
117.538
18.427
12.637
1.000
47.35

ATOM
2364
CD
LYS B
81
118.642
18.163
11.626
1.000
53.28

ATOM
2365
CE
LYS B
81
119.342
19.448
11.209
1.000
57.14

ATOM
2366
NZ
LYS B
81
120.217
19.236
10.022
1.000
61.45

ATOM
2367
C
LYS B
81
118.543
18.637
15.322
1.000
35.44

ATOM
2368
O
LYS B
81
119.491
19.336
14.958
1.000
32.57

ATOM
2369
N
PHE B
82
117.643
19.075
16.201
1.000
33.67

ATOM
2370
CA
PHE B
82
117.687
20.471
16.628
1.000
30.79

ATOM
2371
CB
PHE B
82
116.404
21.198
16.219
1.000
33.81

ATOM
2372
CG
PHE B
82
116.254
21.364
14.714
1.000
34.04

ATOM
2373
CD1
PHE B
82
117.213
22.049
13.985
1.000
32.49

ATOM
2374
CD2
PHE B
82
115.157
20.833
14.049
1.000
31.02

ATOM
2375
CE1
PHE B
82
117.09
322.203
12.616
1.000
33.17

ATOM
2376
CE2
PHE B
82
115.030
20.985
12.682
1.000
29.68

ATOM
2377
CZ
PHE B
82
115.996
21.669
11.963
1.000
33.22

ATOM
2378
C
PHE B
82
117.902
20.639
18.128
1.000
34.16

ATOM
2379
O
PHE B
82
117.977
21.775
18.604
1.000
34.38

ATOM
2380
N
GLY B
83
118.015
19.535
18.859
1.000
36.21

ATOM
2381
CA
GLY B
83
118.420
19.550
20.240
1.000
37.95

ATOM
2382
C
GLY B
83
117.354
19.747
21.287
1.000
40.28

ATOM
2383
O
GLY B
83
117.569
19.334
22.435
1.000
38.88

ATOM
2384
N
ARG B
84
116.230
20.361
20.947
1.000
37.13

ATOM
2385
CA
ARG B
84
115.132
20.596
21.879
1.000
33.93

ATOM
2386
CB
ARG B
84
115.438
21.715
22.874
1.000
26.55

ATOM
2387
CG
ARG B
84
115.871
23.032
22.277
1.000
34.91

ATOM
2388
CD
ARG B
84
115.369
24.232
23.062
1.000
45.07

ATOM
2389
NE
ARG B
84
115.930
24.340
24.401
1.000
52.33

ATOM
2390
CZ
ARG B
84
115.403
24.960
25.444
1.000
56.40

ATOM
2391
NH1
ARG B
84
116.049
24.962
26.607
1.000
64.88

ATOM
2392
NH2
ARG B
84
114.238
25.591
25.372
1.000
32.24

ATOM
2393
C
ARG B
84
113.863
20.943
21.102
1.000
35.43

ATOM
2394
O
ARG B
84
113.976
21.169
19.893
1.000
38.55

ATOM
2395
N
VAL B
85
112.727
20.977
21.792
1.000
25.77

ATOM
2396
CA
VAL B
85
111.474
21.435
21.208
1.000
23.25

ATOM
2397
CB
VAL B
85
110.453
20.303
21.008
1.000
28.26

ATOM
2398
CG1
VAL B
85
109.205
20.870
20.335
1.000
27.90

ATOM
2399
CG2
VAL B
85
111.018
19.159
20.183
1.000
25.21

ATOM
2400
C
VAL B
85
110.836
22.521
22.072
1.000
25.60

ATOM
2401
O
VAL B
85
110.606
22.326
23.263
1.000
29.58

ATOM
2402
N
ASP B
86
110.541
23.669
21.481
1.000
25.06

ATOM
2403
CA
ASP B
86
109.985
24.804
22.195
1.000
24.15

ATOM
2404
CB
ASP B
86
110.675
26.098
21.753
1.000
27.61

ATOM
2405
CG
ASP B
86
112.183
25.984
21.887
1.000
32.39

ATOM
2406
OD1
ASP B
86
112.882
25.895
20.862
1.000
33.23

ATOM
2407
OD2
ASP B
86
112.610
25.970
23.055
1.000
34.44

ATOM
2408
C
ASP B
86
108.490
24.977
21.949
1.000
30.30

ATOM
2409
O
ASP B
86
107.788
25.521
22.798
1.000
21.74

ATOM
2410
N
VAL B
87
108.059
24.524
20.778
1.000
23.56

ATOM
2411
CA
VAL B
87
106.718
24.750
20.265
1.000
19.89

ATOM
2412
CB
VAL B
87
106.701
25.920
19.260
1.000
25.46

ATOM
2413
CG1
VAL B
87
105.346
26.049
18.580
1.000
23.92

ATOM
2414
CG2
VAL B
87
107.072
27.232
19.942
1.000
23.79

ATOM
2415
C
VAL B
87
106.197
23.506
19.563
1.000
24.56

ATOM
2416
O
VAL B
87
106.923
22.816
18.841
1.000
26.61

ATOM
2417
N
ALA B
88
104.922
23.211
19.784
1.000
22.40

ATOM
2418
CA
ALA B
88
104.242
22.158
19.039
1.000
20.37

ATOM
2419
CB
ALA B
88
103.979
20.911
19.848
1.000
19.16

ATOM
2420
C
ALA B
88
102.940
22.763
18.508
1.000
25.15

ATOM
2421
O
ALA B
88
102.254
23.506
19.204
1.000
23.17

ATOM
2422
N
VAL B
89
102.641
22.455
17.254
1.000
23.24

ATOM
2423
CA
VAL B
89
101.405
22.908
16.621
1.000
20.62

ATOM
2424
CB
VAL B
89
101.617
24.043
15.611
1.000
26.07

ATOM
2425
CG1
VAL B
89
100.278
24.578
15.114
1.000
24.86

ATOM
2426
CG2
VAL B
89
102.426
25.180
16.224
1.000
20.28

ATOM
2427
C
VAL B
89
100.760
21.700
15.948
1.000
20.49

ATOM
2428
O
VAL B
89
101.390
21.106
15.061
1.000
22.27

ATOM
2429
N
ASN B
90
99.564
21.369
16.399
1.000
17.06

ATOM
2430
CA
ASN B
90
98.767
20.263
15.895
1.000
21.63

ATOM
2431
CB
ASN B
90
97.912
19.676
17.029
1.000
21.17

ATOM
2432
CG
ASN B
90
98.770
18.964
18.062
1.000
25.12

ATOM
2433
OD1
ASN B
90
99.010
19.453
19.168
1.000
26.62

ATOM
2434
ND2
ASN B
90
99.248
17.781
17.700
1.000
19.87

ATOM
2435
C
ASN B
90
97.873
20.706
14.739
1.000
27.25

ATOM
2436
O
ASN B
90
96.831
21.346
14.926
1.000
24.49

ATOM
2437
N
CYS B
91
98.272
20.379
13.508
1.000
22.65

ATOM
2438
CA
CYS B
91
97.454
20.744
12.352
1.000
22.91

ATOM
2439
CB
CYS B
91
98.256
21.622
11.393
1.000
21.50

ATOM
2440
SG
CYS B
91
98.481
23.331
11.928
1.000
24.36

ATOM
2441
C
CYS B
91
96.938
19.496
11.645
1.000
27.06

ATOM
2442
O
CYS B
91
95.978
19.559
10.883
1.000
25.06

ATOM
2443
N
ALA B
92
97.568
18.349
11.892
1.000
24.70

ATOM
2444
CA
ALA B
92
97.110
17.080
11.342
1.000
26.12

ATOM
2445
CB
ALA B
92
97.914
15.933
11.959
1.000
19.70

ATOM
2446
C
ALA B
92
95.621
16.872
11.572
1.000
29.63

ATOM
2447
O
ALA B
92
95.119
16.947
12.698
1.000
21.23

ATOM
2448
N
GLY B
93
94.889
16.609
10.487
1.000
27.75

ATOM
2449
CA
GLY B
93
93.457
16.386
10.607
1.000
22.27

ATOM
2450
C
GLY B
93
92.818
15.838
9.346
1.000
25.37

ATOM
2451
O
GLY B
93
93.385
15.929
8.258
1.000
21.56

ATOM
2452
N
ILE B
94
91.632
15.264
9.485
1.000
22.61

ATOM
2453
CA
ILE B
94
90.850
14.804
8.346
1.000
24.90

ATOM
2454
CB
ILE B
94
90.800
13.273
8.204
1.000
25.11

ATOM
2455
CG2
ILE B
94
92.115
12.706
7.714
1.000
22.97

ATOM
2456
CG1
ILE B
94
90.338
12.560
9.483
1.000
27.64

ATOM
2457
CD1
ILE B
94
89.890
11.131
9.224
1.000
26.94

ATOM
2458
C
ILE B
94
89.407
15.295
8.479
1.000
25.32

ATOM
2459
O
ILE B
94
88.996
15.736
9.550
1.000
24.04

ATOM
2460
N
ALA B
95
88.659
15.202
7.393
1.000
31.39

ATOM
2461
CA
ALA B
95
87.265
15.611
7.343
1.000
32.56

ATOM
2462
CB
ALA B
95
87.069
16.880
6.525
1.000
25.46

ATOM
2463
C
ALA B
95
86.409
14.505
6.746
1.000
32.05

ATOM
2464
O
ALA B
95
86.857
13.724
5.912
1.000
26.39

ATOM
2465
N
VAL B
96
85.160
14.442
7.191
1.000
27.70

ATOM
2466
CA
VAL B
96
84.185
13.607
6.506
1.000
27.20

ATOM
2467
CB
VAL B
96
83.957
12.218
7.104
1.000
32.47

ATOM
2468
CG1
VAL B
96
85.263
11.457
7.265
1.000
52.62

ATOM
2469
CG2
VAL B
96
83.244
12.333
8.443
1.000
43.39

ATOM
2470
C
VAL B
96
82.857
14.374
6.512
1.000
26.65

ATOM
2471
O
VAL B
96
82.617
15.204
7.398
1.000
25.44

ATOM
2472
N
ALA B
97
82.047
14.075
5.506
1.000
26.05

ATOM
2473
CA
ALA B
97
80.690
14.629
5.475
1.000
22.29

ATOM
2474
CB
ALA B
97
80.509
15.590
4.323
1.000
29.01

ATOM
2475
C
ALA B
97
79.737
13.442
5.426
1.000
25.57

ATOM
2476
O
ALA B
97
79.745
12.662
4.479
1.000
29.16

ATOM
2477
N
SER B
98
78.940
13.271
6.469
1.000
21.75

ATOM
2478
CA
SER B
98
78.024
12.132
6.535
1.000
25.42

ATOM
2479
CB
SER B
98
78.792
10.846
6.799
1.000
26.09

ATOM
2480
OG
SER B
98
77.975
9.704
6.960
1.000
23.21

ATOM
2481
CB
SER B
98
76.998
12.432
7.626
1.000
28.54

ATOM
2482
O
SER B
98
77.383
12.679
8.775
1.000
22.53

ATOM
2483
N
LYS B
99
75.731
12.420
7.235
1.000
22.98

ATOM
2484
CA
LYS B
99
74.636
12.671
8.162
1.000
26.62

ATOM
2485
CB
LYS B
99
73.326
12.836
7.385
1.000
26.24

ATOM
2486
CG
LYS B
99
73.276
14.063
6.492
1.000
25.94

ATOM
2487
CD
LYS B
99
72.099
13.945
5.534
1.000
32.26

ATOM
2488
CE
LYS B
99
71.982
15.187
4.659
1.000
37.24

ATOM
2489
NZ
LYS B
99
70.599
15.299
4.106
1.000
50.59

ATOM
2490
C
LYS B
99
74.461
11.545
9.181
1.000
27.88

ATOM
2491
O
LYS B
99
74.711
10.370
8.884
1.000
21.35

ATOM
2492
N
THR B
100
74.007
11.918
10.382
1.000
21.91

ATOM
2493
CA
THR B
100
73.801
10.934
11.444
1.000
18.81

ATOM
2494
CB
THR B
100
73.223
11.601
12.709
1.000
21.49

ATOM
2495
OG1
THR B
100
74.235
12.450
13.267
1.000
21.98

ATOM
2496
CG2
THR B
100
72.862
10.565
13.755
1.000
18.29

ATOM
2497
C
THR B
100
72.873
9.821
10.988
1.000
23.10

ATOM
2498
O
THR B
100
73.143
8.635
11.153
1.000
23.86

ATOM
2499
N
TYR B
101
71.758
10.242
10.399
1.000
25.05

ATOM
2500
CA
TYR B
101
70.827
9.312
9.782
1.000
25.55

ATOM
2501
CB
TYR B
101
69.788
8.824
10.801
1.000
24.38

ATOM
2502
CG
TYR B
101
68.798
7.861
10.170
1.000
27.81

ATOM
2503
CD1
TYR B
101
67.465
8.207
10.024
1.000
27.63

ATOM
2504
CE1
TYR B
101
66.570
7.330
9.448
1.000
29.00

ATOM
2505
CD2
TYR B
101
69.211
6.614
9.719
1.000
28.85

ATOM
2506
CE2
TYR B
101
68.323
5.730
9.141
1.000
29.92

ATOM
2507
CZ
TYR B
101
67.002
6.099
9.010
1.000
32.68

ATOM
2508
OH
TYR B
101
66.106
5.224
8.434
1.000
33.84

ATOM
2509
C
TYR B
101
70.138
9.977
8.592
1.000
30.29

ATOM
2510
O
TYR B
101
69.842
11.171
8.653
1.000
27.66

ATOM
2511
N
ASN B
102
69.890
9.219
7.533
1.000
32.30

ATOM
2512
CA
ASN B
102
69.095
9.704
6.406
1.000
27.57

ATOM
2513
CB
ASN B
102
69.937
9.723
5.130
1.000
33.98

ATOM
2514
CG
ASN B
102
69.240
10.469
4.002
1.000
36.11

ATOM
2515
OD1
ASN B
102
68.038
10.287
3.797
1.000
36.21

ATOM
2516
ND2
ASN B
102
69.974
11.311
3.283
1.000
25.79

ATOM
2517
C
ASN B
102
67.861
8.827
6.227
1.000
24.40

ATOM
2518
O
ASN B
102
67.974
7.665
5.835
1.000
29.49

ATOM
2519
N
LEU B
103
66.686
9.356
6.540
1.000
26.99

ATOM
2520
CA
LEU B
103
65.448
8.591
6.417
1.000
29.76

ATOM
2521
CB
LEU B
103
64.314
9.311
7.147
1.000
29.43

ATOM
2522
CG
LEU B
103
62.934
8.653
7.112
1.000
31.78

ATOM
2523
CD1
LEU B
103
62.971
7.289
7.788
1.000
34.16

ATOM
2524
CD2
LEU B
B103
61.896
9.556
7.758
1.000
27.01

ATOM
2525
C
LEU B
103
65.085
8.367
4.954
1.000
35.54

ATOM
2526
O
LEU B
103
64.742
7.255
4.545
1.000
40.20

ATOM
2527
N
LYS B
104
65.145
9.416
4.148
1.000
39.57

ATOM
2528
CA
LYS B
104
64.863
9.329
2.721
1.000
42.48

ATOM
2529
CB
LYS B
104
65.030
10.699
2.075
1.000
51.56

ATOM
2530
C
LYS B
104
65.754
8.307
2.024
1.000
39.81

ATOM
2531
O
LYS B
104
65.311
7.619
1.101
1.000
43.72

ATOM
2532
N
LYS B
105
67.005
8.200
2.467
1.000
35.79

ATOM
2533
CA
LYS B
105
67.924
7.211
1.915
1.000
35.08

ATOM
2534
CB
LYS B
105
69.362
7.723
1.913
1.000
42.55

ATOM
2535
CG
LYS B
105
69.810
8.431
0.648
1.000
52.17

ATOM
2536
CD
LYS B
105
71.334
8.483
0.589
1.000
61.85

ATOM
2537
CE
LYS B
105
71.944
7.291
1.310
1.000
67.77

ATOM
2538
NZ
LYS B
105
73.111
7.657
2.157
1.000
69.80

ATOM
2539
C
LYS B
105
67.886
5.909
2.705
1.000
32.76

ATOM
2540
O
LYS B
105
68.341
4.878
2.205
1.000
33.06

ATOM
2541
N
GLY B
106
67.367
5.936
3.932
1.000
26.52

ATOM
2542
CA
GLY B
106
67.455
4.735
4.761
1.000
22.95

ATOM
2543
C
GLY B
106
68.881
4.466
5.188
1.000
27.67

ATOM
2544
O
GLY B
106
69.268
3.325
5.436
1.000
33.60

ATOM
2545
N
GLN B
107
69.706
5.505
5.286
1.000
33.76

ATOM
2546
CA
GLN B
107
71.137
5.336
5.486
1.000
30.81

ATOM
2547
CB
GLN B
107
71.888
6.022
4.355
1.000
28.84

ATOM
2548
C
GLN B
107
71.605
5.873
6.836
1.000
28.73

ATOM
2549
O
GLN B
107
71.132
6.916
7.283
1.000
26.22

ATOM
2550
N
THR B
108
72.524
5.136
7.439
1.000
28.78

ATOM
2551
CA
THR B
108
73.069
5.396
8.764
1.000
30.06

ATOM
2552
CB
THR B
108
72.901
4.154
9.665
1.000
27.78

ATOM
2553
OG1
THR B
108
71.501
3.870
9.817
1.000
28.16

ATOM
2554
CG2
THR B
108
73.471
4.405
11.051
1.000
26.31

ATOM
2555
C
THR B
108
74.549
5.744
8.708
1.000
27.68

ATOM
2556
O
THR B
108
75.304
5.055
8.017
1.000
28.23

ATOM
2557
N
HIS B
109
74.971
6.780
9.423
1.000
26.32

ATOM
2558
CA
HIS B
109
76.405
7.080
9.530
1.000
24.60

ATOM
2559
CB
HIS B
109
76.595
8.232
10.498
1.000
25.11

ATOM
2560
CG
HIS B
109
77.918
8.912
10.561
1.000
23.44

ATOM
2561
CD2
HIS B
109
78.226
10.231
10.518
1.000
24.11

ATOM
2562
ND1
HIS B
109
79.116
8.252
10.721
1.000
22.09

ATOM
2563
CE1
HIS B
109
80.103
9.132
10.759
1.000
20.27

ATOM
2564
NE2
HIS B
109
79.593
10.343
10.640
1.000
21.90

ATOM
2565
C
HIS B
109
77.151
5.845
9.997
1.000
22.44

ATOM
2566
O
HIS B
109
76.727
5.200
10.961
1.000
26.30

ATOM
2567
N
THR B
110
78.256
5.471
9.354
1.000
23.04

ATOM
2568
CA
THR B
110
78.923
4.256
9.823
1.000
21.12

ATOM
2569
CB
THR B
110
79.894
3.654
8.791
1.000
22.73

ATOM
2570
OG1
THR B
110
81.045
4.516
8.728
1.000
25.04

ATOM
2571
CG2
THR B
110
79.256
3.561
7.413
1.000
19.23

ATOM
2572
C
THR B
110
79.741
4.515
11.081
1.000
24.40

ATOM
2573
O
THR B
110
80.307
5.592
11.265
1.000
31.84

ATOM
2574
N
LEU B
111
79.821
3.500
11.937
1.000
27.00

ATOM
2575
CA
LEU B
111
80.605
3.657
13.160
1.000
24.91

ATOM
2576
CB
LEU B
111
80.522
2.369
13.980
1.000
26.44

ATOM
2577
CG
LEU B
111
81.139
2.383
15.380
1.000
28.05

ATOM
2578
CD1
LEU B
111
80.668
3.604
16.161
1.000
25.21

ATOM
2579
CD2
LEU B
111
80.814
1.095
16.125
1.000
26.81

ATOM
2580
C
LEU B
111
82.042
4.029
12.833
1.000
27.53

ATOM
2581
O
LEU B
111
82.637
4.954
13.393
1.000
29.42

ATOM
2582
N
GLU B
112
82.657
3.312
11.891
1.000
28.47

ATOM
2583
CA
GLU B
112
84.097
3.523
11.692
1.000
32.01

ATOM
2584
CB
GLU B
112
84.712
2.374
10.892
1.000
43.42

ATOM
2585
CG
GLU B
112
85.202
1.218
11.745
1.000
58.71

ATOM
2586
CD
GLU B
112
85.624
1.561
13.157
1.000
63.11

ATOM
2587
OE1
GLU B
112
86.853
1.662
13.402
1.000
56.52

ATOM
2588
OE2
GLU B
112
84.754
1.705
14.048
1.000
38.29

ATOM
2589
C
GLU B
112
84.390
4.852
11.019
1.000
29.92

ATOM
2590
O
GLU B
112
85.499
5.371
11.177
1.000
27.14

ATOM
2591
N
ASP B
113
83.435
5.432
10.287
1.000
26.76

ATOM
2592
CA
ASP B
113
83.634
6.806
9.832
1.000
23.28

ATOM
2593
CB
ASP B
113
82.472
7.267
8.962
1.000
28.04

ATOM
2594
CG
ASP B
113
82.718
7.128
7.474
1.000
31.68

ATOM
2595
OD1
ASP B
113
83.873
6.857
7.094
1.000
28.93

ATOM
2596
OD2
ASP B
113
81.748
7.292
6.704
1.000
29.11

ATOM
2597
C
ASP B
113
83.774
7.745
11.033
1.000
23.71

ATOM
2598
O
ASP B
113
84.565
8.688
11.039
1.000
25.19

ATOM
2599
N
PHE B
114
82.981
7.481
12.078
1.000
23.64

ATOM
2600
CA
PHE B
114
83.043
8.327
13.273
1.000
21.55

ATOM
2601
CB
PHE B
114
81.856
8.044
14.192
1.000
21.55

ATOM
2602
CG
PHE B
114
81.712
9.022
15.346
1.000
22.74

ATOM
2603
CD1
PHE B
114
82.303
8.752
16.571
1.000
24.12

ATOM
2604
CD2
PHE B
114
81.001
10.198
15.187
1.000
21.84

ATOM
2605
CE1
PHE B
114
82.174
9.637
17.625
1.000
23.11

ATOM
2606
CE2
PHE B
114
80.850
11.083
16.242
1.000
23.72

ATOM
2607
CZ
PHE B
114
81.447
10.803
17.458
1.000
21.35

ATOM
2608
C
PHE B
114
84.352
8.104
14.023
1.000
21.77

ATOM
2609
O
PHE B
114
85.004
9.058
14.449
1.000
24.80

ATOM
2610
N
GLN B
115
84.716
6.839
14.183
1.000
23.92

ATOM
2611
CA
GLN B
115
85.919
6.434
14.898
1.000
26.72

ATOM
2612
CB
GLN B
115
86.002
4.908
14.970
1.000
28.07

ATOM
2613
CG
GLN B
115
87.126
4.379
15.851
1.000
29.18

ATOM
2614
CD
GLN B
115
86.740
4.463
17.320
1.000
33.93

ATOM
2615
OE1
GLN B
115
8S.710
3.920
17.730
1.000
36.31

ATOM
2616
NE2
GLN B
115
87.560
5.151
18.103
1.000
31.38

ATOM
2617
C
GLN B
115
87.182
6.977
14.242
1.000
25.49

ATOM
2618
O
GLN B
115
88.089
7.449
14.921
1.000
26.49

ATOM
2619
N
ARG B
116
87.244
6.906
12.918
1.000
22.33

ATOM
2620
CA
ARG B
116
88.433
7.339
12.188
1.000
24.36

ATOM
2621
CB
ARG B
116
88.272
7.028
10.700
1.000
22.95

ATOM
2622
C
ARG B
116
88.723
8.818
12.389
1.000
21.93

ATOM
2623
O
ARG B
116
89.868
9.240
12.574
1.000
22.76

ATOM
2624
N
VAL B
117
87.675
9.638
12.347
1.000
22.20

ATOM
2625
CA
VAL B
117
87.852
11.084
12.441
1.000
20.72

ATOM
2626
CB
VAL B
117
86.580
11.816
11.993
1.000
20.31

ATOM
2627
CG1
VAL B
117
86.640
13.287
12.349
1.000
20.26

ATOM
2628
CG2
VAL B
117
86.392
11.669
10.484
1.000
27.13

ATOM
2629
C
VAL B
117
88.249
11.483
13.857
1.000
23.41

ATOM
2630
O
VAL B
117
89.115
12.336
14.039
1.000
26.63

ATOM
2631
N
LEU B
118
87.637
10.854
14.853
1.000
19.32

ATOM
2632
CA
LEU B
118
88.020
10.966
16.248
1.000
23.34

ATOM
2633
CB
LEU B
118
87.227
10.034
17.158
1.000
24.15

ATOM
2634
CG
LEU B
118
85.754
10.307
17.433
1.000
36.11

ATOM
2635
CD1
LEU B
118
85.303
9.517
18.654
1.000
34.48

ATOM
2636
CD2
LEU B
118
85.495
11.793
17.617
1.000
37.25

ATOM
2637
C
LEU B
118
89.497
10.591
16.424
1.000
21.18

ATOM
2638
O
LEU B
118
90.305
11.315
16.996
1.000
24.74

ATOM
2639
N
ASP B
119
89.826
9.409
15.907
1.000
19.51

ATOM
2640
CA
ASP B
119
91.175
8.870
16.015
1.000
23.80

ATOM
2641
CB
ASP B
119
91.255
7.538
15.259
1.000
22.73

ATOM
2642
CG
ASP B
119
90.734
6.387
16.102
1.000
27.64

ATOM
2643
OD1
ASP B
119
90.874
5.229
15.655
1.000
38.04

ATOM
2644
OD2
ASP B
119
90.193
6.626
17.203
1.000
27.24

ATOM
2645
C
ASP B
119
92.228
9.840
15.501
1.000
27.92

ATOM
2646
O
ASP B
119
93.197
10.162
16.197
1.000
24.30

ATOM
2647
N
VAL B
120
92.072
10.333
14.271
1.000
24.11

ATOM
2648
CA
VAL B
120
93.094
11.250
13.774
1.000
21.70

ATOM
2649
CB
VAL B
120
92.997
11.468
12.247
1.000
21.17

ATOM
2650
CG1
VAL B
120
94.025
12.498
11.801
1.000
19.78

ATOM
2651
CG2
VAL B
120
93.201
10.156
11.502
1.000
25.36

ATOM
2652
C
VAL B
120
93.021
12.609
14.455
1.000
18.60

ATOM
2653
O
VAL B
120
94.034
13.143
14.901
1.000
18.90

ATOM
2654
N
ASN B
121
91.827
13.197
14.510
1.000
16.99

ATOM
2655
CA
ASN B
121
91.699
14.592
14.914
1.000
19.35

ATOM
2656
CB
ASN B
121
90.306
15.127
14.534
1.000
23.26

ATOM
2657
CG
ASN B
121
90.183
15.419
13.051
1.000
26.22

ATOM
2658
OD1
ASN B
121
91.063
15.040
12.278
1.000
26.76

ATOM
2659
ND2
ASN B
121
89.110
16.088
12.650
1.000
19.20

ATOM
2660
C
ASN B
121
91.894
14.825
16.409
1.000
19.21

ATOM
2661
O
ASN B
121
92.515
15.818
16.774
1.000
21.98

ATOM
2662
N
LEU B
122
91.341
13.944
17.232
1.000
20.95

ATOM
2663
CA
LEU B
122
91.306
14.176
18.679
1.000
19.05

ATOM
2664
CB
LEU B
122
89.905
13.857
19.189
1.000
18.59

ATOM
2665
CG
LEU B
122
89.615
14.033
20.679
1.000
20.96

ATOM
2666
CD1
LEU B
122
90.069
15.391
21.190
1.000
16.90

ATOM
2667
CD2
LEU B
122
88.126
13.860
20.945
1.000
18.18

ATOM
2668
C
LEU B
122
92.376
13.350
19.377
1.000
20.58

ATOM
2669
O
LEU B
122
93.297
13.880
19.999
1.000
24.53

ATOM
2670
N
MET B
123
92.291
12.025
19.278
1.000
19.48

ATOM
2671
CA
MET B
123
93.308
11.158
19.874
1.000
22.29

ATOM
2672
CB
MET B
123
92.982
9.693
19.590
1.000
22.09

ATOM
2673
CG
MET B
123
93.957
8.703
20.207
1.000
23.89

ATOM
2674
SD
MET B
123
95.361
8.365
19.122
1.000
29.30

ATOM
2675
CE
MET B
123
94.591
7.184
18.008
1.000
26.18

ATOM
2676
C
MET B
123
94.699
11.513
19.363
1.000
26.09

ATOM
2677
O
MET B
123
95.641
11.661
20.142
1.000
23.77

ATOM
2678
N
GLY B
124
94.829
11.663
18.043
1.000
22.76

ATOM
2679
CA
GLY B
124
96.103
11.989
17.421
1.000
23.30

ATOM
2680
C
GLY B
124
96.716
13.248
17.998
1.000
26.58

ATOM
2681
O
GLY B
124
97.890
13.317
18.355
1.000
22.97

ATOM
2682
N
THR B
125
95.907
14.299
18.113
1.000
20.71

ATOM
2683
CA
THR B
125
96.370
15.521
18.762
1.000
18.75

ATOM
2684
CB
THR B
125
95.285
16.611
18.685
1.000
22.80

ATOM
2685
OG1
THR B
125
95.241
17.153
17.356
1.000
23.16

ATOM
2686
CG2
THR B
125
95.604
17.748
19.648
1.000
15.94

ATOM
2687
C
THR B
125
96.743
15.265
20.215
1.000
20.63

ATOM
2688
O
THR B
125
97.778
15.746
20.683
1.000
23.52

ATOM
2689
N
PHE B
126
95.948
14.514
20.983
1.000
20.41

ATOM
2690
CA
PHE B
126
96.358
14.272
22.375
1.000
23.20

ATOM
2691
CB
PHE B
126
95.263
13.545
23.158
1.000
19.10

ATOM
2692
CG
PHE B
126
95.639
13.311
24.616
1.000
25.87

ATOM
2693
CD1
PHE B
126
95.581
14.353
25.523
1.000
22.37

ATOM
2694
CD2
PHE B
126
96.050
12.061
25.050
1.000
26.96

ATOM
2695
CE1
PHE B
126
95.935
14.154
26.850
1.000
22.65

ATOM
2696
CE2
PHE B
126
96.399
11.852
26.375
1.000
23.20

ATOM
2697
CZ
PHE B
126
96.343
12.899
27.274
1.000
20.92

ATOM
2698
C
PHE B
126
97.661
13.478
22.450
1.000
21.16

ATOM
2699
O
PHE B
126
98.532
13.733
23.282
1.000
22.13

ATOM
2700
N
ASN B
127
97.825
12.497
21.575
1.000
20.29

ATOM
2701
CA
ASN B
127
99.040
11.690
21.502
1.000
22.57

ATOM
2702
CE
ASN B
127
98.922
10.706
20.339
1.000
22.19

ATOM
2703
CG
ASN B
127
99.979
9.621
20.359
1.000
28.15

ATOM
2704
OD1
ASN B
127
100.400
9.142
21.411
1.000
27.23

ATOM
2705
ND2
ASN B
127
100.399
9.231
19.159
1.000
23.88

ATOM
2706
C
ASN B
127
100.287
12.547
21.334
1.000
26.24

ATOM
2707
O
ASN B
127
101.293
12.353
22.021
1.000
27.74

ATOM
2708
N
VAL B
128
100.239
13.509
20.412
1.000
21.97

ATOM
2709
CA
VAL B
128
101.374
14.412
20.233
1.000
21.97

ATOM
2710
CE
VAL B
128
101.182
15.276
18.969
1.000
25.49

ATOM
2711
CG1
VAL B
128
102.234
16.367
18.881
1.000
18.12

ATOM
2712
CG2
VAL B
128
101.212
14.383
17.730
1.000
21.07

ATOM
2713
C
VAL B
128
101.571
15.300
21.454
1.000
24.63

ATOM
2714
O
VAL B
128
102.697
15.551
21.878
1.000
24.16

ATOM
2715
N
ILE B
129
100.482
15.802
22.040
1.000
21.34

ATOM
2716
CA
ILE B
129
100.595
16.670
23.210
1.000
21.04

ATOM
2717
CE
ILE B
129
99.207
17.164
23.671
1.000
21.80

ATOM
2718
CG2
ILE B
129
99.282
17.704
25.093
1.000
15.16

ATOM
2719
CG1
ILE B
129
98.559
18.184
22.731
1.000
19.30

ATOM
2720
CD1
ILE B
129
97.089
18.395
23.009
1.000
20.24

ATOM
2721
C
ILE B
129
101.259
15.977
24.395
1.000
21.07

ATOM
2722
O
ILE B
129
102.160
16.538
25.019
1.000
24.73

ATOM
2723
N
ARG B
130
100.821
14.766
24.722
1.000
22.23

ATOM
2724
CA
ARG B
130
101.320
14.074
25.907
1.000
23.38

ATOM
2725
CE
ARG B
130
100.465
12.830
26.183
1.000
21.66

ATOM
2726
CG
ARG B
130
100.867
11.603
25.400
1.000
20.29

ATOM
2727
CD
ARG B
130
99.789
10.542
25.265
1.000
18.80

ATOM
2728
NE
ARG B
130
100.255
9.485
24.364
1.000
22.82

ATOM
2729
CZ
ARG B
130
101.032
8.465
24.704
1.000
28.05

ATOM
2730
NE1
ARG B
130
101.403
7.563
23.800
1.000
23.90

ATOM
2731
NE2
ARG B
130
101.461
8.305
25.951
1.000
20.66

ATOM
2732
C
ARG B
130
102.791
13.701
25.769
1.000
29.73

ATOM
2733
O
ARG B
130
103.571
13.761
26.724
1.000
23.87

ATOM
2734
N
LEU B
131
103.193
13.303
24.568
1.000
27.25

ATOM
2735
CA
LEU B
131
104.565
12.913
24.278
1.000
25.57

ATOM
2736
CB
LEU B
131
104.620
12.045
23.019
1.000
26.19

ATOM
2737
CG
LEU B
131
103.911
10.689
23.075
1.000
28.61

ATOM
2738
CD1
LEU B
131
103.958
9.978
21.721
1.000
23.83

ATOM
2739
CD2
LEU B
131
104.513
9.786
24.142
1.000
31.07

ATOM
2740
C
LEU B
131
105.445
14.145
24.144
1.000
26.19

ATOM
2741
O
LEU B
131
106.565
14.195
24.663
1.000
25.39

ATOM
2742
N
VAL B
132
104.963
15.186
23.466
1.000
21.11

ATOM
2743
CA
VAL B
132
105.780
16.391
23.341
1.000
17.60

ATOM
2744
CB
VAL B
132
105.279
17.364
22.261
1.000
22.25

ATOM
2745
CG1
VAL B
132
104.101
18.197
22.728
1.000
23.13

ATOM
2746
CG2
VAL B
132
106.413
18.301
21.850
1.000
24.17

ATOM
2747
C
VAL B
132
105.874
17.116
24.680
1.000
23.10

ATOM
2748
O
VAL B
132
106.892
17.766
24.950
1.000
25.24

ATOM
2749
N
ALA B
133
104.857
17.013
25.537
1.000
20.04

ATOM
2750
CA
ALA B
133
104.985
17.654
26.852
1.000
22.03

ATOM
2751
CB
ALA B
133
103.694
17.515
27.645
1.000
19.47

ATOM
2752
C
ALA B
133
106.160
17.075
27.631
1.000
21.84

ATOM
2753
O
ALA B
133
106.872
17.783
28.342
1.000
23.39

ATOM
2754
N
GLY B
134
106.368
15.771
27.498
1.000
24.23

ATOM
2755
CA
GLY B
134
107.452
15.085
28.179
1.000
31.61

ATOM
2756
C
GLY B
134
108.812
15.508
27.658
1.000
34.00

ATOM
2757
O
GLY B
134
109.784
15.551
28.414
1.000
29.77

ATOM
2758
N
GLU B
135
108.886
15.826
26.367
1.000
33.32

ATOM
2759
CA
GLU B
135
110.100
16.386
25.792
1.000
28.56

ATOM
2760
CB
GLU B 135
110.039
16.427
24.262
1.000
27.20

ATOM
2761
CG
GLU B
135
109.843
15.075
23.597
1.000
28.76

ATOM
2762
CD
GLU B 135
111.100
14.232
23.700
1.000
35.06

ATOM
2763
OE1
GLU B 135
110.992
13.012
23.929
1.000
47.85

ATOM
2764
OE2
GLU B135
112.204
14.795
23.561
1.000
44.39

ATOM
2765
C
GLU B
135
110.324
17.805
26.301
1.000
27.32

ATOM
2766
O
GLU B
135
111.437
18.185
26.662
1.000
26.88

ATOM
2767
N
MET B
136
109.245
18.602
26.317
1.000
22.38

ATOM
2768
CA
MET B
136
109.416
19.995
26.725
1.000
22.02

ATOM
2769
CB
MET B
136
108.151
20.800
26.448
1.000
23.97

ATOM
2770
CG
MET B
136
107.833
21.067
24.990
1.000
28.51

ATOM
2771
SD
MET B
136
106.121
21.622
24.802
1.000
26.00

ATOM
2772
CE
MET B
136
106.071
22.029
23.057
1.000
22.80

ATOM
2773
C
MET B
136
109.767
20.084
28.205
1.000
20.95

ATOM
2774
O
MET B
136
110.397
21.035
28.665
1.000
27.02

ATOM
2775
N
GLY B
137
109.343
19.092
28.983
1.000
23.73

ATOM
2776
CA
GLY B
137
109.638
19.135
30.413
1.000
30.04

ATOM
2777
C
GLY B
137
111.125
19.064
30.698
1.000
32.99

ATOM
2778
O
GLY B
137
111.555
19.376
31.812
1.000
33.93

ATOM
2779
N
GLN B
138
111.925
18.658
29.718
1.000
29.39

ATOM
2780
CA
GLN B
138
113.375
18.581
29.892
1.000
28.86

ATOM
2781
CB
GLN B
138
113.963
17.515
28.976
1.000
34.26

ATOM
2782
C
GLN B
138
114.033
19.924
29.635
1.000
31.61

ATOM
2783
O
GLN B
138
115.205
20.149
29.939
1.000
33.07

ATOM
2784
N
ASN B
139
113.297
20.877
29.059
1.000
30.51

ATOM
2785
CA
ASN B
139
113.904
22.175
28.786
1.000
29.96

ATOM
2786
CB
ASN B
139
113.033
22.995
27.840
1.000
31.82

ATOM
2787
CG
ASN B
139
112.839
22.378
26.470
1.000
37.24

ATOM
2788
OD1
ASN B
139
113.667
21.614
25.973
1.000
30.68

ATOM
2789
ND2
ASN B
139
111.710
22.731
25.850
1.000
28.36

ATOM
2790
C
ASN B
139
114.095
22.959
30.076
1.000
34.50

ATOM
2791
O
ASN B
139
113.248
22.886
30.972
1.000
32.01

ATOM
2792
N
GLU B
140
115.187
23.712
30.169
1.000
31.95

ATOM
2793
CA
GLU B
140
115.309
24.671
31.263
1.000
32.60

ATOM
2794
CB
GLU B
140
116.719
25.220
31.373
1.000
36.62

ATOM
2795
C
GLU B
140
114.304
25.799
31.033
1.000
31.18

ATOM
2796
O
GLU B
140
114.197
26.259
29.896
1.000
28.53

ATOM
2797
N
PRO B
141
113.584
26.229
32.058
1.000
31.88

ATOM
2798
CD
PRO B
141
113.641
25.759
33.456
1.000
30.29

ATOM
2799
CA
PRO B
141
112.590
27.290
31.875
1.000
31.37

ATOM
2800
CB
PRO B
141
112.002
27.495
33.271
1.000
32.31

ATOM
2801
CG
PRO B
141
112.345
26.259
34.028
1.000
30.62

ATOM
2802
C
PRO B
141
113.257
28.576
31.408
1.000
36.56

ATOM
2803
O
PRO B
141
114.386
28.849
31.811
1.000
38.29

ATOM
2804
N
ASP B
142
112.578
29.361
30.577
1.000
32.11

ATOM
2805
CA
ASP B
142
113.190
30.602
30.108
1.000
29.02

ATOM
2806
CB
ASP B
142
112.523
31.107
28.835
1.000
34.13

ATOM
2807
CG
ASP B
142
111.042
31.388
28.975
1.000
35.91

ATOM
2808
OD1
ASP B
142
110.540
31.478
30.114
1.000
27.63

ATOM
2809
OD2
ASP B
142
110.383
31.505
27.919
1.000
36.65

ATOM
2810
C
ASP B
142
113.113
31.659
31.199
1.000
35.02

ATOM
2811
O
ASP B
142
112.733
31.348
32.329
1.000
34.17

ATOM
2812
N
GLN B
143
113.459
32.893
30.853
1.000
35.14

ATOM
2813
CA
GLN B
143
113.391
34.002
31.801
1.000
37.94

ATOM
2814
CB
GLN B
143
113.878
35.288
31.147
1.000
37.47

ATOM
2815
C
GLN B
143
111.979
34.184
32.344
1.000
39.06

ATOM
2816
O
GLN B
143
111.781
34.729
33.431
1.000
37.62

ATOM
2817
N
GLY B
144
110.979
33.726
31.593
1.000
33.77

ATOM
2818
CA
GLY B
144
109.590
33.862
32.005
1.000
29.37

ATOM
2819
C
GLY B
144
109.113
32.632
32.746
1.000
29.22

ATOM
2820
O
GLY B
144
107.965
32.517
33.166
1.000
31.92

ATOM
2821
N
GLY B
145
110.023
31.673
32.916
1.000
28.73

ATOM
2822
CA
GLY B
145
109.679
30.408
33.540
1.000
27.23

ATOM
2823
C
GLY B
145
109.010
29.468
32.550
1.000
28.54

ATOM
2824
O
GLY B
145
108.404
28.469
32.947
1.000
26.30

ATOM
2825
N
GLN B
146
109.115
29.772
31.257
1.000
26.91

ATOM
2826
CA
GLN B
146
108.395
28.963
30.274
1.000
27.98

ATOM
2827
CB
GLN B
146
107.862
29.872
29.154
1.000
24.94

ATOM
2828
CG
GLN B
146
106.886
29.135
28.247
1.000
32.11

ATOM
2829
CD
GLN B
146
106.239
30.065
27.238
1.000
27.79

ATOM
2830
OE1
GLN B
146
105.335
30.822
27.576
1.000
24.50

ATOM
2831
NE2
GLN B
146
106.727
29.988
26.002
1.000
27.50

ATOM
2832
C
GLN B
146
109.243
27.863
29.657
1.000
26.64

ATOM
2833
O
GLN B
146
110.385
28.076
29.246
1.000
27.40

ATOM
2834
N
ARG B
147
108.680
26.659
29.551
1.000
20.15

ATOM
2835
CA
ARG B
147
109.392
25.561
28.913
1.000
21.33

ATOM
2836
CB
ARG B
147
109.340
24.300
29.782
1.000
22.83

ATOM
2837
CG
ARG B
147
110.180
24.362
31.062
1.000
22.46

ATOM
2838
CD
ARG B
147
110.143
22.991
31.707
1.000
25.58

ATOM
2839
NE
ARG B
147
111.072
22.800
32.805
1.000
26.67

ATOM
2840
CZ
ARG B
147
110.759
22.976
34.080
1.000
32.90

ATOM
2841
NH1
ARG B
147
111.670
22.773
35.023
1.000
35.72

ATOM
2842
NH2
ARG B
147
109.528
23.358
34.404
1.000
28.27

ATOM
2843
C
ARG B
147
108.820
25.211
27.544
1.000
29.41

ATOM
2844
O
ARG B
147
109.465
24.482
26.784
1.000
24.64

ATOM
2845
N
GLY B
148
107.613
25.681
27.214
1.000
26.59

ATOM
2846
CA
GLY B
148
107.026
25.263
25.945
1.000
23.20

ATOM
2847
C
GLY B
148
105.685
25.932
25.685
1.000
28.53

ATOM
2848
O
GLY B
148
105.068
26.467
26.610
1.000
20.78

ATOM
2849
N
VAL B
149
105.245
25.895
24.434
1.000
24.83

ATOM
2850
CA
VAL B
149
103.944
26.359
23.980
1.000
22.50

ATOM
2851
CB
VAL B
149
104.009
27.711
23.253
1.000
22.87

ATOM
2852
CG1
VAL B
149
102.597
28.262
23.025
1.000
25.59

ATOM
2853
CG2
VAL B
149
104.853
28.720
24.007
1.000
28.65

ATOM
2854
C
VAL B
149
103.335
25.328
23.027
1.000
24.60

ATOM
28S5
O
VAL B
149
103.985
24.928
22.062
1.000
21.79

ATOM
2856
N
ILE B
150
102.115
24.886
23.299
1.000
22.21

ATOM
2857
CA
ILE B
150
101.412
23.931
22.457
1.000
22.43

ATOM
2858
CB
ILE B
150
101.063
22.642
23.214
1.000
24.72

ATOM
2859
CG2
ILE B
150
100.208
21.687
22.386
1.000
19.63

ATOM
2860
CD1
ILE B
150
102.294
21.896
23.756
1.000
21.59

ATOM
2861
CD1
ILE B
150
101.918
20.680
24.581
1.000
23.41

ATOM
2862
C
ILE B
150
100.145
24.584
21.898
1.000
24.76

ATOM
2863
O
ILE B
150
99.353
25.137
22.662
1.000
21.45

ATOM
2864
N
ILE B
151
99.976
24.53
220.581
1.000
22.74

ATOM
2865
CA
ILE B
151
98.836
25.139
19.898
1.000
18.41

ATOM
2866
CB
ILE B
151
99.262
26.272
18.954
1.000
20.13

ATOM
2867
CG2
ILE B
151
98.063
27.005
18.358
1.000
13.13

ATOM
2868
CG1
ILE B
151
100.225
27.281
19.595
1.000
23.87

ATOM
2869
CD1
ILE B
151
100.757
28.306
18.615
1.000
27.17

ATOM
2870
C
ILE B
151
98.090
24.068
19.118
1.000
20.55

ATOM
2871
O
ILE B
151
98.702
23.387
18.295
1.000
22.75

ATOM
2872
N
ASN B
152
96.800
23.922
19.383
1.000
20.72

ATOM
2873
CA
ASN B
152
95.978
22.934
18.701
1.000
18.58

ATOM
2874
CB
ASN B
152
95.082
22.197
19.702
1.000
18.64

ATOM
2875
CG
ASN B
152
95.890
21.725
20.896
1.000
22.42

ATOM
2876
OD1
ASN B
152
95.586
22.026
22.051
1.000
31.28

ATOM
2877
ND2
ASN B
152
96.954
20.977
20.642
1.000
15.90

ATOM
2878
C
ASN B
152
95.116
23.588
17.627
1.000
21.08

ATOM
2879
O
ASN B
152
94.934
24.805
17.623
1.000
20.68

ATOM
2880
N
THR B
153
94.584
22.782
16.721
1.000
20.37

ATOM
2881
CA
THR B
153
93.670
23.303
15.706
1.000
21.06

ATOM
2882
CB
THR B
153
94.149
23.034
14.273
1.000
21.72

ATOM
2883
OG1
THR B
153
95.481
23.558
14.123
1.000
20.20

ATOM
2884
CG2
THR B
153
93.262
23.760
13.272
1.000
18.62

ATOM
2885
C
THR B
153
92.299
22.668
15.923
1.000
19.15

ATOM
2886
O
THR B
153
92.150
21.460
15.761
1.000
21.82

ATOM
2887
N
ALA B
154
91.337
23.499
16.317
1.000
17.65

ATOM
2888
CA
ALA B
154
89.967
23.002
16.451
1.000
22.08

ATOM
2889
CB
ALA B
154
89.255
23.587
17.656
1.000
19.39

ATOM
2890
C
ALA B
154
89.252
23.339
15.138
1.000
21.89

ATOM
2891
O
ALA B
154
89.788
22.995
14.076
1.000
21.95

ATOM
2892
N
SER B
155
88.113
24.003
15.248
1.000
19.65

ATOM
2893
CA
SER B
155
87.331
24.459
14.112
1.000
19.95

ATOM
2894
CB
SER B
155
86.953
23.281
13.212
1.000
19.33

ATOM
2895
OG
SER B
155
85.898
23.638
12.326
1.000
20.16

ATOM
2896
CB
SER B
155
86.071
25.161
14.598
1.000
20.44

ATOM
2897
O
SER B
155
85.582
24.855
15.684
1.000
19.66

ATOM
2898
N
VAL B
156
85.494
26.082
13.832
1.000
16.22

ATOM
2899
CA
VAL B
156
84.216
26.649
14.282
1.000
16.46

ATOM
2900
CB
VAL B
156
83.758
27.804
13.390
1.000
22.77

ATOM
2901
CG1
VAL B
156
84.736
28.970
13.469
1.000
23.36

ATOM
2902
CG2
VAL B
156
83.614
27.320
11.952
1.000
25.09

ATOM
2903
C
VAL B
156
83.130
25.577
14.345
1.000
19.15

ATOM
2904
O
VAL B
156
82.119
25.778
15.042
1.000
21.77

ATOM
2905
N
ALA B
157
83.315
24.438
13.682
1.000
17.00

ATOM
2906
CA
ALA B
157
82.380
23.321
13.744
1.000
17.11

ATOM
2907
CB
ALA B
157
82.779
22.211
12.782
1.000
13.23

ATOM
2908
C
ALA B
157
82.250
22.758
15.157
1.000
22.42

ATOM
2909
O
ALA B
157
81.307
22.027
15.471
1.000
24.11

ATOM
2910
N
ALA B
158
83.190
23.098
16.028
1.000
22.00

ATOM
2911
CA
ALA B
158
83.094
22.828
17.447
1.000
22.62

ATOM
2912
CB
ALA B
158
84.350
23.302
18.173
1.000
19.72

ATOM
2913
C
ALA B
158
81.882
23.544
18.043
1.000
23.87

ATOM
2914
O
ALA B
158
81.312
23.092
19.036
1.000
23.62

ATOM
2915
N
PHE B
159
81.514
24.670
17.437
1.000
21.51

ATOM
2916
CA
PHE B
159
80.464
25.527
17.981
1.000
22.39

ATOM
2917
CB
PHE B
159
81.035
26.942
18.156
1.000
21.64

ATOM
2918
CG
PHE B
159
82.255
26.961
19.067
1.000
24.89

ATOM
2919
CD1
PHE B
159
83.487
27.354
18.565
1.000
23.04

ATOM
2920
CD2
PHE B
159
82.143
26.589
20.397
1.000
24.09

ATOM
2921
CE1
PHE B
159
84.599
27.372
19.393
1.000
24.68

ATOM
2922
CE2
PHE B
159
83.250
26.603
21.229
1.000
24.96

ATOM
2923
CZ
PHE B
159
84.473
26.994
20.721
1.000
22.41

ATOM
2924
C
PHE B
159
79.200
25.585
17.133
1.000
25.85

ATOM
2925
O
PHE B
159
78.100
25.721
17.687
1.000
21.57

ATOM
2926
N
GLU B
160
79.327
25.497
15.813
1.000
22.51

ATOM
2927
CA
GLU B
160
78.181
25.504
14.910
1.000
23.96

ATOM
2928
CB
GLU B
160
78.041
26.820
14.150
1.000
26.01

ATOM
2929
CG
GLU B
160
77.979
28.098
14.948
1.000
32.94

ATOM
2930
CD
GLU B
160
79.247
28.924
14.932
1.000
33.82

ATOM
2931
OE1
GLU B
160
79.637
29.411
16.013
1.000
28.19

ATOM
2932
OE2
GLU B
160
79.877
29.109
13.866
1.000
27.13

ATOM
2933
C
GLU B
160
78.309
24.378
13.880
1.000
22.36

ATOM
2934
O
GLU B
160
78.302
24.652
12.675
1.000
26.67

ATOM
2935
N
GLY B
161
78.442
23.144
14.329
1.000
18.77

ATOM
2936
CA
GLY B
161
78.615
22.033
13.392
1.000
22.85

ATOM
2937
C
GLY B
161
77.447
22.008
12.412
1.000
25.07

ATOM
2938
O
GLY B
161
76.305
22.215
12.818
1.000
20.77

ATOM
2939
N
GLN B
162
77.735
21.776
11.142
1.000
23.20

ATOM
2940
CA
GLN B
162
76.717
21.802
10.100
1.000
25.68

ATOM
2941
CB
GLN B
162
77.327
22.268
8.772
1.000
21.32

ATOM
2942
CG
GLN B
162
78.011
23.621
8.830
1.000
22.80

ATOM
2943
CD
GLN B
162
78.260
24.186
7.447
1.000
26.50

ATOM
2944
OE1
GLN B
162
79.170
23.717
6.765
1.000
30.69

ATOM
2945
NE2
GLN B
162
77.474
25.170
7.034
1.000
19.53

ATOM
2946
C
GLN B
162
76.097
20.430
9.898
1.000
23.24

ATOM
2947
O
GLN B
162
76.613
19.436
10.411
1.000
23.86

ATOM
2948
N
VAL B
163
75.010
20.370
9.133
1.000
23.04

ATOM
2949
CA
VAL B
163
74.513
19.067
8.695
1.000
23.64

ATOM
2950
CB
VAL B
163
73.359
19.190
7.685
1.000
21.10

ATOM
2951
CG1
VAL B
163
73.011
17.821
7.112
1.000
24.07

ATOM
2952
CG2
VAL B
163
72.124
19.807
8.331
1.000
18.88

ATOM
2953
C
VAL B
163
75.656
18.277
8.048
1.000
25.39

ATOM
2954
O
VAL B
163
76.390
18.822
7.216
1.000
28.18

ATOM
2955
N
GLY B
164
75.804
17.016
8.423
1.000
24.05

ATOM
2956
CA
GLY B
164
76.838
16.139
7.902
1.000
22.74

ATOM
2957
C
GLY B
164
78.105
16.104
8.741
1.000
25.15

ATOM
2958
O
GLY B
164
78.930
15.201
8.552
1.000
25.10

ATOM
2959
N
GLN B
165
78.283
17.062
9.643
1.000
22.51

ATOM
2960
CA
GLN B
165
79.519
17.249
10.387
1.000
24.93

ATOM
2961
CB
GLN B
165
79.788
18.752
10.551
1.000
23.90

ATOM
2962
CG
GLN B
165
80.258
19.481
9.310
1.000
30.10

ATOM
2963
CD
GLN B
165
80.846
20.839
9.652
1.000
31.96

ATOM
2964
OE1
GLN B
165
80.265
21.595
10.432
1.000
28.58

ATOM
2965
NE2
GLN B
165
82.002
21.157
9.072
1.000
32.65

ATOM
2966
C
GLN B
165
79.551
16.655
11.789
1.000
23.68

ATOM
2967
O
GLN B
165
80.385
17.071
12.594
1.000
24.30

ATOM
2968
N
ALA B
166
78.686
15.714
12.126
1.000
21.51

ATOM
2969
CA
ALA B
166
78.662
15.164
13.481
1.000
20.54

ATOM
2970
CB
ALA B
166
77.593
14.089
13.571
1.000
18.83

ATOM
2971
C
ALA B
166
80.014
14.619
13.924
1.000
25.40

ATOM
2972
O
ALA B
166
80.485
14.947
15.018
1.000
25.59

ATOM
2973
N
ALA B
167
80.685
13.787
13.132
1.000
23.03

ATOM
2974
CA
ALA B
167
81.962
13.230
13.597
1.000
21.41

ATOM
2975
CB
ALA B
167
82.413
12.108
12.678
1.000
21.78

ATOM
2976
C
ALA B
167
83.041
14.294
13.736
1.000
22.03

ATOM
2977
O
ALA B
167
83.735
14.367
14.758
1.000
24.57

ATOM
2978
N
TYR B
168
83.200
15.138
12.732
1.000
16.78

ATOM
2979
CA
TYR B
168
84.171
16.217
12.748
1.000
18.49

ATOM
2980
CB
TYR B
168
84.094
17.005
11.444
1.000
20.42

ATOM
2981
CG
TYR B
168
85.185
18.007
11.174
1.000
17.98

ATOM
2982
CD1
TYR B
168
86.463
17.607
10.803
1.000
21.16

ATOM
2983
CE1
TYR B
168
87.460
18.536
10.555
1.000
20.16

ATOM
2984
CD2
TYR B
168
84.942
19.370
11.282
1.000
17.16

ATOM
2985
CE2
TYR B
168
85.930
20.301
11.035
1.000
21.08

ATOM
2986
CZ
TYR B
168
87.192
19.875
10.670
1.000
23.37

ATOM
2987
OB
TYR B
168
88.163
20.821
10.429
1.000
24.37

ATOM
2988
C
TYR B
168
83.921
17.154
13.927
1.000
24.27

ATOM
2989
O
TYR B
168
84.858
17.511
14.641
1.000
20.90

ATOM
2990
N
SER B
169
82.652
17.544
14.099
1.000
18.79

ATOM
2991
CA
SER B
169
82.284
18.430
15.190
1.000
18.00

ATOM
2992
CB
SER B
169
80.801
18.780
15.129
1.000
21.17

ATOM
2993
OG
SER B
169
80.533
19.822
14.200
1.000
21.93

ATOM
2994
C
SER B
169
82.627
17.795
16.537
1.000
23.23

ATOM
2995
O
SER B
169
83.059
18.494
17.452
1.000
24.85

ATOM
2996
N
ALA B
170
82.432
16.486
16.638
1.000
21.87

ATOM
2997
CA
ALA B
170
82.720
15.772
17.875
1.000
21.87

ATOM
2998
CE
ALA B
170
82.330
14.309
17.743
1.000
18.73

ATOM
2999
C
ALA B
170
84.203
15.900
18.221
1.000
25.27

ATOM
3000
O
ALA B
170
84.587
16.203
19.351
1.000
19.26

ATOM
3001
N
SER B
171
85.004
15.648
17.185
1.000
19.22

ATOM
3002
CA
SER B
171
86.454
15.647
17.335
1.000
19.66

ATOM
3003
CE
SER B
171
87.128
15.093
16.073
1.000
18.82

ATOM
3004
OG
SER B
171
87.134
16.064
15.033
1.000
21.75

ATOM
3005
C
SER B
171
86.960
17.044
17.654
1.000
23.15

ATOM
3006
O
SER B
171
87.856
17.202
18.489
1.000
24.32

ATOM
3007
N
LYS B
172
86.395
18.073
17.009
1.000
20.33

ATOM
3008
CA
LYS B
172
86.919
19.420
17.255
1.000
19.93

ATOM
3009
CE
LYS B
172
86.592
20.350
16.084
1.000
17.49

ATOM
3010
CG
LYS B
172
87.296
19.943
14.791
1.000
19.56

ATOM
3011
CD
LYS B
172
88.807
19.836
14.962
1.000
20.06

ATOM
3012
CE
LYS B
172
89.525
19.640
13.636
1.000
22.40

ATOM
3013
NZ
LYS B
172
91.012
19.804
13.754
1.000
14.90

ATOM
3014
C
LYS B
172
86.413
19.968
18.588
1.000
22.62

ATOM
3015
O
LYS B
172
87.101
20.753
19.247
1.000
20.13

ATOM
3016
N
GLY B
173
85.221
19.547
18.993
1.000
20.91

ATOM
3017
CA
GLY B
173
84.689
19.941
20.296
1.000
18.93

ATOM
3018
C
GLY B
173
85.520
19.315
21.406
1.000
20.82

ATOM
3019
O
GLY B
173
85.720
19.940
22.447
1.000
24.27

ATOM
3020
N
GLY B
174
86.005
18.106
21.175
1.000
18.50

ATOM
3021
CA
GLY B
174
86.899
17.424
22.109
1.000
17.33

ATOM
3022
C
GLY B
174
88.200
18.187
22.265
1.000
22.82

ATOM
3023
O
GLY B
174
88.694
18.342
23.382
1.000
17.85

ATOM
3024
N
ILE B
175
88.762
18.676
21.149
1.000
23.77

ATOM
3025
CA
ILE B
175
89.953
19.506
21.251
1.000
18.10

ATOM
3026
CB
ILE B
175
90.512
19.945
19.888
1.000
23.18

ATOM
3027
CG2
ILE B
175
91.745
20.818
20.126
1.000
14.17

ATOM
3028
CG1
ILE B
175
90.847
18.832
18.900
1.000
20.34

ATOM
3029
CD1
ILE B
175
92.017
17.985
19.344
1.000
28.39

ATOM
3030
C
ILE B
175
89.667
20.770
22.057
1.000
19.76

ATOM
3031
O
ILE B
175
90.452
21.171
22.919
1.000
21.09

ATOM
3032
N
VAL B
176
88.537
21.418
21.770
1.000
13.27

ATOM
3033
CA
VAL B
176
88.169
22.577
22.589
1.000
16.26

ATOM
3034
CB
VAL B
176
86.848
23.209
22.129
1.000
20.98

ATOM
3035
CG1
VAL B
176
86.280
24.144
23.187
1.000
17.07

ATOM
3036
CG2
VAL B
176
87.045
23.961
20.813
1.000
19.89

ATOM
3037
C
VAL B
176
88.069
22.181
24.066
1.000
18.42

ATOM
3038
O
VAL B
176
88.643
22.846
24.932
1.000
19.91

ATOM
3039
N
GLY B
177
87.352
21.108
24.367
1.000
18.87

ATOM
3040
CA
GLY B
177
87.058
20.737
25.745
1.000
21.80

ATOM
3041
C
GLY B
177
88.273
20.415
26.584
1.000
25.98

ATOM
3042
O
GLY B
177
88.351
20.701
27.785
1.000
19.39

ATOM
3043
N
MET B
178
89.275
19.784
25.961
1.000
20.82

ATOM
3044
CA
MET B
178
90.460
19.398
26.718
1.000
18.94

ATOM
3045
CE
MET B
178
91.065
18.115
26.138
1.000
20.57

ATOM
3046
CG
MET B
178
91.703
18.285
24.763
1.000
20.96

ATOM
3047
SD
MET B
178
92.375
16.749
24.092
1.000
24.89

ATOM
3048
CE
MET B
178
93.471
17.405
22.833
1.000
17.24

ATOM
3049
C
MET B
178
91.491
20.514
26.750
1.000
21.46

ATOM
3050
O
MET B
178
92.536
20.344
27.390
1.000
22.19

ATOM
3051
N
THR B
179
91.227
21.638
26.084
1.000
17.14

ATOM
3052
CA
THR B
179
92.236
22.705
26.048
1.000
15.87

ATOM
3053
CB
THR B
179
91.795
23.851
25.128
1.000
19.17

ATOM
3054
OG1
THR B
179
91.840
23.407
23.763
1.000
18.87

ATOM
3055
CG2
THR B
179
92.744
25.035
25.181
1.000
15.02

ATOM
3056
C
THR B
179
92.555
23.238
27.439
1.000
24.29

ATOM
3057
O
THR B
179
93.725
23.373
27.819
1.000
19.80

ATOM
3058
N
LEU B
180
91.541
23.553
28.242
1.000
21.27

ATOM
3059
CA
LEU B
180
91.803
24.095
29.574
1.000
19.96

ATOM
3060
CB
LEU B
180
90.523
24.644
30.212
1.000
14.13

ATOM
3061
CG
LEU B
180
90.683
25.218
31.623
1.000
23.37

ATOM
3062
CD1
LEU B
180
91.668
26.377
31.621
1.000
24.56

ATOM
3063
CD2
LEU B
180
89.332
25.648
32.181
1.000
23.02

ATOM
3064
C
LEU B
180
92.424
23.078
30.525
1.000
18.79

ATOM
3065
O
LEU B
180
93.438
23.415
31.163
1.000
24.04

ATOM
3066
N
PRO B
181
91.861
21.889
30.685
1.000
18.00

ATOM
3067
CD
PRO B
181
90.665
21.327
30.040
1.000
19.72

ATOM
3068
CA
PRO B
181
92.454
20.940
31.646
1.000
19.59

ATOM
3069
CB
PRO B
181
91.563
19.705
31.534
1.000
23.04

ATOM
3070
CG
PRO B
181
90.850
19.848
30.226
1.000
20.73

ATOM
3071
C
PRO B
181
93.896
20.594
31.292
1.000
27.33

ATOM
3072
O
PRO B
181
94.739
20.409
32.174
1.000
20.10

ATOM
3073
N
ILE B
182
94.220
20.508
29.996
1.000
19.63

ATOM
3074
CA
ILE B
182
95.634
20.247
29.679
1.000
18.27

ATOM
3075
CB
ILE B
182
95.813
19.877
28.200
1.000
20.42

ATOM
3076
CG2
ILE B
182
97.282
19.829
27.808
1.000
18.13

ATOM
3077
CG1
ILE B
182
95.125
18.561
27.833
1.000
17.30

ATOM
3078
CD1
ILE B
182
95.026
18.293
26.345
1.000
19.94

ATOM
3079
C
ILE B
182
96.470
21.450
30.080
1.000
22.64

ATOM
3080
O
ILE B
182
97.552
21.273
30.648
1.000
23.28

ATOM
3081
N
ALA B
183
95.981
22.665
29.823
1.000
16.56

ATOM
3082
CA
ALA B
183
96.716
23.844
30.270
1.000
17.31

ATOM
3083
CB
ALA B
183
96.034
25.129
29.836
1.000
20.13

ATOM
3084
C
ALA B
183
96.877
23.807
31.787
1.000
22.11

ATOM
3085
O
ALA B
183
97.921
24.140
32.343
1.000
17.99

ATOM
3086
N
ARG B
184
95.829
23.388
32.492
1.000
19.71

ATOM
3087
CA
ARG B
184
95.925
23.319
33.956
1.000
22.24

ATOM
3088
CB
ARG B
184
94.538
23.027
34.551
1.000
15.89

ATOM
3089
CG
ARG B
184
93.616
24.229
34.372
1.000
15.80

ATOM
3090
CD
ARG B
184
92.143
23.879
34.567
1.000
18.23

ATOM
3091
NE
ARG B
184
91.434
25.074
35.063
1.000
23.39

ATOM
3092
CZ
ARG B
184
90.228
25.034
35.628
1.000
21.65

ATOM
3093
NH1
ARG B
184
89.675
26.163
36.047
1.000
18.77

ATOM
3094
NH2
ARG B
184
89.596
23.878
35.757
1.000
17.16

ATOM
3095
C
ARG B
184
96.971
22.287
34.361
1.000
19.92

ATOM
3096
O
ARG B
184
97.823
22.537
35.216
1.000
18.04

ATOM
3097
N
ASP B
185
96.925
21.123
33.718
1.000
15.09

ATOM
3098
CA
ASP B
185
97.858
20.043
33.988
1.000
19.30

ATOM
3099
CB
ASP B
185
97.691
18.914
32.979
1.000
22.62

ATOM
3100
CG
ASP B
185
96.646
17.872
33.249
1.000
24.49

ATOM
3101
OD1
ASP B
185
96.474
17.005
32.354
1.000
20.08

ATOM
3102
OD2
ASP B
185
96.008
17.896
34.321
1.000
18.64

ATOM
3103
C
ASP B
185
99.310
20.510
33.908
1.000
26.52

ATOM
3104
O
ASP B
185
100.133
20.151
34.753
1.000
21.04

ATOM
3105
N
LEU B
186
99.629
21.284
32.872
1.000
22.36

ATOM
3106
CA
LEU B
186
101.027
21.590
32.551
1.000
23.22

ATOM
3107
CB
LEU B
186
101.228
21.533
31.027
1.000
20.41

ATOM
3108
CG1
LEU B
186
100.941
20.172
30.391
1.000
22.94

ATOM
3109
CD1
LEU B
186
101.144
20.239
28.878
1.000
21.64

ATOM
3110
CD2
LEU B
186
101.818
19.106
31.038
1.000
17.63

ATOM
3111
C
LEU B
186
101.481
22.946
33.058
1.000
22.22

ATOM
3112
O
LEU B
186
102.652
23.319
32.973
1.000
25.41

ATOM
3113
N
ALA B
187
100.555
23.729
33.595
1.000
13.92

ATOM
3114
CA
ALA B
187
100.909
25.000
34.210
1.000
16.83

ATOM
3115
CB
ALA B
187
99.648
25.573
34.846
1.000
17.97

ATOM
3116
C
ALA B
187
102.045
24.894
35.219
1.000
23.80

ATOM
3117
O
ALA B
187
102.964
25.737
35.187
1.000
21.12

ATOM
3118
N
PRO B
188
102.088
23.933
36.134
1.000
25.14

ATOM
3119
CD
PRO B
188
101.118
22.862
36.400
1.000
29.38

ATOM
3120
CA
PRO B
188
103.226
23.871
37.065
1.000
28.38

ATOM
3121
CB
PRO B
188
102.961
22.617
37.909
1.000
29.07

ATOM
3122
CG
PRO B
188
101.522
22.300
37.721
1.000
30.89

ATOM
3123
C
PRO B
188
104.566
23.693
36.364
1.000
33.56

ATOM
3124
O
PRO B
188
105.626
23.900
36.966
1.000
28.73

ATOM
3125
N
ILE B
189
104.572
23.295
35.085
1.000
27.67

ATOM
3126
CA
ILE B
189
105.895
23.163
34.465
1.000
26.87

ATOM
3127
CB
ILE B
189
106.105
21.739
33.932
1.000
30.74

ATOM
3128
CG2
ILE B
189
106.222
20.759
35.101
1.000
36.88

ATOM
3129
CD1
ILE B
189
105.044
21.259
32.943
1.000
26.76

ATOM
3130
CD1
ILE B
189
105.239
19.805
32.560
1.000
31.10

ATOM
3131
C
ILE B
189
106.098
24.202
33.378
1.000
23.49

ATOM
3132
O
ILE B
189
107.081
24.145
32.640
1.000
26.22

ATOM
3133
N
GLY B
190
105.204
25.185
33.267
1.000
18.26

ATOM
3134
CA
GLY B
190
105.447
26.271
32.329
1.000
18.80

ATOM
3135
C
GLY B
190
105.210
25.913
30.880
1.000
23.71

ATOM
3136
O
GLY B
190
105.895
26.420
29.978
1.000
25.00

ATOM
3137
N
ILE B
191
104.230
25.044
30.606
1.000
17.78

ATOM
3138
CA
ILE B
191
103.883
24.834
29.190
1.000
20.17

ATOM
3139
CB
ILE B
191
104.015
23.354
28.822
1.000
18.88

ATOM
3140
CG2
ILE B
191
103.505
23.071
27.422
1.000
23.32

ATOM
3141
CG1
ILE B
191
105.456
22.821
28.991
1.000
18.18

ATOM
3142
CD1
ILE B
191
105.515
21.310
29.030
1.000
18.45

ATOM
3143
C
ILE B
191
102.485
25.372
28.900
1.000
21.54

ATOM
3144
O
ILE B
191
101.498
24.818
29.392
1.000
25.82

ATOM
3145
N
ARG B
192
102.372
26.445
28.127
1.000
16.14

ATOM
3146
CA
ARG B
192
101.081
27.041
27.803
1.000
19.05

ATOM
3147
CB
ARG B
192
101.221
28.467
27.285
1.000
19.93

ATOM
3148
CG
ARG B
192
101.763
29.513
28.236
1.000
19.68

ATOM
3149
CD
ARG B
192
101.600
30.881
27.595
1.000
21.27

ATOM
3150
NE
ARG B
192
102.670
31.168
26.636
1.000
22.16

ATOM
3151
CZ
ARG B
192
102.485
31.544
25.382
1.000
22.96

ATOM
3152
NH1
ARG B
192
101.256
31.674
24.895
1.000
19.21

ATOM
3153
NH2
ARG B
192
103.537
31.784
24.605
1.000
21.25

ATOM
3154
C
ARG B
192
100.361
26.239
26.723
1.000
19.37

ATOM
3155
O
ARG B
192
101.027
25.680
25.848
1.000
24.14

ATOM
3156
N
VAL B
193
99.040
26.191
26.788
1.000
20.05

ATOM
3157
CA
VAL B
193
98.241
25.380
25.863
1.000
18.11

ATOM
3158
CB
VAL B
193
97.685
24.114
26.518
1.000
20.36

ATOM
3159
CG1
VAL B
193
96.889
23.250
25.545
1.000
20.35

ATOM
3160
CG2
VAL B
193
98.814
23.273
27.113
1.000
16.91

ATOM
3161
C
VAL B
193
97.127
26.267
25.310
1.000
23.22

ATOM
3162
O
VAL B
193
96.324
26.809
26.074
1.000
16.71

ATOM
3163
N
MET B
194
97.131
26.421
23.986
1.000
21.51

ATOM
3164
CA
MET B
194
96.216
27.310
23.288
1.000
21.01

ATOM
3165
CB
MET B
194
96.933
28.569
22.790
1.000
18.60

ATOM
3166
CG
MET B
194
97.200
29.614
23.855
1.000
20.05

ATOM
3167
SD
MET B
194
95.704
30.422
24.469
1.000
19.46

ATOM
3168
CE
MET B
194
95.163
31.257
22.966
1.000
14.83

ATOM
3169
C
MET B
194
95.545
26.611
22.109
1.000
23.67

ATOM
3170
O
MET B
194
96.053
25.634
21.564
1.000
19.31

ATOM
3171
N
THR B
195
94.381
27.127
21.706
1.000
19.14

ATOM
3172
CA
THR B
195
93.691
26.481
20.590
1.000
21.41

ATOM
3173
CB
THR B
195
92.552
25.590
21.110
1.000
19.80

ATOM
3174
OG1
THR B
195
93.118
24.424
21.732
1.000
18.08

ATOM
3175
CG2
THR B
195
91.673
25.077
19.981
1.000
20.44

ATOM
3176
C
THR B
195
93.172
27.519
19.602
1.000
20.93

ATOM
3177
O
THR B
195
92.659
28.565
19.997
1.000
22.89

ATOM
3178
N
ILE B
196
93.323
27.219
18.311
1.000
24.23

ATOM
3179
CA
ILE B
196
92.772
28.060
17.250
1.000
21.67

ATOM
3180
CB
ILE B
196
93.815
28.433
16.185
1.000
18.92

ATOM
3181
CG2
ILE B
196
93.167
29.187
15.035
1.000
11.18

ATOM
3182
CG1
ILE B
196
94.987
29.235
16.746
1.000
18.01

ATOM
3183
CD1
ILE B
196
96.221
29.325
15.871
1.000
23.93

ATOM
3184
C
ILE B
196
91.592
27.321
16.617
1.000
19.12

ATOM
3185
O
ILE B
196
91.709
26.122
16.356
1.000
19.48

ATOM
3186
N
ALA B
197
90.492
28.028
16.405
1.000
17.65

ATOM
3187
CA
ALA B
197
89.319
27.474
15.742
1.000
20.33

ATOM
3188
CB
ALA B
197
88.076
27.676
16.602
1.000
15.84

ATOM
3189
C
ALA B
197
89.119
28.125
14.381
1.000
19.04

ATOM
3190
O
ALA B
197
88.425
29.142
14.277
1.000
22.10

ATOM
3191
N
PRO B
198
89.708
27.585
13.325
1.000
17.32

ATOM
3192
CD
PRO B
198
90.585
26.401
13.272
1.000
15.77

ATOM
3193
CA
PRO B
198
89.535
28.199
12.001
1.000
18.83

ATOM
3194
CB
PRO B
198
90.466
27.375
11.106
1.000
18.30

ATOM
3195
CG
PRO B
198
91.429
26.726
12.052
1.000
17.25

ATOM
3196
C
PRO B
198
88.105
28.088
11.492
1.000
17.88

ATOM
3197
O
PRO B
198
87.418
27.110
11.741
1.000
22.07

ATOM
3198
N
GLY B
199
87.624
29.084
10.753
1.000
17.24

ATOM
3199
CA
GLY B
199
86.354
28.939
10.047
1.000
21.59

ATOM
3200
C
GLY B
199
86.582
28.289
8.685
1.000
26.45

ATOM
3201
O
GLY B
199
86.803
27.077
8.621
1.000
32.80

ATOM
3202
N
LEU B
200
86.537
29.074
7.612
1.000
26.29

ATOM
3203
CA
LEU B
200
86.750
28.565
6.261
1.000
26.22

ATOM
3204
CB
LEU B
200
85.593
28.919
5.337
1.000
30.80

ATOM
3205
CG
LEU B
200
84.171
28.547
5.729
1.000
29.38

ATOM
3206
CD1
LEU B
200
83.196
29.355
4.884
1.000
21.97

ATOM
3207
CD2
LEU B
200
83.940
27.051
5.577
1.000
26.34

ATOM
3208
C
LEU B
200
88.034
29.129
5.645
1.000
21.47

ATOM
3209
O
LEU B
200
88.154
30.343
5.478
1.000
23.70

ATOM
3210
N
PHE B
201
88.964
28.244
5.316
1.000
17.48

ATOM
3211
CA
PHE B
201
90.280
28.647
4.858
1.000
20.96

ATOM
3212
CB
PHE B
201
91.342
28.233
5.887
1.000
20.51

ATOM
3213
CG
PHE B
201
91.619
29.319
6.910
1.000
22.85

ATOM
3214
CD1
PHE B
201
90.719
29.547
7.936
1.000
22.28

ATOM
3215
CD2
PHE B
201
92.768
30.090
6.833
1.000
20.32

ATOM
3216
CE1
PHE B
201
90.969
30.543
8.869
1.000
21.15

ATOM
3217
CE2
PHE B
201
93.020
31.086
7.758
1.000
20.28

ATOM
3218
CZ
PHE B
201
92.121
31.308
8.785
1.000
20.28

ATOM
3219
C
PHE B
201
90.646
28.017
3.521
1.000
25.00

ATOM
3220
O
PHE B
201
90.280
26.880
3.226
1.000
24.24

ATOM
3221
N
GLY B
202
91.389
28.781
2.726
1.000
28.46

ATOM
3222
CA
GLY B
202
91.796
28.281
1.426
1.000
27.60

ATOM
3223
C
GLY B
202
92.971
27.335
1.519
1.000
26.65

ATOM
3224
O
GLY B
202
94.051
27.658
1.027
1.000
32.79

ATOM
3225
N
THR B
203
92.793
26.160
2.102
1.000
24.28

ATOM
3226
CA
THR B
203
93.793
25.097
1.999
1.000
26.69

ATOM
3227
CB
THR B
203
93.965
24.347
3.324
1.000
27.45

ATOM
3228
OG1
THR B
203
92.784
23.550
3.515
1.000
25.36

ATOM
3229
CG2
THR B
203
94.091
25.273
4.518
1.000
28.01

ATOM
3230
C
THR B
203
93.324
24.131
0.918
1.000
28.64

ATOM
3231
O
THR B
203
92.175
24.359
0.486
1.000
30.62

ATOM
3232
N
PRO B
204
94.072
23.142
0.466
1.000
28.39

ATOM
3233
CD
PRO B
204
95.462
22.820
0.828
1.000
28.87

ATOM
3234
CA
PRO B
204
93.578
22.220
−0.571
1.000
30.63

ATOM
3235
CB
PRO B
204
94.591
21.068
−0.536
1.000
27.82

ATOM
3236
CG
PRO B
204
95.859
21.748
−0.140
1.000
27.77

ATOM
3237
C
PRO B
204
92.181
21.679
−0.294
1.000
38.86

ATOM
3238
O
PRO B
204
91.429
21.401
−1.232
1.000
34.56

ATOM
3239
N
LEU B
205
91.836
21.548
0.983
1.000
39.43

ATOM
3240
CA
LEU B
205
90.506
21.139
1.411
1.000
33.83

ATOM
3241
CB
LEU B
205
90.451
21.293
2.926
1.000
32.03

ATOM
3242
CG
LEU B
205
89.410
20.595
3.776
1.000
36.51

ATOM
3243
CD1
LEU B
205
88.999
19.229
3.260
1.000
34.60

ATOM
3244
CD2
LEU B
205
89.964
20.456
5.203
1.000
33.53

ATOM
3245
C
LEU B
205
89.426
21.950
0.723
1.000
28.71

ATOM
3246
O
LEU B
205
88.378
21.423
0.342
1.000
37.20

ATOM
3247
N
LEU B
206
89.636
23.251
0.513
1.000
25.71

ATOM
3248
CA
LEU B
206
88.591
24.054
−0.118
1.000
30.76

ATOM
3249
CB
LEU B
206
88.240
25.255
0.766
1.000
36.14

ATOM
3250
CG
LEU B
206
88.103
24.958
2.263
1.000
40.37

ATOM
3251
CD1
LEU B
206
87.571
26.179
2.997
1.000
60.97

ATOM
3252
CD2
LEU B
206
87.208
23.751
2.492
1.000
33.96

ATOM
3253
C
LEU B
206
88.986
24.558
−1.501
1.000
40.20

ATOM
3254
O
LEU B
206
88.165
24.616
−2.423
1.000
30.96

ATOM
3255
N
THR B
207
90.254
24.941
−1.661
1.000
31.29

ATOM
3256
CA
THR B
207
90.678
25.454
−2.963
1.000
39.95

ATOM
3257
CB
THR B
207
92.132
25.965
−2.884
1.000
42.48

ATOM
3258
OG1
THR B
207
92.958
24.995
−2.219
1.000
36.55

ATOM
3259
CG2
THR B
207
92.184
27.251
−2.065
1.000
34.71

ATOM
3260
C
THR B
207
90.537
24.416
−4.073
1.000
39.41

ATOM
3261
O
THR B
207
90.485
24.780
−5.256
1.000
44.36

ATOM
3262
N
SER B
208
90.475
23.130
−3.721
1.000
28.72

ATOM
3263
CA
SER B
208
90.370
22.082
−4.739
1.000
33.20

ATOM
3264
CB
SER B
208
91.057
20.795
−4.288
1.000
33.20

ATOM
3265
OG
SER B
208
90.464
20.257
−3.124
1.000
33.13

ATOM
3266
C
SER B
208
88.912
21.814
−5.098
1.000
42.89

ATOM
3267
O
SER B
208
88.575
20.862
−5.803
1.000
45.91

ATOM
3268
N
LEU B
209
88.031
22.681
−4.603
1.000
38.04

ATOM
3269
CA
LEU B
209
86.621
22.583
−4.940
1.000
35.13

ATOM
3270
CB
LEU B
209
85.756
23.031
−3.768
1.000
39.19

ATOM
3271
CG
LEU B
209
85.885
22.257
−2.457
1.000
55.29

ATOM
3272
CD1
LEU B
209
85.627
23.172
−1.267
1.000
60.85

ATOM
3273
CD2
LEU B
209
84.932
21.066
−2.428
1.000
57.75

ATOM
3274
C
LEU B
209
86.311
23.435
−6.170
1.000
37.91

ATOM
3275
O
LEU B
209
87.022
24.396
−6.475
1.000
30.12

ATOM
3276
N
PRO B
210
85.231
23.068
−6.853
1.000
34.73

ATOM
3277
CD
PRO B
210
84.373
21.918
−6.548
1.000
34.46

ATOM
3278
CA
PRO B
210
84.778
23.819
−8.026
1.000
38.34

ATOM
3279
CB
PRO B
210
83.398
23.230
−8.306
1.000
41.74

ATOM
3280
CG
PRO B
210
83.425
21.867
−7.706
1.000
41.21

ATOM
3281
C
PRO B
210
84.651
25.310
−7.725
1.000
38.15

ATOM
3282
O
PRO B
210
84.266
25.712
−6.627
1.000
41.50

ATOM
3283
N
GLU B
211
84.980
26.128
−8.717
1.000
32.53

ATOM
3284
CA
GLU B
211
84.981
27.576
−8.561
1.000
31.26

ATOM
3285
CB
GLU B
211
85.370
28.233
−9.891
1.000
35.90

ATOM
3286
CG
GLU B
211
84.870
29.659
−10.046
1.000
43.23

ATOM
3287
CD
GLU B
211
85.279
30.303
−11.356
1.000
51.95

ATOM
3288
OE1
GLU B
211
85.853
31.414
−11.323
1.000
62.26

ATOM
3289
OE2
GLU B
211
85.029
29.704
−12.425
1.000
53.28

ATOM
3290
C
GLU B
212
83.642
28.099
−8.061
1.000
32.27

ATOM
3291
O
GLU B
211
83.581
28.997
−7.213
1.000
21.03

ATOM
3292
N
LYS B
212
82.529
27.569
−8.563
1.000
32.31

ATOM
3293
CA
LYS B
212
81.243
28.070
−8.071
1.000
38.47

ATOM
3294
CB
LYS B
212
80.068
27.458
−8.811
1.000
29.32

ATOM
3295
C
LYS B
212
81.148
27.788
−6.577
1.000
43.86

ATOM
3296
O
LYS B
212
80.668
28.602
−5.789
1.000
54.98

ATOM
3297
N
VAL B
213
81.625
26.598
−6.191
1.000
38.14

ATOM
3298
CA
VAL B
213
81.567
26.297
−4.759
1.000
35.85

ATOM
3299
CB
VAL B
213
81.926
24.835
−4.467
1.000
38.37

ATOM
3300
CG1
VAL B
213
81.931
24.560
−2.970
1.000
31.23

ATOM
3301
CG2
VAL B
213
80.936
23.914
−5.173
1.000
41.89

ATOM
3302
C
VAL B
213
82.476
27.256
−3.998
1.000
31.46

ATOM
3303
O
VAL B
213
82.070
27.793
−2.972
1.000
37.88

ATOM
3304
N
ARG B
214
83.691
27.495
−4.475
1.000
37.75

ATOM
3305
CA
ARG B
214
84.587
28.420
−3.777
1.000
41.19

ATOM
3306
CB
ARG B
214
85.934
28.529
−4.503
1.000
39.36

ATOM
3307
CG
ARG B
214
86.647
27.190
−4.626
1.000
43.05

ATOM
3308
CD
ARG B
214
88.093
27.320
−5.068
1.000
40.23

ATOM
3309
NE
ARG B
214
88.247
28.114
−6.277
1.000
35.00

ATOM
3310
CZ
ARG B
214
88.345
27.639
−7.512
1.000
39.48

ATOM
3311
NH1
ARG B
214
88.308
26.332
−7.732
1.000
33.49

ATOM
3312
NH2
ARG B
214
88.481
28.477
−8.536
1.000
38.43

ATOM
3313
C
ARG B
214
83.922
29.783
−3.624
1.000
33.34

ATOM
3314
O
ARG B
214
83.863
30.355
−2.532
1.000
33.42

ATOM
3315
N
ASN B
215
83.400
30.309
−4.724
1.000
29.46

ATOM
3316
CA
ASN B
215
82.698
31.589
−4.675
1.000
24.27

ATOM
3317
CB
ASN B
215
82.091
31.913
−6.036
1.000
27.96

ATOM
3318
CG
ASN B
215
83.116
32.178
−7.116
1.000
49.03

ATOM
3319
OD1
ASN B
215
84.318
32.249
−6.853
1.000
61.54

ATOM
3320
ND2
ASN B
215
82.628
32.326
−8.347
1.000
66.34

ATOM
3321
C
ASN B
215
81.589
31.563
−3.630
1.000
31.46

ATOM
3322
O
ASN B
215
81.385
32.518
−2.888
1.000
40.57

ATOM
3323
N
PHE B
216
80.846
30.457
−3.584
1.000
33.81

ATOM
3324
CA
PHE B
216
79.719
30.371
−2.665
1.000
34.18

ATOM
3325
CB
PHE B
216
78.916
29.090
−2.910
1.000
32.53

ATOM
3326
CG
PHE B
216
77.792
28.911
−1.898
1.000
37.68

ATOM
3327
CD1
PHE B
216
76.862
29.916
−1.702
1.000
44.84

ATOM
3328
CD2
PHE B
216
77.680
27.755
−1.153
1.000
45.52

ATOM
3329
CE1
PHE B
216
75.839
29.772
−0.783
1.000
46.68

ATOM
3330
CE2
PHE B
216
76.661
27.599
−0.233
1.000
47.17

ATOM
3331
CZ
PHE B
216
75.736
28.610
−0.042
1.000
46.55

ATOM
3332
C
PHE B
216
80.187
30.427
−1.211
1.000
39.70

ATOM
3333
O
PHE B
216
79.620
31.156
−0.394
1.000
35.84

ATOM
3334
N
LEU B
217
81.219
29.643
−0.911
1.000
36.33

ATOM
3335
CA
LEU B
217
81.780
29.551
0.430
1.000
30.36

ATOM
3336
CB
LEU B
217
82.852
28.461
0.506
1.000
32.88

ATOM
3337
CG
LEU B
217
82.298
27.035
0.611
1.000
36.90

ATOM
3338
CD1
LEU B
217
83.363
25.994
0.305
1.000
43.23

ATOM
3339
CD2
LEU B
217
81.693
26.802
1.991
1.000
30.83

ATOM
3340
C
LEU B
217
82.332
30.902
0.861
1.000
28.07

ATOM
3341
O
LEU B
217
82.036
31.352
1.966
1.000
26.98

ATOM
3342
N
ALA B
218
83.107
31.532
−0.015
1.000
27.69

ATOM
3343
CA
ALA B
218
83.615
32.869
0.265
1.000
35.60

ATOM
3344
CB
ALA B
218
84.459
33.400
−0.887
1.000
31.53

ATOM
3345
C
ALA B
218
82.466
33.831
0.527
1.000
35.67

ATOM
3346
O
ALA B
218
82.521
34.677
1.416
1.000
30.41

ATOM
3347
N
SER B
219
81.411
33.689
−0.277
1.000
35.07

ATOM
3348
CA
SER B
219
80.254
34.560
−0.141
1.000

ATOM
3349
CB
SER B
219
78.405
33.091
−0.657
1.000
24.81

ATOM
3350
OG
SER B
219
78.405
33.091
−0.657
1.000
24.81

ATOM
3351
CB
SER B
219
79.634
34.508
1.252
1.000
26.91

ATOM
3352
O
SER B
219
78.893
35.438
1.574
1.000
40.31

ATOM
3353
N
GLN B
220
79.901
33.478
2.037
1.000
29.34

ATOM
3354
CA
GLN B
220
79.337
33.292
3.370
1.000
29.90

ATOM
3355
CB
GLN B
220
79.274
31.810
3.738
1.000
36.32

ATOM
3356
CG
GLN B
220
78.756
30.911
2.625
1.000
48.32

ATOM
3357
CD
GLN B
220
77.429
30.306
3.022
1.000
54.56

ATOM
3358
OE1
GLN B
220
76.375
30.908
2.830
1.000
67.54

ATOM
3359
NE2
GLN B
220
77.491
29.095
3.572
1.000
56.82

ATOM
3360
C
GLN B
220
80.138
33.992
4.470
1.000
30.30

ATOM
3361
O
GLN B
220
79.662
34.133
5.605
1.000
23.80

ATOM
3362
N
VAL B
221
81.375
34.404
4.2.81
1.000
25.59

ATOM
3363
CA
VAL B
221
82.170
35.013
5.253
1.000
21.11

ATOM
3364
CB
VAL B
221
83.683
34.827
5.056
1.000
18.83

ATOM
3365
CD1
VAL B
221
84.403
35.365
6.287
1.000
14.24

ATOM
3366
CG2
VAL B
221
84.034
33.366
4.799
1.000
14.24

ATOM
3367
C
VAL B
221
81.826
36.492
5.318
1.000
24.34

ATOM
3368
O
VAL B
221
81.981
37.173
4.296
1.000
26.30

ATOM
3369
N
PRO B
222
81.353
37.005
6.445
1.000
23.91

ATOM
3370
CD
PRO B
222
81.160
36.335
7.743
1.000
24.90

ATOM
3371
CA
PRO B
222
80.914
38.407
6.479
1.000
21.55

ATOM
3372
CB
PRO B
222
80.489
38.615
7.940
1.000
19.51

ATOM
3373
CG
PRO B
222
80.127
37.233
8.396
1.000
21.27

ATOM
3374
C
PRO B
222
81.999
39.392
6.085
1.000
26.91

ATOM
3375
O
PRO B
222
81.791
40.209
5.179
1.000
24.96

ATOM
3376
N
PHE B
223
83.167
39.377
6.731
1.000
24.34

ATOM
3377
CA
PHE B
223
84.216
40.284
6.262
1.000
23.07

ATOM
3378
CB
PHE B
223
83.936
41.746
6.649
1.000
21.27

ATOM
3379
CG
PHE B
223
85.084
42.637
6.178
1.000
24.70

ATOM
3380
CD1
PHE B
223
85.177
42.994
4.842
1.000
29.09

ATOM
3381
CD2
PHE B
223
86.053
43.094
7.051
1.000
22.56

ATOM
3382
CE1
PHE B
223
86.224
43.781
4.379
1.000
25.41

ATOM
3383
CE2
PHE B
223
87.105
43.869
6.597
1.000
25.23

ATOM
3384
CZ
PHE B
223
87.200
44.214
5.258
1.000
21.68

ATOM
3385
C
PHE B
223
85.586
39.845
6.784
1.000
27.57

ATOM
3386
O
PHE B
223
85.715
39.631
7.997
1.000
23.91

ATOM
3387
N
PRO B
224
86.599
39.735
5.933
1.000
28.05

ATOM
3388
CG
PRO B
224
87.984
39.411
6.329
1.000
29.64

ATOM
3389
CA
PRO B
224
86.504
39.941
4.483
1.000
28.44

ATOM
3390
CB
PRO B
224
87.959
40.006
4.022
1.000
30.61

ATOM
3391
CG
PRO B
224
88.696
39.180
5.019
1.000
27.95

ATOM
3392
C
PRO B
224
85.800
38.774
3.803
1.000
25.89

ATOM
3393
O
PRO B
224
85.878
37.651
4.292
1.000
23.18

ATOM
3394
N
SER B
225
85.094
39.059
2.716
1.000
26.20

ATOM
3395
CA
SER B
225
84.219
38.049
2.125
1.000
28.41

ATOM
3396
CB
SER B
225
83.066
38.708
1.367
1.000
37.56

ATOM
3397
OG
SER B
225
82.385
39.622
2.211
1.000
54.93

ATOM
3398
CB
SER B
225
85.006
37.117
1.215
1.000
28.63

ATOM
3399
O
SER B
225
84.844
37.124
−0.003
1.000
28.75

ATOM
3400
N
ARG B
226
85.858
36.310
1.832
1.000
22.36

ATOM
3401
CA
ARG B
226
86.687
35.359
1.115
1.000
22.82

ATOM
3402
CB
ARG B
226
87.892
36.056
0.470
1.000
18.79

ATOM
3403
CG
ARG B
226
88.677
36.899
1.473
1.000
21.54

ATOM
3404
CD
ARG B
226
90.176
36.733
1.316
1.000
25.20

ATOM
3405
NE
ARG B
226
90.922
37.696
2.120
1.000
23.19

ATOM
3406
CZ
ARG B
226
91.575
37.367
3.226
1.000
25.07

ATOM
3407
NE1
ARG B
226
92.224
38.304
3.893
1.000
19.90

ATOM
3408
NE2
ARG B
226
91.576
36.114
3.651
1.000
23.08

ATOM
3409
C
ARG B
226
87.181
34.273
2.064
1.000
26.25

ATOM
3410
O
ARG B
226
87.133
34.410
3.288
1.000
24.82

ATOM
3411
N
LEU B
227
87.670
33.187
1.479
1.000
21.51

ATOM
3412
CA
LEU B
227
88.281
32.148
2.305
1.000
25.72

ATOM
3413
CE
LEU B
227
88.685
30.973
1.412
1.000
25.48

ATOM
3414
CG
LEU B
227
87.517
30.370
0.608
1.000
26.39

ATOM
3415
CD1
LEU B
227
88.031
29.371
−0.415
1.000
23.44

ATOM
3416
CD2
LEU B
227
86.495
29.736
1.543
1.000
18.43

ATOM
3417
C
LEU B
227
89.453
32.727
3.074
1.000
24.64

ATOM
3418
O
LEU B
227
90.092
33.694
2.658
1.000
18.08

ATOM
3419
N
GLY B
228
89.760
32.167
4.249
1.000
26.03

ATOM
3420
CA
GLY B
228
90.925
32.693
4.964
1.000
22.23

ATOM
3421
C
GLY B
228
92.209
32.285
4.257
1.000
20.68

ATOM
3422
O
GLY B
228
92.244
31.206
3.651
1.000
22.79

ATOM
3423
N
ASP B
229
93.247
33.113
4.332
1.000
20.55

ATOM
3424
CA
ASP B
229
94.548
32.733
3.763
1.000
20.20

ATOM
3425
CE
ASP B
229
95.305
33.966
3.311
1.000
26.22

ATOM
3426
CG
ASP B
229
96.686
33.727
2.742
1.000
37.78

ATOM
3427
OD1
ASP B
229
97.180
34.649
2.055
1.000
50.30

ATOM
3428
OD2
ASP B
229
97.311
32.665
2.942
1.000
36.38

ATOM
3429
C
ASP B
229
95.351
31.964
4.809
1.000
18.70

ATOM
3430
O
ASP B
229
95.515
32.497
5.906
1.000
22.47

ATOM
3431
N
PRO B
230
95.839
30.776
4.487
1.000
24.85

ATOM
3432
CD
PRO B
230
95.682
30.076
3.196
1.000
25.08

ATOM
3433
CA
PRO B
230
96.623
29.975
5.441
1.000
24.33

ATOM
3434
CE
PRO B
230
97.245
28.898
4.543
1.000
26.36

ATOM
3435
CG
PRO B
230
96.196
28.690
3.488
1.000
25.22

ATOM
3436
C
PRO B
230
97.701
30.776
6.156
1.000
26.10

ATOM
3437
O
PRO B
230
98.023
30.510
7.317
1.000
24.78

ATOM
3438
N
ALA B
231
98.263
31.777
5.487
1.000
25.30

ATOM
3439
CA
ALA B
231
99.260
32.641
6.098
1.000
24.99

ATOM
3440
CB
ALA B
231
99.850
33.597
5.081
1.000
21.53

ATOM
3441
C
ALA B
231
98.650
33.423
7.260
1.000
27.72

ATOM
3442
O
ALA B
231
99.380
33.872
8.142
1.000
23.63

ATOM
3443
N
GLU B
232
97.326
33.586
7.249
1.000
23.39

ATOM
3444
CA
GLU B
232
96.690
34.297
8.370
1.000
24.37

ATOM
3445
CB
GLU B
232
95.313
34.829
7.971
1.000
24.04

ATOM
3446
CG
GLU B
232
95.399
35.976
6.963
1.000
22.30

ATOM
3447
CD
GLU B
232
94.083
36.265
6.268
1.000
19.98

ATOM
3448
OE1
GLU B
232
93.333
35.320
5.959
1.000
17.23

ATOM
3449
OE2
GLU B
232
93.790
37.451
6.032
1.000
22.71

ATOM
3450
C
GLU B
232
96.619
33.387
9.586
1.000
20.32

ATOM
3451
O
GLU B
232
96.791
33.821
10.728
1.000
23.31

ATOM
3452
N
TYR B
233
96.394
32.097
9.369
1.000
17.51

ATOM
3453
CA
TYR B
233
96.485
31.156
10.490
1.000
20.79

ATOM
3454
CB
TYR B
233
96.161
29.733
10.043
1.000
18.94

ATOM
3455
CG
TYR B
233
96.350
28.654
11.076
1.000
19.81

ATOM
3456
CD1
TYR B
233
95.289
28.296
11.907
1.000
20.70

ATOM
3457
CE1
TYR B
233
95.437
27.303
12.862
1.000
18.77

ATOM
3458
CD2
TYR B
233
97.546
27.974
11.245
1.000
17.63

ATOM
3459
CE2
TYR B
233
97.712
26.992
12.194
1.000
22.14

ATOM
3460
CZ
TYR B
233
96.648
26.658
13.007
1.000
22.85

ATOM
3461
OH
TYR B
233
96.811
25.672
13.953
1.000
22.40

ATOM
3462
C
TYR B
233
97.889
31.236
11.094
1.000
29.44

ATOM
3463
O
TYR B
233
98.077
31.335
12.308
1.000
25.44

ATOM
3464
N
ALA B
234
98.883
31.168
10.212
1.000
21.62

ATOM
3465
CA
ALA B
234
100.282
31.201
10.623
1.000
20.02

ATOM
3466
CE
ALA B
234
101.188
31.127
9.400
1.000
24.84

ATOM
3467
C
ALA B
234
100.594
32.446
11.440
1.000
17.92

ATOM
3468
O
ALA B
234
101.231
32.346
12.492
1.000
25.05

ATOM
3469
N
HIS B
235
100.159
33.611
10.977
1.000
17.22

ATOM
3470
CA
HIS B
235
100.336
34.841
11.739
1.000
18.97

ATOM
3471
CB
HIS B
235
99.660
36.020
11.045
1.000
17.03

ATOM
3472
CG
HIS B
235
99.589
37.276
11.854
1.000
21.49

ATOM
3473
CD2
HIS B
235
98.703
37.758
12.765
1.000
22.09

ATOM
3474
ND1
HIS B
235
100.566
38.248
11.751
1.000
26.88

ATOM
3475
CE1
HIS B
235
100.286
39.259
12.561
1.000
24.36

ATOM
3476
NE2
HIS B
235
99.153
38.983
13.195
1.000
25.35

ATOM
3477
C
HIS B
235
99.768
34.673
13.150
1.000
24.20

ATOM
3478
O
HIS B
235
100.338
35.162
14.127
1.000
20.64

ATOM
3479
N
LEU B
236
98.622
33.999
13.272
1.000
24.19

ATOM
3480
CA
LEU B
236
98.023
33.863
14.602
1.000
22.43

ATOM
3481
CB
LEU B
236
96.560
33.416
14.532
1.000
17.42

ATOM
3482
CG
LEU B
236
95.880
33.237
15.902
1.000
16.92

ATOM
3483
CD1
LEU B
236
96.023
34.506
16.729
1.000
16.92

ATOM
3484
CD2
LEU B
236
94.422
32.851
15.744
1.000
16.70

ATOM
3485
C
LEU B
236
98.846
32.903
15.456
1.000
21.64

ATOM
3486
O
LEU B
236
99.001
33.128
16.659
1.000
20.22

ATOM
3487
N
VAL B
237
99.376
31.834
14.868
1.000
19.99

ATOM
3488
CA
VAL B
237
100.251
30.929
15.608
1.000
18.28

ATOM
3489
CB
VAL B
237
100.792
29.795
14.727
1.000
25.11

ATOM
3490
CG1
VAL B
237
101.981
29.110
15.395
1.000
23.91

ATOM
3491
CG2
VAL B
237
99.705
28.775
14.415
1.000
18.18

ATOM
3492
C
VAL B
237
101.415
31.721
16.194
1.000
24.84

ATOM
3493
O
VAL B
237
101.774
31.589
17.369
1.000
24.82

ATOM
3494
N
GLN B
238
102.015
32.578
15.361
1.000
20.39

ATOM
3495
CA
GLN B
238
103.134
33.377
15.837
1.000
21.98

ATOM
3496
CB
GLN B
238
103.718
34.217
14.695
1.000
26.47

ATOM
3497
CG
GLN B
238
104.840
35.137
15.173
1.000
33.86

ATOM
3498
CD
GLN B
238
105.728
35.611
14.040
1.000
45.57

ATOM
3499
OE1
GLN B
238
105.410
35.440
12.861
1.000
45.00

ATOM
3500
NE2
GLN B
238
106.855
36.220
14.396
1.000
42.07

ATOM
3501
C
GLN B
238
102.749
34.305
16.984
1.000
22.31

ATOM
3502
O
GLN B
238
103.498
34.472
17.950
1.000
26.79

ATOM
3503
N
ALA B
239
101.576
34.930
16.875
1.000
18.16

ATOM
3504
CA
ALA B
239
101.135
35.872
17.902
1.000
18.40

ATOM
3505
CB
ALA B
239
99.819
36.533
17.511
1.000
20.73

ATOM
3506
C
ALA B
239
101.018
35.158
19.250
1.000
20.71

ATOM
3507
O
ALA B
239
101.457
35.685
20.265
1.000
23.16

ATOM
3508
N
ILE B
240
100.450
33.961
19.235
1.000
20.05

ATOM
3509
CA
ILE B
240
100.289
33.138
20.426
1.000
25.35

ATOM
3510
CB
ILE B
240
99.418
31.904
20.136
1.000
21.83

ATOM
3511
CG2
ILE B
240
99.470
30.903
21.280
1.000
19.47

ATOM
3512
CG1
ILE B
240
97.958
32.221
19.798
1.000
15.52

ATOM
3513
CD1
ILE B
240
97.238
31.016
19.220
1.000
15.32

ATOM
3514
C
ILE B
240
101.643
32.700
20.974
1.000
28.29

ATOM
3515
O
ILE B
240
101.861
32.715
22.190
1.000
23.76

ATOM
3516
N
ILE B
241
102.565
32.318
20.090
1.000
22.50

ATOM
3517
CA
ILE B
241
103.911
31.983
20.553
1.000
25.40

ATOM
3518
CB
ILE B
241
104.840
31.538
19.407
1.000
27.14

ATOM
3519
CG2
ILE B
241
106.289
31.468
19.869
1.000
20.81

ATOM
3520
CD1
ILE B
241
104.452
30.211
18.738
1.000
21.73

ATOM
3521
CD1
ILE B
241
105.073
30.067
17.356
1.000
19.24

ATOM
3522
C
ILE B
241
104.525
33.188
21.253
1.000
23.95

ATOM
3523
O
ILE B
241
105.177
33.056
22.288
1.000
22.10

ATOM
3524
N
GLU B
242
104.325
34.378
20.686
1.000
19.53

ATOM
3525
CA
GLU B
242
105.016
35.554
21.188
1.000
20.82

ATOM
3526
CB
GLU B
242
105.098
36.638
20.117
1.000
22.01

ATOM
3527
CG
GLU B
242
105.898
36.269
18.878
1.000
25.93

ATOM
3528
CD
GLU B
242
105.964
37.432
17.897
1.000
30.65

ATOM
3529
OE1
GLU B
242
106.791
37.382
16.965
1.000
39.62

ATOM
3530
OE2
GLU B
242
105.192
38.405
18.052
1.000
35.25

ATOM
3531
C
GLU B
242
104.368
36.145
22.437
1.000
27.37

ATOM
3532
O
GLU B
242
105.070
36.770
23.241
1.000
24.53

ATOM
3533
N
ASN B
243
103.064
35.975
22.607
1.000
22.12

ATOM
3534
CA
ASN B
243
102.369
36.569
23.748
1.000
26.24

ATOM
3535
CB
ASN B
243
100.916
36.907
23.391
1.000
21.07

ATOM
3536
CG
ASN B
243
100.332
37.907
24.370
1.000
22.04

ATOM
3537
OD1
ASN B
243
100.327
37.675
25.580
1.000
22.80

ATOM
3538
ND2
ASN B
243
99.843
39.030
23.849
1.000
21.75

ATOM
3539
C
ASN B
243
102.403
35.645
24.959
1.000
23.87

ATOM
3540
O
ASN B
243
101.770
34.588
24.967
1.000
25.67

ATOM
3541
N
PRO B
244
103.160
36.009
25.986
1.000
23.78

ATOM
3542
CD
PRO B
244
103.897
37.274
26.156
1.000
22.06

ATOM
3543
CA
PRO B
244
103.350
35.103
27.127
1.000
23.04

ATOM
3544
CB
PRO B
244
104.415
35.814
27.969
1.000
22.47

ATOM
3545
CG
PRO B
244
105.017
36.844
27.078
1.000
23.63

ATOM
3546
C
PRO B
244
102.099
34.888
27.964
1.000
20.27

ATOM
3547
O
PRO B
244
102.063
33.958
28.774
1.000
23.10

ATOM
3548
N
PHE B
245
101.068
35.717
27.816
1.000
24.09

ATOM
3549
CA
PHE B
245
99.922
35.612
28.728
1.000
19.94

ATOM
3550
CB
PHE B
245
99.530
37.003
29.232
1.000
24.39

ATOM
3551
CG
PHE B
245
99.015
37.049
30.670
1.000
21.73

ATOM
3552
CD1
PHE B
245
97.758
37.569
30.956
1.000
17.78

ATOM
3553
CD2
PHE B
245
99.799
36.577
31.708
1.000
17.75

ATOM
3554
CE1
PHE B
245
97.290
37.617
32.257
1.000
20.49

ATOM
3555
CE2
PHE B
245
99.324
36.619
33.017
1.000
20.79

ATOM
3556
CZ
PHE B
245
98.067
37.132
33.302
1.000
17.74

ATOM
3557
C
PHE B
245
98.725
34.925
28.084
1.000
27.35

ATOM
3558
O
PHE B
245
97.675
34.806
28.736
1.000
19.89

ATOM
3559
N
LEU B
246
98.842
34.471
26.832
1.000
22.36

ATOM
3560
CA
LEU B
246
97.762
33.710
26.212
1.000
17.89

ATOM
3561
CB
LEU B
246
97.784
33.848
24.686
1.000
22.68

ATOM
3562
CG
LEU B
246
97.091
35.100
24.133
1.000
25.09

ATOM
3563
CD1
LEU B
246
97.472
35.302
22.675
1.000
23.65

ATOM
3564
CD2
LEU B
246
95.578
35.009
24.322
1.000
20.52

ATOM
3565
C
LEU B
246
97.844
32.238
26.587
1.000
23.42

ATOM
3566
O
LEU B
246
98.768
31.511
26.212
1.000
22.20

ATOM
3567
N
ASN B
247
96.845
31.782
27.351
1.000
21.98

ATOM
3568
CA
ASN B
247
96.882
30.399
27.809
1.000
21.01

ATOM
3569
CB
ASN B
247
97.787
30.310
29.039
1.000
21.94

ATOM
3570
CG
ASN B
247
98.210
28.908
29.411
1.000
25.84

ATOM
3571
OD1
ASN B
247
98.028
27.941
28.675
1.000
17.45

ATOM
3572
ND2
ASN B
247
98.792
28.782
30.606
1.000
23.37

ATOM
3573
C
ASN B
247
95.483
29.883
28.121
1.000
21.43

ATOM
3574
O
ASN B
247
94.652
30.609
28.676
1.000
19.82

ATOM
3575
N
GLY B
248
95.237
28.628
27.766
1.000
19.48

ATOM
3576
CA
GLY B
248
94.013
27.950
28.126
1.000
19.31

ATOM
3577
C
GLY B
248
92.796
28.438
27.373
1.000
22.31

ATOM
3578
O
GLY B
248
91.663
28.233
27.819
1.000
17.54

ATOM
3579
N
GLU B
249
93.031
29.070
26.231
1.000
17.27

ATOM
3580
CA
GLU B
249
91.945
29.718
25.494
1.000
16.46

ATOM
3581
CB
GLU B
249
92.194
31.218
25.514
1.000
14.25

ATOM
3582
CG
GLU B
249
91.391
32.096
24.591
1.000
19.57

ATOM
3583
CG
GLU B
249
89.904
32.186
24.864
1.000
21.27

ATOM
3584
OE1
GLU B
249
89.338
33.286
24.699
1.000
24.41

ATOM
3585
OE2
GLU B
249
89.280
31.165
25.211
1.000
21.97

ATOM
3586
C
GLU B
249
91.828
29.176
24.072
1.000
24.78

ATOM
3587
O
GLU B
249
92.772
28.582
23.534
1.000
19.55

ATOM
3588
N
VAL B
250
90.648
29.371
23.494
1.000
21.56

ATOM
3589
CA
VAL B
250
90.339
29.004
22.114
1.000
12.85

ATOM
3590
CB
VAL B
250
89.143
28.047
22.038
1.000
23.39

ATOM
3591
CG1
VAL B
250
88.826
27.692
20.594
1.000
22.07

ATOM
3592
CG2
VAL B
250
89.418
26.790
22.860
1.000
21.03

ATOM
3593
C
VAL B
250
90.048
30.275
21.326
1.000
19.79

ATOM
3594
O
VAL B
250
89.234
31.088
21.776
1.000
18.20

ATOM
3595
N
ILE B
251
90.692
30.490
20.180
1.000
16.00

ATOM
3596
CA
ILE B
251
90.482
31.725
19.431
1.000
17.61

ATOM
3597
CB
ILE B
251
91.816
32.468
19.247
1.000
20.13

ATOM
3598
CG2
ILE B
251
91.679
33.615
18.256
1.000
19.21

ATOM
3599
CG1
ILE B
251
92.413
32.951
20.572
1.000
19.68

ATOM
3600
CD1
ILE B
251
93.807
33.526
20.465
1.000
18.52

ATOM
3602
C
ILE B
251
89.866
31.466
18.061
1.000
20.08

ATOM
3602
O
ILE B
251
90.456
30.740
17.256
1.000
23.04

ATOM
3603
N
ARG B
252
88.699
32.046
17.802
1.00021.13

ATOM
3604
CA
ARG B
252
88.045
31.910
16.506
1.000
20.87

ATOM
3605
CB
ARG B
252
86.572
32.316
16.551
1.000
19.90

ATOM
3606
CG
ARG B
252
85.652
31.342
17.277
1.000
22.38

ATOM
3607
CD
ARG B
252
84.222
31.909
17.273
1.000
23.90

ATOM
3608
NE
ARG B
252
83.591
31.572
15.999
1.000
20.02

ATOM
3609
CZ
ARG B
252
82.532
30.796
15.850
1.000
22.56

ATOM
3610
NH1
ARG B
252
82.029
30.538
14.647
1.000
17.65

ATOM
3611
NH2
ARG B
252
81.959
30.267
16.922
1.000
22.29

ATOM
3612
C
ARG B
252
88.771
32.770
15.468
1.000
18.40

ATOM
3613
O
ARG B
252
88.956
33.959
15.692
1.000
15.46

ATOM
3614
N
LEU B
253
89.172
32.173
14.356
1.000
21.76

ATOM
3615
CA
LEU B
253
89.827
32.918
13.269
1.000
19.75

ATOM
3616
CB
LEU B
253
91.273
32.462
13.119
1.000
16.90

ATOM
3617
CG
LEU B
253
92.110
33.141
12.031
1.000
19.36

ATOM
3618
CD1
LEU B
253
92.373
34.599
12.382
1.000
13.74

ATOM
3619
CD2
LEU B
253
93.411
32.381
11.811
1.000
15.37

ATOM
3620
C
LEU B
253
89.011
32.685
12.005
1.000
21.76

ATOM
3621
O
LEU B
253
89.232
31.685
11.318
1.000
20.48

ATOM
3622
N
ASP B
254
88.040
33.556
11.735
1.000
19.57

ATOM
3623
CA
ASP B
254
86.997
33.164
10.802
1.000
19.40

ATOM
3624
CB
ASP B
254
85.984
32.301
11.591
1.000
13.95

ATOM
3625
CG
ASP B
254
85.259
33.087
12.664
1.000
18.25

ATOM
3626
OD1
ASP B
254
85.428
34.315
12.794
1.000
14.45

ATOM
3627
OD2
ASP B
254
84.480
32.462
13.415
1.000
22.32

ATOM
3628
C
ASP B
254
86.256
34.300
10.122
1.000
21.71

ATOM
3629
O
ASP B
254
85.196
34.050
9.522
1.000
23.65

ATOM
3630
N
GLY B
255
86.713
35.539
10.180
1.000
20.84

ATOM
3631
CA
GLY B
255
86.027
36.608
9.463
1.000
18.31

ATOM
3632
C
GLY B
255
84.584
36.829
9.898
1.000
25.13

ATOM
3633
O
GLY B
255
83.783
37.337
9.102
1.000
19.08

ATOM
3634
N
ALA B
256
84.280
36.453
11.129
1.000
24.78

ATOM
3635
CA
ALA B
256
83.025
36.658
11.830
1.000
21.84

ATOM
3636
CB
ALA B
256
82.632
38.133
11.754
1.000
17.70

ATOM
3637
C
ALA B
256
81.888
35.778
11.325
1.000
20.87

ATOM
3638
O
ALA B
256
80.708
36.023
11.597
1.000
19.77

ATOM
3639
N
ILE B
257
82.197
34.716
10.588
1.000
19.51

ATOM
3640
CA
ILE B
257
81.157
33.804
10.126
1.000
18.52

ATOM
3641
CB
ILE B
257
81.683
32.833
9.057
1.000
16.68

ATOM
3642
CG2
ILE B
257
82.531
31.734
9.681
1.000
23.55

ATOM
3643
CG1
ILE B
257
80.606
32.195
8.177
1.000
18.12

ATOM
3644
CD1
ILE B
257
81.207
31.337
7.073
1.000
15.00

ATOM
3645
C
ILE B
257
80.602
32.990
11.291
1.000
24.02

ATOM
3646
O
ILE B
257
81.287
32.733
12.283
1.000
19.85

ATOM
3647
N
ARG B
258
79.347
32.595
11.153
1.000
21.98

ATOM
3648
CA
ARG B
258
78.698
31.606
12.004
1.000
20.95

ATOM
3649
CB
ARG B
258
77.670
32.216
12.947
1.000
17.82

ATOM
3650
CG
ARG B
258
78.207
33.229
13.949
1.000
17.12

ATOM
3651
CD
ARG B
258
79.175
32.588
14.912
1.000
20.59

ATOM
3652
NE
ARG B
258
79.702
33.469
15.952
1.000
20.13

ATOM
3653
CZ
ARG B
258
80.800
34.200
15.832
1.000
23.28

ATOM
3654
NH1
ARG B
258
81.214
34.974
16.827
1.000
17.97

ATOM
3655
NH2
ARG B
258
81.506
34.173
14.705
1.000
17.45

ATOM
3656
C
ARG B
258
78.078
30.576
11.055
1.000
21.87

ATOM
3657
O
ARG B
258
77.313
30.946
10.160
1.000
23.38

ATOM
3658
N
MET B
259
78.392
29.297
11.206
1.000
21.54

ATOM
3659
CA
MET B
259
77.924
28.325
10.220
1.000
22.43

ATOM
3660
CB
MET B
259
78.739
27.036
10.336
1.000
23.84

ATOM
3661
CG
MET B
259
80.249
27.215
10.293
1.000
28.42

ATOM
3662
SD
MET B
259
80.816
28.247
8.932
1.000
29.19

ATOM
3663
CE
MET B
259
80.445
27.228
7.511
1.000
26.28

ATOM
3664
C
MET B
259
76.447
27.994
10.357
1.000
30.61

ATOM
3665
O
MET B
259
75.928
27.762
11.452
1.000
30.15

ATOM
3666
N
GLN B
260
75.748
27.953
9.220
1.000
29.07

ATOM
3667
CA
GLN B
260
74.339
27.512
9.259
1.000
25.36

ATOM
3668
CB
GLN B
260
73.535
28.432
8.343
1.000
31.16

ATOM
3669
CG
GLN B
260
72.731
29.454
9.136
1.000
45.72

ATOM
3670
CD
GLN B
260
72.532
29.188
10.610
1.000
49.74

ATOM
3671
OE1
GLN B
260
71.445
28.810
11.050
1.000
37.88

ATOM
3672
NE2
GLN B
260
73.538
29.373
11.459
1.000
67.46

ATOM
3673
C
GLN B
260
74.247
26.030
8.956
1.000
24.46

ATOM
3674
O
GLN B
260
75.291
25.449
8.618
1.000
23.06

ATOM
3675
N
PRO B
261
73.101
25.371
9.080
1.000
22.31

ATOM
3676
CD
PRO B
261
71.765
25.894
9.433
1.000
28.76

ATOM
3677
CA
PRO B
261
73.065
23.921
8.879
1.000
21.73

ATOM
3678
CB
PRO B
261
71.567
23.586
8.950
1.000
25.36

ATOM
3679
CG
PRO B
261
70.990
24.665
9.805
1.000
27.61

ATOM
3680
C
PRO B
261
73.626
23.481
7.530
1.000
26.41

ATOM
3681
OT1
PRO B
261
73.474
24.202
6.525
1.000
28.81

ATOM
3682
OT2
PRO B
261
74.233
22.384
7.508
1.000
28.12

ATOM
3683
PN
NAD B
262
94.476
21.958
6.429
1.000
28.31

ATOM
3684
O1N
NAD B
262
93.463
22.904
5.865
1.000
34.51

ATOM
3685
O2N
NAD B
262
95.865
22.443
6.568
1.000
23.47

ATOM
3686
O3P
NAD B
262
94.370
20.567
5.731
1.000
33.68

ATOM
3687
OSM
NAD B
262
93.895
21.576
7.886
1.000
30.78

ATOM
3688
C5M
NAD B
262
94.768
21.765
9.037
1.000
26.31

ATOM
3689
C4M
NAD B
262
93.935
21.757
10.307
1.000
25.70

ATOM
3690
O4M
NAD B
262
92.977
22.828
10.156
1.000
29.89

ATOM
3691
C3M
NAD B
262
93.132
20.450
10.430
1.000
31.27

ATOM
3692
O3M
NAD B
262
92.997
20.071
11.809
1.000
40.08

ATOM
3693
C2M
NAD B
262
91.731
20.826
9.885
1.000
32.57

ATOM
3694
O2M
NAD B
262
90.747
19.918
10.417
1.000
40.60

ATOM
3695
C1M
NAD B
262
91.677
22.240
10.432
1.000
30.08

ATOM
3696
N1N
NAD B
262
90.616
23.120
9.899
1.000
37.23

ATOM
3697
C6N
NAD B
262
89.624
23.559
10.781
1.000
28.95

ATOM
3698
C5N
NAD B
262
88.566
24.365
10.368
1.000
32.41

ATOM
3699
C4N
NAD B
262
88.465
24.847
8.942
1.000
33.49

ATOM
3700
C3N
NAD B
262
89.608
24.363
8.069
1.000
32.22

ATOM
3701
C2N
NAD B
262
90.607
23.542
8.552
1.000
37.43

ATOM
3702
C7N
NAD B
262
89.613
24.852
6.631
1.000
36.14

ATOM
3703
O7N
NAD B
262
88.579
25.278
6.126
1.000
41.68

ATOM
3704
N7N
NAD B
262
90.771
24.795
5.981
1.000
29.37

ATOM
3705
PA
NAD B
262
95.272
19.767
4.701
1.000
37.66

ATOM
3706
O1A
NAD B
262
94.526
18.562
4.361
1.000
32.50

ATOM
3707
O2A
NAD B
262
95.736
20.790
3.767
1.000
30.89

ATOM
3708
O5B
NAD B
262
96.478
19.276
5.642
1.000
41.07

ATOM
3709
C5B
NAD B
262
96.142
18.219
6.581
1.000
31.86

ATOM
3710
C4B
NAD B
262
97.492
17.592
6.832
1.000
27.90

ATOM
3711
O4B
NAD B
262
97.270
16.597
7.826
1.000
27.37

ATOM
3712
C3B
NAD B
262
97.931
16.870
5.543
1.000
22.88

ATOM
3713
O3B
NAD B
262
99.322
17.164
5.210
1.000
29.54

ATOM
3714
C2B
NAD B
262
97.702
15.437
5.925
1.000
24.16

ATOM
3715
O2B
NAD B
262
98.553
14.519
5.247
1.000
28.28

ATOM
3716
C1B
NAD B
262
97.989
15.475
7.430
1.000
26.54

ATOM
3717
N9A
NAD B
262
97.552
14.268
8.121
1.000
25.83

ATOM
3718
C4A
NAD B
262
98.303
13.579
8.987
1.000
20.78

ATOM
3719
N3A
NAD B
262
99.524
13.651
9.529
1.000
17.71

ATOM
3720
C2A
NAD B
262
99.938
12.740
10.403
1.000
15.99

ATOM
3721
N1A
NAD B
262
99.171
11.723
10.781
1.000
21.15

ATOM
3722
C6A
NAD B
262
97.933
11.578
10.284
1.000
27.89

ATOM
3723
C5A
NAD B
262
97.508
12.537
9.367
1.000
24.05

ATOM
3724
N7A
NAD B
262
96.312
12.565
8.759
1.000
22.87

ATOM
3725
C8A
NAD B
262
96.368
13.656
7.986
1.000
18.27

ATOM
3726
N6A
NAD B
262
97.174
10.564
10.660
1.000
24.18

ATOM
3727
CB
SER C
7
104.044
47.282
9.332
1.000
66.78

ATOM
3728
CB
SER C
7
101.832
47.872
10.314
1.000
47.05

ATOM
3729
O
SER C
7
100.991
48.304
9.526
1.000
47.44

ATOM
3730
N
SER C
7
102.108
45.815
8.998
1.000
59.49

ATOM
3731
CA
SER C
7
102.758
46.727
9.929
1.000
50.05

ATOM
3732
N
VAL C
8
101.991
48.376
11.537
1.000
41.20

ATOM
3733
CA
VAL C
8
101.083
49.420
12.005
1.000
36.25

ATOM
3734
CB
VAL C
8
100.808
49.295
13.515
1.000
37.80

ATOM
3735
CG1
VAL C
8
100.118
47.971
13.818
1.000
30.04

ATOM
3736
CG2
VAL C
8
102.100
49.440
14.305
1.000
28.58

ATOM
3737
C
VAL C
8
101.644
50.798
11.690
1.000
32.07

ATOM
3738
O
VAL C
8
101.009
51.814
11.974
1.000
33.78

ATOM
3739
N
LYS C
9
102.836
50.817
11.102
1.000
30.77

ATOM
3740
CA
LYS C
9
103.482
52.078
10.746
1.000
29.01

ATOM
3741
CB
LYS C
9
104.767
51.812
9.976
1.000
28.15

ATOM
3742
C
LYS C
9
102.541
52.963
9.940
1.000
29.94

ATOM
3743
O
LYS C
9
101.941
52.514
8.968
1.000
29.66

ATOM
3744
N
GLY C
10
102.385
54.215
10.360
1.000
31.59

ATOM
3745
CA
GLY C
10
101.522
55.142
9.666
1.000
33.52

ATOM
3746
C
GLY C
10
100.057
55.094
10.031
1.000
32.35

ATOM
3747
O
GLY C
10
99.310
56.020
9.691
1.000
35.47

ATOM
3748
N
LEU C
11
99.599
54.052
10.721
1.000
28.45

ATOM
3749
CA
LEU C
11
98.186
53.987
11.099
1.000
25.53

ATOM
3750
CB
LEU C
11
97.849
52.594
11.639
1.000
24.47

ATOM
3751
CG
LEU C
11
97.907
51.473
10.593
1.000
34.47

ATOM
3752
CD1
LEU C
11
97.628
50.114
11.217
1.000
35.93

ATOM
3753
CD2
LEU C
11
96.927
51.755
9.458
1.000
32.14

ATOM
3754
C
LEU C
11
97.824
55.052
12.125
1.000
25.52

ATOM
3755
O
LEU C
11
98.680
55.511
12.884
1.000
27.62

ATOM
3756
N
VAL C
12
96.557
55.451
12.149
1.000
24.05

ATOM
3757
CA
VAL C
12
96.051
56.379
13.153
1.000
24.59

ATOM
3758
CB
VAL C
12
95.350
57.592
12.516
1.000
28.40

ATOM
3759
CG1
VAL C
12
94.813
58.519
13.597
1.000
22.74

ATOM
3760
CG2
VAL C
12
96.305
58.326
11.584
1.000
26.07

ATOM
3761
C
VAL C
12
95.076
55.672
14.091
1.000
30.65

ATOM
3762
O
VAL C
12
94.058
55.119
13.655
1.000
28.77

ATOM
3763
N
ALA C
13
95.402
55.687
15.386
1.000
25.84

ATOM
3764
CA
ALA C
13
94.551
54.989
16.348
1.000
25.82

ATOM
3765
CB
ALA C
13
95.315
53.854
17.018
1.000
25.53

ATOM
3766
C
ALA C
13
93.994
55.938
17.407
1.000
26.90

ATOM
3767
O
ALA C
13
94.733
56.727
17.992
1.000
28.28

ATOM
3768
N
VAL C
14
92.690
55.845
17.641
1.000
23.52

ATOM
3769
CA
VAL C
14
92.058
56.564
18.750
1.000
24.13

ATOM
3770
CB
VAL C
14
90.708
57.180
18.375
1.000
24.45

ATOM
3771
CG1
VAL C
14
90.033
57.820
19.581
1.000
22.78

ATOM
3772
CG2
VAL C
14
90.876
58.221
17.275
1.000
23.77

ATOM
3773
C
VAL C
14
91.912
55.568
19.903
1.000
27.36

ATOM
3774
O
VAL C
14
91.304
54.511
19.729
1.000
23.19

ATOM
3775
N
ILE C
15
92.497
55.901
21.050
1.000
27.18

ATOM
3776
CA
ILE C
15
92.530
55.001
22.199
1.000
20.98

ATOM
3777
CB
ILE C
15
93.992
54.654
22.542
1.000
21.64

ATOM
3778
CG2
ILE C
15
94.074
53.721
23.739
1.000
24.49

ATOM
3779
CG1
ILE C
15
94.753
54.070
21.352
1.000
25.53

ATOM
3780
CD1
ILE C
15
96.229
53.822
21.576
1.000
30.45

ATOM
3781
C
ILE C
15
91.820
55.612
23.392
1.000
23.68

ATOM
3782
O
ILE C
15
92.291
56.563
24.024
1.000
23.20

ATOM
3783
N
THR C
16
90.642
55.078
23.734
1.000
23.69

ATOM
3784
CA
THR C
16
89.966
55.658
24.904
1.000
24.76

ATOM
3785
CB
THR C
16
88.444
55.452
24.868
1.000
22.95

ATOM
3786
OG1
THR C
16
88.140
54.146
25.361
1.000
22.63

ATOM
3787
CG2
THR C
16
87.938
55.536
23.430
1.000
14.61

ATOM
3788
C
THR C
16
90.564
55.057
26.172
1.000
17.75

ATOM
3789
O
THR C
16
90.998
53.907
26.171
1.000
23.59

ATOM
3790
N
GLY C
17
90.594
55.847
27.240
1.000
25.44

ATOM
3791
CA
GLY C
17
91.312
55.462
28.451
1.000
21.38

ATOM
3792
C
GLY C
17
92.807
55.446
28.172
1.000
26.04

ATOM
3793
O
GLY C
17
93.583
54.716
28.787
1.000
26.02

ATOM
3794
N
GLY C
18
93.241
56.260
27.212
1.000
25.57

ATOM
3795
CA
GLY C
18
94.624
56.224
26.780
1.000
23.27

ATOM
3796
C
GLY C
18
95.607
56.901
27.702
1.000
25.52

ATOM
3797
O
GLY C
18
96.817
56.861
27.435
1.000
25.03

ATOM
3798
N
ALA C
19
95.152
57.541
28.776
1.000
23.60

ATOM
3799
CA
ALA C
19
96.093
58.208
29.676
1.000
22.47

ATOM
3800
CB
ALA C
19
95.423
59.388
30.373
1.000
21.48

ATOM
3801
C
ALA C
19
96.640
57.247
30.715
1.000
28.26

ATOM
3802
O
ALA C
19
97.523
57.562
31.516
1.000
25.69

ATOM
3803
N
SER C
20
96.107
56.022
30.754
1.000
25.74

ATOM
3804
CA
SER C
20
96.517
55.152
31.870
1.000
24.16

ATOM
3805
CB
SER C
20
95.640
55.492
33.083
1.000
25.59

ATOM
3806
OG
SER C
20
95.760
54.584
34.149
1.000
25.32

ATOM
3807
CB
SER C
20
96.449
53.688
31.485
1.000
25.80

ATOM
3808
O
SER C
20
95.846
53.324
30.474
1.000
22.31

ATOM
3809
N
GLY C
21
97.084
52.851
32.302
1.000
24.52

ATOM
3810
CA
GLY C
21
97.035
51.415
32.209
1.000
24.48

ATOM
3811
C
GLY C
21
97.032
50.810
30.830
1.000
27.26

ATOM
3812
O
GLY C
21
97.934
51.074
30.035
1.000
22.91

ATOM
3813
N
LEU C
22
96.052
49.968
30.507
1.000
24.52

ATOM
3814
CA
LEU C
22
96.083
49.212
29.254
1.000
21.40

ATOM
3815
CB
LEU C
22
94.938
48.195
29.237
1.000
20.78

ATOM
3816
CG
LEU C
22
94.886
47.203
30.401
1.000
17.62

ATOM
3817
CD1
LEU C
22
93.684
46.276
30.275
1.000
16.40

ATOM
3818
CD2
LEU C
22
96.149
46.360
30.485
1.000
18.61

ATOM
3819
C
LEU C
22
96.032
50.112
28.022
1.000
22.73

ATOM
3820
O
LEU C
22
96.725
49.853
27.028
1.000
26.59

ATOM
3821
N
GLY C
23
95.224
51.166
28.040
1.000
22.05

ATOM
3822
CA
GLY C
23
95.184
52.107
26.934
1.000
26.20

ATOM
3823
C
GLY C
23
96.510
52.806
26.694
1.000
25.29

ATOM
3824
O
GLY C
23
96.946
52.987
25.552
1.000
23.10

ATOM
3825
N
LEU C
24
97.174
53.224
27.756
1.000
19.82

ATOM
3826
CA
LEU C
24
98.463
53.904
27.656
1.000
21.17

ATOM
3827
CB
LEU C
24
98.914
54.431
29.023
1.000
20.85

ATOM
3828
CG
LEU C
24
100.322
55.038
29.077
1.000
25.39

ATOM
3829
CD1
LEU C
24
100.405
56.276
28.194
1.000
21.88

ATOM
3830
CD2
LEU C
24
100.710
55.359
30.513
1.000
24.95

ATOM
3831
C
LEU C
24
99.534
52.971
27.109
1.000
23.71

ATOM
3832
O
LEU C
24
100.353
53.352
26.274
1.000
26.75

ATOM
3833
N
ALA C
25
99.530
51.733
27.596
1.000
23.88

ATOM
3834
CA
ALA C
25
100.486
50.731
27.129
1.000
23.51

ATOM
3835
CE
ALA C
25
100.339
49.469
27.962
1.000
22.54

ATOM
3836
C
ALA C
25
100.294
50.444
25.646
1.000
26.08

ATOM
3837
O
ALA C
25
101.252
50.214
24.908
1.000
27.79

ATOM
3838
N
THR C
26
99.036
50.458
25.215
1.000
27.03

ATOM
3839
CA
THR C
26
98.726
50.283
23.797
1.000
23.27

ATOM
3840
CB
THR C
26
97.210
50.151
23.588
1.000
23.63

ATOM
3841
OG1
THR C
26
96.757
49.018
24.341
1.000
24.28

ATOM
3842
CG2
THR C
26
96.879
49.871
22.129
1.000
19.08

ATOM
3843
C
THR C
26
99.285
51.445
22.990
1.000
20.18

ATOM
3844
O
THR C
26
99.967
51.246
21.983
1.000
26.90

ATOM
3845
N
ALA C
27
99.013
52.666
23.438
1.000
18.50

ATOM
3846
CA
ALA C
27
99.545
53.852
22.780
1.000
24.38

ATOM
3847
CB
ALA C
27
99.097
55.102
23.521
1.000
24.65

ATOM
3848
C
ALA C
27
101.065
53.784
22.670
1.000
27.80

ATOM
3849
O
ALA C
27
101.645
53.987
21.603
1.000
28.51

ATOM
3850
N
GLU C
28
101.754
53.489
23.761
1.000
25.77

ATOM
3851
CA
GLU C
28
103.204
53.346
23.738
1.000
28.24

ATOM
3852
CE
GLU C
28
103.686
52.865
25.126
1.000
27.28

ATOM
3853
CG
GLU C
28
103.837
54.027
26.089
1.000
30.52

ATOM
3854
CG
GLU C
28
103.849
53.670
27.559
1.000
36.62

ATOM
3855
OE1
GLU C
28
103.834
54.636
28.356
1.000
39.77

ATOM
3856
OE2
GLU C
28
103.875
52.478
27.938
1.000
39.86

ATOM
3857
C
GLU C
28
103.689
52.395
22.657
1.000
29.47

ATOM
3858
O
GLU C
28
104.529
52.716
21.819
1.000
24.48

ATOM
3859
N
ARG C
29
103.163
51.173
22.643
1.000
26.01

ATOM
3860
CA
ARG C
29
103.627
50.179
21.687
1.000
24.39

ATOM
3861
CB
ARG C
29
102.929
48.832
21.940
1.000
22.49

ATOM
3862
CG
ARG C
29
103.387
47.773
20.954
1.000
25.33

ATOM
3863
CD
ARG C
29
102.736
46.417
21.157
1.000
25.09

ATOM
3864
NE
ARC C
29
103.371
45.445
20.252
1.000
26.15

ATOM
3865
CZ
ARC C
29
104.492
44.805
20.567
1.000
29.99

ATOM
3866
NE1
ARC C
29
105.034
43.943
19.722
1.000
32.98

ATOM
3867
NH2
ARG C
29
105.082
45.024
21.735
1.000
29.67

ATOM
3868
C
ARG C
29
103.393
50.615
20.247
1.000
29.05

ATOM
3869
O
ARG C
29
104.290
50.524
19.416
1.000
30.10

ATOM
3870
N
LEU C
30
102.181
51.074
19.944
1.000
24.61

ATOM
3871
CA
LEU C
30
101.845
51.433
18.569
1.000
27.57

ATOM
3872
CE
LEU C
30
100.340
51.702
18.463
1.000
27.67

ATOM
3873
CG
LEU C
30
99.412
50.514
18.748
1.000
26.24

ATOM
3874
CD1
LEU C
30
97.951
50.907
18.577
1.000
17.98

ATOM
3875
CD2
LEU C
30
99.739
49.330
17.852
1.000
26.64

ATOM
3876
C
LEU C
30
102.657
52.632
18.101
1.000
30.46

ATOM
3877
O
LEU C
30
103.199
52.663
16.993
1.000
32.23

ATOM
3878
N
VAL C
31
102.757
53.649
18.946
1.000
25.35

ATOM
3879
CA
VAL C
31
103.564
54.824
18.622
1.000
28.65

ATOM
3880
CE
VAL C
31
103.384
55.913
19.688
1.000
34.14

ATOM
3881
CG1
VAL C
31
104.538
56.899
19.707
1.000
41.82

ATOM
3882
CG2
VAL C
31
102.065
56.648
19.435
1.000
29.57

ATOM
3883
C
VAL C
31
105.019
54.417
18.474
1.000
30.00

ATOM
3884
O
VAL C
31
105.720
54.884
17.575
1.000
34.69

ATOM
3885
N
GLY C
32
105.491
53.529
19.341
1.000
25.99

ATOM
3886
CA
GLY C
32
106.857
53.035
19.228
1.000
28.69

ATOM
3887
C
GLY C
32
107.124
52.338
17.906
1.000
35.56

ATOM
3888
O
CLY C
32
108.267
52.191
17.471
1.000
28.87

ATOM
3889
N
GLN C
33
106.061
51.887
17.249
1.000
36.98

ATOM
3890
CA
GLN C
33
106.139
51.231
15.959
1.000
35.59

ATOM
3891
CB
GLN C
33
105.129
50.079
15.896
1.000
39.66

ATOM
3892
CG
GLN C
33
105.422
48.955
16.881
1.000
44.72

ATOM
3893
CG
GLN C
33
106.200
47.830
16.228
1.000
49.92

ATOM
3894
CE1
GLN C
33
105.897
47.417
15.105
1.000
58.45

ATOM
3895
NE2
GLN C
33
107.213
47.333
16.933
1.000
58.98

ATOM
3896
C
GLN C
33
105.857
52.191
14.812
1.000
33.46

ATOM
3897
O
GLN C
33
105.688
51.726
13.681
1.000
33.18

ATOM
3898
N
GLY C
34
105.779
53.497
15.049
1.000
29.41

ATOM
3899
CA
GLY C
34
105.569
54.436
13.961
1.000
29.74

ATOM
3900
C
GLY C
34
104.129
54.744
13.625
1.000
34.10

ATOM
3901
O
GLY C
34
103.831
55.329
12.575
1.000
29.85

ATOM
3902
N
ALA C
35
103.191
54.367
14.501
1.000
31.11

ATOM
3903
CA
ALA C
35
101.797
54.764
14.286
1.000
24.85

ATOM
3904
CB
ALA C
35
100.850
53.680
14.768
1.000
24.26

ATOM
3905
C
ALA C
35
101.518
56.086
14.980
1.000
26.16

ATOM
3906
O
ALA C
35
102.344
56.612
15.728
1.000
30.99

ATOM
3907
N
SER C
36
100.343
56.674
14.751
1.000
25.80

ATOM
3908
CA
SER C
36
100.006
57.889
15.494
1.000
30.50

ATOM
3909
CB
SER C
36
99.592
59.028
14.564
1.000
29.64

ATOM
3910
OG
SER C
36
100.588
59.261
13.582
1.000
30.71

ATOM
3911
CB
SER C
36
98.904
57.581
16.499
1.000
33.79

ATOM
3912
O
SER C
36
98.000
56.779
16.254
1.000
29.57

ATOM
3913
N
ALA C
37
98.960
58.220
17.667
1.000
30.46

ATOM
3914
CA
ALA C
37
97.940
57.900
18.666
1.000
29.38

ATOM
3915
CB
ALA C
37
98.571
57.180
19.846
1.000
26.18

ATOM
3916
C
ALA C
37
97.195
59.145
19.125
1.000
24.63

ATOM
3917
O
ALA C
37
97.739
60.231
19.270
1.000
31.10

ATOM
3918
N
VAL C
38
95.903
58.948
19.346
1.000
23.46

ATOM
3919
CA
VAL C
38
95.060
59.963
19.960
1.000
25.11

ATOM
3920
CB
VAL C
38
93.825
60.332
19.129
1.000
26.80

ATOM
3921
CG1
VAL C
38
92.957
61.323
19.893
1.000
22.47

ATOM
3922
CG2
VAL C
38
94.251
60.893
17.778
1.000
31.11

ATOM
3923
C
VAL C
38
94.611
59.420
21.315
1.000
28.98

ATOM
3924
O
VAL C
38
93.885
58.425
21.331
1.000
23.94

ATOM
3925
N
LEU C
39
95.066
60.051
22.396
1.000
28.48

ATOM
3926
CA
LEU C
39
94.646
59.587
23.721
1.000
24.19

ATOM
3927
CB
LEU C
39
95.697
59.886
24.775
1.000
24.94

ATOM
3928
CG
LEU C
39
97.140
59.481
24.489
1.000
23.07

ATOM
3929
CD1
LEU C
39
98.018
59.768
25.704
1.000
24.37

ATOM
3930
CD2
LEU C
39
97.225
58.014
24.090
1.000
20.30

ATOM
3931
C
LEU C
39
93.327
60.247
24.098
1.000
24.84

ATOM
3932
O
LEU C
39
93.298
61.411
24.488
1.000
30.15

ATOM
3933
N
LEU C
40
92.230
59.509
23.971
1.000
24.08

ATOM
3934
CA
LEU C
40
90.934
60.058
24.383
1.000
22.68

ATOM
3935
CB
LEU C
40
89.823
59.471
23.529
1.000
18.90

ATOM
3936
CG
LEU C
40
88.475
60.190
23.477
1.000
24.88

ATOM
3937
CD1
LEU C
40
87.713
59.786
22.218
1.000
25.54

ATOM
3938
CD2
LEU C
40
87.628
59.900
24.705
1.000
23.21

ATOM
3939
C
LEU C
40
90.713
59.765
25.863
1.000
23.80

ATOM
3940
O
LEU C
40
90.476
58.618
26.258
1.000
27.07

ATOM
3941
N
ASP C
41
90.796
60.777
26.718
1.000
25.76

ATOM
3942
CA
ASP C
41
90.600
60.487
28.149
1.000
28.47

ATOM
3943
CB
ASP C
41
91.923
60.028
28.746
1.000
21.68

ATOM
3944
CG
ASP C
41
91.767
59.043
29.884
1.000
27.64

ATOM
3945
OD1
ASP C
41
90.911
59.267
30.766
1.000
27.48

ATOM
3946
OD2
ASP C
41
92.503
58.037
29.925
1.000
26.03

ATOM
3947
C
ASP C
41
90.008
61.697
28.857
1.000
28.20

ATOM
3948
O
ASP C
41
89.924
62.770
28.254
1.000
24.75

ATOM
3949
N
LEU C
42
89.579
61.540
30.108
1.000
27.88

ATOM
3950
CA
LEU C
42
88.935
62.638
30.826
1.000
28.79

ATOM
3951
CB
LEU C
42
88.405
62.159
32.179
1.000
27.37

ATOM
3952
CG
LEU C
42
87.154
61.285
32.154
1.000
29.50

ATOM
3953
CD1
LEU C
42
86.833
60.741
33.543
1.000
27.78

ATOM
3954
CD2
LEU C
42
85.933
62.040
31.654
1.000
18.12

ATOM
3955
C
LEU C
42
89.904
63.797
31.016
1.000
27.41

ATOM
3956
O
LEU C
42
91.117
63.609
31.095
1.000
24.79

ATOM
3957
N
PRO C
43
89.386
65.018
31.082
1.000
30.98

ATOM
3958
CD
PRO C
43
87.971
65.382
30.912
1.000
30.13

ATOM
3959
CA
PRO C
43
90.239
66.179
31.336
1.000
29.06

ATOM
3960
CB
PRO C
43
89.245
67.330
31.472
1.000
28.41

ATOM
3961
CG
PRO C
43
88.035
66.874
30.736
1.000
31.21

ATOM
3962
C
PRO C
43
91.032
66.032
32.629
1.000
33.60

ATOM
3963
O
PRO C
43
92.161
66.519
32.738
1.000
37.33

ATOM
3964
N
ASN C
44
90.481
65.352
33.627
1.000
30.55

ATOM
3965
CA
ASN C
44
91.177
65.227
34.903
1.000
40.13

ATOM
3966
CB
ASN C
44
90.175
64.806
35.992
1.000
50.07

ATOM
3967
CG
ASN C
44
89.303
63.658
35.506
1.000
55.50

ATOM
3968
OD1
ASN C
44
88.190
63.885
35.027
1.000
70.86

ATOM
3969
ND2
ASN C
44
89.810
62.439
35.615
1.000
60.21

ATOM
3970
C
ASN C
44
92.324
64.230
34.858
1.000
40.20

ATOM
3971
O
ASN C
44
93.177
64.187
35.751
1.000
41.19

ATOM
3972
N
SER C
45
92.372
63.388
33.824
1.000
35.46

ATOM
3973
CA
SER C
45
93.457
62.399
33.795
1.000
31.90

ATOM
3974
CB
SER C
45
93.128
61.324
32.766
1.000
32.38

ATOM
3975
OG
SER C
45
93.103
61.854
31.450
1.000
28.70

ATOM
3976
CB
SER C
45
94.769
63.103
33.486
1.000
38.08

ATOM
3977
O
SER C
45
94.780
64.329
33.327
1.000
65.11

ATOM
3978
N
GLY C
46
95.879
62.387
33.388
1.000
35.97

ATOM
3979
CA
GLY C
46
97.111
63.008
32.913
1.000
32.68

ATOM
3980
C
GLY C
46
97.340
62.706
31.442
1.000
31.30

ATOM
3981
O
GLY C
46
98.450
62.427
30.976
1.000
31.52

ATOM
3982
N
GLY C
47
96.277
62.742
30.636
1.000
29.98

ATOM
3983
CA
GLY C
47
96.481
62.416
29.226
1.000
29.97

ATOM
3984
C
GLY C
47
97.432
63.390
28.553
1.000
33.91

ATOM
3985
O
GLY C
47
98.246
62.999
27.713
1.000
33.43

ATOM
3986
N
GLU C
48
97.323
64.665
28.921
1.000
32.08

ATOM
3987
CA
GLU C
48
98.109
65.710
28.283
1.000
31.51

ATOM
3988
CB
GLU C
48
97.724
67.092
28.829
1.000
40.11

ATOM
3989
CG
GLU C
48
98.026
68.195
27.818
1.000
49.80

ATOM
3990
CD
GLU C
48
97.555
67.869
26.411
1.000
59.15

ATOM
3991
OE1
GLU C
48
98.394
67.471
25.570
1.000
67.05

ATOM
3992
OE2
GLU C
48
96.346
68.010
26.125
1.000
70.70

ATOM
3993
C
GLU C
48
99.594
65.470
28.468
1.000
30.68

ATOM
3994
O
GLU C
48
100.397
65.536
27.540
1.000
35.10

ATOM
3995
N
ALA C
49
99.972
65.167
29.703
1.000
32.08

ATOM
3996
CA
ALA C
49
101.347
64.793
29.995
1.000
31.11

ATOM
3997
CB
ALA C
49
101.531
64.660
31.508
1.000
30.63

ATOM
3998
C
ALA C
49
101.746
63.503
29.298
1.000
30.77

ATOM
3999
O
ALA C
49
102.884
63.340
28.838
1.000
29.44

ATOM
4000
N
GLN C
50
100.846
62.522
29.199
1.000
29.35

ATOM
4001
CA
GLN C
50
101.279
61.262
28.586
1.000
26.90

ATOM
4002
CB
GLN C
50
100.269
60.141
28.800
1.000
28.09

ATOM
4003
CG
GLN C
50
99.978
59.785
30.251
1.000
26.70

ATOM
4004
CG
GLN C
50
101.166
59.197
30.982
1.000
32.02

ATOM
4005
OE1
GLN C
50
101.166
59.082
32.210
1.000
48.10

ATOM
4006
NE2
GLN C
50
102.214
58.801
30.271
1.000
22.28

ATOM
4007
C
GLN C
50
101.550
61.478
27.096
1.000
27.62

ATOM
4008
O
GLN C
50
102.562
61.021
26.560
1.000
30.87

ATOM
4009
N
ALA C
51
100.657
62.187
26.428
1.000
27.39

ATOM
4010
CA
ALA C
51
100.819
62.514
25.014
1.000
28.62

ATOM
4011
CB
ALA C
51
99.605
63.287
24.526
1.000
30.43

ATOM
4012
C
ALA C
51
102.098
63.308
24.788
1.000
31.90

ATOM
4013
O
ALA C
51
102.817
63.085
23.815
1.000
32.71

ATOM
4014
N
LY5 C
52
102.390
64.227
25.704
1.000
31.86

ATOM
4015
CA
LY5 C
52
103.638
64.978
25.670
1.000
33.03

ATOM
4016
CB
LY5 C
52
103.662
66.008
26.800
1.000
39.70

ATOM
4017
CG
LY5 C
52
105.039
66.230
27.402
1.000
53.96

ATOM
4018
CG
LY5 C
52
105.132
65.671
28.815
1.000
63.00

ATOM
4019
CE
LYS C
52
106.125
64.528
28.890
1.000
69.80

ATOM
4020
NZ
LYS C
52
105.816
63.592
30.016
1.000
78.05

ATOM
4021
C
LYS C
52
104.831
64.045
25.782
1.000
30.59

ATOM
4022
O
LYS C
52
105.826
64.168
25.065
1.000
32.36

ATOM
4023
N
LYS C
53
104.769
63.067
26.683
1.000
31.21

ATOM
4024
CA
LYS C
53
105.885
62.120
26.736
1.000
35.16

ATOM
4025
CB
LYS C
53
105.802
61.244
27.977
1.000
36.21

ATOM
4026
C
LYS C
53
105.939
61.247
25.489
1.000
36.60

ATOM
4027
O
LYS C
53
107.020
60.790
25.098
1.000
40.19

ATOM
4028
N
LEU C
54
104.815
60.969
24.826
1.000
34.36

ATOM
4029
CA
LEU C
54
104.927
59.996
23.720
1.000
32.18

ATOM
4030
CB
LEU C
54
103.615
59.222
23.560
1.000
27.50

ATOM
4031
CG
LEU C
54
103.407
58.081
24.561
1.000
31.07

ATOM
4032
CD1
LEU C
54
102.020
57.479
24.408
1.000
30.58

ATOM
4033
CD2
LEU C
54
104.489
57.021
24.404
1.000
31.81

ATOM
4034
C
LEU C
54
105.329
60.632
22.401
1.000
31.63

ATOM
4035
O
LEU C
54
105.575
59.930
21.414
1.000
40.05

ATOM
4036
N
GLY C
55
105.421
61.960
22.329
1.000
32.10

ATOM
4037
CA
GLY C
55
105.961
62.577
21.136
1.000
29.95

ATOM
4038
C
GLY C
55
104.947
63.194
20.196
1.000
32.28

ATOM
4039
O
GLY C
55
103.735
63.209
20.418
1.000
28.53

ATOM
4040
N
ASN C
56
105.486
63.720
19.106
1.000
33.04

ATOM
4041
CA
ASN C
56
104.760
64.427
18.070
1.000
38.21

ATOM
4042
CE
ASN C
56
105.748
65.028
17.056
1.000
44.18

ATOM
4043
CG
ASN C
56
106.691
66.006
17.736
1.000
51.34

ATOM
4044
OD1
ASN C
56
107.868
66.077
17.392
1.000
62.21

ATOM
4045
ND2
ASN C
56
106.166
66.740
18.711
1.000
49.99

ATOM
4046
C
ASN C
56
103.766
63.540
17.342
1.000
34.73

ATOM
4047
O
ASN C
56
102.839
64.058
16.713
1.000
36.02

ATOM
4048
N
ASN C
57
103.925
62.221
17.402
1.000
34.43

ATOM
4049
CA
ASN C
57
102.899
61.365
16.805
1.000
33.18

ATOM
4050
CE
ASN C
57
103.541
60.105
16.224
1.000
33.00

ATOM
4051
CG
ASN C
57
104.198
60.389
14.891
1.000
37.58

ATOM
4052
OD1
ASN C
57
105.119
59.679
14.495
1.000
47.98

ATOM
4053
ND2
ASN C
57
103.734
61.415
14.195
1.000
38.58

ATOM
4054
C
ASN C
57
101.813
60.990
17.802
1.000
33.50

ATOM
4055
O
ASN C
57
101.035
60.062
17.575
1.000
27.41

ATOM
4056
N
CYS C
58
101.751
61.711
18.918
1.000
33.01

ATOM
4057
CA
CYS C
58
100.719
61.391
19.908
1.000
31.29

ATOM
4058
CB
CYS C
58
101.301
60.555
21.051
1.000
30.99

ATOM
4059
SG
CYS C
58
100.105
60.157
22.353
1.000
31.90

ATOM
4060
C
CYS C
58
100.076
62.656
20.444
1.000
28.04

ATOM
4061
O
CYS C
58
100.747
63.580
20.893
1.000
32.84

ATOM
4062
N
VAL C
59
98.745
62.722
20.402
1.000
30.91

ATOM
4063
CA
VAL C
59
98.084
63.892
20.974
1.000
29.23

ATOM
4064
CE
VAL C
59
97.517
64.839
19.902
1.000
33.71

ATOM
4065
CG1
VAL C
59
98.594
65.184
18.884
1.000
36.94

ATOM
4066
CG2
VAL C
59
96.317
64.225
19.204
1.000
30.60

ATOM
4067
C
VAL C
59
96.965
63.455
21.921
1.000
30.45

ATOM
4068
O
VAL C
59
96.410
62.366
21.791
1.000
27.62

ATOM
4069
N
PHE C
60
96.666
64.341
22.860
1.000
28.52

ATOM
4070
CA
PHE C
60
95.618
64.140
23.848
1.000
27.23

ATOM
4071
CE
PHE C
60
96.073
64.674
25.208
1.000
27.71

ATOM
4072
CG
PHE C
60
94.982
64.718
26.262
1.000
30.69

ATOM
4073
CD1
PHE C
60
94.254
63.580
26.584
1.000
30.34

ATOM
4074
CD2
PHE C
60
94.691
65.899
26.918
1.000
31.41

ATOM
4075
CE1
PHE C
60
93.260
63.630
27.542
1.000
28.34

ATOM
4076
CE2
PHE C
60
93.700
65.958
27.882
1.000
28.62

ATOM
4077
CZ
PHE C
60
92.979
64.818
28.190
1.000
26.15

ATOM
4078
C
PHE C
60
94.330
64.833
23.424
1.000
31.08

ATOM
4079
O
PHE C
60
94.338
66.017
23.092
1.000
30.75

ATOM
4080
N
ALA C
61
93.213
64.110
23.432
1.000
28.65

ATOM
4081
CA
ALA C
61
91.925
64.751
23.174
1.000
24.00

ATOM
4082
CE
ALA C
61
91.280
64.183
21.925
1.000
29.56

ATOM
4083
C
ALA C
61
91.026
64.567
24.391
1.000
30.42

ATOM
4084
O
ALA C
61
90.471
63.479
24.582
1.000
32.76

ATOM
4085
N
PRO C
62
90.882
65.595
25.217
1.000
30.73

ATOM
4086
CD
PRO C
62
91.412
66.960
25.062
1.000
28.67

ATOM
4087
CA
PRO C
62
90.102
63.446
26.455
1.000
30.54

ATOM
4088
CB
PRO C
62
90.213
66.817
27.120
1.000
29.29

ATOM
4089
CG
PRO C
62
90.544
67.755
26.004
1.000
30.27

ATOM
4090
C
PRO C
62
88.652
65.112
26.132
1.000
30.80

ATOM
4091
O
PRO C
62
87.986
65.781
25.338
1.000
31.42

ATOM
4092
N
ALA C
63
88.135
64.040
26.739
1.000
26.61

ATOM
4093
CA
ALA C
63
86.749
63.698
26.433
1.000
28.05

ATOM
4094
CB
ALA C
63
86.632
63.221
24.990
1.000
24.16

ATOM
4095
C
ALA C
63
86.204
62.638
27.384
1.000
25.50

ATOM
4096
O
ALA C
63
86.947
61.773
27.836
1.000
26.31

ATOM
4097
N
ASP C
64
84.904
62.744
27.626
1.000
24.58

ATOM
4098
CA
ASP C
64
84.120
61.747
28.329
1.000
27.67

ATOM
4099
CB
ASP C
64
83.094
62.409
29.247
1.000
26.67

ATOM
4100
CG
ASP C
64
82.271
61.419
30.050
1.000
28.82

ATOM
4101
OD1
ASP C
64
81.576
61.883
30.984
1.000
33.57

ATOM
4102
OD2
ASP C
64
82.294
60.201
29.768
1.000
25.98

ATOM
4103
C
ASP C
64
83.426
60.859
27.298
1.000
25.59

ATOM
4104
O
ASP C
64
82.706
61.389
26.465
1.000
22.07

ATOM
4105
N
VAL C
65
83.639
59.554
27.361
1.000
26.21

ATOM
4106
CA
VAL C
65
83.080
58.646
26.369
1.000
24.93

ATOM
4107
CB
VAL C
65
83.678
57.227
26.476
1.000
22.24

ATOM
4108
CG1
VAL C
65
85.150
57.2S4
26.085
1.000
16.05

ATOM
4109
CG2
VAL C
65
83.488
56.662
27.874
1.000
22.57

ATOM
4110
C
VAL C
65
81.563
58.544
26.450
1.000
23.05

ATOM
4111
O
VAL C
65
80.938
58.056
25.506
1.000
25.98

ATOM
4112
N
THR C
66
80.938
58.991
27.533
1.000
23.18

ATOM
4113
CA
THR C
66
79.481
58.909
27.619
1.000
24.21

ATOM
4114
CB
THR C
66
78.997
58.858
29.078
1.000
24.93

ATOM
4115
OG1
THR C
66
79.413
60.068
29.732
1.000
26.10

ATOM
4116
CG2
THR C
66
79.633
57.690
29.823
1.000
25.34

ATOM
4117
C
THR C
66
78.803
60.099
26.951
1.000
27.97

ATOM
4118
O
THR C
66
77.575
60.186
26.898
1.000
27.71

ATOM
4119
N
SER C
67
79.585
61.042
26.442
1.000
26.34

ATOM
4120
CA
SER C
67
79.029
62.246
25.852
1.000
25.87

ATOM
4121
CB
SER C
67
79.689
63.482
26.475
1.000
21.35

ATOM
4122
OG
SER C
67
79.591
64.S78
25.568
1.000
28.25

ATOM
4123
CB
SER C
67
79.219
62.277
24.341
1.000
26.46

ATOM
4124
O
SER C
67
80.341
62.168
23.844
1.000
29.77

ATOM
4125
N
GLU C
68
78.127
62.428
23.610
1.000
28.34

ATOM
4126
CA
GLU C
68
78.170
62.504
22.156
1.000
31.50

ATOM
4127
CB
GLU C
68
76.753
62.721
21.616
1.000
32.05

ATOM
4128
CG
GLU C
68
76.684
62.853
20.104
1.000
33.54

ATOM
4129
CD
GLU C
68
75.253
62.873
19.607
1.000
35.59

ATOM
4130
OE1
GLU C
68
74.801
61.833
19.095
1.000
38.18

ATOM
4131
OE2
GLU C
68
74.581
63.915
19.722
1.000
44.21

ATOM
4132
C
GLU C
68
79.089
63.626
21.680
1.000
30.11

ATOM
4133
O
GLU C
68
79.968
63.428
20.844
1.000
28.18

ATOM
4134
N
LYS C
69
78.862
64.808
22.240
1.000
24.11

ATOM
413S
CA
LYS C
69
79.592
66.004
21.867
1.000
28.20

ATOM
4136
CB
LYS C
69
79.047
67.213
22.629
1.000
35.93

ATOM
4137
G
LYS C
69
81.089
65.862
22.105
1.000
27.82

ATOM
4138
O
LYS C
69
81.906
66.263
21.283
1.000
27.44

ATOM
4139
N
ASP C
70
81.475
65.301
23.241
1.000
26.83

ATOM
4140
CA
ASP C
70
82.889
65.152
23.559
1.000
27.75

ATOM
4141
CB
ASP C
70
83.065
64.567
24.965
1.000
30.47

ATOM
4142
CG
ASP C
70
82.823
65.574
26.070
1.000
29.80

ATOM
4143
OD1
ASP C
70
82.332
66.682
25.773
1.000
33.69

ATOM
4144
OD2
ASP C
70
83.117
65.260
27.241
1.000
31.02

ATOM
4145
C
ASP C
70
83.586
64.243
22.561
1.000
24.38

ATOM
4146
O
ASP C
70
84.688
64.503
22.101
1.000
30.02

ATOM
4147
N
VAL C
71
82.952
63.127
22.221
1.000
27.61

ATOM
4148
CA
VAL C
71
83.622
62.165
21.339
1.000
26.47

ATOM
4149
CB
VAL C
71
82.864
60.834
21.378
1.000
27.37

ATOM
4150
CG1
VAL C
71
83.334
59.880
20.294
1.000
24.28

ATOM
4151
CG2
VAL C
71
83.017
60.198
22.758
1.000
25.10

ATOM
4152
C
VAL C
71
83.705
62.753
19.936
1.000
27.36

ATOM
4153
O
VAL C
71
84.659
62.525
19.198
1.000
26.11

ATOM
4154
N
GLN C
72
82.679
63.523
19.578
1.000
25.77

ATOM
4155
CA
GLN C
72
82.674
64.223
18.296
1.000
28.67

ATOM
4156
CB
GLN C
72
81.335
64.952
18.120
1.000
28.15

ATOM
4157
CG
GLN C
72
80.246
63.991
17.643
1.000
29.52

ATOM
4158
CD
GLN C
72
78.888
64.644
17.523
1.000
35.68

ATOM
4159
OE1
GLN C
72
78.543
65.538
18.295
1.000
41.19

ATOM
4160
NE2
GLN C
72
78.111
64.190
16.545
1.000
41.33

ATOM
4161
C
GLN C
72
83.847
65.184
18.218
1.000
26.89

ATOM
4162
O
GLN C
72
84.553
65.280
17.213
1.000
29.43

ATOM
4163
N
THR C
73
84.069
65.908
19.310
1.000
25.94

ATOM
4164
CA
THR C
73
85.192
66.835
19.397
1.000
31.15

ATOM
4165
CB
THR C
73
85.154
67.610
20.731
1.000
36.88

ATOM
4166
OG1
THR C
73
83.936
68.365
20.792
1.000
35.60

ATOM
4167
CG2
THR C
73
86.302
68.600
20.821
1.000
35.19

ATOM
4168
C
THR C
73
86.522
66.114
19.268
1.000
30.75

ATOM
4169
O
THR C
73
87.393
66.469
18.471
1.000
34.22

ATOM
4170
N
ALA C
74
86.708
65.058
20.060
1.000
23.49

ATOM
4171
CA
ALA C
74
87.961
64.318
19.966
1.000
22.59

ATOM
4172
CB
ALA C
74
87.997
63.269
21.072
1.000
29.44

ATOM
4173
C
ALA C
74
88.145
63.676
18.598
1.000
27.87

ATOM
4174
O
ALA C
74
89.250
63.617
18.057
1.000
30.18

ATOM
4175
N
LEU C
75
87.069
63.168
17.991
1.000
25.90

ATOM
4176
CA
LEU C
75
87.221
62.568
16.671
1.000
27.31

ATOM
4177
CB
LEU C
75
85.939
61.827
16.293
1.000
27.10

ATOM
4178
CG
LEU C
75
85.631
60.560
17.089
1.000
26.63

ATOM
4179
CD1
LEU C
75
84.376
59.891
16.544
1.000
25.59

ATOM
4180
CD2
LEU C
75
86.809
59.596
17.085
1.000
21.82

ATOM
4181
C
LEU C
75
87.570
63.625
15.627
1.000
26.22

ATOM
4182
O
LEU C
75
88.385
63.397
14.736
1.000
27.99

ATOM
4183
N
ALA C
76
86.965
64.798
15.733
1.000
27.36

ATOM
4184
CA
ALA C
76
87.272
65.918
14.852
1.000
32.93

ATOM
4185
CB
ALA C
76
86.361
67.096
15.146
1.000
29.31

ATOM
4186
C
ALA C
76
88.739
66.314
14.998
1.000
38.15

ATOM
4187
O
ALA C
76
89.433
66.565
14.012
1.000
34.89

ATOM
4188
N
LEU C
77
89.202
66.352
16.247
1.000
34.23

ATOM
4189
CA
LEU C
77
90.606
66.642
16.522
1.000
29.46

ATOM
4190
CB
LEU C
77
90.848
66.660
18.026
1.000
31.15

ATOM
4191
CG
LEU C
77
92.189
67.144
18.567
1.000
33.61

ATOM
4192
CD1
LEU C
77
92.028
67.757
19.953
1.000
38.66

ATOM
4193
CD2
LEU C
77
93.200
66.013
18.627
1.000
30.53

ATOM
4194
C
LEU C
77
91.499
65.619
15.831
1.000
33.47

ATOM
4195
O
LEU C
77
92.480
65.970
15.166
1.000
37.01

ATOM
4196
N
ALA C
78
91.162
64.338
15.990
1.000
28.96

ATOM
4197
CA
ALA C
78
91.990
63.287
15.407
1.000
31.24

ATOM
4198
CB
ALA C
78
91.465
61.905
15.761
1.000
32.91

ATOM
4199
C
ALA C
78
92.072
63.446
13.891
1.000
31.97

ATOM
4200
O
ALA C
78
93.137
63.329
13.293
1.000
33.08

ATOM
4201
N
LYS C
79
90.923
63.717
13.284
1.000
33.42

ATOM
4202
CA
LYS C
79
90.882
63.915
11.840
1.000
37.37

ATOM
4203
CB
LYS C
79
89.446
64.115
11.390
1.000
32.88

ATOM
4204
G
LYS C
79
91.777
65.092
11.459
1.000
38.05

ATOM
4205
O
LYS C
79
92.616
64.988
10.565
1.000
36.55

ATOM
4206
N
GLY C
80
91.582
66.192
12.174
1.000
36.20

ATOM
4207
CA
GLY C
80
92.298
67.424
11.934
1.000
40.19

ATOM
4208
C
GLY C
80
93.796
67.287
12.069
1.000
42.52

ATOM
4209
O
GLY C
80
94.556
67.884
11.303
1.000
42.68

ATOM
4210
N
LYS C
81
94.261
66.511
13.043
1.000
36.24

ATOM
4211
CA
LYS C
81
95.704
66.397
13.241
1.000
32.94

ATOM
4212
CB
LYS C
81
95.971
66.098
14.717
1.000
38.74

ATOM
4213
CG
LYS C
81
97.400
65.692
15.034
1.000
46.40

ATOM
4214
CD
LYS C
81
98.200
66.940
15.392
1.000
53.53

ATOM
4215
CE
LYS C
81
99.576
66.590
15.931
1.000
57.14

ATOM
4216
NZ
LYS C
81
100.629
67.536
15.458
1.000
61.84

ATOM
4217
G
LYS C
81
96.334
65.319
12.371
1.000
36.28

ATOM
4218
O
LYS C
81
97.445
65.464
11.850
1.000
33.53

ATOM
4219
N
PHE C
82
95.645
64.189
12.197
1.000
31.94

ATOM
4220
CA
PHE C
82
96.300
63.051
11.561
1.000
31.79

ATOM
4221
CB
PHE C
82
96.397
61.876
12.544
1.000
35.42

ATOM
4222
CG
PHE C
82
97.306
62.153
13.737
1.000
33.42

ATOM
4223
CD1
PHE C
82
98.607
62.586
13.571
1.000
29.90

ATOM
4224
CD2
PHE C
82
96.833
61.979
15.027
1.000
30.22

ATOM
4225
CE1
PHE C
82
99.410
62.839
14.665
1.000
34.59

ATOM
4226
CE2
PHE C
82
97.631
62.218
16.128
1.000
30.43

ATOM
4227
CZ
PHE C
82
98.935
62.652
15.953
1.000
32.82

ATOM
4228
C
PHE C
82
95.601
62.606
10.284
1.000
31.97

ATOM
4229
O
PHE C
82
96.012
61.617
9.681
1.000
33.07

ATOM
4230
N
GLY C
83
94.564
63.330
9.882
1.000
36.06

ATOM
4231
CA
GLY C
83
93.905
63.142
8.614
1.000
36.63

ATOM
4232
C
GLY C
83
92.850
62.066
8.554
1.000
38.62

ATOM
4233
O
GLY C
83
91.883
62.213
7.800
1.000
37.81

ATOM
4234
N
ARG C
84
93.009
60.993
9.320
1.000
35.39

ATOM
4235
CA
ARG C
84
92.071
59.880
9.284
1.000
33.37

ATOM
4236
CB
ARG C
84
92.318
58.979
8.067
1.000
28.21

ATOM
4237
CG
ARG C
84
93.743
58.498
7.891
1.000
35.27

ATOM
4238
CG
ARG C
84
93.826
57.071
7.382
1.000
44.86

ATOM
4239
NE
ARG C
84
93.436
56.944
5.991
1.000
51.21

ATOM
4240
CZ
ARG C
84
93.063
55.842
5.359
1.000
56.61

ATOM
4241
NE1
ARG C
84
92.734
55.900
4.069
1.000
64.31

ATOM
4242
NE2
ARG C
84
93.001
54.662
5.962
1.000
35.41

ATOM
4243
C
ARG C
84
92.154
59.048
10.565
1.000
33.24

ATOM
4244
O
ARG C
84
93.077
59.225
11.362
1.000
35.72

ATOM
4245
N
VAL C
85
91.184
58.149
10.735
1.000
26.45

ATOM
4246
CA
VAL C
85
91.223
57.211
11.857
1.000
26.63

ATOM
4247
CB
VAL C
85
90.098
57.408
12.883
1.000
27.68

ATOM
4248
CD1
VAL C
85
90.208
56.362
13.985
1.000
26.03

ATOM
4249
CG2
VAL C
85
90.133
58.808
13.477
1.000
22.07

ATOM
4250
C
VAL C
85
91.178
55.785
11.315
1.000
26.47

ATOM
4251
O
VAL C
85
90.213
55.387
10.671
1.000
27.69

ATOM
4252
N
ASP C
86
92.247
55.035
11.586
1.000
27.28

ATOM
4253
CA
ASP C
86
92.348
53.677
11.069
1.000
25.47

ATOM
4254
CB
ASP C
86
93.793
53.404
10.635
1.000
25.79

ATOM
4255
CG
ASP C
86
94.222
54.369
9.543
1.000
31.04

ATOM
4256
OD1
ASP C
86
95.098
55.218
9.787
1.000
28.57

ATOM
4257
OD2
ASP C
86
93.649
54.261
8.441
1.000
33.34

ATOM
4258
C
ASP C
86
91.927
52.636
12.097
1.000
25.22

ATOM
4259
O
ASP C
86
91.471
51.552
11.752
1.000
22.72

ATOM
4260
N
VAL C
87
92.117
52.981
13.362
1.000
20.25

ATOM
4261
CA
VAL C
87
91.938
52.047
14.462
1.000
18.61

ATOM
4262
CB
VAL C
87
93.281
51.429
14.889
1.000
25.48

ATOM
4263
CG1
VAL C
87
93.126
50.625
16.171
1.000
24.24

ATOM
4264
CG2
VAL C
87
93.843
50.546
13.778
1.000
23.75

ATOM
4265
C
VAL C
87
91.309
52.749
15.661
1.000
23.53

ATOM
4266
O
VAL C
87
91.644
53.890
15.975
1.000
24.10

ATOM
4267
N
ALA C
88
90.396
52.044
16.322
1.000
22.81

ATOM
4268
CA
ALA C
88
89.820
52.530
17.569
1.000
23.04

ATOM
4269
CB
ALA C
88
88.371
52.947
17.406
1.000
19.18

ATOM
4270
C
ALA C
88
89.957
51.435
18.628
1.000
26.02

ATOM
4271
O
ALA C
88
89.630
50.275
18.361
1.000
26.64

ATOM
4272
N
VAL C
89
90.447
51.822
19.803
1.000
22.97

ATOM
4273
CA
VAL C
89
90.595
50.868
20.901
1.000
22.55

ATOM
4274
CB
VAL C
89
92.063
50.633
21.292
1.000
26.76

ATOM
4275
CG1
VAL C
89
92.157
49.550
22.359
1.000
22.89

ATOM
4276
CG2
VAL C
89
92.899
50.249
20.077
1.000
21.77

ATOM
4277
C
VAL C
89
89.831
51.369
22.125
1.000
19.84

ATOM
4278
O
VAL C
89
90.222
52.384
22.700
1.000
21.07

ATOM
4279
N
ASN C
90
88.770
50.668
22.508
1.000
18.37

ATOM
4280
CA
ASN C
90
88.013
51.077
23.694
1.000
24.05

ATOM
4281
CB
ASN C
90
86.560
50.599
23.584
1.000
21.08

ATOM
4282
CG
ASN C
90
85.808
51.301
22.463
1.000
25.47

ATOM
4283
OD1
ASN C
90
85.517
50.707
21.423
1.000
23.05

ATOM
4284
ND2
ASN C
90
85.498
52.578
22.676
1.000
19.99

ATOM
4285
C
ASN C
90
88.659
50.558
24.979
1.000
25.39

ATOM
4286
O
ASN C
90
88.522
49.381
25.323
1.000
22.97

ATOM
4287
N
CYS C
91
89.374
51.440
25.685
1.000
20.95

ATOM
4288
CA
CYS C
91
89.929
51.040
26.976
1.000
24.57

ATOM
4289
CB
CYS C
91
91.455
51.216
26.981
1.000
24.07

ATOM
4290
SG
CYS C
91
92.321
49.981
25.961
1.000
24.05

ATOM
4291
C
CYS C
91
89.304
51.806
28.136
1.000
24.51

ATOM
4292
O
CYS C
91
89.453
51.395
29.290
1.000
23.54

ATOM
4293
N
ALA C
92
88.606
52.908
27.884
1.000
23.37

ATOM
4294
CA
ALA C
92
87.988
53.646
28.991
1.000
27.55

ATOM
4295
CB
ALA C
92
87.234
54.856
28.466
1.000
16.49

ATOM
4296
C
ALA C
92
87.063
52.747
29.808
1.000
30.67

ATOM
4297
O
ALA C
92
86.174
52.068
29.271
1.000
22.30

ATOM
4298
N
GLY C
93
87.263
52.718
31.131
1.000
24.95

ATOM
4299
CA
GLY C
93
86.399
51.890
31.957
1.000
21.65

ATOM
4300
C
GLY C
93
86.592
52.105
33.444
1.000
26.09

ATOM
4301
O
GLY C
93
87.604
52.633
33.902
1.000
21.98

ATOM
4302
N
ILE C
94
85.600
51.700
34.228
1.000
24.72

ATOM
4303
CA
ILE C
94
85.639
51.835
35.682
1.000
20.97

ATOM
4304
CB
ILE C
94
84.789
53.009
36.177
1.000
21.91

ATOM
4305
CG2
ILE C
94
85.395
54.339
35.748
1.000
25.24

ATOM
4306
CD1
ILE C
94
83.326
52.933
35.735
1.000
26.80

ATOM
4307
CD1
THR C
94
82.402
53.851
36.510
1.000
28.94

ATOM
4308
C
ILE C
94
85.121
50.552
36.321
1.000
25.27

ATOM
4309
O
ILE C
94
84.464
49.767
35.639
1.000
20.88

ATOM
4310
N
ALA C
95
85.413
50.354
37.596
1.000
31.52

ATOM
4311
CA
ALA C
95
85.032
49.161
38.336
1.000
31.13

ATOM
4312
CB
ALA C
95
86.266
48.327
38.644
1.000
24.85

ATOM
4313
C
ALA C
95
84.336
49.510
39.642
1.000
29.69

ATOM
4314
O
ALA C
95
84.583
50.576
40.208
1.000
26.96

ATOM
4315
N
VAL C
96
83.483
48.626
40.137
1.000
26.02

ATOM
4316
CA
VAL C
96
82.972
48.747
41.493
1.000
24.18

ATOM
4317
CB
VAL C
96
81.621
49.475
41.630
1.000
34.59

ATOM
4318
CG1
VAL C
96
81.680
50.876
41.043
1.000
51.91

ATOM
4319
CG2
VAL C
96
80.504
48.674
40.977
1.000
37.98

ATOM
4320
C
VAL C
96
82.807
47.349
42.081
1.000
23.92

ATOM
4321
O
VAL C
96
82.559
46.370
41.386
1.000
25.46

ATOM
4322
N
ALA C
97
82.941
47.232
43.398
1.000
22.45

ATOM
4323
CA
ALA C
97
82.609
45.956
44.034
1.000
18.77

ATOM
4324
CB
ALA C
97
83.802
45.389
44.753
1.000
28.21

ATOM
4325
C
ALA C
97
81.424
46.210
44.957
1.000
25.22

ATOM
4326
O
ALA C
97
81.513
47.063
45.845
1.000
29.86

ATOM
4327
N
SER C
98
80.327
45.506
44.731
1.000
23.38

ATOM
4328
CA
SER C
98
79.141
45.722
45.577
1.000
25.77

ATOM
4329
CB
SER C
98
78.519
47.070
45.248
1.000
24.89

ATOM
4330
OG
SER C
98
77.352
47.382
45.971
1.000
22.27

ATOM
4331
CB
SER C
98
78.192
44.551
45.385
1.000
25.87

ATOM
4332
O
SER C
98
77.767
44.267
44.262
1.000
21.71

ATOM
4333
N
LYS C
99
77.878
43.851
46.468
1.000
19.96

ATOM
4334
CA
LYS C
99
76.949
42.736
46.442
1.000
24.20

ATOM
4335
CE
LYS C
99
76.821
42.103
47.829
1.000
25.97

ATOM
4336
CG
LYS C
99
78.029
41.351
48.356
1.000
28.65

ATOM
4337
CD
LYS C
99
77.583
40.149
49.176
1.000
31.25

ATOM
4338
CE
LYS C
99
78.568
39.776
50.268
1.000
38.05

ATOM
4339
NZ
LYS C
99
77.913
38.887
51.278
1.000
51.74

ATOM
4340
C
LYS C
99
75.544
43.156
46.018
1.000
25.56

ATOM
4341
O
LYS C
99
75.089
44.241
46.380
1.000
25.47

ATOM
4342
N
THR C
100
74.855
42.300
45.278
1.000
21.51

ATOM
4343
CA
THR C
100
73.478
42.560
44.866
1.000
17.21

ATOM
4344
CB
THR C
100
72.898
41.354
44.112
1.000
22.90

ATOM
4345
OG1
THR C
100
73.639
41.178
42.892
1.000
24.84

ATOM
4346
CG2
THR C
100
71.440
41.604
43.740
1.000
23.05

ATOM
4347
C
THR C
100
72.596
42.860
46.076
1.000
23.89

ATOM
4348
O
THR C
100
71.833
43.819
46.092
1.000
22.63

ATOM
4349
N
TYR C
101
72.737
42.017
47.093
1.000
23.56

ATOM
4350
CA
TYR C
101
72.063
42.148
48.366
1.000
23.20

ATOM
4351
CB
TYR C
101
70.660
41.516
48.343
1.000
20.29

ATOM
4352
CG
TYR C
101
69.964
41.701
49.688
1.000
25.09

ATOM
4353
CD1
TYR C
101
69.746
40.620
50.525
1.000
25.63

ATOM
4354
CE1
TYR C
101
69.122
40.784
51.744
1.000
29.97

ATOM
4355
CD2
TYR C
101
69.550
42.958
50.107
1.000
27.65

ATOM
4356
CE2
TYR C
101
68.920
43.133
51.330
1.000
31.37

ATOM
4357
CZ
TYR C
101
68.711
42.037
52.143
1.000
32.86

ATOM
4358
OH
TYR C
101
68.089
42.179
53.362
1.000
34.12

ATOM
4359
C
TYR C
101
72.892
41.502
49.476
1.000
27.30

ATOM
4360
O
TYR C
101
73.412
40.404
49.274
1.000
25.60

ATOM
4361
N
ASN C
102
73.006
42.164
50.622
1.000
29.43

ATOM
4362
CA
ASN C
102
73.716
41.595
51.770
1.000
28.87

ATOM
4363
CB
ASN C
102
74.869
42.506
52.184
1.000
30.71

ATOM
4364
CG
ASN C
102
75.751
41.924
53.273
1.000
34.19

ATOM
4365
OD1
ASN C
102
75.292
41.152
54.113
1.000
33.00

ATOM
4366
ND2
ASN C
102
77.031
42.283
53.289
1.000
23.49

ATOM
4367
C
ASN C
102
72.762
41.379
52.941
1.000
24.06

ATOM
4368
O
ASN C
102
72.368
42.358
53.583
1.000
28.89

ATOM
4369
N
LEU C
103
72.388
40.138
53.225
1.000
24.08

ATOM
4370
CA
LEU C
103
71.398
39.899
54.278
1.000
30.00

ATOM
4371
CB
LEU C
103
70.947
38.441
54.299
1.000
28.45

ATOM
4372
CG
LEU C
103
69.917
38.042
55.361
1.000
32.39

ATOM
4373
CD1
LEU C
103
68.610
38.804
55.196
1.000
33.98

ATOM
4374
CD2
LEU C
103
69.651
36.543
55.326
1.000
25.45

ATOM
4375
C
LEU C
103
71.933
40.322
55.646
1.000
35.26

ATOM
4376
O
LEU C
103
71.299
41.113
56.348
1.000
38.65

ATOM
4377
N
LYS C
104
73.090
39.802
56.024
1.000
39.01

ATOM
4378
CA
LYS C
104
73.708
40.104
57.306
1.000
41.66

ATOM
4379
CB
LYS C
104
75.103
39.498
57.386
1.000
47.98

ATOM
4380
C
LYS C
104
73.770
41.607
57.562
1.000
38.16

ATOM
4381
O
LYS C
104
73.509
42.058
58.678
1.000
44.94

ATOM
4382
N
LYS C
105
74.103
42.377
56.534
1.000
32.61

ATOM
4383
CA
LYS C
105
74.220
43.824
56.663
1.000
33.58

ATOM
4384
CB
LYS C
105
7S.308
44.376
55.741
1.000
40.90

ATOM
4385
CG
LYS C
105
76.696
44.469
56.339
1.00O
51.19

ATOM
4386
CD
LYS C
105
77.585
45.413
55.548
1.000
62.16

ATOM
4387
CE
LYS C
105
76.859
46.019
54.356
1.000
69.04

ATOM
4388
NZ
LYS C
105
77.114
47.481
54.221
1.000
70.89

ATOM
4389
C
LYS C
105
72.908
44.517
56.323
1.000
30.56

ATOM
4390
O
LYS C
105
72.767
45.726
56.514
1.000
30.90

ATOM
4391
N
GLY C
106
71.950
43.761
55.790
1.000
26.43

ATOM
4392
CA
GLY C
106
70.712
44.375
55.311
1.000
27.03

ATOM
4393
C
GLY C
106
71.008
45.502
54.337
1.000
27.69

ATOM
4394
O
GLY C
106
70.444
46.595
54.418
1.000
32.58

ATOM
4395
N
GLN C
107
71.925
45.261
53.399
1.000
29.25

ATOM
4396
CA
GLN C
107
72.291
46.325
52.464
1.000
29.86

ATOM
4397
CB
GLN C
107
73.738
46.748
52.653
1.000
28.35

ATOM
4398
C
GLN C
107
72.049
45.893
51.016
1.000
29.83

ATOM
4399
O
GLN C
107
72.332
44.747
50.660
1.000
25.04

ATOM
4400
N
THR C
108
71.525
46.830
50.239
1.000
27.41

ATOM
4401
CA
THR C
108
71.163
46.631
48.847
1.000
28.51

ATOM
4402
CB
THR C
108
69.712
47.082
48.588
1.000
26.57

ATOM
4403
OD1
THR C
108
68.811
46.331
49.402
1.000
23.48

ATOM
4404
CG2
THR C
108
69.313
46.770
47.151
1.000
26.36

ATOM
4405
C
THR C
108
72.078
47.398
47.899
1.000
22.28

ATOM
4406
O
THR C
108
72.327
48.582
48.122
1.000
21.53

ATOM
4407
N
HIS C
109
72.564
46.729
46.859
1.000
25.01

ATOM
4408
CA
HIS C
109
73.295
47.402
45.783
1.000
22.12

ATOM
4409
CB
HIS C
109
73.530
46.456
44.612
1.000
23.18

ATOM
4410
CG
HIS C
109
74.490
46.905
43.558
1.000
21.71

ATOM
4411
CD2
HIS C
109
75.506
46.241
42.955
1.000
22.92

ATOM
4412
ND1
HIS C
109
74.482
48.155
42.986
1.000
20.66

ATOM
4413
CE1
HIS C
109
75.447
48.248
42.084
1.000
21.46

ATOM
4414
NE2
HIS C
109
76.089
47.098
42.044
1.000
21.40

ATOM
4415
C
HIS C
109
72.508
48.624
45.334
1.000
20.47

ATOM
4416
O
HIS C
109
71.301
48.553
45.084
1.000
25.75

ATOM
4417
N
THR C
110
73.153
49.786
45.235
1.000
20.46

ATOM
4418
CA
THR C
110
72.348
50.934
44.829
1.000
21.09

ATOM
4419
CB
THR C
110
72.993
52.284
45.189
1.000
22.39

ATOM
4420
OG1
THR C
110
74.177
52.416
44.393
1.000
24.12

ATOM
4421
CG2
THR C
110
73.375
52.322
46.661
1.000
20.02

ATOM
4422
C
THR C
110
72.118
50.930
43.325
1.000
24.72

ATOM
4423
O
THR C
110
72.919
50.413
42.558
1.000
29.03

ATOM
4424
N
LEU C
111
71.002
51.524
42.921
1.000
25.48

ATOM
4425
CA
LEU C
111
70.718
51.623
41.495
1.000
24.76

ATOM
4426
CB
LEU C
111
69.317
52.216
41.309
1.000
25.46

ATOM
4427
CG
LEU C
111
68.749
52.087
39.890
1.000
25.35

ATOM
4428
CD1
LEU C
111
68.710
50.626
39.469
1.000
22.50

ATOM
4429
CD2
LEU C
111
67.374
52.735
39.816
1.000
27.56

ATOM
4430
C
LEU C
111
71.772
52.457
40.786
1.000
25.44

ATOM
4431
O
LEU C
111
72.270
52.101
39.719
1.000
23.31

ATOM
4432
N
GLU C
112
72.163
53.605
41.348
1.000
25.18

ATOM
4433
CA
GLU C
112
73.093
54.443
40.590
1.000
31.68

ATOM
4434
CB
GLU C
112
73.186
55.837
41.215
1.000
41.48

ATOM
4435
CG
GLU C
112
72.266
56.860
40.577
1.000
58.29

ATOM
4436
CD
GLU C
112
71.704
56.498
39.220
1.000
62.69

ATOM
4437
OE1
GLU C
112
72.217
57.028
38.204
1.000
56.30

ATOM
4438
OE2
GLU C
112
70.738
55.700
39.142
1.000
39.60

ATOM
4439
C
GLU C
112
74.479
53.821
40.454
1.000
29.28

ATOM
4440
O
GLU C
112
75.175
54.140
39.479
1.000
21.19

ATOM
4441
N
ASP C
113
74.898
52.960
41.375
1.000
26.57

ATOM
4442
CA
ASP C
113
76.177
52.263
41.200
1.000
24.79

ATOM
4443
CB
ASP C
113
76.544
51.445
42.428
1.000
24.71

ATOM
4444
CG
ASP C
113
77.406
52.158
43.439
1.000
26.72

ATOM
4445
OD1
ASP C
113
78.053
53.164
43.098
1.000
25.92

ATOM
4446
OD2
ASP C
113
77.449
51.724
44.608
1.000
30.58

ATOM
4447
C
ASP C
113
76.101
51.338
39.986
1.000
21.47

ATOM
4448
O
ASP C
113
77.048
51.172
39.224
1.000
26.34

ATOM
4449
N
PHE C
114
74.942
50.711
39.794
1.000
19.80

ATOM
4450
CA
PHE C
114
74.759
49.855
38.624
1.000
21.89

ATOM
4451
CB
PHE C
114
73.493
49.015
38.774
1.000
21.43

ATOM
4452
CG
PHE C
114
73.344
47.960
37.684
1.000
22.40

ATOM
4453
CD1
PHE C
114
72.610
48.247
36.541
1.000
22.43

ATOM
4454
CD2
PHE C
114
73.933
46.719
37.817
1.000
18.60

ATOM
4455
CE1
PHE C
114
72.485
47.298
35.551
1.000
21.11

ATOM
4456
CE2
PHE C
114
73.803
45.764
36.826
1.000
23.20

ATOM
4457
CZ
PHE C
114
73.068
46.053
35.693
1.000
16.97

ATOM
4458
C
PHE C
114
74.702
50.692
37.346
1.000
22.83

ATOM
4459
O
PHE C
114
75.297
50.331
36.333
1.000
25.15

ATOM
4460
N
GLN C
115
73.991
51.808
37.403
1.000
21.70

ATOM
4461
CA
GLN C
115
73.818
52.709
36.281
1.000
26.11

ATOM
4462
CB
GLN C
115
72.795
53.799
36.630
1.000
26.45

ATOM
4463
CG
GLN C
115
72.395
54.654
35.434
1.000
30.61

ATOM
4464
CD
GLN C
115
71.550
53.875
34.441
1.000
33.27

ATOM
4465
OE1
GLN C
115
70.493
53.348
34.790
1.000
33.80

ATOM
4466
NE2
GLN C
115
72.024
53.798
33.202
1.000
30.59

ATOM
4467
C
GLN C
115
75.117
53.375
35.839
1.000
26.35

ATOM
4468
O
GLN C
115
75.372
53.460
34.632
1.000
28.81

ATOM
4469
N
ARG C
116
75.923
53.849
36.784
1.000
19.66

ATOM
4470
CA
ARG C
116
77.158
54.545
36.427
1.000
21.15

ATOM
4471
CB
ARG C
116
77.751
55.189
37.675
1.000
26.20

ATOM
4472
C
ARG C
116
78.179
53.619
35.783
1.000
22.02

ATOM
4473
O
ARG C
116
78.970
53.981
34.907
1.000
24.22

ATOM
4474
N
VAL C
117
78.204
52.359
36.213
1.000
21.35

ATOM
4475
CA
VAL C
117
79.119
51.397
35.597
1.000
20.76

ATOM
4476
CB
VAL C
117
79.266
50.152
36.481
1.000
21.27

ATOM
4477
CG1
VAL C
117
79.904
49.002
35.725
1.000
19.89

ATOM
4478
CG2
VAL C
117
80.101
50.504
37.711
1.000
26.91

ATOM
4479
C
VAL C
117
78.649
51.028
34.196
1.000
21.72

ATOM
4480
O
VAL C
117
79.461
50.885
33.281
1.000
27.53

ATOM
4481
N
LEU C
118
77.347
50.875
34.001
1.000
21.28

ATOM
4482
CA
LEU C
118
76.767
50.593
32.699
1.000
22.07

ATOM
4483
CB
LEU C
118
75.257
50.445
32.813
1.000
22.40

ATOM
4484
CG
LEU C
118
74.619
49.086
33.041
1.000
34.91

ATOM
4485
CD1
LEU C
118
73.187
49.096
32.499
1.000
33.59

ATOM
4486
CD2
LEU C
118
75.415
47.952
32.414
1.000
37.45

ATOM
4487
C
LEU C
118
77.062
51.715
31.693
1.000
25.15

ATOM
4488
O
LEU C
118
77.454
51.474
30.554
1.000
22.17

ATOM
4489
N
ASP C
119
76.840
52.945
32.142
1.000
25.17

ATOM
4490
CA
ASP C
119
77.042
54.136
31.331
1.000
23.07

ATOM
4491
CB
ASP C
119
76.673
55.397
32.119
1.000
21.46

ATOM
4492
CG
ASP C
119
75.171
55.573
32.250
1.000
24.19

ATOM
4493
OD1
ASP C
119
74.732
56.626
32.757
1.000
35.16

ATOM
4494
OD2
ASP C
119
74.428
54.649
31.852
1.000
26.39

ATOM
4495
C
ASP C
119
78.473
54.263
30.817
1.000
30.13

ATOM
4496
O
ASP C
119
78.692
54.440
29.608
1.000
22.50

ATOM
4497
N
VAL C
120
79.466
54.183
31.709
1.000
24.43

ATOM
4498
CA
VAL C
120
80.837
54.384
31.223
1.000
22.41

ATOM
4499
CB
VAL C
120
81.829
54.644
32.372
1.000
23.24

ATOM
4500
CG1
VAL C
120
83.263
54.680
31.870
1.000
22.29

ATOM
4501
CG2
VAL C
120
81.508
55.957
33.077
1.000
24.06

ATOM
4502
C
VAL C
120
81.316
53.194
30.406
1.000
17.91

ATOM
4503
O
VAL C
120
81.848
53.385
29.305
1.000
26.22

ATOM
4504
N
ASN C
121
81.146
51.974
30.908
1.000
13.92

ATOM
4505
CA
ASN C
121
81.797
50.821
30.295
1.000
18.63

ATOM
4506
CB
ASN C
121
81.877
49.626
31.250
1.000
20.72

ATOM
4507
CG
ASN C
121
82.729
49.879
32.474
1.000
24.64

ATOM
4508
OD1
ASN C
121
83.339
50.939
32.605
1.000
23.75

ATOM
4509
ND2
ASN C
121
82.776
48.902
33.373
1.000
21.68

ATOM
4510
C
ASN C
121
81.108
50.345
29.023
1.000
19.66

ATOM
4511
O
ASN C
121
81.782
49.961
28.060
1.000
22.39

ATOM
4512
N
LEU C
122
79.784
50.343
29.034
1.000
21.72

ATOM
4513
CA
LEU C
122
79.019
49.750
27.940
1.000
18.43

ATOM
4514
CE
LEU C
122
77.882
48.904
28.508
1.000
17.19

ATOM
4515
CG
LEU C
122
76.918
48.259
27.511
1.000
21.34

ATOM
4516
CD1
LEU C
122
77.683
47.507
26.435
1.000
18.33

ATOM
4517
CD2
LEU C
122
75.938
47.348
28.237
1.000
16.15

ATOM
4518
C
LEU C
122
78.500
50.817
26.990
1.000
21.38

ATOM
4519
O
LEU C
122
78.807
50.810
25.796
1.000
28.84

ATOM
4520
N
MET C
123
77.706
51.739
27.510
1.000
19.47

ATOM
4521
CA
MET C
123
77.180
52.834
26.709
1.000
21.09

ATOM
4522
CE
MET C
123
76.191
53.662
27.528
1.000
23.37

ATOM
4523
CG
MET C
123
75.557
54.811
26.761
1.000
25.26

ATOM
4524
SD
MET C
123
76.474
56.352
26.889
1.000
27.76

ATOM
4525
CE
MET C
123
76.109
56.826
28.585
1.000
24.30

ATOM
4526
C
MET C
123
78.311
53.710
26.186
1.000
26.12

ATOM
4527
O
MET C
123
78.294
54.131
25.026
1.000
27.11

ATOM
4528
N
GLY C
124
79.294
53.998
27.025
1.000
23.16

ATOM
4529
CA
GLY C
124
80.457
54.773
26.620
1.000
24.75

ATOM
4530
C
GLY C
124
81.211
54.112
25.479
1.000
26.45

ATOM
4531
O
GLY C
124
81.589
54.753
24.500
1.000
23.18

ATOM
4532
N
THR C
125
81.440
52.807
25.577
1.000
22.27

ATOM
4533
CA
THR C
125
82.099
52.096
24.480
1.000
20.93

ATOM
4534
CE
THR C
125
82.436
50.653
24.889
1.000
21.42

ATOM
4535
OG1
THR C
125
83.661
50.663
25.648
1.000
21.32

ATOM
4536
CG2
THR C
125
82.677
49.761
23.677
1.000
21.31

ATOM
4537
C
THR C
125
81.232
52.132
23.227
1.000
22.04

ATOM
4538
O
THR C
125
81.731
52.449
22.141
1.000
22.04

ATOM
4539
N
PHE C
126
79.938
51.849
23.321
1.000
22.32

ATOM
4540
CA
PHE C
126
79.086
51.916
22.134
1.000
23.46

ATOM
4541
CB
PHE C
126
77.644
51.478
22.431
1.000
17.51

ATOM
4542
CG
PHE C
126
76.778
51.434
21.177
1.000
26.11

ATOM
4543
CD1
PHE C
126
76.857
50.374
20.293
1.000
22.75

ATOM
4544
CD2
PHE C
126
75.888
52.458
20.889
1.000
28.36

ATOM
4545
CE1
PHE C
126
76.083
50.328
19.149
1.000
17.53

ATOM
4546
CE2
PHE C
126
75.108
52.433
19.749
1.000
23.72

ATOM
4547
CE
PHE C
126
75.205
51.364
18.876
1.000
21.00

ATOM
4548
C
PHE C
126
79.066
53.322
21.541
1.000
23.15

ATOM
4549
O
PHE C
126
79.013
53.494
20.317
1.000
21.11

ATOM
4550
N
ASN C
127
79.106
54.356
22.373
1.000
18.49

ATOM
4551
CA
ASN C
127
79.088
55.727
21.869
1.000
23.03

ATOM
4552
CE
ASN C
127
79.101
56.743
23.008
1.000
21.45

ATOM
4553
CG
ASN C
127
78.811
58.157
22.556
1.000
25.25

ATOM
4554
OD1
ASN C
127
78.014
58.378
21.642
1.000
29.13

ATOM
4555
ND2
ASN C
127
79.444
59.142
23.178
1.000
21.91

ATOM
4556
C
ASN C
127
80.275
55.975
20.937
1.000
25.87

ATOM
4557
O
ASN C
127
80.132
56.542
19.855
1.000
28.62

ATOM
4558
N
VAL C
128
81.462
55.550
21.358
1.000
24.08

ATOM
4559
CA
VAL C
128
82.651
55.701
20.526
1.000
21.95

ATOM
4560
CE
VAL C
128
83.914
55.317
21.317
1.000
26.51

ATOM
4561
CD1
VAL C
128
85.134
55.394
20.406
1.000
22.25

ATOM
4562
CG2
VAL C
128
84.064
56.225
22.528
1.000
22.93

ATOM
4563
C
VAL C
128
82.555
54.854
19.264
1.000
23.58

ATOM
4564
O
VAL C
128
82.918
55.250
18.153
1.000
25.79

ATOM
4565
N
ILE C
129
82.028
53.643
19.408
1.000
20.57

ATOM
4566
CA
ILE C
129
81.911
52.748
18.263
1.000
20.61

ATOM
4567
CB
ILE C
129
81.347
51.377
18.686
1.000
19.62

ATOM
4568
CG2
ILE C
129
80.846
50.638
17.458
1.000
17.68

ATOM
4569
CG1
ILE C
129
82.345
50.542
19.491
1.000
18.07

ATOM
4570
CD1
ILE C
129
81.885
49.185
19.946
1.000
14.79

ATOM
4571
C
ILE C
129
81.046
53.324
17.151
1.000
25.58

ATOM
4572
O
ILE C
129
81.456
53.326
15.982
1.000
24.80

ATOM
4573
N
ARG C
130
79.849
53.789
17.487
1.000
22.22

ATOM
4574
CA
ARG C
130
78.908
54.263
16.478
1.000
22.61

ATOM
4575
CB
ARG C
130
77.534
54.507
17.124
1.000
24.83

ATOM
4576
CG
ARG C
130
77.407
55.858
17.785
1.000
20.11

ATOM
4577
CG
ARG C
130
76.273
56.001
18.789
1.000
22.05

ATOM
4578
NE
ARG C
130
76.439
57.318
19.415
1.000
27.62

ATOM
4579
CZ
ARG C
130
75.884
58.453
19.041
1.000
24.47

ATOM
4580
NE1
ARG C
130
76.165
59.557
19.720
1.000
23.28

ATOM
4581
NE2
ARG C
130
75.054
58.521
18.014
1.000
20.98

ATOM
4582
C
ARG C
130
79.421
55.523
15.796
1.000
27.40

ATOM
4583
O
ARG C
130
79.228
55.740
14.594
1.000
23.73

ATOM
4584
N
LEU C
131
80.103
56.372
16.567
1.000
23.20

ATOM
4585
CA
LEU C
131
80.646
57.606
16.013
1.000
26.88

ATOM
4586
CB
LEU C
131
80.905
58.629
17.127
1.000
23.30

ATOM
4587
CG
LEU C
131
79.654
59.282
17.728
1.000
28.73

ATOM
4588
CD1
LEU C
131
79.998
60.155
18.926
1.000
20.58

ATOM
4589
CD2
LEU C
131
78.925
60.105
16.673
1.000
33.54

ATOM
4590
C
LEU C
131
81.917
57.344
15.213
1.000
29.94

ATOM
4591
O
LEU C
131
82.072
57.881
14.115
1.000
25.36

ATOM
4592
N
VAL C
132
82.834
56.531
15.740
1.000
22.06

ATOM
4593
CA
VAL C
132
84.060
56.279
14.987
1.000
19.86

ATOM
4594
CB
VAL C
132
85.144
55.586
15.823
1.000
20.83

ATOM
4595
CG1
VAL C
132
84.951
54.087
15.879
1.000
20.03

ATOM
4596
CG2
VAL C
132
86.517
55.930
15.238
1.000
23.88

ATOM
4597
C
VAL C
132
83.760
55.452
13.735
1.000
22.63

ATOM
4598
O
VAL C
132
84.474
55.583
12.735
1.000
26.93

ATOM
4599
N
ALA C
133
82.711
54.633
13.750
1.000
16.38

ATOM
4600
CA
ALA C
133
82.362
53.861
12.560
1.000
22.93

ATOM
4601
CB
ALA C
133
81.248
52.865
12.849
1.000
23.49

ATOM
4602
C
ALA C
133
81.967
54.783
11.408
1.000
25.68

ATOM
4603
O
ALA C
133
82.304
54.533
10.248
1.000
25.79

ATOM
4604
N
GLY C
134
81.258
55.870
11.697
1.000
26.27

ATOM
4605
CA
GLY C
134
80.967
56.883
10.693
1.000
29.86

ATOM
4606
C
GLY C
134
82.235
57.527
10.168
1.000
35.29

ATOM
4607
O
GLY C
134
82.350
57.894
8.995
1.000
32.90

ATOM
4608
N
GLU C
135
83.254
57.680
11.022
1.000
33.22

ATOM
4609
CA
GLU C
135
84.500
58.252
10.509
1.000
27.55

ATOM
4610
CE
GLU C
135
85.392
58.749
11.645
1.000
27.14

ATOM
4611
CG
GLU C
135
84.779
59.910
12.415
1.000
31.58

ATOM
4612
CD
GLU C
135
84.524
61.133
11.549
1.000
34.25

ATOM
4613
OE1
GLU C
135
83.509
61.813
11.805
1.000
48.00

ATOM
4614
OE2
GLU C
135
85.313
61.402
10.623
1.000
44.39

ATOM
4615
C
GLU C
135
85.249
57.245
9.654
1.000
27.65

ATOM
4616
O
GLU C
135
85.776
57.596
8.595
1.000
31.08

ATOM
4617
N
MET C
136
85.293
55.991
10.094
1.000
20.13

ATOM
4618
CA
MET C
136
85.986
55.000
9.275
1.000
22.80

ATOM
4619
CB
MET C
136
86.163
53.693
10.043
1.000
24.93

ATOM
4620
CG
MET C
136
87.064
53.805
11.266
1.000
26.00

ATOM
4621
SD
MET C
136
87.004
52.294
12.257
1.000
26.60

ATOM
4622
CE
MET C
136
88.201
52.656
13.540
1.000
25.70

ATOM
4623
C
MET C
136
85.225
54.755
7.978
1.000
21.26

ATOM
4624
O
MET C
136
85.756
54.286
6.973
1.000
26.59

ATOM
4625
N
GLY C
137
83.936
55.076
7.981
1.000
26.75

ATOM
4626
CA
GLY C
137
83.143
54.888
6.766
1.000
31.17

ATOM
4627
C
GLY C
137
83.660
55.747
5.622
1.000
33.76

ATOM
4628
O
GLY C
137
83.484
35.416
4.447
1.000
32.88

ATOM
4629
N
GLN C
138
84.303
56.859
5.974
1.000
27.37

ATOM
4630
CA
GLN C
138
84.791
57.797
4.973
1.000
28.73

ATOM
4631
CE
GLN C
138
84.859
59.194
5.578
1.000
32.69

ATOM
4632
C
GLN C
138
86.141
57.384
4.411
1.000
32.99

ATOM
4633
O
GLN C
138
86.671
58.018
3.497
1.000
36.53

ATOM
4634
N
ASN C
139
86.745
56.324
4.942
1.000
31.67

ATOM
4635
CA
ASN C
139
88.056
55.934
4.429
1.000
30.49

ATOM
4636
CE
ASN C
139
88.847
55.085
5.419
1.000
31.45

ATOM
4637
CG
ASN C
139
89.086
55.684
6.785
1.000
34.68

ATOM
4638
OD1
ASN C
139
89.055
56.894
7.000
1.000
33.74

ATOM
4639
ND2
ASN C
139
89.334
54.812
7.762
1.000
28.28

ATOM
4640
C
ASN C
139
87.884
55.142
3.136
1.000
30.33

ATOM
4641
O
ASN C
139
86.907
54.415
2.977
1.000
31.18

ATOM
4642
N
GLU C
140
88.838
55.260
2.219
1.000
32.41

ATOM
4643
CA
GLU C
140
88.838
54.364
1.063
1.000
33.47

ATOM
4644
CE
GLU C
140
89.741
54.885
−0.038
1.000
36.95

ATOM
4645
C
GLU C
140
89.274
52.976
1.528
1.000
33.19

ATOM
4646
O
GLU C
140
90.249
52.875
2.283
1.000
30.54

ATOM
4647
N
PRO C
141
88.575
51.929
1.111
1.000
30.85

ATOM
4648
CD
PRO C
141
87.385
51.919
0.252
1.000
28.75

ATOM
4649
CA
PRO C
141
88.970
50.578
1.528
1.000
31.41

ATOM
4650
CB
PRO C
141
87.893
49.670
0.942
1.000
31.98

ATOM
4651
CG
PRO C
141
86.781
50.569
0.534
1.000
33.28

ATOM
4652
C
PRO C
141
90.330
50.204
0.948
1.000
37.57

ATOM
4653
O
PRO C
141
90.625
50.524
−0.205
1.000
39.30

ATOM
4654
N
ASP C
142
91.151
49.522
1.745
1.000
32.93

ATOM
4655
CA
ASP C
142
92.444
49.095
1.212
1.000
31.17

ATOM
4656
CB
ASP C
142
93.376
48.639
2.322
1.000
32.74

ATOM
4657
CG
ASP C
142
92.888
47.444
3.108
1.000
34.79

ATOM
4658
OD1
ASP C
142
91.946
46.748
2.677
1.000
23.82

ATOM
4659
OD2
ASP C
142
93.479
47.192
4.185
1.000
36.00

ATOM
4660
C
ASP C
142
92.223
47.986
0.182
1.000
35.49

ATOM
4661
O
ASP C
142
91.079
47.730
−0.205
1.000
28.21

ATOM
4662
N
GLN C
143
93.321
47.372
−0.234
1.000
34.68

ATOM
4663
CA
GLN C
143
93.292
46.328
−1.248
1.000
38.05

ATOM
4664
CE
GLN C
143
94.716
45.927
−1.617
1.000
37.56

ATOM
4665
C
GLN C
143
92.502
45.115
−0.776
1.000
39.79

ATOM
4666
O
GLN C
143
92.057
44.304
−1.596
1.000
39.29

ATOM
4667
N
GLY C
144
92.336
44.982
0.539
1.000
34.34

ATOM
4668
CA
GLY C
144
91.609
43.857
1.105
1.000
30.14

ATOM
4669
C
GLY C
144
90.163
44.224
1.396
1.000
30.98

ATOM
4670
O
GLY C
144
89.417
43.410
1.939
1.000
33.23

ATOM
4671
N
GLY C
145
89.767
45.439
1.035
1.000
28.94

ATOM
4672
CA
GLY C
145
88.407
45.893
1.253
1.000
24.37

ATOM
4673
C
GLY C
145
88.236
46.543
2.603
1.000
26.97

ATOM
4674
O
GLY C
145
87.132
46.942
2.981
1.000
25.24

ATOM
4675
N
GLN C
146
89.310
46.676
3.378
1.000
28.50

ATOM
4676
CA
GLN C
146
89.168
47.169
4.746
1.000
27.93

ATOM
4677
CE
GLN C
146
90.248
46.534
5.635
1.000
27.83

ATOM
4678
CG
GLN C
146
89.994
46.739
7.126
1.000
30.00

ATOM
4679
CD
GLN C
146
90.976
45.937
7.966
1.000
29.61

ATOM
4680
OE1
GLN C
146
90.812
44.731
8.172
1.000
27.76

ATOM
4681
NE2
GLN C
146
92.007
46.631
8.437
1.000
24.62

ATOM
4682
C
GLN C
146
89.249
48.685
4.869
1.000
27.94

ATOM
4683
O
GLN C
146
90.091
49.343
4.260
1.000
30.22

ATOM
4684
N
ARG C
147
88.364
49.237
5.689
1.000
22.37

ATOM
4685
CA
ARG C
147
88.337
50.649
6.015
1.000
21.86

ATOM
4686
CE
ARG C
147
86.936
51.211
5.751
1.000
21.94

ATOM
4687
CG
ARG C
147
86.559
51.337
4.277
1.000
23.66

ATOM
4688
CD
ARG C
147
85.272
52.142
4.189
1.000
28.50

ATOM
4689
NE
ARG C
147
84.833
52.483
2.843
1.000
29.48

ATOM
4690
CZ
ARG C
147
83.997
51.726
2.144
1.000
30.36

ATOM
4691
NE1
ARG C
147
83.625
52.086
0.927
1.000
40.21

ATOM
4692
NH2
ARG C
147
83.528
50.599
2.656
1.000
30.57

ATOM
4693
C
ARG C
147
88.704
50.934
7.468
1.000
23.83

ATOM
4694
O
ARG C
147
89.023
52.084
7.799
1.000
21.61

ATOM
4695
N
GLY C
148
88.657
49.944
8.359
1.000
23.27

ATOM
4696
CA
GLY C
148
88.977
50.241
9.754
1.000
22.95

ATOM
4697
C
GLY C
148
88.910
49.030
10.663
1.000
23.86

ATOM
4698
O
GLY C
148
88.404
47.983
10.263
1.000
23.15

ATOM
4699
N
VAL C
149
89.433
49.170
11.880
1.000
21.41

ATOM
4700
CA
VAL C
149
89.438
48.111
12.873
1.000
21.07

ATOM
4701
CB
VAL C
149
90.815
47.434
13.047
1.000
24.01

ATOM
4702
CG1
VAL C
149
90.663
46.155
13.860
1.000
25.18

ATOM
4703
CG2
VAL C
149
91.461
47.147
11.702
1.000
31.46

ATOM
4704
C
VAL C
149
89.015
48.660
14.236
1.000
21.87

ATOM
4705
O
VAL C
149
89.573
49.650
14.719
1.000
22.20

ATOM
4706
N
ILE C
150
88.036
48.009
14.854
1.000
21.29

ATOM
4707
CA
ILE C
150
87.581
48.459
16.177
1.000
22.11

ATOM
4708
CB
ILE C
150
86.120
48.928
16.138
1.000
23.77

ATOM
4709
CG2
ILE C
150
85.599
49.309
17.516
1.000
22.27

ATOM
4710
CG1
ILE C
150
85.895
50.080
15.154
1.000
22.12

ATOM
4711
CD1
ILE C
150
84.436
50.412
14.925
1.000
22.79

ATOM
4712
C
ILE C
150
87.781
47.333
17.185
1.000
21.41

ATOM
4713
O
ILE C
150
87.392
46.194
16.955
1.000
23.38

ATOM
4714
N
ILE C
151
88.421
47.652
18.294
1.000
20.58

ATOM
4715
CA
ILE C
151
88.771
46.712
19.354
1.000
21.20

ATOM
4716
CB
ILE C
151
90.297
46.547
19.456
1.000
19.12

ATOM
4717
CG2
ILE C
151
90.718
45.602
20.566
1.000
16.71

ATOM
4718
CG1
ILE C
151
90.934
46.101
18.134
1.000
24.71

ATOM
4719
CD1
ILE C
151
92.445
46.052
18.169
1.000
24.82

ATOM
4720
C
ILE C
151
88.203
47.214
20.680
1.000
21.43

ATOM
4721
O
ILE C
151
88.441
48.370
21.032
1.000
23.16

ATOM
4722
N
ASN C
152
87.456
46.374
21.384
1.000
19.89

ATOM
4723
CA
ASN C
152
86.858
46.780
22.658
1.000
20.31

ATOM
4724
CB
ASN C
152
85.338
46.577
22.645
1.000
18.41

ATOM
4725
CG
ASN C
152
84.762
47.031
21.311
1.000
17.45

ATOM
4726
OD1
ASN C
152
84.199
46.232
20.564
1.000
34.00

ATOM
4727
ND2
ASN C
152
84.929
48.310
21.028
1.000
15.97

ATOM
4728
C
ASN C
152
87.458
45.995
23.816
1.000
22.13

ATOM
4729
O
ASN C
152
88.053
44.942
23.593
1.000
19.05

ATOM
4730
N
THR C
153
87.298
46.505
25.036
1.000
22.52

ATOM
4731
CA
THR C
153
87.802
45.768
26.192
1.000
19.48

ATOM
4732
CB
THR C
153
88.770
46.586
27.056
1.000
19.67

ATOM
4733
OG1
THR C
153
89.765
47.237
26.247
1.000
20.53

ATOM
4734
CG2
THR C
153
89.519
45.635
27.984
1.000
18.55

ATOM
4735
C
THR C
153
86.647
45.286
27.065
1.000
19.43

ATOM
4736
O
THR C
153
85.923
46.104
27.629
1.000
19.18

ATOM
4737
N
ALA C
154
86.504
43.967
27.145
1.000
17.96

ATOM
4738
CA
ALA C
154
85.546
43.388
28.091
1.000
23.21

ATOM
4739
CB
ALA C
154
84.783
42.231
27.479
1.000
16.13

ATOM
4740
C
ALA C
154
86.313
42.982
29.354
1.000
17.34

ATOM
4741
O
ALA C
154
87.034
43.830
29.893
1.000
20.75

ATOM
4742
N
SER C
155
86.155
41.747
29.783
1.000
20.86

ATOM
4743
CA
SER C
155
86.764
41.215
30.997
1.000
18.50

ATOM
4744
CB
SER C
155
86.326
42.008
32.231
1.000
20.65

ATOM
4745
OG
SER C
155
86.621
41.304
33.431
1.000
19.32

ATOM
4746
CB
SER C
155
86.363
39.764
31.180
1.000
18.55

ATOM
4747
O
SER C
155
85.277
39.408
30.715
1.000
17.19

ATOM
4748
N
VAL C
156
87.165
38.924
31.847
1.000
17.22

ATOM
4749
CA
VAL C
156
86.673
37.573
32.114
1.000
17.81

ATOM
4750
CB
VAL C
156
87.760
36.650
32.704
1.000
22.90

ATOM
4751
CG1
VAL C
156
88.915
36.479
31.725
1.000
24.56

ATOM
4752
CG2
VAL C
156
88.283
37.194
34.019
1.000
22.39

ATOM
4753
C
VAL C
156
85.464
37.589
33.060
1.000
15.91

ATOM
4754
O
VAL C
156
84.755
36.586
33.186
1.000
18.83

ATOM
4755
N
ALA C
157
85.215
38.704
33.730
1.000
15.01

ATOM
4756
CA
ALA C
157
84.041
38.914
34.563
1.000
14.91

ATOM
4757
CB
ALA C
157
84.140
40.284
35.218
1.000
13.46

ATOM
4758
C
ALA C
157
82.748
38.820
33.761
1.000
23.2.4

ATOM
4759
O
ALA C
157
81.685
38.651
34.360
1.000
22.64

ATOM
4760
N
ALA C
158
82.854
38.929
32.432
1.000
19.67

ATOM
4761
CA
ALA C
158
81.729
38.712
31.540
1.000
20.27

ATOM
4762
CB
ALA C
158
82.059
39.109
30.107
1.000
20.82

ATOM
4763
C
ALA C
158
81.304
37.253
31.572
1.000
20.48

ATOM
4764
O
ALA C
158
80.159
36.916
31.264
1.000
22.01

ATOM
4765
N
PHE C
159
82.244
36.380
31.953
1.000
17.98

ATOM
4766
CA
PHE C
159
81.928
34.952
31.954
1.000
21.05

ATOM
4767
CB
PHE C
159
82.917
34.205
31.056
1.000
22.40

ATOM
4768
CG
PHE C
159
83.083
34.828
29.675
1.000
24.42

ATOM
4769
CD1
PHE C
159
84.241
35.502
29.325
1.000
21.89

ATOM
4770
CD2
PHE C
159
82.056
34.719
28.749
1.000
25.13

ATOM
4771
CE1
PHE C
159
84.378
36.056
28.058
1.000
23.61

ATOM
4772
CE2
PHE C
159
82.192
35.266
27.481
1.000
25.88

ATOM
4773
CZ
PHE C
159
83.350
35.932
27.140
1.000
19.73

ATOM
4774
C
PHE C
159
81.926
34.345
33.358
1.000
25.32

ATOM
4775
O
PHE C
159
81.134
33.437
33.625
1.000
24.04

ATOM
4776
N
GLU C
160
82.779
34.802
34.258
1.000
21.14

ATOM
4777
CA
GLU C
160
82.875
34.281
35.615
1.000
24.99

ATOM
4778
CE
GLU C
160
84.158
33.484
35.857
1.000
25.61

ATOM
4779
CG
GLU C
160
84.429
32.284
34.995
1.000
30.25

ATOM
4780
CD
GLU C
160
85.521
32.475
33.964
1.000
32.66

ATOM
4781
OE1
GLU C
160
85.262
32.081
32.809
1.000
32.29

ATOM
4782
OE2
GLU C
160
86.617
33.001
34.246
1.000
22.74

ATOM
4783
C
GLU C
160
82.864
35.434
36.624
1.000
22.02

ATOM
4784
O
GLU C
160
83.791
35.528
37.437
1.000
21.01

ATOM
4785
N
GLY C
161
81.866
36.304
36.567
1.000
17.29

ATOM
4786
CA
GLY C
161
81.851
37.439
37.491
1.000
19.00

ATOM
4787
C
GLY C
161
81.868
36.907
38.928
1.000
20.23

ATOM
4788
O
GLY C
161
81.181
35.925
39.227
1.000
17.32

ATOM
4789
N
GLN C
162
82.649
37.541
39.781
1.000
18.84

ATOM
4790
CA
GLN C
162
82.813
37.127
41.171
1.000
22.71

ATOM
4791
CE
GLN C
162
84.206
37.487
41.685
1.000
21.68

ATOM
4792
CG
GLN C
162
85.379
36.970
40.862
1.000
23.66

ATOM
4793
CD
GLN C
162
86.694
37.252
41.577
1.000
24.38

ATOM
4794
OE1
GLN C
162
87.191
38.376
41.561
1.000
25.66

ATOM
4795
NE2
GLN C
162
87.262
36.237
42.215
1.000
22.36

ATOM
4796
C
GLN C
162
81.789
37.808
42.070
1.000
23.11

ATOM
4797
O
GLN C
162
81.098
38.733
41.640
1.000
21.46

ATOM
4798
N
VAL C
163
81.711
37.370
43.324
1.000
24.81

ATOM
4799
CA
VAL C
163
80.852
38.059
44.290
1.000
21.14

ATOM
4800
CE
VAL C
163
80.982
37.467
45.699
1.000
18.37

ATOM
4801
CG1
VAL C
163
80.299
38.340
46.731
1.000
22.10

ATOM
4802
CG2
VAL C
163
80.409
36.053
45.714
1.000
14.21

ATOM
4803
C
VAL C
163
81.224
39.537
44.312
1.000
23.76

ATOM
4804
O
VAL C
163
82.409
39.853
44.407
1.000
25.31

ATOM
4805
N
GLY C
164
80.234
40.420
44.203
1.000
19.76

ATOM
4806
CA
GLY C
164
80.469
41.844
44.194
1.000
18.89

ATOM
4807
C
GLY C
164
80.568
42.442
42.804
1.000
23.71

ATOM
4808
O
GLY C
164
80.662
43.669
42.678
1.000
25.11

ATOM
4809
N
GLN C
165
80.556
41.604
41.775
1.000
19.10

ATOM
4810
CA
GLN C
165
80.814
42.018
40.411
1.000
23.28

ATOM
4811
CB
GLN C
165
81.804
41.016
39.777
1.000
21.58

ATOM
4812
CG
GLN C
165
83.259
41.287
40.143
1.000
24.62

ATOM
4813
CD
GLN C
165
84.213
40.621
39.167
1.000
25.83

ATOM
4814
OE1
GLN C
165
84.081
39.433
38.878
1.000
23.28

ATOM
4815
NE2
GLN C
165
85.168
41.380
38.658
1.000
24.36

ATOM
4816
C
GLN C
165
79.596
42.094
39.507
1.000
25.66

ATOM
4817
O
GLN C
165
79.767
42.167
38.281
1.000
22.34

ATOM
4818
N
ALA C
166
78.382
42.080
40.032
1.000
19.52

ATOM
4819
CA
ALA C
166
77.190
42.135
39.191
1.000
19.44

ATOM
4820
CB
ALA C
166
75.942
42.227
40.065
1.000
21.99

ATOM
4821
C
ALA C
166
77.195
43.288
38.199
1.000
22.65

ATOM
4822
O
ALA C
166
76.961
43.089
37.001
1.000
24.51

ATOM
4823
N
ALA C
167
77.441
44.520
38.631
1.000
18.71

ATOM
4824
CA
ALA C
167
77.378
45.643
37.693
1.000
19.62

ATOM
4825
CE
ALA C
167
77.455
46.966
38.438
1.000
19.07

ATOM
4826
C
ALA C
167
78.485
45.553
36.648
1.000
23.28

ATOM
4827
O
ALA C
167
78.252
45.719
35.448
1.000
21.18

ATOM
4828
N
TYR C
168
79.709
45.290
37.101
1.000
19.90

ATOM
4829
CA
TYR C
168
80.830
45.168
36.171
1.000
18.57

ATOM
4830
CE
TYR C
168
82.120
44.873
36.916
1.000
20.89

ATOM
4831
CG
TYR C
168
83.408
45.040
36.139
1.000
19.26

ATOM
4832
CD1
TYR C
168
83.852
46.293
35.737
1.000
19.37

ATOM
4833
CE1
TYR C
168
85.030
46.461
35.030
1.000
18.00

ATOM
4834
CD2
TYR C
168
84.195
43.936
35.814
1.000
16.76

ATOM
4835
CE2
TYR C
168
85.379
44.090
35.105
1.000
17.87

ATOM
4836
CZ
TYR C
168
85.783
45.348
34.717
1.000
21.43

ATOM
4837
OH
TYR C
168
86.957
45.507
34.022
1.000
20.56

ATOM
4838
C
TYR C
168
80.528
44.073
35.155
1.000
21.19

ATOM
4839
O
TYR C
168
80.721
44.258
33.956
1.000
23.83

ATOM
4840
N
SER C
169
80.037
42.938
35.647
1.000
20.45

ATOM
4841
CA
SER C
169
79.751
41.804
34.780
1.000
17.69

ATOM
4842
CB
SER C
169
79.316
40.582
35.587
1.000
17.03

ATOM
4843
OG
SER C
169
80.453
39.915
36.117
1.000
19.86

ATOM
4844
CB
SER C
169
78.692
42.157
33.741
1.000
24.37

ATOM
4845
O
SER C
169
78.810
41.724
32.586
1.000
24.38

ATOM
4846
N
ALA C
170
77.682
42.920
34.151
1.000
22.07

ATOM
4847
CA
ALA C
170
76.612
43.285
33.214
1.000
18.30

ATOM
4848
CE
ALA C
170
75.502
44.022
33.939
1.000
16.49

ATOM
4849
C
ALA C
170
77.189
44.135
32.089
1.000
22.43

ATOM
4850
O
ALA C
170
76.948
43.962
30.898
1.000
22.50

ATOM
4851
N
SER C
171
78.009
45.113
32.495
1.000
20.04

ATOM
4852
CA
SER C
171
78.564
46.029
31.503
1.000
18.05

ATOM
4853
CE
SER C
171
79.284
47.187
32.185
1.000
18.91

ATOM
4854
OG
SER C
171
80.590
46.838
32.608
1.000
22.61

ATOM
4855
CB
SER C
171
79.486
45.276
30.547
1.000
21.94

ATOM
4856
O
SER C
171
79.442
45.523
29.341
1.000
24.60

ATOM
4857
N
LYS C
172
80.310
44.365
31.066
1.000
15.08

ATOM
4858
CA
LYS C
172
81.277
43.690
30.207
1.000
19.64

ATOM
4859
CB
LYS C
172
82.467
43.186
31.026
1.000
19.41

ATOM
4860
CG
LYS C
172
83.239
44.295
31.722
1.000
16.40

ATOM
4861
CD
LYS C
172
83.739
45.356
30.767
1.000
21.19

ATOM
4862
CE
LYS C
172
84.930
46.123
31.313
1.000
16.40

ATOM
4863
NZ
LYS C
172
85.562
47.002
30.286
1.000
17.94

ATOM
4864
G
LYS C
172
80.621
42.556
29.427
1.000
23.18

ATOM
4865
O
LYS C
172
81.032
42.214
28.313
1.000
20.83

ATOM
4866
N
GLY C
173
79.574
41.964
29.995
1.000
19.64

ATOM
4867
CA
GLY C
173
78.793
40.984
29.258
1.000
16.61

ATOM
4868
C
GLY C
173
78.080
41.671
28.099
1.000
20.08

ATOM
4869
O
GLY C
173
77.848
41.054
27.062
1.000
19.57

ATOM
4870
N
GLY C
174
77.738
42.944
28.280
1.000
19.74

ATOM
4871
CA
GLY C
174
77.081
43.697
27.218
1.000
18.27

ATOM
4872
C
GLY C
174
78.045
43.907
26.056
1.000
23.73

ATOM
4873
O
GLY C
174
77.672
43.840
24.882
1.000
19.78

ATOM
4874
N
ILE C
175
79.303
44.172
26.389
1.000
23.27

ATOM
4875
CA
ILE C
175
80.330
44.337
25.365
1.000
20.71

ATOM
4876
CE
ILE C
175
81.688
44.695
25.994
1.000
23.26

ATOM
4877
CG2
ILE C
175
82.770
44.772
24.926
1.000
20.37

ATOM
4878
CG1
ILE C
175
81.688
45.982
26.829
1.000
21.73

ATOM
4879
CD1
ILE C
175
81.456
47.221
25.992
1.000
30.34

ATOM
4880
C
ILE C
175
80.487
43.065
24.541
1.000
20.73

ATOM
4881
O
ILE C
175
80.526
43.084
23.313
1.000
23.88

ATOM
4882
N
VAL C
176
80.585
41.936
25.239
1.000
15.48

ATOM
4883
CA
VAL C
176
80.725
40.651
24.573
1.000
14.04

ATOM
4884
CB
VAL C
176
80.845
39.518
25.610
1.000
19.74

ATOM
4885
CG1
VAL C
176
80.575
38.161
24.987
1.000
18.87

ATOM
4886
CG2
VAL C
176
82.226
39.560
26.249
1.000
19.59

ATOM
4887
C
VAL C
176
79.539
40.390
23.660
1.000
20.41

ATOM
4888
O
VAL C
176
79.680
40.023
22.493
1.000
20.54

ATOM
4889
N
GLY C
177
78.334
40.569
24.193
1.000
19.61

ATOM
4890
CA
GLY C
177
77.136
40.316
23.424
1.000
16.92

ATOM
4891
C
GLY C
177
76.986
41.203
22.213
1.000
21.30

ATOM
4892
O
GLY C
177
76.382
40.812
21.208
1.000
24.01

ATOM
4893
N
MET C
178
77.496
42.432
22.215
1.000
19.61

ATOM
4894
CA
MET C
178
77.233
43.272
21.046
1.000
17.86

ATOM
4895
CB
MET C
178
76.979
44.720
21.454
1.000
17.13

ATOM
4896
CG
MET C
178
78.191
45.421
22.045
1.000
21.09

ATOM
4897
SD
MET C
178
77.817
47.098
22.590
1.000
24.03

ATOM
4898
CE
MET C
178
79.476
47.732
22.850
1.000
18.90

ATOM
4899
C
MET C
178
78.374
43.192
20.039
1.000
21.69

ATOM
4900
O
MET C
178
78.306
43.821
18.980
1.000
22.15

ATOM
4901
N
THR C
179
79.413
42.419
20.350
1.000
18.49

ATOM
4902
CA
THR C
179
80.552
42.343
19.435
1.000
19.38

ATOM
4903
CB
THR C
179
81.715
41.578
20.077
1.000
18.75

ATOM
4904
OG1
THR C
179
82.308
42.431
21.076
1.000
18.08

ATOM
4905
CG2
THR C
179
82.821
41.290
19.072
1.000
15.74

ATOM
4906
C
THR C
179
80.138
41.746
18.094
1.000
23.48

ATOM
4907
O
THR C
179
80.402
42.366
17.054
1.000
20.76

ATOM
4908
N
LEU C
180
79.481
40.588
18.052
1.000
19.56

ATOM
4909
CA
LEU C
180
79.110
39.991
16.771
1.000
17.92

ATOM
4910
CE
LEU C
180
78.526
38.592
16.974
1.000
18.98

ATOM
4911
CG
LEU C
180
78.152
37.823
15.702
1.000
24.14

ATOM
4912
CD1
LEU C
180
79.365
37.659
14.797
1.000
26.21

ATOM
4913
CD2
LEU C
180
77.569
36.461
16.040
1.000
20.39

ATOM
4914
C
LEU C
180
78.122
40.839
15.977
1.000
21.92

ATOM
4915
O
LEU C
180
78.396
41.090
14.788
1.000
22.82

ATOM
4916
N
PRO C
181
77.001
41.271
16.543
1.000
21.19

ATOM
4917
CD
PRO C
181
76.478
41.009
17.891
1.000
20.31

ATOM
4918
CA
PRO C
181
76.067
42.119
15.783
1.000
23.54

ATOM
4919
CB
PRO C
181
74.987
42.531
16.795
1.000
22.69

ATOM
4920
CG
PRO C
181
75.557
42.179
18.132
1.000
19.47

ATOM
4921
C
PRO C
181
76.735
43.365
15.219
1.000
25.60

ATOM
4922
O
PRO C
181
76.450
43.782
14.095
1.000
20.77

ATOM
4923
N
ILE C
182
77.631
44.003
15.963
1.000
20.42

ATOM
4924
CA
ILE C
182
78.267
45.199
15.389
1.000
17.66

ATOM
4925
CE
ILE C
182
78.947
46.036
16.481
1.000
16.77

ATOM
4926
CG2
ILE C
182
79.697
47.205
15.870
1.000
18.19

ATOM
4927
CG1
ILE C
182
77.971
46.528
17.557
1.000
18.40

ATOM
4928
CD1
ILE C
182
78.654
47.095
18.788
1.000
21.84

ATOM
4929
C
ILE C
182
79.230
44.797
14.285
1.000
23.52

ATOM
4930
O
ILE C
182
79.357
45.488
13.268
1.000
23.23

ATOM
4931
N
ALA C
183
79.919
43.670
14.421
1.000
21.40

ATOM
4932
CA
ALA C
183
80.709
43.151
13.304
1.000
21.08

ATOM
4933
CB
ALA C
183
81.451
41.870
13.661
1.000
20.13

ATOM
4934
C
ALA C
183
79.796
42.897
12.108
1.000
24.15

ATOM
4935
O
ALA C
183
80.139
43.202
10.963
1.000
21.19

ATOM
4936
N
ARG C
184
78.613
42.333
12.359
1.000
21.19

ATOM
4937
CA
ARG C
184
77.712
42.082
11.228
1.000
22.02

ATOM
4938
CB
ARG C
184
76.515
41.222
11.642
1.000
17.02

ATOM
4939
CG
ARG C
184
76.907
39.790
11.944
1.000
16.66

ATOM
4940
CD
ARG C
184
75.783
38.999
12.591
1.000
16.59

ATOM
4941
NE
ARG C
184
76.015
37.569
12.471
1.000
18.43

ATOM
4942
CZ
ARG C
184
75.293
36.593
12.985
1.000
18.80

ATOM
4943
NH1
ARG C
184
75.632
35.331
12.776
1.000
18.86

ATOM
4944
NH2
ARG C
184
74.219
36.873
13.715
1.000
21.57

ATOM
4945
C
ARG C
184
77.259
43.401
10.614
1.000
21.95

ATOM
4946
O
ARG C
184
77.243
43.521
9.383
1.000
21.48

ATOM
4947
N
ASP C
185
76.913
44.384
11.444
1.000
15.88

ATOM
4948
CA
ASP C
185
76.477
45.675
10.916
1.000
19.50

ATOM
4949
CB
ASP C
185
76.280
46.734
11.997
1.000
19.32

ATOM
4950
CG
ASP C
185
75.036
46.630
12.843
1.000
23.51

ATOM
4951
OD1
ASP C
185
75.002
47.321
13.882
1.000
23.02

ATOM
4952
OD2
ASP C
185
74.096
45.882
12.515
1.000
16.66

ATOM
4953
C
ASP C
185
77.502
46.249
9.930
1.000
24.98

ATOM
4954
O
ASP C
185
77.166
46.681
8.832
1.000
20.75

ATOM
4955
N
LEU C
186
78.763
46.257
10.344
1.000
18.62

ATOM
4956
CA
LEU C
186
79.810
46.982
9.640
1.000
20.87

ATOM
4957
CB
LEU C
186
80.820
47.496
10.677
1.000
19.42

ATOM
4958
CG
LEU C
186
80.255
48.395
11.775
1.000
22.20

ATOM
4959
CD1
LEU C
186
81.361
48.953
12.672
1.000
17.85

ATOM
4960
CD2
LEU C
186
79.458
49.547
11.178
1.000
21.31

ATOM
4961
C
LEU C
186
80.528
46.154
8.586
1.000
21.49

ATOM
4962
O
LEU C
186
81.397
46.655
7.861
1.000
23.84

ATOM
4963
N
ALA C
187
80.183
44.878
8.511
1.000
14.05

ATOM
4964
CA
ALA C
187
80.825
43.985
7.554
1.000
17.54

ATOM
4965
CB
ALA C
187
80.217
42.594
7.650
1.000
15.77

ATOM
4966
C
ALA C
187
80.757
44.492
6.117
1.000
23.42

ATOM
4967
O
ALA C
187
81.804
44.388
5.460
1.000
24.58

ATOM
4968
N
PRO C
188
79.646
44.987
5.594
1.000
26.75

ATOM
4969
CD
PRO C
188
78.301
45.092
6.198
1.000
31.00

ATOM
4970
CA
PRO C
188
79.633
45.490
4.212
1.000
26.89

ATOM
4971
CB
PRO C
188
78.166
45.866
3.952
1.000
26.16

ATOM
4972
CG
PRO C
188
77.395
45.132
4.995
1.000
31.72

ATOM
4973
C
PRO C
188
80.485
46.730
4.014
1.000
31.65

ATOM
4974
O
PRO C
188
80.776
47.121
2.878
1.000
33.18

ATOM
4975
N
ILE C
189
80.914
47.408
5.076
1.000
26.20

ATOM
4976
CA
ILE C
189
81.786
48.555
4.792
1.000
27.86

ATOM
4977
CE
ILE C
189
81.251
49.840
5.440
1.000
33.18

ATOM
4978
CG2
ILE C
189
80.027
50.313
4.657
1.000
37.79

ATOM
4979
CG1
ILE C
189
80.947
49.727
6.931
1.000
28.57

ATOM
4980
CD1
ILE C
189
80.160
50.922
7.453
1.000
30.62

ATOM
4981
C
ILE C
189
83.220
48.297
5.238
1.000
23.24

ATOM
4982
O
ILE C
189
84.030
49.216
5.327
1.000
23.19

ATOM
4983
N
GLY C
190
83.524
47.029
5.501
1.000
19.61

ATOM
4984
CA
GLY C
190
84.877
46.607
5.781
1.000
21.76

ATOM
4985
C
GLY C
190
85.479
47.116
7.065
1.000
23.87

ATOM
4986
O
GLY C
190
86.657
47.460
7.125
1.000
24.45

ATOM
4987
N
ILE C
191
84.685
47.169
8.138
1.000
23.04

ATOM
4988
CA
ILE C
191
85.276
47.514
9.433
1.000
21.87

ATOM
4989
CE
ILE C
191
84.574
48.715
10.074
1.000
20.61

ATOM
4990
CG2
ILE C
191
85.197
49.005
11.436
1.000
24.73

ATOM
4991
CG1
ILE C
191
84.550
49.983
9.218
1.000
20.90

ATOM
4992
CD1
ILE C
191
83.650
51.064
9.783
1.000
19.84

ATOM
4993
C
ILE C
191
85.201
46.304
10.363
1.000
24.63

ATOM
4994
O
ILE C
191
84.091
45.842
10.665
1.000
26.08

ATOM
4995
N
ARG C
192
86.344
45.779
10.794
1.000
20.62

ATOM
4996
CA
ARG C
192
86.350
44.608
11.674
1.000
21.27

ATOM
4997
CB
ARG C
192
87.679
43.852
11.626
1.000
20.62

ATOM
4998
CG
ARG C
192
87.985
43.203
10.285
1.000
20.90

ATOM
4999
CD
ARG C
192
89.210
42.323
10.330
1.000
18.84

ATOM
5000
NE
ARG C
192
90.478
43.041
10.348
1.000
23.01

ATOM
5001
CZ
ARG C
192
91.355
43.045
11.346
1.000
22.55

ATOM
5002
NE1
ARG C
192
91.114
42.367
12.458
1.000
22.22

ATOM
5003
NH2
ARG C
192
92.487
43.730
11.251
1.000
20.98

ATOM
5004
C
ARG C
192
86.057
45.037
13.114
1.000
20.57

ATOM
5005
O
ARG C
192
86.400
46.163
13.482
1.000
20.36

ATOM
5006
N
VAL C
193
85.419
44.161
13.885
1.000
20.86

ATOM
5007
CA
VAL C
193
85.130
44.469
15.292
1.000
23.25

ATOM
5008
CE
VAL C
193
83.659
44.842
15.515
1.000
23.85

ATOM
5009
CG1
VAL C
193
83.404
45.258
16.960
1.000
21.43

ATOM
5010
CG2
VAL C
193
83.258
45.976
14.575
1.000
18.16

ATOM
5011
C
VAL C
193
85.519
43.281
16.170
1.000
20.12

ATOM
5012
O
VAL C
193
85.008
42.175
15.996
1.000
16.74

ATOM
5013
N
MET C
194
86.437
43.515
17.099
1.000
18.39

ATOM
5014
CA
MET C
194
86.997
42.465
17.942
1.000
19.21

ATOM
5015
CB
MET C
194
88.421
42.135
17.486
1.000
22.24

ATOM
5016
CG
MET C
194
88.499
41.328
16.192
1.000
19.86

ATOM
5017
SD
MET C
194
88.078
39.591
16.432
1.000
19.40

ATOM
5018
CE
MET C
194
89.322
39.131
17.648
1.000
17.87

ATOM
5019
C
MET C
194
87.013
42.862
19.415
1.000
21.78

ATOM
5020
O
MET C
194
87.041
44.030
19.794
1.000
18.51

ATOM
5021
N
THR C
195
87.010
41.871
20.302
1.000
20.94

ATOM
5022
CA
THR C
195
87.027
42.216
21.729
1.000
20.90

ATOM
5023
CB
THR C
195
85.629
41.984
22.337
1.000
22.49

ATOM
5024
OG1
THR C
195
84.713
42.952
21.794
1.000
19.71

ATOM
5025
CG2
THR C
195
85.641
42.176
23.843
1.000
20.67

ATOM
5026
C
THR C
195
88.067
41.404
22.478
1.000
18.58

ATOM
5027
O
THR C
195
88.280
40.218
22.235
1.000
21.52

ATOM
5028
N
THR C
196
88.758
42.057
23.410
1.000
21.00

ATOM
5029
CA
ILE C
196
89.699
41.346
24.271
1.000
20.59

ATOM
5030
CE
ILE C
196
91.080
42.016
24.288
1.000
22.02

ATOM
5031
CG2
ILE C
196
91.954
41.401
25.365
1.000
13.39

ATOM
5032
CG1
ILE C
196
91.783
42.010
22.923
1.000
17.94

ATOM
5033
CD
ILE C
196
92.835
43.078
22.761
1.000
17.09

ATOM
5034
C
ILE C
196
89.116
41.295
25.687
1.000
17.92

ATOM
5035
O
ILE C
196
88.617
42.327
26.135
1.000
18.00

ATOM
5036
N
ALA C
197
89.174
40.135
26.328
1.000
17.64

ATOM
5037
CA
ALA C
197
88.730
40.004
27.714
1.000
19.48

ATOM
5038
CE
ALA C
197
87.709
38.893
27.885
1.000
15.55

ATOM
5039
C
ALA C
197
89.935
39.750
28.611
1.000
17.38

ATOM
5040
O
ALA C
197
90.373
38.612
28.764
1.000
21.58

ATOM
5041
N
PRO C
198
90.505
40.791
29.198
1.000
14.98

ATOM
5042
CD
PRO C
198
90.131
42.210
29.075
1.000
14.59

ATOM
5043
CA
PRO C
198
91.655
40.584
30.080
1.000
16.28

ATOM
5044
CE
PRO C
198
92.103
42.012
30.398
1.000
17.97

ATOM
5045
CG
PRO C
198
91.423
42.907
29.412
1.000
14.71

ATOM
5046
C
PRO C
198
91.249
39.874
31.368
1.000
20.85

ATOM
5047
O
PRO C
198
90.121
40.024
31.837
1.000
20.67

ATOM
5048
N
GLY C
199
92.145
39.101
31.962
1.000
18.62

ATOM
5049
CA
GLY C
199
91.876
38.524
33.287
1.000
20.40

ATOM
5050
C
GLY C
199
92.267
39.544
34.351
1.000
24.59

ATOM
5051
O
GLY C
199
91.475
40.429
34.678
1.000
27.81

ATOM
5052
N
LEU C
200
93.486
39.442
34.871
1.000
22.82

ATOM
5053
CA
LEU C
200
93.987
40.368
35.882
1.000
23.36

ATOM
5054
CE
LEU C
200
94.232
39.641
37.207
1.000
28.78

ATOM
5055
CG
LEU C
200
93.115
38.748
37.751
1.000
28.91

ATOM
5056
CD1
LEU C
200
93.669
37.767
38.771
1.000
25.33

ATOM
5057
CD2
LEU C
200
92.004
39.596
38.359
1.000
26.21

ATOM
5058
C
LEU C
200
95.284
41.027
35.427
1.000
22.30

ATOM
5059
O
LEU C
200
96.275
40.332
35.157
1.000
26.10

ATOM
5060
N
PHE C
201
95.300
42.353
35.329
1.000
18.24

ATOM
5061
CA
PHE C
201
96.485
43.048
34.842
1.000
21.20

ATOM
5062
CB
PHE C
201
96.197
43.708
33.490
1.000
20.11

ATOM
5063
CG
PHE C
201
96.364
42.761
32.305
1.000
22.13

ATOM
5064
CD1
PHE C
201
95.433
41.770
32.063
1.000
20.96

ATOM
5065
CD2
PHE C
201
97.455
42.886
31.460
1.000
21.03

ATOM
5066
CE1
PHE C
201
95.583
40.920
30.980
1.000
21.62

ATOM
5067
CE2
PHE C
201
97.605
42.044
30.374
1.000
22.29

ATOM
5068
CZ
PHE C
201
96.666
41.062
30.134
1.000
15.56

ATOM
5069
C
PHE C
201
96.955
44.125
35.813
1.000
24.21

ATOM
5070
O
PHE C
201
96.132
44.768
36.461
1.000
26.00

ATOM
5071
N
GLY C
202
98.265
44.325
35.892
1.000
25.77

ATOM
5072
CA
GLY C
202
98.844
45.302
36.792
1.000
26.53

ATOM
5073
C
GLY C
202
98.711
46.729
36.318
1.000
25.89

ATOM
5074
O
GLY C
202
99.636
47.319
35.753
1.000
32.59

ATOM
5075
N
THR C
203
97.549
47.321
36.542
1.000
22.53

ATOM
5076
CA
THR C
203
97.288
48.706
36.172
1.000
23.17

ATOM
5077
CB
THR C
203
96.258
48.779
35.032
1.000
27.13

ATOM
5078
OD1
THR C
203
94.986
48.433
35.585
1.000
25.92

ATOM
5079
CG2
THR C
203
96.567
47.775
33.934
1.000
27.46

ATOM
5080
C
THR C
203
96.769
49.464
37.391
1.000
29.62

ATOM
5081
O
THR C
203
96.437
48.801
38.392
1.000
25.16

ATOM
5082
N
PRO C
204
96.688
50.788
37.353
1.000
27.16

ATOM
5083
CD
PRO C
204
97.155
51.684
36.277
1.000
27.74

ATOM
5084
CA
PRO C
204
96.107
51.546
38.471
1.000
30.12

ATOM
5085
CE
PRO C
204
96.141
52.996
37.970
1.000
28.02

ATOM
5086
CG
PRO C
204
97.239
53.024
36.956
1.000
27.83

ATOM
5087
C
PRO C
204
94.663
51.176
38.797
1.000
37.24

ATOM
5088
O
PRO C
204
94.143
51.572
39.851
1.000
35.02

ATOM
5089
N
LEU C
205
93.981
50.433
37.927
1.000
35.79

ATOM
5090
CA
LEU C
205
92.608
50.024
38.223
1.000
30.70

ATOM
5091
CB
LEU C
205
92.033
49.167
37.101
1.000
29.09

ATOM
5092
CG
LEU C
205
90.536
48.854
37.159
1.000
35.68

ATOM
5093
CD1
LEU C
205
89.730
50.060
36.699
1.000
31.89

ATOM
5094
CD2
LEU C
205
90.211
47.615
36.337
1.000
31.92

ATOM
5095
C
LEU C
205
92.579
49.247
39.538
1.000
30.14

ATOM
5096
O
LEU C
205
91.648
49.387
40.329
1.000
36.81

ATOM
5097
N
LEU C
206
93.605
48.425
39.734
1.000
31.90

ATOM
5098
CA
LEU C
206
93.699
47.534
40.879
1.000
29.40

ATOM
5099
CE
LEU C
206
94.474
46.273
40.479
1.000
25.89

ATOM
5100
CG
LEU C
206
93.872
45.442
39.343
1.000
28.59

ATOM
5101
CD1
LEU C
206
94.364
43.998
39.404
1.000
29.19

ATOM
5102
CD2
LEU C
206
92.356
45.484
39.370
1.000
27.50

ATOM
5103
C
LEU C
206
94.370
48.172
42.086
1.000
40.42

ATOM
5104
O
LEU C
206
94.515
47.526
43.129
1.000
39.05

ATOM
5105
N
THR C
207
94.798
49.431
41.989
1.000
42.35

ATOM
5106
CA
THR C
207
95.542
50.010
43.106
1.000
48.45

ATOM
5107
CE
THR C
207
96.139
51.382
42.745
1.000
49.14

ATOM
5108
OG1
THR C
207
97.202
51.198
41.798
1.000
62.11

ATOM
5109
CG2
THR C
207
96.756
52.042
43.969
1.000
47.12

ATOM
5110
C
THR C
207
94.670
50.1534
4.352
1.000
52.40

ATOM
5111
O
THR C
207
95.223
50.1784
5.452
1.000
44.87

ATOM
5112
N
SER C
208
93.364
50.2404
4.157
1.000
57.38

ATOM
5113
CA
SER C
208
92.357
50.4864
5.172
1.000
59.32

ATOM
5114
CE
SER C
208
90.995
50.7944
4.529
1.000
59.37

ATOM
5115
OG
SER C
208
91.092
51.8534
3.591
1.000
80.12

ATOM
5116
CB
SER C
208
92.166
49.3194
6.133
1.000
61.87

ATOM
5117
O
SER C
208
91.367
49.4084
7.070
1.000
69.52

ATOM
5118
N
LEU C
209
92.876
48.2144
5.915
1.000
54.77

ATOM
5119
CA
LEU C
209
92.625
47.0524
6.762
1.000
53.13

ATOM
5120
CE
LEU C
209
92.245
45.838
45.916
1.000
53.90

ATOM
5121
CG
LEU C
209
91.531
46.076
44.587
1.000
49.79

ATOM
5122
CD1
LEU C
209
92.130
45.191
43.502
1.000
35.07

ATOM
5123
CD2
LEU C
209
90.036
45.831
44.712
1.000
30.84

ATOM
5124
C
LEU C
209
93.833
46.716
47.635
1.000
48.32

ATOM
5125
O
LEU C
209
94.971
47.000
47.273
1.000
49.62

ATOM
5126
N
PRO C
210
93.533
46.098
48.773
1.000
43.75

ATOM
5127
CD
PRO C
210
92.167
45.769
49.215
1.000
47.38

ATOM
5128
CA
PRO C
210
94.543
45.654
49.726
1.000
47.32

ATOM
5129
CB
PRO C
210
93.764
44.736
50.672
1.000
44.91

ATOM
5130
CG
PRO C
210
92.356
45.210
50.596
1.000
42.82

ATOM
5131
C
PRO C
210
95.624
44.825
49.039
1.000
55.73

ATOM
5132
O
PRO C
210
95.271
43.950
48.245
1.000
51.13

ATOM
5133
N
GLU C
211
96.882
45.104
49.355
1.000
62.78

ATOM
5134
CA
GLU C
211
97.985
44.332
48.782
1.000
65.71

ATOM
5135
CB
GLU C
211
99.313
44.751
49.413
1.000
73.61

ATOM
5136
CG
GLU C
211
100.508
43.921
48.979
1.000
78.96

ATOM
5137
CD
GLU C
211
101.366
44.592
47.924
1.000
83.27

ATOM
5138
OE1
GLU C
211
100.804
45.229
47.007
1.000
78.56

ATOM
5139
OE2
GLU C
211
102.610
44.481
48.011
1.000
91.83

ATOM
5140
C
GLU C
211
97.738
42.840
48.950
1.000
57.45

ATOM
5141
O
GLU C
211
97.930
42.039
48.037
1.000
57.10

ATOM
5142
N
LYS C
212
97.276
42.425
50.129
1.000
54.71

ATOM
5143
CA
LYS C
212
96.958
41.008
50.289
1.000
53.11

ATOM
5144
CB
LYS C
212
96.545
40.709
51.719
1.000
61.51

ATOM
5145
C
LYS C
212
95.863
40.596
49.315
1.000
54.29

ATOM
5146
O
LYS C
212
95.752
39.430
48.933
1.000
47.94

ATOM
5147
N
VAL C
213
95.031
41.550
48.895
1.000
55.78

ATOM
5148
CA
VAL C
213
93.969
41.196
47.948
1.000
59.39

ATOM
5149
CB
VAL C
213
92.876
42.278
47.901
1.000
63.29

ATOM
5150
CG1
VAL C
213
91.983
42.096
46.683
1.000
59.66

ATOM
5151
CG2
VAL C
213
92.047
42.243
49.180
1.000
60.14

ATOM
5152
C
VAL C
213
94.538
40.956
46.553
1.000
53.95

ATOM
5153
O
VAL C
213
94.379
39.880
45.971
1.000
42.35

ATOM
5154
N
ARG C
214
95.216
41.958
46.006
1.000
47.03

ATOM
5155
CA
ARG C
214
95.901
41.833
44.729
1.000
45.10

ATOM
5156
CB
ARG C
214
96.803
43.047
44.497
1.000
45.03

ATOM
5157
CG
ARG C
214
96.359
43.982
43.393
1.000
50.46

ATOM
5158
CD
ARG C
214
97.469
44.945
43.009
1.000
53.70

ATOM
5159
NE
ARG C
214
98.264
45.387
44.148
1.000
52.31

ATOM
5160
CZ
ARG C
214
97.821
46.112
45.165
1.000
49.37

ATOM
5161
NE1
ARG C
214
96.555
46.504
45.225
1.000
41.96

ATOM
5162
NH2
ARG C
214
98.657
46.447
46.139
1.000
51.95

ATOM
5163
C
ARG C
214
96.753
40.570
44.668
1.000
38.21

ATOM
5164
O
ARG C
214
96.561
39.721
43.803
1.000
46.16

ATOM
5165
N
ASN C
215
97.704
40.460
45.592
1.000
39.14

ATOM
5166
CA
ASN C
215
98.666
39.359
45.567
1.000
43.82

ATOM
5167
CE
ASN C
215
99.623
39.443
46.757
1.000
42.67

ATOM
5168
CG
ASN C
215
100.568
40.622
46.684
1.000
43.42

ATOM
5169
OD1
ASN C
215
101.050
40.994
45.614
1.000
54.29

ATOM
5170
ND2
ASN C
215
100.863
41.229
47.828
1.000
46.57

ATOM
5171
C
ASN C
215
97.947
38.016
45.537
1.000
42.43

ATOM
5172
O
ASN C
215
98.311
37.108
44.786
1.000
52.24

ATOM
5173
N
PHE C
216
96.905
37.889
46.356
1.000
36.32

ATOM
5174
CA
PHE C
216
96.124
36.660
46.348
1.000
33.94

ATOM
5175
CB
PHE C
216
94.936
36.737
47.306
1.000
37.12

ATOM
5176
CG
PHE C
216
94.029
35.518
47.179
1.000
43.40

ATOM
5177
CD1
PHE C
216
94.485
34.270
47.573
1.000
46.19

ATOM
5178
CD2
PHE C
216
92.751
35.642
46.668
1.000
44.18

ATOM
5179
CE1
PHE C
216
93.678
33.155
47.457
1.000
49.58

ATOM
5180
CE2
PHE C
216
91.937
34.532
46.553
1.000
46.42

ATOM
5181
CZ
PHE C
216
92.400
33.288
46.943
1.000
48.68

ATOM
5182
C
PHE C
216
95.622
36.362
44.932
1.000
36.62

ATOM
5183
O
PHE C
216
95.951
35.308
44.393
1.000
35.34

ATOM
5184
N
LEU C
217
94.855
37.295
44.383
1.000
38.86

ATOM
5185
CA
LEU C
217
94.374
37.250
43.005
1.000
36.55

ATOM
5186
CB
LEU C
217
93.819
38.603
42.563
1.000
41.84

ATOM
5187
CG
LEU C
217
92.476
39.049
43.142
1.000
35.99

ATOM
5188
CD1
LEU C
217
92.146
40.475
42.727
1.000
34.52

ATOM
5189
CD2
LEU C
217
91.359
38.112
42.714
1.000
41.78

ATOM
5190
C
LEU C
217
95.515
36.823
42.083
1.000
23.70

ATOM
5191
O
LEU C
217
95.412
35.855
41.336
1.000
39.82

ATOM
5192
N
ALA C
218
96.620
37.555
42.184
1.000
29.42

ATOM
5193
CA
ALA C
218
97.825
37.237
41.433
1.000
33.94

ATOM
5194
CB
ALA C
218
98.973
38.118
41.913
1.000
39.99

ATOM
5195
C
ALA C
218
98.203
35.767
41.540
1.000
36.98

ATOM
5196
O
ALA C
218
98.544
35.103
40.556
1.000
33.61

ATOM
5197
N
SER C
219
98.161
35.216
42.751
1.000
33.61

ATOM
5198
CA
SER C
219
98.612
33.844
42.946
1.000
33.83

ATOM
5199
CB
SER C
219
98.711
33.556
44.453
1.000
37.13

ATOM
5200
OG
SER C
219
97.402
33.337
44.963
1.000
40.94

ATOM
5201
C
SER C
219
97.701
32.806
42.301
1.000
35.38

ATOM
5202
O
SER C
219
98.063
31.628
42.222
1.000
28.50

ATOM
5203
N
GLN C
220
96.522
33.218
41.845
1.000
33.22

ATOM
5204
CA
GLN C
220
95.554
32.316
41.242
1.000
29.91

ATOM
5205
CE
GLN C
220
94.138
32.880
41.421
1.000
35.00

ATOM
5206
CG
GLN C
220
93.738
33.114
42.865
1.000
45.83

ATOM
5207
CD
GLN C
220
93.228
31.841
43.519
1.000
55.68

ATOM
5208
OE1
GLN C
220
94.027
31.086
44.081
1.000
68.62

ATOM
5209
NE2
GLN C
220
91.922
31.615
43.432
1.000
59.51

ATOM
5210
C
GLN C
220
95.780
32.064
39.754
1.000
26.22

ATOM
5211
O
GLN C
220
95.211
31.112
39.214
1.000
25.79

ATOM
5212
N
VAL C
221
96.581
32.877
39.073
1.000
23.25

ATOM
5213
CA
VAL C
221
96.763
32.666
37.628
1.000
20.94

ATOM
5214
CB
VAL C
221
97.491
33.870
37.009
1.000
21.52

ATOM
5215
CG1
VAL C
221
97.605
33.689
35.502
1.000
15.39

ATOM
5216
CG2
VAL C
221
96.782
35.168
37.379
1.000
17.44

ATOM
5217
C
VAL C
221
97.548
31.396
37.375
1.000
25.25

ATOM
5218
O
VAL C
221
98.681
31.277
37.853
1.000
26.36

ATOM
5219
N
PRO C
222
96.990
30.413
36.682
1.000
26.70

ATOM
5220
CD
PRO C
222
95.643
30.367
36.087
1.000
22.74

ATOM
5221
CA
PRO C
222
97.725
29.149
36.494
1.000
24.77

ATOM
5222
CE
PRO C
222
96.800
28.347
35.573
1.000
17.60

ATOM
S223
CG
PRO C
222
95.440
28.884
35.910
1.000
20.38

ATOM
5224
C
PRO C
222
99.108
29.320
35.885
1.000
28.74

ATOM
5225
O
PRO C
222
100.083
28.833
36.476
1.000
24.95

ATOM
5226
N
PHE C
223
99.278
29.975
34.742
1.000
21.18

ATOM
5227
CA
PHE C
223
100.619
30.161
34.198
1.000
17.83

ATOM
5228
CB
PHE C
223
101.253
28.859
33.680
1.000
17.91

ATOM
5229
CG
PHE C
223
102.659
29.160
33.145
1.000
27.36

ATOM
5230
CD1
PHE C
223
103.708
29.418
34.013
1.000
29.04

ATOM
5231
CD2
PHE C
223
102.917
29.189
31.788
1.000
23.22

ATOM
5232
CE1
PHE C
223
104.980
29.711
33.556
1.000
25.46

ATOM
5233
CE2
PHE C
223
104.179
29.483
31.314
1.000
23.84

ATOM
5234
CZ
PHE C
223
105.216
29.750
32.189
1.000
25.17

ATOM
5235
C
PHE C
223
100.609
31.174
33.058
1.000
27.06

ATOM
5236
O
PHE C
223
99.820
31.006
32.117
1.000
27.00

ATOM
5237
N
PRO C
224
101.451
32.202
33.097
1.000
27.86

ATOM
5238
CD
PRO C
224
101.553
33.223
32.041
1.000
27.73

ATOM
5239
CA
PRO C
224
102.399
32.439
34.187
1.000
29.28

ATOM
5240
CB
PRO C
224
103.372
33.462
33.601
1.000
32.92

ATOM
5241
CG
PRO C
224
102.618
34.157
32.523
1.000
29.32

ATOM
5242
C
PRO C
224
101.716
33.013
35.425
1.000
27.75

ATOM
5243
O
PRO C
224
100.771
33.787
35.301
1.000
23.30

ATOM
5244
N
SER C
225
102.188
32.606
36.593
1.000
25.01

ATOM
5245
CA
SER C
225
101.558
32.933
37.859
1.000
29.07

ATOM
5246
CB
SER C
225
102.016
31.948
38.947
1.000
37.20

ATOM
5247
OG
SER C
225
101.612
30.634
38.598
1.000
57.33

ATOM
5248
CB
SER C
225
101.858
34.350
38.315
1.000
29.02

ATOM
5249
O
SER C
225
102.663
34.588
39.219
1.000
31.13

ATOM
5250
N
ARG C
226
101.192
35.299
37.675
1.000
22.75

ATOM
5251
CA
ARG C
226
101.418
36.713
37.970
1.000
21.78

ATOM
5252
CB
ARG C
226
102.787
37.164
37.456
1.000
21.27

ATOM
5253
CG
ARG C
226
102.998
36.810
35.981
1.000
20.87

ATOM
5254
CD
ARG C
226
103.943
37.804
35.323
1.000
23.93

ATOM
5255
NE
ARG C
226
104.283
37.417
33.956
1.000
22.64

ATOM
5256
CZ
ARG C
226
103.702
37.904
32.866
1.000
29.11

ATOM
5257
NH1
ARG C
226
104.094
37.476
31.668
1.000
20.68

ATOM
5258
NH2
ARG C
226
102.735
38.808
32.972
1.000
20.52

ATOM
5259
C
ARG C
226
100.330
37.550
37.321
1.000
24.27

ATOM
5260
O
ARG C
226
99.580
37.031
36.486
1.000
26.38

ATOM
5261
N
LEU C
227
100.248
38.823
37.697
1.000
22.29

ATOM
5262
CA
LEU C
227
99.365
39.717
36.947
1.000
25.06

ATOM
5263
CB
LEU C
227
99.292
41.089
37.621
1.000
23.75

ATOM
5264
CG
LEU C
227
98.844
41.076
39.092
1.000
23.95

ATOM
5265
CD1
LEU C
227
98.975
42.444
39.742
1.000
21.02

ATOM
5266
CD2
LEU C
227
97.414
40.579
39.194
1.000
19.70

ATOM
5267
C
LEU C
227
99.875
39.829
35.514
1.000
26.87

ATOM
5268
O
LEU C
227
101.080
39.746
35.238
1.000
20.04

ATOM
5269
N
GLY C
228
98.964
40.039
34.562
1.000
24.87

ATOM
5270
CA
GLY C
228
99.408
40.279
33.192
1.000
18.72

ATOM
5271
C
GLY C
228
100.106
41.627
33.089
1.000
21.14

ATOM
5272
O
GLY C
228
99.800
42.564
33.835
1.000
21.52

ATOM
5273
N
ASP C
229
101.045
41.742
32.159
1.000
24.60

ATOM
5274
CA
ASP C
229
101.741
43.004
31.910
1.000
21.43

ATOM
5275
CB
ASP C
229
103.164
42.746
31.442
1.000
26.01

ATOM
5276
CG
ASP C
229
104.006
44.001
31.340
1.000
37.41

ATOM
5277
OD1
ASP C
229
105.238
43.880
31.526
1.000
53.25

ATOM
5278
OD2
ASP C
229
103.477
45.102
31.082
1.000
38.34

ATOM
5279
C
ASP C
229
100.973
43.799
30.860
1.000
19.57

ATOM
5280
O
ASP C
229
100.660
43.204
29.824
1.000
23.49

ATOM
5281
N
PRO C
230
100.661
45.059
31.112
1.000
22.69

ATOM
5282
CD
PRO C
230
100.998
45.823
32.326
1.000
23.91

ATOM
5283
CA
PRO C
230
99.893
45.861
30.152
1.000
21.64

ATOM
5284
CB
PRO C
230
100.031
47.287
30.691
1.000
23.94

ATOM
5285
CG
PRO C
230
100.194
47.090
32.168
1.000
24.54

ATOM
5286
C
PRO C
230
100.469
45.765
28.744
1.000
25.45

ATOM
5287
O
PRO C
230
99.706
45.781
27.779
1.000
25.01

ATOM
5288
N
ALA C
231
101.789
45.633
28.634
1.000
24.95

ATOM
5289
CA
ALA C
231
102.414
45.495
27.322
1.000
27.22

ATOM
5290
CB
ALA C
231
103.933
45.490
27.425
1.000
23.00

ATOM
5291
C
ALA C
231
101.924
44.231
26.614
1.000
25.34

ATOM
5292
O
ALA C
231
101.917
44.192
25.385
1.000
27.31

ATOM
5293
N
GLU C
232
101.523
43.222
27.375
1.000
23.62

ATOM
5294
CA
GLU C
232
100.996
41.976
26.806
1.000
21.90

ATOM
5295
CB
GLU C
232
100.999
40.864
27.853
1.000
21.70

ATOM
5296
CG
GLU C
232
102.395
40.453
28.301
1.000
24.49

ATOM
5297
CD
GLU C
232
102.451
39.569
29.525
1.000
22.86

ATOM
5298
OE1
GLU C
232
101.660
39.769
30.476
1.000
23.68

ATOM
5299
OE2
GLU C
232
103.296
38.648
29.576
1.000
22.83

ATOM
5300
C
GLU C
232
99.607
42.219
26.227
1.000
20.51

ATOM
5301
O
GLU C
232
99.202
41.633
25.226
1.000
21.77

ATOM
5302
N
TYR C
233
98.841
43.115
26.856
1.000
20.18

ATOM
5303
CA
TYR C
233
97.570
43.521
26.259
1.000
23.47

ATOM
5304
CB
TYR C
233
96.766
44.393
27.226
1.000
20.77

ATOM
5305
CG
TYR C
233
95.509
44.996
26.634
1.000
21.03

ATOM
5306
CD1
TYR C
233
94.302
44.305
26.635
1.000
19.12

ATOM
5307
CE1
TYR C
233
93.168
44.884
26.084
1.000
19.16

ATOM
5308
CD2
TYR C
233
95.521
46.266
26.069
1.000
17.67

ATOM
5309
CB2
TYR C
233
94.404
46.838
25.520
1.000
21.50

ATOM
5310
CZ
TYR C
233
93.215
46.140
25.530
1.000
20.40

ATOM
5311
OH
TYR C
233
92.105
46.738
24.972
1.000
20.20

ATOM
5312
C
TYR C
233
97.856
44.254
24.947
1.000
26.17

ATOM
5313
O
TYR C
233
97.257
44.012
23.905
1.000
24.88

ATOM
5314
N
ALA C
234
98.775
45.210
24.983
1.000
23.28

ATOM
5315
CA
ALA C
234
99.122
45.986
23.793
1.000
20.34

ATOM
5316
CE
ALA C
234
100.225
46.981
24.114
1.000
25.63

ATOM
5317
C
ALA C
234
99.527
45.064
22.646
1.000
20.70

ATOM
5318
O
ALA C
234
99.126
45.278
21.502
1.000
22.04

ATOM
5319
N
HIS C
235
100.323
44.045
22.979
1.000
21.74

ATOM
5320
CA
HIS C
235
100.803
43.110
21.969
1.000
22.45

ATOM
5321
CE
HIS C
235
101.734
42.052
22.566
1.000
20.97

ATOM
5322
CG
HIS C
235
102.042
40.900
21.653
1.000
23.06

ATOM
5323
CD2
HIS C
235
101.439
39.716
21.406
1.000
20.44

ATOM
5324
ND1
HIS C
235
103.151
40.917
20.829
1.000
29.37

ATOM
5325
CB1
HIS C
235
103.200
39.803
20.128
1.000
24.08

ATOM
5326
NE2
HIS C
235
102.168
39.049
20.453
1.000
23.74

ATOM
5327
C
HIS C
235
99.617
42.442
21.274
1.000
25.47

ATOM
5328
O
HIS C
235
99.652
42.256
20.057
1.000
19.63

ATOM
5329
N
LEU C
236
98.602
42.055
22.035
1.000
24.60

ATOM
5330
CA
LEU C
236
97.441
41.381
21.445
1.000
22.50

ATOM
5331
CB
LEU C
236
96.574
40.764
22.537
1.000
18.41

ATOM
5332
CG
LEU C
236
95.340
39.987
22.079
1.000
21.33

ATOM
5333
CD1
LEU C
236
95.711
38.877
21.105
1.000
17.49

ATOM
5334
CD2
LEU C
236
94.587
39.408
23.281
1.000
15.39

ATOM
5335
C
LEU C
236
96.631
42.339
20.576
1.000
22.47

ATOM
5336
O
LEU C
236
96.032
41.921
19.585
1.000
21.32

ATOM
5337
N
VAL C
237
96.603
43.614
20.927
1.000
21.37

ATOM
5338
CA
VAL C
237
95.941
44.639
20.133
1.000
23.21

ATOM
5339
CB
VAL C
237
96.008
46.029
20.800
1.000
24.40

ATOM
5340
CG1
VAL C
237
95.579
47.111
19.808
1.000
23.54

ATOM
5341
CG2
VAL C
237
95.158
46.088
22.064
1.000
21.30

ATOM
5342
C
VAL C
237
96.587
44.742
18.750
1.000
27.11

ATOM
5343
O
VAL C
237
95.920
44.818
17.718
1.000
20.91

ATOM
5344
N
GLN C
238
97.920
44.767
18.730
1.000
23.43

ATOM
5345
CA
GLN C
238
98.648
44.860
17.471
1.000
20.96

ATOM
5346
CB
GLN C
238
100.156
44.994
17.711
1.000
25.92

ATOM
5347
CG
GLN C
238
100.944
45.076
16.406
1.000
34.72

ATOM
5348
CD
GLN C
238
102.331
45.670
16.621
1.000
45.75

ATOM
5349
CG1
GLN C
238
102.671
46.122
17.718
1.000
42.99

ATOM
5350
NE2
GLN C
238
103.139
45.672
15.565
1.000
37.12

ATOM
5351
C
GLN C
238
98.406
43.631
16.610
1.000
17.47

ATOM
5352
O
GLN C
238
98.163
43.729
15.409
1.000
31.42

ATOM
5353
N
ALA C
239
98.471
42.462
17.226
1.000
13.40

ATOM
5354
CA
ALA C
239
98.173
41.199
16.561
1.000
17.82

ATOM
5355
CB
ALA C
239
98.167
40.051
17.556
1.000
20.85

ATOM
5356
C
ALA C
239
96.831
41.264
15.840
1.000
23.82

ATOM
5357
O
ALA C
239
96.671
40.812
14.702
1.000
22.62

ATOM
5358
N
ILE C
240
95.851
41.848
16.538
1.000
21.62

ATOM
5359
CA
ILE C
240
94.500
41.902
15.974
1.000
25.07

ATOM
5360
CE
ILE C
240
93.479
42.245
17.069
1.000
24.15

ATOM
5361
CG2
ILE C
240
92.127
42.582
16.473
1.000
20.46

ATOM
5362
CD1
ILE C
240
93.340
41.152
18.139
1.000
17.17

ATOM
5363
CD1
ILE C
240
92.579
41.637
19.357
1.000
21.22

ATOM
5364
C
ILE C
240
94.461
42.901
14.826
1.000
25.22

ATOM
5365
O
ILE C
240
93.910
42.633
13.759
1.000
21.79

ATOM
5366
N
ILE C
241
95.074
44.064
15.038
1.000
20.24

ATOM
5367
CA
ILE C
241
95.171
45.059
13.974
1.000
25.86

ATOM
5368
CB
ILE C
241
95.974
46.291
14.416
1.000
27.53

ATOM
5369
CG2
ILE C
241
96.380
47.147
13.218
1.000
24.99

ATOM
5370
CG1
ILE C
241
95.266
47.162
15.465
1.000
23.00

ATOM
5371
CD1
ILE C
241
96.201
48.192
16.082
1.000
20.65

ATOM
5372
C
ILE C
241
95.810
44.445
12.731
1.000
27.42

ATOM
5373
O
ILE C
241
95.363
44.672
11.603
1.000
25.67

ATOM
5374
N
GLU C
242
96.864
43.656
12.910
1.000
21.24

ATOM
5375
CA
GLU C
242
97.615
43.141
11.764
1.000
23.07

ATOM
5376
CE
GLU C
242
98.992
42.649
12.234
1.000
21.75

ATOM
5377
CG
GLU C
242
99.880
43.739
12.813
1.000
23.24

ATOM
5378
CD
GLU C
242
101.247
43.211
13.211
1.000
32.86

ATOM
5379
OE1
GLU C
242
102.164
44.031
13.422
1.000
41.93

ATOM
5380
OE2
GLU C
242
101.415
41.976
13.324
1.000
38.32

ATOM
5381
C
GLU C
242
96.896
42.024
11.021
1.000
27.62

ATOM
5382
O
GLU C
242
97.032
41.898
9.796
1.000
25.36

ATOM
5383
N
ASN C
243
96.135
41.200
11.737
1.000
20.54

ATOM
5384
CA
ASN C
243
95.539
40.009
11.155
1.000
22.70

ATOM
5385
CE
ASN C
243
95.428
38.910
12.223
1.000
20.67

ATOM
5386
CG
ASN C
243
95.172
37.550
11.608
1.000
23.57

ATOM
5387
OD1
ASN C
243
94.183
37.346
10.889
1.000
21.00

ATOM
5388
ND2
ASN C
243
96.072
36.619
11.899
1.000
16.27

ATOM
5389
C
ASN C
243
94.167
40.275
10.537
1.000
29.01

ATOM
5390
O
ASN C
243
93.188
40.455
11.263
1.000
22.16

ATOM
5391
N
PRO C
244
94.109
40.284
9.210
1.000
26.89

ATOM
5392
CD
PRO C
244
95.226
39.922
8.304
1.000
24.01

ATOM
5393
CA
PRO C
244
92.906
40.668
8.481
1.000
21.88

ATOM
5394
CB
PRO C
244
93.357
40.639
7.003
1.000
24.45

ATOM
5395
CG
PRO C
244
94.849
40.632
7.029
1.000
26.59

ATOM
5396
C
PRO C
244
91.731
39.713
8.622
1.000
21.54

ATOM
5397
O
PRO C
244
90.608
40.076
8.233
1.000
23.93

ATOM
5398
N
PHE C
245
91.930
38.505
9.143
1.000
21.82

ATOM
5399
CA
PHE C
245
90.804
37.570
9.215
1.000
19.75

ATOM
5400
CE
PHE C
245
91.205
36.179
8.726
1.000
21.43

ATOM
5401
CG
PHE C
245
90.140
35.467
7.909
1.000
19.34

ATOM
5402
CD1
PHE C
245
89.744
34.179
8.236
1.000
17.81

ATOM
5403
CD2
PHE C
245
89.551
36.074
6.816
1.000
18.35

ATOM
5404
CE1
PHE C
245
88.777
33.508
7.502
1.000
20.11

ATOM
5405
CE2
PHE C
245
88.574
35.423
6.080
1.000
16.76

ATOM
5406
CZ
PHE C
245
88.181
34.145
6.416
1.000
17.96

ATOM
5407
C
PHE C
245
90.221
37.480
10.620
1.000
24.50

ATOM
5408
O
PHE C
245
89.310
36.688
10.858
1.000
20.21

ATOM
5409
N
LEU C
246
90.718
38.285
11.553
1.000
24.14

ATOM
5410
CA
LEU C
246
90.183
38.270
12.917
1.000
25.12

ATOM
5411
CB
LEU C
246
91.275
38.644
13.922
1.000
21.84

ATOM
5412
CG
LEU C
246
92.216
37.516
14.350
1.000
22.81

ATOM
5413
CD1
LEU C
246
93.366
38.063
15.192
1.000
22.23

ATOM
5414
CD2
LEU C
246
91.469
36.427
15.117
1.000
18.03

ATOM
5415
C
LEU C
246
88.987
39.208
13.042
1.000
18.79

ATOM
5416
O
LEU C
246
89.135
40.426
12.967
1.000
17.92

ATOM
5417
N
ASN C
247
87.801
38.631
13.232
1.000
19.81

ATOM
5418
CA
ASN C
247
86.606
39.468
13.280
1.000
22.54

ATOM
5419
CE
ASN C
247
86.151
39.746
11.839
1.000
20.64

ATOM
5420
CG
ASN C
247
85.230
40.938
11.705
1.000
27.10

ATOM
5421
OD1
ASN C
247
84.935
41.661
12.663
1.000
18.27

ATOM
5422
ND2
ASN C
247
84.767
41.143
10.468
1.000
23.10

ATOM
5423
C
ASN C
247
85.473
38.824
14.070
1.000
17.99

ATOM
5424
O
ASN C
247
85.265
37.616
14.005
1.000
16.75

ATOM
5425
N
GLY C
248
84.724
39.640
14.801
1.000
19.04

ATOM
5426
CA
GLY C
248
83.533
39.197
15.497
1.000
19.49

ATOM
5427
C
GLY C
248
83.815
38.330
16.704
1.000
19.73

ATOM
5428
O
GLY C
248
82.903
37.601
17.111
1.000
17.58

ATOM
5429
N
GLU C
249
85.017
38.381
17.268
1.000
15.98

ATOM
5430
CA
GLU C
249
85.389
37.405
18.302
1.000
16.41

ATOM
5431
CB
GLU C
249
86.452
36.453
17.759
1.000
18.31

ATOM
5432
CG
GLU C
249
87.296
35.682
18.759
1.000
19.50

ATOM
5433
CD
GLU C
249
86.549
34.567
19.453
1.000
21.59

ATOM
5434
OE1
GLU C
249
87.127
33.491
19.715
1.000
24.29

ATOM
5435
OE2
GLU C
249
85.352
34.729
19.758
1.000
21.15

ATOM
5436
C
GLU C
249
85.860
38.084
19.582
1.000
16.54

ATOM
5437
O
GLU C
249
86.310
39.231
19.581
1.000
20.08

ATOM
5438
N
VAL C
250
85.741
37.363
20.688
1.000
19.50

ATOM
5439
CA
VAL C
250
86.236
37.744
22.003
1.000
14.75

ATOM
5440
CB
VAL C
250
85.148
37.588
23.088
1.000
23.09

ATOM
5441
CD1
VAL C
250
85.708
37.916
24.463
1.000
20.21

ATOM
5442
CG2
VAL C
250
83.952
38.474
22.781
1.000
21.17

ATOM
5443
C
VAL C
250
87.427
36.864
22.366
1.000
16.06

ATOM
5444
O
VAL C
250
87.336
35.642
22.225
1.000
17.76

ATOM
5445
N
ILE C
251
88.533
37.440
22.813
1.000
18.46

ATOM
5446
CA
ILE C
251
89.715
36.640
23.141
1.000
19.52

ATOM
5447
CB
ILE C
251
90.914
37.049
22.261
1.000
19.31

ATOM
5448
CG2
ILE C
251
92.214
36.427
22.753
1.000
17.15

ATOM
5449
CG1
ILE C
251
90.679
36.759
20.775
1.000
17.56

ATOM
5450
CD1
ILE C
251
91.777
37.281
19.878
1.000
19.77

ATOM
5451
C
ILE C
251
90.104
36.808
24.602
1.000
17.13

ATOM
5452
O
ILE C
251
90.381
37.941
25.018
1.000
20.67

ATOM
5453
N
ARG C
252
90.135
35.707
25.349
1.000
17.57

ATOM
5454
CA
ARG C
252
90.583
35.804
26.737
1.000
20.50

ATOM
5455
CB
ARG C
252
90.206
34.567
27.548
1.000
20.54

ATOM
5456
CG
ARG C
252
88.710
34.394
27.774
1.000
23.09

ATOM
5457
CD
ARG C
252
88.441
33.054
28.452
1.000
21.26

ATOM
5458
NE
ARG C
252
88.769
33.163
29.873
1.000
20.67

ATOM
5459
CZ
ARG C
252
87.918
33.016
30.878
1.000
20.65

ATOM
5460
NE1
ARG C
252
88.351
33.143
32.127
1.000
16.60

ATOM
5461
NH2
ARG C
252
86.649
32.746
30.628
1.000
20.79

ATOM
5462
C
ARG C
252
92.099
35.983
26.807
1.000
19.07

ATOM
5463
O
ARG C
252
92.836
35.200
26.213
1.000
15.41

ATOM
5464
N
LEU C
253
92.545
36.990
27.541
1.000
18.07

ATOM
5465
CA
LEU C
253
93.977
37.197
27.787
1.000
17.32

ATOM
5466
CB
LEU C
253
94.418
38.517
27.174
1.000
15.25

ATOM
5467
CG
LEU C
253
95.903
38.874
27.253
1.000
21.28

ATOM
5468
CD1
LEU C
253
96.755
37.831
26.548
1.000
15.73

ATOM
5469
CD2
LEU C
253
96.176
40.255
26.668
1.000
15.80

ATOM
5470
C
LEU C
253
94.202
37.152
29.293
1.000
20.34

ATOM
5471
O
LEU C
253
94.062
38.178
29.959
1.000
18.61

ATOM
5472
N
ASP C
254
94.497
35.971
29.835
1.000
18.39

ATOM
5473
CA
ASP C
254
94.326
35.800
31.271
1.000
19.65

ATOM
5474
CB
ASP C
254
92.830
35.489
31.527
1.000
16.16

ATOM
5475
CG
ASP C
254
92.380
34.224
30.832
1.000
21.05

ATOM
5476
OD1
ASP C
254
93.218
33.505
30.235
1.000
19.41

ATOM
5477
OD2
ASP C
254
91.166
33.922
30.868
1.000
21.82

ATOM
5478
C
ASP C
254
95.142
34.697
31.910
1.000
21.58

ATOM
5479
O
ASP C
254
94.835
34.302
33.044
1.000
21.93

ATOM
S480
N
GLY C
255
96.168
34.157
31.255
1.000
19.98

ATOM
5481
CA
GLY C
255
97.016
33.180
31.921
1.000
13.04

ATOM
5482
C
GLY C
255
96.292
31.902
32.291
1.000
23.38

ATOM
5483
O
GLY C
255
96.812
31.094
33.075
1.000
21.76

ATOM
5484
N
ALA C
256
95.114
31.704
31.719
1.000
23.49

ATOM
5485
CA
ALA C
256
94.304
30.505
31.855
1.000
20.27

ATOM
5486
CB
ALA C
256
95.173
29.251
31.752
1.000
18.94

ATOM
5487
C
ALA C
256
93.516
30.495
33.165
1.000
18.75

ATOM
5488
O
ALA C
256
92.982
29.464
33.581
1.000
17.98

ATOM
5489
N
ILE C
257
93.419
31.643
33.826
1.000
15.35

ATOM
5490
CA
ILE C
257
92.646
31.696
35.059
1.000
21.12

ATOM
5491
CB
ILE C
257
92.908
33.007
35.832
1.000
21.24

ATOM
5492
CG2
ILE C
257
92.148
34.173
35.216
1.000
23.06

ATOM
5493
CG1
ILE C
257
92.613
32.911
37.335
1.000
19.13

ATOM
5494
CD1
ILE C
257
92.930
34.191
38.084
1.000
19.06

ATOM
5495
C
ILE C
257
91.155
31.560
34.783
1.000
25.65

ATOM
5496
O
ILE C
257
90.677
31.973
33.729
1.000
19.69

ATOM
5497
N
ARG C
258
90.438
30.984
35.738
1.000
24.39

ATOM
5498
CA
ARG C
258
88.975
30.985
35.778
1.000
18.78

ATOM
5499
CB
ARG C
258
88.376
29.617
35.523
1.000
17.15

ATOM
5500
CG
ARG C
258
88.687
28.985
34.162
1.000
21.49

ATOM
5501
CD
ARG C
258
88.076
29.820
33.052
1.000
23.58

ATOM
5502
NE
ARG C
258
88.246
29.289
31.709
1.000
23.32

ATOM
5503
CZ
ARG C
258
89.257
29.573
30.900
1.000
21.26

ATOM
5504
NE1
ARG C
258
89.306
29.031
29.691
1.000
17.94

ATOM
5505
NH2
ARG C
258
90.225
30.393
31.296
1.000
17.93

ATOM
5506
C
ARG C
258
88.576
31.524
37.157
1.000
22.89

ATOM
5507
O
ARG C
258
88.988
30.986
38.188
1.000
18.51

ATOM
5508
N
MET C
259
87.810
32.604
37.219
1.000
22.41

ATOM
5509
CA
MET C
259
87.600
33.245
38.516
1.000
22.89

ATOM
5510
CB
MET C
259
87.145
34.696
38.321
1.000
23.35

ATOM
5511
CG
MET C
259
88.029
35.503
37.385
1.000
27.42

ATOM
5512
SD
MET C
259
89.757
35.470
37.881
1.000
26.67

ATOM
5513
CE
MET C
259
89.731
36.436
39.387
1.000
27.72

ATOM
5514
C
MET C
259
86.575
32.521
39.377
1.000
26.70

ATOM
5515
O
MET C
259
85.478
32.178
38.947
1.000
25.54

ATOM
5516
N
GLN C
260
86.946
32.305
40.631
1.000
30.71

ATOM
5517
CA
GLN C
260
86.079
31.691
41.635
1.000
25.02

ATOM
5518
CB
GLN C
260
86.967
30.983
42.653
1.000
27.72

ATOM
5519
CG
GLN C
260
87.077
29.489
42.447
1.000
41.57

ATOM
5520
CD
GLN C
260
86.158
28.897
41.402
1.000
49.91

ATOM
5521
OE1
GLN C
260
85.118
28.302
41.686
1.000
38.22

ATOM
5522
NE2
GLN C
260
86.536
29.040
40.134
1.000
67.27

ATOM
5523
C
GLN C
260
85.182
32.743
42.277
1.000
25.92

ATOM
5524
O
GLN C
260
85.403
33.942
42.054
1.000
24.17

ATOM
5525
N
PRO C
261
84.165
32.365
43.041
1.000
23.99

ATOM
5526
CD
PRO C
261
83.744
30.987
43.359
1.000
24.97

ATOM
5527
CA
PRO C
261
83.289
33.372
43.662
1.000
22.83

ATOM
5528
CB
PRO C
261
82.411
32.512
44.584
1.000
24.86

ATOM
5529
CG
PRO C
261
82.334
31.209
43.849
1.000
25.45

ATOM
5530
C
PRO C
261
84.067
34.409
44.457
1.000
22.13

ATOM
5531
OT1
PRO C
261
85.046
33.998
45.112
1.000
24.75

ATOM
5532
OT2
PRO C
261
83.742
35.620
44.416
1.000
17.73

ATOM
5533
PN
LIG C
262
92.798
49.871
33.096
1.000
25.36

ATOM
5534
O1N
LIG C
262
93.331
48.582
33.757
1.000
23.33

ATOM
5535
O2N
LIG C
262
93.836
50.420
32.122
1.000
22.34

ATOM
5536
O3P
LIG C
262
92.507
50.871
34.244
1.000
30.26

ATOM
5537
O5M
LIG C
262
91.425
49.583
32.332
1.000
24.41

ATOM
5538
C5M
LIG C
262
91.307
49.563
30.881
1.000
31.36

ATOM
5539
C4M
LIG C
262
90.121
48.645
30.417
1.000
32.73

ATOM
5540
O4M
LIG C
262
90.448
47.263
30.689
1.000
32.21

ATOM
5541
C3M
LIG C
262
88.788
48.924
31.157
1.000
30.15

ATOM
5542
O3M
LIG C
262
87.691
48.676
30.252
1.000
18.36

ATOM
5543
C2M
LIG C
262
88.844
47.876
32.303
1.000
22.20

ATOM
5544
O2M
LIG C
262
87.499
47.638
32.766
1.000
20.27

ATOM
5545
C1M
LIG C
262
89.414
46.665
31.519
1.000
26.13

ATOM
5546
N1N
LIG C
262
89.909
45.522
32.334
1.000
20.70

ATOM
5547
C6N
LIG C
262
89.174
44.261
32.234
1.000
15.32

ATOM
5548
C5N
LIG C
262
89.567
43.176
32.919
1.000
17.17

ATOM
5549
C4N
LIG C
262
90.602
43.316
34.065
1.000
24.88

ATOM
5550
C3N
LIG C
262
91.525
44.563
33.874
1.000
22.18

ATOM
5551
C2N
LIG C
262
91.080
45.645
33.211
1.000
20.26

ATOM
5552
C7N
LIG C
262
92.742
44.623
34.786
1.000
15.83

ATOM
5553
O7N
LIG C
262
93.089
43.625
35.432
1.000
23.87

ATOM
5554
N7N
LIG C
262
93.389
45.767
34.842
1.000
19.65

ATOM
5555
PA
LIG C
262
92.957
52.330
34.413
1.000
25.29

ATOM
5556
O1A
LIG C
262
92.097
52.960
35.526
1.000
22.89

ATOM
5557
O2A
LIG C
262
94.442
52.459
34.747
1.000
23.14

ATOM
5558
O5B
LIG C
262
92.661
53.176
33.089
1.000
24.87

ATOM
5559
C5B
LIG C
262
91.287
53.396
32.644
1.000
23.91

ATOM
5560
C4B
LIG C
262
91.188
54.791
31.966
1.000
22.53

ATOM
5561
O4B
LIG C
262
89.830
55.059
31.517
1.000
24.50

ATOM
5562
C3B
LIG C
262
91.629
55.950
32.901
1.000
25.27

ATOM
5563
O3B
LIG C
262
92.747
56.674
32.359
1.000
23.62

ATOM
5564
C2B
LIG C
262
90.370
56.828
32.945
1.000
24.04

ATOM
5565
O2B
LIG C
262
90.615
58.207
33.212
1.000
22.80

ATOM
5566
C1B
LIG C
262
89.689
56.509
31.591
1.000
25.73

ATOM
5567
N9A
LIG C
262
88.235
56.865
31.670
1.000
25.45

ATOM
5568
C4A
LIG C
262
87.449
57.586
30.775
1.000
27.43

ATOM
5569
N3A
LIG C
262
87.701
58.238
29.493
1.000
22.57

ATOM
5570
C2A
LIG C
262
86.659
58.824
28.955
1.000
29.08

ATOM
5571
N1A
LIG C
262
85.421
58.916
29.403
1.000
34.71

ATOM
5572
C6A
LIG C
262
85.094
58.361
30.556
1.000
25.70

ATOM
5573
C5A
LIG C
262
86.096
57.654
31.327
1.000
25.70

ATOM
5574
N7A
LIG C
262
86.008
56.994
32.545
1.000
27.04

ATOM
5575
C8A
LIG C
262
87.303
56.572
32.659
1.000
22.87

ATOM
5576
N6A
LIG C
262
83.874
58.533
31.055
1.000
21.84

ATOM
5577
C
LIG C
262
87.768
44.396
41.110
1.000
44.98

ATOM
5578
C1
LIG C
262
86.511
43.552
41.617
1.000
48.30

ATOM
5579
N
LIG C
262
86.430
43.126
42.940
1.000
48.50

ATOM
5580
O
LIG C
262
85.605
43.293
40.797
1.000
65.58

ATOM
5581
C2
LIG C
262
87.563
43.453
43.877
1.000
51.16

ATOM
5582
C3
LIG C
262
88.661
42.332
43.896
1.000
52.13

ATOM
5583
C4
LIG C
262
85.251
42.324
43.394
1.000
42.63

ATOM
5584
CB
LIG C
262
85.547
40.804
43.209
1.000
53.20

ATOM
5585
C6
LIG C
262
86.952
40.386
43.681
1.000
61.97

ATOM
5586
C7
LIG C
262
88.182
41.098
43.084
1.000
58.52

ATOM
5587
C8
LIG C
262
87.768
45.903
41.567
1.000
36.21

ATOM
5588
C9
LIG C
262
89.004
46.569
41.608
1.000
38.49

ATOM
5589
C10
LIG C
262
89.074
47.902
41.999
1.000
36.24

ATOM
5590
C11
LIG C
262
87.912
48.581
42.357
1.000
39.07

ATOM
5591
C12
LIG C
262
86.681
47.933
42.332
1.000
39.17

ATOM
5592
C13
LIG C
262
86.610
46.607
41.906
1.000
37.44

ATOM
5593
C15
LIG C
262
87.326
45.081
38.785
1.000
36.27

ATOM
5594
N1
LIG C
262
87.409
45.213
37.494
1.000
33.45

ATOM
5595
C16
LIG C
262
88.460
44.477
36.824
1.000
31.46

ATOM
5596
C17
LIG C
262
89.357
43.657
37.546
1.000
38.18

ATOM
5597
C18
LIG C
262
89.189
43.536
39.079
1.000
40.16

ATOM
5598
N2
LIG C
262
88.040
44.343
39.596
1.000
42.60

ATOM
5599
S
LIG C
262
90.274
42.506
40.037
1.000
37.80

ATOM
5600
C19
LIG C
262
90.242
43.067
36.680
1.000
36.22

ATOM
5601
N3
LIG C
262
89.906
43.510
35.401
1.000
27.95

ATOM
5602
N4
LIG C
262
88.875
44.403
35.1515
1.000
28.88

ATOM
5603
CB
SER D
7
53.786
21.308
43.599
1.000
44.31

ATOM
5604
CB
SER D
7
55.174
23.307
43.111
1.000
42.72

ATOM
5605
O
SER D
7
55.885
23.720
44.027
1.000
47.89

ATOM
5606
N
SER D
7
56.230
21.111
43.360
1.000
57.68

ATOM
5607
CA
SER D
7
55.040
21.806
42.892
1.000
49.63

ATOM
5608
N
VAL D
8
54.494
24.107
42.293
1.000
38.26

ATOM
5609
CA
VAL D
8
54.523
25.551
42.518
1.000
36.32

ATOM
5610
CB
VAL D
8
54.535
26.343
41.198
1.000
39.50

ATOM
5611
CD1
VAL D
8
55.802
26.044
40.408
1.000
35.22

ATOM
5612
CG2
VAL D
8
53.297
26.026
40.374
1.000
29.19

ATOM
5613
C
VAL D
8
53.322
25.979
43.354
1.000
30.87

ATOM
5614
O
VAL D
8
53.141
27.156
43.662
1.000
32.37

ATOM
5615
N
LYS D
9
52.480
25.013
43.716
1.000
26.77

ATOM
5616
CA
LYS D
9
51.272
25.363
44.468
1.000
29.29

ATOM
5617
CB
LYS D
9
50.441
24.118
44.724
1.000
28.07

ATOM
5618
C
LYS D
9
51.638
26.078
45.761
1.000
31.62

ATOM
5619
O
LYS D
9
52.452
25.599
46.552
1.000
32.26

ATOM
5620
N
GLY D
10
51.051
27.248
45.989
1.000
34.81

ATOM
5621
CA
GLY D
10
51.322
28.015
47.187
1.000
30.81

ATOM
5622
C
GLY D
10
52.453
29.007
47.078
1.000
33.23

ATOM
5623
O
GLY D
10
52.595
29.858
47.972
1.000
38.22

ATOM
5624
N
LEU D
11
53.281
28.950
46.032
1.000
29.06

ATOM
5625
CA
LEU D
11
54.341
29.952
45.907
1.000
27.91

ATOM
5626
CB
LEU D
11
55.443
29.526
44.933
1.000
26.09

ATOM
5627
CG
LEU D
11
56.089
28.165
45.194
1.000
33.28

ATOM
5628
CD1
LEU D
11
57.196
27.900
44.183
1.000
37.73

ATOM
5629
CD2
LEU D
11
56.621
28.095
46.615
1.000
29.82

ATOM
5630
C
LEU D
11
53.763
31.284
45.430
1.000
24.63

ATOM
5631
O
LEU D
11
52.771
31.295
44.706
1.000
23.43

ATOM
5632
N
VAL D
12
54.404
32.369
45.829
1.000
21.94

ATOM
5633
CA
VAL D
12
54.083
33.706
45.366
1.000
23.89

ATOM
5634
CB
VAL D
12
53.982
34.683
46.548
1.000
26.77

ATOM
5635
CG1
VAL D
12
53.686
36.091
46.052
1.000
23.82

ATOM
5636
CG2
VAL D
12
52.918
34.211
47.534
1.000
26.90

ATOM
5637
C
VAL D
12
55.133
34.211
44.377
1.000
29.60

ATOM
5638
O
VAL D
12
56.302
34.357
44.727
1.000
26.47

ATOM
5639
N
ALA D
13
54.713
34.480
43.144
1.000
29.25

ATOM
5640
CA
ALA D
13
55.601
34.896
42.073
1.000
23.99

ATOM
5641
CB
ALA D
13
55.430
33.937
40.899
1.000
23.74

ATOM
5642
C
ALA D
13
55.353
36.314
41.589
1.000
25.67

ATOM
5643
O
ALA D
13
54.228
36.704
41.266
1.000
30.62

ATOM
5644
N
VAL D
14
56.414
37.106
41.512
1.000
19.86

ATOM
5645
CA
VAL D
14
56.311
38.445
40.929
1.000
21.74

ATOM
5646
CB
VAL D
14
57.112
39.480
41.716
1.000
24.02

ATOM
5647
CD1
VAL D
14
57.244
40.807
40.988
1.000
22.87

ATOM
5648
CG2
VAL D
14
56.442
39.698
43.074
1.000
26.38

ATOM
5649
C
VAL D
14
56.791
38.337
39.483
1.000
28.01

ATOM
5650
O
VAL D
14
57.918
37.883
39.272
1.000
27.09

ATOM
5651
N
ILE D
15
55.940
38.706
38.537
1.000
23.88

ATOM
5652
CA
ILE D
15
56.238
38.541
37.107
1.000
22.25

ATOM
5653
CB
ILE D
15
55.209
37.576
36.480
1.000
24.05

ATOM
5654
CG2
ILE D
15
55.384
37.441
34.975
1.000
24.05

ATOM
5655
CD1
ILE D
15
55.217
36.202
37.157
1.000
25.78

ATOM
5656
CD1
ILE D
15
54.092
35.286
36.735
1.000
27.73

ATOM
5657
C
ILE D
15
56.236
39.867
36.377
1.000
23.91

ATOM
5658
O
ILE D
15
55.197
40.468
36.084
1.000
22.19

ATOM
5659
N
THR D
16
57.422
40.381
36.057
1.000
22.27

ATOM
5660
CA
THR D
16
57.473
41.647
35.332
1.000
21.40

ATOM
5661
CB
THR D
16
58.852
42.310
35.441
1.000
22.25

ATOM
5662
OD1
THR D
16
59.739
41.705
34.490
1.000
20.62

ATOM
5663
CG2
THR D
16
59.449
42.046
36.817
1.000
18.29

ATOM
5664
C
THR D
16
57.118
41.385
33.869
1.000
20.63

ATOM
5665
O
THR D
16
57.369
40.282
33.371
1.000
22.61

ATOM
5666
N
GLY D
17
56.532
42.383
33.216
1.000
21.88

ATOM
5667
CA
GLY D
17
56.018
42.192
31.864
1.000
23.48

ATOM
5668
C
GLY D
17
54.858
41.203
31.908
1.000
26.78

ATOM
5669
O
GLY D
17
54.552
40.526
30.929
1.000
21.03

ATOM
5670
N
GLY D
18
54.204
41.113
33.073
1.000
24.25

ATOM
5671
CA
GLY D
18
53.134
40.161
33.270
1.000
20.46

ATOM
5672
C
GLY D
18
51.874
40.412
32.475
1.000
23.10

ATOM
5673
O
GLY D
18
51.018
39.524
32.358
1.000
23.13

ATOM
5674
N
ALA D
19
51.687
41.600
31.895
1.000
23.45

ATOM
5675
CA
ALA D
19
50.447
41.865
31.168
1.000
23.54

ATOM
5676
CB
ALA D
19
50.253
43.372
31.030
1.000
20.54

ATOM
5677
C
ALA D
19
50.413
41.221
29.793
1.000
30.19

ATOM
5678
O
ALA D
19
49.368
41.176
29.136
1.000
31.79

ATOM
5679
N
SER D
20
51.542
40.719
29.294
1.000
26.00

ATOM
5680
CA
SER D
20
51.553
40.290
27.891
1.000
25.37

ATOM
5681
CB
SER D
20
51.882
41.515
27.031
1.000
27.24

ATOM
5682
OG
SER D
20
52.044
41.220
25.656
1.000
28.53

ATOM
5683
C
SER D
20
52.538
39.156
27.637
1.000
29.51

ATOM
5684
O
SER D
20
53.405
38.868
28.468
1.000
26.87

ATOM
5685
N
GLY D
21
52.401
38.522
26.478
1.000
26.73

ATOM
5686
CA
GLY D
21
53.282
37.503
25.962
1.000
23.45

ATOM
5687
C
GLY D
21
53.811
36.496
26.953
1.000
27.95

ATOM
5688
O
GLY D
21
53.075
35.789
27.642
1.000
22.21

ATOM
5689
N
LEU D
22
55.138
36.386
27.043
1.000
23.99

ATOM
5690
CA
LEU D
22
55.762
35.360
27.868
1.000
20.60

ATOM
5691
CB
LEU D
22
57.284
35.376
27.669
1.000
21.35

ATOM
5692
CG
LEU D
22
57.781
35.299
26.219
1.000
20.42

ATOM
5693
CD1
LEU D
22
59.304
35.218
26.169
1.000
17.83

ATOM
5694
CD2
LEU D
22
57.149
34.113
25.507
1.000
17.30

ATOM
5695
C
LEU D
22
55.418
35.543
29.342
1.000
18.64

ATOM
5696
O
LEU D
22
55.110
34.564
30.024
1.000
23.17

ATOM
5697
N
GLY D
23
55.470
36.772
29.837
1.000
20.39

ATOM
5698
CA
GLY D
23
55.160
37.003
31.250
1.000
26.89

ATOM
5699
C
GLY D
23
53.729
36.587
31.565
1.000
28.07

ATOM
5700
O
GLY D
23
53.461
35.908
32.559
1.000
23.44

ATOM
5701
N
LEU D
24
52.798
36.985
30.692
1.000
20.84

ATOM
5702
CA
LEU D
24
51.399
36.626
30.897
1.000
20.18

ATOM
5703
CB
LEU D
24
50.506
37.238
29.813
1.000
20.69

ATOM
5704
CG
LEU D
24
49.044
36.782
29.835
1.000
23.66

ATOM
5705
CD1
LEU D
24
48.396
37.166
31.159
1.000
22.35

ATOM
5706
CD2
LEU D
24
48.263
37.369
28.667
1.000
23.89

ATOM
5707
C
LEU D
24
51.211
35.116
30.911
1.000
23.44

ATOM
5708
O
LEU D
24
50.522
34.570
31.770
1.000
23.82

ATOM
5709
N
ALA D
25
51.827
34.444
29.936
1.000
25.43

ATOM
5710
CA
ALA D
25
51.716
32.995
29.824
1.000
20.00

ATOM
5711
CB
ALA D
25
52.417
32.500
28.560
1.000
22.34

ATOM
5712
C
ALA D
25
52.290
32.296
31.049
1.000
24.36

ATOM
5713
O
ALA D
25
51.801
31.264
31.514
1.000
26.51

ATOM
5714
N
THR D
26
53.360
32.880
31.582
1.000
24.33

ATOM
5715
CA
THR D
26
53.939
32.353
32.816
1.000
22.92

ATOM
5716
CB
THR D
26
55.245
33.096
33.133
1.000
25.10

ATOM
5717
OG1
THR D
26
56.140
32.896
32.023
1.000
22.29

ATOM
5718
CG2
THR D
26
55.950
32.532
34.356
1.000
18.54

ATOM
5719
C
THR D
26
52.926
32.461
33.948
1.000
21.41

ATOM
5720
O
THR D
26
52.680
31.516
34.693
1.000
25.68

ATOM
5721
N
ALA D
27
52.308
33.630
34.070
1.000
21.76

ATOM
5722
CA
ALA D
27
51.305
33.847
35.110
1.000
25.16

ATOM
5723
CB
ALA D
27
50.825
35.288
35.048
1.000
26.09

ATOM
5724
C
ALA D
27
50.158
32.863
34.969
1.000
27.42

ATOM
5725
O
ALA D
27
49.716
32.221
35.925
1.000
23.96

ATOM
5726
N
GLU D
28
49.668
32.736
33.740
1.000
23.93

ATOM
5727
CA
GLU D
28
48.597
31.791
33.452
1.000
26.72

ATOM
5728
CB
GLU D
28
48.315
31.748
31.938
1.000
24.65

ATOM
5729
CG
GLU D
28
47.483
32.934
31.478
1.000
29.35

ATOM
5730
CD
GLU D
28
47.321
33.034
29.978
1.000
36.70

ATOM
5731
OE1
GLU D
28
46.571
33.939
29.548
1.000
40.71

ATOM
5732
OE2
GLU D
28
47.928
32.235
29.233
1.000
41.27

ATOM
5733
C
GLU D
28
48.941
30.392
33.936
1.000
29.67

ATOM
5734
O
GLU D
28
48.133
29.698
34.550
1.000
23.91

ATOM
5735
N
ARG D
29
50.172
29.962
33.633
1.000
26.23

ATOM
5736
CA
ARG D
29
50.523
28.585
33.958
1.000
23.90

ATOM
5737
CB
ARG D
29
51.803
28.148
33.242
1.000
23.31

ATOM
5738
CG
ARG D
29
52.083
26.668
33.457
1.000
25.31

ATOM
5739
CD
ARG D
29
53.346
26.249
32.723
1.000
26.40

ATOM
5740
NE
ARG D
29
53.683
24.857
33.006
1.000
26.23

ATOM
5741
CZ
ARG D
29
53.139
23.821
32.384
1.000
30.28

ATOM
5742
NE1
ARG D
29
53.514
22.595
32.717
1.000
31.68

ATOM
5743
NH2
ARG D
29
52.228
23.996
31.437
1.000
28.63

ATOM
5744
C
ARG D
29
50.683
28.409
35.458
1.000
28.09

ATOM
5745
O
ARG D
29
50.170
27.451
36.043
1.000
34.40

ATOM
5746
N
LEU D
30
51.387
29.336
36.106
1.000
23.92

ATOM
5747
CA
LEU 0
30
51.611
29.157
37.541
1.000
25.83

ATOM
5748
CE
LEU D
30
52.632
30.169
38.042
1.000
28.15

ATOM
5749
CG
LEU D
30
54.051
30.067
37.460
1.000
26.33

ATOM
5750
CD1
LEU D
30
54.925
31.168
38.048
1.000
18.28

ATOM
5751
CD2
LEU D
30
54.641
28.690
37.714
1.000
25.83

ATOM
5752
C
LEU D
30
50.301
29.263
38.310
1.000
32.25

ATOM
5753
O
LEU D
30
50.025
28.452
39.205
1.000
32.13

ATOM
5754
N
VAL D
31
49.483
30.260
37.968
1.000
28.07

ATOM
5755
CA
VAL D
31
48.206
30.370
38.681
1.000
30.63

ATOM
5756
CB
VAL D
31
47.387
31.593
38.255
1.000
33.71

ATOM
5757
CD1
VAL D
31
45.995
31.535
38.883
1.000
43.21

ATOM
5758
CG2
VAL D
31
48.069
32.889
38.652
1.000
28.34

ATOM
5759
C
VAL D
31
47.410
29.084
38.467
1.000
33.51

ATOM
5760
O
VAL D
31
46.844
28.504
39.398
1.000
34.58

ATOM
5761
N
GLY D
32
47.411
28.612
37.220
1.000
27.31

ATOM
5762
CA
GLY D
32
46.738
27.367
36.888
1.000
26.97

ATOM
5763
C
GLY D
32
47.258
26.226
37.749
1.000
36.82

ATOM
5764
O
GLY D
32
46.510
25.290
38.045
1.000
33.72

ATOM
5765
N
GLN D
33
48.523
26.305
38.162
1.000
34.44

ATOM
5766
CA
GLN D
33
49.118
25.225
38.942
1.000
36.67

ATOM
5767
CB
GLN D
33
50.598
25.042
38.600
1.000
40.13

ATOM
5768
CG
GLN D
33
50.936
24.989
37.130
1.000
44.78

ATOM
5769
CD
GLN D
33
50.949
23.598
36.543
1.000
49.17

ATOM
5770
OE1
GLN D
33
50.361
22.654
37.070
1.000
57.52

ATOM
5771
NE2
GLN D
33
51.641
23.474
35.415
1.000
56.34

ATOM
5772
C
GLN D
33
48.992
25.447
40.449
1.000
34.31

ATOM
5773
O
GLN D
33
49.590
24.700
41.232
1.000
32.93

ATOM
5774
N
GLY D
34
48.233
26.456
40.867
1.000
33.15

ATOM
5775
CA
GLY D
34
48.047
26.729
42.280
1.000
29.31

ATOM
5776
C
GLY D
34
48.915
27.821
42.841
1.000
32.67

ATOM
5777
O
GLY D
34
48.846
28.101
44.047
1.000
33.83

ATOM
5778
N
ALA D
35
49.757
28.501
42.055
1.000
26.73

ATOM
5779
CA
ALA D
35
50.585
29.543
42.668
1.000
22.64

ATOM
5780
CB
ALA D
35
51.868
29.730
41.868
1.000
25.14

ATOM
5781
C
ALA D
35
49.853
30.869
42.767
1.000
22.80

ATOM
5782
O
ALA D
35
48.780
31.033
42.187
1.000
27.59

ATOM
5783
N
SER D
36
50.425
31.840
43.480
1.000
24.27

ATOM
5784
CA
SER D
36
49.868
33.188
43.417
1.000
29.41

ATOM
5785
CE
SER D
36
49.675
33.820
44.794
1.000
28.13

ATOM
5786
OG
SER D
36
48.888
33.000
45.629
1.000
35.10

ATOM
5787
CB
SER D
36
50.780
34.070
42.566
1.000
34.62

ATOM
5788
O
SER D
36
52.001
33.922
42.600
1.000
26.36

ATOM
5789
N
ALA D
37
50.183
34.989
41.804
1.000
30.49

ATOM
5790
CA
ALA D
37
51.027
35.871
41.007
1.000
29.17

ATOM
5791
CB
ALA D
37
50.974
35.474
39.531
1.000
29.10

ATOM
5792
C
ALA D
37
50.639
37.334
41.162
1.000
24.61

ATOM
5793
O
ALA D
37
49.474
37.691
41.294
1.000
29.85

ATOM
5794
N
VAL D
38
51.665
38.171
41.122
1.000
23.25

ATOM
5795
CA
VAL D
38
51.557
39.605
40.983
1.000
22.55

ATOM
5796
CB
VAL D
38
52.353
40.353
42.059
1.000
26.24

ATOM
5797
CG1
VAL D
38
52.402
41.841
41.739
1.000
25.94

ATOM
5798
CG2
VAL D
38
51.759
40.097
43.435
1.000
30.97

ATOM
5799
C
VAL D
38
52.098
40.009
39.606
1.000
29.14

ATOM
5800
O
VAL D
38
53.286
39.804
39.349
1.000
22.57

ATOM
5801
N
LEU D
39
51.233
40.554
38.765
1.000
27.12

ATOM
5802
CA
LEU D
39
51.591
41.039
37.446
1.000
24.31

ATOM
5803
CE
LEU D
39
50.407
41.028
36.480
1.000
23.52

ATOM
5804
CD
LEU D
39
49.520
39.788
36.443
1.000
22.65

ATOM
5805
CD1
LEU D
39
48.490
39.894
35.319
1.000
23.91

ATOM
5806
CD2
LEU D
39
50.323
38.512
36.274
1.000
20.23

ATOM
5807
C
LEU D
39
52.135
42.463
37.552
1.000
26.76

ATOM
5808
O
LEU D
39
51.395
43.411
37.806
1.000
27.20

ATOM
5809
N
LEU D
40
53.446
42.591
37.357
1.000
24.31

ATOM
5810
CA
LEU D
40
54.093
43.898
37.390
1.000
21.37

ATOM
5811
CB
LEU D
40
55.397
43.828
38.163
1.000
17.64

ATOM
5812
CG
LEU D
40
56.086
45.095
38.628
1.000
25.08

ATOM
5813
CD1
LEU D
40
57.124
44.741
39.693
1.000
28.62

ATOM
5814
CD2
LEU D
40
56.791
45.854
37.505
1.000
26.98

ATOM
5815
C
LEU D
40
54.300
44.376
35.954
1.000
27.49

ATOM
5816
O
LEU D
40
55.085
43.804
35.204
1.000
25.14

ATOM
5817
N
ASP D
41
53.609
45.447
35.588
1.000
30.57

ATOM
5818
CA
ASP D
41
53.638
45.950
34.221
1.000
26.01

ATOM
5819
CB
ASP D
41
52.768
45.058
33.334
1.000
20.45

ATOM
5820
CG
ASP D
41
53.280
45.012
31.903
1.000
26.61

ATOM
5821
OD1
ASP D
41
53.563
46.116
31.385
1.000
25.97

ATOM
5822
OD2
ASP D
41
53.385
43.906
31.331
1.000
23.68

ATOM
5823
C
ASP D
41
53.181
47.404
34.179
1.000
29.66

ATOM
5824
O
ASP D
41
52.708
47.942
35.186
1.000
24.67

ATOM
5825
N
LEU D
42
53.341
48.039
33.022
1.000
26.33

ATOM
5826
CA
LEU D
42
53.102
49.477
32.902
1.000
28.41

ATOM
5827
CE
LEU D
42
53.603
49.989
31.549
1.000
26.22

ATOM
5828
CD
LEU D
42
55.111
49.853
31.294
1.000
29.25

ATOM
5829
CD1
LEU D
42
55.433
50.075
29.825
1.000
25.00

ATOM
5830
CD2
LEU D
42
55.908
50.811
32.166
1.000
18.73

ATOM
5831
C
LEU D
42
51.623
49.797
33.102
1.000
25.26

ATOM
5832
O
LEU D
42
50.789
48.919
32.898
1.000
19.04

ATOM
5833
N
PRO D
43
51.318
51.028
33.489
1.000
30.00

ATOM
5834
CD
PRO D
43
52.263
52.138
33.658
1.000
29.98

ATOM
5835
CA
PRO D
43
49.934
51.405
33.789
1.000
31.92

ATOM
5836
CE
PRO D
43
50.025
52.856
34.254
1.000
27.79

ATOM
5837
CG
PRO D
43
51.444
53.272
34.182
1.000
33.26

ATOM
5838
C
PRO D
43
49.022
51.329
32.565
1.000
31.69

ATOM
5839
O
PRO D
43
47.857
50.955
32.686
1.000
32.45

ATOM
5840
N
ASN D
44
49.559
51.699
31.407
1.000
29.00

ATOM
5841
CA
ASN D
44
48.730
51.669
30.199
1.000
39.63

ATOM
5842
CB
ASN D
44
49.250
52.700
29.196
1.000
46.89

ATOM
5843
CG
ASN D
44
50.723
52.510
28.894
1.000
51.07

ATOM
5844
OD1
ASN D
44
51.612
53.038
29.546
1.000
67.13

ATOM
5845
ND2
ASN D
44
50.973
51.715
27.861
1.000
61.81

ATOM
5846
C
ASN D
44
48.686
50.276
29.595
1.000
36.13

ATOM
5847
O
ASN D
44
48.082
50.038
28.548
1.000
38.91

ATOM
5848
N
SER D
45
49.338
49.310
30.242
1.000
32.04

ATOM
5849
CA
SER D
45
49.150
47.933
29.771
1.000
32.95

ATOM
5850
CE
SER D
45
50.283
47.018
30.216
1.000
32.23

ATOM
5851
OG
SER D
45
50.313
46.891
31.627
1.000
27.59

ATOM
5852
CB
SER D
45
47.794
47.444
30.273
1.000
35.99

ATOM
5853
O
SER D
45
47.174
48.092
31.123
1.000
65.28

ATOM
5854
N
GLY D
46
47.305
46.319
29.762
1.000
33.63

ATOM
5855
CA
GLY D
46
46.034
45.794
30.260
1.000
32.91

ATOM
5856
C
GLY D
46
46.236
44.777
31.371
1.000
30.01

ATOM
5857
O
GLY D
46
45.515
43.789
31.487
1.000
32.99

ATOM
5858
N
GLY D
47
47.243
44.993
32.219
1.000
29.82

ATOM
5859
CA
GLY D
47
47.540
44.036
33.276
1.000
31.13

ATOM
5860
C
GLY D
47
46.400
43.836
34.250
1.000
30.46

ATOM
5861
O
GLY D
47
46.091
42.704
34.629
1.000
29.55

ATOM
5862
N
GLU D
48
45.764
44.926
34.673
1.000
31.20

ATOM
5863
CA
GLU D
48
44.610
44.847
35.571
1.000
30.44

ATOM
5864
CE
GLU D
48
44.007
46.232
35.788
1.000
34.81

ATOM
5865
CG
GLU D
48
42.910
46.303
36.839
1.000
46.31

ATOM
5866
CD
GLU D
48
43.264
45.576
38.121
1.000
57.55

ATOM
5867
OE1
GLU D
48
42.788
44.440
38.332
1.000
64.75

ATOM
5868
OE2
GLU D
48
44.023
46.137
38.941
1.000
70.34

ATOM
5869
C
GLU D
48
43.578
43.881
35.000
1.000
31.02

ATOM
5870
O
GLU D
48
43.094
42.976
35.674
1.000
32.79

ATOM
5871
N
ALA D
49
43.253
44.080
33.719
1.000
31.35

ATOM
5872
CA
ALA D
49
42.284
43.191
33.085
1.000
32.00

ATOM
5873
CE
ALA D
49
41.990
43.667
31.667
1.000
32.18

ATOM
5874
C
ALA D
49
42.772
41.751
33.072
1.000
30.17

ATOM
5875
O
ALA D
49
41.971
40.815
33.149
1.000
23.01

ATOM
5876
N
GLN D
50
44.091
41.551
32.957
1.000
28.22

ATOM
5877
CA
GLN D
50
44.565
40.162
32.932
1.000
27.11

ATOM
5878
CE
GLN D
50
45.975
40.035
32.359
1.000
27.94

ATOM
5879
CG
GLN D
50
46.147
40.500
30.926
1.000
27.74

ATOM
5880
CD
GLN D
50
45.418
39.660
29.904
1.000
32.10

ATOM
5881
OE1
GLN D
50
45.275
40.065
28.743
1.000
48.53

ATOM
5882
NE2
GLN D
50
44.946
38.480
30.284
1.000
25.90

ATOM
5883
C
GLN D
50
44.521
39.579
34.341
1.000
24.98

ATOM
5884
O
GLN D
50
44.135
38.425
34.537
1.000
29.20

ATOM
5885
N
ALA D
51
44.917
40.376
35.331
1.000
25.27

ATOM
5886
CA
ALA D
51
44.834
39.906
36.715
1.000
28.77

ATOM
5887
CB
ALA D
51
45.420
40.936
37.659
1.000
27.87

ATOM
5888
C
ALA D
51
43.385
39.585
37.072
1.000
31.97

ATOM
5889
O
ALA D
51
43.079
38.543
37.656
1.000
29.01

ATOM
5890
N
LYS D
52
42.464
40.482
36.699
1.000
29.02

ATOM
5891
CA
LYS D
52
41.060
40.239
37.044
1.000
33.68

ATOM
5892
CE
LYS D
52
40.197
41.411
36.587
1.000
40.45

ATOM
5893
CG
LYS D
52
38.775
41.054
36.190
1.000
51.10

ATOM
5894
CD
LYS D
52
38.480
41.572
34.787
1.000
61.95

ATOM
5895
CE
LYS D
52
38.743
40.511
33.728
1.000
61.99

ATOM
5896
NZ
LYS D
52
39.088
41.105
32.407
1.000
39.68

ATOM
5897
C
LYS D
52
40.579
38.918
36.457
1.000
32.76

ATOM
5898
O
LYS D
52
39.896
38.129
37.111
1.000
30.38

ATOM
5899
N
LYS D
53
40.949
38.658
35.205
1.000
31.19

ATOM
5900
CA
LYS D
53
40.590
37.407
34.564
1.000
32.46

ATOM
5901
CE
LYS D
53
41.041
37.418
33.103
1.000
35.74

ATOM
5902
C
LYS D
53
41.200
36.197
35.253
1.000
35.48

ATOM
5903
O
LYS D
53
40.652
35.092
35.205
1.000
38.08

ATOM
5904
N
LEU D
54
42.362
36.356
35.893
1.000
36.19

ATOM
5905
CA
LEU D
54
43.025
35.150
36.405
1.000
33.49

ATOM
5906
CE
LEU D
54
44.546
35.358
36.360
1.000
29.70

ATOM
5907
CG
LEU D
54
45.159
35.051
34.981
1.000
27.61

ATOM
5908
CD1
LEU D
54
46.577
35.580
34.901
1.000
29.55

ATOM
5909
CD2
LEU D
54
45.092
33.561
34.695
1.000
28.19

ATOM
5910
C
LEU D
54
42.555
34.759
37.792
1.000
31.35

ATOM
5911
O
LEU D
54
42.955
33.725
38.330
1.000
37.80

ATOM
5912
N
GLY D
55
41.686
35.562
38.406
1.000
34.60

ATOM
5913
CA
GLY D
55
41.066
35.155
39.655
1.000
30.33

ATOM
5914
C
GLY D
55
41.688
35.717
40.911
1.000
29.00

ATOM
5915
O
GLY D
55
42.597
36.540
40.837
1.000
24.79

ATOM
5916
N
ASN D
56
41.193
35.276
42.067
1.000
32.09

ATOM
5917
CA
ASN D
56
41.627
35.767
43.363
1.000
38.75

ATOM
5918
CB
ASN D
56
40.961
34.951
44.486
1.000
45.97

ATOM
5919
CG
ASN D
56
39.487
35.267
44.619
1.000
51.94

ATOM
5920
OD1
ASN D
56
38.654
34.375
44.752
1.000
60.92

ATOM
5921
ND2
ASN D
56
39.196
36.563
44.586
1.000
52.08

ATOM
5922
C
ASN D
56
43.133
35.681
43.581
1.000
35.02

ATOM
5923
O
ASN D
56
43.683
36.439
44.372
1.000
37.38

ATOM
5924
N
ASN D
57
43.777
34.739
42.899
1.000
36.49

ATOM
5925
CA
ASN D
57
45.174
34.441
43.206
1.000
34.75

ATOM
5926
CB
ASN D
57
45.380
32.927
43.173
1.000
32.81

ATOM
5927
CG
ASN D
57
44.745
32.237
44.369
1.000
38.51

ATOM
5928
OD1
ASN D
57
44.193
31.141
44.258
1.000
46.63

ATOM
5929
ND2
ASN D
57
44.829
32.884
45.527
1.000
40.21

ATOM
5930
C
ASN D
57
46.131
35.146
42.257
1.000
35.44

ATOM
5931
O
ASN D
57
47.289
34.760
42.091
1.000
31.41

ATOM
5932
N
CYS D
58
45.653
36.206
41.621
1.000
32.36

ATOM
5933
CA
CYS D
58
46.481
37.022
40.743
1.000
29.88

ATOM
5934
CB
CYS D
58
46.313
36.559
39.291
1.000
28.72

ATOM
5935
SG
CYS D
58
47.357
37.481
38.125
1.000
29.29

ATOM
5936
C
CYS D
58
46.128
38.494
40.875
1.000
27.06

ATOM
5937
O
CYS D
58
44.974
38.899
40.701
1.000
27.89

ATOM
5938
N
VAL D
59
47.097
39.347
41.185
1.000
26.91

ATOM
5939
CA
VAL D
59
46.804
40.781
41.220
1.000
28.98

ATOM
5940
CB
VAL D
59
46.808
41.346
42.650
1.000
32.06

ATOM
5941
CG1
VAL D
59
45.829
40.568
43.524
1.000
34.22

ATOM
5942
CG2
VAL D
59
48.215
41.316
43.222
1.000
31.06

ATOM
5943
C
VAL D
59
47.810
41.570
40.383
1.000
31.95

ATOM
5944
O
VAL D
59
48.907
41.095
40.090
1.000
29.89

ATOM
5945
N
PHE D
60
47.420
42.780
40.006
1.000
28.61

ATOM
5946
CA
PHE D
60
48.225
43.643
39.154
1.000
28.36

ATOM
5947
CB
PHE D
60
47.342
44.259
38.061
1.000
26.03

ATOM
5948
CG
PHE D
60
48.022
45.361
37.268
1.000
26.77

ATOM
5949
CD1
PHE D
60
49.131
45.076
36.490
1.000
31.57

ATOM
5950
CD2
PHE D
60
47.566
46.662
37.297
1.000
28.37

ATOM
5951
CE1
PHE D
60
49.760
46.071
35.759
1.000
29.22

ATOM
5952
CE2
PHE D
60
48.181
47.668
36.574
1.000
28.34

ATOM
5953
CZ
PHE D
60
49.287
47.371
35.802
1.000
27.71

ATOM
5954
C
PHE D
60
48.910
44.731
39.970
1.000
30.78

ATOM
5955
O
PHE D
60
48.294
45.377
40.816
1.000
25.79

ATOM
5956
N
ALA D
61
50.196
44.935
39.715
1.000
28.24

ATOM
5957
CA
ALA D
61
50.955
46.014
40.331
1.000
25.80

ATOM
5958
CB
ALA D
61
52.099
45.458
41.164
1.000
27.20

ATOM
5959
C
ALA D
61
51.485
46.952
39.252
1.000
26.85

ATOM
5960
O
ALA D
61
52.432
46.595
38.549
1.000
30.94

ATOM
5961
N
PRO D
62
50.896
48.131
39.111
1.000
29.26

ATOM
5962
CD
PRO D
62
49.790
48.672
39.919
1.000
24.84

ATOM
5963
CA
PRO D
62
51.336
49.068
38.070
1.000
27.67

ATOM
5964
CB
PRO D
62
50.329
50.217
38.185
1.000
28.36

ATOM
5965
CG
PRO D
62
49.837
50.141
39.597
1.000
28.36

ATOM
5966
C
PRO D
62
52.739
49.588
38.345
1.000
29.75

ATOM
5967
O
PRO D
62
53.019
50.135
39.416
1.000
30.01

ATOM
5968
N
ALA D
63
53.667
49.441
37.401
1.000
26.51

ATOM
5969
CA
ALA D
63
55.017
49.923
37.679
1.000
27.47

ATOM
5970
CB
ALA D
63
55.634
49.131
38.832
1.000
24.94

ATOM
5971
C
ALA D
63
55.933
49.840
36.456
1.000
22.74

ATOM
5972
O
ALA D
63
55.773
48.942
35.634
1.000
22.77

ATOM
5973
N
ASP D
64
56.862
50.775
36.406
1.000
22.65

ATOM
5974
CA
ASP D
64
57.968
50.830
35.458
1.000
26.50

ATOM
5975
CB
ASP D
64
58.212
52.271
35.037
1.000
21.81

ATOM
5976
CG
ASP D
64
59.270
52.434
33.969
1.000
28.32

ATOM
5977
OD1
ASP D
64
59.229
53.472
33.272
1.000
33.50

ATOM
5978
OD2
ASP D
64
60.140
51.549
33.820
1.000
29.49

ATOM
5979
C
ASP D
64
59.214
50.235
36.107
1.000
25.03

ATOM
5980
O
ASP D
64
59.679
50.774
37.112
1.000
22.61

ATOM
5981
N
VAL D
65
59.758
49.150
35.574
1.000
27.71

ATOM
5982
CA
VAL D
65
60.893
48.476
36.207
1.000
25.12

ATOM
5983
CB
VAL D
65
61.241
47.133
35.540
1.000
20.68

ATOM
5984
CG1
VAL D
65
60.113
46.122
35.682
1.000
16.74

ATOM
5985
CG2
VAL D
65
61.566
47.314
34.065
1.000
23.11

ATOM
5986
C
VAL D
65
62.136
49.356
36.230
1.000
23.46

ATOM
5987
O
VAL D
65
63.080
49.064
36.976
1.000
25.73

ATOM
5988
N
THR D
66
62.195
50.444
35.460
1.000
19.65

ATOM
5989
CA
THR D
66
63.362
51.313
35.578
1.000
20.93

ATOM
5990
CB
THR D
66
63.553
52.221
34.349
1.000
24.85

ATOM
5991
OG1
THR D
66
62.389
53.045
34.196
1.000
27.53

ATOM
5992
CG2
THR D
66
63.691
51.407
33.076
1.000
27.72

ATOM
5993
C
THR D
66
63.272
52.221
36.803
1.000
27.29

ATOM
5994
O
THR D
66
64.143
53.067
37.028
1.000
26.24

ATOM
5995
N
SER D
67
62.208
52.064
37.593
1.000
27.60

ATOM
5996
CA
SER D
67
61.987
52.986
38.698
1.000
27.65

ATOM
5997
CB
SER D
67
60.599
53.649
38.564
1.000
24.23

ATOM
5998
OG
SER D
67
60.362
54.377
39.765
1.000
29.46

ATOM
5999
C
SER D
67
62.083
52.320
40.063
1.000
24.57

ATOM
6000
O
SER D
67
61.375
51.358
40.341
1.000
25.87

ATOM
6001
N
GLU D
68
62.947
52.826
40.930
1.000
27.01

ATOM
6002
CA
GLU D
68
63.092
52.281
42.277
1.000
28.26

ATOM
6003
CB
GLU D
68
64.172
53.068
43.020
1.000
29.92

ATOM
6004
CG
GLU D
68
64.439
52.624
44.449
1.000
33.31

ATOM
6005
CD
GLU D
68
65.710
53.252
45.002
1.000
37.25

ATOM
6006
OE1
GLU D
68
66.756
52.568
45.036
1.000
34.88

ATOM
6007
OE2
GLU D
68
65.671
54.437
45.393
1.000
42.89

ATOM
6008
C
GLU D
68
61.772
52.340
43.036
1.000
26.65

ATOM
6009
O
GLU D
68
61.299
51.352
43.598
1.000
22.12

ATOM
6010
N
LYS D
69
61.174
53.533
43.037
1.000
21.31

ATOM
6011
CA
LYS D
69
59.927
53.743
43.769
1.000
27.84

ATOM
6012
CB
LYS D
69
59.507
55.207
43.685
1.000
33.93

ATOM
6013
C
LYS D
69
58.813
52.832
43.275
1.000
29.51

ATOM
6014
O
LYS D
69
58.129
52.184
44.075
1.000
28.88

ATOM
6015
N
ASP D
70
58.619
52.756
41.961
1.000
24.87

ATOM
6016
CA
ASP D
70
57.585
51.889
41.411
1.000
28.61

ATOM
6017
CB
ASP D
70
57.550
51.965
39.883
1.000
31.79

ATOM
6018
CG
ASP D
70
56.975
53.251
39.331
1.000
30.51

ATOM
6019
OD1
ASP D
70
56.695
54.179
40.118
1.000
32.19

ATOM
6020
OD2
ASP D
70
56.817
53.319
38.093
1.000
29.00

ATOM
6021
C
ASP D
70
57.799
50.435
41.805
1.000
25.20

ATOM
6022
O
ASP D
70
56.881
49.687
42.137
1.000
28.32

ATOM
6023
N
VAL D
71
59.060
49.986
41.755
1.000
26.27

ATOM
6024
CA
VAL D
71
59.277
48.575
42.094
1.000
23.48

ATOM
6025
CB
VAL D
71
60.668
48.105
41.660
1.000
25.09

ATOM
6026
CG1
VAL D
71
60.897
46.670
42.096
1.000
21.61

ATOM
6027
CG2
VAL D
71
60.808
48.237
40.144
1.000
30.05

ATOM
6028
C
VAL D
71
59.064
48.376
43.590
1.000
23.38

ATOM
6029
O
VAL D
71
58.490
47.379
44.032
1.000
24.10

ATOM
6030
N
GLN D
72
59.526
49.361
44.370
1.000
23.68

ATOM
6031
CA
GLN D
72
59.295
49.251
45.817
1.000
29.60

ATOM
6032
CB
GLN D
72
59.922
50.435
46.543
1.000
27.41

ATOM
6033
CG
GLN D
72
61.441
50.369
46.601
1.000
30.50

ATOM
6034
CD
GLN D
72
62.070
51.677
47.037
1.000
36.83

ATOM
6035
OE1
GLN D
72
61.498
52.751
46.847
1.000
42.88

ATOM
6036
NE2
GLN D
72
63.258
51.588
47.626
1.000
40.04

ATOM
6037
C
GLN D
72
57.800
49.156
46.082
1.000
25.91

ATOM
6038
O
GLN D
72
57.298
48.323
46.823
1.000
29.83

ATOM
6039
N
THR D
73
57.042
50.033
45.418
1.000
26.69

ATOM
6040
CA
THR D
73
55.589
49.988
45.579
1.000
28.25

ATOM
6041
CB
THR D
73
54.934
51.109
44.755
1.000
35.55

ATOM
6042
OG1
THR D
73
55.318
52.363
45.340
1.000
37.75

ATOM
6043
CG2
THR D
73
53.419
51.024
44.814
1.000
36.99

ATOM
6044
C
THR D
73
55.025
48.643
45.176
1.000
32.13

ATOM
6045
O
THR D
73
54.256
48.009
45.909
1.000
38.91

ATOM
6046
N
ALA D
74
55.384
48.152
43.988
1.000
26.62

ATOM
6047
CA
ALA D
74
54.786
46.877
43.587
1.000
22.02

ATOM
6048
CB
ALA D
74
55.130
46.562
42.135
1.000
26.82

ATOM
6049
C
ALA D
74
55.216
45.759
44.519
1.000
25.59

ATOM
6050
O
ALA D
74
54.449
44.827
44.777
1.000
33.16

ATOM
6051
N
LEU D
75
56.434
45.794
45.066
1.000
25.61

ATOM
6052
CA
LEU D
75
56.769
44.677
45.966
1.000
27.99

ATOM
6053
CB
LEU D
75
58.271
44.644
46.246
1.000
28.13

ATOM
6054
CG
LEU D
75
59.134
44.234
45.044
1.000
26.15

ATOM
6055
CD1
LEU D
75
60.612
44.405
45.366
1.000
27.79

ATOM
6056
CD2
LEU D
75
58.822
42.805
44.640
1.000
21.18

ATOM
6057
C
LEU D
75
55.975
44.769
47.269
1.000
26.60

ATOM
6058
O
LEU D
75
55.493
43.758
47.778
1.000
26.29

ATOM
6059
N
ALA D
76
55.826
45.973
47.811
1.000
25.68

ATOM
6060
CA
ALA D
76
55.045
46.128
49.042
1.000
33.09

ATOM
6061
CB
ALA D
76
55.104
47.564
49.541
1.000
31.43

ATOM
6062
C
ALA D
76
53.603
45.692
48.819
1.000
37.27

ATOM
6063
O
ALA D
76
52.960
45.065
49.666
1.000
35.63

ATOM
6064
N
LEU D
77
53.078
46.023
47.639
1.000
36.38

ATOM
6065
CA
LEU D
77
51.740
45.556
47.265
1.000
29.31

ATOM
6066
CB
LEU D
77
51.398
46.024
45.856
1.000
33.44

ATOM
6067
CG
LEU D
77
49.932
46.072
45.431
1.000
38.05

ATOM
6068
CD1
LEU D
77
49.777
47.044
44.263
1.000
38.40

ATOM
6069
CD2
LEU D
77
49.396
44.700
45.059
1.000
30.81

ATOM
6070
C
LEU D
77
51.689
44.041
47.351
1.000
31.64

ATOM
6071
O
LEU D
77
50.752
43.432
47.855
1.000
36.47

ATOM
6072
N
ALA D
78
52.756
43.408
46.848
1.000
31.80

ATOM
6073
CA
ALA D
78
52.815
41.950
46.860
1.000
34.05

ATOM
6074
CB
ALA D
78
54.036
41.462
46.087
1.000
31.79

ATOM
6075
C
ALA D
78
52.847
41.404
48.281
1.000
29.19

ATOM
6076
O
ALA D
78
52.165
40.436
48.622
1.000
26.82

ATOM
6077
N
LYS D
79
53.680
42.016
49.119
1.000
30.72

ATOM
6078
CA
LYS D
79
53.809
41.519
50.488
1.000
35.21

ATOM
6079
CB
LYS D
79
54.853
42.314
51.247
1.000
32.89

ATOM
6080
C
LYS D
79
52.449
41.576
51.185
1.000
38.85

ATOM
6081
O
LYS D
79
52.023
40.609
51.809
1.000
35.65

ATOM
6082
N
GLY D
80
51.800
42.728
51.047
1.000
39.97

ATOM
6083
CA
GLY D
80
50.507
42.973
51.649
1.000
40.46

ATOM
6084
C
GLY D
80
49.414
42.076
51.129
1.000
42.76

ATOM
6085
O
GLY D
80
48.458
41.739
51.836
1.000
41.31

ATOM
6086
N
LYS D
81
49.502
41.656
49.864
1.000
36.98

ATOM
6087
CA
LYS D
81
48.411
40.821
49.363
1.000
34.65

ATOM
6088
CB
LYS D
81
48.184
41.075
47.868
1.000
38.61

ATOM
6089
CG
LYS D
81
47.306
40.047
47.182
1.000
46.80

ATOM
6090
CD
LYS D
81
45.842
40.198
47.558
1.000
53.26

ATOM
6091
CE
LYS D
81
45.053
38.941
47.237
1.000
57.99

ATOM
6092
NZ
LYS D
81
43.619
39.237
46.954
1.000
62.28

ATOM
6093
C
LYS D
81
48.675
39.350
49.631
1.000
36.61

ATOM
6094
O
LYS D
81
47.745
38.577
49.879
1.000
35.63

ATOM
6095
N
PHE D
82
49.939
38.922
49.579
1.000
32.32

ATOM
6096
CA
PHE D
82
50.180
37.487
49.705
1.000
30.51

ATOM
6097
CB
PHE D
82
50.694
36.929
48.365
1.000
34.03

ATOM
6098
CG
PHE D
82
49.646
37.028
47.262
1.000
33.10

ATOM
6099
CD1
PHE D
82
48.471
36.303
47.370
1.000
30.63

ATOM
6100
CD2
PHE D
82
49.839
37.838
46.156
1.000
28.41

ATOM
6101
CE1
PHE D
82
47.500
36.390
46.390
1.000
34.05

ATOM
6102
CE2
PHE D
82
48.877
37.925
45.167
1.000
29.55

ATOM
6103
CZ
PHE D
82
47.707
37.198
45.288
1.000
34.23

ATOM
6104
C
PHE D
82
51.160
37.149
50.815
1.000
31.92

ATOM
6105
O
PHE D
82
51.437
35.967
51.032
1.000
35.21

ATOM
6106
N
GLY D
83
51.683
38.153
51.506
1.000
33.75

ATOM
6107
CA
GLY D
83
52.547
37.968
52.646
1.000
37.01

ATOM
6108
C
GLY D
83
54.012
37.721
52.376
1.000
41.28

ATOM
6109
O
GLY D
83
54.848
37.931
53.263
1.000
37.16

ATOM
6110
N
ARG D
84
54.365
37.263
51.176
1.000
37.51

ATOM
6111
CA
ARG D
84
55.746
36.920
50.867
1.000
32.37

ATOM
6112
CB
ARG D
84
56.147
35.583
51.493
1.000
27.65

ATOM
6113
CG
ARG D
84
55.156
34.453
51.321
1.000
34.94

ATOM
6114
CD
ARG D
84
55.813
33.082
51.292
1.000
43.12

ATOM
6115
NE
ARG D
84
56.425
32.711
52.553
1.000
51.85

ATOM
6116
CZ
ARG D
84
57.511
31.989
52.773
1.000
56.19

ATOM
6117
NE1
ARG D
84
57.895
31.773
54.028
1.000
62.19

ATOM
6118
NH2
ARG D
84
58.221
31.477
51.772
1.000
34.76

ATOM
6119
C
ARG D
84
55.960
36.869
49.354
1.000
33.88

ATOM
6120
O
ARG D
84
55.003
36.941
48.589
1.000
35.01

ATOM
6121
N
VAL D
85
57.219
36.758
48.954
1.000
29.87

ATOM
6122
CA
VAL D
85
57.626
36.532
47.576
1.000
26.11

ATOM
6123
CB
VAL D
85
58.282
37.762
46.934
1.000
28.50

ATOM
6124
CG1
VAL D
85
58.505
37.488
45.447
1.000
29.52

ATOM
6125
CG2
VAL D
85
57.442
39.012
47.126
1.000
25.93

ATOM
6126
C
VAL D
85
58.604
35.356
47.510
1.000
25.14

ATOM
6127
O
VAL D
85
59.683
35.397
48.102
1.000
25.12

ATOM
6128
N
ASP D
86
58.218
34.306
46.803
1.000
25.70

ATOM
6129
CA
ASP D
86
58.998
33.093
46.654
1.000
24.79

ATOM
6130
CE
ASP D
86
58.104
31.850
46.759
1.000
26.03

ATOM
6131
CG
ASP D
86
57.298
31.824
48.045
1.000
31.97

ATOM
6132
OD1
ASP D
86
56.057
31.880
47.996
1.000
31.52

ATOM
6133
OD2
ASP D
86
57.903
31.755
49.137
1.000
34.74

ATOM
6134
C
ASP D
86
59.723
33.039
45.309
1.000
29.22

ATOM
6135
O
ASP D
86
60.778
32.410
45.217
1.000
24.49

ATOM
6136
N
VAL D
87
59.153
33.674
44.288
1.000
21.53

ATOM
6137
CA
VAL D
87
59.718
33.601
42.941
1.000
21.23

ATOM
6138
CB
VAL D
87
58.939
32.574
42.089
1.000
26.73

ATOM
6139
CG1
VAL D
87
59.413
32.610
40.639
1.000
25.47

ATOM
6140
CG2
VAL D
87
59.064
31.172
42.670
1.000
24.94

ATOM
6141
C
VAL D
87
59.664
34.939
42.222
1.000
24.90

ATOM
6142
O
VAL D
87
58.639
35.624
42.292
1.000
27.16

ATOM
6143
N
ALA D
88
60.734
35.313
41.521
1.000
22.93

ATOM
6144
CA
ALA D
88
60.677
36.485
40.646
1.000
22.19

ATOM
6145
CB
ALA D
88
61.602
37.591
41.104
1.000
17.29

ATOM
6146
C
ALA D
88
60.993
36.071
39.203
1.000
24.09

ATOM
6147
O
ALA D
88
61.921
35.296
38.964
1.000
23.46

ATOM
6148
N
VAL D
89
60.197
36.577
38.274
1.000
20.82

ATOM
6149
CA
VAL D
89
60.382
36.313
36.850
1.000
21.18

ATOM
6150
CE
VAL D
89
59.299
35.426
36.219
1.000
27.30

ATOM
6151
CG1
VAL D
89
59.716
35.012
34.810
1.000
18.72

ATOM
6152
CG2
VAL D
89
58.998
34.168
37.028
1.000
15.99

ATOM
6153
C
VAL D
89
60.414
37.654
36.116
1.000
22.82

ATOM
6154
O
VAL D
89
59.413
38.373
36.103
1.000
24.02

ATOM
6155
N
ASN D
90
61.565
37.980
35.539
1.000
20.51

ATOM
6156
CA
ASN D
90
61.733
39.203
34.774
1.000
20.17

ATOM
6157
CB
ASN D
90
63.161
39.739
34.930
1.000
19.28

ATOM
6158
CG
ASN D
90
63.473
40.175
36.344
1.000
21.33

ATOM
6159
OD1
ASN D
90
64.242
39.531
37.061
1.000
24.72

ATOM
6160
ND2
ASN D
90
62.896
41.282
36.769
1.000
17.80

ATOM
6161
C
ASN D
90
61.417
38.960
33.297
1.000
24.77

ATOM
6162
O
ASN D
90
62.168
38.277
32.594
1.000
26.87

ATOM
6163
N
CYS D
91
60.310
39.511
32.807
1.000
23.72

ATOM
6164
CA
CYS D
91
59.947
39.394
31.401
1.000
23.76

ATOM
6165
CB
CYS D
91
58.650
38.599
31.207
1.000
17.89

ATOM
6166
SG
CYS D
91
58.869
36.834
31.517
1.000
25.59

ATOM
6167
C
CYS D
91
59.815
40.766
30.749
1.000
26.58

ATOM
6168
O
CYS D
91
59.791
40.871
29.515
1.000
21.51

ATOM
6169
N
ALA D
92
59.755
41.811
31.566
1.000
21.43

ATOM
6170
CA
ALA D
92
59.687
43.167
31.039
1.000
23.48

ATOM
6171
CB
ALA D
92
59.741
44.198
32.158
1.000
15.96

ATOM
6172
C
ALA D
92
60.820
43.419
30.046
1.000
29.54

ATOM
6173
O
ALA D
92
61.996
43.186
30.345
1.000
22.45

ATOM
6174
N
GLY D
93
60.480
43.905
28.853
1.000
26.21

ATOM
6175
CA
GLY D
93
61.520
44.147
27.865
1.000
20.92

ATOM
6176
C
GLY D
93
61.011
44.826
26.608
1.000
26.44

ATOM
6177
O
GLY D
93
59.832
44.733
26.267
1.000
21.58

ATOM
6178
N
ILE D
94
61.915
45.504
25.908
1.000
22.55

ATOM
6179
CA
ILE D
94
61.599
46.146
24.644
1.000
22.55

ATOM
6180
CB
ILE D
94
61.573
47.682
24.730
1.000
22.02

ATOM
6181
CG2
ILE D
94
60.365
48.150
25.521
1.000
23.98

ATOM
6182
CG1
ILE D
94
62.885
48.264
25.259
1.000
23.94

ATOM
6183
CD1
ILE D
94
63.023
49.759
25.097
1.000
26.35

ATOM
6184
C
ILE D
94
62.642
45.766
23.586
1.000
25.24

ATOM
6185
O
ILE D
94
63.715
45.245
23.892
1.000
17.15

ATOM
6186
N
ALA D
95
62.279
46.051
22.345
1.000
30.45

ATOM
6187
CA
ALA D
95
63.094
45.746
21.183
1.000
29.43

ATOM
6188
CE
ALA D
95
62.431
44.635
20.377
1.000
25.68

ATOM
6189
C
ALA D
95
63.289
46.976
20.312
1.000
31.25

ATOM
6190
O
ALA D
95
62.416
47.841
20.228
1.000
26.09

ATOM
6191
N
VAL D
96
64.447
47.066
19.662
1.000
27.30

ATOM
6192
CA
VAL D
96
64.634
48.064
18.625
1.000
25.24

ATOM
6193
CB
VAL D
96
65.327
49.365
19.058
1.000
36.51

ATOM
6194
CG1
VAL D
96
64.693
49.957
20.306
1.000
52.71

ATOM
6195
CG2
VAL D
96
66.817
49.129
19.280
1.000
41.65

ATOM
6196
C
VAL D
96
65.470
47.431
17.506
1.000
25.45

ATOM
6197
O
VAL D
96
66.282
46.535
17.727
1.000
21.54

ATOM
6198
N
ALA D
97
65.243
47.926
16.299
1.000
21.06

ATOM
6199
CA
ALA D
97
66.067
47.468
15.176
1.000
21.96

ATOM
6200
CE
ALA D
97
65.236
46.724
14.157
1.000
27.78

ATOM
6201
C
ALA D
97
66.751
48.710
14.617
1.000
24.35

ATOM
6202
O
ALA D
97
66.062
49.615
14.147
1.000
27.82

ATOM
6203
N
SER D
98
68.074
48.763
14.702
1.000
21.21

ATOM
6204
CA
SER D
98
68.799
49.939
14.223
1.000
25.16

ATOM
6205
CE
SER D
98
68.582
51.111
15.175
1.000
22.16

ATOM
6206
OG
SER D
98
69.228
52.299
14.765
1.000
23.19

ATOM
6207
C
SER D
98
70.278
49.604
14.069
1.000
27.15

ATOM
6208
O
SER D
98
70.929
49.216
15.042
1.000
21.76

ATOM
6209
N
LYS D
99
70.792
49.761
12.854
1.000
21.91

ATOM
6210
CA
LYS D
99
72.201
49.518
12.579
1.000
24.27

ATOM
6211
CE
LYS D
99
72.471
49.620
11.070
1.000
24.05

ATOM
6212
CG
LYS D
99
71.911
48.450
10.278
1.000
24.66

ATOM
6213
CD
LYS D
99
71.701
48.833
8.820
1.000
31.29

ATOM
6214
CE
LYS D
99
71.044
47.714
8.034
1.000
36.32

ATOM
6215
NZ
LYS D
99
71.644
47.527
6.685
1.000
50.21

ATOM
6216
C
LYS D
99
73.128
50.488
13.304
1.000
24.08

ATOM
6217
O
LYS D
99
72.824
51.672
13.449
1.000
21.85

ATOM
6218
N
THR D
100
74.282
49.979
13.746
1.000
19.95

ATOM
6219
CA
THR D
100
75.254
50.836
14.422
1.000
19.55

ATOM
6220
CB
THR D
100
76.545
50.079
14.781
1.000
21.22

ATOM
6221
OG1
THR D
100
76.257
48.985
15.655
1.000
24.03

ATOM
6222
CG2
THR D
100
77.466
51.030
15.532
1.000
22.24

ATOM
6223
C
THR D
100
75.622
52.043
13.566
1.000
21.15

ATOM
6224
O
THR D
100
75.636
53.187
14.026
1.000
19.49

ATOM
6225
N
TYR D
101
75.917
51.761
12.299
1.000
20.95

ATOM
6226
CA
TYR D
101
76.167
52.806
11.312
1.000
22.24

ATOM
6227
CB
TYR D
101
77.625
53.287
11.272
1.000
23.19

ATOM
6228
CG
TYR D
101
77.835
54.290
10.152
1.000
24.99

ATOM
6229
CD1
TYR D
101
78.536
53.962
9.004
1.000
30.17

ATOM
6230
CE1
TYR D
101
78.715
54.887
7.989
1.000
33.21

ATOM
6231
CD2
TYR D
101
77.308
55.568
10.251
1.000
29.66

ATOM
6232
CE2
TYR D
101
77.474
56.503
9.247
1.000
29.30

ATOM
6233
CZ
TYR D
101
78.180
56.150
8.118
1.000
34.03

ATOM
6234
OH
TYR D
101
78.352
57.072
7.109
1.000
33.32

ATOM
6235
C
TYR D
101
75.754
52.275
9.940
1.000
29.72

ATOM
6236
O
TYR D
101
76.075
51.134
9.609
1.000
26.97

ATOM
6237
N
ASN D
102
75.036
53.098
9.185
1.000
29.84

ATOM
6238
CA
ASN D
102
74.534
52.672
7.879
1.000
27.82

ATOM
6239
CB
ASN D
102
73.013
52.716
7.886
1.000
29.39

ATOM
6240
CG
ASN D
102
72.379
52.247
6.594
1.000
37.37

ATOM
6241
OD1
ASN D
102
73.063
52.102
5.579
1.000
39.57

ATOM
6242
ND2
ASN D
102
71.070
52.010
6.634
1.000
26.10

ATOM
6243
C
ASN D
102
75.118
53.566
6.792
1.000
27.53

ATOM
6244
O
ASN D
102
74.664
54.693
6.601
1.000
28.16

ATOM
6245
N
LEU D
103
76.145
53.089
6.092
1.000
30.38

ATOM
6246
CA
LEU D
103
76.778
53.927
5.077
1.000
32.06

ATOM
6247
CB
LEU D
103
78.029
53.267
4.499
1.000
31.44

ATOM
6248
CG
LEU D
103
78.845
54.165
3.556
1.000
31.02

ATOM
6249
CD1
LEU D
103
79.382
55.382
4.291
1.000
34.86

ATOM
6250
CD2
LEU D
103
79.975
53.376
2.910
1.000
31.19

ATOM
6251
C
LEU D
103
75.799
54.252
3.951
1.000
38.73

ATOM
6252
O
LEU D
103
75.758
55.382
3.458
1.000
41.00

ATOM
6253
N
LYS D
104
75.006
53.256
3.568
1.000
42.41

ATOM
6254
CA
LYS D
104
74.059
53.402
2.469
1.000
42.43

ATOM
6255
CB
LYS D
104
73.257
52.117
2.304
1.000
49.29

ATOM
6256
C
LYS D
104
73.135
54.594
2.672
1.000
38.48

ATOM
6257
O
LYS D
104
72.873
55.374
1.758
1.000
46.32

ATOM
6258
N
LYS D
105
72.629
54.738
3.882
1.000
34.33

ATOM
6259
CA
LYS D
105
71.759
55.831
4.272
1.000
34.50

ATOM
6260
CB
LYS D
105
70.730
55.320
5.280
1.000
43.73

ATOM
6261
CG
LYS D
105
69.341
55.017
4.762
1.000
51.53

ATOM
6262
CD
LYS D
105
68.334
55.177
5.902
1.000
60.99

ATOM
6263
CE
LYS D
105
68.852
56.167
6.937
1.000
66.55

ATOM
6264
NZ
LYS D
105
68.589
55.715
8.329
1.000
70.72

ATOM
6265
C
LYS D
105
72.544
56.954
4.927
1.000
31.68

ATOM
6266
O
LYS D
105
71.971
57.994
5.265
1.000
34.61

ATOM
6267
N
GLY D
106
73.844
56.744
5.149
1.000
26.87

ATOM
6268
CA
GLY D
106
74.599
57.744
5.902
1.000
24.09

ATOM
6269
C
GLY D
106
73.997
57.951
7.281
1.000
29.52

ATOM
6270
O
GLY D
106
73.940
59.070
7.794
1.000
36.21

ATOM
6271
N
GLN D
107
73.531
56.873
7.908
1.000
31.56

ATOM
6272
CA
GLN D
107
72.821
56.986
9.176
1.000
31.60

ATOM
6273
CB
GLN D
107
71.414
56.420
9.023
1.000
31.54

ATOM
6274
C
GLN D
107
73.535
56.282
10.326
1.000
27.83

ATOM
6275
O
GLN D
107
74.124
55.221
10.139
1.000
21.99

ATOM
6276
N
THR D
108
73.450
56.914
11.488
1.000
28.97

ATOM
6277
CA
THR D
108
74.099
56.498
12.718
1.000
27.95

ATOM
6278
CB
THR D
108
75.039
57.610
13.230
1.000
27.01

ATOM
6279
OG1
THR D
108
76.069
57.806
12.244
1.000
26.81

ATOM
6280
CG2
THR D
108
75.712
57.203
14.535
1.000
23.92

ATOM
6281
C
THR D
108
73.093
56.158
13.813
1.000
25.94

ATOM
6282
O
THR D
108
72.169
56.930
14.057
1.000
24.57

ATOM
6283
N
HIS D
109
73.288
55.017
14.460
1.000
24.99

ATOM
6284
CA
HIS D
109
72.481
54.609
15.610
1.000
22.08

ATOM
6285
CB
HIS D
109
73.066
53.330
16.199
1.000
24.31

ATOM
6286
CG
HIS D
109
72.217
52.581
17.173
1.000
21.11

ATOM
6287
CD2
HIS D
109
71.849
51.281
17.199
1.000
22.29

ATOM
6288
ND1
HIS D
109
71.647
53.161
18.289
1.000
21.14

ATOM
6289
CE1
HIS D
109
70.961
52.248
18.953
1.000
22.36

ATOM
6290
NE2
HIS D
109
71.064
51.090
18.313
1.000
24.23

ATOM
6291
C
HIS D
109
72.442
55.727
16.634
1.000
21.13

ATOM
6292
O
HIS D
109
73.475
56.295
16.997
1.000
24.86

ATOM
6293
N
THR D
110
71.265
56.105
17.134
1.000
22.33

ATOM
6294
CA
THR D
110
71.270
57.195
18.113
1.000
21.15

ATOM
6295
CB
THR D
110
69.891
57.855
18.291
1.000
24.47

ATOM
6296
OG1
THR D
110
69.064
56.917
19.003
1.000
24.44

ATOM
6297
CG2
THR D
110
69.245
58.154
16.947
1.000
22.97

ATOM
6298
C
THR D
110
71.697
56.698
19.488
1.000
22.11

ATOM
6299
O
THR D
110
71.439
55.555
19.857
1.000
28.62

ATOM
6300
N
LEU D
111
72.331
57.585
20.245
1.000
25.58

ATOM
6301
CA
LEU D
111
72.736
57.213
21.601
1.000
24.13

ATOM
6302
CB
LEU D
111
73.554
58.351
22.214
1.000
22.07

ATOM
6303
CG
LEU D
111
74.351
58.004
23.473
1.000
27.10

ATOM
6304
CD1
LEU D
111
75.280
56.822
23.222
1.000
23.25

ATOM
6305
CD2
LEU D
111
75.156
59.199
23.966
1.000
26.98

ATOM
6306
C
LEU D
111
71.519
56.871
22.448
1.000
25.93

ATOM
6307
O
LEU D
111
71.495
55.918
23.234
1.000
25.17

ATOM
6308
N
GLU D
112
70.447
57.654
22.311
1.000
24.62

ATOM
6309
CA
GLU D
112
69.296
57.407
23.179
1.000
31.12

ATOM
6310
CB
GLU D
112
68.320
58.590
23.145
1.000
42.68

ATOM
6311
CG
GLU D
112
68.495
59.531
24.328
1.000
59.94

ATOM
6312
CD
GLU D
112
69.326
58.988
25.477
1.000
63.78

ATOM
6313
OE1
GLU D
112
68.742
58.501
26.473
1.000
57.36

ATOM
6314
OE2
GLU D
112
70.577
59.055
25.393
1.000
40.17

ATOM
6315
C
GLU D
112
68.584
56.108
22.842
1.000
29.53

ATOM
6316
O
GLU D
112
68.017
55.506
23.759
1.000
27.04

ATOM
6317
N
ASP D
113
68.608
55.665
21.591
1.000
26.11

ATOM
6318
CA
ASP D
113
68.051
54.351
21.270
1.000
25.53

ATOM
6319
CB
ASP D
113
68.096
54.113
19.759
1.000
25.99

ATOM
6320
CG
ASP D
113
66.784
54.448
19.072
1.000
30.30

ATOM
6321
OD1
ASP D
113
65.844
54.914
19.753
1.000
32.37

ATOM
6322
OD2
ASP D
113
66.656
54.246
17.848
1.000
28.37

ATOM
6323
C
ASP D
113
68.805
53.247
22.013
1.000
24.25

ATOM
6324
O
ASP D
113
68.240
52.244
22.448
1.000
24.18

ATOM
6325
N
PHE D
114
70.115
53.436
22.152
1.000
19.95

ATOM
6326
CA
PHE D
114
70.939
52.464
22.872
1.000
22.83

ATOM
6327
CB
PHE D
114
72.420
52.714
22.607
1.000
20.00

ATOM
6328
CG
PHE D
114
73.343
51.605
23.067
1.000
22.08

ATOM
6329
CD1
PHE D
114
73.985
51.682
24.292
1.000
22.82

ATOM
6330
CD2
PHE D
114
73.561
50.494
22.270
1.000
21.94

ATOM
6331
CE1
PHE D
114
74.820
50.666
24.715
1.000
20.62

ATOM
6332
CE2
PHE D
114
74.398
49.476
22.680
1.000
21.46

ATOM
6333
CZ
PHE D
114
75.039
49.576
23.899
1.000
18.59

ATOM
6334
C
PHE D
114
70.643
52.534
24.372
1.000
21.87

ATOM
6335
O
PHE D
114
70.464
51.496
25.009
1.000
21.31

ATOM
6336
N
GLN D
115
70.583
53.743
24.913
1.000
24.02

ATOM
6337
CA
GLN D
115
70.370
53.959
26.344
1.000
24.66

ATOM
6338
CB
GLN D
115
70.477
55.444
26.700
1.000
25.07

ATOM
6339
CG
GLN D
115
70.334
55.724
28.197
1.000
29.62

ATOM
6340
CD
GLN D
115
71.606
55.421
28.961
1.000
32.26

ATOM
6341
OE1
GLN D
115
72.679
55.907
28.602
1.000
32.00

ATOM
6342
NE2
GLN D
115
71.525
54.622
30.019
1.000
29.01

ATOM
6343
C
GLN D
115
69.016
53.433
26.802
1.000
22.64

ATOM
6344
O
GLN D
115
68.895
52.844
27.871
1.000
26.88

ATOM
6345
N
ARG D
116
67.982
53.648
25.998
1.000
21.99

ATOM
6346
CA
ARG D
116
66.637
53.224
26.372
1.000
23.55

ATOM
6347
CB
ARG D
116
65.640
53.763
25.350
1.000
27.00

ATOM
6348
C
ARG D
116
66.532
51.711
26.504
1.000
23.39

ATOM
6349
O
ARG D
116
65.906
51.149
27.406
1.000
21.70

ATOM
6350
N
VAL D
117
67.144
50.989
25.573
1.000
21.56

ATOM
6351
CA
VAL D
117
67.073
49.533
25.582
1.000
23.53

ATOM
6352
CB
VAL D
117
67.609
48.990
24.239
1.000
22.11

ATOM
6353
CG1
VAL D
117
67.774
47.484
24.260
1.000
16.76

ATOM
6354
CG2
VAL D
117
66.664
49.411
23.115
1.000
26.84

ATOM
6355
C
VAL D
117
67.846
48.937
26.753
1.000
20.88

ATOM
6356
O
VAL D
117
67.446
47.933
27.343
1.000
22.24

ATOM
6357
N
LEU D
118
68.975
49.539
27.087
1.000
18.85

ATOM
6358
CA
LEU D
118
69.789
49.147
28.221
1.000
23.19

ATOM
6359
CB
LEU D
118
71.041
50.009
28.348
1.000
23.72

ATOM
6360
CG
LEU D
118
72.317
49.661
27.600
1.000
37.64

ATOM
6361
CD1
LEU D
118
73.527
50.143
28.402
1.000
34.18

ATOM
6362
CD2
LEU D
118
72.426
48.174
27.297
1.000
39.23

ATOM
6363
C
LEU D
118
69.018
49.334
29.531
1.000
24.46

ATOM
6364
O
LEU D
118
68.965
48.499
30.430
1.000
26.50

ATOM
6365
N
ASP D
119
68.433
50.529
29.604
1.000
23.45

ATOM
6366
CA
ASP D
119
67.734
50.943
30.813
1.000
20.49

ATOM
6367
CE
ASP D
119
67.298
52.402
30.675
1.000
21.70

ATOM
6368
CG
ASP D
119
68.469
53.349
30.876
1.000
24.66

ATOM
6369
OD1
ASP D
119
68.249
54.577
30.868
1.000
37.01

ATOM
6370
OD2
ASP D
119
69.614
52.870
31.041
1.000
27.68

ATOM
6371
C
ASP D
119
66.559
50.025
31.098
1.000
26.03

ATOM
6372
O
ASP D
119
66.410
49.543
32.222
1.000
22.46

ATOM
6373
N
VAL D
120
65.718
49.766
30.094
1.000
26.23

ATOM
6374
CA
VAL D
120
64.566
48.908
30.351
1.000
22.36

ATOM
6375
CB
VAL D
120
63.511
48.983
29.231
1.000
22.81

ATOM
6376
CG1
VAL D
120
62.412
47.954
29.466
1.000
19.93

ATOM
6377
CG2
VAL D
120
62.907
50.375
29.137
1.000
28.30

ATOM
6378
C
VAL D
120
64.978
47.450
30.514
1.000
22.74

ATOM
6379
O
VAL D
120
64.605
46.804
31.495
1.000
24.55

ATOM
6380
N
ASN D
121
65.734
46.919
29.547
1.000
18.38

ATOM
6381
CA
ASN D
121
66.020
45.497
29.514
1.000
15.30

ATOM
6382
CB
ASN D
121
66.583
45.094
28.143
1.000
20.69

ATOM
6383
CG
ASN D
121
65.530
45.119
27.056
1.000
26.58

ATOM
6384
OD1
ASN D
121
64.352
45.388
27.314
1.000
27.53

ATOM
6385
ND2
ASN D
121
65.934
44.844
25.825
1.000
21.69

ATOM
6386
C
ASN D
121
67.013
45.050
30.583
1.000
18.37

ATOM
6387
O
ASN D
121
66.808
43.983
31.166
1.000
20.46

ATOM
6388
N
LEU D
122
68.053
45.842
30.793
1.000
20.17

ATOM
6389
CA
LEU D
122
69.172
45.423
31.640
1.000
18.87

ATOM
6390
CB
LEU D
122
70.488
45.759
30.940
1.000
20.22

ATOM
6391
CG
LEU D
122
71.785
45.431
31.679
1.000
22.50

ATOM
6392
CD1
LEU D
122
71.791
43.969
32.116
1.000
19.47

ATOM
6393
CD2
LEU D
122
73.002
45.739
30.815
1.000
13.29

ATOM
6394
C
LEU D
122
69.097
46.064
33.024
1.000
22.74

ATOM
6395
O
LEU D
122
69.042
45.339
34.022
1.000
23.12

ATOM
6396
N
MET D
123
69.094
47.391
33.110
1.000
19.62

ATOM
6397
CA
MET D
123
69.023
48.058
34.414
1.000
21.53

ATOM
6398
CB
MET D
123
69.176
49.565
34.258
1.000
24.22

ATOM
6399
CG
MET D
123
69.034
50.403
35.516
1.000
25.27

ATOM
6400
SD
MET D
123
67.343
50.956
35.801
1.000
26.68

ATOM
6401
CE
MET D
123
67.209
52.315
34.650
1.000
23.05

ATOM
6402
C
MET D
123
67.712
47.704
35.106
1.000
26.27

ATOM
6403
O
MET D
123
67.674
47.364
36.288
1.000
22.41

ATOM
6404
N
GLY D
124
66.604
47.765
34.368
1.000
23.16

ATOM
6405
CA
GLY D
124
65.306
47.408
34.921
1.000
23.30

ATOM
6406
C
GLY D
124
65.311
46.009
35.507
1.000
28.26

ATOM
6407
O
GLY D
124
64.760
45.783
36.589
1.000
25.60

ATOM
6408
N
THR D
125
65.922
45.053
34.808
1.000
21.28

ATOM
6409
CA
THR D
125
65.981
43.687
35.340
1.000
18.79

ATOM
6410
CB
THR D
125
66.528
42.692
34.307
1.000
19.73

ATOM
6411
OG1
THR D
125
65.460
42.277
33.438
1.000
20.94

ATOM
6412
CG2
THR D
125
67.039
41.421
34.966
1.000
19.51

ATOM
6413
C
THR D
125
66.813
43.663
36.617
1.000
20.50

ATOM
6414
O
THR D
125
66.383
43.054
37.602
1.000
22.54

ATOM
6415
N
PHE D
126
67.969
44.318
36.623
1.000
22.38

ATOM
6416
CA
PHE D
126
68.769
44.394
37.843
1.000
23.35

ATOM
6417
CE
PHE D
126
70.122
45.087
37.643
1.000
18.53

ATOM
6418
CG
PHE D
126
70.989
45.079
38.896
1.000
25.35

ATOM
6419
CD1
PHE D
126
71.667
43.943
39.293
1.000
24.48

ATOM
6420
CD2
PHE D
126
71.132
46.214
39.680
1.000
29.37

ATOM
6421
CE1
PHE D
126
72.463
43.925
40.430
1.000
21.17

ATOM
6422
CE2
PHE D
126
71.925
46.210
40.819
1.000
27.18

ATOM
6423
CZ
PHE D
126
72.606
45.063
41.200
1.000
20.25

ATOM
6424
C
PHE D
126
68.004
45.117
38.951
1.000
22.47

ATOM
6425
O
PHE D
126
68.123
44.694
40.101
1.000
19.76

ATOM
6426
N
ASN D
127
67.248
46.155
38.616
1.000
19.34

ATOM
6427
CA
ASN D
127
66.464
46.884
39.614
1.000
23.88

ATOM
6428
CE
ASN D
127
65.681
48.036
38.975
1.000
22.44

ATOM
6429
CG
ASN D
127
65.039
48.962
39.988
1.000
30.06

ATOM
6430
OD1
ASN D
127
65.566
49.201
41.082
1.000
29.26

ATOM
6431
ND2
ASN D
127
63.878
49.514
39.644
1.000
22.96

ATOM
6432
C
ASN D
127
65.518
45.947
40.358
1.000
25.51

ATOM
6433
O
ASN D
127
65.516
45.912
41.594
1.000
29.94

ATOM
6434
N
VAL D
128
64.727
45.177
39.621
1.000
22.04

ATOM
6435
CA
VAL D
128
63.826
44.206
40.243
1.000
24.33

ATOM
6436
CE
VAL D
128
62.956
43.507
39.181
1.000
23.82

ATOM
6437
CG1
VAL D
128
62.112
42.395
39.772
1.000
19.10

ATOM
6438
CG2
VAL D
128
62.057
44.530
38.493
1.000
24.29

ATOM
6439
C
VAL D
128
64.591
43.173
41.058
1.000
25.09

ATOM
6440
O
VAL D
128
64.237
42.900
42.210
1.000
24.73

ATOM
6441
N
ILE D
129
65.646
42.588
40.500
1.000
19.60

ATOM
6442
CA
ILE D
129
66.413
41.570
41.212
1.000
20.00

ATOM
6443
CB
ILE D
129
67.623
41.085
40.386
1.000
19.71

ATOM
6444
CG2
ILE D
129
68.625
40.382
41.290
1.000
20.01

ATOM
6445
CG1
ILE D
129
67.294
40.185
39.197
1.000
20.97

ATOM
6446
CD1
ILE D
129
68.461
40.025
38.231
1.000
20.09

ATOM
6447
C
ILE D
129
66.944
42.064
42.555
1.000
22.83

ATOM
6448
O
ILE D
129
66.847
41.373
43.577
1.000
23.59

ATOM
6449
N
ARG D
130
67.537
43.259
42.570
1.000
21.25

ATOM
6450
CA
ARG D
130
68.158
43.727
43.813
1.000
23.54

ATOM
6451
CE
ARG D
130
68.999
44.977
43.560
1.000
22.14

ATOM
6452
CG
ARG D
130
68.195
46.253
43.482
1.000
20.61

ATOM
6453
CD
ARG D
130
68.975
47.455
42.942
1.000
19.85

ATOM
6454
NE
ARG D
130
67.980
48.538
42.867
1.000
25.36

ATOM
6455
CZ
ARG D
130
67.805
49.473
43.786
1.000
25.50

ATOM
6456
NH1
ARG D
130
66.868
50.401
43.628
1.000
20.78

ATOM
6457
NH2
ARG D
130
68.580
49.482
44.857
1.000
19.51

ATOM
6458
C
ARG D
130
67.096
43.971
44.877
1.000
27.48

ATOM
6459
O
ARG D
130
67.303
43.695
46.061
1.000
23.84

ATOM
6460
N
LEU D
131
65.932
44.474
44.473
1.000
27.06

ATOM
6461
CA
LEU D
131
64.884
44.753
45.458
1.000
28.21

ATOM
6462
CB
LEU D
131
63.895
45.787
44.910
1.000
23.68

ATOM
6463
CG
LEU D
131
64.445
47.216
44.808
1.000
26.52

ATOM
6464
CD1
LEU D
131
63.477
48.145
44.089
1.000
23.04

ATOM
6465
CD2
LEU D
131
64.770
47.782
46.188
1.000
32.33

ATOM
6466
C
LEU D
131
64.189
43.471
45.891
1.000
29.02

ATOM
6467
O
LEU D
131
63.973
43.244
47.089
1.000
26.84

ATOM
6468
N
VAL D
132
63.846
42.601
44.947
1.000
18.42

ATOM
6469
CA
VAL D
132
63.159
41.367
45.325
1.000
18.90

ATOM
6470
CB
VAL D
132
62.618
40.598
44.106
1.000
23.35

ATOM
6471
CG1
VAL D
132
63.708
39.751
43.463
1.000
23.66

ATOM
6472
CG2
VAL D
132
61.446
39.715
44.506
1.000
22.79

ATOM
6473
C
VAL D
132
64.073
40.451
46.132
1.000
23.76

ATOM
6474
O
VAL D
132
63.616
39.657
46.953
1.000
27.48

ATOM
6475
N
ALA D
133
65.389
40.531
45.932
1.000
22.04

ATOM
6476
CA
ALA D
133
66.297
39.729
46.754
1.000
23.76

ATOM
6477
CB
ALA D
133
67.730
39.926
46.302
1.000
20.82

ATOM
6478
C
ALA D
133
66.148
40.103
48.230
1.000
24.85

ATOM
6479
O
ALA D
133
66.290
39.282
49.131
1.000
23.50

ATOM
6480
N
GLY D
134
65.852
41.376
48.460
1.000
26.12

ATOM
6481
CA
GLY D
134
65.563
41.870
49.793
1.000
32.35

ATOM
6482
C
GLY D
134
64.285
41.284
50.357
1.000
34.57

ATOM
6483
O
GLY D
134
64.202
41.047
51.568
1.000
35.22

ATOM
6484
N
GLU D
135
63.277
41.038
49.523
1.000
30.01

ATOM
6485
CA
GLU D
135
62.034
40.496
50.068
1.000
28.91

ATOM
6486
CE
GLU D
135
60.839
40.738
49.147
1.000
26.20

ATOM
6487
CG
GLU D
135
60.598
42.200
48.824
1.000
30.37

ATOM
6488
CD
GLU D
135
60.124
42.990
50.027
1.000
35.33

ATOM
6489
OE1
GLU D
135
60.588
44.135
50.204
1.000
44.37

ATOM
6490
OE2
GLU D
135
59.294
42.447
50.785
1.000
45.78

ATOM
6491
C
GLU D
135
62.163
39.001
50.343
1.000
30.94

ATOM
6492
O
GLU D
135
61.616
38.487
51.323
1.000
32.39

ATOM
6493
N
MET D
136
62.873
38.287
49.475
1.000
23.95

ATOM
6494
CA
MET D
136
63.071
36.860
49.680
1.000
23.00

ATOM
6495
CB
MET D
136
63.685
36.218
48.428
1.000
27.92

ATOM
6496
CG
MET D
136
62.749
36.166
47.227
1.000
30.16

ATOM
6497
SD
MET D
136
63.670
35.935
45.689
1.000
23.75

ATOM
6498
CE
MET D
136
62.344
35.879
44.489
1.000
20.24

ATOM
6499
C
MET D
136
63.986
36.591
50.868
1.000
21.34

ATOM
6500
O
MET D
136
63.924
35.549
51.518
1.000
26.69

ATOM
6501
N
GLY D
137
64.877
37.539
51.158
1.000
23.58

ATOM
6502
CA
GLY D
137
65.799
37.353
52.276
1.000
27.87

ATOM
6503
C
GLY D
137
65.026
37.196
53.578
1.000
34.97

ATOM
6504
O
GLY D
137
65.484
36.540
54.512
1.000
32.81

ATOM
6505
N
GLN D
138
63.837
37.798
53.610
1.000
29.09

ATOM
6506
CA
GLN D
138
62.998
37.802
54.802
1.000
30.46

ATOM
6507
CB
GLN D
138
61.956
38.908
54.691
1.000
33.07

ATOM
6508
C
GLN D
138
62.327
36.459
55.039
1.000
34.33

ATOM
6509
O
GLN D
138
61.800
36.204
56.124
1.000
36.30

ATOM
6510
N
ASN D
139
62.341
35.587
54.028
1.000
31.51

ATOM
6511
CA
ASN D
139
61.696
34.291
54.219
1.000
28.20

ATOM
6512
CB
ASN D
139
61.363
33.612
52.900
1.000
27.26

ATOM
6513
CG
ASN D
139
60.572
34.464
51.932
1.000
34.45

ATOM
6514
OD1
ASN D
139
59.779
35.315
52.340
1.000
32.80

ATOM
6515
ND2
ASN D
139
60.798
34.227
50.642
1.000
25.07

ATOM
6516
C
ASN D
139
62.606
33.367
55.024
1.000
32.92

ATOM
6517
O
ASN D
139
63.820
33.396
54.827
1.000
30.48

ATOM
6518
N
GLU D
140
62.025
32.552
55.903
1.000
30.73

ATOM
6519
CA
GLU D
140
62.828
31.514
56.550
1.000
32.23

ATOM
6520
CE
GLU D
140
62.098
30.903
57.730
1.000
38.83

ATOM
6521
C
GLU D
140
63.174
30.453
55.510
1.000
32.14

ATOM
6522
O
GLU D
140
62.303
30.103
54.706
1.000
31.41

ATOM
6523
N
PRO D
141
64.397
29.942
55.494
1.000
30.57

ATOM
6524
CD
PRO D
141
65.498
30.258
56.412
1.000
30.81

ATOM
6525
CA
PRO D
141
64.771
28.949
54.483
1.000
28.26

ATOM
6526
CB
PRO D
141
66.204
28.575
54.847
1.000
32.66

ATOM
6527
CG
PRO D
141
66.701
29.650
55.748
1.000
32.60

ATOM
6528
C
PRO D
141
63.877
27.717
54.550
1.000
35.61

ATOM
6529
O
PRO D
141
63.444
27.315
55.630
1.000
38.04

ATOM
6530
N
ASP D
142
63.595
27.116
53.391
1.000
31.00

ATOM
6531
CA
ASP D
142
62.833
25.868
53.394
1.000
30.24

ATOM
6532
CB
ASP D
142
62.203
25.612
52.035
1.000
35.96

ATOM
6533
CG
ASP D
142
63.154
25.321
50.898
1.000
34.68

ATOM
6534
OD1
ASP D
142
64.363
25.098
51.104
1.000
27.65

ATOM
6535
OD2
ASP D
142
62.670
25.303
49.742
1.000
33.75

ATOM
6536
C
ASP D
142
63.741
24.710
53.799
1.000
34.08

ATOM
6537
O
ASP D
142
64.880
24.929
54.213
1.000
29.73

ATOM
6538
N
GLN D
143
63.245
23.487
53.653
1.000
34.49

ATOM
6539
CA
GLN D
143
64.011
22.307
54.043
1.000
39.62

ATOM
6540
CB
GLN D
143
63.204
21.045
53.757
1.000
38.01

ATOM
6541
C
GLN D
143
65.369
22.242
53.346
1.000
41.65

ATOM
6542
O
GLN D
143
66.328
21.695
53.900
1.000
35.45

ATOM
6543
N
GLY D
144
65.443
22.791
52.136
1.000
37.16

ATOM
6544
CA
GLY D
144
66.661
22.736
51.337
1.000
30.96

ATOM
6545
C
GLY D
144
67.455
24.022
51.448
1.000
31.88

ATOM
6546
O
GLY D
144
68.358
24.282
50.651
1.000
29.80

ATOM
6547
N
GLY D
145
67.119
24.841
52.445
1.000
28.25

ATOM
6548
CA
GLY D
145
67.786
26.101
52.691
1.000
24.94

ATOM
6549
C
GLY D
145
67.436
27.188
51.692
1.000
25.03

ATOM
6550
O
GLY D
145
68.057
28.252
51.660
1.000
22.98

ATOM
6551
N
GLN D
146
66.438
26.952
50.854
1.000
23.54

ATOM
6552
CA
GLN D
146
66.079
27.907
49.818
1.000
25.58

ATOM
6553
CB
GLN D
146
65.402
27.173
48.646
1.000
26.63

ATOM
6554
CG
GLN D
146
65.240
28.068
47.420
1.000
31.76

ATOM
6555
CD
GLN D
146
64.934
27.273
46.163
1.000
30.74

ATOM
6556
OE1
GLN D
146
65.837
26.723
45.538
1.000
26.69

ATOM
6557
NE2
GLN D
146
63.659
27.205
45.802
1.000
26.20

ATOM
6558
C
GLN D
146
65.155
29.015
50.305
1.000
27.84

ATOM
6559
O
GLN D
146
64.176
28.757
51.009
1.000
29.88

ATOM
6560
N
ARG D
147
65.476
30.248
49.918
1.000
21.77

ATOM
6561
CA
ARG D
147
64.660
31.403
50.244
1.000
20.05

ATOM
6562
CB
ARG D
147
65.524
32.520
50.844
1.000
19.56

ATOM
6563
CG
ARG D
147
65.830
32.272
52.325
1.000
20.31

ATOM
6564
CD
ARG D
147
66.349
33.569
52.933
1.000
25.52

ATOM
6565
NE
ARG D
147
66.652
33.413
54.348
1.000
27.20

ATOM
6566
CZ
ARG D
147
67.852
33.105
54.824
1.000
33.45

ATOM
6567
NH1
ARG D
147
68.015
32.991
56.135
1.000
36.21

ATOM
6568
NH2
ARG D
147
68.871
32.911
53.997
1.000
25.45

ATOM
6569
C
ARG D
147
63.920
31.950
49.032
1.000
27.39

ATOM
6570
O
ARG D
147
62.966
32.713
49.198
1.000
27.36

ATOM
6571
N
GLY D
148
64.343
31.588
47.822
1.000
26.76

ATOM
6572
CA
GLY D
148
63.609
32.056
46.647
1.000
24.31

ATOM
6573
C
GLY D
148
64.307
31.704
45.344
1.000
26.16

ATOM
6574
O
GLY D
148
65.459
31.252
45.369
1.000
23.81

ATOM
6575
N
VAL D
149
63.606
31.924
44.235
1.000
22.84

ATOM
6576
CA
VAL D
149
64.141
31.695
42.891
1.000
22.49

ATOM
6577
CB
VAL D
149
63.528
30.432
42.267
1.000
23.53

ATOM
6578
CG1
VAL D
149
64.113
30.124
40.899
1.000
24.88

ATOM
6579
CG2
VAL D
149
63.759
29.246
43.201
1.000
29.26

ATOM
6580
C
VAL D
149
63.912
32.905
41.991
1.000
24.44

ATOM
6581
O
VAL D
149
62.822
33.468
41.902
1.000
19.35

ATOM
6582
N
ILE D
150
64.972
33.336
41.313
1.000
23.79

ATOM
6583
CA
ILE D
150
64.904
34.472
40.398
1.000
20.68

ATOM
6584
CB
ILE D
150
65.857
35.590
40.835
1.000
23.33

ATOM
6585
CG2
ILE D
150
65.950
36.705
39.800
1.000
23.62

ATOM
6586
CG1
ILE D
150
65.499
36.157
42.217
1.000
22.16

ATOM
6587
CD1
ILE D
150
66.361
37.303
42.679
1.000
22.90

ATOM
6588
C
ILE D
150
65.221
34.002
38.978
1.000
23.90

ATOM
6589
O
ILE D
150
66.265
33.381
38.752
1.000
24.70

ATOM
6590
N
ILE D
151
64.323
34.284
38.042
1.000
19.69

ATOM
6591
CA
ILE D
151
64.461
33.829
36.660
1.000
18.08

ATOM
6592
CB
ILE D
151
63.373
32.811
36.275
1.000
20.01

ATOM
6593
CG2
ILE D
151
63.556
32.325
34.840
1.000
16.55

ATOM
6594
CG
ILE D
151
63.272
31.620
37.227
1.000
21.12

ATOM
6595
CD1
ILE D
151
62.210
30.603
36.855
1.000
22.94

ATOM
6596
C
ILE D
151
64.402
35.029
35.721
1.000
23.47

ATOM
6597
O
ILE D
151
63.402
35.757
35.733
1.000
23.16

ATOM
6598
N
ASN D
152
65.469
35.201
34.939
1.000
22.25

ATOM
6599
CA
ASN D
152
65.566
36.340
34.031
1.000
17.00

ATOM
6600
CB
ASN D
152
66.939
36.993
34.163
1.000
18.22

ATOM
6601
CG
ASN D
152
67.347
37.129
35.623
1.000
22.84

ATOM
6602
OD1
ASN D
152
68.340
36.563
36.091
1.000
31.50

ATOM
6603
ND2
ASN D
152
66.542
37.898
36.341
1.000
16.63

ATOM
6604
C
ASN D
152
65.316
35.937
32.581
1.000
20.23

ATOM
6605
O
ASN D
152
65.391
34.767
32.229
1.000
21.50

ATOM
6606
N
THR D
153
65.014
36.907
31.733
1.000
23.06

ATOM
6607
CA
THR D
153
64.800
36.646
30.313
1.000
20.08

ATOM
6608
CB
THR D
153
63.407
37.093
29.843
1.000
22.69

ATOM
6609
OG1
THR D
153
62.392
36.524
30.690
1.000
19.08

ATOM
6610
CG2
THR D
153
63.126
36.586
28.434
1.000
22.90

ATOM
6611
C
THR D
153
65.868
37.376
29.503
1.000
19.71

ATOM
6612
O
THR D
153
65.902
38.606
29.459
1.000
18.87

ATOM
6613
N
ALA D
154
66.757
36.605
28.882
1.000
19.04

ATOM
6614
CA
ALA D
154
67.764
37.172
27.989
1.000
20.22

ATOM
6615
CB
ALA D
154
69.095
36.482
28.191
1.000
14.81

ATOM
6616
C
ALA D
154
67.240
37.026
26.557
1.000
21.98

ATOM
6617
O
ALA D
154
66.100
37.430
26.300
1.000
20.90

ATOM
6618
N
SER D
155
68.029
36.446
25.669
1.000
22.69

ATOM
6619
CA
SER D
155
67.658
36.189
24.279
1.000
20.37

ATOM
6620
CE
SER D
155
67.301
37.486
23.550
1.000
21.64

ATOM
6621
OG
SER D
155
67.329
37.338
22.133
1.000
21.48

ATOM
6622
C
SER D
155
68.801
35.494
23.554
1.000
18.34

ATOM
6623
O
SER D
155
69.956
35.714
23.932
1.000
19.68

ATOM
6624
N
VAL D
156
68.553
34.690
22.514
1.000
15.42

ATOM
6625
CA
VAL D
156
69.710
34.158
21.782
1.000
17.65

ATOM
6626
CB
VAL D
156
69.313
33.125
20.714
1.000
21.51

ATOM
6627
CG1
VAL D
156
68.671
31.920
21.384
1.000
23.31

ATOM
6628
CG2
VAL D
156
68.391
33.752
19.683
1.000
24.15

ATOM
6629
C
VAL D
156
70.522
35.265
21.125
1.000
15.00

ATOM
6630
O
VAL D
156
71.678
35.056
20.758
1.000
21.65

ATOM
6631
N
ALA D
157
69.976
36.468
20.988
1.000
17.14

ATOM
6632
CA
ALA D
157
70.710
37.651
20.578
1.000
17.24

ATOM
6633
CB
ALA D
157
69.769
38.855
20.568
1.000
13.94

ATOM
6634
C
ALA D
157
71.916
37.921
21.470
1.000
23.46

ATOM
6635
O
ALA D
157
72.845
38.627
21.064
1.000
21.41

ATOM
6636
N
ALA D
158
71.942
37.380
22.689
1.000
23.28

ATOM
6637
CA
ALA D
158
73.113
37.504
23.546
1.000
23.19

ATOM
6638
CE
ALA D
158
72.861
36.891
24.918
1.000
18.33

ATOM
6639
C
ALA D
158
74.327
36.834
22.904
1.000
20.07

ATOM
6640
O
ALA D
158
75.477
37.201
23.164
1.000
18.25

ATOM
6641
N
PHE D
159
74.043
35.844
22.068
1.000
16.93

ATOM
6642
CA
PHE D
159
75.090
34.998
21.504
1.000
20.37

ATOM
6643
CE
PHE D
159
74.764
33.527
21.785
1.000
22.16

ATOM
6644
CG
PHE D
159
74.507
33.240
23.261
1.000
23.66

ATOM
6645
CD1
PHE D
159
73.247
32.850
23.687
1.000
24.05

ATOM
6646
CD2
PHE D
159
75.528
33.361
24.184
1.000
21.58

ATOM
6647
CE1
PHE D
159
72.996
32.585
25.025
1.000
21.33

ATOM
6648
CE2
PHE D
159
75.285
33.112
25.522
1.000
26.43

ATOM
6649
CZ
PHE D
159
74.024
32.723
25.940
1.000
22.81

ATOM
6650
C
PHE D
159
75.301
35.191
20.004
1.000
26.53

ATOM
6651
O
PHE D
159
76.448
35.093
19.557
1.000
22.13

ATOM
6652
N
GLU D
160
74.247
35.455
19.235
1.000
22.81

ATOM
6653
CA
GLU D
160
74.367
35.655
17.797
1.000
25.82

ATOM
6654
CB
GLU D
160
73.868
34.471
16.977
1.000
26.92

ATOM
6655
CG
GLU D
160
74.398
33.097
17.272
1.000
31.97

ATOM
6656
CD
GLU D
160
73.390
32.186
17.945
1.000
33.94

ATOM
6657
OE1
GLU D
160
73.834
31.464
18.863
1.000
27.97

ATOM
6658
OE2
GLU D
160
72.188
32.168
17.592
1.000
26.48

ATOM
6659
C
GLU D
160
73.553
36.876
17.356
1.000
21.87

ATOM
6660
O
GLU D
160
72.678
36.727
16.497
1.000
19.91

ATOM
6661
N
GLY D
161
73.821
38.038
17.936
1.000
18.43

ATOM
6662
CA
GLY D
161
73.065
39.235
17.596
1.000
18.74

ATOM
6663
C
GLY D
161
73.061
39.461
16.090
1.000
23.77

ATOM
6664
O
GLY D
161
74.125
39.344
15.479
1.000
20.48

ATOM
6665
N
GLN D
162
71.900
39.766
15.529
1.000
20.27

ATOM
6666
CA
GLN D
162
71.720
39.960
14.104
1.000
23.42

ATOM
6667
CB
GLN D
162
70.259
39.671
13.743
1.000
21.25

ATOM
6668
CG
GLN D
162
69.841
38.219
13.946
1.000
23.82

ATOM
6669
CD
GLN D
162
68.525
37.938
13.233
1.000
27.75

ATOM
6670
OE1
GLN D
162
67.457
38.360
13.678
1.000
28.35

ATOM
6671
NE2
GLN D
162
68.613
37.233
12.110
1.000
23.89

ATOM
6672
C
GLN D
162
72.061
41.373
13.650
1.000
27.25

ATOM
6673
O
GLN D
162
72.231
42.269
14.481
1.000
19.80

ATOM
6674
N
VAL D
163
72.134
41.570
12.323
1.000
21.48

ATOM
6675
CA
VAL D
163
72.258
42.948
11.835
1.000
19.83

ATOM
6676
CB
VAL D
163
72.277
43.041
10.302
1.000
20.25

ATOM
6677
CG1
VAL D
163
72.244
44.493
9.853
1.000
20.85

ATOM
6678
CG2
VAL D
163
73.516
42.368
9.723
1.000
13.02

ATOM
6679
C
VAL D
163
71.087
43.765
12.382
1.000
22.78

ATOM
6680
O
VAL D
163
69.938
43.310
12.304
1.000
26.26

ATOM
6681
N
GLY D
164
71.354
44.932
12.951
1.000
21.30

ATOM
6682
CA
GLY D
164
70.329
45.774
13.539
1.000
20.37

ATOM
6683
C
GLY D
164
70.094
45.539
15.021
1.000
22.49

ATOM
6684
O
GLY D
164
69.353
46.305
15.649
1.000
24.72

ATOM
6685
N
GLN D
165
70.695
44.515
15.613
1.000
23.42

ATOM
6686
CA
GLN D
165
70.439
44.131
16.990
1.000
23.82

ATOM
6687
CB
GLN D
165
70.290
42.598
17.070
1.000
22.26

ATOM
6688
CG
GLN D
165
68.949
42.087
16.586
1.000
27.27

ATOM
6689
CD
GLN D
165
68.682
40.656
16.998
1.000
27.39

ATOM
6690
OE1
GLN D
165
69.560
39.798
16.983
1.000
23.93

ATOM
6691
NE2
GLN D
165
67.434
40.395
17.379
1.000
30.12

ATOM
6692
C
GLN D
165
71.506
44.522
18.001
1.000
23.76

ATOM
6693
O
GLN D
165
71.501
43.947
19.103
1.000
24.07

ATOM
6694
N
ALA D
166
72.408
45.444
17.708
1.000
17.21

ATOM
6695
CA
ALA D
166
73.443
45.806
18.674
1.000
19.58

ATOM
6696
CB
ALA D
166
74.299
46.938
18.104
1.000
21.71

ATOM
6697
C
ALA D
166
72.925
46.236
20.043
1.000
21.41

ATOM
6698
O
ALA D
166
73.392
45.739
21.072
1.000
21.84

ATOM
6699
N
ALA D
167
71.987
47.182
20.137
1.000
19.77

ATOM
6700
CA
ALA D
167
71.574
47.641
21.470
1.000
20.56

ATOM
6701
CB
ALA D
167
70.649
48.841
21.357
1.000
19.93

ATOM
6702
C
ALA D
167
70.916
46.514
22.258
1.000
23.33

ATOM
6703
O
ALA D
167
71.250
46.237
23.410
1.000
23.45

ATOM
6704
N
TYR D
168
69.963
45.845
21.612
1.000
21.23

ATOM
6705
CA
TYR D
168
69.279
44.702
22.199
1.000
18.68

ATOM
6706
CE
TYR D
168
68.301
44.123
21.175
1.000
19.46

ATOM
6707
CG
TYR D
168
67.308
43.119
21.706
1.000
17.17

ATOM
6708
CD1
TYR D
168
66.289
43.509
22.577
1.000
20.81

ATOM
6709
CE1
TYR D
168
65.389
42.575
23.056
1.000
17.29

ATOM
6710
CD2
TYR D
168
67.393
41.785
21.336
1.000
14.49

ATOM
6711
CE2
TYR D
168
66.496
40.846
21.809
1.000
18.56

ATOM
6712
CZ
TYR D
168
65.494
41.263
22.672
1.000
22.02

ATOM
6713
OH
TYR D
168
64.599
40.334
23.142
1.000
21.10

ATOM
6714
C
TYR D
168
70.264
43.634
22.647
1.000
22.16

ATOM
6715
O
TYR D
168
70.176
43.093
23.750
1.000
22.67

ATOM
6716
N
SER D
169
71.222
43.314
21.778
1.000
19.55

ATOM
6717
CA
SER D
169
72.216
42.298
22.096
1.000
17.20

ATOM
6718
CE
SER D
169
73.152
42.059
20.915
1.000
18.47

ATOM
6719
OG
SER D
169
72.489
41.424
19.838
1.000
21.29

ATOM
6720
C
SER D
169
73.023
42.705
23.328
1.000
20.02

ATOM
6721
O
SER D
169
73.348
41.871
24.172
1.000
24.34

ATOM
6722
N
ALA D
170
73.343
43.985
23.419
1.000
20.02

ATOM
6723
CA
ALA D
170
74.107
44.518
24.540
1.000
17.28

ATOM
6724
CB
ALA D
170
74.415
45.986
24.317
1.000
16.21

ATOM
6725
C
ALA D
170
73.324
44.324
25.834
1.000
22.82

ATOM
6726
O
ALA D
170
73.862
43.921
26.866
1.000
21.81

ATOM
6727
N
SER D
171
72.027
44.617
25.765
1.000
19.01

ATOM
6728
CA
SER D
171
71.196
44.486
26.965
1.000
20.11

ATOM
6729
CE
SER D
171
69.838
45.160
26.723
1.000
18.33

ATOM
6730
OG
SER D
171
68.954
44.319
26.011
1.000
16.83

ATOM
6731
C
SER D
171
71.042
43.034
27.378
1.000
18.43

ATOM
6732
O
SER D
171
71.058
42.715
28.571
1.000
25.54

ATOM
6733
N
LYS D
172
70.894
42.104
26.438
1.000
16.24

ATOM
6734
CA
LYS D
172
70.682
40.710
26.836
1.000
18.91

ATOM
6735
CB
LYS D
172
69.934
39.934
25.747
1.000
18.86

ATOM
6736
CG
LYS D
172
68.587
40.565
25.386
1.000
18.26

ATOM
6737
CD
LYS D
172
67.692
40.665
26.608
1.000
22.32

ATOM
6738
CE
LYS D
172
66.249
40.992
26.239
1.000
20.18

ATOM
6739
NZ
LYS D
172
65.329
40.645
27.368
1.000
15.72

ATOM
6740
C
LYS D
172
72.001
40.028
27.183
1.000
22.11

ATOM
6741
O
LYS D
172
72.064
39.103
27.992
1.000
18.61

ATOM
6742
N
GLY D
173
73.093
40.486
26.578
1.000
22.19

ATOM
6743
CA
GLY D
173
74.416
39.982
26.932
1.000
21.20

ATOM
6744
C
GLY D
173
74.755
40.367
28.368
1.000
24.62

ATOM
6745
O
GLY D
173
75.413
39.611
29.088
1.000
19.92

ATOM
6746
N
GLY D
174
74.290
41.550
28.754
1.000
18.59

ATOM
6747
CA
GLY D
174
74.439
42.031
30.122
1.000
20.37

ATOM
6748
C
GLY D
174
73.709
41.098
31.069
1.000
18.89

ATOM
6749
O
GLY D
174
74.213
40.687
32.107
1.000
18.97

ATOM
6750
N
ILE D
175
72.486
40.722
30.700
1.000
20.45

ATOM
6751
CA
ILE D
175
71.723
39.800
31.524
1.000
17.82

ATOM
6752
CB
ILE D
175
70.355
39.443
30.914
1.000
20.89

ATOM
6753
CG2
ILE D
175
69.652
38.433
31.819
1.000
20.20

ATOM
6754
CD1
ILE D
175
69.440
40.623
30.598
1.000
23.10

ATOM
6755
CD1
ILE D
175
68.826
41.265
31.823
1.000
32.75

ATOM
6756
C
ILE D
175
72.507
38.502
31.715
1.000
21.19

ATOM
6757
O
ILE D
175
72.707
38.002
32.820
1.000
19.56

ATOM
6758
N
VAL D
176
72.955
37.955
30.580
1.000
14.04

ATOM
6759
CA
VAL D
176
73.713
36.712
30.628
1.000
11.58

ATOM
6760
CB
VAL D
176
74.130
36.242
29.227
1.000
17.57

ATOM
6761
CD1
VAL D
176
75.234
35.197
29.299
1.000
17.28

ATOM
6762
CG2
VAL D
176
72.935
35.658
28.488
1.000
17.75

ATOM
6763
C
VAL D
176
74.926
36.885
31.530
1.000
17.55

ATOM
6764
O
VAL D
176
75.165
36.092
32.446
1.000
21.64

ATOM
6765
N
GLY D
177
75.699
37.937
31.293
1.000
18.96

ATOM
6766
CA
GLY D
177
76.901
38.179
32.074
1.000
22.45

ATOM
6767
C
GLY D
177
76.665
38.201
33.569
1.000
23.71

ATOM
6768
O
GLY D
177
77.389
37.578
34.353
1.000
23.04

ATOM
6769
N
MET D
178
75.642
38.921
34.024
1.000
20.74

ATOM
6770
CA
MET D
178
75.510
39.100
35.474
1.000
16.25

ATOM
6771
CB
MET D
178
74.805
40.429
35.761
1.000
17.85

ATOM
6772
CG
MET D
178
73.310
40.419
35.552
1.000
20.61

ATOM
6773
SD
MET D
178
72.557
42.064
35.615
1.000
22.26

ATOM
6774
CE
MET D
178
70.829
41.601
35.430
1.000
20.09

ATOM
6775
C
MET D
178
74.798
37.935
36.138
1.000
21.07

ATOM
6776
O
MET D
178
74.650
37.936
37.365
1.000
26.74

ATOM
6777
N
THR D
179
74.365
36.937
35.377
1.000
17.91

ATOM
6778
CA
THR D
179
73.662
35.794
35.963
1.000
17.03

ATOM
6779
CE
THR D
179
73.222
34.809
34.867
1.000
17.80

ATOM
6780
OG1
THR D
179
72.125
35.389
34.132
1.000
20.57

ATOM
6781
CG2
THR D
179
72.653
33.530
35.435
1.000
13.48

ATOM
6782
C
THR D
179
74.503
35.081
37.016
1.000
24.62

ATOM
6783
O
THR D
179
74.029
34.783
38.118
1.000
19.91

ATOM
6784
N
LEU D
180
75.766
34.780
36.726
1.000
22.11

ATOM
6785
CA
LEU D
180
76.579
34.011
37.660
1.000
20.85

ATOM
6786
CB
LEU D
180
77.853
33.468
37.000
1.000
17.23

ATOM
6787
CG
LEU D
180
78.726
32.563
37.868
1.000
23.31

ATOM
6788
CD1
LEU D
180
77.953
31.346
38.359
1.000
24.22

ATOM
6789
CD2
LEU D
180
79.961
32.102
37.105
1.000
20.74

ATOM
6790
C
LEU D
180
76.966
34.827
38.885
1.000
17.46

ATOM
6791
O
LEU D
180
76.746
34.341
40.005
1.000
22.39

ATOM
6792
N
PRO D
181
77.537
36.015
38.738
1.000
20.05

ATOM
6793
CD
PRO D
181
77.909
36.728
37.503
1.000
20.38

ATOM
6794
CA
PRO D
181
77.888
36.811
39.924
1.000
19.83

ATOM
6795
CE
PRO D
181
78.326
38.161
39.362
1.000
21.03

ATOM
6796
CG
PRO D
181
77.874
38.169
37.937
1.000
18.92

ATOM
6797
C
PRO D
181
76.689
37.006
40.852
1.000
27.11

ATOM
6798
O
PRO D
181
76.820
36.935
42.073
1.000
21.78

ATOM
6799
N
ILE D
182
75.503
37.244
40.292
1.000
19.37

ATOM
6800
CA
ILE D
182
74.352
37.452
41.183
1.000
21.03

ATOM
6801
CB
ILE D
182
73.147
38.033
40.425
1.000
21.11

ATOM
6802
CG2
ILE D
182
71.913
38.080
41.319
1.000
21.57

ATOM
6803
CG1
ILE D
182
73.455
39.408
39.820
1.000
16.88

ATOM
6804
CD1
ILE D
182
72.306
40.003
39.025
1.000
17.64

ATOM
6805
C
ILE D
182
74.017
36.152
41.893
1.000
23.82

ATOM
6806
O
ILE D
182
73.800
36.167
43.107
1.000
26.22

ATOM
6807
N
ALA D
183
74.005
35.031
41.184
1.000
17.60

ATOM
6808
CA
ALA D
183
73.869
33.728
41.811
1.000
19.31

ATOM
6809
CE
ALA D
183
74.016
32.621
40.773
1.000
21.49

ATOM
6810
C
ALA D
183
74.896
33.551
42.927
1.000
26.28

ATOM
6811
O
ALA D
183
74.589
33.085
44.030
1.000
23.11

ATOM
6812
N
ARG D
184
76.151
33.915
42.660
1.000
22.78

ATOM
6813
CA
ARG D
184
77.187
33.722
43.684
1.000
22.18

ATOM
6814
CE
ARG D
184
78.580
33.916
43.085
1.000
18.95

ATOM
6815
CG
ARG D
184
78.931
32.878
42.009
1.000
17.71

ATOM
6816
CD
ARG D
184
80.151
33.303
41.199
1.000
17.27

ATOM
6817
NE
ARG D
184
80.957
32.169
40.756
1.000
22.17

ATOM
6818
CZ
ARG D
184
82.097
32.262
40.075
1.000
20.70

ATOM
6819
NE1
ARG D
184
82.769
31.175
39.713
1.000
18.72

ATOM
6820
NH2
ARG D
184
82.604
33.433
39.729
1.000
20.42

ATOM
6821
C
ARG D
184
76.928
34.665
44.856
1.000
21.95

ATOM
6822
O
ARG D
184
77.117
34.326
46.023
1.000
20.58

ATOM
6823
N
ASP D
185
76.481
35.880
44.553
1.000
17.40

ATOM
6824
CA
ASP D
185
76.133
36.868
45.5S9
1.000
21.73

ATOM
6825
CE
ASP D
185
75.556
38.119
44.889
1.000
23.14

ATOM
6826
CG
ASP D
185
76.585
39.134
44.439
1.000
24.36

ATOM
6827
OD1
ASP D
185
76.175
40.163
43.853
1.000
18.99

ATOM
6828
OD2
ASP D
185
77.797
38.915
44.663
1.000
18.75

ATOM
6829
C
ASP D
185
75.106
36.341
46.558
1.000
24.87

ATOM
6830
O
ASP D
185
75.252
36.478
47.770
1.000
21.06

ATOM
6831
N
LEU D
186
74.045
35.743
46.034
1.000
19.83

ATOM
6832
CA
LEU D
186
72.899
35.313
46.806
1.000
19.79

ATOM
6833
CB
LEU D
186
71.614
35.532
45.994
1.000
20.78

ATOM
6834
CG
LEU D
186
71.429
36.936
45.408
1.000
20.00

ATOM
6835
CD1
LEU D
186
70.170
37.010
44.564
1.000
19.62

ATOM
6836
CD2
LEU D
186
71.393
37.976
46.520
1.000
19.25

ATOM
6837
C
LEU D
186
73.005
33.854
47.219
1.000
22.76

ATOM
6838
O
LEU D
186
72.143
33.371
47.959
1.000
23.72

ATOM
6839
N
ALA D
187
74.028
33.132
46.764
1.000
15.74

ATOM
6840
CA
ALA D
187
74.188
31.740
47.180
1.000
17.58

ATOM
6841
CB
ALA D
187
75.487
31.143
46.634
1.000
15.12

ATOM
6842
C
ALA D
187
74.159
31.552
48.696
1.000
23.20

ATOM
6843
O
ALA D
187
73.479
30.621
49.150
1.000
21.94

ATOM
6844
N
PRO D
188
74.875
32.326
49.499
1.000
29.64

ATOM
6845
CD
PRO D
188
75.803
33.421
49.152
1.000
28.61

ATOM
6846
CA
PRO D
188
74.830
32.099
50.954
1.000
30.11

ATOM
6847
CB
PRO D
188
75.861
33.088
51.519
1.000
29.57

ATOM
6848
CG
PRO D
188
76.705
33.486
50.354
1.000
33.79

ATOM
6849
C
PRO D
188
73.473
32.383
51.576
1.000
32.97

ATOM
6850
O
PRO D
188
73.255
32.077
52.759
1.000
31.98

ATOM
6851
N
ILE D
189
72.517
32.962
50.845
1.000
29.31

ATOM
6852
CA
ILE D
189
71.210
33.125
51.505
1.000
26.68

ATOM
6853
CB
ILE D
189
70.758
34.590
51.557
1.000
30.84

ATOM
6854
CG2
ILE D
189
71.669
35.406
52.466
1.000
35.78

ATOM
6855
CG1
ILE D
189
70.637
35.290
50.199
1.000
24.66

ATOM
6856
CD1
ILE D
189
70.003
36.662
50.353
1.000
27.16

ATOM
6857
C
ILE D
189
70.141
32.266
50.844
1.000
23.68

ATOM
6858
O
ILE D
189
68.958
32.358
51.180
1.000
25.41

ATOM
6859
N
GLY D
190
70.549
31.397
49.922
1.000
19.61

ATOM
6860
CA
GLY D
190
69.627
30.428
49.369
1.000
20.36

ATOM
6861
C
GLY D
190
68.728
30.959
48.283
1.000
23.23

ATOM
6862
O
GLY D
190
67.612
30.458
48.095
1.000
25.02

ATOM
6863
N
ILE D
191
69.182
31.962
47.526
1.000
17.82

ATOM
6864
CA
ILE D
191
68.337
32.406
46.411
1.000
20.45

ATOM
6865
CB
ILE D
191
68.109
33.923
46.468
1.000
20.65

ATOM
6866
CG2
ILE D
191
67.353
34.418
45.249
1.000
21.25

ATOM
6867
CD1
ILE D
191
67.405
34.371
47.764
1.000
20.50

ATOM
6868
CD1
ILE D
191
67.413
35.881
47.921
1.000
22.01

ATOM
6869
C
ILE D
191
68.967
31.985
45.089
1.000
23.63

ATOM
6870
O
ILE D
191
70.081
32.408
44.781
1.000
23.08

ATOM
6871
N
ARG D
192
68.262
31.147
44.326
1.000
20.80

ATOM
6872
CA
ARG D
192
68.796
30.736
43.025
1.000
18.93

ATOM
6873
CB
ARG D
192
68.201
29.418
42.545
1.000
18.33

ATOM
6874
CG
ARG D
192
68.551
28.224
43.416
1.000
22.10

ATOM
6875
CD
ARG D
192
68.122
26.915
42.778
1.000
21.75

ATOM
6876
NE
ARG D
192
66.697
26.654
42.903
1.000
17.92

ATOM
6877
CZ
ARG D
192
65.845
26.507
41.903
1.000
22.86

ATOM
6878
NH1
ARG D
192
66.271
26.602
40.645
1.000
20.64

ATOM
6879
NH2
ARG D
192
64.562
26.265
42.159
1.000
21.71

ATOM
6880
C
ARG D
192
68.527
31.823
41.989
1.000
20.00

ATOM
6881
O
ARG D
192
67.505
32.498
42.062
1.000
18.87

ATOM
6882
N
VAL D
193
69.451
31.960
41.050
1.000
23.51

ATOM
6883
CA
VAL D
193
69.317
32.881
39.924
1.000
20.41

ATOM
6884
CB
VAL D
193
70.296
34.057
39.981
1.000
18.86

ATOM
6885
CG1
VAL D
193
69.897
35.108
38.951
1.000
21.21

ATOM
6886
CG2
VAL D
193
70.350
34.707
41.353
1.000
18.23

ATOM
6887
C
VAL D
193
69.512
32.096
38.623
1.000
20.97

ATOM
6888
O
VAL D
193
70.555
31.457
38.454
1.000
17.73

ATOM
6889
N
MET D
194
68.513
32.133
37.756
1.000
20.64

ATOM
6890
CA
MET D
194
68.529
31.440
36.476
1.000
22.07

ATOM
6891
CE
MET D
194
67.648
30.190
36.500
1.000
21.33

ATOM
6892
CG
MET D
194
68.224
29.017
37.281
1.000
20.38

ATOM
6893
SD
MET D
194
69.616
28.228
36.442
1.000
20.76

ATOM
6894
CE
MET D
194
68.837
27.768
34.884
1.000
17.01

ATOM
6895
C
MET D
194
68.073
32.356
35.339
1.000
27.30

ATOM
6896
O
MET D
194
67.397
33.367
35.539
1.000
21.16

ATOM
6897
N
THR D
195
68.455
31.985
34.114
1.000
23.91

ATOM
6898
CA
THR D
195
68.128
32.823
32.962
1.000
20.67

ATOM
6899
CB
THR D
195
69.312
33.716
32.570
1.000
18.13

ATOM
6900
OG1
THR D
195
69.548
34.706
33.575
1.000
19.08

ATOM
6901
CG2
THR D
195
68.991
34.480
31.288
1.000
22.37

ATOM
6902
C
THR D
195
67.724
31.964
31.771
1.000
18.10

ATOM
6903
O
THR D
195
68.327
30.934
31.484
1.000
22.46

ATOM
6904
N
ILE D
196
66.684
32.390
31.071
1.000
18.33

ATOM
6905
CA
ILE D
196
66.212
31.696
29.883
1.000
20.86

ATOM
6906
CE
ILE D
196
64.703
31.394
29.937
1.000
22.77

ATOM
6907
CG2
ILE D
196
64.239
30.731
28.643
1.000
14.26

ATOM
6908
CG1
ILE D
196
64.281
30.579
31.162
1.000
18.84

ATOM
6909
CD1
ILE D
196
62.793
30.588
31.442
1.000
22.27

ATOM
6910
C
ILE D
196
66.532
32.575
28.673
1.000
20.83

ATOM
6911
O
ILE D
196
66.290
33.784
28.750
1.000
20.98

ATOM
6912
N
ALA D
197
67.078
31.999
27.608
1.000
17.54

ATOM
6913
CA
ALA D
197
67.345
32.773
26.391
1.000
20.67

ATOM
6914
CE
ALA D
197
68.792
32.645
25.951
1.000
13.19

ATOM
6915
C
ALA D
197
66.403
32.309
25.282
1.000
17.72

ATOM
6916
O
ALA D
197
66.687
31.344
24.578
1.000
18.42

ATOM
6917
N
PRO D
198
65.261
32.961
25.124
1.000
17.47

ATOM
6918
CD
PRO D
198
64.771
34.152
25.846
1.000
15.15

ATOM
6919
CA
PRO D
198
64.300
32.495
24.121
1.000
17.20

ATOM
6920
CE
PRO D
198
63.032
33.292
24.430
1.000
17.15

ATOM
6921
CG
PRO D
198
63.273
33.967
25.750
1.000
17.24

ATOM
6922
C
PRO D
198
64.791
32.817
22.712
1.000
22.31

ATOM
6923
O
PRO D
198
65.467
33.829
22.497
1.000
19.83

ATOM
6924
N
GLY D
199
64.436
31.965
21.749
1.000
17.55

ATOM
6925
CA
GLY D
199
64.755
32.287
20.357
1.000
21.07

ATOM
6926
C
GLY D
199
63.681
33.220
19.807
1.000
24.15

ATOM
6927
O
GLY D
199
63.736
34.427
20.012
1.000
27.73

ATOM
6928
N
LEU D
200
62.713
32.635
19.118
1.000
24.38

ATOM
6929
CA
LEU D
200
61.623
33.365
18.488
1.000
24.40

ATOM
6930
CE
LEU D
200
61.721
33.221
16.967
1.000
28.91

ATOM
6931
CG
LEU D
200
63.108
33.444
16.346
1.000
27.16

ATOM
6932
CD1
LEU D
200
63.130
32.970
14.899
1.000
24.33

ATOM
6933
CD2
LEU D
200
63.516
34.904
16.436
1.000
25.63

ATOM
6934
C
LEU D
200
60.277
32.847
18.981
1.000
18.97

ATOM
6935
O
LEU D
200
60.000
31.656
18.864
1.000
22.53

ATOM
6936
N
PHE D
201
59.451
33.728
19.530
1.000
18.45

ATOM
6937
CA
PHE D
201
58.189
33.308
20.124
1.000
22.22

ATOM
6938
CE
PHE D
201
58.225
33.382
21.657
1.000
17.08

ATOM
6939
CG
PHE D
201
58.836
32.160
22.310
1.000
21.74

ATOM
6940
CD1
PHE D
201
60.205
31.942
22.252
1.000
19.60

ATOM
6941
CD2
PHE D
201
58.040
31.245
22.973
1.000
22.47

ATOM
6942
CE1
PHE D
201
60.756
30.818
22.845
1.000
18.88

ATOM
6943
CE2
PHE D
201
58.586
30.117
23.556
1.000
23.20

ATOM
6944
CZ
PHE D
201
59.952
29.898
23.490
1.000
18.53

ATOM
6945
C
PHE D
201
57.036
34.178
19.635
1.000
23.36

ATOM
6946
O
PHE D
201
57.182
35.383
19.451
1.000
24.36

ATOM
6947
N
GLY D
202
55.883
33.547
19.455
1.000
26.66

ATOM
6948
CA
GLY D
202
54.685
34.243
19.015
1.000
29.50

ATOM
6949
C
GLY D
202
54.093
35.130
20.095
1.000
28.23

ATOM
6950
O
GLY D
202
53.208
34.713
20.838
1.000
32.75

ATOM
6951
N
THR D
203
54.592
36.358
20.189
1.000
26.75

ATOM
6952
CA
THR D
203
54.092
37.329
21.155
1.000
26.92

ATOM
6953
CB
THR D
203
55.088
37.519
22.314
1.000
27.56

ATOM
6954
OG1
THR D
203
56.204
38.265
21.819
1.000
25.50

ATOM
6955
CG2
THR D
203
55.616
36.186
22.821
1.000
27.78

ATOM
6956
C
THR D
203
53.858
38.666
20.461
1.000
29.42

ATOM
6957
O
THR D
203
54.258
38.806
19.297
1.000
24.92

ATOM
6958
N
PRO D
204
53.218
39.635
21.103
1.000
27.18

ATOM
6959
CD
PRO D
204
52.478
39.519
22.386
1.000
31.23

ATOM
6960
CA
PRO D
204
53.106
40.986
20.553
1.000
28.92

ATOM
6961
CB
PRO D
204
52.302
41.731
21.634
1.000
28.70

ATOM
6962
CG
PRO D
204
51.473
40.641
22.248
1.000
28.07

ATOM
6963
C
PRO D
204
54.434
41.703
20.347
1.000
34.10

ATOM
6964
O
PRO D
204
54.463
42.748
19.681
1.000
27.57

ATOM
6965
N
LEU D
205
55.538
41.207
20.886
1.000
36.63

ATOM
6966
CA
LEU D
205
56.839
41.839
20.646
1.000
31.29

ATOM
6967
CB
LEU D
205
57.970
41.039
21.289
1.000
25.52

ATOM
6968
CG
LEU D
205
59.327
41.738
21.381
1.000
33.83

ATOM
6969
CD1
LEU D
205
59.273
42.904
22.357
1.000
31.80

ATOM
6970
CD2
LEU D
205
60.421
40.756
21.777
1.000
30.03

ATOM
6971
C
LEU D
205
57.101
41.988
19.140
1.000
27.67

ATOM
6972
O
LEU D
205
57.624
43.019
18.719
1.000
29.68

ATOM
6973
N
LEU D
206
56.733
40.950
18.405
1.000
22.15

ATOM
6974
CA
LEU D
206
56.956
40.766
16.983
1.000
35.07

ATOM
6975
CB
LEU D
206
57.054
39.268
16.650
1.000
30.73

ATOM
6976
CG
LEU D
206
58.128
38.495
17.421
1.000
32.57

ATOM
6977
CD1
LEU D
206
58.364
37.143
16.772
1.000
23.12

ATOM
6978
CD2
LEU D
206
59.406
39.318
17.516
1.000
28.08

ATOM
6979
C
LEU D
206
55.868
41.380
16.110
1.000
38.19

ATOM
6980
O
LEU D
206
55.972
41.388
14.881
1.000
44.19

ATOM
6981
N
THR D
207
54.818
41.901
16.733
1.000
35.74

ATOM
6982
CA
THR D
207
53.710
42.454
15.950
1.000
36.62

ATOM
6983
CB
THR D
207
52.642
42.991
16.923
1.000
42.60

ATOM
6984
OG1
THR D
207
51.904
41.854
17.406
1.000
42.42

ATOM
6985
CG2
THR D
207
51.661
43.916
16.235
1.000
51.83

ATOM
6986
C
THR D
207
54.164
43.523
14.976
1.000
37.29

ATOM
6987
O
THR D
207
53.783
43.529
13.800
1.000
36.09

ATOM
6988
N
SER D
208
55.003
44.456
15.420
1.000
37.42

ATOM
6989
CA
SER D
208
55.423
45.544
14.547
1.000
36.45

ATOM
6990
CB
SER D
208
56.185
46.605
15.354
1.000
35.67

ATOM
6991
OG
SER D
208
57.285
46.018
16.032
1.000
47.68

ATOM
6992
CB
SER D
208
56.301
45.092
13.389
1.000
42.44

ATOM
6993
O
SER D
208
56.751
45.943
12.609
1.000
62.16

ATOM
6994
N
LEU D
209
56.581
43.800
13.229
1.000
31.60

ATOM
6995
CA
LEU D
209
57.357
43.396
12.058
1.000
32.92

ATOM
6996
CB
LEU D
209
58.180
42.136
12.299
1.000
35.21

ATOM
6997
CG
LEU D
209
59.199
42.141
13.437
1.000
37.69

ATOM
6998
CD1
LEU D
209
59.658
40.717
13.734
1.000
26.82

ATOM
6999
CD2
LEU D
209
60.373
43.050
13.107
1.000
40.66

ATOM
7000
C
LEU D
209
56.412
43.134
10.888
1.000
40.62

ATOM
7001
O
LEU D
209
55.250
42.782
11.113
1.000
53.21

ATOM
7002
N
PRO D
210
56.905
43.287
9.666
1.000
40.78

ATOM
7003
CD
PRO D
210
58.218
43.811
9.264
1.000
44.53

ATOM
7004
CA
PRO D
210
56.087
42.897
8.513
1.000
33.12

ATOM
7005
CB
PRO D
210
56.967
43.192
7.308
1.000
39.69

ATOM
7006
CG
PRO D
210
58.040
44.099
7.801
1.000
44.13

ATOM
7007
C
PRO D
210
55.796
41.405
8.614
1.000
36.19

ATOM
7008
O
PRO D
210
56.693
40.624
8.946
1.000
42.06

ATOM
7009
N
GLU D
211
54.557
41.025
8.332
1.000
38.31

ATOM
7010
CA
GLU D
211
54.148
39.627
8.332
1.000
37.48

ATOM
7011
CE
GLU D
211
52.757
39.506
7.704
1.000
39.60

ATOM
7012
CG
GLU D
211
52.665
38.453
6.614
1.000
49.11

ATOM
7013
CD
GLU D
211
52.074
37.151
7.118
1.000
61.74

ATOM
7014
OE1
GLU D
211
51.238
36.564
6.399
1.000
74.58

ATOM
7015
OE2
GLU D
211
52.450
36.715
8.230
1.000
74.33

ATOM
7016
C
GLU D
211
55.138
38.739
7.586
1.000
42.31

ATOM
7017
O
GLU D
211
55.365
37.585
7.954
1.000
36.56

ATOM
7018
N
LYS D
212
55.738
39.262
6.519
1.000
45.52

ATOM
7019
CA
LYS D
212
56.702
38.481
5.748
1.000
50.03

ATOM
7020
CE
LYS D
212
57.078
39.216
4.469
1.000
48.73

ATOM
7021
C
LYS D
212
57.937
38.146
6.580
1.000
45.32

ATOM
7022
O
LYS D
212
58.293
36.969
6.677
1.000
61.00

ATOM
7023
N
VAL D
213
58.583
39.142
7.177
1.000
37.48

ATOM
7024
CA
VAL D
213
59.729
38.909
8.051
1.000
40.78

ATOM
7025
CE
VAL D
213
60.171
40.192
8.779
1.000
39.38

ATOM
7026
CG1
VAL D
213
61.448
39.944
9.570
1.000
46.30

ATOM
7027
CG2
VAL D
213
60.376
41.330
7.794
1.000
31.44

ATOM
7028
C
VAL D
213
59.407
37.836
9.091
1.000
42.11

ATOM
7029
O
VAL D
213
60.143
36.868
9.280
1.000
39.28

ATOM
7030
N
ARG D
214
58.272
38.029
9.760
1.000
43.00

ATOM
7031
CA
ARG D
214
57.786
37.063
10.736
1.000
46.17

ATOM
7032
CE
ARG D
214
56.400
37.494
11.234
1.000
50.42

ATOM
7033
CG
ARG D
214
56.061
36.950
12.611
1.000
56.83

ATOM
7034
CD
ARG D
214
55.009
37.791
13.317
1.000
65.91

ATOM
7035
NE
ARG D
214
53.760
37.850
12.561
1.000
69.02

ATOM
7036
CZ
ARG D
214
53.306
38.955
11.979
1.000
65.60

ATOM
7037
NE1
ARG D
214
54.004
40.080
12.073
1.000
45.07

ATOM
7038
NE2
ARG D
214
52.163
38.933
11.308
1.000
67.95

ATOM
7039
C
ARG D
214
57.728
35.645
10.179
1.000
41.11

ATOM
7040
O
ARG D
214
58.314
34.726
10.761
1.000
35.07

ATOM
7041
N
ASN D
215
57.034
35.415
9.062
1.000
30.80

ATOM
7042
CA
ASN D
215
56.975
34.059
8.515
1.000
31.83

ATOM
7043
CE
ASN D
215
56.004
33.938
7.338
1.000
37.92

ATOM
7044
CG
ASN D
215
54.623
34.458
7.692
1.000
43.95

ATOM
7045
OD1
ASN D
215
54.286
34.601
8.868
1.000
50.88

ATOM
7046
ND2
ASN D
215
53.821
34.753
6.678
1.000
41.53

ATOM
7047
C
ASN D
215
58.356
33.591
8.078
1.000
26.95

ATOM
7048
O
ASN D
215
58.701
32.421
8.239
1.000
38.41

ATOM
7049
N
PHE D
216
59.168
34.494
7.535
1.000
29.37

ATOM
7050
CA
PHE D
216
60.509
34.039
7.173
1.000
32.74

ATOM
7051
CE
PHE D
216
61.264
35.120
6.393
1.000
39.51

ATOM
7052
CG
PHE D
216
62.718
34.703
6.173
1.000
50.14

ATOM
7053
CD1
PHE D
216
63.025
33.727
5.238
1.000
49.41

ATOM
7054
CD2
PHE D
216
63.742
35.278
6.902
1.000
50.29

ATOM
7055
CE1
PHE D
216
64.335
33.334
5.035
1.000
44.06

ATOM
7056
CE2
PHE D
216
65.054
34.893
6.701
1.000
46.56

ATOM
7057
CZ
PHE D
216
65.348
33.918
5.769
1.000
46.69

ATOM
7058
C
PHE D
216
61.305
33.649
8.414
1.000
39.85

ATOM
7059
O
PHE D
216
62.079
32.688
8.442
1.000
30.19

ATOM
7060
N
LEU D
217
61.137
34.418
9.490
1.000
37.21

ATOM
7061
CA
LEU D
217
61.880
34.075
10.706
1.000
37.90

ATOM
7062
CE
LEU D
217
61.666
35.177
11.744
1.000
34.46

ATOM
7063
CG
LEU D
217
62.236
36.544
11.361
1.000
39.81

ATOM
7064
CD1
LEU D
217
61.332
37.662
11.855
1.000
60.47

ATOM
7065
CD2
LEU D
217
63.649
36.688
11.905
1.000
46.98

ATOM
7066
C
LEU D
217
61.451
32.719
11.245
1.000
36.78

ATOM
7067
O
LEU D
217
62.230
31.827
11.578
1.000
29.88

ATOM
7068
N
ALA D
218
60.133
32.559
11.332
1.000
43.92

ATOM
7069
CA
ALA D
218
59.557
31.298
11.776
1.000
43.98

ATOM
7070
CE
ALA D
218
58.040
31.379
11.691
1.000
38.83

ATOM
7071
C
ALA D
218
60.094
30.130
10.954
1.000
40.99

ATOM
7072
O
ALA D
218
60.383
29.067
11.503
1.000
32.70

ATOM
7073
N
SER D
219
60.227
30.335
9.647
1.000
34.44

ATOM
7074
CA
SER D
219
60.633
29.263
8.743
1.000
35.59

ATOM
7075
CB
SER D
219
60.428
29.707
7.285
1.000
23.01

ATOM
7076
OG
SER D
219
61.418
30.652
6.916
1.000
30.06

ATOM
7077
CB
SER D
219
62.072
28.823
8.963
1.000
33.93

ATOM
7078
O
SER D
219
62.477
27.748
8.509
1.000
33.39

ATOM
7079
N
GLN D
220
62.897
29.608
9.655
1.000
30.98

ATOM
7080
CA
GLN D
220
64.276
29.166
9.859
1.000
27.90

ATOM
7081
CB
GLN D
220
65.195
30.396
9.853
1.000
36.24

ATOM
7082
CG
GLN D
220
65.232
31.099
8.503
1.000
46.18

ATOM
7083
CD
GLN D
220
66.163
30.411
7.518
1.000
54.81

ATOM
7084
OE1
GLN D
220
65.767
29.453
6.849
1.000
66.52

ATOM
7085
NE2
GLN D
220
67.395
30.899
7.444
1.000
60.18

ATOM
7086
C
GLN D
220
64.496
28.378
11.136
1.000
28.60

ATOM
7087
O
GLN D
220
65.625
27.979
11.455
1.000
28.34

ATOM
7088
N
VAL D
221
63.440
28.128
11.908
1.000
25.05

ATOM
7089
CA
VAL D
221
63.609
27.295
13.105
1.000
19.69

ATOM
7090
CB
VAL D
221
62.413
27.458
14.059
1.000
20.39

ATOM
7091
CD1
VAL D
221
62.610
26.648
15.335
1.000
17.64

ATOM
7092
CG2
VAL D
221
62.203
28.931
14.383
1.000
18.24

ATOM
7093
C
VAL D
221
63.780
25.845
12.681
1.000
23.22

ATOM
7094
O
VAL D
221
62.887
25.317
12.012
1.000
24.53

ATOM
7095
N
PRO D
222
64.880
25.184
13.016
1.000
24.73

ATOM
7096
CD
PRO D
222
66.023
25.665
13.817
1.000
24.93

ATOM
7097
CA
PRO D
222
65.088
23.800
12.563
1.000
21.41

ATOM
7098
CB
PRO D
222
66.427
23.404
13.205
1.000
16.76

ATOM
7099
CG
PRO D
222
67.124
24.722
13.388
1.000
21.93

ATOM
7100
C
PRO D
222
64.003
22.834
13.008
1.000
29.64

ATOM
7101
O
PRO D
222
63.404
22.156
12.161
1.000
28.28

ATOM
7102
N
PHE D
223
63.736
22.722
14.313
1.000
23.80

ATOM
7103
CA
PHE D
223
62.666
21.830
14.735
1.000
22.47

ATOM
7104
CB
PHE D
223
63.024
20.345
14.635
1.000
23.46

ATOM
7105
CG
PHE D
223
61.800
19.501
14.996
1.000
26.96

ATOM
7106
CD1
PHE D
223
60.745
19.389
14.106
1.000
27.25

ATOM
7107
CD2
PHE D
223
61.727
18.848
16.214
1.000
24.04

ATOM
7108
CE1
PHE D
223
59.625
18.638
14.426
1.000
26.15

ATOM
7109
CE2
PHE D
223
60.612
18.098
16.536
1.000
24.75

ATOM
7110
CZ
PHE D
223
59.556
17.995
15.647
1.000
24.07

ATOM
7111
C
PHE D
223
62.245
22.127
16.172
1.000
27.70

ATOM
7112
O
PHE D
223
63.118
22.190
17.041
1.000
26.86

ATOM
7113
N
PRO D
224
60.960
22.305
16.446
1.000
29.69

ATOM
7114
CD
PRO D
224
60.423
22.503
17.808
1.000
28.64

ATOM
7115
CA
PRO D
224
59.899
22.326
15.434
1.000
28.89

ATOM
7116
CB
PRO D
224
58.618
22.234
16.255
1.000
31.37

ATOM
7117
CG
PRO D
224
58.975
22.838
17.575
1.000
30.74

ATOM
7118
C
PRO D
224
59.930
23.631
14.638
1.000
27.50

ATOM
7119
O
PRO D
224
60.332
24.659
15.179
1.000
23.79

ATOM
7120
N
SER D
225
59.562
23.535
13.368
1.000
26.30

ATOM
7121
CA
SER D
225
59.718
24.654
12.448
1.000
30.56

ATOM
7122
CE
SER D
225
59.863
24.205
10.995
1.000
39.18

ATOM
7123
OG
SER D
225
60.424
22.921
10.825
1.000
56.39

ATOM
7124
CB
SER D
225
58.529
25.608
12.578
1.000
29.67

ATOM
7125
O
SER D
225
57.621
25.653
11.753
1.000
27.17

ATOM
7126
N
ARG D
226
58.561
26.389
13.650
1.000
26.12

ATOM
7127
CA
ARG D
226
57.502
27.349
13.938
1.000
23.63

ATOM
7128
CB
ARG D
226
56.244
26.629
14.420
1.000
20.50

ATOM
7129
CG
ARG D
226
56.534
25.671
15.576
1.000
19.56

ATOM
7130
CD
ARG D
226
55.319
25.523
16.471
1.000
25.12

ATOM
7131
NE
ARG D
226
55.428
24.429
17.437
1.000
24.67

ATOM
7132
CZ
ARG D
226
55.846
24.588
18.692
1.000
26.53

ATOM
7133
NH1
ARG D
226
55.915
23.545
19.508
1.000
21.62

ATOM
7134
NR2
ARG D
226
56.198
25.789
19.128
1.000
22.97

ATOM
7135
C
ARG D
226
57.985
28.311
15.012
1.000
25.88

ATOM
7136
O
ARG D
226
59.002
28.034
15.650
1.000
27.19

ATOM
7137
N
LEU D
227
57.272
29.410
15.216
1.000
22.50

ATOM
7138
CA
LEU D
227
57.614
30.242
16.371
1.000
25.88

ATOM
7139
CB
LEU D
227
56.803
31.533
16.326
1.000
26.52

ATOM
7140
CG
LEU D
227
57.095
32.428
15.114
1.000
24.01

ATOM
7141
CD1
LEU D
227
56.142
33.614
15.088
1.000
22.93

ATOM
7142
CD2
LEU D
227
58.547
32.883
15.124
1.000
18.44

ATOM
7143
C
LEU D
227
57.366
29.458
17.652
1.000
24.33

ATOM
7144
O
LEU D
227
56.537
28.548
17.677
1.000
20.20

ATOM
7145
N
GLY D
228
58.081
29.787
18.721
1.000
21.98

ATOM
7146
CA
GLY D
228
57.837
29.125
19.996
1.000
20.07

ATOM
7147
C
GLY D
228
56.496
29.562
20.569
1.000
20.67

ATOM
7148
O
GLY D
228
56.058
30.683
20.327
1.000
25.18

ATOM
7149
N
ASP D
229
55.840
28.688
21.311
1.000
21.96

ATOM
7150
CA
ASP D
229
54.566
28.978
21.971
1.000
22.40

ATOM
7151
CB
ASP D
229
53.751
27.696
22.030
1.000
25.51

ATOM
7152
CG
ASP D
229
52.428
27.776
22.752
1.000
38.71

ATOM
7153
OD1
ASP D
229
51.577
26.898
22.478
1.000
53.25

ATOM
7154
OD2
ASP D
229
52.189
28.671
23.585
1.000
37.19

ATOM
7155
C
ASP D
229
54.842
29.536
23.365
1.000
21.25

ATOM
7156
O
ASP D
229
55.580
28.891
24.119
1.000
22.74

ATOM
7157
N
PRO D
230
54.299
30.688
23.715
1.000
23.51

ATOM
7158
CD
PRO D
230
53.440
31.547
22.877
1.000
25.76

ATOM
7159
CA
PRO D
230
54.527
31.282
25.042
1.000
24.49

ATOM
7160
CB
PRO D
230
53.474
32.399
25.093
1.000
24.44

ATOM
7161
CG
PRO D
230
53.403
32.840
23.656
1.000
23.90

ATOM
7162
C
PRO D
230
54.331
30.298
26.184
1.000
24.91

ATOM
7163
O
PRO D
230
55.048
30.381
27.185
1.000
23.08

ATOM
7164
N
ALA D
231
53.405
29.354
26.066
1.000
25.76

ATOM
7165
CA
ALA D
231
53.263
28.311
27.083
1.000
25.88

ATOM
7166
CB
ALA D
231
52.139
27.341
26.750
1.000
16.85

ATOM
7167
C
ALA D
231
54.545
27.504
27.256
1.000
26.87

ATOM
7168
O
ALA D
231
54.831
27.004
28.343
1.000
24.96

ATOM
7169
N
GLU D
232
55.310
27.376
26.170
1.000
22.61

ATOM
7170
CA
GLU D
232
56.565
26.623
26.239
1.000
22.59

ATOM
7171
CB
GLU D
232
57.072
26.343
24.825
1.000
23.36

ATOM
7172
CG
GLU D
232
56.259
25.290
24.103
1.000
22.39

ATOM
7173
CD
GLU D
232
56.491
25.243
22.609
1.000
23.33

ATOM
7174
OE1
GLU D
232
56.947
26.228
21.994
1.000
24.03

ATOM
7175
OE2
GLU D
232
56.200
24.169
22.042
1.000
27.05

ATOM
7176
C
GLU D
232
57.586
27.376
27.080
1.000
21.77

ATOM
7177
O
GLU D
232
58.351
26.775
27.831
1.000
21.99

ATOM
7178
N
TYR D
233
57.391
28.707
26.993
1.000
19.90

ATOM
7179
CA
TYR D
233
58.405
29.480
27.927
1.000
20.05

ATOM
7180
CB
TYR D
233
58.302
30.975
27.612
1.000
19.81

ATOM
7181
CG
TYR D
233
59.053
31.863
28.575
1.000
21.66

ATOM
7182
CD1
TYR D
233
60.405
32.127
28.406
1.000
17.10

ATOM
7183
CE1
TYR D
233
61.093
32.938
29.284
1.000
17.27

ATOM
7184
CD2
TYR D
233
58.410
32.448
29.662
1.000
20.72

ATOM
7185
CE2
TYR D
233
59.098
33.258
30.543
1.000
21.75

ATOM
7186
CZ
TYR D
233
60.437
33.503
30.355
1.000
19.73

ATOM
7187
OH
TYR D
233
61.105
34.314
31.242
1.000
21.89

ATOM
7188
C
TYR D
233
57.961
29.200
29.361
1.000
28.08

ATOM
7189
O
TYR D
233
58.773
28.926
30.248
1.000
29.73

ATOM
7190
N
ALA D
234
56.656
29.275
29.598
1.000
25.56

ATOM
7191
CA
ALA D
234
56.071
29.079
30.922
1.000
19.98

ATOM
7192
CB
ALA D
234
54.555
29.223
30.853
1.000
20.85

ATOM
7193
C
ALA D
234
56.444
27.720
31.507
1.000
19.41

ATOM
7194
O
ALA D
234
56.819
27.634
32.677
1.000
25.32

ATOM
7195
N
HIS D
235
56.347
26.661
30.704
1.000
18.96

ATOM
7196
CA
HIS D
235
56.787
25.340
31.116
1.000
19.06

ATOM
7197
CB
HIS D
235
56.705
24.328
29.966
1.000
21.94

ATOM
7198
CG
HIS D
235
57.338
23.000
30.265
1.000
24.66

ATOM
7199
CD2
HIS D
235
58.590
22.520
30.052
1.000
22.51

ATOM
7200
ND1
HIS D
235
56.639
21.962
30.849
1.000
27.58

ATOM
7201
CE1
HIS D
235
57.430
20.914
30.994
1.000
22.15

ATOM
7202
NE2
HIS D
235
58.625
21.232
30.516
1.000
26.23

ATOM
7203
C
HIS D
235
58.223
25.382
31.632
1.000
25.27

ATOM
7204
O
HIS D
235
58.518
24.777
32.666
1.000
28.14

ATOM
7205
N
LEU D
236
59.126
26.059
30.917
1.000
22.13

ATOM
7206
CA
LEU D
236
60.521
26.045
31.352
1.000
21.53

ATOM
7207
CB
LEU D
236
61.454
26.669
30.313
1.000
21.08

ATOM
7208
CG
LEU D
236
62.939
26.690
30.708
1.000
18.33

ATOM
7209
CD1
LEU D
236
63.415
25.289
31.058
1.000
15.49

ATOM
7210
CD2
LEU D
236
63.801
27.274
29.595
1.000
20.04

ATOM
7211
C
LEU D
236
60.683
26.782
32.680
1.000
22.66

ATOM
7212
O
LEU D
236
61.451
26.354
33.544
1.000
22.41

ATOM
7213
N
VAL D
237
59.961
27.884
32.848
1.000
22.04

ATOM
7214
CA
VAL D
237
59.983
28.619
34.110
1.000
19.35

ATOM
7215
CB
VAL D
237
59.040
29.831
34.088
1.000
23.88

ATOM
7216
CG1
VAL D
237
58.862
30.404
35.490
1.000
24.78

ATOM
7217
CG2
VAL D
237
59.556
30.915
33.146
1.000
20.31

ATOM
7218
C
VAL D
237
59.597
27.686
35.250
1.000
24.98

ATOM
7219
O
VAL D
237
60.241
27.617
36.293
1.000
25.46

ATOM
7220
N
GLN D
238
58.515
26.934
35.045
1.000
26.56

ATOM
7221
CA
GLN D
238
58.071
25.992
36.061
1.000
23.40

ATOM
7222
CB
GLN D
238
56.793
25.272
35.615
1.000
27.07

ATOM
7223
CG
GLN D
238
56.445
24.107
36.536
1.000
35.35

ATOM
7224
CD
GLN D
238
55.029
23.607
36.317
1.000
46.19

ATOM
7225
OE1
GLN D
238
54.174
24.356
35.832
1.000
45.64

ATOM
7226
NE2
GLN D
238
54.789
22.342
36.664
1.000
44.19

ATOM
7227
C
GLN D
238
59.133
24.943
36.376
1.000
22.17

ATOM
7228
O
GLN D
238
59.384
24.636
37.542
1.000
27.26

ATOM
7229
N
ALA D
239
59.739
24.383
35.333
1.000
17.35

ATOM
7230
CA
ALA D
239
60.759
23.354
35.530
1.000
17.80

ATOM
7231
CB
ALA D
239
61.226
22.829
34.177
1.000
22.63

ATOM
7232
C
ALA D
239
61.934
23.882
36.339
1.000
22.18

ATOM
7233
O
ALA D
239
62.531
23.165
37.148
1.000
24.37

ATOM
7234
N
ILE D
240
62.280
25.149
36.123
1.000
20.99

ATOM
7235
CA
ILE D
240
63.384
25.757
36.870
1.000
25.46

ATOM
7236
CB
ILE D
240
63.847
27.078
36.229
1.000
23.16

ATOM
7237
CG2
ILE D
240
64.781
27.836
37.160
1.000
20.68

ATOM
7238
CG1
ILE D
240
64.496
26.888
34.852
1.000
19.72

ATOM
7239
CD1
ILE D
240
64.804
28.190
34.147
1.000
22.08

ATOM
7240
C
ILE D
240
62.977
26.005
38.318
1.000
28.16

ATOM
7241
O
ILE D
240
63.778
25.837
39.241
1.000
22.51

ATOM
7242
N
ILE D
241
61.718
26.410
38.512
1.000
21.64

ATOM
7243
CA
ILE D
241
61.278
26.665
39.891
1.000
28.25

ATOM
7244
CB
ILE D
241
59.868
27.273
39.917
1.000
27.90

ATOM
7245
CG2
ILE D
241
59.182
27.110
41.264
1.000
26.14

ATOM
7246
CG1
ILE D
241
59.842
28.752
39.508
1.000
22.68

ATOM
7247
CD1
ILE D
241
58.490
29.205
38.990
1.000
22.21

ATOM
7248
C
ILE D
241
61.345
25.369
40.689
1.000
29.32

ATOM
7249
O
ILE D
241
61.787
25.334
41.840
1.000
26.76

ATOM
7250
N
GLU D
242
60.919
24.291
40.042
1.000
21.42

ATOM
7251
CA
GLU D
242
60.801
22.989
40.655
1.000
23.60

ATOM
7252
CB
GLU D
242
59.922
22.114
39.746
1.000
24.58

ATOM
7253
CG
GLU D
242
58.454
22.521
39.744
1.000
26.39

ATOM
7254
CD
GLU D
242
57.567
21.445
39.142
1.000
30.24

ATOM
7255
OE1
GLU D
242
56.334
21.526
39.303
1.000
39.48

ATOM
7256
OE2
GLU D
242
58.113
20.516
38.508
1.000
38.42

ATOM
7257
C
GLU D
242
62.128
22.289
40.908
1.000
28.27

ATOM
7258
O
GLU D
242
62.259
21.554
41.891
1.000
25.03

ATOM
7259
N
ASN D
243
63.121
22.467
40.042
1.000
20.97

ATOM
7260
CA
ASN D
243
64.362
21.711
40.207
1.000
21.86

ATOM
7261
CB
ASN D
243
64.983
21.403
38.843
1.000
22.88

ATOM
7262
CG
ASN D
243
66.147
20.435
38.957
1.000
22.69

ATOM
7263
OD1
ASN D
243
67.066
20.629
39.753
1.000
23.72

ATOM
7264
ND2
ASN D
243
66.104
19.391
38.158
1.000
18.75

ATOM
7265
C
ASN D
243
65.360
22.460
41.078
1.000
26.32

ATOM
7266
O
ASN D
243
65.862
23.517
40.692
1.000
24.83

ATOM
7267
N
PRO D
244
65.642
21.918
42.259
1.000
25.17

ATOM
7268
CD
PRO D
244
65.169
20.615
42.752
1.000
24.25

ATOM
7269
CA
PRO D
244
66.474
22.616
43.236
1.000
21.82

ATOM
7270
CB
PRO D
244
66.451
21.675
44.453
1.000
24.37

ATOM
7271
CG
PRO D
244
65.267
20.792
44.243
1.000
27.61

ATOM
7272
C
PRO D
244
67.922
22.825
42.819
1.000
20.75

ATOM
7273
O
PRO D
244
68.605
23.663
43.408
1.000
19.99

ATOM
7274
N
PHE D
245
68.429
22.091
41.830
1.000
23.06

ATOM
7275
CA
PHE D
245
69.865
22.153
41.541
1.000
19.95

ATOM
7276
CB
PHE D
245
70.400
20.720
41.389
1.000
21.93

ATOM
7277
CG
PHE D
245
71.836
20.520
41.853
1.000
20.86

ATOM
7278
CD1
PHE D
245
72.829
20.123
40.974
1.000
16.58

ATOM
7279
CD2
PHE D
245
72.179
20.743
43.176
1.000
17.52

ATOM
7280
CE1
PHE D
245
74.133
19.956
41.402
1.000
20.48

ATOM
7281
CE2
PHE D
245
73.476
20.574
43.610
1.000
17.54

ATOM
7282
CZ
PHE D
245
74.469
20.180
42.723
1.000
17.22

ATOM
7283
C
PHE D
245
70.193
22.997
40.319
1.000
25.51

ATOM
7284
O
PHE D
245
71.362
23.052
39.917
1.000
21.54

ATOM
7285
N
LEU D
246
69.233
23.672
39.703
1.000
23.04

ATOM
7286
CA
LEU D
246
69.482
24.581
38.593
1.000
21.38

ATOM
7287
CB
LEU D
246
68.263
24.699
37.661
1.000
20.45

ATOM
7288
CG
LEU D
246
68.043
23.564
36.661
1.000
24.84

ATOM
7289
CD1
LEU D
246
66.692
23.681
35.969
1.000
21.22

ATOM
7290
CD2
LEU D
246
69.174
23.543
35.631
1.000
21.12

ATOM
7291
C
LEU D
246
69.832
25.969
39.114
1.000
21.29

ATOM
7292
O
LEU D
246
68.995
26.664
39.697
1.000
21.82

ATOM
7293
N
ASN D
247
71.059
26.414
38.900
1.000
17.26

ATOM
7294
CA
ASN D
247
71.489
27.713
39.389
1.000
18.30

ATOM
7295
CB
ASN D
247
71.856
27.597
40.880
1.000
23.01

ATOM
7296
CG
ASN D
247
71.921
28.933
41.591
1.000
27.53

ATOM
7297
OD1
ASN D
247
71.495
29.959
41.059
1.000
21.47

ATOM
7298
ND2
ASN D
247
72.465
28.964
42.807
1.000
21.65

ATOM
7299
C
ASN D
247
72.678
28.254
38.597
1.000
18.72

ATOM
7300
O
ASN D
247
73.562
27.492
38.201
1.000
19.15

ATOM
7301
N
GLY D
248
72.714
29.563
38.391
1.000
18.94

ATOM
7302
CA
GLY D
248
73.794
30.276
37.752
1.000
19.96

ATOM
7303
C
GLY D
248
73.964
29.984
36.278
1.000
22.95

ATOM
7304
O
GLY D
248
75.043
30.179
35.703
1.000
20.62

ATOM
7305
N
GLU D
249
72.902
29.517
35.635
1.000
17.77

ATOM
7306
CA
GLU D
249
73.018
29.050
34.253
1.000
15.96

ATOM
7307
CB
GLU D
249
72.851
27.529
34.256
1.000
17.48

ATOM
7308
CG
GLU D
249
72.390
26.859
32.984
1.000
16.91

ATOM
7309
CD
GLU D
249
73.427
26.784
31.889
1.000
19.08

ATOM
7310
OE1
GLU D
249
73.463
25.784
31.143
1.000
22.69

ATOM
7311
OE2
GLU D
249
74.224
27.732
31.777
1.000
21.40

ATOM
7312
C
GLU D
249
72.020
29.759
33.348
1.000
22.60

ATOM
7313
O
GLU D
249
71.012
30.307
33.796
1.000
17.66

ATOM
7314
N
VAL D
250
72.327
29.756
32.053
1.000
19.97

ATOM
7315
CA
VAL D
250
71.486
30.277
30.994
1.000
15.24

ATOM
7316
CB
VAL D
250
72.245
31.284
30.115
1.000
22.54

ATOM
7317
CG1
VAL D
250
71.343
31.787
28.994
1.000
19.92

ATOM
7318
CG2
VAL D
250
72.767
32.445
30.941
1.000
19.32

ATOM
7319
C
VAL D
250
70.976
29.127
30.124
1.000
19.92

ATOM
7320
O
VAL D
250
71.768
28.270
29.725
1.000
19.42

ATOM
7321
N
ILE D
251
69.679
29.091
29.826
1.000
16.97

ATOM
7322
CA
ILE D
251
69.132
27.997
29.033
1.000
20.11

ATOM
7323
CB
ILE D
251
68.074
27.197
29.821
1.000
19.46

ATOM
7324
CG2
ILE D
251
67.514
26.093
28.930
1.000
19.68

ATOM
7325
CG1
ILE D
251
68.593
26.668
31.158
1.000
13.76

ATOM
7326
CD1
ILE D
251
67.692
25.683
31.850
1.000
17.14

ATOM
7327
C
ILE D
251
68.500
28.495
27.738
1.000
18.55

ATOM
7328
O
ILE D
251
67.578
29.312
27.763
1.000
20.22

ATOM
7329
N
ARG D
252
69.005
27.995
26.614
1.000
21.00

ATOM
7330
CA
ARG D
252
68.451
28.372
25.316
1.000
20.07

ATOM
7331
CB
ARG D
252
69.442
28.127
24.185
1.000
20.58

ATOM
7332
CG
ARG D
252
70.728
28.928
24.222
1.000
22.33

ATOM
7333
CD
ARG D
252
71.650
28.523
23.073
1.000
21.13

ATOM
7334
NE
ARG D
252
71.050
28.861
21.784
1.000
18.85

ATOM
7335
CZ
ARG D
252
71.557
29.701
20.900
1.000
18.85

ATOM
7336
NH1
ARG D
252
70.918
29.927
19.764
1.000
16.90

ATOM
7337
NH2
ARG D
252
72.699
30.323
21.132
1.000
20.07

ATOM
7338
C
ARG D
252
67.172
27.578
25.040
1.000
19.42

ATOM
7339
O
ARG D
252
67.152
26.351
25.152
1.000
17.60

ATOM
7340
N
LEU D
253
66.114
28.290
24.675
1.000
17.77

ATOM
7341
CA
LEU D
253
64.837
27.685
24.320
1.000
17.55

ATOM
7342
CB
LEU D
253
63.789
28.077
25.359
1.000
20.36

ATOM
7343
CG
LEU D
253
62.383
27.489
25.190
1.000
19.52

ATOM
7344
CD1
LEU D
253
62.424
25.980
25.318
1.000
12.98

ATOM
7345
CD2
LEU D
253
61.427
28.098
26.216
1.000
17.81

ATOM
7346
C
LEU D
253
64.464
28.176
22.925
1.000
22.27

ATOM
7347
O
LEU D
253
63.866
29.242
22.798
1.000
18.37

ATOM
7348
N
ASP D
254
64.845
27.447
21.875
1.000
17.63

ATOM
7349
CA
ASP D
254
64.848
28.079
20.561
1.000
19.74

ATOM
7350
CB
ASP D
254
66.170
28.856
20.403
1.000
16.22

ATOM
7351
CG
ASP D
254
67.383
27.959
20.577
1.000
21.64

ATOM
7352
OD1
ASP D
254
67.232
26.720
20.613
1.000
18.65

ATOM
7353
OD2
ASP D
254
68.520
28.473
20.878
1.000
23.91

ATOM
7354
C
ASP D
254
64.726
27.139
19.378
1.000
20.09

ATOM
7355
O
ASP D
254
65.018
27.559
18.255
1.000
22.74

ATOM
7356
N
GLY D
255
64.305
25.897
19.582
1.000
22.35

ATOM
7357
CA
GLY D
255
64.101
24.976
18.468
1.000
18.23

ATOM
7358
C
GLY D
255
65.387
24.678
17.715
1.000
23.86

ATOM
7359
O
GLY D
255
65.338
24.219
16.567
1.000
21.75

ATOM
7360
N
ALA D
256
66.502
24.941
18.375
1.000
19.53

ATOM
7361
CA
ALA D
256
67.855
24.721
17.891
1.000
20.22

ATOM
7362
CB
ALA D
256
67.986
23.287
17.391
1.000
19.78

ATOM
7363
C
ALA D
256
68.267
25.702
16.802
1.000
22.63

ATOM
7364
O
ALA D
256
69.219
25.455
16.056
1.000
21.69

ATOM
7365
N
ILE D
257
67.569
26.833
16.682
1.000
19.23

ATOM
7366
CA
ILE D
257
67.982
27.829
15.698
1.000
16.07

ATOM
7367
CB
ILE D
257
66.915
28.924
15.518
1.000
18.79

ATOM
7368
CG2
ILE D
257
66.903
29.894
16.692
1.000
22.52

ATOM
7369
CG1
ILE D
257
67.039
29.710
14.207
1.000
16.43

ATOM
7370
CD1
ILE D
257
65.990
30.785
14.047
1.000
16.38

ATOM
7371
C
ILE D
257
69.300
28.484
16.102
1.000
25.38

ATOM
7372
O
ILE D
257
69.626
28.535
17.284
1.000
21.27

ATOM
7373
N
ARG D
258
70.040
28.974
15.122
1.000
21.25

ATOM
7374
CA
ARG D
258
71.191
29.848
15.281
1.000
17.34

ATOM
7375
CE
ARG D
258
72.497
29.119
14.962
1.000
18.94

ATOM
7376
CG
ARG D
258
72.797
27.932
15.880
1.000
17.46

ATOM
7377
CD
ARD D
258
72.975
28.415
17.307
1.000
22.03

ATOM
7378
NE
ARD D
258
73.280
27.368
18.263
1.000
22.14

ATOM
7379
CZ
ARD D
258
72.412
26.609
18.913
1.000
24.72

ATOM
7380
NE1
ARG D
258
72.883
25.698
19.764
1.000
20.30

ATOM
7381
NH2
ARG D
258
71.104
26.745
18.728
1.000
19.58

ATOM
7382
C
ARG D
258
70.997
31.053
14.369
1.000
23.77

ATOM
7383
O
ARD D
258
70.781
30.903
13.156
1.000
24.03

ATOM
7384
N
MET D
259
71.039
32.278
14.888
1.000
21.77

ATOM
7385
CA
MET D
259
70.662
33.390
14.014
1.000
25.38

ATOM
7386
CB
MET D
259
70.191
34.592
14.839
1.000
24.28

ATOM
7387
CD
MET D
259
69.122
34.266
15.865
1.000
23.82

ATOM
7388
SD
MET D
259
67.734
33.346
15.167
1.000
28.80

ATOM
7389
CE
MET D
259
66.976
34.600
14.133
1.000
26.61

ATOM
7390
C
MET D
259
71.794
33.830
13.091
1.000
30.90

ATOM
7391
O
MET D
259
72.937
34.018
13.496
1.000
30.51

ATOM
7392
N
GLN D
260
71.450
34.025
11.828
1.000
30.38

ATOM
7393
CA
GLN D
260
72.343
34.553
10.806
1.000
25.30

ATOM
7394
CE
GLN D
260
71.913
33.950
9.466
1.000
30.57

ATOM
7395
CD
GLN D
260
72.719
32.746
9.023
1.000
43.46

ATOM
7396
CD
GLN D
260
74.004
32.515
9.785
1.000
50.86

ATOM
7397
OE1
GLN D
260
75.109
32.788
9.311
1.000
41.52

ATOM
7398
NE2
GLN D
260
73.899
32.001
11.006
1.000
68.66

ATOM
7399
C
GLN D
260
72.308
36.073
10.795
1.000
24.41

ATOM
7400
O
GLN D
260
71.451
36.657
11.475
1.000
20.57

ATOM
7401
N
PRO D
261
73.191
36.756
10.080
1.000
24.38

ATOM
7402
CD
PRO D
261
74.281
36.227
9.234
1.000
26.73

ATOM
7403
CA
PRO D
261
73.183
38.228
10.080
1.000
22.57

ATOM
7404
CB
PRO D
261
74.205
38.582
8.992
1.000
23.87

ATOM
7405
CD
PRO D
261
75.174
37.436
9.068
1.000
25.59

ATOM
7406
C
PRO D
261
71.814
38.793
9.723
1.000
25.02

ATOM
7407
OT1
PRO D
261
71.101
38.072
9.000
1.000
27.55

ATOM
7408
OT2
PRO D
261
71.488
39.902
10.183
1.000
22.37

ATOM
7409
PN
LIG D
262
57.422
39.435
25.068
1.000
23.15

ATOM
7410
O1N
LIG D
262
57.806
38.514
23.885
1.000
25.67

ATOM
7411
O2N
LIG D
262
56.360
38.756
25.925
1.000
26.40

ATOM
7412
O3P
LIG D
262
56.913
40.769
24.463
1.000
23.02

ATOM
7413
OSM
LIG D
262
58.744
39.749
25.910
1.000
24.23

ATOM
7414
C5M
LIG D
262
59.075
39.020
27.127
1.000
18.88

ATOM
7415
C4M
LIG D
262
60.636
38.980
27.309
1.000
18.29

ATOM
7416
O4M
LIG D
262
61.167
38.014
26.391
1.000
22.02

ATOM
7417
C3M
LIG D
262
61.315
40.324
26.955
1.000
18.81

ATOM
7418
O3M
LIG D
262
62.389
40.543
27.900
1.000
22.74

ATOM
7419
C2M
LIG D
262
61.878
40.076
25.532
1.000
14.35

ATOM
7420
O2M
LIG D
262
62.962
41.002
25.316
1.000
20.42

ATOM
7421
C1M
LIG D
262
62.259
38.591
25.613
1.000
20.56

ATOM
7422
N1N
LIG D
262
62.462
37.840
24.339
1.000
22.42

ATOM
7423
C6N
LIG D
262
63.798
37.319
24.034
1.000
25.78

ATOM
7424
C5N
LIG D
262
64.040
36.661
22.882
1.000
26.30

ATOM
7425
C4N
LIG D
262
62.985
36.644
21.748
1.000
26.65

ATOM
7426
C3N
LIG D
262
61.541
36.889
22.299
1.000
22.98

ATOM
7427
C2N
LIG D
262
61.342
37.606
23.421
1.000
23.56

ATOM
7428
C7N
LIG D
262
60.403
36.620
21.333
1.000
20.05

ATOM
7429
O7N
LIG D
262
60.607
36.003
20.279
1.000
22.45

ATOM
7430
N7N
LIG D
262
59.213
37.076
21.680
1.000
14.14

ATOM
7431
PA
LIG D
262
55.631
41.515
24.912
1.000
26.46

ATOM
7432
O1A
LIG D
262
55.631
42.919
24.316
1.000
24.54

ATOM
7433
O2A
LIG D
262
54.364
40.750
24.508
1.000
29.61

ATOM
7434
O5B
LIG D
262
55.637
41.666
26.507
1.000
26.93

ATOM
7435
C5B
LIG D
262
56.576
42.588
27.145
1.000
20.55

ATOM
7436
C4B
LIG D
262
55.898
43.240
28.393
1.000
23.80

ATOM
7437
O4B
LIG D
262
56.880
44.008
29.138
1.000
21.67

ATOM
7438
C3B
LIG D
262
54.724
44.179
27.988
1.000
24.11

ATOM
7439
O3B
LIG D
262
53.525
43.815
28.694
1.000
22.60

ATOM
7440
C2B
LIG D
262
55.237
45.558
28.426
1.000
28.11

ATOM
7441
O2B
LIG D
262
54.192
46.481
28.755
1.000
27.28

ATOM
7442
C1B
LIG D
262
56.225
45.221
29.568
1.000
19.96

ATOM
7443
N9A
LIG D
262
57.210
46.336
29.738
1.000
22.28

ATOM
7444
C4A
LIG D
262
57.558
46.962
30.940
1.000
20.80

ATOM
7445
N3A
LIG D
262
57.133
46.764
32.324
1.000
19.84

ATOM
7446
C2A
LIG D
262
57.705
47.570
33.190
1.000
15.71

ATOM
7447
N1A
LIG D
262
58.594
48.507
32.971
1.000
24.24

ATOM
7448
C6A
LIG D
262
59.043
48.762
31.754
1.000
20.94

ATOM
7449
C5A
LIG D
262
58.541
47.990
30.639
1.000
23.41

ATOM
7450
N7A
LIG D
262
58.836
48.041
29.278
1.000
30.14

ATOM
7451
C8A
LIG D
262
58.005
47.040
28.846
1.000
21.02

ATOM
7452
N6A
LIG D
262
59.761
49.860
31.547
1.000
18.74

ATOM
7453
C
LIG D
262
63.468
42.004
16.293
1.000
37.19

ATOM
7454
C1
LIG D
262
64.908
42.400
15.731
1.000
40.91

ATOM
7455
N
LIG D
262
65.122
42.614
14.374
1.000
46.58

ATOM
7456
O
LIG D
262
65.816
42.505
16.583
1.000
32.75

ATOM
7457
C2
LIG D
262
63.981
42.485
13.406
1.000
51.55

ATOM
7458
C3
LIG D
262
63.916
41.176
12.560
1.000
55.49

ATOM
7459
C4
LIG D
262
66.506
42.952
13.906
1.000
38.70

ATOM
7460
C5
LIG D
262
67.250
41.676
13.422
1.000
39.77

ATOM
7461
C6
LIG D
262
66.495
40.887
12.339
1.000
43.74

ATOM
7462
C7
LIG D
262
65.145
40.259
12.747
1.000
52.09

ATOM
7463
C8
LIG D
262
62.498
43.226
16.479
1.000
26.51

ATOM
7464
C9
LIG D
262
61.135
42.962
16.665
1.000
35.63

ATOM
7465
C10
LIG D
262
60.228
44.006
16.841
1.000
32.64

ATOM
7466
C11
LIG D
262
60.671
45.323
16.828
1.000
28.46

ATOM
7467
C12
LIG D
262
62.026
45.594
16.657
1.000
31.49

ATOM
7468
C13
LIG D
262
62.930
44.554
16.461
1.000
24.95

ATOM
7469
C15
LIG D
262
63.762
41.769
18.722
1.000
32.41

ATOM
7470
N1
LIG D
262
63.815
41.274
19.918
1.000
31.72

ATOM
7471
C16
LIG D
262
63.550
39.860
20.066
1.000
31.24

ATOM
7472
C17
LIG D
262
63.243
39.052
18.946
1.000
27.85

ATOM
7473
C18
LIG D
262
63.219
39.705
17.545
1.000
34.74

ATOM
7474
N2
LIG D
262
63.493
41.175
17.586
1.000
39.88

ATOM
7475
S
LIG D
262
62.871
38.731
16.107
1.000
32.53

ATOM
7476
C19
LIG D
262
63.019
37.761
19.346
1.000
27.53

ATOM
7477
N3
LIG D
262
63.217
37.741
20.731
1.000
33.77

ATOM
7478
N4
LIG D
262
63.516
39.014
21.153
1.000
30.88

ATOM
7479
O
HOH
301
92.776
12.297
31.743
1.000
20.14

ATOM
7480
O
HOH
302
77.559
34.144
9.282
1.000
20.43

ATOM
7481
O
HOH
303
80.425
29.345
40.907
1.000
16.20

ATOM
7482
O
HOH
304
91.952
31.264
29.002
1.000
16.74

ATOM
7483
O
HOH
305
94.801
36.551
34.544
1.000
22.14

ATOM
7484
O
HOH
306
65.211
42.139
29.804
1.000
22.38

ATOM
7485
O
HOH
307
100.866
4.606
25.942
1.000
22.10

ATOM
7486
O
HOH
308
70.380
25.625
13.725
1.000
25.15

ATOM
7487
O
HOH
309
98.836
38.721
8.048
1.000
20.62

ATOM
7488
O
HOH
310
73.571
6.226
35.060
1.000
32.14

ATOM
7489
O
HOH
311
88.880
24.223
27.409
1.000
20.29

ATOM
7490
O
HOH
312
72.760
24.489
37.007
1.000
18.84

ATOM
7491
O
HOH
313
94.756
19.229
14.119
1.000
26.27

ATOM
7492
O
HOH
314
87.327
22.157
29.706
1.000
16.82

ATOM
7493
O
HOH
315
63.431
29.981
17.877
1.000
23.03

ATOM
7494
O
HOH
316
84.014
35.114
15.138
1.000
20.55

ATOM
7495
O
HOH
317
87.485
35.486
13.797
1.000
25.53

ATOM
7496
O
HOH
318
83.964
52.541
27.664
1.000
18.55

ATOM
7497
O
HOH
319
77.741
41.945
42.922
1.000
16.89

ATOM
7498
O
HOH
320
93.152
52.197
29.838
1.000
24.83

ATOM
7499
O
HOH
321
97.176
7.390
32.191
1.000
25.52

ATOM
7500
O
HOH
322
77.957
35.854
11.120
1.000
18.59

ATOM
7501
O
HOH
323
85.629
53.769
25.435
1.000
18.98

ATOM
7502
O
HOH
324
86.538
32.202
24.492
1.000
40.93

ATOM
7503
O
HOH
325
87.007
49.918
27.784
1.000
27.18

ATOM
7504
O
HOH
326
77.600
20.706
41.125
1.000
21.42

ATOM
7505
O
HOH
327
78.902
55.159
40.598
1.000
42.52

ATOM
7506
O
HOH
328
81.133
17.266
35.954
1.000
23.52

ATOM
7507
O
HOH
329
113.031
19.892
24.590
1.000
29.70

ATOM
7508
O
HOH
330
104.459
32.288
29.421
1.000
22.61

ATOM
7509
O
HOH
331
78.966
10.036
27.642
1.000
28.79

ATOM
7510
O
HOH
332
82.521
27.789
41.932
1.000
24.45

ATOM
7511
O
HOH
333
78.816
22.190
17.044
1.000
21.49

ATOM
7512
O
HOH
334
90.214
12.158
32.342
1.000
19.15

ATOM
7513
O
HOH
335
75.406
27.047
28.515
1.000
46.66

ATOM
7514
O
HOH
336
67.009
36.757
18.236
1.000
29.57

ATOM
7515
O
HOH
337
88.708
40.365
34.712
1.000
20.85

ATOM
7516
O
HOH
338
61.508
16.582
41.397
1.000
29.21

ATOM
7517
O
HOH
339
79.952
36.047
34.651
1.000
22.65

ATOM
7518
O
HOH
340
69.698
25.567
20.952
1.000
20.27

ATOM
7519
O
HOH
341
78.040
6.743
26.436
1.000
16.46

ATOM
7520
O
HOH
342
112.979
15.545
31.632
1.000
32.19

ATOM
7521
O
HOH
343
76.376
14.721
10.758
1.000
27.36

ATOM
7522
O
HOH
344
69.396
52.971
44.875
1.000
19.26

ATOM
7523
O
HOH
345
94.466
33.698
27.831
1.000
18.87

ATOM
7524
O
HOH
346
62.211
43.111
34.699
1.000
18.14

ATOM
7525
O
HOH
347
79.228
32.834
46.344
1.000
25.33

ATOM
7526
O
HOH
348
91.707
29.243
37.874
1.000
22.18

ATOM
7527
O
HOH
349
95.704
15.420
15.073
1.000
24.76

ATOM
7528
O
HOH
350
63.929
53.848
21.940
1.000
39.40

ATOM
7529
O
HOH
351
80.675
45.514
39.966
1.000
17.96

ATOM
7530
O
HOH
352
78.369
45.158
41.405
1.000
23.26

ATOM
7531
O
HOH
353
55.124
29.871
13.566
1.000
26.74

ATOM
7532
O
HOH
354
85.117
31.485
28.658
1.000
32.69

ATOM
7533
O
HOH
355
75.734
38.342
20.028
1.000
24.32

ATOM
7534
O
HOH
356
74.602
22.606
21.931
1.000
23.88

ATOM
7535
O
HOH
357
81.874
37.548
19.721
1.000
17.64

ATOM
7536
O
HOH
358
63.070
49.539
15.889
1.000
30.23

ATOM
7537
O
HOH
359
98.248
16.502
15.469
1.000
17.16

ATOM
7538
O
HOH
360
76.327
11.060
26.671
1.000
24.63

ATOM
7539
O
HOH
361
74.997
29.485
22.470
1.000
39.59

ATOM
7540
O
HOH
362
104.920
40.576
24.671
1.000
31.70

ATOM
7541
O
HOH
363
79.230
38.710
20.312
1.000
29.49

ATOM
7542
O
HOH
364
99.247
52.723
33.905
1.000
35.67

ATOM
7543
O
HOH
365
63.759
24.391
44.403
1.000
34.65

ATOM
7544
O
HOH
366
48.099
14.793
14.578
1.000
36.68

ATOM
7545
O
HOH
367
55.097
3.198
34.387
1.000
37.64

ATOM
7546
O
HOH
368
66.645
44.792
48.647
1.000
31.11

ATOM
7547
O
HOH
369
78.813
0.682
11.091
1.000
25.32

ATOM
7548
O
HOH
370
116.182
20.584
26.457
1.000
42.78

ATOM
7549
O
HOH
371
72.392
60.443
19.265
1.000
27.98

ATOM
7550
O
HOH
372
85.512
19.921
35.425
1.000
26.77

ATOM
7551
O
HOH
373
75.463
31.905
33.759
1.000
30.07

ATOM
7552
O
HOH
374
79.323
7.223
7.370
1.000
25.70

ATOM
7553
O
HOH
375
82.491
27.441
44.754
1.000
27.05

ATOM
7554
O
HOH
376
86.109
27.617
30.944
1.000
27.46

ATOM
7555
O
HOH
377
43.566
47.081
32.187
1.000
16.13

ATOM
7556
O
HOH
378
103.241
48.462
25.650
1.000
24.71

ATOM
7557
O
HOH
379
69.968
37.248
17.438
1.000
23.41

ATOM
7558
O
HOH
380
89.350
26.980
26.742
1.000
20.25

ATOM
7559
O
HOH
381
51.634
43.602
24.654
1.000
30.52

ATOM
7560
O
HOH
382
114.006
8.766
15.300
1.000
24.65

ATOM
7561
O
HOH
383
84.217
48.991
29.017
1.000
31.07

ATOM
7562
O
HOH
384
91.931
27.844
35.321
1.000
17.17

ATOM
7563
O
HOH
385
85.192
48.196
25.874
1.000
29.60

ATOM
7564
O
HOH
386
115.322
21.322
4.709
1.000
20.42

ATOM
7565
O
HOH
387
66.453
24.956
22.897
1.000
29.29

ATOM
7566
O
HOH
388
56.086
39.303
28.854
1.000
22.55

ATOM
7567
O
HOH
389
79.289
8.651
45.437
1.000
42.77

ATOM
7568
O
HOH
390
76.016
49.742
45.810
1.000
27.62

ATOM
7569
O
HOH
391
69.096
54.578
16.314
1.000
19.36

ATOM
7570
O
HOH
392
79.524
40.851
4.029
1.000
35.85

ATOM
7571
O
HOH
393
97.800
21.307
7.889
1.000
18.96

ATOM
7572
O
HOH
394
60.387
3.283
17.265
1.000
39.16

ATOM
7573
O
HOH
395
70.626
54.803
43.647
1.000
26.49

ATOM
7574
O
HOH
396
82.133
24.094
23.840
1.000
32.45

ATOM
7575
O
HOH
397
79.984
13.271
10.506
1.000
31.95

ATOM
7576
O
HOH
398
69.755
27.539
12.357
1.000
19.92

ATOM
7577
O
HOH
399
54.427
53.254
36.600
1.000
31.14

ATOM
7578
O
HOH
400
76.245
41.299
7.666
1.000
32.49

ATOM
7579
O
HOH
401
102.361
4.194
11.337
1.000
32.26

ATOM
7580
O
HOH
402
65.368
39.607
32.062
1.000
18.45

ATOM
7581
O
HOH
403
77.627
33.285
17.947
1.000
32.18

ATOM
7582
O
HOH
404
84.225
68.543
24.460
1.000
30.38

ATOM
7583
O
HOH
405
106.651
33.242
30.436
1.000
26.95

ATOM
7584
O
HOH
406
75.077
45.385
49.011
1.000
29.52

ATOM
7585
O
HOH
407
79.455
27.085
30.595
1.000
46.96

ATOM
7586
O
HOH
408
51.139
29.211
29.538
1.000
21.79

ATOM
7587
O
HOH
409
64.552
55.161
40.457
1.000
29.93

ATOM
7588
O
HOH
410
107.550
27.293
35.489
1.000
30.38

ATOM
7589
O
HOH
411
53.653
44.875
20.990
1.000
42.39

ATOM
7590
O
HOH
412
68.940
50.613
10.578
1.000
33.53

ATOM
7591
O
HOH
413
77.823
37.269
27.398
1.000
52.66

ATOM
7592
O
HOH
414
88.020
33.385
−1.498
1.000
23.87

ATOM
7593
O
HOH
415
73.543
9.125
6.557
1.000
37.72

ATOM
7594
O
HOH
416
58.879
47.725
48.958
1.000
29.83

ATOM
7595
O
HOH
417
76.336
65.330
23.962
1.000
22.36

ATOM
7596
O
HOH
418
52.443
49.100
42.295
1.000
24.67

ATOM
7597
O
HOH
419
70.535
6.347
41.406
1.000
27.74

ATOM
7598
O
HOH
420
88.288
67.546
11.973
1.000
30.11

ATOM
7599
O
HOH
421
69.212
56.275
41.596
1.000
32.93

ATOM
7600
O
HOH
422
64.777
−7.683
32.662
1.000
39.39

ATOM
7601
O
HOH
423
85.507
37.769
37.127
1.000
26.18

ATOM
7602
O
HOH
424
60.769
−5.497
35.178
1.000
35.95

ATOM
7603
O
HOH
425
76.724
9.020
28.963
1.000
26.73

ATOM
7604
O
HOH
426
88.772
58.307
9.168
1.000
35.00

ATOM
7605
O
HOH
427
92.867
17.963
14.820
1.000
24.96

ATOM
7606
O
HOH
428
46.765
52.287
25.746
1.000
31.05

ATOM
7607
O
HOH
429
84.460
45.572
38.946
1.000
32.72

ATOM
7608
O
HOH
430
75.187
5.894
25.803
1.000
23.00

ATOM
7609
O
HOH
431
59.372
37.396
51.274
1.000
25.28

ATOM
7610
O
HOH
432
90.348
42.583
7.062
1.000
24.06

ATOM
7611
O
HOH
433
59.054
18.728
19.491
1.000
26.20

ATOM
7612
O
HOH
434
87.471
8.190
6.913
1.000
38.33

ATOM
7613
O
HOH
435
57.945
16.732
23.289
1.000
40.80

ATOM
7614
O
HOH
436
63.529
44.279
32.431
1.000
19.37

ATOM
7615
O
HOH
437
101.843
39.707
39.930
1.000
28.87

ATOM
7616
O
HOH
438
64.407
24.039
48.731
1.000
37.91

ATOM
7617
O
HOH
439
88.442
7.691
52.002
1.000
42.77

ATOM
7618
O
HOH
440
72.465
31.064
44.572
1.000
21.67

ATOM
7619
O
HOH
441
68.994
41.346
10.123
1.000
42.94

ATOM
7620
O
HOH
442
79.097
44.850
49.113
1.000
29.22

ATOM
7621
O
HOH
443
54.574
41.823
5.022
1.000
43.31

ATOM
7622
O
HOH
444
62.894
40.739
30.750
1.000
27.05

ATOM
7623
O
HOH
445
87.850
39.681
37.054
1.000
29.04

ATOM
7624
O
HOH
446
102.935
6.383
30.051
1.000
26.13

ATOM
7625
O
HOH
447
81.399
0.725
10.978
1.000
31.16

ATOM
7626
O
HOH
448
75.791
2.055
7.947
1.000
36.53

ATOM
7627
O
HOH
449
70.507
48.423
17.926
1.000
20.58

ATOM
7628
O
HOH
450
105.650
12.383
27.890
1.000
26.46

ATOM
7629
O
HOH
451
82.895
43.409
9.910
1.000
20.55

ATOM
7630
O
HOH
452
110.272
15.926
31.003
1.000
26.86

ATOM
7631
O
HOH
453
68.815
46.589
18.947
1.000
21.05

ATOM
7632
O
HOH
454
76.594
34.173
33.922
1.000
26.38

ATOM
7633
O
HOH
455
54.072
46.868
24.653
1.000
30.30

ATOM
7634
O
HOH
456
91.069
42.715
4.402
1.000
27.91

ATOM
7635
O
HOH
457
81.997
14.819
10.048
1.000
20.02

ATOM
7636
O
HOH
458
67.486
23.662
48.188
1.000
22.81

ATOM
7637
O
HOH
459
52.296
49.095
47.652
1.000
25.11

ATOM
7638
O
HOH
460
75.602
26.828
36.321
1.000
24.34

ATOM
7639
O
HOH
461
77.276
34.990
6.677
1.000
21.15

ATOM
7640
O
HOH
462
58.803
46.498
21.948
1.000
46.48

ATOM
7641
O
HOH
463
65.913
54.952
36.668
1.000
45.96

ATOM
7642
O
HOH
464
86.907
10.226
56.341
1.000
49.82

ATOM
7643
O
HOH
465
75.050
24.660
23.343
1.000
30.62

ATOM
7644
O
HOH
466
85.073
24.898
42.520
1.000
33.55

ATOM
7645
O
HOH
467
100.013
26.261
2.735
1.000
25.57

ATOM
7646
O
HOH
468
102.785
31.581
6.162
1.000
30.61

ATOM
7647
O
HOH
469
89.302
53.313
35.809
1.000
30.13

ATOM
7648
O
HOH
470
99.425
16.286
2.376
1.000
26.49

ATOM
7649
O
HOH
471
54.696
54.570
33.861
1.000
24.27

ATOM
7650
O
HOH
472
66.678
17.442
45.628
1.000
36.63

ATOM
7651
O
HOH
473
88.323
39.792
39.649
1.000
29.12

ATOM
7652
O
HOH
474
75.968
30.164
31.264
1.000
23.90

ATOM
7653
O
HOH
475
76.155
27.321
18.568
1.000
38.98

ATOM
7654
O
HOH
476
101.777
17.659
38.545
1.000
38.91

ATOM
7655
O
HOH
477
54.564
21.181
19.102
1.000
36.10

ATOM
7656
O
HOH
478
85.523
31.838
7.876
1.000
22.22

ATOM
7657
O
HOH
479
100.112
10.630
34.314
1.000
37.69

ATOM
7658
O
HOH
480
82.501
35.202
20.962
1.000
25.05

ATOM
7659
O
HOH
481
102.572
64.683
21.745
1.000
26.48

ATOM
7660
O
HOH
482
73.557
38.100
49.865
1.000
32.24

ATOM
7661
O
HOH
483
114.148
7.806
13.007
1.000
26.89

ATOM
7662
O
HOH
484
44.492
43.400
40.299
1.000
32.81

ATOM
7663
O
HOH
485
74.717
60.776
16.043
1.000
33.98

ATOM
7664
O
HOH
486
78.365
30.500
32.549
1.000
39.62

ATOM
7665
O
HOH
487
115.947
27.013
6.468
1.000
35.66

ATOM
7666
O
HOH
488
102.897
41.478
35.832
1.000
37.34

ATOM
7667
O
HOH
489
84.341
57.813
34.619
1.000
29.69

ATOM
7668
O
HOH
490
100.125
3.494
19.130
1.000
26.61

ATOM
7669
O
HOH
491
50.809
20.138
18.682
1.000
52.18

ATOM
7670
O
HOH
492
86.185
28.643
28.091
1.000
42.40

ATOM
7671
O
HOH
493
99.822
58.547
9.222
1.000
35.54

ATOM
7672
O
HOH
494
78.317
33.116
28.899
1.000
33.46

ATOM
7673
O
HOH
495
83.739
18.024
36.847
1.000
33.56

ATOM
7674
O
HOH
496
75.125
59.664
10.426
1.000
32.84

ATOM
7675
O
HOH
497
76.115
31.609
28.684
1.000
24.76

ATOM
7676
O
HOH
498
77.499
24.626
24.992
1.000
24.37

ATOM
7677
O
HOH
499
92.431
54.586
37.374
1.000
32.36

ATOM
7678
O
HOH
500
67.858
50.628
47.734
1.000
30.18

ATOM
7679
O
HOH
501
98.318
1.761
23.333
1.000
30.71

ATOM
7680
O
HOH
502
72.986
15.557
47.384
1.000
34.73

ATOM
7681
O
HOH
503
68.995
54.791
36.757
1.000
31.47

ATOM
7682
O
HOH
504
101.723
41.946
18.346
1.000
30.00

ATOM
7683
O
HOH
505
82.264
34.952
23.539
1.000
25.17

ATOM
7684
O
HOH
506
56.697
47.408
25.618
1.000
31.14

ATOM
7685
O
HOH
507
87.847
28.731
25.957
1.000
28.11

ATOM
7686
O
HOH
508
95.244
10.416
8.064
1.000
32.16

ATOM
7687
O
HOH
509
56.627
19.004
18.253
1.000
26.24

ATOM
7688
O
HOH
510
57.854
45.037
24.642
1.000
36.65

ATOM
7689
O
HOH
511
78.741
32.690
33.128
1.000
29.92

ATOM
7690
O
HOH
512
104.124
6.696
9.404
1.000
27.70

ATOM
7691
O
HOH
513
116.359
9.727
16.189
1.000
34.95

ATOM
7692
O
HOH
514
49.109
30.125
27.987
1.000
33.92

ATOM
7693
O
HOH
515
73.757
37.904
52.165
1.000
34.57

ATOM
7694
O
HOH
516
83.597
64.886
14.692
1.000
36.49

ATOM
7695
O
HOH
517
55.248
17.298
19.521
1.000
37.21

ATOM
7696
O
HOH
518
54.874
22.157
16.029
1.000
45.14

ATOM
7697
O
HOH
519
66.187
58.150
19.372
1.000
42.85

ATOM
7698
O
HOH
520
72.069
57.310
32.850
1.000
29.22

ATOM
7699
O
HOH
521
99.114
18.960
37.026
1.000
33.10

ATOM
7700
O
HOH
522
59.194
14.762
9.954
1.000
51.08

ATOM
7701
O
HOH
523
96.552
27.459
39.703
1.000
47.86

ATOM
7702
O
HOH
524
67.085
25.696
9.189
1.000
47.80

ATOM
7703
O
HOH
525
101.022
43.581
7.126
1.000
37.40

ATOM
7704
O
HOH
526
78.966
23.519
21.132
1.000
27.15

ATOM
7705
O
HOH
527
96.487
2.281
30.380
1.000
32.71

ATOM
7706
O
HOH
528
84.740
37.917
45.393
1.000
28.40

ATOM
7707
O
HOH
529
98.413
2.783
25.894
1.000
39.61

ATOM
7708
O
HOH
530
82.799
55.750
1.882
1.000
43.02

ATOM
7709
O
HOH
531
96.924
23.856
37.478
1.000
29.70

ATOM
7710
O
HOH
532
105.207
57.177
15.684
1.000
33.51

ATOM
7711
O
HOH
533
50.454
48.206
49.545
1.000
47.69

ATOM
7712
O
HOH
534
104.933
47.130
24.713
1.000
40.72

ATOM
7713
O
HOH
535
110.866
10.401
21.494
1.000
37.91

ATOM
7714
O
HOH
536
92.838
24.232
42.078
1.000
41.89

ATOM
7715
O
HOH
537
67.555
24.966
46.015
1.000
29.13

ATOM
7716
O
HOH
538
78.053
36.477
22.849
1.000
47.09

ATOM
7717
O
HOH
539
112.925
12.201
22.087
1.000
37.50

ATOM
7718
O
HOH
540
50.757
35.007
25.917
1.000
33.90

ATOM
7719
O
HOH
541
68.640
−1.430
15.611
1.000
48.67

ATOM
7720
O
HOH
542
51.543
45.251
27.533
1.000
26.17

ATOM
7721
O
HOH
543
58.896
50.709
28.085
1.000
37.22

ATOM
7722
O
HOH
544
84.790
47.138
1.717
1.000
32.58

ATOM
7723
O
HOH
545
49.348
51.235
50.952
1.000
61.64

ATOM
7724
O
HOH
546
85.811
28.025
23.962
1.000
29.92

ATOM
7725
O
HOH
547
57.308
49.674
25.259
1.000
41.81

ATOM
7726
O
HOH
548
76.408
21.933
19.985
1.000
32.05

ATOM
7727
O
HOH
549
49.802
38.458
25.007
1.000
23.83

ATOM
7728
O
HOH
550
53.861
44.618
23.701
1.000
27.79

ATOM
7729
O
HOH
551
102.428
18.900
34.815
1.000
32.12

ATOM
7730
O
HOH
552
78.711
57.445
12.607
1.000
32.79

ATOM
7731
O
HOH
553
99.312
7.498
33.442
1.000
43.12

ATOM
7732
O
HOH
554
98.312
66.410
31.867
1.000
58.37

ATOM
7733
O
HOH
555
92.039
18.350
40.142
1.000
41.97

ATOM
7734
O
HOH
556
79.528
25.044
23.137
1.000
39.55

ATOM
7735
O
HOH
557
93.544
44.872
5.133
1.000
33.79

ATOM
7736
O
HOH
558
89.336
10.465
52.529
1.000
55.29

ATOM
7737
O
HOH
559
83.570
4.908
36.103
1.000
31.60

ATOM
7738
O
HOH
560
90.408
2.929
31.118
1.000
47.04

ATOM
7739
O
HOH
561
70.523
60.411
20.819
1.000
29.91

ATOM
7740
O
HOH
562
64.140
9.753
40.136
1.000
33.59

ATOM
7741
O
HOH
563
78.895
34.022
31.118
1.000
41.66

ATOM
7742
O
HOH
564
95.467
56.193
35.984
1.000
31.97

ATOM
7743
O
HOH
565
59.692
29.845
54.331
1.000
57.27

ATOM
7744
O
HOH
566
80.239
−2.789
16.441
1.000
63.02

ATOM
7745
O
HOH
567
65.591
55.864
34.198
1.000
42.97

ATOM
7746
O
HOH
568
74.992
59.983
27.745
1.000
27.69

ATOM
7747
O
HOH
569
86.483
67.882
25.098
1.000
31.30

ATOM
7748
O
HOH
570
115.448
11.042
22.216
1.000
43.17

ATOM
7749
O
HOH
571
60.226
17.619
34.965
1.000
35.98

ATOM
7750
O
HOH
572
54.360
30.727
49.850
1.000
32.70

ATOM
7751
O
HOH
573
79.679
2.761
38.548
1.000
28.97

ATOM
7752
O
HOH
574
84.928
67.660
11.745
1.000
44.86

ATOM
7753
O
HOH
575
42.718
39.055
40.104
1.000
25.99

ATOM
7754
O
HOH
576
83.908
26.100
25.540
1.000
36.04

ATOM
7755
O
HOH
577
79.031
30.325
46.969
1.000
47.65

ATOM
7756
O
HOH
578
75.839
21.026
5.657
1.000
33.97

ATOM
7757
O
HOH
579
65.299
−7.114
42.215
1.000
34.12

ATOM
7758
O
HOH
580
94.282
20.055
16.879
1.000
32.93

ATOM
7759
O
HOH
581
80.726
4.373
35.442
1.000
33.52

ATOM
7760
O
HOH
582
58.177
44.900
50.843
1.000
39.41

[0204] All data collection was carried out on an MAR Research (Hamburg, Germany) 345-mm image plate system installed on a Rigaku RU-200B rotating anode x-ray generator equipped with Osmic mirrors (Osmic, Inc., Troy, Mich.) and using an X-stream cryogenic system (obtained from Molecular Structure Corporation, The Woodlands, Tex.). Data from 0.5° oscillations were integrated and scaled using DENZO and SCALEPACK (Otwinowski et al., Methods Enzymology, Vol. 276, pp. 307-326 (1997)). Crystals were mounted in a fiber loop, dipped in mother liquor with 25% glycerol added, and flash-cooled in liquid nitrogen for data collection at 100° K. An initial data set was collected to 2.4 Å resolution, which was used to obtain a molecular replacement solution. The space group was identified as C2, with an ERAB or HADH2 tetramer in the asymmetric unit.

[0205] The structure was determined by molecular replacement using the program EPMR (Kissinger et al., Acta Crystallography, Vol. D55, pp. 484-491 (1999)) with the wild-type protein tetramer as the search model. A solution was obtained with a correlation coefficient of 0.682 (R-factor=0.361) for data between 15 and 4 Å.

[0206] A subsequent data set was collected to a resolution of 2.0 Å., and this data set was used for refinement. Initial refinement was carried out using standard rigid-body, simulated-annealing, positional, and temperature factor refinement protocols in X-PLOR Version 3.1 (Brünger, XPLOR Manual, Version 3.1, Yale University Press, New Haven, Conn. (1992)) with the application of non-crystallographic symmetry (NCS) restraints. The progress of the refinement was monitored by the free R-factor (Brunger, Nature, Vol. 355, pp. 472-475 (1992)) using 5% of the reflections taken from thin resolution shells. The final stages of refinement were performed using SHELX-97 (Sheldrick et al., Methods Enzymology, Vol. 277, pp. 319-344 (1997)). All data from 25.0 to 2.0 Å were used, and a bulk solvent correction was applied. Local NCS restraints were applied throughout the refinement to residues 5-205 and 220-261 of each monomer. X-FIT (McRee, Journal of Molecular Graphics, Vol. 10, pp. 44-46 (1992)) was used for rebuilding and visual analysis of the structural model. Two-hundred eighty-two (282) water molecules were fit using the automatic water fitting procedures in SHELX while monitoring the effect on the free R factor. The final, refined model includes residues 5-261 of each of the four monomers in the asymmetric unit, with one NAD molecule bound to each monomer and an inhibitor molecule bound to three of the monomers. The final crystallographic R-factor was 0.215 (Rfree=0.265) for all unique data between 25.0 and 2.0 Å resolution. The RMS deviations from target stereochemistry (Engh et al., Acta Crystallography, Vol. A47, pp. 392-400 (1991)) were 0.005 Å for bond lengths and 1.5° for bond angles. All backbone dihedral angles fall in allowed regions of the Ramachandran plot except those for Ala 154, which occurs in a generously allowed region in all four monomers, and which forms a part of the nucleotide-binding pocket. Proline 224 participates in a cis peptide bond.

[0207] E. The ERAB or HADH2 Crystal Structure

[0208] Wild-type ERAB or HADH2 forms a tetramer in solution (He et al. (1998), supra). Likewise, a tetramer occupied the asymmetric unit of the crystal of the C214R mutant ERAB or HADH2. The conformations of the four subunits were essentially identical with the exception of a mobile loop near the substrate-binding site. Each ERAB or HADH2 monomer (FIG. 1) formed a single domain with the overall polypeptide chain topology characteristic of the SDR family of enzymes (Jörnvall et al., Biochemistry, Vol. 34, pp. 6003-6013 (1995)). The entire polypeptide chain of each of the four monomers had clearly defined electron density with the exception of the first five residues of each monomer, which were apparently disordered. ERAB or HADH2 contained a “Rossman fold” dinucleotide-binding motif (Rossman et al., The Enzymes, Academic Press, NY, pp. 61-102 (1975)), comprising a core β-sheet of seven parallel strands sandwiched between two sets of three α-helices.

[0209] Certain important aspects of the chain fold in ERAB or HADH2 arose from two insertions in the wild-type ERAB or HADH2 sequence relative to other members of the SDR family (see FIG. 2). These insertions formed structural elements that extended from opposite ends of each monomer (FIG. 1B). The first insertion residues (102-107) formed a short β hairpin structure (βDE1,βDE2) that extended the enzyme surface on one side of the substrate-binding cleft. This insertion also extended a monomer-monomer interface in the tetramer by contacting helix αE2 of an adjacent subunit. A second insertion (residues 141-146) extended the loop between αE2 and βE. This loop, which had extensive internal hydrogen bonding, did not lie near any active site region in the tetramer, but contacted Phe223 of an adjacent subunit and extends the subunit interface. Although the functional significance of these two structural elements of the protein is unknown, antibodies raised against peptides that encompass these insertion regions block the interaction of ERAB or HADH2 with β-amyloid (Yan et al. (1997), supra).

[0210] A ribbon representation of the ERAB or HADH2 tetramer is shown in FIG. 3. The subunit interactions in the ERAB or HADH2 tetramer closely resembled those in the tetramers formed by certain other members of the SDR family, including 3α, 20β-hydroxysteroid dehydrogenase [Ghosh et al., Proceedings of National Academy of Science, USA, Vol. 88, pp. 10064-10068 (1991)] and 7α-hydroxysteroid dehydrogenase [Tanaka et al., Biochemistry, Vol. 35, pp. 7715-7730 (1996)]. The subunits in the tetramer were related by three mutually perpendicular two-fold axes, and each subunit contacted each of the other three subunits. The four active site regions were exposed on the outside of the tetramer, with a distance of about 31 Å between the reactive C4 atoms in the nicotinamide ring of each bound NAD+ cofactor.

[0211] Electron density for the bound NAD+ was clearly visible in all four subunits. Electron density for the inhibitor Compound I, however, was seen in only three of the four monomers in the asymmetric unit. The fourth monomer was involved in a crystal packing interaction that appeared to alter the conformation of the loop formed by residues 205 to 220, which formed one side of the substrate-binding cavity in the enzyme. The binding cleft was narrowed slightly in this monomer, which apparently precluded inhibitor binding. Therefore crystal formation and occupation of the fourth binding site by the inhibitor may be mutually exclusive.

[0212] Conversely, the corresponding region in other members of the SDR family has been observed to be mobile. In 7α-hydroxysteroid dehydrogenase, this region undergoes a large conformational change upon substrate binding (Tanaka et al. (1996) supra). The same region in Drosophila alcohol dehydrogenase is disordered in the enzyme-NAD+ complex and assumes differing conformations in the presence of different bound inhibitors (Benach et al., Journal of Molecular Biology, Vol. 289, No. 2, pp. 335-55 (1999)). In the crystal structure of cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase, this region is also observed to be disordered in the absence of substrate (Hülsmeyer et al., Protein Science, Vol. 7, pp. 1286-1293 (1998)). The flexibility of the substrate-binding flap may be important in allowing these enzymes to accommodate multiple substrates.

[0213] In the presence of inhibitor Compound I, the substrate-binding cavity formed a long, narrow cleft. One side of the cleft was composed of residues from two strands of the protein (residues 95-99 and 155-168). Residues 205-217, which formed part of the flexible substrate-binding flap, formed the other side of the cleft. Residue 214, which was mutated from Cys to Arg to facilitate crystallization, lay within this region but projected toward the exterior of the protein away from the substrate-binding cleft and was not in proximity to the bound inhibitor. The floor of the cleft was formed by the carboxy-terminus of the protein (residues 257-261). The substrate-binding cleft was largely hydrophobic in nature. A series of lysine residues (Lys 99, Lys 104, Lys 105) lay outside of the cleft at the site of the β-hairpin insertion region. These residues lay about 20 to 30 Å away from the reactive C4 atom of the NAD+, which corresponded to the distance between the phosphates and the reactive carbonyl group in an extended acetoacetyl-CoA molecule. This insertion in ERAB or HADH2 may therefore contribute to the affinity of the enzyme for acetoacetyl-CoA as a substrate.

[0214] While the invention has been described in conjunction with examples and preferred embodiments thereof, it is to be understood that the foregoing description is exemplary and explanatory in nature, and is intended to illustrate the invention and its preferred embodiments. Thus, the invention is intended to be defined not by the above description, but by the following claims and their equivalents.

Peptide mutant of human ERAB or HADH2, its X-ray crystal structure, and materials and method for identification of inhibitors thereof

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