Structures of substrate binding pockets of SCF complexes

[0001] A portion of the disclosure of this patent document contains material that is subject to copyright protection. The copyright owner has no objection to the facsimile reproduction by anyone of the patent document or patent disclosure, as it appears in the Patent and Trademark Office patent file or records, but otherwise reserves all copyright rights whatsoever.

FIELD OF THE INVENTION

[0002] The present invention relates to binding pockets of Skp1-Cdc53/Cullin-F-box protein (SCF) E3 ubiquitin ligases associated with substrate selection and/or orientation. In particular, the invention relates to a crystal comprising such binding pockets. The crystal may be useful for modeling and/or synthesizing mimetics of a binding pocket or ligands that associate with the binding pocket. Such mimetics or ligands may be capable of acting as modulators of the interactions of an SCF E3 ubiquitin ligase and its substrates, and they may be useful for treating, inhibiting, or preventing diseases modulated by such interactions.

[0003] Methods are also provided for regulating an SCF E3 ubiquitin ligase comprising changing a binding pocket associated with substrate selection and/or orientation.

BACKGROUND

[0004] The ubiquitin proteolytic system controls the precisely timed degradation of regulatory proteins in signaling, development and cell cycle progression. Substrate ubiquitination is catalyzed by a cascade of enzymes, termed E1, E2 and E3, which activate and then conjugate ubiquitin to the substrate (Hershko and Ciechanover, 1998). E3 enzymes, also known as ubiquitin ligases, contain substrate-specific recognition domains and catalyze the final step in ubiquitin transfer. Recognition is mediated by primary sequence elements in the substrate, referred to as degrons (Varshavsky, 1991). Control of the E3-substrate interaction forms the basis for regulated proteolysis; often post-translational substrate modification, most commonly phosphorylation, serves to target substrates to their cognate E3 enzymes (Deshaies, 1999). Two main classes of E3 enzyme are now evident, as characterized by the presence of either a HECT domain or a RING domain. The HECT domain class forms a catalytically essential thioester with ubiquitin, whereas the RING domain class relies on the E2 enzymes to provide catalytic activity (Pickart, 2001). The RING domain forms an E2 docking site and orients the substrate with respect to the E2.

[0005] Phosphorylation-dependent degrons direct substrates to a recently described class of multisubunit E3 enzymes termed Skp1-Cdc53/Cullin-F-box protein (SCF) complexes. SCF complexes are built on an invariant core machinery comprised of the adapter protein Skp1, the scaffold protein Cdc53 (called Cull in metazoans), and the RING-H2 domain protein Rbx1 (also called Roc1 or Hrt1), which interacts with an E2 enzyme, usually Cdc34 (Pickart, 2001). Substrates are brought to the core complex by one of a large family of variable adapter subunits called F-box proteins, each of which targets a limited number of specific substrates (Bai et al., 1996, Patton et al., 1998). F-box proteins typically have a bipartite structure with an N-terminal ˜40 amino acid F-box motif and a C-terminal protein-protein interaction domain, such as WD40 repeats or leucine rich repeats, which bind substrates (Bai et al, 1996; Feldman et al, 1997; Skowyra et al., 1997). The overall architecture of SCF complexes is conserved in several related ubiquitin ligase complexes including the Anaphase Promoting Complex/Cyclosome and the Von Hippel Lindau (VHL) tumor suppressor protein complex, each of which contain cullin family members, RING-H2 domain and substrate recognition subunits (Pickart, 2001; Kaelin, 2002).

[0006] Cell cycle progression depends on the precisely timed elimination of cyclins and cyclin-dependent kinase (CDK) inhibitors by the ubiquitin system (Harper et al, 2002). In yeast, G1 cyclin CDK activity phosphorylates a CDK inhibitor called Sic1, whose degradation is necessary for onset of B-type cyclin CDK activity and DNA replication (Schwob et al., 1994). Phospho-Sic1 is specifically recognized by the F-box protein Cdc4, which recruits Sic1 for ubiquitination by the Cdc34-SCF complex (Bai et al., 1996; Feldman et al., 1997; Skowyra et al., 1997). Stable forms of Sic1 that lack CDK phosphorylation sites cause a G1 phase arrest (Verma et al., 1997), whereas deletion of SIC1 causes premature DNA replication and rampant genome instability (Lengronne and Schwob, 2002). Cdc4 recruits several other substrates to the SCF core complex in a phosphorylation dependent manner, including the Cln-Cdc28 inhibitor/cytoskeletal scaffold protein Far1, the replication protein Cdc6 and the transcription factor Gcn4 (Patton et al., 1998). The F-box protein Grr1 functions in an analogous manner to render G1 cyclins unstable throughout the cell cycle, in a manner that depends on recognition of phospho-epitopes by the LRR domain of Grr1 (Skowyra et al, 1997; Hsiung et al, 2001).

[0007] In the metazoan cell cycle, SCF complexes target phosphorylated forms of the CDK inhibitor p27Kip1 and cyclin E, among other substrates. Interestingly, F-box protein specificity for these substrates is reversed compared to yeast, in that the WD40 domain of hCdc4/Fbw7/Ago/SEL-10 recognizes cyclin E (Strohmaier et al., 2001; Koepp et al., 2001; Moberg et al., 2001), whereas the LRR domain of Skp2 recognizes p27Kip1 in conjunction with the CDK-binding protein Cks1 (Harper, 2001). Both of these degradation pathways are perturbed in cancer cells. Many primary tumors express high levels of Skp2, which leads to premature degradation of p27Kip1 and cell cycle entry (Harper, 2001). Conversely, loss of Cdc4 function causes deregulation of cyclin E-CDK2 activity, which leads to precocious S phase entry and genome instability (Spruck et al., 1999). Mutations in the Drosophila homolog of CDC4, called ago, were isolated as homozygous recessive alleles in a screen for excess cell proliferation, a defect attributed to ectopic cyclin E activity (Moberg et al., 2001). Mutations in hCDC4 have been detected in several cancer cell lines that exhibit high levels of cyclin E (Moberg et al., 2001; Strohmaier et al., 2001), as well as in a significant fraction of primary endometrial cancers (Spruck et al., 2002). In addition, hCDC4 is located in the 4q32region, which is often deleted in various cancers (Spruck et al., 2002). Significantly, a high level of cyclin E correlates strongly with low survival rates in breast cancer (Keyomarsi et al., 2002). Other important substrates appear to be targeted for degradation by Cdc4 orthologs in a phosphorylation-dependent manner, including actived forms of the developmental regulator Notch and the presenilins, which are implicated in familial early onset Alzheimer's disease (Lai, 2002; Selkoe, 2001). SCF-dependent proteolysis also mediates other important signaling events, including phosphorylation-dependent degradation of the NFκB inhibitor IκBα and the proto-oncogene product β-catenin by the F-box protein β-TrCP (Pickart, 2001).

[0008] Several F-box proteins can recognize short phosphopeptide motifs that correspond to substrate sequences. However, it is unknown whether such interactions are analogous to phosphorylation-dependent interactions of SH2, PTB, 14-3-3, WW and FHA domains, each of which has been crystallized with its cognate phosphopeptide (Yaffe and Elia, 2001). For many SCF substrates, including Sic1, Cdc6 and Cln2, phosphorylation on multiple dispersed sites is required for recognition and degradation (Patton et al., 1998). We recently defined a high affinity consensus phosphopeptide binding motif for Cdc4, termed the Cdc4 phospho-degron (CPD), which bears the consensus I/L-I/L/P-pT-P-<KR>4 [SEQ ID NO:1], where < > indicates a disallowed residue (Nash et al., 2001). The P0 phospho-threonine residue, or less favorably a phospho-serine residue, and the P+1 proline are essential for interaction with Cdc4. Unexpectedly, the CPD consensus is at odds with the CDK phosphorylation site consensus, S/T-P-X-K/R [SEQ ID NO:2](Endicott et al., 1999). Thus, substrate recognition by the targeting kinase is counter-balanced against the targeting component of the degradation machinery. All nine CPD sites in Sic1 have one or more sub-optimal features: all lack consensus hydrophobic residues in the P−1 or P−2 positions, four have serine in place of threonine in the P0 position, and seven contain a disfavored basic residue in one of the +2 to +5 positions. Unexpectedly, Sic1 must be phosphorylated on at least six of its nine sites in order to allow recognition by Cdc4 (Nash et al., 2001). This requirement for multi-site phosphorylation in principle renders the rate of Sic1 degradation proportional to the sixth power of G1 CDK concentration (Ferrell, 1996). The inherently ultrasensitive nature of the Sic1 degradation reaction appears critical for the coordinated initiation of DNA replication by S phase CDK activity (Nash et al., 2001; Lengronne and Schwob, 2002).

[0009] The mechanism of the ubiquitin conjugation reaction is not well understood. The ability of E2-E3 enzyme complexes to form polymers of ubiquitin, itself an 8 kDa protein, on a protein substrate presumably demands a large catalytic cradle simply to accommodate the initial reactants (Pickart, 2001). The sequential addition of ubiquitin moieties onto the substrate must also entail considerable flexibility of the substrate and/or the enzyme complex in order to extend the ubiquitin chain. Recent structure determination and modeling of three E2-E3 complexes has provided insight into these issues. A complex of the E2 enzyme UbCH7 and the HECT domain enzyme E6AP reveals a distance of ˜50 Å between the E2 and E3 active sites, suggesting that catalytic transfer of ubiquitin requires large scale movements in an as yet undefined process (Huang et al., 1999). Similarly, a complex between UbCH7 and the RING domain E3 c-Cb1 contains a substantial gap between the E2 active site and the substrate binding site on c-Cb1 (Zheng et al., 2000). Structures of the SOCS-box adapter protein VHL in complex with a hydroxylated substrate peptide have recently been solved (Kaelin, 2002), but the orientation of the substrate binding site with respect to the E2 enzyme is unknown. Finally, structure determination and molecular modeling of the holo-SCFskp2 complex again suggests a distance of ˜50 Å between the substrate binding LRR domain in Skp2 and the E2 active site (Zheng et al., 2002). Notably, the extensive interdigitation of the Skp1-Skp2 interface and the Skp2 inter-domain interface rigidly fixes the orientation of the LRRs of Skp2, suggesting that the F-box protein might hold the substrate in a very precise orientation with respect to the E2 enzyme (Schulman et al., 2000). However, because the substrate binding site on Skp2 has not been determined, either by mutation or by co-crystallization with substrate peptide, it is not possible to deduce how SCF substrates might be positioned with respect to the E2 catalytic site.

SUMMARY OF THE INVENTION

[0010] Applicants have determined the structures of binding pockets of SCF E3 ubiquitin ligases involved in substrate recognition and/or orientation. More particularly, Applicants have solved the x-ray crystal structure of binding pockets of F-box proteins/F-box protein-Skp1 complexes of SCF E3 ubiquitin ligases that interact with Cdc4 phospho-degron (CPD) motifs.

[0011] Solving the crystal structure has enabled the determination of key structural features of substrate binding pockets of a SCF E3 ubiquitin ligase, particularly the shape of binding pockets, or parts thereof, that permit association of a substrate with a SCF E3 ubiquitin ligase or part thereof. The crystal structure also enables the determination of key structural features in substrates or ligands that interact or associate with the binding pockets.

[0012] Knowledge of the structural features of substrate binding pockets of a SCF E3 ubiquitin ligase is of significant utility in drug discovery. The SCF E3 ubiquitin ligase substrate interaction is the basis of many biological mechanisms. In particular it is the basis for regulated ubiquitin proteolysis resulting in degradation of regulatory proteins involved in signaling, development, and cell cycle progression. In addition, drugs may exert their effects through association with the binding pockets of SCF E3 ubiquitin ligases. The associations may occur with all or any parts of a binding pocket. An understanding of the association of a drug with binding pockets of SCF E3 ubiquitin ligases will lead to the design and optimization of drugs having more favorable associations with their targets and thus provide improved biological effects. Therefore, information about the shape and structure of substrate binding pockets of SCF E3 ubiquitin ligases is invaluable in designing potential modulators of the SCF E3 ubiquitin ligases for use in treating diseases and conditions associated with or modulated by the SCF ubiquitin ligases, including cancer and Alzheimer's Disease.

[0013] The present invention relates to an isolated binding pocket of an SCF E3 ubiquitin ligase involved in substrate recognition and/or orientation. In an embodiment, the invention relates to a binding pocket of an F-box protein/F-box protein-Skp1 complex of a SCF E3 ubiquitin ligase that interacts with a Cdc4 phospho-degron (CPD) motif. In an aspect of the invention, the binding pocket regulates the binding of a CPD motif to a SCF E3 ubiquitin ligase.

[0014] In an embodiment, the invention comprises the structure of a WD repeat domain of an F-box protein. The structure may also comprise a helical linker of an F-box protein and optionally an F-box domain of an F-box protein. Still further the structure may comprise a Skp1 protein.

[0015] The invention also relates to a crystal comprising a binding pocket of a SCF E3 ubiquitin ligase involved in substrate recognition and/or orientation.

[0016] In an embodiment, the invention provides a crystal comprising a WD repeat domain of an F-box protein. The crystal may also comprise a helical linker of an F-box protein and optionally an F-box domain of an F-box protein. Still further the crystal may comprise a Skp1 protein.

[0017] The present invention also contemplates molecules or molecular complexes that comprise all or parts of either one or more binding pockets of the invention, or homologs of these binding pockets that have similar structure and shape.

[0018] The invention also contemplates a crystal comprising a binding pocket of a SCF E3 ubiquitin ligase involved with substrate recognition and/or orientation in association with a substrate (e.g. CPD motif). A substrate may be complexed or associated with a binding pocket. The invention further contemplates a crystal comprising a binding pocket of a SCF E3 ubiquitin ligase involved with substrate recognition and/or orientation in association with a ligand. A ligand may be a modulator of the activity of a SCF E3 ubiquitin ligase. A ligand may be complexed or associated with a binding pocket

[0019] In an aspect the invention contemplates a crystal comprising a binding pocket of an SCF E3 ubiquitin ligase involved in substrate recognition and/or orientation complexed with a substrate from which it is possible to derive structural data for the substrate.

[0020] The shape and structure of a binding pocket may be defined by selected atomic contacts in the pocket. In an embodiment, the binding pocket is defined by one or more atomic interactions or enzyme atomic contacts as set forth in Table 3 or Table 4. Each of the atomic interactions is defined in Table 3 or Table 4 by an atomic contact (more preferably, a specific atom where indicated) on the F-box protein and by an atomic contact (more preferably a specific atom where indicated) on the substrate. The atomic interactions are also defined by an atomic contact on one portion of the F-box protein and an atomic contact on another portion of the F-box protein.

[0021] An isolated polypeptide comprising a binding pocket with the shape and structure of a binding pocket described herein is also within the scope of the invention.

[0022] The invention also provides a method for preparing a crystal of the invention, preferably a crystal of a binding pocket of an SCF E3 ubiquitin ligase involved in substrate recognition and/or orientation, or a complex of such a binding pocket and a substrate.

[0023] Crystal structures of the invention enable a model to be produced for a binding pocket of the invention, or complexes or parts thereof. The models will provide structural information about the interactions of a substrate or ligand with a binding pocket. Models may also be produced for substrates and ligands. A model and/or the crystal structure of the present invention may be stored on a computer-readable medium.

[0024] The present invention includes a model of a binding pocket of the present invention that substantially represents the structural coordinates specified in Table 6 or portions thereof. The invention also includes a model that comprises modifications of the structure substantially represented by the structural coordinates specified in Table 6. A model is a representation or image that predicts the actual structure of the binding pocket. As such, a model is a tool that can be used to probe the relationship between a binding pocket's structure and function at the atomic level, and to design molecules that can modulate the binding site and accordingly activity of an F-box protein or SCF complex.

[0025] Thus, the invention provides a model of: (a) a binding pocket of an SCF E3 ubiquitin ligase involved in substrate recognition and/or orientation; and (b) a modification of the model of (a).

[0026] A method is also provided for producing a model of the invention representing a binding pocket of an SCF E3 ubiquitin ligase involved in substrate recognition and/or orientation, comprising representing amino acids of the binding pocket at substantially the structural coordinates specified in Table 6.

[0027] A crystal and/or model of the invention may be used in a method of determining the secondary and/or tertiary structures of a polypeptide or binding pocket with incompletely characterised structure. Thus, a method is provided for determining at least a portion of the secondary and/or tertiary structure of molecules or molecular complexes which contain at least some structurally similar features to a binding pocket of the invention. This is achieved by using at least some of the structural coordinates set out in Table 6.

[0028] A crystal of the invention may be useful for designing, modeling, identifying, evaluating, and/or synthesizing mimetics of a binding pocket or ligands or substrates that associate with a binding pocket. Such mimetics or ligands may be capable of acting as modulators of an F-box protein or SCF E3 ubiquitin ligase activity, and they may be useful for treating, inhibiting, or preventing diseases modulated by such a protein or ligase.

[0029] Thus, the present invention contemplates a method of identifying a modulator of a F-box protein or an SCF E3 ubiquitin ligase comprising the step of applying the structural coordinates of a binding pocket, or atomic interactions, or atomic contacts of a binding pocket, to computationally evaluate a test ligand or substrate for its ability to associate with the binding pocket, or part thereof. Use of the structural coordinates of a binding pocket, or atomic interactions, or atomic contacts of a binding pocket to design or identify a modulator is also provided.

[0030] In an embodiment, the invention contemplates a method of identifying a modulator of an F-box protein or an SCF E3 ubiquitin ligase comprising determining if a test agent inhibits or potentiates the interaction of an F-box protein or SCF E3 ubiquitin ligase with its substrate.

[0031] The invention further contemplates classes of modulators of F-box proteins or SCF E3 ubiquitin ligases based on the shape and structure of a ligand or substrate defined in relation to the molecule's spatial association with a binding pocket of the invention. Generally, a method is provided for designing potential inhibitors of an F-box protein-substrate interaction or SCF E3 ubiquitin ligase-substrate interaction comprising the step of applying the structural coordinates of a substrate or ligand defined in relation to its spatial association with a binding pocket, or a part thereof, to generate a compound that is capable of associating with the binding pocket.

[0032] It will be appreciated that a modulator of an F-box protein or SCF E3 ubiquitin ligase may be identified by generating an actual secondary or three-dimensional model of a binding pocket, synthesizing a compound, and examining the components to find whether the required interaction occurs.

[0033] A potential modulator of an F-box protein or SCF E3 ubiquitin ligase identified by a method of the present invention may be confirmed as a modulator by synthesizing the compound, and testing its effect on the F-box protein or SCF E3 ubiquitin ligase in an assay.

[0034] A modulator of the invention may be converted using customary methods into pharmaceutical compositions. A modulator may be formulated into a pharmaceutical composition containing a modulator either alone or together with other active substances.

[0035] Therefore, the methods of the invention for identifying modulators may comprise one or more of the following additional steps:

[0036] (a) testing whether the modulator is a modulator of the activity of an F-box protein or an SCF E3 ubiquitin ligase, preferably testing the activity of the modulator in cellular assays and animal model assays;

[0037] (b) modifying the modulator;

[0038] (c) optionally rerunning steps (a) or (b); and

[0039] (d) preparing a pharmaceutical composition comprising the modulator.

[0040] Steps (a), (b) (c) and (d) may be carried out in any order, at different points in time, and they need not be sequential.

[0041] Still another aspect of the present invention provides a method of conducting a drug discovery business comprising:

[0042] (a) providing one or more systems employing the atomic interactions, atomic contacts, or structural coordinates of a binding pocket of an F-box protein or SCF E3 ubiquitin ligase involved in substrate recognition and/or orientation, for identifying agents by their ability to inhibit or potentiate the atomic interactions or atomic contacts of a binding pocket;

[0043] (b) conducting therapeutic profiling of agents identified in step (a), or further analogs thereof, for efficacy and toxicity in animals; and

[0044] (c) formulating a pharmaceutical preparation including one or more agents identified in step (b) as having an acceptable therapeutic profile.

[0045] A further aspect of the present invention provides a method of conducting a drug discovery business comprising:

[0046] (a) providing one or more systems for identifying agents by their ability to inhibit or potentiate the interaction between an F-box protein or SCF complex and its substrate; and

[0047] (b) conducting therapeutic profiling of agents identified in step (a), or further analogs thereof, for efficacy and toxicity in animals; and

[0048] (c) formulating a pharmaceutical preparation including one or more agents identified in step (b) as having an acceptable therapeutic profile.

[0049] In certain embodiments, the subject methods can also include a step of establishing a distribution system for distributing the pharmaceutical preparation for sale, and may optionally include establishing a sales group for marketing the pharmaceutical preparation.

[0050] Yet another aspect of the invention provides a method of conducting a target discovery business comprising:

[0051] (a) providing one or more systems employing the atomic interactions, atomic contacts, or structural coordinates of a binding pocket of an F-box protein or SCF complex involved in substrate recognition and/or orientation, for identifying agents by their ability to inhibit or potentiate the atomic interactions or atomic contacts;

[0052] (b) (optionally) conducting therapeutic profiling of agents identified in step (a) for efficacy and toxicity in animals; and

[0053] (c) licensing, to a third party, the rights for further drug development and/or sales for agents identified in step (a), or analogs thereof.

[0054] Methods are also provided for regulating an F-box protein—substrate interaction or an SCF E3 ubiquitin ligase-substrate interaction by changing a binding pocket involved in substrate recognition and/or orientation. A binding pocket may be changed by altering amino acid residues forming the binding pocket (e.g. introducing mutations) or using a modulator.

[0055] The invention also contemplates a method of treating or preventing a condition or disease associated with an F-box protein or an SCF E3 ubiquitin ligase in a cellular organism, comprising:

[0056] (a) administering a modulator of the invention in an acceptable pharmaceutical preparation; and

[0057] (b) potentiating or inhibiting the F-box protein or SCF E3 ubiquitin ligase to treat or prevent the disease.

[0058] In an embodiment the condition or disease is cancer or Alzheimer's disease.

[0059] The invention provides for the use of a modulator identified by the methods of the invention in the preparation of a medicament to treat or prevent a disease in a cellular organism. Use of modulators of the invention to manufacture a medicament is also provided.

[0060] These and other aspects of the present invention will become evident upon reference to the following detailed description and Tables, and attached drawings.

DESCRIPTION OF THE DRAWINGS AND TABLES

[0061] The present invention will now be described only by way of example, in which reference will be made to the following Figures:

[0062]
FIG. 1 shows structure based sequence alignments of (A) Skp1 orthologs and (B) Cdc4 orthologs (red) and paralogs (black). Human Fbw7 and P-TrCP1 are isoforms 1 and 2, respectively. Secondary structure elements are colored as in FIG. 2A. Disordered regions in the crystal structure are shown as dashed lines. Red residues are essential for the Cdc4 function, blue residues strongly influence but do not abrogate function, green residues are non-essential but conserved around the binding pocket, and yellow residues are conserved elsewhere. Circles indicate mutations associated with excessive cell proliferation in flies and/or cancer in humans. Deletion of residues 37-64 in Skp1 is denoted by a triangle and a replacement of two closely placed loops from residues 602-605 and 609-624 is denoted by the underline of the short interloop sequence Gly-Glu-Leu. Insertions to optimize sequence alignments are indicated by number of residues inserted in gray. The non-standard β-strand element 91 in ScCdc4 is marked by the red asterisk and is shown in full at the bottom of the alignment. Residues that anchor helix α6 to the F-box domain are marked by green hearts, those that anchor helix α6 to the WD40 domain by red hearts and those that make direct contact between the WD40 domain and F-box domain by blue asterisks. [SEQ ID NOs 3-16.]

[0063]
FIG. 2 shows an overview of the Skp1-Cdc4-CPD complex. (A) Ribbon representation of Skp1 and the F-box domain (274-319), the helical linker region (331-366), and the WD40 domain of Cdc4 (367-744) coloured green, red, pink, and blue, respectively. The bound cyclin E derived CPD peptide is shown in purple with the phosphothreonine moiety shown in ball and stick representation. Secondary structure elements are indicated. Positions of disordered loop regions are shown as ribbon breaks. All ribbons representations were generated using Ribbons. (B) Ribbons representation highlighting the WD 40 domain of Cdc4. β propeller blades are denoted PB1 to PB8, and the component secondary structure elements are indicated. Ribbons and CPD peptide are coloured as in (A). Position of the WD40 domain is identical to that in FIGS. 4A to 4C. (C) The structured linkage between the WD40 domain and the F box domain of Cdc4.

[0064]
FIG. 3 shows an overview of the CPD binding region of the Ccdc4 WD40 repeat domain. (A) Molecular surface representation of the CPD binding pocket indicating invariant and highly conserved residues. Basic, hydrophobic and small residues are coloured blue, green and orange respectively. The bound CPD is shown in ball and stick representation with carbon, nitrogen, oxygen and phosphorous atoms coloured white, blue, red and yellow respectively. All surface representation were generated using Grasp. (B) Surface representation of CPD binding region as oriented in (A) coloured according to electrostatic potential. Blue and red indicate regions of positive and negative potential respectively (10 to −10 kBT). Residues of the bound CPD are labeled. (C) Stereo ribbons representation highlighting side chains and molecular interactions in the CPD binding pocket. CPD residues and highly conserved and invariant Cdc4 residues are displayed in ball and stick representation. Sites of mutation that give rise to severe loss of function are coloured red, and intermediate loss of function are coloured yellow (see Table 5). All other highly conserved and invariant residues are coloured green. Reference propeller blades of the WD40 repeat domain are indicated. (D) Stereo ribbons representation of the CPD binding pocket highlighting cancer causing mutations in drosophila and human Cdc4 orthologues. Arginine mutations in H-cell lines or entrometrial cells are coloured red. Drosophila mutations are coloured blue and Cdc4 temperature sensitive mutations (Rosamond personal communication) are coloured yellow. (E) Multiple Anomalous Dispersion phased electron density map corresponding to the CPD bound to the WD40 repeat domain of Cdc4. Refined CPD model is shown in ball and stick representation. Figure generate using O. (F) Schematic of CPD binding pocket interactions with the CPD peptide.

[0065]
FIG. 4 shows (A) Stereo ribbons representation of the human Skp1-Skp2 complex superimposed on the yeast Skp1-Cdc4-CPD complex. Human Skp1-Skp2 and yeast Skp1-Cdc4 were superimposed through a least squares optimization of Skp1, strands 1 to 3 and a-helices 1 to 6 (RMSD=0.74 Å). The yeast Skp1-Cdc4 complex is coloured as in FIG. 2. Human Skp1, the Skp2 F-box, and the Skp2 Leucine-rich repeat domain are coloured orange, green, and light blue, respectively. Skp1 and F box secondary structure elements that deviate significantly in size and position between the two structures are labeled. (B) Model of the SCFCdc4-CPD E2 complex. The yeast Skp1-Cdc4-CPD complex is coloured as in FIG. 2. Cull, Rbx1, and E2 proteins are coloured pink, red, and light blue, respectively. The arrow indicates the distance between the peptide binding site and the active site cysteine of the E2. The structure was generated using the ternary complex of the cullin cdc53, rbx1, Skp1, previously reported, and superimposing the E2 structure from the E2/Cb1 ring finger structure and the structure of Skp1, Cdc4 and a phosphorylated CPD peptide

[0066]
FIG. 5 shows (A) Selection of Sic1 phosphoisoforms by wild type and mutant forms of Cdc4. (B) In vitro ubiquitination of Sic1 isoforms by wild type and mutant SCFCdc4 complexes. (C) Natural CPD sites deviate from the optimal CPD by one or more or more residues.

[0067]
FIG. 6 shows substrate orientation within the Skp1-Cdc4-CPD complex. (A) Comparison of the ScSkp1-ScCdc4-CPD complex and the hSkp1-hSkp2 complex. Complexes were superimposed through a least squares optimization of Skp1 β-strands 1 to 3 and a-helices 1 to 6 (RMSD Cα=0.74 Å). Skp1 and F-box secondary structure elements that deviate significantly in size and position between the two structures are labeled. (B) Model of the ubiquitin-E2-SCFCd4-CPD complex. The arrow indicates the 59 Å distance separating the phosphate group of the CPD and the active site cysteine of the E2.

[0068]
FIG. 7 shows the CPD binding pocket of the WD40 domain. (A) Surface representation of the CPD binding pocket indicating invariant and highly conserved residues. Basic (blue), hydrophobic (green) and small polar residues (orange) are shown. The bound CPD is in ball and stick representation with carbon (white), nitrogen (blue), oxygen (red) and phosphorous (yellow) atoms shown. (B) Surface representation of CPD binding region indicating electrostatic potential. Blue and red indicate regions of positive and negative potential, respectively, over the range 10 to −10 kBT. (C) Stereo ribbons representation of side chains and molecular interactions in the CPD binding pocket. Highly conserved and invariant side chains of Cdc4 and the CPD are displayed in ball and stick representation. Sites of mutation that give rise to severe and intermediate loss of function (see FIG. 8) are colored red and blue, respectively; non-essential residues are colored green.

[0069] (D) Schematic of CPD Binding Pocket Interactions With the CPD Peptide.

[0070]
FIG. 8 shows structure-guided mutational analysis of Cdc4. (A) Residues required for interaction of phospho-Sic1 and Cdc4 in vitro. Sic1 was phosphorylated with Cln2-Cdc28 kinase and captured onto resin loaded with either wild type or the indicated mutant forms of Skp1-Cdc4 complex. (B) Residues essential for Cdc4 function in vivo. Complementation of a cdc4Δ strain by the indicated alleles was assessed in a plasmid shuffle assay. The R485A, R467A and R534A mutations in Cdc4 have been previously shown to disrupt function in vivo (Nash et al., 2001) and so are not shown. (C) Effect of Cdc4 mutations on sensitivity to increased SIC1 dosage. Strains bearing indicated CDC4 alleles were tested for sensitivity to overexpression of wild type SIC1 and a partially stabilized version, SIC1Thr33Val from the GAL1 promoter. Strains were incubated on galactose or glucose medium for 2 days at 30° C.

[0071]
FIG. 9 shows the modulation of the multisite requirement for phospho-Sic1-Cdc4 interaction. (A) All natural CPD sites in Sic1 deviate from the CPD consensus. Underlined residues indicate sub-optimal residues at the P−1 and P−2 positions, boxed residues indicate sub-optimal basic residues at the P+2 to P+5 positions and asterisks indicate a sub-optimal pSer at the P0 position. (B) Capture of Sic1 phospho-isoforms by wild type and mutant Cdc4. Pools of differentially phosphorylated Sic1 were captured on Skp1-Cdc4 resin, using either wild type or the indicated mutant forms of Cdc4 compromised for selection at the P−1 position (V384N W717N) or the P+2 to P+5 positions (K402A R443D). The input and bound phospho-Sic1 isoform pools were resolved by denaturing IEF-2D gel electrophoresis and visualized by anti-Sic1 immunoblot. (C) Ubiquitination of phospho-Sic1 isoforms by wild type and mutant SCFCdc4 complexes. Pools of differently phosphorylated Sic1 were incubated in solution with an equimolar amount of the indicated SCFCdC4 complexes, Cdc34, ubiquitin and ATP for 1 h at 30° C. Input and reaction products were separated and visualized as in (B). Arrows indicate the less phosphorylated forms of Sic1 captured by Cdc4 selection mutants. Asterisk indicates more extensively ubiquitinated species (D) Possible interaction mechanisms for single site and multi-site dependent substrate binding to Cdc4. In a two-site cooperative interaction model (left), a primary high affinity CPD binding site acts in conjunction with a secondary weak CPD binding site. The free energy for the two interactions is additive and so the overall Kd increases multiplicatively. In a single-site allovalent interaction (right), multiple low affinity CPD sites engage a single CPD binding site on Cdc4 in equilibrium. The high local concentration of CPD sites increases the probability of binding such that Sic1 is unable to diffuse away from Cdc4 before re-binding occurs. The probability of re-binding increases as an exponential function of the number of CPD sites, thus accounting for the apparent cooperativity of the interaction.

[0072] The present invention will now be described only by way of example, in which reference will be made to the following Tables:

[0073] Table 1 shows data collection, structure determination and refinement statistics of a crystal of the invention.

[0074] Table 2 shows data collection, structure determination and refinement statistics of a crystal of the invention.

[0075] Table 3 shows intermolecular contacts in a binding pocket of the invention.

[0076] Table 4 shows intermolecular contacts in a binding pocket of the invention.

[0077] Table 5 shows mutant cdc4 polyppeptides of the invention. Mutational analysis of the CPD binding surface. Mutants were tested in vitro by ability to bind phosphorylated Sic1 and then captured onto GST-Skp1/Cdc4 resin and detected with anti-sic1 antibody. Mutants were tested in vivo by ability to degrade GAL1-SIC1 or various phosphorylation mutants. Sites are as follows: 3=Thr 33, Thr 45, Ser 76; 4=Thr 5, Thr 33, Thr 45, Ser 76; 5=Thr 2, Thr 5, Thr 33, Thr 45, Ser 76; 6=Thr 2, Thr 5, Thr 33, Thr 45, Ser 69, Ser 76; 7=Thr 2, Thr 5, Thr 33, Thr 45, Ser 69, Ser 76, Ser 80. GAL1-SIC1 plasmids were transformed into a cdc4Δ strain containing a copy of CDC4 on a TRP1 ARS CEN plasmid. Strains were incubated for 2 days at 30° C.

[0078] Table 6 shows the structural coordinates of a binding pocket of the invention.

[0079] In Table 6, from the left, the second column identifies the atom number; the third identifies the atom type; the fourth identifies the amino acid type; the sixth identifies the residue number; the seventh identifies the x coordinates; the eighth identifies the y coordinates; the ninth identifies the z coordinates; the tenth identifies the occupancy; and the eleventh identifies the temperature factor.

[0080] Table 7 lists the oligonucleotides used in the studies described in the examples.

[0081] Table 8 lists the plasmids used in the studies described in the examples.

DETAILED DESCRIPTION OF THE INVENTION

[0082] In accordance with the present invention there may be employed conventional molecular biology, microbiology, and recombinant DNA techniques within the skill of the art. Such techniques are explained fully in the literature. See for example, Sambrook, Fritsch, & Maniatis, Molecular Cloning: A Laboratory Manual, Second Edition (1989) Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.); DNA Cloning: A Practical Approach, Volumes I and II (D. N. Glover ed. 1985); Oligonucleotide Synthesis (M. J. Gait ed. 1984); Nucleic Acid Hybridization B. D. Hames & S. J. Higgins eds. (1985); Transcription and Translation B. D. Hames & S. J. Higgins eds (1984); Animal Cell Culture R. I. Freshney, ed. (1986); Immobilized Cells and enzymes IRL Press, (1986); and B. Perbal, A Practical Guide to Molecular Cloning (1984).

[0083] Glossary

[0084] Abbreviations for amino acid residues are the standard 3-letter and/or 1-letter codes used in the art to refer to one of the 20 common L-amino acids. Likewise abbreviations for nucleic acids are the standard codes used in the art.

[0085] “Skp1-Cdc53/Cullin-F-box protein (SCF) E3 ubiquitin ligases” or “SCF complex” refers to a protein complex comprising the adaptor protein Skp1, the scaffold protein cdc53/cullin, a RING-H2 domain protein Rbx1 (also called Roc1 or Hrt1), and an F-box protein, which protein complex augments or otherwise facilitates the ubiquitination of a protein. In certain aspects of the present invention an SCF complex refers to a complex comprising Skp1 and an F box protein or parts thereof.

[0086] In the context of the present invention the term “F-box protein” refers to a protein comprising a characteristic structural motif called the F-box as described in Bai et al, (1996 Cell 86: 263-274) and a protein-protein interaction domain, in particular a WD40 repeat motif or domain. Examples of F-box Proteins include Cdc4 polypeptides, and homologs or portions thereof, preferably portions that interact with a CPD motif (e.g. WD repeat).

[0087] A “WD40 repeat”, “WD40 motif”, or “WD repeat domain” is generally defined as a contiguous sequence of about 25 to 50 amino acids with relatively-well conserved sets of amino acids [i.e. Trp-Asp (WD)] at the ends (amino- and carboxyl-terminal) of the sequence. (For reviews see Neer E J, Schmidt C J, Nambudripad R & Smith TF: “The ancient regulatory-protein family of WD-repeat proteins,” Nature 371, 297-300 (1994) PMID: 8090199; and Smith TF, Gaitatzes CG, Saxena K & Neer EJ: “The WD-repeat: a common architecture for diverse functions,” TIBS 24, 181-185 (1999) PMID: 10322433.) A WD repeat motif or domain can also be defined as a domain of an F-box protein that interacts with a CPD motif or like motif.

[0088] Examples of WD-repeat-containing proteins are cdc4 polypeptides, Met30 homologues and orthologues (see for example, GenBank Accession No. P39014 or MT30_YEAST—SEQ ID NO.17) and β-TRCP homologues and orthologues (see for example, GenBank Accession No. NP—033901—SEQ ID NO.18). Other WD40 repeat-containing proteins will, however, be appreciated by those skilled in the art. A WD40-repeat protein also includes a part of the protein. A person skilled in the art may conduct searches to identify proteins that contain WD-40 repeats, in particular F-box proteins. For example, on-line databases such as GenBank or SwissProt can be searched, either with an entire sequence of a WD-40-containing protein, or with a consensus WD-40 repeat sequence. Various search algorithms and/or programs may be used, including FASTA, BLAST or ENTREZ. FASTA and BLAST are available as a part of the GCG sequence analysis package (University of Wisconsin, Madison, Wis.). ENTREZ is available through the National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, Md. The number of WD-40 repeats in a particular protein can range from two to more than eight.

[0089] A “Cdc4 Phospho-Degron motif” or “CPD motif” is a motif that targets substrates for ubiquitination by SCF complexes. The motif can be defined by the consensus sequence X2-X3-pThr-Pro-X4 (SEQ ID NO.19), more particularly X2-X3-pThr-Pro-X4-X5-X6-X7 (SEQ ID NO.20), wherein X2 represents Leu, Pro, or Ile, preferably Leu or Ile; X3 represents Leu, Ile, Val, or Pro, preferably Ile, Leu, or Pro; X4 represents any amino acid except basic and bulky hydrophobic amino acids, preferably X4, X5 and X6 represent any amino acid except basic and bulky hydrophobic amino acids, preferably X4 is any amino acid except Arg, Lys, Tyr, or Trp, more preferably X4 is Ile, Val, Pro, or Gln, preferably X5 and X6 are any amino acid except Arg, Lys, or Tyr and more preferably X5 is Gln, Leu, Met, Thr, or Glu, and X6 is Gin, Ala, Thr, Glu, or Ser; and X7 is any amino acid, preferably not a basic or bulky hydrophobic amino acid, more preferably X7 is any amino acid except Arg, Lys, or Tyr, most preferably X7 is Leu, Trp, Asp, Pro, or Gly. A CPD motif preferably comprises the consensus sequence -Leu/Gly/Tyr-Pro-pThr-Pro- (SEQ ID NO.21).

[0090] A CPD motif containing protein includes proteins comprising the CPD motif including but not limited to Gcn4, Cyclin E, Far1, Ash1, Sic1, Pc17, Cdc16, p27kip1, Cln2, and transcription factors such as β catenin or IKβα, and homologues of these proteins. The term includes but is not limited to all homologs, orthologs, naturally occurring allelic variants, isoforms and precursors of the polypeptides. Other proteins containing CPD motif sequences may be identified with a protein homology search, for example by searching available databases such as GenBank or SwissProt and various search algorithms and/or programs may be used including FASTA, BLAST (available as a part of the GCG sequence analysis package, University of Wisconsin, Madison, Wis.), or ENTREZ (National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, Md.).

[0091] The term “substrate” refers to a protein that interacts with an F-box protein targeting it for ubiquitin-dependent proteolysis, or a protein targeted for F-box dependent degradation. Examples of substrates are CPD motif containing proteins including Gcn4, CyclinE, Far1, Ash1, Sic1, Pc17, Cdc16, p27kip1; Cln2, and, transcription factors such as β catenin or Iκβα. The term also refers to a part of a protein that interacts with an F-box protein, including a CPD motif, and analogues of substrates or parts thereof

[0092] A “ligand” refers to a compound or entity that associates with a binding pocket, or modulators of an F-box protein or SCF E3 ubiquitin ligase, including inhibitors. A ligand may be designed rationally by using a model according to the present invention.

[0093] The terms “cdc4 polypeptide” is used to refer to polypeptides of the cdc4 family of proteins characterized by an F-box motif and WD repeats. The term includes but is not limited to all homologs, orthologs, naturally occurring allelic variants, isoforms and precursors of the polypeptides of GenBank Accession Nos. S56245 or SEQ ID NO. 22 (Saccharomyces cerevisiae cdc4), CAA65538 or SEQ ID NO. 23 (Candida albicans cdc4), AAL07271 or SEQ ID NO.24 (human cdc4), AAC47809 or SEQ ID NO.25 (sel-10), AAK57547 or SEQ ID NO.26 (Homo sapiens F-box protein FBW7), and AAG09623F or SEQ ID NO. 27 (Homo sapiens F box protein FBX30). In general, for example, naturally occurring allelic variants will share significant homology (70-90%) to these sequences. Allelic variants may contain conservative amino acid substitutions from cdc4 sequences or will contain a substitution of an amino acid from a corresponding position in a cdc4 homologue such as, for example, the human homologue. [See Strohmaier,H., Nature 413 (6853), 316-322 (2001) for a description and sequence of human cdc4]. The term also includes the mutant cdc4 polypeptides described herein. FIG. 1 shows a structure based sequence alignment of cdc4 orthologs and paralogs.

[0094] The term “cdc53” or “cdc53 polypeptide” is used interchangeably herein with the term “cullins” when referring to a vertebrate homolog of the yeast cdc53 protein. The term “cullin polypeptide” or “cullin protein”, refers to a member of the cullins family, e.g., any one of cul-1, -2, -3, -4, -5, or -6. The term includes but is not limited to all homologs, naturally occurring allelic variants, isoforms and precursors of a cdc53 polypeptide or cullin of GenBank Accession Nos. AAB38821 or SEQ ID NO. 28 (Saccharomyces cerevisiae cdc53), AAC36304 or SEQ ID NO. 29 (Homo sapiens cullin 3), AAC51190 or SEQ ID NO. 30 (Homo sapiens cullin 2), NP 003581 or SEQ ID NO. 31 (Homo sapiens cullin 3), AF126404—1 or SEQ ID NO. 32 (Homo sapiens cullin 2), CUL1_CAEEL or SEQ ID NO. 33 (Caenorhabditis elegans cullin 1), AAA85085 or SEQ ID NO. 34 (Drosophila melanogaster cullin 1) and the cullins described in Kipreos ET (Cell 1996 Jun. 14;85(6):829-39). In general for example, naturally occurring allelic variants of cdc53 will share significant homology (70-90%) to the cdc53 or cullin sequences. Allelic variants may contain conservative amino acid substitutions from the cdc4 sequence or will contain a substitution of an amino acid from a corresponding position in a cdc4 homolog such as, for example, the human homolog.

[0095] The term “Skp1” or “Skp1 polypeptide” is used to refer to polypeptides that connect cell cycle regulators to the ubiquitin proteolysis machinery by associating with F-box proteins through the F-box motif. The term includes but is not limited to all homologs, naturally occurring allelic variants, isoforms and precursors of Skp1 of GenBank Accession Nos. SKP1_SCHPO or SEQ ID NO. 35 (Schizosaccharomyces pombe), BAB62325 or SEQ ID NO. 36 (Schizosaccharomyces pombe), AAC49492 or SEQ ID NO. 37 (Saccharomyces cerevisiae), and AAB17500 or SEQ ID NO. 38 (Saccharomyces cerevisiae). In general, for example, naturally occurring allelic variants of Skp1 will share significant homology (70-90%) to the Skp1 sequences. Allelic variants may contain conservative amino acid substitutions from the Skp1 sequence or will contain a substitution of an amino acid from a corresponding position in a Skp1 homolog such as, for example, the human homolog. FIG. 1 shows a structure based sequence alignment of Skp1 homologues.

[0096] A CPD motif and WD repeat or proteins containing same, cdc4 polypeptides, cdc53, Skp1, substrates, and SCF complexes, may be from any species, particularly a mammalian species, including bovine, ovine, porcine, murine, equine, preferably the human species, and from any source, whether natural, synthetic, semi-synthetic, or recombinant.

[0097] The term “agonist” of a binding pocket refers to a compound or ligand that interacts with the binding pocket and maintains or increases the activity of the binding pocket to which it binds. The term includes partial agonists and inverse agonists. Agonists may include proteins, peptides, nucleic acids, carbohydrates, or any other molecules that bind to a binding pocket. Agonists also include a molecule derived from a binding pocket. Peptide mimetics, synthetic molecules with physical structures designed to mimic structural features of particular peptides, may serve as agonists. The stimulation may be direct, or indirect, or by a competitive or non-competitive mechanism. The term includes partial agonists and inverse agonists.

[0098] As used herein, the term “partial agonist” means an agonist that is unable to evoke the maximal response of a biological system, even at a concentration sufficient to saturate the specific receptors.

[0099] As used herein, the term “partial inverse agonist” is an inverse agonist that evokes a submaximal response to a biological system, even at a concentration sufficient to saturate the specific receptors. At high concentrations, it will diminish the actions of a full inverse agonist.

[0100] The term “antagonist”, as used herein, refers to a ligand or compound that binds a binding pocket but does not maintain the activity of the binding pocket to which it binds. The term can also includes a ligand that reduces the action of another agent, such as an agonist. An antagonistic action may result from a combination of the substance being antagonised (chemical antagonism) or the production of an opposite effect through a different protein (functional antagonism or physiological antagonism) or as a consequence of competition for the binding site of an intermediate that links a protein to the effect observed (indirect antagonism). The antagonist may act at the same site as the agonist (competitive antagonism). Antagonists may include proteins, peptides, nucleic acids, carbohydrates, or any other molecules that bind to a binding pocket. Antagonists also include a molecule derived from a binding pocket. Peptide mimetics, synthetic molecules with physical structures designed to mimic structural features of particular peptides, may serve

[0101] As used herein, the term “competitive antagonism” refers to the competition between an agonist and an antagonist for a binding pocket of a protein that occurs when the binding of agonist and antagonist becomes mutually exclusive. This may be because the agonist and antagonist compete for the same binding sites or pockets, or combine with adjacent but overlapping sites. A third possibility is that different sites are involved but that they influence the receptor macromolecules in such a way that agonist and antagonist molecules cannot be bound at the same time. If the agonist and antagonist form only short lived combinations with a binding pocket so that equilibrium between agonist, antagonist and binding pocket is reached during the presence of the agonist, the antagonism will be surmountable over a wide range of concentrations. In contrast, some antagonists, when in close enough proximity to their binding site, may form a stable covalent bond with it and the antagonism becomes insurmountable when no spare receptors remain.

[0102] By being “derived from” a binding pocket is meant any molecular entity which is identical or substantially equivalent to the binding pocket. A peptide derived from a binding pocket may encompass the amino acid sequence of a naturally occurring binding pocket, any portion of that binding pocket or other molecular entity that functions to bind to an associated or interacting binding pocket. A peptide derived from such a binding pocket will interact directly or indirectly with an associated molecule in such a way as to mimic the native binding pocket. Such peptides may include competitive inhibitors, peptide mimetics, and the like. The entity will not include a full length sequence of a wild-type molecule. Peptide mimetics, synthetic molecules with physical structures designed to mimic structural features of particular peptides, may serve as inhibitors or enhancers.

[0103] “Peptide mimetics” are structures which serve as substitutes for peptides in interactions between molecules (See Morgan et al (1989), Ann. Reports Med. Chem. 24:243-252 for a review). Peptide mimetics include synthetic structures which may or may not contain amino acids and/or peptide bonds but retain the structural and functional features of a peptide, or agonist or antagonist (i.e. enhancer or inhibitor) of a binding pocket. Peptide mimetics also include peptoids, oligopeptoids (Simon et al (1972) Proc. Natl. Acad, Sci USA 89:9367); and peptide libraries containing peptides of a designed length representing all possible sequences of amino acids corresponding to a motif, peptide, or agonist or antagonist (i.e. enhancer or inhibitor) of the invention.

[0104] Sequences are “homologous” or considered “homologs” when at least about 70% (preferably at least about 80 to 90%, and most preferably at least 95%) of the nucleotides or amino acids match over a defined length of the molecule. “Substantially homologous” also includes sequences showing identity to the specified sequence. Percent identity can be determined electronically, e.g., by using the MEGALIGN program (DNASTAR, Inc., Madison Wis.) which can create alignments between two or more sequences according to different methods, e.g., the clustal method. (See, e.g., Higgins, D. G. and P. M. Sharp (1988) Gene 73:237-244.) Percent identity can also be determined by other methods known in the art, (e.g., the Jotun Hein method. (See, e.g., Hein, J. (1990) Methods Enzymol. 183:626-645) or by varying hybridization conditions). Preferably, the amino acid or nucleic acid sequences have an alignment score of greater than 5 (in standard deviation units) using the program ALIGN with the mutation gap matrix and a gap penalty of 6 or greater (Dayhoff).

[0105] Binding Pocket

[0106] “Binding pocket” refers to a region or site of an F-box protein or molecular complex thereof (e.g. Skp1-F-box complex, SCF E3 ubiquitin ligase) involved in substrate selection and/or orientation. As the result of its shape, a binding pocket associates with another region of an F-box protein or SCF complex or with a substrate or a part thereof.

[0107] In an aspect of the invention a binding pocket comprises one or more of the residues involved in selection and/or orientation of a substrate or ligand.

[0108] In an aspect of the invention a binding pocket is provided that comprises the WD40 repeat domain of an F-box protein. In another embodiment the binding pocket comprises a WD40 repeat domain and a helical linker of an F-box protein. In a further embodiment, the binding pocket comprises a WD40 repeat domain, a helical linker and an F-box domain of an F-box protein. In an embodiment the F-box protein is a cdc4 polypeptide or portion thereof.

[0109] A binding pocket of the invention may comprise a WD40 repeat domain characterized by one or more of the following characteristics:

[0110] (a) a 7 or 8 blade β-propeller structure, in particular a 8 blade β-propeller structure;

[0111] (b) a disk like structure characterized by a cavity in the middle and two opposing circular surfaces of different size;

[0112] (c) a conical frustum of about 40 Å top surface and about 50 Å bottom surface, an overall thickness of 30 Å and a central pore of 6 Å diameter; and

[0113] (d) a CPD binding site on the top surface of the frustum of (c) and running across the edge of the pore, while the bottom surface of the frustum links to the F-box domain.

[0114] A binding pocket of the invention may be characterized by one or more of the following characteristics:

[0115] (i) a dedicated pThr-Pro binding pocket;

[0116] (ii) a deep hydrophobic pocket that selects hydrophobic residues N-terminal to the phosphorylation site of a CPD, and

[0117] (iii) a through space electrostatic selection against basic residues C-terminal to the phosphorylation site of a CPD.

[0118] A binding pocket of the invention may comprise a helical linker characterized by a helices that form a stalk and pedestal like structure that connects and orients a WD repeat domain. The helical linker binding pocket can also be characterized by one or more of the following:

[0119] (a) a helix (e.g. α6 in FIG. 2 or FIG. 6) that is 30 Å in length and is anchored at its N-terminus to the hydrophobic core of the F-box/helical extension and at its C-terminus to the hydrophobic core of a WD repeat domain,

[0120] (b) the helix of (a) (e.g. α6) anchored at its amino terminus to an F-box through hydrophobic interactions (e.g. involving α6 residues Phe 355, Leu356, and F box residues Ile295, Ile296, Leu315, Leu 319 and Trp316 of Cdc4 or the corresponding residues in Cdc4 homologs, variants, precursors etc.);

[0121] (c) a second helix (e.g. helix 5) packed along the base of the helix of (a) or (b) opposite to the F-box domain through hydrophobic interactions (e.g. involving Tyr342, Leu338, and Leu 334 of Cdc4 or the corresponding residues in Cdc4 homologs, variants, precursors etc.);

[0122] (d) the helix of (a) (e.g. helix α6) anchored at its C-terminus through hydrophobic interactions;

[0123] (e) a C-terminal end of helix α6 inserted obliquely between propeller blades P7 and β8 of a WD40 domain through van der Wals and hydrophobic interactions (e.g. involving Trp365 and Ile361 with WD40 domain residues Val687, Ile696, Leu726, and Phe743 in β-propeller blades 7 and 8 of Cdc4 or the corresponding residues in Cdc4 homologs, variants, precursors etc.).

[0124] A CPD motif binding pocket of the invention may comprise a hydrophobic pocket that surrounds the open central channel of a 7 or 8 blade WD repeat propeller. A binding pocket of Cdc4 is more particularly characterized by one or more of the following:

[0125] (a) a WD repeat domain surface composed of invariant and highly conserved residues from β-propeller blades;

[0126] (b) a three-sided pocket formed by Trp426, Thr386, and Arg 485 (or the corresponding residues in Cdc4 homologs, variants, precursors etc.);

[0127] (c) a three-sided pocket formed by Trp426, Thr441, Thr 465, and Arg 485 (or the corresponding residues in Cdc4 homologs, variants, precursors etc.);

[0128] (d) a hydrophobic pocket composed of Trp 426, Trp 717, Thr 386, and Val 384 (or the corresponding residues in Cdc4 homologs, variants, precursors etc.);

[0129] (e) a pocket formed by Leu634, Met590, and Tyr574 (or the corresponding residues in Cdc4 homologs, variants, precursors etc.); and

[0130] (f) a pocket formed by Arg485, Arg467, Arg534, Tyr548, and Arg572 (or the corresponding residues in Cdc4 homologs, variants, precursors etc.);

[0131] A binding pocket may comprise one or more of the amino acid residues for an F-box protein crystal or F-box protein—substrate crystal identified in Table 3 or Table 4. In an aspect the binding pocket comprises the atomic contacts of atomic interactions 1 to 4 or interactions 5 to 8/9 identified in Table 3 or Table 4. In an aspect of the invention the binding pocket comprises all of the amino acid residues identified in Table 3 or Table 4.

[0132] The term “binding pocket” (BP) also includes a homolog of the binding pocket or a portion thereof. As used herein, the term “homolog” in reference to a binding pocket refers to a binding pocket or a portion thereof which may have deletions, insertions or substitutions of amino acid residues as long as the binding specificity is retained. In this regard, deliberate amino acid substitutions may be made on the basis of similarity in polarity, charge, solubility, hydrophobicity, hydrophilicity, and/or the amphipathic nature of the residues as long as the binding specificity of the binding pocket is retained.

[0133] As used herein, the term “portion thereof” means the structural coordinates corresponding to a sufficient number of amino acid residues of a binding pocket (or homologs thereof) that are capable of associating with a substrate (e.g. CPD motif) or ligand. For example, the structural coordinates provided in a crystal structure may contain a subset of the amino acid residues in a binding pocket which may be useful in the modelling and design of compounds that bind to the binding pocket.

[0134] Crystal

[0135] The invention provides crystal structures. As used herein, the term “crystal” or “crystalline” means a structure (such as a three dimensional (3D) solid aggregate) in which the plane faces intersect at definite angles and in which there is a regular structure (such as internal structure) of the constituent chemical species. The term “crystal” can include any one of: a solid physical crystal form such as an experimentally prepared crystal, a crystal structure derivable from the crystal (including secondary and/or tertiary and/or quaternary structural elements), a 2D and/or 3D model based on the crystal structure, a representation thereof such as a schematic representation thereof or a diagrammatic representation thereof, or a data set thereof for a computer.

[0136] In one aspect, the crystal is usable in X-ray crystallography techniques. Here, the crystals used can withstand exposure to X-ray beams used to produce a diffraction pattern data necessary to solve the X-ray crystallographic structure. A crystal may be characterized as being capable of diffracting x-rays in a pattern defined by one of the crystal forms depicted in Blundel et al 1976, Protein Crystallography, Academic Press.

[0137] A crystal of the invention is generally produced in a laboratory; that is, it is an isolated crystal produced by an individual.

[0138] The invention contemplates a crystal comprising a binding pocket of the invention, in particular a binding pocket of an F-box protein or SCF complex or portion thereof, involved in substrate selection and/or orientation.

[0139] In an aspect of the invention a crystal is provided that comprises the WD40 repeat domain of an F-box protein, in particular Cdc4. In another embodiment the crystal comprises a WD40 repeat domain and a helical linker of an F-box protein. In a further embodiment, the crystal comprises a WD40 repeat domain, a helical linker and an F-box domain of an F-box protein. In an embodiment the F-box protein is a cdc4 polypeptide or portion thereof.

[0140] A crystal of the invention comprising a WD40 repeat domain, in particular a Cdc4 polypeptide WD40 repeat domain, may be characterized by one or more of the following characteristics:

[0141] (a) a 7 or 8 blade β-propeller structure, in particular a 8 blade β-propeller structure;

[0142] (b) a disk like structure characterized by a cavity in the middle and two opposing circular surfaces of different size;

[0143] (c) a conical frustum of about 40 Å top surface and about 50 Å bottom surface, an overall thickness of 30 Å and a central pore of 6 Å diameter; and

[0144] (d) a CPD binding site on the top surface of the frustum of (c) and running across the edge of the pore, while the bottom surface of the frustum links to the F-box domain.

[0145] Each blade of the α-propeller structure can be further characterized by 4 anti-parallel α-strands. The disk like structure can also be characterized by a smaller surface comprising a CPD binding site and a bottom surface anchored by a helix (e.g. helix α6) of a helical extension of the F-box protein. As illustrated in FIGS. 2 and 3 the structure is further characterized by β-propeller blade 2 consisting of 5β-strands and a strand β9′ forming a parallel arrangement with strand β9.

[0146] A crystal of a binding pocket of an F-box protein of the invention, in particular a Cdc4 polypeptide, may be characterized by one or more of the following characteristics:

[0147] (i) a dedicated pThr-Pro binding pocket;

[0148] (ii) a deep hydrophobic pocket that selects hydrophobic residues N-terminal to the phosphorylation site of a CPD motif, and

[0149] (iii) a through space electrostatic selection against basic residues C-terminal to the phosphorylation site of a CPD motif.

[0150] In a preferred embodiment, a crystal of a WD40 repeat domain has the structure illustrated in FIG. 2 or 3.

[0151] A crystal of the invention can comprise a helical linker characterized by α helices that form a stalk and pedestal like structure that connects and orients a WD repeat domain. A helical linker structure of a Cdc4 polypeptide can also be characterized by one or more of the following structures: (a) a helix (e.g. α6 in FIG. 2 or FIG. 6) that is

[0152] 30 Å in length and is anchored at its N-terminus to the hydrophobic core of the F-box/helical extension and at its C-terminus to the hydrophobic core of a WD repeat domain,

[0153] (b) the helix of (a) (e.g. α6) anchored at its amino terminus to an F-box through hydrophobic interactions (e.g. involving α6 residues Phe 355, Leu356, and F box residues Ile295, Ile296, Leu315, and Trp316 or the corresponding residues in Cdc4 homologs, variants, precursors etc.));

[0154] (c) a second helix (e.g. helix 5) packed along the base of the helix of (a) or (b) opposite to the F-box domain through hydrophobic interactions (e.g. involving Tyr342, Leu338, and Leu 334) (or the corresponding residues in Cdc4 homologs, variants, precursors etc.);

[0155] (d) the helix of (a) (e.g. helix α6) anchored at its C-terminus through hydrophobic interactions;

[0156] (e) a C-terminal end of helix α6 inserted obliquely between propeller blades β7 and β8 of the WD40 domain through van der Wals and hydrophobic interactions (e.g. involving Trp365 and Ile361 with WD40 domain residues Val687, 11e696, Leu726, and Phe743 in β-propeller bnlades 7 and 8 (or the corresponding residues in Cdc4 homologs, variants, precursors etc.).

[0157] In a preferred embodiment, a crystal of a helical linker has the structure illustrated in FIG. 2.

[0158] A crystal of the invention may comprise a CPD motif binding pocket that is characterized by a hydrophobic pocket that surrounds the open central channel of a 7 or 8 blade WD repeat propeller. A crystal of a Cdc4 polypeptide may be more particularly characterized by one or more of the following:

[0159] (a) a WD repeat domain surface composed of invariant and highly conserved residues from β-propeller blades;

[0160] (b) a three-sided pocket formed by Trp426, Thr386, and Arg 485 (or the corresponding residues in Cdc4 homologs, variants, precursors etc.);

[0161] (c) a three-sided pocket formed by Trp426, Thr441, Thr 465, and Arg 485 (or the corresponding residues in Cdc4 homologs, variants, precursors etc.);

[0162] (d) a hydrophobic pocket composed of Trp 426, Trp 717, Thr 386, and Val 384(or the corresponding residues in Cdc4 homologs, variants, precursors etc.);

[0163] (e) a pocket formed by Leu634, MetS90, and Tyr574 (or the corresponding residues in Cdc4 homologs, variants, precursors etc.); and

[0164] (f) a pocket formed by Arg485, Arg467, Arg534, Tyr548, and Arg572 (or the corresponding residues in Cdc4 homologs, variants, precursors etc.).

[0165] In a preferred embodiment, a crystal of a CPD motif binding pocket has the structure illustrated in FIG. 3, 4, 6 or 7

[0166] In a further aspect of the invention a crystal is provided comprising an F-box domain comprising five a helices. In a preferred embodiment, a crystal of an F-box domain has the structure illustrated in FIG. 2 or FIG. 6.

[0167] A crystal of the invention may comprise an F-box protein characterized by one or more of the following:

[0168] (a) an F-box domain consisting of five a helices;

[0169] (b) a WD 40 repeat domain characterized by 7 or 8 copies of a WD40 repeat motif forming a 7 or 8 blade α-propeller structure; and

[0170] (c) two a helices that together with two a helices of the F-box domain forming a stalk and pedestal like structure that connects and orients the WD40 domain.

[0171] With reference to a crystal of the present invention, residues in a binding pocket may be defined by their spatial proximity to a substrate or ligand in the crystal structure. For example, a binding pocket may be defined by its proximity to a substrate molecule, or modulator.

[0172] A crystal of the invention includes a binding pocket in association with one or more moieties, including heavy-metal atoms i.e. a derivative crystal, or one or more substrates or ligands i.e. a co-crystal.

[0173] The term “associate”, “association” or “associating” refers to a condition of proximity between a moiety (i.e. chemical entity or compound or portions or fragments thereof), and a binding pocket. The association may be non-covalent i.e. where the juxtaposition is energetically favored by for example, hydrogen-bonding, van der Waals, or electrostatic or hydrophobic interactions, or it may be covalent.

[0174] The term “heavy-metal atoms” refers to an atom that can be used to solve an x-ray crystallography phase problem, including but not limited to a transition element, a lanthanide metal, or an actinide metal. Lanthanide metals include elements with atomic numbers between 57 and 71, inclusive. Actinide metals include elements with atomic numbers between 89 and 103, inclusive.

[0175] Multiwavelength anomalous diffraction (MAD) phasing may be used to solve protein structures using selenomethionyl (SeMet) proteins. Therefore, a complex of the invention may comprise a crystalline binding pocket with selenium on the methionine residues of the protein.

[0176] A crystal may comprise a complex between a binding pocket and one or more substrates or ligands. In other words the binding pocket may be associated with one or more ligands or molecules in the crystal. The ligand may be any compound that is capable of stably and specifically associating with the binding pocket. A ligand may, for example, be a modulator or analogue thereof. Therefore, a crystal may comprise a binding pocket comprising two or more of the amino acid residues of an F-box protein structure as described herein, that are capable of associating with or coordinating a CPD motif as described herein.

[0177] In an embodiment, a crystal of the invention comprises a complex between a binding pocket, and a substrate or analogue thereof. Therefore, the present invention also provides a crystal comprising a binding pocket of an F-box protein or a SCF complex and a substrate or analogue thereof. A substrate may be for example, a CPD motif or CPD motif containing protein. An analog of a substrate is one which mimics the substrate molecule, binding in the binding pocket, but which is incapable (or has a significantly reduced capacity) to take part in SCF E3 ubiquitin ligase activity.

[0178] In an embodiment, a crystal comprising a WD repeat domain of a Cdc4 polypeptide and a CPD motif is provided, which is characterized by one or more of the following:

[0179] (a) a WD 40 repeat domain characterized by 7 or 8 copies of a WD40 repeat motif forming a 7 or 8 blade β-propeller structure comprising β-propeller blades 1, 2, 3, 4, 5, 6, and 7, and optionally 8;

[0180] (b) the CPD motif binds in an extended manner across β-propeller blade 2 with the N-terminus oriented toward the central cavity of the WD repeat domain and the C-terminus oriented towards the outer rim;

[0181] (c) the CPD binding surface of the WD repeat domain is composed of invariant and highly conserved residues from β-propeller blades 1 to 6 and optionally 8;

[0182] (d) a P0 phosphate pThr of the CPD motif forms direct electrostatic interactions with the guanidium groups of Arg 485, Arg 467, and Arg 534 and a direct hydrogen bond with the side chain of Tyr 548 (or the corresponding residues in Cdc4 homologs, variants, precursors etc.);

[0183] (e) P+1 proline side chains of the CPD motif project into a three-sided pocket on the CPD binding surface formed by the side chain of Trp 426 and Arg485 or Trp 426, Thr441, Thr465, and Arg 485 (or the corresponding residues in Cdc4 homologs, variants, precursors etc.); and

[0184] (f) P+1 leucine side chain of the CPD motif is oriented towards a hydrophobic pocket composed of residues Trp 426, Trp 717, Thr 386, and Val 384 (or the corresponding residues in Cdc4 homologs, variants, precursors etc.).

[0185] In a preferred embodiment, a crystal of a complex of a WD repeat domain and a CPD motif has the structure illustrated in FIG. 2, 3, 4, 6, or 7.

[0186] A crystal or secondary or three-dimensional structure of a binding pocket of an F-box protein, may be specifically defined by one or more of the atomic contacts of the atomic interactions identified in Table 3 or Table 4. The atomic interactions in Table 3 or Table 4 are defined therein by an atomic contact (more preferably, a specific atom of an amino acid residue where indicated) on the F box protein, in particular on the WD40 repeat domain or helical linker, and an atomic contact (more preferably, a specific atom of an amino acid residue where indicated) on a substrate e.g. CPD motif, or an atomic contact (more preferably, a specific atom of an amino acid residue where indicated) on another region of the F-box protein (e.g. helical linker or F-box domain). In certain embodiments, a crystal of the invention comprises the atomic contacts of atomic interactions 1 to 8 identified in Table 3 or Table 4. In certain particular embodiments a crystal is provided comprising the atomic contacts of atomic interactions 1 to −4 or 5 to 8. Preferably, a crystal is defined by the atoms of the atomic contacts in the binding pocket having the structural coordinates for the atoms listed in Table 6.

[0187] A structure of a complex may be defined by selected intermolecular contacts, preferably the structural coordinates of the intermolecular contacts as defined in Table 6, preferably interactions 5 to 8.

[0188] A crystal of the invention may comprise one or more of the following groups of amino acid residues: (a) Ile 295, Ile 296, Leu 315, Trp 316, Leu 319, Phe 355, and Leu 356; (b) Val 687, Ile 696, Leu 726, Phe 743, Trp 365, and Ile 364; (c) Asn 684, Arg 700, and Glu 323; (d) Arg 485, Arg 467, Arg 534, Tyr 548; (e) Trp 426, Arg 485, Thr 441, and Thr 465; (f) Trp 426, Trp 717, Thr 386, and Val 384; (g) Tyr 574, Thr 386 and Val 384; (h) Tyr 574, Met 590, and Leo 634; and (i) the corresponding residues in Cdc4 homologs, paralogs, variants, or precursors. Preferably the atoms of the amino acid residues have the structural coordinates as set out in Table 6.

[0189] A crystal of the invention may enable the determination of structural data for a substrate or ligand. In order to be able to derive structural data for a ligand, or substrate it is necessary for the molecule to have sufficiently strong electron density to enable a model of the molecule to be built using standard techniques. For example, there should be sufficient electron density to allow a model to be built using XTALVIEW (McRee 1992 J. Mol. Graphics. 10 44-46).

[0190] A crystal of the invention may belong to space group P32. The term “space group” refers to the lattice and symmetry of the crystal. In a space group designation the capital letter indicates the lattice type and the other symbols represent symmetry operations that can be carried out on the contents of the asymmetric unit without changing its appearance.

[0191] A crystal of the invention may comprise a unit cell having the following unit dimensions: α=107.7 Å, b=107.7 Å, c=168.3 Å, α=γ=90°, p=120°. The term “unit cell” refers to the smallest and simplest volume element (i.e. parallelpiped-shaped block) of a crystal that is completely representative of the unit of pattern of the crystal. The unit cell axial lengths are represented by a, b, and c. Those of skill in the art understand that a set of atomic coordinates determined by X-ray crystallography is not without standard error.

[0192] In a preferred embodiment, a crystal of the invention has the structural coordinates as shown in Table 6. As used herein, the term “structural coordinates” refers to a set of values that define the position of one or more amino acid residues with reference to a system of axes. The term refers to a data set that defines the three dimensional structure of a molecule or molecules (e.g. Cartesian coordinates, temperature factors, and occupancies). Structural coordinates can be slightly modified and still render nearly identical three dimensional structures. A measure of a unique set of structural coordinates is the root-mean-square deviation of the resulting structure. Structural coordinates that render three dimensional structures (in particular a three dimensional structure of a ligand binding pocket) that deviate from one another by a root-mean-square deviation of less than 5 Å, 4 Å, 3 Å, 2 Å, 1.5 Å, 1.0 Å, or 0.5 Å may be viewed by a person of ordinary skill in the art as very similar.

[0193] Variations in structural coordinates may be generated because of mathematical manipulations of the structural coordinates of a structure or binding pocket described herein. For example, the structural coordinates of Table 6 may be manipulated by crystallographic permutations of the structural coordinates, fractionalization of the structural coordinates, integer additions or substractions to sets of the structural coordinates, inversion of the structural coordinates or any combination of the above.

[0194] Variations in the crystal structure due to mutations, additions, substitutions, and/or deletions of the amino acids, or other changes in any of the components that make up the crystal may also account for modifications in structural coordinates. If such modifications are within an acceptable standard error as compared to the original structural coordinates, the resulting structure may be the same. Therefore, a ligand that bound to a binding pocket of an F-box protein, would also be expected to bind to another binding pocket whose structural coordinates defined a shape that fell within the acceptable error. Such modified structures of a binding pocket thereof are also within the scope of the invention.

[0195] Various computational analyses may be used to determine whether a molecule or the binding pocket thereof is sufficiently similar to all or parts of an F-box or a binding pocket thereof. Such analyses may be carried out using conventional software applications and methods as described herein.

[0196] A crystal of the invention may also be specifically characterised by the parameters, diffraction statistics and/or refinement statistics set out in Table 1 or in Table 2.

[0197] Illustrations of particular crystals of the invention are shown in FIGS. 2, 3, 4, 6 and 7.

[0198] Method of Making a Crystal

[0199] The present invention also provides a method of making a crystal according to the invention. The crystal may be formed from an aqueous solution comprising a purified polypeptide comprising an F-box protein including a variant, part, homolog, or fragment thereof (e.g. a binding pocket). A method may utilize a purified polypeptide comprising a binding pocket to form a crystal. A method may utilize one or more purified mutant polypeptides as described herein. In an embodiment, a mutant cdc4 polypeptide is used to make crystals.

[0200] The term “purified” in reference to a polypeptide, does not require absolute purity such as a homogenous preparation rather it represents an indication that the polypeptide is relatively purer than in the natural environment. Generally, a purified polypeptide is substantially free of other proteins, lipids, carbohydrates, or other materials with which it is naturally associated, preferably at a functionally significant level for example at least 85% pure, more preferably at least 95% pure, most preferably at least 99% pure. A skilled artisan can purify a polypeptide comprising using standard techniques for protein purification. A substantially pure polypeptide will yield a single major band on a non-reducing polyacrylamide gel. Purity of the polypeptide can also be determined by amino-terminal amino acid sequence analysis.

[0201] A polypeptide used in the method may be chemically synthesized in whole or in part using techniques that are well-known in the art. Alternatively, methods are well known to the skilled artisan to construct expression vectors containing a native or mutated protein coding sequence and appropriate transcriptional/translational control signals. These methods include in vitro recombinant DNA techniques, synthetic techniques, and in vivo recombination/genetic recombination. See for example the techniques described in Sambrook et al. (Molecular Cloning: A Laboratory Manual, 2nd Edition, Cold Spring Harbor Laboratory press (1989)), and other laboratory textbooks. (See also Sarker et al, Glycoconjugate J. 7:380, 1990; Sarker et al, Proc. Natl. Acad, Sci. USA 88:234-238, 1991, Sarker et al, Glycoconjugate J. 11: 204-209, 1994; Hull et al, Biochem Biophys Res Commun 176:608, 1991 and Pownall et al, Genomics 12:699-704, 1992).

[0202] Crystals may be grown from an aqueous solution containing the purified polypeptide by a variety of conventional processes. These processes include batch, liquid, bridge, dialysis, vapor diffusion, and hanging drop methods. (See for example, McPherson, 1982 John Wiley, New York; McPherson, 1990, Eur. J. Biochem. 189: 1-23; Webber. 1991, Adv. Protein Chem. 41:1-36). Generally, native crystals of the invention are grown by adding precipitants to the concentrated solution of the polypeptide. The precipitants are added at a concentration just below that necessary to precipitate the protein. Water is removed by controlled evaporation to produce precipitating conditions, which are maintained until crystal growth ceases.

[0203] Derivative crystals of the invention can be obtained by soaking native crystals in a solution containing salts of heavy metal atoms. A complex of the invention can be obtained by soaking a native crystal in a solution containing a compound that binds the polypeptide, or they can be obtained by co-crystallizing the polypeptide in the presence of one or more compounds. In order to obtain co-crystals with a compound which binds deep within the tertiary structure of the polypeptide it is necessary to use the second method.

[0204] Once the crystal is grown it can be placed in a glass capillary tube and mounted onto a holding device connected to an X-ray generator and an X-ray detection device. Collection of X-ray diffraction patterns are well documented by those skilled in the art (See for example, Ducruix and Geige, 1992, IRL Press, Oxford, England). A beam of X-rays enter the crystal and diffract from the crystal. An X-ray detection device can be utilized to record the diffraction patterns emanating from the crystal. Suitable devices include the Marr 345 imaging plate detector system with an RU200 rotating anode generator.

[0205] Multiwavelength anomalous diffraction (MAD) phasing using selenomethionyl (SeMet) proteins may be used to determine a crystal of the invention. Thus, the invention contemplates a method for determining a crystal structure of the invention using a selenomethionyl derivative of an F-box protein or SCF complex, including a variant, part, homolog or fragement thereof.

[0206] Methods for obtaining the three dimensional structure of the crystalline form of a molecule or complex are described herein and known to those skilled in the art (see Ducruix and Geige 1992, IRL Press, Oxford, England). Generally, the x-ray crystal structure is given by the diffraction patterns. Each diffraction pattern reflection is characterized as a vector and the data collected at this stage determines the amplitude of each vector. The phases of the vectors may be determined by the isomorphous replacement method where heavy atoms soaked into the crystal are used as reference points in the X-ray analysis (see for example, Otwinowski, 1991, Daresbury, United Kingdom, 80-86). The phases of the vectors may also be determined by molecular replacement (see for example, Naraza, 1994, Proteins 11:281-296). The amplitudes and phases of vectors from the crystalline form determined in accordance with these methods can be used to analyze other related crystalline polypeptides.

[0207] The unit cell dimensions and symmetry, and vector amplitude and phase information can be used in a Fourier transform function to calculate the electron density in the unit cell i.e. to generate an experimental electron density map. This may be accomplished using the PHASES package (Furey, 1990). Amino acid sequence structures are fit to the experimental electron density map (i.e. model building) using computer programs (e.g. Jones, TA. et al, Acta Crystallogr A47, 100-119, 1991). This structure can also be used to calculate a theoretical electron density map. The theoretical and experimental electron density maps can be compared and the agreement between the maps can be described by a parameter referred to as R-factor. A high degree of overlap in the maps is represented by a low value R-factor. The R-factor can be minimized by using computer programs that refine the structure to achieve agreement between the theoretical and observed electron density map. For example, the XPLOR program, developed by Brunger (1992, Nature 355:472-475) can be used for model refinement.

[0208] A three dimensional structure of the molecule or complex may be described by atoms that fit the theoretical electron density characterized by a minimum R value. Files can be created for the structure that defines each atom by coordinates in three dimensions.

[0209] Mutant CDC4 Polypeptides

[0210] The present invention provides novel mutant cdc4 polypeptides.

[0211] A particular mutant of the present invention is a polypeptide having an amino acid sequence of a cdc4 polypeptide wherein amino acid residues are replaced or deleted providing a cdc4 polypeptide that can be produced by recombinant techniques and retains its activity, for example its ability to associate with a CPD motif.

[0212] In an aspect a cdc4 sequence is mutated by deleting the region from the beginning of the F-box domain to the end of the WD40 repeat domain. In particular, terminal residues 1 to 262 and 745 to 779 can be deleted from the cdc4 seqeunce.

[0213] Other additions, substitutions, and/or deletions may be made to the cdc4 mutants of the present invention. In an embodiment cdc4 can be engineered to remove flexible loops comprising residues 601 to 604 and 609 to 624.

[0214] Particular mutant cdc4 polypeptides of the invention are also identified in Table 5.

[0215] The present invention also relates to nucleic acid molecules or polynucleotides encoding a cdc4 mutant polypeptide. The polynucleotides can be used to transform host cells to express the cdc4 mutant polypeptides of the invention. They can also be used as a probe to detect related enzymes.

[0216] The present invention still further relates to recombinant vectors that include the nucleic acid molecules of the invention. The nucleic acid molecules of the invention may be inserted into an appropriate vector, and the vector may contain the necessary elements for the transcription and translation of an inserted coding sequence. Accordingly, vectors may be constructed which comprise a nucleic acid molecule of the invention, and where appropriate one or more transcription and translation elements linked to the nucleic acid molecule. A vector can be used to transform host cells. Therefore, the invention provides host cells containing a vector of the invention. As well, the invention provides methods of making such vectors and host cells.

[0217] The mutant cdc4 polypeptides of the invention can be encoded, expressed, and purified by any one of a number of methods known to those skilled in the art. Preferred production methods will depend on many factors including the costs and availability of materials and other economic considerations. The optimum production procedure for a given situation will be apparent to those skilled in the art through minimal experimentation.

[0218] In accordance with an aspect of the present invention, there is provided a process for producing a cdc4 mutant polypeptide by recombinant techniques utilizing the nucleic acid molecules of the invention. The method may comprise culturing recombinant host cells containing a nucleic acid sequence encoding a cdc4 mutant polypeptide, under conditions promoting expression of the cdc4 mutant polypeptide, and subsequent recovery of the cdc4 mutant polypeptide.

[0219] The invention further broadly contemplates a recombinant cdc4 mutant polypeptide obtained using a method of the invention.

[0220] A cdc4 mutant polypeptide of the invention may be conjugated with other molecules, such as polypeptides, to prepare fusion polypeptides or chimeric polypeptides. This may be accomplished, for example, by the synthesis of N-terminal or C-terminal fusion polypeptides.

[0221] The invention further contemplates antibodies having specificity against a cdc4 mutant polypeptide of the invention. Antibodies may be labeled with a detectable substance and used to detect cdc4 mutant polypeptides. In another embodiment, the invention provides an isolated antibody that binds specifically to a cdc4 mutant polypeptide.

[0222] The cdc4 mutant polypeptides of the present invention are particularly well suited for use in screening methods for identifying modulators of cdc4 or SCF complexes.

[0223] Still further the invention provides a method for evaluating a test compound for its ability to modulate the biological activity of a cdc4 polypepide. In this application, “modulate” refers to a change or an alteration in the biological activity of a cdc4 polypeptide. Modulation may be an increase or a decrease in activity, a change in characteristics (e.g. kinetic characteristics), or any other change in the biological, functional, or immunological properties of the polypeptide.

[0224] The substances and compounds identified using the methods of the invention, may be used to modulate the biological activity of a cdc4 polypeptide or a SCF complex, and they may be used in the treatment of conditions mediated by a cdc4 polypeptide or SCF complex. Accordingly, the substances and compounds may be formulated into compositions for administration to individuals suffering from one or more of these conditions. Therefore, the present invention also relates to a composition comprising one or more of a substance or compound identified using a method of the invention, and a pharmaceutically acceptable carrier, excipient or diluent. A method for treating or preventing these conditions is also provided comprising administering to a patient in need thereof, a composition of the invention.

[0225] Model

[0226] A crystal structure of the present invention may be used to make a model of a binding pocket of a SCF E3 ubiquitin ligase, in particular an F-box protein, that is involved in substrate selection and/or orientation. A model may, for example, be a structural model or a computer model. A model may represent the secondary, tertiary and/or quaternary structure of the binding pocket. The model itself may be in two or three dimensions. It is possible for a computer model to be in three dimensions despite the constraints imposed by a conventional computer screen, if it is possible to scroll along at least a pair of axes, causing “rotation” of the image.

[0227] As used herein, the term “modelling” includes the quantitative and qualitative analysis of molecular structure and/or function based on atomic structural information and interaction models. The term “modelling” includes conventional numeric-based molecular dynamic and energy minimization models, interactive computer graphic models, modified molecular mechanics models, distance geometry and other structure-based constraint models.

[0228] Preferably, modelling is performed using a computer and may be further optimized using known methods. This is called modelling optimisation.

[0229] An integral step to an approach of the invention for designing modulators (e.g. inhibitors) of a subject F-box protein or SCF complex involves construction of computer graphics models of a binding pocket of the invention which can be used to design pharmacophores by rational drug design. For instance, for an inhibitor to interact optimally with the subject binding pocket, it will generally be desirable that it have a shape which is at least partly complimentary to that of a particular binding pocket of the protein, as for example those binding pockets of the protein which are involved in recognition of a ligand (e.g. substrate). Additionally, other factors, including electrostatic interactions, hydrogen bonding, hydrophobic interactions, desolvation effects, and cooperative motions of ligand and receptor, all influence the binding effect and should be taken into account in attempts to design bioactive modulators (e.g. inhibitors).

[0230] As described herein, a computer-generated molecular model of the subject binding pockets can be created. In preferred embodiments, at least the Cα-carbon positions of the binding pockets are mapped to a particular coordinate pattern, such as the coordinates for a binding pocket in Table 6, by homology modeling, and the structure of the protein and velocities of each atom are calculated at a simulation temperature (To) at which the docking simulation is to be determined. Typically, such a protocol involves primarily the prediction of side-chain conformations in the modeled binding pocket, while assuming a main-chain trace taken from a tertiary structure such as provided in Table 6 and the Figures. Computer programs for performing energy minimization routines are commonly used to generate molecular models. For example, both the CHARMM (Brooks et al. (1983) J Comput Chem 4:187-217) and AMBER (Weiner et al (1981) J. Comput. Chem. 106: 765) algorithms handle all of the molecular system setup, force field calculation, and analysis (see also, Eisenfield et al. (1991) Am J Physiol 261:C376-386; Lybrand (1991) J Pharm Belg 46:49-54; Froimowitz (1990) Biotechniques 8:640-644; Burbam et al. (1990) Proteins 7:99-111; Pedersen (1985) Environ Health Perspect 61:185-190; and Kini et al. (1991) J Biomol Struct Dyn 9:475-488). At the heart of these programs is a set of subroutines that, given the position of every atom in the model, calculate the total potential energy of the system and the force on each atom. These programs may utilize a starting set of atomic coordinates, such as the coordinates provided in Table 6, the parameters for the various terms of the potential energy function, and a description of the molecular topology (the covalent structure). Common features of such molecular modeling methods include: provisions for handling hydrogen bonds and other constraint forces; the use of periodic boundary conditions; and provisions for occasionally adjusting positions, velocities, or other parameters in order to maintain or change temperature, pressure, volume, forces of constraint, or other externally controlled conditions.

[0231] Most conventional energy minimization methods use the input data described above and the fact that the potential energy function is an explicit, differentiable function of Cartesian coordinates, to calculate the potential energy and its gradient (which gives the force on each atom) for any set of atomic positions. This information can be used to generate a new set of coordinates in an effort to reduce the total potential energy and, by repeating this process over and over, to optimize the molecular structure under a given set of external conditions. These energy minimization methods are routinely applied to molecules similar to the subject proteins as well as nucleic acids, polymers and zeolites.

[0232] In general, energy minimization methods can be carried out for a given temperature, Tis, which may be different than the docking simulation temperature, To. Upon energy minimization of the molecule at Ti, coordinates and velocities of all the atoms in the system are computed. Additionally, the normal modes of the system are calculated. It will be appreciated by those skilled in the art that each normal mode is a collective, periodic motion, with all parts of the system moving in phase with each other, and that the motion of the molecule is the superposition of all normal modes. For a given temperature, the mean square amplitude of motion in a particular mode is inversely proportional to the effective force constant for that mode, so that the motion of the molecule will often be dominated by the low frequency vibrations.

[0233] After the molecular model has been energy minimized at Ti, the system is “heated” or “cooled” to the simulation temperature, Ti, by carrying out an equilibration run where the velocities of the atoms are scaled in a step-wise manner until the desired temperature, To, is reached. The system is further equilibrated for a specified period of time until certain properties of the system, such as average kinetic energy, remain constant. The coordinates and velocities of each atom are then obtained from the equilibrated system.

[0234] Further energy minimization routines can also be carried out. For example, a second class of methods involves calculating approximate solutions to the constrained EOM for the protein. These methods use an iterative approach to solve for the Lagrange multipliers and, typically, only need a few iterations if the corrections required are small. The most popular method of this type, SHAKE (Ryckaert et al. (1977) J Comput Phys 23:327; and Van Gunsteren et al. (1977) Mol Phys 34:13 11) is easy to implement and scales as O(N) as the number of constraints increases. Therefore, the method is applicable to macromolecules such as F-box proteins. An alternative method, RATTLE (Anderson (1983) J Comput Phys 52:24) is based on the velocity version of the Verlet algorithm. Like SHAKE, RATTLE is an iterative algorithm and can be used to energy minimize the model of the subject protein.

[0235] Overlays and super positioning with a three dimensional model of a binding pocket of the invention may be used for modelling optimisation. Additionally alignment and/or modelling can be used as a guide for the placement of mutations on a binding pocket to characterize the nature of the site in the context of a cell.

[0236] The three dimensional structure of a new crystal may be modelled using molecular replacement. The term “molecular replacement” refers to a method that involves generating a preliminary model of a molecule or complex whose structural coordinates are unknown, by orienting and positioning a molecule whose structural coordinates are known within the unit cell of the unknown crystal, so as best to account for the observed diffraction pattern of the unknown crystal. Phases can then be calculated from this model and combined with the observed amplitudes to give an approximate Fourier synthesis of the structure whose coordinates are unknown. This, in turn, can be subject to any of the several forms of refinement to provide a final, accurate structure of the unknown crystal. Lattman, E., “Use of the Rotation and Translation Functions”, in Methods in Enzymology, 115, pp. 55-77 (1985); M. G. Rossmann, ed., “The Molecular Replacement Method”, Int. Sci. Rev. Ser., No. 13, Gordon & Breach, New York, (1972).

[0237] Commonly used computer software packages for molecular replacement are X-PLOR (Brunger 1992, Nature 355: 472-475), AMoRE (Navaza, 1994, Acta Crystallogr. A50:157-163), the CCP4 package (Collaborative Computational Project, Number 4, “The CCP4 Suite: Programs for Protein Crystallography”, Acta Cryst., Vol. D50, pp. 760-763, 1994), the MERLOT package (P. M. D. Fitzgerald, J. Appl. Cryst., Vol. 21, pp. 273-278, 1988) and XTALVIEW (McCree et al (1992) J. Mol. Graphics 10: 44-46. It is preferable that the resulting structure not exhibit a root-mean-square deviation of more than 3 Å.

[0238] Molecular replacement computer programs generally involve the following steps: (1) determining the number of molecules in the unit cell and defining the angles between them (self rotation function); (2) rotating the known structure against diffraction data to define the orientation of the molecules in the unit cell (rotation function); (3) translating the known structure in three dimensions to correctly position the molecules in the unit cell (translation function); (4) determining the phases of the X-ray diffraction data and calculating an R-factor calculated from the reference data set and from the new data wherein an R-factor between 30-50% indicates that the orientations of the atoms in the unit cell have been reasonably determined by the method; and (5) optionally, decreasing the R-factor to about 20% by refining the new electron density map using iterative refinement techniques known to those skilled in the art (refinement).

[0239] The quality of the model may be analysed using a program such as PROCHECK or 3D-Profiler [Laskowski et al 1993 J. Appl. Cryst. 26:283-291; Luthy R. et al, Nature 356: 83-85, 1992; and Bowie, J. U. et al, Science 253: 164-170, 1991]. Once any irregularities have been resolved, the entire structure may be further refined.

[0240] Other molecular modelling techniques may also be employed in accordance with this invention. See, e.g., Cohen, N. C. et al, “Molecular Modelling Software and Methods for Medicinal Chemistry”, J. Med. Chem., 33, pp. 883-894 (1990). See also, Navia, M. A. and M. A. Murcko, “The Use of Structural Information in Drug Design”, Current Opinions in Structural Biology, 2, pp. 202-210 (1992).

[0241] Using the structural coordinates of crystal provided by the invention, molecular modelling may be used to determine the structural coordinates of a crystalline mutant or homolog of a SCF complex or F-box binding pocket involved in substrate selection and/or orientation. By the same token a crystal of the invention can be used to provide a model of a substrate or ligand. Modelling techniques can then be used to approximate the three dimensional structure of substrate or ligand derivatives and other components which may be able to mimic the atomic contacts between a substrate or ligand and binding pocket.

[0242] Computer Format of Crystals/Models

[0243] Information derivable from a crystal of the present invention (for example the structural coordinates) and/or the model of the present invention may be provided in a computer-readable format.

[0244] Therefore, the invention provides a computer readable medium or a machine readable storage medium which comprises the structural coordinates of a binding pocket of an SCF complex of F box protein described herein including all or any parts thereof, or substrates or ligands including portions thereof. Such storage medium or storage medium encoded with these data are capable of displaying on a computer screen or similar viewing device, a three-dimensional graphical representation of a molecule or molecular complex which comprises such binding pockets or similarly shaped homologous binding pockets. Thus, the invention also provides computerized representations of the secondary or three-dimensional structures of a binding pocket of the invention, including any electronic, magnetic, or electromagnetic storage forms of the data needed to define the structures such that the data will be computer readable for purposes of display and/or manipulation.

[0245] In an aspect the invention provides a computer for producing a three-dimensional representation of a molecule or molecular complex, wherein said molecule or molecular complex comprises a binding pocket defined by structural coordinates of a binding pocket or structural coordinates of atoms of a substrate or ligand, or a three-dimensional representation of a homolog of said molecule or molecular complex, wherein said homolog comprises a binding pocket, or substrate or ligand that has a root mean square deviation from the backbone atoms not more than 1.5 angstroms wherein said computer comprises:

[0246] (a) a machine-readable data storage medium comprising a data storage material encoded with machine readable data wherein said data comprises the structural coordinates of a binding pocket or a substrate according to Table 6;

[0247] (b) a working memory for storing instructions for processing said machine-readable data;

[0248] (c) a central-processing unit coupled to said working memory and to said machine-readable data storage medium for processing said machine readable data into said three-dimensional representation; and

[0249] (d) a display coupled to said central-processing unit for displaying said three-dimensional representation.

[0250] The invention also provides a computer for determining at least a portion of the structural coordinates corresponding to an X-ray diffraction pattern of a molecule or molecular complex wherein said computer comprises:

[0251] (a) a machine-readable data storage medium comprising a data storage material encoded with machine readable data wherein said data comprises the structural coordinates according to Table 6;

[0252] (b) a machine-readable data storage medium comprising a data storage material encoded with machine readable data wherein said data comprises an X-ray diffraction pattern of said molecule or molecular complex;

[0253] (c) a working memory for storing instructions for processing said machine-readable data of (a) and (b);

[0254] (d) a central-processing unit coupled to said working memory and to said machine-readable data storage medium of (a) and (b) for performing a Fourier transform of the machine readable data of (a) and for processing said machine readable data of (b) into structural coordinates; and

[0255] (e) a display coupled to said central-processing unit for displaying said structural coordinates of said molecule or molecular complex.

[0256] Structural Studies

[0257] The present invention also provides a method for determining the secondary and/or tertiary structures of a pol)peptide or part or complexes thereof by using a crystal, or a model according to the present invention. The polypeptide or part thereof may be any polypeptide or part thereof for which the secondary and or tertiary structure is uncharacterised or incompletely characterised. In a preferred embodiment the polypeptide shares (or is predicted to share) some structural or functional homology to a crystal of the present invention. For example, the polypeptide may show a degree of structural homology over some or all parts of the primary amino acid sequence.

[0258] The polypeptide may be an F-box protein, or part thereof with a different specificity for a substrate. Alternatively (or in addition) the polypeptide may be an F-box protein from a different species.

[0259] The polypeptide may be a mutant of a wild-type F-box protein. A mutant may arise naturally, or may be made artificially (for example using molecular biology techniques). The mutant may also not be “made” at all in the conventional sense, but merely tested theoretically using the model of the present invention. A mutant may or may not be functional.

[0260] Thus, using a model of the present invention, the effect of a particular mutation on the overall two and/or three dimensional structure of an F-box protein or SCF complex or the interaction between a binding pocket of an F-box protein or SCF complex and a substrate or ligand can be investigated.

[0261] Alternatively, the polypeptide may perform an analogous function or be suspected to show a similar mechanism to an F-box protein.

[0262] The polypeptide may also be the same as the polypeptide of the crystal, but in association with a different substrate or ligand (for example, modulator or inhibitor) or cofactor. In this way it is possible to investigate the effect of altering the substrate or ligand with which the polypeptide is associated on the structure of the binding pocket.

[0263] Secondary or tertiary structure may be determined by applying the structural coordinates of a crystal or model of the present invention to other data such as an amino acid sequence, X-ray crystallographic diffraction data, or nuclear magnetic resonance (NMR) data. Homology modeling, molecular replacement, and nuclear magnetic resonance methods using these other data sets are described below.

[0264] Homology modeling (also known as comparative modeling or knowledge-based modeling) methods develop a three dimensional model from a polypeptide sequence based on the structures of known proteins (i.e. an F-box structure or complex thereof described herein). The method utilizes a computer model of a crystal of the present invention (the “known structure”), a computer representation of the amino acid sequence of the polypeptide with an unknown structure, and standard computer representations of the structures of amino acids. The method in particular comprises the steps of; (a) identifying structurally conserved and variable regions in the known structure; (b) aligning the amino acid sequences of the known structure and unknown structure (c) generating co-ordinates of main chain atoms and side chain atoms in structurally conserved and variable regions of the unknown structure based on the coordinates of the known structure thereby obtaining a homology model; and (d) refining the homology model to obtain a three dimensional structure for the unknown structure. This method is well known to those skilled in the art (Greer, 1985, Science 228, 1055; Bundell et al 1988, Eur. J. Biochem. 172, 513; Knighton et al., 1992, Science 258:130-135, http://biochem.vt.edu/courses/modeling/homology.htn). Computer programs that can be used in homology modelling are Quanta and the Homology module in the Insight II modelling package distributed by Molecular Simulations Inc, or MODELLER (Rockefeller University, www.iucr.ac.uk/sinris-top/logical/prg-modeller.html).

[0265] In step (a) of the homology modelling method, a known structure is examined to identify the structurally conserved regions (SCRs) from which an average structure, or framework, can be constructed for these regions of the protein. Variable regions (VRs), in which known structures may differ in conformation, also must be identified. SCRs generally correspond to the elements of secondary structure, such as alpha-helices and beta-sheets, and to ligand- and substrate-binding sites. The VRs usually lie on the surface of the proteins and form the loops where the main chain turns.

[0266] Many methods are available for sequence alignment of known structures and unknown structures. Sequence alignments generally are based on the dynamic programming algorithm of Needleman and Wunsch [J. Mol. Biol. 48: 442-453, 1970]. Current methods include FASTA, Smith-Waterman, and BLASTP, with the BLASTP method differing from the other two in not allowing gaps. Scoring of alignments typically involves construction of a 20×20 matrix in which identical amino acids and those of similar character (i.e., conservative substitutions) may be scored higher than those of different character. Substitution schemes which may be used to score alignments include the scoring matrices PAM (Dayhoff et al., Meth. Enzymol. 91: 524-545, 1983), and BLOSUM (Henikoff and Henikoff, Proc. Nat. Acad. Sci. USA 89: 10915-0919, 1992), and the matrices based on alignments derived from three-dimensional structures including that of Johnson and Overington (JO matrices) (J. Mol. Biol. 233: 716-738, 1993).

[0267] Alignment based solely on sequence may be used; however, other structural features also may be taken into account. In Quanta, multiple sequence alignment algorithms are available that may be used when aligning a sequence of the unknown with the known structures. Four scoring systems (i.e. sequence homology, secondary structure homology, residue accessibility homology, CA-CA distance homology) are available, each of which may be evaluated during an alignment so that relative statistical weights may be assigned.

[0268] When generating coordinates for the unknown structure, main chain atoms and side chain atoms, both in SCRs and VRs need to be modelled. A variety of approaches known to those skilled in the art may be used to assign co-ordinates to the unknown. In particular, the co-ordinates of the main chain atoms of SCRs will be transferred to the unknown structure. VRs correspond most often to the loops on the surface of the polypeptide and if a loop in the known structure is a good model for the unknown, then the main chain co-ordinates of the known structure may be copied. Side chain coordinates of SCRs and VRs are copied if the residue type in the unknown is identical to or very similar to that in the known structure. For other side chain coordinates, a side chain rotamer library may be used to define the side chain coordinates. When a good model for a loop cannot be found fragment databases may be searched for loops in other proteins that may provide a suitable model for the unknown. If desired, the loop may then be subjected to conformational searching to identify low energy conformers if desired.

[0269] Once a homology model has been generated it is analyzed to determine its correctness. A computer program available to assist in this analysis is the Protein Health module in Quanta which provides a variety of tests. Other programs that provide structure analysis along with output include PROCHECK and 3D-Profiler [Luthy R. et al, Nature 356: 83-85, 1992; and Bowie, J. U. et al, Science 253: 164-170, 1991]. Once any irregularities have been resolved, the entire structure may be further refined. Refinement may consist of energy minimization with restraints, especially for the SCRs. Restraints may be gradually removed for subsequent minimizations. Molecular dynamics may also be applied in conjunction with energy minimization.

[0270] Molecular replacement involves applying a known structure to solve the X-ray crystallographic data set of a polypeptide of unknown structure. The method can be used to define the phases describing the X-ray diffraction data of a polypeptide of unknown structure when only the amplitudes are known. Thus in an embodiment of the invention, a method is provided for determining three dimensional structures of polypeptides with unknown structure by applying the structural coordinates of a crystal of the present invention to provide an X-ray crystallographic data set for a polypeptide of unknown structure, and (b) determining a low energy conformation of the resulting structure.

[0271] The structural coordinates of a crystal of the present invention may be applied to nuclear magnetic resonance (NMR) data to determine the three dimensional structures of polypeptides with uncharacterised or incompletely characterised sturcture. (See for example, Wuthrich, 1986, John Wiley and Sons, New York: 176-199; Pflugrath et al., 1986, J. Molecular Biology 189: 383-386; Kline et al., 1986 J. Molecular Biology 189:377-382). While the secondary structure of a polypeptide may often be determined by NMR data, the spatial connections between individual pieces of secondary structure are not as readily determined. The structural coordinates of a polypeptide defined by X-ray crystallography can guide the NMR spectroscopist to an understanding of the spatial interactions between secondary structural elements in a polypeptide of related structure. Information on spatial interactions between secondary structural elements can greatly simplify Nuclear Overhauser Effect (NOE) data from two-dimensional NMR experiments. In addition, applying the structural coordinates after the determination of secondary structure by NMR techniques simplifies the assignment of NOE's relating to particular amino acids in the polypeptide sequence and does not greatly bias the NMR analysis of polypeptide structure.

[0272] In an embodiment, the invention relates to a method of determining three dimensional structures of polypeptides with unknown structures, by applying the structural coordinates of a crystal of the present invention to nuclear magnetic resonance (NMR) data of the unknown structure. This method comprises the steps of: (a) determining the secondary structure of an unknown structure using NMR data; and (b) simplifying the assignment of through-space interactions of amino acids. The term “through-space interactions” defines the orientation of the secondary structural elements in the three dimensional structure and the distances between amino acids from different portions of the amino acid sequence. The term “assignment” defines a method of analyzing NMR data and identifying which amino acids give rise to signals in the NMR spectrum.

[0273] Screening Methods

[0274] Another aspect of the present invention is the design and identification of agents that inhibit or potentiate an interaction between an F-box protein or an SCF E3 ubiquitin ligase and a substrate. The rationale design and identification of agents can be accomplished by utilizing the structural coordinates that define a binding pocket of the present invention involved in substrate selection and/or orientation.

[0275] The structures described herein, and the structures of other polypeptides determined by homology modeling, molecular replacement, and NMR techniques described herein can also be applied to modulator design and identification methods.

[0276] The invention contemplates molecular models, in particular three-dimensional molecular models of binding pockets of the present invention involved in substrate selection and/or orientation, and their use as templates for the design of agents able to mimic or inhibit substrate binding (e.g. modulators).

[0277] In certain embodiments, the present invention provides a method of screening for a ligand that associates with a binding pocket and/or modulates the function of a F-box protein or SCF complex by using a crystal or a model according to the present invention. The method may involve investigating whether a test compound is capable of associating with or binding a binding pocket, and/or inhibiting or enhancing interactions of atomic contacts in a binding pocket.

[0278] In accordance with an aspect of the present invention, a method is provided for screening for a ligand capable of binding to a binding pocket, wherein the method comprises using a crystal or model according to the invention.

[0279] In another aspect, the invention relates to a method of screening for a ligand capable of binding to a binding pocket, wherein the binding pocket is defined by the structural coordinates given herein, the method comprising contacting the binding pocket with a test compound and determining if the test compound binds to the binding pocket.

[0280] In one embodiment, the present invention provides a method of screening for a test compound capable of interacting with one or more key amino acid residues of a binding pocket of the present invention. For example, a test compound that interacts with one or more of amino acids of a binding pocket may prevent interaction of the F-box protein or complex thereof and its substrate resulting in modification of the SCF E3 ubiquitin ligase activity.

[0281] Another aspect of the invention provides a process comprising the steps of:

[0282] (a) performing a method of screening for a ligand described above;

[0283] (b) identifying one or more ligands capable of binding to a binding pocket; and

[0284] (c) preparing a quantity of said one or more ligands.

[0285] A further aspect of the invention provides a process comprising the steps of;

[0286] (a) performing a method of screening for a ligand as described above;

[0287] (b) identifying one or more ligands capable of binding to a binding pocket; and

[0288] (c) preparing a pharmaceutical composition comprising said one or more ligands.

[0289] Once a test compound capable of interacting with one or more key amino acid residues in a binding pocket of the present invention has been identified, further steps may be carried out either to select and/or modify compounds and/or to modify existing compounds, to modulate the interaction with the key amino acid residues in the binding pocket.

[0290] Yet another aspect of the invention provides a process comprising the steps of;

[0291] (a) performing the method of screening for a ligand as described above;

[0292] (b) identifying one or more ligands capable of binding to a binding pocket;

[0293] (c) modifying said one or more ligands capable of binding to a binding pocket;

[0294] (d) performing said method of screening for a ligand as described above; and

[0295] (e) optionally preparing a pharmaceutical composition comprising said one or more ligands.

[0296] In another aspect of the invention, a method of screening for a test compound is provided comprising screening for test compounds that affect (inhibit or potentiate) an interaction between an F-box protein or SCF complex and a substrate as defined by interactions 1 to 4 or 5 to 8/9 in Table 3 or Table 4.

[0297] As used herein, the term “test compound” means any compound which is potentially capable of associating with a binding pocket, inhibiting or enhancing interactions of atomic contacts in a binding pocket. If, after testing, it is determined that the test compound does bind to the binding pocket, inhibits or enhances interactions of atomic contacts in a binding pocket, it is known as a “ligand”.

[0298] The test compound may be designed or obtained from a library of compounds which may comprise peptides, as well as other compounds, such as small organic molecules and particularly new lead compounds. By way of example, the test compound may be a natural substance, a biological macromolecule, or an extract made from biological materials such as bacteria, fungi, or animal (particularly mammalian) cells or tissues, an organic or an inorganic molecule, a synthetic test compound, a semi-synthetic test compound, a carbohydrate, a monosaccharide, an oligosaccharide or polysaccharide, a glycolipid, a glycopeptide, a saponin, a heterocyclic compound, a structural or functional mimetic, a peptide, a peptidomimetic, a derivatised test compound, a peptide cleaved from a whole protein, or a peptide synthesised synthetically (such as, by way of example, either using a peptide synthesizer or by recombinant techniques or combinations thereof), a recombinant test compound, a natural or a non-natural test compound, a fusion protein or equivalent thereof and mutants, derivatives or combinations thereof.

[0299] The increasing availability of biomacromolecule structures of potential pharmacophoric molecules that have been solved crystallographically has prompted the development of a variety of direct computational methods for molecular design, in which the steric and electronic properties of substrate binding sites are use to guide the design of potential ligands (Cohen et al. (1990) J. Med. Cam. 33: 883-894; Kuntz et al. (1982) J. Mol. Biol 161: 269-288; DesJarlais (1988) J. Med. Cam. 31: 722-729; Bartlett et al. (1989) (Spec. Publ., Roy. Soc. Chem.) 78: 182-196; Goodford et al. (1985) J. Med. Cam. 28: 849-857; DesJarlais et al. J. Med. Cam. 29: 2149-2153). Directed methods generally fall into two categories: (1) design by analogy in which 3-D structures of known molecules (such as from a crystallographic database) are docked to the structure and scored for goodness-of-fit; and (2) de novo design, in which the ligand model is constructed piece-wise. The latter approach, in particular, can facilitate the development of novel molecules, uniquely designed to bind to the subject binding pockets.

[0300] The test compound may be screened as part of a library or a data base of molecules. Modulators of a binding pocket of the present invention may be identified by docking a computer representation of compounds from one or more database of molecules. Data bases which may be used include ACD (Molecular Designs Limited), NCI (National Cancer Institute), CCDC (Cambridge Crystallographic Data Center), CAST (Chemical Abstract Service), Derwent (Derwent Information Limited), Maybridge (Maybridge Chemical Company Ltd), Aldrich (Aldrich Chemical Company), DOCK (University of California in San Francisco), and the Directory of Natural Products (Chapman & Hall). Computer programs such as CONCORD (Tripos Associates) or DB-Converter (Molecular Simulations Limited) can be used to convert a data set represented in two dimensions to one represented in three dimensions.

[0301] Test compounds may tested for their capacity to fit spatially into a binding pocket. As used herein, the term “fits spatially” means that the three-dimensional structure of the test compound is accommodated geometrically in a cavity of a binding pocket. The test compound can then be considered to be a ligand.

[0302] A favourable geometric fit occurs when the surface area of the test compound is in close proximity with the surface area of the cavity of a binding pocket without forming unfavorable interactions. A favourable complementary interaction occurs where the test compound interacts by hydrophobic, aromatic, ionic, dipolar, or hydrogen donating and accepting forces. Unfavourable interactions may be steric hindrance between atoms in the test compound and atoms in the binding pocket.

[0303] If a model of the present invention is a computer model, the test compounds may be positioned in a binding pocket through computational docking. If, on the other hand, the model of the present invention is a structural model, the test compounds may be positioned in the binding pocket by, for example, manual docking.

[0304] As used herein the term “docking” refers to a process of placing a compound in close proximity with a binding pocket, or a process of finding low energy conformations of a test compound/binding pocket complex.

[0305] A screening method of the present invention may comprise the following steps:

[0306] (i) generating a computer model of a binding pocket using a crystal according to the invention;

[0307] (ii) docking a computer representation of a test compound with the computer model; and

[0308] (iii) analysing the fit of the compound in the binding pocket.

[0309] In an aspect of the invention, a method is provided comprising the following steps:

[0310] (a) docking a computer representation of a structure of a test compound into a computer representation of a binding pocket defined in accordance with the invention using a computer program, or by interactively moving the representation of the test compound into the representation of the binding pocket;

[0311] (b) characterizing the geometry and the complementary interactions formed between the atoms of the binding pocket and the compound; optionally

[0312] (c) searching libraries for molecular fragments which can fit into the empty space between the compound and the binding pocket and can be linked to the compound; and

[0313] (d) linking the fragments found in (c) to the compound and evaluating the new modified compound.

[0314] In an embodiment of the invention, a method is provided which comprises the following steps:

[0315] (a) docking a computer representation of a test compound from a computer data base with a computer representation of a selected binding pocket defined in accordance with the invention to define a complex;

[0316] (b) determining a conformation of the complex with a favorable fit and favourable complementary interactions; and

[0317] (c) identifying test compounds that best fit the selected binding pocket as potential modulators of a F-box protein or SCF complex comprising the binding pocket.

[0318] In another embodiment of the invention, a method is provided which comprises docking a computer representation of a selected binding pocket defined by the atomic interactions, atomic contacts, or structural coordinates in accordance with the invention to define a complex. In particular a method is provided comprising:

[0319] (a) docking a computer representation of a test compound from a computer database with a computer representation of a selected binding pocket defined by the atomic interactions, atomic contacts, or structural coordinates described herein;

[0320] (b) determining a conformation of the complex with a favorable fit and favourable complementary interactions; and

[0321] (c) identifying test compounds that best fit the selected binding pocket as potential modulators of the a F-box protein or SCF complex comprising the binding pocket

[0322] A model used in a screening method may comprise a binding pocket either alone or in association with one or more ligands and/or cofactors. For example, the model may comprise the binding pocket in association with a substrate (or analogue thereof), and/or modulator.

[0323] If the model comprises an unassociated binding pocket, then the selected site under investigation may be the binding pocket itself. The test compound may, for example, mimic a known ligand (e.g. substrate) for an F-box protein in order to interact with the binding pocket. The selected site may alternatively be another site on the F-box protein.

[0324] If the model comprises an associated binding pocket, for example a binding pocket in association with a substrate or ligand, the selected site may be the binding pocket or a site made up of the binding pocket and the complexed substrate or ligand, or a site on the substrate or ligand itself. The test compound may be investigated for its capacity to modulate the interaction with the associated molecule.

[0325] The screening methods described herein may be applied to a plurality of test compounds, to identify those that best fit the selected site. A test compound (or plurality of test compounds) may be selected on the basis of their similarity to a substrate or ligand for an F-box protein. For example, the screening method may comprise the following steps:

[0326] (i) generating a computer model of a binding pocket in complex with a substrate or ligand;

[0327] (ii) searching for a test compound with a similar three dimensional structure and/or similar chemical groups as the substrate or ligand; and

[0328] (iii) evaluating the fit of the test compound in the binding pocket.

[0329] Searching may be carried out using a database of computer representations of potential compounds, using methods known in the art.

[0330] The present invention also provides a method for designing ligands for F-box proteins or SCF complexes. It is well known in the art to use a screening method as described above to identify a test compound with promising fit, but then to use this test compound as a starting point to design a ligand with improved fit to the model. Such techniques are known as “structure-based ligand design” (See Kuntz et al., 1994, Acc. Chem. Res. 27:117; Guida, 1994, Current Opinion in Struc. Biol. 4: 777; and Colman, 1994, Current Opinion in Struc. Biol. 4: 868, for reviews of structure-based drug design and identification; and Kuntz et al 1982, J. Mol. Biol. 162:269; Kuntz et al., 1994, Acc. Chem. Res. 27: 117; Meng et al., 1992, J. Compt. Chem. 13: 505; Bohm, 1994, J. Comp. Aided Molec. Design 8: 623 for methods of structure-based modulator design).

[0331] Examples of computer programs that may be used for structure-based ligand design are CAVEAT (Bartlett et al., 1989, in “Chemical and Biological Problems in Molecular Recognition”, Roberts, S. M. Ley, S. V.; Campbell, N. M. eds; Royal Society of Chemistry: Cambridge, pp 182-196); FLOG (Miller et al., 1994, J. Comp. Aided Molec. Design 8:153); PRO Modulator (Clark et al., 1995 J. Comp. Aided Molec. Design 9:13); MCSS (Miranker and Karplus, 1991, Proteins: Structure, Fuction, and Genetics 8:195); and, GRID (Goodford, 1985, J. Med. Chem. 28:849).

[0332] The method may comprise the following steps:

[0333] (i) docking a model of a test compound with a model of a binding pocket;

[0334] (ii) identifying one or more groups on the test compound which may be modified to improve their fit in the binding pocket;

[0335] (iii) replacing one or more identified groups to produce a modified test compound model; and

[0336] (iv) docking the modified test compound model with the model of the binding pocket.

[0337] Evaluation of fit may comprise the following steps:

[0338] (a) mapping chemical features of a test compound such as by hydrogen bond donors or acceptors, hydrophobic/lipophilic sites, positively ionizable sites, or negatively ionizable sites; and

[0339] (b) adding geometric constraints to selected mapped features.

[0340] The fit of the modified test compound may then be evaluated using the same criteria.

[0341] The chemical modification of a group may either enhance or reduce hydrogen bonding interaction, charge interaction, hydrophobic interaction, Van Der Waals interaction or dipole interaction between the test compound and the key amino acid residue(s) of the binding pocket. Preferably the group modifications involve the addition removal or replacement of substituents onto the test compound such that the substituents are positioned to collide or to bind preferentially with one or more amino acid residues that correspond to the key amino acid residues of the binding pocket.

[0342] If a modified test compound model has an improved fit, then it may bind to a binding pocket and be considered to be a “ligand”. Rational modification of groups may be made with the aid of libraries of molecular fragments which may be screened for their capacity to fit into the available space and to interact with the appropriate atoms. Databases of computer representations of libraries of chemical groups are available commercially, for this purpose.

[0343] The test compound may also be modified “in situ” (i.e. once docked into the potential binding pocket), enabling immediate evaluation of the effect of replacing selected groups. The computer representation of the test compound may be modified by deleting a chemical group or groups, or by adding a chemical group or groups. After each modification to a compound, the atoms of the modified compound and potential binding pocket can be shifted in conformation and the distance between the modulator and the binding pocket atoms may be scored on the basis of geometric fit and favourable complementary interactions between the molecules. This technique is described in detail in Molecular Simulations User Manual, 1995 in LUDI.

[0344] Examples of ligand building and/or searching computer programs include programs in the Molecular Simulations Package (Catalyst), ISIS/HOST, ISIS/BASE, and ISIS/DRAW (Molecular Designs Limited), and UNITY (Tripos Associates).

[0345] The “starting point” for rational ligand design may be a known substrate or lignad. For example, in order to identify potential modulators of an F-box protein, a logical approach would be to start with a known ligand or substrate to produce a molecule which mimics the binding of the ligand or substrate. Such a molecule may, for example, act as a competitive inhibitor for the true substrate or ligand, or may bind so strongly that the interaction (and inhibition) is effectively irreversible.

[0346] Such a method may comprise the following steps:

[0347] (i) generating a computer model of a binding pocket in complex with a substrate or ligand;

[0348] (ii) replacing one or more groups on the ligand model to produce a modified substrate or ligand; and

[0349] (iii) evaluating the fit of the modified substrate or ligand in the binding pocket.

[0350] The replacement groups could be selected and replaced using a compound construction program which replaces computer representations of chemical groups with groups from a computer database, where the representations of the compounds are defined by structural coordinates.

[0351] In an embodiment, a screening method is provided for identifying a substrate or ligand of an F-box protein, comprising the step of using the structural coordinates of a CPD motif defined in relation to its spatial association with a binding pocket of the invention, to generate a compound that is capable of associating with the binding pocket.

[0352] In an embodiment of the invention, a screening method is provided for identifying a ligand of an F-box protein, in particular a cdc4 protein, comprising the step of using the structural coordinates of the CPD motif listed in Table 6 to generate a compound for associating with a binding pocket of an F-box protein, in particular a cdc4 protein as described herein. The following steps are employed in a particular method of the invention: (a) generating a computer representation of a CPD motif defined by its structural coordinates listed in Table 6; and (b) searching for molecules in a data base that are structurally or chemically similar to the defined CPD motif, using a searching computer program, or replacing portions of the CPD motif with similar chemical structures from a database using a compound building computer program.

[0353] A screening method is provided for identifying a ligand of an F-box protein, in particular a cdc4 protein, or a SCF complex comprising the step of using the structural coordinates of a binding pocket comprising a WD40 repeat or part thereof listed in Table 6 to generate a compound for associating with a F-box domain of an F-box protein. The following steps are employed in a particular method of the invention: (a) generating a computer representation of a binding pocket comprising a WD40 repeat region or part thereof defined by its structural coordinates listed in Table 6; and (b) searching for molecules in a data base that are structurally or chemically similar to the defined binding pocket using a searching computer program, or replacing portions of the binding pocket with structures from a database using a compound building computer program.

[0354] A screening method is provided for identifying a ligand of an F-box protein, in particular a cdc4 protein, of a SCF complex comprising the step of using the structural coordinates of a binding pocket comprising an F-box domain or part thereof, or helical linker listed in Table 6 to generate a compound for associating with a F-box domain or helical linker of an F-box protein. The following steps are employed in a particular method of the invention: (a) generating a computer representation of a binding pocket comprising a an F-box domain or part thereof, or helical linker defined by its structural coordinates listed in Table 4; and (b) searching for molecules in a data base that are structurally or chemically similar to the defined binding pocket using a searching computer program, or replacing portions of the binding pocket with structures from a database using a compound building computer program.

[0355] The screening methods of the present invention may be used to identify compounds or entities that associate with a molecule that associates with an F-box protein, in particular a cdc4 protein, or an SCF complex.

[0356] In an illustrative embodiment, the design of potential modulators or substrates for SCF complexes begins from the general perspective of shape complimentarity for an active site and substrate specificity subsites of the receptor, and a search algorithm is employed which is capable of scanning a database of small molecules of known three-dimensional structure for candidates which fit geometrically into the target protein site. It is not expected that the molecules found in the shape search will necessarily be leads themselves, since no evaluation of chemical interaction need necessarily be made during the initial search. Rather, it is anticipated that such candidates might act as the framework for further design, providing molecular skeletons to which appropriate atomic replacements can be made. Of course, the chemical complimentarity of these molecules can be evaluated, but it is expected that atom types will be changed to maximize the electrostatic, hydrogen bonding, and hydrophobic interactions with the receptor. Most algorithms of this type provide a method for finding a wide assortment of chemical structures that are complementary to the shape of a binding site of a subject molecule or complex. Each of a set of small molecules from a particular data-base, such as the Cambridge Crystallographic Data Bank (CCDB) (Allen et al. (1973) J. Chem. Doc. 13: 119), is individually docked to the binding pocket of the invention, in a number of geometrically permissible orientations with use of a docking algorithm. In a preferred embodiment, a set of computer algorithms called DOCK, can be used to characterize the shape of invaginations and grooves that form active sites and recognition surfaces of a subject molecule or complex (Kuntz et al. (1982) J. Mol. Biol 161: 269-288). The program can also search a database of small molecules for templates whose shapes are complementary to particular binding pockets or sites of a receptor (DesJarlais et al. (1988) J Med Chem 31: 722-729). These templates normally require modification to achieve good chemical and electrostatic interactions (DesJarlais et al. (1989) ACS Symp Ser 413: 60-69). However, the program has been shown to position accurately known cofactors for ligands based on shape constraints alone.

[0357] The orientations are evaluated for goodness-of-fit and the best are kept for further examination using molecular mechanics programs, such as AMBER or CHARMM. Such algorithms have previously proven successful in finding a variety of molecules that are complementary in shape to a given binding site of a molecule or complex, and have been shown to have several attractive features. First, such algorithms can retrieve a remarkable diversity of molecular architectures. Second, the best structures have, in previous applications to other proteins, demonstrated impressive shape complementarity over an extended surface area. Third, the overall approach appears to be quite robust with respect to small uncertainties in positioning of the candidate atoms.

[0358] Goodford (1985, J Med Chem 28:849-857) and Boobbyer et al. (1989, J Med Chem 32:1083-1094) have produced a computer program (GRID) which seeks to determine regions of high affinity for different chemical groups (termed probes) on the molecular surface of the binding site. GRID hence provides a tool for suggesting modifications to known ligands that might enhance binding. It may be anticipated that some of the sites discerned by GRID as regions of high affinity correspond to “pharmacophoric patterns” determined inferentially from a series of known ligands. As used herein, a pharmacophoric pattern is a geometric arrangement of features of the anticipated ligand that is believed to be important for binding. Attempts have been made to use pharmacophoric patterns as a search screen for novel ligands (Jakes et al. (1987) J Mol Graph 5:41-48; Brint et al. (1987) J Mol Graph 5:49-56; Jakes et al. (1986) J Mol Graph 4:12-20); however, the constraint of steric and “chemical” fit in the putative (and possibly unknown) binding pocket or site is ignored. Goodsell and Olson (1990, Proteins: Struct Funct Genet 8:195-202) have used the Metropolis (simulated annealing) algorithm to dock a single known ligand into a target protein. They allow torsional flexibility in the ligand and use GRID interaction energy maps as rapid lookup tables for computing approximate interaction energies. Given the large number of degrees of freedom available to the ligand, the Metropolis algorithm is time-consuming and is unsuited to searching a candidate database of a few thousand small molecules.

[0359] Yet a further embodiment of the present invention utilizes a computer algorithm such as CLIX which searches such databases as CCDB for small molecules which can be oriented in a binding pocket or site in a way that is both sterically acceptable and has a high likelihood of achieving favorable chemical interactions between the candidate molecule and the surrounding amino acid residues. The method is based on characterizing a binding pocket in terms of an ensemble of favorable binding positions for different chemical groups and then searching for orientations of the candidate molecules that cause maximum spatial coincidence of individual candidate chemical groups with members of the ensemble. The current availability of computer power dictates that a computer-based search for novel ligands follows a breadth-first strategy. A breadth-first strategy aims to reduce progressively the size of the potential candidate search space by the application of increasingly stringent criteria, as opposed to a depth-first strategy wherein a maximally detailed analysis of one candidate is performed before proceeding to the next. CLIX conforms to this strategy in that its analysis of binding is rudimentary—it seeks to satisfy the necessary conditions of steric fit and of having individual groups in “correct” places for bonding, without imposing the sufficient condition that favorable bonding interactions actually occur. A ranked “shortlist” of molecules, in their favored orientations, is produced which can then be examined on a molecule-by-molecule basis, using computer graphics and more sophisticated molecular modeling techniques. CLIX is also capable of suggesting changes to the substituent chemical groups of the candidate molecules that might enhance binding.

[0360] The algorithmic details of CLIX is described in Lawerence et al. (1992) Proteins 12:31-41, and the CLIX algorithm can be summarized as follows. The GRID program is used to determine discrete favorable interaction positions (termed target sites) in the binding pocket or site of the protein for a wide variety of representative chemical groups. For each candidate ligand in the CCDB an exhaustive attempt is made to make coincident, in a spatial sense in the binding site of the protein, a pair of the candidate's substituent chemical groups with a pair of corresponding favorable interaction sites proposed by GRID. All possible combinations of pairs of ligand groups with pairs of GRID sites are considered during this procedure. Upon locating such coincidence, the program rotates the candidate ligand about the two pairs of groups and checks for steric hindrance and coincidence of other candidate atomic groups with appropriate target sites. Particular candidate/orientation combinations that are good geometric fits in the binding site and show sufficient coincidence of atomic groups with GRID sites are retained.

[0361] Consistent with the breadth-first strategy, this approach involves simplifying assumptions. Rigid protein and small molecule geometry is maintained throughout. As a first approximation rigid geometry is acceptable as the energy minimized coordinates of a deduced structure, describe an energy minimum for the molecule, albeit a local one. If the surface residues of the site of interest are not involved in crystal contacts then the crystal configuration of those residues is used merely as a starting point for energy minimization, and potential solution structures for those residues determined. The deduced structure should reasonably mimic the mean solution configuration.

[0362] A further assumption implicit in CLIX is that the potential ligand, when introduced into the binding pocket or site of a receptor, does not induce change in the protein's stereochemistry or partial charge distribution and so alter the basis on which the GRID interaction energy maps were computed. It must also be stressed that the interaction sites predicted by GRID are used in a positional and type sense only, i.e., when a candidate atomic group is placed at a site predicted as favorable by GRID, no check is made to ensure that the bond geometry, the state of protonation, or the partial charge distribution favors a strong interaction between the protein and that group. Such detailed analysis should form part of more advanced modeling of candidates identified in the CLIX shortlist.

[0363] Yet another embodiment of a computer-assisted molecular design method for identifying ligands of a binding pocket of the invention comprises the de novo synthesis of potential ligands by algorithmic connection of small molecular fragments that will exhibit the desired structural and electrostatic complementarity with an active site or binding pocket of the receptor. The methodology employs a large template set of small molecules with are iteratively pieced together in a model of a binding pocket. Each stage of ligand growth is evaluated according to a molecular mechanics-based energy function, which considers van der Waals and coulombic interactions, internal strain energy of the lengthening ligand, and desolvation of both ligand and receptor. The search space can be managed by use of a data tree that is kept under control by pruning according to the binding criteria.

[0364] In an illustrative embodiment, the search space is limited to consider only amino acids and amino acid analogs as the molecular building blocks. Such a methodology generally employs a large template set of amino acid conformations, though need not be restricted to just the 20 natural amino acids, as it can easily be extended to include other related fragments of interest to the medicinal chemist, e.g. amino acid analogs. The putative ligands that result from this construction method are peptides and peptide-like compounds rather than the small organic molecules that are typically the goal of drug design research. The appeal of the peptide building approach is not that peptides are preferable to organics as potential pharmaceutical agents, but rather that: (1) they can be generated relatively rapidly de novo; (2) their energetics can be studied by well-parameterized force field methods; (3) they are much easier to synthesize than are most organics; and (4) they can be used in a variety of ways, for peptidomimetic ligand design, protein-protein binding studies, and even as shape templates in the more commonly used 3D organic database search approach described above.

[0365] Such a de novo peptide design method has been incorporated in a software package called GROW (Moon et al. (1991) Proteins 11:314-328). In a typical design session, standard interactive graphical modeling methods are employed to define the structural environment in which GROW is to operate. For instance, environment could be an active site binding pocket of an F-box protein, or it could be a set of features on the protein's surface to which the user wishes to bind a peptide-like molecule. The GROW program then operates to generate a set of potential ligand molecules. Interactive modeling methods then come into play again, for examination of the resulting molecules, and for selection of one or more of them for further refinement.

[0366] To illustrate, GROW operates on an atomic coordinate file generated by the user in the interactive modeling session, such as the coordinates provided in Table 4, or the coordinates of a binding pocket or active site as described in Tables 2 and 4 plus a small fragment (e.g., an acetyl group) positioned in the active site to provide a starting point for peptide growth. These are referred to as “site” atoms and “seed” atoms, respectively. A second file provided by the user contains a number of control parameters to guide the peptide growth (Moon et al. (1991) Proteins 11:314-328).

[0367] The operation of the GROW algorithm is conceptually fairly simple. GROW proceeds in an iterative fashion, to systematically attach to the seed fragment each amino acid template in a large preconstructed library of amino acid conformations. When a template has been attached, it is scored for goodness-of-fit to the receptor site or binding pocket, and then the next template in the library is attached to the seed. After all the templates have been tested, only the highest scoring ones are retained for the next level of growth. This procedure is repeated for the second growth level; each library template is attached in turn to each of the bonded seed/amino acid molecules that were retained from the first step, and then scored. Again, only the best of the bonded seed/dipeptide molecules that result are retained for the third level of growth. The growth of peptides can proceed in the N-to-C direction only, the reverse direction only, or in alternating directions, depending on the initial control specifications supplied by the user. Successive growth levels therefore generate peptides that are lengthened by one residue. The procedure terminates when the user-defined peptide length has been reached, at which point the user can select from the constructed peptides those to be studied further. The resulting data provided by the GROW procedure includes not only residue sequences and scores, but also atomic coordinates of the peptides, related directly to the coordinate system of the binding site atoms.

[0368] In yet another embodiment, potential pharmacophoric compounds can be determined using a method based on an energy minimization-quenched molecular dynamics algorithm for determining energetically favorable positions of functional groups in the binding pockets of the invention. The method can aid in the design of molecules that incorporate such functional groups by modification of known ligands or de novo construction.

[0369] For example, the multiple copy simultaneous search method (MCSS) described by Miranker et al. (1991) Proteins 11: 29-34 may be employed. To determine and characterize a local minima of a functional group in the forcefield of the protein, multiple copies of selected functional groups are first distributed in a binding pocket of interest on the F-box protein. Energy minimization of these copies by molecular mechanics or quenched dynamics yields the distinct local minima. The neighborhood of these minima can then be explored by a grid search or by constrained minimization. In one embodiment, the MCSS method uses the classical time dependent Hartee (TDH) approximation to simultaneously minimize or quench many identical groups in the forcefield of the protein.

[0370] Implementation of the MCSS algorithm requires a choice of functional groups and a molecular mechanics model for each of them. Groups must be simple enough to be easily characterized and manipulated (3-6 atoms, few or no dihedral degrees of freedom), yet complex enough to approximate the steric and electrostatic interactions that the functional group would have in binding to the pocket or site of interest in the F-box protein. A preferred set is, for example, one in which most organic molecules can be described as a collection of such groups (Patai's Guide to the Chemistry of Functional Groups, ed. S. Patai (New York: John Wiley, and Sons, (1989)). This includes fragments such as acetonitrile, methanol, acetate, methyl ammonium, dimethyl ether, methane, and acetaldehyde.

[0371] Determination of the local energy minima in the binding pocket or site requires that many starting positions be sampled. This can be achieved by distributing, for example, 1,000-5,000 groups at random inside a sphere centered on the binding site; only the space not occupied by the protein needs to be considered. If the interaction energy of a particular group at a certain location with the protein is more positive than a given cut-off (e.g. 5.0 kcal/mole) the group is discarded from that site. Given the set of starting positions, all the fragments are minimized simultaneously by use of the TDH approximation (Elber et al. (1990) J Am Chem Soc 112: 9161-9175). In this method, the forces on each fragment consist of its internal forces and those due to the protein. The essential element of this method is that the interactions between the fragments are omitted and the forces on the protein are normalized to those due to a single fragment. In this way simultaneous minimization or dynamics of any number of functional groups in the field of a single protein can be performed.

[0372] Minimization is performed successively on subsets of, for example 100, of the randomly placed groups. After a certain number of step intervals, such as 1,000 intervals, the results can be examined to eliminate groups converging to the same minimum. This process is repeated until minimization is complete (e.g. RMS gradient of 0.01 kcal/mole/C). Thus the resulting energy minimized set of molecules comprises what amounts to a set of disconnected fragments in three dimensions representing potential pharmacophores.

[0373] The next step then is to connect the pharmacophoric pieces with spacers assembled from small chemical entities (atoms, chains, or ring moieties). In a preferred embodiment, each of the disconnected can be linked in space to generate a single molecule using such computer programs as, for example, NEWLEAD (Tschinke et al. (1993) J Med Chem 36: 3863,3870). The procedure adopted by NEWLEAD executes the following sequence of commands: (1) connect two isolated moieties, (2) retain the intermediate solutions for further processing, (3) repeat the above steps for each of the intermediate solutions until no disconnected units are found, and (4) output the final solutions, each of which is a single molecule. Such a program can use for example, three types of spacers: library spacers, single-atom spacers, and fuse-ring spacers. The library spacers are optimized structures of small molecules such as ethylene, benzene and methylamide. The output produced by programs such as NEWLEAD consist of a set of molecules containing the original fragments now connected by spacers. The atoms belonging to the input fragments maintain their original orientations in space. The molecules are chemically plausible because of the simple makeup of the spacers and functional groups, and energetically acceptable because of the rejection of solutions with van-der Waals radii violations.

[0374] Compounds and entities (e.g. ligands) of F-box proteins, in particular cdc4 proteins, or SCF complexes identified using the above-described methods may be prepared using methods described in standard reference sources utilized by those skilled in the art. For example, organic compounds may be prepared by organic synthetic methods described in references such as March, 1994, Advanced Organic Chemistry: Reactions, Mechanisms, and Structure, New York, McGraw Hill.

[0375] Test compounds and ligands which are identified using a crystal or model of the present invention can be screened in assays such as those well known in the art. Screening may be for example in vitro, in cell culture, and/or in vivo. Biological screening assays preferably centre on activity-based response models, binding assays (which measure how well a compound binds to a binding pocket of a receptor), and bacterial, yeast, and animal cell lines (which measure the biological effect of a compound in a cell). The assays may be automated for high throughput screening in which large numbers of compounds can be tested to identify compounds with the desired activity. The biological assay may also be an assay for the binding activity of a compound that selectively binds to the binding pocket compared to other receptors.

[0376] Ligands/Compounds Identified by Screening Methods

[0377] The present invention provides a ligand or compound identified by a screening method of the present invention. A ligand or compound may have been designed rationally by using a model according to the present invention. A ligand or compound identified using the screening methods of the invention may specifically associate with a target compound, or part thereof (e.g. a binding pocket). In the present invention the target compound may be the F-box protein or SCF complex or part thereof, or a molecule that is capable of associating with an F-box protein or SCF complex or part thereof (for example a substrate).

[0378] A ligand or compound identified using a screening method of the invention may act as a “modulator”, i.e. a compound which affects the activity of an F-box protein or SCF complex. A modulator may reduce, enhance or alter the biological function of an F-box protein or an SCF E3 ubiquitin ligase. For example a modulator may modulate the capacity of the F-box protein or an SCF E3 ubiquitin ligase to interact with its substrate. An alteration in biological function may be characterised by a change in specificity. For example, a modulator may cause the F-box protein to interact with a different substrate. In order to exert its function, the modulator commonly binds to a binding pocket.

[0379] A “modulator” which is capable of reducing the biological function of the enzyme may also be known as an inhibitor. Preferably an inhibitor reduces or blocks the capacity of the F-box protein or an SCF E3 ubiquitin ligase to interact with its substrate thus reducing or blocking ubiquitination of the substrate. The inhibitor may mimic the binding of a substrate, for example, it may be a substrate analogue. A substrate analogue may be designed by considering the interactions between the substrate and the F-box protein or an SCF E3 ubiquitin ligase (for example, by using information derivable from the crystal of the invention) and specifically altering one or more groups (as described above).

[0380] The present invention also provides a method for modulating the activity of an F-box protein, in particular a cdc4 protein, using a modulator according to the present invention. The invention also provides a method for modulating (e.g. potentiating or inhibiting) ubiquitination of a substrate by an SCF E3 ubiquitin ligase, by potentiating or inhibiting the substrate binding pocket of the ligase. Inhibition of ubiquitination of a substrate may decrease signaling and inhibit cellular processes that may be involved in disease. It would be possible to monitor cellular processes following such treatments by a number of methods known in the art.

[0381] A modulator may be an agonist, partial agonist, partial inverse agonist or antagonist of an F-box protein.

[0382] As mentioned above, a substrate or an identified ligand may act as a ligand model (for example, a template) for the development of other compounds. A modulator may be a mimetic of a substrate or ligand.

[0383] Like the test compound (see above) a modulator may be one or a variety of different sorts of molecule. (See examples herein.) A modulator may be an endogenous physiological compound, or it may be a natural or synthetic compound. The term “modulator” also refers to a chemically modified ligand or substrate.

[0384] The technique suitable for preparing a modulator will depend on its chemical nature. For example, peptides can be synthesized by solid phase techniques (Roberge J Y et al (1995) Science 269: 202-204) and automated synthesis may be achieved, for example, using the ABI 43 1 A Peptide Synthesizer (Perkin Elmer) in accordance with the instructions provided by the manufacturer. Once cleaved from the resin, the peptide may be purified by preparative high performance liquid chromatography (e.g., Creighton (1983) Proteins Structures and Molecular Principles, WH Freeman and Co, New York N.Y.). The composition of the synthetic peptides may be confirmed by amino acid analysis or sequencing (e.g., the Edman degradation procedure; Creighton, supra).

[0385] If a modulator is a nucleotide, or a polypeptide expressable therefrom, it may be synthesized, in whole or in part, using chemical methods well known in the art (see Caruthers M H et al (1980) Nuc Acids Res Symp Ser 215-23, Horn T et al (1980) Nuc Acids Res Symp Ser 225-232), or it may be prepared using recombinant techniques well known in the art.

[0386] Organic compounds may be prepared by organic synthetic methods described in references such as March, 1994, Advanced Organic Chemistry: Reactions, Mechanisms, and Structure, New York, McGraw Hill.

[0387] The invention also relates to classes of modulators of F-box proteins, in particular cdc4 proteins based on the structure and shape of a substrate or component thereof, defined in relation to the substrate's spatial association with a crystal structure of the invention or part thereof.

[0388] A class of modulators may comprise a compound containing a structure of a CPD motif. In particular, the modulators can comprise a CPD motif having the structural coordinates of the CPD motif in the active site binding pocket of an F-box protein. In an embodiment, a modulator comprises the structural coordinates of a CPD motif having the structural coordinates listed in Table 6.

[0389] The invention contemplates all optical isomers and racemic forms of the modulators of the invention.

[0390] Pharmaceutical Composition

[0391] The present invention also provides for the use of a modulator according to the invention, in the manufacture of a medicament to treat and/or prevent a disease in a mammalian patient. There is also provided a pharmaceutical composition comprising such a modulator and a method of treating and/or preventing a disease comprising the step of administering such a modulator or pharmaceutical composition to a subject, preferably a mammalian patient.

[0392] The pharmaceutical compositions may be for human or animal usage in human and veterinary medicine and will typically comprise a pharmaceutically acceptable carrier, diluent, excipient, adjuvant or combination thereof.

[0393] Acceptable carriers or diluents for therapeutic use are well known in the pharmaceutical art, and are described, for example, in Remington's Pharmaceutical Sciences, Mack Publishing Co. (A. R. Gennaro edit. 1985). The choice of pharmaceutical carrier, excipient or diluent can be selected with regard to the intended route of administration and standard pharmaceutical practice. The pharmaceutical compositions may comprise as—or in addition to—the carrier, excipient or diluent any suitable binder(s), lubricant(s), suspending agent(s), coating agent(s), solubilising agent(s).

[0394] Preservatives, stabilizers, dyes and even flavouring agents may be provided in the pharmaceutical composition. Examples of preservatives include sodium benzoate, sorbic acid and esters of p-hydroxybenzoic acid. Antioxidants and suspending agents may also be used.

[0395] The routes for administration (delivery) include, but are not limited to, one or more of: oral (e.g. as a tablet, capsule, or as an ingestable solution), topical, mucosal (e.g. as a nasal spray or aerosol for inhalation), nasal, parenteral (e.g. by an injectable form), gastrointestinal, intraspinal, intraperitoneal, intramuscular, intravenous, intrauterine, intraocular, intradermal, intracranial, intratracheal, intravaginal, intracerebroventricular, intracerebral, subcutaneous, ophthalmic (including intravitreal or intracameral), transdermal, rectal, buccal, vaginal, epidural, sublingual.

[0396] Where the pharmaceutical composition is to be delivered mucosally through the gastrointestinal mucosa, it should be able to remain stable during transit though the gastrointestinal tract; for example, it should be resistant to proteolytic degradation, stable at acid pH and resistant to the detergent effects of bile.

[0397] Where appropriate, the pharmaceutical compositions can be administered by inhalation, in the form of a suppository or pessary, topically in the form of a lotion, gel, hydrogel, solution, cream, ointment or dusting powder, by use of a skin patch, orally in the form of tablets containing excipients such as starch or lactose or chalk, or in capsules or ovules either alone or in admixture with excipients, or in the form of elixirs, solutions or suspensions containing flavouring or colouring agents, or they can be injected parenterally, for example intravenously, intramuscularly or subcutaneously. For parenteral administration, the compositions may be best used in the form of a sterile aqueous solution which may contain other substances, for example enough salts or monosaccharides to make the solution isotonic with blood. The aqueous solutions should be suitably buffered (preferably to a pH of from 3 to 9), if necessary. The preparation of suitable parenteral formulations under sterile conditions is readily accomplished by standard pharmaceutical techniques well-known to those skilled in the art.

[0398] If the agent of the present invention is administered parenterally, then examples of such administration include one or more of: intravenously, intra-arterially, intraperitoneally, intrathecally, intraventricularly, intraurethrally, intrasternally, intracranially, intramuscularly or subcutaneously administering the agent; and/or by using infusion techniques.

[0399] For buccal or sublingual administration the compositions may be administered in the form of tablets or lozenges which can be formulated in a conventional manner.

[0400] The tablets may contain excipients such as microcrystalline cellulose, lactose, sodium citrate, calcium carbonate, dibasic calcium phosphate and glycine, disintegrants such as starch (preferably corn, potato or tapioca starch), sodium starch glycollate, croscarmellose sodium and certain complex silicates, and granulation binders such as polyvinylpyrrolidone, hydroxypropylmethylcellulose (HPMC), hydroxypropylcellulose (HPC), sucrose, gelatin and acacia. Additionally, lubricating agents such as magnesium stearate, stearic acid, glyceryl behenate and talc may be included.

[0401] Solid compositions of a similar type may also be employed as fillers in gelatin capsules. Preferred excipients in this regard include lactose, starch, cellulose, milk sugar or high molecular weight polyethylene glycols. For aqueous suspensions and/or elixirs, the agent may be combined with various sweetening or flavouring agents, colouring matter or dyes, with emulsifying and/or suspending agents and with diluents such as water, ethanol, propylene glycol and glycerin, and combinations thereof.

[0402] As indicated, a therapeutic agent (e.g. modulator) of the present invention can be administered intranasally or by inhalation and is conveniently delivered in the form of a dry powder inhaler or an aerosol spray presentation from a pressurised container, pump, spray or nebuliser with the use of a suitable propellant, e.g. dichlorodifluoromethane, trichlorofluoromethane, dichlorotetrafluoroethane, a hydrofluoroalkane such as 1,1,1,2-tetrafluoroethane (HFA 134A™) or 1,1,1,2,3,3,3-heptafluoropropane (HFA 227EA™), carbon dioxide or other suitable gas. In the case of a pressurised aerosol, the dosage unit may be determined by providing a valve to deliver a metered amount. The pressurised container, pump, spray or nebuliser may contain a solution or suspension of the active compound, e.g. using a mixture of ethanol and the propellant as the solvent, which may additionally contain a lubricant, e.g. sorbitan trioleate. Capsules and cartridges (made, for example, from gelatin) for use in an inhaler or insufflator may be formulated to contain a powder mix of the agent and a suitable powder base such as lactose or starch.

[0403] Therapeutic administration of polypeptide modulators may also be accomplished using gene therapy. A nucleic acid including a promoter operatively linked to a heterologous polypeptide may be used to produce high-level expression of the polypeptide in cells transfected with the nucleic acid. DNA or isolated nucleic acids may be introduced into cells of a subject by conventional nucleic acid delivery systems. Suitable delivery systems include liposomes, naked DNA, and receptor-mediated delivery systems, and viral vectors such as retroviruses, herpes viruses, and adenoviruses.

[0404] Applications

[0405] The invention further provides a method of treating a mammal, the method comprising administering to a mammal a modulator or pharmaceutical composition of the present invention.

[0406] In particular, the invention contemplates a method of treating or preventing a condition or disease associated with an F-box protein or SCF complex in a cellular organism, comprising:

[0407] (a) administering a modulator of the invention in an acceptable pharmaceutical preparation; and

[0408] (b) activating or inhibiting an F-box protein or SCF complex or their interaction with a substrate to treat or prevent the disease.

[0409] The invention provides for the use of a modulator identified by the methods of the invention in the preparation of a medicament to treat or prevent a disease in a cellular organism. Use of modulators of the invention to manufacture a medicament is also provided.

[0410] Typically, a physician will determine the actual dosage of a modulator or pharmaceutical composition of the invention that will be most suitable for an individual subject and it will vary with the age, weight and response of the particular patient and severity of the condition. There can, of course, be individual instances where higher or lower dosage ranges are merited.

[0411] The specific dose level and frequency of dosage for any particular patient may be varied and will depend upon a variety of factors including the activity of the specific compound employed, the metabolic stability and length of action of that compound, the age, body weight, general health, sex, diet, mode and time of administration, rate of excretion, drug combination, the severity of the particular condition, and the individual undergoing therapy. By way of example, the pharmaceutical composition of the present invention may be administered in accordance with a regimen of 1 to 10 times per day, such as once or twice per day.

[0412] For oral and parenteral administration to human patients, the daily dosage level of the agent may be in single or divided doses.

[0413] The modulators and compositions of the invention may be useful in the prevention and treatment of conditions involving aberrant F-box proteins or SCF complexes. In particular the modulators and compositions may be useful in treating cancer or Alzheimer's Disease.

[0414] Conditions which may be prevented or treated in accordance with the invention include but are not limited to lymphoproliferative conditions, and malignant and pre-malignant conditions. Malignant and pre-malignant conditions may include solid tumors, B cell lymphomas, chronic lymphocytic leukemia, chronic myelogenous leukemia, prostate hypertrophy, Hirschsprung disease, glioblastoma, breast and ovarian cancer, adenocarcinoma of the salivary gland, premyelocytic leukemia, prostate cancer, multiple endocrine neoplasia type IIA and IIB, medullary thyroid carcinoma, papillary carcinoma, papillary renal carcinoma, hepatocellular carcinoma, gastrointestinal stromal tumors, sporadic mastocytosis, acute myeloid leukemia, large cell lymphoma or Alk lymphoma, chronic myeloid leukemia, hematological/solid tumors, papillary thyroid carcinoma, stem cell leukemia/lymphoma syndrome, acute myelogenous leukemia, osteosarcoma, multiple myeloma, preneoplastic liver foci, and resistance to chemotherapy.

[0415] Modulators and compositions of the invention may be used to restore function to a mutant F-box protein, in particular a mutant cdc4 polypeptide. Modulators and compositions of the invention, in particular inhibitors may also have utility in treating diseases associated with F-box mutations, in particular cdc4 polypeptide mutations, in combination with other cancer mutations, Notch pathway mutations or presenilin mutations.

[0416] A modulator of the invention may be used to promote binding of a substrate to a SCF complex. In an embodiment a modulator that associates (preferably with high affinity) with a binding pocket of a SCF complex as described herein, is linked to an agent that binds to a substrate to be ubiquitinated by a SCF complex. A modulator-agent-substrate complex where the modulator is derived from a binding pocket of an F-box protein as described herein may be used in treating diseases associated with a mutant F-box protein.

[0417] Therapeutic efficacy and toxicity of compositions and modulators of the invention may be determined by standard pharmaceutical procedures in cell cultures or with experimental animals, such as by calculating the ED50 (the dose therapeutically effective in 50% of the population) or LD50 (the dose lethal to 50% of the population) statistics. The therapeutic index is the dose ratio of therapeutic to toxic effects and it can be expressed as the ED50/LD50 ratio. Pharmaceutical compositions that exhibit large therapeutic indices are preferred.

[0418] The invention will now be illustrated by the following non-limiting examples:

EXAMPLE 1

[0419] The following methods were used in the investigation described in the example:

[0420] Methods

[0421] Cloning, Protein Expression and Purification

[0422] The Cdc4 fragment employed for crystalization, which is deleted for terminal residues 1 to 262 and 745 to 779, extends from the beginning of the F-box domain to the end of the WD40 repeat domain. The N-terminal deletion removes a poorly conserved sequence of 226 amino acids and a conserved element of approximately 40 residues termed the D-domain that immediately precedes the fbox domain and that has been implicated in molecular multimerization. The C terminal deletion removes residues not conserved amongst different Cdc4 homologues. Both Skp1 and Cdc4 were engineered to remove flexible loops, namely residues 36-55 in Skp1 and residues 601 to 604 and 609 to 624 in Cdc4.

[0423] A PCR product containing CDC4(263-744) was cloned into the EheI(SfoI) and BamH1 sites of pPROEX HTb. In parallel, a PCR product containing SKP1Δ37-64 was cloned into the NdeI and BamHI sites of pGEX2T-TEV. An SspI GST-SKP1-containing fragment from this construct was cloned into the StuI site of the Cdc4 construct described above such that CDC4 and SKP1 were in opposite orientations. A non-homologous region in CDC4 encoding amino acids 602-624 was then replaced by the DNA sequence GGCGAACTG [SEQ ID NO. 39], which encodes the shorter peptide sequence Gly-Glu-Leu.

[0424] The Cdc4/skp1 complex was expressed in E. coli B934 (DE3) cells grown in minimal media suplemented with a mixture of selenomethionine (40 ug/ml) and methionine (0.4 ug/ml). Cells were induced with 0.2 mM isopropyl-β-D-thiogalactopyranoside (IPTG) at 15° C. overnight. Cell pellets were resuspended in 50 mM hepes pH 7.5, 500 mM NaCl, 10% glycerol, and 5 mM Imidazole, lysed with a cell homogenizer (Emulsiflex C-5, Avistin) followed by a 20 sec sonication (vibra cell, Betatec). The lysate was then clarified by centrifugation at 65 000×g for 40 min. The supernatant was loaded onto a 5 ml metal chelating column (Pharmacia) and eluted in high imidazole. This fraction was loaded onto a glutathione-sepharose column (Pharmacia) and the bound complex was eluted by overnight digestion with TEV protease (Canadian Life). Eluted protein was dialysed to remove DTT and EDTA and reloaded onto a metal chelating column. The flow through containing the complex was concentrated and applied to a Superdex S 75 gel filtration column (Pharmacia). Fractions containing the complex were concentrated in a buffer containing 10 mM hepes pH 7.5, 250 mM NaCl, and 1 m M DTT.

[0425] Crystallization, Data Collection, and Structure Determination

[0426] Hanging drops containing 1 μl of 21 mg/ml protein plus 1.2 molar equivilents of the CPD peptide sequence were mixed with equal volumes of reservoir buffer containing 0.1 M Tris pH 8.5, and 1.5 M ammonium sulphate. Crystals were flash frozen in reservoir buffer supplemented with 15% glycerol. Crystals of the space group P32, (α=107.7 Å, b=107.7 Å, c=168.3 Å, α=γ=90°, β=120°), with two molecules of the complex in the asymmetric unit were obtained at 20° C. A Multiple Anomalous Dispersion (MAD) experiment was performed on a frozen crystal at the Advanced Photon Source (Argonne, Ill.) (APS) beamline BM 14-B and BM 14-D(λ1=0.9798 Å, λ2=0.9800 Å, λ3=0.9000 Å) using a Quantum 4 ADSC CCD detector. Data processing and reduction was carried out with the HKL program suite (Otwinowski and Minor, 1997). The programs SHARP (de La Fortelle and Bricogne, 1997) and SnB (Miller et al., 1994) were used in combination to locate and refine 19 of the 22 Se sites. Following density modification with Solomon (Abrahams and Leslie, 1996), a partial model was generated using 0 (Jones et al., 1991) and refined using CNS (Brunger et al., 1998) to a working R value of 24.09% and a free R value of 28.71%. Pertinent statistics for data collection and refinement are shown in Table 1.

[0427] The increased order of the second CPDs may be due to a crystal packing interaction involving the c-terminus of the CPD. While the main chain termini of the second CPD are discernable (FIG. 3e), the precise backbone and side chain conformations for the P−2 Leu, P−3 Gly, P+4 Ser, and P+5 Gly are less reliably determined.

[0428] Mutagenesis

[0429] Point mutants were obtained by a PCR-based approach using oligos provided in supplementary information and Pfu polymerase (Stratagene). Once verified by sequencing the mutants were sub-cloned into the appropriate vectors as listed in the supplementary information. Alanine insertion mutations were obtained using the Kunkel method (ref) and then sub-cloned into the vectors indicated in the supplementary information.

[0430] Shuffle Experiments

[0431] All mutants on a TRP1 ARS CEN plasmid were transformed into a cdc4Δ strain (MT 1259) containing a wildtype copy of CDC4 on a URA3 ARS CEN plasmid. Cells were plated on either Trp−Ura− or 5-FOA medium for 2 days at 30° C. Viable cells on 5-FOA were grown in Trp medium and transformed with either wild type GAL1-SIC1, GAL1-SIC T45A, or GAL1-SIC T33V on a LEU2 ARS CEN pasmid. Cells were then plated on Leu- Trp-plates containing either glucose or galactose and incubated for 2 days at 30° C.

[0432] Sic1-Cdc4 Interactions.

[0433] Bacterially expressed His6-Sic1 was phosphorylated with Cln2-Cdc28 kinase purified from baculovirus infected Sf9 cells as described before (Nature paper). 1 ug of WT or mutant Cdc4-GST-Skp1, immoblized on GSH-Sepharose resin, was incubated with 0.5 ug phospho-Sic1 at 4 C for 1 h and washed 4 times. Captured complexes were resolved on SDS-PAGE and Sic1 visualized by anti-Sic1 Western blotting and ECL. For IEF-2D analysis, several Sic1 phosphorylation reactions were carried out for different time periods to obtain a spectrum of Sic1 that were phosphorylated at different numbers of its nine CDK sites. This pool of phospho-Sic1 (2.5 ug) was incubated with 5 μg of WT or mutant Cdc4-GST-Skp1 as described above. Different phosphorylation states of Sic1 were separated by denaturing isoelectric focusing (IEF)-2D gel electrophoresis and visualized by anti-Sic1 Western blotting and ECL. IEF was performed using pH 3-10NL Immobiline gel strips and IPGphore IEF system (Amersham pharmacia).

[0434] Results

[0435] The x-ray crystal structure presented herein consists of a ternary complex of yeast Skp1 bound to a fragment of Cdc4, and a 9mer high affinity CPD phosphopeptide (FIG. 2). The Cdc4 fragment, which is deleted for terminal residues 1 to 262 and 745 to 779, extends from the beginning of the F-box domain to the end of the WD40 repeat domain.

[0436] Skp1-Cdc4 Fbox: Skp1 forms an elongated structure with a mixed α/β topology identical to that reported for human Skp1 (Schulman et al, 2000). The topology consists of a three-strand (denoted β1 to β3) β-sheet and eight α-helices, denoted α1 to α8 (FIG. 2a). The structure of Cdc4 from its amino terminus consists of an F-box domain, an α-helical extension or linker, and a WD40 repeat domain (FIG. 2a,b). The F-box domain comprises five a helices (denoted α0 to α4){tilde over (.)} This topology differs slightly from that reported for the F-box domain of hSkp2 (Schulman et al, 2000), which consists of a loop region L1 and three helices denoted α1 to α3. Helix α0 in Cdc4 corresponds most closely in sequence and position to the loop region L1 of Skp2 while a half turn remnant of helix α4 is discernable in the transition sequence between the Skp2 F-box and Leucine Repeat domains. As observed in the Skp1-Skp2 complex, Skp1 and the F-box domain of Cdc4 associate by the interdigiation of helixes α0 to α3 of Cdc4 with helices α5 to α8 of Skp1. This mode of inter-domain association is characterized by a common and continuous hydrophobic core that spans the two protein domains.

[0437] Cdc4 helical linker and WD40 domain: Following the F-box domain of Cdc4 is a helical extension that forms a structured bridge to the WD40 repeat domain. The helical extension consists of two α-helices α5 and α6 that together with helices α3 and α4 of the F-box domain form a stalk and pedestal like structure that connects and orients the WD40 domain (FIG. 2c).

[0438] Eight copies of the WD40 repeat motif in Cdc4 form an 8 blade β-propeller structure. Each blade, composed of 4 anti-parallel β-strands, is related by 8-fold pseudo symmetry about a central axis (FIG. 2b). As first shown for G-protein gamma subunit (Sondek 1996), the WD40 repeat motif of approximately 40 amino acids composes the outer β-strand of one propeller blade and the inner three strands of the adjacent blade. A continuous circular arrangement of blades is formed by the association of the first and last WD40 repeat motifs to form the 8th propeller blade. Interestingly, a 7 β-propeller blade structure was anticipated for Cdc4 and its orthologues (and generally all WD40 repeat F-box adaptors), which is attributable in part to the cryptic nature of the 8th WD40 repeat motif (FIG. 1). Based on the structure based sequence alignment in FIG. 1, it is predicted that the other WD40 class of F-box adaptor proteins (i.e. the Met30 orthologues and βTRCP orthologues) will form 7-blade β-propeller structures.

[0439] The WD40 repeat domain forms a disk like structure characterized by a cavity in the middle and two opposing circular surfaces of slightly different size. The smaller of the two surfaces composes the CPD binding site. On the bottom surface is anchored helix α6 of the helical extension, which inserts obliquely between propeller blades β7 and β8. Interestingly, β-propeller blade 2 consists of 5 β-strands. The outermost strand of this blade, denoted β91, is non-standard and arises from an amino acid insert in the connecting loop between α-strands 12 and 13. Strand β91, forms a parallel arrangement with strand β9, which differs from the anti parallel architecture of all other 1-strand elements in the WD40 domain structure. A large insert in the β12-β13 linker is absent from dr, ce, hu, mu Cdc4 homologues suggesting that a 5 {tilde over (β)} strand propeller blade 2 is unique to the fungal homologues.

[0440] A fixed orientation between the F-box domain and WD40 domain of Cdc4 is maintained largely through the integrity of the stalk like helix α6 of the helical extension (FIG. 2c). Helix α6 is 30 Å in length, and is anchored at its N-terminus to the hydrophobic core of the F-box/helical extension and at its C-terminus to the hydrophobic core of the WD40 repeat domain. In contrast to the intermolecular connection between Skp1 and the F-box domain, the connection between the F-box domain and WD40 repeat domain appears less rigidly structured.

[0441] At its amino terminus, helix α6 anchors to the F-box through hydrophobic interactions involving α6 residues Phe 355 and Leu 356 and F-box residues Ile 295, and Ile 296, Leu 315, Trp 316, and Leu 319 (FIG. 2c). Helix α5 packs along side the base of helix α6 opposite to the F-box domain through hydrophobic packing interactions involving Tyr342, Leu 338 and Leu 334. At its C-terminus, helix α6 anchors through hydrophobic interactions involving residues Trp 365 and Ile 364 with WD repeat residues Val 687, Ile 696, Leu 726 and Phe 743 in β-propeller blades 7 and 8. Asn 364 of helix α6 also forms a tight hydrogen bond interaction with the backbone carbonyl group of Phe 743 in propeller blade 8. The noted interactions (with the exception of interactions involving helix α5) involve residues that are conserved across most WD40 F-box adaptor proteins including the Met30 orthologues and β-TRCP orthologues, which suggests that the linkage between WD40 and F-box domains are similarly structured in these proteins. Helix α6 in β-TRCP, however, appears to be one α-helical turn longer (FIG. 1).

[0442] Outside of stalk helix α6, only two close contacts (<3.5 Å) are observed between the WD40 repeat domain and other regions of Cdc4. These contacts consist of hydrogen bonds between Asn684 and Arg700 in the loop regions of propeller blade 7 with Glu 323 in the α4-α5 linker of the helical extension. Both, hydrogen bonds are maintained in the two Cdc4 molecules of the crystal asymmetric unit but all three residues are poorly conserved amongst Cdc4 orthologues (FIG. 1). The lack of additional stabilizing interactions suggests that the F-box/WD40 domain linkage is not exceedingly rigid, and indeed, the WD40 domain in the two molecules of the asymmetric unit differ relative to their F-box domains by a 5 degree rotation about helix α6.

[0443] WD40 domain phosphopeptide recognition: A nine-mer CPD consisting of the sequence acetyl-Gly,Leu,Leu,pThr,Pro,Pro,Gln,Ser,Gly-amide [SEQ ID NO.40] is bound to the front face of the WD40 domain of Cdc4. In the two WD40 repeat domain/CPD complexes of the crystal asymmetric unit, a central core of 4 CPD residues corresponding to the sequence Leu, pThr, Pro, Pro [SEQ ID NO.41] is well ordered.

[0444] These residues have been modeled unambiguously in unbiased experimental electron density maps (FIG. 3e). Interpretable electron density is also apparent for the P−2 Leu, P−3 Gly, P+3 Gln, P+4 Ser, and P+5Gly positions of the second CPD (no interpretable electron density is apparent for these residues in the first CPD). The CPD binds in an extended manner across β-propeller blade 2 with the N-terminus oriented towards the central cavity of the WD40 repeat domain and the C-terminus oriented towards the outer rim. The CPD binding surface of Cdc4 is composed of invariant and highly conserved residues from β-propeller blades 1 to 6 and 8 and represents the most conserved part of the WD40 repeat domain surface (FIG. 3a,c).

[0445] Cdc4 displays an absolute requirement for phosphorylation at Ser or Thr at the P−0 position of the CPD. In the crystal structure, the P0 pThr phosphate group is coordinated by an intricate network of electrostatic interactions and hydrogen bonds involving residues absolutely conserved across all Cdc4 orthologues (FIG. 3c). The P0 phosphate group forms direct electrostatic interactions with the guanidinium groups of Arg 485, Arg 467, and Arg 534 and a direct hydrogen bond with the side chain of Tyr 548. The side chain of Tyr 548 is coordinated by stacking interactions with the guanidinium group of Arg 572, which in turn is coordinated by a hydrogen bond to the side chain of Tyr 574. Although Cdc4 shows a strong (6 fold) preference for pThr over pSer, the structural basis for this selectivity is not obvious. In the crystal structure, the Cy methyl group of Thr is directed towards solvent and does not make contact with the CPD binding surface of Cdc4. This binding preference may be due to the greater side chain rotational stability arising from the Thr β-branch structure.

[0446] Cdc4 displays an absolute requirement for proline in the p+1 CPD position. In the crystal structure, the P+1 proline side chain projects into a three-sided pocket on the CPD binding surface. The side chain of Trp 426 forms one side of the pocket and packs in a coplanar manner with the P+1 proline side chain. On its other side, the Trp 426 side chain packs tightly against the side chain of Thr 386. The opposite side of the P+1 binding pocket is formed by the side chain of Arg 485. Arg 485 coordinates the P+1 Proline through van der Wals side chain interactions and through a direct hydrogen bond to the Proline backbone carbonyl group. This represents the sole direct hydrogen bond interaction between Cdc4 and the CPD main chain. The side chains of Thr 441 and Thr 465 define the remaining side of the P+1 Proline binding pocket, with the Cy side chain groups composing a hydrophobic surface. The hydroxyl groups of Thr 441 and 465 orient away from the P+1 binding pocket, where they are well placed to influence binding specificity for CPD residues C-terminal to the P+1 position. Unlike Trp 426, Thr 386 and Arg 485, which are invariant amongst the Cdc4 orthologues, Thr 441 and Thr 465 are substituted with Ile in the S. pombe Cdc4 orthologue Pop1. The modeling studies suggest that this substitution has no effect on the P+1 binding pocket but may perturb CPD binding specificity C-terminal to the P+1 positions through steric effects (Ile is bigger than Thr) and by increasing the hydrophobic character of the surface.

[0447] Cdc4 displays a strong preference for the hydrophobic residues Leu, Ile and Proline at the P−1 and P−2 CPD positions. In the crystal structure, the P−1 Leucine side-chain is oriented towards a hydrophobic pocket composed of invariant residues Trp 426, Trp 717, and Thr 386, and the conserved hydrophobic residue Val 384. While less precisely modeled, the main chain position of Leu+2 lies in close proximity to a third hydrophobic pocket composed of the invariant residue Tyr574, and the conserved hydrophobic residues Met 590 and Leu634.

[0448] Cdc4 displays little preference for residues in the P+2 to P+5 CPD positions. In the crystal structure, the side chain of P+2 Pro is directed towards solvent (which would account for the lack of selectivity at this position), while the main chain conformation of Pro+1 and Pro+2, causes the CPD to kink away from the peptide-binding surface from the Pro+2 position onwards. As a result, only one additional close contact with Cdc4 is made by the CPD following the Pro+1 position, which consists of a weak hydrogen bond (sub-optimal geometry) between the P+4 Gln side chain and the side chain of Arg 485.

[0449] Adjacent to the P+1 proline binding pocket, Ser 464, Thr 441 and Thr 465 are well placed to exert specificity for the +3 and +4 CPD positions if an extended rather than kinked conformation of the CPD were adopted. As noted, Thr 441 and 465 are substituted with Ile in the Cdc4 orthologue pop1 in S. pombe. While nothing is known about the effect of this substitution on CPD recognition, it is predicted that this could have some effect on substrate selectivity for the P+2 to P+5 CPD positions.

[0450] Cdc4 displays strong selectivity against Arginine and Lysine in positions −2, −1, +2, +3 and +4. This selectivity may be due to electrostatic repulsion generated by the invariant Cdc4 residues Argininc 572, 534, 467, 485 and 443, which dominate the local electrostatic character of the CPD binding site. Lys 402 is also well placed to contribute to repulsive effects but this position is not conserved amongst the Cdc4 orthologues. The selectivity against positively charged residues in the P−2 to P−1 CPD positions can also be reconciled in part by the hydrophobic nature of the P−1 and P−2 binding pockets and indeed, oppositely charged Glu and Asp residues are also disfavored at these CPD positions.

[0451] Comparison with Skp1-Skp2 Complex:

[0452] Skp2 is a representative member of a second class of F-box adaptor proteins, which possesses a leucine repeat domain in place of the WD40 repeat of Cdc4. In addition to providing a first structural view of a Skp1 homologue and an F-box domain, the structure of the Skp1/Skp2 complex revealed a mode of molecular association predicted to be employed by all Skp1/F-box homologues. The Cdc4/Skp1/CPD structure confirms the fold of the individual Skp1 and F-box domains and their mode of association. Superposition of yeast and h Skp1 strands β1-β3 and helices α1 to α7 (RMSD Cα=0.74 Å) reveals a close correspondence between F-box helixes α1 to α3 with only Skp1 helix α8 and F-box helix α4 showing significant deviations between the two structures. In addition, only the first half of helix α8 is ordered in ySkp1 and only ha half turn fragment of the F-box helix α4 is apparent in Skp2. The differences in positions and lengths of F-box helices α4 and Skp1 helices α8 reflects the different roles these secondary structure elements play in the linkage between their respective F-box and ligand binding domains.

[0453] The structure of the Skp1/Skp2 complex revealed a solid/substantial linkage between its Leucine Repeat and the F-box domains, a feature predicted to be shared by all Skp2 F-box orthologues. In Skp2, the F-box domain helix α4 terminates abruptly and without an appreciable linker, makes an immediate transition to the Leu Repeat domain fold This linkage is enhanced by a β-strand projecting back from C-terminus of the Leu repeat domain and helix α8 projecting forward from Skp1. The sum of linker region interactions compose a local hydrophobic network that links the hydrophobic cores of the F-box domain with that of the LRR domain. This contrast sharply with the corresponding linkage of Cdc4, which is composes primarily by a lengthy inter-domain linker (the helical extension) and which lacks significant involvement of Skp1 or the WD40 repeat domain for stabilization.

[0454] Although the Skp2 and Cdc4 F-box adaptor proteins employ structurally divergent ligand binding domains, the general position of the WD40 and LLR domains are surprisingly similar. The precise ligand-binding site on Skp2 has not been determined but mutagenesis sties on the Skp2 orthologue in Met30 have mapped the ligated binding site to the inner side of the curved surface. If the Skp2 binding site is inferred from the overlap with the Cdc4 CPD binding site, the CPD site would map to the lateral side of the Leu repeat domain.

[0455] Model of the SCFCdc4 E2 Complex

[0456] The structure of Cdc4 bound to substrate provides a missing piece of the larger SCF structural puzzle and sheds light on how substrate is presented for ubiqutination. A complete model of the SCFCdc4-E2-substrate complex consisting of an E2, a cullin, a ring finger domain, an F-box adaptor, Skp1, and CPD has been constructed using the structures of individual component proteins and/or larger assemblies determined previously (FIG. 4). Two interesting features are apparent. Firstly, a separation distance between the E2 active site cysteine and the peptide-binding site of Cdc4 is very large at 64 Å and second Cdc4 presents the CPD peptide with a direct line of sight to the E2.

[0457] Mutational Analysis of CPD Binding Surface

[0458] In order to probe the functional importance of amino acid residues on the highly conserved peptide binding surface, a panel of Cdc4 mutants (both single and double mutant) were generated and tested each for its ability to bind phospho Sic1 and Skp1 in vitro using a pull down assay and for its ability to substitute for wt-cdc4 in vivo using a cell viability assay. Of 12 single site mutants tested, only Arg 467. Arg485Ala Arg534Ala, and Trp 426 abolished both cell viability in vivo and phosphoSic1 binding in vitro. Together, these residues compose most of the interaction surface with the pThr, Pro CPD core. Interestingly, Tyr 548, the only other amino acid on the surface of CDC4 to directly contact P0 phosphate group, is fractional in vivo but is compromised for CPD binding in vitro. Mutation of the adjacent residue Arg572 to Ala shows the same behavior. For the Arg572 mutation, the inablity to bind psic1 in vitro appears due to its tendency to aggregation. Presumably in the context of the full SCF complex in vivo this mutant is sufficiently well behaved to bind phospho Sic1.

[0459] All other single site mutants including Arg443Ala, Lys402Ala, Tyr574Ala, Trp717, Val384, and the double site mutant Thr441/465IIe, K404D/R443D and V384N/W717N are viable when expressed in the cdc4 delete and are fully competent for phosphoSic1 binding in vitro.

[0460] Since the cell viability assay nay be masking subtle functional roles for the conserved Cdc4 residues, function was assayed in vivo under more stringent conditions in which Sic1 wt or the stabilized mutants, Sic1 (T33V) or Sic1(T45A) are over-expressed under a galactose promoter. This should amplify defects in cdc4 function. Under these conditions, Trp 717, Tyr 548 and the double mutant K404D/R443D are lethal showing that these residues are in fact important for functions

[0461] Role of the Stem and Pedestal Structure

[0462] To probe the role of the F-box WD40 inter-domain linker, point mutations, insertions or deletions were introduced into the stem and pedestal structure of Cdc4 and protein function was assessed as performed for the peptide binding site mutants.

[0463] Deletion of helix α5 or introduction of Proline and Glycine helix destabilizing residues within the helix had no effect n Cdc4 function both in vitro and in vivo. This result is consistent with the poorly conserved nature f helix α5 and its flanking linker regions. Helix 5 appears entirely absent from human, mouse and drosophila homologues and helix destabilizing substitutions in helix 5 incorporating glycine and proline, are observed in the worm and fungal homologues (FIG. 1). A more invasive deletion of helix 5 that deletes part of the linkers to helix 4 and helix 6 was inviable in yeast. This mutant is properly folded as evidence by the finding that the protein can bind both Skp1 and phospho Sic 1 in vitro. This mutation should likely disrupt the positioning of helix 6 relative to the fbox domain (the linker is too short to span the two secondary structure elements).

[0464] The introduction of helix destabilizing residues in helix α6 or the lengthening of the helix by the insertion of one, two, three, four, 8 or 12 amino acid residues also disrupted protein function in vivo, without while maintaining the ability of Cdc4 to to bind pSic1 and Skp1. These results are consistent with a possible role for helix 6 in presenting bound substrates in a specific geometric orientation.

[0465] It is peculiar that such a spindly structure is sufficient to maintain rigidity. Perhaps in the context of the dimer, additional contacts help to stabilize position of the WD repeats with respect to the other part of the protein Indeed, the N terminal dimerization domain is required for function. Or perhaps a modicum of flexibility is important for the catalytic mechanism.

[0466] Probing Substrate Selectivity Against Positively Charged Residues

[0467] Cdc4 bind Sic1 in a multi site dependent manner. Each of the phosphorylation sites in Sic1 are sub-optimal in isolation but series of 5 to 7, they work coopertively to bind to Cdc4 through an avidity effect. Part of the subs optimal character of the sites is due to the presence of Lysine in the +2 to +5 positions. From the crystal structure, the selectivity against positive residues appear to arise from electrostatic replusion from highly conserved residues on the CPD binding surface of Cdc4. To test this hypothesis, two residues not directly involved in phosphopeptide binding were mutated and then the multi site requirement for phosphoSic1 binding was evaluated (FIG. 5c).

[0468] Using an IEF pull down assay, wild type Cdc4 is shown to selectively binds to the 5,6 and 7 site phosphorylated phosphoSic1 from a pool of single to 9 site phosphorylated forms. In contrast, the double mutant binds to 3,4,5,6,7 site phosphorylated forms of Sic1 (FIG. 5a). This supports the notion of selectivity and the basis for avidity that may be important for setting sensitive threshold for cell cycle progression (FIG. 5b). The same effect was observed for a double mutant.

[0469] Cancer Causing Mutations in Drosophila and Human Cdc4

[0470] Mutations in human and fly orthologues of yCdc4 give rise to cancers (see Table below). All mis-sense mutations map to the WD40 CPD binding domain and either have been demonstrated or are predicted to perturb CPD binding function. In previous studies, two cancer cell lines tested positive for mutations at Arginine 534 and Arg 467 (Arg 534 and Arg 467 in yCdc4). In the crystal structure, these residues make a direct binding interaction with the P0 phospho group and our mutational analysis demonstrates an absolute requirement of these residues for CPD binding. In another study, two entrometrial cancerous tissue samples tested positive for mutations equivalent to Arg467 and Arg 485 in yCdc4. As f r the tumor cell line mutations, these mutations affect key residues required for CPD recognition.

[0471] Two mutations characterized in drosophila cancer include Ala118Val and Gly1132Glu, corresponding to yCdc4 positions Ser532 and Gly546 respectively. The first of these mutations, involve the substitution of a small Ala/Ser residue with a bulkier b-branched Valine residue. This may compromise CPD binding function through steric effects on the position of Arg434, Arg467, Arg534 triad. In the crystal structure, Ala/Ser is positioned centrally amongst the triad. The second drosophila mutation, Gly1132Glu, maps to β-strand 15 of propeller blade 4 in yCdc4. This position is within the core of the protein and mutation here likely acts by disrupting the overall WD40 domain fold or through local perturbations of structure that indirectly affect the phosphate binding pocket. Glycine in this position of the WD40 repeat motif is highly conserved. The temperature sensitive alleles previously characterized including Gly398Glu in propeller blade 1 and Ser438Asn in propeller blade 2 likely act by disrupting the fold in a similar manner to disrupt the overall WD fold. These are more distantly located from the CPD binding pocket.

[0472] Cancer Mutations

1H-cell linesDrosophilaEntrometrialOrlickyRosamondArg534(425)LeuSer/Ala532(1118)ValArg467(465)HisArg534AlaGly398GlnArg 467(385)CysGly546(1132)GluArg485(479)GlnArg467AlaSer438AsnArg485AlaTrp426Ala

[0473] Discussion

[0474] Recognition of Phosphorylated Substrates by the Ubiquitin System

[0475] Substrate selection by Cdc4. The structure of the Skp1-Cdc4-CPD complex reveals the basis for phosphorylation-dependent recognition, the specificity of which is governed by three primary determinants. The substrate phospho-threonine is locked in place by direct contacts with three conserved and essential Arg residues. The preference for hydrophobic residues at the P−1 position (and perhaps P−2 position) is enforced by a hydrophobic pocket that lines the center of the WD40 propeller. Finally, the bias against basic residues at P+2 to P+5 is established by two conserved Arg residues positioned on the top of the propeller directly in-line with the axis of the bound peptide. These conclusions are supported by mutagenesis of key residues in Cdc4 and by structure-based engineering of Cdc4 to accept sub-optimal CPD sequences.

[0476] The construction of the Cdc4 phospho-peptide binding module differs from that of known phospho-Ser/Thr binding modules in an important respect. Known phospho-recognition domains, such as 14-3-3, WW and FHA domains appear to be composed of a series of dedicated interaction sites, each of which contributes incrementally to the overall binding interaction (Yaffe and Elia, 2001). The Cdc4-substrate interaction is dominated by extensively coordinated phospho-Thr and Pro residues, as well as by a striking positive electrostatic potential around the binding site. The hydrophobic pocket that selects residues in the P−2 and P−1 positions also contributes to binding affinity. In contrast to other phospho-recognition modules, however, the strong binding of the phosphorylated residue is partially offset by specific selection against basic residues in the substrate peptide, through electrostatic repulsion from a basic patch downstream of the phosphate binding pocket. These features allow the binding affinity for any given peptide to be precisely tuned. Thus, all of the natural CPD motifs in Sic1 are sub-optimal in one or more respects; indeed only peptides derived from the T45 site exhibit any detectable interaction with Cdc4 (Nash et al., 2001). These features establish a requirement for substrate phosphorylation on multiple sites, which mediate a high affinity interaction in a manner that depends cooperatively on the number of phosphorylated residues.

[0477] In the case of wild type Sic1, at least six sites must be phosphorylated for high affinity binding by Cdc4. As shown here, mutation of the basic selection residues shifts the binding equilibrium to lower phosphorylated forms while in previous studies, it was demonstrated that introduction of a single optimal CPD into Sic1 causes premature Sic1 degradation and genome stability (Nash et al., 2001). An advantage of this system is that not only can the affinity of individual sites be tuned over a broad range, but the number and spacing of sites can be readily varied to establish a threshold for the targeting kinase. Thus Cdc4 is able to target numerous critical factors for phosphorylation-dependent degradation, including the Cdk inhibitor Sic1, the polarization factor Far1, the replication initiator Cdc6 and the transcription factor Gcn4, all of which may be controlled with different kinetics and different phosphorylation thresholds (Deshaies, 1999). These properties distinguish Cdc4 from other known phospho-peptide binding modules that typically interact with dedicated sites on their substrates through a single high affinity interaction (Pawson and Nash, 2000; Yaffe and Elia, 2001).

[0478] The mechanism that engenders a cooperative binding effect remains to be determined. In principle, multiple interactions sites might increase binding either by engaging more than one binding site on Cdc4, or by decreasing the probability of dissociation from Cdc4 (Deshaies and Ferrell, 2001; Harper, 2002; Nash et al., 2001). Cooperative interactions for the dual SH2 domain phosphatase SH-PTP2 and 14-3-3% rely on two substrate binding sites for high affinity recognition of bivalent ligands (Eck et al., 1996; Yaffe et al., 1997). Notably though, inspection of the WD40 surface does not reveal any other potential ligand binding pockets or grooves that might accommodate a phosphorylated peptide motif. Although secondary weak phospho-dependent interactions might occur, it is not obvious from the structure where such putative secondary sites might be located. In favor of the probabilistic cooperativity effect, mathematical modeling suggests that cooperative behaviour arises for the interaction between a single binding site and a polyvalent ligand as a function of the number of ligand sites. In effect multiple ligand sites increase the local concentration of ligand beyond a diffusion limited threshold for escape from the receptor. In the absence of candidate secondary sites, the simplest model is favored in which Cdc4 contains only a single phospho-dependent binding site.

[0479] Comparison to other phospho-peptide binding domains. The structure of the Cdc4 WD40 domain provides direct evidence that WD40-type repeats can assemble into propellers with more than seven blades (Fulop and Jones, 1999). One consequence of the additional blade is an enlarged channel through the center of the propeller, which creates a wide binding pocket that accommodates the core Leu-pThr-Pro ligand. This pocket contrasts to all other phospho-Ser/Thr binding domains, which engage their ligand through more shallow surface contacts within loops that extend from the core domain. WD40 domains are known to interact with other proteins in at least two different modes. In the Gb transducin and TUP1 WD40 domains, the protein interaction region occurs across the top of the propeller, much as in the case of Cdc4 (Sprague et al., 2000; Wall et al., 1995). In a second mode, defined for the WD40 domain of clathrin and the b-arrestin peptide, a “peptide-in-groove” interaction occurs on the bottom edge of the propeller between the b-strands of the second blade (ter Haar et al., 2000). Modeling of b-TrCP, which binds the consensus motif DpSGXXpS [SEQ ID NO.42] in IkBa, b-catenin, and Vpu (Yaffe and Elia, 2001), suggests that an extensive basic region on the top of the propeller will engage substrate peptides in an analogous manner to Cdc4.

[0480] Spatial orientation of SCF substrates. A conserved feature between all E3 structures solved to date is the large distance between the substrate binding site and the catalytic site (Huang et al., 1999; Zheng et al., 2002; Zheng et al., 2000). Modeling of the Skp1-Cdc4 complex onto a model of the Skp1-Cull-Rbx1-E2 complex suggests that the substrate is positioned for direct frontal attack by the E2 catalytic site but that a gap of some about 65 Å must be bridged between the two sites, presumably by the substrate polypeptide. Unexpectedly, superposition of the WD40 domain of Cdc4 with the LRR of Skp2 does not align the defined phosphopeptide binding pocket of Cdc4 with a potential phospho-recognition site of on the concave face of the LRR repeats (Zheng et al., 2002), at least as defined by mutational analysis of the related F-box protein Grr1 in yeast (Hsiung et al., 2001). If the relative position of substrates in the WD40 versus LRR class of F-box proteins differs, spatial plasticity in substrate presentation must be possible. This notion is consistent with the fact that the HIV protein Vpu is able to redirect the specificity of the F-box protein b-TrCP by bridging bTrCP to the host cell protein CD4, in a manner that depends on phospho-dependent recognition of Vpu by b-TrCP (Margottin et al., 1998). Similarly, it is possible to create synthetic adapters that bridge the substrate recognition site of an F-box protein to an ectopic substrate (Sakamoto et al., 2001). Finally, by definition all E3s must able to accommodate the substrate and the elongating ubiquitin chain generated by repeated catalytic cycles (Pickart, 2001). All of these points argue for considerable spatial leeway, and possibly flexibility of F-box protein orientations within the SCF catalytic cavity.

[0481] Based on the extensive Skp1-Skp2 interface, and on the inactivation of Cul1 by insertion of a flexible linker, it has been proposed that SCF complexes, and perhaps E3 enzymes in general, must present substrates to the catalytic site in a rigidly defined fashion (Zheng et al., 2002). However, the WD40 domain and the F-box of Cdc4 are linked only by a single α-helical stalk, with additional surface contact between the domains, all of which is mediated by non-conserved residues. It is thus somewhat difficult to reconcile the properties of the two F-box protein structures solved to date. Although it may be that regions truncated from Cdc4 to enable crystallization may normally help stabilize the interface, none of these regions are highly conserved between closely related Cdc4 family members. Perturbation of the rotational and translational position of the WD40 domain by introduction of additional residues into the stalk abrogates function in all cases, except for a long insertion of 12 residues. The fact that this gross structural change can be tolerated implies a degree of comformational plasticity with the catalytic cradle. This plasticity may facilitate the access of multiple ubiquitination sites within Sic1 to the catalytic center, as directed by the multiple low affinity CPD motifs in Sic1.

[0482] Insights into substrate recognition by human Cdc4. In metazoans, Cdc4 targets multiple critical regulators of cell division and development. Among these, cyclin E is a crucial substrate because its abundance must be strictly controlled in order to avoid precocious S phase entry and attendant genome instability (Spruck et al., 1999). Notably, it has been recently reported that mutational inactivation of hCDC4 occurs in several cancer cell lines that exhibit high levels of cyclin E (Moberg et al., 2001; Strohmaier et al., 2001). In addition, hCDC4 may be mutated in up to 30% of endometrial cancers (Spruck et al., 2002). Quite strikingly, known cancer associated mutations in hCDC4 alter phospho Thr-binding residues. Given the probable requirement for homodimerization in active SCF complexes (Kominami et al., 1998; Suzuki et al., 2000), such mutations might be expected to acts in a partial dominant negative manner. Other critical substrates that appear to bind Cdc4 in a phosphorylation dependent manner include SEL-10, a negative regulator of the LIN-12/Notch pathway (Hubbard et al., 1997) that targets the transcriptionally active Notch intracellular domain for degradation (Gupta-Rossi et al., 2002; Wu et al., 2001) and the presenilins, dominant mutations in which predispose to familial early onset Alzheimer's disease (Selkoe, 2001; Wu et al., 1998). Mutations that interfere with hCdc4 activity may therefore compound multiple disease phenotypes.

[0483] Yeast and human Cdc4 exhibit a high degree of structural similarity, especially in the critical substrate binding region, and moreover, Cdc4 family members are functionally conserved since the hCdc4 substrate cyclin E is efficiently degraded in yeast in a CDC4-dependent manner (Koepp et al., 2001; Nash et al., 2001; Strohmaier et al., 2001). The structure of yeast Cdc4 thus affords insights for rational drug design. Significantly, the low affinity of individual natural CDP sites that engender the requirement for multisite phosphorylation means that even compounds of moderate affinity can readily out-compete the binding of fully phosphorylated substrates (Nash et al., 2001). Naively, inhibition of hCdc4-substrate interactions would be expected to exacerbate the deregulated proliferation caused by stabilization of cyclinE, Notch-IC or presenilin. However, if Cdc4 or Cdc4-like activities limiting for growth, Cdc4 antagonists may have heightened toxicity in cells that are hypomorphic for Cdc4 function. Alternatively, disruption of hCdc4 function may cause synthetic lethal effects in combination with otherwise non-lethal mutations in functionally overlapping pathways (Tong et al., 2001).

EXAMPLE 2

[0484] The following methods were used in the investigation described in the example: Protein expression and purification. The Cdc4 fragment employed for crystallization was deleted for residues 1-262, 602-605, 609-624, and 745-779 to remove loop regions based on sequence alignments and limited proteolysis of the intact SCFCdc4 complex. Skp1 was deleted for a non-conserved loop insertion spanning residues 37-64. A GSTSkp1-His6Cdc4 complex was co-expressed from plasmid pMT3169 in B934 (DE3) bacterial strain (Stratagene) cells grown in minimal media supplemented with a mixture of selenomethionine (40 μg/ml) and methionine (0.4 ug/ml) and purified by double affinity tag chromatography (Nash et al., 2001). All mutations were constructed by standard methods using oligonucleotides listed in Table 7 and sequence verified in their entirety. Mutants were sub-cloned into pMT3055 or pMT3217 for expression in bacteria or yeast, respectively, as listed in Table 8. The WD40 domain of the helix α6 linker mutants Ala1, Ala2, Ala12, and helix α6 breaker could not be stably expressed in bacteria; the Ala12 mutant also could not be expressed in yeast.

[0485] Crystallization, data collection, structure determination and modeling. Hanging drops containing 1 μl of 20 mg/ml protein and 1.2 molar equivalents of the cyclin E derived CPD peptide (acetyl-Gly-Leu-Leu-pThr-Pro-Pro-Gln-Ser-Gly-amide) [SEQ ID NO 40]in buffer (10 mM HEPES pH 7.5, 250 mM NaCl, 1 mM DTT) were mixed with equal volume of reservoir buffer (0.1 M Tris pH 8.5, 1.5 M ammonium sulphate). Crystals of the space group P32, (α=107.7 Å, b=107.7 Å, c=168.3 Å, α=γ=90°, β=120°), with two Cdc4-Skp1-CPD complexes in the asymmetric unit were obtained at 20° C. A Multiple Anomalous Dispersion (MAD) experiment was performed on a frozen crystal at the Advanced Photon Source (Argonne, Ill.) beamline BM 14-C and BM 14-D (λ1=0.9798 Å, λ2=0.9800 Å, λ3=0.9000 Å) using a Quantum 4 ADSC CCD detector. Data processing and reduction were carried out with the HKL program suite (Otwinowski and Minor, 1997). The programs SHARP (de La Fortelle and Bricogne, 1997) and SnB (Miller et al., 1994) were used in combination to locate and refine 19 of the total 22 selenium sites. Following phasing and density modification, a model was built using O (Jones et al., 1991) and refined to 2.7 Å resolution with NCS restraints using CNS (Brunger et al., 1998) to a working Rvalue of 23.8% and Rfree of 27.3%. Pertinent statistics for data collection and refinement are shown in Table 2. Amino acids 37-74, and 104-115 of Skp1 and amino acids 497-507 of Cdc4 were disordered and could not be modeled. 89.1% of the residues occupy the most favored regions of the Ramachandran plot, 10.8% the additional allowed region and 0.2% the generously allowed region.

[0486] Ribbons representations were generated using Ribbons (Carson, 1991), surface representations were generated using Grasp (Nicholls et al., 1991) and electron density maps were generated using O (Jones et al., 1991). A model of the ubiquitin-E2-SCFCdc4-CPD complex was generated by superposition of the Skp1 subunits of the Skp1-Cdc4-CPD structure and the Skp1-Cul1-Rbx1 structure (PDB ID 1LDK) (Zheng et al., 2002), the RING finger domains from Rbx1 in the same Skp1-Cul1-Rbx1 complex and from the Cb1 subunit of the Cb1-UbCH7 structure (PDB ID 1FBV) (Zheng et al., 2000), and the E2 subunits of the Cb1-UbCH7 structure and an NMR-based Ubc1-ubiquitin model (PDB ID 1FXT) (Hamilton et al., 2001). The Skp1, RING domain and E2 subunits overlapped with RMSD values of 1.01 Å, 2.09 Å, and 2.04 Å respectively.

[0487] Cdc4 functional assays. CDC4 mutant alleles were assessed for complementation of a cdc4A strain in a plasmid shuffle assay (Nash et al., 2001). Sensitivity to SIC1 dosage was determined by transformation with pMT837 (GAL1-SIC1) or pMT767 (GAL1-SIC1T33V) and plating on glucose medium or galactose medium. For in vitro capture of phospho-Sic1 by Cdc4, 0.5 μg of bacterially-expressed HIS6Sic1 was phosphorylated with immobilized Cln2-Cdc28 kinase from baculovirus-infected Sf9 cells and then incubated with 1 μg of immobilized wild type or mutant Cdc4263-744-GST-Skp1, at 4° C. for 1 hr, washed 4 times and visualized by anti-Sic1 immunoblot. For isoelectric focusing (IEF)-2D gel analyses, an evenly distributed pool of phospho-Sic1 isoforms was generated by combining different time points in a Sic1 phosphorylation reaction. 2.5 μg of the phospho-Sic1 pool was bound to 5 μg of immobilized wild type or mutant Cdc41-744-GST-Skp1. Captured isoforms were separated by denaturing IEF-2D gel electrophoresis using pH3-10NL Immobiline gel strips (Amersham) and visualized by anti-Sic1 immunoblot. Alternatively, the pool of phospho-Sic1 isoforms was incubated in solution with a ubiquitination reaction mix containing ATP, ubiquitin, yeast E1, Cdc34 and either wild type or mutant SCFCdc4 complex, composed of a 1:1 ratio of bacterial Cdc4-GST-Skp1 and insect cell-produced Cdc53-Rbx1, at 30° C. for 1 h as previously described (Nash et al., 2001).

[0488] Results

[0489] Alignment of Skp1 and Cdc4 homologs from various species and limited proteolysis of full length recombinant proteins were used to deduce loop regions in Saccharomyces cerevisiae Skp1 and Cdc4 that might interfere with protein crystallization (FIG. 1). Crystals of a ternary complex of ScSkp1 bound to ScCdc4 and a CPD phosphopeptide were obtained that diffracted to a resolution of 2.7 Å (Table 2). For Skp1, a non-essential loop spanning residues 37-64 was removed. The Cdc4 fragment used extends from residues 263 to 744, which encompasses the F-box motif to the end of the WD40 domain, and was engineered to remove two predicted loop regions (FIG. 1B). This Cdc4 construct lacks an essential ˜40 reside domain that precedes the F-box in different WD40 domain containing F-box protein family embers (Wolf et al, 1999). The high affinity CPD phosphopeptide corresponds to nine residues of human cyclin E, Gly-Leu-Leu-pThr-Pro-Pro-Gln-Ser-Gly, [SEQ ID NO. 40] which binds Cdc4 with a Kd of 1 μM (Nash et al., 2001).

[0490] The F-box interface. Yeast Skp1 forms an elongated structure with a mixed α/β topology identical to that reported for human Skp1 (Schulman et al., 2000) and consists of a three-strand β sheet, denoted β1 to β3, and eight α-helices, denoted α1 to α8 (FIG. 2A). The structure of Cdc4 consists of an F-box domain, an α-helical linker, and a WD40 domain (FIG. 2A,B,C). The F-box domain is comprised of five α helices, denoted α0 to α4. This topology differs slightly from that reported for the F-box domain of hSkp2, which consists of a loop region L1 and three helices denoted 1 to α3 (Schulman et al., 2000) Helix α0 in Cdc4 corresponds most closely in sequence and position to the loop region L1 of hSkp2 while a half turn ant of Cdc4 helix α4 is discernable in the transition sequence between the hSkp2 F-box and the LRR domain. As observed in the hSkp1-hSkp2 complex, ScSkp1 and the F-box domain of Cdc4 associate by interdigitation of helixes α0 to α3 Cdc4 with helices α5 to α8 of Skp1, with the interface itself comprised of an inter-protein 4-helix bundle. This mode of association gives rise to a contiguous hydrophobic core that spans Skp1 and the F-box domain of Cdc4. Superposition of the yeast and human structures reveals that Skp1 helix α8 and F-box helix α4 deviate significantly in that only the first half of helix α8 is ordered in ScSkp1 and only a half turn fragment of the F-box helix α4 is apparent in hSkp2 (FIG. 6A). The difference in position and length of F-box helix α4 and Skp1 helix α8 reflects the different roles these secondary structure elements play in the linkage between their respective F-box and ligand binding domains, as described below.

[0491] The WD40 domain. Eight copies of the WD40 repeat motif in Cdc4 form an 8 blade β-propeller structure (FIG. 6B). The WD40 repeat motif of approximately 40 residues composes the outer β-strand of one propeller blade and the inner three stands of the adjacent blade in a continuous circular arrangement (Fulop and Jones, 1999). The actual Cdc4 structure contrasts to the 7 blade β-propeller predicted for Cdc4 and its orthologs based on previously solved WD40 domain structures, all of which contain only 7 blades (Koepp et al., 2001; Nash et al., 2001). This discrepancy is attributable to the cryptic nature of the 8th WD40 repeat motif. Structure based sequence alignment suggests that the WD40 domains of the F-box proteins Met30 and β-TRCP will form canonical 7-blade β-propeller structures (FIG. 1B). A variant five β-strand structure occurs in blade 2, in which a large insert in tie β12-β13 linker allows the outermost β91 strand to run parallel to the β9 strand. This five strand composition is unique to the fungal Cdc4 orthologs. In terms of overall structural dimensions, the WD40 domain resembles a conical frustum of 40 Å diameter top surface and 50 Å bottom surface, an overall thickness of 30 Å and a central pore of 6 Å diameter. The CPD binding site resides on the top surface of the frustum and runs across the edge of the pore, while the bottom surface of the frustum links to the F-box domain.

[0492] The F-box to WD40 domain linker. The F-box domain of Cdc4 is followed by a helical extension that forms a structured bridge to the WD40 domain. The bridge consists of two α-helices, α5 and α6, that together with helices α3 and α4 of the F-box domain form a platform and stalk-like structure that positions the WD40 domain well away from the F-box domain (FIG. 2A,C). The relative orientation of the F-box domain and WD40 domain is imposed almost entirely through the integrity of the stalk-like helix α6, which is 30 Å in length. The N-terminal end of helix α6 is anchored into the hydrophobic core of the F-box domain through interactions involving α6 residues Phe 355 and Leu 356 and F-box residues Ile 295, and Ile 296, Leu 315, Trp 316, and Leu 319 (FIG. 2C). Helix α5 packs along side the base of helix α6 opposite to the F-box domain through hydrophobic interactions involving Tyr342, Leu 338 and Leu 334. The C-terminal end of helix α6 inserts obliquely between propeller blades α7 and α8 of the WD40 domain through van der Wals and hydrophobic interactions involving residues Trp 365 and Ile 361 with WD40 domain residues Val 687, Ile 696, Leu 726 and Phe 743 in propeller blades 7 and 8. Asn 364 of helix α6 also forms a tight hydrogen bond with the backbone carbonyl group of Phe 743 in propeller blade 8. The conservation of many of these residues, with the possible exception of those within helix α5, suggests that a structured linkage between the WD40 and F-box domains may be a common feature of the WD40 family F-box proteins.

[0493] The interdomain connection between the F-box and the WD40 domains of Cdc4 appears less rigidly structured than the corresponding region in hSkp2 (FIG. 6A). Outside of the stalk helix α6, only two close contacts (<3.5 Å) are observed between the WD40 domain and other regions of Cdc4 (FIG. 2C). These contacts consist of hydrogen bonds between Asn684 and Arg700 in two loop regions of propeller blade 7 with Glu 323 in the α4-α5 linker of the helical extension. Both hydrogen bonds are maintained in the two Cdc4 molecules of the crystal asymmetric unit but all three residues are poorly conserved amongst Cdc4 orthologues (FIG. 1B). The lack of additional stabilizing interactions suggests that the F-box to WD40 domain linker is not exceedingly rigid, and indeed, the WD40 domain in the two Cdc4 molecules of the crystal asymmetric unit differ relative to their F-box domains by a 5° rotation about the long axis of helix α6. In contrast, in hSkp2 the F-box domain helix α4 terminates abruptly in an immediate transition to the LRR domain fold such that the adjoined domains form a rigid hydrophobic core (Schulman et al., 2000). Although the Skp2 and Cdc4 families of F-box proteins employ structurally divergent F-box interfaces, the general position of the WD40 and LLR domains are nonetheless similar (FIG. 6A).

[0494] Model of the SCFCdCdc4E2 complex. The structure of the Skp1-Cdc4-CPD complex sheds light on how substrates are presented by the F-box protein to the E2 for ubiquitin transfer. A complete model of the E2-SCFCdc4-substrate complex consisting of ubiquitin, hUbc7, hCul1, hRbx1, ScCdc4, ScSkp1, and the CPD peptide is shown in FIG. 6B. This model is based on the reconstructed E2-SCFSkp2 complex derived by Pavletich and colleagues (Zheng et al., 2002), in conjunction with an NMR-based ubiquitin-E2 thioester model (Hamilton et al., 2001). Two interesting features are apparent. First, the distance between the E2 active site cysteine and the phosphate group of the bound CPD peptide is approximately 59 Å, which is similar to the spacing reported between the substrate interaction site and the E3 catalytic site in the hUbc7-Cb1 structure (Zheng et al., 2000). Secondly, the WD40 domain presents the CPD peptide in a direct line-of-sight to the E2. Although the ligand-binding site on hSkp2 has not been determined, mutagenesis studies on the LRR-containing F-box protein Grr1 in yeast suggest that substrates bind to the inner side of the curved repeat surface (Hsiung et al., 2001). If the position of this site is maintained in hSkp2, then the LRR domain of Skp2 is predicted to project substrates in an orthogonal direction to that of the Cdc4 WD40 domain (FIG. 6A).

[0495] Phosphopeptide recognition. The CPD binding surface represents the most conserved part of the WD40 repeat domain structure (FIG. 7A-D). The central CPD sequence Leu-pThr-Pro-Pro [SEQ ID NO. 41] was modeled unambiguously in unbiased experimental electron density maps in both Skp1-Cdc4-CPD complexes of the crystal asymmetric unit (FIG. 3). Interpretable electron density is also apparent for the P−2 Leu, P+3 Gln, P+4 Ser, and P+5 Gly positions, but only in one complex of the crystal asymmetric unit. The CPD peptide binds in an extended manner across β-propeller blade 2 with the N-terminus oriented towards the central pore of the WD40 domain and the C-terminus oriented towards the outer rim. Identical substrate peptide orientations and contacts were observed for an independent Skp1-Cdc4-CPD structure with a phosphopeptide derived from the transcription factor Gcn4, which is a physiological substrate of Cdc4 in yeast (Meimoun et al., 2000; Chi et al., 2001). However, of the Gcn4 peptide sequence, Phe-Leu-Pro-pThr-Pro-Val-Leu-Glu-Asp [SEQ ID NO. 43], only the core residues Pro-pThr-Pro had discernable electron density.

[0496] The CPD sequence requirements for the CPD-Cdc4 interaction are fully accounted for by structural elements in the WD40 domain. An absolute requirement for phosphorylation at Ser or Thr at the P−0 position of the CPD derives from a network of electrostatic interactions and hydrogen bonds that coordinate the P0 pThr phosphate group (FIG. 7C, D). This interaction is mediated by residues that are conserved across all Cdc4 orthologs (FIG. 1B). The P0 phosphate group forms direct electrostatic interactions with the guanidinium groups of Arg485, Arg467, and Arg534 and a direct hydrogen bond with the side chain of Tyr548. The side chain of Tyr548 is coordinated by stacking interactions with the guanidinium group of Arg572, which in turn is coordinated by a hydrogen bond to the side chain of Tyr574. Although Cdc4 shows a 6-fold preference for pThr over pSer (Nash et al., 2001), the structural basis for this selectivity is not obvious since the Cy methyl group of Thr is directed towards solvent and does not make contact with the WD40 domain surface.

[0497] A second absolute requirement for CPD-Cdc4 interaction rests on the P+1 proline, the side chain of which projects into a three-sided pocket on the WD40 surface. One side of this pocket is formed by the side chain of Trp 426, which packs in a coplanar manner with the P+1 proline side chain. The opposite side of this binding pocket is formed by the side chain of Arg 485 via coordination of the proline side chain and backbone carbonyl group through van der Waals and hydrogen bonding interactions, respectively. The side chains of Thr 441 and Thr 465 define the remaining side of the P+1 proline binding pocket, with Cy side chain groups composing a hydrophobic surface. The hydroxyl groups of Thr 441 and 465 orient away from the P+1 binding pocket, where they are well placed to influence binding specificity for CPD residues C-terminal to the P+1 position. Unlike Trp 426 and Arg 485, which are invariant amongst the Cdc4 orthologs, Thr 441 and Thr 465 are both substituted with lie in the S. pombe Cdc4 ortholog Pop1 (FIG. 1B). This substitution might restrict CPD sequences able to bind Pop1 through steric or hydrophobic constraints on residues C-terminal to the P+1 proline position.

[0498] Cdc4 displays a strong preference for the hydrophobic residues Leu/Ile/Pro at the P−1 and Leu/Ile at the P−2 CPD positions. In the crystal structure, the P−1 Leucine side-chain fits into a hydrophobic pocket composed of invariant residues Trp 426, Trp 717, and Thr 386, and the conserved hydrophobic residue Val 384. While less precisely modeled, the main chain position of Leu−2 lies in close proximity to a third hydrophobic pocket composed of the invariant residue Tyr574, and the conserved hydrophobic residues Met 590 and Leu634. The hydrophobic character of the P−1 and P−2 pockets is manifest as selection against both charged and small polar residues at these positions in the CPD consensus (Nash et al., 2001).

[0499] The WD40 phospho-recognition domain of Cdc4 is unusual in that it exhibits strong selectivity against either Arg or Lys residues in the P+2 to P+5 CPD positions, but otherwise shows no sequence preference at these positions (Nash et al., 2001). In the crystal structure, the side chain of P+2 Pro is directed towards solvent, while the main chain conformation of Pro+1 and Pro+2 causes the CPD to kink away from the peptide-binding surface from the Pro+2 position onward. As a result, only one additional contact with Cdc4 is made by the CPD following the Pro+1 position, namely a weak hydrogen bond with sub-optimal geometry between the P+4 Gin side chain and the side chain of Arg 485. Because the P+1 Pro main chain is forced away from the WD40 domain surface, the selection against basic residues in the P+2, +3, +4 and +5 positions in the CPD consensus is almost certainly due to through-space electrostatic repulsion. This effect arises from a dominant positive electrostatic potential generated by both the invariant triad of Arg residues that comprise the core pThr-Pro binding pocket, and by a radial extension of the surface due to Arg 572, Arg 443 and Lys 402, the former two of which are conserved amongst Cdc4 orthologs (FIG. 7B).

[0500] A number of natural mutations detected in metazoan orthologs of Cdc4 corroborate the structure-based analysis. Two ovarian cancer cell lines bear missense mutations at conserved Arg residues that correspond to Arg 467 and Arg 534 in yeast Cdc4 (Moberg et al., 2001). In the crystal structure, these residues make direct contact with the P0 phosphate group and are essential for function (FIG. 7C, D). In a recent study of human primary endometrial tumors, mutations in phosphate-binding Arg residues equivalent to Arg 467 and Arg 485 were detected in 2 of 13 tumor samples (Spruck et al., 2002). Other cancer-associated nonsense and frameshift mutations truncate hCdc4 within the WD40 domain (Moberg et al., 2001; Strohmaier et al., 2001; Spruck et al., 2002). Similarly, all three characterized mutations in the Drosophila ago gene that lead to excess cell proliferation affect the WD40 domain (Moberg et al., 2001). One of these mutations, Ala1118Val, corresponding to position SerS32 in ScCdc4 substitutes a conserved small residue with a bulkier residue at the center of the critical Arg 434-Arg467-Arg534 triad (FIG. 7C).

[0501] Mutational analysis of the F-box to WD40 domain linker. To probe the importance of orientation and rigidity in the F-box WD40 inter-domain linker, point mutations, insertions or deletions were introduced into the platform and stalk structure of Cdc4. None of these deletions affected the ability of the recombinant proteins to bind phospho-Sic1 in vitro or protein abundance in vivo (FIG. 8A and data not shown). Introduction of the helix destabilizing residues glycine and proline into helix α5 did not compromise Cdc4 function in vivo (FIG. 8B), consistent with the poorly conserved nature of this region (FIG. 1B). However, two different deletions of helix α5 eliminated Cdc4 function in vivo, indicating that the F-box-WD40 domain interface is an essential structural component. Similarly, placement of helix destabilizing residues at the center of helix α6 or the lengthening of this helix by the insertion of one, two, three, four, 8 or 12 amino acid residues disrupted Cdc4 function in vivo. Helix α6 is thus critical for productive orientation of the WD40 domain.

[0502] Mutational analysis of the CPD binding surface. Previous mutational analysis based on sequence conservation in the Cdc4 family identified Arg467, Arg485 and Arg534 as essential for substrate binding and function in yeast (Nash et al., 2001). Two of the three corresponding residues in hCdc4, Arg 417 and Arg 457, are essential for the binding of phospho-cyclin E, while the third corresponding to Arg485 was not tested (Koepp et al., 2001). To systematically probe the role of residues that form the highly conserved peptide binding surface, a panel of Cdc4 mutants was generated and each were tested for pSic1 binding in vitro, complementation of a cdc4A strain and sensitivity to increased SIC1 dosage. Four mutants, Arg467Ala, Arg485Ala, Arg534Ala, and Trp426Ala were unable to bind phospho-Sic1 in vitro or complement a cdc4A strain, but were fully competent for Skp1 binding (FIG. 8A, B). The essential function of these residues is not confined to elimination of Sic1 because none of the corresponding mutant alleles were able to rescue a cdc4Δ sic1Δ strain. These results reflect the critical structural role played by these residues in coordination of the P0 phosphate and the P+1 proline of the CPD. Mutation of the remaining phosphate-coordinating residue, Tyr548, did not cause loss of viability but did result in dosage sensitivity to SICThr33Val, which encodes a partially stabilized version of Sic1 (FIG. 8C). Mutation of Arg 572 had the same effect, as befits the observed stacking interaction between this residue and Tyr 548. Although both mutants were severely impaired for binding to phospho-Sic1 in vitro, this effect may be exacerbated by the tendency of these recombinant proteins to aggregate. In summary, the six residues that directly or indirectly coordinate the primary pThr-Pro core motif are critical for CPD recognition in vitro and Cdc4 function in vivo.

[0503] Disruption of residues that confer selection at the P−2, P−1 and P+2 to P+5 positions had only modest effects on the ability of Cdc4 to target pSic1. A Trp717Asn mutation predicted to disrupt the P−1 pocket conferred sensitivity to dosage of SIC1Thr33Val, but did not overtly affect the pSic1-Cdc4 interaction in vitro. Individual mutations in all other residues that are well positioned to affect substrate selection, namely Arg443Ala, Arg443Asp, Lys402Ala, Tyr574Phe and Val384Asn were indistinguishable from wild type in each of the assays used. Substrate selection residues on the WD40 surface thus contribute only modestly if at all to the essential function of Cdc4. As described below, however, these residues play a subtle but critical role in setting the phosphorylation threshold for the CPD-Cdc4 interaction.

[0504] Modulation of CPD substrate selectivity. A critical feature of the Sic1-Cdc4 interaction is the requirement for phosphorylation of Sic1 on multiple sites. To enforce this requirement, each of the phosphorylation sites in the native Sic1 sequence are sub-optimal in one or more respects (FIG. 9A). The Cdc4-CPD structure suggests that selectivity against basic residues may be due to electrostatic repulsion generated from the conserved patch of basic residues in and around the CPD binding pocket, while selection for hydrophobic residues arises from the P−1 pocket that is composed in part by Val 384 and Trp717. To examine the basis for selection against sub-optimal CPD motifs, the effects of mutations in non-essential residues in these two regions on the multisite phosphorylation requirement for Sic1 recognition were assessed.

[0505] The ability of Cdc4 to capture various phosphoisoforms of wild type Sic1 from a pool of recombinant Sic1 that had been phosphorylated to various extents by Cln2-Cdc28 was monitored. As resolved by isoelectric focusing, this pool contained roughly equal amounts of Sic1 phosphorylated on 1, 2, 3, 4, 5, 6, 7, 8 and 9 sites. Wild type Cdc4 was only able to capture Sic1 phosphorylated on six or more sites (FIG. 9B). This result formally demonstrates the transition in binding affinity between 5 and 6 phosphorylation sites, as initially inferred from capture of a series of Sic1 phosphorylation site mutants by Cdc4 (Nash et al., 2001). The role of positive electrostatic potential in selecting against sub-optimal CPD sequences with basic residues at C-terminal positions was tested with the Lys402Ala Arg443Asp double mutant. This mutant was able to select Sic1 phosphoisoforms that contained as few as three phosphorylation sites (FIG. 9B). The ability of the Lys402Ala Arg443Asp double mutant to capture lower phosphorylated forms of Sic1 is also evident in one-dimensional SDS-PAGE (FIG. 8A). Similarly, perturbation of the P−1 hydrophobic pocket with a Val384Asn Trp717Asn double mutation allowed capture of Sic1 phosphorylated on as few as four sites. These in vitro binding results were recapitulated in solution-based in vitro ubiquitination assays with wild type and mutant forms of Cdc4. Both double mutant forms of Cdc4 were able to convert Sic1 phosphoryated on four or five sites to oligo-ubiquitinated species, whereas wild type Cdc4 was unable to do so (FIG. 9C). The double mutants were, however, less efficient than wild type at elaborating fully ubiquitinated species of phospho-Sic1, perhaps because of protein stability effects or interference with catalytic steps after substrate binding. This interpretation is consistent with the sensitivity of strains bearing the double mutant alleles to SIC1Thr33Val dosage (FIG. 8B). Overall, re-engineering of negative selection residues in the Cdc4 WD40 domain supports the notion that the series of sub-optimal CPD motifs in Sic1 sets a high phosphorylation threshold for its recognition by Cdc4.

[0506] Discussion

[0507] The structure of the Skp1-Cdc4-CPD complex provides direct visualization of substrate orientation within an SCF complex. Insights gained from the structure include the unexpectedly frail interface between the F-box and the WD40 repeat domain, the basis for dedicated pThr-Pro dipeptide recognition by a novel eight-blade WD40 propeller, and a detailed understanding of the basis for selection against natural CPD sequences. The latter feature appears to be tailored to enforce multisite phosphorylation dependent degradation of Sic1, which in turn would help engender a highly cooperative onset of DNA replication (Nash et al., 2001). Similar principles may well operate for other Cdc4 substrates, including cyclin E, NotchIC and presenilin in mammalian cells (Strohmaier et al., 2001; Lai, 2002; Selkoe, 2001). Because yeast and human Cdc4 are structurally and functionally analogous (Nash et al., 2001; Strohmaier et al., 2001; Koepp et al., 2001), the structure of yeast Cdc4 affords obvious insights for pharmacological modulation of hCdc4 function in these pathways. Interestingly, a significant proportion of characterized human and fly CDC4 mutations alter residues in the CPD binding pocket. Given the probable requirement for homodimerization in active SCF complexes (Wolf et al., 1999), such mutations might act in a partial dominant negative manner to confer a growth advantage in the heterozygous state.

[0508] Phospho-recognition by Cdc4. The specificity of phosphorylation-dependent recognition by the WD40 domain of Cdc4 is governed by three main determinants: (i) a dedicated pThr-Pro binding pocket; (ii) a deep hydrophobic pocket that selects hydrophobic residues N-terminal to the phosphorylation site, and (iii) a through space electrostatic selection against basic residues C-terminal to the phosphorylation site. As for all documented phospho-dependent lipid/protein recognition modules, the Cdc4 WD40 domain employs arginine residues to directly contact the phosphate group of the ligand. However, unlike most domains in which adjacent residues impose subtle effects on specificity (Yaffe and Elia, 2001), the P+1 proline is an integral component of the core binding determinant (Nash et al., 2001). In the Cdc4-CPD co-crystal, ligand residues are locked in place by direct contact of the phosphate and proline carbonyl groups with three conserved and essential Arg residues, while the proline side chain inserts into a tight hydrophobic pocket formed by Trp426, Thr441, and Thr465. Because the phospho-binding pocket infrastructure has no obvious demarcation between the pThr and Pro binding sites, the Cdc4 WD40 domain is in effect a dedicated pThr-Pro binding module.

[0509] Comparison to other peptide recognition modules. Interesting parallels can be drawn between the Cdc4 WD40 domain, 14-3-3 domains and the class IV WW domains, which all have the ability to recognize phospho-Ser/Thr epitopes in the context of adjacent proline residues (Yaffe and Elia, 2001). The interaction of the Pin1 class IV WW domain with a pSer-Pro peptide differs from Cdc4 in that it does not rely on an extensive network of Arg residues for phosphate coordination (Verdecia et al., 2000). However, a striking similarity between Pin1 and Cdc4 lies in the P+1 proline binding pocket, which in both cases depend on a highly conserved tryptophan side chain to engage the P+1 proline pyrrolidine ring through a coplanar interaction. In contrast to Cdc4, Pin1 actually displays a preference for Arg in the P+2 position, such that the binding specificity of the pSer-Pro recognition domain closely matches that of the targeting CDK enzymes.

[0510] 14-3-3 domains bind pSer epitopes with a preference, but not an absolute requirement, for proline residues at the P+2 position (Yaffe et al., 1997). This less stringent selection arises because the 14-3-3 proline binding pocket is able to accommodate other residues with propensity to form β-turns. Interestingly, the proline preferences in both the 14-3-3 and Cdc4 WD40 domains give rise to the same qualitative effect: in each case the prolines terminate direct interactions between the peptide and the ligand binding domain by orienting the peptide away from the domain surface. In the case of Cdc4, biologically significant electrostatic effects operate in spite of the loss of direct peptide contact. Physiologically relevant substrate anti-selection mediated by charge repulsion is unique amongst known protein interaction modules.

[0511] The structure of the Cdc4 WD40 domain provides direct evidence that WD40-type repeats can assemble into propellers with more than seven blades (Fulop and Jones, 1999). WD40 domains are known to interact with other proteins in at least two different modes, either across the front face of the propeller, as in the case of Cdc4, or on the outer edge of the propeller as in the case of clathrin (ter Haar et al., 2000). Modeling of the F-box protein P-TrCP, which binds the doubly phosphorylated consensus motif DpSGXXpS [SEQ ID NO. 42] in IκβBβ-catenin, and Vpu (Yaffe and Elia, 2001), reveals an extensive conserved basic region on the front face of the propeller, which may engage substrate phosphoepitopes in an analogous manner to Cdc4.

[0512] Spatial orientation of SCF substrates. A conserved feature between all E3 structures solved to date is the substantial distance between the substrate binding site and the catalytic site (Huang et al., 1999; Zheng et al., 2000; Zheng et al., 2002). Superposition of the Skp1-Cdc4 complex onto a model of the Skp1-Cull-Rbx1-E2-ubiquitin complex suggests that the substrate is positioned for direct frontal attack by the E2 catalytic site, but that a gap of some 59 Å between the two sites must be bridged, presumably by the substrate polypeptide. The disordered structure of Sic1 lends itself to this possibility (Nash et al., 2001). Intriguingly, overlay of the WD40 domain of Cdc4 with the LRR of Skp2 does not align the defined phosphopeptide binding pocket of Cdc4 with a potential phospho-recognition site on the concave face of the LRR repeats (Zheng et al., 2002), at least as defined by mutational analysis of the related F-box protein Grr1 in yeast (Hsiung et al., 2001). If the relative position of substrates in the WD40 versus LRR class of F-box proteins do in fact differ, spatial leeway in substrate presentation must be possible.

[0513] Based on the extensive Skp1-Skp2 interface, and on the inactivation of Cull by insertion of a flexible linker, it has been proposed that SCF complexes, and perhaps E3 enzymes in general, must present substrates to the catalytic site in a rigidly defined fashion (Zheng et al., 2002). Unexpectedly, the WD40 domain and the F-box of Cdc4 are linked only by a single α-helical stalk, with very limited additional contacts. Despite the lack of sequence conservation in the a helix 6 structure that supports the WD40 domain, spatial constraints are nevertheless evident, as shown by the sensitivity of the structure to rotational and translational shifts caused by insertion of additional residues into the stalk. It is also possible that regions truncated from Cdc4 to enable crystallization may normally help stabilize the inter-domain interface.

[0514] Cooperativity in substrate selection by Cdc4. The properties of the Cdc4 phosphopeptide binding module differ from those of other known modules in the important respect that the interaction with core recognition elements is partially offset by specific selection against basic residues in the substrate peptide. This feature establishes an intrinsic antagonism between the recognition mechanism and the targeting CDK kinases, which prefer Ser/Thr-Pro sites with C-terminal basic residues (Endicott et al., 1999). Significantly, all of the natural CPD motifs in Sic1 contain one or more mismatches to the optimal CPD consensus. This system based on positive and negative ligand selection may not only set an elevated threshold for kinase activity, but may also allow the threshold to be precisely tuned for any given substrate by varying the number, spacing and properties of each site. Thus, Cdc4 is able to target numerous critical factors for phosphorylation-dependent degradation, including the Cdk inhibitor Sic1, the CDK inhibitor and polarization factor Far1, the replication initiator Cdc6 and the transcription factor Gcn4, all of which may be controlled with different kinetics and different phosphorylation thresholds (Patton et al., 1998). In one extreme, typified by Gcn4 and cyclin E, the substrate may contain a high affinity site that is augmented by several minor low affinity sites (Meimoun et al., 2000; Chi et al., 2001; Strohmaier et al., 2001). In the other, more akin to Sic1, a large number of weak sites may cooperate to drive high affinity binding only when a phosphorylation threshold is reached. As shown here, mutation of either the distal basic selection region or the P−1 pocket in Cdc4 shifts the binding equilibrium to lower phosphorylated forms of Sic1, which, in the absence of other structural effects that may compromise Cdc4, would be predicted to cause premature DNA replication and genome stability (Nash et al., 2001). These features distinguish Cdc4 from other known phospho-peptide binding modules characterized to date that typically interact with dedicated sites on their substrates through a single high affinity interaction.

[0515] The mechanism that underlies the cooperative binding transition of the phospho-Sic1-Cdc4 interaction between five and six phosphorylation sites remains to be determined. In principle, multiple interactions sites might increase binding by engaging more than one binding site on Cdc4 (FIG. 9D). This type of cooperative interaction is common in biological systems, as in the avidity of antibodies for polyvalent ligands and pathogen-host interactions (Mammen et al., 1998). Analogous cooperative binding interactions occur in signaling pathways. For instance, the dual SH2 domain phosphatase SH-PTP2 and the 14-3-3ζ protein both engage two substrate binding sites on their respective ligands (Eck et al., 1996; Yaffe et al., 1997). However, inspection of the Cdc4 WD40 domain surface does not reveal any obvious ligand binding sites that might accommodate a second phosphorylated peptide motif, nor is there any biochemical evidence for secondary binding sites (Nash et al., 2001). In addition, the wide range of substrates and site spacing accommodated by Cdc4, including random concatamers of synthetic CPD sites (Nash et al., 2001), is a priori difficult to explain by two or more fixed binding sites on Cdc4.

[0516] Instead, a model is favored that requires only a single phospho-dependent binding site on Cdc4 (FIG. 9D). In this scheme, phosphorylation of multiple CPD sites on Sic1 increases the local concentration of sites around Cdc4 once the first CPD site is bound, to the point where diffusion limited escape from the receptor is overwhelmed by the probability of re-binding of any one CPD site. In a sense, Sic1 becomes kinetically trapped in close proximity to Cdc4. Mathematical modeling of an idealized polyvalent ligand-monovalent receptor interaction indicates that the rate of ligand escape from the receptor exhibits a negative exponential dependence on the number of ligand sites. The term allovalent is proposed to describe the ability of multiple weak spatially separated ligand sites to cooperatively interact with a single receptor site. The prevalence of multisite phosphorylation (Cohen, 2000), and indeed of polyvalent ligands in general (Mammen et al., 1998), suggests that this type of behavior may underlie many biological processes.

[0517] The present invention is not to be limited in scope by the specific embodiments described herein, since such embodiments are intended as but single illustrations of one aspect of the invention and any functionally equivalent embodiments are within the scope of this invention. Indeed, various modifications of the invention in addition to those shown and described herein will become apparent to those skilled in the art from the foregoing description and accompanying drawings. Such modifications are intended to fall within the scope of the appended claims. In particular it will be appreciated that the references to specific amino acid residues for particular a SCF complexes, and components thereof (e.g. F-box protein) illustrated in the Tables and Figures, in no way limits the scope of the invention and it will be appreciated that a person skilled in the art could determine the specific corresponding amino acid residues for other SCF complexes and components thereof.

[0518] All publications, patents and patent applications referred to herein are incorporated by reference in their entirety to the same extent as if each individual publication, patent or patent application was specifically and individually indicated to be incorporated by reference in its entirety. All publications, patents and patent applications mentioned herein are incorporated herein by reference for the purpose of describing and disclosing the cell lines, vectors, methodologies etc. which are reported therein which might be used in connection with the invention. Nothing herein is to be construed as an admission that the invention is not entitled to antedate such disclosure by virtue of prior invention.

[0519] It must be noted that as used herein and in the appended claims, the singular forms “a”, “an”, and “the” include plural reference unless the context clearly dictates otherwise. Thus, for example, reference to “a host cell” includes a plurality of such host cells, reference to the “antibody” is a reference to one or more antibodies and equivalents thereof known to those skilled in the art, and so forth.

2TABLE 1Data Collection, Structure Determination, and RefinementStatisticsPeakInflectionRemoteWavelength (Å)0.97980.98000.9000Resolution (Å)2.82.92.7Rsym (%) 5.9 (38.7) 6.1 (36.1) 5.0 (28.9)Total Reflections311509187010298371Unique Reflections10716796027116218Completeness (%)99.8 (99.1)99.3 (98.3)97.7 (93.6)I/σ9.9 (2.7)7.4 (2.1)10.1 (2.9) Phasing PowerRefinement statisticsResolution range (Å)20-2.8Reflections103863Rfactor/Rfree (%)24.09/28.71Rms deviationsBonds (Å)0.0091Angles (°)1.3453Space group P32: a = b = 107.7 Å, c = 168.3 Å; a = b = 90°, c = 120°; Two molecules per asymmetric unit. 1Data for the highest resolution shell (2.90-2.80 Å) 2Rsym = 100 × Σ|I − |/Σ, where I is the observed intensity and is the average intensity from multiple observations of symmetry-related reflections. 3Phasing power for isomorphous and anomalous acentric reflections, where phasing power = <(|Fh,c|/phase-integrated lack of closure)>. 4Rfree was calculated with 8.8% of the data.

[0520]

3

TABLE 2

Data Collection, Structure Determination, and Refinement

Statistics

Peak
Inflection
Remote

Phasing Statistics

Wavelength (Å)
0.9798
0.9800
0.9000

Resolution (Å)
2.8 (2.9-2.8)
2.9 (3.0-2.9)
2.7 (2.8-2.7)

Rsym (%)
5.9 (37.2)
6.1 (36.1)
5.0 (28.9)

Total Reflections
311509
187010
298371

Unique Reflections
107167
96027
116218

Completeness (%)
99.8 (99.1)
99.3 (98.3)
97.7 (93.6)

I/σ
9.9 (2.7)
7.4 (2.1)
10.1 (2.9)

Phasing Power
5.2/1.3
4.0/0.94
0/0.91

(ISO/ANO)

Refinement statistics

(remote wavelength)

Resolution range (Å)
20-2.7
# protein
9364

atoms

Reflections
113960
# water
72

molecules

Rfactor/Rfree (%)
23.8/27.3

Rms deviations

Bonds (Å)
0.0089

Angles (°)
1.42

Space group P32: a = b = 107.7 Å, c = 168.3 Å; a = b = 90°, c = 120°

Two Skp1-Cdc4-CPD complexes per asymmetric unit

Numbers given in parantheses refer to data for the highest resolution shell.

1
Rsym = 100 × Σ|I − |/Σ, where I is the observed intensity and is the average intensity from multiple observations of symmetry-related reflections.

2
Phasing power for isomorphous and anomalous acentric reflections, = <[|Fh(calc)/phase-integrated lack of closure]>.

3
Rfree was calculated with 8.8% of the data.

[0521]

4

TABLE 3

Atomic Contacts of a Substrate Binding Pocket

No. of

Atomic
CDC4 WD40 Motif
CDC4 atomic
CPD Motif

Interaction
Atomic Contact
Contact
Atomic Contact

1
Ile 295
Phe 255

Ile296
Leu356

Leu 315

Trp 316 Leu 319

2
Val 687
Trp 365

Ile 696
Ile 364

Leu 726

Phe 743

3
Phe 743
Asn 364

4
Asn 684
Glu 323

Arg 700

5
Arg 485

PO pTyr

Arg 467

Phosphate

Arg 534

Tyr 548

6
Trp 426

P + 1 Proline side

Arg 485

chain

Thr 386

Thr 441

Thr 465

7
Trp 426

P + 1 Leucine side

Trp 717

chain

Thr 386

Val 384

8
Tyr 574

Leucine + 2

Thr 386

Val 384

[0522]

5

TABLE 4

Atomic Contacts of a Substrate Binding Pocket

No. of
CDC4 WD40

Atomic

Atomic
Motif/F-box Domain
CDC4 atomic
CPD Motif
Interaction

Interaction
Atomic Contact
Contact
Atomic Contact
Property

1
Ile 295
Phe 355

hydrophobic

Ile296
Leu356

interactions and

Leu 315

van der Wals

Trp 316

interactions

Leu 319

2
Val 687
Trp 365

van der Wals and

Ile 696
Ile 361

hydrophobic

Leu 726

interactions

Phe 743

3
Phe 743
Asn 364

hydrogen bond

4
Asn 684
Glu 323

hydrogen bonds

Arg 700

5
Arg 485

PO pTyr or pSer
electrostatic

Arg 467

Phosphate at P-O
interactions

Arg 534

position of CPD
hydrogen bond

Tyr 548

6
Trp 426

P + 1 Proline side
hydrogen and van

Arg 485

chain and
der Wals

Thr 441

backbone carbonyl
hydrophobic

Thr 465

of CPD
interations

7
Trp 426

P − 1 Leucine (or
hydrophobic

Trp 717

Ile/Pro) side chain
interactions

Thr 386

Val 384

8
Tyr 574

Leucine − 2
hydrophobic

Met 590

Leu/Ile at P − 2
interactions

Leu 634

position

9.
Tyr 342

hydrophobic

Leu 338

interactions

Leu 334

[0523]

6

TABLE 5

Determinants of pThr-Pro binding

P-Sic1
gal
gal
gal

pull down
Sic1 wt
Sic1T45A
Sic1T33V
gal Sic1-7
gal Sic1-6
gal Sic1-5
gal Sic1-4
gal Sic1-3
shuffle

WT
bind
alive
dead
alive

alive

R443A
bind
alive
dead
alive

alive

R467A
no bind

dead

R485A
no bind

dead

R534A
no bind

dead

R572A
no bind
alive
dead
dead

alive

alive

W426A
no bind

dead

V384N
bind
alive
dead
alive

alive

K402A
bind
alive
dead
alive

alive

R443D
bind
alive
dead
alive

alive

Y548F
no bind
alive
dead
dead

alive

Y574F
bind
alive
dead
alive

alive

W717N
bind
alive
dead
dead

alive

T441I/T465I
(in progress)

(in progress)

K402A/R443D
bind
alive
dead
dead

alive

W717N/V384N
bind
alive
dead
dead

alive

quad
(in progress)

dead

[0524]

7

TABLE 6

REMARK peptide link removed (applied DPEP) : from A 31 to A 45

REMARK peptide link removed (applied DPEP) : from A 73 to A 86

REMARK peptide link removed (applied DPEP) : from B 496 to B 508

REMARK peptide link removed (applied DPEP) : from C 31 to C 45

REMARK peptide link removed (applied DPEP) : from C 73 to C 86

REMARK peptide link removed (applied DPEP) : from D 496 to D 508

REMARK peptide link removed (applied DPPP) : from E 4 to E 5

REMARK coordinates from minimization and B-factor refinement

REMARK refinement resolution: 20 - 2.8 A

REMARK starting r= 0.2415 free_r= 0.2846

REMARK final r= 0.2409 free_r= 0.2871

REMARK rmsd bonds= 0.009114 rmsd angles= 1.34531

REMARK B rmsd for bonded mainchain atoms= 1.230 target= 1.5

REMARK B rmsd for bonded sidechain atoms= 1.778 target= 2.0

REMARK B rmsd for angle mainchain atoms= 2.103 target= 2.0

REMARK B rmsd for angle sidechain atoms= 2.675 target= 2.5

REMARK target= mlf final wa= 2.77695

REMARK final rweight= 0.1078 (with wa= 2.77695)

REMARK md-method= torsion annealing schedule= constant

REMARK starting temperature= 2000 total md steps= 1 * 100

REMARK cycles= 2 coordinate steps= 20 B-factor steps= 10

REMARK sg= P3(2) a= 107.669 b= 107.669 c= 168.3 alpha= 90 beta= 90 gamma= 120

REMARK topology file 1 : CNS_TOPPAR:protein.top

REMARK topology file 2 : CNS_TOPPAR:dna-rna.top

REMARK topology file 3 : CNS_TOPPAR:water.top

REMARK topology file 4 : CNS_TOPPAR:ion.top

REMARK topology file 5 : CNS_TOPPAR:tpo.top

REMARK parameter file 1 : CNS_TOPPAR:protein_rep.param

REMARK parameter file 2 : CNS_TOPPAR:dna-rna_rep.param

REMARK parameter file 3 : CNS_TOPPAR:water_rep.param

REMARK parameter file 4 : CNS_TOPPAR:ion.param

REMARK parameter file 5 : CNS_TOPPAR:tpo.param

REMARK molecular structure file: automatic

REMARK input coordinates: 36modl.pdb

REMARK reflection file= remote.cv

REMARK ncs= none

REMARK B-correction resolution: 6.0 - 2.8

REMARK initial B-factor correction applied to fobs :

REMARK B11= 1.580 B22= 1.580 B33= −3.160

REMARK B12= −3.767 B13= 0.000 B23= 0.000

REMARK B-factor correction applied to coordinate array B: 0.915

REMARK bulk solvent: density level= 0.324998 e/A{circumflex over ( )}3, B-factor= 34.4718 A+E,+CIR 2

REMARK reflections with |Fobs|/sigma_F < 0.0 rejected

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

REMARK anomalous diffraction data was input

REMARK theoretical total number of refl. in resol. range: 107240 (100.0%)

REMARK number of unobserved reflections (no entry or |F|=0): 3377 (3.1%)

REMARK number of reflections rejected: 0 (0.0%)

REMARK total number of reflections used: 103863 (96.9%)

REMARK number of reflections in working set: 93784 (87.5%)

REMARK number of reflections in test set: 10079 (9.4%)

CRYST1 107.669 107.669 168.300 90.00 90.00 120.00 P 32

REMARK FILENAME=“ref37.pdb”

REMARK DATE:28-Jun-2002 13:23:24 created by user: orlicky

REMARK VERSION:1.1

ATOM
1
CB
SER A
2
72.279
75.039
74.638
1.00
40.45
A

ATOM
2
OG
SER A
2
72.875
75.230
73.368
1.00
36.62
A

ATOM
3
C
SER A
2
70.142
75.473
73.446
1.00
40.01
A

ATOM
4
O
SER A
2
69.547
74.397
73.338
1.00
39.92
A

ATOM
5
N
SER A
2
70.277
75.520
76.026
1.00
40.09
A

ATOM
6
CA
SER A
2
70.953
75.797
74.713
1.00
40.80
A

ATOM
7
N
ASN A
3
70.145
76.398
72.482
1.00
38.91
A

ATOM
8
CA
ASN A
3
69.428
76.196
71.221
1.00
37.67
A

ATOM
9
CB
ASN A
3
68.480
77.367
70.926
1.00
38.01
A

ATOM
10
CG
ASN A
3
67.193
77.305
71.736
1.00
38.13
A

ATOM
11
OD1
ASN A
3
66.616
76.236
71.944
1.00
38.39
A

ATOM
12
ND2
ASN A
3
66.733
78.458
72.184
1.00
36.20
A

ATOM
13
C
ASN A
3
70.310
75.996
69.990
1.00
35.89
A

ATOM
14
O
ASN A
3
71.503
76.275
69.995
1.00
34.48
A

ATOM
15
N
VAL A
4
69.685
75.500
68.928
1.00
36.46
A

ATOM
16
CA
VAL A
4
70.343
75.275
67.639
1.00
33.96
A

ATOM
17
CB
VAL A
4
70.545
73.750
67.383
1.00
33.36
A

ATOM
18
CG1
VAL A
4
70.533
73.449
65.916
1.00
33.70
A

ATOM
19
CG2
VAL A
4
71.855
73.295
67.985
1.00
34.50
A

ATOM
20
C
VAL A
4
69.415
75.889
66.584
1.00
31.88
A

ATOM
21
O
VAL A
4
68.209
76.036
66.818
1.00
31.04
A

ATOM
22
N
VAL A
5
69.972
76.282
65.443
1.00
31.25
A

ATOM
23
CA
VAL A
5
69.146
76.853
64.376
1.00
31.10
A

ATOM
24
CB
VAL A
5
69.458
78.346
64.086
1.00
31.85
A

ATOM
25
CG1
VAL A
5
68.586
78.825
62.927
1.00
32.81
A

ATOM
26
CG2
VAL A
5
69.188
79.192
65.314
1.00
31.47
A

ATOM
27
C
VAL A
5
69.339
76.075
63.089
1.00
29.35
A

ATOM
28
O
VAL A
5
70.448
75.952
62.588
1.00
29.57
A

ATOM
29
N
LEU A
6
68.232
75.561
62.574
1.00
28.63
A

ATOM
30
CA
LEU A
6
68.206
74.777
61.355
1.00
28.72
A

ATOM
31
CB
LEU A
6
67.299
73.558
61.559
1.00
27.60
A

ATOM
32
CG
LEU A
6
67.585
72.619
62.739
1.00
25.63
A

ATOM
33
CD1
LEU A
6
66.684
71.402
62.592
1.00
24.10
A

ATOM
34
CD2
LEU A
6
69.043
72.205
62.781
1.00
21.89
A

ATOM
35
C
LEU A
6
67.667
75.632
60.208
1.00
28.54
A

ATOM
36
O
LEU A
6
66.577
76.200
60.316
1.00
28.48
A

ATOM
37
N
VAL A
7
68.416
75.740
59.112
1.00
27.74
A

ATOM
38
CA
VAL A
7
67.945
76.548
57.978
1.00
25.90
A

ATOM
39
CB
VAL A
7
69.092
77.413
57.366
1.00
25.69
A

ATOM
40
CG1
VAL A
7
68.515
78.450
56.403
1.00
25.12
A

ATOM
41
CG2
VAL A
7
69.889
78.077
58.450
1.00
22.70
A

ATOM
42
C
VAL A
7
67.374
75.650
56.869
1.00
24.30
A

ATOM
43
O
VAL A
7
68.069
74.768
56.337
1.00
21.91
A

ATOM
44
N
SER A
8
66.111
75.881
56.522
1.00
23.21
A

ATOM
45
CA
SER A
8
65.453
75.091
55.486
1.00
23.15
A

ATOM
46
CB
SER A
8
63.966
75.433
55.375
1.00
21.22
A

ATOM
47
OG
SER A
8
63.794
76.735
54.826
1.00
20.44
A

ATOM
48
C
SER A
8
66.093
75.428
54.167
1.00
25.17
A

ATOM
49
O
SER A
8
66.851
76.389
54.054
1.00
27.53
A

ATOM
50
N
GLY A
9
65.782
74.635
53.155
1.00
26.78
A

ATOM
51
CA
GLY A
9
66.329
74.914
51.847
1.00
26.99
A

ATOM
52
C
GLY A
9
65.726
76.208
51.320
1.00
27.95
A

ATOM
53
O
GLY A
9
66.120
76.682
50.256
1.00
29.65
A

ATOM
54
N
GLU A
10
64.762
76.782
52.039
1.00
26.66
A

ATOM
55
CA
GLU A
10
64.160
78.025
51.582
1.00
25.22
A

ATOM
56
CB
GLU A
10
62.637
77.927
51.610
1.00
24.78
A

ATOM
57
CG
GLU A
10
62.045
76.721
50.905
1.00
24.26
A

ATOM
58
CD
GLU A
10
60.543
76.567
51.203
1.00
27.17
A

ATOM
59
OE1
GLU A
10
59.747
77.407
50.727
1.00
27.67
A

ATOM
60
OE2
GLU A
10
60.144
75.617
51.929
1.00
28.38
A

ATOM
61
C
GLU A
10
64.598
79.236
52.416
1.00
25.50
A

ATOM
62
O
GLU A
10
63.853
80.213
52.538
1.00
24.72
A

ATOM
63
N
GLY A
11
65.794
79.164
52.995
1.00
25.06
A

ATOM
64
CA
GLY A
11
66.299
80.264
53.792
1.00
25.04
A

ATOM
65
C
GLY A
11
65.740
80.473
55.192
1.00
25.64
A

ATOM
66
O
GLY A
11
66.399
81.110
56.016
1.00
25.60
A

ATOM
67
N
GLU A
12
64.552
79.946
55.483
1.00
26.56
A

ATOM
68
CA
GLU A
12
63.945
80.113
56.806
1.00
27.47
A

ATOM
69
CB
GLU A
12
62.510
79.614
56.782
1.00
26.92
A

ATOM
70
CG
GLU A
12
61.661
80.451
55.874
1.00
32.01
A

ATOM
71
CD
GLU A
12
60.215
80.003
55.841
1.00
35.92
A

ATOM
72
OE1
GLU A
12
59.912
78.942
55.244
1.00
37.74
A

ATOM
73
OE2
GLU A
12
59.367
80.716
56.419
1.00
39.01
A

ATOM
74
C
GLU A
12
64.705
79.459
57.951
1.00
28.74
A

ATOM
75
O
GLU A
12
65.222
78.345
57.826
1.00
29.61
A

ATOM
76
N
ARG A
13
64.804
80.170
59.069
1.00
29.55
A

ATOM
77
CA
ARG A
13
65.513
79.615
60.207
1.00
30.68
A

ATOM
78
CB
ARG A
13
66.457
80.651
60.832
1.00
32.30
A

ATOM
79
CG
ARG A
13
66.654
81.907
60.002
1.00
34.52
A

ATOM
80
CD
ARG A
13
67.459
82.959
60.756
1.00
35.08
A

ATOM
81
NE
ARG A
13
68.816
82.514
61.051
1.00
36.91
A

ATOM
82
CZ
ARG A
13
69.454
82.778
62.188
1.00
37.09
A

ATOM
83
NH1
ARG A
13
68.846
83.485
63.129
1.00
35.87
A

ATOM
84
NH2
ARG A
13
70.691
82.328
62.391
1.00
37.00
A

ATOM
85
C
ARG A
13
64.511
79.130
61.238
1.00
29.61
A

ATOM
86
O
ARG A
13
63.494
79.783
61.506
1.00
29.30
A

ATOM
87
N
PHE A
14
64.809
77.962
61.789
1.00
28.74
A

ATOM
88
CA
PHE A
14
63.980
77.337
62.797
1.00
28.90
A

ATOM
89
CB
PHE A
14
63.507
75.945
62.356
1.00
27.81
A

ATOM
90
CG
PHE A
14
62.614
75.946
61.147
1.00
26.25
A

ATOM
91
CD1
PHE A
14
63.149
75.925
59.867
1.00
25.67
A

ATOM
92
CD2
PHE A
14
61.235
75.955
61.291
1.00
27.94
A

ATOM
93
CE1
PHE A
14
62.324
75.912
58.745
1.00
25.90
A

ATOM
94
CE2
PHE A
14
60.393
75.942
60.174
1.00
27.89
A

ATOM
95
CZ
PHE A
14
60.940
75.921
58.896
1.00
26.23
A

ATOM
96
C
PHE A
14
64.847
77.185
64.032
1.00
30.32
A

ATOM
97
O
PHE A
14
66.004
76.760
63.959
1.00
30.71
A

ATOM
98
N
THR A
15
64.305
77.558
65.176
1.00
32.94
A

ATOM
99
CA
THR A
15
65.067
77.412
66.396
1.00
34.55
A

ATOM
100
CB
THR A
15
64.910
78.650
67.275
1.00
34.81
A

ATOM
101
OG1
THR A
15
65.362
79.797
66.548
1.00
35.82
A

ATOM
102
CG2
THR A
15
65.737
78.509
68.541
1.00
36.02
A

ATOM
103
C
THR A
15
64.535
76.179
67.119
1.00
34.29
A

ATOM
104
O
THR A
15
63.358
75.830
66.984
1.00
35.01
A

ATOM
105
N
VAL A
16
65.398
75.501
67.859
1.00
34.16
A

ATOM
106
CA
VAL A
16
64.954
74.330
68.592
1.00
36.47
A

ATOM
107
CB
VAL A
16
64.597
73.166
67.628
1.00
38.19
A

ATOM
108
CG1
VAL A
16
65.697
72.981
66.579
1.00
37.94
A

ATOM
109
CG2
VAL A
16
64.403
71.884
68.421
1.00
40.71
A

ATOM
110
C
VAL A
16
65.992
73.862
69.601
1.00
36.55
A

ATOM
111
O
VAL A
16
67.199
74.020
69.398
1.00
36.18
A

ATOM
112
N
ASP A
17
65.511
73.294
70.699
1.00
36.09
A

ATOM
113
CA
ASP A
17
66.398
72.817
71.750
1.00
36.61
A

ATOM
114
CB
ASP A
17
65.586
72.082
72.812
1.00
38.44
A

ATOM
115
CG
ASP A
17
66.458
71.416
73.840
1.00
40.95
A

ATOM
116
OD1
ASP A
17
66.418
70.164
73.924
1.00
43.10
A

ATOM
117
OD2
ASP A
17
67.184
72.137
74.556
1.00
41.69
A

ATOM
118
C
ASP A
17
67.499
71.902
71.196
1.00
35.77
A

ATOM
119
O
ASP A
17
67.218
70.903
70.543
1.00
33.05
A

ATOM
120
N
LYS A
18
68.757
72.245
71.471
1.00
36.17
A

ATOM
121
CA
LYS A
18
69.897
71.473
70.972
1.00
35.91
A

ATOM
122
CB
LYS A
18
71.208
72.003
71.541
1.00
35.90
A

ATOM
123
CG
LYS A
18
72.397
71.086
71.239
1.00
36.70
A

ATOM
124
CD
LYS A
18
73.679
71.525
71.964
1.00
37.63
A

ATOM
125
CE
LYS A
18
74.131
72.918
71.523
1.00
38.26
A

ATOM
126
NZ
LYS A
18
75.528
73.223
71.956
1.00
38.28
A

ATOM
127
C
LYS A
18
69.776
70.010
71.319
1.00
36.47
A

ATOM
128
O
LYS A
18
70.048
69.129
70.497
1.00
35.04
A

ATOM
129
N
LYS A
19
69.388
69.756
72.559
1.00
38.15
A

ATOM
130
CA
LYS A
19
69.220
68.393
73.011
1.00
38.79
A

ATOM
131
CB
LYS A
19
68.733
68.374
74.456
1.00
39.52
A

ATOM
132
CG
LYS A
19
68.597
66.980
75.018
0.00
40.07
A

ATOM
133
CD
LYS A
19
68.074
66.996
76.439
0.00
40.81
A

ATOM
134
CE
LYS A
19
66.638
67.489
76.505
0.00
41.30
A

ATOM
135
NZ
LYS A
19
66.086
67.373
77.885
0.00
41.65
A

ATOM
136
C
LYS A
19
68.202
67.734
72.084
1.00
38.59
A

ATOM
137
O
LYS A
19
68.508
66.734
71.445
1.00
39.10
A

ATOM
138
N
ILE A
20
67.004
68.304
71.984
1.00
37.46
A

ATOM
139
CA
ILE A
20
65.991
67.725
71.112
1.00
37.39
A

ATOM
140
CB
ILE A
20
64.685
68.503
71.168
1.00
36.72
A

ATOM
141
CG2
ILE A
20
63.687
67.918
70.167
1.00
36.45
A

ATOM
142
CG1
ILE A
20
64.118
68.440
72.572
1.00
35.02
A

ATOM
143
CD1
ILE A
20
62.910
69.280
72.751
1.00
36.54
A

ATOM
144
C
ILE A
20
66.432
67.678
69.660
1.00
37.89
A

ATOM
145
O
ILE A
20
66.157
66.718
68.954
1.00
38.16
A

ATOM
146
N
ALA A
21
67.125
68.717
69.218
1.00
39.24
A

ATOM
147
CA
ALA A
21
67.591
68.793
67.843
1.00
38.28
A

ATOM
148
CB
ALA A
21
68.197
70.154
67.570
1.00
38.24
A

ATOM
149
C
ALA A
21
68.609
67.719
67.589
1.00
38.38
A

ATOM
150
O
ALA A
21
68.798
67.294
66.455
1.00
38.91
A

ATOM
151
N
GLU A
22
69.281
67.276
68.640
1.00
38.98
A

ATOM
152
CA
GLU A
22
70.280
66.242
68.449
1.00
39.28
A

ATOM
153
CB
GLU A
22
71.102
66.063
69.717
1.00
42.76
A

ATOM
154
CG
GLU A
22
72.116
67.162
69.962
1.00
47.53
A

ATOM
155
CD
GLU A
22
72.856
66.948
71.259
1.00
50.36
A

ATOM
156
OE1
GLU A
22
73.381
65.827
71.444
1.00
50.70
A

ATOM
157
OE2
GLU A
22
72.907
67.891
72.089
1.00
52.73
A

ATOM
158
C
GLU A
22
69.666
64.913
68.021
1.00
37.58
A

ATOM
159
O
GLU A
22
70.391
63.955
67.805
1.00
37.40
A

ATOM
160
N
ARG A
23
68.342
64.850
67.890
1.00
36.03
A

ATOM
161
CA
ARG A
23
67.706
63.615
67.459
1.00
34.62
A

ATOM
162
CB
ARG A
23
66.200
63.765
67.306
1.00
33.59
A

ATOM
163
CG
ARG A
23
65.509
62.431
67.022
1.00
33.69
A

ATOM
164
CD
ARG A
23
65.708
61.463
68.191
1.00
33.70
A

ATOM
165
NE
ARG A
23
64.457
61.196
68.901
1.00
34.45
A

ATOM
166
CZ
ARG A
23
64.360
60.622
70.100
1.00
33.77
A

ATOM
167
NH1
ARG A
23
65.447
60.243
70.764
1.00
34.73
A

ATOM
168
NH2
ARG A
23
63.164
60.414
70.633
1.00
29.73
A

ATOM
169
C
ARG A
23
68.270
63.248
66.116
1.00
35.80
A

ATOM
170
O
ARG A
23
68.362
62.077
65.769
1.00
37.71
A

ATOM
171
N
SER A
24
68.629
64.266
65.345
1.00
37.45
A

ATOM
172
CA
SER A
24
69.208
64.072
64.018
1.00
37.69
A

ATOM
173
CB
SER A
24
69.047
65.344
63.187
1.00
36.12
A

ATOM
174
OG
SER A
24
69.929
65.337
62.084
1.00
32.96
A

ATOM
175
C
SER A
24
70.686
63.729
64.127
1.00
38.12
A

ATOM
176
O
SER A
24
71.506
64.581
64.466
1.00
36.69
A

ATOM
177
N
LEU A
25
71.022
62.478
63.837
1.00
40.01
A

ATOM
178
CA
LEU A
25
72.409
62.036
63.901
1.00
42.65
A

ATOM
179
CB
LEU A
25
72.534
60.580
63.436
1.00
43.67
A

ATOM
180
CG
LEU A
25
71.996
59.493
64.383
1.00
43.11
A

ATOM
181
CD1
LEU A
25
72.208
58.104
63.794
1.00
41.75
A

ATOM
182
CD2
LEU A
25
72.703
59.615
65.713
1.00
41.72
A

ATOM
183
C
LEU A
25
73.313
62.916
63.054
1.00
42.76
A

ATOM
184
O
LEU A
25
74.475
63.112
63.394
1.00
42.58
A

ATOM
185
N
LEU A
26
72.779
63.442
61.954
1.00
44.29
A

ATOM
186
CA
LEU A
26
73.554
64.309
61.070
1.00
46.11
A

ATOM
187
CB
LEU A
26
72.701
64.742
59.875
1.00
46.16
A

ATOM
188
CG
LEU A
26
73.318
65.721
58.868
1.00
45.56
A

ATOM
189
CD1
LED A
26
74.571
65.123
58.268
1.00
44.90
A

ATOM
190
CD2
LED A
26
72.303
66.050
57.774
1.00
45.90
A

ATOM
191
C
LED A
26
73.992
65.524
61.866
1.00
47.66
A

ATOM
192
O
LED A
26
75.140
65.962
61.770
1.00
47.34
A

ATOM
193
N
LEU A
27
73.060
66.055
62.655
1.00
50.27
A

ATOM
194
CA
LED A
27
73.312
67.212
63.508
1.00
52.62
A

ATOM
195
CB
LEU A
27
71.985
67.831
63.963
1.00
52.60
A

ATOM
196
CG
LED A
27
72.112
68.911
65.046
1.00
52.80
A

ATOM
197
CD1
LEU A
27
72.872
70.114
64.501
1.00
52.04
A

ATOM
198
CD2
LED A
27
70.729
69.314
65.513
1.00
52.96
A

ATOM
199
C
LED A
27
74.145
66.835
64.742
1.00
54.44
A

ATOM
200
O
LED A
27
75.085
67.540
65.100
1.00
54.34
A

ATOM
201
N
LYS A
28
73.786
65.726
65.387
1.00
56.05
A

ATOM
202
CA
LYS A
28
74.491
65.255
66.574
1.00
57.53
A

ATOM
203
CB
LYS A
28
73.880
63.942
67.059
1.00
58.27
A

ATOM
204
CG
LYS A
28
74.486
63.418
68.347
0.00
58.77
A

ATOM
205
CD
LYS A
28
73.864
62.093
68.750
0.00
59.35
A

ATOM
206
CE
LYS A
28
74.520
61.545
70.004
0.00
59.70
A

ATOM
207
NZ
LYS A
28
73.986
60.205
70.367
0.00
59.95
A

ATOM
208
C
LYS A
28
75.974
65.049
66.297
0.00
58.99
A

ATOM
209
O
LYS A
28
76.811
65.183
67.191
0.00
58.95
A

ATOM
210
N
ASN A
29
76.290
64.716
65.052
1.00
60.36
A

ATOM
211
CA
ASN A
29
77.667
64.489
64.647
1.00
62.38
A

ATOM
212
CB
ASN A
29
77.729
63.509
63.484
1.00
63.15
A

ATOM
213
CG
ASN A
29
77.458
62.085
63.908
1.00
64.88
A

ATOM
214
OD1
ASN A
29
77.410
61.185
63.068
1.00
67.16
A

ATOM
215
ND2
ASN A
29
77.285
61.865
65.215
1.00
64.20
A

ATOM
216
C
ASN A
29
78.326
65.778
64.227
1.00
63.19
A

ATOM
217
O
ASN A
29
79.547
65.852
64.106
1.00
63.26
A

ATOM
218
N
TYR A
30
77.514
66.797
63.993
1.00
64.46
A

ATOM
219
CA
TYR A
30
78.049
68.083
63.583
1.00
65.53
A

ATOM
220
CB
TYR A
30
76.898
69.085
63.417
1.00
67.82
A

ATOM
221
CG
TYR A
30
77.127
70.172
62.379
1.00
68.70
A

ATOM
222
CD1
TYR A
30
77.416
69.853
61.050
1.00
68.47
A

ATOM
223
CE1
TYR A
30
77.595
70.854
60.092
1.00
69.31
A

ATOM
224
CD2
TYR A
30
77.024
71.522
62.722
1.00
68.53
A

ATOM
225
CE2
TYR A
30
77.201
72.528
61.774
1.00
69.17
A

ATOM
226
CZ
TYR A
30
77.485
72.190
60.464
1.00
69.54
A

ATOM
227
OH
TYR A
30
77.651
73.191
59.534
1.00
69.67
A

ATOM
228
C
TYR A
30
79.043
68.550
64.658
1.00
65.21
A

ATOM
229
O
TYR A
30
79.894
69.395
64.391
1.00
64.91
A

ATOM
230
N
VAL A
31
78.935
67.964
65.856
1.00
64.85
A

ATOM
231
CA
VAL A
31
79.786
68.271
67.019
1.00
62.98
A

ATOM
232
CB
VAL A
31
81.049
67.351
67.096
1.00
62.18
A

ATOM
233
CG1
VAL A
31
80.624
65.903
67.216
1.00
61.36
A

ATOM
234
CG2
VAL A
31
81.961
67.562
65.882
1.00
60.58
A

ATOM
235
C
VAL A
31
80.256
69.712
67.123
1.00
62.08
A

ATOM
236
O
VAL A
31
80.624
70.168
68.203
1.00
60.74
A

ATOM
237
N
ILE A
45
76.524
76.394
65.711
1.00
42.05
A

ATOM
238
CA
ILE A
45
75.216
76.668
66.290
1.00
41.90
A

ATOM
239
CB
ILE A
45
75.276
77.864
67.310
1.00
42.05
A

ATOM
240
CG2
ILE A
45
75.089
79.191
66.601
1.00
40.06
A

ATOM
241
CG1
ILE A
45
74.171
77.726
68.363
1.00
43.22
A

ATOM
242
CD1
ILE A
45
74.407
76.620
69.388
1.00
43.84
A

ATOM
243
C
ILE A
45
74.180
76.963
65.195
1.00
41.36
A

ATOM
244
O
ILE A
45
73.021
77.252
65.488
1.00
41.48
A

ATOM
245
N
VAL A
46
74.592
76.918
63.933
1.00
39.64
A

ATOM
246
CA
VAL A
46
73.635
77.132
62.849
1.00
39.19
A

ATOM
247
CB
VAL A
46
73.675
78.579
62.293
1.00
37.60
A

ATOM
248
CG1
VAL A
46
72.665
78.729
61.166
1.00
35.40
A

ATOM
249
CG2
VAL A
46
73.346
79.567
63.390
1.00
38.18
A

ATOM
250
C
VAL A
46
73.917
76.159
61.715
1.00
39.41
A

ATOM
251
O
VAL A
46
74.815
76.385
60.905
1.00
41.28
A

ATOM
252
N
MSE A
47
73.160
75.069
61.655
1.00
38.13
A

ATOM
253
CA
MSE A
47
73.390
74.093
60.606
1.00
37.60
A

ATOM
254
CB
MSE A
47
73.419
72.680
61.169
1.00
40.79
A

ATOM
255
CG
MSE A
47
73.777
71.642
60.118
1.00
44.02
A

ATOM
256
SE
MSE A
47
73.314
69.875
60.679
1.00
50.37
A

ATOM
257
CE
MSE A
47
71.388
70.111
60.653
1.00
48.04
A

ATOM
258
C
MSE A
47
72.402
74.138
59.465
1.00
36.07
A

ATOM
259
O
MSE A
47
71.195
74.213
59.670
1.00
36.45
A

ATOM
260
N
PRO A
48
72.917
74.093
58.229
1.00
34.97
A

ATOM
261
CD
PRO A
48
74.305
74.434
57.870
1.00
34.19
A

ATOM
262
CA
PRO A
48
72.066
74.128
57.040
1.00
34.14
A

ATOM
263
CB
PRO A
48
73.041
74.516
55.929
1.00
33.07
A

ATOM
264
CG
PRO A
48
74.103
75.290
56.654
1.00
33.93
A

ATOM
265
C
PRO A
48
71.369
72.806
56.729
1.00
33.52
A

ATOM
266
O
PRO A
48
71.922
71.727
56.946
1.00
32.95
A

ATOM
267
N
VAL A
49
70.140
72.906
56.231
1.00
32.78
A

ATOM
268
CA
VAL A
49
69.383
71.731
55.828
1.00
32.43
A

ATOM
269
CB
VAL A
49
68.073
71.538
56.671
1.00
31.33
A

ATOM
270
CG1
VAL A
49
67.575
70.120
56.539
1.00
30.50
A

ATOM
271
CG2
VAL A
49
68.327
71.845
58.141
1.00
34.13
A

ATOM
272
C
VAL A
49
69.062
71.991
54.340
1.00
32.95
A

ATOM
273
O
VAL A
49
67.958
72.412
53.977
1.00
32.24
A

ATOM
274
N
PRO A
50
70.060
71.757
53.460
1.00
33.40
A

ATOM
275
CD
PRO A
50
71.393
71.237
53.811
1.00
33.34
A

ATOM
276
CA
PRO A
50
69.971
71.942
52.010
1.00
32.39
A

ATOM
277
CB
PRO A
50
71.310
71.409
51.512
1.00
32.52
A

ATOM
278
CG
PRO A
50
72.217
71.682
52.627
1.00
33.15
A

ATOM
279
C
PRO A
50
68.813
71.229
51.343
1.00
31.05
A

ATOM
280
O
PRO A
50
68.509
70.079
51.648
1.00
31.50
A

ATOM
281
N
ASN A
51
68.176
71.936
50.420
1.00
30.37
A

ATOM
282
CA
ASN A
51
67.071
71.387
49.645
1.00
30.66
A

ATOM
283
CB
ASN A
51
67.648
70.432
48.595
1.00
31.76
A

ATOM
284
CG
ASN A
51
69.069
70.813
48.175
1.00
30.85
A

ATOM
285
OD1
ASN A
51
69.262
71.794
47.478
1.00
27.98
A

ATOM
286
ND2
ASN A
51
70.072
70.031
48.620
1.00
33.14
A

ATOM
287
C
ASN A
51
65.978
70.665
50.450
1.00
29.20
A

ATOM
288
O
ASN A
51
65.588
69.551
50.120
1.00
26.62
A

ATOM
289
N
VAL A
52
65.500
71.292
51.512
1.00
29.33
A

ATOM
290
CA
VAL A
52
64.435
70.692
52.283
1.00
29.38
A

ATOM
291
CB
VAL A
52
64.913
70.157
53.640
1.00
30.20
A

ATOM
292
CG1
VAL A
52
63.747
69.506
54.390
1.00
26.29
A

ATOM
293
CG2
VAL A
52
66.022
69.129
53.420
1.00
29.10
A

ATOM
294
C
VAL A
52
63.401
71.774
52.492
1.00
29.83
A

ATOM
295
O
VAL A
52
63.693
72.821
53.058
1.00
29.62
A

ATOM
296
N
ARG A
53
62.199
71.504
51.992
1.00
30.70
A

ATOM
297
CA
ARG A
53
61.064
72.411
52.063
1.00
31.16
A

ATOM
298
CB
ARG A
53
59.814
71.667
51.580
1.00
35.30
A

ATOM
299
CG
ARG A
53
58.775
72.499
50.846
1.00
39.79
A

ATOM
300
CD
ARG A
53
57.564
71.636
50.474
1.00
42.92
A

ATOM
301
NE
ARG A
53
56.700
72.283
49.491
1.00
47.91
A

ATOM
302
CZ
ARG A
53
55.889
73.308
49.749
1.00
50.95
A

ATOM
303
NH1
ARG A
53
55.815
73.814
50.972
1.00
53.87
A

ATOM
304
NH2
ARC A
53
55.158
73.844
48.776
1.00
52.85
A

ATOM
305
C
ARC A
53
60.864
72.876
53.505
1.00
30.38
A

ATOM
306
O
ARC A
53
60.860
72.068
54.425
1.00
31.84
A

ATOM
307
N
SER A
54
60.694
74.173
53.708
1.00
27.65
A

ATOM
308
CA
SER A
54
60.481
74.670
55.050
1.00
24.25
A

ATOM
309
CB
SER A
54
60.094
76.142
55.013
1.00
23.48
A

ATOM
310
OC
SER A
54
61.197
76.935
54.642
1.00
22.07
A

ATOM
311
C
SER A
54
59.386
73.866
55.742
1.00
22.74
A

ATOM
312
O
SER A
54
59.611
73.280
56.792
1.00
21.74
A

ATOM
313
N
SER A
55
58.204
73.835
55.143
1.00
22.72
A

ATOM
314
CA
SER A
55
57.078
73.114
55.707
1.00
22.82
A

ATOM
315
CB
SER A
55
55.913
73.117
54.736
1.00
20.88
A

ATOM
316
OC
SER A
55
56.159
72.211
53.683
1.00
23.15
A

ATOM
317
C
SER A
55
57.432
71.670
56.042
1.00
24.40
A

ATOM
318
O
SER A
55
56.780
71.034
56.877
1.00
27.21
A

ATOM
319
N
VAL A
56
58.457
71.144
55.387
1.00
21.45
A

ATOM
320
CA
VAL A
56
58.862
69.782
55.662
1.00
20.79
A

ATOM
321
CB
VAL A
56
59.648
69.194
54.488
1.00
19.14
A

ATOM
322
CG1
VAL A
56
60.254
67.875
54.889
1.00
16.99
A

ATOM
323
CG2
VAL A
56
58.738
69.029
53.301
1.00
18.04
A

ATOM
324
C
VAL A
56
59.719
69.727
56.924
1.00
21.47
A

ATOM
325
O
VAL A
56
59.498
68.903
57.797
1.00
21.73
A

ATOM
326
N
LEU A
57
60.703
70.606
57.010
1.00
22.90
A

ATOM
327
CA
LEU A
57
61.573
70.645
58.159
1.00
24.53
A

ATOM
328
CB
LEU A
57
62.647
71.696
57.937
1.00
24.08
A

ATOM
329
CG
LEU A
57
63.681
71.859
59.042
1.00
24.59
A

ATOM
330
CD1
LEU A
57
64.030
70.523
59.664
1.00
23.09
A

ATOM
331
CD2
LEU A
57
64.924
72.530
58.438
1.00
23.83
A

ATOM
332
C
LEU A
57
60.760
70.949
59.411
1.00
27.00
A

ATOM
333
O
LEU A
57
61.044
70.424
60.486
1.00
27.31
A

ATOM
334
N
GLN A
58
59.740
71.790
59.270
1.00
28.60
A

ATOM
335
CA
GLN A
58
58.885
72.133
60.402
1.00
29.92
A

ATOM
336
CB
GLN A
58
57.789
73.112
59.979
1.00
29.50
A

ATOM
337
CG
GLN A
58
56.729
73.358
61.044
1.00
29.08
A

ATOM
338
CD
GLN A
58
55.975
74.654
60.815
1.00
27.90
A

ATOM
339
OE1
GLN A
58
56.591
75.700
60.657
1.00
30.17
A

ATOM
340
NE2
GLN A
58
54.648
74.594
60.802
1.00
25.55
A

ATOM
341
C
GLN A
58
58.257
70.845
60.886
1.00
30.93
A

ATOM
342
O
GLN A
58
58.354
70.483
62.065
1.00
33.35
A

ATOM
343
N
LYS A
59
57.609
70.156
59.955
1.00
30.29
A

ATOM
344
CA
LYS A
59
56.976
68.880
60.248
1.00
29.48
A

ATOM
345
CB
LYS A
59
56.581
68.209
58.937
1.00
28.21
A

ATOM
346
CG
LYS A
59
55.283
67.470
58.978
1.00
29.03
A

ATOM
347
CD
LYS A
59
54.108
68.397
59.081
1.00
27.32
A

ATOM
348
CE
LYS A
59
52.834
67.608
58.857
1.00
26.80
A

ATOM
349
NZ
LYS A
59
52.804
66.508
59.824
1.00
25.00
A

ATOM
350
C
LYS A
59
58.004
68.017
61.006
1.00
29.46
A

ATOM
351
O
LYS A
59
57.709
67.465
62.070
1.00
29.02
A

ATOM
352
N
VAL A
60
59.217
67.929
60.467
1.00
28.15
A

ATOM
353
CA
VAL A
60
60.259
67.142
61.106
1.00
28.14
A

ATOM
354
CB
VAL A
60
61.573
67.226
60.319
1.00
28.15
A

ATOM
355
CG1
VAL A
60
62.731
66.715
61.152
1.00
27.46
A

ATOM
356
CG2
VAL A
60
61.455
66.386
59.060
1.00
29.05
A

ATOM
357
C
VAL A
60
60.495
67.574
62.543
1.00
28.57
A

ATOM
358
O
VAL A
60
60.434
66.762
63.465
1.00
29.28
A

ATOM
359
N
ILE A
61
60.768
68.853
62.734
1.00
28.79
A

ATOM
360
CA
ILE A
61
61.007
69.375
64.068
1.00
28.54
A

ATOM
361
CB
ILE A
61
61.195
70.903
64.001
1.00
27.31
A

ATOM
362
CG2
ILE A
61
61.238
71.501
65.391
1.00
26.36
A

ATOM
363
CG1
ILE A
61
62.482
71.202
63.223
1.00
27.68
A

ATOM
364
CD1
ILE A
61
62.737
72.660
62.979
1.00
27.54
A

ATOM
365
C
ILE A
61
59.860
69.020
65.016
1.00
29.35
A

ATOM
366
O
ILE A
61
60.086
68.538
66.131
1.00
27.58
A

ATOM
367
N
GLU A
62
58.627
69.247
64.572
1.00
30.00
A

ATOM
368
CA
GLU A
62
57.473
68.949
65.415
1.00
31.73
A

ATOM
369
CB
GLU A
62
56.169
69.203
64.667
1.00
29.92
A

ATOM
370
CG
GLU A
62
55.043
68.328
65.181
1.00
30.57
A

ATOM
371
CD
GLU A
62
53.688
68.775
64.703
1.00
31.86
A

ATOM
372
OE1
GLU A
62
53.530
68.966
63.470
1.00
33.09
A

ATOM
373
OE2
GLU A
62
52.781
68.934
65.562
1.00
31.63
A

ATOM
374
C
GLU A
62
57.480
67.505
65.907
1.00
32.78
A

ATOM
375
O
GLU A
62
57.035
67.207
67.017
1.00
32.73
A

ATOM
376
N
TRP A
63
57.965
66.610
65.057
1.00
34.15
A

ATOM
377
CA
TRP A
63
58.029
65.204
65.394
1.00
34.37
A

ATOM
378
CB
TRP A
63
58.259
64.380
64.127
1.00
33.74
A

ATOM
379
CG
TRP A
63
58.189
62.915
64.354
1.00
31.94
A

ATOM
380
CD2
TRP A
63
59.254
62.071
64.798
1.00
30.34
A

ATOM
381
CE2
TRP A
63
58.729
60.775
64.937
1.00
29.79
A

ATOM
382
CE3
TRP A
63
60.601
62.287
65.104
1.00
29.39
A

ATOM
383
CD1
TRP A
63
57.092
62.120
64.235
1.00
31.15
A

ATOM
384
NE1
TRP A
63
57.406
60.829
64.584
1.00
30.29
A

ATOM
385
CZ2
TRP A
63
59.506
59.698
65.361
1.00
29.60
A

ATOM
386
CZ3
TRP A
63
61.372
61.211
65.528
1.00
28.85
A

ATOM
387
CH2
TRP A
63
60.821
59.937
65.654
1.00
27.95
A

ATOM
388
C
TRP A
63
59.181
64.989
66.372
1.00
34.92
A

ATOM
389
O
TRP A
63
59.146
64.078
67.182
1.00
36.00
A

ATOM
390
N
ALA A
64
60.195
65.840
66.316
1.00
35.06
A

ATOM
391
CA
ALA A
64
61.332
65.673
67.207
1.00
36.52
A

ATOM
392
CB
ALA A
64
62.567
66.371
66.621
1.00
35.61
A

ATOM
393
C
ALA A
64
61.071
66.166
68.636
1.00
38.06
A

ATOM
394
O
ALA A
64
61.606
65.607
69.602
1.00
38.15
A

ATOM
395
N
GLU A
65
60.266
67.218
68.764
1.00
38.68
A

ATOM
396
CA
GLU A
65
59.934
67.776
70.063
1.00
38.24
A

ATOM
397
CB
GLU A
65
59.405
69.201
69.912
1.00
38.18
A

ATOM
398
CG
GLU A
65
60.459
70.151
69.397
1.00
38.80
A

ATOM
399
CD
GLU A
65
59.895
71.454
68.840
1.00
39.78
A

ATOM
400
OE1
GLU A
65
58.673
71.527
68.547
1.00
38.29
A

ATOM
401
OE2
GLU A
65
60.695
72.408
68.683
1.00
39.80
A

ATOM
402
C
GLU A
65
58.879
66.902
70.708
1.00
38.37
A

ATOM
403
O
GLU A
65
58.835
66.742
71.925
1.00
39.26
A

ATOM
404
N
HIS A
66
58.024
66.312
69.896
1.00
38.38
A

ATOM
405
CA
HIS A
66
57.006
65.482
70.479
1.00
40.16
A

ATOM
406
CB
HIS A
66
55.929
65.179
69.465
1.00
39.56
A

ATOM
407
CG
HIS A
66
54.902
64.215
69.955
1.00
39.86
A

ATOM
408
CD2
HIS A
66
53.613
64.399
70.320
1.00
39.39
A

ATOM
409
ND1
HIS A
66
55.137
62.859
70.036
1.00
38.45
A

ATOM
410
CE1
HIS A
66
54.031
62.248
70.418
1.00
38.21
A

ATOM
411
NE2
HIS A
66
53.091
63.159
70.595
1.00
39.69
A

ATOM
412
C
HIS A
66
57.616
64.205
71.002
1.00
42.15
A

ATOM
413
O
HIS A
66
57.115
63.619
71.959
1.00
44.74
A

ATOM
414
N
HIS A
67
58.701
63.775
70.377
1.00
43.11
A

ATOM
415
CA
HIS A
67
59.388
62.573
70.807
1.00
44.64
A

ATOM
416
CB
HIS A
67
59.711
61.681
69.598
1.00
43.57
A

ATOM
417
CG
HIS A
67
58.524
60.951
69.046
1.00
42.88
A

ATOM
418
CD2
HIS A
67
58.088
59.684
69.241
1.00
42.35
A

ATOM
419
ND1
HIS A
67
57.615
61.540
68.194
1.00
43.39
A

ATOM
420
CE1
HIS A
67
56.673
60.667
67.886
1.00
41.93
A

ATOM
421
NE2
HIS A
67
56.936
59.533
68.508
1.00
40.92
A

ATOM
422
C
HIS A
67
60.673
62.989
71.512
1.00
46.18
A

ATOM
423
O
HIS A
67
61.767
62.552
71.144
1.00
47.55
A

ATOM
424
N
ARG A
68
60.541
63.842
72.524
1.00
47.19
A

ATOM
425
CA
ARG A
68
61.704
64.322
73.270
1.00
48.05
A

ATOM
426
CB
ARG A
68
61.390
65.665
73.959
1.00
47.55
A

ATOM
427
CG
ARG A
68
60.459
65.576
75.163
1.00
47.12
A

ATOM
428
CD
ARG A
68
60.219
66.943
75.813
1.00
45.40
A

ATOM
429
NE
ARG A
68
59.137
67.657
75.151
1.00
44.72
A

ATOM
430
CZ
ARG A
68
57.849
67.387
75.342
1.00
44.29
A

ATOM
431
NH1
ARG A
68
57.485
66.434
76.179
1.00
46.93
A

ATOM
432
NH2
ARG A
68
56.915
68.043
74.678
1.00
45.61
A

ATOM
433
C
ARG A
68
62.187
63.308
74.303
1.00
49.19
A

ATOM
434
O
ARG A
68
63.383
63.228
74.593
1.00
48.48
A

ATOM
435
N
ASP A
69
61.261
62.525
74.848
1.00
51.12
A

ATOM
436
CA
ASP A
69
61.626
61.531
75.853
1.00
52.05
A

ATOM
437
CB
ASP A
69
60.967
61.862
77.187
1.00
50.12
A

ATOM
438
CG
ASP A
69
61.351
63.221
77.684
1.00
49.36
A

ATOM
439
OD1
ASP A
69
62.572
63.496
77.736
1.00
48.50
A

ATOM
440
OD2
ASP A
69
60.440
64.010
78.015
1.00
49.39
A

ATOM
441
C
ASP A
69
61.245
60.126
75.442
1.00
52.86
A

ATOM
442
O
ASP A
69
60.787
59.335
76.261
1.00
52.94
A

ATOM
443
N
SER A
70
61.437
59.812
74.170
1.00
54.02
A

ATOM
444
CA
SER A
70
61.106
58.488
73.690
1.00
55.97
A

ATOM
445
CB
SER A
70
60.259
58.588
72.425
1.00
54.70
A

ATOM
446
OG
SER A
70
59.031
59.239
72.703
1.00
54.60
A

ATOM
447
C
SER A
70
62.379
57.702
73.425
1.00
58.22
A

ATOM
448
O
SER A
70
63.463
58.273
73.306
1.00
58.71
A

ATOM
449
N
ASN A
71
62.252
56.385
73.362
1.00
60.80
A

ATOM
450
CA
ASN A
71
63.403
55.545
73.105
1.00
64.11
A

ATOM
451
CB
ASN A
71
63.999
55.049
74.421
1.00
62.74
A

ATOM
452
CG
ASN A
71
64.012
56.121
75.495
1.00
62.42
A

ATOM
453
OD1
ASN A
71
63.016
56.332
76.183
1.00
61.70
A

ATOM
454
ND2
ASN A
71
65.139
56.811
75.636
1.00
62.41
A

ATOM
455
C
ASN A
71
62.957
54.377
72.247
1.00
67.50
A

ATOM
456
O
ASN A
71
62.140
53.558
72.669
1.00
68.91
A

ATOM
457
N
PHE A
72
63.486
54.313
71.030
1.00
70.54
A

ATOM
458
CA
PHE A
72
63.134
53.245
70.110
1.00
72.15
A

ATOM
459
CB
PHE A
72
62.792
53.827
68.721
1.00
72.15
A

ATOM
460
CG
PHE A
72
61.940
55.087
68.759
1.00
71.12
A

ATOM
461
CD1
PHE A
72
62.539
56.349
68.784
1.00
70.74
A

ATOM
462
CD2
PHE A
72
60.546
55.012
68.765
1.00
70.32
A

ATOM
463
CE1
PHE A
72
61.767
57.514
68.814
1.00
70.31
A

ATOM
464
CE2
PHE A
72
59.768
56.173
68.796
1.00
70.64
A

ATOM
465
CZ
PHE A
72
60.383
57.425
68.821
1.00
70.21
A

ATOM
466
C
PHE A
72
64.307
52.261
70.001
1.00
73.60
A

ATOM
467
O
PHE A
72
65.466
52.623
70.226
1.00
73.93
A

ATOM
468
N
PRO A
73
64.012
50.992
69.685
1.00
75.25
A

ATOM
469
CD
PRO A
73
62.656
50.410
69.635
1.00
75.90
A

ATOM
470
CA
PRO A
73
65.039
49.952
69.545
1.00
75.83
A

ATOM
471
CB
PRO A
73
64.230
48.732
69.122
1.00
76.63
A

ATOM
472
CG
PRO A
73
62.924
48.937
69.852
1.00
76.34
A

ATOM
473
C
PRO A
73
66.099
50.325
68.511
0.00
76.16
A

ATOM
474
O
PRO A
73
67.292
50.365
68.813
0.00
76.37
A

ATOM
475
N
VAL A
86
52.596
52.678
63.351
1.00
68.06
A

ATOM
476
CA
VAL A
86
52.119
51.882
64.474
1.00
69.23
A

ATOM
477
CB
VAL A
86
53.259
50.998
65.073
1.00
69.13
A

ATOM
478
CG1
VAL A
86
52.716
50.130
66.203
1.00
68.76
A

ATOM
479
CG2
VAL A
86
53.864
50.111
63.989
1.00
69.85
A

ATOM
480
C
VAL A
86
51.576
52.809
65.562
1.00
69.62
A

ATOM
481
O
VAL A
86
50.459
52.627
66.061
1.00
69.53
A

ATOM
482
N
ASP A
87
52.368
53.821
65.907
1.00
69.73
A

ATOM
483
CA
ASP A
87
51.995
54.792
66.936
1.00
68.97
A

ATOM
484
CB
ASP A
87
53.177
55.726
67.223
1.00
70.05
A

ATOM
485
CG
ASP A
87
52.982
56.555
68.487
1.00
70.55
A

ATOM
486
OD1
ASP A
87
52.047
57.386
68.514
1.00
70.97
A

ATOM
487
OD2
ASP A
87
53.768
56.374
69.447
1.00
69.47
A

ATOM
488
C
ASP A
87
50.766
55.609
66.528
1.00
67.85
A

ATOM
489
O
ASP A
87
50.574
55.925
65.353
1.00
67.51
A

ATOM
490
N
SER A
88
49.936
55.948
67.510
1.00
66.47
A

ATOM
491
CA
SER A
88
48.714
56.708
67.263
1.00
64.69
A

ATOM
492
CB
SER A
88
47.872
56.772
68.537
1.00
65.29
A

ATOM
493
OG
SER A
88
46.724
57.579
68.337
1.00
66.37
A

ATOM
494
C
SER A
88
48.976
58.124
66.770
1.00
62.66
A

ATOM
495
O
SER A
88
48.420
58.553
65.755
1.00
61.70
A

ATOM
496
N
TRP A
89
49.824
58.843
67.498
1.00
60.57
A

ATOM
497
CA
TRP A
89
50.161
60.221
67.160
1.00
58.68
A

ATOM
498
CB
TRP A
89
50.999
60.836
68.281
1.00
57.33
A

ATOM
499
CG
TRP A
89
51.130
62.296
68.148
1.00
56.37
A

ATOM
500
CD2
TRP A
89
52.229
62.998
67.571
1.00
56.15
A

ATOM
501
CE2
TRP A
89
51.892
64.365
67.574
1.00
55.64
A

ATOM
502
CE3
TRP A
89
53.463
62.605
67.044
1.00
55.77
A

ATOM
503
CD1
TRP A
89
50.201
63.231
68.477
1.00
54.82
A

ATOM
504
NE1
TRP A
89
50.649
64.480
68.136
1.00
54.93
A

ATOM
505
CZ2
TRP A
89
52.755
65.342
67.072
1.00
55.82
A

ATOM
506
CZ3
TRP A
89
54.315
63.579
66.544
1.00
55.23
A

ATOM
507
CH2
TRP A
89
53.957
64.927
66.561
1.00
55.54
A

ATOM
508
C
TRP A
89
50.915
60.332
65.831
1.00
57.32
A

ATOM
509
O
TRP A
89
50.679
61.248
65.045
1.00
57.65
A

ATOM
510
NA
SP A
90
51.827
59.398
65.593
1.00
55.46
A

ATOM
511
CA
ASP A
90
52.602
59.387
64.366
1.00
53.21
A

ATOM
512
CB
ASP A
90
53.710
58.353
64.472
1.00
51.45
A

ATOM
513
CG
ASP A
90
54.795
58.795
65.396
1.00
51.44
A

ATOM
514
OD1
ASP A
90
54.462
59.439
66.401
1.00
53.33
A

ATOM
515
OD2
ASP A
90
55.975
58.511
65.134
1.00
51.16
A

ATOM
516
C
ASP A
90
51.731
59.082
63.162
1.00
53.01
A

ATOM
517
O
ASP A
90
51.943
59.625
62.076
1.00
53.15
A

ATOM
518
N
ARG A
91
50.746
58.214
63.362
1.00
52.99
A

ATOM
519
CA
ARG A
91
49.835
57.822
62.293
1.00
52.82
A

ATOM
520
CB
ARG A
91
48.865
56.747
62.802
1.00
53.81
A

ATOM
521
CG
ARG A
91
47.856
56.264
61.770
1.00
56.18
A

ATOM
522
CD
ARG A
91
47.412
54.828
62.031
1.00
58.29
A

ATOM
523
NE
ARG A
91
46.995
54.617
63.412
1.00
61.35
A

ATOM
524
CZ
ARG A
91
45.922
55.168
63.972
1.00
62.36
A

ATOM
525
NH1
ARG A
91
45.138
55.972
63.267
1.00
64.03
A

ATOM
526
NH2
ARG A
91
45.640
54.925
65.246
1.00
63.29
A

ATOM
527
C
ARG A
91
49.065
59.014
61.728
1.00
51.91
A

ATOM
528
O
ARG A
91
48.829
59.086
60.522
1.00
51.24
A

ATOM
529
N
GLU A
92
48.683
59.946
62.599
1.00
50.83
A

ATOM
530
CA
GLU A
92
47.955
61.136
62.172
1.00
50.40
A

ATOM
531
CB
GLU A
92
47.181
61.750
63.337
1.00
52.44
A

ATOM
532
CG
GLU A
92
46.026
60.914
63.856
1.00
58.05
A

ATOM
533
CD
GLU A
92
44.989
60.594
62.787
1.00
60.95
A

ATOM
534
OE1
GLU A
92
44.493
61.541
62.125
1.00
61.85
A

ATOM
535
OE2
GLU A
92
44.670
59.392
62.621
1.00
61.47
A

ATOM
536
C
GLU A
92
48.929
62.174
61.632
1.00
48.17
A

ATOM
537
O
GLU A
92
48.689
62.784
60.589
1.00
48.86
A

ATOM
538
N
PHE A
93
50.020
62.376
62.364
1.00
45.11
A

ATOM
539
CA
PHE A
93
51.056
63.325
61.989
1.00
42.22
A

ATOM
540
CB
PHE A
93
52.241
63.197
62.930
1.00
39.86
A

ATOM
541
CG
PHE A
93
53.473
63.881
62.431
1.00
38.61
A

ATOM
542
CD1
PHE A
93
53.560
65.270
62.434
1.00
38.78
A

ATOM
543
CD2
PHE A
93
54.550
63.139
61.949
1.00
38.41
A

ATOM
544
CE1
PHE A
93
54.706
65.920
61.962
1.00
37.98
A

ATOM
545
CE2
PHE A
93
55.702
63.771
61.474
1.00
37.53
A

ATOM
546
CZ
PHE A
93
55.782
65.169
61.482
1.00
37.66
A

ATOM
547
C
PHE A
93
51.529
63.039
60.586
1.00
41.92
A

ATOM
548
O
PHE A
93
51.915
63.940
59.847
1.00
42.62
A

ATOM
549
N
LEU A
94
51.513
61.766
60.229
1.00
41.18
A

ATOM
550
CA
LEU A
94
51.938
61.368
58.913
1.00
40.65
A

ATOM
551
CB
LEU A
94
52.602
60.008
58.986
1.00
39.81
A

ATOM
552
CG
LEU A
94
53.987
60.082
59.611
1.00
40.12
A

ATOM
553
CD1
LEU A
94
54.560
58.682
59.692
1.00
40.00
A

ATOM
554
CD2
LEU A
94
54.889
60.998
58.785
1.00
38.29
A

ATOM
555
C
LEU A
94
50.792
61.333
57.927
1.00
41.17
A

ATOM
556
O
LEU A
94
51.010
61.120
56.737
1.00
41.27
A

ATOM
557
N
LYS A
95
49.575
61.553
58.413
1.00
41.25
A

ATOM
558
CA
LYS A
95
48.420
61.534
57.532
1.00
42.22
A

ATOM
559
CB
LYS A
95
47.120
61.460
58.342
1.00
43.14
A

ATOM
560
CG
LYS A
95
45.925
61.168
57.438
1.00
47.48
A

ATOM
561
CD
LYS A
95
44.586
61.331
58.138
1.00
51.30
A

ATOM
562
CE
LYS A
95
44.392
60.305
59.252
1.00
53.68
A

ATOM
563
NZ
LYS A
95
43.042
60.431
59.895
1.00
54.53
A

ATOM
564
C
LYS A
95
48.390
62.762
56.616
1.00
41.83
A

ATOM
565
O
LYS A
95
47.450
63.552
56.650
1.00
42.87
A

ATOM
566
N
VAL A
96
49.406
62.890
55.770
1.00
41.34
A

ATOM
567
CA
VAL A
96
49.545
64.023
54.856
1.00
40.71
A

ATOM
568
CB
VAL A
96
50.909
64.673
55.057
1.00
40.36
A

ATOM
569
CG1
VAL A
96
51.034
65.180
56.471
1.00
39.98
A

ATOM
570
CG2
VAL A
96
51.990
63.651
54.777
1.00
38.65
A

ATOM
571
C
VAL A
96
49.446
63.611
53.385
1.00
41.10
A

ATOM
572
O
VAL A
96
49.074
62.482
53.077
1.00
39.99
A

ATOM
573
N
ASP A
97
49.789
64.518
52.471
1.00
41.74
A

ATOM
574
CA
ASP A
97
49.729
64.155
51.064
1.00
43.35
A

ATOM
575
CB
ASP A
97
49.500
65.386
50.168
1.00
46.03
A

ATOM
576
CG
ASP A
97
50.694
66.307
50.088
1.00
49.27
A

ATOM
577
OD1
ASP A
97
51.762
65.862
49.621
1.00
51.92
A

ATOM
578
OD2
ASP A
97
50.560
67.490
50.476
1.00
50.75
A

ATOM
579
C
ASP A
97
50.976
63.369
50.642
1.00
42.71
A

ATOM
580
O
ASP A
97
52.039
63.493
51.249
1.00
42.39
A

ATOM
581
N
GLN A
98
50.815
62.549
49.606
1.00
41.92
A

ATOM
582
CA
GLN A
98
51.867
61.690
49.097
1.00
40.58
A

ATOM
583
CB
GLN A
98
51.392
60.988
47.807
1.00
42.66
A

ATOM
584
CG
GLN A
98
49.949
60.414
47.882
1.00
43.12
A

ATOM
585
CD
GLN A
98
49.666
59.270
46.905
1.00
43.62
A

ATOM
586
OE1
CLN A
98
48.516
58.876
46.720
1.00
42.97
A

ATOM
587
NE2
GLN A
98
50.712
58.732
46.290
1.00
44.27
A

ATOM
588
C
GLN A
98
53.173
62.428
48.870
1.00
39.89
A

ATOM
589
O
GLN A
98
54.234
61.905
49.180
1.00
38.30
A

ATOM
590
N
GLU A
99
53.114
63.640
48.330
1.00
40.88
A

ATOM
591
CA
GLU A
99
54.343
64.404
48.118
1.00
40.74
A

ATOM
592
CB
GLU A
99
54.035
65.695
47.377
1.00
41.69
A

ATOM
593
CG
GLU A
99
53.880
65.494
45.903
1.00
47.00
A

ATOM
594
CD
GLU A
99
55.182
65.074
45.254
1.00
48.98
A

ATOM
595
OE1
GLU A
99
56.236
65.569
45.721
1.00
50.30
A

ATOM
596
OE2
GLU A
99
55.154
64.274
44.284
1.00
48.68
A

ATOM
597
C
GLU A
99
54.984
64.710
49.474
1.00
39.87
A

ATOM
598
O
GLU A
99
56.164
64.426
49.691
1.00
39.94
A

ATOM
599
N
MSE A
100
54.187
65.272
50.382
1.00
39.05
A

ATOM
600
CA
MSE A
100
54.637
65.617
51.729
1.00
39.03
A

ATOM
601
CB
MSE A
100
53.434
66.000
52.603
1.00
45.07
A

ATOM
602
CG
MSE A
100
53.726
66.188
54.093
1.00
50.78
A

ATOM
603
SE
MSE A
100
54.480
67.900
54.500
1.00
61.41
A

ATOM
604
CE
MSE A
100
56.351
67.467
54.330
1.00
55.82
A

ATOM
605
C
MSE A
100
55.366
64.446
52.371
1.00
36.07
A

ATOM
606
O
MSE A
100
56.517
64.561
52.789
1.00
34.98
A

ATOM
607
N
LEU A
101
54.681
63.316
52.436
1.00
32.38
A

ATOM
608
CA
LEU A
101
55.238
62.126
53.031
1.00
31.39
A

ATOM
609
CB
LEU A
101
54.241
60.993
52.880
1.00
30.22
A

ATOM
610
CG
LEU A
101
54.616
59.676
53.538
1.00
29.99
A

ATOM
611
CD1
LEU A
101
54.859
59.906
55.028
1.00
29.67
A

ATOM
612
CD2
LEU A
101
53.501
58.674
53.287
1.00
26.62
A

ATOM
613
C
LEU A
101
56.571
61.745
52.394
1.00
31.59
A

ATOM
614
O
LEU A
101
57.523
61.341
53.077
1.00
32.03
A

ATOM
615
N
TYR A
102
56.624
61.872
51.076
1.00
30.32
A

ATOM
616
CA
TYR A
102
57.814
61.556
50.311
1.00
29.70
A

ATOM
617
CB
TYR A
102
57.550
61.840
48.838
1.00
29.09
A

ATOM
618
CG
TYR A
102
58.765
61.747
47.940
1.00
27.92
A

ATOM
619
CD1
TYR A
102
59.402
60.530
47.709
1.00
27.22
A

ATOM
620
CE1
TYR A
102
60.478
60.441
46.831
1.00
27.22
A

ATOM
621
CD2
TYR A
102
59.243
62.873
47.274
1.00
26.92
A

ATOM
622
CE2
TYR A
102
60.314
62.792
46.401
1.00
24.90
A

ATOM
623
CZ
TYR A
102
60.921
61.580
46.181
1.00
26.49
A

ATOM
624
OH
TYR A
102
61.959
61.497
45.299
1.00
26.37
A

ATOM
625
C
TYR A
102
58.970
62.409
50.796
1.00
30.50
A

ATOM
626
O
TYR A
102
60.057
61.905
51.125
1.00
30.28
A

ATOM
627
N
GLU A
103
58.731
63.715
50.839
1.00
31.34
A

ATOM
628
CA
GLU A
103
59.763
64.645
51.276
1.00
32.16
A

ATOM
629
CB
GLU A
103
59.314
66.088
50.966
1.00
32.79
A

ATOM
630
CG
GLU A
103
58.921
66.251
49.492
1.00
35.11
A

ATOM
631
CD
GLU A
103
58.538
67.673
49.065
1.00
37.94
A

ATOM
632
OE1
GLU A
103
57.628
68.279
49.685
1.00
37.38
A

ATOM
633
OE2
GLU A
103
59.138
68.175
48.084
1.00
37.07
A

ATOM
634
C
GLU A
103
60.128
64.438
52.760
1.00
30.98
A

ATOM
635
O
GLU A
103
61.292
64.600
53.136
1.00
30.87
A

ATOM
636
N
ILE A
104
59.159
64.038
53.588
1.00
29.27
A

ATOM
637
CA
ILE A
104
59.426
63.804
55.011
1.00
28.70
A

ATOM
638
CB
ILE A
104
58.113
63.589
55.813
1.00
28.55
A

ATOM
639
CG2
ILE A
104
58.424
62.958
57.189
1.00
29.44
A

ATOM
640
CG1
ILE A
104
57.396
64.942
55.975
1.00
26.70
A

ATOM
641
CD1
ILE A
104
56.098
64.917
56.782
1.00
22.17
A

ATOM
642
C
ILE A
104
60.359
62.609
55.221
1.00
27.96
A

ATOM
643
O
ILE A
104
61.180
62.591
56.144
1.00
26.87
A

ATOM
644
N
ILE A
105
60.225
61.609
54.360
1.00
27.92
A

ATOM
645
CA
ILE A
105
61.082
60.439
54.435
1.00
26.71
A

ATOM
646
CB
ILE A
105
60.543
59.321
53.534
1.00
26.61
A

ATOM
647
CG2
ILE A
105
61.590
58.215
53.388
1.00
25.95
A

ATOM
648
CG1
ILE A
105
59.200
58.836
54.106
1.00
26.49
A

ATOM
649
CD1
ILE A
105
58.546
57.701
53.349
1.00
26.37
A

ATOM
650
C
ILE A
105
62.500
60.825
54.017
1.00
26.46
A

ATOM
651
O
ILE A
105
63.484
60.401
54.639
1.00
26.10
A

ATOM
652
N
LEU A
106
62.603
61.648
52.975
1.00
25.01
A

ATOM
653
CA
LEU A
106
63.915
62.084
52.505
1.00
24.17
A

ATOM
654
CB
LEU A
106
63.802
62.917
51.230
1.00
23.30
A

ATOM
655
CG
LEU A
106
63.211
62.283
49.961
1.00
22.86
A

ATOM
656
CD1
LEU A
106
63.415
63.252
48.829
1.00
19.46
A

ATOM
657
CD2
LEU A
106
63.875
60.950
49.639
1.00
17.99
A

ATOM
658
C
LEU A
106
64.612
62.904
53.574
1.00
24.05
A

ATOM
659
O
LEU A
106
65.792
62.701
53.860
1.00
24.80
A

ATOM
660
N
ALA A
107
63.875
63.835
54.168
1.00
23.58
A

ATOM
661
CA
ALA A
107
64.430
64.676
55.218
1.00
23.64
A

ATOM
662
CB
ALA A
107
63.388
65.684
55.684
1.00
21.11
A

ATOM
663
C
ALA A
107
64.901
63.817
56.393
1.00
23.90
A

ATOM
664
O
ALA A
107
65.978
64.046
56.952
1.00
23.39
A

ATOM
665
N
ALA A
108
64.093
62.838
56.779
1.00
24.83
A

ATOM
666
CA
ALA A
108
64.479
61.970
57.879
1.00
27.43
A

ATOM
667
CB
ALA A
108
63.343
60.984
58.215
1.00
27.65
A

ATOM
668
C
ALA A
108
65.727
61.211
57.456
1.00
28.80
A

ATOM
669
O
ALA A
108
66.646
61.009
58.249
1.00
29.92
A

ATOM
670
N
ASN A
109
65.763
60.794
56.196
1.00
28.89
A

ATOM
671
CA
ASN A
109
66.920
60.062
55.719
1.00
29.68
A

ATOM
672
CB
ASN A
109
66.631
59.416
54.361
1.00
31.27
A

ATOM
673
CG
ASN A
109
67.744
58.480
53.915
1.00
31.80
A

ATOM
674
OD1
ASN A
109
68.755
58.912
53.362
1.00
31.60
A

ATOM
675
ND2
ASN A
109
67.568
57.186
54.178
1.00
32.93
A

ATOM
676
C
ASN A
109
68.153
60.956
55.628
1.00
30.29
A

ATOM
677
O
ASN A
109
69.248
60.524
55.959
1.00
30.81
A

ATOM
678
N
TYR A
110
67.992
62.197
55.177
1.00
31.42
A

ATOM
679
CA
TYR A
110
69.133
63.105
55.080
1.00
31.10
A

ATOM
680
CB
TYR A
110
68.756
64.363
54.312
1.00
29.98
A

ATOM
681
CG
TYR A
110
69.819
65.437
54.351
1.00
30.69
A

ATOM
682
CD1
TYR A
110
71.057
65.237
53.736
1.00
29.71
A

ATOM
683
CE1
TYR A
110
72.022
66.241
53.716
1.00
30.17
A

ATOM
684
CD2
TYR A
110
69.571
66.674
54.965
1.00
31.52
A

ATOM
685
CE2
TYR A
110
70.526
67.686
54.954
1.00
31.71
A

ATOM
686
CZ
TYR A
110
71.750
67.463
54.318
1.00
32.53
A

ATOM
687
OH
TYR A
110
72.680
68.481
54.226
1.00
33.63
A

ATOM
688
C
TYR A
110
69.620
63.515
56.463
1.00
31.73
A

ATOM
689
O
TYR A
110
70.818
63.603
56.694
1.00
32.81
A

ATOM
690
N
LEU A
111
68.682
63.770
57.371
1.00
30.92
A

ATOM
691
CA
LEU A
111
69.016
64.184
58.719
1.00
31.21
A

ATOM
692
CB
LEU A
111
67.870
64.994
59.317
1.00
28.89
A

ATOM
693
CG
LEU A
111
67.630
66.380
58.734
1.00
26.61
A

ATOM
694
CD1
LEU A
111
66.251
66.831
59.141
1.00
24.78
A

ATOM
695
CD2
LEU A
111
68.694
67.360
59.200
1.00
24.10
A

ATOM
696
C
LEU A
111
69.337
63.006
59.624
1.00
33.12
A

ATOM
697
O
LEU A
111
69.590
63.181
60.816
1.00
34.02
A

ATOM
698
N
ASN A
112
69.319
61.805
59.062
1.00
33.71
A

ATOM
699
CA
ASN A
112
69.620
60.588
59.820
1.00
34.83
A

ATOM
700
CB
ASN A
112
71.102
60.570
60.204
1.00
33.95
A

ATOM
701
CG
ASN A
112
71.644
59.164
60.365
1.00
33.26
A

ATOM
702
OD1
ASN A
112
71.015
58.322
60.977
1.00
34.03
A

ATOM
703
ND2
ASN A
112
72.820
58.913
59.813
1.00
34.72
A

ATOM
704
C
ASN A
112
68.764
60.460
61.091
1.00
35.67
A

ATOM
705
O
ASN A
112
69.272
60.582
62.209
1.00
37.75
A

ATOM
706
N
ILE A
113
67.472
60.203
60.906
1.00
35.48
A

ATOM
707
CA
ILE A
113
66.517
60.055
62.005
1.00
35.39
A

ATOM
708
CB
ILE A
113
65.531
61.253
62.034
1.00
35.97
A

ATOM
709
CG2
ILE A
113
64.563
61.125
63.200
1.00
35.08
A

ATOM
710
CG1
ILE A
113
66.307
62.567
62.154
1.00
36.19
A

ATOM
711
CD1
ILE A
113
65.427
63.795
62.132
1.00
33.68
A

ATOM
712
C
ILE A
113
65.738
58.761
61.763
1.00
35.67
A

ATOM
713
O
ILE A
113
64.564
58.789
61.381
1.00
33.98
A

ATOM
714
N
LYS A
114
66.408
57.632
61.988
1.00
37.77
A

ATOM
715
CA
LYS A
114
65.827
56.299
61.775
1.00
39.09
A

ATOM
716
CB
LYS A
114
66.697
55.238
62.461
1.00
41.82
A

ATOM
717
CG
LYS A
114
67.835
54.703
61.601
1.00
45.96
A

ATOM
718
CD
LYS A
114
68.786
55.789
61.081
1.00
47.81
A

ATOM
719
CE
LYS A
114
69.952
55.145
60.306
1.00
49.70
A

ATOM
720
NZ
LYS A
114
69.498
54.249
59.161
1.00
51.87
A

ATOM
721
C
LYS A
114
64.372
56.128
62.216
1.00
37.68
A

ATOM
722
O
LYS A
114
63.521
55.697
61.438
1.00
38.17
A

ATOM
723
N
PRO A
115
64.076
56.435
63.484
1.00
36.13
A

ATOM
724
CD
PRO A
115
65.015
56.886
64.526
1.00
34.15
A

ATOM
725
CA
PRO A
115
62.715
56.314
64.011
1.00
34.44
A

ATOM
726
CB
PRO A
115
62.815
57.022
65.351
1.00
34.06
A

ATOM
727
CG
PRO A
115
64.220
56.680
65.777
1.00
35.33
A

ATOM
728
C
PRO A
115
61.694
56.968
63.076
1.00
33.56
A

ATOM
729
O
PRO A
115
60.658
56.384
62.763
1.00
33.50
A

ATOM
730
N
LEU A
116
62.001
58.179
62.622
1.00
31.71
A

ATOM
731
CA
LEU A
116
61.108
58.903
61.733
1.00
30.40
A

ATOM
732
CB
LEU A
116
61.583
60.347
61.567
1.00
29.42
A

ATOM
733
CG
LEU A
116
60.603
61.229
60.796
1.00
28.24
A

ATOM
734
CD1
LEU A
116
59.268
61.223
61.507
1.00
28.18
A

ATOM
735
CD2
LEU A
116
61.144
62.633
60.674
1.00
29.52
A

ATOM
736
C
LEU A
116
61.005
58.211
60.375
1.00
30.54
A

ATOM
737
O
LEU A
116
59.909
58.046
59.823
1.00
29.43
A

ATOM
738
N
LEU A
117
62.150
57.804
59.836
1.00
30.80
A

ATOM
739
CA
LEU A
117
62.193
57.097
58.555
1.00
30.78
A

ATOM
740
CB
LEU A
117
63.632
56.678
58.223
1.00
28.60
A

ATOM
741
CG
LEU A
117
63.843
55.833
56.966
1.00
27.90
A

ATOM
742
CD1
LEU A
117
63.388
56.587
55.756
1.00
26.40
A

ATOM
743
CD2
LEU A
117
65.304
55.467
56.830
1.00
29.33
A

ATOM
744
C
LEU A
117
61.311
55.856
58.624
1.00
32.57
A

ATOM
745
O
LEU A
117
60.403
55.675
57.800
1.00
33.66
A

ATOM
746
N
ASP A
118
61.588
55.002
59.608
1.00
32.30
A

ATOM
747
CA
ASP A
118
60.821
53.781
59.777
1.00
32.82
A

ATOM
748
CB
ASP A
118
61.241
53.035
61.046
1.00
34.51
A

ATOM
749
CG
ASP A
118
62.660
52.481
60.958
1.00
38.01
A

ATOM
750
OD1
ASP A
118
63.075
52.088
59.841
1.00
37.92
A

ATOM
751
OD2
ASP A
118
63.355
52.432
62.007
1.00
38.31
A

ATOM
752
C
ASP A
118
59.345
54.104
59.836
1.00
32.67
A

ATOM
753
O
ASP A
118
58.533
53.458
59.160
1.00
33.71
A

ATOM
754
N
ALA A
119
58.997
55.109
60.632
1.00
31.48
A

ATOM
755
CA
ALA A
119
57.600
55.512
60.774
1.00
32.03
A

ATOM
756
CB
ALA A
119
57.512
56.753
61.625
1.00
31.77
A

ATOM
757
C
ALA A
119
56.961
55.774
59.418
1.00
32.00
A

ATOM
758
O
ALA A
119
55.932
55.185
59.071
1.00
31.09
A

ATOM
759
N
GLY A
120
57.582
56.673
58.660
1.00
32.93
A

ATOM
760
CA
GLY A
120
57.081
57.007
57.341
1.00
33.63
A

ATOM
761
C
GLY A
120
57.019
55.773
56.469
1.00
33.78
A

ATOM
762
O
GLY A
120
56.045
55.571
55.748
1.00
33.76
A

ATOM
763
N
CYS A
121
58.056
54.944
56.522
1.00
34.09
A

ATOM
764
CA
CYS A
121
58.048
53.735
55.714
1.00
37.06
A

ATOM
765
CB
CYS A
121
59.370
52.985
55.852
1.00
37.59
A

ATOM
766
SG
CYS A
121
60.672
53.684
54.825
1.00
37.93
A

ATOM
767
C
CYS A
121
56.882
52.814
56.063
1.00
36.49
A

ATOM
768
O
CYS A
121
56.222
52.272
55.177
1.00
37.36
A

ATOM
769
N
LYS A
122
56.617
52.645
57.348
1.00
36.54
A

ATOM
770
CA
LYS A
122
55.525
51.786
57.766
1.00
37.44
A

ATOM
771
CB
LYS A
122
55.445
51.751
59.288
1.00
38.22
A

ATOM
772
CG
LYS A
122
56.652
51.150
59.950
1.00
38.67
A

ATOM
773
CD
LYS A
122
56.424
51.081
61.441
1.00
42.04
A

ATOM
774
CE
LYS A
122
57.663
50.592
62.185
1.00
42.25
A

ATOM
775
NZ
LYS A
122
57.394
50.419
63.636
1.00
41.74
A

ATOM
776
C
LYS A
122
54.197
52.276
57.208
1.00
36.82
A

ATOM
777
O
LYS A
122
53.340
51.479
56.812
1.00
36.50
A

ATOM
778
N
VAL A
123
54.035
53.595
57.187
1.00
36.30
A

ATOM
779
CA
VAL A
123
52.810
54.208
56.699
1.00
35.72
A

ATOM
780
CB
VAL A
123
52.832
55.718
56.967
1.00
36.26
A

ATOM
781
CG1
VAL A
123
51.483
56.319
56.621
1.00
36.90
A

ATOM
782
CG2
VAL A
123
53.170
55.966
58.429
1.00
35.63
A

ATOM
783
C
VAL A
123
52.576
53.929
55.208
1.00
35.46
A

ATOM
784
O
VAL A
123
51.448
53.633
54.793
1.00
33.96
A

ATOM
785
N
VAL A
124
53.639
54.007
54.406
1.00
35.31
A

ATOM
786
CA
VAL A
124
53.510
53.737
52.970
1.00
34.89
A

ATOM
787
CB
VAL A
124
54.815
54.026
52.177
1.00
34.43
A

ATOM
788
CG1
VAL A
124
54.564
53.832
50.682
1.00
32.55
A

ATOM
789
CG2
VAL A
124
55.294
55.442
52.449
1.00
34.56
A

ATOM
790
C
VAL A
124
53.135
52.273
52.767
1.00
34.07
A

ATOM
791
O
VAL A
124
52.317
51.947
51.898
1.00
34.52
A

ATOM
792
N
ALA A
125
53.734
51.401
53.575
1.00
32.52
A

ATOM
793
CA
ALA A
125
53.452
49.974
53.500
1.00
33.46
A

ATOM
794
CB
ALA A
125
54.294
49.221
54.496
1.00
31.49
A

ATOM
795
C
ALA A
125
51.975
49.757
53.805
1.00
35.59
A

ATOM
796
O
ALA A
125
51.283
48.987
53.127
1.00
35.62
A

ATOM
797
N
GLU A
126
51.495
50.462
54.823
1.00
37.35
A

ATOM
798
CA
GLU A
126
50.107
50.357
55.213
1.00
37.88
A

ATOM
799
CB
GLU A
126
49.864
51.130
56.494
1.00
39.94
A

ATOM
800
CG
GLU A
126
50.589
50.522
57.658
1.00
44.44
A

ATOM
801
CD
GLU A
126
49.884
50.789
58.974
1.00
47.25
A

ATOM
802
OE1
GLU A
126
49.926
51.949
59.454
1.00
46.76
A

ATOM
803
OE2
GLU A
126
49.271
49.832
59.516
1.00
49.61
A

ATOM
804
C
GLU A
126
49.149
50.812
54.142
1.00
37.12
A

ATOM
805
O
GLU A
126
47.974
50.472
54.189
1.00
36.85
A

ATOM
806
N
MSE A
127
49.648
51.573
53.176
1.00
37.83
A

ATOM
807
CA
MSE A
127
48.814
52.035
52.085
1.00
38.50
A

ATOM
808
CB
MSE A
127
49.473
53.225
51.396
1.00
39.64
A

ATOM
809
CG
MSE A
127
49.682
54.471
52.264
1.00
40.86
A

ATOM
810
SE
MSE A
127
50.428
55.994
51.160
1.00
44.01
A

ATOM
811
CE
MSE A
127
48.774
56.477
50.261
1.00
43.47
A

ATOM
812
C
MSE A
127
48.621
50.885
51.092
1.00
38.76
A

ATOM
813
O
MSE A
127
47.586
50.792
50.443
1.00
38.95
A

ATOM
814
N
ILE A
128
49.607
49.997
51.003
1.00
39.74
A

ATOM
815
CA
ILE A
128
49.552
48.849
50.090
1.00
40.70
A

ATOM
816
CB
ILE A
128
50.989
48.359
49.755
1.00
39.21
A

ATOM
817
CG2
ILE A
128
50.935
47.158
48.828
1.00
39.17
A

ATOM
818
CG1
ILE A
128
51.797
49.518
49.163
1.00
37.59
A

ATOM
819
CD1
ILE A
128
53.148
49.159
48.595
1.00
35.03
A

ATOM
820
C
ILE A
128
48.777
47.698
50.736
1.00
42.24
A

ATOM
821
O
ILE A
128
47.886
47.098
50.132
1.00
40.92
A

ATOM
822
N
ARG A
129
49.147
47.412
51.980
1.00
46.16
A

ATOM
823
CA
ARG A
129
48.556
46.350
52.792
1.00
49.18
A

ATOM
824
CB
ARG A
129
48.696
46.701
54.268
1.00
50.29
A

ATOM
825
CG
ARG A
129
48.224
45.614
55.205
1.00
53.92
A

ATOM
826
CD
ARG A
129
48.566
45.978
56.643
1.00
58.68
A

ATOM
827
NE
ARG A
129
49.936
46.490
56.743
1.00
62.87
A

ATOM
828
CZ
ARG A
129
50.553
46.798
57.881
1.00
64.32
A

ATOM
829
NH1
ARG A
129
49.927
46.647
59.045
1.00
64.82
A

ATOM
830
NH2
ARG A
129
51.799
47.258
57.850
1.00
64.62
A

ATOM
831
C
ARG A
129
47.094
46.044
52.498
1.00
49.27
A

ATOM
832
O
ARG A
129
46.230
46.920
52.589
1.00
49.24
A

ATOM
833
N
GLY A
130
46.839
44.785
52.158
1.00
48.73
A

ATOM
834
CA
GLY A
130
45.492
44.354
51.873
1.00
49.33
A

ATOM
835
C
GLY A
130
44.843
44.937
50.632
1.00
50.07
A

ATOM
836
O
GLY A
130
43.619
44.856
50.486
1.00
49.22
A

ATOM
837
N
ARG A
131
45.630
45.523
49.735
1.00
49.98
A

ATOM
838
CA
ARG A
131
45.048
46.086
48.524
1.00
50.73
A

ATOM
839
CB
ARG A
131
45.402
47.573
48.410
1.00
51.87
A

ATOM
840
CG
ARG A
131
44.801
48.429
49.545
1.00
54.75
A

ATOM
841
CD
ARG A
131
45.035
49.929
49.340
1.00
57.52
A

ATOM
842
NE
ARG A
131
44.412
50.438
48.116
1.00
60.43
A

ATOM
843
CZ
ARG A
131
43.098
50.531
47.910
1.00
61.10
A

ATOM
844
NH1
ARG A
131
42.248
50.147
48.855
1.00
60.79
A

ATOM
845
NH2
ARG A
131
42.634
51.009
46.755
1.00
61.77
A

ATOM
846
C
ARG A
131
45.447
45.325
47.261
1.00
50.69
A

ATOM
847
O
ARG A
131
46.432
44.592
47.249
1.00
51.15
A

ATOM
848
N
SER A
132
44.670
45.494
46.199
1.00
50.35
A

ATOM
849
CA
SER A
132
44.941
44.798
44.950
1.00
50.32
A

ATOM
850
CB
SER A
132
43.630
44.489
44.224
1.00
49.61
A

ATOM
851
OG
SER A
132
43.082
45.662
43.648
1.00
48.59
A

ATOM
852
G
SER A
132
45.837
45.608
44.023
1.00
50.87
A

ATOM
853
O
SER A
132
46.056
46.808
44.235
1.00
50.23
A

ATOM
854
N
PRO A
133
46.359
44.957
42.970
1.00
50.57
A

ATOM
855
CD
PRO A
133
46.253
43.520
42.659
1.00
49.65
A

ATOM
856
CA
PRO A
133
47.230
45.628
42.006
1.00
50.93
A

ATOM
857
CB
PRO A
133
47.392
44.581
40.914
1.00
50.37
A

ATOM
858
CG
PRO A
133
47.405
43.315
41.698
1.00
50.36
A

ATOM
859
C
PRO A
133
46.616
46.915
41.483
1.00
51.56
A

ATOM
860
O
PRO A
133
47.263
47.964
41.480
1.00
52.20
A

ATOM
861
N
GLU A
134
45.364
46.839
41.044
1.00
51.94
A

ATOM
862
CA
GLU A
134
44.693
48.021
40.516
1.00
52.22
A

ATOM
863
CB
GLU A
134
43.395
47.637
39.811
1.00
54.08
A

ATOM
864
CG
GLU A
134
43.436
47.886
38.314
1.00
58.97
A

ATOM
865
CD
GLU A
134
43.821
49.320
37.974
1.00
62.39
A

ATOM
866
OE1
GLU A
134
43.122
50.254
38.436
1.00
63.15
A

ATOM
867
OE2
GLU A
134
44.823
49.513
37.243
1.00
64.67
A

ATOM
868
C
GLU A
134
44.406
49.035
41.610
1.00
50.15
A

ATOM
869
O
GLU A
134
44.400
50.244
41.355
1.00
49.58
A

ATOM
870
N
GLU A
135
44.177
48.539
42.823
1.00
47.26
A

ATOM
871
CA
GLU A
135
43.904
49.412
43.948
1.00
45.19
A

ATOM
872
CB
GLU A
135
43.390
48.613
45.142
1.00
44.69
A

ATOM
873
CG
GLU A
135
41.973
48.135
44.948
1.00
47.13
A

ATOM
874
CD
GLU A
135
41.333
47.585
46.207
1.00
49.00
A

ATOM
875
OE1
GLU A
135
41.857
46.590
46.766
1.00
49.49
A

ATOM
876
OE2
GLU A
135
40.295
48.153
46.633
1.00
50.00
A

ATOM
877
C
GLU A
135
45.160
50.162
44.328
1.00
43.66
A

ATOM
878
O
GLU A
135
45.113
51.349
44.650
1.00
42.57
A

ATOM
879
N
ILE A
136
46.288
49.467
44.269
1.00
41.78
A

ATOM
880
CA
ILE A
136
47.558
50.077
44.622
1.00
41.23
A

ATOM
881
CB
ILE A
136
48.646
49.014
44.782
1.00
39.22
A

ATOM
882
CG2
ILE A
136
49.957
49.675
45.197
1.00
37.75
A

ATOM
883
CG1
ILE A
136
48.180
47.970
45.801
1.00
37.01
A

ATOM
884
CD1
ILE A
136
49.154
46.847
46.033
1.00
34.37
A

ATOM
885
C
ILE A
136
47.993
51.065
43.558
1.00
42.50
A

ATOM
886
O
ILE A
136
48.490
52.162
43.856
1.00
42.93
A

ATOM
887
N
ARG A
137
47.787 50.651
42.314
1.00
42.34
A

ATOM
888
CA
ARG A
137
48.144
51.439
41.151
1.00
41.82
A

ATOM
889
CB
ARG A
137
47.844
50.636
39.884
1.00
42.65
A

ATOM
890
CG
ARG A
137
48.949
50.635
38.849
1.00
43.90
A

ATOM
891
CD
ARG A
137
48.594
49.715
37.679
1.00
45.63
A

ATOM
892
NE
ARG A
137
48.503
48.315
38.092
1.00
47.76
A

ATOM
893
CZ
ARG A
137
47.567
47.477
37.664
1.00
48.21
A

ATOM
894
NH1
ARG A
137
46.644
47.901
36.810
1.00
49.10
A

ATOM
895
NH2
ARG A
137
47.546
46.226
38.099
1.00
48.10
A

ATOM
896
C
ARG A
137
47.348
52.736
41.156
1.00
40.67
A

ATOM
897
O
ARG A
137
47.821
53.773
40.685
1.00
39.93
A

ATOM
898
N
ARG A
138
46.134
52.677
41.694
1.00
40.67
A

ATOM
899
CA
ARG A
138
45.276
53.864
41.756
1.00
40.88
A

ATOM
900
CB
ARG A
138
43.807
53.456
41.932
1.00
39.95
A

ATOM
901
CG
ARG A
138
43.140
52.934
40.660
0.00
41.86
A

ATOM
902
CD
ARG A
138
43.070
53.989
39.550
0.00
42.76
A

ATOM
903
NE
ARG A
138
44.301
54.072
38.764
0.00
43.72
A

ATOM
904
CZ
ARG A
138
44.443
54.802
37.659
0.00
44.10
A

ATOM
905
NH1
ARG A
138
43.430
55.523
37.196
0.00
44.35
A

ATOM
906
NH2
ARG A
138
45.602
54.812
37.015
0.00
44.35
A

ATOM
907
C
ARG A
138
45.706
54.791
42.895
1.00
39.80
A

ATOM
908
O
ARG A
138
45.705
56.016
42.762
1.00
39.09
A

ATOM
909
N
THR A
139
46.083
54.177
44.008
1.00
39.87
A

ATOM
910
CA
THR A
139
46.544
54.877
45.193
1.00
39.93
A

ATOM
911
CB
THR A
139
47.058
53.872
46.234
1.00
40.30
A

ATOM
912
OG1
THR A
139
45.971
53.054
46.689
1.00
40.58
A

ATOM
913
CG2
THR A
139
47.684
54.602
47.420
1.00
41.79
A

ATOM
914
C
THR A
139
47.674
55.849
44.881
1.00
41.13
A

ATOM
915
O
THR A
139
47.752
56.941
45.455
1.00
42.14
A

ATOM
916
N
PHE A
140
48.559
55.443
43.978
1.00
41.08
A

ATOM
917
CA
PHE A
140
49.705
56.267
43.607
1.00
39.57
A

ATOM
918
CB
PHE A
140
50.986
55.449
43.755
1.00
38.91
A

ATOM
919
CG
PHE A
140
51.220
54.943
45.145
1.00
38.38
A

ATOM
920
CD1
PHE A
140
51.519
55.824
46.174
1.00
38.13
A

ATOM
921
CD2
PHE A
140
51.122
53.588
45.432
1.00
37.94
A

ATOM
922
GE1
PHE A
140
51.722
55.364
47.464
1.00
38.18
A

ATOM
923
GE2
PHE A
140
51.323
53.118
46.721
1.00
37.42
A

ATOM
924
CZ
PHE A
140
51.622
54.008
47.739
1.00
38.51
A

ATOM
925
C
PHE A
140
49.600
56.779
42.185
1.00
39.01
A

ATOM
926
O
PHE A
140
50.512
57.434
41.685
1.00
39.06
A

ATOM
927
N
ASN A
141
48.485
56.483
41.537
1.00
38.54
A

ATOM
928
CA
ASN A
141
48.294
56.894
40.162
1.00
38.58
A

ATOM
929
CB
ASN A
141
48.220
58.407
40.049
1.00
39.46
A

ATOM
930
CG
ASN A
141
47.787
58.847
38.669
1.00
41.82
A

ATOM
931
OD1
ASN A
141
46.655
58.592
38.257
1.00
44.53
A

ATOM
932
ND2
ASN A
141
48.687
59.495
37.938
1.00
42.34
A

ATOM
933
C
ASN A
141
49.439
56.378
39.296
1.00
38.74
A

ATOM
934
O
ASN A
141
50.031
57.122
38.503
1.00
38.59
A

ATOM
935
N
ILE A
142
49.738
55.093
39.459
1.00
38.05
A

ATOM
936
CA
ILE A
142
50.800
54.429
38.715
1.00
37.68
A

ATOM
937
CB
ILE A
142
51.425
53.321
39.561
1.00
36.00
A

ATOM
938
CG2
ILE A
142
52.451
52.563
38.755
1.00
34.95
A

ATOM
939
CG1
ILE A
142
52.021
53.921
40.829
1.00
35.82
A

ATOM
940
CD1
ILE A
142
52.449
52.875
41.837
1.00
36.82
A

ATOM
941
C
ILE A
142
50.239
53.819
37.440
1.00
38.81
A

ATOM
942
O
ILE A
142
49.121
53.321
37.441
1.00
39.45
A

ATOM
943
N
VAL A
143
51.022
53.855
36.361
1.00
40.31
A

ATOM
944
CA
VAL A
143
50.620
53.310
35.053
1.00
40.27
A

ATOM
945
CB
VAL A
143
51.373
54.017
33.905
1.00
42.11
A

ATOM
946
CG1
VAL A
143
51.035
53.348
32.567
1.00
42.72
A

ATOM
947
CG2
VAL A
143
51.016
55.493
33.877
1.00
41.43
A

ATOM
948
C
VAL A
143
50.868
51.808
34.881
1.00
39.19
A

ATOM
949
O
VAL A
143
51.955
51.309
35.172
1.00
38.15
A

ATOM
950
N
ASN A
144
49.869
51.107
34.359
1.00
38.94
A

ATOM
951
CA
ASN A
144
49.968
49.670
34.137
1.00
39.16
A

ATOM
952
CB
ASN A
144
48.575
49.048
34.256
1.00
39.51
A

ATOM
953
CG
ASN A
144
48.570
47.573
33.959
1.00
40.78
A

ATOM
954
OD1
ASN A
144
49.586
46.903
34.090
1.00
44.00
A

ATOM
955
ND2
ASN A
144
47.421
47.052
33.574
1.00
41.05
A

ATOM
956
C
ASN A
144
50.582
49.341
32.775
1.00
38.55
A

ATOM
957
O
ASN A
144
49.876
48.975
31.839
1.00
37.91
A

ATOM
958
N
ASP A
145
51.902
49.448
32.685
1.00
38.25
A

ATOM
959
CA
ASP A
145
52.624
49.190
31.440
1.00
39.85
A

ATOM
960
CB
ASP A
145
53.996
49.862
31.498
1.00
39.46
A

ATOM
961
CG
ASP A
145
54.766
49.490
32.750
1.00
39.69
A

ATOM
962
OD1
ASP A
145
54.213
48.735
33.587
1.00
39.21
A

ATOM
963
OD2
ASP A
145
55.918
49.947
32.895
1.00
38.21
A

ATOM
964
C
ASP A
145
52.798
47.712
31.092
1.00
40.13
A

ATOM
965
O
ASP A
145
53.702
47.343
30.337
1.00
39.56
A

ATOM
966
N
PHE A
146
51.938
46.870
31.652
1.00
40.47
A

ATOM
967
CA
PHE A
146
51.978
45.440
31.377
1.00
40.10
A

ATOM
968
CB
PHE A
146
51.371
44.644
32.541
1.00
39.31
A

ATOM
969
CG
PHE A
146
52.301
44.453
33.699
1.00
40.02
A

ATOM
970
CD1
PHE A
146
53.534
43.850
33.520
1.00
39.21
A

ATOM
971
CD2
PHE A
146
51.952
44.889
34.971
1.00
39.97
A

ATOM
972
CE1
PHE A
146
54.407
43.690
34.591
1.00
39.41
A

ATOM
973
CE2
PHE A
146
52.827
44.731
36.051
1.00
38.93
A

ATOM
974
CZ
PHE A
146
54.053
44.131
35.858
1.00
38.17
A

ATOM
975
C
PHE A
146
51.167
45.171
30.113
1.00
40.82
A

ATOM
976
O
PHE A
146
50.013
45.603
29.999
1.00
41.89
A

ATOM
977
N
THR A
147
51.773
44.476
29.154
1.00
40.38
A

ATOM
978
CA
THR A
147
51.073
44.137
27.922
1.00
38.81
A

ATOM
979
CB
THR A
147
51.999
43.509
26.877
1.00
38.98
A

ATOM
980
OG1
THR A
147
52.651
42.373
27.456
1.00
39.24
A

ATOM
981
CG2
THR A
147
53.030
44.498
26.395
1.00
36.50
A

ATOM
982
C
THR A
147
50.062
43.070
28.286
1.00
38.78
A

ATOM
983
O
THR A
147
50.233
42.343
29.268
1.00
37.08
A

ATOM
984
N
PRO A
148
49.003
42.943
27.485
1.00
39.53
A

ATOM
985
CD
PRO A
148
48.718
43.722
26.266
1.00
39.08
A

ATOM
986
CA
PRO A
148
47.958
41.947
27.732
1.00
40.59
A

ATOM
987
CB
PRO A
148
47.166
41.970
26.428
1.00
39.52
A

ATOM
988
CG
PRO A
148
47.260
43.419
26.034
1.00
39.40
A

ATOM
989
C
PRO A
148
48.505
40.545
28.078
1.00
42.69
A

ATOM
990
O
PRO A
148
48.007
39.876
28.984
1.00
43.05
A

ATOM
991
N
GLU A
149
49.546
40.123
27.370
1.00
45.32
A

ATOM
992
CA
GLU A
149
50.155
38.814
27.572
1.00
46.47
A

ATOM
993
CB
GLU A
149
51.059
38.496
26.395
1.00
44.18
A

ATOM
994
CG
GLU A
149
51.681
37.137
26.430
1.00
43.56
A

ATOM
995
CD
GLU A
149
52.660
36.955
25.311
1.00
43.86
A

ATOM
996
OE1
GLU A
149
53.660
37.699
25.279
1.00
43.12
A

ATOM
997
OE2
GLU A
149
52.430
36.075
24.458
1.00
44.44
A

ATOM
998
C
GLU A
149
50.974
38.773
28.845
1.00
48.79
A

ATOM
999
O
GLU A
149
50.852
37.856
29.660
1.00
49.11
A

ATOM
1000
N
GLU A
150
51.826
39.773
29.006
1.00
52.88
A

ATOM
1001
CA
GLU A
150
52.676
39.855
30.180
1.00
56.79
A

ATOM
1002
CB
GLU A
150
53.548
41.105
30.090
1.00
56.56
A

ATOM
1003
CG
GLU A
150
54.707
41.109
31.045
1.00
57.96
A

ATOM
1004
CD
GLU A
150
55.774
40.103
30.660
1.00
59.33
A

ATOM
1005
OE1
GLU A
150
55.489
38.887
30.639
1.00
60.34
A

ATOM
1006
OE2
GLU A
150
56.907
40.533
30.372
1.00
60.87
A

ATOM
1007
C
GLU A
150
51.804
39.913
31.433
1.00
59.23
A

ATOM
1008
O
GLU A
150
52.187
39.417
32.488
1.00
59.36
A

ATOM
1009
N
GLU A
151
50.627
40.519
31.305
1.00
62.33
A

ATOM
1010
CA
GLU A
151
49.701
40.651
32.424
1.00
64.96
A

ATOM
1011
CB
GLU A
151
48.477
41.452
31.982
1.00
65.44
A

ATOM
1012
CG
GLU A
151
48.102
42.579
32.923
1.00
66.38
A

ATOM
1013
CD
GLU A
151
47.141
43.563
32.287
1.00
67.52
A

ATOM
1014
OE1
GLU A
151
47.510
44.187
31.269
1.00
67.49
A

ATOM
1015
OE2
GLU A
151
46.014
43.713
32.803
1.00
68.18
A

ATOM
1016
C
GLU A
151
49.270
39.286
32.954
1.00
66.62
A

ATOM
1017
O
GLU A
151
49.543
38.943
34.104
1.00
66.87
A

ATOM
1018
N
ALA A
152
48.602
38.512
32.106
1.00
68.29
A

ATOM
1019
CA
ALA A
152
48.137
37.181
32.474
1.00
70.15
A

ATOM
1020
CB
ALA A
152
47.511
36.503
31.268
1.00
70.09
A

ATOM
1021
C
ALA A
152
49.280
36.327
33.014
1.00
71.79
A

ATOM
1022
O
ALA A
152
49.085
35.503
33.903
1.00
71.18
A

ATOM
1023
N
ALA A
153
50.477
36.526
32.475
1.00
74.38
A

ATOM
1024
CA
ALA A
153
51.632
35.761
32.917
1.00
76.96
A

ATOM
1025
CB
ALA A
153
52.834
36.056
32.020
1.00
76.52
A

ATOM
1026
C
ALA A
153
51.969
36.069
34.376
1.00
79.23
A

ATOM
1027
O
ALA A
153
53.040
35.700
34.863
1.00
80.18
A

ATOM
1028
N
ILE A
154
51.061
36.759
35.067
1.00
80.86
A

ATOM
1029
CA
ILE A
154
51.257
37.103
36.479
1.00
82.60
A

ATOM
1030
CB
ILE A
154
51.680
38.592
36.656
1.00
81.99
A

ATOM
1031
CG2
ILE A
154
51.889
38.898
38.134
0.00
82.34
A

ATOM
1032
CG1
ILE A
154
52.986
38.866
35.905
1.00
81.41
A

ATOM
1033
CD1
ILE A
154
53.347
40.336
35.822
0.00
81.80
A

ATOM
1034
C
ILE A
154
49.976
36.834
37.285
1.00
83.80
A

ATOM
1035
O
ILE A
154
49.036
37.633
37.272
1.00
83.56
A

ATOM
1036
N
ARG A
155
49.956
35.697
37.982
1.00
85.60
A

ATOM
1037
CA
ARG A
155
48.807
35.284
38.783
1.00
86.76
A

ATOM
1038
CB
ARG A
155
48.632
36.208
39.992
0.00
87.40
A

ATOM
1039
CG
ARG A
155
49.431
35.788
41.222
0.00
88.39
A

ATOM
1040
CD
ARG A
155
50.925
35.725
40.946
0.00
89.22
A

ATOM
1041
NE
ARG A
155
51.668
35.196
42.087
0.00
89.99
A

ATOM
1042
CZ
ARG A
155
51.561
33.949
42.535
0.00
90.38
A

ATOM
1043
NH1
ARG A
155
50.740
33.095
41.937
0.00
90.63
A

ATOM
1044
NH2
ARG A
155
52.272
33.555
43.584
0.00
90.63
A

ATOM
1045
C
ARG A
155
47.543
35.286
37.933
1.00
87.04
A

ATOM
1046
O
ARG A
155
46.710
36.199
38.125
1.00
87.33
A

ATOM
1047
OXT
ARG A
155
47.413
34.380
37.075
1.00
86.76
A

ATOM
1048
CB
LED B
270
49.350
65.486
42.241
1.00
56.04
B

ATOM
1049
CG
LED B
270
48.859
64.640
41.059
1.00
56.55
B

ATOM
1050
CD1
LED B
270
47.337
64.629
41.020
1.00
55.59
B

ATOM
1051
CD2
LEU B
270
49.424
65.209
39.762
1.00
56.75
B

ATOM
1052
C
LED B
270
49.537
63.882
44.208
1.00
54.79
B

ATOM
1053
O
LEU B
270
50.136
63.918
45.287
1.00
55.23
B

ATOM
1054
N
LED B
270
49.056
66.304
44.560
1.00
56.05
B

ATOM
1055
CA
LED B
270
48.835
65.142
43.652
1.00
55.53
B

ATOM
1056
N
LYS B
271
49.463
62.779
43.462
1.00
52.96
B

ATOM
1057
CA
LYS B
271
50.053
61.495
43.865
1.00
49.38
B

ATOM
1058
CB
LYS B
271
49.292
60.338
43.210
1.00
48.76
B

ATOM
1059
CG
LYS B
271
47.793
60.523
43.065
1.00
48.20
B

ATOM
1060
CD
LYS B
271
47.049
59.967
44.264
1.00
48.26
B

ATOM
1061
CE
LYS B
271
45.545
59.892
44.014
1.00
46.84
B

ATOM
1062
NZ
LYS B
271
45.188
59.152
42.766
1.00
47.61
B

ATOM
1063
C
LYS B
271
51.521
61.364
43.462
1.00
47.55
B

ATOM
1064
O
LYS B
271
52.069
62.218
42.764
1.00
47.27
B

ATOM
1065
N
ARG B
272
52.138
60.263
43.883
1.00
45.44
B

ATOM
1066
CA
ARG B
272
53.529
59.981
43.558
1.00
42.97
B

ATOM
1067
CB
ARG B
272
54.444
60.845
44.404
1.00
42.52
B

ATOM
1068
CG
ARG B
272
55.897
60.542
44.181
1.00
44.05
B

ATOM
1069
CD
ARG B
272
56.741
61.677
44.691
1.00
45.19
B

ATOM
1070
NE
ARG B
272
57.927
61.836
43.866
1.00
46.68
B

ATOM
1071
CZ
ARG B
272
58.416
63.009
43.491
1.00
47.36
B

ATOM
1072
NH1
ARG B
272
57.816
64.130
43.868
1.00
46.52
B

ATOM
1073
NH2
ARG B
272
59.505
63.056
42.737
1.00
48.34
B

ATOM
1074
C
ARG B
272
53.911
58.517
43.753
1.00
41.43
B

ATOM
1075
O
ARG B
272
53.678
57.944
44.816
1.00
41.22
B

ATOM
1076
N
ASP B
273
54.495
57.911
42.724
1.00
39.99
B

ATOM
1077
CA
ASP B
273
54.914
56.517
42.821
1.00
37.49
B

ATOM
1078
CB
ASP B
273
55.435
56.006
41.487
1.00
38.41
B

ATOM
1079
CG
ASP B
273
55.631
54.508
41.482
1.00
40.70
B

ATOM
1080
OD1
ASP B
273
56.269
53.969
42.423
1.00
39.39
B

ATOM
1081
OD2
ASP B
273
55.143
53.874
40.525
1.00
43.85
B

ATOM
1082
C
ASP B
273
56.040
56.474
43.829
1.00
35.40
B

ATOM
1083
O
ASP B
273
57.218
56.453
43.463
1.00
33.99
B

ATOM
1084
N
LEU B
274
55.671
56.460
45.101
1.00
33.28
B

ATOM
1085
CA
LEU B
274
56.646
56.450
46.170
1.00
32.55
B

ATOM
1086
CB
LEU B
274
55.937
56.322
47.514
1.00
32.85
B

ATOM
1087
CG
LEU B
274
55.728
57.659
48.229
1.00
34.16
B

ATOM
1088
CD1
LEU B
274
54.930
58.598
47.361
1.00
33.65
B

ATOM
1089
CD2
LEU B
274
55.035
57.421
49.561
1.00
35.07
B

ATOM
1090
C
LEU B
274
57.723
55.391
46.066
1.00
31.70
B

ATOM
1091
O
LEU B
274
58.903
55.687
46.250
1.00
31.68
B

ATOM
1092
N
ILE B
275
57.338
54.160
45.756
1.00
31.28
B

ATOM
1093
CA
ILE B
275
58.338
53.115
45.687
1.00
30.61
B

ATOM
1094
CB
ILE B
275
57.703
51.700
45.636
1.00
31.77
B

ATOM
1095
CG2
ILE B
275
56.364
51.696
46.322
1.00
29.79
B

ATOM
1096
CG1
ILE B
275
57.579
51.245
44.196
1.00
34.36
B

ATOM
1097
CD1
ILE B
275
58.058
49.838
44.000
1.00
34.82
B

ATOM
1098
C
ILE B
275
59.325
53.301
44.535
1.00
29.10
B

ATOM
1099
O
ILE B
275
60.495
52.944
44.675
1.00
28.41
B

ATOM
1100
N
THR B
276
58.893
53.846
43.398
1.00
28.07
B

ATOM
1101
CA
THR B
276
59.875
54.056
42.336
1.00
29.79
B

ATOM
1102
CB
THR B
276
59.259
54.160
40.906
1.00
29.82
B

ATOM
1103
OG1
THR B
276
58.327
55.236
40.859
1.00
33.40
B

ATOM
1104
CG2
THR B
276
58.569
52.869
40.507
1.00
31.42
B

ATOM
1105
C
THR B
276
60.718
55.314
42.580
1.00
28.87
B

ATOM
1106
O
THR B
276
61.885
55.341
42.222
1.00
29.74
B

ATOM
1107
N
SER B
277
60.145
56.333
43.211
1.00
27.47
B

ATOM
1108
CA
SER B
277
60.867
57.567
43.454
1.00
27.08
B

ATOM
1109
CB
SER B
277
59.877
58.706
43.664
1.00
28.54
B

ATOM
1110
OG
SER B
277
59.027
58.861
42.533
1.00
29.07
B

ATOM
1111
C
SER B
277
61.843
57.511
44.622
1.00
28.04
B

ATOM
1112
O
SER B
277
62.850
58.200
44.607
1.00
29.44
B

ATOM
1113
N
LEU B
278
61.546
56.717
45.644
1.00
28.55
B

ATOM
1114
CA
LEU B
278
62.443
56.606
46.786
1.00
28.04
B

ATOM
1115
CB
LEU B
278
61.777
55.854
47.921
1.00
27.87
B

ATOM
1116
CG
LEU B
278
61.098
56.650
49.043
1.00
29.93
B

ATOM
1117
CD1
LEU B
278
62.130
57.593
49.658
1.00
30.19
B

ATOM
1118
CD2
LEU B
278
59.898
57.407
48.526
1.00
28.70
B

ATOM
1119
C
LEU B
278
63.697
55.857
46.401
1.00
29.78
B

ATOM
1120
O
LEU B
278
63.728
55.140
45.398
1.00
30.41
B

ATOM
1121
N
PRO B
279
64.771
56.039
47.171
1.00
30.02
B

ATOM
1122
CD
PRO B
279
65.103
57.050
48.187
1.00
29.94
B

ATOM
1123
CA
PRO B
279
65.948
55.281
46.764
1.00
30.32
B

ATOM
1124
CB
PRO B
279
67.068
55.907
47.584
1.00
29.20
B

ATOM
1125
CG
PRO B
279
66.371
56.499
48.763
1.00
31.41
B

ATOM
1126
C
PRO B
279
65.690
53.813
47.094
1.00
32.64
B

ATOM
1127
O
PRO B
279
64.946
53.494
48.026
1.00
32.21
B

ATOM
1128
N
PHE B
280
66.291
52.927
46.308
1.00
34.93
B

ATOM
1129
CA
PHE B
280
66.122
51.495
46.476
1.00
35.83
B

ATOM
1130
CB
PHE B
280
67.177
50.745
45.671
1.00
35.18
B

ATOM
1131
CG
PHE B
280
67.040
49.266
45.752
1.00
35.73
B

ATOM
1132
CD1
PHE B
280
65.871
48.644
45.307
1.00
35.82
B

ATOM
1133
CD2
PHE B
280
68.050
48.493
46.319
1.00
34.88
B

ATOM
1134
CE1
PHE B
280
65.703
47.266
45.430
1.00
37.94
B

ATOM
1135
CE2
PHE B
280
67.897
47.111
46.452
1.00
36.63
B

ATOM
1136
CZ
PHE B
280
66.717
46.489
46.006
1.00
36.74
B

ATOM
1137
C
PHE B
280
66.172
51.017
47.917
1.00
37.41
B

ATOM
1138
O
PHE B
280
65.263
50.331
48.371
1.00
39.64
B

ATOM
1139
N
GLU B
281
67.235
51.366
48.634
1.00
38.02
B

ATOM
1140
CA
GLU B
281
67.391
50.934
50.017
1.00
38.96
B

ATOM
1141
CB
GLU B
281
68.622
51.584
50.659
1.00
42.67
B

ATOM
1142
CG
GLU B
281
69.932
51.424
49.875
1.00
49.17
B

ATOM
1143
CD
GLU B
281
70.188
49.992
49.394
1.00
51.93
B

ATOM
1144
OE1
GLU B
281
69.840
49.030
50.127
1.00
51.55
B

ATOM
1145
OE2
GLU B
281
70.747
49.845
48.276
1.00
53.97
B

ATOM
1146
C
GLU B
281
66.169
51.251
50.859
1.00
38.70
B

ATOM
1147
O
GLU B
281
65.863
50.516
51.796
1.00
40.56
B

ATOM
1148
N
ILE B
282
65.472
52.338
50.531
1.00
36.39
B

ATOM
1149
CA
ILE B
282
64.289
52.728
51.291
1.00
33.47
B

ATOM
1150
CB
ILE B
282
64.019
54.250
51.194
1.00
33.48
B

ATOM
1151
CG2
ILE B
282
62.633
54.581
51.721
1.00
31.07
B

ATOM
1152
CG1
ILE B
282
65.091
55.007
51.974
1.00
33.33
B

ATOM
1153
CD1
ILE B
282
64.849
56.494
52.090
1.00
35.69
B

ATOM
1154
C
ILE B
282
63.030
51.984
50.891
1.00
32.60
B

ATOM
1155
O
ILE B
282
62.238
51.614
51.748
1.00
33.74
B

ATOM
1156
N
SER B
283
62.833
51.753
49.602
1.00
32.28
B

ATOM
1157
CA
SER B
283
61.632
51.052
49.180
1.00
31.76
B

ATOM
1158
CB
SER B
283
61.531
51.043
47.665
1.00
30.24
B

ATOM
1159
OG
SER B
283
60.948
52.260
47.227
1.00
30.65
B

ATOM
1160
C
SER B
283
61.554
49.642
49.732
1.00
32.64
B

ATOM
1161
O
SER B
283
60.460
49.145
50.033
1.00
31.74
B

ATOM
1162
N
LEU B
284
62.715
49.011
49.891
1.00
34.08
B

ATOM
1163
CA
LEU B
284
62.761
47.661
50.433
1.00
36.79
B

ATOM
1164
CB
LEU B
284
64.158
47.070
50.303
1.00
38.54
B

ATOM
1165
CG
LEU B
284
64.620
46.663
48.913
1.00
40.73
B

ATOM
1166
CO1
LEU B
284
65.953
45.935
49.085
1.00
41.39
B

ATOM
1167
CD2
LEU B
284
63.598
45.746
48.237
1.00
39.81
B

ATOM
1168
C
LEU B
284
62.331
47.606
51.903
1.00
37.57
B

ATOM
1169
O
LEU B
284
61.731
46.629
52.333
1.00
37.16
B

ATOM
1170
N
LYS B
285
62.654
48.636
52.679
1.00
37.42
B

ATOM
1171
CA
LYS B
285
62.258
48.638
54.071
1.00
37.32
B

ATOM
1172
CB
LYS B
285
62.706
49.927
54.757
1.00
37.90
B

ATOM
1173
CG
LYS B
285
64.221
50.101
54.711
1.00
41.29
B

ATOM
1174
CD
LYS B
285
64.714
51.417
55.305
1.00
43.06
B

ATOM
1175
CE
LYS B
285
64.504
51.487
56.811
1.00
44.78
B

ATOM
1176
NZ
LYS B
285
63.347
52.365
57.139
1.00
44.95
B

ATOM
1177
C
LYS B
285
60.754
48.531
54.078
1.00
36.58
B

ATOM
1178
O
LYS B
285
60.170
47.774
54.859
1.00
36.75
B

ATOM
1179
N
ILE B
286
60.137
49.268
53.163
1.00
34.81
B

ATOM
1180
CA
ILE B
286
58.687
49.286
53.038
1.00
34.65
B

ATOM
1181
CB
ILE B
286
58.233
50.340
51.988
1.00
35.18
B

ATOM
1182
CG2
ILE B
286
56.723
50.435
51.961
1.00
34.75
B

ATOM
1183
CG1
ILE B
286
58.778
51.721
52.361
1.00
36.78
B

ATOM
1184
CD1
ILE B
286
58.517
52.777
51.304
1.00
35.35
B

ATOM
1185
C
ILE B
286
58.141
47.909
52.646
1.00
34.49
B

ATOM
1186
O
ILE B
286
57.109
47.469
53.163
1.00
34.87
B

ATOM
1187
N
PHE B
287
58.825
47.232
51.726
1.00
32.88
B

ATOM
1188
CA
PHE B
287
58.373
45.915
51.300
1.00
30.31
B

ATOM
1189
CB
PHE B
287
59.086
45.501
50.002
1.00
26.38
B

ATOM
1190
CG
PHE B
287
58.530
46.184
48.785
1.00
23.19
B

ATOM
1191
CD1
PHE B
287
57.189
46.000
48.444
1.00
21.80
B

ATOM
1192
CD2
PHE B
287
59.300
47.078
48.043
1.00
20.28
B

ATOM
1193
CE1
PHE B
287
56.617
46.699
47.397
1.00
21.72
B

ATOM
1194
CE2
PHE B
287
58.740
47.788
46.985
1.00
21.62
B

ATOM
1195
CZ
PHE B
287
57.389
47.599
46.659
1.00
23.65
B

ATOM
1196
C
PHE B
287
58.566
44.899
52.419
1.00
31.61
B

ATOM
1197
O
PHE B
287
57.864
43.887
52.487
1.00
32.92
B

ATOM
1198
N
ASN B
288
59.498
45.191
53.320
1.00
32.92
B

ATOM
1199
CA
ASN B
288
59.747
44.316
54.460
1.00
34.33
B

ATOM
1200
CB
ASN B
288
61.117
44.574
55.067
1.00
34.27
B

ATOM
1201
CG
ASN B
288
62.228
43.993
54.243
1.00
35.15
B

ATOM
1202
OD1
ASN B
288
62.325
42.768
54.077
1.00
34.77
B

ATOM
1203
ND2
ASN B
288
63.086
44.865
53.717
1.00
37.02
B

ATOM
1204
C
ASN B
288
58.699
44.515
55.538
1.00
34.60
B

ATOM
1205
O
ASN B
288
58.700
43.801
56.537
1.00
35.55
B

ATOM
1206
N
TYR B
289
57.833
45.507
55.347
1.00
33.60
B

ATOM
1207
CA
TYR B
289
56.757
45.786
56.286
1.00
32.28
B

ATOM
1208
CB
TYR B
289
56.597
47.288
56.536
1.00
30.88
B

ATOM
1209
CG
TYR B
289
57.639
47.906
57.444
1.00
31.04
B

ATOM
1210
CD1
TYR B
289
57.824
47.445
58.743
1.00
29.76
B

ATOM
1211
CE1
TYR B
289
58.783
48.005
59.577
1.00
28.80
B

ATOM
1212
CD2
TYR B
289
58.441
48.954
57.001
1.00
30.42
B

ATOM
1213
CE2
TYR B
289
59.404
49.520
57.828
1.00
30.11
B

ATOM
1214
CZ
TYR B
289
59.572
49.036
59.117
1.00
29.29
B

ATOM
1215
OH
TYR B
289
60.550
49.565
59.927
1.00
27.49
B

ATOM
1216
C
TYR B
289
55.454
45.259
55.712
1.00
33.20
B

ATOM
1217
O
TYR B
289
54.381
45.681
56.131
1.00
34.61
B

ATOM
1218
N
LEU B
290
55.538
44.348
54.750
1.00
32.98
B

ATOM
1219
CA
LEU B
290
54.335
43.794
54.148
1.00
33.98
B

ATOM
1220
CB
LEU B
290
54.181
44.325
52.736
1.00
33.99
B

ATOM
1221
CG
LEU B
290
53.894
45.813
52.594
1.00
34.25
B

ATOM
1222
CD1
LEU B
290
53.690
46.102
51.123
1.00
32.35
B

ATOM
1223
CD2
LEU B
290
52.629
46.192
53.393
1.00
35.31
B

ATOM
1224
C
LEU B
290
54.340
42.284
54.112
1.00
35.59
B

ATOM
1225
O
LEU B
290
55.366
41.686
53.832
1.00
37.73
B

ATOM
1226
N
GLN B
291
53.200
41.660
54.390
1.00
36.68
B

ATOM
1227
CA
GLN B
291
53.126
40.198
54.364
1.00
37.99
B

ATOM
1228
CB
GLN B
291
51.808
39.715
54.956
1.00
39.90
B

ATOM
1229
CGG
LN B
291
51.514
40.243
56.338
1.00
42.72
B

ATOM
1230
CD
GLN B
291
50.510
39.378
57.067
1.00
45.38
B

ATOM
1231
OE1
GLN B
291
49.376
39.196
56.609
1.00
45.17
B

ATOM
1232
NE2
GLN B
291
50.925
38.824
58.209
1.00
48.06
B

ATOM
1233
C
GLN B
291
53.254
39.696
52.937
1.00
37.97
B

ATOM
1234
O
GLN B
291
52.727
40.304
52.005
1.00
37.21
B

ATOM
1235
N
PHE B
292
53.924
38.566
52.769
1.00
39.53
B

ATOM
1236
CA
PHE B
292
54.154
38.038
51.430
1.00
42.10
B

ATOM
1237
CB
PHE B
292
54.592
36.565
51.510
1.00
43.75
B

ATOM
1238
CG
PHE B
292
53.463
35.605
51.727
1.00
44.90
B

ATOM
1239
CD1
PHE B
292
52.799
35.038
50.641
1.00
43.90
B

ATOM
1240
CD2
PHE B
292
53.050
35.280
53.014
1.00
45.10
B

ATOM
1241
CE1
PHE B
292
51.742
34.161
50.831
1.00
43.67
B

ATOM
1242
CE2
PHE B
292
51.992
34.403
53.217
1.00
44.65
B

ATOM
1243
CZ
PHE B
292
51.336
33.842
52.121
1.00
44.41
B

ATOM
1244
C
PHE B
292
52.990
38.217
50.441
1.00
42.01
B

ATOM
1245
O
PHE B
292
53.214
38.553
49.280
1.00
43.29
B

ATOM
1246
N
GLU B
293
51.753
38.018
50.884
1.00
41.02
B

ATOM
1247
CA
GLU B
293
50.605
38.176
49.985
1.00
40.82
B

ATOM
1248
CB
GLU B
293
49.289
38.028
50.769
1.00
41.39
B

ATOM
1249
CG
GLU B
293
49.056
36.617
51.350
1.00
42.89
B

ATOM
1250
CD
GLU B
293
49.451
36.480
52.818
1.00
43.53
B

ATOM
1251
OE1
GLU B
293
50.507
37.006
53.222
1.00
44.09
B

ATOM
1252
OE2
GLU B
293
48.704
35.825
53.572
1.00
45.55
B

ATOM
1253
C
GLU B
293
50.641
39.524
49.258
1.00
40.05
B

ATOM
1254
O
GLU B
293
50.375
39.603
48.056
1.00
38.85
B

ATOM
1255
N
ASP B
294
50.991
40.573
50.000
1.00
40.23
B

ATOM
1256
CA
ASP B
294
51.074
41.923
49.450
1.00
40.33
B

ATOM
1257
CB
ASP B
294
51.198
42.958
50.579
1.00
41.12
B

ATOM
1258
CG
ASP B
294
49.949
43.030
51.464
1.00
42.16
B

ATOM
1259
OD1
ASP B
294
48.815
42.987
50.925
1.00
43.30
B

ATOM
1260
OD2
ASP B
294
50.099
43.150
52.699
1.00
41.57
B

ATOM
1261
C
ASP B
294
52.259
42.074
48.490
1.00
38.83
B

ATOM
1262
O
ASP B
294
52.151
42.714
47.446
1.00
37.73
B

ATOM
1263
N
ILE B
295
53.390
41.477
48.840
1.00
37.53
B

ATOM
1264
CA
ILE B
295
54.561
41.573
47.994
1.00
36.43
B

ATOM
1265
CB
ILE B
295
55.751
40.853
48.638
1.00
35.75
B

ATOM
1266
CG2
ILE B
295
56.926
40.801
47.660
1.00
35.40
B

ATOM
1267
CG1
ILE B
295
56.107
41.574
49.950
1.00
36.24
B

ATOM
1268
CD1
ILE B
295
57.303
41.033
50.709
1.00
36.08
B

ATOM
1269
C
ILE B
295
54.257
40.987
46.623
1.00
36.37
B

ATOM
1270
O
ILE B
295
54.707
41.504
45.593
1.00
36.01
B

ATOM
1271
N
ILE B
296
53.470
39.919
46.616
1.00
36.36
B

ATOM
1272
CA
ILE B
296
53.094
39.262
45.375
1.00
36.96
B

ATOM
1273
CB
ILE B
296
52.329
37.967
45.665
1.00
37.13
B

ATOM
1274
CG2
ILE B
296
51.771
37.366
44.389
1.00
37.11
B

ATOM
1275
CG1
ILE B
296
53.276
36.961
46.288
1.00
36.41
B

ATOM
1276
CD1
ILE B
296
52.601
35.679
46.620
1.00
38.88
B

ATOM
1277
C
ILE B
296
52.256
40.159
44.473
1.00
36.89
B

ATOM
1278
O
ILE B
296
52.554
40.297
43.293
1.00
37.07
B

ATOM
1279
N
ASN B
297
51.208
40.769
45.008
1.00
37.95
B

ATOM
1280
CA
ASN B
297
50.385
41.649
44.186
1.00
38.86
B

ATOM
1281
CB
ASN B
297
49.240
42.246
44.980
1.00
41.69
B

ATOM
1282
CG
ASN B
297
48.368
41.213
45.583
1.00
43.05
B

ATOM
1283
OD1
ASN B
297
47.914
40.293
44.897
1.00
44.19
B

ATOM
1284
ND2
ASN B
297
48.114
41.345
46.880
1.00
43.88
B

ATOM
1285
C
ASN B
297
51.207
42.810
43.705
1.00
37.72
B

ATOM
1286
O
ASN B
297
50.953
43.360
42.632
1.00
36.87
B

ATOM
1287
N
SER B
298
52.167
43.207
44.531
1.00
36.60
B

ATOM
1288
CA
SER B
298
53.006
44.339
44.194
1.00
35.31
B

ATOM
1289
CB
SER B
298
53.926
44.673
45.366
1.00
32.10
B

ATOM
1290
OG
SER B
298
53.156
45.195
46.435
1.00
29.27
B

ATOM
1291
C
SER B
298
53.784
44.022
42.939
1.00
35.81
B

ATOM
1292
O
SER B
298
54.037
44.901
42.111
1.00
35.32
B

ATOM
1293
N
LEU B
299
54.136
42.750
42.793
1.00
36.25
B

ATOM
1294
CA
LEU B
299
54.871
42.291
41.625
1.00
36.42
B

ATOM
1295
CB
LEU B
299
55.218
40.814
41.771
1.00
35.83
B

ATOM
1296
CG
LEU B
299
56.431
40.528
42.654
1.00
36.52
B

ATOM
1297
CD1
LEU B
299
56.674
39.028
42.727
1.00
37.64
B

ATOM
1298
CD2
LEU B
299
57.655
41.224
42.065
1.00
35.78
B

ATOM
1299
C
LEU B
299
54.082
42.509
40.343
1.00
36.00
B

ATOM
1300
O
LEU B
299
54.660
42.539
39.256
1.00
36.92
B

ATOM
1301
N
CLY B
300
52.769
42.678
40.474
1.00
35.04
B

ATOM
1302
CA
GLY B
300
51.940
42.890
39.303
1.00
35.67
B

ATOM
1303
C
GLY B
300
51.417
44.305
39.186
1.00
35.69
B

ATOM
1304
O
GLY B
300
50.538
44.602
38.379
1.00
35.37
B

ATOM
1305
N
VAL B
301
51.958
45.194
39.998
1.00
36.32
B

ATOM
1306
CA
VAL B
301
51.523
46.569
39.969
1.00
36.62
B

ATOM
1307
CB
VAL B
301
51.953
47.291
41.247
1.00
37.56
B

ATOM
1308
CG1
VAL B
301
51.752
48.789
41.087
1.00
37.50
B

ATOM
1309
CG2
VAL B
301
51.133
46.752
42.436
1.00
35.20
B

ATOM
1310
C
VAL B
301
52.071
47.288
38.751
1.00
36.72
B

ATOM
1311
O
VAL B
301
51.321
47.910
38.017
1.00
37.30
B

ATOM
1312
N
SER B
302
53.378
47.201
38.534
1.00
37.60
B

ATOM
1313
CA
SER B
302
54.005
47.844
37.382
1.00
37.90
B

ATOM
1314
CB
SER B
302
54.317
49.311
37.684
1.00
37.39
B

ATOM
1315
OG
SER B
302
55.530
49.417
38.419
1.00
36.20
B

ATOM
1316
C
SER B
302
55.316
47.129
37.067
1.00
39.64
B

ATOM
1317
O
SER B
302
55.867
46.392
37.901
1.00
38.64
B

ATOM
1318
N
GLN B
303
55.821
47.371
35.861
1.00
40.39
B

ATOM
1319
CA
GLN B
303
57.087
46.781
35.428
1.00
41.46
B

ATOM
1320
CB
GLN B
303
57.436
47.239
34.013
1.00
41.20
B

ATOM
1321
CG
GLN B
303
56.696
46.481
32.950
1.00
43.64
B

ATOM
1322
CD
GLN B
303
57.199
45.068
32.815
1.00
44.54
B

ATOM
1323
OE1
GLN B
303
57.771
44.517
33.751
1.00
46.50
B

ATOM
1324
NE2
GLN B
303
56.986
44.466
31.650
1.00
44.23
B

ATOM
1325
C
GLN B
303
58.241
47.140
36.360
1.00
41.74
B

ATOM
1326
O
GLN B
303
59.163
46.345
36.561
1.00
41.80
B

ATOM
1327
N
ASN B
304
58.194
48.338
36.928
1.00
42.15
B

ATOM
1328
CA
ASN B
304
59.251
48.758
37.826
1.00
41.69
B

ATOM
1329
CB
ASN B
304
59.237
50.263
38.014
1.00
43.58
B

ATOM
1330
CG
ASN B
304
60.623
50.861
37.924
1.00
45.74
B

ATOM
1331
OD1
ASN B
304
61.599
50.302
38.459
1.00
46.54
B

ATOM
1332
ND2
ASN B
304
60.728
52.009
37.240
1.00
47.34
B

ATOM
1333
G
ASN B
304
59.130
48.100
39.174
1.00
41.16
B

ATOM
1334
O
ASN B
304
60.126
47.650
39.739
1.00
40.69
B

ATOM
1335
N
TRP B
305
57.910
48.060
39.700
1.00
40.22
B

ATOM
1336
CA
TRP B
305
57.687
47.439
40.992
1.00
39.44
B

ATOM
1337
CB
TRP B
305
56.201
47.464
41.357
1.00
40.05
B

ATOM
1338
CG
TRP B
305
55.742
48.762
41.945
1.00
41.46
B

ATOM
1339
CD2
TRP B
305
54.933
48.939
43.120
1.00
42.85
B

ATOM
1340
CE2
TRP B
305
54.724
50.324
43.277
1.00
43.18
B

ATOM
1341
CE3
TRP B
305
54.363
48.060
44.054
1.00
43.70
B

ATOM
1342
CD1
TRP B
305
55.983
50.007
41.456
1.00
41.95
B

ATOM
1343
NE1
TRP B
305
55.375
50.953
42.248
1.00
43.45
B

ATOM
1344
CZ2
TRP B
305
53.966
50.858
44.336
1.00
43.29
B

ATOM
1345
CZ3
TRP B
305
53.608
48.591
45.108
1.00
43.59
B

ATOM
1346
CH2
TRP B
305
53.419
49.976
45.237
1.00
43.13
B

ATOM
1347
C
TRP B
305
58.186
46.007
40.930
1.00
39.39
B

ATOM
1348
O
TRP B
305
58.909
45.556
41.818
1.00
40.05
B

ATOM
1349
N
ASN B
306
57.808
45.300
39.868
1.00
38.31
B

ATOM
1350
CA
ASN B
306
58.213
43.915
39.699
1.00
36.89
B

ATOM
1351
CB
ASN B
306
57.558
43.318
38.449
1.00
39.69
B

ATOM
1352
CG
ASN B
306
57.874
41.836
38.265
1.00
41.87
B

ATOM
1353
OD1
ASN B
306
58.898
41.465
37.690
1.00
42.36
B

ATOM
1354
ND2
ASN B
306
56.989
40.983
38.763
1.00
44.37
B

ATOM
1355
C
ASN B
306
59.730
43.817
39.608
1.00
35.41
B

ATOM
1356
O
ASN B
306
60.333
42.902
40.170
1.00
35.33
B

ATOM
1357
N
LYS B
307
60.353
44.765
38.917
1.00
34.02
B

ATOM
1358
CA
LYS B
307
61.804
44.750
38.786
1.00
34.18
B

ATOM
1359
CB
LYS B
307
62.245
45.720
37.686
1.00
34.16
B

ATOM
1360
CG
LYS B
307
63.753
45.889
37.572
1.00
34.46
B

ATOM
1361
CD
LYS B
307
64.121
46.934
36.524
1.00
36.66
B

ATOM
1362
CE
LYS B
307
63.783
46.479
35.089
1.00
39.17
B

ATOM
1363
NZ
LYS B
307
62.308
46.327
34.816
1.00
41.27
B

ATOM
1364
C
LYS B
307
62.491
45.096
40.110
1.00
34.15
B

ATOM
1365
O
LYS B
307
63.484
44.476
40.486
1.00
35.79
B

ATOM
1366
N
ILE B
308
61.967
46.089
40.814
1.00
33.56
B

ATOM
1367
CA
ILE B
308
62.539
46.483
42.090
1.00
32.11
B

ATOM
1368
CB
ILE B
308
61.790
47.706
42.670
1.00
31.25
B

ATOM
1369
CG2
ILE B
308
62.235
47.954
44.118
1.00
29.28
B

ATOM
1370
CG1
ILE B
308
62.010
48.918
41.746
1.00
30.74
B

ATOM
1371
CD1
ILE B
308
61.163
50.148
42.057
1.00
30.81
B

ATOM
1372
C
ILE B
308
62.455
45.330
43.083
1.00
32.53
B

ATOM
1373
O
ILE B
308
63.432
44.996
43.741
1.00
33.24
B

ATOM
1374
N
ILE B
309
61.288
44.706
43.174
1.00
32.71
B

ATOM
1375
CA
ILE B
309
61.094
43.616
44.120
1.00
32.29
B

ATOM
1376
CB
ILE B
309
59.605
43.255
44.224
1.00
31.48
B

ATOM
1377
CG2
ILE B
309
59.436
41.944
44.993
1.00
28.42
B

ATOM
1378
CG1
ILE B
309
58.860
44.419
44.894
1.00
29.43
B

ATOM
1379
CD1
ILE B
309
57.377
44.244
45.030
1.00
29.32
B

ATOM
1380
C
ILE B
309
61.881
42.360
43.801
1.00
32.95
B

ATOM
1381
O
ILE B
309
62.297
41.616
44.705
1.00
33.10
B

ATOM
1382
N
ARG B
310
62.088
42.120
42.515
1.00
32.48
B

ATOM
1383
CA
ARG B
310
62.807
40.929
42.113
1.00
31.41
B

ATOM
1384
CB
ARG B
310
62.401
40.562
40.701
1.00
30.53
B

ATOM
1385
CG
ARG B
310
61.047
39.954
40.749
1.00
32.30
B

ATOM
1386
CD
ARG B
310
60.974
38.823
39.812
1.00
33.94
B

ATOM
1387
NE
ARG B
310
60.659
39.310
38.485
1.00
36.53
B

ATOM
1388
CZ
ARG B
310
60.989
38.682
37.369
1.00
37.75
B

ATOM
1389
NH1
ARG B
310
61.656
37.535
37.428
1.00
36.97
B

ATOM
1390
NH2
ARG B
310
60.649
39.205
36.200
1.00
38.45
B

ATOM
1391
C
ARG B
310
64.302
41.065
42.259
1.00
30.16
B

ATOM
1392
O
ARG B
310
65.059
40.091
42.152
1.00
28.61
B

ATOM
1393
N
LYS B
311
64.717
42.283
42.552
1.00
29.95
B

ATOM
1394
CA
LYS B
311
66.122
42.542
42.727
1.00
31.78
B

ATOM
1395
CB
LYS B
311
66.419
44.014
42.471
1.00
30.98
B

ATOM
1396
CG
LYS B
311
67.876
44.355
42.676
1.00
34.65
B

ATOM
1397
CD
LYS B
311
68.141
45.839
42.539
0.00
34.39
B

ATOM
1398
CE
LYS B
311
68.033
46.305
41.095
0.00
35.04
B

ATOM
1399
NZ
LYS B
311
66.665
46.176
40.520
0.00
35.23
B

ATOM
1400
C
LYS B
311
66.589
42.154
44.127
1.00
31.89
B

ATOM
1401
O
LYS B
311
67.761
41.815
44.325
1.00
31.11
B

ATOM
1402
N
SER B
312
65.666
42.181
45.088
1.00
32.44
B

ATOM
1403
CA
SER B
312
65.997
41.868
46.479
1.00
34.40
B

ATOM
1404
CB
SER B
312
64.998
42.541
47.433
1.00
35.97
B

ATOM
1405
OG
SER B
312
65.318
42.268
48.793
1.00
37.24
B

ATOM
1406
C
SER B
312
66.068
40.389
46.825
1.00
33.58
B

ATOM
1407
O
SER B
312
65.154
39.629
46.532
1.00
35.14
B

ATOM
1408
N
THR B
313
67.160
39.990
47.460
1.00
32.17
B

ATOM
1409
CA
THR B
313
67.314
38.613
47.867
1.00
32.11
B

ATOM
1410
CB
THR B
313
68.760
38.142
47.682
1.00
34.02
B

ATOM
1411
OG1
THR B
313
68.921
37.648
46.346
1.00
35.15
B

ATOM
1412
CG2
THR B
313
69.114
37.055
48.685
1.00
33.55
B

ATOM
1413
C
THR B
313
66.913
38.532
49.329
1.00
30.50
B

ATOM
1414
O
THR B
313
66.318
37.553
49.764
1.00
31.15
B

ATOM
1415
N
SER B
314
67.219
39.583
50.078
1.00
29.28
B

ATOM
1416
CA
SER B
314
66.881
39.648
51.493
1.00
28.64
B

ATOM
1417
CB
SER B
314
67.307
40.990
52.076
1.00
28.48
B

ATOM
1418
OG
SER B
314
68.696
40.979
52.349
1.00
33.47
B

ATOM
1419
C
SER B
314
65.397
39.479
51.710
1.00
27.68
B

ATOM
1420
O
SER B
314
64.966
38.738
52.592
1.00
28.00
B

ATOM
1421
N
LEU B
315
64.629
40.182
50.890
1.00
25.95
B

ATOM
1422
CA
LEU B
315
63.190
40.158
50.967
1.00
24.83
B

ATOM
1423
CB
LEU B
315
62.614
40.721
49.676
1.00
22.38
B

ATOM
1424
CG
LEU B
315
61.151
41.129
49.740
1.00
21.41
B

ATOM
1425
CD1
LEU B
315
61.006
42.400
50.604
1.00
20.01
B

ATOM
1426
CD2
LEU B
315
60.662
41.376
48.345
1.00
19.89
B

ATOM
1427
C
LEU B
315
62.675
38.745
51.206
1.00
26.71
B

ATOM
1428
O
LEU B
315
61.894
38.494
52.141
1.00
27.54
B

ATOM
1429
N
TRP B
316
63.110
37.813
50.369
1.00
26.88
B

ATOM
1430
CA
TRP B
316
62.665
36.439
50.534
1.00
27.42
B

ATOM
1431
CB
TRP B
316
62.776
35.691
49.204
1.00
27.04
B

ATOM
1432
CG
TRP B
316
62.021
36.416
48.176
1.00
25.52
B

ATOM
1433
CD2
TRP B
316
60.600
36.519
48.088
1.00
25.34
B

ATOM
1434
CE2
TRP B
316
60.313
37.456
47.071
1.00
24.36
B

ATOM
1435
CE3
TRP B
316
59.540
35.920
48.778
1.00
26.16
B

ATOM
1436
CD1
TRP B
316
62.526
37.262
47.232
1.00
25.54
B

ATOM
1437
NE1
TRP B
316
61.507
37.892
46.566
1.00
23.85
B

ATOM
1438
CZ2
TRP B
316
59.003
37.808
46.728
1.00
23.50
B

ATOM
1439
CZ3
TRP B
316
58.236
36.272
48.438
1.00
24.82
B

ATOM
1440
CH2
TRP B
316
57.981
37.209
47.421
1.00
24.99
B

ATOM
1441
C
TRP B
316
63.402
35.720
51.656
1.00
27.65
B

ATOM
1442
O
TRP B
316
62.786
34.989
52.446
1.00
27.76
B

ATOM
1443
N
LYS B
317
64.709
35.934
51.744
1.00
27.10
B

ATOM
1444
CA
LYS B
317
65.455
35.304
52.817
1.00
28.92
B

ATOM
1445
CB
LYS B
317
66.907
35.788
52.830
1.00
30.51
B

ATOM
1446
CG
LYS B
317
67.768
35.175
53.935
1.00
32.68
B

ATOM
1447
CD
LYS B
317
69.209
35.655
53.820
1.00
35.89
B

ATOM
1448
CE
LYS B
317
69.849
35.839
55.186
1.00
37.32
B

ATOM
1449
NZ
LYS B
317
69.169
36.927
55.978
1.00
39.48
B

ATOM
1450
C
LYS B
317
64.764
35.597
54.164
1.00
29.21
B

ATOM
1451
O
LYS B
317
64.560
34.682
54.975
1.00
28.72
B

ATOM
1452
N
LYS B
318
64.373
36.851
54.394
1.00
27.41
B

ATOM
1453
CA
LYS B
318
63.698
37.182
55.640
1.00
27.23
B

ATOM
1454
CB
LYS B
318
63.287
38.657
55.685
1.00
28.22
B

ATOM
1455
CG
LYS B
318
64.448
39.580
55.982
1.00
29.33
B

ATOM
1456
CD
LYS B
318
64.011
40.989
56.263
1.00
29.29
B

ATOM
1457
CE
LYS B
318
65.211
41.805
56.726
1.00
31.20
B

ATOM
1458
NZ
LYS B
318
66.332
41.748
55.749
1.00
29.62
B

ATOM
1459
C
LYS B
318
62.475
36.318
55.846
1.00
28.19
B

ATOM
1460
O
LYS B
318
62.325
35.651
56.881
1.00
29.19
B

ATOM
1461
N
LEU B
319
61.598
36.346
54.847
1.00
28.31
B

ATOM
1462
CA
LEU B
319
60.353
35.576
54.851
1.00
26.08
B

ATOM
1463
CB
LEU B
319
59.644
35.756
53.499
1.00
24.60
B

ATOM
1464
CG
LEU B
319
58.949
37.106
53.299
1.00
23.31
B

ATOM
1465
CD1
LEU B
319
58.929
37.501
51.828
1.00
25.42
B

ATOM
1466
CD2
LEU B
319
57.550
37.030
53.849
1.00
20.66
B

ATOM
1467
C
LEU B
319
60.661
34.104
55.115
1.00
24.68
B

ATOM
1468
O
LEU B
319
60.126
33.511
56.051
1.00
24.33
B

ATOM
1469
N
LEU B
320
61.521
33.515
54.292
1.00
24.37
B

ATOM
1470
CA
LEU B
320
61.887
32.119
54.496
1.00
24.33
B

ATOM
1471
CB
LEU B
320
63.119
31.777
53.678
1.00
20.97
B

ATOM
1472
CG
LEU B
320
62.711
31.425
52.272
1.00
20.93
B

ATOM
1473
CD1
LEU B
320
63.945
31.333
51.431
1.00
21.63
B

ATOM
1474
CD2
LEU B
320
61.936
30.117
52.276
1.00
17.66
B

ATOM
1475
C
LEU B
320
62.166
31.800
55.967
1.00
24.55
B

ATOM
1476
O
LEU B
320
61.744
30.769
56.491
1.00
25.31
B

ATOM
1477
N
ILE B
321
62.883
32.706
56.615
1.00
24.47
B

ATOM
1478
CA
ILE B
321
63.253
32.579
58.009
1.00
23.96
B

ATOM
1479
CB
ILE B
321
64.450
33.531
58.315
1.00
25.52
B

ATOM
1480
CG2
ILE B
321
64.759
33.556
59.806
1.00
25.19
B

ATOM
1481
CG1
ILE B
321
65.671
33.094
57.498
1.00
23.92
B

ATOM
1482
CD1
ILE B
321
66.951
33.873
57.782
1.00
24.41
B

ATOM
1483
C
ILE B
321
62.065
32.882
58.928
1.00
23.22
B

ATOM
1484
O
ILE B
321
61.902
32.240
59.952
1.00
24.18
B

ATOM
1485
N
SER B
322
61.239
33.853
58.563
1.00
23.04
B

ATOM
1486
CA
SER B
322
60.079
34.200
59.370
1.00
23.65
B

ATOM
1487
CB
SER B
322
59.248
35.266
58.670
1.00
21.62
B

ATOM
1488
OG
SER B
322
60.030
36.403
58.387
1.00
24.32
B

ATOM
1489
C
SER B
322
59.203
32.990
59.581
1.00
24.95
B

ATOM
1490
O
SER B
322
58.789
32.691
60.696
1.00
28.00
B

ATOM
1491
N
GLD B
323
58.926
32.302
58.485
1.00
25.30
B

ATOM
1492
CA
GLD B
323
58.066
31.135
58.486
1.00
25.97
B

ATOM
1493
CB
GLD B
323
57.480
30.974
57.091
1.00
26.35
B

ATOM
1494
CG
GLD B
323
56.792
32.239
56.646
1.00
27.43
B

ATOM
1495
CD
GLD B
323
55.441
32.431
57.307
1.00
27.80 B

ATOM
1496
OE1
GLD B
323
55.239
31.878
58.409
1.00
25.90
B

ATOM
1497
OE2
GLD B
323
54.590
33.142
56.718
1.00
28.13
B

ATOM
1498
C
GLD B
323
58.745
29.855
58.917
1.00
25.13
B

ATOM
1499
O
GLD B
323
58.123
28.792
58.931
1.00
25.20
B

ATOM
1500
N
ASN B
324
60.019
29.966
59.276
1.00
24.08
B

ATOM
1501
CA
ASN B
324
60.808
28.816
59.708
1.00
24.96
B

ATOM
1502
CB
ASN B
324
60.203
28.185
60.974
1.00
26.02
B

ATOM
1503
CG
ASN B
324
60.051
29.187
62.108
1.00
28.82
B

ATOM
1504
OD1
ASN B
324
61.030
29.766
62.605
1.00
29.61
B

ATOM
1505
ND2
ASN B
324
58.813
29.402
62.518
1.00
29.76
B

ATOM
1506
C
ASN B
324
60.906
27.776
58.588
1.00
24.92
B

ATOM
1507
O
ASN B
324
60.642
26.596
58.786
1.00
23.18
B

ATOM
1508
N
PHE B
325
61.269
28.226
57.395
1.00
25.71
B

ATOM
1509
CA
PHE B
325
61.406
27.304
56.287
1.00
25.91
B

ATOM
1510
CB
PHE B
325
60.839
27.913
55.008
1.00
24.25
B

ATOM
1511
CG
PHE B
325
59.334
27.935
54.987
1.00
23.73
B

ATOM
1512
CD1
PHE B
325
58.644
28.984
54.394
1.00
23.04
B

ATOM
1513
CD2
PHE B
325
58.604
26.925
55.616
1.00
20.21
B

ATOM
1514
CE1
PHE B
325
57.259
29.025
54.437
1.00
20.96
B

ATOM
1515
CE2
PHE B
325
57.227
26.964
55.658
1.00
18.74
B

ATOM
1516
CZ
PHE B
325
56.555
28.015
55.073
1.00
19.51
B

ATOM
1517
C
PHE B
325
62.861
26.972
56.156
1.00
26.92
B

ATOM
1518
O
PHE B
325
63.232
26.019
55.478
1.00
28.62
B

ATOM
1519
N
VAL B
326
63.683
27.766
56.833
1.00
27.50
B

ATOM
1520
CA
VAL B
326
65.127
27.577
56.849
1.00
27.18
B

ATOM
1521
CB
VAL B
326
65.773
28.060
55.532
1.00
25.75
B

ATOM
1522
CG1
VAL B
326
66.019
29.553
55.587
1.00
23.02
B

ATOM
1523
CG2
VAL B
326
67.061
27.316
55.288
1.00
26.04
B

ATOM
1524
C
VAL B
326
65.685
28.408
57.993
1.00
28.22
B

ATOM
1525
O
VAL B
326
64.998
29.274
58.533
1.00
28.23
B

ATOM
1526
N
SER B
327
66.932
28.154
58.361
1.00
29.87
B

ATOM
1527
CA
SER B
327
67.547
28.926
59.427
1.00
32.04
B

ATOM
1528
CB
SER B
327
67.867
28.053
60.643
1.00
32.92
B

ATOM
1529
OG
SER B
327
69.012
27.244
60.404
1.00
35.60
B

ATOM
1530
C
SER B
327
68.837
29.511
58.905
1.00
33.44
B

ATOM
1531
O
SER B
327
69.404
29.024
57.925
1.00
35.13
B

ATOM
1532
N
PRO B
328
69.328
30.561
59.568
1.00
34.95
B

ATOM
1533
CD
PRO B
328
68.703
31.277
60.698
1.00
34.72
B

ATOM
1534
CA
PRO B
328
70.570
31.208
59.161
1.00
35.43
B

ATOM
1535
CB
PRO B
328
70.906
32.056
60.372
1.00
34.44
B

ATOM
1536
CG
PRO B
328
69.541
32.530
60.792
1.00
34.00
B

ATOM
1537
C
PRO B
328
71.674
30.211
58.789
1.00
37.33
B

ATOM
1538
O
PRO B
328
72.413
30.428
57.820
1.00
38.07
B

ATOM
1539
N
LYS B
329
71.779
29.106
59.524
1.00
38.13
B

ATOM
1540
CA
LYS B
329
72.830
28.126
59.222
1.00
39.44
B

ATOM
1541
CB
LYS B
329
73.088
27.201
60.423
1.00
41.96
B

ATOM
1542
CG
LYS B
329
73.334
27.911
61.736
1.00
44.54
B

ATOM
1543
CD
LYS B
329
74.564
28.801
61.693
1.00
46.08
B

ATOM
1544
CE
LYS B
329
74.745
29.475
63.047
1.00
47.88
B

ATOM
1545
NZ
LYS B
329
73.510
30.241
63.384
1.00
48.71
B

ATOM
1546
C
LYS B
329
72.539
27.255
58.005
1.00
38.23
B

ATOM
1547
O
LYS B
329
73.444
26.922
57.230
1.00
37.43
B

ATOM
1548
N
GLY B
330
71.279
26.863
57.858
1.00
36.83
B

ATOM
1549
CA
GLY B
330
70.904
26.026
56.733
1.00
34.91
B

ATOM
1550
C
GLY B
330
70.671
26.809
55.458
1.00
33.34
B

ATOM
1551
O
GLY B
330
70.432
26.217
54.402
1.00
31.96
B

ATOM
1552
N
PHE B
331
70.742
28.136
55.554
1.00
32.27
B

ATOM
1553
CA
PHE B
331
70.517
28.977
54.388
1.00
32.81
B

ATOM
1554
CB
PHE B
331
70.778
30.454
54.688
1.00
32.71
B

ATOM
1555
CG
PHE B
331
70.365
31.374
53.561
1.00
35.02
B

ATOM
1556
CD1
PHE B
331
69.013
31.631
53.319
1.00
34.88
B

ATOM
1557
CD2
PHE B
331
71.323
31.971
52.727
1.00
36.79
B

ATOM
1558
CE1
PHE B
331
68.609
32.466
52.274
1.00
35.03
B

ATOM
1559
CE2
PHE B
331
70.933
32.816
51.670
1.00
36.82
B

ATOM
1560
CZ
PHE B
331
69.568
33.061
51.446
1.00
36.85
B

ATOM
1561
C
PHE B
331
71.333
28.600
53.164
1.00
32.72
B

ATOM
1562
O
PHE B
331
70.779
28.197
52.143
1.00
32.53
B

ATOM
1563
N
ASN B
332
72.650
28.725
53.261
1.00
33.63
B

ATOM
1564
CA
ASN B
332
73.495
28.430
52.116
1.00
34.96
B

ATOM
1565
CB
ASN B
332
74.956
28.510
52.503
1.00
35.07
B

ATOM
1566
CG
ASN B
332
75.386
29.925
52.769
1.00
36.45
B

ATOM
1567
OD1
ASN B
332
74.860
30.864
52.165
1.00
36.09
B

ATOM
1568
ND2
ASN B
332
76.352
30.096
53.666
1.00
37.34
B

ATOM
1569
C
ASN B
332
73.204
27.105
51.457
1.00
35.37
B

ATOM
1570
O
ASN B
332
73.006
27.034
50.240
1.00
34.82
B

ATOM
1571
N
SER B
333
73.174
26.050
52.253
1.00
36.35
B

ATOM
1572
CA
SER B
333
72.897
24.749
51.696
1.00
38.23
B

ATOM
1573
CB
SER B
333
72.767
23.724
52.804
1.00
37.83
B

ATOM
1574
OG
SER B
333
72.509
22.458
52.236
1.00
43.08
B

ATOM
1575
C
SER B
333
71.615
24.785
50.867
1.00
38.81
B

ATOM
1576
O
SER B
333
71.522
24.144
49.814
1.00
39.26
B

ATOM
1577
N
LEU B
334
70.629
25.533
51.357
1.00
38.86
B

ATOM
1578
CA
LEU B
334
69.338
25.688
50.685
1.00
37.16
B

ATOM
1579
CB
LEU B
334
68.446
26.645
51.486
1.00
34.21
B

ATOM
1580
CG
LEU B
334
67.149
27.126
50.830
1.00
33.30
B

ATOM
1581
CD1
LEU B
334
66.189
25.957
50.642
1.00
29.33
B

ATOM
1582
CD2
LEU B
334
66.528
28.209
51.688
1.00
31.65
B

ATOM
1583
C
LEU B
334
69.574
26.251
49.291
1.00
37.44
B

ATOM
1584
O
LEU B
334
69.105
25.700
48.293
1.00
36.40
B

ATOM
1585
N
ASN B
335
70.306
27.361
49.248
1.00
38.10
B

ATOM
1586
CA
ASN B
335
70.647
28.032
48.001
1.00
38.02
B

ATOM
1587
CB
ASN B
335
71.590
29.188
48.289
1.00
37.88
B

ATOM
1588
CG
ASN B
335
70.871
30.496
48.329
1.00
40.34
B

ATOM
1589
OD1
ASN B
335
71.266
31.422
49.033
1.00
43.76
B

ATOM
1590
ND2
ASN B
335
69.800
30.591
47.556
1.00
41.28
B

ATOM
1591
C
ASN B
335
71.292
27.070
47.013
1.00
38.24
B

ATOM
1592
O
ASN B
335
70.906
27.003
45.847
1.00
38.64
B

ATOM
1593
N
LEU B
336
72.274
26.325
47.498
1.00
36.78
B

ATOM
1594
CA
LEU B
336
72.978
25.364
46.683
1.00
35.71
B

ATOM
1595
CB
LEU B
336
74.041
24.658
47.522
1.00
35.78
B

ATOM
1596
CG
LEU B
336
74.991
23.682
46.827
1.00
35.54
B

ATOM
1597
CD1
LEU B
336
75.977
24.436
45.942
1.00
35.55
B

ATOM
1598
CD2
LEU B
336
75.716
22.899
47.883
1.00
36.31
B

ATOM
1599
C
LEU B
336
71.997
24.336
46.123
1.00
35.77
B

ATOM
1600
O
LEU B
336
72.075
23.961
44.954
1.00
37.71
B

ATOM
1601
N
LYS B
337
71.068
23.876
46.953
1.00
34.49
B

ATOM
1602
CA
LYS B
337
70.097
22.878
46.508
1.00
31.85
B

ATOM
1603
CB
LYS B
337
69.310
22.320
47.704
1.00
30.25
B

ATOM
1604
CG
LYS B
337
68.298
21.237
47.321
1.00
32.14
B

ATOM
1605
CD
LYS B
337
67.438
20.697
48.512
1.00
35.02
B

ATOM
1606
CE
LYS B
337
66.544
21.789
49.173
1.00
35.41
B

ATOM
1607
NZ
LYS B
337
65.466
21.260
50.081
1.00
32.74
B

ATOM
1608
C
LYS B
337
69.129
23.433
45.461
1.00
30.95
B

ATOM
1609
O
LYS B
337
68.793
22.740
44.519
1.00
29.84
B

ATOM
1610
N
LEU B
338
68.690
24.679
45.636
1.00
31.30
B

ATOM
1611
CA
LEU B
338
67.755
25.324
44.714
1.00
30.02
B

ATOM
1612
CB
LEU B
338
67.218
26.621
45.317
1.00
29.04
B

ATOM
1613
CG
LEU B
338
66.157
26.563
46.434
1.00
29.18
B

ATOM
1614
CD1
LEU B
338
65.834
27.996
46.909
1.00
25.48
B

ATOM
1615
CD2
LEU B
338
64.897
25.881
45.919
1.00
26.03
B

ATOM
1616
C
LEU B
338
68.433
25.639
43.400
1.00
30.20
B

ATOM
1617
O
LEU B
338
67.809
25.643
42.340
1.00
29.78
B

ATOM
1618
N
SER B
339
69.724
25.918
43.487
1.00
30.16
B

ATOM
1619
CA
SER B
339
70.510
26.227
42.317
1.00
29.06
B

ATOM
1620
CB
SER B
339
71.913
26.656
42.712
1.00
27.05
B

ATOM
1621
OG
SER B
339
72.665
26.965
41.560
1.00
25.97
B

ATOM
1622
C
SER B
339
70.598
24.979
41.483
1.00
30.90
B

ATOM
1623
O
SER B
339
70.580
25.029
40.254
1.00
32.89
B

ATOM
1624
N
GLN B
340
70.701
23.842
42.149
1.00
30.57
B

ATOM
1625
CA
GLN B
340
70.796
22.605
41.409
1.00
31.13
B

ATOM
1626
CB
GLN B
340
71.238
21.496
42.334
1.00
32.53
B

ATOM
1627
CG
GLN B
340
72.619
21.768
42.867
1.00
35.89
B

ATOM
1628
CD
GLN B
340
73.040
20.758
43.900
1.00
36.30
B

ATOM
1629
OE1
GLN B
340
72.209
19.975
44.393
1.00
37.07
B

ATOM
1630
NE2
GLN B
340
74.332
20.765
44.248
1.00
34.68
B

ATOM
1631
C
GLN B
340
69.471
22.276
40.774
1.00
31.71
B

ATOM
1632
O
GLN B
340
69.418
21.644
39.726
1.00
32.80
B

ATOM
1633
N
LYS B
341
68.403
22.738
41.408
1.00
32.39
B

ATOM
1634
CA
LYS B
341
67.047
22.505
40.942
1.00
33.18
B

ATOM
1635
CB
LYS B
341
66.086
22.760
42.094
1.00
34.86
B

ATOM
1636
CG
LYS B
341
64.697
22.223
41.889
1.00
38.21
B

ATOM
1637
CD
LYS B
341
63.793
22.574
43.061
1.00
40.03
B

ATOM
1638
CE
LYS B
341
62.406
21.980
42.836
1.00
42.58
B

ATOM
1639
NZ
LYS B
341
61.380
22.609
43.719
1.00
42.83
B

ATOM
1640
C
LYS B
341
66.661
23.392
39.764
1.00
34.36
B

ATOM
1641
O
LYS B
341
66.041
22.939
38.805
1.00
34.14
B

ATOM
1642
N
TYR B
342
67.043
24.658
39.857
1.00
34.90
B

ATOM
1643
CA
TYR B
342
66.734
25.660
38.853
1.00
35.01
B

ATOM
1644
CB
TYR B
342
65.844
26.695
39.497
1.00
37.87
B

ATOM
1645
CG
TYR B
342
64.647
26.082
40.153
1.00
41.65
B

ATOM
1646
CD1
TYR B
342
63.646
25.507
39.384
1.00
42.60
B

ATOM
1647
CE1
TYR B
342
62.525
24.958
39.968
1.00
45.40
B

ATOM
1648
CD2
TYR B
342
64.501
26.088
41.538
1.00
42.64
B

ATOM
1649
CE2
TYR B
342
63.376
25.540
42.139
1.00
44.31
B

ATOM
1650
CZ
TYR B
342
62.386
24.978
41.343
1.00
45.73
B

ATOM
1651
OH
TYR B
342
61.232
24.462
41.896
1.00
46.50
B

ATOM
1652
C
TYR B
342
67.991
26.339
38.343
1.00
34.71
B

ATOM
1653
O
TYR B
342
68.287
27.467
38.729
1.00
35.57
B

ATOM
1654
N
PRO B
343
68.754
25.663
37.474
1.00
34.09
B

ATOM
1655
CD
PRO B
343
68.568
24.298
36.955
1.00
33.06
B

ATOM
1656
CA
PRO B
343
69.982
26.256
36.942
1.00
34.15
B

ATOM
1657
CB
PRO B
343
70.427
25.231
35.902
1.00
32.61
B

ATOM
1658
CG
PRO B
343
69.940
23.953
36.458
1.00
30.81
B

ATOM
1659
C
PRO B
343
69.805
27.655
36.332
1.00
34.54
B

ATOM
1660
O
PRO B
343
70.562
28.577
36.639
1.00
34.01
B

ATOM
1661
N
LYS B
344
68.793
27.803
35.483
1.00
34.28
B

ATOM
1662
CA
LYS B
344
68.537
29.063
34.799
1.00
34.41
B

ATOM
1663
CB
LYS B
344
67.823
28.791
33.483
1.00
34.70
B

ATOM
1664
CG
LYS B
344
68.487
27.758
32.623
1.00
32.84
B

ATOM
1665
CD
LYS B
344
67.566
27.409
31.505
1.00
32.13
B

ATOM
1666
CE
LYS B
344
67.769
25.984
31.078
1.00
32.95
B

ATOM
1667
NZ
LYS B
344
66.694
25.581
30.144
1.00
35.30
B

ATOM
1668
C
LYS B
344
67.778
30.156
35.547
1.00
34.52
B

ATOM
1669
CD
LYS B
344
67.446
31.188
34.950
1.00
33.51
B

ATOM
1670
N
LEU B
345
67.475
29.921
36.825
1.00
32.93
B

ATOM
1671
CA
LEU B
345
66.792
30.916
37.663
1.00
30.85
B

ATOM
1672
CB
LEU B
345
65.856
30.253
38.660
1.00
28.33
B

ATOM
1673
CG
LEU B
345
64.506
29.850
38.111
1.00
27.26
B

ATOM
1674
CD1
LEU B
345
63.691
29.121
39.179
1.00
24.62
B

ATOM
1675
CD2
LEU B
345
63.804
31.102
37.655
1.00
26.44
B

ATOM
1676
C
LEU B
345
67.834
31.674
38.440
1.00
31.07
B

ATOM
1677
O
LEU B
345
68.961
31.210
38.580
1.00
31.79
B

ATOM
1678
N
SER B
346
67.458
32.830
38.970
1.00
33.11
B

ATOM
1679
CA
SER B
346
68.392
33.653
39.754
1.00
34.10
B

ATOM
1680
CB
SER B
346
68.283
35.114
39.349
1.00
34.20
B

ATOM
1681
OG
SER B
346
67.035
35.623
39.779
1.00
37.09
B

ATOM
1682
C
SER B
346
68.098
33.563
41.247
1.00
33.12
B

ATOM
1683
O
SER B
346
66.971
33.302
41.655
1.00
33.78
B

ATOM
1684
N
GLN B
347
69.113
33.814
42.056
1.00
32.28
B

ATOM
1685
CA
GLN B
347
68.950
33.749
43.495
1.00
32.88
B

ATOM
1686
CB
GLN B
347
70.071
34.502
44.177
1.00
33.73
B

ATOM
1687
CG
GLN B
347
70.009
34.451
45.667
1.00
33.40
B

ATOM
1688
CD
GLN B
347
71.105
35.276
46.251
1.00
36.19
B

ATOM
1689
OE1
GLN B
347
71.164
36.494
46.031
1.00
38.25
B

ATOM
1690
NE2
GLN B
347
72.006
34.627
46.984
1.00
36.38
B

ATOM
1691
C
GLN B
347
67.620
34.314
43.973
1.00
31.82
B

ATOM
1692
O
GLN B
347
66.834
33.616
44.620
1.00
31.26
B

ATOM
1693
N
GLN B
348
67.370
35.581
43.661
1.00
30.61
B

ATOM
1694
CA
GLN B
348
66.121
36.195
44.076
1.00
30.85
B

ATOM
1695
CB
GLN B
348
65.984
37.626
43.542
1.00
31.61
B

ATOM
1696
CG
GLN B
348
67.092
38.583
43.958
1.00
31.41
B

ATOM
1697
CD
GLN B
348
68.291
38.552
43.014
1.00
30.33
B

ATOM
1698
OE1
GLN B
348
69.055
39.512
42.942
1.00
29.04
B

ATOM
1699
NE2
GLN B
348
68.461
37.452
42.296
1.00
29.86
B

ATOM
1700
C
GLN B
348
64.942
35.364
43.593
1.00
29.45
B

ATOM
1701
O
GLN B
348
64.183
34.831
44.400
1.00
28.92
B

ATOM
1702
N
ASP B
349
64.776
35.236
42.283
1.00
28.60
B

ATOM
1703
CA
ASP B
349
63.646
34.458
41.805
1.00
27.39
B

ATOM
1704
CB
ASP B
349
63.631
34.372
40.282
1.00
28.50
B

ATOM
1705
CG
ASP B
349
63.164
35.666
39.632
1.00
30.39
B

ATOM
1706
OD1
ASP B
349
62.212
36.306
40.153
1.00
29.22
B

ATOM
1707
OD2
ASP B
349
63.744
36.034
38.590
1.00
31.83
B

ATOM
1708
C
ASP B
349
63.571
33.061
42.404
1.00
25.37
B

ATOM
1709
O
ASP B
349
62.476
32.546
42.597
1.00
24.91
B

ATOM
1710
N
ARG B
350
64.720
32.454
42.695
1.00
22.81
B

ATOM
1711
CA
ARG B
350
64.746
31.117
43.280
1.00
21.59
B

ATOM
1712
CB
ARG B
350
66.178
30.611
43.428
1.00
23.28
B

ATOM
1713
CG
ARG B
350
66.787
30.106
42.133
1.00
27.24
B

ATOM
1714
CD
ARG B
350
68.195
29.544
42.333
1.00
26.74
B

ATOM
1715
NE
ARG B
350
68.820
29.271
41.051
1.00
27.71
B

ATOM
1716
CZ
ARG B
350
70.128
29.218
40.860
1.00
29.79
B

ATOM
1717
NH1
ARG B
350
70.956
29.416
41.878
1.00
31.36
B

ATOM
1718
NH2
ARG B
350
70.604
28.990
39.642
1.00
31.57
B

ATOM
1719
C
ARG B
350
64.094
31.124
44.651
1.00
20.94
B

ATOM
1720
O
ARG B
350
63.103
30.429
44.893
1.00
20.47
B

ATOM
1721
N
LEU B
351
64.672
31.909
45.549
1.00
18.79
B

ATOM
1722
CA
LEU B
351
64.157
32.026
46.890
1.00
17.44
B

ATOM
1723
CB
LEU B
351
64.895
33.143
47.624
1.00
14.47
B

ATOM
1724
CG
LEU B
351
66.358
32.799
47.897
1.00
14.78
B

ATOM
1725
CD1
LEU B
351
66.992
33.900
48.730
1.00
17.09
B

ATOM
1726
CD2
LEU B
351
66.466
31.467
48.619
1.00
12.98
B

ATOM
1727
C
LEU B
351
62.638
32.247
46.942
1.00
18.50
B

ATOM
1728
O
LEU B
351
61.958
31.715
47.826
1.00
17.10
B

ATOM
1729
N
ARG B
352
62.092
33.003
45.995
1.00
18.20
B

ATOM
1730
CA
ARG B
352
60.652
33.246
45.997
1.00
20.70
B

ATOM
1731
CB
ARG B
352
60.301
34.404
45.060
1.00
22.90
B

ATOM
1732
CG
ARG B
352
58.821
34.519
44.704
1.00
21.25
B

ATOM
1733
CD
ARG B
352
58.577
35.861
44.037
1.00
24.96
B

ATOM
1734
NE
ARG B
352
59.336
36.027
42.793
1.00
26.60
B

ATOM
1735
CZ
ARG B
352
58.840
35.772
41.588
1.00
24.08
B

ATOM
1736
NH1
ARG B
352
57.589
35.344
41.468
1.00
25.95
B

ATOM
1737
NH2
ARG B
352
59.582
35.955
40.508
1.00
23.94
B

ATOM
1738
C
ARG B
352
59.868
32.014
45.590
1.00
20.80
B

ATOM
1739
O
ARG B
352
58.812
31.701
46.151
1.00
20.69
B

ATOM
1740
N
LEU B
353
60.385
31.308
44.601
1.00
22.07
B

ATOM
1741
CA
LEU B
353
59.703
30.115
44.135
1.00
24.32
B

ATOM
1742
CB
LEU B
353
60.494
29.510
42.971
1.00
24.67
B

ATOM
1743
CG
LEU B
353
59.774
28.524
42.058
1.00
26.68
B

ATOM
1744
CO1
LEU B
353
59.623
27.208
42.767
1.00
28.84
B

ATOM
1745
CD2
LEU B
353
58.420
29.098
41.635
1.00
28.75
B

ATOM
1746
C
LEU B
353
59.614
29.166
45.336
1.00
25.14
B

ATOM
1747
O
LEU B
353
58.568
28.566
45.604
1.00
24.06
B

ATOM
1748
N
SER B
354
60.728
29.085
46.063
1.00
25.53
B

ATOM
1749
CA
SER B
354
60.867
28.264
47.262
1.00
26.14
B

ATOM
1750
CB
SER B
354
62.273
28.450
47.849
1.00
25.96
B

ATOM
1751
OG
SER B
354
62.454
27.730
49.061
1.00
23.97
B

ATOM
1752
C
SER B
354
59.830
28.656
48.313
1.00
27.19
B

ATOM
1753
O
SER B
354
59.098
27.818
48.837
1.00
27.24
B

ATOM
1754
N
PHE B
355
59.769
29.941
48.625
1.00
27.04
B

ATOM
1755
CA
PHE B
355
58.822
30.390
49.616
1.00
26.23
B

ATOM
1756
CB
PHE B
355
58.954
31.882
49.854
1.00
27.13
B

ATOM
1757
CG
PHE B
355
58.041
32.400
50.920
1.00
26.97
B

ATOM
1758
CD1
PHE B
355
56.736
32.763
50.626
1.00
26.60
B

ATOM
1759
CD2
PHE B
355
58.495
32.522
52.228
1.00
28.32
B

ATOM
1760
CE1
PHE B
355
55.892
33.236
51.626
1.00
27.60
B

ATOM
1761
CE2
PHE B
355
57.661
32.992
53.237
1.00
26.91
B

ATOM
1762
CZ
PHE B
355
56.360
33.353
52.934
1.00
27.81
B

ATOM
1763
C
PHE B
355
57.413
30.087
49.203
1.00
25.95
B

ATOM
1764
O
PHE B
355
56.687
29.427
49.929
1.00
25.86
B

ATOM
1765
N
LEU B
356
57.015
30.575
48.037
1.00
27.00
B

ATOM
1766
CA
LEU B
356
55.655
30.337
47.570
1.00
27.63
B

ATOM
1767
CB
LEU B
356
55.487
30.886
46.144
1.00
28.43
B

ATOM
1768
CG
LEU B
356
55.485
32.412
45.923
1.00
28.92
B

ATOM
1769
CD1
LEU B
356
55.449
32.704
44.421
1.00
28.25
B

ATOM
1770
CD2
LEU B
356
54.299
33.063
46.620
1.00
26.99
B

ATOM
1771
C
LEU B
356
55.297
28.842
47.618
1.00
26.51
B

ATOM
1772
O
LEU B
356
54.170
28.492
47.910
1.00
25.42
B

ATOM
1773
N
GLU B
357
56.267
27.976
47.343
1.00
27.82
B

ATOM
1774
CA
GLU B
357
56.051
26.537
47.357
1.00
28.89
B

ATOM
1775
CB
GLU B
357
57.223
25.841
46.668
1.00
30.18
B

ATOM
1776
CG
GLU B
357
57.193
24.319
46.727
1.00
34.82
B

ATOM
1777
CD
GLU B
357
58.032
23.659
45.640
1.00
38.48
B

ATOM
1778
OE1
GLU B
357
59.254
23.926
45.569
1.00
41.06
B

ATOM
1779
OE2
GLU B
357
57.460
22.870
44.849
1.00
40.28
B

ATOM
1780
C
GLU B
357
55.899
26.016
48.790
1.00
29.56
B

ATOM
1781
O
GLU B
357
55.055
25.165
49.072
1.00
30.56
B

ATOM
1782
N
ASN B
358
56.722
26.529
49.692
1.00
27.38
B

ATOM
1783
CA
ASN B
358
56.659
26.124
51.072
1.00
26.16
B

ATOM
1784
CB
ASN B
358
57.913
26.583
51.804
1.00
24.91
B

ATOM
1785
CG
ASN B
358
58.964
25.505
51.866
1.00
24.24
B

ATOM
1786
OD1
ASN B
358
60.149
25.794
51.827
1.00
24.48
B

ATOM
1787
ND2
ASN B
358
58.530
24.242
51.976
1.00
23.61
B

ATOM
1788
C
ASN B
358
55.440
26.669
51.796
1.00
27.01
B

ATOM
1789
O
ASN B
358
54.743
25.940
52.500
1.00
29.45
B

ATOM
1790
N
ILE B
359
55.169
27.948
51.603
1.00
25.54
B

ATOM
1791
CA
ILE B
359
54.066
28.576
52.287
1.00
24.86
B

ATOM
1792
CB
ILE B
359
53.989
30.111
51.964
1.00
23.57
B

ATOM
1793
CG2
ILE B
359
53.438
30.361
50.544
1.00
22.38
B

ATOM
1794
CG1
ILE B
359
53.099
30.808
52.994
1.00
21.88
B

ATOM
1795
CD1
ILE B
359
53.627
30.735
54.428
1.00
17.84
B

ATOM
1796
C
ILE B
359
52.726
27.929
51.992
1.00
27.18
B

ATOM
1797
O
ILE B
359
51.864
27.842
52.859
1.00
27.37
B

ATOM
1798
N
PHE B
360
52.533
27.457
50.775
1.00
29.04
B

ATOM
1799
CA
PHE B
360
51.260
26.850
50.480
1.00
30.13
B

ATOM
1800
CB
PHE B
360
50.977
26.994
48.976
1.00
31.09
B

ATOM
1801
CG
PHE B
360
50.729
28.441
48.552
1.00
35.13
B

ATOM
1802
CD1
PHE B
360
49.750
29.214
49.196
1.00
36.04
B

ATOM
1803
CD2
PHE B
360
51.480
29.040
47.540
1.00
35.99
B

ATOM
1804
CE1
PHE B
360
49.531
30.554
48.837
1.00
36.47
B

ATOM
1805
CE2
PHE B
360
51.265
30.380
47.177
1.00
37.16
B

ATOM
1806
CZ
PHE B
360
50.290
31.138
47.827
1.00
35.98
B

ATOM
1807
C
PHE B
360
51.137
25.414
51.019
1.00
28.89
B

ATOM
1808
O
PHE B
360
50.040
24.932
51.282
1.00
29.91
B

ATOM
1809
N
ILE B
361
52.258
24.739
51.221
1.00
26.91
B

ATOM
1810
CA
ILE B
361
52.212
23.405
51.799
1.00
25.90
B

ATOM
1811
CE
ILE B
361
53.567
22.687
51.626
1.00
24.75
B

ATOM
1812
CG2
ILE B
361
53.707
21.556
52.648
1.00
20.19
B

ATOM
1813
CG1
ILE B
361
53.695
22.198
50.187
1.00
21.38
B

ATOM
1814
CD1
ILE B
361
55.017
21.579
49.880
1.00
21.49
B

ATOM
1815
C
ILE B
361
51.894
23.539
53.303
1.00
25.76
B

ATOM
1816
O
ILE B
361
51.165
22.724
53.854
1.00
25.25
B

ATOM
1817
N
LEU B
362
52.455
24.558
53.955
1.00
24.78
B

ATOM
1818
CA
LEU B
362
52.200
24.780
55.367
1.00
24.80
B

ATOM
1819
CB
LEU B
362
53.097
25.890
55.942
1.00
24.95
B

ATOM
1820
CG
LEU B
362
52.861
26.232
57.439
1.00
25.61
B

ATOM
1821
CD1
LEU B
362
53.251
25.034
58.290
1.00
23.05
B

ATOM
1822
CD2
LEU B
362
53.682
27.448
57.891
1.00
24.66
B

ATOM
1823
C
LEU B
362
50.746
25.192
55.479
1.00
24.68
B

ATOM
1824
O
LEU B
362
50.075
24.847
56.440
1.00
25.14
B

ATOM
1825
N
LYS B
363
50.262
25.932
54.485
1.00
26.90
B

ATOM
1826
CA
LYS B
363
48.870
26.397
54.455
1.00
28.18
B

ATOM
1827
CB
LYS B
363
48.607
27.192
53.178
1.00
30.22
B

ATOM
1828
CG
LYS B
363
48.946
28.677
53.262
1.00
34.21
B

ATOM
1829
CD
LYS B
363
47.787
29.466
53.860
1.00
35.29
B

ATOM
1830
CE
LYS B
363
48.036
30.984
53.859
1.00
38.15
B

ATOM
1831
NZ
LYS B
363
48.196
31.608
52.486
1.00
38.16
B

ATOM
1832
C
LYS B
363
47.931
25.209
54.497
1.00
27.14
B

ATOM
1833
O
LYS B
363
46.852
25.288
55.076
1.00
27.91
B

ATOM
1834
N
ASN B
364
48.365
24.119
53.872
1.00
26.50
B

ATOM
1835
CA
ASN B
364
47.602
22.893
53.809
1.00
28.02
B

ATOM
1836
CB
ASN B
364
48.119
21.990
52.692
1.00
29.30
B

ATOM
1837
CG
ASN B
364
47.742
22.485
51.311
1.00
30.37
B

ATOM
1838
OD1
ASN B
364
48.127
21.882
50.299
1.00
29.53
B

ATOM
1839
ND2
ASN B
364
46.982
23.584
51.255
1.00
31.60
B

ATOM
1840
C
ASN B
364
47.696
22.129
55.106
1.00
27.69
B

ATOM
1841
O
ASN B
364
46.716
21.551
55.559
1.00
28.47
B

ATOM
1842
N
TRP B
365
48.882
22.093
55.693
1.00
26.51
B

ATOM
1843
CA
TRP B
365
49.039
21.371
56.938
1.00
27.73
B

ATOM
1844
CB
TRP B
365
50.489
21.397
57.400
1.00
29.20
B

ATOM
1845
CG
TRP B
365
51.351
20.381
56.790
1.00
29.13
B

ATOM
1846
CD2
TRP B
365
51.742
19.142
57.379
1.00
29.19
B

ATOM
1847
CE2
TRP B
365
52.638
18.523
56.489
1.00
28.54
B

ATOM
1848
CE3
TRP B
365
51.425
18.495
58.579
1.00
29.88
B

ATOM
1849
CD1
TRP B
365
51.989
20.460
55.598
1.00
28.45
B

ATOM
1850
NE1
TRP B
365
52.771
19.351
55.406
1.00
27.81
B

ATOM
1851
CZ2
TRP B
365
53.230
17.282
56.758
1.00
28.80
B

ATOM
1852
CZ3
TRP B
365
52.018
17.257
58.842
1.00
29.52
B

ATOM
1853
CH2
TRP B
365
52.909
16.671
57.934
1.00
27.59
B

ATOM
1854
C
TRP B
365
48.183
21.976
58.037
1.00
27.25
B

ATOM
1855
O
TRP B
365
47.686
21.262
58.898
1.00
27.54
B

ATOM
1856
N
TYR B
366
48.015
23.293
57.985
1.00
25.59
B

ATOM
1857
CA
TYR B
366
47.271
24.038
58.989
1.00
25.83
B

ATOM
1858
CB
TYR B
366
47.858
25.433
59.127
1.00
24.61
B

ATOM
1859
CG
TYR B
366
49.220
25.559
59.761
1.00
22.97
B

ATOM
1860
CD1
TYR B
366
49.803
24.511
60.469
1.00
23.61
B

ATOM
1861
CE1
TYR B
366
50.999
24.699
61.170
1.00
21.04
B

ATOM
1862
CD2
TYR B
366
49.871
26.779
59.760
1.00
21.89
B

ATOM
1863
CE2
TYR B
366
51.050
26.968
60.452
1.00
20.89
B

ATOM
1864
CZ
TYR B
366
51.603
25.940
61.153
1.00
20.92
B

ATOM
1865
OH
TYR B
366
52.741
26.179
61.878
1.00
21.34
B

ATOM
1866
C
TYR B
366
45.781
24.205
58.730
1.00
26.75
B

ATOM
1867
O
TYR B
366
45.053
24.659
59.618
1.00
25.47
B

ATOM
1868
N
ASN B
367
45.343
23.874
57.516
1.00
27.78
B

ATOM
1869
CA
ASN B
367
43.935
23.993
57.137
1.00
28.96
B

ATOM
1870
CB
ASN B
367
43.789
24.062
55.611
1.00
27.81
B

ATOM
1871
CG
ASN B
367
42.420
24.542
55.172
1.00
27.70
B

ATOM
1872
OD1
ASN B
367
41.462
24.533
55.944
1.00
29.38
B

ATOM
1873
ND2
ASN B
367
42.321
24.957
53.915
1.00
27.06
B

ATOM
1874
C
ASN B
367
43.184
22.772
57.668
1.00
29.83
B

ATOM
1875
O
ASN B
367
43.454
21.638
57.253
1.00
30.52
B

ATOM
1876
N
PRO B
368
42.246
22.988
58.613
1.00
30.10
B

ATOM
1877
CD
PRO B
368
41.884
24.278
59.227
1.00
28.86
B

ATOM
1878
CA
PRO B
368
41.458
21.889
59.200
1.00
29.62
B

ATOM
1879
CB
PRO B
368
40.654
22.578
60.304
1.00
28.09
B

ATOM
1880
CG
PRO B
368
41.398
23.839
60.573
1.00
28.33
B

ATOM
1881
C
PRO B
368
40.534
21.318
58.133
1.00
29.34
B

ATOM
1882
O
PRO B
368
40.223
20.133
58.118
1.00
28.44
B

ATOM
1883
N
LYS B
369
40.083
22.202
57.256
1.00
29.08
B

ATOM
1884
CA
LYS B
369
39.202
21.814
56.187
1.00
30.72
B

ATOM
1885
CB
LYS B
369
38.417
23.044
55.697
1.00
32.78
B

ATOM
1886
CG
LYS B
369
37.095
23.310
56.487
1.00
34.07
B

ATOM
1887
CD
LYS B
369
36.649
24.778
56.462
1.00
36.76
B

ATOM
1888
CE
LYS B
369
36.882
25.442
55.098
1.00
38.43
B

ATOM
1889
NZ
LYS B
369
36.568
26.906
55.151
1.00
41.21
B

ATOM
1890
C
LYS B
369
39.977
21.145
55.050
1.00
30.60
B

ATOM
1891
O
LYS B
369
39.389
20.779
54.040
1.00
32.44
B

ATOM
1892
N
PHE B
370
41.293
20.985
55.207
1.00
29.96
B

ATOM
1893
CA
PHE B
370
42.111
20.335
54.175
1.00
28.15
B

ATOM
1894
CB
PHE B
370
43.422
21.107
53.934
1.00
29.31
B

ATOM
1895
CG
PHE B
370
44.447
20.330
53.124
1.00
31.81
B

ATOM
1896
CD1
PHE B
370
45.283
19.394
53.738
1.00
34.71
B

ATOM
1897
CD2
PHE B
370
44.536
20.484
51.745
1.00
31.92
B

ATOM
1898
CE1
PHE B
370
46.185
18.625
52.992
1.00
34.80
B

ATOM
1899
CE2
PHE B
370
45.436
19.718
50.992
1.00
33.21
B

ATOM
1900
CZ
PHE B
370
46.259
18.785
51.622
1.00
33.35
B

ATOM
1901
C
PHE B
370
42.431
18.886
54.537
1.00
26.13
B

ATOM
1902
O
PHE B
370
42.750
18.584
55.682
1.00
26.19
B

ATOM
1903
N
VAL B
371
42.352
17.993
53.556
1.00
25.26
B

ATOM
1904
CA
VAL B
371
42.656
16.590
53.811
1.00
24.76
B

ATOM
1905
CB
VAL B
371
41.419
15.694
53.697
1.00
25.22
B

ATOM
1906
CG1
VAL B
371
41.736
14.297
54.237
1.00
22.91
B

ATOM
1907
CG2
VAL B
371
40.257
16.324
54.442
1.00
23.49
B

ATOM
1908
C
VAL B
371
43.712
16.062
52.863
1.00
24.14
B

ATOM
1909
O
VAL B
371
43.585
16.188
51.653
1.00
23.89
B

ATOM
1910
N
PRO B
372
44.767
15.447
53.418
1.00
24.76
B

ATOM
1911
CD
PRO B
372
44.861
15.087
54.840
1.00
25.65
B

ATOM
1912
CA
PRO B
372
45.889
14.878
52.678
1.00
25.57
B

ATOM
1913
CB
PRO B
372
46.835
14.390
53.769
1.00
25.32
B

ATOM
1914
CG
PRO B
372
46.318
14.998
55.041
1.00
26.54
B

ATOM
1915
C
PRO B
372
45.421
13.720
51.863
1.00
27.92
B

ATOM
1916
O
PRO B
372
44.359
13.144
52.143
1.00
29.78
B

ATOM
1917
N
GLN B
373
46.223
13.375
50.858
1.00
28.98
B

ATOM
1918
CA
GLN B
373
45.940
12.222
50.002
1.00
29.41
B

ATOM
1919
CB
GLN B
373
46.566
12.412
48.600
1.00
29.51
B

ATOM
1920
CG
GLN B
373
45.660
13.145
47.586
1.00
29.73
B

ATOM
1921
CD
GLN B
373
46.354
13.455
46.247
1.00
30.26
B

ATOM
1922
OE1
GLN B
373
47.091
14.429
46.129
1.00
30.70
B

ATOM
1923
NE2
GLN B
373
46.113
12.621
45.240
1.00
30.61
B

ATOM
1924
C
GLN B
373
46.554
11.029
50.758
1.00
28.67
B

ATOM
1925
O
GLN B
373
47.662
11.119
51.274
1.00
28.24
B

ATOM
1926
N
ARG B
374
45.803
9.936
50.845
1.00
28.06
B

ATOM
1927
CA
ARG B
374
46.213
8.728
51.557
1.00
25.68
B

ATOM
1928
CB
ARG B
374
45.030
8.254
52.416
1.00
25.68
B

ATOM
1929
CG
ARG B
374
45.173
6.929
53.159
1.00
24.87
B

ATOM
1930
CD
ARG B
374
45.727
7.099
54.544
1.00
25.14
B

ATOM
1931
NE
ARG B
374
45.604
5.872
55.347
1.00
26.59
B

ATOM
1932
CZ
ARG B
374
44.549
5.554
56.099
1.00
24.91
B

ATOM
1933
NH1
ARG B
374
43.503
6.370
56.171
1.00
23.91
B

ATOM
1934
NH2
ARG B
374
44.533
4.407
56.770
1.00
23.39
B

ATOM
1935
C
ARG B
374
46.650
7.619
50.598
1.00
25.60
B

ATOM
1936
O
ARG B
374
45.978
7.352
49.591
1.00
25.61
B

ATOM
1937
N
THR B
375
47.790
7.000
50.909
1.00
24.83
B

ATOM
1938
CA
THR B
375
48.325
5.895
50.124
1.00
24.29
B

ATOM
1939
CB
THR B
375
49.562
6.298
49.278
1.00
24.62
B

ATOM
1940
OG1
THR B
375
49.334
7.559
48.630
1.00
26.27
B

ATOM
1941
CG2
THR B
375
49.845
5.228
48.217
1.00
22.20
B

ATOM
1942
C
THR B
375
48.787
4.844
51.125
1.00
25.05
B

ATOM
1943
O
THR B
375
49.710
5.108
51.889
1.00
25.56
B

ATOM
1944
N
THR B
376
48.149
3.669
51.122
1.00
25.33
B

ATOM
1945
CA
THR B
376
48.509
2.571
52.034
1.00
25.61
B

ATOM
1946
CB
THR B
376
47.254
1.951
52.733
1.00
23.00
B

ATOM
1947
OG1
THR B
376
46.361
2.992
53.148
1.00
23.90
B

ATOM
1948
CG2
THR B
376
47.678
1.125
53.956
1.00
21.63
B

ATOM
1949
C
THR B
376
49.224
1.439
51.273
1.00
27.50
B

ATOM
1950
O
THR B
376
48.696
0.916
50.303
1.00
27.69
B

ATOM
1951
N
LEU B
377
50.413
1.058
51.735
1.00
29.38
B

ATOM
1952
CA
LEU B
377
51.204
−0.001
51.119
1.00
29.82
B

ATOM
1953
CB
LEU B
377
52.540
0.574
50.650
1.00
27.89
B

ATOM
1954
CG
LEU B
377
52.396
1.871
49.837
1.00
27.64
B

ATOM
1955
CD1
LEU B
377
53.754
2.507
49.549
1.00
23.10
B

ATOM
1956
CD2
LEU B
377
51.643
1.570
48.562
1.00
26.07
B

ATOM
1957
C
LEU B
377
51.451
−1.131
52.125
1.00
32.73
B

ATOM
1958
O
LEU B
377
51.328
−0.925
53.327
1.00
32.89
B

ATOM
1959
N
ARG B
378
51.815
−2.315
51.633
1.00
36.51
B

ATOM
1960
CA
ARG B
378
52.071
−3.463
52.498
1.00
39.20
B

ATOM
1961
CB
ARG B
378
52.180
−4.757
51.678
1.00
42.06
B

ATOM
1962
CG
ARG B
378
52.510
−6.019
52.506
1.00
45.42
B

ATOM
1963
CD
ARG B
378
52.472
−7.335
51.682
1.00
48.17
B

ATOM
1964
NE
ARG B
378
51.210
−7.513
50.958
1.00
51.30
B

ATOM
1965
CZ
ARG B
378
50.850
−8.616
50.306
1.00
52.70
B

ATOM
1966
NH1
ARG B
378
51.655
−9.673
50.281
1.00
53.25
B

ATOM
1967
NH2
ARG B
378
49.684
−8.654
49.664
1.00
54.26
B

ATOM
1968
C
ARG B
378
53.333
−3.278
53.307
1.00
40.74
B

ATOM
1969
O
ARG B
378
54.339
−2.747
52.819
1.00
40.15
B

ATOM
1970
N
GLY B
379
53.266
−3.735
54.555
1.00
42.99
B

ATOM
1971
CA
GLY B
379
54.394
−3.628
55.463
1.00
43.31
B

ATOM
1972
C
GLY B
379
55.221
−4.897
55.532
1.00
43.80
B

ATOM
1973
O
GLY B
379
55.501
−5.532
54.516
1.00
42.41
B

ATOM
1974
N
HIS B
380
55.609
−5.264
56.747
1.00
44.62
B

ATOM
1975
CA
HIS B
380
56.421
−6.451
56.972
1.00
45.57
B

ATOM
1976
CB
HIS B
380
57.468
−6.163
58.049
1.00
42.95
B

ATOM
1977
CG
HIS B
380
58.489
−5.148
57.640
1.00
41.43
B

ATOM
1978
CD2
HIS B
380
58.369
−3.842
57.307
1.00
39.61
B

ATOM
1979
ND1
HIS B
380
59.833
−5.444
57.559
1.00
40.42
B

ATOM
1980
CE1
HIS B
380
60.497
−4.362
57.195
1.00
39.52
B

ATOM
1981
NE2
HIS B
380
59.633
−3.376
57.037
1.00
39.67
B

ATOM
1982
C
HIS B
380
55.552
−7.627
57.398
1.00
47.13
B

ATOM
1983
O
HIS B
380
54.374
−7.457
57.690
1.00
47.01
B

ATOM
1984
N
MSE B
381
56.127
−8.822
57.440
1.00
49.63
B

ATOM
1985
CA
MSE B
381
55.350
−9.979
57.826
1.00
51.34
B

ATOM
1986
CB
MSE B
381
56.181
−11.238
57.658
1.00
54.42
B

ATOM
1987
CG
MSE B
381
56.131
−11.740
56.225
1.00
60.08
B

ATOM
1988
SE
MSE B
381
57.583
−12.923
55.737
1.00
69.56
B

ATOM
1989
CE
MSE B
381
56.901
−14.517
56.629
1.00
64.33
B

ATOM
1990
C
MSE B
381
54.800
−9.860
59.227
1.00
51.47
B

ATOM
1991
O
MSE B
381
53.645
−10.193
59.464
1.00
53.52
B

ATOM
1992
N
THR B
382
55.608
−9.366
60.158
1.00
50.41
B

ATOM
1993
CA
THR B
382
55.159
−9.204
61.539
1.00
48.29
B

ATOM
1994
CB
THR B
382
56.367
−9.222
62.513
1.00
48.92
B

ATOM
1995
OG1
THR B
382
55.931
−8.858
63.825
1.00
49.73
B

ATOM
1996
CG2
THR B
382
57.457
−8.259
62.048
1.00
51.19
B

ATOM
1997
C
THR B
382
54.361
−7.903
61.674
1.00
46.73
B

ATOM
1998
O
THR B
382
54.511
−6.990
60.858
1.00
45.72
B

ATOM
1999
N
SER B
383
53.510
−7.818
62.695
1.00
45.75
B

ATOM
2000
CA
SER B
383
52.667
−6.631
62.888
1.00
44.00
B

ATOM
2001
CB
SER B
383
51.418
−6.988
63.706
1.00
44.17
B

ATOM
2002
OG
SER B
383
51.707
−6.998
65.093
1.00
44.67
B

ATOM
2003
C
SER B
383
53.363
−5.440
63.552
1.00
42.52
B

ATOM
2004
O
SER B
383
52.739
−4.400
63.769
1.00
42.16
B

ATOM
2005
N
VAL B
384
54.645
−5.584
63.875
1.00
40.61
B

ATOM
2006
CA
VAL B
384
55.368
−4.496
64.519
1.00
38.88
B

ATOM
2007
CB
VAL B
384
55.785
−4.868
65.971
1.00
37.56
B

ATOM
2008
CG1
VAL B
384
56.490
−3.706
66.635
1.00
34.97
B

ATOM
2009
CG2
VAL B
384
54.570
−5.273
66.772
1.00
37.83
B

ATOM
2010
C
VAL B
384
56.617
−4.090
63.756
1.00
38.38
B

ATOM
2011
O
VAL B
384
57.507
−4.906
63.506
1.00
38.18
B

ATOM
2012
N
ILE B
385
56.674
−2.823
63.372
1.00
37.92
B

ATOM
2013
CA
ILE B
385
57.842
−2.330
62.674
1.00
38.47
B

ATOM
2014
CB
ILE B
385
57.462
−1.284
61.570
1.00
38.37
B

ATOM
2015
CG2
ILE B
385
58.692
−0.795
60.853
1.00
35.43
B

ATOM
2016
CG1
ILE B
385
56.610
−1.951
60.483
1.00
38.29
B

ATOM
2017
CD1
ILE B
385
56.296
−1.048
59.293
1.00
40.13
B

ATOM
2018
C
ILE B
385
58.752
−1.744
63.758
1.00
38.62
B

ATOM
2019
O
ILE B
385
58.295
−1.054
64.679
1.00
39.76
B

ATOM
2020
N
THR B
386
60.040
−2.057
63.649
1.00
37.77
B

ATOM
2021
CA
THR B
386
61.053
−1.643
64.616
1.00
34.37
B

ATOM
2022
CB
THP. B
386
62.142
−2.722
64.734
1.00
32.81
B

ATOM
2023
OG1
THR B
386
62.810
−2.855
63.473
1.00
31.89
B

ATOM
2024
CG2
THR B
386
61.528
−4.050
65.098
1.00
32.45
B

ATOM
2025
C
THR B
386
61.740
−0.329
64.281
1.00
32.70
B

ATOM
2026
O
THR B
386
62.088
0.438
65.167
1.00
33.06
B

ATOM
2027
N
CYS B
387
61.947
−0.058
63.005
1.00
31.07
B

ATOM
2028
CA
CYS B
387
62.627
1.178
62.659
1.00
30.70
B

ATOM
2029
CB
CYS B
387
64.140
0.964
62.769
1.00
29.49
B

ATOM
2030
SG
CYS B
387
64.707
−0.568
62.008
1.00
32.59
B

ATOM
2031
C
CYS B
387
62.250
1.702
61.268
1.00
29.94
B

ATOM
2032
O
CYS B
387
61.896
0.927
60.365
1.00
27.25
B

ATOM
2033
N
LEU B
388
62.349
3.021
61.097
1.00
29.32
B

ATOM
2034
CA
LEU B
388
62.001
3.659
59.828
1.00
28.34
B

ATOM
2035
CB
LEU B
388
60.534
4.097
59.878
1.00
28.15
B

ATOM
2036
CG
LEU B
388
59.848
4.716
58.662
1.00
25.84
B

ATOM
2037
CD1
LEU B
388
58.358
4.729
58.925
1.00
26.04
B

ATOM
2038
CD2
LEU B
388
60.361
6.117
58.401
1.00
24.86
B

ATOM
2039
C
LEU B
388
62.885
4.851
59.479
1.00
26.75
B

ATOM
2040
O
LEU B
388
63.211
5.661
60.336
1.00
25.66
B

ATOM
2041
N
GLN B
389
63.284
4.947
58.214
1.00
27.43
B

ATOM
2042
CA
GLN B
389
64.112
6.067
57.753
1.00
27.85
B

ATOM
2043
CB
GLN B
389
65.505
5.589
57.308
1.00
28.80
B

ATOM
2044
CG
GLN B
389
66.450
5.215
58.443
1.00
29.07
B

ATOM
2045
CD
GLN B
389
66.900
6.425
59.249
1.00
29.82
B

ATOM
2046
OE1
GLN B
389
67.815
7.152
58.849
1.00
30.35
B

ATOM
2047
NE2
GLN B
389
66.244
6.654
60.383
1.00
27.50
B

ATOM
2048
C
GLN B
389
63.417
6.718
56.577
1.00
26.75
B

ATOM
2049
O
GLN B
389
62.792
6.035
55.766
1.00
26.92
B

ATOM
2050
N
PHE B
390
63.532
8.037
56.483
1.00
26.42
B

ATOM
2051
CA
PHE B
390
62.928
8.778
55.382
1.00
26.53
B

ATOM
2052
CB
PHE B
390
61.606
9.405
55.833
1.00
24.52
B

ATOM
2053
CG
PHE B
390
60.846
10.069
54.728
1.00
23.83
B

ATOM
2054
CD1
PHE B
390
60.614
9.408
53.530
1.00
24.31
B

ATOM
2055
CD2
PHE B
390
60.357
11.358
54.883
1.00
24.82
B

ATOM
2056
CE1
PHE B
390
59.906
10.021
52.496
1.00
24.43
B

ATOM
2057
CE2
PHE B
390
59.643
11.985
53.851
1.00
26.18
B

ATOM
2058
CZ
PHE B
390
59.418
11.316
52.657
1.00
25.05
B

ATOM
2059
C
PHE B
390
63.885
9.852
54.853
1.00
28.00
B

ATOM
2060
O
PHE B
390
64.003
10.930
55.439
1.00
26.52
B

ATOM
2061
N
GLU B
391
64.591
9.532
53.761
1.00
31.44
B

ATOM
2062
CA
GLU B
391
65.552
10.459
53.112
1.00
34.19
B

ATOM
2063
CB
GLU B
391
66.958
10.374
53.753
1.00
35.50
B

ATOM
2064
CG
GLU B
391
67.082
9.731
55.143
1.00
38.57
B

ATOM
2065
CD
GLU B
391
66.652
10.654
56.306
1.00
40.82
B

ATOM
2066
OE1
GLU B
391
66.842
11.896
56.199
1.00
38.26
B

ATOM
2067
OE2
GLU B
391
66.138
10.116
57.327
1.00
41.64
B

ATOM
2068
C
GLU B
391
65.706
10.165
51.602
1.00
34.30
B

ATOM
2069
O
GLU B
391
65.415
9.060
51.141
1.00
32.53
B

ATOM
2070
N
ASP B
392
66.179
11.151
50.842
1.00
35.27
B

ATOM
2071
CA
ASP B
392
66.388
10.979
49.395
1.00
35.87
B

ATOM
2072
CB
ASP B
392
67.633
10.114
49.106
1.00
35.92
B

ATOM
2073
CG
ASP B
392
68.941
10.886
49.139
1.00
36.64
B

ATOM
2074
OD1
ASP B
392
68.967
12.093
48.795
1.00
37.84
B

ATOM
2075
OD2
ASP B
392
69.964
10.253
49.492
1.00
36.21
B

ATOM
2076
C
ASP B
392
65.215
10.300
48.673
1.00
36.11
B

ATOM
2077
O
ASP B
392
65.452
9.465
47.805
1.00
36.71
B

ATOM
2078
N
ASN B
393
63.968
10.618
49.018
1.00
35.71
B

ATOM
2079
CA
ASN B
393
62.805
9.999
48.347
1.00
35.51
B

ATOM
2080
CB
ASN B
393
62.861
10.281
46.847
1.00
34.88
B

ATOM
2081
CG
ASN B
393
62.762
11.755
46.544
1.00
37.09
B

ATOM
2082
OD1
ASN B
393
61.672
12.328
46.584
1.00
36.85
B

ATOM
2083
ND2
ASN B
393
63.903
12.388
46.255
1.00
37.57
B

ATOM
2084
C
ASN B
393
62.633
8.489
48.570
1.00
35.26
B

ATOM
2085
O
ASN B
393
61.925
7.805
47.817
1.00
34.05
B

ATOM
2086
N
TYR B
394
63.283
7.990
49.618
1.00
35.44
B

ATOM
2087
CA
TYR B
394
63.246
6.585
50.004
1.00
33.92
B

ATOM
2088
CB
TYR B
394
64.660
6.006
50.087
1.00
34.53
B

ATOM
2089
CG
TYR B
394
65.314
5.705
48.772
1.00
35.08
B

ATOM
2090
CD1
TYR B
394
64.808
4.707
47.944
1.00
33.82
B

ATOM
2091
CE1
TYR B
394
65.424
4.394
46.753
1.00
35.67
B

ATOM
2092
CD2
TYR B
394
66.461
6.393
48.370
1.00
33.92
B

ATOM
2093
CE2
TYR B
394
67.093
6.091
47.179
1.00
36.23
B

ATOM
2094
CZ
TYR B
394
66.571
5.090
46.369
1.00
37.49
B

ATOM
2095
OH
TYR B
394
67.184
4.785
45.167
1.00
39.46
B

ATOM
2096
C
TYR B
394
62.652
6.473
51.393
1.00
33.94
B

ATOM
2097
O
TYR B
394
62.973
7.268
52.281
1.00
32.72
B

ATOM
2098
N
VAL B
395
61.804
5.470
51.575
1.00
33.59
B

ATOM
2099
CA
VAL B
395
61.200
5.196
52.864
1.00
33.27
B

ATOM
2100
CB
VAL B
395
59.655
5.170
52.787
1.00
33.84
B

ATOM
2101
CG1
VAL B
395
59.055
4.927
54.167
1.00
32.25
B

ATOM
2102
CG2
VAL B
395
59.145
6.467
52.213
1.00
34.69
B

ATOM
2103
C
VAL B
395
61.708
3.803
53.182
1.00
33.68
B

ATOM
2104
O
VAL B
395
61.334
2.822
52.526
1.00
35.51
B

ATOM
2105
N
ILE B
396
62.592
3.701
54.163
1.00
33.52
B

ATOM
2106
CA
ILE B
396
63.113
2.386
54.508
1.00
32.85
B

ATOM
2107
CB
ILE B
396
64.666
2.403
54.579
1.00
33.18
B

ATOM
2108
CG2
ILE B
396
65.207
0.998
54.438
1.00
32.95
B

ATOM
2109
CG1
ILE B
396
65.238
3.231
53.434
1.00
32.57
B

ATOM
2110
CD1
ILE B
396
66.704
3.519
53.594
1.00
34.98
B

ATOM
2111
C
ILE B
396
62.527
1.999
55.862
1.00
30.96
B

ATOM
2112
O
ILE B
396
62.550
2.787
56.805
1.00
29.47
B

ATOM
2113
N
THR B
397
61.977
0.792
55.943
1.00
29.81
B

ATOM
2114
CA
THR B
397
61.397
0.303
57.188
1.00
30.52
B

ATOM
2115
CB
THR B
397
59.883
0.014
57.087
1.00
28.68
B

ATOM
2116
OG1
THR B
397
59.685
−1.096
56.216
1.00
27.52
B

ATOM
2117
CG2
THR B
397
59.127
1.206
56.561
1.00
28.88
B

ATOM
2118
C
THR B
397
62.052
−1.012
57.574
1.00
32.66
B

ATOM
2119
O
THR B
397
62.495
−1.768
56.708
1.00
32.93
B

ATOM
2120
N
GLY B
398
62.095
−1.283
58.878
1.00
34.04
B

ATOM
2121
CA
GLY B
398
62.673
−2.521
59.377
1.00
36.31
B

ATOM
2122
C
GLY B
398
61.790
−3.205
60.409
1.00
38.57
B

ATOM
2123
O
GLY B
398
61.203
−2.535
61.257
1.00
38.84
B

ATOM
2124
N
ALA B
399
61.692
−4.532
60.347
1.00
40.48
B

ATOM
2125
CA
ALA B
399
60.870
−5.274
61.304
1.00
43.09
B

ATOM
2126
CB
ALA B
399
59.540
−5.687
60.660
1.00
43.54
B

ATOM
2127
C
ALA B
399
61.577
−6.506
61.870
1.00
44.04
B

ATOM
2128
O
ALA B
399
62.688
−6.838
61.461
1.00
43.75
B

ATOM
2129
N
ASP B
400
60.921
−7.182
62.811
1.00
45.72
B

ATOM
2130
CA
ASP B
400
61.498
−8.363
63.446
1.00
47.39
B

ATOM
2131
CB
ASP B
400
60.854
−8.596
64.820
1.00
48.07
B

ATOM
2132
CG
ASP B
400
61.569
−9.666
65.626
1.00
48.91
B

ATOM
2133
OD1
ASP B
400
62.791
−9.515
65.869
1.00
49.38
B

ATOM
2134
OD2
ASP B
400
60.910
−10.656
66.012
1.00
48.62
B

ATOM
2135
C
ASP B
400
61.347
−9.610
62.579
1.00
47.48
B

ATOM
2136
O
ASP B
400
61.522
−10.735
63.048
1.00
49.06
B

ATOM
2137
N
ASP B
401
61.014
−9.403
61.313
1.00
46.02
B

ATOM
2138
CA
ASP B
401
60.851
−10.501
60.378
1.00
43.80
B

ATOM
2139
CB
ASP B
401
59.688
−10.192
59.436
1.00
45.11
B

ATOM
2140
CG
ASP B
401
59.962
−8.996
58.541
1.00
46.35
B

ATOM
2141
OD1
ASP B
401
60.797
−8.130
58.909
1.00
46.25
B

ATOM
2142
OD2
ASP B
401
59.325
−8.919
57.465
1.00
47.47
B

ATOM
2143
C
ASP B
401
62.147
−10.661
59.592
1.00
42.18
B

ATOM
2144
O
ASP B
401
62.153
−11.209
58.498
1.00
40.84
B

ATOM
2145
N
LYS B
402
63.241
−10.171
60.174
1.00
42.03
B

ATOM
2146
CA
LYS B
402
64.581
−10.221
59.577
1.00
41.37
B

ATOM
2147
CB
LYS B
402
65.061
−11.671
59.394
1.00
41.89
B

ATOM
2148
CG
LYS B
402
64.777
−12.595
60.546
1.00
40.16
B

ATOM
2149
CD
LYS B
402
65.248
−14.004
60.249
1.00
39.21
B

ATOM
2150
CE
LYS B
402
64.973
−14.910
61.453
1.00
41.18
B

ATOM
2151
NZ
LYS B
402
65.506
−16.306
61.313
1.00
41.31
B

ATOM
2152
C
LYS B
402
64.584
−9.545
58.217
1.00
41.18
B

ATOM
2153
O
LYS B
402
65.387
−9.880
57.350
1.00
41.03
B

ATOM
2154
N
MSE B
403
63.700
−8.583
58.021
1.00
41.52
B

ATOM
2155
CA
MSE B
403
63.643
−7.932
56.731
1.00
41.52
B

ATOM
2156
CB
MSE B
403
62.364
−8.354
56.024
1.00
44.20
B

ATOM
2157
CG
MSE B
403
62.593
−8.927
54.649
1.00
49.51
B

ATOM
2158
CE
MSE B
403
63.401
−10.704
54.630
1.00
56.96
B

ATOM
2159
CE
MSE B
403
61.754
−11.724
54.910
1.00
52.63
B

ATOM
2160
C
MSE B
403
63.728
−6.408
56.765
1.00
39.82
B

ATOM
2161
O
MSE B
403
63.396
−5.758
57.763
1.00
39.40
B

ATOM
2162
N
ILE B
404
64.163
−5.861
55.638
1.00
37.19
B

ATOM
2163
CA
ILE B
404
64.305
−4.432
55.441
1.00
34.55
B

ATOM
2164
CB
ILE B
404
65.790
−4.049
55.290
1.00
33.79
B

ATOM
2165
CG2
ILE B
404
65.904
−2.619
54.750
1.00
32.01
B

ATOM
2166
CG1
ILE B
404
66.516
−4.256
56.628
1.00
32.98
B

ATOM
2167
CD1
ILE B
404
68.003
−3.868
56.634
1.00
32.54
B

ATOM
2168
C
ILE B
404
63.576
−4.060
54.152
1.00
34.51
B

ATOM
2169
O
ILE B
404
63.994
−4.455
53.061
1.00
33.17
B

ATOM
2170
N
ARG B
405
62.489
−3.303
54.275
1.00
34.07
B

ATOM
2171
CA
ARG B
405
61.714
−2.890
53.104
1.00
34.11
B

ATOM
2172
CB
ARG B
405
60.222
−3.145
53.349
1.00
31.76
B

ATOM
2173
CG
ARG B
405
59.877
−4.612
53.569
1.00
29.64
B

ATOM
2174
CD
ARG B
405
58.419
−4.820
53.979
1.00
28.14
B

ATOM
2175
NE
ARG B
405
57.449
−4.457
52.948
1.00
28.57
B

ATOM
2176
CZ
ARG B
405
57.252
−5.129
51.813
1.00
28.90
B

ATOM
2177
NH1
ARG B
405
57.964
−6.215
51.537
1.00
25.04
B

ATOM
2178
NH2
ARG B
405
56.311
−4.728
50.960
1.00
29.02
B

ATOM
2179
C
ARG B
405
61.912
−1.425
52.730
1.00
34.97
B

ATOM
2180
O
ARG B
405
61.823
−0.545
53.580
1.00
37.29
B

ATOM
2181
N
VAL B
406
62.180
−1.157
51.460
1.00
34.65
B

ATOM
2182
CA
VAL B
406
62.353
0.218
51.027
1.00
35.39
B

ATOM
2183
CB
VAL B
406
63.710
0.421
50.341
1.00
38.27
B

ATOM
2184
CG1
VAL B
406
63.886
−0.606
49.251
1.00
39.50
B

ATOM
2185
CG2
VAL B
406
63.789
1.831
49.759
1.00
38.99
B

ATOM
2186
C
VAL B
406
61.257
0.576
50.041
1.00
34.13
B

ATOM
2187
O
VAL B
406
60.867
−0.250
49.213
1.00
35.33
B

ATOM
2188
N
TYR B
407
60.763
1.806
50.127
1.00
32.42
B

ATOM
2189
CA
TYR B
407
59.694
2.263
49.236
1.00
30.87
B

ATOM
2190
CB
TYR B
407
58.409
2.537
50.032
1.00
30.46
B

ATOM
2191
CG
TYR B
407
57.953
1.435
50.967
1.00
29.77
B

ATOM
2192
CD1
TYR B
407
58.682
1.115
52.121
1.00
27.81
B

ATOM
2193
CE1
TYR B
407
58.269
0.081
52.962
1.00
27.20
B

ATOM
2194
CD2
TYR B
407
56.795
0.695
50.682
1.00
29.18
B

ATOM
2195
CE2
TYR B
407
56.376
−0.335
51.511
1.00
27.89
B

ATOM
2196
CZ
TYR B
407
57.114
−0.645
52.646
1.00
27.80
B

ATOM
2197
OH
TYR B
407
56.711
−1.705
53.430
1.00
26.41
B

ATOM
2198
C
TYR B
407
60.058
3.552
48.507
1.00
29.93
B

ATOM
2199
O
TYR B
407
61.078
4.180
48.790
1.00
30.68
B

ATOM
2200
N
ASP B
408
59.189
3.947
47.583
1.00
29.96
B

ATOM
2201
CA
ASP B
408
59.360
5.181
46.825
1.00
30.52
B

ATOM
2202
CB
ASP B
408
59.226
4.920
45.325
1.00
32.17
B

ATOM
2203
CG
ASP B
408
59.430
6.178
44.504
1.00
35.42
B

ATOM
2204
OD1
ASP B
408
60.450
6.868
44.721
1.00
37.74
B

ATOM
2205
OD2
ASP B
408
58.579
6.483
43.644
1.00
37.68
B

ATOM
2206
C
ASP B
408
58.296
6.195
47.264
1.00
29.92
B

ATOM
2207
O
ASP B
408
57.095
5.995
47.024
1.00
29.81
B

ATOM
2208
N
SER B
409
58.743
7.284
47.895
1.00
28.80
B

ATOM
2209
CA
SER B
409
57.848
8.338
48.400
1.00
28.18
B

ATOM
2210
CB
SER B
409
58.581
9.202
49.442
1.00
25.85
B

ATOM
2211
OG
SER B
409
59.652
9.932
48.869
1.00
23.45
B

ATOM
2212
C
SER B
409
57.253
9.245
47.320
1.00
29.34
B

ATOM
2213
O
SER B
409
56.259
9.941
47.562
1.00
27.47
B

ATOM
2214
N
ILE B
410
57.861
9.224
46.133
1.00
31.65
B

ATOM
2215
CA
ILE B
410
57.421
10.037
44.994
1.00
34.03
B

ATOM
2216
CB
ILE B
410
58.558
10.242
43.972
1.00
35.56
B

ATOM
2217
CG2
ILE B
410
58.032
11.052
42.783
1.00
34.67
B

ATOM
2218
CG1
ILE B
410
59.747
10.947
44.616
1.00
34.10
B

ATOM
2219
CD1
ILE B
410
60.988
10.910
43.752
1.00
33.88
B

ATOM
2220
C
ILE B
410
56.259
9.409
44.217
1.00
34.05
B

ATOM
2221
O
ILE B
410
55.330
10.101
43.818
1.00
33.24
B

ATOM
2222
N
ASN B
411
56.354
8.107
43.972
1.00
34.44
B

ATOM
2223
CA
ASN B
411
55.327
7.390
43.246
1.00
36.84
B

ATOM
2224
CB
ASN B
411
55.955
6.377
42.273
1.00
39.14
B

ATOM
2225
CG
ASN B
411
56.312
6.993
40.911
1.00
41.27
B

ATOM
2226
OD1
ASN B
411
56.852
8.100
40.834
1.00
41.10
B

ATOM
2227
ND2
ASN B
411
56.017
6.261
39.832
1.00
42.48
B

ATOM
2228
C
ASN B
411
54.428
6.663
44.238
1.00
37.14
B

ATOM
2229
O
ASN B
411
53.466
6.001
43.848
1.00
37.86
B

ATOM
2230
N
LYS B
412
54.748
6.776
45.522
1.00
36.65
B

ATOM
2231
CA
LYS B
412
53.944
6.121
46.546
1.00
35.90
B

ATOM
2232
CB
LYS B
412
52.537
6.742
46.595
1.00
35.46
B

ATOM
2233
CG
LYS B
412
52.373
7.994
47.470
1.00
34.91
B

ATOM
2234
CD
LYS B
412
53.251
9.163
47.023
1.00
33.80
B

ATOM
2235
CE
LYS B
412
52.905
10.407
47.809
1.00
32.17
B

ATOM
2236
NZ
LYS B
412
53.762
11.553
47.463
1.00
32.35
B

ATOM
2237
C
LYS B
412
53.812
4.629
46.256
1.00
35.57
B

ATOM
2238
O
LYS B
412
52.703
4.092
46.252
1.00
35.07
B

ATOM
2239
N
LYS B
413
54.932
3.959
46.007
1.00
35.95
B

ATOM
2240
CA
LYS B
413
54.901
2.523
45.721
1.00
36.16
B

ATOM
2241
CB
LYS B
413
54.977
2.254
44.205
1.00
36.93
B

ATOM
2242
CG
LYS B
413
53.730
2.627
43.387
1.00
40.07
B

ATOM
2243
CD
LYS B
413
53.913
2.308
41.900
1.00
41.03
B

ATOM
2244
CE
LYS B
413
52.629
2.529
41.105
1.00
42.27
B

ATOM
2245
NZ
LYS B
413
51.504
1.699
41.610
1.00
43.62
B

ATOM
2246
C
LYS B
413
56.047
1.798
46.402
1.00
35.81
B

ATOM
2247
O
LYS B
413
57.012
2.417
46.841
1.00
33.26
B

ATOM
2248
N
PHE B
414
55.904
0.481
46.503
1.00
38.03
B

ATOM
2249
CA
PHE B
414
56.909
−0.402
47.090
1.00
39.76
B

ATOM
2250
CB
PHE B
414
56.267
−1.749
47.454
1.00
40.36
B

ATOM
2251
CG
PHE B
414
57.257
−2.806
47.872
1.00
42.43
B

ATOM
2252
CD1
PHE B
414
57.994
−2.667
49.046
1.00
43.87
B

ATOM
2253
CD2
PHE B
414
57.499
−3.914
47.058
1.00
41.81
B

ATOM
2254
CE1
PHE B
414
58.965
−3.614
49.398
1.00
43.95
B

ATOM
2255
CE2
PHE B
414
58.466
−4.863
47.401
1.00
41.35
B

ATOM
2256
CZ
PHE B
414
59.201
−4.712
48.571
1.00
42.36
B

ATOM
2257
C
PHE B
414
57.970
−0.598
46.003
1.00
40.17
B

ATOM
2258
O
PHE B
414
57.642
−0.894
44.854
1.00
39.12
B

ATOM
2259
N
LEU B
415
59.236
−0.425
46.361
1.00
41.37
B

ATOM
2260
CA
LEU B
415
60.305
−0.558
45.386
1.00
42.80
B

ATOM
2261
CB
LEU B
415
61.350
0.539
45.608
1.00
44.70
B

ATOM
2262
CG
LEU B
415
62.211
0.891
44.391
1.00
46.65
B

ATOM
2263
CD1
LEU B
415
61.335
1.453
43.273
1.00
46.10
B

ATOM
2264
CD2
LEU B
415
63.277
1.905
44.794
1.00
47.87
B

ATOM
2265
C
LEU B
415
60.950
−1.941
45.464
1.00
43.04
B

ATOM
2266
O
LEU B
415
60.930
−2.699
44.503
1.00
42.67
B

ATOM
2267
N
LEU B
416
61.531
−2.288
46.600
1.00
43.99
B

ATOM
2268
CA
LEU B
416
62.140
−3.607
46.711
1.00
44.67
B

ATOM
2269
CB
LEU B
416
63.471
−3.667
45.948
1.00
43.56
B

ATOM
2270
CG
LEU B
416
64.709
−3.198
46.703
1.00
42.12
B

ATOM
2271
CD1
LEU B
416
65.621
−4.380
46.873
1.00
45.95
B

ATOM
2272
CD2
LEU B
416
65.421
−2.101
45.951
1.00
41.53
B

ATOM
2273
C
LEU B
416
62.363
−3.960
48.165
1.00
44.94
B

ATOM
2274
O
LEU B
416
62.183
−3.123
49.060
1.00
45.50
B

ATOM
2275
N
GLN B
417
62.747
−5.212
48.393
1.00
45.21
B

ATOM
2276
CA
GLN B
417
62.999
−5.712
49.744
1.00
45.08
B

ATOM
2277
CB
GLN B
417
61.984
−6.808
50.120
1.00
43.81
B

ATOM
2278
CG
GLN B
417
62.106
−7.321
51.555
1.00
40.41
B

ATOM
2279
CD
GLN B
417
61.077
−8.383
51.890
1.00
39.74
B

ATOM
2280
OE1
GLN B
417
61.135
−9.507
51.390
1.00
41.92
B

ATOM
2281
NE2
GLN B
417
60.129
−8.033
52.741
1.00
38.39
B

ATOM
2282
C
GLN B
417
64.412
−6.279
49.844
1.00
44.86
B

ATOM
2283
O
GLN B
417
64.906
−6.895
48.897
1.00
43.18
B

ATOM
2284
N
LEU B
418
65.053
−6.053
50.991
1.00
45.20
B

ATOM
2285
CA
LEU B
418
66.408
−6.536
51.246
1.00
44.82
B

ATOM
2286
CB
LEU B
418
67.329
−5.373
51.654
1.00
42.07
B

ATOM
2287
CG
LEU B
418
67.665
−4.358
50.550
1.00
40.04
B

ATOM
2288
CD1
LEU B
418
67.984
−2.989
51.123
1.00
38.25
B

ATOM
2289
CD2
LEU B
418
68.804
−4.885
49.746
1.00
39.20
B

ATOM
2290
C
LEU B
418
66.337
−7.584
52.357
1.00
46.53
B

ATOM
2291
O
LEU B
418
65.728
−7.355
53.411
1.00
46.91
B

ATOM
2292
N
SER B
419
66.929
−8.747
52.086
1.00
47.50
B

ATOM
2293
CA
SER B
419
66.966
−9.854
53.037
1.00
47.26
B

ATOM
2294
CB
SER B
419
66.219
−11.066
52.489
1.00
47.58
B

ATOM
2295
OG
SER B
419
66.861
−11.552
51.330
1.00
47.48
B

ATOM
2296
C
SER B
419
68.423
−10.219
53.282
1.00
47.06
B

ATOM
2297
O
SER B
419
69.267
−10.064
52.396
1.00
46.04
B

ATOM
2298
N
GLY B
420
68.700
−10.697
54.493
1.00
47.22
B

ATOM
2299
CA
GLY B
420
70.047
−11.059
54.886
1.00
46.53
B

ATOM
2300
C
GLY B
420
70.121
−11.386
56.366
1.00
47.16
B

ATOM
2301
O
GLY B
420
70.335
−12.546
56.715
1.00
48.39
B

ATOM
2302
N
HIS B
421
69.927
−10.390
57.237
1.00
46.12
B

ATOM
2303
CA
HIS B
421
69.999
−10.611
58.697
1.00
44.26
B

ATOM
2304
CB
HIS B
421
69.340
−9.451
59.469
1.00
42.53
B

ATOM
2305
CG
HIS B
421
70.144
−8.187
59.459
1.00
41.48
B

ATOM
2306
CD2
HIS B
421
70.083
−7.102
58.653
1.00
41.32
B

ATOM
2307
ND1
HIS B
421
71.231
−7.991
60.282
1.00
41.41
B

ATOM
2308
CE1
HIS B
421
71.811
−6.845
59.977
1.00
41.09
B

ATOM
2309
NE2
HIS B
421
71.135
−6.286
58.990
1.00
40.64
B

ATOM
2310
C
HIS B
421
69.374
−11.937
59.142
1.00
44.07
B

ATOM
2311
O
HIS B
421
68.254
−12.277
58.746
1.00
43.02
B

ATOM
2312
N
ASP B
422
70.103
−12.687
59.964
1.00
43.55
B

ATOM
2313
CA
ASP B
422
69.599
−13.967
60.447
1.00
43.78
B

ATOM
2314
CB
ASP B
422
70.752
−14.881
60.881
1.00
46.42
B

ATOM
2315
CG
ASP B
422
71.843
−15.013
59.811
1.00
48.64
B

ATOM
2316
OD1
ASP B
422
71.518
−15.368
58.649
1.00
47.48
B

ATOM
2317
OD2
ASP B
422
73.030
−14.762
60.145
1.00
50.00
B

ATOM
2318
C
ASP B
422
68.634
−13.762
61.609
1.00
42.50
B

ATOM
2319
O
ASP B
422
67.970
−14.701
62.048
1.00
41.14
B

ATOM
2320
N
GLY B
423
68.561
−12.527
62.099
1.00
42.77
B

ATOM
2321
CA
GLY B
423
67.659
−12.192
63.195
1.00
42.60
B

ATOM
2322
C
GLY B
423
66.843
−10.950
62.865
1.00
41.88
B

ATOM
2323
O
GLY B
423
67.107
−10.300
61.855
1.00
42.25
B

ATOM
2324
N
GLY B
424
65.854
−10.615
63.694
1.00
41.87
B

ATOM
2325
CA
GLY B
424
65.036
−9.432
63.433
1.00
41.62
B

ATOM
2326
C
GLY B
424
65.863
−8.158
63.492
1.00
41.35
B

ATOM
2327
O
GLY B
424
66.673
−7.994
64.389
1.00
41.29
B

ATOM
2328
N
VAL B
425
65.682
−7.254
62.541
1.00
41.10
B

ATOM
2329
CA
VAL B
425
66.452
−6.015
62.557
1.00
42.45
B

ATOM
2330
CB
VAL B
425
66.622
−5.464
61.137
1.00
44.73
B

ATOM
2331
CG1
VAL B
425
65.322
−5.641
60.365
1.00
45.42
B

ATOM
2332
CG2
VAL B
425
67.028
−3.987
61.187
1.00
45.68
B

ATOM
2333
C
VAL B
425
65.796
−4.946
63.433
1.00
41.72
B

ATOM
2334
O
VAL B
425
64.600
−4.702
63.318
1.00
42.42
B

ATOM
2335
N
TRP B
426
66.575
−4.305
64.301
1.00
40.55
B

ATOM
2336
CA
TRP B
426
66.016
−3.284
65.177
1.00
39.71
B

ATOM
2337
CB
TRP B
426
66.069
−3.755
66.632
1.00
36.69
B

ATOM
2338
CG
TRP B
426
65.117
−4.874
66.920
1.00
34.11
B

ATOM
2339
CD2
TRP B
426
63.831
−4.774
67.558
1.00
32.48
B

ATOM
2340
CE2
TRP B
426
63.275
−6.072
67.578
1.00
30.88
B

ATOM
2341
CE3
TRP B
426
63.098
−3.715
68.110
1.00
30.22
B

ATOM
2342
CD1
TRP B
426
65.278
−6.185
66.594
1.00
33.27
B

ATOM
2343
NE1
TRP B
426
64.179
−6.910
66.984
1.00
32.30
B

ATOM
2344
CZ2
TRP B
426
62.017
−6.344
68.129
1.00
31.05
B

ATOM
2345
CZ3
TRP B
426
61.845
−3.984
68.661
1.00
30.71
B

ATOM
2346
CH2
TRP B
426
61.319
−5.289
68.666
1.00
30.24
B

ATOM
2347
C
TRP B
426
66.631
−1.889
65.066
1.00
40.31
B

ATOM
2348
O
TRP B
426
66.089
−0.930
65.607
1.00
40.76
B

ATOM
2349
N
ALA B
427
67.759
−1.774
64.379
1.00
41.09
B

ATOM
2350
CA
ALA B
427
68.400
−0.482
64.198
1.00
42.24
B

ATOM
2351
CB
ALA B
427
69.783
−0.481
64.816
1.00
42.58
B

ATOM
2352
C
ALA B
427
68.488
−0.284
62.695
1.00
43.39
B

ATOM
2353
O
ALA B
427
68.658
−1.251
61.952
1.00
44.01
B

ATOM
2354
N
LEU B
428
68.375
0.963
62.248
1.00
44.59
B

ATOM
2355
CA
LEU B
428
68.401
1.261
60.821
1.00
44.89
B

ATOM
2356
CB
LEU B
428
67.015
0.996
60.230
1.00
45.56
B

ATOM
2357
CG
LEU B
428
66.894
0.895
58.717
1.00
46.48
B

ATOM
2358
CD1
LEU B
428
67.730
−0.281
58.221
1.00
47.28
B

ATOM
2359
CD2
LEU B
428
65.434
0.710
58.349
1.00
46.47
B

ATOM
2360
C
LEU B
428
68.761
2.714
60.608
1.00
44.99
B

ATOM
2361
O
LEU B
428
68.132
3.596
61.178
1.00
46.41
B

ATOM
2362
N
LYS B
429
69.766
2.969
59.785
1.00
44.76
B

ATOM
2363
CA
LYS B
429
70.189
4.341
59.519
1.00
44.20
B

ATOM
2364
CB
LYS B
429
71.478
4.631
60.288
1.00
43.86
B

ATOM
2365
CG
LYS B
429
72.022
6.021
60.108
1.00
43.02
B

ATOM
2366
CD
LYS B
429
71.151
7.060
60.779
1.00
40.87
B

ATOM
2367
CE
LYS B
429
71.741
8.447
60.560
1.00
38.32
B

ATOM
2368
NZ
LYS B
429
71.164
9.464
61.464
1.00
34.95
B

ATOM
2369
C
LYS B
429
70.406
4.457
58.021
1.00
44.44
B

ATOM
2370
O
LYS B
429
70.534
3.445
57.344
1.00
44.65
B

ATOM
2371
N
TYR B
430
70.430
5.677
57.496
1.00
45.98
B

ATOM
2372
CA
TYR B
430
70.617
5.884
56.052
1.00
46.60
B

ATOM
2373
CB
TYR B
430
69.403
6.616
55.458
1.00
43.95
B

ATOM
2374
CG
TYR B
430
69.496
6.911
53.973
1.00
41.46
B

ATOM
2375
CD1
TYR B
430
69.092
5.976
53.027
1.00
40.19
B

ATOM
2376
CE1
TYR B
430
69.153
6.255
51.664
1.00
38.85
B

ATOM
2377
CD2
TYR B
430
69.968
8.137
53.520
1.00
40.10
B

ATOM
2378
CE2
TYR B
430
70.034
8.430
52.164
1.00
39.82
B

ATOM
2379
CZ
TYR B
430
69.625
7.486
51.232
1.00
39.47
B

ATOM
2380
OH
TYR B
430
69.691
7.784
49.874
1.00
37.41
B

ATOM
2381
C
TYR B
430
71.872
6.696
55.767
1.00
47.43
B

ATOM
2382
O
TYR B
430
72.320
7.476
56.603
1.00
48.99
B

ATOM
2383
N
ALA B
431
72.439
6.516
54.582
1.00
48.65
B

ATOM
2384
CA
ALA B
431
73.634
7.263
54.196
1.00
48.95
B

ATOM
2385
CB
ALA B
431
74.882
6.412
54.420
1.00
49.04
B

ATOM
2386
C
ALA B
431
73.533
7.683
52.732
1.00
49.00
B

ATOM
2387
O
ALA B
431
73.298
6.860
51.842
1.00
48.35
B

ATOM
2388
N
HIS B
432
73.729
8.967
52.482
1.00
49.81
B

ATOM
2389
CA
HIS B
432
73.627
9.485
51.126
1.00
52.51
B

ATOM
2390
CB
HIS B
432
74.421
10.787
50.978
1.00
55.86
B

ATOM
2391
CG
HIS B
432
74.148
11.508
49.695
1.00
60.52
B

ATOM
2392
CD2
HIS B
432
74.984
12.012
48.757
1.00
62.00
B

ATOM
2393
ND1
HIS B
432
72.869
11.750
49.238
1.00
62.73
B

ATOM
2394
CE1
HIS B
432
72.930
12.368
48.072
1.00
63.55
B

ATOM
2395
NE2
HIS B
432
74.202
12.539
47.757
1.00
63.41
B

ATOM
2396
C
HIS B
432
74.084
8.497
50.059
1.00
51.80
B

ATOM
2397
O
HIS B
432
75.031
7.737
50.266
1.00
53.10
B

ATOM
2398
N
GLY B
433
73.391
8.508
48.923
1.00
50.58
B

ATOM
2399
CA
GLY B
433
73.741
7.633
47.819
1.00
47.93
B

ATOM
2400
C
GLY B
433
72.921
6.368
47.714
1.00
47.35
B

ATOM
2401
O
GLY B
433
73.272
5.462
46.963
1.00
47.94
B

ATOM
2402
N
GLY B
434
71.823
6.293
48.452
1.00
46.94
B

ATOM
2403
CA
GLY B
434
71.016
5.090
48.392
1.00
45.51
B

ATOM
2404
C
GLY B
434
71.722
3.980
49.147
1.00
44.93
B

ATOM
2405
O
GLY B
434
71.599
2.804
48.824
1.00
45.17
B

ATOM
2406
N
ILE B
435
72.501
4.353
50.151
1.00
44.36
B

ATOM
2407
CA
ILE B
435
73.183
3.352
50.943
1.00
43.99
B

ATOM
2408
CB
ILE B
435
74.701
3.520
50.874
1.00
43.64
B

ATOM
2409
CG2
ILE B
435
75.375
2.722
51.989
1.00
43.26
B

ATOM
2410
CG1
ILE B
435
75.196
3.022
49.528
1.00
43.31
B

ATOM
2411
CD1
ILE B
435
76.656
3.223
49.321
1.00
45.00
B

ATOM
2412
C
ILE B
435
72.724
3.435
52.395
1.00
44.68
B

ATOM
2413
O
ILE B
435
72.570
4.518
52.956
1.00
42.73
B

ATOM
2414
N
LEU B
436
72.486
2.283
53.000
1.00
44.69
B

ATOM
2415
CA
LEU B
436
72.051
2.273
54.376
1.00
46.18
B

ATOM
2416
CB
LEU B
436
70.545
2.006
54.468
1.00
46.74
B

ATOM
2417
CG
LEU B
436
70.020
0.623
54.084
1.00
46.70
B

ATOM
2418
CD1
LEU B
436
68.660
0.398
54.708
1.00
47.92
B

ATOM
2419
CD2
LEU B
436
69.953
0.506
52.574
1.00
48.12
B

ATOM
2420
C
LEU B
436
72.816
1.224
55.176
1.00
47.09
B

ATOM
2421
O
LEU B
436
73.360
0.268
54.619
1.00
46.99
B

ATOM
2422
N
VAL B
437
72.862
1.418
56.488
1.00
46.98
B

ATOM
2423
CA
VAL B
437
73.552
0.497
57.376
1.00
48.04
B

ATOM
2424
CB
VAL B
437
74.617
1.244
58.228
1.00
49.43
B

ATOM
2425
CG1
VAL B
437
75.517
0.251
58.948
1.00
48.59
B

ATOM
2426
CG2
VAL B
437
75.443
2.180
57.333
1.00
49.25
B

ATOM
2427
C
VAL B
437
72.481
−0.062
58.299
1.00
46.89
B

ATOM
2428
O
VAL B
437
71.430
0.551
58.449
1.00
47.34
B

ATOM
2429
N
SER B
438
72.722
−1.222
58.902
1.00
45.63
B

ATOM
2430
CA
SER B
438
71.741
−1.788
59.820
1.00
44.89
B

ATOM
2431
CB
SER B
438
70.729
−2.644
59.072
1.00
44.08
B

ATOM
2432
OG
SER B
438
71.355
−3.758
58.467
1.00
44.83
B

ATOM
2433
C
SER B
438
72.377
−2.622
60.914
1.00
44.82
B

ATOM
2434
O
SER B
438
73.561
−2.949
60.857
1.00
44.21
B

ATOM
2435
N
GLY B
439
71.568
−2.945
61.916
1.00
45.02
B

ATOM
2436
CA
GLY B
439
72.020
‘3.751
63.027
1.00
45.90
B

ATOM
2437
C
GLY B
439
70.855
−4.596
63.498
1.00
46.75
B

ATOM
2438
O
GLY B
439
69.809
−4.054
63.843
1.00
45.99
B

ATOM
2439
N
SER B
440
71.006
−5.915
63.496
1.00
49.24
B

ATOM
2440
CA
SER B
440
69.919
−6.773
63.957
1.00
53.65
B

ATOM
2441
CB
SER B
440
69.429
−7.707
62.842
1.00
54.51
B

ATOM
2442
OG
SER B
440
70.342
−8.766
62.610
1.00
56.40
B

ATOM
2443
C
SER B
440
70.368
−7.612
65.146
1.00
54.82
B

ATOM
2444
O
SER B
440
71.474
−7.447
65.660
1.00
54.64
B

ATOM
2445
N
T5R B
441
69.490
−8.509
65.576
1.00
57.06
B

ATOM
2446
CA
THR B
441
69.769
−9.392
66.695
1.00
59.13
B

ATOM
2447
CB
THR B
441
68.498
−10.086
67.165
1.00
57.43
B

ATOM
2448
OG1
THR B
441
67.489
−9.101
67.397
1.00
55.10
B

ATOM
2449
CG2
THR B
441
68.761
−10.835
68.455
1.00
59.62
B

ATOM
2450
C
T5R B
441
70.778
−10.442
66.262
1.00
61.73
B

ATOM
2451
O
THR B
441
71.212
−11.280
67.048
1.00
62.25
B

ATOM
2452
N
ASP B
442
71.142
−10.379
64.989
1.00
64.11
B

ATOM
2453
CA
ASP B
442
72.098
−11.292
64.403
1.00
65.34
B

ATOM
2454
CB
ASP B
442
72.028
−11.183
62.877
1.00
69.79
B

ATOM
2455
CG
ASP B
442
72.888
−12.220
62.171
1.00
76.04
B

ATOM
2456
OD1
ASP B
442
72.837
−13.413
62.567
1.00
78.67
B

ATOM
2457
OD2
ASP B
442
73.607
−11.846
61.208
1.00
78.25
B

ATOM
2458
C
ASP B
442
73.490
−10.929
64.903
1.00
64.29
B

ATOM
2459
O
ASP B
442
74.469
−11.621
64.626
1.00
65.24
B

ATOM
2460
N
ARG B
443
73.561
−9.843
65.662
1.00
62.52
B

ATOM
2461
CA
ARG B
443
74.817
−9.346
66.214
1.00
60.60
B

ATOM
2462
CB
ARG B
443
75.495
−10.412
67.088
1.00
61.78
B

ATOM
2463
CG
ARG B
443
74.629
−10.891
68.231
1.00
64.13
B

ATOM
2464
CD
ARG B
443
75.329
−11.918
69.100
1.00
65.45
B

ATOM
2465
NE
ARG B
443
75.805
−13.045
68.312
1.00
68.14
B

ATOM
2466
CZ
ARG B
443
76.062
−14.252
68.804
1.00
69.90
B

ATOM
2467
NH1
ARG B
443
75.885
−14.495
70.096
1.00
69.79
B

ATOM
2468
NH2
ARG B
443
76.493
−15.219
67.998
1.00
70.62
B

ATOM
2469
C
ARG B
443
75.754
−8.904
65.100
1.00
58.12
B

ATOM
2470
O
ARG B
443
76.972
−8.886
65.266
1.00
58.34
B

ATOM
2471
N
THR B
444
75.183
−8.534
63.960
1.00
55.54
B

ATOM
2472
CA
THR B
444
76.005
−8.092
62.841
1.00
53.90
B

ATOM
2473
CB
THR B
444
75.945
−9.106
61.671
1.00
54.03
B

ATOM
2474
OG1
THR B
444
74.590
−9.262
61.232
1.00
53.30
B

ATOM
2475
CG2
THR B
444
76.482
−10.464
62.113
1.00
53.83
B

ATOM
2476
C
THR B
444
75.567
−6.727
62.338
1.00
51.81
B

ATOM
2477
O
THR B
444
74.401
−6.377
62.409
1.00
52.22
B

ATOM
2478
N
VAL B
445
76.510
−5.945
61.846
1.00
49.88
B

ATOM
2479
CA
VAL B
445
76.169
−4.641
61.330
1.00
49.27
B

ATOM
2480
CB
VAL B
445
77.158
−3.569
61.825
1.00
48.34
B

ATOM
2481
CG1
VAL B
445
76.756
−2.196
61.303
1.00
47.11
B

ATOM
2482
CG2
VAL B
445
77.192
−3.566
63.349
1.00
48.46
B

ATOM
2483
C
VAL B
445
76.233
−4.745
59.813
1.00
50.36
B

ATOM
2484
O
VAL B
445
77.308
−4.656
59.209
1.00
50.35
B

ATOM
2485
N
ARG B
446
75.080
−4.959
59.194
1.00
50.86
B

ATOM
2486
CA
ARG B
446
75.039
−5.081
57.749
1.00
51.42
B

ATOM
2487
CB
ARG B
446
74.024
−6.152
57.329
1.00
52.81
B

ATOM
2488
CG
ARG B
446
74.384
−7.595
57.725
1.00
53.32
B

ATOM
2489
CD
ARG B
446
73.563
−8.565
56.893
1.00
54.70
B

ATOM
2490
NE
ARG B
446
73.801
−9.970
57.206
1.00
55.46
B

ATOM
2491
CZ
ARG B
446
73.462
−10.545
58.353
1.00
57.14
B

ATOM
2492
NH1
ARG B
446
72.878
−9.834
59.303
1.00
59.85
B

ATOM
2493
NH2
ARG B
446
73.677
−11.839
58.548
1.00
57.51
B

ATOM
2494
C
ARG B
446
74.712
−3.759
57.058
1.00
50.94
B

ATOM
2495
O
ARG B
446
73.764
−3.066
57.427
1.00
51.11
B

ATOM
2496
N
VAL B
447
75.525
−3.414
56.063
1.00
49.98
B

ATOM
2497
CA
VAL B
447
75.338
−2.198
55.280
1.00
49.12
B

ATOM
2498
CB
VAL B
447
76.661
−1.360
55.196
1.00
49.77
B

ATOM
2499
CG1
VAL B
447
77.858
−2.268
55.110
1.00
48.80
B

ATOM
2500
CG2
VAL B
447
76.631
−0.433
53.984
1.00
50.29
B

ATOM
2501
C
VAL B
447
74.876
−2.650
53.893
1.00
47.59
B

ATOM
2502
O
VAL B
447
75.433
−3.584
53.334
1.00
46.28
B

ATOM
2503
N
TRP B
448
73.841
−2.001
53.361
1.00
47.07
B

ATOM
2504
CA
TRP B
448
73.278
−2.349
52.058
1.00
46.70
B

ATOM
2505
CB
TRP B
448
71.807
−2.704
52.201
1.00
43.15
B

ATOM
2506
CG
TRP B
448
71.506
−3.423
53.437
1.00
40.87
B

ATOM
2507
CD2
TRP B
448
71.126
−4.793
53.554
1.00
39.93
B

ATOM
2508
CE2
TRP B
448
70.984
−5.067
54.925
1.00
39.42
B

ATOM
2509
CE3
TRP B
448
70.907
−5.820
52.635
1.00
38.21
B

ATOM
2510
CD1
TRP B
448
71.565
−2.930
54.698
1.00
40.70
B

ATOM
2511
NE1
TRP B
448
71.253
−3.910
55.603
1.00
40.18
B

ATOM
2512
CZ2
TRP B
448
70.620
−6.324
55.400
1.00
39.77
B

ATOM
2513
CZ3
TRP B
448
70.547
−7.073
53.110
1.00
38.97
B

ATOM
2514
CH2
TRP B
448
70.413
−7.314
54.480
1.00
38.38
B

ATOM
2515
C
TRP B
448
73.383
−1.223
51.038
1.00
48.93
B

ATOM
2516
O
TRP B
448
73.774
−0.096
51.360
1.00
49.67
B

ATOM
2517
N
ASP B
449
73.001
−1.542
49.803
1.00
51.05
B

ATOM
2518
CA
ASP B
449
73.014
−0.586
48.698
1.00
52.47
B

ATOM
2519
CB
ASP B
449
74.247
−0.830
47.826
1.00
53.58
B

ATOM
2520
CG
ASP B
449
74.259
0.024
46.568
1.00
55.71
B

ATOM
2521
OD1
ASP B
449
73.432
−0.234
45.662
1.00
56.14
B

ATOM
2522
OD2
ASP B
449
75.095
0.954
46.489
1.00
55.67
B

ATOM
2523
C
ASP B
449
71.733
−0.750
47.867
1.00
52.24
B

ATOM
2524
O
ASP B
449
71.541
−1.777
47.225
1.00
52.13
B

ATOM
2525
N
ILE B
450
70.864
0.260
47.883
1.00
52.28
B

ATOM
2526
CA
ILE B
450
69.607
0.199
47.135
1.00
52.23
B

ATOM
2527
CB
ILE B
450
68.729
1.477
47.359
1.00
51.25
B

ATOM
2528
CG2
ILE B
450
67.411
1.352
46.609
1.00
50.40
B

ATOM
2529
CG1
ILE B
450
68.430
1.658
48.851
1.00
50.03
B

ATOM
2530
CO1
ILE B
450
67.617
2.890
49.180
1.00
49.00
B

ATOM
2531
C
ILE B
450
69.849
0.024
45.639
1.00
52.47
B

ATOM
2532
O
ILE B
450
69.266
−0.860
45.024
1.00
52.87
B

ATOM
2533
N
LYS B
451
70.705
0.863
45.060
1.00
53.03
B

ATOM
2534
CA
LYS B
451
71.008
0.779
43.638
1.00
53.15
B

ATOM
2535
CB
LYS B
451
72.346
1.458
43.339
1.00
53.71
B

ATOM
2536
CG
LYS B
451
72.315
2.978
43.471
0.00
54.77
B

ATOM
2537
CD
LYS B
451
71.228
3.578
42.581
0.00
55.27
B

ATOM
2538
CE
LYS B
451
71.190
5.104
42.643
0.00
55.45
B

ATOM
2539
NZ
LYS B
451
72.286
5.761
41.877
0.00
55.61
B

ATOM
2540
C
LYS B
451
71.059
−0.684
43.212
1.00
53.22
B

ATOM
2541
O
LYS B
451
70.241
−1.139
42.415
1.00
51.85
B

ATOM
2542
N
LYS B
452
72.007
−1.428
43.765
1.00
54.30
B

ATOM
2543
CA
LYS B
452
72.138
−2.833
43.431
1.00
55.55
B

ATOM
2544
CB
LYS B
452
73.549
−3.321
43.756
1.00
56.49
B

ATOM
2545
CG
LYS B
452
74.596
−2.840
42.773
0.00
57.18
B

ATOM
2546
CD
LYS B
452
74.345
−3.420
41.393
0.00
57.78
B

ATOM
2547
CE
LYS B
452
75.353
−2.896
40.391
0.00
58.13
B

ATOM
2548
NZ
LYS B
452
75.066
−3.409
39.027
0.00
58.45
B

ATOM
2549
C
LYS B
452
71.113
−3.701
44.147
1.00
56.44
B

ATOM
2550
O
LYS B
452
70.797
−4.790
43.679
1.00
58.17
B

ATOM
2551
N
GLY B
453
70.594
−3.234
45.279
1.00
56.96
B

ATOM
2552
CA
GLY B
453
69.605
−4.013
46.013
1.00
57.08
B

ATOM
2553
C
GLY B
453
70.167
−5.275
46.650
1.00
57.02
B

ATOM
2554
O
GLY B
453
69.573
−6.353
46.568
1.00
56.26
B

ATOM
2555
N
CYS B
454
71.319
−5.143
47.297
1.00
57.42
B

ATOM
2556
CA
CYS B
454
71.958
−6.281
47.945
1.00
57.82
B

ATOM
2557
CB
CYS B
454
72.844
−7.024
46.937
1.00
59.05
B

ATOM
2558
SG
CYS B
454
74.118
−5.986
46.135
1.00
59.80
B

ATOM
2559
C
GY5 B
454
72.800
−5.834
49.136
1.00
57.12
B

ATOM
2560
O
CYS B
454
73.084
−4.644
49.300
1.00
57.22
B

ATOM
2561
N
CYS B
455
73.196
−6.798
49.961
1.00
55.66
B

ATOM
2562
CA
CYS B
455
74.021
−6.529
51.136
1.00
54.95
B

ATOM
2563
CB
CYS B
455
73.831
−7.667
52.140
1.00
54.92
B

ATOM
2564
SG
GY5 B
455
74.504
−7.375
53.769
1.00
58.03
B

ATOM
2565
C
GY5 B
455
75.485
−6.436
50.678
1.00
54.21
B

ATOM
2566
O
CYS B
455
76.024
−7.404
50.146
1.00
55.39
B

ATOM
2567
N
THR B
456
76.120
−5.277
50.875
1.00
52.48
B

ATOM
2568
CA
THR B
456
77.514
−5.074
50.446
1.00
50.81
B

ATOM
2569
CB
THR B
456
77.771
−3.609
49.987
1.00
50.32
B

ATOM
2570
OG1
THR B
456
77.631
−2.712
51.095
1.00
50.40
B

ATOM
2571
CG2
THR B
456
76.808
−3.217
48.894
1.00
49.71
B

ATOM
2572
C
THR B
456
78.608
−5.434
51.472
1.00
49.16
B

ATOM
2573
O
THR B
456
79.773
−5.613
51.109
1.00
49.26
B

ATOM
2574
N
HIS B
457
78.242
−5.537
52.743
1.00
46.55
B

ATOM
2575
CA
HIS B
457
79.205
−5.871
53.780
1.00
43.83
B

ATOM
2576
CB
HIS B
457
79.956
−4.615
54.229
1.00
43.71
B

ATOM
2577
CG
HIS B
457
80.731
−3.947
53.136
1.00
44.34
B

ATOM
2578
CD2
HIS B
457
80.557
−2.753
52.524
1.00
44.60
B

ATOM
2579
ND1
HIS B
457
81.832
−4.524
52.543
1.00
44.61
B

ATOM
2580
CE1
HIS B
457
82.305
−3.711
51.615
1.00
44.83
B

ATOM
2581
NE2
HIS B
457
81.550
−2.630
51.584
1.00
43.67
B

ATOM
2582
C
HIS B
457
78.512
−6.512
54.979
1.00
42.72
B

ATOM
2583
O
HIS B
457
77.307
−6.342
55.178
1.00
41.66
B

ATOM
2584
N
VAL B
458
79.275
−7.255
55.776
1.00
42.43
B

ATOM
2585
CA
VAL B
458
78.725
−7.918
56.958
1.00
40.96
B

ATOM
2586
CB
VAL B
458
78.386
−9.383
56.655
1.00
41.12
B

ATOM
2587
CG1
VAL B
458
77.331
−9.883
57.628
1.00
39.96
B

ATOM
2588
CG2
VAL B
458
77.913
−9.519
55.225
1.00
40.46
B

ATOM
2589
C
VAL B
458
79.711
−7.852
58.130
1.00
39.97
B

ATOM
2590
O
VAL B
458
80.391
−8.820
58.456
1.00
38.56
B

ATOM
2591
N
PHE B
459
79.744
−6.690
58.768
1.00
40.60
B

ATOM
2592
CA
PHE B
459
80.623
−6.413
59.892
1.00
41.18
B

ATOM
2593
CB
PHE B
459
80.675
−4.901
60.084
1.00
38.09
B

ATOM
2594
CG
PHE B
459
81.196
−4.158
58.881
1.00
36.10
B

ATOM
2595
CD1
PHE B
459
81.182
−2.765
58.850
1.00
34.95
B

ATOM
2596
CD2
PHE B
459
81.767
−4.847
57.813
1.00
34.29
B

ATOM
2597
CE1
PHE B
459
81.741
−2.055
57.773
1.00
34.55
B

ATOM
2598
CE2
PHE B
459
82.328
−4.160
56.734
1.00
35.73
B

ATOM
2599
CZ
PHE B
459
82.317
−2.755
56.713
1.00
36.03
B

ATOM
2600
C
PHE B
459
80.237
−7.104
61.209
1.00
43.45
B

ATOM
2601
O
PHE B
459
79.357
−6.630
61.921
1.00
44.50
B

ATOM
2602
N
GLU B
460
80.900
−8.216
61.538
1.00
46.24
B

ATOM
2603
CA
GLU B
460
80.608
−8.939
62.783
1.00
47.21
B

ATOM
2604
CB
GLU B
460
80.750
−10.456
62.599
1.00
46.96
B

ATOM
2605
CG
GLU B
460
79.920
−11.030
61.473
1.00
51.03
B

ATOM
2606
CD
GLU B
460
79.971
−12.553
61.386
1.00
52.17
B

ATOM
2607
OE1
GLU B
460
81.079
−13.110
61.261
1.00
54.35
B

ATOM
2608
OE2
GLU B
460
78.897
−13.194
61.428
1.00
51.82
B

ATOM
2609
C
GLU B
460
81.532
−8.491
63.909
1.00
47.31
B

ATOM
2610
O
GUI B
460
82.567
−7.863
63.674
1.00
45.71
B

ATOM
2611
N
GLY B
461
81.147
−8.835
65.134
1.00
48.17
B

ATOM
2612
CA
GLY B
461
81.928
−8.456
66.292
1.00
49.82
B

ATOM
2613
C
GLY B
461
81.102
−8.363
67.561
1.00
50.83
B

ATOM
2614
O
GLY B
461
81.379
−9.074
68.529
1.00
50.20
B

ATOM
2615
N
HIS B
462
80.086
−7.501
67.565
1.00
51.06
B

ATOM
2616
CA
HIS B
462
79.251
−7.346
68.750
1.00
51.73
B

ATOM
2617
CB
HIS B
462
78.010
−6.487
68.443
1.00
50.07
B

ATOM
2618
CG
HIS B
462
78.284
−5.011
68.421
1.00
48.90
B

ATOM
2619
CD2
HIS B
462
78.451
−4.151
67.388
1.00
48.64
B

ATOM
2620
ND1
HIS B
462
78.443
−4.264
69.568
1.00
49.43
B

ATOM
2621
CE1
HIS B
462
78.697
−3.009
69.242
1.00
50.51
B

ATOM
2622
NE2
HIS B
462
78.708
−2.914
67.925
1.00
48.70
B

ATOM
2623
C
HIS B
462
78.846
−8.707
69.315
1.00
52.82
B

ATOM
2624
O
HIS B
462
78.076
−9.459
68.704
1.00
53.62
B

ATOM
2625
N
ASN B
463
79.394
−9.013
70.490
1.00
53.69
B

ATOM
2626
CA
ASN B
463
79.140
−10.269
71.186
1.00
53.67
B

ATOM
2627
CB
ASN B
463
80.119
−10.413
72.369
0.00
53.95
B

ATOM
2628
CG
ASN B
463
81.588
−10.299
71.945
1.00
54.43
B

ATOM
2629
OD1
ASN B
463
82.173
−11.235
71.378
1.00
55.63
B

ATOM
2630
ND2
ASN B
463
82.184
−9.140
72.216
1.00
52.98
B

ATOM
2631
C
ASN B
463
77.699
−10.312
71.686
1.00
53.05
B

ATOM
2632
O
ASN B
463
77.353
−11.133
72.525
1.00
53.74
B

ATOM
2633
N
SER B
464
76.867
−9.414
71.162
1.00
53.52
B

ATOM
2634
CA
SER B
464
75.455
−9.330
71.540
1.00
51.56
B

ATOM
2635
CB
SER B
464
75.324
−8.732
72.946
1.00
52.15
B

ATOM
2636
OG
SER B
464
74.010
−8.925
73.444
1.00
54.03
B

ATOM
2637
C
SER B
464
74.645
−8.487
70.527
1.00
49.85
B

ATOM
2638
O
SER B
464
75.210
−7.852
69.622
1.00
47.81
B

ATOM
2639
N
THR B
465
73.321
−8.496
70.695
1.00
48.25
B

ATOM
2640
CA
THR B
465
72.390
−7.767
69.824
1.00
47.13
B

ATOM
2641
CB
THR B
465
70.924
−7.847
70.344
1.00
48.31
B

ATOM
2642
OG1
THR B
465
70.510
−9.214
70.418
1.00
51.43
B

ATOM
2643
CG2
THR B
465
69.971
−7.098
69.412
1.00
49.57
B

ATOM
2644
C
THR B
465
72.734
−6.292
69.669
1.00
45.19
B

ATOM
2645
O
THR B
465
73.067
−5.617
70.643
1.00
45.46
B

ATOM
2646
N
VAL B
466
72.636
−5.804
68.433
1.00
42.21
B

ATOM
2647
CA
VAL B
466
72.912
−4.406
68.125
1.00
39.22
B

ATOM
2648
CB
VAL B
466
73.293
−4.241
66.643
1.00
38.21
B

ATOM
2649
CG1
VAL B
466
73.798
−2.829
66.378
1.00
37.18
B

ATOM
2650
CG2
VAL B
466
74.354
−5.264
66.285
1.00
35.99
B

ATOM
2651
C
VAL B
466
71.626
−3.638
68.430
1.00
37.88
B

ATOM
2652
O
VAL B
466
70.655
−3.738
67.691
1.00
35.76
B

ATOM
2653
N
ARG B
467
71.623
−2.886
69.530
1.00
37.28
B

ATOM
2654
CA
ARG B
467
70.440
−2.145
69.938
1.00
36.20
B

ATOM
2655
CB
ARG B
467
70.399
−1.987
71.468
1.00
36.76
B

ATOM
2656
CG
ARG B
467
69.038
−1.513
72.012
1.00
36.98
B

ATOM
2657
CD
ARG B
467
67.945
−2.559
71.762
1.00
39.61
B

ATOM
2658
NE
ARG B
467
66.563
−2.103
71.979
1.00
40.08
B

ATOM
2659
CZ
ARG B
467
65.928
−1.213
71.220
1.00
38.58
B

ATOM
2660
NH1
ARG B
467
66.539
−0.654
70.184
1.00
36.43
B

ATOM
2661
NH2
ARG B
467
64.664
−0.913
71.476
1.00
39.24
B

ATOM
2662
C
ARG B
467
70.314
−0.773
69.283
1.00
35.21
B

ATOM
2663
O
ARG B
467
69.225
−0.213
69.247
1.00
36.67
B

ATOM
2664
N
CYS B
468
71.400
−0.222
68.758
1.00
33.04
B

ATOM
2665
CA
CYS B
468
71.304
1.088
68.127
1.00
33.09
B

ATOM
2666
CB
CYS B
468
71.069
2.167
69.186
1.00
32.72
B

ATOM
2667
SG
CYS B
468
72.414
2.394
70.339
1.00
34.24
B

ATOM
2668
C
CYS B
468
72.533
1.406
67.292
1.00
32.45
B

ATOM
2669
O
CYS B
468
73.473
0.618
67.263
1.00
33.24
B

ATOM
2670
N
LEU B
469
72.522
2.546
66.605
1.00
31.75
B

ATOM
2671
CA
LEU B
469
73.643
2.908
65.747
1.00
32.36
B

ATOM
2672
CB
LEU B
469
73.750
1.917
64.576
1.00
32.24
B

ATOM
2673
CG
LEU B
469
72.822
2.067
63.362
1.00
31.67
B

ATOM
2674
CD1
LEU B
469
73.563
2.673
62.174
1.00
33.01
B

ATOM
2675
CD2
LEU B
469
72.311
0.704
62.982
1.00
33.19
B

ATOM
2676
C
LEU B
469
73.491
4.309
65.179
1.00
32.21
B

ATOM
2677
O
LEU B
469
72.434
4.910
65.285
1.00
32.62
B

ATOM
2678
N
ASP B
470
74.552
4.833
64.581
1.00
33.12
B

ATOM
2679
CA
ASP B
470
74.481
6.149
63.972
1.00
34.33
B

ATOM
2680
CB
ASP B
470
74.431
7.223
65.055
1.00
33.47
B

ATOM
2681
CG
ASP B
470
74.098
8.585
64.501
1.00
32.01
B

ATOM
2682
OD1
ASP B
470
73.302
8.647
63.551
1.00
35.18
B

ATOM
2683
OD2
ASP B
470
74.614
9.589
65.021
1.00
29.33
B

ATOM
2684
C
ASP B
470
75.704
6.330
63.083
1.00
35.86
B

ATOM
2685
O
ASP B
470
76.619
5.509
63.124
1.00
36.56
B

ATOM
2686
N
ILE B
471
75.712
7.384
62.269
1.00
37.44
B

ATOM
2687
CA
ILE B
471
76.841
7.663
61.380
1.00
37.88
B

ATOM
2688
CB
ILE B
471
76.465
7.465
59.889
1.00
36.84
B

ATOM
2689
CG2
ILE B
471
77.698
7.683
59.005
1.00
36.56
B

ATOM
2690
CG1
ILE B
471
75.942
6.050
59.649
1.00
36.63
B

ATOM
2691
CD1
ILE B
471
75.305
5.868
58.283
1.00
35.99
B

ATOM
2692
C
ILE B
471
77.309
9.106
61.569
1.00
38.95
B

ATOM
2693
O
ILE B
471
76.493
10.013
61.769
1.00
39.67
B

ATOM
2694
N
VAL B
472
78.625
9.305
61.522
1.00
39.62
B

ATOM
2695
CA
VAL B
472
79.219
10.631
61.670
1.00
40.41
B

ATOM
2696
CB
VAL B
472
79.932
10.786
63.018
1.00
39.84
B

ATOM
2697
CG1
VAL B
472
78.967
10.468
64.158
1.00
37.97
B

ATOM
2698
CG2
VAL B
472
81.150
9.862
63.066
1.00
38.84
B

ATOM
2699
C
VAL B
472
80.255
10.802
60.579
1.00
42.22
B

ATOM
2700
O
VAL B
472
80.780
9.820
60.064
1.00
41.41
B

ATOM
2701
N
GLU B
473
80.544
12.048
60.227
1.00
44.76
B

ATOM
2702
CA
GLU B
473
81.539
12.329
59.207
1.00
48.54
B

ATOM
2703
CB
GLU B
473
80.872
12.865
57.934
1.00
49.21
B

ATOM
2704
CG
GLU B
473
81.851
13.193
56.784
1.00
51.32
B

ATOM
2705
CD
GLU B
473
81.143
13.514
55.465
1.00
51.78
B

ATOM
2706
OE1
GLU B
473
80.489
12.609
54.902
1.00
52.52
B

ATOM
2707
OE2
GLU B
473
81.232
14.670
54.996
1.00
52.59
B

ATOM
2708
C
GLU B
473
82.568
13.329
59.737
1.00
50.91
B

ATOM
2709
O
GLU B
473
82.225
14.419
60.205
1.00
50.21
B

ATOM
2710
N
TYR B
474
83.835
12.933
59.683
1.00
53.85
B

ATOM
2711
CA
TYR B
474
84.927
13.775
60.151
1.00
56.31
B

ATOM
2712
CB
TYR B
474
85.504
13.214
61.450
1.00
57.48
B

ATOM
2713
CG
TYR B
474
86.410
14.180
62.164
1.00
59.70
B

ATOM
2714
CD1
TYR B
474
85.925
15.408
62.613
1.00
60.47
B

ATOM
2715
CE1
TYR B
474
86.744
16.305
63.285
1.00
60.97
B

ATOM
2716
CD2
TYR B
474
87.749
13.870
62.402
1.00
60.68
B

ATOM
2717
CE2
TYR B
474
88.581
14.763
63.075
1.00
61.50
B

ATOM
2718
CZ
TYR B
474
88.068
15.978
63.514
1.00
61.92
B

ATOM
2719
OH
TYR B
474
88.875
16.861
64.194
1.00
63.90
B

ATOM
2720
C
TYR B
474
86.001
13.795
59.075
1.00
56.54
B

ATOM
2721
O
TYR B
474
86.293
12.768
58.460
1.00
56.18
B

ATOM
2722
N
LYS B
475
86.589
14.966
58.856
1.00
58.01
B

ATOM
2723
CA
LYS B
475
87.623
15.128
57.840
1.00
59.54
B

ATOM
2724
CB
LYS B
475
88.958
14.579
58.351
1.00
60.12
B

ATOM
2725
CG
LYS B
475
89.453
15.213
59.653
1.00
60.74
B

ATOM
2726
CD
LYS B
475
89.934
16.642
59.449
1.00
61.48
B

ATOM
2727
CE
LYS B
475
90.341
17.283
60.765
0.00
61.92
B

ATOM
2728
NZ
LYS B
475
90.797
18.687
60.568
0.00
62.37
B

ATOM
2729
C
LYS B
475
87.200
14.393
56.563
1.00
60.31
B

ATOM
2730
O
LYS B
475
87.882
13.481
56.093
1.00
61.02
B

ATOM
2731
N
ASN B
476
86.057
14.796
56.020
1.00
60.89
B

ATOM
2732
CA
ASN B
476
85.523
14.199
54.813
1.00
60.87
B

ATOM
2733
CB
ASN B
476
86.260
14.759
53.594
1.00
63.50
B

ATOM
2734
CG
ASN B
476
85.792
16.172
53.224
1.00
66.46
B

ATOM
2735
OD1
ASN B
476
84.649
16.361
52.785
1.00
68.68
B

ATOM
2736
ND2
ASN B
476
86.668
17.167
53.405
1.00
65.78
B

ATOM
2737
C
ASN B
476
85.593
12.676
54.843
1.00
60.30
B

ATOM
2738
O
ASN B
476
85.828
12.036
53.822
1.00
61.52
B

ATOM
2739
N
ILE B
477
85.379
12.095
56.018
1.00
58.81
B

ATOM
2740
CA
ILE B
477
85.395
10.642
56.155
1.00
57.40
B

ATOM
2741
CB
ILE B
477
86.720
10.148
56.780
1.00
58.27
B

ATOM
2742
CG2
ILE B
477
86.741
8.618
56.804
1.00
58.03
B

ATOM
2743
CG1
ILE B
477
87.903
10.659
55.960
0.00
58.14
B

ATOM
2744
CD1
ILE B
477
89.253
10.422
56.599
0.00
58.25
B

ATOM
2745
C
ILE B
477
84.224
10.183
57.030
1.00
55.59
B

ATOM
2746
O
ILE B
477
84.050
10.661
58.151
1.00
55.65
B

ATOM
2747
N
LYS B
478
83.423
9.257
56.515
1.00
52.92
B

ATOM
2748
CA
LYS B
478
82.281
8.760
57.264
1.00
51.69
B

ATOM
2749
CB
LYS B
478
81.106
8.479
56.322
1.00
50.04
B

ATOM
2750
CG
LYS B
478
80.324
9.717
55.899
1.00
47.12
B

ATOM
2751
CD
LYS B
478
78.972
9.329
55.324
1.00
46.70
B

ATOM
2752
CE
LYS B
478
78.106
10.553
55.048
1.00
45.79
B

ATOM
2753
NZ
LYS B
478
76.681
10.181
54.803
1.00
44.56
B

ATOM
2754
C
LYS B
478
82.591
7.509
58.090
1.00
52.07
B

ATOM
2755
O
LYS B
478
83.279
6.593
57.620
1.00
53.19
B

ATOM
2756
N
TYR B
479
82.076
7.485
59.323
1.00
51.09
B

ATOM
2757
CA
TYR B
479
82.273
6.363
60.250
1.00
49.59
B

ATOM
2758
CB
TYR B
479
83.083
6.815
61.492
1.00
50.00
B

ATOM
2759
CG
TYR B
479
84.438
7.442
61.183
1.00
49.78
B

ATOM
2760
CD1
TYR B
479
84.526
8.594
60.402
1.00
50.71
B

ATOM
2761
CE1
TYR B
479
85.754
9.165
60.062
1.00
49.52
B

ATOM
2762
CD2
TYR B
479
85.629
6.869
61.630
1.00
49.70
B

ATOM
2763
CE2
TYR B
479
86.870
7.438
61.291
1.00
49.93
B

ATOM
2764
CZ
TYR B
479
86.918
8.586
60.502
1.00
49.57
B

ATOM
2765
OH
TYR B
479
88.115
9.155
60.126
1.00
48.42
B

ATOM
2766
C
TYR B
479
80.922
5.790
60.698
1.00
48.39
B

ATOM
2767
O
TYR B
479
79.877
6.381
60.463
1.00
47.95
B

ATOM
2768
N
ILE B
480
80.954
4.629
61.337
1.00
48.14
B

ATOM
2769
CA
ILE B
480
79.742
3.986
61.828
1.00
47.98
B

ATOM
2770
CB
ILE B
480
79.470
2.669
61.090
1.00
47.82
B

ATOM
2771
CG2
ILE B
480
78.250
1.983
61.679
1.00
48.23
B

ATOM
2772
CG1
ILE B
480
79.275
2.929
59.599
1.00
47.92
B

ATOM
2773
CD1
ILE B
480
79.279
1.675
58.768
1.00
46.66
B

ATOM
2774
C
ILE B
480
79.930
3.651
63.308
1.00
48.77
B

ATOM
2775
O
ILE B
480
80.961
3.089
63.699
1.00
49.54
B

ATOM
2776
N
VAL B
481
78.931
3.982
64.124
1.00
48.38
B

ATOM
2777
CA
VAL B
481
78.975
3.718
65.566
1.00
46.50
B

ATOM
2778
CB
VAL B
481
78.917
5.041
66.382
1.00
46.27
B

ATOM
2779
CG1
VAL B
481
79.048
4.749
67.871
1.00
44.39
B

ATOM
2780
CG2
VAL B
481
80.004
5.990
65.914
1.00
45.50
B

ATOM
2781
C
VAL B
481
77.778
2.855
65.962
1.00
45.57
B

ATOM
2782
O
VAL B
481
76.634
3.281
65.823
1.00
45.94
B

ATOM
2783
N
THR B
482
78.039
1.652
66.460
1.00
43.78
B

ATOM
2784
CA
THR B
482
76.963
0.752
66.865
1.00
43.35
B

ATOM
2785
CB
THR B
482
77.050
−0.608
66.091
1.00
44.57
B

ATOM
2786
OG1
THR B
482
78.422
−0.943
65.851
1.00
44.68
B

ATOM
2787
CG2
THR B
482
76.315
−0.523
64.748
1.00
44.18
B

ATOM
2788
C
THR B
482
76.946
0.475
68.379
1.00
42.32
B

ATOM
2789
O
THR B
482
77.979
0.184
68.977
1.00
42.34
B

ATOM
2790
N
GLY B
483
75.769
0.583
68.991
1.00
41.18
B

ATOM
2791
CA
GLY B
483
75.643
0.319
70.410
1.00
42.21
B

ATOM
2792
C
GLY B
483
75.021
−1.057
70.556
1.00
43.25
B

ATOM
2793
O
GLY B
483
74.069
−1.385
69.837
1.00
44.15
B

ATOM
2794
N
SER B
484
75.536
−1.865
71.479
1.00
42.55
B

ATOM
2795
CA
SER B
484
75.018
−3.216
71.650
1.00
42.61
B

ATOM
2796
CB
SER B
484
76.015
−4.236
71.071
1.00
42.00
B

ATOM
2797
OG
SER B
484
75.676
−5.572
71.425
1.00
39.48
B

ATOM
2798
C
SER B
484
74.721
−3.560
73.099
1.00
43.04
B

ATOM
2799
O
SER B
484
75.118
−2.833
74.007
1.00
43.14
B

ATOM
2800
N
ARG B
485
73.993
−4.664
73.294
1.00
43.38
B

ATOM
2801
CA
ARG B
485
73.628
−5.182
74.618
1.00
42.66
B

ATOM
2802
CB
ARG B
485
72.532
−6.233
74.484
1.00
41.35
B

ATOM
2803
CG
ARG B
485
71.309
−5.751
73.737
1.00
41.63
B

ATOM
2804
CD
ARG B
485
70.170
−5.535
74.696
1.00
40.30
B

ATOM
2805
NE
ARG B
485
69.101
−6.499
74.462
1.00
41.39
B

ATOM
2806
CZ
ARG B
485
67.859
−6.154
74.146
1.00
42.42
B

ATOM
2807
NH1
ARG B
485
67.547
−4.874
74.029
1.00
44.59
B

ATOM
2808
NH2
ARG B
485
66.927
−7.076
73.964
1.00
41.56
B

ATOM
2809
C
ARG B
485
74.879
−5.837
75.200
1.00
43.12
B

ATOM
2810
O
ARG B
485
74.845
−6.448
76.264
1.00
42.36
B

ATOM
2811
N
ASP B
486
75.974
−5.714
74.463
1.00
43.89
B

ATOM
2812
CA
ASP B
486
77.232
−6.263
74.880
1.00
44.86
B

ATOM
2813
CB
ASP B
486
78.100
−6.572
73.646
1.00
45.64
B

ATOM
2814
CG
ASP B
486
78.713
−5.327
73.012
1.00
46.63
B

ATOM
2815
OD1
ASP B
486
78.016
−4.298
72.888
1.00
46.93
B

ATOM
2816
OD2
ASP B
486
79.897
−5.387
72.619
1.00
47.67
B

ATOM
2817
C
ASP B
486
77.887
−5.242
75.807
1.00
45.67
B

ATOM
2818
O
ASP B
486
78.967
−5.486
76.344
1.00
46.05
B

ATOM
2819
N
ASN B
487
77.207
−4.108
76.003
1.00
45.49
B

ATOM
2820
CA
ASN B
487
77.673
−3.017
76.873
1.00
44.88
B

ATOM
2821
CB
ASN B
487
78.223
−3.571
78.188
1.00
44.56
B

ATOM
2822
CG
ASN B
487
77.171
−4.261
79.021
1.00
45.76
B

ATOM
2823
OD1
ASN B
487
76.153
−4.717
78.508
1.00
47.63
B

ATOM
2824
ND2
ASN B
487
77.421
−4.359
80.317
1.00
45.91
B

ATOM
2825
C
ASN B
487
78.748
−2.146
76.242
1.00
44.09
B

ATOM
2826
O
ASN B
487
79.333
−1.306
76.920
1.00
43.58
B

ATOM
2827
N
THR B
488
79.009
−2.347
74.953
1.00
44.03
B

ATOM
2828
CA
THR B
488
80.038
−1.576
74.267
1.00
45.88
B

ATOM
2829
CB
THR B
488
81.264
−2.458
73.895
1.00
46.72
B

ATOM
2830
OG1
THR B
488
81.026
−3.098
72.633
1.00
46.03
B

ATOM
2831
CG2
THR B
488
81.498
−3.545
74.958
1.00
47.35
B

ATOM
2832
C
THR B
488
79.525
−0.958
72.971
1.00
46.36
B

ATOM
2833
O
THR B
488
78.403
−1.224
72.542
1.00
47.28
B

ATOM
2834
N
LEU B
489
80.369
−0.135
72.355
1.00
45.88
B

ATOM
2835
CA
LEU B
489
80.053
0.511
71.090
1.00
46.03
B

ATOM
2836
CB
LEU B
489
79.848
2.015
71.269
1.00
45.02
B

ATOM
2837
CG
LEU B
489
78.651
2.443
72.110
1.00
44.47
B

ATOM
2838
CD1
LEU B
489
79.093
2.732
73.518
1.00
43.21
B

ATOM
2839
CD2
LEU B
489
78.011
3.655
71.484
1.00
45.05
B

ATOM
2840
C
LEU B
489
81.186
0.293
70.102
1.00
47.37
B

ATOM
2841
O
LEU B
489
82.281
0.840
70.280
1.00
48.75
B

ATOM
2842
N
HIS B
490
80.930
−0.507
69.067
1.00
46.28
B

ATOM
2843
CA
HIS B
490
81.940
−0.766
68.040
1.00
44.43
B

ATOM
2844
CB
HIS B
490
81.680
−2.105
67.363
1.00
46.31
B

ATOM
2845
CG
HIS B
490
81.979
−3.288
68.226
1.00
48.42
B

ATOM
2846
CD2
HIS B
490
82.601
−4.456
67.944
1.00
48.94
B

ATOM
2847
ND1
HIS B
490
81.584
−3.371
69.544
1.00
48.72
B

ATOM
2848
CE1
HIS B
490
81.947
−4.542
70.035
1.00
48.74
B

ATOM
2849
NE2
HIS B
490
82.566
−5.220
69.084
1.00
49.32
B

ATOM
2850
C
HIS B
490
81.932
0.332
66.988
1.00
41.63
B

ATOM
2851
O
HIS B
490
80.873
0.804
66.598
1.00
39.88
B

ATOM
2852
N
VAL B
491
83.119
0.727
66.537
1.00
41.79
B

ATOM
2853
CA
VAL B
491
83.268
1.774
65.523
1.00
43.45
B

ATOM
2854
CB
VAL B
491
84.258
2.873
65.987
1.00
43.37
B

ATOM
2855
CG1
VAL B
491
84.565
3.838
64.843
1.00
43.14
B

ATOM
2856
CG2
VAL B
491
83.661
3.642
67.158
1.00
42.84
B

ATOM
2857
C
VAL B
491
83.773
1.199
64.201
1.00
43.94
B

ATOM
2858
O
VAL B
491
84.794
0.515
64.165
1.00
45.06
B

ATOM
2859
N
TRP B
492
83.056
1.479
63.115
1.00
44.26
B

ATOM
2860
CA
TRP B
492
83.453
0.982
61.804
1.00
43.81
B

ATOM
2861
CB
TRP B
492
82.481
−0.086
61.312
1.00
42.52
B

ATOM
2862
CG
TRP B
492
81.869
−0.922
62.399
1.00
42.97
B

ATOM
2863
CD2
TRP B
492
82.119
−2.308
62.661
1.00
43.02
B

ATOM
2864
CE2
TRP B
492
81.258
−2.696
63.721
1.00
42.64
B

ATOM
2865
CE3
TRP B
492
82.980
−3.262
62.102
1.00
42.84
B

ATOM
2866
CD1
TRP B
492
80.906
−0.535
63.289
1.00
42.27
B

ATOM
2867
NE1
TRP B
492
80.532
−1.593
64.081
1.00
42.22
B

ATOM
2868
CZ2
TRP B
492
81.231
−4.000
64.235
1.00
43.33
B

ATOM
2869
CZ3
TRP B
492
82.955
−4.562
62.613
1.00
43.23
B

ATOM
2870
CR2
TRP B
492
82.083
−4.917
63.670
1.00
43.67
B

ATOM
2871
C
TRP B
492
83.493
2.123
60.804
1.00
44.22
B

ATOM
2872
O
TRP B
492
83.061
3.233
61.094
1.00
43.90
B

ATOM
2873
N
LYS B
493
84.033
1.847
59.627
1.00
45.31
B

ATOM
2874
CA
LYS B
493
84.115
2.855
58.596
1.00
46.28
B

ATOM
2875
CB
LYS B
493
85.515
2.896
57.997
1.00
47.20
B

ATOM
2876
CG
LYS B
493
86.600
3.104
59.021
1.00
48.93
B

ATOM
2877
CD
LYS B
493
87.962
3.179
58.363
0.00
48.94
B

ATOM
2878
CE
LYS B
493
89.061
3.374
59.394
0.00
49.30
B

ATOM
2879
NZ
LYS B
493
90.390
3.550
58.746
0.00
49.52
B

ATOM
2880
C
LYS B
493
83.108
2.522
57.518
1.00
47.32
B

ATOM
2881
O
LYS B
493
82.863
1.349
57.220
1.00
47.63
B

ATOM
2882
N
LEU B
494
82.514
3.563
56.952
1.00
47.99
B

ATOM
2883
CA
LEU B
494
81.539
3.395
55.895
1.00
48.33
B

ATOM
2884
CB
LEU B
494
80.733
4.674
55.717
1.00
48.56
B

ATOM
2885
CG
LEU B
494
79.698
4.594
54.604
1.00
48.11
B

ATOM
2886
CD1
LEU B
494
78.587
3.650
55.032
1.00
47.88
B

ATOM
2887
CD2
LEU B
494
79.156
5.988
54.313
1.00
49.20
B

ATOM
2888
C
LEU B
494
82.298
3.086
54.618
1.00
48.60
B

ATOM
2889
O
LEU B
494
83.009
3.938
54.096
1.00
48.84
B

ATOM
2890
N
PRO B
495
82.170
1.856
54.109
1.00
48.59
B

ATOM
2891
CD
PRO B
495
81.485
0.713
54.729
1.00
48.94
B

ATOM
2892
CA
PRO B
495
82.850
1.438
52.887
1.00
50.38
B

ATOM
2893
CB
PRO B
495
82.345
0.014
52.693
1.00
49.35
B

ATOM
2894
CG
PRO B
495
82.201
−0.461
54.107
1.00
48.48
B

ATOM
2895
C
PRO B
495
82.561
2.342
51.693
1.00
52.37
B

ATOM
2896
O
PRO B
495
81.415
2.741
51.456
1.00
53.23
B

ATOM
2897
N
LYS B
496
83.625
2.669
50.963
1.00
53.80
B

ATOM
2898
CA
LYS B
496
83.557
3.519
49.784
1.00
54.63
B

ATOM
2899
CB
LYS B
496
84.934
4.155
49.529
1.00
55.28
B

ATOM
2900
CG
LYS B
496
86.118
3.196
49.670
1.00
54.90
B

ATOM
2901
CD
LYS B
496
87.443
3.945
49.624
1.00
54.86
B

ATOM
2902
CE
LYS B
496
88.625
3.017
49.840
0.00
55.42
B

ATOM
2903
NZ
LYS B
496
89.917
3.759
49.828
0.00
55.70
B

ATOM
2904
C
LYS B
496
83.100
2.731
48.559
1.00
54.70
B

ATOM
2905
O
LYS B
496
82.693
3.317
47.553
1.00
54.41
B

ATOM
2906
N
ASP B
508
80.076
−10.950
44.143
1.00
87.67
B

ATOM
2907
CA
ASP B
508
81.314
−10.630
44.843
1.00
87.56
B

ATOM
2908
CB
ASP B
508
82.398
−10.224
43.855
1.00
85.57
B

ATOM
2909
CG
ASP B
508
82.370
−8.742
43.565
1.00
84.40
B

ATOM
2910
OD1
ASP B
508
81.334
−8.260
43.072
1.00
83.24
B

ATOM
2911
OD2
ASP B
508
83.371
−8.056
43.855
1.00
83.59
B

ATOM
2912
C
ASP B
508
81.080
−9.451
45.781
1.00
88.88
B

ATOM
2913
O
ASP B
508
82.036
−8.810
46.225
1.00
89.19
B

ATOM
2914
N
TYR B
509
79.812
−9.155
46.066
1.00
89.80
B

ATOM
2915
CA
TYR B
509
79.455
−8.033
46.939
1.00
89.61
B

ATOM
2916
CB
TYR B
509
78.210
−7.309
46.397
1.00
90.86
B

ATOM
2917
CG
TYR B
509
78.488
−5.981
45.705
1.00
92.99
B

ATOM
2918
CD1
TYR B
509
77.576
−5.455
44.774
1.00
94.09
B

ATOM
2919
CE1
TYR B
509
77.817
−4.236
44.120
1.00
94.93
B

ATOM
2920
CD2
TYR B
509
79.653
−5.252
45.974
1.00
93.03
B

ATOM
2921
CE2
TYR B
509
79.906
−4.032
45.329
1.00
94.38
B

ATOM
2922
CZ
TYR B
509
78.986
−3.530
44.401
1.00
95.32
B

ATOM
2923
OH
TYR B
509
79.241
−2.342
43.743
1.00
95.61
B

ATOM
2924
C
TYR B
509
79.236
−8.425
48.404
1.00
88.37
B

ATOM
2925
O
TYR B
509
79.772
−7.770
49.301
1.00
89.80
B

ATOM
2926
N
PRO B
510
78.448
−9.487
48.672
1.00
86.15
B

ATOM
2927
CD
PRO B
510
77.598
−10.261
47.751
1.00
84.82
B

ATOM
2928
CA
PRO B
510
78.214
−9.897
50.067
1.00
83.98
B

ATOM
2929
CB
PRO B
510
77.276
−11.093
49.923
1.00
84.08
B

ATOM
2930
CG
PRO B
510
76.518
−10.763
48.676
1.00
84.98
B

ATOM
2931
C
PRO B
510
79.508
−10.265
50.800
1.00
81.81
B

ATOM
2932
O
PRO B
510
79.788
−11.441
51.017
1.00
81.76
B

ATOM
2933
N
LEU B
511
80.289
−9.254
51.176
1.00
79.52
B

ATOM
2934
CA
LEU B
511
81.556
−9.462
51.875
1.00
77.45
B

ATOM
2935
CB
LEU B
511
82.466
−8.246
51.701
1.00
75.86
B

ATOM
2936
CG
LEU B
511
82.803
−7.866
50.264
1.00
74.15
B

ATOM
2937
CD1
LEU B
511
83.709
−6.653
50.229
1.00
72.84
B

ATOM
2938
CD2
LEU B
511
83.463
−9.053
49.601
1.00
74.63
B

ATOM
2939
C
LEU B
511
81.323
−9.689
53.355
1.00
77.25
B

ATOM
2940
O
LEU B
511
80.682
−8.878
54.020
1.00
77.95
B

ATOM
2941
N
VAL B
512
81.856
−10.785
53.877
1.00
76.40
B

ATOM
2942
CA
VAL B
512
81.683
−11.100
55.286
1.00
75.66
B

ATOM
2943
CB
VAL B
512
81.075
−12.495
55.458
1.00
74.68
B

ATOM
2944
CG1
VAL B
512
80.748
−12.736
56.917
1.00
73.65
B

ATOM
2945
CG2
VAL B
512
79.843
−12.625
54.587
1.00
73.90
B

ATOM
2946
C
VAL B
512
83.009
−11.040
56.029
1.00
75.90
B

ATOM
2947
O
VAL B
512
84.015
−11.558
55.560
1.00
76.65
B

ATOM
2948
N
PHE B
513
83.007
−10.394
57.187
1.00
75.87
B

ATOM
2949
CA
PHE B
513
84.218
−10.275
57.986
1.00
75.67
B

ATOM
2950
CB
PHE B
513
84.669
−8.820
58.058
1.00
74.40
B

ATOM
2951
CG
PHE B
513
84.758
−8.148
56.722
1.00
74.06
B

ATOM
2952
CD1
PHE B
513
83.611
−7.885
55.981
1.00
74.40
B

ATOM
2953
CD2
PHE B
513
85.987
−7.765
56.208
1.00
74.00
B

ATOM
2954
CE1
PHE B
513
83.686
−7.246
54.752
1.00
74.32
B

ATOM
2955
CE2
PHE B
513
86.077
−7.126
54.979
1.00
73.93
B

ATOM
2956
CZ
PHE B
513
84.921
−6.865
54.249
1.00
74.51
B

ATOM
2957
C
PHE B
513
83.893
−10.780
59.378
1.00
76.17
B

ATOM
2958
O
PHE B
513
83.367
−10.041
60.207
1.00
76.66
B

ATOM
2959
N
HIS B
514
84.203
−12.043
59.631
1.00
76.08
B

ATOM
2960
CA
HIS B
514
83.906
−12.636
60.919
1.00
76.38
B

ATOM
2961
CB
HIS B
514
83.697
−14.139
60.758
1.00
78.44
B

ATOM
2962
CG
HIS B
514
84.803
−14.820
60.022
1.00
81.60
B

ATOM
2963
CD2
HIS B
514
85.579
−15.876
60.360
1.00
82.68
B

ATOM
2964
ND1
HIS B
514
85.232
−14.407
58.780
1.00
82.91
B

ATOM
2965
CE1
HIS B
514
86.228
−15.180
58.384
1.00
84.06
B

ATOM
2966
NE2
HIS B
514
86.458
−16.079
59.324
1.00
83.92
B

ATOM
2967
C
HIS B
514
84.981
−12.355
61.948
1.00
75.65
B

ATOM
2968
O
HIS B
514
84.997
−12.964
63.016
1.00
75.17
B

ATOM
2969
N
THR B
515
85.880
−11.431
61.632
1.00
75.12
B

ATOM
2970
CA
THR B
515
86.931
−11.076
62.573
1.00
75.68
B

ATOM
2971
CB
THR B
515
88.219
−11.871
62.315
1.00
75.87
B

ATOM
2972
OG1
THR B
515
87.936
−13.276
62.363
1.00
75.87
B

ATOM
2973
CG2
THR B
515
89.255
−11.538
63.375
1.00
74.95
B

ATOM
2974
C
THR B
515
87.245
−9.590
62.492
1.00
75.55
B

ATOM
2975
O
THR B
515
87.642
−9.087
61.445
1.00
75.60
B

ATOM
2976
N
PRO B
516
87.061
−8.869
63.606
1.00
75.61
B

ATOM
2977
CD
PRO B
516
86.520
−9.405
64.867
1.00
76.30
B

ATOM
2978
CA
PRO B
516
87.308
−7.430
63.722
1.00
75.87
B

ATOM
2979
CB
PRO B
516
87.056
−7.161
65.202
1.00
76.07
B

ATOM
2980
CG
PRO B
516
86.008
−8.162
65.550
1.00
76.54
B

ATOM
2981
C
PRO B
516
88.719
−7.025
63.299
1.00
76.37
B

ATOM
2982
O
PRO B
516
88.897
−6.183
62.415
1.00
75.84
B

ATOM
2983
N
GLU B
517
89.714
−7.626
63.949
1.00
76.93
B

ATOM
2984
CA
GLU B
517
91.126
−7.356
63.676
1.00
76.76
B

ATOM
2985
CB
GLU B
517
91.996
−8.320
64.492
1.00
78.63
B

ATOM
2986
CG
GLU B
517
93.496
−8.083
64.384
1.00
81.28
B

ATOM
2987
CD
GLU B
517
93.944
−6.839
65.123
1.00
82.27
B

ATOM
2988
OE1
GLU B
517
95.171
−6.593
65.192
1.00
83.01
B

ATOM
2989
OE2
GLU B
517
93.066
−6.107
65.630
1.00
82.62
B

ATOM
2990
C
GLU B
517
91.448
−7.505
62.189
1.00
75.46
B

ATOM
2991
O
GLU B
517
92.318
−6.812
61.663
1.00
75.08
B

ATOM
2992
N
GLU B
518
90.733
−8.411
61.525
1.00
73.54
B

ATOM
2993
CA
GLU B
518
90.927
−8.681
60.106
1.00
71.48
B

ATOM
2994
CB
GLU B
518
90.530
−10.124
59.793
0.00
72.44
B

ATOM
2995
CG
GLU B
518
90.797
−10.526
58.359
0.00
73.10
B

ATOM
2996
CD
GLU B
518
90.441
−11.970
58.079
0.00
73.51
B

ATOM
2997
OE1
GLU B
518
89.258
−12.335
58.243
0.00
73.72
B

ATOM
2998
OE2
GLU B
518
91.346
−12.741
57.695
0.00
73.72
B

ATOM
2999
C
GLU B
518
90.145
−7.730
59.199
1.00
70.28
B

ATOM
3000
O
GLU B
518
90.596
−7.400
58.098
1.00
69.72
B

ATOM
3001
N
ASN B
519
88.977
−7.296
59.676
1.00
68.04
B

ATOM
3002
CA
ASN B
519
88.087
−6.380
58.947
1.00
65.05
B

ATOM
3003
CB
ASN B
519
86.773
−6.224
59.718
1.00
63.79
B

ATOM
3004
CG
ASN B
519
85.805
−5.267
59.053
1.00
62.26
B

ATOM
3005
OD1
ASN B
519
84.702
−5.066
59.548
1.00
62.79
B

ATOM
3006
ND2
ASN B
519
86.204
−4.676
57.933
1.00
60.05
B

ATOM
3007
C
ASN B
519
88.716
−5.000
58.728
1.00
63.93
B

ATOM
3008
O
ASN B
519
88.842
−4.220
59.669
1.00
64.23
B

ATOM
3009
N
PRO B
520
89.090
−4.673
57.473
1.00
62.40
B

ATOM
3010
CD
PRO B
520
88.866
−5.499
56.274
1.00
61.90
B

ATOM
3011
CA
PRO B
520
89.711
−3.396
57.096
1.00
60.68
B

ATOM
3012
CB
PRO B
520
89.820
−3.497
55.577
1.00
60.59
B

ATOM
3013
CG
PRO B
520
89.895
−4.957
55.331
1.00
61.94
B

ATOM
3014
C
PRO B
520
88.906
−2.174
57.500
1.00
60.35
B

ATOM
3015
O
PRO B
520
89.403
−1.049
57.445
1.00
60.91
B

ATOM
3016
N
TYR B
521
87.657
−2.399
57.888
1.00
58.53
B

ATOM
3017
CA
TYR B
521
86.774
−1.314
58.276
1.00
56.62
B

ATOM
3018
CB
TYR B
521
85.410
−1.538
57.636
1.00
56.52
B

ATOM
3019
CG
TYR B
521
85.470
−1.631
56.133
1.00
55.43
B

ATOM
3020
CD1
TYR B
521
85.625
−0.493
55.356
1.00
53.35
B

ATOM
3021
CE1
TYR B
521
85.684
−0.568
53.980
1.00
52.25
B

ATOM
3022
CD2
TYR B
521
85.378
−2.860
55.487
1.00
55.47
B

ATOM
3023
CE2
TYR B
521
85.437
−2.946
54.109
1.00
54.04
B

ATOM
3024
CZ
TYR B
521
85.587
−1.792
53.360
1.00
53.20
B

ATOM
3025
OH
TYR B
521
85.611
−1.862
51.986
1.00
53.19
B

ATOM
3026
C
TYR B
521
86.618
−1.168
59.782
1.00
56.07
B

ATOM
3027
O
TYR B
521
86.225
−0.109
60.264
1.00
55.68
B

ATOM
3028
N
PHE B
522
86.929
−2.227
60.521
1.00
55.73
B

ATOM
3029
CA
PHE B
522
86.797
−2.207
61.969
1.00
55.79
B

ATOM
3030
CB
PHE B
522
86.993
−3.605
62.543
1.00
57.01
B

ATOM
3031
CG
PHE B
522
86.935
−3.654
64.046
1.00
59.45
B

ATOM
3032
CD1
PHE B
522
85.730
−3.458
64.719
1.00
60.43
B

ATOM
3033
CD2
PHE B
522
88.084
−3.895
64.794
1.00
59.23
B

ATOM
3034
CE1
PHE B
522
85.672
−3.505
66.119
1.00
60.50
B

ATOM
3035
CE2
PHE B
522
88.032
−3.943
66.192
1.00
59.21
B

ATOM
3036
CZ
PHE B
522
86.825
−3.749
66.856
1.00
58.74
B

ATOM
3037
C
PHE B
522
87.764
−1.267
62.668
1.00
55.79
B

ATOM
3038
O
PHE B
522
88.899
−1.643
62.962
1.00
56.44
B

ATOM
3039
N
VAL B
523
87.314
−0.048
62.951
1.00
56.06
B

ATOM
3040
CA
VAL B
523
88.155
0.924
63.650
1.00
55.15
B

ATOM
3041
CB
VAL B
523
87.445
2.271
63.817
1.00
53.14
B

ATOM
3042
CG1
VAL B
523
88.324
3.223
64.601
1.00
51.48
B

ATOM
3043
CG2
VAL B
523
87.113
2.844
62.460
1.00
53.68
B

ATOM
3044
C
VAL B
523
88.506
0.384
65.035
1.00
55.15
B

ATOM
3045
O
VAL B
523
89.675
0.140
65.331
1.00
55.89
B

ATOM
3046
N
GLY B
524
87.489
0.187
65.870
1.00
53.67
B

ATOM
3047
CA
GLY B
524
87.726
−0.325
67.205
1.00
52.15
B

ATOM
3048
C
GLY B
524
86.521
−0.286
68.127
1.00
50.48
B

ATOM
3049
O
GLY B
524
85.504
0.329
67.821
1.00
50.52
B

ATOM
3050
N
VAL B
525
86.643
−0.933
69.277
1.00
48.79
B

ATOM
3051
CA
VAL B
525
85.555
−0.975
70.232
1.00
48.07
B

ATOM
3052
CB
VAL B
525
85.354
−2.418
70.744
1.00
46.89
B

ATOM
3053
CG1
VAL B
525
86.674
−3.138
70.750
1.00
45.99
B

ATOM
3054
CG2
VAL B
525
84.732
−2.403
72.130
1.00
45.90
B

ATOM
3055
C
VAL B
525
85.800
−0.015
71.392
1.00
47.57
B

ATOM
3056
O
VAL B
525
86.938
0.175
71.805
1.00
46.79
B

ATOM
3057
N
LEU B
526
84.727
0.603
71.894
1.00
48.52
B

ATOM
3058
CA
LEU B
526
84.811
1.567
73.005
1.00
48.97
B

ATOM
3059
CB
LEU B
526
84.199
2.910
72.583
1.00
47.57
B

ATOM
3060
CG
LEU B
526
84.696
3.601
71.310
1.00
47.85
B

ATOM
3061
CD1
LEU B
526
83.713
4.694
70.936
1.00
48.90
B

ATOM
3062
CD2
LEU B
526
86.082
4.170
71.496
1.00
46.34
B

ATOM
3063
C
LEU B
526
84.078
1.047
74.257
1.00
49.07
B

ATOM
3064
O
LEU B
526
82.862
1.207
74.382
1.00
49.55
B

ATOM
3065
N
ARG B
527
84.820
0.425
75.174
1.00
48.77
B

ATOM
3066
CA
ARG B
527
84.239
−0.119
76.402
1.00
48.18
B

ATOM
3067
CB
ARG B
527
85.016
−1.349
76.877
1.00
47.43
B

ATOM
3068
CG
ARG B
527
84.725
−2.604
76.074
1.00
47.62
B

ATOM
3069
CD
ARG B
527
85.540
−3.794
76.557
1.00
45.88
B

ATOM
3070
NE
ARG B
527
86.528
−4.196
75.561
1.00
44.94
B

ATOM
3071
CZ
ARG B
527
86.259
−4.860
74.439
1.00
43.61
B

ATOM
3072
NH1
ARG B
527
85.014
−5.218
74.152
1.00
41.64
B

ATOM
3073
NH2
ARG B
527
87.246
−5.158
73.594
1.00
41.55
B

ATOM
3074
C
ARG B
527
84.214
0.907
77.515
1.00
47.73
B

ATOM
3075
O
ARG B
527
85.162
1.662
77.703
1.00
46.73
B

ATOM
3076
N
GLY B
528
83.120
0.929
78.259
1.00
48.05
B

ATOM
3077
CA
GLY B
528
83.013
1.888
79.338
1.00
49.61
B

ATOM
3078
C
GLY B
528
81.677
1.823
80.047
1.00
50.20
B

ATOM
3079
O
GLY B
528
81.510
2.397
81.120
1.00
50.44
B

ATOM
3080
N
HIS B
529
80.718
1.126
79.448
1.00
51.40
B

ATOM
3081
CA
HIS B
529
79.392
0.990
80.040
1.00
52.69
B

ATOM
3082
CB
HIS B
529
78.308
1.270
78.997
1.00
53.42
B

ATOM
3083
CG
HIS B
529
77.908
2.711
78.931
1.00
54.66
B

ATOM
3084
CD2
HIS B
529
78.036
3.710
79.836
1.00
54.96
B

ATOM
3085
ND1
HIS B
529
77.284
3.264
77.835
1.00
54.53
B

ATOM
3086
CE1
HIS B
529
77.046
4.542
78.066
1.00
54.69
B

ATOM
3087
NE2
HIS B
529
77.493
4.837
79.273
1.00
55.98
B

ATOM
3088
C
HIS B
529
79.174
−0.376
80.664
1.00
52.47
B

ATOM
3089
O
HIS B
529
79.576
−1.396
80.112
1.00
53.72
B

ATOM
3090
N
MSE B
530
78.531
−0.379
81.825
1.00
52.35
B

ATOM
3091
CA
MSE B
530
78.260
−1.603
82.568
1.00
51.79
B

ATOM
3092
CB
MSE B
530
78.325
−1.325
84.068
1.00
54.89
B

ATOM
3093
CG
MSE B
530
79.640
−0.727
84.520
1.00
59.05
B

ATOM
3094
SE
MSE B
530
81.160
−1.831
84.066
1.00
66.13
B

ATOM
3095
CE
MSE B
530
81.008
−3.077
85.560
1.00
62.20
B

ATOM
3096
C
MSE B
530
76.894
−2.153
82.241
1.00
50.13
B

ATOM
3097
O
MSE B
530
76.318
−2.887
83.036
1.00
49.11
B

ATOM
3098
N
ALA B
531
76.379
−1.800
81.070
1.00
49.94
B

ATOM
3099
CA
ALA B
531
75.055
−2.246
80.658
1.00
48.69
B

ATOM
3100
CB
ALA B
531
73.999
−1.553
81.498
1.00
48.43
B

ATOM
3101
C
ALA B
531
74.843
−1.928
79.189
1.00
47.77
B

ATOM
3102
O
ALA B
531
75.669
−1.256
78.566
1.00
48.05
B

ATOM
3103
N
SER B
532
73.731
−2.414
78.645
1.00
46.82
B.

ATOM
3104
CA
SER B
532
73.380
−2.196
77.242
1.00
45.70
B

ATOM
3105
CB
SER B
532
72.036
−2.855
76.921
1.00
45.79
B

ATOM
3106
OG
SER B
532
71.413
−2.223
75.811
1.00
44.70
B

ATOM
3107
C
SER B
532
73.306
−0.733
76.839
1.00
44.93
B

ATOM
3108
O
SER B
532
72.834
0.118
77.595
1.00
45.32
B

ATOM
3109
N
VAL B
533
73.775
−0.469
75.627
1.00
43.79
B

ATOM
3110
CA
VAL B
533
73.771
0.865
75.038
1.00
43.92
B

ATOM
3111
CB
VAL B
533
75.002
1.045
74.123
1.00
42.68
B

ATOM
3112
CG1
VAL B
533
74.893
2.335
73.336
1.00
42.48
B

ATOM
3113
CG2
VAL B
533
76.274
1.027
74.965
1.00
41.21
B

ATOM
3114
C
VAL B
533
72.480
1.013
74.215
1.00
43.88
B

ATOM
3115
O
VAL B
533
72.398
0.518
73.085
1.00
43.85
B

ATOM
3116
N
ARG B
534
71.479
1.689
74.787
1.00
42.61
B

ATOM
3117
CA
ARG B
534
70.174
1.867
74.136
1.00
40.98
B

ATOM
3118
CB
ARG B
534
69.074
2.081
75.177
1.00
41.23
B

ATOM
3119
CG
ARG B
534
67.896
1.146
75.017
1.00
42.21
B

ATOM
3120
CD
ARG B
534
66.586
1.862
74.752
1.00
43.49
B

ATOM
3121
NE
ARG B
534
66.301
2.077
73.331
1.00
45.72
B

ATOM
3122
CZ
ARG B
534
65.097
1.903
72.792
1.00
47.54
B

ATOM
3123
NH1
ARG B
534
64.093
1.508
73.563
1.00
46.82
B

ATOM
3124
NH2
ARG B
534
64.884
2.136
71.499
1.00
50.38
B

ATOM
3125
C
ARG B
534
70.104
3.015
73.162
1.00
39.36
B

ATOM
3126
O
ARG B
534
69.339
2.975
72.200
1.00
38.05
B

ATOM
3127
N
THR B
535
70.889
4.050
73.426
1.00
38.74
B

ATOM
3128
CA
THR B
535
70.869
5.217
72.566
1.00
38.25
B

ATOM
3129
CB
THR B
535
70.062
6.362
73.233
1.00
39.86
B

ATOM
3130
OG1
THR B
535
70.130
7.534
72.411
1.00
42.15
B

ATOM
3131
CG2
THR B
535
70.596
6.661
74.630
1.00
39.79
B

ATOM
3132
C
THR B
535
72.263
5.686
72.189
1.00
36.40
B

ATOM
3133
O
THR B
535
73.212
5.478
72.934
1.00
34.48
B

ATOM
3134
N
VAL B
536
72.369
6.300
71.013
1.00
36.97
B

ATOM
3135
CA
VAL B
536
73.637
6.798
70.482
1.00
38.48
B

ATOM
3136
CB
VAL B
536
74.365
5.725
69.663
1.00
39.79
B

ATOM
3137
CG1
VAL B
536
75.570
6.344
68.958
1.00
39.98
B

ATOM
3138
CG2
VAL B
536
74.807
4.588
70.561
1.00
42.70
B

ATOM
3139
C
VAL B
536
73.417
7.969
69.538
1.00
37.98
B

ATOM
3140
O
VAL B
536
72.705
7.836
68.544
1.00
39.94
B

ATOM
3141
N
SER B
537
74.037
9.105
69.832
1.00
36.75
B

ATOM
3142
CA
SER B
537
73.904
10.281
68.978
1.00
35.47
B

ATOM
3143
CB
SER B
537
72.974
11.296
69.646
1.00
36.17
B

ATOM
3144
OG
SER B
537
73.057
12.572
69.032
1.00
36.43
B

ATOM
3145
C
SER B
537
75.280
10.889
68.744
1.00
34.85
B

ATOM
3146
O
SER B
537
76.071
11.009
69.671
1.00
33.64
B

ATOM
3147
N
GLY B
538
75.575
11.258
67.507
1.00
34.65
B

ATOM
3148
CA
GLY B
538
76.875
11.836
67.243
1.00
37.80
B

ATOM
3149
C
GLY B
538
76.900
12.740
66.030
1.00
39.65
B

ATOM
3150
O
GLY B
538
75.937
12.783
65.270
1.00
39.10
B

ATOM
3151
N
HIS B
539
78.004
13.462
65.857
1.00
42.51
B

ATOM
3152
CA
HIS B
539
78.193
14.382
64.736
1.00
44.95
B

ATOM
3153
CB
HIS B
539
77.370
15.657
64.927
1.00
48.76
B

ATOM
3154
CG
HIS B
539
75.912
15.402
65.134
1.00
54.64
B

ATOM
3155
CD2
HIS B
539
75.121
15.566
66.221
1.00
55.81
B

ATOM
3156
ND1
HIS B
539
75.112
14.845
64.158
1.00
55.89
B

ATOM
3157
CE1
HIS B
539
73.891
14.677
64.635
1.00
56.19
B

ATOM
3158
NE2
HIS B
539
73.870
15.106
65.885
1.00
56.92
B

ATOM
3159
C
HIS B
539
79.665
14.753
64.709
1.00
45.08
B

ATOM
3160
O
HIS B
539
80.167
15.351
65.659
1.00
45.61
B

ATOM
3161
N
GLY B
540
80.357
14.409
63.627
1.00
44.60
B

ATOM
3162
CA
GLY B
540
81.773
14.727
63.538
1.00
44.51
B

ATOM
3163
C
GLY B
540
82.612
13.714
64.300
1.00
44.45
B

ATOM
3164
O
GLY B
540
82.356
12.519
64.188
1.00
44.43
B

ATOM
3165
N
ASN B
541
83.612
14.182
65.054
1.00
44.24
B

ATOM
3166
CA
ASN B
541
84.482
13.304
65.841
1.00
43.77
B

ATOM
3167
CB
ASN B
541
85.914
13.855
65.925
1.00
43.91
B

ATOM
3168
CG
ASN B
541
86.011
15.119
66.773
1.00
45.62
B

ATOM
3169
OD1
ASN B
541
85.399
16.139
66.449
1.00
46.42
B

ATOM
3170
ND2
ASN B
541
86.783
15.054
67.867
1.00
45.00
B

ATOM
3171
C
ASN B
541
83.949
13.134
67.257
1.00
43.38
B

ATOM
3172
O
ASN B
541
84.662
12.651
68.139
1.00
44.20
B

ATOM
3173
N
ILE B
542
82.697
13.530
67.475
1.00
41.65
B

ATOM
3174
CA
ILE B
542
82.067
13.418
68.789
1.00
40.51
B

ATOM
3175
CB
ILE B
542
81.681
14.821
69.350
1.00
41.10
B

ATOM
3176
CG2
ILE B
542
81.158
14.690
70.779
1.00
39.51
B

ATOM
3177
CG1
ILE B
542
82.893
15.753
69.325
1.00
39.00
B

ATOM
3178
CD1
ILE B
542
84.043
15.278
70.192
1.00
38.09
B

ATOM
3179
C
ILE B
542
80.795
12.560
68.744
1.00
39.78
B

ATOM
3180
O
ILE B
542
79.939
12.740
67.870
1.00
38.52
B

ATOM
3181
N
VAL B
543
80.687
11.630
69.691
1.00
38.75
B

ATOM
3182
CA
VAL B
543
79.523
10.752
69.799
1.00
38.25
B

ATOM
3183
CB
VAL B
543
79.775
9.342
69.183
1.00
37.58
B

ATOM
3184
CG1
VAL B
543
78.596
8.430
69.454
1.00
34.60
B

ATOM
3185
CG2
VAL B
543
79.995
9.459
67.678
1.00
39.64
B

ATOM
3186
C
VAL B
543
79.198
10.573
71.270
1.00
37.91
B

ATOM
3187
O
VAL B
543
80.098
10.411
72.091
1.00
40.30
B

ATOM
3188
N
VAL B
544
77.913
10.602
71.605
1.00
35.82
B

ATOM
3189
CA
VAL B
544
77.490
10.435
72.985
1.00
32.38
B

ATOM
3190
CB
VAL B
544
76.637
11.600
73.437
1.00
31.34
B

ATOM
3191
CG1
VAL B
544
76.364
11.471
74.913
1.00
31.93
B

ATOM
3192
CG2
VAL B
544
77.321
12.904
73.104
1.00
30.92
B

ATOM
3193
C
VAL B
544
76.652
9.186
73.089
1.00
31.39
B

ATOM
3194
O
VAL B
544
75.764
8.976
72.279
1.00
32.39
B

ATOM
3195
N
SER B
545
76.913
8.359
74.089
1.00
31.37
B

ATOM
3196
CA
SER B
545
76.136
7.135
74.238
1.00
32.82
B

ATOM
3197
CB
SER B
545
77.067
5.911
74.166
1.00
33.04
B

ATOM
3198
OG
SER B
545
77.887
5.768
75.328
1.00
31.94
B

ATOM
3199
C
SER B
545
75.290
7.062
75.522
1.00
34.31
B

ATOM
3200
O
SER B
545
75.663
7.595
76.576
1.00
35.23
B

ATOM
3201
N
GLY B
546
74.157
6.373
75.421
1.00
35.10
B

ATOM
3202
CA
GLY B
546
73.271
6.209
76.558
1.00
35.16
B

ATOM
3203
C
GLY B
546
73.064
4.744
76.889
1.00
35.12
B

ATOM
3204
O
GLY B
546
72.627
3.952
76.048
1.00
36.06
B

ATOM
3205
N
SER B
547
73.370
4.377
78.122
1.00
34.92
B

ATOM
3206
CA
SER B
547
73.219
2.996
78.520
1.00
35.83
B

ATOM
3207
CB
SER B
547
74.542
2.450
79.054
1.00
36.42
B

ATOM
3208
OG
SER B
547
74.376
1.145
79.580
1.00
37.41
B

ATOM
3209
C
SER B
547
72.146
2.811
79.569
1.00
36.27
B

ATOM
3210
O
SER B
547
71.561
3.776
80.043
1.00
35.05
B

ATOM
3211
N
TYR B
548
71.881
1.555
79.908
1.00
38.32
B

ATOM
3212
CA
TYR B
548
70.890
1.227
80.916
1.00
40.30
B

ATOM
3213
CB
TYR B
548
70.288
−0.146
80.629
1.00
42.68
B

ATOM
3214
CG
TYR B
548
69.117
−0.134
79.670
1.00
45.80
B

ATOM
3215
CD1
TYR B
548
68.593
1.068
79.174
1.00
47.24
B

ATOM
3216
CE1
TYR B
548
67.472
1.074
78.345
1.00
47.96
B

ATOM
3217
CD2
TYR B
548
68.494
−1.322
79.302
1.00
45.36
B

ATOM
3218
CE2
TYR B
548
67.385
−1.325
78.481
1.00
46.33
B

ATOM
3219
CZ
TYR B
548
66.873
−0.135
78.008
1.00
47.54
B

ATOM
3220
OH
TYR B
548
65.744
−0.162
77.223
1.00
49.19
B

ATOM
3221
C
TYR B
548
71.550
1.228
82.289
1.00
40.55
B

ATOM
3222
O
TYR B
548
70.898
0.990
83.305
1.00
40.82
B

ATOM
3223
N
ASP B
549
72.852
1.496
82.315
1.00
40.33
B

ATOM
3224
CA
ASP B
549
73.574
1.523
83.572
1.00
40.21
B

ATOM
3225
CB
ASP B
549
75.053
1.177
83.352
1.00
38.64
B

ATOM
3226
CG
ASP B
549
75.813
2.287
82.659
1.00
39.21
B

ATOM
3227
OD1
ASP B
549
75.195
3.348
82.399
1.00
39.42
B

ATOM
3228
OD2
ASP B
549
77.025
2.106
82.389
1.00
35.60
B

ATOM
3229
C
ASP B
549
73.437
2.905
84.207
1.00
41.08
B

ATOM
3230
O
ASP B
549
74.180
3.251
85.125
1.00
41.91
B

ATOM
3231
N
ASN B
550
72.490
3.693
83.696
1.00
41.46
B

ATOM
3232
CA
ASN B
550
72.213
5.043
84.208
1.00
41.90
B

ATOM
3233
CB
ASN B
550
71.853
4.982
85.696
1.00
42.29
B

ATOM
3234
CG
ASN B
550
70.885
3.882
86.013
1.00
42.40
B

ATOM
3235
OD1
ASN B
550
70.421
3.181
85.117
1.00
44.98
B

ATOM
3236
ND2
ASN B
550
70.563
3.723
87.289
1.00
41.54
B

ATOM
3237
C
ASN B
550
73.430
5.944
84.049
1.00
41.35
B

ATOM
3238
O
ASN B
550
73.934
6.498
85.034
1.00
41.70
B

ATOM
3239
N
THR B
551
73.891
6.101
82.816
1.00
40.29
B

ATOM
3240
CA
THR B
551
75.081
6.890
82.562
1.00
40.46
B

ATOM
3241
CB
THR B
551
76.344
6.109
83.031
1.00
40.37
B

ATOM
3242
OG1
THR B
551
76.524
6.278
84.437
1.00
40.39
B

ATOM
3243
CG2
THR B
551
77.576
6.547
82.288
1.00
39.19
B

ATOM
3244
C
THR B
551
75.230
7.167
81.080
1.00
41.05
B

ATOM
3245
O
THR B
551
74.793
6.374
80.250
1.00
41.68
B

ATOM
3246
N
LEU B
552
75.849
8.295
80.754
1.00
40.71
B

ATOM
3247
CA
LEU B
552
76.098
8.659
79.368
1.00
40.16
B

ATOM
3248
CB
LEU B
552
75.354
9.943
78.994
1.00
39.03
B

ATOM
3249
CG
LEU B
552
73.828
9.882
78.968
1.00
38.53
B

ATOM
3250
CD1
LEU B
552
73.257
10.693
80.130
1.00
38.23
B

ATOM
3251
CD2
LEU B
552
73.327
10.416
77.631
1.00
37.33
B

ATOM
3252
C
LEU B
552
77.591
8.888
79.253
1.00
40.99
B

ATOM
3253
O
LEU B
552
78.225
9.325
80.213
1.00
41.44
B

ATOM
3254
N
ILE B
553
78.160
8.579
78.093
1.00
41.46
B

ATOM
3255
CA
ILE B
553
79.589
8.788
77.879
1.00
41.69
B

ATOM
3256
CB
ILE B
553
80.366
7.452
77.679
1.00
41.75
B

ATOM
3257
CG2
ILE B
553
81.854
7.746
77.598
1.00
41.32
B

ATOM
3258
CG1
ILE B
553
80.077
6.451
78.811
1.00
42.93
B

ATOM
3259
CD1
ILE B
553
80.616
6.835
80.176
1.00
42.43
B

ATOM
3260
C
ILE B
553
79.774
9.615
76.612
1.00
41.85
B

ATOM
3261
O
ILE B
553
79.057
9.419
75.631
1.00
41.17
B

ATOM
3262
N
VAL B
554
80.724
10.547
76.638
1.00
42.67
B

ATOM
3263
CA
VAL B
554
81.022
11.371
75.467
1.00
43.83
B

ATOM
3264
CB
VAL B
554
81.216
12.850
75.832
1.00
43.23
B

ATOM
3265
CG1
VAL B
554
81.219
13.690
74.566
1.00
41.99
B

ATOM
3266
CG2
VAL B
554
80.143
13.294
76.799
1.00
43.78
B

ATOM
3267
C
VAL B
554
82.344
10.858
74.907
1.00
44.98
B

ATOM
3268
O
VAL B
554
83.391
11.108
75.489
1.00
45.12
B

ATOM
3269
N
TRP B
555
82.305
10.152
73.782
1.00
46.53
B

ATOM
3270
CA
TRP B
555
83.526
9.603
73.198
1.00
48.33
B

ATOM
3271
CB
TRP B
555
83.264
8.193
72.652
1.00
48.73
B

ATOM
3272
CG
TRP B
555
82.491
7.287
73.562
1.00
48.42
B

ATOM
3273
CD2
TRP B
555
83.024
6.244
74.390
1.00
49.05
B

ATOM
3274
CE2
TRP B
555
81.934
5.644
75.060
1.00
49.51
B

ATOM
3275
CE3
TRP B
555
84.317
5.758
74.629
1.00
48.35
B

ATOM
3276
CD1
TRP B
555
81.140
7.281
73.762
1.00
48.53
B

ATOM
3277
NE1
TRP B
555
80.797
6.296
74.661
1.00
49.31
B

ATOM
3278
CZ2
TRP B
555
82.099
4.579
75.958
1.00
49.91
B

ATOM
3279
CZ3
TRP B
555
84.481
4.698
75.523
1.00
47.73
B

ATOM
3280
CR2
TRP B
555
83.378
4.121
76.174
1.00
48.67
B

ATOM
3281
C
TRP B
555
84.119
10.455
72.074
1.00
49.09
B

ATOM
3282
O
TRP B
555
83.424
11.253
71.451
1.00
48.46
B

ATOM
3283
N
ASP B
556
85.411
10.265
71.816
1.00
51.15
B

ATOM
3284
CA
ASP B
556
86.119
10.978
70.745
1.00
52.97
B

ATOM
3285
CB
ASP B
556
87.358
11.705
71.295
1.00
53.47
B

ATOM
3286
CG
ASP B
556
88.047
12.594
70.247
1.00
53.63
B

ATOM
3287
OD1
ASP B
556
88.097
12.203
69.060
1.00
52.44
B

ATOM
3288
OD2
ASP B
556
88.552
13.683
70.615
1.00
53.83
B

ATOM
3289
C
ASP B
556
86.569
9.933
69.726
1.00
53.38
B

ATOM
3290
O
ASP B
556
87.740
9.560
69.688
1.00
54.18
B

ATOM
3291
N
VAL B
557
85.635
9.460
68.909
1.00
54.03
B

ATOM
3292
CA
VAL B
557
85.925
8.446
67.896
1.00
53.93
B

ATOM
3293
CB
VAL B
557
84.859
8.493
66.780
1.00
53.70
B

ATOM
3294
CG1
VAL B
557
85.210
7.519
65.660
1.00
54.83
B

ATOM
3295
CG2
VAL B
557
83.502
8.151
67.370
1.00
52.75
B

ATOM
3296
C
VAL B
557
87.327
8.578
67.295
1.00
54.01
B

ATOM
3297
O
VAL B
557
88.014
7.575
67.065
1.00
53.12
B

ATOM
3298
N
ALA B
558
87.752
9.817
67.063
1.00
54.57
B

ATOM
3299
CA
ALA B
558
89.071
10.087
66.497
1.00
55.27
B

ATOM
3300
CB
ALA B
558
89.249
11.577
66.286
1.00
54.44
B

ATOM
3301
C
ALA B
558
90.189
9.554
67.393
1.00
56.09
B

ATOM
3302
O
ALA B
558
91.154
8.948
66.917
1.00
57.14
B

ATOM
3303
N
GLN B
559
90.054
9.779
68.693
1.00
56.27
B

ATOM
3304
CA
GLN B
559
91.052
9.325
69.652
1.00
56.00
B

ATOM
3305
CB
GLN B
559
91.358
10.445
70.643
1.00
57.58
B

ATOM
3306
CG
GLN B
559
91.679
11.771
69.977
1.00
60.76
B

ATOM
3307
CD
GLN B
559
92.288
12.773
70.944
1.00
63.21
B

ATOM
3308
OE1
GLN B
559
91.798
12.942
72.072
1.00
63.29
B

ATOM
3309
NE2
GLN B
559
93.360
13.449
70.510
1.00
62.95
B

ATOM
3310
C
GLN B
559
90.556
8.090
70.400
1.00
54.82
B

ATOM
3311
O
CLN B
559
91.131
7.679
71.407
1.00
53.08
B

ATOM
3312
N
MSE B
560
89.486
7.500
69.885
1.00
54.44
B

ATOM
3313
CA
MSE B
560
88.881
6.322
70.487
1.00
54.74
B

ATOM
3314
CB
MSE B
560
89.450
5.055
69.844
1.00
54.65
B

ATOM
3315
CG
MSE B
560
89.124
4.912
68.360
1.00
54.73
B

ATOM
3316
SE
MSE B
560
87.225
4.845
67.991
1.00
57.83
B

ATOM
3317
CE
MSE B
560
86.882
2.985
68.379
1.00
53.96
B

ATOM
3318
C
MSE B
560
89.041
6.275
72.013
1.00
54.33
B

ATOM
3319
O
MSE B
560
89.330
5.230
72.600
1.00
54.09
B

ATOM
3320
N
LYS B
561
88.838
7.419
72.654
1.00
53.76
B

ATOM
3321
CA
LYS B
561
88.945
7.494
74.100
1.00
53.03
B

ATOM
3322
CB
LYS B
561
90.168
8.331
74.473
0.00
53.61
B

ATOM
3323
CG
LYS B
561
90.538
8.294
75.933
0.00
54.07
B

ATOM
3324
CD
LYS B
561
91.867
8.981
76.146
0.00
54.52
B

ATOM
3325
CE
LYS B
561
92.219
9.039
77.612
0.00
54.82
B

ATOM
3326
NZ
LYS B
561
91.225
9.852
78.361
0.00
55.11
B

ATOM
3327
C
LYS B
561
87.663
8.092
74.690
1.00
52.48
B

ATOM
3328
O
LYS B
561
86.786
8.548
73.952
1.00
53.43
B

ATOM
3329
N
CYS B
562
87.553
8.063
76.018
1.00
50.98
B

ATOM
3330
CA
CYS B
562
86.394
8.601
76.740
1.00
48.94
B

ATOM
3331
CB
CYS B
562
86.209
7.834
78.056
1.00
49.61
B

ATOM
3332
SG
CYS B
562
85.037
8.536
79.259
1.00
51.47
B

ATOM
3333
C
CYS B
562
86.646
10.076
77.029
1.00
47.64
B

ATOM
3334
O
CYS B
562
87.772
10.450
77.339
1.00
48.22
B

ATOM
3335
N
LEU B
563
85.616
10.915
76.909
1.00
46.12
B

ATOM
3336
CA
LEU B
563
85.771
12.346
77.175
1.00
44.98
B

ATOM
3337
CB
LEU B
563
85.149
13.187
76.051
1.00
44.96
B

ATOM
3338
CG
LEU B
563
85.894
13.179
74.706
1.00
46.73
B

ATOM
3339
CD1
LEU B
563
85.234
14.142
73.721
1.00
45.90
B

ATOM
3340
CD2
LEU B
563
87.346
13.583
74.931
1.00
45.81
B

ATOM
3341
C
LEU B
563
85.165
12.731
78.518
1.00
43.88
B

ATOM
3342
O
LEU B
563
85.823
13.367
79.348
1.00
43.62
B

ATOM
3343
N
TYR B
564
83.913
12.345
78.731
1.00
42.63
B

ATOM
3344
CA
TYR B
564
83.244
12.632
79.986
1.00
41.64
B

ATOM
3345
CB
TYR B
564
82.429
13.918
79.887
1.00
41.63
B

ATOM
3346
CG
TYR B
564
83.248
15.149
79.592
1.00
42.86
B

ATOM
3347
CD1
TYR B
564
83.298
15.684
78.308
1.00
43.33
B

ATOM
3348
CE1
TYR B
564
84.049
16.819
78.036
1.00
45.08
B

ATOM
3349
CD2
TYR B
564
83.976
15.782
80.602
1.00
43.76
B

ATOM
3350
CE2
TYR B
564
84.732
16.916
80.341
1.00
43.78
B

ATOM
3351
CZ
TYR B
564
84.760
17.426
79.060
1.00
46.05
B

ATOM
3352
OH
TYR B
564
85.492
18.558
78.795
1.00
48.58
B

ATOM
3353
C
TYR B
564
82.321
11.491
80.356
1.00
41.77
B

ATOM
3354
O
TYR B
564
81.899
10.722
79.489
1.00
42.27
B

ATOM
3355
N
ILE B
565
82.011
11.391
81.647
1.00
41.33
B

ATOM
3356
CA
ILE B
565
81.116
10.358
82.156
1.00
40.82
B

ATOM
3357
CB
ILE B
565
81.828
9.414
83.169
1.00
41.48
B

ATOM
3358
CG2
ILE B
565
80.934
8.234
83.486
1.00
40.38
B

ATOM
3359
CG1
ILE B
565
83.126
8.862
82.582
1.00
40.59
B

ATOM
3360
CD1
ILE B
565
83.907
8.008
83.571
1.00
41.08
B

ATOM
3361
C
ILE B
565
79.938
11.020
82.860
1.00
40.09
B

ATOM
3362
O
ILE B
565
79.853
11.020
84.089
1.00
41.84
B

ATOM
3363
N
LEU B
566
79.033
11.582
82.067
1.00
38.80
B

ATOM
3364
CA
LEU B
566
77.841
12.256
82.580
1.00
36.98
B

ATOM
3365
CB
LEU B
566
76.990
12.754
81.421
1.00
36.01
B

ATOM
3366
CG
LEU B
566
77.792
13.369
80.272
1.00
35.51
B

ATOM
3367
CD1
LEU B
566
76.846
13.709
79.138
1.00
34.67
B

ATOM
3368
CD2
LEU B
566
78.541
14.592
80.757
1.00
33.68
B

ATOM
3369
C
LEU B
566
77.010
11.306
83.411
1.00
36.96
B

ATOM
3370
O
LEU B
566
76.354
10.414
82.877
1.00
36.93
B

ATOM
3371
N
SER B
567
77.021
11.498
84.721
1.00
37.95
B

ATOM
3372
CA
SER B
567
76.252
10.628
85.601
1.00
39.30
B

ATOM
3373
CB
SER B
567
77.191
9.655
86.305
1.00
39.73
B

ATOM
3374
OG
SER B
567
78.238
10.359
86.940
1.00
40.54
B

ATOM
3375
C
SER B
567
75.466
11.417
86.635
1.00
39.56
B

ATOM
3376
O
SER B
567
76.007
12.260
87.344
1.00
39.82
B

ATOM
3377
N
GLY B
568
74.181
11.116
86.728
1.00
40.79
B

ATOM
3378
CA
GLY B
568
73.338
11.798
87.685
1.00
40.25
B

ATOM
3379
C
GLY B
568
71.949
11.190
87.704
1.00
40.41
B

ATOM
3380
O
GLY B
568
71.270
11.232
88.723
1.00
41.14
B

ATOM
3381
N
HIS B
569
71.513
10.636
86.575
1.00
40.65
B

ATOM
3382
CA
HIS B
569
70.197
10.017
86.508
1.00
40.96
B

ATOM
3383
CB
HIS B
569
69.865
9.568
85.077
1.00
40.33
B

ATOM
3384
CG
HIS B
569
69.511
10.695
84.151
1.00
40.43
B

ATOM
3385
CD2
HIS B
569
68.558
11.657
84.232
1.00
39.98
B

ATOM
3386
ND1
HIS B
569
70.194
10.936
82.977
1.00
40.06
B

ATOM
3387
CE1
HIS B
569
69.681
11.995
82.378
1.00
38.53
B

ATOM
3388
NE2
HIS B
569
68.687
12.452
83.118
1.00
38.90
B

ATOM
3389
C
HIS B
569
70.193
8.822
87.448
1.00
40.82
B

ATOM
3390
O
HIS B
569
71.239
8.242
87.743
1.00
39.68
B

ATOM
3391
N
THR B
570
69.007
8.464
87.915
1.00
41.28
B

ATOM
3392
CA
THR B
570
68.857
7.364
88.838
1.00
41.75
B

ATOM
3393
CB
THR B
570
68.025
7.806
90.042
1.00
42.58
B

ATOM
3394
OG1
THR B
570
68.417
9.135
90.414
1.00
41.17
B

ATOM
3395
CG2
THR B
570
68.265
6.872
91.226
1.00
44.09
B

ATOM
3396
C
THR B
570
68.201
6.169
88.168
1.00
41.63
B

ATOM
3397
O
THR B
570
67.554
5.348
88.824
1.00
42.87
B

ATOM
3398
N
ASP B
571
68.348
6.087
86.852
1.00
40.41
B

ATOM
3399
CA
ASP B
571
67.795
4.969
86.116
1.00
38.73
B

ATOM
3400
CB
ASP B
571
66.273
4.960
86.200
1.00
37.92
B

ATOM
3401
CG
ASP B
571
65.726
3.569
86.446
1.00
38.68
B

ATOM
3402
OD1
ASP B
571
66.270
2.616
85.852
1.00
37.31
B

ATOM
3403
OD2
ASP B
571
64.757
3.425
87.225
1.00
39.84
B

ATOM
3404
C
ASP B
571
68.240
4.941
84.663
1.00
38.21
B

ATOM
3405
O
ASP B
571
68.800
5.914
84.147
1.00
37.05
B

ATOM
3406
N
ARG B
572
67.994
3.806
84.016
1.00
38.06
B

ATOM
3407
CA
ARG B
572
68.365
3.602
82.620
1.00
38.61
B

ATOM
3408
CB
ARG B
572
67.761
2.282
82.102
1.00
39.79
B

ATOM
3409
CG
ARG B
572
66.409
1.944
82.735
1.00
42.08
B

ATOM
3410
CD
ARG B
572
65.669
0.771
82.066
1.00
43.20
B

ATOM
3411
NE
ARG B
572
66.402
−0.497
82.046
1.00
42.53
B

ATOM
3412
CZ
ARG B
572
65.859
−1.671
81.722
1.00
42.93
B

ATOM
3413
NH1
ARG B
572
64.573
−1.757
81.395
1.00
41.39
B

ATOM
3414
NH2
ARG B
572
66.605
−2.764
81.708
1.00
43.19
B

ATOM
3415
C
ARG B
572
67.961
4.764
81.712
1.00
37.29
B

ATOM
3416
O
ARG B
572
66.923
5.408
81.911
1.00
37.19
B

ATOM
3417
N
ILE B
573
68.803
5.022
80.716
1.00
34.87
B

ATOM
3418
CA
ILE B
573
68.589
6.088
79.739
1.00
32.30
B

ATOM
3419
CB
ILE B
573
69.914
6.783
79.417
1.00
31.72
B

ATOM
3420
CG2
ILE B
573
69.736
7.751
78.276
1.00
29.59
B

ATOM
3421
CG1
ILE B
573
70.434
7.465
80.678
1.00
33.36
B

ATOM
3422
CD1
ILE B
573
71.875
7.918
80.574
1.00
34.32
B

ATOM
3423
C
ILE B
573
68.024
5.489
78.454
1.00
30.51
B

ATOM
3424
O
ILE B
573
68.467
4.441
78.009
1.00
29.57
B

ATOM
3425
N
TYR B
574
67.039
6.148
77.862
1.00
29.36
B

ATOM
3426
CA
TYR B
574
66.453
5.629
76.638
1.00
29.00
B

ATOM
3427
CB
TYR B
574
64.944
5.478
76.795
1.00
29.33
B

ATOM
3428
CG
TYR B
574
64.557
4.229
77.537
1.00
31.08
B

ATOM
3429
CD1
TYR B
574
65.140
3.926
78.754
1.00
33.15
B

ATOM
3430
CE1
TYR B
574
64.782
2.797
79.465
1.00
33.55
B

ATOM
3431
CD2
TYR B
574
63.596
3.358
77.036
1.00
32.28
B

ATOM
3432
CE2
TYR B
574
63.225
2.209
77.748
1.00
32.21
B

ATOM
3433
CZ
TYR B
574
63.828
1.947
78.970
1.00
32.73
B

ATOM
3434
OH
TYR B
574
63.457
0.871
79.743
1.00
34.36
B

ATOM
3435
C
TYR B
574
66.745
6.452
75.393
1.00
28.82
B

ATOM
3436
O
TYR B
574
66.611
5.965
74.264
1.00
28.32
B

ATOM
3437
N
SER B
575
67.169
7.692
75.590
1.00
28.07
B

ATOM
3438
CA
SER B
575
67.431
8.564
74.461
1.00
27.39
B

ATOM
3439
CB
SER B
575
66.101
9.147
73.980
1.00
27.09
B

ATOM
3440
OC
SER B
575
66.260
9.948
72.833
1.00
23.40
B

ATOM
3441
C
SER B
575
68.368
9.690
74.832
1.00
27.21
B

ATOM
3442
O
SER B
575
68.400
10.124
75.979
1.00
29.42
B

ATOM
3443
N
THR B
576
69.131
10.169
73.859
1.00
26.42
B

ATOM
3444
CA
THR B
576
70.036
11.279
74.101
1.00
24.44
B

ATOM
3445
CB
THR B
576
71.350
10.794
74.680
1.00
23.42
B

ATOM
3446
OG1
THR B
576
72.176
11.925
74.958
1.00
22.28
B

ATOM
3447
CG2
THR B
576
72.070
9.898
73.680
1.00
23.95
B

ATOM
3448
C
THR B
576
70.314
11.995
72.782
1.00
24.66
B

ATOM
3449
O
THR B
576
70.225
11.405
71.712
1.00
23.66
B

ATOM
3450
N
ILE B
577
70.639
13.274
72.843
1.00
25.19
B

ATOM
3451
CA
ILE B
577
70.938
13.979
71.615
1.00
24.85
B

ATOM
3452
CB
ILE B
577
69.767
14.869
71.172
1.00
23.89
B

ATOM
3453
CG2
ILE B
577
70.271
15.939
70.202
1.00
21.80
B

ATOM
3454
CG1
ILE B
577
68.671
14.011
70.538
1.00
23.81
B

ATOM
3455
CD1
ILE B
577
67.376
14.750
70.224
1.00
21.31
B

ATOM
3456
C
ILE B
577
72.163
14.851
71.802
1.00
26.44
B

ATOM
3457
O
ILE B
577
72.324
15.497
72.833
1.00
26.92
B

ATOM
3458
N
TYR B
578
73.037
14.850
70.802
1.00
27.45
B

ATOM
3459
CA
TYR B
578
74.235
15.672
70.848
1.00
27.93
B

ATOM
3460
CB
TYR B
578
75.423
14.925
70.226
1.00
28.17
B

ATOM
3461
CG
TYR B
578
76.688
15.757
70.084
1.00
30.25
B

ATOM
3462
CD1
TYR B
578
77.096
16.629
71.089
1.00
28.62
B

ATOM
3463
CE1
TYR B
578
78.235
17.416
70.934
1.00
29.38
B

ATOM
3464
CD2
TYR B
578
77.464
15.690
68.922
1.00
31.91
B

ATOM
3465
CE2
TYR B
578
78.607
16.476
68.762
1.00
30.14
B

ATOM
3466
CZ
TYR B
578
78.980
17.334
69.767
1.00
29.57
B

ATOM
3467
OH
TYR B
578
80.082
18.135
69.605
1.00
31.32
B

ATOM
3468
C
TYR B
578
73.943
16.980
70.117
1.00
27.87
B

ATOM
3469
O
TYR B
578
73.789
17.017
68.897
1.00
27.54
B

ATOM
3470
N
ASP B
579
73.832
18.045
70.901
1.00
28.90
B

ATOM
3471
CA
ASP B
579
73.551
19.369
70.380
1.00
30.92
B

ATOM
3472
CB
ASP B
579
72.799
20.203
71.416
1.00
30.53
B

ATOM
3473
CG
ASP B
579
72.248
21.473
70.839
1.00
34.02
B

ATOM
3474
OD1
ASP B
579
72.845
21.995
69.868
1.00
35.60
B

ATOM
3475
OD2
ASP B
579
71.219
21.968
71.357
1.00
37.17
B

ATOM
3476
C
ASP B
579
74.871
20.026
70.035
1.00
31.94
B

ATOM
3477
O
ASP B
579
75.344
20.923
70.732
1.00
30.49
B

ATOM
3478
N
HIS B
580
75.461
19.557
68.945
1.00
34.88
B

ATOM
3479
CA
HIS B
580
76.731
20.085
68.492
1.00
38.67
B

ATOM
3480
CB
HIS B
580
77.133
19.422
67.170
1.00
40.80
B

ATOM
3481
CG
HIS B
580
76.123
19.579
66.080
1.00
44.94
B

ATOM
3482
CD2
HIS B
580
76.268
19.900
64.773
1.00
46.55
B

ATOM
3483
ND1
HIS B
580
74.778
19.359
66.276
1.00
47.64
B

ATOM
3484
CE1
HIS B
580
74.135
19.532
65.132
1.00
47.95
B

ATOM
3485
NE2
HIS B
580
75.016
19.860
64.206
1.00
46.75
B

ATOM
3486
C
HIS B
580
76.684
21.601
68.364
1.00
39.17
B

ATOM
3487
O
HIS B
580
77.545
22.297
68.907
1.00
40.61
B

ATOM
3488
N
GLU B
581
75.673
22.122
67.681
1.00
39.97
B

ATOM
3489
CA
GLU B
581
75.563
23.566
67.529
1.00
40.63
B

ATOM
3490
CB
GLU B
581
74.162
23.960
67.078
1.00
42.60
B

ATOM
3491
CG
GLU B
581
73.991
25.469
66.960
1.00
46.26
B

ATOM
3492
CD
GLU B
581
72.848
25.853
66.052
1.00
47.68
B

ATOM
3493
OE1
GLU B
581
72.857
25.407
64.880
1.00
48.93
B

ATOM
3494
OE2
GLU B
581
71.952
26.598
66.508
1.00
48.37
B

ATOM
3495
C
GLU B
581
75.871
24.279
68.836
1.00
40.05
B

ATOM
3496
O
GLU B
581
76.810
25.063
68.916
1.00
40.37
B

ATOM
3497
N
ARG B
582
75.074
23.998
69.859
1.00
39.74
B

ATOM
3498
CA
ARG B
582
75.266
24.622
71.151
1.00
38.74
B

ATOM
3499
CB
ARG B
582
73.939
24.647
71.899
1.00
37.10
B

ATOM
3500
CG
ARG B
582
73.131
25.905
71.619
1.00
37.06
B

ATOM
3501
CD
ARG B
582
71.654
25.749
71.970
1.00
35.83
B

ATOM
3502
NE
ARG B
582
70.962
24.890
71.012
1.00
35.08
B

ATOM
3503
CZ
ARG B
582
70.041
25.312
70.154
1.00
34.96
B

ATOM
3504
NH1
ARG B
582
69.691
26.591
70.130
1.00
32.75
B

ATOM
3505
NH2
ARG B
582
69.466
24.448
69.327
1.00
35.91
B

ATOM
3506
C
ARG B
582
76.356
23.971
71.989
1.00
39.71
B

ATOM
3507
O
ARG B
582
76.775
24.529
73.003
1.00
40.75
B

ATOM
3508
N
LYS B
583
76.825
22.804
71.548
1.00
40.22
B

ATOM
3509
CA
LYS B
583
77.881
22.056
72.240
1.00
39.65
B

ATOM
3510
CB
LYS B
583
79.089
22.961
72.487
1.00
41.30
B

ATOM
3511
CG
LYS B
583
80.401
22.212
72.649
1.00
43.06
B

ATOM
3512
CD
LYS B
583
80.866
21.664
71.311
1.00
46.02
B

ATOM
3513
CE
LYS B
583
81.196
22.806
70.367
1.00
46.16
B

ATOM
3514
NZ
LYS B
583
82.256
23.657
70.976
1.00
46.38
B

ATOM
3515
C
LYS B
583
77.357
21.524
73.574
1.00
38.48
B

ATOM
3516
O
LYS B
583
77.990
21.689
74.615
1.00
37.90
B

ATOM
3517
N
ARG B
584
76.202
20.871
73.526
1.00
36.80
B

ATOM
3518
CA
ARG B
584
75.575
20.343
74.728
1.00
36.72
B

ATOM
3519
CB
ARG B
584
74.436
21.278
75.140
1.00
35.58
B

ATOM
3520
CG
ARG B
584
74.930
22.481
75.916
1.00
38.40
B

ATOM
3521
CD
ARG B
584
74.542
23.820
75.330
1.00
37.40
B

ATOM
3522
NE
ARG B
584
73.160
24.166
75.635
1.00
39.31
B

ATOM
3523
CZ
ARG B
584
72.723
25.408
75.833
1.00
40.87
B

ATOM
3524
NH1
ARG B
584
73.556
26.437
75.759
1.00
40.61
B

ATOM
3525
NH2
ARG B
584
71.448
25.617
76.122
1.00
40.77
B

ATOM
3526
C
ARG B
584
75.045
18.915
74.573
1.00
36.65
B

ATOM
3527
O
ARG B
584
75.211
18.298
73.522
1.00
36.06
B

ATOM
3528
N
CYS B
585
74.443
18.372
75.631
1.00
36.04
B

ATOM
3529
CA
CYS B
585
73.847
17.043
75.534
1.00
34.78
B

ATOM
3530
CB
CYS B
585
74.778
15.936
75.994
1.00
36.01
B

ATOM
3531
SG
CYS B
585
73.955
14.322
75.938
1.00
38.57
B

ATOM
3532
C
CYS B
585
72.566
16.929
76.330
1.00
33.64
B

ATOM
3533
O
CYS B
585
72.503
17.328
77.495
1.00
33.83
B

ATOM
3534
N
ILE B
586
71.544
16.397
75.668
1.00
31.40
B

ATOM
3535
CA
ILE B
586
70.247
16.182
76.277
1.00
31.62
B

ATOM
3536
CB
ILE B
586
69.079
16.610
75.325
1.00
29.83
B

ATOM
3537
CG2
ILE B
586
67.725
16.305
75.961
1.00
25.17
B

ATOM
3538
CG1
ILE B
586
69.155
18.111
75.009
1.00
28.59
B

ATOM
3539
CD1
ILE B
586
69.610
18.438
73.588
1.00
27.79
B

ATOM
3540
C
ILE B
586
70.135
14.680
76.534
1.00
33.85
B

ATOM
3541
O
ILE B
586
70.530
13.882
75.679
1.00
35.25
B

ATOM
3542
N
SER B
587
69.634
14.291
77.712
1.00
34.29
B

ATOM
3543
CA
SER B
587
69.428
12.870
78.031
1.00
34.28
B

ATOM
3544
CB
SER B
587
70.548
12.320
78.933
1.00
33.74
B

ATOM
3545
OG
SER B
587
70.727
13.066
80.122
1.00
34.80
B

ATOM
3546
C
SER B
587
68.060
12.648
78.685
1.00
33.99
B

ATOM
3547
O
SER B
587
67.639
13.419
79.546
1.00
32.52
B

ATOM
3548
N
ALA B
588
67.355
11.615
78.233
1.00
34.19
B

ATOM
3549
CA
ALA B
588
66.054
11.286
78.793
1.00
35.71
B

ATOM
3550
CB
ALA B
588
65.006
11.155
77.699
1.00
35.73
B

ATOM
3551
C
ALA B
588
66.259
9.960
79.495
1.00
36.25
B

ATOM
3552
O
ALA B
588
66.752
9.016
78.884
1.00
37.28
B

ATOM
3553
N
SER B
589
65.929
9.906
80.786
1.00
36.81
B

ATOM
3554
CA
SER B
589
66.084
8.684
81.582
1.00
35.90
B

ATOM
3555
CB
SER B
589
66.888
8.950
82.851
1.00
34.91
B

ATOM
3556
OG
SER B
589
66.512
8.030
83.870
1.00
32.54
B

ATOM
3557
C
SER B
589
64.761
8.093
82.005
1.00
35.49
B

ATOM
3558
O
SER B
589
63.714
8.712
81.844
1.00
34.24
B

ATOM
3559
N
MSE B
590
64.826
6.883
82.550
1.00
36.42
B

ATOM
3560
CA
MSE B
590
63.648
6.188
83.040
1.00
36.64
B

ATOM
3561
CB
MSE B
590
63.949
4.702
83.249
1.00
39.18
B

ATOM
3562
CG
MSE B
590
62.896
3.948
84.060
1.00
41.10
B

ATOM
3563
SE
MSE B
590
63.091
2.012
83.900
1.00
46.30
B

ATOM
3564
CE
MSE B
590
61.725
1.645
82.565
1.00
45.20
B

ATOM
3565
C
MSE B
590
63.241
6.819
84.361
1.00
35.83
B

ATOM
3566
O
MSE B
590
62.152
6.554
84.860
1.00
35.48
B

ATOM
3567
N
ASP B
591
64.116
7.650
84.932
1.00
35.51
B

ATOM
3568
CA
ASP B
591
63.791
8.301
86.198
1.00
34.59
B

ATOM
3569
CB
ASP B
591
65.051
8.767
86.951
1.00
34.80
B

ATOM
3570
CG
ASP B
591
65.874
9.763
86.177
1.00
34.10
B

ATOM
3571
OD1
ASP B
591
65.329
10.459
85.300
1.00
35.66
B

ATOM
3572
OD2
ASP B
591
67.081
9.869
86.466
1.00
33.64
B

ATOM
3573
C
ASP B
591
62.838
9.463
85.986
1.00
33.76
B

ATOM
3574
O
ASP B
591
62.767
10.373
86.801
1.00
31.76
B

ATOM
3575
N
THR B
592
62.120
9.418
84.866
1.00
35.29
B

ATOM
3576
CA
THR B
592
61.120
10.419
84.536
1.00
34.85
B

ATOM
3577
CB
THR B
592
59.984
10.372
85.631
1.00
34.66
B

ATOM
3578
OG1
THR B
592
58.742
10.820
85.079
1.00
38.41
B

ATOM
3579
CG2
THR B
592
60.338
11.235
86.830
1.00
34.65
B

ATOM
3580
C
THR B
592
61.745
11.811
84.403
1.00
33.52
B

ATOM
3581
O
THR B
592
61.049
12.815
84.455
1.00
33.23
B

ATOM
3582
N
THR B
593
63.053
11.858
84.169
1.00
32.55
B

ATOM
3583
CA
THR B
593
63.764
13.130
84.070
1.00
32.86
B

ATOM
3584
CB
THR B
593
64.786
13.239
85.217
1.00
34.19
B

ATOM
3585
OG1
THR B
593
64.082
13.389
86.454
1.00
36.50
B

ATOM
3586
CG2
THR B
593
65.730
14.430
85.018
1.00
38.69
B

ATOM
3587
C
THR B
593
64.500
13.423
82.765
1.00
33.21
B

ATOM
3588
O
THR B
593
64.856
12.519
82.015
1.00
32.79
B

ATOM
3589
N
ILE B
594
64.714
14.705
82.488
1.00
33.30
B

ATOM
3590
CA
ILE B
594
65.471
15.103
81.309
1.00
33.34
B

ATOM
3591
CB
ILE B
594
64.612
15.829
80.249
1.00
31.46
B

ATOM
3592
CG2
ILE B
594
65.496
16.322
79.132
1.00
29.37
B

ATOM
3593
CO1
ILE B
594
63.534
14.902
79.690
1.00
32.39
B

ATOM
3594
CD1
ILE B
594
62.436
15.642
78.920
1.00
27.89
B

ATOM
3595
C
ILE B
594
66.497
16.104
81.824
1.00
35.21
B

ATOM
3596
O
ILE B
594
66.161
16.973
82.628
1.00
37.01
B

ATOM
3597
N
ARG B
595
67.749
15.977
81.402
1.00
35.67
B

ATOM
3598
CA
ARG B
595
68.735
16.947
81.834
1.00
36.60
B

ATOM
3599
CB
ARG B
595
69.447
16.482
83.104
1.00
39.57
B

ATOM
3600
CO
ARG B
595
70.237
15.219
83.020
1.00
41.84
B

ATOM
3601
CD
ARG B
595
70.672
14.865
84.428
1.00
43.91
B

ATOM
3602
NE
ARG B
595
69.554
14.397
85.240
1.00
44.22
B

ATOM
3603
CZ
ARG B
595
69.658
14.054
86.518
1.00
45.26
B

ATOM
3604
NH1
ARG B
595
70.848
14.147
87.121
1.00
44.50
B

ATOM
3605
NH2
ARG B
595
68.586
13.589
87.170
1.00
41.38
B

ATOM
3606
C
ARG B
595
69.731
17.324
80.751
1.00
36.11
B

ATOM
3607
O
ARG B
595
70.067
16.512
79.880
1.00
36.08
B

ATOM
3608
N
ILE B
596
70.173
18.579
80.791
1.00
34.47
B

ATOM
3609
CA
ILE B
596
71.116
19.084
79.807
1.00
34.38
B

ATOM
3610
CB
ILE B
596
70.662
20.479
79.263
1.00
35.15
B

ATOM
3611
CG2
ILE B
596
71.746
21.058
78.357
1.00
35.63
B

ATOM
3612
CG1
ILE B
596
69.390
20.334
78.401
1.00
36.12
B

ATOM
3613
CD1
ILE B
596
68.175
19.723
79.073
1.00
29.57
B

ATOM
3614
C
ILE B
596
72.515
19.174
80.415
1.00
32.98
B

ATOM
3615
O
ILE B
596
72.679
19.563
81.570
1.00
30.78
B

ATOM
3616
N
TRP B
597
73.520
18.795
79.638
1.00
33.10
B

ATOM
3617
CA
TRP B
597
74.892
18.821
80.124
1.00
34.71
B

ATOM
3618
CB
TRP B
597
75.493
17.404
80.117
1.00
34.39
B

ATOM
3619
CG
TRP B
597
74.577
16.341
80.645
1.00
33.10
B

ATOM
3620
CD2
TRP B
597
74.691
15.653
81.893
1.00
33.20
B

ATOM
3621
CE2
TRP B
597
73.607
14.752
81.974
1.00
33.38
B

ATOM
3622
CE3
TRP B
597
75.599
15.713
82.956
1.00
33.08
B

ATOM
3623
CD1
TRP B
597
73.463
15.842
80.035
1.00
33.47
B

ATOM
3624
NE1
TRP B
597
72.874
14.884
80.826
1.00
32.94
B

ATOM
3625
CZ2
TRP B
597
73.411
13.912
83.072
1.00
33.63
B

ATOM
3626
CZ3
TRP B
597
75.406
14.878
84.051
1.00
32.87
B

ATOM
3627
CH2
TRP B
597
74.314
13.989
84.101
1.00
33.13
B

ATOM
3628
C
TRP B
597
75.725
19.726
79.229
1.00
35.90
B

ATOM
3629
O
TRP B
597
75.455
19.837
78.028
1.00
36.19
B

ATOM
3630
N
ASP B
598
76.731
20.372
79.817
1.00
36.61
B

ATOM
3631
CA
ASP B
598
77.631
21.265
79.082
1.00
38.19
B

ATOM
3632
CB
ASP B
598
78.156
22.369
80.018
1.00
36.98
B

ATOM
3633
CG
ASP B
598
78.999
23.410
79.291
1.00
37.20
B

ATOM
3634
OD1
ASP B
598
79.604
23.089
78.240
1.00
36.53
B

ATOM
3635
OD2
ASP B
598
79.059
24.553
79.786
1.00
37.52
B

ATOM
3636
C
ASP B
598
78.806
20.426
78.574
1.00
39.00
B

ATOM
3637
O
ASP B
598
79.670
20.050
79.349
1.00
39.73
B

ATOM
3638
N
LEU B
599
78.847
20.126
77.282
1.00
40.71
B

ATOM
3639
CA
LEU B
599
79.942
19.320
76.747
1.00
42.08
B

ATOM
3640
CB
LEU B
599
79.593
18.805
75.344
1.00
40.52
B

ATOM
3641
CG
LEU B
599
78.606
17.628
75.251
1.00
40.62
B

ATOM
3642
CO1
LEU B
599
79.264
16.437
74.600
1.00
38.01
B

ATOM
3643
CO2
LEU B
599
78.096
17.258
76.638
1.00
38.10
B

ATOM
3644
C
LEU B
599
81.295
20.025
76.721
1.00
43.84
B

ATOM
3645
O
LEU B
599
82.256
19.494
76.165
1.00
44.70
B

ATOM
3646
N
GLU B
600
81.373
21.216
77.315
1.00
44.72
B

ATOM
3647
CA
GLU B
600
82.637
21.941
77.358
1.00
45.68
B

ATOM
3648
CB
GLU B
600
82.412
23.413
77.697
1.00
48.89
B

ATOM
3649
CG
GLU B
600
83.460
24.367
77.128
1.00
52.63
B

ATOM
3650
CD
GLU B
600
84.762
24.375
77.924
1.00
56.18
B

ATOM
3651
OE1
GLU B
600
84.739
24.763
79.120
1.00
58.19
B

ATOM
3652
OE2
GLU B
600
85.811
23.997
77.353
1.00
57.88
B

ATOM
3653
C
GLU B
600
83.480
21.254
78.419
1.00
45.43
B

ATOM
3654
O
GLU B
600
84.683
21.083
78.242
1.00
46.22
B

ATOM
3655
N
ASN B
605
82.844
20.855
79.518
1.00
44.31
B

ATOM
3656
CA
ASN B
605
83.543
20.124
80.568
1.00
43.89
B

ATOM
3657
CB
ASN B
605
84.285
21.077
81.520
1.00
46.09
B

ATOM
3658
CG
ASN B
605
85.808
21.121
81.248
1.00
50.14
B

ATOM
3659
OD1
ASN B
605
86.508
20.093
81.348
1.00
50.14
B

ATOM
3660
ND2
ASN B
605
86.320
22.314
80.900
1.00
49.96
B

ATOM
3661
C
ASN B
605
82.630
19.186
81.346
1.00
41.67
B

ATOM
3662
O
ASN B
605
82.756
19.054
82.554
1.00
43.82
B

ATOM
3663
N
GLY B
606
81.718
18.525
80.638
1.00
38.96
B

ATOM
3664
CA
GLY B
606
80.804
17.584
81.268
1.00
35.37
B

ATOM
3665
C
GLY B
606
80.059
18.044
82.512
1.00
34.56
B

ATOM
3666
O
GLY B
606
79.668
17.231
83.350
1.00
32.65
B

ATOM
3667
N
GLU B
607
79.846
19.348
82.622
1.00
34.50
B

ATOM
3668
CA
GLU B
607
79.147
19.921
83.757
1.00
35.96
B

ATOM
3669
CB
GLU B
607
79.616
21.367
83.976
1.00
36.06
B

ATOM
3670
CG
GLU B
607
81.114
21.618
83.763
1.00
39.20
B

ATOM
3671
CD
GLU B
607
81.468
21.981
82.321
1.00
39.57
B

ATOM
3672
OE1
GLU B
607
80.924
21.353
81.405
1.00
41.63
B

ATOM
3673
OE2
GLU B
607
82.301
22.877
82.097
1.00
38.72
B

ATOM
3674
C
GLU B
607
77.622
19.892
83.504
1.00
37.13
B

ATOM
3675
O
GLU B
607
77.157
20.165
82.391
1.00
36.86
B

ATOM
3676
N
LEU B
608
76.850
19.539
84.530
1.00
37.44
B

ATOM
3677
CA
LEU B
608
75.395
19.513
84.412
1.00
37.50
B

ATOM
3678
CB
LEU B
608
74.753
18.822
85.622
1.00
37.08
B

ATOM
3679
CG
LEU B
608
73.218
18.925
85.723
1.00
37.03
B

ATOM
3680
CD1
LEU B
608
72.593
18.036
84.658
1.00
36.12
B

ATOM
3681
CD2
LEU B
608
72.724
18.533
87.127
1.00
34.40
B

ATOM
3682
C
LEU B
608
74.912
20.962
84.339
1.00
38.65
B

ATOM
3683
O
LEU B
608
75.442
21.833
85.030
1.00
38.26
B

ATOM
3684
N
MSE B
625
73.902
21.210
83.510
1.00
39.30
B

ATOM
3685
CA
MSE B
625
73.368
22.553
83.329
1.00
39.07
B

ATOM
3686
CB
MSE B
625
73.266
22.890
81.842
1.00
41.00
B

ATOM
3687
CG
MSE B
625
74.571
23.323
81.217
1.00
43.67
B

ATOM
3688
SE
MSE B
625
74.423
23.805
79.359
1.00
50.89
B

ATOM
3689
CE
MSE B
625
73.882
25.650
79.578
1.00
45.39
B

ATOM
3690
C
MSE B
625
72.008
22.737
83.946
1.00
38.75
B

ATOM
3691
O
MSE B
625
71.803
23.605
84.795
1.00
39.63
B

ATOM
3692
N
TYR B
626
71.068
21.919
83.495
1.00
38.88
B

ATOM
3693
CA
TYR B
626
69.700
22.003
83.975
1.00
37.07
B

ATOM
3694
CB
TYR B
626
68.861
22.841
83.016
1.00
35.69
B

ATOM
3695
CG
TYR B
626
69.457
24.160
82.618
1.00
34.35
B

ATOM
3696
CD1
TYR B
626
69.560
25.199
83.535
1.00
33.06
B

ATOM
3697
CE1
TYR B
626
70.013
26.447
83.150
1.00
32.14
B

ATOM
3698
CD2
TYR B
626
69.840
24.397
81.295
1.00
34.51
B

ATOM
3699
CE2
TYR B
626
70.296
25.646
80.896
1.00
33.07
B

ATOM
3700
CZ
TYR B
626
70.373
26.671
81.833
1.00
31.79
B

ATOM
3701
OH
TYR B
626
70.753
27.933
81.446
1.00
28.57
B

ATOM
3702
C
TYR B
626
69.067
20.635
84.040
1.00
36.34
B

ATOM
3703
O
TYR B
626
69.528
19.690
83.410
1.00
37.33
B

ATOM
3704
N
THR B
627
67.992
20.560
84.809
1.00
36.28
B

ATOM
3705
CA
THR B
627
67.203
19.357
84.958
1.00
34.33
B

ATOM
3706
CB
THR B
627
67.340
18.744
86.373
1.00
32.94
B

ATOM
3707
OG1
THR B
627
68.684
18.292
86.562
1.00
30.38
B

ATOM
3708
CG2
THR B
627
66.391
17.544
86.535
1.00
32.04
B

ATOM
3709
C
THR B
627
65.764
19.808
84.719
1.00
34.24
B

ATOM
3710
O
THR B
627
65.248
20.700
85.400
1.00
33.46
B

ATOM
3711
N
LEU B
628
65.137
19.204
83.722
1.00
34.53
B

ATOM
3712
CA
LEU B
628
63.772
19.525
83.355
1.00
34.30
B

ATOM
3713
CB
LEU B
628
63.636
19.558
81.835
1.00
35.54
B

ATOM
3714
CG
LEU B
628
64.814
20.120
81.056
1.00
36.04
B

ATOM
3715
CO1
LEU B
628
64.459
20.071
79.591
1.00
37.79
B

ATOM
3716
CD2
LEU B
628
65.137
21.538
81.500
1.00
35.35
B

ATOM
3717
C
LEU B
628
62.844
18.454
83.886
1.00
32.68
B

ATOM
3718
O
LEU B
628
63.055
17.261
83.647
1.00
33.72
B

ATOM
3719
N
GLN B
629
61.805
18.882
84.582
1.00
30.62
B

ATOM
3720
CA
GLN B
629
60.849
17.949
85.127
1.00
30.70
B

ATOM
3721
CB
GLN B
629
60.774
18.082
86.647
1.00
28.58
B

ATOM
3722
CG
GLN B
629
59.867
17.050
87.257
1.00
27.57
B

ATOM
3723
CD
GLN B
629
60.402
15.655
87.063
1.00
28.68
B

ATOM
3724
OE1
GLN B
629
59.733
14.775
86.486
1.00
28.51
B

ATOM
3725
NE2
GLN B
629
61.620
15.434
87.545
1.00
27.17
B

ATOM
3726
C
GLN B
629
59.473
18.204
84.544
1.00
31.36
B

ATOM
3727
O
GLN B
629
58.677
18.958
85.104
1.00
31.90
B

ATOM
3728
N
GLY B
630
59.183
17.567
83.424
1.00
31.87
B

ATOM
3729
CA
GLY B
630
57.889
17.767
82.804
1.00
33.15
B

ATOM
3730
C
GLY B
630
57.254
16.467
82.364
1.00
33.55
B

ATOM
3731
O
GLY B
630
56.511
16.425
81.385
1.00
35.60
B

ATOM
3732
N
HIS B
631
57.553
15.400
83.092
1.00
32.53
B

ATOM
3733
CA
HIS B
631
57.023
14.083
82.784
1.00
30.78
B

ATOM
3734
CB
HIS B
631
57.943
13.368
81.792
1.00
28.27
B

ATOM
3735
CG
HIS B
631
58.054
14.052
80.466
1.00
24.31
B

ATOM
3736
CD2
HIS B
631
59.003
14.874
79.965
1.00
21.91
B

ATOM
3737
ND1
HIS B
631
57.118
13.895
79.467
1.00
26.41
B

ATOM
3738
CE1
HIS B
631
57.487
14.587
78.405
1.00
22.90
B

ATOM
3739
NE2
HIS B
631
58.629
15.190
78.681
1.00
22.42
B

ATOM
3740
C
HIS B
631
56.957
13.302
84.091
1.00
30.77
B

ATOM
3741
O
HIS B
631
57.834
13.437
84.948
1.00
30.31
B

ATOM
3742
N
THR B
632
55.916
12.489
84.239
1.00
31.40
B

ATOM
3743
CA
THR B
632
55.716
11.690
85.447
1.00
32.08
B

ATOM
3744
CB
THR B
632
54.281
11.742
85.914
1.00
32.58
B

ATOM
3745
OG1
THR B
632
53.446
11.255
84.860
1.00
33.44
B

ATOM
3746
CG2
THR B
632
53.877
13.151
86.274
1.00
31.80
B

ATOM
3747
C
THR B
632
55.990
10.233
85.152
1.00
32.55
B

ATOM
3748
O
THR B
632
55.790
9.367
86.000
1.00
33.19
B

ATOM
3749
N
ALA B
633
56.442
9.963
83.941
1.00
32.22
B

ATOM
3750
CA
ALA B
633
56.721
8.604
83.537
1.00
32.78
B

ATOM
3751
CB
ALA B
633
55.596
8.106
82.627
1.00
33.46
B

ATOM
3752
C
ALA B
633
58.048
8.649
82.786
1.00
33.18
B

ATOM
3753
O
ALA B
633
58.570
9.730
82.526
1.00
34.34
B

ATOM
3754
N
LEU B
634
58.606
7.502
82.419
1.00
32.23
B

ATOM
3755
CA
LEU B
634
59.881
7.559
81.718
1.00
31.56
B

ATOM
3756
CE
LEU B
634
60.531
6.176
81.610
1.00
32.84
B

ATOM
3757
CG
LEU B
634
59.855
5.099
80.783
1.00
33.81
B

ATOM
3758
CD1
LEU B
634
58.372
5.151
81.095
1.00
37.82
B

ATOM
3759
CD2
LEU B
634
60.122
5.300
79.304
1.00
32.77
B

ATOM
3760
C
LEU B
634
59.787
8.214
80.353
1.00
29.60
B

ATOM
3761
O
LEU B
634
58.807
8.072
79.620
1.00
27.99
B

ATOM
3762
N
VAL B
635
60.835
8.961
80.045
1.00
27.96
B

ATOM
3763
CA
VAL B
635
60.945
9.688
78.803
1.00
25.69
B

ATOM
3764
CB
VAL B
635
61.584
11.046
79.038
1.00
27.20
B

ATOM
3765
CG1
VAL B
635
61.377
11.926
77.810
1.00
28.07
B

ATOM
3766
CG2
VAL B
635
61.000
11.679
80.302
1.00
25.75
B

ATOM
3767
C
VAL B
635
61.827
8.948
77.840
1.00
23.61
B

ATOM
3768
O
VAL B
635
63.046
9.033
77.942
1.00
23.52
B

ATOM
3769
N
GLY B
636
61.219
8.248
76.891
1.00
22.88
B

ATOM
3770
CA
GLY B
636
61.998
7.488
75.928
1.00
22.35
B

ATOM
3771
C
GLY B
636
62.224
8.089
74.550
1.00
23.37
B

ATOM
3772
O
GLY B
636
62.907
7.480
73.736
1.00
24.09
B

ATOM
3773
N
LEU B
637
61.656
9.262
74.277
1.00
23.96
B

ATOM
3774
CA
LEU B
637
61.827
9.904
72.981
1.00
23.22
B

ATOM
3775
CB
LEU B
637
60.503
9.934
72.228
1.00
22.08
B

ATOM
3776
CG
LEU B
637
59.913
8.534
72.102
1.00
21.07
B

ATOM
3777
CD1
LEU B
637
58.494
8.554
71.516
1.00
18.52
B

ATOM
3778
CD2
LEU B
637
60.863
7.724
71.261
1.00
18.91
B

ATOM
3779
C
LEU B
637
62.328
11.317
73.164
1.00
25.24
B

ATOM
3780
O
LEU B
637
62.058
11.945
74.197
1.00
25.36
B

ATOM
3781
N
LEU B
638
63.048
11.797
72.142
1.00
26.06
B

ATOM
3782
CA
LEU B
638
63.635
13.147
72.077
1.00
25.52
B

ATOM
3783
CB
LEU B
638
64.907
13.258
72.926
1.00
25.76
B

ATOM
3784
CG
LEU B
638
64.857
13.321
74.453
1.00
26.07
B

ATOM
3785
CD1
LEU B
638
66.285
13.384
74.983
1.00
27.82
B

ATOM
3786
CD2
LEU B
638
64.073
14.535
74.897
1.00
25.88
B

ATOM
3787
C
LEU B
638
64.022
13.494
70.653
1.00
25.17
B

ATOM
3788
O
LEU B
638
64.529
12.644
69.919
1.00
25.44
B

ATOM
3789
N
ARG B
639
63.771
14.744
70.268
1.00
25.50
B

ATOM
3790
CA
ARG B
639
64.126
15.260
68.942
1.00
25.66
B

ATOM
3791
CB
ARG B
639
63.033
14.936
67.901
1.00
25.21
B

ATOM
3792
CG
ARG B
639
62.720
13.427
67.878
1.00
28.60
B

ATOM
3793
CD
ARG B
639
62.173
12.811
66.583
1.00
28.49
B

ATOM
3794
NE
ARG B
639
63.252
12.293
65.730
1.00
30.47
B

ATOM
3795
CZ
ARG B
639
63.131
11.295
64.851
1.00
30.02
B

ATOM
3796
NH1
ARG B
639
61.970
10.668
64.684
1.00
27.71
B

ATOM
3797
NH2
ARG B
639
64.183
10.926
64.123
1.00
32.50
B

ATOM
3798
C
ARG B
639
64.379
16.760
69.078
1.00
25.33
B

ATOM
3799
O
ARG B
639
63.738
17.442
69.877
1.00
24.41
B

ATOM
3800
N
LEU B
640
65.355
17.258
68.332
1.00
26.36
B

ATOM
3801
CA
LEU B
640
65.707
18.661
68.408
1.00
27.00
B

ATOM
3802
CB
LEU B
640
67.214
18.808
68.563
1.00
28.00
B

ATOM
3803
CG
LEU B
640
67.688
19.504
69.834
1.00
27.72
B

ATOM
3804
CD1
LEU B
640
69.188
19.757
69.737
1.00
25.31
B

ATOM
3805
CD2
LEU B
640
66.914
20.802
70.019
1.00
25.63
B

ATOM
3806
C
LEU B
640
65.263
19.432
67.189
1.00
27.04
B

ATOM
3807
O
LEU B
640
65.759
19.210
66.097
1.00
27.98
B

ATOM
3808
N
SER B
641
64.310
20.329
67.373
1.00
29.24
B

ATOM
3809
CA
SER B
641
63.828
21.138
66.271
1.00
30.57
B

ATOM
3810
CB
SER B
641
62.359
21.509
66.504
1.00
31.54
B

ATOM
3811
OG
SER B
641
62.025
22.763
65.944
1.00
30.17
B

ATOM
3812
C
SER B
641
64.718
22.366
66.277
1.00
31.05
B

ATOM
3813
O
SER B
641
65.499
22.560
67.198
1.00
32.13
B

ATOM
3814
N
ASP B
642
64.628
23.194
65.254
1.00
32.29
B

ATOM
3815
CA
ASP B
642
65.472
24.373
65.210
1.00
32.45
B

ATOM
3816
CB
ASP B
642
65.293
25.059
63.870
1.00
36.58
B

ATOM
3817
CG
ASP B
642
66.575
25.652
63.360
1.00
40.19
B

ATOM
3818
OD1
ASP B
642
67.336
24.914
62.681
1.00
41.18
B

ATOM
3819
OD2
ASP B
642
66.816
26.848
63.661
1.00
42.03
B

ATOM
3820
C
ASP B
642
65.140
25.348
66.344
1.00
31.30
B

ATOM
3821
O
ASP B
642
65.996
26.095
66.809
1.00
28.33
B

ATOM
3822
N
LYS B
643
63.876
25.332
66.759
1.00
30.65
B

ATOM
3823
CA
LYS B
643
63.373
26.190
67.818
1.00
28.54
B

ATOM
3824
CB
LYS B
643
62.069
26.888
67.407
1.00
28.11
B

ATOM
3825
CG
LYS B
643
62.141
27.807
66.210
1.00
30.60
B

ATOM
3826
CD
LYS B
643
63.196
28.902
66.364
1.00
32.54
B

ATOM
3827
CE
LYS B
643
63.332
29.736
65.070
1.00
33.58
B

ATOM
3828
NZ
LYS B
643
63.760
28.917
63.873
1.00
33.86
B

ATOM
3829
C
LYS B
643
63.047
25.391
69.077
1.00
28.15
B

ATOM
3830
O
LYS B
643
63.019
25.951
70.163
1.00
28.92
B

ATOM
3831
N
PHE B
644
62.787
24.094
68.957
1.00
26.09
B

ATOM
3832
CA
PHE B
644
62.413
23.353
70.152
1.00
24.49
B

ATOM
3833
CB
PHE B
644
60.931
22.958
70.115
1.00
21.46
B

ATOM
3834
CG
PHE B
644
60.015
24.023
69.613
1.00
20.17
B

ATOM
3835
CD1
PHE B
644
59.720
24.125
68.258
1.00
22.46
B

ATOM
3836
CD2
PHE B
644
59.404
24.896
70.493
1.00
20.58
B

ATOM
3837
CE1
PHE B
644
58.816
25.079
67.783
1.00
20.21
B

ATOM
3838
CE2
PHE B
644
58.501
25.855
70.035
1.00
20.45
B

ATOM
3839
CZ
PHE B
644
58.207
25.942
68.674
1.00
20.84
B

ATOM
3840
C
PHE B
644
63.186
22.087
70.457
1.00
25.20
B

ATOM
3841
O
PHE B
644
63.886
21.534
69.613
1.00
24.80
B

ATOM
3842
N
LEU B
645
63.054
21.649
71.701
1.00
25.69
B

ATOM
3843
CA
LEU B
645
63.630
20.396
72.151
1.00
25.88
B

ATOM
3844
CB
LEU B
645
64.547
20.586
73.359
1.00
26.05
B

ATOM
3845
CG
LEU B
645
64.777
19.327
74.233
1.00
27.77
B

ATOM
3846
CD1
LEU B
645
66.044
18.602
73.852
1.00
28.34
B

ATOM
3847
CD2
LEU B
645
64.864
19.739
75.692
1.00
29.93
B

ATOM
3848
C
LEU B
645
62.349
19.704
72.590
1.00
26.32
B

ATOM
3849
O
LEU B
645
61.743
20.096
73.591
1.00
27.97
B

ATOM
3850
N
VAL B
646
61.910
18.706
71.834
1.00
25.54
B

ATOM
3851
CA
VAL B
646
60.688
18.005
72.191
1.00
25.91
B

ATOM
3852
CB
VAL B
646
59.892
17.651
70.918
1.00
25.69
B

ATOM
3853
CG1
VAL B
646
58.554
17.036
71.293
1.00
26.37
B

ATOM
3854
CG2
VAL B
646
59.681
18.909
70.069
1.00
23.92
B

ATOM
3855
C
VAL B
646
61.003
16.734
72.986
1.00
26.60
B

ATOM
3856
O
VAL B
646
62.051
16.130
72.780
1.00
27.76
B

ATOM
3857
N
SER B
647
60.121
16.358
73.916
1.00
27.17
B

ATOM
3858
CA
SER B
647
60.281
15.130
74.711
1.00
27.29
B

ATOM
3859
CB
SER B
647
60.956
15.417
76.054
1.00
27.08
B

ATOM
3860
OG
SER B
647
60.210
16.325
76.850
1.00
27.93
B

ATOM
3861
C
SER B
647
58.905
14.512
74.942
1.00
28.49
B

ATOM
3862
O
SER B
647
57.943
15.227
75.219
1.00
29.23
B

ATOM
3863
N
ALA B
648
58.819
13.189
74.800
1.00
28.67
B

ATOM
3864
CA
ALA B
648
57.568
12.454
74.976
1.00
28.62
B

ATOM
3865
CB
ALA B
648
57.093
11.906
73.630
1.00
28.17
B

ATOM
3866
C
ALA B
648
57.760
11.306
75.972
1.00
30.51
B

ATOM
3867
O
ALA B
648
58.756
10.577
75.898
1.00
31.42
B

ATOM
3868
N
ALA B
649
56.807
11.146
76.894
1.00
30.32
B

ATOM
3869
CA
ALA B
649
56.883
10.098
77.911
1.00
30.33
B

ATOM
3870
CB
ALA B
649
56.720
10.700
79.305
1.00
29.35
B

ATOM
3871
C
ALA B
649
55.863
8.988
77.711
1.00
31.09
B

ATOM
3872
O
ALA B
649
54.995
9.080
76.850
1.00
30.54
B

ATOM
3873
N
ALA B
650
55.981
7.941
78.530
1.00
32.95
B

ATOM
3874
CA
ALA B
650
55.103
6.768
78.483
1.00
32.69
B

ATOM
3875
CB
ALA B
650
55.783
5.597
79.194
1.00
30.66
B

ATOM
3876
C
ALA B
650
53.733
7.019
79.098
1.00
33.02
B

ATOM
3877
O
ALA B
650
52.941
6.091
79.251
1.00
32.69
B

ATOM
3878
N
ASP B
651
53.471
8.270
79.463
1.00
34.34
B

ATOM
3879
CA
ASP B
651
52.200
8.661
80.063
1.00
35.15
B

ATOM
3880
CB
ASP B
651
52.456
9.528
81.287
1.00
36.84
B

ATOM
3881
CG
ASP B
651
53.402
10.663
80.993
1.00
40.07
B

ATOM
3882
OD1
ASP B
651
53.652
10.935
79.800
1.00
40.99
B

ATOM
3883
OD2
ASP B
651
53.895
11.299
81.950
1.00
43.26
B

ATOM
3884
C
ASP B
651
51.347
9.441
79.068
1.00
35.49
B

ATOM
3885
O
ASP B
651
50.282
9.948
79.418
1.00
35.89
B

ATOM
3886
N
GLY B
652
51.833
9.542
77.834
1.00
34.99
B

ATOM
3887
CA
GLY B
652
51.110
10.260
76.802
1.00
34.08
B

ATOM
3888
C
GLY B
652
51.434
11.738
76.730
1.00
34.36
B

ATOM
3889
O
GLY B
652
50.877
12.449
75.891
1.00
36.08
B

ATOM
3890
N
SER B
653
52.336
12.198
77.595
1.00
32.03
B

ATOM
3891
CA
SER B
653
52.720
13.605
77.635
1.00
30.49
B

ATOM
3892
CB
SER B
653
53.176
13.995
79.050
1.00
31.53
B

ATOM
3893
OG
SER B
653
54.387
13.358
79.428
1.00
31.63
B

ATOM
3894
C
SER B
653
53.810
13.962
76.633
1.00
29.75
B

ATOM
3895
O
SER B
653
54.702
13.165
76.361
1.00
28.99
B

ATOM
3896
N
ILE B
654
53.733
15.175
76.097
1.00
30.15
B

ATOM
3897
CA
ILE B
654
54.703
15.655
75.115
1.00
30.00
B

ATOM
3898
CB
ILE B
654
54.083
15.708
73.706
1.00
29.09
B

ATOM
3899
CG2
ILE B
654
55.115
16.144
72.686
1.00
28.47
B

ATOM
3900
CG1
ILE B
654
53.548
14.336
73.318
1.00
28.15
B

ATOM
3901
CD1
ILE B
654
52.204
14.400
72.675
1.00
30.38
B

ATOM
3902
C
ILE B
654
55.109
17.061
75.508
1.00
30.87
B

ATOM
3903
O
ILE B
654
54.285
17.974
75.484
1.00
32.52
B

ATOM
3904
N
ARG B
655
56.371
17.241
75.878
1.00
30.22
B

ATOM
3905
CA
ARG B
655
56.835
18.570
76.271
1.00
29.48
B

ATOM
3906
CB
ARG B
655
57.614
18.492
77.589
1.00
31.26
B

ATOM
3907
CG
ARG B
655
56.773
18.219
78.827
1.00
34.00
B

ATOM
3908
CD
ARG B
655
56.140
19.500
79.287
1.00
40.70
B

ATOM
3909
NE
ARG B
655
55.601
19.484
80.657
1.00
45.23
B

ATOM
3910
CZ
ARG B
655
54.582
18.735
81.075
1.00
48.41
B

ATOM
3911
NH1
ARG B
655
53.979
17.909
80.234
1.00
49.81
B

ATOM
3912
NH2
ARG B
655
54.137
18.847
82.324
1.00
50.20
B

ATOM
3913
C
ARG B
655
57.712
19.195
75.187
1.00
28.14
B

ATOM
3914
O
ARG B
655
58.462
18.501
74.500
1.00
27.90
B

ATOM
3915
N
GLY B
656
57.582
20.507
75.033
1.00
26.00
B

ATOM
3916
CA
GLY B
656
58.365
21.237
74.065
1.00
24.28
B

ATOM
3917
C
GLY B
656
59.047
22.348
74.830
1.00
24.73
B

ATOM
3918
O
GLY B
656
58.384
23.228
75.386
1.00
26.11
B

ATOM
3919
N
TRP B
657
60.373
22.296
74.883
1.00
24.11
B

ATOM
3920
CA
TRP B
657
61.163
23.294
75.601
1.00
23.50
B

ATOM
3921
CB
TRP B
657
62.139
22.602
76.550
1.00
22.75
B

ATOM
3922
CG
TRP B
657
61.579
21.381
77.189
1.00
21.95
B

ATOM
3923
CD2
TRP B
657
61.213
21.230
78.562
1.00
19.79
B

ATOM
3924
CE2
TRP B
657
60.639
19.948
78.698
1.00
20.88
B

ATOM
3925
CE3
TRP B
657
61.320
22.048
79.691
1.00
19.86
B

ATOM
3926
CD1
TRP B
657
61.231
20.213
76.566
1.00
20.79
B

ATOM
3927
NE1
TRP B
657
60.657
19.350
77.469
1.00
20.21
B

ATOM
3928
CZ2
TRP B
657
60.160
19.478
79.926
1.00
21.49
B

ATOM
3929
CZ3
TRP B
657
60.846
21.570
80.915
1.00
20.44
B

ATOM
3930
CR2
TRP B
657
60.278
20.301
81.019
1.00
20.36
B

ATOM
3931
C
TRP B
657
61.966
24.122
74.610
1.00
24.96
B

ATOM
3932
O
TRP B
657
62.262
23.673
73.498
1.00
24.34
B

ATOM
3933
N
ASP B
658
62.331
25.331
75.014
1.00
26.03
B

ATOM
3934
CA
ASP B
658
63.126
26.181
74.137
1.00
28.03
B

ATOM
3935
CB
ASP B
658
63.307
27.565
74.741
1.00
28.12
B

ATOM
3936
CG
ASP B
658
64.031
28.494
73.805
1.00
29.75
B

ATOM
3937
OD1
ASP B
658
65.264
28.356
73.641
1.00
28.58
B

ATOM
3938
OD2
ASP B
658
63.352
29.351
73.209
1.00
31.24
B

ATOM
3939
C
ASP B
658
64.498
25.538
73.961
1.00
28.55
B

ATOM
3940
O
ASP B
658
65.168
25.253
74.948
1.00
31.11
B

ATOM
3941
N
ALA B
659
64.924
25.334
72.719
1.00
27.30
B

ATOM
3942
CA
ALA B
659
66.209
24.689
72.443
1.00
28.28
B

ATOM
3943
CB
ALA B
659
66.413
24.549
70.945
1.00
26.59
B

ATOM
3944
C
ALA B
659
67.430
25.362
73.047
1.00
29.08
B

ATOM
3945
O
ALA B
659
68.518
24.784
73.067
1.00
30.37
B

ATOM
3946
N
ASN B
660
67.272
26.577
73.544
1.00
29.04
B

ATOM
3947
CA
ASN B
660
68.419
27.256
74.090
1.00
29.15
B

ATOM
3948
CB
ASN B
660
68.618
28.573
73.361
1.00
32.02
B

ATOM
3949
CG
ASN B
660
69.953
29.185
73.646
1.00
36.15
B

ATOM
3950
OD1
ASN B
660
70.999
28.600
73.342
1.00
39.04
B

ATOM
3951
ND2
ASN B
660
69.939
30.371
74.238
1.00
38.31
B

ATOM
3952
C
ASN B
660
68.334
27.474
75.582
1.00
28.96
B

ATOM
3953
O
ASN B
660
69.262
27.138
76.301
1.00
30.76
B

ATOM
3954
N
ASP B
661
67.225
28.024
76.059
1.00
28.20
B

ATOM
3955
CA
ASP B
661
67.073
28.249
77.485
1.00
26.87
B

ATOM
3956
CB
ASP B
661
66.553
29.663
77.745
1.00
29.19
B

ATOM
3957
CG
ASP B
661
65.311
29.984
76.942
1.00
30.92
B

ATOM
3958
OD1
ASP B
661
65.314
31.019
76.232
1.00
32.39
B

ATOM
3959
OD2
ASP B
661
64.334
29.209
77.023
1.00
30.85
B

ATOM
3960
C
ASP B
661
66.147
27.217
78.129
1.00
26.15
B

ATOM
3961
O
ASP B
661
66.041
27.165
79.346
1.00
28.27
B

ATOM
3962
N
TYR B
662
65.474
26.409
77.317
1.00
22.94
B

ATOM
3963
CA
TYR B
662
64.590
25.365
77.819
1.00
21.57
B

ATOM
3964
CB
TYR B
662
65.407
24.340
78.623
1.00
20.55
B

ATOM
3965
CG
TYR B
662
66.647
23.879
77.871
1.00
21.52
B

ATOM
3966
CD1
TYR B
662
67.867
24.533
78.019
1.00
19.76
B

ATOM
3967
CE1
TYR B
662
68.960
24.193
77.231
1.00
18.58
B

ATOM
3968
CD2
TYR B
662
66.567
22.861
76.919
1.00
20.80
B

ATOM
3969
CE2
TYR B
662
67.659
22.519
76.126
1.00
18.36
B

ATOM
3970
CZ
TYR B
662
68.851
23.192
76.287
1.00
18.65
B

ATOM
3971
OH
TYR B
662
69.935
22.893
75.493
1.00
18.77
B

ATOM
3972
C
TYR B
662
63.346
25.808
78.604
1.00
21.16
B

ATOM
3973
O
TYR B
662
62.835
25.068
79.443
1.00
20.62
B

ATOM
3974
N
SER B
663
62.864
27.015
78.327
1.00
21.52
B

ATOM
3975
CA
SER B
663
61.642
27.500
78.954
1.00
21.24
B

ATOM
3976
CB
SER B
663
61.458
28.993
78.699
1.00
19.14
B

ATOM
3977
OG
SER B
663
61.441
29.273
77.312
1.00
19.19
B

ATOM
3978
C
SER B
663
60.496
26.728
78.294
1.00
21.60
B

ATOM
3979
O
SER B
663
60.585
26.352
77.123
1.00
20.87
B

ATOM
3980
N
ARG B
664
59.436
26.489
79.057
1.00
22.75
B

ATOM
3981
CA
ARG B
664
58.267
25.755
78.592
1.00
23.75
B

ATOM
3982
CB
ARG B
664
57.317
25.544
79.764
1.00
26.18
B

ATOM
3983
CG
ARG B
664
58.032
24.928
80.948
1.00
33.56
B

ATOM
3984
CD
ARG B
664
57.130
24.061
81.812
1.00
39.29
B

ATOM
3985
NE
ARG B
664
57.925
23.331
82.801
1.00
43.83
B

ATOM
3986
CZ
ARG B
664
57.446
22.404
83.625
1.00
47.40
B

ATOM
3987
NH1
ARG B
664
56.158
22.076
83.594
1.00
48.81
B

ATOM
3988
NH2
ARG B
664
58.265
21.796
84.474
1.00
48.40
B

ATOM
3989
C
ARG B
664
57.540
26.436
77.433
1.00
23.79
B

ATOM
3990
O
ARG B
664
56.829
27.420
77.632
1.00
23.72
B

ATOM
3991
N
LYS B
665
57.702
25.886
76.228
1.00
23.87
B

ATOM
3992
CA
LYS B
665
57.091
26.453
75.021
1.00
24.18
B

ATOM
3993
CB
LYS B
665
58.099
26.400
73.869
1.00
25.26
B

ATOM
3994
CG
LYS B
665
59.088
27.551
73.869
1.00
26.13
B

ATOM
3995
CD
LYS B
665
58.423
28.779
73.292
1.00
31.91
B

ATOM
3996
CE
LYS B
665
59.389
29.964
73.126
1.00
34.51
B

ATOM
3997
NZ
LYS B
665
59.804
30.608
74.426
1.00
40.98
B

ATOM
3998
C
LYS B
665
55.760
25.844
74.588
1.00
22.25
B

ATOM
3999
O
LYS B
665
54.943
26.514
73.956
1.00
21.84
B

ATOM
4000
N
PHE B
666
55.555
24.574
74.917
1.00
22.07
B

ATOM
4001
CA
PHE B
666
54.308
23.875
74.604
1.00
22.00
B

ATOM
4002
CB
PHE B
666
54.109
23.776
73.076
1.00
21.53
B

ATOM
4003
CG
PHE B
666
55.017
22.786
72.373
1.00
21.45
B

ATOM
4004
CD1
PHE B
666
54.744
21.420
72.408
1.00
21.12
B

ATOM
4005
CD2
PHE B
666
56.134
23.218
71.664
1.00
20.63
B

ATOM
4006
CE1
PHE B
666
55.562
20.506
71.758
1.00
17.08
B

ATOM
4007
CE2
PHE B
666
56.951
22.303
71.015
1.00
19.89
B

ATOM
4008
CZ
PHE B
666
56.659
20.947
71.066
1.00
17.19
B

ATOM
4009
C
PHE B
666
54.272
22.494
75.288
1.00
22.61
B

ATOM
4010
O
PHE B
666
55.323
21.938
75.618
1.00
24.01
B

ATOM
4011
N
SER B
667
53.068
21.973
75.538
1.00
22.74
B

ATOM
4012
CA
SER B
667
52.891
20.674
76.200
1.00
23.29
B

ATOM
4013
CB
SER B
667
52.827
20.831
77.717
1.00
22.23
B

ATOM
4014
OG
SER B
667
51.487
20.937
78.145
1.00
23.02
B

ATOM
4015
C
SER B
667
51.596
20.014
75.737
1.00
24.06
B

ATOM
4016
O
SER B
667
50.525
20.635
75.772
1.00
23.18
B

ATOM
4017
N
TYR B
668
51.703
18.751
75.321
1.00
24.19
B

ATOM
4018
CA
TYR B
668
50.554
17.999
74.834
1.00
24.45
B

ATOM
4019
CB
TYR B
668
50.633
17.810
73.324
1.00
24.25
B

ATOM
4020
CG
TYR B
668
50.638
19.089
72.543
1.00
24.38
B

ATOM
4021
CD1
TYR B
668
51.752
19.452
71.785
1.00
23.71
B

ATOM
4022
CE1
TYR B
668
51.759
20.610
71.024
1.00
24.24
B

ATOM
4023
CD2
TYR B
668
49.519
19.924
72.528
1.00
24.84
B

ATOM
4024
CE2
TYR B
668
49.514
21.091
71.770
1.00
25.84
B

ATOM
4025
CZ
TYR B
668
50.643
21.426
71.017
1.00
26.29
B

ATOM
4026
OH
TYR B
668
50.656
22.572
70.263
1.00
27.29
B

ATOM
4027
C
TYR B
668
50.391
16.634
75.462
1.00
23.76
B

ATOM
4028
O
TYR B
668
51.364
15.944
75.751
1.00
23.84
B

ATOM
4029
N
HIS B
669
49.144
16.223
75.612
1.00
24.21
B

ATOM
4030
CA
HIS B
669
48.864
14.948
76.225
1.00
26.26
B

ATOM
4031
CB
HIS B
669
48.329
15.214
77.623
1.00
27.79
B

ATOM
4032
CG
HIS B
669
48.682
14.159
78.607
1.00
30.20
B

ATOM
4033
CD2
HIS B
669
48.174
12.921
78.797
1.00
32.47
B

ATOM
4034
ND1
HIS B
669
49.695
14.309
79.526
1.00
30.16
B

ATOM
4035
CE1
HIS B
669
49.796
13.205
80.244
1.00
31.69
B

ATOM
4036
NE2
HIS B
669
48.884
12.347
79.822
1.00
32.65
B

ATOM
4037
C
HIS B
669
47.836
14.157
75.421
1.00
25.01
B

ATOM
4038
O
HIS B
669
46.743
14.662
75.167
1.00
25.41
B

ATOM
4039
N
HIS B
670
48.163
12.936
75.003
1.00
24.99
B

ATOM
4040
CA
HIS B
670
47.173
12.152
74.262
1.00
26.67
B

ATOM
4041
CB
HIS B
670
47.788
10.894
73.644
1.00
26.67
B

ATOM
4042
CG
HIS B
670
48.526
11.149
72.367
1.00
28.25
B

ATOM
4043
CD2
HIS B
670
49.149
12.266
71.911
1.00
27.02
B

ATOM
4044
ND1
HIS B
670
48.704
10.187
71.399
1.00
28.10
B

ATOM
4045
CE1
HIS B
670
49.404
10.697
70.398
1.00
27.39
B

ATOM
4046
NE2
HIS B
670
49.685
11.955
70.687
1.00
25.82
B

ATOM
4047
C
HIS B
670
46.033
11.766
75.198
1.00
28.34
B

ATOM
4048
O
HIS B
670
46.255
11.292
76.320
1.00
28.98
B

ATOM
4049
N
THR B
671
44.812
11.970
74.717
1.00
29.18
B

ATOM
4050
CA
THR B
671
43.597
11.706
75.479
1.00
29.09
B

ATOM
4051
CB
THR B
671
42.363
11.963
74.600
1.00
28.97
B

ATOM
4052
OG1
THR B
671
42.582
11.400
73.299
1.00
29.48
B

ATOM
4053
CG2
THR B
671
42.108
13.457
74.470
1.00
28.78
B

ATOM
4054
C
THR B
671
43.434
10.341
76.127
1.00
27.51
B

ATOM
4055
O
THR B
671
42.911
10.245
77.234
1.00
26.92
B

ATOM
4056
N
ASN B
672
43.857
9.291
75.436
1.00
28.14
B

ATOM
4057
CA
ASN B
672
43.715
7.936
75.961
1.00
29.14
B

ATOM
4058
CB
ASN B
672
43.528
6.943
74.808
1.00
30.07
B

ATOM
4059
CG
ASN B
672
44.774
6.802
73.954
1.00
31.70
B

ATOM
4060
OD1
ASN B
672
45.721
7.592
74.082
1.00
32.55
B

ATOM
4061
ND2
ASN B
672
44.779
5.803
73.067
1.00
30.68
B

ATOM
4062
C
ASN B
672
44.911
7.538
76.819
1.00
27.80
B

ATOM
4063
O
ASN B
672
45.184
6.354
77.040
1.00
25.74
B

ATOM
4064
N
LEU B
673
45.624
8.554
77.283
1.00
27.49
B

ATOM
4065
CA
LEU B
673
46.771
8.370
78.152
1.00
28.57
B

ATOM
4066
CB
LEU B
673
46.267
8.132
79.581
1.00
26.43
B

ATOM
4067
CG
LEU B
673
45.295
9.183
80.132
1.00
27.88
B

ATOM
4068
CD1
LEU B
673
44.949
8.826
81.572
1.00
28.51
B

ATOM
4069
CD2
LEU B
673
45.898
10.581
80.067
1.00
26.47
B

ATOM
4070
C
LEU B
673
47.711
7.243
77.727
1.00
28.78
B

ATOM
4071
O
LEU B
673
48.353
6.613
78.560
1.00
28.06
B

ATOM
4072
N
SER B
674
47.805
6.992
76.431
1.00
29.36
B

ATOM
4073
CA
SER B
674
48.676
5.926
75.960
1.00
29.70
B

ATOM
4074
CB
SER B
674
48.207
5.459
74.585
1.00
32.41
B

ATOM
4075
OG
SER B
674
46.859
5.039
74.652
1.00
35.35
B

ATOM
4076
G
SER B
674
50.140
6.353
75.892
1.00
27.54
B

ATOM
4077
O
SER B
674
50.438
7.522
75.678
1.00
27.24
B

ATOM
4078
N
ALA B
675
51.053
5.407
76.074
1.00
25.24
B

ATOM
4079
CA
ALA B
675
52.455
5.748
76.006
1.00
24.53
B

ATOM
4080
CB
ALA B
675
53.304
4.573
76.393
1.00
25.14
B

ATOM
4081
C
ALA B
675
52.793
6.179
74.589
1.00
25.51
B

ATOM
4082
O
ALA B
675
52.484
5.472
73.610
1.00
26.90
B

ATOM
4083
N
ILE B
676
53.429
7.340
74.485
1.00
23.80
B

ATOM
4084
CA
ILE B
676
53.824
7.880
73.200
1.00
23.18
B

ATOM
4085
CB
ILE B
676
54.457
9.276
73.354
1.00
22.28
B

ATOM
4086
CG2
ILE B
676
54.960
9.749
71.999
1.00
26.37
B

ATOM
4087
CG1
ILE B
676
53.437
10.265
73.913
1.00
20.36
B

ATOM
4088
CD1
ILE B
676
52.158
10.388
73.112
1.00
19.30
B

ATOM
4089
C
ILE B
676
54.835
6.966
72.505
1.00
23.03
B

ATOM
4090
O
ILE B
676
55.939
6.770
73.005
1.00
22.66
B

ATOM
4091
N
THR B
677
54.454
6.432
71.344
1.00
23.91
B

ATOM
4092
CA
THR B
677
55.310
5.536
70.554
1.00
24.45
B

ATOM
4093
CB
THR B
677
54.495
4.625
69.663
1.00
21.85
B

ATOM
4094
OG1
THR B
677
53.512
3.966
70.447
1.00
21.96
B

ATOM
4095
CG2
THR B
677
55.406
3.590
69.020
1.00
27.86
B

ATOM
4096
C
THR B
677
56.291
6.286
69.642
1.00
26.36
B

ATOM
4097
O
THR B
677
57.469
5.953
69.580
1.00
26.98
B

ATOM
4098
N
THR B
678
55.787
7.252
68.884
1.00
27.47
B

ATOM
4099
CA
THR B
678
56.647
8.070
68.046
1.00
28.85
B

ATOM
4100
CB
THR B
678
56.939
7.483
66.615
1.00
31.08
B

ATOM
4101
OG1
THR B
678
55.731
7.007
66.003
1.00
33.29
B

ATOM
4102
CG2
THR B
678
57.971
6.378
66.698
1.00
35.12
B

ATOM
4103
C
THR B
678
56.070
9.447
67.831
1.00
28.29
B

ATOM
4104
O
THR B
678
54.934
9.742
68.215
1.00
29.19
B

ATOM
4105
N
PHE B
679
56.889
10.273
67.194
1.00
27.12
B

ATOM
4106
CA
PHE B
679
56.552
11.621
66.835
1.00
24.71
B

ATOM
4107
CB
PHE B
679
56.246
12.453
68.085
1.00
25.37
B

ATOM
4108
CG
PHE B
679
57.481
12.945
68.829
1.00
24.77
B

ATOM
4109
CD1
PHE B
679
58.206
14.061
68.374
1.00
21.98
B

ATOM
4110
CD2
PHE B
679
57.916
12.293
69.990
1.00
24.36
B

ATOM
4111
CE1
PHE B
679
59.331
14.509
69.063
1.00
19.92
B

ATOM
4112
CE2
PHE B
679
59.032
12.736
70.671
1.00
22.18
B

ATOM
4113
CZ
PHE B
679
59.739
13.845
70.207
1.00
21.94
B

ATOM
4114
C
PHE B
679
57.762
12.174
66.095
1.00
24.89
B

ATOM
4115
O
PHE B
679
58.894
11.669
66.212
1.00
21.91
B

ATOM
4116
N
TYR B
680
57.504
13.231
65.338
1.00
25.98
B

ATOM
4117
CA
TYR B
680
58.516
13.918
64.557
1.00
25.00
B

ATOM
4118
CB
TYR B
680
58.418
13.438
63.104
1.00
23.81
B

ATOM
4119
CG
TYR B
680
59.668
13.711
62.317
1.00
27.68
B

ATOM
4120
CD1
TYR B
680
60.795
12.881
62.429
1.00
26.50
B

ATOM
4121
CE1
TYR B
680
62.003
13.232
61.812
1.00
27.92
B

ATOM
4122
CD2
TYR B
680
59.780
14.881
61.559
1.00
28.23
B

ATOM
4123
CE2
TYR B
680
60.971
15.237
60.949
1.00
27.91
B

ATOM
4124
CZ
TYR B
680
62.074
14.427
61.080
1.00
28.40
B

ATOM
4125
OH
TYR B
680
63.253
14.870
60.531
1.00
31.86
B

ATOM
4126
C
TYR B
680
58.122
15.405
64.735
1.00
23.73
B

ATOM
4127
O
TYR B
680
56.975
15.684
65.090
1.00
22.88
B

ATOM
4128
N
VAL B
681
59.053
16.340
64.520
1.00
23.01
B

ATOM
4129
CA
VAL B
681
58.785
17.781
64.698
1.00
21.87
B

ATOM
4130
CB
VAL B
681
59.211
18.315
66.071
1.00
20.14
B

ATOM
4131
CG1
VAL B
681
58.030
18.505
66.979
1.00
18.83
B

ATOM
4132
CG2
VAL B
681
60.254
17.397
66.641
1.00
21.44
B

ATOM
4133
C
VAL B
681
59.556
18.695
63.781
1.00
21.58
B

ATOM
4134
O
VAL B
681
60.694
18.427
63.399
1.00
19.29
B

ATOM
4135
N
SER 8
682
58.928
19.818
63.480
1.00
21.27
B

ATOM
4136
CA
SER B
682
59.554
20.864
62.685
1.00
20.48
B

ATOM
4137
CB
SER B
682
58.923
20.956
61.300
1.00
19.96
B

ATOM
4138
OG
SER B
682
57.535
21.230
61.396
1.00
20.38
B

ATOM
4139
C
SER B
682
59.174
22.065
63.518
1.00
20.44
B

ATOM
4140
O
SER B
682
58.332
21.944
64.407
1.00
22.67
B

ATOM
4141
N
ASP B
683
59.797
23.207
63.275
1.00
19.98
B

ATOM
4142
CA
ASP B
683
59.441
24.394
64.036
1.00
19.73
B

ATOM
4143
CB
ASP B
683
60.212
25.638
63.547
1.00
20.26
B

ATOM
4144
CG
ASP B
683
61.708
25.650
63.959
1.00
21.54
B

ATOM
4145
OD1
ASP B
683
62.132
24.891
64.860
1.00
19.41
B

ATOM
4146
OD2
ASP B
683
62.468
26.460
63.377
1.00
22.23
B

ATOM
4147
C
ASP B
683
57.936
24.665
63.889
1.00
18.98
B

ATOM
4148
O
ASP B
683
57.351
25.254
64.782
1.00
19.03
B

ATOM
4149
N
ASN B
684
57.311
24.214
62.800
1.00
18.67
B

ATOM
4150
CA
ASN B
684
55.888
24.482
62.579
1.00
20.77
B

ATOM
4151
CB
ASN B
684
55.644
24.891
61.136
1.00
20.60
B

ATOM
4152
CG
ASN B
684
56.303
26.196
60.780
1.00
23.83
B

ATOM
4153
OD1
ASN B
684
56.062
27.233
61.419
1.00
24.57
B

ATOM
4154
ND2
ASN B
684
57.134
26.165
59.741
1.00
23.71
B

ATOM
4155
C
ASN B
684
54.874
23.392
62.886
1.00
22.90
B

ATOM
4156
O
ASN B
684
53.687
23.690
63.077
1.00
22.24
B

ATOM
4157
N
ILE B
685
55.327
22.140
62.890
1.00
23.24
B

ATOM
4158
CA
ILE B
685
54.449
20.997
63.118
1.00
20.82
B

ATOM
4159
CB
ILE B
685
54.156
20.257
61.778
1.00
19.24
B

ATOM
4160
CG2
ILE B
685
53.256
19.057
62.014
1.00
18.99
B

ATOM
4161
CG1
ILE B
685
53.488
21.211
60.784
1.00
17.58
B

ATOM
4162
CD1
ILE B
685
52.067
21.562
61.120
1.00
17.99
B

ATOM
4163
C
ILE B
685
55.037
19.993
64.100
1.00
21.40
B

ATOM
4164
O
ILE B
685
56.263
19.961
64.315
1.00
21.31
B

ATOM
4165
N
LEU B
686
54.137
19.207
64.697
1.00
20.50
B

ATOM
4166
CA
LEU B
686
54.461
18.147
65.648
1.00
21.98
B

ATOM
4167
CB
LEU B
686
54.273
18.612
67.108
1.00
23.37
B

ATOM
4168
CG
LEU B
686
54.138
17.518
68.189
1.00
24.30
B

ATOM
4169
CD1
LEU B
686
55.479
16.866
68.430
1.00
24.15
B

ATOM
4170
CD2
LEU B
686
53.595
18.098
69.475
1.00
22.84
B

ATOM
4171
C
LEU B
686
53.475
17.026
65.361
1.00
22.92
B

ATOM
4172
O
LEU B
686
52.297
17.167
65.650
1.00
25.29
B

ATOM
4173
N
VAL B
687
53.927
15.924
64.780
1.00
21.99
B

ATOM
4174
CA
VAL B
687
53.018
14.817
64.511
1.00
21.64
B

ATOM
4175
CB
VAL B
687
53.186
14.346
63.000
1.00
22.41
B

ATOM
4176
CG1
VAL B
687
52.604
12.949
62.796
1.00
21.78
B

ATOM
4177
CG2
VAL B
687
52.476
15.325
62.052
1.00
19.88
B

ATOM
4178
C
VAL B
687
53.345
13.700
65.542
1.00
21.43
B

ATOM
4179
O
VAL B
687
54.476
13.202
65.599
1.00
21.65
B

ATOM
4180
N
SER B
688
52.387
13.330
66.390
1.00
21.20
B

ATOM
4181
CA
SER B
688
52.654
12.302
67.412
1.00
21.07
B

ATOM
4182
CB
SER B
688
52.601
12.920
68.812
1.00
21.19
B

ATOM
4183
OG
SER B
688
51.336
13.509
69.074
1.00
19.67
B

ATOM
4184
C
SER B
688
51.706
11.118
67.373
1.00
21.57
B

ATOM
4185
O
SER B
688
50.511
11.265
67.104
1.00
21.58
B

ATOM
4186
N
GLY B
689
52.221
9.935
67.674
1.00
23.31
B

ATOM
4187
CA
GLY B
689
51.348
8.778
67.635
1.00
25.20
B

ATOM
4188
C
GLY B
689
51.498
7.793
68.779
1.00
26.22
B

ATOM
4189
O
GLY B
689
52.590
7.549
69.295
1.00
26.74
B

ATOM
4190
N
SER B
690
50.372
7.245
69.200
1.00
26.47
B

ATOM
4191
CA
SER B
690
50.350
6.247
70.253
1.00
29.04
B

ATOM
4192
CB
SER B
690
49.977
6.881
71.601
1.00
30.51
B

ATOM
4193
OG
SER B
690
48.577
7.150
71.674
1.00
31.85
B

ATOM
4194
C
SER B
690
49.261
5.262
69.818
1.00
29.64
B

ATOM
4195
O
SER B
690
48.624
5.462
68.788
1.00
31.71
B

ATOM
4196
N
GLU B
691
49.037
4.213
70.599
1.00
29.52
B

ATOM
4197
CA
GLU B
691
48.005
3.239
70.280
1.00
28.36
B

ATOM
4198
CB
GLU B
691
47.857
2.282
71.452
1.00
28.07
B

ATOM
4199
CG
GLU B
691
46.563
1.512
71.496
1.00
32.75
B

ATOM
4200
CD
GLU B
691
46.531
0.499
72.635
1.00
35.90
B

ATOM
4201
OE1
GLU B
691
47.285
−0.507
72.575
1.00
37.07
B

ATOM
4202
OE2
GLU B
691
45.751
0.712
73.594
1.00
36.72
B

ATOM
4203
C
GLU B
691
46.689
3.970
70.013
1.00
27.98
B

ATOM
4204
O
GLU B
691
46.356
4.921
70.713
1.00
29.12
B

ATOM
4205
N
ASN B
692
45.968
3.554
68.974
1.00
27.34
B

ATOM
4206
CA
ASN B
692
44.678
4.159
68.617
1.00
27.55
B

ATOM
4207
CB
ASN B
692
43.625
3.832
69.671
1.00
30.51
B

ATOM
4208
CG
ASN B
692
43.363
2.347
69.797
1.00
33.53
B

ATOM
4209
OD1
ASN B
692
42.997
1.866
70.874
1.00
34.93
B

ATOM
4210
ND2
ASN B
692
43.537
1.607
68.694
1.00
36.41
B

ATOM
4211
C
ASN B
692
44.671
5.671
68.417
1.00
28.06
B

ATOM
4212
O
ASN B
692
43.611
6.271
68.227
1.00
27.85
B

ATOM
4213
N
GLN B
693
45.836
6.300
68.455
1.00
27.40
B

ATOM
4214
CA
GLN B
693
45.883
7.737
68.270
1.00
26.47
B

ATOM
4215
CB
GLN B
693
46.046
8.410
69.627
1.00
26.45
B

ATOM
4216
CG
GLN B
693
44.860
8.235
70.547
1.00
27.10
B

ATOM
4217
CD
GLN B
693
44.499
9.523
71.245
1.00
27.21
B

ATOM
4218
OE1
GLN B
693
45.360
10.211
71.776
1.00
28.92
B

ATOM
4219
NE2
GLN B
693
43.224
9.859
71.243
1.00
29.30
B

ATOM
4220
C
GLN B
693
46.999
8.200
67.320
1.00
26.29
B

ATOM
4221
O
GLN B
693
48.105
7.655
67.332
1.00
27.55
B

ATOM
4222
N
PHE B
694
46.700
9.196
66.487
1.00
24.60
B

ATOM
4223
CA
PHE B
694
47.675
9.771
65.551
1.00
22.51
B

ATOM
4224
CB
PHE B
694
47.612
9.073
64.184
1.00
20.48
B

ATOM
4225
CG
PHE B
694
48.701
9.499
63.210
1.00
20.42
B

ATOM
4226
CD1
PHE B
694
49.967
8.922
63.241
1.00
20.85
B

ATOM
4227
CD2
PHE B
694
48.441
10.465
62.237
1.00
21.71
B

ATOM
4228
CE1
PHE B
694
50.956
9.301
62.312
1.00
21.35
B

ATOM
4229
CE2
PHE B
694
49.421
10.851
61.304
1.00
20.94
B

ATOM
4230
CZ
PHE B
694
50.674
10.269
61.343
1.00
20.97
B

ATOM
4231
C
PHE B
694
47.234
11.227
65.445
1.00
22.04
B

ATOM
4232
O
PHE B
694
46.146
11.508
64.951
1.00
22.64
B

ATOM
4233
N
ASN B
695
48.065
12.142
65.947
1.00
22.40
B

ATOM
4234
CA
ASN B
695
47.741
13.570
65.946
1.00
22.71
B

ATOM
4235
CB
ASN B
695
47.542
14.102
67.383
1.00
24.16
B

ATOM
4236
CG
ASN B
695
46.687
13.194
68.246
1.00
27.03
B

ATOM
4237
OD1
ASN B
695
47.145
12.735
69.297
1.00
30.17
B

ATOM
4238
ND2
ASN B
695
45.441
12.930
67.817
1.00
28.07
B

ATOM
4239
C
ASN B
695
48.762
14.477
65.261
1.00
21.75
B

ATOM
4240
O
ASN B
695
49.960
14.194
65.232
1.00
20.80
B

ATOM
4241
N
ILE B
696
48.248
15.588
64.734
1.00
21.52
B

ATOM
4242
CA
ILE B
696
49.024
16.622
64.045
1.00
20.16
B

ATOM
4243
CB
ILE B
696
48.592
16.711
62.556
1.00
17.92
B

ATOM
4244
CG2
ILE B
696
49.367
17.768
61.821
1.00
16.21
B

ATOM
4245
CG1
ILE B
696
48.860
15.371
61.883
1.00
16.96
B

ATOM
4246
CD1
ILE B
696
48.335
15.277
60.471
1.00
14.78
B

ATOM
4247
C
ILE B
696
48.732
17.922
64.803
1.00
20.71
B

ATOM
4248
O
ILE B
696
47.589
18.207
65.167
1.00
20.57
B

ATOM
4249
N
TYR B
697
49.779
18.690
65.057
1.00
21.04
B

ATOM
4250
CA
TYR B
697
49.651
19.916
65.816
1.00
22.01
B

ATOM
4251
CB
TYR B
697
50.334
19.746
67.174
1.00
22.18
B

ATOM
4252
CG
TYR B
697
49.748
18.654
68.027
1.00
22.67
B

ATOM
4253
CD1
TYR B
697
48.702
18.919
68.917
1.00
21.46
B

ATOM
4254
CE1
TYR B
697
48.167
17.910
69.717
1.00
20.34
B

ATOM
4255
CD2
TYR B
697
50.244
17.349
67.952
1.00
22.41
B

ATOM
4256
CE2
TYR B
697
49.717
16.331
68.746
1.00
22.87
B

ATOM
4257
CZ
TYR B
697
48.685
16.615
69.627
1.00
21.85
B

ATOM
4258
OH
TYR B
697
48.212
15.607
70.431
1.00
22.33
B

ATOM
4259
C
TYR B
697
50.244
21.121
65.112
1.00
23.61
B

ATOM
4260
O
TYR B
697
51.334
21.080
64.538
1.00
25.65
B

ATOM
4261
N
ASN B
698
49.491
22.202
65.162
1.00
23.81
B

ATOM
4262
CA
ASN B
698
49.913
23.449
64.594
1.00
23.42
B

ATOM
4263
CB
ASN B
698
48.680
24.254
64.224
1.00
26.51
B

ATOM
4264
CG
ASN B
698
49.020
25.531
63.512
1.00
28.61
B

ATOM
4265
OD1
ASN B
698
49.959
26.238
63.897
1.00
28.06
B

ATOM
4266
ND2
ASN B
698
48.255
25.849
62.472
1.00
29.88
B

ATOM
4267
C
ASN B
698
50.658
24.079
65.778
1.00
23.71
B

ATOM
4268
O
ASN B
698
50.047
24.586
66.726
1.00
22.24
B

ATOM
4269
N
LEU B
699
51.980
23.982
65.732
1.00
23.60
B

ATOM
4270
CA
LEU B
699
52.841
24.497
66.773
1.00
24.06
B

ATOM
4271
CB
LEU B
699
54.270
24.037
66.517
1.00
22.91
B

ATOM
4272
CG
LEU B
699
54.837
22.996
67.475
1.00
23.91
B

ATOM
4273
CD1
LEU B
699
53.784
21.972
67.874
1.00
24.32
B

ATOM
4274
CD2
LEU B
699
56.028
22.362
66.832
1.00
22.79
B

ATOM
4275
C
LEU B
699
52.801
26.001
66.862
1.00
25.53
B

ATOM
4276
O
LEU B
699
53.498
26.580
67.681
1.00
27.08
B

ATOM
4277
N
ARG B
700
52.004
26.631
66.002
1.00
26.51
B

ATOM
4278
CA
ARG B
700
51.863
28.087
65.997
1.00
25.40
B

ATOM
4279
CB
ARG B
700
51.489
28.600
64.609
1.00
27.54
B

ATOM
4280
CG
ARG B
700
52.549
28.502
63.543
1.00
28.72
B

ATOM
4281
CD
ARG B
700
53.706
29.422
63.820
1.00
31.33
B

ATOM
4282
NE
ARG B
700
54.598
29.480
62.671
1.00
34.27
B

ATOM
4283
CZ
ARG B
700
54.233
29.908
61.464
1.00
36.22
B

ATOM
4284
NH1
ARG B
700
52.989
30.318
61.259
1.00
35.49
B

ATOM
4285
NH2
ARG B
700
55.107
29.920
60.457
1.00
38.36
B

ATOM
4286
C
ARG B
700
50.724
28.431
66.942
1.00
24.24
B

ATOM
4287
O
ARG B
700
50.914
29.118
67.928
1.00
22.77
B

ATOM
4288
N
SER B
701
49.532
27.949
66.620
1.00
23.91
B

ATOM
4289
CA
SER B
701
48.358
28.202
67.435
1.00
23.69
B

ATOM
4290
CB
SER B
701
47.105
27.928
66.633
1.00
21.95
B

ATOM
4291
OG
SER B
701
47.096
26.574
66.220
1.00
21.41
B

ATOM
4292
C
SER B
701
48.342
27.281
68.627
1.00
25.56
B

ATOM
4293
O
SER B
701
47.546
27.467
69.541
1.00
27.95
B

ATOM
4294
N
GLY B
702
49.207
26.273
68.606
1.00
25.80
B

ATOM
4295
CA
GLY B
702
49.252
25.311
69.688
1.00
25.16
B

ATOM
4296
C
GLY B
702
48.080
24.351
69.601
1.00
25.57
B

ATOM
4297
O
GLY B
702
47.963
23.464
70.427
1.00
27.20
B

ATOM
4298
N
LYS B
703
47.221
24.498
68.597
1.00
26.86
B

ATOM
4299
CA
LYS B
703
46.049
23.630
68.485
1.00
29.85
B

ATOM
4300
CB
LYS B
703
44.846
24.452
67.982
1.00
31.50
B

ATOM
4301
CG
LYS B
703
44.521
25.679
68.857
1.00
35.32
B

ATOM
4302
CD
LYS B
703
43.066
26.160
68.704
1.00
35.78
B

ATOM
4303
CE
LYS B
703
42.529
26.768
70.007
1.00
39.24
B

ATOM
4304
NZ
LYS B
703
42.643
25.841
71.218
1.00
39.02
B

ATOM
4305
C
LYS B
703
46.199
22.357
67.631
1.00
29.87
B

ATOM
4306
O
LYS B
703
47.079
22.245
66.786
1.00
31.67
B

ATOM
4307
N
LEU B
704
45.314
21.403
67.868
1.00
29.38
B

ATOM
4308
CA
LEU B
704
45.319
20.152
67.149
1.00
29.31
B

ATOM
4309
CB
LEU B
704
44.445
19.169
67.892
1.00
28.56
B

ATOM
4310
CG
LEU B
704
44.409
17.731
67.419
1.00
29.17
B

ATOM
4311
CD1
LEU B
704
45.768
17.030
67.620
1.00
29.83
B

ATOM
4312
CD2
LEU B
704
43.340
17.041
68.206
1.00
28.68
B

ATOM
4313
C
LEU B
704
44.732
20.390
65.772
1.00
30.18
B

ATOM
4314
O
LEU B
704
43.610
20.880
65.669
1.00
32.27
B

ATOM
4315
N
VAL B
705
45.458
20.053
64.709
1.00
30.79
B

ATOM
4316
CA
VAL B
705
44.908
20.275
63.371
1.00
31.43
B

ATOM
4317
CB
VAL B
705
46.012
20.551
62.322
1.00
30.01
B

ATOM
4318
CG1
VAL B
705
45.368
20.883
60.976
1.00
28.32
B

ATOM
4319
CG2
VAL B
705
46.889
21.685
62.776
1.00
29.54
B

ATOM
4320
C
VAL B
705
44.069
19.087
62.904
1.00
32.61
B

ATOM
4321
O
VAL B
705
42.930
19.252
62.462
1.00
32.10
B

ATOM
4322
N
HIS B
706
44.641
17.890
63.003
1.00
35.60
B

ATOM
4323
CA
HIS B
706
43.949
16.665
62.613
1.00
37.51
B

ATOM
4324
CB
HIS B
706
44.515
16.131
61.302
1.00
40.51
B

ATOM
4325
CG
HIS B
706
44.191
16.972
60.110
1.00
43.09
B

ATOM
4326
CD2
HIS B
706
44.947
17.845
59.402
1.00
44.48
B

ATOM
4327
ND1
HIS B
706
42.946
16.973
59.521
1.00
43.58
B

ATOM
4328
CE1
HIS B
706
42.948
17.814
58.501
1.00
44.83
B

ATOM
4329
NE2
HIS B
706
44.149
18.357
58.407
1.00
45.93
B

ATOM
4330
C
HIS B
706
44.109
15.583
63.676
1.00
37.67
B

ATOM
4331
O
HIS B
706
45.189
15.396
64.267
1.00
38.10
B

ATOM
4332
N
ALA B
707
43.032
14.852
63.917
1.00
37.33
B

ATOM
4333
CA
ALA B
707
43.104
13.773
64.891
1.00
35.31
B

ATOM
4334
CB
ALA B
707
42.368
14.163
66.163
1.00
33.61
B

ATOM
4335
C
ALA B
707
42.540
12.479
64.322
1.00
33.93
B

ATOM
4336
O
ALA B
707
42.616
11.455
64.979
1.00
33.97
B

ATOM
4337
N
ASN B
708
42.000
12.508
63.103
1.00
32.93
B

ATOM
4338
CA
ASN B
708
41.438
11.278
62.566
1.00
32.08
B

ATOM
4339
CB
ASN B
708
39.900
11.381
62.527
1.00
30.21
B

ATOM
4340
CG
ASN B
708
39.282
11.431
63.935
1.00
29.73
B

ATOM
4341
OD1
ASN B
708
39.641
10.644
64.808
1.00
32.17
B

ATOM
4342
ND2
ASN B
708
38.369
12.355
64.155
1.00
27.91
B

ATOM
4343
C
ASN B
708
41.998
10.810
61.227
1.00
31.64
B

ATOM
4344
O
ASN B
708
41.468
9.888
60.605
1.00
30.96
B

ATOM
4345
N
ILE B
709
43.104
11.412
60.803
1.00
31.19
B

ATOM
4346
CA
ILE B
709
43.709
11.050
59.526
1.00
29.76
B

ATOM
4347
CB
ILE B
709
45.027
11.813
59.279
1.00
30.79
B

ATOM
4348
CG2
ILE B
709
45.414
11.698
57.830
1.00
30.87
B

ATOM
4349
CG1
ILE B
709
44.846
13.292
59.585
1.00
31.89
B

ATOM
4350
CD1
ILE B
709
43.831
13.966
58.690
1.00
33.84
B

ATOM
4351
C
ILE B
709
43.992
9.554
59.404
1.00
27.56
B

ATOM
4352
O
ILE B
709
43.923
9.003
58.316
1.00
28.85
B

ATOM
4353
N
LEU B
710
44.335
8.892
60.498
1.00
24.88
B

ATOM
4354
CA
LEU B
710
44.600
7.464
60.406
1.00
23.14
B

ATOM
4355
CB
LEU B
710
46.101
7.207
60.581
1.00
19.23
B

ATOM
4356
CG
LEU B
710
47.171
7.770
59.617
1.00
17.21
B

ATOM
4357
CD1
LEU B
710
48.565
7.336
60.119
1.00
12.65
B

ATOM
4358
CD2
LEU B
710
46.952
7.271
58.159
1.00
11.32
B

ATOM
4359
C
LEU B
710
43.787
6.738
61.491
1.00
24.82
B

ATOM
4360
O
LEU B
710
44.278
5.820
62.165
1.00
26.12
B

ATOM
4361
N
LYS B
711
42.540
7.172
61.668
1.00
24.22
B

ATOM
4362
CA
LYS B
711
41.672
6.583
62.678
1.00
23.87
B

ATOM
4363
CB
LYS B
711
40.223
7.113
62.551
1.00
23.07
B

ATOM
4364
CG
LYS B
711
39.704
7.286
61.127
0.00
24.07
B

ATOM
4365
CD
LYS B
711
39.138
6.000
60.567
0.00
24.51
B

ATOM
4366
CE
LYS B
711
38.815
6.171
59.096
0.00
24.91
B

ATOM
4367
NZ
LYS B
711
38.073
5.005
58.557
0.00
25.25
B

ATOM
4368
C
LYS B
711
41.697
5.066
62.640
1.00
22.54
B

ATOM
4369
O
LYS B
711
41.789
4.435
63.682
1.00
21.78
B

ATOM
4370
N
ASP B
712
41.656
4.474
61.450
1.00
24.59
B

ATOM
4371
CA
ASP B
712
41.649
3.009
61.346
1.00
26.66
B

ATOM
4372
CB
ASP B
712
41.358
2.577
59.902
1.00
27.40
B

ATOM
4373
CG
ASP B
712
42.533
2.779
58.971
1.00
29.97
B

ATOM
4374
OD1
ASP B
712
43.376
3.660
59.238
1.00
31.04
B

ATOM
4375
OD2
ASP B
712
42.601
2.059
57.945
1.00
32.95
B

ATOM
4376
C
ASP B
712
42.908
2.320
61.846
1.00
27.18
B

ATOM
4377
O
ASP B
712
42.933
1.100
61.992
1.00
28.41
B

ATOM
4378
N
ALA B
713
43.943
3.099
62.131
1.00
26.51
B

ATOM
4379
CA
ALA B
713
45.192
2.526
62.600
1.00
27.91
B

ATOM
4380
CB
ALA B
713
46.334
3.505
62.337
1.00
25.17
B

ATOM
4381
C
ALA B
713
45.117
2.185
64.091
1.00
29.57
B

ATOM
4382
O
ALA B
713
44.650
3.003
64.889
1.00
30.09
B

ATOM
4383
N
ASP B
714
45.584
0.991
64.467
1.00
30.92
B

ATOM
4384
CA
ASP B
714
45.568
0.564
65.873
1.00
33.02
B

ATOM
4385
CB
ASP B
714
45.300
−0.947
65.975
1.00
34.69
B

ATOM
4386
CG
ASP B
714
43.997
−1.348
65.333
1.00
36.43
B

ATOM
4387
OD1
ASP B
714
42.933
−0.920
65.810
1.00
38.16
B

ATOM
4388
OD2
ASP B
714
44.033
−2.089
64.337
1.00
40.68
B

ATOM
4389
C
ASP B
714
46.871
0.908
66.620
1.00
33.35
B

ATOM
4390
O
ASP B
714
46.871
1.124
67.837
1.00
33.65
B

ATOM
4391
N
GLN B
715
47.979
0.948
65.888
1.00
32.50
B

ATOM
4392
CA
GLN B
715
49.272
1.292
66.470
1.00
31.33
B

ATOM
4393
CB
GLN B
715
50.053
0.028
66.851
1.00
32.90
B

ATOM
4394
CG
GLN B
715
49.555
−0.657
68.107
1.00
36.42
B

ATOM
4395
CD
GLN B
715
49.806
0.172
69.355
1.00
39.19
B

ATOM
4396
OE1
GLN B
715
49.528
−0.273
70.465
1.00
39.45
B

ATOM
4397
NE2
GLN B
715
50.342
1.389
69.175
1.00
41.12
B

ATOM
4398
CG
LN B
715
50.063
2.123
65.465
1.00
29.87
B

ATOM
4399
O
GLN B
715
49.897
1.967
64.254
1.00
28.89
B

ATOM
4400
N
ILE B
716
50.885
3.038
65.968
1.00
28.35
B

ATOM
4401
CA
ILE B
716
51.712
3.875
65.102
1.00
26.58
B

ATOM
4402
CB
ILE B
716
51.360
5.388
65.216
1.00
26.71
B

ATOM
4403
CG2
ILE B
716
52.387
6.226
64.452
1.00
24.23
B

ATOM
4404
CG1
ILE B
716
49.979
5.655
64.611
1.00
27.09
B

ATOM
4405
CD1
ILE B
716
48.830
5.042
65.381
1.00
29.06
B

ATOM
4406
C
ILE B
716
53.137
3.644
65.567
1.00
26.24
B

ATOM
4407
O
ILE B
716
53.563
4.184
66.583
1.00
25.69
B

ATOM
4408
N
TRP B
717
53.870
2.833
64.818
1.00
25.09
B

ATOM
4409
CA
TRP B
717
55.219
2.505
65.198
1.00
25.49
B

ATOM
4410
CB
TRP B
717
55.658
1.210
64.497
1.00
28.30
B

ATOM
4411
CG
TRP B
717
54.780
0.010
64.877
1.00
31.04
B

ATOM
4412
CD2
TRP B
717
54.454
−0.438
66.203
1.00
29.45
B

ATOM
4413
CE2
TRP B
717
53.559
−1.521
66.071
1.00
29.85
B

ATOM
4414
CE3
TRP B
717
54.828
−0.029
67.483
1.00
30.32
B

ATOM
4415
CD1
TRP B
717
54.091
−0.807
64.024
1.00
30.88
B

ATOM
4416
NE1
TRP B
717
53.353
−1.724
64.736
1.00
29.32
B

ATOM
4417
CZ2
TRP B
717
53.027
−2.199
67.172
1.00
33.01
B

ATOM
4418
CZ3
TRP B
717
54.295
−0.706
68.583
1.00
33.00
B

ATOM
4419
CH2
TRP B
717
53.406
−1.778
68.416
1.00
32.26
B

ATOM
4420
C
TRP B
717
56.207
3.611
64.925
1.00
25.13
B

ATOM
4421
O
TRP B
717
56.995
3.961
65.782
1.00
27.18
B

ATOM
4422
N
SER B
718
56.163
4.189
63.743
1.00
24.84
B

ATOM
4423
CA
SER B
718
57.127
5.212
63.423
1.00
24.34
B

ATOM
4424
CB
SER B
718
58.314
4.536
62.727
1.00
24.77
B

ATOM
4425
OG
SER B
718
59.315
5.464
62.352
1.00
29.36
B

ATOM
4426
C
SER B
718
56.477
6.265
62.533
1.00
23.95
B

ATOM
4427
O
SER B
718
55.668
5.949
61.663
1.00
24.34
B

ATOM
4428
N
VAL B
719
56.813
7.521
62.754
1.00
21.34
B

ATOM
4429
CA
VAL B
719
56.236
8.549
61.934
1.00
20.74
B

ATOM
4430
CB
VAL B
719
55.041
9.202
62.663
1.00
20.34
B

ATOM
4431
CG1
VAL B
719
55.531
10.069
63.799
1.00
20.79
B

ATOM
4432
CG2
VAL B
719
54.182
9.964
61.685
1.00
20.98
B

ATOM
4433
C
VAL B
719
57.355
9.538
61.608
1.00
21.48
B

ATOM
4434
O
VAL B
719
58.204
9.840
62.452
1.00
21.37
B

ATOM
4435
N
ASN B
720
57.391
10.001
60.368
1.00
20.75
B

ATOM
4436
CA
ASN B
720
58.434
10.915
59.950
1.00
20.33
B

ATOM
4437
CB
ASN B
720
59.582
10.130
59.331
1.00
19.95
B

ATOM
4438
CG
ASN B
720
60.744
11.013
58.939
1.00
20.71
B

ATOM
4439
OD1
ASN B
720
60.570
12.186
58.613
1.00
22.75
B

ATOM
4440
ND2
ASN B
720
61.934
10.452
58.960
1.00
19.81
B

ATOM
4441
C
ASN B
720
57.831
11.792
58.885
1.00
21.17
B

ATOM
4442
O
ASN B
720
57.037
11.318
58.078
1.00
23.00
B

ATOM
4443
N
PHE B
721
58.187
13.067
58.850
1.00
20.66
B

ATOM
4444
CA
PHE B
721
57.630
13.907
57.791
1.00
21.75
B

ATOM
4445
CB
PHE B
721
56.339
14.591
58.289
1.00
17.46
B

ATOM
4446
CG
PHE B
721
56.556
15.653
59.312
1.00
14.32
B

ATOM
4447
CO1
PHE B
721
56.870
16.939
58.921
1.00
10.85
B

ATOM
4448
CD2
PHE B
721
56.404
15.387
60.660
1.00
11.84
B

ATOM
4449
CE1
PHE B
721
57.028
17.953
59.855
1.00
10.06
B

ATOM
4450
CE2
PHE B
721
56.561
16.405
61.607
1.00
13.14
B

ATOM
4451
CZ
PHE B
721
56.873
17.693
61.198
1.00
12.02
B

ATOM
4452
C
PHE B
721
58.656
14.902
57.259
1.00
22.48
B

ATOM
4453
O
PHE B
721
59.528
15.344
58.000
1.00
21.67
B

ATOM
4454
N
LYS B
722
58.584
15.205
55.961
1.00
24.01
B

ATOM
4455
CA
LYS B
722
59.508
16.161
55.320
1.00
24.93
B

ATOM
4456
CB
LYS B
722
60.752
15.450
54.783
1.00
25.59
B

ATOM
4457
CG
LYS B
722
61.838
15.134
55.800
1.00
27.22
B

ATOM
4458
CD
LYS B
722
62.834
16.283
55.958
0.00
27.08
B

ATOM
4459
CE
LYS B
722
62.210
17.519
56.576
0.00
27.46
B

ATOM
4460
NZ
LYS B
722
63.225
18.601
56.697
0.00
27.62
B

ATOM
4461
C
LYS B
722
58.838
16.863
54.151
1.00
24.47
B

ATOM
4462
O
LYS B
722
58.571
16.242
53.121
1.00
25.21
B

ATOM
4463
N
GLY B
723
58.569
18.153
54.298
1.00
24.23
B

ATOM
4464
CA
GLY B
723
57.937
18.872
53.209
1.00
26.31
B

ATOM
4465
C
GLY B
723
56.464
18.536
53.019
1.00
28.74
B

ATOM
4466
O
GLY B
723
55.694
18.529
53.979
1.00
29.75
B

ATOM
4467
N
LYS B
724
56.057
18.235
51.794
1.00
28.84
B

ATOM
4468
CA
LYS B
724
54.652
17.941
51.530
1.00
29.80
B

ATOM
4469
CB
LYS B
724
54.352
18.219
50.074
1.00
31.52
B

ATOM
4470
CG
LYS B
724
55.436
17.698
49.171
1.00
32.34
B

ATOM
4471
CD
LYS B
724
54.881
16.783
48.115
1.00
33.78
B

ATOM
4472
CE
LYS B
724
55.974
16.447
47.107
1.00
35.08
B

ATOM
4473
NZ
LYS B
724
56.379
17.659
46.344
1.00
33.47
B

ATOM
4474
C
LYS B
724
54.184
16.535
51.841
1.00
29.68
B

ATOM
4475
O
LYS B
724
52.988
16.260
51.801
1.00
28.58
B

ATOM
4476
N
THR B
725
55.121
15.643
52.135
1.00
29.01
B

ATOM
4477
CA
THR B
725
54.768
14.261
52.412
1.00
28.07
B

ATOM
4478
CB
THR B
725
55.459
13.315
51.372
1.00
28.24
B

ATOM
4479
OG1
THR B
725
55.740
12.040
51.957
1.00
28.44
B

ATOM
4480
CG2
THR B
725
56.732
13.943
50.850
1.00
29.05
B

ATOM
4481
C
THR B
725
55.081
13.853
53.847
1.00
27.60
B

ATOM
4482
O
THR B
725
56.070
14.292
54.445
1.00
27.85
B

ATOM
4483
N
LEU B
726
54.190
13.036
54.399
1.00
26.00
B

ATOM
4484
CA
LEU B
726
54.310
12.528
55.755
1.00
24.86
B

ATOM
4485
CB
LEU B
726
53.147
13.030
56.612
1.00
23.41
B

ATOM
4486
CG
LEU B
726
52.907
12.266
57.924
1.00
21.65
B

ATOM
4487
OD1
LEU B
726
54.123
12.369
58.805
1.00
24.41
B

ATOM
4488
CD2
LEU B
726
51.698
12.816
58.643
1.00
21.21
B

ATOM
4489
C
LEU B
726
54.254
11.014
55.677
1.00
25.90
B

ATOM
4490
O
LEU B
726
53.370
10.464
55.019
1.00
27.58
B

ATOM
4491
N
VAL B
727
55.196
10.329
56.315
1.00
24.78
B

ATOM
4492
CA
VAL B
727
55.151
8.875
56.283
1.00
25.06
B

ATOM
4493
CB
VAL B
727
56.388
8.256
55.556
1.00
23.86
B

ATOM
4494
CG1
VAL B
727
56.432
8.730
54.129
1.00
22.56
B

ATOM
4495
CG2
VAL B
727
57.678
8.571
56.296
1.00
23.51
B

ATOM
4496
C
VAL B
727
55.009
8.257
57.680
1.00
25.61
B

ATOM
4497
O
VAL B
727
55.637
8.717
58.641
1.00
25.40
B

ATOM
4498
N
ALA B
728
54.163
7.224
57.775
1.00
26.51
B

ATOM
4499
CA
ALA B
728
53.898
6.501
59.028
1.00
27.01
B

ATOM
4500
CB
ALA B
728
52.656
7.087
59.692
1.00
25.86
B

ATOM
4501
C
ALA B
728
53.734
4.960
58.886
1.00
27.72
B

ATOM
4502
O
ALA B
728
52.981
4.480
58.039
1.00
28.25
B

ATOM
4503
N
ALA B
729
54.457
4.204
59.718
1.00
29.53
B

ATOM
4504
CA
ALA B
729
54.401
2.735
59.745
1.00
30.38
B

ATOM
4505
CB
ALA B
729
55.761
2.150
60.042
1.00
26.88
B

ATOM
4506
C
ALA B
729
53.441
2.404
60.876
1.00
32.48
B

ATOM
4507
O
ALA B
729
53.692
2.754
62.036
1.00
32.95
B

ATOM
4508
N
VAL B
730
52.358
1.710
60.541
1.00
34.76
B

ATOM
4509
CA
VAL B
730
51.326
1.409
61.520
1.00
36.48
B

ATOM
4510
CB
VAL B
730
50.133
2.339
61.277
1.00
35.80
B

ATOM
4511
CG1
VAL B
730
50.546
3.802
61.484
1.00
35.67
B

ATOM
4512
CG2
VAL B
730
49.642
2.148
59.859
1.00
35.12
B

ATOM
4513
C
VAL B
730
50.819
−0.022
61.471
1.00
37.73
B

ATOM
4514
O
VAL B
730
51.069
−0.738
60.507
1.00
39.94
B

ATOM
4515
N
GLU B
731
50.102
−0.422
62.520
1.00
38.43
B

ATOM
4516
CA
GLU B
731
49.509
−1.755
62.608
1.00
38.21
B

ATOM
4517
CB
GLU B
731
49.851
−2.413
63.929
1.00
37.52
B

ATOM
4518
CG
GLU B
731
49.515
−3.869
63.933
1.00
39.46
B

ATOM
4519
CD
GLU B
731
49.255
−4.398
65.328
1.00
41.40
B

ATOM
4520
OE1
GLU B
731
48.163
−4.105
65.873
1.00
41.33
B

ATOM
4521
OE2
GLU B
731
50.140
−5.101
65.877
1.00
42.25
B

ATOM
4522
C
GLU B
731
47.996
−1.611
62.504
1.00
39.22
B

ATOM
4523
O
GLU B
731
47.393
−0.781
63.189
1.00
38.41
B

ATOM
4524
N
LYS B
732
47.382
−2.424
61.652
1.00
41.10
B

ATOM
4525
CA
LYS B
732
45.938
−2.358
61.449
1.00
43.00
B

ATOM
4526
CB
LYS B
732
45.635
−1.485
60.226
1.00
42.61
B

ATOM
4527
CG
LYS B
732
46.197
−0.077
60.333
0.00
43.37
B

ATOM
4528
CD
LYS B
732
46.607
0.492
58.981
0.00
43.64
B

ATOM
4529
CE
LYS B
732
45.431
0.678
58.036
0.00
43.89
B

ATOM
4530
NZ
LYS B
732
45.868
1.358
56.783
0.00
44.01
B

ATOM
4531
C
LYS B
732
45.381
−3.753
61.237
1.00
44.67
B

ATOM
4532
O
LYS B
732
45.879
−4.500
60.393
1.00
45.72
B

ATOM
4533
N
ASP B
733
44.350
−4.100
62.004
1.00
46.86
B

ATOM
4534
CA
ASP B
733
43.717
−5.417
61.898
1.00
48.20
B

ATOM
4535
CB
ASP B
733
43.098
−5.602
60.502
1.00
51.83
B

ATOM
4536
CG
ASP B
733
42.192
−6.824
60.411
1.00
54.62
B

ATOM
4537
OD1
ASP B
733
42.658
−7.894
59.947
1.00
55.49
B

ATOM
4538
OD2
ASP B
733
41.009
−6.708
60.812
1.00
55.81
B

ATOM
4539
C
ASP B
733
44.744
−6.520
62.159
1.00
46.65
B

ATOM
4540
O
ASP B
733
44.653
−7.621
61.614
1.00
46.27
B

ATOM
4541
N
GLY B
734
45.739
−6.203
62.977
1.00
45.55
B

ATOM
4542
CA
GLY B
734
46.749
−7.182
63.308
1.00
45.42
B

ATOM
4543
C
GLY B
734
47.792
−7.446
62.245
1.00
45.85
B

ATOM
4544
O
GLY B
734
48.334
−8.548
62.183
1.00
46.44
B

ATOM
4545
N
GLN B
735
48.073
−6.454
61.401
1.00
46.81
B

ATOM
4546
CA
GLN B
735
49.093
−6.599
60.355
1.00
47.05
B

ATOM
4547
CB
GLN B
735
48.461
−7.018
59.028
1.00
48.17
B

ATOM
4548
CG
GLN B
735
48.028
−8.461
59.027
1.00
52.88
B

ATOM
4549
CD
GLN B
735
46.961
−8.755
57.990
1.00
56.44
B

ATOM
4550
OE1
GLN B
735
46.245
−9.766
58.087
1.00
58.95
B

ATOM
4551
NE2
GLN B
735
46.840
−7.878
56.993
1.00
55.74
B

ATOM
4552
C
GLN B
735
49.897
−5.317
60.176
1.00
45.22
B

ATOM
4553
O
GLN B
735
49.597
−4.297
60.789
1.00
46.16
B

ATOM
4554
N
SER B
736
50.924
−5.394
59.336
1.00
42.48
B

ATOM
4555
CA
SER B
736
51.817
−4.278
59.061
1.00
39.38
B

ATOM
4556
CB
SER B
736
53.256
−4.791
59.003
1.00
40.16
B

ATOM
4557
OG
SER B
736
54.176
−3.797
59.394
1.00
40.72
B

ATOM
4558
C
SER B
736
51.468
−3.563
57.753
1.00
37.61
B

ATOM
4559
O
SER B
736
51.155
−4.193
56.734
1.00
37.66
B

ATOM
4560
N
PHE B
737
51.549
−2.239
57.797
1.00
33.84
B

ATOM
4561
CA
PHE B
737
51.228
−1.405
56.655
1.00
31.74
B

ATOM
4562
CB
PHE B
737
49.753
−1.006
56.716
1.00
32.02
B

ATOM
4563
CG
PHE B
737
48.802
−2.099
56.337
1.00
33.36
B

ATOM
4564
CD1
PHE B
737
48.776
−2.582
55.041
1.00
34.70
B

ATOM
4565
CD2
PHE B
737
47.894
−2.606
57.255
1.00
35.15
B

ATOM
4566
CE1
PHE B
737
47.857
−3.545
54.655
1.00
36.59
B

ATOM
4567
CE2
PHE B
737
46.964
−3.573
56.878
1.00
35.49
B

ATOM
4568
CZ
PHE B
737
46.946
−4.044
55.573
1.00
36.38
B

ATOM
4569
C
PHE B
737
52.077
−0.134
56.644
1.00
30.68
B

ATOM
4570
O
PHE B
737
52.650
0.254
57.665
1.00
31.62
B

ATOM
4571
N
LEU B
738
52.165
0.510
55.485
1.00
27.59
B

ATOM
4572
CA
LEU B
738
52.905
1.758
55.373
1.00
25.56
B

ATOM
4573
CB
LEU B
738
54.042
1.679
54.355
1.00
25.25
B

ATOM
4574
CG
LEU B
738
54.884
2.973
54.305
1.00
25.05
B

ATOM
4575
CD1
LEU B
738
55.668
3.104
55.614
1.00
22.91
B

ATOM
4576
CD2
LEU B
738
55.839
2.973
53.131
1.00
21.80
B

ATOM
4577
C
LEU B
738
51.947
2.841
54.922
1.00
24.87
B

ATOM
4578
O
LEU B
738
51.336
2.743
53.864
1.00
23.89
B

ATOM
4579
N
GLU B
739
51.820
3.882
55.728
1.00
24.71
B

ATOM
4580
CA
GLU B
739
50.940
4.976
55.372
1.00
23.29
B

ATOM
4581
CB
GLU B
739
50.206
5.458
56.612
1.00
24.09
B

ATOM
4582
CG
GLU B
739
48.692
5.452
56.495
1.00
28.17
B

ATOM
4583
CD
GLU B
739
48.058
4.066
56.517
1.00
28.62
B

ATOM
4584
OE1
GLU B
739
48.352
3.273
57.426
1.00
31.20
B

ATOM
4585
OE2
GLU B
739
47.232
3.782
55.633
1.00
28.53
B

ATOM
4586
C
GLU B
739
51.795
6.094
54.780
1.00
20.71
B

ATOM
4587
O
GLU B
739
52.906
6.329
55.235
1.00
20.52
B

ATOM
4588
N
ILE B
740
51.290
6.740
53.732
1.00
19.91
B

ATOM
4589
CA
ILE B
740
51.968
7.868
53.075
1.00
19.31
B

ATOM
4590
CB
ILE B
740
52.572
7.473
51.720
1.00
17.66
B

ATOM
4591
CG2
ILE B
740
53.171
8.701
51.030
1.00
15.65
B

ATOM
4592
CG1
ILE B
740
53.604
6.379
51.926
1.00
16.52
B

ATOM
4593
CD1
ILE B
740
54.155
5.833
50.629
1.00
18.73
B

ATOM
4594
C
ILE B
740
50.891
8.923
52.849
1.00
19.07
B

ATOM
4595
O
ILE B
740
49.886
8.655
52.209
1.00
19.78
B

ATOM
4596
N
LEU B
741
51.106
10.111
53.395
1.00
19.72
B

ATOM
4597
CA
LEU B
741
50.151
11.188
53.259
1.00
21.30
B

ATOM
4598
CB
LEU B
741
49.728
11.648
54.645
1.00
22.07
B

ATOM
4599
CG
LEU B
741
49.077
10.572
55.530
1.00
23.25
B

ATOM
4600
CD1
LEU B
741
48.660
11.188
56.855
1.00
23.41
B

ATOM
4601
CD2
LEU B
741
47.856
9.989
54.825
1.00
23.48
B

ATOM
4602
C
LEU B
741
50.732
12.357
52.461
1.00
22.75
B

ATOM
4603
O
LEU B
741
51.891
12.745
52.656
1.00
24.38
B

ATOM
4604
N
ASP B
742
49.918
12.918
51.571
1.00
23.48
B

ATOM
4605
CA
ASP B
742
50.324
14.032
50.711
1.00
24.55
B

ATOM
4606
CB
ASP B
742
49.931
13.723
49.276
1.00
26.67
B

ATOM
4607
CG
ASP B
742
50.733
14.515
48.271
1.00
28.63
B

ATOM
4608
OD1
ASP B
742
50.840
15.760
48.424
1.00
28.82
B

ATOM
4609
OD2
ASP B
742
51.245
13.879
47.328
1.00
28.63
B

ATOM
4610
C
ASP B
742
49.688
15.363
51.103
1.00
25.06
B

ATOM
4611
O
ASP B
742
48.481
15.436
51.305
1.00
26.84
B

ATOM
4612
N
PHE B
743
50.484
16.423
51.183
1.00
25.71
B

ATOM
4613
CA
PHE B
743
49.943
17.731
51.558
1.00
27.52
B

ATOM
4614
CB
PHE B
743
50.486
18.191
52.912
1.00
26.16
B

ATOM
4615
CG
PHE B
743
49.997
17.388
54.073
1.00
24.94
B

ATOM
4616
CD1
PHE B
743
50.565
16.158
54.378
1.00
24.17
B

ATOM
4617
CD2
PHE B
743
48.980
17.887
54.890
1.00
23.91
B

ATOM
4618
CE1
PHE B
743
50.132
15.437
55.490
1.00
24.90
B

ATOM
4619
CE2
PHE B
743
48.537
17.184
56.000
1.00
21.83
B

ATOM
4620
CZ
PHE B
743
49.111
15.957
56.306
1.00
23.09
B

ATOM
4621
C
PHE B
743
50.249
18.808
50.530
1.00
29.26
B

ATOM
4622
O
PHE B
743
50.140
20.005
50.808
1.00
29.97
B

ATOM
4623
N
SER B
744
50.646
18.372
49.344
1.00
30.92
B

ATOM
4624
CA
SER B
744
50.955
19.277
48.245
1.00
32.47
B

ATOM
4625
CB
SER B
744
51.761
18.531
47.188
1.00
32.25
B

ATOM
4626
OG
SER B
744
51.080
17.346
46.824
1.00
29.83
B

ATOM
4627
C
SER B
744
49.649
19.790
47.629
1.00
34.01
B

ATOM
4628
O
SER B
744
49.524
21.028
47.432
1.00
35.67
B

ATOM
4629
OXT
SER B
744
48.778
18.934
47.348
1.00
33.32
B

ATOM
4630
CB
SER C
2
79.559
36.638
46.340
1.00
43.57
C

ATOM
4631
OG
SER C
2
79.993
37.690
45.505
1.00
44.36
C

ATOM
4632
C
SER C
2
78.062
35.376
44.763
1.00
44.40
C

ATOM
4633
O
SER C
2
78.864
34.452
44.588
1.00
45.41
C

ATOM
4634
N
SER C
2
77.555
35.428
47.144
1.00
45.64
C

ATOM
4635
CA
SER C
2
78.115
36.241
46.021
1.00
44.62
C

ATOM
4636
N
ASN C
3
77.108
35.678
43.890
1.00
43.20
C

ATOM
4637
CA
ASN C
3
76.921
34.908
42.666
1.00
41.97
C

ATOM
4638
CB
ASN C
3
75.435
34.551
42.505
1.00
43.04
C

ATOM
4639
CG
ASN C
3
74.952
33.552
43.535
1.00
43.55
C

ATOM
4640
OD1
ASN C
3
75.330
32.375
43.512
1.00
43.93
C

ATOM
4641
ND2
ASN C
3
74.105
34.017
44.448
1.00
43.67
C

ATOM
4642
C
ASN C
3
77.392
35.617
41.399
1.00
40.54
C

ATOM
4643
O
ASN C
3
77.723
36.800
41.401
1.00
40.39
C

ATOM
4644
N
VAL C
4
77.408
34.868
40.306
1.00
39.54
C

ATOM
4645
CA
VAL C
4
77.794
35.409
39.014
1.00
37.85
C

ATOM
4646
CB
VAL C
4
79.259
35.135
38.677
1.00
37.25
C

ATOM
4647
CG1
VAL C
4
80.128
36.252
39.212
1.00
37.46
C

ATOM
4648
CG2
VAL C
4
79.678
33.798
39.261
1.00
36.73
C

ATOM
4649
C
VAL C
4
76.959
34.717
37.975
1.00
36.19
C

ATOM
4650
O
VAL C
4
76.617
33.547
38.128
1.00
37.44
C

ATOM
4651
N
VAL C
5
76.627
35.440
36.917
1.00
33.92
C

ATOM
4652
CA
VAL C
5
75.844
34.864
35.846
1.00
31.07
C

ATOM
4653
CB
VAL C
5
74.812
35.871
35.315
1.00
29.79
C

ATOM
4654
CG1
VAL C
5
74.186
35.342
34.041
1.00
30.11
C

ATOM
4655
CG2
VAL C
5
73.735
36.100
36.359
1.00
28.61
C

ATOM
4656
C
VAL C
5
76.731
34.410
34.693
1.00
29.84
C

ATOM
4657
O
VAL C
5
77.601
35.147
34.233
1.00
29.90
C

ATOM
4658
N
LEU C
6
76.513
33.177
34.251
1.00
29.14
C

ATOM
4659
CA
LEU C
6
77.236
32.597
33.116
1.00
28.08
C

ATOM
4660
CB
LEU C
6
77.863
31.253
33.510
1.00
27.11
C

ATOM
4661
CG
LEU C
6
78.872
31.221
34.675
1.00
24.97
C

ATOM
4662
CD1
LEU C
6
79.528
29.845
34.700
1.00
24.15
C

ATOM
4663
CD2
LEU C
6
79.919
32.293
34.529
1.00
22.63
C

ATOM
4664
C
LEU C
6
76.201
32.405
31.990
1.00
27.51
C

ATOM
4665
O
LEU C
6
75.218
31.673
32.139
1.00
26.06
C

ATOM
4666
N
VAL C
7
76.422
33.083
30.869
1.00
28.04
C

ATOM
4667
CA
VAL C
7
75.498
33.035
29.732
1.00
29.08
C

ATOM
4668
CB
VAL C
7
75.410
34.425
29.046
1.00
30.10
C

ATOM
4669
CG1
VAL C
7
74.517
34.349
27.805
1.00
30.31
C

ATOM
4670
CG2
VAL C
7
74.887
35.454
30.033
1.00
28.75
C

ATOM
4671
C
VAL C
7
75.861
31.988
28.678
1.00
29.01
C

ATOM
4672
O
VAL C
7
77.008
31.913
28.226
1.00
28.23
C

ATOM
4673
N
SER C
8
74.865
31.191
28.291
1.00
28.51
C

ATOM
4674
CA
SER C
8
75.063
30.147
27.296
1.00
27.88
C

ATOM
4675
CB
SER C
8
74.009
29.037
27.418
1.00
28.20
C

ATOM
4676
OG
SER C
8
72.804
29.396
26.748
1.00
25.94
C

ATOM
4677
C
SER C
8
74.965
30.741
25.898
1.00
28.40
C

ATOM
4678
O
SER C
8
74.359
31.803
25.707
1.00
27.07
C

ATOM
4679
N
GLY C
9
75.574
30.034
24.941
1.00
27.46
C

ATOM
4680
CA
GLY C
9
75.569
30.450
23.553
1.00
26.64
C

ATOM
4681
C
GLY C
9
74.142
30.602
23.067
1.00
26.05
C

ATOM
4682
O
GLY C
9
73.874
31.296
22.085
1.00
26.15
C

ATOM
4683
N
GLU C
10
73.219
29.941
23.752
1.00
24.38
C

ATOM
4684
CA
GLU C
10
71.824
30.034
23.400
1.00
23.90
C

ATOM
4685
CB
GLU C
10
71.116
28.716
23.732
1.00
24.63
C

ATOM
4686
CG
GLU C
10
71.338
27.635
22.678
1.00
29.19
C

ATOM
4687
CD
GLU C
10
71.102
26.213
23.204
1.00
33.43
C

ATOM
4688
OE1
GLU C
10
70.758
25.307
22.400
1.00
35.21
C

ATOM
4689
OE2
GLU C
10
71.281
25.992
24.420
1.00
36.33
C

ATOM
4690
C
GLU C
10
71.186
31.221
24.133
1.00
23.12
C

ATOM
4691
O
GLU C
10
69.975
31.374
24.128
1.00
20.55
C

ATOM
4692
N
GLY C
11
72.008
32.064
24.756
1.00
25.05
C

ATOM
4693
CA
GLY C
11
71.491
33.228
25.458
1.00
26.75
C

ATOM
4694
C
GLY C
11
70.939
33.036
26.861
1.00
29.02
C

ATOM
4695
O
GLY C
11
70.676
34.022
27.557
1.00
28.98
C

ATOM
4696
N
GLU C
12
70.757
31.782
27.276
1.00
29.73
C

ATOM
4697
CA
GLU C
12
70.238
31.469
28.604
1.00
29.91
C

ATOM
4698
CB
GLU C
12
69.778
30.009
28.657
1.00
29.67
C

ATOM
4699
CG
GLU C
12
68.537
29.805
27.817
1.00
29.78
C

ATOM
4700
CD
GLU C
12
67.792
28.516
28.112
1.00
31.45
C

ATOM
4701
OE1
GLU C
12
68.320
27.419
27.801
1.00
31.80
C

ATOM
4702
OE2
GLU C
12
66.663
28.603
28.651
1.00
32.30
C

ATOM
4703
C
GLU C
12
71.231
31.769
29.730
1.00
31.37
C

ATOM
4704
O
GLU C
12
72.364
31.288
29.723
1.00
31.63
C

ATOM
4705
N
ARG C
13
70.793
32.579
30.693
1.00
32.45
C

ATOM
4706
CA
ARG C
13
71.642
32.983
31.807
1.00
33.31
C

ATOM
4707
CB
ARG C
13
71.215
34.341
32.335
1.00
33.47
C

ATOM
4708
CG
ARG C
13
70.328
35.124
31.392
1.00
35.00
C

ATOM
4709
CD
ARG C
13
69.909
36.383
32.092
1.00
35.56
C

ATOM
4710
NE
ARG C
13
71.082
37.195
32.375
1.00
39.21
C

ATOM
4711
CZ
ARG C
13
71.210
37.997
33.423
1.00
40.03
C

ATOM
4712
NH1
ARG C
13
70.231
38.093
34.310
1.00
39.27
C

ATOM
4713
NH2
ARG C
13
72.310
38.726
33.566
1.00
40.62
C

ATOM
4714
C
ARG C
13
71.607
31.997
32.949
1.00
33.28
C

ATOM
4715
O
ARG C
13
70.534
31.584
33.387
1.00
33.83
C

ATOM
4716
N
PHE C
14
72.790
31.626
33.431
1.00
33.28
C

ATOM
4717
CA
PHE C
14
72.916
30.692
34.545
1.00
32.01
C

ATOM
4718
CB
PHE C
14
73.791
29.488
34.180
1.00
32.03
C

ATOM
4719
CG
PHE C
14
73.173
28.552
33.175
1.00
32.79
C

ATOM
4720
CD1
PHE C
14
73.005
28.935
31.850
1.00
33.70
C

ATOM
4721
CD2
PHE C
14
72.815
27.256
33.545
1.00
32.47
C

ATOM
4722
CE1
PHE C
14
72.491
28.032
30.910
1.00
34.61
C

ATOM
4723
CE2
PHE C
14
72.301
26.349
32.620
1.00
30.80
C

ATOM
4724
CZ
PHE C
14
72.141
26.731
31.300
1.00
31.82
C

ATOM
4725
C
PHE C
14
73.560
31.394
35.733
1.00
31.30
C

ATOM
4726
O
PHE C
14
74.669
31.918
35.633
1.00
30.38
C

ATOM
4727
N
THR C
15
72.860
31.403
36.857
1.00
30.28
C

ATOM
4728
CA
THR C
15
73.387
32.013
38.066
1.00
29.27
C

ATOM
4729
CB
THR C
15
72.253
32.635
38.900
1.00
28.06
C

ATOM
4730
OG1
THR C
15
71.567
33.612
38.111
1.00
27.43
C

ATOM
4731
CG2
THR C
15
72.801
33.282
40.158
1.00
25.34
C

ATOM
4732
C
THR C
15
74.060
30.925
38.901
1.00
29.98
C

ATOM
4733
O
THR C
15
73.521
29.827
39.032
1.00
30.73
C

ATOM
4734
N
VAL C
16
75.244
31.211
39.435
1.00
30.04
C

ATOM
4735
CA
VAL C
16
75.943
30.254
40.291
1.00
31.88
C

ATOM
4736
CB
VAL C
16
76.853
29.283
39.491
1.00
32.07
C

ATOM
4737
CG1
VAL C
16
76.035
28.547
38.455
1.00
35.42
C

ATOM
4738
CG2
VAL C
16
77.988
30.034
38.823
1.00
34.64
C

ATOM
4739
C
VAL C
16
76.793
30.991
41.327
1.00
32.89
C

ATOM
4740
O
VAL C
16
77.097
32.176
41.168
1.00
32.60
C

ATOM
4741
N
ASP C
17
77.170
30.286
42.390
1.00
33.45
C

ATOM
4742
CA
ASP C
17
77.976
30.874
43.455
1.00
33.69
C

ATOM
4743
CB
ASP C
17
78.117
29.888
44.618
1.00
35.66
C

ATOM
4744
CG
ASP C
17
79.027
30.419
45.727
1.00
38.16
C

ATOM
4745
OD1
ASP C
17
78.721
31.520
46.269
1.00
38.20
C

ATOM
4746
OD2
ASP C
17
80.037
29.741
46.047
1.00
36.91
C

ATOM
4747
C
ASP C
17
79.347
31.221
42.911
1.00
33.45
C

ATOM
4748
O
ASP C
17
80.034
30.352
42.391
1.00
32.08
C

ATOM
4749
N
LYS C
18
79.768
32.475
43.045
1.00
35.48
C

ATOM
4750
CA
LYS C
18
81.068
32.853
42.495
1.00
39.15
C

ATOM
4751
CB
LYS C
18
81.378
34.325
42.766
1.00
40.50
C

ATOM
4752
CG
LYS C
18
81.886
34.630
44.144
1.00
45.70
C

ATOM
4753
CD
LYS C
18
82.169
36.128
44.285
1.00
48.13
C

ATOM
4754
CE
LYS C
18
83.245
36.589
43.318
1.00
48.38
C

ATOM
4755
NZ
LYS C
18
84.546
35.898
43.581
1.00
49.06
C

ATOM
4756
C
LYS C
18
82.212
31.978
42.993
1.00
38.99
C

ATOM
4757
O
LYS C
18
83.109
31.638
42.228
1.00
38.11
C

ATOM
4758
N
LYS C
19
82.177
31.596
44.263
1.00
39.59
C

ATOM
4759
CA
LYS C
19
83.232
30.759
44.813
1.00
38.98
C

ATOM
4760
CB
LYS C
19
82.940
30.429
46.274
0.00
39.52
C

ATOM
4761
CG
LYS C
19
84.077
29.703
46.968
0.00
40.25
C

ATOM
4762
CD
LYS C
19
83.738
29.363
48.404
0.00
40.84
C

ATOM
4763
CE
LYS C
19
82.586
28.380
48.468
0.00
41.18
C

ATOM
4764
NZ
LYS C
19
82.206
28.077
49.871
0.00
41.44
C

ATOM
4765
C
LYS C
19
83.364
29.470
44.010
1.00
38.49
C

ATOM
4766
O
LYS C
19
84.475
29.025
43.725
1.00
37.49
C

ATOM
4767
N
ILE C
20
82.223
28.877
43.651
1.00
39.86
C

ATOM
4768
CA
ILE C
20
82.167
27.631
42.858
1.00
40.16
C

ATOM
4769
CB
ILE C
20
80.725
27.037
42.836
1.00
39.38
C

ATOM
4770
CG2
ILE C
20
80.705
25.698
42.109
1.00
38.50
C

ATOM
4771
CG1
ILE C
20
80.225
26.858
44.270
1.00
39.70
C

ATOM
4772
CD1
ILE C
20
78.801
26.351
44.371
1.00
41.15
C

ATOM
4773
C
ILE C
20
82.588
27.949
41.421
1.00
40.51
C

ATOM
4774
O
ILE C
20
83.424
27.272
40.841
1.00
39.84
C

ATOM
4775
N
ALA C
21
81.999
28.999
40.865
1.00
41.64
C

ATOM
4776
CA
ALA C
21
82.312
29.423
39.524
1.00
43.06
C

ATOM
4777
CB
ALA C
21
81.635
30.753
39.229
1.00
43.43
C

ATOM
4778
C
ALA C
21
83.818
29.554
39.349
1.00
43.95
C

ATOM
4779
O
ALA C
21
84.353
29.186
38.307
1.00
45.27
C

ATOM
4780
N
GLU C
22
84.506
30.090
40.354
1.00
44.60
C

ATOM
4781
CA
GLU C
22
85.958
30.254
40.266
1.00
44.95
C

ATOM
4782
CB
GLU C
22
86.546
30.773
41.582
1.00
47.05
C

ATOM
4783
CG
GLU C
22
86.200
32.217
41.915
1.00
50.65
C

ATOM
4784
CD
GLU C
22
87.063
32.769
43.035
1.00
52.85
C

ATOM
4785
OE1
GLU C
22
87.098
32.164
44.125
1.00
54.88
C

ATOM
4786
OE2
GLU C
22
87.716
33.809
42.826
1.00
54.85
C

ATOM
4787
C
GLU C
22
86.652
28.949
39.898
1.00
43.86
C

ATOM
4788
O
GLU C
22
87.851
28.933
39.637
1.00
43.78
C

ATOM
4789
N
ARG C
23
85.912
27.849
39.893
1.00
42.42
C

ATOM
4790
CA
ARG C
23
86.498
26.576
39.517
1.00
42.71
C

ATOM
4791
CB
ARG C
23
85.442
25.496
39.602
1.00
43.00
C

ATOM
4792
CG
ARG C
23
85.870
24.197
39.043
1.00
44.32
C

ATOM
4793
CD
ARG C
23
86.100
23.258
40.161
1.00
46.65
C

ATOM
4794
NE
ARG C
23
87.502
23.204
40.508
1.00
47.94
C

ATOM
4795
CZ
ARG C
23
87.967
22.532
41.548
1.00
48.45
C

ATOM
4796
NE1
ARG C
23
87.122
21.875
42.338
1.00
46.40
C

ATOM
4797
NH2
ARG C
23
89.274
22.493
41.768
1.00
50.58
C

ATOM
4798
C
ARG C
23
86.956
26.742
38.072
1.00
42.33
C

ATOM
4799
O
ARG C
23
87.703
25.926
37.536
1.00
41.75
C

ATOM
4800
N
SER C
24
86.461
27.812
37.458
1.00
42.76
C

ATOM
4801
CA
SER C
24
86.773
28.177
36.087
1.00
43.35
C

ATOM
4802
CB
SER C
24
85.531
28.757
35.406
1.00
42.29
C

ATOM
4803
OC
SER C
24
85.845
29.241
34.116
1.00
39.65
C

ATOM
4804
C
SER C
24
87.868
29.235
36.113
1.00
44.08
C

ATOM
4805
O
SER C
24
87.591
30.403
36.361
1.00
44.37
C

ATOM
4806
N
LEU C
25
89.109
28.830
35.875
1.00
45.48
C

ATOM
4807
CA
LEU C
25
90.217
29.773
35.875
1.00
47.35
C

ATOM
4808
CB
LEU C
25
91.490
29.117
35.350
1.00
48.27
C

ATOM
4809
CG
LEU C
25
92.107
28.027
36.219
1.00
48.77
C

ATOM
4810
CD1
LEU C
25
93.392
27.506
35.595
0.00
48.78
C

ATOM
4811
CD2
LEU C
25
92.365
28.610
37.598
1.00
48.53
C

ATOM
4812
C
LEU C
25
89.871
30.932
34.979
1.00
48.70
C

ATOM
4813
O
LEU C
25
90.293
32.064
35.233
1.00
48.05
C

ATOM
4814
N
LEU C
26
89.116
30.635
33.919
1.00
50.30
C

ATOM
4815
CA
LEU C
26
88.703
31.658
32.956
1.00
50.59
C

ATOM
4816
CB
LEU C
26
87.901
31.046
31.787
1.00
50.13
C

ATOM
4817
CG
LEU C
26
87.543
31.994
30.621
1.00
49.31
C

ATOM
4818
CD1
LEU C
26
88.810
32.356
29.880
1.00
49.37
C

ATOM
4819
CD2
LEU C
26
86.542
31.346
29.655
1.00
49.24
C

ATOM
4820
C
LEU C
26
87.857
32.687
33.689
1.00
50.59
C

ATOM
4821
O
LEU C
26
88.005
33.888
33.478
1.00
50.43
C

ATOM
4822
N
LEU C
27
86.980
32.210
34.562
1.00
51.20
C

ATOM
4823
CA
LEU C
27
86.132
33.103
35.325
1.00
53.37
C

ATOM
4824
CB
LEU C
27
84.930
32.324
35.871
1.00
54.39
C

ATOM
4825
CG
LEU C
27
83.811
33.095
36.583
1.00
55.55
C

ATOM
4826
CD1
LEU C
27
84.258
33.408
37.990
1.00
56.54
C

ATOM
4827
CD2
LEU C
27
83.445
34.376
35.817
1.00
55.58
C

ATOM
4828
C
LEU C
27
86.947
33.775
36.446
1.00
54.11
C

ATOM
4829
O
LEU C
27
86.669
34.918
36.822
1.00
54.13
C

ATOM
4830
N
LYS C
28
87.960
33.077
36.961
1.00
54.29
C

ATOM
4831
CA
LYS C
28
88.816
33.650
37.993
1.00
54.46
C

ATOM
4832
CB
LYS C
28
89.825
32.623
38.506
1.00
54.18
C

ATOM
4833
CG
LYS C
28
89.252
31.586
39.446
1.00
54.09
C

ATOM
4834
CD
LYS C
28
90.359
30.727
40.048
0.00
54.84
C

ATOM
4835
CE
LYS C
28
91.404
31.584
40.756
0.00
55.16
C

ATOM
4836
NZ
LYS C
28
90.817
32.412
41.846
0.00
55.54
C

ATOM
4837
C
LYS C
28
89.565
34.851
37.408
1.00
55.03
C

ATOM
4838
O
LYS C
28
89.502
35.943
37.956
1.00
54.89
C

ATOM
4839
N
ASN C
29
90.269
34.657
36.295
1.00
56.14
C

ATOM
4840
CA
ASN C
29
91.006
35.758
35.671
1.00
57.16
C

ATOM
4841
CB
ASN C
29
91.659
35.319
34.354
1.00
57.83
C

ATOM
4842
CG
ASN C
29
92.642
34.173
34.532
1.00
58.99
C

ATOM
4843
OD1
ASN C
29
93.170
33.633
33.558
1.00
59.61
C

ATOM
4844
ND2
ASN C
29
92.895
33.800
35.776
1.00
59.68
C

ATOM
4845
C
ASN C
29
90.071
36.923
35.375
1.00
57.45
C

ATOM
4846
O
ASN C
29
90.455
38.079
35.525
1.00
57.22
C

ATOM
4847
N
TYR C
30
88.849
36.620
34.943
1.00
57.89
C

ATOM
4848
CA
TYR C
30
87.882
37.664
34.615
1.00
58.66
C

ATOM
4849
CB
TYR C
30
86.516
37.039
34.317
1.00
57.87
C

ATOM
4850
CG
TYR C
30
85.636
37.872
33.409
1.00
56.71
C

ATOM
4851
CD1
TYR C
30
86.054
38.229
32.133
1.00
55.67
C

ATOM
4852
CE1
TYR C
30
85.231
38.968
31.282
1.00
55.50
C

ATOM
4853
CD2
TYR C
30
84.373
38.276
33.818
1.00
56.61
C

ATOM
4854
CE2
TYR C
30
83.539
39.014
32.979
1.00
56.59
C

ATOM
4855
CZ
TYR C
30
83.972
39.355
31.712
1.00
56.92
C

ATOM
4856
OH
TYR C
30
83.132
40.065
30.873
1.00
57.63
C

ATOM
4857
C
TYR C
30
87.787
38.649
35.783
1.00
60.59
C

ATOM
4858
O
TYR C
30
87.482
39.830
35.590
1.00
59.71
C

ATOM
4859
N
LEU C
31
88.062
38.146
36.989
1.00
62.33
C

ATOM
4860
CA
LEU C
31
88.047
38.932
38.230
1.00
62.29
C

ATOM
4861
CB
LEU C
31
89.371
39.712
38.370
1.00
62.08
C

ATOM
4862
CG
LEU C
31
89.853
40.603
37.215
1.00
61.04
C

ATOM
4863
CO1
LEU C
31
89.303
42.000
37.370
1.00
60.84
C

ATOM
4864
CD2
LEU C
31
91.363
40.639
37.205
1.00
61.22
C

ATOM
4865
C
LEU C
31
86.860
39.875
38.358
1.00
62.55
C

ATOM
4866
O
LEU C
31
85.754
39.555
37.917
1.00
63.88
C

ATOM
4867
N
ILE C
45
80.545
40.215
37.240
1.00
45.54
C

ATOM
4868
CA
ILE C
45
79.354
39.523
37.719
1.00
45.75
C

ATOM
4869
CB
ILE C
45
78.323
40.511
38.318
1.00
46.06
C

ATOM
4870
CG2
ILE C
45
77.704
41.376
37.213
1.00
43.89
C

ATOM
4871
CG1
ILE C
45
77.248
39.723
39.075
1.00
46.70
C

ATOM
4872
CD1
ILE C
45
76.128
40.574
39.614
1.00
48.94
C

ATOM
4873
C
ILE C
45
78.665
38.702
36.617
1.00
45.24
C

ATOM
4874
O
ILE C
45
78.069
37.659
36.904
1.00
45.32
C

ATOM
4875
N
VAL C
46
78.758
39.158
35.364
1.00
43.40
C

ATOM
4876
CA
VAL C
46
78.154
38.438
34.237
1.00
41.39
C

ATOM
4877
CB
VAL C
46
76.974
39.226
33.613
1.00
41.64
C

ATOM
4878
CG1
VAL C
46
76.308
38.378
32.531
1.00
41.02
C

ATOM
4879
CG2
VAL C
46
75.962
39.604
34.690
1.00
41.38
C

ATOM
4880
C
VAL C
46
79.154
38.131
33.123
1.00
39.66
C

ATOM
4881
O
VAL C
46
79.480
39.005
32.318
1.00
40.66
C

ATOM
4882
N
MSE C
47
79.635
36.892
33.071
1.00
38.75
C

ATOM
4883
CA
MSE C
47
80.597
36.501
32.039
1.00
37.26
C

ATOM
4884
CB
MSE C
47
81.753
35.691
32.641
1.00
38.19
C

ATOM
4885
CG
MSE C
47
82.901
35.488
31.668
1.00
40.50
C

ATOM
4886
SE
MSE C
47
84.215
34.179
32.219
1.00
47.69
C

ATOM
4887
CE
MSE C
47
83.332
32.527
31.723
1.00
41.93
C

ATOM
4888
C
MSE C
47
79.924
35.669
30.954
1.00
34.30
C

ATOM
4889
O
MSE C
47
79.108
34.793
31.246
1.00
32.32
C

ATOM
4890
N
PRO C
48
80.240
35.954
29.682
1.00
32.53
C

ATOM
4891
CD
PRO C
48
80.789
37.227
29.204
1.00
31.72
C

ATOM
4892
CA
PRO C
48
79.655
35.207
28.566
1.00
32.32
C

ATOM
4893
CB
PRO C
48
79.787
36.176
27.389
1.00
31.12
C

ATOM
4894
CG
PRO C
48
79.872
37.514
28.049
1.00
31.73
C

ATOM
4895
C
PRO C
48
80.408
33.895
28.302
1.00
31.55
C

ATOM
4896
O
PRO C
48
81.615
33.809
28.506
1.00
32.35
C

ATOM
4897
N
VAL C
49
79.696
32.864
27.874
1.00
30.22
C

ATOM
4898
CA
VAL C
49
80.347
31.609
27.553
1.00
29.45
C

ATOM
4899
CB
VAL C
49
79.832
30.440
28.418
1.00
30.65
C

ATOM
4900
CG1
VAL C
49
80.731
29.222
28.234
1.00
29.09
C

ATOM
4901
CG2
VAL C
49
79.803
30.851
29.872
1.00
31.28
C

ATOM
4902
C
VAL C
49
79.958
31.389
26.105
1.00
28.38
C

ATOM
4903
O
VAL C
49
79.011
30.660
25.798
1.00
28.07
C

ATOM
4904
N
PRO C
50
80.673
32.049
25.191
1.00
27.28
C

ATOM
4905
CD
PRO C
50
81.736
33.036
25.433
1.00
27.20
C

ATOM
4906
CA
PRO C
50
80.410
31.937
23.765
1.00
26.24
C

ATOM
4907
CB
PRO C
50
81.504
32.810
23.158
1.00
26.55
C

ATOM
4908
CG
PRO C
50
81.687
33.866
24.182
1.00
25.75
C

ATOM
4909
C
PRO C
50
80.426
30.516
23.202
1.00
26.07
C

ATOM
4910
O
PRO C
50
81.292
29.698
23.529
1.00
25.12
C

ATOM
4911
N
ASN C
51
79.447
30.247
22.347
1.00
25.23
C

ATOM
4912
CA
ASN C
51
79.317
28.975
21.668
1.00
25.26
C

ATOM
4913
CB
ASN C
51
80.446
28.820
20.660
1.00
26.35
C

ATOM
4914
CG
ASN C
51
80.554
30.005
19.737
1.00
27.98
C

ATOM
4915
OD1
ASN C
51
79.567
30.413
19.116
1.00
28.79
C

ATOM
4916
ND2
ASN C
51
81.752
30.578
19.644
1.00
27.02
C

ATOM
4917
C
ASN C
51
79.299
27.762
22.558
1.00
24.62
C

ATOM
4918
O
ASN C
51
80.090
26.861
22.374
1.00
25.28
C

ATOM
4919
N
VAL C
52
78.388
27.726
23.510
1.00
25.26
C

ATOM
4920
CA
VAL C
52
78.284
26.592
24.395
1.00
25.46
C

ATOM
4921
CB
VAL C
52
78.983
26.866
25.714
1.00
27.00
C

ATOM
4922
CG1
VAL C
52
78.759
25.698
26.668
1.00
26.64
C

ATOM
4923
CG2
VAL C
52
80.473
27.098
25.487
1.00
27.68
C

ATOM
4924
C
VAL C
52
76.808
26.404
24.685
1.00
27.92
C

ATOM
4925
O
VAL C
52
76.181
27.275
25.305
1.00
30.25
C

ATOM
4926
N
ARG C
53
76.246
25.278
24.249
1.00
28.81
C

ATOM
4927
CA
ARG C
53
74.824
25.012
24.478
1.00
29.52
C

ATOM
4928
CB
ARG C
53
74.393
23.688
23.845
1.00
32.39
C

ATOM
4929
CG
ARG C
53
74.401
23.661
22.337
1.00
37.27
C

ATOM
4930
CD
ARG C
53
73.908
22.307
21.839
1.00
42.50
C

ATOM
4931
NE
ARG C
53
74.746
21.181
22.276
1.00
47.26
C

ATOM
4932
CZ
ARG C
53
74.285
20.079
22.871
1.00
49.64
C

ATOM
4933
NH1
ARG C
53
72.984
19.945
23.114
1.00
48.76
C

ATOM
4934
NH2
ARG C
53
75.126
19.106
23.216
1.00
50.78
C

ATOM
4935
C
ARG C
53
74.465
24.959
25.964
1.00
28.83
C

ATOM
4936
O
ARG C
53
75.226
24.471
26.794
1.00
27.65
C

ATOM
4937
N
SER C
54
73.274
25.454
26.268
1.00
27.01
C

ATOM
4938
CA
SER C
54
72.769
25.467
27.613
1.00
24.06
C

ATOM
4939
CB
SER C
54
71.302
25.871
27.612
1.00
22.38
C

ATOM
4940
OC
SER C
54
71.159
27.162
27.056
1.00
20.31
C

ATOM
4941
C
SER C
54
72.946
24.093
28.246
1.00
24.61
C

ATOM
4942
O
SER C
54
73.676
23.948
29.223
1.00
26.72
C

ATOM
4943
N
SER C
55
72.306
23.071
27.698
1.00
23.42
C

ATOM
4944
CA
SER C
55
72.455
21.735
28.268
1.00
22.33
C

ATOM
4945
CB
SER C
55
71.922
20.684
27.304
1.00
19.49
C

ATOM
4946
OG
SER C
55
72.598
20.765
26.075
1.00
22.52
C

ATOM
4947
C
SER C
55
73.909
21.414
28.610
1.00
21.51
C

ATOM
4948
O
SER C
55
74.168
20.766
29.613
1.00
23.53
C

ATOM
4949
N
VAL C
56
74.851
21.884
27.795
1.00
20.84
C

ATOM
4950
CA
VAL C
56
76.274
21.624
28.031
1.00
20.83
C

ATOM
4951
CB
VAL C
56
77.137
21.998
26.757
1.00
20.76
C

ATOM
4952
CG1
VAL C
56
78.593
21.624
26.953
1.00
16.97
C

ATOM
4953
CG2
VAL C
56
76.583
21.284
25.514
1.00
20.88
C

ATOM
4954
C
VAL C
56
76.768
22.418
29.260
1.00
19.61
C

ATOM
4955
O
VAL C
56
77.375
21.849
30.172
1.00
18.87
C

ATOM
4956
N
LEU C
57
76.515
23.724
29.271
1.00
19.82
C

ATOM
4957
CA
LEU C
57
76.906
24.588
30.379
1.00
20.45
C

ATOM
4958
CB
LEU C
57
76.487
26.026
30.075
1.00
17.81
C

ATOM
4959
CG
LEU C
57
76.896
27.099
31.084
1.00
15.76
C

ATOM
4960
CD1
LEU C
57
78.375
27.066
31.281
1.00
14.13
C

ATOM
4961
CD2
LEU C
57
76.451
28.463
30.589
1.00
17.83
C

ATOM
4962
C
LEU C
57
76.231
24.116
31.678
1.00
21.81
C

ATOM
4963
O
LEU C
57
76.842
24.076
32.744
1.00
22.15
C

ATOM
4964
N
GLN C
58
74.956
23.777
31.588
1.00
22.64
C

ATOM
4965
CA
GLN C
58
74.255
23.311
32.757
1.00
24.92
C

ATOM
4966
CB
GLN C
58
72.811
22.991
32.418
1.00
25.24
C

ATOM
4967
CG
GLN C
58
72.079
22.366
33.567
1.00
27.25
C

ATOM
4968
CD
GLN C
58
70.636
22.144
33.271
1.00
28.40
C

ATOM
4969
OE1
GLN C
58
70.047
21.177
33.740
1.00
31.18
C

ATOM
4970
NE2
GLN C
58
70.043
23.041
32.500
1.00
29.28
C

ATOM
4971
C
GLN C
58
74.938
22.065
33.282
1.00
26.17
C

ATOM
4972
O
GLN C
58
75.060
21.872
34.487
1.00
27.72
C

ATOM
4973
N
LYS C
59
75.375
21.209
32.373
1.00
27.32
C

ATOM
4974
CA
LYS C
59
76.047
19.990
32.771
1.00
29.09
C

ATOM
4975
CB
LYS C
59
76.229
19.093
31.549
1.00
29.32
C

ATOM
4976
CG
LYS C
59
76.548
17.651
31.869
1.00
32.80
C

ATOM
4977
CD
LYS C
59
75.309
16.788
31.972
1.00
32.66
C

ATOM
4978
CE
LYS C
59
75.708
15.346
32.280
1.00
34.41
C

ATOM
4979
NZ
LYS C
59
74.566
14.374
32.116
1.00
36.74
C

ATOM
4980
C
LYS C
59
77.406
20.346
33.412
1.00
31.23
C

ATOM
4981
O
LYS C
59
77.793
19.750
34.418
1.00
32.05
C

ATOM
4982
N
VAL C
60
78.116
21.320
32.837
1.00
31.14
C

ATOM
4983
CA
VAL C
60
79.416
21.769
33.350
1.00
30.44
C

ATOM
4984
CB
VAL C
60
80.022
22.893
32.461
1.00
30.16
C

ATOM
4985
CG1
VAL C
60
81.236
23.514
33.139
1.00
28.33
C

ATOM
4986
CG2
VAL C
60
80.422
22.325
31.109
1.00
32.07
C

ATOM
4987
C
VAL C
60
79.310
22.314
34.767
1.00
31.68
C

ATOM
4988
O
VAL C
60
80.078
21.953
35.650
1.00
32.71
C

ATOM
4989
N
ILE C
61
78.356
23.204
34.969
1.00
32.12
C

ATOM
4990
CA
ILE C
61
78.140
23.804
36.262
1.00
31.24
C

ATOM
4991
CB
ILE C
61
77.021
24.824
36.170
1.00
31.54
G

ATOM
4992
CG2
ILE C
61
76.601
25.279
37.564
1.00
28.63
G

ATOM
4993
CG1
ILE C
61
77.497
25.982
35.297
1.00
31.49
G

ATOM
4994
CD1
ILE C
61
76.388
26.850
34.795
1.00
32.68
G

ATOM
4995
C
ILE C
61
77.780
22.749
37.289
1.00
31.52
G

ATOM
4996
O
ILE C
61
78.360
22.707
38.368
1.00
31.59
G

ATOM
4997
N
GLU G
62
76.836
21.881
36.955
1.00
31.93
G

ATOM
4998
CA
GLU G
62
76.443
20.861
37.907
1.00
33.23
G

ATOM
4999
CB
GLU G
62
75.295
20.025
37.375
1.00
32.43
G

ATOM
5000
CG
GLU G
62
75.721
18.813
36.636
1.00
34.09
G

ATOM
5001
CD
GLU G
62
74.649
17.762
36.649
1.00
35.90
G

ATOM
5002
OE1
GLU G
62
74.307
17.292
37.757
1.00
35.78
G

ATOM
5003
OE2
GLU G
62
74.143
17.408
35.558
1.00
37.89
G

ATOM
5004
C
GLU G
62
77.595
19.939
38.278
1.00
33.56
G

ATOM
5005
O
GLU G
62
77.462
19.096
39.161
1.00
34.70
G

ATOM
5006
N
TRP C
63
78.717
20.086
37.593
1.00
33.45
G

ATOM
5007
CA
TRP C
63
79.872
19.269
37.888
1.00
33.70
G

ATOM
5008
CB
TRP C
63
80.670
18.991
36.622
1.00
33.66
G

ATOM
5009
CG
TRP C
63
81.955
18.280
36.884
1.00
33.52
G

ATOM
5010
CD2
TRP C
63
83.211
18.876
37.231
1.00
32.28
G

ATOM
5011
CE2
TRP C
63
84.142
17.826
37.386
1.00
32.37
G

ATOM
5012
CE3
TRP C
63
83.639
20.196
37.429
1.00
31.95
G

ATOM
5013
CD1
TRP C
63
82.167
16.935
36.846
1.00
34.55
G

ATOM
5014
NE1
TRP C
63
83.481
16.653
37.143
1.00
34.74
G

ATOM
5015
CZ2
TRP C
63
85.476
18.049
37.726
1.00
32.07
G

ATOM
5016
CZ3
TRP C
63
84.965
20.424
37.768
1.00
31.44
G

ATOM
5017
CH2
TRP C
63
85.871
19.351
37.914
1.00
32.65
G

ATOM
5018
C
TRP C
63
80.726
20.067
38.853
1.00
34.67
G

ATOM
5019
O
TRP C
63
81.367
19.512
39.733
1.00
36.11
G

ATOM
5020
N
ALA C
64
80.737
21.380
38.686
1.00
36.01
C

ATOM
5021
CA
ALA C
64
81.537
22.234
39.551
1.00
38.09
C

ATOM
5022
CB
ALA C
64
81.604
23.652
38.975
1.00
38.34
C

ATOM
5023
C
ALA C
64
80.954
22.270
40.954
1.00
38.84
C

ATOM
5024
O
ALA C
64
81.653
22.010
41.928
1.00
40.17
C

ATOM
5025
N
GLU C
65
79.670
22.605
41.045
1.00
39.31
C

ATOM
5026
CA
GLU C
65
78.981
22.675
42.322
1.00
39.42
C

ATOM
5027
CB
GLU C
65
77.483
22.928
42.099
1.00
37.23
C

ATOM
5028
CG
GLU C
65
77.202
24.210
41.330
1.00
34.34
C

ATOM
5029
CD
GLU C
65
75.724
24.533
41.190
1.00
33.67
C

ATOM
5030
OE1
GLU C
65
74.926
23.651
40.805
1.00
33.23
C

ATOM
5031
OE2
GLU C
65
75.356
25.688
41.455
1.00
33.33
C

ATOM
5032
C
GLU C
65
79.196
21.376
43.101
1.00
41.07
C

ATOM
5033
O
GLU C
65
79.379
21.406
44.315
1.00
41.60
C

ATOM
5034
N
HIS C
66
79.190
20.240
42.403
1.00
42.63
C

ATOM
5035
CA
HIS C
66
79.391
18.944
43.059
1.00
44.78
C

ATOM
5036
CB
HIS C
66
78.988
17.796
42.119
1.00
44.20
C

ATOM
5037
CG
HIS C
66
79.334
16.420
42.622
1.00
44.62
C

ATOM
5038
CD2
HIS C
66
78.548
15.363
42.937
1.00
43.92
C

ATOM
5039
ND1
HIS C
66
80.634
15.972
42.740
1.00
45.83
C

ATOM
5040
CE1
HIS C
66
80.633
14.699
43.095
1.00
43.67
C

ATOM
5041
NE2
HIS C
66
79.379
14.305
43.221
1.00
42.62
C

ATOM
5042
C
HIS C
66
80.823
18.750
43.544
1.00
46.51
C

ATOM
5043
O
HIS C
66
81.063
18.025
44.505
1.00
47.99
C

ATOM
5044
N
HIS C
67
81.781
19.393
42.894
1.00
47.66
C

ATOM
5045
CA
HIS C
67
83.163
19.249
43.321
1.00
49.37
C

ATOM
5046
CB
HIS C
67
84.059
18.952
42.127
1.00
50.68
C

ATOM
5047
CG
HIS C
67
83.964
17.541
41.652
1.00
52.46
C

ATOM
5048
CD2
HIS C
67
83.878
16.378
42.337
1.00
53.35
C

ATOM
5049
ND1
HIS C
67
83.926
17.205
40.318
1.00
54.03
C

ATOM
5050
CE1
HIS C
67
83.815
15.894
40.199
1.00
53.47
C

ATOM
5051
NE2
HIS C
67
83.783
15.369
41.410
1.00
54.73
C

ATOM
5052
C
HIS C
67
83.634
20.496
44.013
1.00
50.00
C

ATOM
5053
O
HIS C
67
84.831
20.793
44.022
1.00
49.65
C

ATOM
5054
N
ARG C
68
82.685
21.219
44.603
1.00
50.89
C

ATOM
5055
CA
ARG C
68
82.996
22.468
45.295
1.00
52.52
C

ATOM
5056
CB
ARG C
68
81.721
23.137
45.804
1.00
51.55
C

ATOM
5057
CG
ARG C
68
80.882
22.281
46.708
1.00
51.00
C

ATOM
5058
CD
ARG C
68
79.609
23.021
47.114
1.00
51.32
C

ATOM
5059
NE
ARG C
68
78.436
22.163
46.984
1.00
50.65
C

ATOM
5060
CZ
ARG C
68
78.319
20.978
47.571
1.00
49.83
C

ATOM
5061
NH1
ARG C
68
79.299
20.514
48.331
1.00
53.30
C

ATOM
5062
NH2
ARG C
68
77.232
20.249
47.391
1.00
50.27
C

ATOM
5063
C
ARG C
68
83.967
22.310
46.442
1.00
53.96
C

ATOM
5064
O
ARG C
68
84.685
23.243
46.784
1.00
54.35
C

ATOM
5065
N
ASP C
69
83.993
21.134
47.046
1.00
56.66
C

ATOM
5066
CA
ASP C
69
84.905
20.921
48.150
1.00
59.49
C

ATOM
5067
CB
ASP C
69
84.147
20.357
49.361
1.00
58.83
C

ATOM
5068
CG
ASP C
69
82.957
21.232
49.774
1.00
58.82
C

ATOM
5069
OD1
ASP C
69
83.161
22.430
50.067
1.00
57.19
C

ATOM
5070
OD2
ASP C
69
81.814
20.718
49.806
1.00
58.80
C

ATOM
5071
C
ASP C
69
86.032
19.986
47.722
1.00
61.81
C

ATOM
5072
O
ASP C
69
87.029
19.849
48.426
1.00
64.04
C

ATOM
5073
N
SER C
70
85.890
19.355
46.561
1.00
62.80
C

ATOM
5074
CA
SER C
70
86.928
18.445
46.089
1.00
63.95
C

ATOM
5075
CB
SER C
70
86.501
17.796
44.777
1.00
64.08
C

ATOM
5076
OG
SER C
70
85.355
16.996
44.990
1.00
65.02
C

ATOM
5077
C
SER C
70
88.264
19.161
45.914
1.00
64.84
C

ATOM
5078
O
SER C
70
88.305
20.371
45.697
1.00
65.35
C

ATOM
5079
N
ASN C
71
89.360
18.418
46.029
1.00
65.33
C

ATOM
5080
CA
ASN C
71
90.678
19.015
45.878
1.00
65.77
C

ATOM
5081
CB
ASN C
71
91.549
18.684
47.091
1.00
67.38
C

ATOM
5082
CG
ASN C
71
90.805
18.874
48.409
1.00
70.03
C

ATOM
5083
OD1
ASN C
71
90.234
19.943
48.673
1.00
70.29
C

ATOM
5084
ND2
ASN C
71
90.807
17.832
49.246
1.00
70.86
C

ATOM
5085
C
ASN C
71
91.311
18.488
44.603
1.00
65.48
C

ATOM
5086
O
ASN C
71
91.311
17.280
44.351
1.00
65.01
C

ATOM
5087
N
PHE C
72
91.830
19.404
43.792
1.00
64.80
C

ATOM
5088
CA
PHE C
72
92.463
19.045
42.529
1.00
64.53
C

ATOM
5089
CB
PHE C
72
91.585
19.473
41.342
1.00
60.50
C

ATOM
5090
CG
PHE C
72
90.272
18.736
41.247
1.00
55.74
C

ATOM
5091
CD1
PHE C
72
89.068
19.433
41.235
1.00
53.23
C

ATOM
5092
CD2
PHE C
72
90.238
17.349
41.154
1.00
52.78
C

ATOM
5093
CE1
PHE C
72
87.856
18.758
41.127
1.00
51.24
C

ATOM
5094
CE2
PHE C
72
89.027
16.672
41.047
1.00
50.62
C

ATOM
5095
CZ
PHE C
72
87.837
17.378
41.034
1.00
50.12
C

ATOM
5096
C
PHE C
72
93.818
19.728
42.417
1.00
66.62
C

ATOM
5097
O
PHE C
72
93.940
20.918
42.709
1.00
67.09
C

ATOM
5098
N
PRO C
73
94.853
18.981
41.988
1.00
68.12
C

ATOM
5099
CD
PRO C
73
94.775
17.557
41.611
1.00
68.63
C

ATOM
5100
CA
PRO C
73
96.220
19.493
41.823
1.00
68.91
C

ATOM
5101
CB
PRO C
73
96.935
18.342
41.118
1.00
69.55
C

ATOM
5102
CG
PRO C
73
96.219
17.133
41.636
1.00
69.28
C

ATOM
5103
C
PRO C
73
96.257
20.778
40.990
1.00
69.17
C

ATOM
5104
O
PRO C
73
96.598
21.853
41.487
1.00
69.84
C

ATOM
5105
N
VAL C
86
90.900
7.286
36.371
1.00
88.13
C

ATOM
5106
CA
VAL C
86
90.597
6.804
37.711
1.00
88.42
C

ATOM
5107
CB
VAL C
86
91.894
6.677
38.553
1.00
87.81
C

ATOM
5108
CG1
VAL C
86
92.562
5.342
38.273
0.00
87.97
C

ATOM
5109
CG2
VAL C
86
92.855
7.813
38.214
1.00
86.72
C

ATOM
5110
C
VAL C
86
89.573
7.685
38.445
1.00
88.62
C

ATOM
5111
O
VAL C
86
89.901
8.362
39.423
1.00
88.93
C

ATOM
5112
N
ASP C
87
88.328
7.661
37.964
1.00
88.31
C

ATOM
5113
CA
ASP C
87
87.230
8.443
38.547
1.00
87.51
C

ATOM
5114
CB
ASP C
87
86.568
9.310
37.475
0.00
88.63
C

ATOM
5115
CG
ASP C
87
87.538
10.229
36.783
1.00
89.65
C

ATOM
5116
OD1
ASP C
87
87.832
11.313
37.331
1.00
90.42
C

ATOM
5117
OD2
ASP C
87
88.011
9.859
35.688
1.00
89.70
C

ATOM
5118
C
ASP C
87
86.150
7.559
39.166
1.00
86.41
C

ATOM
5119
O
ASP C
87
86.396
6.413
39.543
0.00
86.24
C

ATOM
5120
N
SER C
88
84.944
8.110
39.245
1.00
84.26
C

ATOM
5121
CA
SER C
88
83.803
7.402
39.800
1.00
82.05
C

ATOM
5122
CB
SER C
88
83.872
7.398
41.324
1.00
81.81
C

ATOM
5123
OG
SER C
88
82.634
6.987
41.874
1.00
81.31
C

ATOM
5124
C
SER C
88
82.508
8.067
39.360
1.00
80.69
C

ATOM
5125
O
SER C
88
81.919
7.704
38.342
1.00
81.28
C

ATOM
5126
N
TRP C
89
82.066
9.042
40.144
1.00
77.91
C

ATOM
5127
CA
TRP C
89
80.848
9.780
39.848
1.00
74.10
C

ATOM
5128
CB
TRP C
89
80.646
10.859
40.905
1.00
73.48
C

ATOM
5129
CG
TRP C
89
79.446
11.708
40.702
1.00
72.20
C

ATOM
5130
CD2
TRP C
89
79.428
13.044
40.197
1.00
71.86
C

ATOM
5131
CE2
TRP C
89
78.088
13.476
40.209
1.00
71.45
C

ATOM
5132
CE3
TRP C
89
80.418
13.919
39.735
1.00
71.66
C

ATOM
5133
CD1
TRP C
89
78.153
11.388
40.988
1.00
71.28
C

ATOM
5134
NE1
TRP C
89
77.329
12.446
40.698
1.00
70.67
C

ATOM
5135
CZ2
TRP C
89
77.711
14.750
39.780
1.00
71.55
C

ATOM
5136
CZ3
TRP C
89
80.043
15.184
39.308
1.00
71.26
C

ATOM
5137
CH2
TRP C
89
78.701
15.587
39.334
1.00
71.21
C

ATOM
5138
C
TRP C
89
80.995
10.415
38.473
1.00
72.28
C

ATOM
5139
O
TRP C
89
80.021
10.567
37.740
1.00
72.30
C

ATOM
5140
N
ASP C
90
82.229
10.779
38.136
1.00
70.00
C

ATOM
5141
CA
ASP C
90
82.543
11.389
36.848
1.00
67.79
C

ATOM
5142
CB
ASP C
90
84.011
11.810
36.808
1.00
64.52
C

ATOM
5143
CG
ASP C
90
84.300
13.010
37.685
1.00
61.24
C

ATOM
5144
OD1
ASP C
90
83.453
13.363
38.530
1.00
59.13
C

ATOM
5145
OD2
ASP C
90
85.388
13.594
37.533
1.00
58.53
C

ATOM
5146
C
ASP C
90
82.261
10.436
35.691
1.00
67.74
C

ATOM
5147
O
ASP C
90
81.888
10.868
34.597
1.00
68.39
C

ATOM
5148
N
ARG C
91
82.460
9.142
35.926
1.00
67.23
C

ATOM
5149
CA
ARG C
91
82.197
8.140
34.895
1.00
66.43
C

ATOM
5150
CB
ARG C
91
82.671
6.755
35.345
0.00
67.74
C

ATOM
5151
CG
ARG C
91
82.250
5.602
34.429
0.00
69.73
C

ATOM
5152
CD
ARG C
91
82.769
5.731
32.997
0.00
71.43
C

ATOM
5153
NE
ARG C
91
81.880
6.509
32.132
1.00
73.30
C

ATOM
5154
CZ
ARG C
91
81.888
6.448
30.803
1.00
73.96
C

ATOM
5155
NH1
ARG C
91
82.739
5.645
30.176
1.00
75.13
C

ATOM
5156
NH2
ARG C
91
81.038
7.180
30.098
1.00
73.71
C

ATOM
5157
C
ARG C
91
80.707
8.091
34.580
1.00
64.28
C

ATOM
5158
O
ARG C
91
80.322
8.005
33.416
1.00
64.65
C

ATOM
5159
N
GLU C
92
79.871
8.156
35.611
1.00
61.21
C

ATOM
5160
CA
GLU C
92
78.434
8.111
35.398
1.00
59.24
C

ATOM
5161
CB
GLU C
92
77.709
7.733
36.691
1.00
61.28
C

ATOM
5162
CG
GLU C
92
76.200
7.577
36.529
1.00
63.29
C

ATOM
5163
CD
GLU C
92
75.816
6.698
35.345
1.00
64.91
C

ATOM
5164
OE1
GLU C
92
76.430
5.618
35.171
1.00
65.27
C

ATOM
5165
OE2
GLU C
92
74.888
7.087
34.599
1.00
65.86
C

ATOM
5166
C
GLU C
92
77.947
9.463
34.908
1.00
56.10
C

ATOM
5167
O
GLU C
92
76.846
9.587
34.379
1.00
55.26
C

ATOM
5168
N
PHE C
93
78.786
10.473
35.088
1.00
52.97
C

ATOM
5169
CA
PHE C
93
78.470
11.828
34.669
1.00
49.46
C

ATOM
5170
CB
PHE C
93
79.271
12.821
35.504
1.00
47.72
C

ATOM
5171
CG
PHE C
93
79.168
14.237
35.031
1.00
46.31
C

ATOM
5172
CD1
PHE C
93
77.975
14.936
35.134
1.00
46.80
C

ATOM
5173
CD2
PHE C
93
80.274
14.880
34.487
1.00
46.30
C

ATOM
5174
GE1
PHE C
93
77.881
16.260
34.698
1.00
46.57
C

ATOM
5175
CE2
PHE C
93
80.194
16.200
34.048
1.00
45.89
C

ATOM
5176
CZ
PHE C
93
78.995
16.891
34.155
1.00
46.39
C

ATOM
5177
C
PHE C
93
78.805
12.007
33.195
1.00
48.24
C

ATOM
5178
O
PHE C
93
78.194
12.829
32.512
1.00
48.29
C

ATOM
5179
N
LEU C
94
79.777
11.241
32.706
1.00
46.95
C

ATOM
5180
CA
LEU C
94
80.181
11.334
31.304
1.00
46.69
C

ATOM
5181
CB
LEU C
94
81.711
11.421
31.201
1.00
43.72
C

ATOM
5182
CG
LEU C
94
82.347
12.602
31.931
1.00
42.20
C

ATOM
5183
CD1
LEU C
94
83.827
12.571
31.708
1.00
42.01
C

ATOM
5184
CD2
LEU C
94
81.761
13.918
31.444
1.00
40.79
C

ATOM
5185
C
LEU C
94
79.657
10.163
30.470
1.00
46.61
C

ATOM
5186
O
LEU C
94
80.084
9.950
29.331
1.00
47.53
C

ATOM
5187
N
LYS C
95
78.721
9.416
31.044
1.00
46.24
C

ATOM
5188
CA
LYS C
95
78.123
8.260
30.382
1.00
46.42
C

ATOM
5189
CB
LYS C
95
77.447
7.372
31.436
1.00
48.23
C

ATOM
5190
CG
LYS C
95
77.259
5.915
31.045
1.00
48.85
C

ATOM
5191
CD
LYS C
95
75.858
5.649
30.493
1.00
50.94
C

ATOM
5192
CE
LYS C
95
74.749
5.845
31.556
1.00
51.20
C

ATOM
5193
NZ
LYS C
95
74.537
7.259
32.014
1.00
49.42
C

ATOM
5194
C
LYS C
95
77.103
8.758
29.359
1.00
45.40
C

ATOM
5195
O
LYS C
95
76.000
8.222
29.234
1.00
45.79
C

ATOM
5196
N
VAL C
96
77.495
9.797
28.631
1.00
42.97
C

ATOM
5197
CA
VAL C
96
76.648
10.418
27.627
1.00
39.32
C

ATOM
5198
CB
VAL C
96
76.748
11.930
27.759
1.00
38.19
C

ATOM
5199
CG1
VAL C
96
76.296
12.335
29.143
1.00
37.83
C

ATOM
5200
CG2
VAL C
96
78.182
12.369
27.543
1.00
37.61
C

ATOM
5201
C
VAL C
96
77.069
9.973
26.224
1.00
39.45
C

ATOM
5202
O
VAL C
96
77.934
9.110
26.077
1.00
39.51
C

ATOM
5203
N
ASP C
97
76.448
10.545
25.197
1.00
38.96
C

ATOM
5204
CA
ASP C
97
76.776
10.194
23.820
1.00
38.45
C

ATOM
5205
CB
ASP C
97
75.596
10.485
22.907
1.00
40.12
C

ATOM
5206
CG
ASP C
97
75.212
11.951
22.907
1.00
41.57
C

ATOM
5207
OD1
ASP C
97
76.061
12.785
23.289
1.00
41.15
C

ATOM
5208
OD2
ASP C
97
74.066
12.271
22.516
1.00
42.19
C

ATOM
5209
C
ASP C
97
77.986
10.982
23.328
1.00
38.55
C

ATOM
5210
O
ASP C
97
78.331
12.014
23.893
1.00
37.77
C

ATOM
5211
N
GLN C
98
78.612
10.505
22.259
1.00
39.05
C

ATOM
5212
CA
GLN C
98
79.794
11.157
21.717
1.00
38.40
C

ATOM
5213
CB
GLN C
98
80.225
10.485
20.415
1.00
38.10
C

ATOM
5214
CG
GLN C
98
80.605
9.023
20.544
1.00
36.09
C

ATOM
5215
CD
GLN C
98
81.275
8.497
19.298
1.00
36.91
C

ATOM
5216
OE1
GLN C
98
81.239
9.130
18.236
1.00
36.92
C

ATOM
5217
NE2
GLN C
98
81.881
7.324
19.412
1.00
36.42
C

ATOM
5218
C
GLN C
98
79.650
12.653
21.470
1.00
39.08
C

ATOM
5219
O
GLN C
98
80.599
13.401
21.692
1.00
40.00
C

ATOM
5220
N
GLU C
99
78.486
13.088
21.001
1.00
39.22
C

ATOM
5221
CA
GLU C
99
78.271
14.502
20.726
1.00
40.50
C

ATOM
5222
CB
GLU C
99
76.891
14.717
20.126
1.00
42.47
C

ATOM
5223
CG
GLU C
99
76.918
15.343
18.756
1.00
45.54
C

ATOM
5224
CD
GLU C
99
77.806
16.577
18.697
1.00
47.73
C

ATOM
5225
OE1
GLU C
99
77.552
17.541
19.462
1.00
47.01
C

ATOM
5226
OE2
GLU C
99
78.757
16.577
17.881
1.00
47.67
C

ATOM
5227
C
GLU C
99
78.387
15.335
21.990
1.00
41.46
C

ATOM
5228
O
GLU C
99
78.980
16.418
21.993
1.00
41.51
C

ATOM
5229
N
MSE C
100
77.788
14.831
23.061
1.00
41.97
C

ATOM
5230
CA
MSE C
100
77.818
15.518
24.335
1.00
41.69
C

ATOM
5231
CB
MSE C
100
76.885
14.824
25.333
1.00
45.69
C

ATOM
5232
CG
MSE C
100
76.914
15.403
26.735
1.00
51.76
C

ATOM
5233
SE
MSE C
100
76.090
17.140
26.925
1.00
62.68
C

ATOM
5234
CE
MSE C
100
77.565
18.303
26.510
1.00
57.90
C

ATOM
5235
C
MSE C
100
79.243
15.546
24.867
1.00
39.87
C

ATOM
5236
O
MSE C
100
79.810
16.626
25.037
1.00
39.79
C

ATOM
5237
N
LEU C
101
79.835
14.376
25.115
1.00
37.39
C

ATOM
5238
CA
LEU C
101
81.199
14.341
25.651
1.00
34.99
C

ATOM
5239
CB
LEU C
101
81.809
12.938
25.539
1.00
33.34
C

ATOM
5240
OG
LEU C
101
83.130
12.730
26.289
1.00
30.53
C

ATOM
5241
OD1
LEU C
101
82.896
12.845
27.780
1.00
31.52
C

ATOM
5242
OD2
LEU C
101
83.684
11.363
25.965
1.00
30.51
C

ATOM
5243
C
LEU C
101
82.067
15.347
24.904
1.00
34.53
C

ATOM
5244
O
LEU C
101
82.753
16.184
25.516
1.00
34.23
C

ATOM
5245
N
TYR C
102
82.011
15.274
23.577
1.00
31.29
C

ATOM
5246
CA
TYR C
102
82.770
16.179
22.716
1.00
28.61
C

ATOM
5247
CB
TYR C
102
82.335
15.955
21.258
1.00
27.71
C

ATOM
5248
CG
TYR C
102
82.876
16.976
20.288
1.00
26.47
C

ATOM
5249
CD1
TYR C
102
84.220
16.970
19.896
1.00
24.67
C

ATOM
5250
CE1
TYR C
102
84.708
17.930
19.005
1.00
23.69
C

ATOM
5251
CD2
TYR C
102
82.040
17.960
19.774
1.00
25.15
C

ATOM
5252
CE2
TYR C
102
82.505
18.913
18.899
1.00
23.80
C

ATOM
5253
CZ
TYR C
102
83.827
18.899
18.512
1.00
23.80
C

ATOM
5254
OH
TYR C
102
84.237
19.853
17.626
1.00
21.51
C

ATOM
5255
C
TYR C
102
82.572
17.659
23.131
1.00
27.38
C

ATOM
5256
O
TYR C
102
83.536
18.383
23.433
1.00
23.78
C

ATOM
5257
N
GLU C
103
81.314
18.092
23.155
1.00
28.53
C

ATOM
5258
CA
GLU C
103
80.979
19.462
23.532
1.00
29.26
C

ATOM
5259
CB
GLU C
103
79.483
19.706
23.342
1.00
30.52
C

ATOM
5260
CG
GLU C
103
79.063
19.574
21.888
1.00
33.75
C

ATOM
5261
CD
GLU C
103
77.781
20.318
21.565
1.00
36.95
C

ATOM
5262
OE1
GLU C
103
77.729
21.549
21.820
1.00
41.36
C

ATOM
5263
OE2
GLU C
103
76.832
19.682
21.053
1.00
35.81
C

ATOM
5264
C
GLU C
103
81.397
19.817
24.954
1.00
27.19
C

ATOM
5265
O
GLU C
103
81.801
20.950
25.217
1.00
27.16
C

ATOM
5266
N
ILE C
104
81.317
18.855
25.870
1.00
26.37
C

ATOM
5267
CA
ILE C
104
81.717
19.114
27.254
1.00
25.70
C

ATOM
5268
CB
ILE C
104
81.356
17.913
28.167
1.00
25.25
C

ATOM
5269
CG2
ILE C
104
82.091
17.986
29.485
1.00
25.29
C

ATOM
5270
CG1
ILE C
104
79.859
17.935
28.450
1.00
25.32
C

ATOM
5271
OD1
ILE C
104
79.346
16.709
29.127
1.00
25.12
C

ATOM
5272
C
ILE C
104
83.210
19.423
27.310
1.00
24.54
C

ATOM
5273
O
ILE C
104
83.614
20.452
27.848
1.00
22.76
C

ATOM
5274
N
ILE C
105
84.011
18.528
26.731
1.00
24.67
C

ATOM
5275
CA
ILE C
105
85.464
18.687
26.673
1.00
23.37
C

ATOM
5276
CB
ILE C
105
86.120
17.563
25.834
1.00
22.40
C

ATOM
5277
CG2
ILE C
105
87.524
17.985
25.410
1.00
22.41
C

ATOM
5278
CG1
ILE C
105
86.143
16.249
26.630
1.00
22.74
C

ATOM
5279
CD1
ILE C
105
86.616
15.035
25.826
1.00
19.84
C

ATOM
5280
C
ILE C
105
85.844
20.038
26.057
1.00
24.11
C

ATOM
5281
O
ILE C
105
86.885
20.601
26.383
1.00
23.21
C

ATOM
5282
N
LEU C
106
85.007
20.568
25.170
1.00
25.59
C

ATOM
5283
CA
LEU C
106
85.341
21.845
24.546
1.00
26.22
C

ATOM
5284
CB
LEU C
106
84.550
22.060
23.251
1.00
24.35
C

ATOM
5285
CG
LEU C
106
84.955
21.288
21.982
1.00
24.05
C

ATOM
5286
CD1
LEU C
106
84.041
21.702
20.824
1.00
19.50
C

ATOM
5287
CD2
LEU C
106
86.411
21.582
21.631
1.00
19.81
C

ATOM
5288
C
LEU C
106
85.051
22.972
25.504
1.00
27.00
C

ATOM
5289
O
LEU C
106
85.876
23.871
25.700
1.00
28.04
C

ATOM
5290
N
ALA C
107
83.870
22.908
26.107
1.00
27.32
C

ATOM
5291
CA
ALA C
107
83.432
23.921
27.054
1.00
27.07
C

ATOM
5292
CB
ALA C
107
82.044
23.574
27.562
1.00
27.09
C

ATOM
5293
C
ALA C
107
84.417
23.967
28.210
1.00
26.97
C

ATOM
5294
O
ALA C
107
84.759
25.040
28.720
1.00
25.71
C

ATOM
5295
N
ALA C
108
84.866
22.786
28.621
1.00
27.46
C

ATOM
5296
CA
ALA C
108
85.809
22.688
29.726
1.00
28.55
C

ATOM
5297
CB
ALA C
108
86.059
21.230
30.069
1.00
27.60
C

ATOM
5298
C
ALA C
108
87.119
23.383
29.363
1.00
29.01
C

ATOM
5299
O
ALA C
108
87.595
24.264
30.085
1.00
29.74
C

ATOM
5300
N
ASN C
109
87.684
22.988
28.227
1.00
28.31
C

ATOM
5301
CA
ASN C
109
88.934
23.554
27.723
1.00
27.27
C

ATOM
5302
CB
ASN C
109
89.213
22.988
26.323
1.00
27.05
C

ATOM
5303
CG
ASN C
109
90.436
23.594
25.666
1.00
24.65
C

ATOM
5304
OD1
ASN C
109
91.542
23.472
26.167
1.00
22.66
C

ATOM
5305
ND2
ASN C
109
90.236
24.235
24.517
1.00
24.60
C

ATOM
5306
C
ASN C
109
88.848
25.074
27.661
1.00
27.03
C

ATOM
5307
O
ASN C
109
89.755
25.770
28.109
1.00
28.21
C

ATOM
5308
N
TYR C
110
87.743
25.575
27.118
1.00
26.52
C

ATOM
5309
CA
TYR C
110
87.528
27.003
26.969
1.00
26.57
C

ATOM
5310
CE
TYR C
110
86.268
27.267
26.139
1.00
25.48
C

ATOM
5311
CG
TYR C
110
85.938
28.734
26.018
1.00
24.82
C

ATOM
5312
CD1
TYR C
110
86.780
29.596
25.317
1.00
26.81
C

ATOM
5313
CE1
TYR C
110
86.543
30.968
25.273
1.00
26.16
C

ATOM
5314
CD2
TYR C
110
84.838
29.282
26.669
1.00
24.41
C

ATOM
5315
CE2
TYR C
110
84.596
30.658
26.628
1.00
24.83
C

ATOM
5316
CZ
TYR C
110
85.455
31.486
25.930
1.00
24.87
C

ATOM
5317
OH
TYR C
110
85.234
32.835
25.889
1.00
25.53
C

ATOM
5318
C
TYR C
110
87.371
27.682
28.308
1.00
27.74
C

ATOM
5319
O
TYR C
110
87.907
28.767
28.546
1.00
27.37
C

ATOM
5320
N
LEU C
111
86.610
27.040
29.178
1.00
28.23
C

ATOM
5321
CA
LEU C
111
86.348
27.593
30.485
1.00
28.18
C

ATOM
5322
CE
LEU C
111
85.067
26.958
31.031
1.00
25.97
C

ATOM
5323
CG
LEU C
111
83.874
27.827
31.434
1.00
24.04
C

ATOM
5324
CD1
LEU C
111
83.755
29.132
30.657
1.00
19.70
C

ATOM
5325
CD2
LEU C
111
82.653
26.963
31.273
1.00
24.33
C

ATOM
5326
C
LEU C
111
87.547
27.373
31.410
1.00
29.42
C

ATOM
5327
O
LEU C
111
87.524
27.765
32.578
1.00
31.45
C

ATOM
5328
N
ASN C
112
88.601
26.761
30.875
1.00
29.81
C

ATOM
5329
CA
ASN C
112
89.825
26.513
31.640
1.00
31.10
C

ATOM
5330
CB
ASN C
112
90.498
27.835
32.006
1.00
31.09
C

ATOM
5331
CG
ASN C
112
91.974
27.673
32.371
1.00
32.09
C

ATOM
5332
OD1
ASN C
112
92.448
26.579
32.719
1.00
29.20
C

ATOM
5333
ND2
ASN C
112
92.708
28.783
32.300
1.00
33.07
C

ATOM
5334
C
ASN C
112
89.563
25.740
32.927
1.00
32.17
C

ATOM
5335
O
ASN C
112
89.805
26.237
34.030
1.00
33.29
C

ATOM
5336
N
ILE C
113
89.055
24.527
32.789
1.00
31.11
C

ATOM
5337
CA
ILE C
113
88.798
23.717
33.954
1.00
30.18
C

ATOM
5338
CE
ILE C
113
87.322
23.467
34.163
1.00
30.05
C

ATOM
5339
CG2
ILE C
113
87.131
22.660
35.442
1.00
28.92
C

ATOM
5340
CG1
ILE C
113
86.564
24.789
34.234
1.00
28.96
C

ATOM
5341
CD1
ILE C
113
85.076
24.575
34.283
1.00
28.52
C

ATOM
5342
C
ILE C
113
89.473
22.384
33.751
1.00
30.85
C

ATOM
5343
O
ILE C
113
88.834
21.400
33.387
1.00
29.72
C

ATOM
5344
N
LYS C
114
90.778
22.368
33.998
1.00
31.38
C

ATOM
5345
CA
LYS C
114
91.595
21.173
33.838
1.00
31.36
C

ATOM
5346
CB
LYS C
114
93.003
21.440
34.383
1.00
32.37
C

ATOM
5347
CG
LYS C
114
93.901
20.219
34.344
1.00
34.25
C

ATOM
5348
CD
LYS C
114
95.372
20.555
34.550
1.00
35.39
C

ATOM
5349
CE
LYS C
114
96.190
19.289
34.455
1.00
36.88
C

ATOM
5350
NZ
LYS C
114
95.863
18.587
33.190
1.00
40.06
C

ATOM
5351
C
LYS C
114
91.035
19.876
34.437
1.00
30.61
C

ATOM
5352
O
LYS C
114
91.054
18.841
33.785
1.00
30.70
C

ATOM
5353
N
PRO C
115
90.530
19.916
35.681
1.00
30.70
C

ATOM
5354
CD
PRO C
115
90.401
21.106
36.545
1.00
31.09
C

ATOM
5355
CA
PRO C
115
89.970
18.719
36.338
1.00
30.04
C

ATOM
5356
CB
PRO C
115
89.365
19.276
37.626
1.00
30.45
C

ATOM
5357
CG
PRO C
115
90.220
20.489
37.912
1.00
31.85
C

ATOM
5358
C
PRO C
115
88.914
18.030
35.482
1.00
29.80
C

ATOM
5359
O
PRO C
115
88.935
16.806
35.295
1.00
30.05
C

ATOM
5360
N
LEU C
116
87.981
18.833
34.974
1.00
29.91
C

ATOM
5361
CA
LEU C
116
86.904
18.330
34.114
1.00
29.38
C

ATOM
5362
CB
LEU C
116
85.797
19.376
33.980
1.00
27.77
C

ATOM
5363
CG
LEU C
116
84.628
18.909
33.138
1.00
27.38
C

ATOM
5364
CD1
LEU C
116
84.043
17.676
33.768
1.00
27.48
C

ATOM
5365
CD2
LEU C
116
83.597
20.023
33.027
1.00
27.97
C

ATOM
5366
C
LEU C
116
87.464
17.974
32.731
1.00
28.24
C

ATOM
5367
O
LEU C
116
87.042
17.003
32.107
1.00
28.34
C

ATOM
5368
N
LEU C
117
88.433
18.756
32.272
1.00
26.39
C

ATOM
5369
CA
LEU C
117
89.051
18.494
30.993
1.00
26.69
C

ATOM
5370
CB
LEU C
117
90.112
19.547
30.701
1.00
24.99
C

ATOM
5371
CG
LEU C
117
90.893
19.362
29.397
1.00
24.42
C

ATOM
5372
CD1
LEU C
117
89.943
19.112
28.225
1.00
23.60
C

ATOM
5373
CD2
LEU C
117
91.738
20.593
29.154
1.00
22.70
C

ATOM
5374
C
LEU C
117
89.680
17.100
30.981
1.00
28.34
C

ATOM
5375
O
LEU C
117
89.397
16.288
30.093
1.00
29.22
C

ATOM
5376
N
ASP C
118
90.528
16.826
31.973
1.00
29.30
C

ATOM
5377
CA
ASP C
118
91.207
15.532
32.105
1.00
29.52
C

ATOM
5378
CB
ASP C
118
92.117
15.538
33.347
1.00
32.96
C

ATOM
5379
CG
ASP C
118
93.158
16.668
33.316
1.00
36.46
C

ATOM
5380
OD1
ASP C
118
93.138
17.470
32.353
1.00
37.36
C

ATOM
5381
OD2
ASP C
118
93.990
16.757
34.253
1.00
36.80
C

ATOM
5382
C
ASP C
118
90.213
14.365
32.186
1.00
28.84
C

ATOM
5383
O
ASP C
118
90.289
13.418
31.391
1.00
28.39
C

ATOM
5384
N
ALA C
119
89.288
14.419
33.142
1.00
26.34
C

ATOM
5385
CA
ALA C
119
88.293
13.348
33.262
1.00
25.58
C

ATOM
5386
CB
ALA C
119
87.208
13.741
34.258
1.00
26.08
C

ATOM
5387
C
ALA C
119
87.654
13.022
31.899
1.00
24.81
C

ATOM
5388
O
ALA C
119
87.489
11.852
31.540
1.00
23.57
C

ATOM
5389
N
GLY C
120
87.282
14.060
31.154
1.00
22.99
C

ATOM
5390
CA
GLY C
120
86.695
13.840
29.850
1.00
23.36
C

ATOM
5391
C
GLY C
120
87.654
13.095
28.932
1.00
23.32
C

ATOM
5392
O
GLY C
120
87.284
12.124
28.282
1.00
22.39
C

ATOM
5393
N
CYS C
121
88.902
13.541
28.901
1.00
23.17
C

ATOM
5394
CA
CYS C
121
89.918
12.935
28.065
1.00
23.66
C

ATOM
5395
CB
CYS C
121
91.184
13.762
28.144
1.00
24.22
C

ATOM
5396
SG
CYS C
121
90.981
15.370
27.390
1.00
31.59
C

ATOM
5397
C
CYS C
121
90.215
11.497
28.425
1.00
24.08
C

ATOM
5398
O
CYS C
121
90.601
10.703
27.570
1.00
25.40
C

ATOM
5399
N
LYS C
122
90.026
11.155
29.692
1.00
25.04
C

ATOM
5400
CA
LYS C
122
90.270
9.796
30.138
1.00
24.59
C

ATOM
5401
CB
LYS C
122
90.293
9.740
31.672
1.00
25.68
C

ATOM
5402
CG
LYS C
122
91.396
10.599
32.270
1.00
26.14
C

ATOM
5403
CD
LYS C
122
91.580
10.400
33.763
1.00
27.91
C

ATOM
5404
CE
LYS C
122
92.594
11.421
34.315
1.00
29.43
C

ATOM
5405
NZ
LYS C
122
93.121
11.095
35.679
1.00
31.16
C

ATOM
5406
C
LYS C
122
89.179
8.897
29.571
1.00
24.85
C

ATOM
5407
O
LYS C
122
89.451
7.798
29.080
1.00
24.38
C

ATOM
5408
N
VAL C
123
87.940
9.366
29.611
1.00
26.05
C

ATOM
5409
CA
VAL C
123
86.856
8.555
29.071
1.00
27.70
C

ATOM
5410
CE
VAL C
123
85.509
9.274
29.197
1.00
28.31
C

ATOM
5411
CG1
VAL C
123
84.389
8.383
28.667
1.00
28.23
C

ATOM
5412
CG2
VAL C
123
85.272
9.627
30.650
1.00
26.87
C

ATOM
5413
C
VAL C
123
87.142
8.223
27.606
1.00
27.72
C

ATOM
5414
O
VAL C
123
86.946
7.083
27.165
1.00
27.83
C

ATOM
5415
N
VAL C
124
87.618
9.212
26.855
1.00
27.26
C

ATOM
5416
CA
VAL C
124
87.947
8.982
25.452
1.00
27.88
C

ATOM
5417
CB
VAL C
124
88.458
10.274
24.776
1.00
26.84
C

ATOM
5418
CG1
VAL C
124
88.953
9.959
23.368
1.00
26.47
C

ATOM
5419
CG2
VAL C
124
87.322
11.304
24.713
1.00
23.58
C

ATOM
5420
C
VAL C
124
89.008
7.880
25.343
1.00
28.21
C

ATOM
5421
O
VAL C
124
88.830
6.898
24.599
1.00
27.09
C

ATOM
5422
N
ALA C
125
90.097
8.041
26.095
1.00
26.95
C

ATOM
5423
CA
ALA C
125
91.170
7.050
26.102
1.00
29.33
C

ATOM
5424
CB
ALA C
125
92.268
7.479
27.044
1.00
27.76
C

ATOM
5425
C
ALA C
125
90.653
5.661
26.501
1.00
31.95
C

ATOM
5426
O
ALA C
125
91.063
4.647
25.930
1.00
32.25
C

ATOM
5427
N
GLU C
126
89.749
5.617
27.476
1.00
34.71
C

ATOM
5428
CA
CLU C
126
89.179
4.356
27.919
1.00
36.70
C

ATOM
5429
CE
GLU C
126
88.333
4.572
29.173
1.00
39.48
C

ATOM
5430
CG
GLU C
126
87.803
3.290
29.782
1.00
45.29
C

ATOM
5431
CD
GLU C
126
88.919
2.320
30.166
1.00
50.81
C

ATOM
5432
OE1
GLU C
126
89.934
2.813
30.740
1.00
52.04
C

ATOM
5433
OE2
GLU C
126
88.780
1.083
29.904
1.00
50.45
C

ATOM
5434
C
GLU C
126
88.325
3.739
26.813
1.00
35.98
C

ATOM
5435
O
GLU C
126
87.849
2.628
26.968
1.00
33.64
C

ATOM
5436
N
MSE C
127
88.123
4.477
25.717
1.00
37.74
C

ATOM
5437
CA
MSE C
127
87.355
3.994
24.563
1.00
39.73
C

ATOM
5438
CB
MSE C
127
86.592
5.129
23.866
1.00
41.63
C

ATOM
5439
CG
MSE C
127
85.526
5.848
24.700
1.00
42.19
C

ATOM
5440
SE
MSE C
127
84.412
7.110
23.629
1.00
43.57
C

ATOM
5441
CE
MSE C
127
82.969
5.916
23.133
1.00
43.96
C

ATOM
5442
C
MSE C
127
88.295
3.377
23.530
1.00
40.34
C

ATOM
5443
O
MSE C
127
87.885
2.517
22.753
1.00
41.30
C

ATOM
5444
N
ILE C
128
89.544
3.835
23.506
1.00
40.42
C

ATOM
5445
CA
ILE C
128
90.516
3.309
22.559
1.00
39.85
C

ATOM
5446
CE
ILE C
128
91.552
4.378
22.130
1.00
39.70
C

ATOM
5447
CG2
ILE C
128
92.689
3.746
21.349
1.00
39.51
C

ATOM
5448
CG1
ILE C
128
90.879
5.426
21.254
1.00
38.45
C

ATOM
5449
CD1
ILE C
128
90.118
6.401
22.035
1.00
40.80
C

ATOM
5450
C
ILE C
128
91.245
2.174
23.224
1.00
39.58
C

ATOM
5451
O
ILE C
128
91.534
1.156
22.603
1.00
40.22
C

ATOM
5452
N
ARG C
129
91.518
2.353
24.508
1.00
39.78
C

ATOM
5453
CA
ARG C
129
92.230
1.362
25.300
1.00
38.47
C

ATOM
5454
CB
ARG C
129
91.959
1.599
26.781
1.00
39.40
C

ATOM
5455
CG
ARG C
129
93.052
1.083
27.689
1.00
38.81
C

ATOM
5456
CD
ARG C
129
92.731
1.379
29.130
1.00
40.09
C

ATOM
5457
NE
ARG C
129
92.640
2.812
29.456
1.00
42.40
C

ATOM
5458
CZ
ARG C
129
93.651
3.680
29.437
1.00
41.54
C

ATOM
5459
NH1
ARG C
129
94.869
3.283
29.089
1.00
41.83
C

ATOM
5460
NH2
ARG C
129
93.443
4.937
29.815
1.00
39.32
C

ATOM
5461
C
ARG C
129
91.863
−0.066
24.940
1.00
37.14
C

ATOM
5462
O
ARG C
129
90.682
−0.428
24.875
1.00
34.49
C

ATOM
5463
N
CLY C
130
92.900
−0.860
24.688
1.00
36.58
C

ATOM
5464
CA
GLY C
130
92.732
−2.264
24.356
1.00
36.84
C

ATOM
5465
C
GLY C
130
92.098
−2.656
23.032
1.00
36.85
C

ATOM
5466
O
GLY C
130
92.210
−3.816
22.626
1.00
37.50
C

ATOM
5467
N
ARG C
131
91.431
−1.721
22.359
1.00
37.11
C

ATOM
5468
CA
ARG C
131
90.787
−2.017
21.073
1.00
37.10
C

ATOM
5469
CB
ARG C
131
89.711
−0.973
20.771
1.00
39.22
C

ATOM
5470
CG
ARG C
131
88.431
−1.131
21.569
1.00
41.84
C

ATOM
5471
CD
ARG C
131
87.839
−2.509
21.363
1.00
45.09
C

ATOM
5472
NE
ARG C
131
86.396
−2.558
21.604
1.00
47.90
C

ATOM
5473
CZ
ARG C
131
85.479
−2.055
20.780
1.00
49.21
C

ATOM
5474
NH1
ARG C
131
85.846
−1.459
19.656
1.00
49.53
C

ATOM
5475
NH2
ARG C
131
84.191
−2.155
21.073
1.00
51.64
C

ATOM
5476
C
ARG C
131
91.760
−2.084
19.894
1.00
35.38
C

ATOM
5477
O
ARG C
131
92.917
−1.676
19.989
1.00
34.16
C

ATOM
5478
N
SER C
132
91.277
−2.610
18.781
1.00
33.40
C

ATOM
5479
CA
SER C
132
92.093
−2.717
17.585
1.00
32.90
C

ATOM
5480
CB
SER C
132
91.933
−4.096
16.966
1.00
31.03
C

ATOM
5481
OC
SER C
132
90.581
−4.307
16.607
1.00
31.69
C

ATOM
5482
C
SER C
132
91.646
−1.661
16.576
1.00
32.11
C

ATOM
5483
O
SER C
132
90.585
−1.054
16.738
1.00
30.91
C

ATOM
5484
N
PRO C
133
92.462
−1.422
15.532
1.00
31.16
C

ATOM
5485
CD
PRO C
133
93.848
−1.900
15.407
1.00
29.35
C

ATOM
5486
CA
PRO C
133
92.180
−0.451
14.480
1.00
32.65
C

ATOM
5487
CB
PRO C
133
93.219
−0.801
13.441
1.00
29.52
C

ATOM
5488
CG
PRO C
133
94.400
−1.021
14.307
1.00
29.23
C

ATOM
5489
C
PRO C
133
90.754
−0.514
13.963
1.00
35.83
C

ATOM
5490
O
PRO C
133
90.054
0.504
13.909
1.00
36.35
C

ATOM
5491
N
GLU C
134
90.318
−1.709
13.588
1.00
38.45
C

ATOM
5492
CA
GLU C
134
88.962
−1.875
13.104
1.00
41.11
C

ATOM
5493
CB
GLU C
134
88.765
−3.265
12.494
1.00
44.05
C

ATOM
5494
CG
GLU C
134
88.697
−3.264
10.965
1.00
49.94
C

ATOM
5495
CD
GLU C
134
87.779
−2.177
10.405
1.00
52.39
C

ATOM
5496
OE1
GLU C
134
86.664
−2.011
10.958
1.00
54.43
C

ATOM
5497
OE2
GLU C
134
88.173
−1.503
9.413
1.00
51.18
C

ATOM
5498
C
GLU C
134
87.968
−1.660
14.249
1.00
41.19
C

ATOM
5499
O
GLU C
134
86.913
−1.040
14.062
1.00
40.64
C

ATOM
5500
N
GLU C
135
88.297
−2.162
15.437
1.00
41.33
C

ATOM
5501
CA
GLU C
135
87.399
−1.978
16.575
1.00
42.01
C

ATOM
5502
CB
GLU C
135
87.915
−2.697
17.820
1.00
42.98
C

ATOM
5503
CG
GLU C
135
87.961
−4.198
17.745
1.00
44.16
C

ATOM
5504
CD
GLU C
135
88.393
−4.796
19.073
1.00
46.95
C

ATOM
5505
OE1
GLU C
135
89.419
−4.323
19.629
1.00
46.77
C

ATOM
5506
OE2
GLU C
135
87.712
−5.728
19.565
1.00
48.28
C

ATOM
5507
C
GLU C
135
87.226
−0.489
16.908
1.00
40.82
C

ATOM
5508
O
GLU C
135
86.152
−0.055
17.328
1.00
42.69
C

ATOM
5509
N
ILE C
136
88.284
0.292
16.718
1.00
37.69
C

ATOM
5510
CA
ILE C
136
88.224
1.718
16.997
1.00
33.59
C

ATOM
5511
CB
ILE C
136
89.638
2.316
17.096
1.00
32.05
C

ATOM
5512
CG2
ILE C
136
89.552
3.838
17.349
1.00
27.02
C

ATOM
5513
CG1
ILE C
136
90.412
1.564
18.196
1.00
29.01
C

ATOM
5514
CD1
ILE C
136
91.859
1.992
18.390
1.00
26.23
C

ATOM
5515
C
ILE C
136
87.442
2.419
15.903
1.00
33.18
C

ATOM
5516
O
ILE C
136
86.631
3.299
16.171
1.00
31.83
C

ATOM
5517
N
ARG C
137
87.669
2.021
14.661
1.00
34.42
C

ATOM
5518
CA
ARG C
137
86.955
2.652
13.566
1.00
34.64
C

ATOM
5519
CB
ARG C
137
87.352
2.008
12.253
1.00
33.73
C

ATOM
5520
CG
ARG C
137
88.809
2.218
11.916
1.00
34.55
C

ATOM
5521
CD
ARG C
137
89.226
1.238
10.851
1.00
34.62
C

ATOM
5522
NE
ARG C
137
90.665
1.216
10.644
1.00
33.99
C

ATOM
5523
CZ
ARG C
137
91.340
0.120
10.328
1.00
34.12
C

ATOM
5524
NH1
ARG C
137
90.694
−1.029
10.197
1.00
32.84
C

ATOM
5525
NH2
ARG C
137
92.651
0.176
10.125
1.00
34.77
C

ATOM
5526
C
ARG C
137
85.454
2.549
13.774
1.00
35.03
C

ATOM
5527
O
ARG C
137
84.745
3.538
13.638
1.00
34.65
C

ATOM
5528
N
ARG C
138
84.968
1.366
14.132
1.00
35.13
C

ATOM
5529
CA
ARG C
138
83.539
1.211
14.328
1.00
36.00
C

ATOM
5530
CB
ARG C
138
83.176
−0.270
14.439
1.00
38.78
C

ATOM
5531
CG
ARG C
138
83.339
−1.037
13.114
1.00
43.46
C

ATOM
5532
CD
ARG C
138
82.329
−0.608
12.030
0.00
47.14
C

ATOM
5533
NE
ARG C
138
82.537
0.734
11.466
0.00
51.00
C

ATOM
5534
CZ
ARG C
138
83.462
1.061
10.563
1.00
54.05
C

ATOM
5535
NH1
ARG C
138
84.302
0.146
10.095
1.00
55.91
C

ATOM
5536
NH2
ARG C
138
83.532
2.307
10.105
1.00
54.20
C

ATOM
5537
C
ARG C
138
83.008
1.990
15.528
1.00
34.39
C

ATOM
5538
O
ARG C
138
81.816
2.264
15.626
1.00
34.40
C

ATOM
5539
N
THR C
139
83.895
2.377
16.426
1.00
31.97
C

ATOM
5540
CA
THR C
139
83.486
3.123
17.596
1.00
29.98
C

ATOM
5541
CB
THR C
139
84.575
3.077
18.624
1.00
30.24
C

ATOM
5542
OG1
THR C
139
84.946
1.713
18.825
1.00
31.86
C

ATOM
5543
CG2
THR C
139
84.120
3.697
19.923
1.00
28.26
C

ATOM
5544
C
THR C
139
83.214
4.573
17.265
1.00
29.86
C

ATOM
5545
O
THR C
139
82.267
5.180
17.767
1.00
30.37
C

ATOM
5546
N
PHE C
140
84.053
5.138
16.415
1.00
29.19
C

ATOM
5547
CA
PHE C
140
83.883
6.525
16.045
1.00
28.27
C

ATOM
5548
CB
PHE C
140
85.229
7.230
16.152
1.00
25.82
C

ATOM
5549
CG
PHE C
140
85.797
7.223
17.537
1.00
23.52
C

ATOM
5550
CD1
PHE C
140
85.228
7.990
18.543
1.00
22.27
C

ATOM
5551
CD2
PHE C
140
86.907
6.452
17.844
1.00
22.34
C

ATOM
5552
CE1
PHE C
140
85.767
7.982
19.839
1.00
20.23
C

ATOM
5553
CE2
PHE C
140
87.450
6.441
19.135
1.00
18.70
C

ATOM
5554
CZ
PHE C
140
86.880
7.204
20.126
1.00
17.04
C

ATOM
5555
C
PHE C
140
83.307
6.697
14.647
1.00
28.75
C

ATOM
5556
O
PHE C
140
83.087
7.822
14.221
1.00
30.09
C

ATOM
5557
N
ASN C
141
83.027
5.585
13.964
1.00
29.40
C

ATOM
5558
CA
ASN C
141
82.521
5.589
12.580
1.00
30.10
C

ATOM
5559
CB
ASN C
141
81.182
6.335
12.434
1.00
30.86
C

ATOM
5560
CG
ASN C
141
80.620
6.279
10.991
1.00
32.35
C

ATOM
5561
OD1
ASN C
141
80.549
5.206
10.385
1.00
30.84
C

ATOM
5562
ND2
ASN C
141
80.212
7.436
10.453
1.00
32.26
C

ATOM
5563
C
ASN C
141
83.554
6.256
11.680
1.00
30.32
C

ATOM
5564
O
ASN C
141
83.223
7.047
10.803
1.00
31.59
C

ATOM
5565
N
ILE C
142
84.821
5.953
11.907
1.00
29.73
C

ATOM
5566
CA
ILE C
142
85.867
6.548
11.091
1.00
30.11
C

ATOM
5567
CB
ILE C
142
87.151
6.830
11.983
1.00
29.75
C

ATOM
5568
CG2
ILE C
142
87.180
5.925
13.180
1.00
31.60
C

ATOM
5569
CG1
ILE C
142
88.428
6.712
11.164
1.00
29.84
C

ATOM
5570
CD1
ILE C
142
88.925
8.056
10.663
1.00
36.02
C

ATOM
5571
C
ILE C
142
86.129
5.630
9.885
1.00
28.78
C

ATOM
5572
O
ILE C
142
86.070
4.412
10.004
1.00
27.70
C

ATOM
5573
N
VAL C
143
86.355
6.201
8.708
1.00
28.81
C

ATOM
5574
CA
VAL C
143
86.594
5.344
7.556
1.00
28.92
C

ATOM
5575
CB
VAL C
143
86.022
5.937
6.250
1.00
27.33
C

ATOM
5576
CG1
VAL C
143
86.549
5.165
5.056
1.00
27.92
C

ATOM
5577
CG2
VAL C
143
84.494
5.866
6.269
1.00
26.26
C

ATOM
5578
C
VAL C
143
88.071
5.084
7.356
1.00
28.95
C

ATOM
5579
O
VAL C
143
88.905
5.971
7.539
1.00
31.52
C

ATOM
5580
N
ASN C
144
88.387
3.845
7.006
1.00
27.50
C

ATOM
5581
CA
ASN C
144
89.754
3.434
6.761
1.00
26.06
C

ATOM
5582
CB
ASN C
144
89.837
1.907
6.798
1.00
27.42
C

ATOM
5583
CG
ASN C
144
91.258
1.377
6.661
1.00
28.39
C

ATOM
5584
OD1
ASN C
144
91.528
0.242
7.035
1.00
28.70
C

ATOM
5585
ND2
ASN C
144
92.162
2.185
6.119
1.00
30.75
C

ATOM
5586
C
ASN C
144
90.074
3.942
5.371
1.00
26.48
C

ATOM
5587
O
ASN C
144
89.519
3.458
4.394
1.00
26.51
C

ATOM
5588
N
ASP C
145
90.964
4.918
5.277
1.00
26.34
C

ATOM
5589
CA
ASP C
145
91.315
5.492
3.988
1.00
27.61
C

ATOM
5590
CB
ASP C
145
91.245
7.018
4.058
1.00
28.15
C

ATOM
5591
CG
ASP C
145
91.840
7.570
5.336
1.00
28.20
C

ATOM
5592
OD1
ASP C
145
92.508
6.808
6.080
1.00
26.63
C

ATOM
5593
OD2
ASP C
145
91.639
8.780
5.595
1.00
29.52
C

ATOM
5594
C
ASP C
145
92.684
5.086
3.479
1.00
28.92
C

ATOM
5595
O
ASP C
145
93.208
5.708
2.549
1.00
29.06
C

ATOM
5596
N
PHE C
146
93.262
4.050
4.083
1.00
28.68
C

ATOM
5597
CA
PHE C
146
94.585
3.572
3.685
1.00
29.48
C

ATOM
5598
CB
PHE C
146
95.222
2.744
4.799
1.00
31.05
C

ATOM
5599
CG
PHE C
146
95.709
3.550
5.955
1.00
33.63
C

ATOM
5600
CO1
PHE C
146
96.641
4.574
5.761
1.00
34.53
C

ATOM
5601
CD2
PHE C
146
95.277
3.254
7.250
1.00
33.58
C

ATOM
5602
CE1
PHE C
146
97.147
5.292
6.841
1.00
35.14
C

ATOM
5603
CE2
PHE C
146
95.767
3.956
8.338
1.00
34.74
C

ATOM
5604
CZ
PHE C
146
96.709
4.981
8.136
1.00
36.19
C

ATOM
5605
C
PHE C
146
94.596
2.727
2.431
1.00
28.86
C

ATOM
5606
O
PHE C
146
93.889
1.725
2.355
1.00
30.57
C

ATOM
5607
N
THR C
147
95.423
3.109
1.460
1.00
28.83
C

ATOM
5608
CA
THR C
147
95.536
2.339
0.222
1.00
30.01
C

ATOM
5609
CB
THR C
147
96.556
2.946
−0.783
1.00
29.36
C

ATOM
5610
OG1
THR C
147
97.817
3.147
−0.128
1.00
29.97
C

ATOM
5611
CG2
THR C
147
96.046
4.252
−1.355
1.00
27.00
C

ATOM
5612
C
THR C
147
96.049
0.948
0.552
1.00
30.37
C

ATOM
5613
O
THR C
147
96.708
0.745
1.563
1.00
31.13
C

ATOM
5614
N
PRO C
148
95.751
−0.032
−0.299
1.00
31.61
C

ATOM
5615
CD
PRO C
148
94.879
−0.031
−1.485
1.00
31.67
C

ATOM
5616
CA
PRO C
148
96.241
−1.375
−0.010
1.00
32.60
C

ATOM
5617
CB
PRO C
148
95.903
−2.141
−1.282
1.00
31.26
C

ATOM
5618
CG
PRO C
148
94.611
−1.527
−1.697
1.00
30.19
C

ATOM
5619
C
PRO C
148
97.734
−1.327
0.255
1.00
34.28
C

ATOM
5620
O
PRO C
148
98.244
−2.067
1.087
1.00
35.43
C

ATOM
5621
N
GLU C
149
98.441
−0.445
−0.437
1.00
37.73
C

ATOM
5622
CA
GLU C
149
99.873
−0.372
−0.221
1.00
41.17
C

ATOM
5623
CB
GLU C
149
100.532
0.535
−1.266
1.00
39.75
C

ATOM
5624
CG
GLU C
149
102.038
0.662
−1.083
1.00
39.00
C

ATOM
5625
CD
GLU C
149
102.703
1.461
−2.171
1.00
39.73
C

ATOM
5626
OE1
GLU C
149
102.443
2.683
−2.265
1.00
39.67
C

ATOM
5627
OE2
GLU C
149
103.490
0.868
−2.938
1.00
39.04
C

ATOM
5628
C
GLU C
149
100.183
0.120
1.195
1.00
44.52
C

ATOM
5629
O
GLU C
149
100.646
−0.656
2.032
1.00
44.69
C

ATOM
5630
N
GUI C
150
99.914
1.398
1.460
1.00
48.03
C

ATOM
5631
CA
GLU C
150
100.161
1.995
2.774
1.00
51.71
C

ATOM
5632
CB
GLU C
150
99.557
3.407
2.822
1.00
52.60
C

ATOM
5633
CG
GLU C
150
100.095
4.362
1.763
1.00
56.26
C

ATOM
5634
CD
GLU C
150
101.508
4.869
2.052
1.00
57.57
C

ATOM
5635
OE1
GLU C
150
101.735
5.354
3.178
1.00
58.02
C

ATOM
5636
OE2
GLU C
150
102.381
4.803
1.153
1.00
58.12
C

ATOM
5637
C
GLU C
150
99.603
1.136
3.938
1.00
53.38
C

ATOM
5638
O
GLU C
150
100.159
1.112
5.042
1.00
52.61
C

ATOM
5639
N
GLU C
151
98.515
0.420
3.677
1.00
55.17
C

ATOM
5640
CA
GLU C
151
97.891
−0.431
4.681
1.00
58.21
C

ATOM
5641
CB
GLU C
151
96.636
−1.087
4.097
1.00
60.47
C

ATOM
5642
CG
GLU C
151
95.349
−0.835
4.868
1.00
62.11
C

ATOM
5643
CD
GLU C
151
94.154
−1.512
4.222
1.00
63.63
C

ATOM
5644
OE1
GLU C
151
94.025
−1.410
2.978
1.00
64.05
C

ATOM
5645
OE2
GLU C
151
93.347
−2.135
4.955
1.00
63.74
C

ATOM
5646
C
GLU C
151
98.845
−1.519
5.182
1.00
59.56
C

ATOM
5647
O
GLU C
151
99.118
−1.609
6.375
1.00
60.86
C

ATOM
5648
N
ALA C
152
99.345
−2.346
4.269
1.00
60.60
C

ATOM
5649
CA
ALA C
152
100.263
−3.422
4.626
1.00
61.88
C

ATOM
5650
CB
ALA C
152
100.455
−4.356
3.439
1.00
61.89
C

ATOM
5651
C
ALA C
152
101.616
−2.881
5.080
1.00
62.64
C

ATOM
5652
O
ALA C
152
102.398
−3.589
5.699
1.00
62.91
C

ATOM
5653
N
ALA C
153
101.888
−1.622
4.769
1.00
64.35
C

ATOM
5654
CA
ALA C
153
103.146
−1.005
5.144
1.00
66.65
C

ATOM
5655
CB
ALA C
153
103.441
0.166
4.222
1.00
66.57
C

ATOM
5656
C
ALA C
153
103.114
−0.534
6.593
1.00
68.35
C

ATOM
5657
O
ALA C
153
104.159
−0.238
7.177
1.00
67.40
C

ATOM
5658
N
ILE C
154
101.913
−0.463
7.167
1.00
70.84
C

ATOM
5659
CA
ILE C
154
101.753
−0.021
8.549
1.00
73.04
C

ATOM
5660
CB
ILE C
154
100.276
0.333
8.874
1.00
72.44
C

ATOM
5661
CG2
ILE C
154
100.160
0.823
10.308
0.00
73.15
C

ATOM
5662
CG1
ILE C
154
99.768
1.405
7.906
0.00
73.18
C

ATOM
5663
CD1
ILE C
154
100.596
2.681
7.891
0.00
73.32
C

ATOM
5664
C
ILE C
154
102.242
−1.083
9.530
1.00
74.39
C

ATOM
5665
O
ILE C
154
103.164
−0.836
10.314
1.00
75.10
C

ATOM
5666
N
ARG C
155
101.638
−2.267
9.481
1.00
75.33
C

ATOM
5667
CA
ARG C
155
102.035
−3.343
10.386
1.00
77.14
C

ATOM
5668
CB
ARG C
155
101.354
−4.655
9.970
1.00
77.56
C

ATOM
5669
CG
ARG C
155
101.473
−4.969
8.491
1.00
79.06
C

ATOM
5670
CD
ARG C
155
100.453
−6.012
8.042
1.00
79.84
C

ATOM
5671
NE
ARG C
155
101.032
−7.346
7.880
1.00
82.03
C

ATOM
5672
CZ
ARG C
155
101.458
−8.120
8.876
1.00
83.21
C

ATOM
5673
NH1
ARG C
155
101.376
−7.702
10.130
1.00
83.46
C

ATOM
5674
NH2
ARG C
155
101.967
−9.320
8.617
1.00
83.34
C

ATOM
5675
C
ARG C
155
103.557
−3.521
10.429
1.00
77.49
C

ATOM
5676
O
ARG C
155
104.141
−3.689
11.505
1.00
76.81
C

ATOM
5677
N
ARG C
156
104.185
−3.454
9.256
1.00
78.72
C

ATOM
5678
CA
ARG C
156
105.631
−3.611
9.120
1.00
80.26
C

ATOM
5679
CB
ARG C
156
106.371
−2.543
9.936
1.00
79.66
C

ATOM
5680
CG
ARG C
156
106.197
−1.128
9.442
1.00
78.84
C

ATOM
5681
CD
ARG C
156
106.951
−0.151
10.332
1.00
78.63
C

ATOM
5682
NE
ARG C
156
106.958
1.201
9.777
1.00
79.37
C

ATOM
5683
CZ
ARG C
156
107.560
2.243
10.344
1.00
79.78
C

ATOM
5684
NH1
ARG C
156
108.210
2.098
11.492
1.00
80.21
C

ATOM
5685
NH2
ARG C
156
107.513
3.434
9.763
1.00
79.89
C

ATOM
5686
C
ARG C
156
106.075
−4.997
9.586
1.00
81.59
C

ATOM
5687
O
ARG C
156
106.298
−5.862
8.715
0.00
81.82
C

ATOM
5688
OXT
ARG C 156
106.182
−5.207
10.817
1.00
83.28
C

ATOM
5689
CB
LEU D
270
75.377
10.305
15.206
1.00
63.79
D

ATOM
5690
CG
LEU D
270
75.038
9.447
13.983
1.00
64.88
D

ATOM
5691
CD1
LEU D
270
73.550
9.589
13.707
1.00
64.89
D

ATOM
5692
CD2
LEU D
270
75.842
9.894
12.762
1.00
64.87
D

ATOM
5693
C
LEU D
270
77.526
9.458
16.216
1.00
61.89
D

ATOM
5694
O
LEU D
270
78.274
9.273
17.176
1.00
61.69
D

ATOM
5695
N
LEU D
270
75.776
10.456
17.643
1.00
62.12
D

ATOM
5696
CA
LEU D
270
76.015
9.627
16.425
1.00
62.72
D

ATOM
5697
N
LYS D
271
77.975
9.523
14.966
1.00
60.94
D

ATOM
5698
CA
LYS D
271
79.394
9.377
14.666
1.00
59.23
D

ATOM
5699
CB
LYS D
271
79.635
9.177
13.157
1.00
61.06
D

ATOM
5700
CG
LYS D
271
79.243
10.362
12.273
1.00
61.84
D

ATOM
5701
CD
LYS D
271
79.810
10.233
10.859
1.00
62.36
D

ATOM
5702
CE
LYS D
271
81.303
10.589
10.782
1.00
63.95
D

ATOM
5703
NZ
LYS D
271
82.195
9.772
11.664
1.00
62.34
D

ATOM
5704
C
LYS D
271
80.146
10.607
15.114
1.00
56.61
D

ATOM
5705
O
LYS D
271
79.604
11.715
15.119
1.00
56.97
D

ATOM
5706
N
ARG D
272
81.403
10.412
15.483
1.00
53.78
D

ATOM
5707
CA
ARG D
272
82.212
11.531
15.902
1.00
51.25
D

ATOM
5708
CB
ARG D
272
81.625
12.153
17.159
1.00
50.62
D

ATOM
5709
CG
ARG D
272
81.295
13.617
16.977
1.00
50.35
D

ATOM
5710
CD
ARG D
272
82.497
14.465
17.304
1.00
50.29
D

ATOM
5711
NE
ARG D
272
82.835
15.461
16.290
1.00
50.91
D

ATOM
5712
CZ
ARG D
272
82.084
16.507
15.950
1.00
50.34
D

ATOM
5713
NH1
ARG D
272
80.913
16.720
16.528
1.00
50.37
D

ATOM
5714
NH2
ARG D
272
82.528
17.376
15.049
1.00
50.67
D

ATOM
5715
C
ARG D
272
83.652
11.142
16.124
1.00
49.27
D

ATOM
5716
O
ARG D
272
83.995
10.497
17.112
1.00
50.77
D

ATOM
5717
N
ASP D
273
84.498
11.523
15.180
1.00
45.44
D

ATOM
5718
CA
ASP D
273
85.904
11.229
15.310
1.00
40.81
D

ATOM
5719
CB
ASP D
273
86.582
11.281
13.951
1.00
40.44
D

ATOM
5720
CG
ASP D
273
87.998
10.765
13.997
1.00
40.32
D

ATOM
5721
OD1
ASP D
273
88.731
11.138
14.939
1.00
40.48
D

ATOM
5722
OD2
ASP D
273
88.377
9.991
13.094
1.00
40.70
D

ATOM
5723
C
ASP D
273
86.486
12.295
16.231
1.00
38.02
D

ATOM
5724
O
ASP D
273
87.082
13.269
15.771
1.00
36.97
D

ATOM
5725
N
LEU D
274
86.301
12.096
17.536
1.00
35.35
D

ATOM
5726
CA
LEU D
274
86.783
13.026
18.562
1.00
32.44
D

ATOM
5727
CB
LEU D
274
86.596
12.405
19.957
1.00
32.29
D

ATOM
5728
CG
LEU D
274
85.237
11.729
20.146
1.00
33.44
D

ATOM
5729
CD1
LEU D
274
85.148
10.949
21.454
1.00
33.06
D

ATOM
5730
CD2
LEU D
274
84.185
12.796
20.076
1.00
33.99
D

ATOM
5731
C
LEU D
274
88.250
13.443
18.376
1.00
30.29
D

ATOM
5732
O
LEU D
274
88.589
14.620
18.487
1.00
29.35
D

ATOM
5733
N
ILE D
275
89.119
12.481
18.090
1.00
27.97
D

ATOM
5734
CA
ILE D
275
90.529
12.790
17.919
1.00
26.53
D

ATOM
5735
CB
ILE D
275
91.366
11.487
17.721
1.00
26.41
D

ATOM
5736
CG2
ILE D
275
92.798
11.829
17.316
1.00
25.43
D

ATOM
5737
CG1
ILE D
275
91.390
10.679
19.029
1.00
24.46
D

ATOM
5738
CD1
ILE D
275
92.026
11.404
20.207
1.00
19.75
D

ATOM
5739
C
ILE D
275
90.738
13.764
16.748
1.00
26.48
D

ATOM
5740
O
ILE D
275
91.490
14.743
16.855
1.00
26.90
D

ATOM
5741
N
THR D
276
90.052
13.503
15.642
1.00
24.10
D

ATOM
5742
CA
THR D
276
90.134
14.348
14.469
1.00
22.65
D

ATOM
5743
CB
THR D
276
89.447
13.632
13.273
1.00
21.40
D

ATOM
5744
OG1
THR D
276
90.221
12.483
12.942
1.00
21.35
D

ATOM
5745
CG2
THR D
276
89.321
14.528
12.052
1.00
18.26
D

ATOM
5746
C
THR D
276
89.477
15.711
14.769
1.00
23.50
D

ATOM
5747
O
THR D
276
90.041
16.768
14.462
1.00
22.31
D

ATOM
5748
N
SER D
277
88.305
15.673
15.397
1.00
23.60
D

ATOM
5749
CA
SER D
277
87.582
16.883
15.745
1.00
25.64
D

ATOM
5750
CB
SER D
277
86.156
16.544
16.144
1.00
25.38
D

ATOM
5751
OG
SER D
277
85.440
16.087
15.019
1.00
27.48
D

ATOM
5752
C
SER D
277
88.215
17.739
16.837
1.00
26.65
D

ATOM
5753
O
SER D
277
88.380
18.939
16.657
1.00
29.61
D

ATOM
5754
N
LEU D
278
88.561
17.147
17.970
1.00
25.91
D

ATOM
5755
CA
LEU D
278
89.180
17.922
19.035
1.00
26.38
D

ATOM
5756
CB
LEU D
278
89.564
17.027
20.218
1.00
26.10
D

ATOM
5757
CG
LEU D
278
88.426
16.811
21.194
1.00
24.98
D

ATOM
5758
CD1
LEU D
278
88.017
18.153
21.792
1.00
26.21
D

ATOM
5759
CD2
LEU D
278
87.257
16.190
20.458
1.00
28.73
D

ATOM
5760
C
LEU D
278
90.426
18.621
18.530
1.00
26.46
D

ATOM
5761
O
LEU D
278
91.038
18.189
17.549
1.00
27.90
D

ATOM
5762
N
PRO D
279
90.803
19.733
19.177
1.00
26.62
D

ATOM
5763
CD
PRO D
279
89.970
20.521
20.096
1.00
26.92
D

ATOM
5764
CA
PRO D
279
91.994
20.496
18.799
1.00
27.49
D

ATOM
5765
CB
PRO D
279
91.940
21.686
19.739
1.00
26.12
D

ATOM
5766
CG
PRO D
279
90.495
21.922
19.861
1.00
25.59
D

ATOM
5767
C
PRO D
279
93.212
19.620
19.047
1.00
29.22
D

ATOM
5768
O
PRO D
279
93.221
18.827
19.991
1.00
30.55
D

ATOM
5769
N
PHE D
280
94.234
19.775
18.210
1.00
29.38
D

ATOM
5770
CA
PHE D
280
95.452
18.980
18.303
1.00
29.08
D

ATOM
5771
CB
PHE D
280
96.567
19.668
17.518
1.00
30.38
D

ATOM
5772
CG
PHE D
280
97.839
18.871
17.438
1.00
33.85
D

ATOM
5773
CD1
PHE D
280
97.849
17.585
16.890
1.00
35.64
D

ATOM
5774
CD2
PHE D
280
99.038
19.415
17.886
1.00
34.62
D

ATOM
5775
CE1
PHE D
280
99.045
16.852
16.789
1.00
36.28
D

ATOM
5776
CE2
PHE D
280
100.237
18.696
17.790
1.00
35.86
D

ATOM
5777
CZ
PHE D
280
100.242
17.410
17.239
1.00
36.27
D

ATOM
5778
C
PHE D
280
95.883
18.747
19.746
1.00
28.87
D

ATOM
5779
O
PHE D
280
96.100
17.611
20.167
1.00
28.22
D

ATOM
5780
N
GLU D
281
95.977
19.824
20.513
1.00
29.70
D

ATOM
5781
CA
GLU D
281
96.394
19.735
21.906
1.00
30.73
D

ATOM
5782
CB
GLU D
281
96.367
21.124
22.544
1.00
30.74
D

ATOM
5783
CG
GLU D
281
96.958
22.225
21.686
1.00
35.82
D

ATOM
5784
CD
GLU D
281
96.181
22.455
20.365
1.00
39.11
D

ATOM
5785
OE1
GLU D
281
94.927
22.371
20.364
1.00
37.33
D

ATOM
5786
OE2
GLU D
281
96.838
22.734
19.329
1.00
41.78
D

ATOM
5787
C
GLU D
281
95.508
18.767
22.707
1.00
30.47
D

ATOM
5788
O
GLU D
281
95.998
17.800
23.291
1.00
29.60
D

ATOM
5789
N
ILE D
282
94.200
19.006
22.731
1.00
30.62
D

ATOM
5790
CA
ILE D
282
93.326
18.115
23.495
1.00
30.51
D

ATOM
5791
CB
ILE D
282
91.826
18.479
23.367
1.00
28.68
D

ATOM
5792
CG2
ILE D
282
90.973
17.454
24.096
1.00
25.40
D

ATOM
5793
CG1
ILE D
282
91.559
19.841
24.002
1.00
28.37
D

ATOM
5794
CD1
ILE D
282
92.338
20.960
23.374
1.00
29.50
D

ATOM
5795
C
ILE D
282
93.506
16.667
23.085
1.00
30.93
D

ATOM
5796
O
ILE D
282
93.569
15.798
23.939
1.00
32.03
D

ATOM
5797
N
SER D
283
93.597
16.403
21.786
1.00
33.38
D

ATOM
5798
CA
SER D
283
93.773
15.037
21.315
1.00
33.57
D

ATOM
5799
CB
SER D
283
93.729
14.991
19.793
1.00
33.09
D

ATOM
5800
OG
SER D
283
92.440
14.625
19.343
1.00
33.69
D

ATOM
5801
C
SER D
283
95.060
14.383
21.806
1.00
34.43
D

ATOM
5802
O
SER D
283
95.102
13.171
21.996
1.00
35.71
D

ATOM
5803
N
LEU D
284
96.121
15.158
21.996
1.00
33.67
D

ATOM
5804
CA
LEU D
284
97.345
14.541
22.479
1.00
33.99
D

ATOM
5805
CB
LEU D
284
98.511
15.514
22.412
1.00
34.78
D

ATOM
5806
CG
LEU D
284
98.908
15.828
20.966
1.00
37.92
D

ATOM
5807
CD1
LEU D
284
99.965
16.921
20.972
1.00
38.44
D

ATOM
5808
CD2
LEU D
284
99.424
14.571
20.264
1.00
35.81
D

ATOM
5809
C
LEU D
284
97.105
14.089
23.908
1.00
34.14
D

ATOM
5810
O
LEU D
284
97.469
12.972
24.268
1.00
35.96
D

ATOM
5811
N
LYS D
285
96.470
14.944
24.710
1.00
32.83
D

ATOM
5812
CA
LYS D
285
96.180
14.598
26.094
1.00
31.02
D

ATOM
5813
CB
LYS D
285
95.192
15.590
26.711
1.00
32.29
D

ATOM
5814
CG
LYS D
285
95.694
17.027
26.672
1.00
34.86
D

ATOM
5815
CD
LYS D
285
94.977
17.944
27.659
1.00
38.81
D

ATOM
5816
CE
LYS D
285
95.626
17.931
29.043
1.00
41.32
D

ATOM
5817
NZ
LYS D
285
95.083
19.055
29.866
1.00
43.73
D

ATOM
5818
C
LYS D
285
95.603
13.194
26.129
1.00
28.79
D

ATOM
5819
O
LYS D
285
96.124
12.305
26.823
1.00
29.62
D

ATOM
5820
N
ILE D
286
94.538
12.991
25.360
1.00
25.19
D

ATOM
5821
CA
ILE D
286
93.898
11.681
25.281
1.00
24.05
D

ATOM
5822
CB
ILE D
286
92.834
11.660
24.148
1.00
22.82
D

ATOM
5823
CG2
ILE D
286
92.176
10.291
24.060
1.00
21.24
D

ATOM
5824
CG1
ILE D
286
91.800
12.757
24.414
1.00
23.94
D

ATOM
5825
CD1
ILE D
286
90.731
12.886
23.321
1.00
23.24
D

ATOM
5826
C
ILE D
286
94.950
10.583
25.036
1.00
23.79
D

ATOM
5827
O
ILE D
286
94.970
9.573
25.738
1.00
22.04
D

ATOM
5828
N
PHE D
287
95.825
10.788
24.051
1.00
21.07
D

ATOM
5829
CA
PHE D
287
96.844
9.790
23.746
1.00
21.11
D

ATOM
5830
CB
PHE D
287
97.596
10.147
22.469
1.00
20.53
D

ATOM
5831
CG
PHE D
287
96.842
9.818
21.221
1.00
20.94
D

ATOM
5832
CD1
PHE D
287
96.528
8.495
20.915
1.00
18.61
D

ATOM
5833
CD2
PHE D
287
96.445
10.831
20.340
1.00
20.85
D

ATOM
5834
CE1
PHE D
287
95.835
8.184
19.754
1.00
17.26
D

ATOM
5835
CE2
PHE D
287
95.752
10.525
19.177
1.00
18.21
D

ATOM
5836
CZ
PHE D
287
95.444
9.204
18.876
1.00
16.07
D

ATOM
5837
C
PHE D
287
97.849
9.539
24.859
1.00
21.96
D

ATOM
5838
O
PHE D
287
98.314
8.418
25.035
1.00
20.26
D

ATOM
5839
N
ASN D
288
98.182
10.592
25.593
1.00
23.06
D

ATOM
5840
CA
ASN D
288
99.128
10.494
26.677
1.00
25.24
D

ATOM
5841
CB
ASN D
288
99.598
11.892
27.089
1.00
25.50
D

ATOM
5842
CG
ASN D
288
100.691
12.432
26.166
1.00
27.45
D

ATOM
5843
OD1
ASN D
288
101.539
11.660
25.680
1.00
29.10
D

ATOM
5844
ND2
ASN D
288
100.696
13.750
25.936
1.00
25.61
D

ATOM
5845
C
ASN D
288
98.585
9.695
27.883
1.00
28.89
D

ATOM
5846
O
ASN D
288
99.331
9.376
28.815
1.00
28.16
D

ATOM
5847
N
TYR D
289
97.289
9.368
27.846
1.00
30.81
D

ATOM
5848
CA
TYR D
289
96.633
8.560
28.879
1.00
33.41
D

ATOM
5849
CB
TYR D
289
95.210
9.038
29.193
1.00
35.09
D

ATOM
5850
CG
TYR D
289
95.100
10.237
30.098
1.00
38.19
D

ATOM
5851
CD1
TYR D
289
95.713
10.256
31.343
1.00
37.23
D

ATOM
5852
CE1
TYR D
289
95.585
11.353
32.182
1.00
37.83
D

ATOM
5853
CD2
TYR D
289
94.353
11.348
29.713
1.00
38.71
D

ATOM
5854
CE2
TYR D
289
94.219
12.447
30.543
1.00
39.19
D

ATOM
5855
CZ
TYR D
289
94.838
12.449
31.778
1.00
38.07
D

ATOM
5856
OH
TYR D
289
94.716
13.558
32.596
1.00
37.65
D

ATOM
5857
C
TYR D
289
96.496
7.129
28.375
1.00
34.42
D

ATOM
5858
O
TYR D
289
95.852
6.288
29.016
1.00
34.85
D

ATOM
5859
N
LEU D
290
97.076
6.857
27.215
1.00
34.95
D

ATOM
5860
CA
LEU D
290
96.980
5.530
26.632
1.00
36.71
D

ATOM
5861
CB
LEU D
290
96.488
5.621
25.189
1.00
37.91
D

ATOM
5862
CG
LEU D
290
95.004
5.925
24.991
1.00
38.82
D

ATOM
5863
CD1
LEU D
290
94.740
6.136
23.516
1.00
39.93
D

ATOM
5864
CD2
LEU D
290
94.159
4.764
25.535
1.00
37.72
D

ATOM
5865
C
LEU D
290
98.302
4.802
26.664
1.00
37.19
D

ATOM
5866
O
LEU D
290
99.354
5.419
26.628
1.00
37.91
D

ATOM
5867
N
GLN D
291
98.256
3.482
26.744
1.00
38.53
D

ATOM
5868
CA
GLN D
291
99.493
2.736
26.771
1.00
39.34
D

ATOM
5869
CB
GLN D
291
99.251
1.308
27.236
1.00
40.51
D

ATOM
5870
CG
GLN D
291
98.786
1.213
28.657
1.00
43.34
D

ATOM
5871
CD
GLN D
291
98.666
−0.215
29.102
1.00
46.99
D

ATOM
5872
OE1
GLN D
291
99.662
−0.945
29.172
1.00
50.86
D

ATOM
5873
NE2
GLN D
291
97.444
−0.638
29.398
1.00
49.26
D

ATOM
5874
C
GLN D
291
100.090
2.749
25.374
1.00
38.68
D

ATOM
5875
O
GLN D
291
99.393
2.990
24.383
1.00
39.01
D

ATOM
5876
N
PHE D
292
101.386
2.482
25.308
1.00
35.62
D

ATOM
5877
CA
PHE D
292
102.096
2.492
24.059
1.00
32.95
D

ATOM
5878
CB
PHE D
292
103.583
2.209
24.335
1.00
32.02
D

ATOM
5879
CG
PHE D
292
104.010
0.795
24.109
1.00
29.67
D

ATOM
5880
CD1
PHE D
292
104.290
0.349
22.829
1.00
30.05
D

ATOM
5881
CD2
PHE D
292
104.221
−0.064
25.176
1.00
29.27
D

ATOM
5882
CE1
PHE D
292
104.788
−0.932
22.613
1.00
30.66
D

ATOM
5883
CE2
PHE D
292
104.719
−1.348
24.972
1.00
29.01
D

ATOM
5884
CZ
PHE D
292
105.004
−1.781
23.686
1.00
29.86
D

ATOM
5885
C
PHE D
292
101.477
1.552
23.035
1.00
32.44
D

ATOM
5886
O
PHE D
292
101.384
1.894
21.852
1.00
33.62
D

ATOM
5887
N
GLU D
293
101.018
0.389
23.481
1.00
31.32
D

ATOM
5888
CA
GLU D
293
100.396
−0.551
22.560
1.00
29.89
D

ATOM
5889
CB
GLU D
293
99.974
−1.819
23.296
1.00
29.10
D

ATOM
5890
CG
GLU D
293
101.135
−2.712
23.586
1.00
30.44
D

ATOM
5891
CD
GLU D
293
101.534
−2.717
25.053
1.00
31.93
D

ATOM
5892
OE1
GLU D
293
101.473
−1.647
25.722
1.00
28.98
D

ATOM
5893
OE2
GLU D
293
101.924
−3.815
25.518
1.00
32.42
D

ATOM
5894
C
GLU D
293
99.187
0.044
21.864
1.00
28.52
D

ATOM
5895
O
GLU D
293
98.978
−0.193
20.679
1.00
26.63
D

ATOM
5896
N
ASP D
294
98.391
0.802
22.615
1.00
29.50
D

ATOM
5897
CA
ASP D
294
97.193
1.431
22.081
1.00
30.32
D

ATOM
5898
CB
ASP D
294
96.330
2.030
23.210
1.00
32.63
D

ATOM
5899
CG
ASP D
294
95.768
0.968
24.183
1.00
36.82
D

ATOM
5900
OD1
ASP D
294
95.503
−0.192
23.772
1.00
39.44
D

ATOM
5901
OD2
ASP D
294
95.563
1.309
25.369
1.00
38.44
D

ATOM
5902
C
ASP D
294
97.585
2.542
21.103
1.00
29.40
D

ATOM
5903
O
ASP D
294
96.796
2.930
20.245
1.00
27.84
D

ATOM
5904
N
ILE D
295
98.805
3.050
21.237
1.00
28.17
D

ATOM
5905
CA
ILE D
295
99.266
4.114
20.362
1.00
28.34
D

ATOM
5906
CB
ILE D
295
100.510
4.784
20.917
1.00
28.05
D

ATOM
5907
CG2
ILE D
295
100.845
5.998
20.077
1.00
25.51
D

ATOM
5908
CG1
ILE D
295
100.294
5.145
22.392
1.00
30.16
D

ATOM
5909
CD1
ILE D
295
99.338
6.283
22.658
1.00
31.34
D

ATOM
5910
C
ILE D
295
99.605
3.549
18.990
1.00
28.98
D

ATOM
5911
O
ILE D
295
99.310
4.151
17.956
1.00
28.75
D

ATOM
5912
N
ILE D
296
100.227
2.381
18.996
1.00
29.17
D

ATOM
5913
CA
ILE D
296
100.612
1.715
17.768
1.00
30.36
D

ATOM
5914
CB
ILE D
296
101.521
0.491
18.085
1.00
30.31
D

ATOM
5915
CG2
ILE D
296
101.236
−0.660
17.148
1.00
28.53
D

ATOM
5916
CG1
ILE D
296
102.987
0.911
17.989
1.00
31.04
D

ATOM
5917
CD1
ILE D
296
103.353
2.115
18.829
1.00
32.07
D

ATOM
5918
C
ILE D
296
99.379
1.308
16.965
1.00
30.74
D

ATOM
5919
O
ILE D
296
99.376
1.398
15.741
1.00
30.48
D

ATOM
5920
N
ASN D
297
98.330
0.865
17.642
1.00
31.12
D

ATOM
5921
CA
ASN D
297
97.121
0.506
16.924
1.00
33.08
D

ATOM
5922
CB
ASN D
297
96.096
−0.099
17.865
1.00
33.38
D

ATOM
5923
CG
ASN D
297
96.393
−1.537
18.171
1.00
37.25
D

ATOM
5924
OD1
ASN D
297
95.953
−2.067
19.194
1.00
37.85
D

ATOM
5925
ND2
ASN D
297
97.143
−2.196
17.270
1.00
37.30
D

ATOM
5926
C
ASN D
297
96.548
1.767
16.316
1.00
33.81
D

ATOM
5927
O
ASN D
297
96.220
1.817
15.123
1.00
34.30
D

ATOM
5928
N
SER D
298
96.435
2.780
17.168
1.00
32.14
D

ATOM
5929
CA
SER D
298
95.912
4.079
16.792
1.00
30.45
D

ATOM
5930
CB
SER D
298
96.100
5.073
17.939
1.00
29.96
D

ATOM
5931
OG
SER D
298
95.395
4.648
19.087
1.00
27.42
D

ATOM
5932
C
SER D
298
96.656
4.566
15.583
1.00
30.58
D

ATOM
5933
O
SER D
298
96.103
5.255
14.731
1.00
32.34
D

ATOM
5934
N
LEU D
299
97.930
4.216
15.514
1.00
29.49
D

ATOM
5935
CA
LEU D
299
98.738
4.628
14.387
1.00
28.00
D

ATOM
5936
CB
LEU D
299
100.164
4.131
14.570
1.00
28.12
D

ATOM
5937
CG
LEU D
299
101.291
5.098
14.240
1.00
28.83
D

ATOM
5938
CD1
LEU D
299
101.105
6.442
14.938
1.00
28.49
D

ATOM
5939
CD2
LEU D
299
102.595
4.455
14.703
1.00
30.72
D

ATOM
5940
C
LEU D
299
98.147
4.063
13.108
1.00
27.04
D

ATOM
5941
O
LEU D
299
98.382
4.608
12.045
1.00
28.76
D

ATOM
5942
N
GLY D
300
97.356
2.996
13.212
1.00
25.60
D

ATOM
5943
CA
GLY D
300
96.783
2.387
12.018
1.00
25.16
D

ATOM
5944
C
GLY D
300
95.268
2.423
11.857
1.00
25.49
D

ATOM
5945
O
GLY D
300
94.665
1.528
11.258
1.00
24.96
D

ATOM
5946
N
VAL D
301
94.661
3.476
12.381
1.00
26.14
D

ATOM
5947
CA
VAL D
301
93.223
3.677
12.335
1.00
25.65
D

ATOM
5948
CB
VAL D
301
92.783
4.425
13.635
1.00
25.13
D

ATOM
5949
CG1
VAL D
301
91.377
4.975
13.523
1.00
23.49
D

ATOM
5950
CG2
VAL D
301
92.881
3.470
14.818
1.00
25.09
D

ATOM
5951
C
VAL D
301
92.853
4.482
11.085
1.00
26.83
D

ATOM
5952
O
VAL D
301
91.895
4.160
10.386
1.00
29.06
D

ATOM
5953
N
SER D
302
93.624
5.517
10.781
1.00
27.15
D

ATOM
5954
CA
SER D
302
93.321
6.327
9.611
1.00
27.14
D

ATOM
5955
CB
SER D
302
92.021
7.096
9.832
1.00
26.96
D

ATOM
5956
OG
SER D
302
92.186
8.048
10.876
1.00
28.29
D

ATOM
5957
C
SER D
302
94.442
7.308
9.329
1.00
26.93
D

ATOM
5958
O
SER D
302
95.174
7.696
10.239
1.00
27.64
D

ATOM
5959
N
GLN D
303
94.558
7.720
8.067
1.00
26.82
D

ATOM
5960
CA
GLN D
303
95.596
8.658
7.661
1.00
25.04
D

ATOM
5961
CB
GLN D
303
95.362
9.166
6.244
1.00
23.83
D

ATOM
5962
CG
GLN D
303
95.865
8.261
5.154
1.00
29.99
D

ATOM
5963
CD
GLN D
303
97.398
8.160
5.090
1.00
32.84
D

ATOM
5964
OE1
GLN D
303
97.942
7.457
4.239
1.00
34.49
D

ATOM
5965
NE2
GLN D
303
98.091
8.863
5.986
1.00
36.06
D

ATOM
5966
C
GLN D
303
95.653
9.852
8.587
1.00
23.97
D

ATOM
5967
O
GLN D
303
96.743
10.343
8.901
1.00
22.53
D

ATOM
5968
N
ASN D
304
94.490
10.322
9.034
1.00
22.85
D

ATOM
5969
CA
ASN D
304
94.479
11.487
9.908
1.00
24.54
D

ATOM
5970
CB
ASN D
304
93.082
12.042
10.095
1.00
25.34
D

ATOM
5971
CG
ASN D
304
93.105
13.358
10.814
1.00
28.24
D

ATOM
5972
OD1
ASN D
304
92.215
13.657
11.613
1.00
30.04
D

ATOM
5973
ND2
ASN D
304
94.143
14.163
10.544
1.00
29.46
D

ATOM
5974
C
ASN D
304
95.058
11.172
11.270
1.00
25.25
D

ATOM
5975
O
ASN D
304
95.876
11.928
11.820
1.00
24.93
D

ATOM
5976
N
TRP D
305
94.609
10.063
11.835
1.00
25.15
D

ATOM
5977
CA
TRP D
305
95.139
9.658
13.118
1.00
25.51
D

ATOM
5978
CB
TRP D
305
94.447
8.373
13.587
1.00
25.43
D

ATOM
5979
CG
TRP D
305
93.138
8.630
14.311
1.00
26.00
D

ATOM
5980
CD2
TRP D
305
92.614
7.880
15.410
1.00
26.49
D

ATOM
5981
CE2
TRP D
305
91.351
8.425
15.730
1.00
24.97
D

ATOM
5982
CE3
TRP D
305
93.090
6.796
16.157
1.00
27.62
D

ATOM
5983
CD1
TRP D
305
92.199
9.581
14.015
1.00
25.09
D

ATOM
5984
NE1
TRP D
305
91.122
9.461
14.864
1.00
24.10
D

ATOM
5985
CZ2
TRP D
305
90.559
7.918
16.764
1.00
23.76
D

ATOM
5986
CZ3
TRP D
305
92.299
6.297
17.183
1.00
25.00
D

ATOM
5987
CH2
TRP D
305
91.053
6.859
17.474
1.00
24.03
D

ATOM
5988
C
TRP D
305
96.656
9.477
12.935
1.00
24.69
D

ATOM
5989
O
TRP D
305
97.445
9.992
13.734
1.00
25.68
D

ATOM
5990
N
ASN D
306
97.054
8.786
11.863
1.00
22.23
D

ATOM
5991
CA
ASN D
306
98.471
8.583
11.555
1.00
21.36
D

ATOM
5992
CB
ASN D
306
98.669
7.946
10.182
1.00
19.88
D

ATOM
5993
CG
ASN D
306
100.134
7.572
9.920
1.00
20.62
D

ATOM
5994
OD1
ASN D
306
100.608
6.526
10.394
1.00
21.63
D

ATOM
5995
ND2
ASN D
306
100.860
8.427
9.176
1.00
16.92
D

ATOM
5996
C
ASN D
306
99.203
9.913
11.517
1.00
21.93
D

ATOM
5997
O
ASN D
306
100.356
10.009
11.912
1.00
21.70
D

ATOM
5998
N
LYS D
307
98.533
10.930
11.000
1.00
22.01
D

ATOM
5999
CA
LYS D
307
99.134
12.235
10.907
1.00
23.12
D

ATOM
6000
CB
LYS D
307
98.270
13.136
10.027
1.00
24.42
D

ATOM
6001
CG
LYS D
307
98.897
14.469
9.657
1.00
25.07
D

ATOM
6002
CD
LYS D
307
97.803
15.504
9.446
1.00
29.41
D

ATOM
6003
CE
LYS D
307
98.290
16.723
8.650
1.00
31.20
D

ATOM
6004
NZ
LYS D
307
98.710
16.351
7.251
1.00
30.25
D

ATOM
6005
C
LYS D
307
99.298
12.868
12.284
1.00
24.28
D

ATOM
6006
O
LYS D
307
100.387
13.292
12.654
1.00
26.10
D

ATOM
6007
N
ILE D
308
98.214
12.902
13.047
1.00
23.74
D

ATOM
6008
CA
ILE D
308
98.217
13.520
14.359
1.00
25.31
D

ATOM
6009
CB
ILE D
308
96.843
13.350
15.042
1.00
27.23
D

ATOM
6010
CG2
ILE D
308
96.899
13.810
16.475
1.00
27.28
D

ATOM
6011
CG1
ILE D
308
95.794
14.187
14.294
1.00
28.70
D

ATOM
6012
CD1
ILE D
308
94.383
14.048
14.808
1.00
26.95
D

ATOM
6013
C
ILE D
308
99.298
13.018
15.292
1.00
25.96
D

ATOM
6014
O
ILE D
308
100.079
13.797
15.838
1.00
24.81
D

ATOM
6015
N
ILE D
309
99.353
11.710
15.464
1.00
26.12
D

ATOM
6016
CA
ILE D
309
100.314
11.115
16.359
1.00
25.75
D

ATOM
6017
CB
ILE D
309
99.990
9.603
16.538
1.00
25.30
D

ATOM
6018
CG2
ILE D
309
100.995
8.937
17.437
1.00
24.21
D

ATOM
6019
CG1
ILE D
309
98.617
9.437
17.181
1.00
21.52
D

ATOM
6020
CD1
ILE D
309
98.160
8.023
17.261
1.00
23.28
D

ATOM
6021
C
ILE D
309
101.755
11.313
15.906
1.00
26.74
D

ATOM
6022
O
ILE D
309
102.626
11.586
16.729
1.00
27.84
D

ATOM
6023
N
ARG D
310
102.026
11.177
14.610
1.00
28.38
D

ATOM
6024
CA
ARG D
310
103.401
11.350
14.098
1.00
29.18
D

ATOM
6025
CB
ARG D
310
103.513
10.811
12.663
1.00
28.52
D

ATOM
6026
CG
ARG D
310
103.531
9.277
12.560
1.00
30.67
D

ATOM
6027
CD
ARG D
310
103.052
8.787
11.186
1.00
34.25
D

ATOM
6028
NE
ARG D
310
104.098
8.252
10.323
1.00
36.16
D

ATOM
6029
CZ
ARG D
310
105.097
8.969
9.827
1.00
38.55
D

ATOM
6030
NH1
ARG D
310
105.200
10.259
10.095
1.00
42.20
D

ATOM
6031
NH2
ARG D
310
106.009
8.391
9.069
1.00
41.89
D

ATOM
6032
C
ARG D
310
103.838
12.811
14.139
1.00
28.88
D

ATOM
6033
O
ARG D
310
104.996
13.133
13.873
1.00
28.32
D

ATOM
6034
N
LYS D
311
102.900
13.681
14.496
1.00
29.76
D

ATOM
6035
CA
LYS D
311
103.172
15.104
14.570
1.00
32.11
D

ATOM
6036
CB
LYS D
311
101.894
15.868
14.227
1.00
32.03
D

ATOM
6037
CG
LYS D
311
102.061
17.362
14.098
1.00
36.15
D

ATOM
6038
CD
LYS D
311
100.731
18.049
13.814
1.00
39.43
D

ATOM
6039
CE
LYS D
311
100.895
19.580
13.814
1.00
42.31
D

ATOM
6040
NZ
LYS D
311
100.575
20.231
15.122
1.00
42.00
D

ATOM
6041
C
LYS D
311
103.728
15.564
15.934
1.00
32.85
D

ATOM
6042
O
LYS D
311
104.467
16.545
15.992
1.00
32.33
D

ATOM
6043
N
SER D
312
103.395
14.855
17.017
1.00
33.76
D

ATOM
6044
CA
SER D
312
103.857
15.223
18.365
1.00
33.60
D

ATOM
6045
CB
SER D
312
102.835
14.787
19.421
1.00
35.34
D

ATOM
6046
OG
SER D
312
103.198
15.271
20.712
1.00
39.47
D

ATOM
6047
C
SER D
312
105.222
14.667
18.781
1.00
31.68
D

ATOM
6048
O
SER D
312
105.456
13.468
18.728
1.00
32.40
D

ATOM
6049
N
THR D
313
106.125
15.543
19.198
1.00
30.17
D

ATOM
6050
CA
THR D
313
107.429
15.095
19.651
1.00
29.28
D

ATOM
6051
CB
THR D
313
108.502
16.214
19.480
1.00
30.08
D

ATOM
6052
OG1
THR D
313
109.122
16.072
18.199
1.00
31.16
D

ATOM
6053
CG2
THR D
313
109.580
16.132
20.558
1.00
30.05
D

ATOM
6054
C
THR D
313
107.270
14.701
21.128
1.00
27.77
D

ATOM
6055
O
THR D
313
107.658
13.603
21.538
1.00
26.51
D

ATOM
6056
N
SER D
314
106.666
15.599
21.901
1.00
26.12
D

ATOM
6057
CA
SER D
314
106.420
15.370
23.311
1.00
26.42
D

ATOM
6058
CB
SER D
314
105.499
16.454
23.886
1.00
25.86
D

ATOM
6059
OG
SER D
314
104.133
16.191
23.589
1.00
25.20
D

ATOM
6060
C
SER D
314
105.755
14.011
23.534
1.00
26.86
D

ATOM
6061
O
SER D
314
106.064
13.314
24.486
1.00
27.19
D

ATOM
6062
N
LEU D
315
104.830
13.633
22.668
1.00
26.78
D

ATOM
6063
CA
LEU D
315
104.169
12.368
22.851
1.00
26.12
D

ATOM
6064
CB
LEU D
315
103.148
12.167
21.741
1.00
25.84
D

ATOM
6065
CG
LEU D
315
102.212
10.960
21.711
1.00
26.39
D

ATOM
6066
CD1
LEU D
315
101.094
11.269
20.721
1.00
27.77
D

ATOM
6067
CD2
LEU D
315
102.933
9.691
21.303
1.00
24.47
D

ATOM
6068
C
LEU D
315
105.186
11.229
22.899
1.00
26.05
D

ATOM
6069
O
LEU D
315
105.108
10.373
23.780
1.00
27.85
D

ATOM
6070
N
TRP D
316
106.165
11.224
21.998
1.00
24.50
D

ATOM
6071
CA
TRP D
316
107.141
10.138
22.011
1.00
25.89
D

ATOM
6072
CB
TRP D
316
107.751
9.952
20.607
1.00
24.16
D

ATOM
6073
CG
TRP D
316
106.708
9.452
19.635
1.00
21.27
D

ATOM
6074
CD2
TRP D
316
106.177
8.123
19.565
1.00
18.61
D

ATOM
6075
CE2
TRP D
316
105.107
8.146
18.646
1.00
18.90
D

ATOM
6076
CE3
TRP D
316
106.498
6.917
20.193
1.00
20.19
D

ATOM
6077
CD1
TRP D
316
105.959
10.206
18.767
1.00
20.28
D

ATOM
6078
NE1
TRP D
316
104.994
9.428
18.177
1.00
19.42
D

ATOM
6079
CZ2
TRP D
316
104.351
7.007
18.344
1.00
19.58
D

ATOM
6080
CZ3
TRP D
316
105.741
5.778
19.892
1.00
21.16
D

ATOM
6081
CH2
TRP D
316
104.682
5.835
18.975
1.00
20.34
D

ATOM
6082
C
TRP D
316
108.216
10.292
23.091
1.00
27.23
D

ATOM
6083
O
TRP D
316
108.854
9.311
23.519
1.00
27.64
D

ATOM
6084
N
LYS D
317
108.374
11.525
23.556
1.00
27.58
D

ATOM
6085
CA
LYS D
317
109.332
11.847
24.602
1.00
27.23
D

ATOM
6086
CS
LYS D
317
109.463
13.360
24.759
1.00
29.14
D

ATOM
6087
CG
LYS D
317
110.589
13.760
25.682
1.00
32.80
D

ATOM
6088
CD
LYS D
317
110.743
15.264
25.749
1.00
35.26
D

ATOM
6089
CE
LYS D
317
111.774
15.652
26.805
1.00
37.31
D

ATOM
6090
NZ
LYS D
317
111.793
17.120
27.068
1.00
37.03
D

ATOM
6091
C
LYS D
317
108.822
11.275
25.910
1.00
25.94
D

ATOM
6092
O
LYS D
317
109.570
10.685
26.689
1.00
25.94
D

ATOM
6093
N
LYS D
318
107.533
11.473
26.142
1.00
23.54
D

ATOM
6094
CA
LYS D
318
106.921
10.980
27.345
1.00
21.52
D

ATOM
6095
CB
LYS D
318
105.457
11.403
27.426
1.00
19.84
D

ATOM
6096
CG
LYS D
318
105.276
12.802
27.949
1.00
15.81
D

ATOM
6097
CD
LYS D
318
103.822
13.127
28.039
1.00
17.16
D

ATOM
6098
CE
LYS D
318
103.592
14.588
28.439
1.00
19.94
D

ATOM
6099
NZ
LYS D
318
104.446
15.524
27.676
1.00
22.18
D

ATOM
6100
C
LYS D
318
107.026
9.474
27.389
1.00
21.47
D

ATOM
6101
O
LYS D
318
107.353
8.890
28.423
1.00
22.72
D

ATOM
6102
N
LEU D
319
106.754
8.825
26.271
1.00
20.41
D

ATOM
6103
CA
LEU D
319
106.834
7.373
26.259
1.00
19.54
D

ATOM
6104
CB
LEU D
319
106.427
6.839
24.894
1.00
17.41
D

ATOM
6105
CG
LEU D
319
104.933
6.610
24.750
1.00
14.60
D

ATOM
6106
CD1
LEU D
319
104.590
6.417
23.307
1.00
15.84
D

ATOM
6107
CD2
LEU D
319
104.520
5.398
25.581
1.00
13.04
D

ATOM
6108
C
LEU D
319
108.232
6.901
26.605
1.00
19.33
D

ATOM
6109
O
LEU D
319
108.395
6.014
27.441
1.00
18.41
D

ATOM
6110
N
LEU D
320
109.239
7.493
25.961
1.00
20.82
D

ATOM
6111
CA
LEU D
320
110.624
7.099
26.217
1.00
21.24
D

ATOM
6112
CB
LEU D
320
111.589
7.926
25.344
1.00
17.94
D

ATOM
6113
CG
LEU D
320
111.710
7.492
23.869
1.00
18.89
D

ATOM
6114
CD1
LEU D
320
112.467
8.533
23.030
1.00
16.82
D

ATOM
6115
CD2
LEU D
320
112.402
6.158
23.797
1.00
15.44
D

ATOM
6116
C
LEU D
320
110.965
7.259
27.701
1.00
22.18
D

ATOM
6117
O
LEU D
320
111.574
6.383
28.310
1.00
23.23
D

ATOM
6118
N
ILE D
321
110.545
8.375
28.281
1.00
22.59
D

ATOM
6119
CA
ILE D
321
110.824
8.661
29.676
1.00
22.13
D

ATOM
6120
CB
ILE D
321
110.462
10.125
30.007
1.00
21.71
D

ATOM
6121
CG2
ILE D
321
110.406
10.336
31.509
1.00
20.64
D

ATOM
6122
CG1
ILE D
321
111.471
11.053
29.324
1.00
20.39
D

ATOM
6123
CD1
ILE D
321
111.312
12.527
29.639
1.00
17.62
D

ATOM
6124
C
ILE D
321
110.112
7.729
30.641
1.00
21.87
D

ATOM
6125
O
ILE D
321
110.726
7.204
31.551
1.00
23.61
D

ATOM
6126
N
SER D
322
108.819
7.526
30.449
1.00
22.79
D

ATOM
6127
CA
SER D
322
108.082
6.663
31.345
1.00
23.92
D

ATOM
6128
CB
SER D
322
106.610
6.624
30.943
1.00
24.36
D

ATOM
6129
OG
SER D
322
106.464
6.398
29.554
1.00
28.99
D

ATOM
6130
C
SER D
322
108.668
5.256
31.377
1.00
25.68
D

ATOM
6131
O
SER D
322
108.780
4.660
32.440
1.00
27.76
D

ATOM
6132
N
GLU D
323
109.041
4.718
30.222
1.00
24.70
D

ATOM
6133
CA
GLU D
323
109.625
3.389
30.188
1.00
23.55
D

ATOM
6134
CB
GLU D
323
109.581
2.835
28.775
1.00
24.33
D

ATOM
6135
CG
GLU D
323
108.228
2.303
28.385
1.00
25.11
D

ATOM
6136
CD
GLU D
323
107.953
0.951
29.008
1.00
26.37
D

ATOM
6137
OE1
GLU D
323
108.775
0.024
28.805
1.00
26.30
D

ATOM
6138
OE2
GLU D
323
106.920
0.809
29.695
1.00
27.36
D

ATOM
6139
C
GLU D
323
111.059
3.448
30.678
1.00
23.31
D

ATOM
6140
O
GLU D
323
111.773
2.443
30.684
1.00
23.15
D

ATOM
6141
N
ASN D
324
111.467
4.644
31.091
1.00
22.23
D

ATOM
6142
CA
ASN D
324
112.812
4.891
31.592
1.00
22.59
D

ATOM
6143
CB
ASN D
324
113.038
4.090
32.877
1.00
22.90
D

ATOM
6144
CG
ASN D
324
111.864
4.200
33.858
1.00
26.71
D

ATOM
6145
OD1
ASN D
324
111.346
5.294
34.109
1.00
25.11
D

ATOM
6146
ND2
ASN D
324
111.450
3.056
34.430
1.00
28.34
D

ATOM
6147
C
ASN D
324
113.911
4.565
30.560
1.00
23.12
D

ATOM
6148
O
ASN D
324
114.971
4.031
30.914
1.00
23.08
D

ATOM
6149
N
PHE D
325
113.667
4.881
29.285
1.00
22.49
D

ATOM
6150
CA
PHE D
325
114.673
4.613
28.246
1.00
22.20
D

ATOM
6151
CB
PHE D
325
114.005
4.332
26.882
1.00
18.54
D

ATOM
6152
CG
PHE D
325
113.296
2.991
26.806
1.00
18.28
D

ATOM
6153
CD1
PHE D
325
112.080
2.864
26.117
1.00
17.36
D

ATOM
6154
CD2
PHE D
325
113.828
1.860
27.425
1.00
17.01
D

ATOM
6155
CE1
PHE D
325
111.404
1.631
26.053
1.00
15.65
D

ATOM
6156
CE2
PHE D
325
113.165
0.617
27.369
1.00
16.41
D

ATOM
6157
CZ
PHE D
325
111.942
0.508
26.677
1.00
16.67
D

ATOM
6158
C
PHE D
325
115.640
5.798
28.136
1.00
21.95
D

ATOM
6159
O
PHE D
325
116.735
5.686
27.578
1.00
21.44
D

ATOM
6160
N
VAL D
326
115.240
6.925
28.707
1.00
21.18
D

ATOM
6161
CA
VAL D
326
116.059
8.113
28.642
1.00
21.85
D

ATOM
6162
CB
VAL D
326
115.922
8.765
27.238
1.00
21.90
D

ATOM
6163
CG1
VAL D
326
114.455
9.085
26.972
1.00
22.16
D

ATOM
6164
CG2
VAL D
326
116.772
10.016
27.133
1.00
19.90
D

ATOM
6165
C
VAL D
326
115.619
9.084
29.725
1.00
22.99
D

ATOM
6166
O
VAL D
326
114.453
9.105
30.121
1.00
23.26
D

ATOM
6167
N
SER D
327
116.571
9.869
30.215
1.00
26.57
D

ATOM
6168
CA
SER D
327
116.308
10.853
31.257
1.00
30.18
D

ATOM
6169
CB
SER D
327
117.552
11.111
32.099
1.00
28.88
D

ATOM
6170
OG
SER D
327
117.794
10.061
33.008
1.00
34.20
D

ATOM
6171
C
SER D
327
115.914
12.167
30.648
1.00
32.93
D

ATOM
6172
O
SER D
327
116.304
12.488
29.533
1.00
33.50
D

ATOM
6173
N
PRO D
328
115.141
12.958
31.384
1.00
36.30
D

ATOM
6174
CD
PRO D
328
114.483
12.591
32.644
1.00
38.28
D

ATOM
6175
CA
PRO D
328
114.693
14.269
30.923
1.00
38.59
D

ATOM
6176
CB
PRO D
328
113.988
14.834
32.140
1.00
38.19
D

ATOM
6177
CG
PRO D
328
113.360
13.609
32.728
1.00
39.16
D

ATOM
6178
C
PRO D
328
115.900
15.110
30.526
1.00
40.86
D

ATOM
6179
O
PRO D
328
115.886
15.787
29.496
1.00
42.18
D

ATOM
6180
N
LYS D
329
116.955
15.053
31.332
1.00
41.28
D

ATOM
6181
CA
LYS D
329
118.143
15.826
31.027
1.00
42.86
D

ATOM
6182
CB
LYS D
329
118.861
16.228
32.327
1.00
46.62
D

ATOM
6183
CG
LYS D
329
118.066
17.272
33.169
1.00
49.10
D

ATOM
6184
CD
LYS D
329
118.615
17.445
34.594
1.00
50.67
D

ATOM
6185
CE
LYS D
329
120.077
17.887
34.606
1.00
51.76
D

ATOM
6186
NZ
LYS D
329
120.645
17.988
35.993
1.00
51.50
D

ATOM
6187
C
LYS D
329
119.078
15.102
30.073
1.00
42.35
D

ATOM
6188
O
LYS D
329
120.060
15.671
29.609
1.00
43.19
D

ATOM
6189
N
GLY D
330
118.766
13.850
29.765
1.00
41.86
D

ATOM
6190
CA
GLY D
330
119.597
13.107
28.837
1.00
40.87
D

ATOM
6191
C
GLY D
330
118.961
13.089
27.456
1.00
42.32
D

ATOM
6192
O
GLY D
330
119.470
12.461
26.528
1.00
41.14
D

ATOM
6193
N
PHE D
331
117.849
13.798
27.304
1.00
44.29
D

ATOM
6194
CA
PHE D
331
117.148
13.809
26.026
1.00
46.40
D

ATOM
6195
CB
PHE D
331
115.887
14.660
26.119
1.00
47.33
D

ATOM
6196
CG
PHE D
331
114.896
14.396
25.016
1.00
49.12
D

ATOM
6197
CD1
PHE D
331
114.198
13.188
24.958
1.00
48.42
D

ATOM
6198
CD2
PHE D
331
114.658
15.359
24.033
1.00
49.78
D

ATOM
6199
CE1
PHE D
331
113.273
12.942
23.939
1.00
48.28
D

ATOM
6200
CE2
PHE D
331
113.735
15.128
23.008
1.00
49.07
D

ATOM
6201
CZ
PHE D
331
113.042
13.917
22.958
1.00
49.05
D

ATOM
6202
C
PHE D
331
117.983
14.276
24.846
1.00
46.95
D

ATOM
6203
O
PHE D
331
118.017
13.613
23.815
1.00
48.73
D

ATOM
6204
N
ASN D
332
118.651
15.414
24.997
1.00
47.11
D

ATOM
6205
CA
ASN D
332
119.477
15.972
23.932
1.00
46.02
D

ATOM
6206
CB
ASN D
332
120.255
17.161
24.463
1.00
47.82
D

ATOM
6207
CG
ASN D
332
119.497
18.440
24.335
1.00
49.50
D

ATOM
6208
OD1
ASN D
332
118.322
18.519
24.692
1.00
50.47
D

ATOM
6209
ND2
ASN D
332
120.165
19.468
23.815
1.00
52.34
D

ATOM
6210
C
ASN D
332
120.451
14.972
23.336
1.00
45.93
D

ATOM
6211
O
ASN D
332
120.420
14.681
22.140
1.00
45.54
D

ATOM
6212
N
SER D
333
121.326
14.443
24.175
1.00
46.43
D

ATOM
6213
CA
SER D
333
122.308
13.487
23.702
1.00
45.98
D

ATOM
6214
CB
SER D
333
123.043
12.863
24.885
1.00
46.48
D

ATOM
6215
OG
SER D
333
123.853
11.783
24.454
1.00
49.00
D

ATOM
6216
C
SER D
333
121.659
12.392
22.851
1.00
44.33
D

ATOM
6217
O
SER D
333
122.129
12.099
21.751
1.00
44.40
D

ATOM
6218
N
LED D
334
120.577
11.795
23.344
1.00
42.68
D

ATOM
6219
CA
LED D
334
119.912
10.728
22.591
1.00
41.52
D

ATOM
6220
CB
LED D
334
118.777
10.098
23.407
1.00
39.72
D

ATOM
6221
CG
LED D
334
117.873
9.152
22.604
1.00
38.51
D

ATOM
6222
CD1
LED D
334
118.687
7.997
22.053
1.00
37.25
D

ATOM
6223
CD2
LED D
334
116.746
8.651
23.475
1.00
37.57
D

ATOM
6224
C
LED D
334
119.352
11.228
21.268
1.00
39.88
D

ATOM
6225
O
LEU D
334
119.439
10.553
20.242
1.00
37.95
D

ATOM
6226
N
ASN D
335
118.758
12.410
21.304
1.00
39.39
D

ATOM
6227
CA
ASN D
335
118.202
12.973
20.096
1.00
39.71
D

ATOM
6228
CB
ASN D
335
117.463
14.263
20.399
1.00
40.92
D

ATOM
6229
CG
ASN D
335
116.080
14.255
19.829
1.00
42.75
D

ATOM
6230
OD1
ASN D
335
115.879
13.877
18.676
1.00
43.99
D

ATOM
6231
ND2
ASN D
335
115.108
14.669
20.630
1.00
44.96
D

ATOM
6232
C
ASN D
335
119.299
13.229
19.066
1.00
38.88
D

ATOM
6233
O
ASN D
335
119.209
12.772
17.926
1.00
39.28
D

ATOM
6234
N
LED D
336
120.341
13.945
19.469
1.00
36.54
D

ATOM
6235
CA
LED D
336
121.426
14.216
18.555
1.00
35.78
D

ATOM
6236
CB
LED D
336
122.488
15.081
19.230
1.00
35.28
D

ATOM
6237
CG
LED D
336
123.704
15.571
18.421
1.00
35.06
D

ATOM
6238
CD1
LED D
336
124.755
14.482
18.364
1.00
33.88
D

ATOM
6239
CD2
LED D
336
123.284
16.002
17.027
1.00
33.93
D

ATOM
6240
C
LED D
336
122.021
12.905
18.034
1.00
36.03
D

ATOM
6241
O
LED D
336
122.542
12.857
16.920
1.00
37.69
D

ATOM
6242
N
LYS D
337
121.919
11.833
18.812
1.00
36.19
D

ATOM
6243
CA
LYS D
337
122.439
10.529
18.378
1.00
37.20
D

ATOM
6244
CB
LYS D
337
122.452
9.533
19.547
1.00
38.40
D

ATOM
6245
CG
LYS D
337
123.706
9.512
20.409
1.00
40.10
D

ATOM
6246
CD
LYS D
337
124.743
8.543
19.848
1.00
41.01
D

ATOM
6247
CE
LYS D
337
125.896
8.283
20.827
1.00
41.41
D

ATOM
6248
NZ
LYS D
337
125.504
7.528
22.071
1.00
40.33
D

ATOM
6249
C
LYS D
337
121.576
9.939
17.257
1.00
37.31
D

ATOM
6250
O
LYS D
337
122.081
9.279
16.344
1.00
37.48
D

ATOM
6251
N
LED D
338
120.268
10.164
17.347
1.00
36.91
D

ATOM
6252
CA
LED D
338
119.332
9.654
16.351
1.00
36.87
D

ATOM
6253
CB
LED D
338
117.893
9.797
16.863
1.00
35.09
D

ATOM
6254
CG
LED D
338
117.529
8.902
18.052
1.00
33.33
D

ATOM
6255
CD1
LED D
338
116.175
9.300
18.621
1.00
31.89
D

ATOM
6256
CD2
LED D
338
117.533
7.450
17.600
1.00
31.70
D

ATOM
6257
C
LED D
338
119.513
10.412
15.044
1.00
37.22
D

ATOM
6258
O
LED D
338
119.418
9.841
13.968
1.00
36.68
D

ATOM
6259
N
SER D
339
119.791
11.703
15.161
1.00
37.23
D

ATOM
6260
CA
SER D
339
120.000
12.537
14.006
1.00
35.92
D

ATOM
6261
CB
SER D
339
120.390
13.933
14.426
1.00
34.24
D

ATOM
6262
OG
SER D
339
120.457
14.756
13.283
1.00
37.68
D

ATOM
6263
C
SER D
339
121.094
11.973
13.124
1.00
36.83
D

ATOM
6264
O
SER D
339
120.978
12.005
11.908
1.00
36.94
D

ATOM
6265
N
GLN D
340
122.161
11.467
13.735
1.00
36.98
D

ATOM
6266
CA
GLN D
340
123.266
10.895
12.975
1.00
37.54
D

ATOM
6267
CB
GLN D
340
124.443
10.581
13.883
1.00
38.76
D

ATOM
6268
CG
GLN D
340
124.489
11.408
15.144
1.00
42.76
D

ATOM
6269
CD
GLN D
340
125.519
12.491
15.095
1.00
43.21
D

ATOM
6270
OE1
GLN D
340
125.816
13.113
16.105
1.00
43.96
D

ATOM
6271
NE2
GLN D
340
126.077
12.727
13.917
1.00
47.75
D

ATOM
6272
C
GLN D
340
122.786
9.592
12.376
1.00
38.02
D

ATOM
6273
O
GLN D
340
123.099
9.254
11.235
1.00
36.84
D

ATOM
6274
N
LYS D
341
122.023
8.857
13.172
1.00
38.91
D

ATOM
6275
CA
LYS D
341
121.503
7.564
12.759
1.00
40.04
D

ATOM
6276
CB
LYS D
341
120.908
6.842
13.979
1.00
41.15
D

ATOM
6277
CG
LYS D
341
120.440
5.417
13.722
1.00
43.83
D

ATOM
6278
CD
LYS D
341
121.542
4.580
13.081
1.00
46.84
D

ATOM
6279
CE
LYS D
341
121.018
3.233
12.559
1.00
48.14
D

ATOM
6280
NZ
LYS D
341
122.101
2.428
11.901
1.00
48.02
D

ATOM
6281
C
LYS D
341
120.463
7.656
11.641
1.00
40.03
D

ATOM
6282
O
LYS D
341
120.548
6.935
10.647
1.00
40.71
D

ATOM
6283
N
TYR D
342
119.494
8.551
11.804
1.00
39.52
D

ATOM
6284
CA
TYR D
342
118.413
8.726
10.840
1.00
39.22
D

ATOM
6285
CB
TYR D
342
117.084
8.349
11.504
1.00
40.25
D

ATOM
6286
CG
TYR D
342
117.093
6.975
12.120
1.00
41.96
D

ATOM
6287
CD1
TYR D
342
117.151
5.839
11.322
1.00
44.58
D

ATOM
6288
CE1
TYR D
342
117.195
4.559
11.887
1.00
46.16
D

ATOM
6289
CD2
TYR D
342
117.076
6.805
13.501
1.00
43.49
D

ATOM
6290
CE2
TYR D
342
117.119
5.530
14.078
1.00
44.33
D

ATOM
6291
CZ
TYR D
342
117.180
4.412
13.263
1.00
45.41
D

ATOM
6292
OH
TYR D
342
117.244
3.145
13.796
1.00
44.64
D

ATOM
6293
C
TYR D
342
118.315
10.155
10.287
1.00
38.30
D

ATOM
6294
O
TYR D
342
117.437
10.926
10.687
1.00
38.68
D

ATOM
6295
N
PRO D
343
119.207
10.522
9.354
1.00
36.69
D

ATOM
6296
CD
PRO D
343
120.303
9.690
8.831
1.00
33.93
D

ATOM
6297
CA
PRO D
343
119.222
11.859
8.744
1.00
35.64
D

ATOM
6298
CB
PRO D
343
120.322
11.747
7.701
1.00
33.94
D

ATOM
6299
CG
PRO D
343
121.227
10.708
8.264
1.00
33.00
D

ATOM
6300
C
PRO D
343
117.897
12.243
8.100
1.00
36.66
D

ATOM
6301
O
PRO D
343
117.387
13.353
8.298
1.00
36.68
D

ATOM
6302
N
LYS D
344
117.345
11.306
7.333
1.00
37.98
D

ATOM
6303
CA
LYS D
344
116.097
11.521
6.600
1.00
38.87
D

ATOM
6304
CB
LYS D
344
116.021
10.554
5.402
1.00
40.52
D

ATOM
6305
CG
LYS D
344
116.552
9.140
5.658
1.00
43.94
D

ATOM
6306
CD
LYS D
344
115.598
8.274
6.494
1.00
44.39
D

ATOM
6307
CE
LYS D
344
116.370
7.166
7.227
1.00
43.37
D

ATOM
6308
NZ
LYS D
344
117.439
7.751
8.094
1.00
37.93
D

ATOM
6309
C
LYS D
344
114.791
11.471
7.396
1.00
37.24
D

ATOM
6310
O
LYS D
344
113.779
12.011
6.947
1.00
38.60
D

ATOM
6311
N
LEU D
345
114.808
10.851
8.572
1.00
34.93
D

ATOM
6312
CA
LEU D
345
113.597
10.766
9.382
1.00
32.64
D

ATOM
6313
CB
LEU D
345
113.670
9.573
10.329
1.00
31.24
D

ATOM
6314
CG
LEU D
345
113.726
8.216
9.628
1.00
29.39
D

ATOM
6315
CD1
LEU D
345
113.660
7.118
10.667
1.00
30.86
D

ATOM
6316
CD2
LEU D
345
112.560
8.084
8.666
1.00
30.92
D

ATOM
6317
C
LEU D
345
113.376
12.033
10.176
1.00
31.59
D

ATOM
6318
O
LEU D
345
114.318
12.780
10.422
1.00
32.92
D

ATOM
6319
N
SER D
346
112.130
12.298
10.557
1.00
30.59
D

ATOM
6320
CA
SER D
346
111.836
13.500
11.338
1.00
29.97
D

ATOM
6321
CB
SER D
346
110.377
13.931
11.158
1.00
29.48
D

ATOM
6322
OG
SER D
346
109.498
12.856
11.422
1.00
30.59
D

ATOM
6323
C
SER D
346
112.101
13.212
12.800
1.00
29.74
D

ATOM
6324
O
SER D
346
112.387
12.069
13.184
1.00
28.91
D

ATOM
6325
N
GLN D
347
111.992
14.233
13.634
1.00
28.38
D

ATOM
6326
CA
GLN D
347
112.255
13.991
15.036
1.00
28.40
D

ATOM
6327
CB
GLN D
347
112.237
15.291
15.818
1.00
29.66
D

ATOM
6328
CG
GLN D
347
112.819
15.144
17.190
1.00
32.02
D

ATOM
6329
CD
GLN D
347
112.905
16.474
17.879
1.00
35.29
D

ATOM
6330
OE1
GLN D
347
111.889
17.161
18.035
1.00
38.15
D

ATOM
6331
NE2
GLN D
347
114.111
16.861
18.292
1.00
33.64
D

ATOM
6332
C
GLN D
347
111.277
13.007
15.663
1.00
26.76
D

ATOM
6333
O
GLN D
347
111.694
12.085
16.357
1.00
26.57
D

ATOM
6334
N
GLN D
348
109.984
13.203
15.427
1.00
25.38
D

ATOM
6335
CA
GLN D
348
108.996
12.306
16.001
1.00
24.96
D

ATOM
6336
CS
GLN D
348
107.581
12.739
15.657
1.00
24.21
D

ATOM
6337
CG
GLN D
348
107.267
14.152
16.034
1.00
24.28
D

ATOM
6338
CD
GLN D
348
107.648
15.126
14.947
1.00
23.84
D

ATOM
6339
OE1
GLN D
348
108.598
14.899
14.211
1.00
24.03
D

ATOM
6340
NE2
GLN D
348
106.908
16.224
14.845
1.00
24.64
D

ATOM
6341
C
GLN D
348
109.209
10.896
15.483
1.00
26.54
D

ATOM
6342
O
GLN D
348
109.118
9.921
16.233
1.00
27.22
D

ATOM
6343
N
ASP D
349
109.499
10.791
14.193
1.00
26.70
D

ATOM
6344
CA
ASP D
349
109.718
9.500
13.588
1.00
26.16
D

ATOM
6345
CB
ASP D
349
109.918
9.666
12.086
1.00
30.05
D

ATOM
6346
CG
ASP D
349
108.666
9.338
11.295
1.00
33.76
D

ATOM
6347
OD1
ASP D
349
107.598
9.889
11.612
1.00
35.36
D

ATOM
6348
OD2
ASP D
349
108.754
8.521
10.354
1.00
37.16
D

ATOM
6349
C
ASP D
349
110.900
8.775
14.220
1.00
25.17
D

ATOM
6350
O
ASP D
349
110.815
7.578
14.508
1.00
25.67
D

ATOM
6351
N
ARG D
350
111.999
9.491
14.430
1.00
23.55
D

ATOM
6352
CA
ARG D
350
113.194
8.906
15.047
1.00
23.54
D

ATOM
6353
CS
ARG D
350
114.265
9.981
15.252
1.00
25.20
D

ATOM
6354
CG
ARG D
350
114.885
10.512
13.994
1.00
25.82
D

ATOM
6355
CD
ARG D
350
115.595
11.837
14.220
1.00
25.92
D

ATOM
6356
NE
ARG D
350
116.255
12.230
12.977
1.00
28.94
D

ATOM
6357
CZ
ARG D
350
116.707
13.448
12.698
1.00
29.47
D

ATOM
6358
NH1
ARG D
350
116.590
14.440
13.568
1.00
32.83
D

ATOM
6359
NH2
ARG D
350
117.281
13.673
11.534
1.00
31.17
D

ATOM
6360
C
ARG D
350
112.831
8.343
16.416
1.00
23.18
D

ATOM
6361
O
ARG D
350
112.968
7.148
16.679
1.00
22.24
D

ATOM
6362
N
LEU D
351
112.376
9.242
17.282
1.00
21.94
D

ATOM
6363
CA
LEU D
351
111.991
8.890
18.627
1.00
20.55
D

ATOM
6364
CB
LEU D
351
111.307
10.082
19.297
1.00
18.30
D

ATOM
6365
CG
LEU D
351
112.227
11.278
19.543
1.00
15.70
D

ATOM
6366
CD1
LEU D
351
111.401
12.443
19.998
1.00
14.97
D

ATOM
6367
CD2
LEU D
351
113.315
10.927
20.561
1.00
12.36
D

ATOM
6368
C
LEU D
351
111.081
7.671
18.627
1.00
20.79
D

ATOM
6369
O
LEU D
351
111.175
6.824
19.508
1.00
21.85
D

ATOM
6370
N
ARG D
352
110.211
7.569
17.631
1.00
21.27
D

ATOM
6371
CA
ARG D
352
109.333
6.421
17.566
1.00
22.32
D

ATOM
6372
CB
ARG D
352
108.251
6.616
16.517
1.00
23.50
D

ATOM
6373
CG
ARG D
352
107.278
5.440
16.398
1.00
25.41
D

ATOM
6374
CD
ARG D
352
106.075
5.874
15.568
1.00
26.94
D

ATOM
6375
NE
ARG D
352
106.491
6.312
14.248
1.00
27.67
D

ATOM
6376
CZ
ARG D
352
106.345
5.590
13.151
1.00
27.98
D

ATOM
6377
NH1
ARG D
352
105.772
4.384
13.223
1.00
28.77
D

ATOM
6378
NH2
ARG D
352
106.801
6.071
11.997
1.00
28.35
D

ATOM
6379
C
ARG D
352
110.132
5.156
17.257
1.00
22.65
D

ATOM
6380
O
ARG D
352
109.852
4.088
17.809
1.00
22.75
D

ATOM
6381
N
LEU D
353
111.129
5.236
16.389
1.00
23.22
D

ATOM
6382
CA
LEU D
353
111.877
4.014
16.139
1.00
25.64
D

ATOM
6383
CB
LEUD D
353
112.853
4.180
14.974
1.00
27.60
D

ATOM
6384
CG
LEU D
353
112.211
4.675
13.687
1.00
31.53
D

ATOM
6385
CD1
LEU D
353
113.257
4.543
12.590
1.00
34.73
D

ATOM
6386
CD2
LEU D
353
110.948
3.847
13.321
1.00
34.02
D

ATOM
6387
C
LEU D
353
112.640
3.650
17.408
1.00
24.34
D

ATOM
6388
O
LEU D
353
112.766
2.477
17.748
1.00
24.26
D

ATOM
6389
N
SER D
354
113.135
4.654
18.124
1.00
24.48
D

ATOM
6390
CA
SER D
354
113.888
4.379
19.339
1.00
24.64
D

ATOM
6391
CB
SER D
354
114.399
5.670
19.953
1.00
24.29
O

ATOM
6392
OG
SER D
354
115.774
5.509
20.223
1.00
27.22
O

ATOM
6393
C
SER D
354
113.045
3.623
20.345
1.00
23.77
D

ATOM
6394
O
SER D
354
113.439
2.566
20.828
1.00
22.40
D

ATOM
6395
N
PHE D
355
111.879
4.169
20.646
1.00
23.57
D

ATOM
6396
CA
PHE D
355
110.979
3.533
21.573
1.00
25.63
D

ATOM
6397
CB
PHE D
355
109.660
4.283
21.596
1.00
26.61
D

ATOM
6398
CG
PHE D
355
108.725
3.795
22.636
1.00
27.78
D

ATOM
6399
CD1
PHE D
355
109.055
3.919
23.978
1.00
29.88
D

ATOM
6400
CD2
PHE D
355
107.526
3.189
22.286
1.00
29.67
D

ATOM
6401
CE1
PHE D
355
108.205
3.443
24.972
1.00
29.34
D

ATOM
6402
CE2
PHE D
355
106.664
2.707
23.269
1.00
30.25
D

ATOM
6403
CZ
PHE D
355
107.011
2.836
24.614
1.00
29.64
D

ATOM
6404
C
PHE D
355
110.731
2.089
21.156
1.00
26.53
D

ATOM
6405
O
PHE D
355
110.970
1.156
21.920
1.00
26.93
D

ATOM
6406
N
LEU D
356
110.257
1.904
19.931
1.00
27.97
D

ATOM
6407
CA
LEU D
356
109.975
0.557
19.441
1.00
29.40
D

ATOM
6408
CB
LEU D
356
109.502
0.601
17.990
1.00
29.41
D

ATOM
6409
CG
LEU D
356
108.233
1.408
17.701
1.00
30.81
D

ATOM
6410
CD1
LEU D
356
108.091
1.510
16.193
1.00
30.03
D

ATOM
6411
CD2
LEU D
356
107.001
0.766
18.334
1.00
27.79
D

ATOM
6412
C
LEU D
35
111.164
−0.387
19.557
1.00
29.19
D

ATOM
6413
O
LEU D
356
111.011
−1.540
19.954
1.00
29.03
D

ATOM
6414
N
GLU D
357
112.348
0.106
19.223
1.00
29.15
D

ATOM
6415
CA
GLU D
357
113.525
−0.723
19.296
1.00
30.63
D

ATOM
6416
CB
GLU D
357
114.677
−0.053
18.560
1.00
32.16
D

ATOM
6417
CG
GLU D
357
115.697
−1.025
18.007
1.00
37.30
D

ATOM
6418
CD
GLU D
357
117.086
−0.418
17.930
1.00
40.82
D

ATOM
6419
OE1
GLU D
357
117.248
0.639
17.262
1.00
41.37
D

ATOM
6420
OE2
GLU D
357
118.017
−1.000
18.548
1.00
41.48
D

ATOM
6421
C
GLU D
357
113.946
−1.025
20.741
1.00
32.26
D

ATOM
6422
O
GLU D
357
114.599
−2.041
21.016
1.00
31.90
D

ATOM
6423
N
ASN D
358
113.571
−0.148
21.665
1.00
29.36
D

ATOM
6424
CA
ASN D
358
113.939
−0.341
23.046
1.00
27.42
D

ATOM
6425
CB
ASN D
358
114.060
1.000
23.750
1.00
27.90
D

ATOM
6426
CG
ASN D
358
115.443
1.598
23.610
1.00
28.81
D

ATOM
6427
OD1
ASN D
358
115.621
2.656
23.006
1.00
29.58
D

ATOM
6428
ND2
ASN D
358
116.439
0.916
24.171
1.00
29.80
D

ATOM
6429
C
ASN D
358
112.996
−1.248
23.793
1.00
27.49
D

ATOM
6430
O
ASN D
358
113.404
−1.974
24.700
1.00
27.75
D

ATOM
6431
N
ILE D
359
111.732
−1.217
23.408
1.00
27.57
D

ATOM
6432
CA
ILE D
359
110.757
−2.076
24.046
1.00
28.89
D

ATOM
6433
CB
ILE D
359
109.361
−1.821
23.510
1.00
29.72
D

ATOM
6434
CG2
ILE D
359
108.342
−2.575
24.322
1.00
28.76
D

ATOM
6435
OG1
ILE D
359
109.058
−0.336
23.581
1.00
32.82
D

ATOM
6436
CD1
ILE D
359
108.196
0.120
22.444
1.00
36.53
D

ATOM
6437
C
ILE D
359
111.161
−3.466
23.629
1.00
28.09
D

ATOM
6438
O
ILE D
359
111.164
−4.389
24.425
1.00
27.60
D

ATOM
6439
N
PHE D
360
111.518
−3.592
22.361
1.00
29.39
D

ATOM
6440
CA
PHE D
360
111.926
−4.864
21.810
1.00
30.15
D

ATOM
6441
CB
PHE D
360
112.415
−4.654
20.372
1.00
32.47
D

ATOM
6442
CG
PHE D
360
112.998
−5.885
19.738
1.00
33.66
D

ATOM
6443
CD1
PHE D
360
112.236
−7.045
19.600
1.00
34.21
D

ATOM
6444
CD2
PHE D
360
114.327
−5.898
19.326
1.00
34.66
D

ATOM
6445
CE1
PHE D
360
112.790
−8.201
19.071
1.00
34.86
D

ATOM
6446
CE2
PHE D
360
114.894
−7.044
18.796
1.00
36.23
D

ATOM
6447
CZ
PHE D
360
114.124
−8.202
18.670
1.00
35.77
D

ATOM
6448
C
PHE D
360
113.015
−5.503
22.654
1.00
29.32
D

ATOM
6449
O
PHE D
360
112.879
−6.641
23.092
1.00
29.82
D

ATOM
6450
N
ILE D
361
114.093
−4.762
22.880
1.00
28.24
D

ATOM
6451
CA
ILE D
361
115.222
−5.254
23.660
1.00
26.57
D

ATOM
6452
CB
ILE D
361
116.376
−4.219
23.597
1.00
26.56
D

ATOM
6453
CG2
ILE D
361
117.540
−4.638
24.502
1.00
24.26
D

ATOM
6454
CG1
ILE D
361
116.855
−4.117
22.140
1.00
25.22
D

ATOM
6455
CD1
ILE D
361
117.841
−3.000
21.868
1.00
25.88
D

ATOM
6456
C
ILE D
361
114.834
−5.578
25.111
1.00
25.14
D

ATOM
6457
O
ILE D
361
115.238
−6.610
25.656
1.00
24.17
D

ATOM
6458
N
LEU D
362
114.027
−4.712
25.718
1.00
22.80
D

ATOM
6459
CA
LEU D
362
113.591
−4.915
27.098
1.00
23.19
D

ATOM
6460
CB
LEU D
362
112.801
−3.700
27.576
1.00
20.92
D

ATOM
6461
CG
LEU D
362
112.565
−3.604
29.077
1.00
20.66
D

ATOM
6462
CD1
LEU D
362
113.860
−3.753
29.867
1.00
18.78
D

ATOM
6463
CD2
LEU D
362
111.917
−2.273
29.338
1.00
20.71
D

ATOM
6464
C
LEU D
362
112.773
−6.196
27.330
1.00
23.63
D

ATOM
6465
O
LEU D
362
112.997
−6.915
28.311
1.00
23.67
D

ATOM
6466
N
LYS D
363
111.824
−6.453
26.434
1.00
23.53
D

ATOM
6467
CA
LYS D
363
110.986
−7.639
26.477
1.00
24.42
D

ATOM
6468
CB
LYS D
363
110.156
−7.743
25.191
1.00
26.43
D

ATOM
6469
CG
LYS D
363
108.730
−7.209
25.270
1.00
30.86
D

ATOM
6470
CD
LYS D
363
108.669
−5.840
25.929
1.00
33.41
D

ATOM
6471
CE
LYS D
363
107.226
−5.421
26.252
1.00
35.72
D

ATOM
6472
NZ
LYS D
363
107.204
−4.294
27.264
1.00
35.50
D

ATOM
6473
C
LYS D
363
111.901
−8.859
26.573
1.00
25.36
D

ATOM
6474
O
LYS D
363
111.629
−9.802
27.311
1.00
25.60
D

ATOM
6475
N
ASN D
364
112.988
−8.829
25.809
1.00
25.23
D

ATOM
6476
CA
ASN D
364
113.935
−9.927
25.799
1.00
25.39
D

ATOM
6477
CB
ASN D
364
114.980
−9.737
24.712
1.00
25.02
D

ATOM
6478
CG
ASN D
364
114.436
−9.985
23.348
1.00
26.12
D

ATOM
6479
OD1
ASN D
364
115.038
−9.589
22.348
1.00
25.32
D

ATOM
6480
ND2
ASN D
364
113.286
−10.66
223.283
1.00
27.95
D

ATOM
6481
C
ASN D
364
114.640
−10.030
27.118
1.00
26.63
D

ATOM
6482
O
ASN D
364
114.785
−11.120
27.665
1.00
28.76
D

ATOM
6483
N
TRP D
365
115.101
−8.901
27.635
1.00
26.04
D

ATOM
6484
CA
TRP D
365
115.794
−8.937
28.906
1.00
25.62
D

ATOM
6485
CB
TRP D
365
116.211
−7.535
29.357
1.00
23.36
D

ATOM
6486
CG
TRP D
365
117.514
−7.035
28.789
1.00
19.48
D

ATOM
6487
CD2
TRP D
365
118.801
−7.069
29.427
1.00
16.99
D

ATOM
6488
CE2
TRP D
365
119.706
−6.410
28.572
1.00
15.60
D

ATOM
6489
CE3
TRP D
365
119.275
−7.589
30.640
1.00
15.17
D

ATOM
6490
CD1
TRP D
365
117.691
−6.387
27.613
1.00
17.39
D

ATOM
6491
NE1
TRP D
365
119.001
−6.003
27.473
1.00
14.98
D

ATOM
6492
CZ2
TRP D
365
121.072
−6.249
28.892
1.00
15.36
D

ATOM
6493
CZ3
TRP D
365
120.628
−7.428
30.956
1.00
13.84
D

ATOM
6494
CH2
TRP D
365
121.509
−6.762
30.081
1.00
10.82
D

ATOM
6495
C
TRP D
365
114.868
−9.538
29.947
1.00
26.26
D

ATOM
6496
O
TRP D
365
115.267
−10.422
30.693
1.00
28.48
D

ATOM
6497
N
TYR D
366
113.621
−9.084
29.956
1.00
24.80
D

ATOM
6498
CA
TYR D
366
112.641
−9.530
30.934
1.00
23.32
D

ATOM
6499
CB
TYR D
366
111.480
−8.553
30.947
1.00
17.63
D

ATOM
6500
CG
TYR D
366
111.793
−7.211
31.597
1.00
16.02
D

ATOM
6501
CD1
TYR D
366
113.058
−6.914
32.118
1.00
14.32
D

ATOM
6502
CE1
TYR D
366
113.304
−5.681
32.726
1.00
11.48
D

ATOM
6503
CD2
TYR D
366
110.808
−6.243
31.712
1.00
13.79
D

ATOM
6504
CE2
TYR D
366
111.054
−5.033
32.320
1.00
11.61
D

ATOM
6505
CZ
TYR D
366
112.283
−4.760
32.812
1.00
11.97
D

ATOM
6506
OH
TYR D
366
112.475
−3.532
33.364
1.00
15.79
D

ATOM
6507
C
TYR D
366
112.112
−10.939
30.762
1.00
25.30
D

ATOM
6508
O
TYR D
366
111.620
−11.548
31.715
1.00
25.60
D

ATOM
6509
N
ASN D
367
112.227
−11.441
29.538
1.00
27.79
D

ATOM
6510
CA
ASN D
367
111.757
−12.770
29.160
1.00
28.52
D

ATOM
6511
CE
ASN D
367
111.596
−12.837
27.642
1.00
29.23
D

ATOM
6512
CG
ASN D
367
111.047
−14.162
27.168
1.00
29.51
D

ATOM
6513
OD1
ASN D
367
111.045
−15.165
27.907
1.00
29.16
D

ATOM
6514
ND2
ASN D
367
110.588
−14.183
25.915
1.00
28.51
D

ATOM
6515
C
ASN D
367
112.706
−13.872
29.617
1.00
28.04
D

ATOM
6516
O
ASN D
367
113.779
−14.076
29.042
1.00
28.99
D

ATOM
6517
N
PRO D
368
112.306
−14.606
30.659
1.00
27.46
D

ATOM
6518
CD
PRO D
368
111.038
−14.427
31.394
1.00
27.49
D

ATOM
6519
CA
PRO D
368
113.094
−15.701
31.228
1.00
26.35
D

ATOM
6520
CB
PRO D
368
112.174
−16.249
32.313
1.00
26.40
D

ATOM
6521
CG
PRO D
368
111.350
−15.041
32.703
1.00
26.24
D

ATOM
6522
C
PRO D
368
113.470
−16.766
30.207
1.00
25.90
D

ATOM
6523
O
PRO D
368
114.556
−17.338
30.270
1.00
23.69
D

ATOM
6524
N
LYS D
369
112.570
−17.027
29.264
1.00
26.98
D

ATOM
6525
CA
LYS D
369
112.815
−18.051
28.249
1.00
27.69
D

ATOM
6526
CB
LYS D
369
111.483
−18.478
27.605
1.00
27.37
D

ATOM
6527
CG
LYS D
369
111.523
−19.857
26.933
1.00
28.34
D

ATOM
6528
CD
LYS D
369
110.159
−20.280
26.431
0.00
28.71
D

ATOM
6529
CE
LYS D
369
109.692
−19.395
25.288
0.00
29.07
D

ATOM
6530
NZ
LYS D
369
108.385
−19.851
24.737
0.00
29.21
D

ATOM
6531
C
LYS D
369
113.815
−17.602
27.170
1.00
28.21
D

ATOM
6532
O
LYS D
369
114.404
−18.432
26.466
1.00
27.80
D

ATOM
6533
N
PHE D
370
114.027
−16.295
27.055
1.00
28.20
D

ATOM
6534
CA
PHE D
370
114.945
−15.779
26.048
1.00
29.53
D

ATOM
6535
CB
PHE D
370
114.804
−14.267
25.930
1.00
30.24
D

ATOM
6536
CG
PHE D
370
115.741
−13.647
24.926
1.00
31.46
D

ATOM
6537
CD1
PHE D
370
117.107
−13.497
25.208
1.00
32.17
D

ATOM
6538
CD2
PHE D
370
115.253
−13.184
23.711
1.00
31.98
D

ATOM
6539
CE1
PHE D
370
117.970
−12.894
24.301
1.00
30.34
D

ATOM
6540
CE2
PHE D
370
116.105
−12.580
22.795
1.00
32.40
D

ATOM
6541
CZ
PHE D
370
117.473
−12.434
23.098
1.00
31.69
D

ATOM
6542
C
PHE D
370
116.418
−16.125
26.250
1.00
29.47
D

ATOM
6543
O
PHE D
370
116.990
−15.909
27.323
1.00
30.76
D

ATOM
6544
N
VAL D
371
117.038
−16.623
25.186
1.00
28.02
D

ATOM
6545
CA
VAL D
371
118.441
−16.986
25.252
1.00
27.30
D

ATOM
6546
CB
VAL D
371
118.648
−18.446
24.756
1.00
26.04
D

ATOM
6547
CG1
VAL D
371
120.104
−18.829
24.825
1.00
22.81
D

ATOM
6548
CG2
VAL D
371
117.827
−19.396
25.624
1.00
22.71
D

ATOM
6549
C
VAL D
371
119.309
−15.995
24.469
1.00
28.27
D

ATOM
6550
O
VAL D
371
119.221
−15.880
23.248
1.00
27.93
D

ATOM
6551
N
PRO D
372
120.161
−15.251
25.188
1.00
29.70
D

ATOM
6552
CD
PRO D
372
120.326
−15.276
26.648
1.00
29.18
D

ATOM
6553
CA
PRO D
372
121.057
−14.258
24.597
1.00
31.17
D

ATOM
6554
CB
PRO D
372
121.744
−13.642
25.816
1.00
29.97
D

ATOM
6555
CG
PRO D
372
120.796
−13.886
26.914
1.00
30.31
D

ATOM
6556
C
PRO D
372
122.071
−14.884
23.659
1.00
32.23
D

ATOM
6557
O
PRO D
372
122.136
−16.104
23.515
1.00
33.92
D

ATOM
6558
N
GLN D
373
122.860
−14.033
23.019
1.00
32.64
D

ATOM
6559
CA
GLN D
373
123.907
−14.511
22.144
1.00
31.91
D

ATOM
6560
CB
GLN D
373
123.945
−13.701
20.865
1.00
31.03
D

ATOM
6561
CG
GLN D
373
124.881
−14.279
19.845
1.00
31.69
D

ATOM
6562
CD
GLN D
373
125.575
−13.202
19.069
1.00
32.49
D

ATOM
6563
OE1
GLN D
373
124.937
−12.328
18.502
1.00
33.06
D

ATOM
6564
NE2
GLN D
373
126.892
−13.251
19.045
1.00
34.46
D

ATOM
6565
C
GLN D
373
125.203
−14.315
22.925
1.00
31.35
D

ATOM
6566
O
GLN D
373
125.612
−13.192
23.224
1.00
31.52
D

ATOM
6567
N
ARG D
374
125.842
−15.418
23.264
1.00
29.71
D

ATOM
6568
CA
ARG D
374
127.059
−15.342
24.024
1.00
29.87
D

ATOM
6569
CB
ARG D
374
127.054
−16.417
25.102
1.00
30.39
D

ATOM
6570
CG
ARG D
374
128.347
−16.511
25.854
1.00
31.03
D

ATOM
6571
CD
ARG D
374
128.261
−17.597
26.873
1.00
31.27
D

ATOM
6572
NE
ARG D
374
129.475
−17.599
27.658
1.00
32.88
D

ATOM
6573
CZ
ARG D
374
129.738
−18.450
28.637
1.00
33.11
D

ATOM
6574
NH1
ARG D
374
128.856
−19.390
28.956
1.00
31.68
D

ATOM
6575
NH2
ARG D
374
130.889
−18.343
29.301
1.00
33.83
D

ATOM
6576
C
ARG D
374
128.306
−15.477
23.161
1.00
30.20
D

ATOM
6577
O
ARG D
374
128.383
−16.319
22.268
1.00
30.52
D

ATOM
6578
N
THR D
375
129.298
−14.654
23.463
1.00
30.06
D

ATOM
6579
CA
THR D
375
130.543
−14.641
22.724
1.00
29.07
D

ATOM
6580
CB
THR D
375
130.574
−13.423
21.801
1.00
29.18
D

ATOM
6581
OG1
THR D
375
129.254
−13.177
21.294
1.00
30.22
D

ATOM
6582
CG2
THR D
375
131.520
−13.650
20.650
1.00
27.55
D

ATOM
6583
C
THR D
375
131.666
−14.506
23.749
1.00
29.99
D

ATOM
6584
O
THR D
375
131.743
−13.505
24.473
1.00
30.81
D

ATOM
6585
N
THR D
376
132.537
−15.504
23.824
1.00
29.02
D

ATOM
6586
CA
THR D
376
133.631
−15.459
24.789
1.00
28.35
D

ATOM
6587
CB
THR D
376
133.775
−16.810
25.551
1.00
26.89
D

ATOM
6588
OG1
THR D
376
132.516
−17.174
26.129
1.00
24.67
D

ATOM
6589
CG2
THR D
376
134.822
−16.700
26.648
1.00
25.06
D

ATOM
6590
C
THR D
376
134.959
−15.155
24.120
1.00
29.32
D

ATOM
6591
O
THR D
376
135.386
−15.886
23.234
1.00
28.86
D

ATOM
6592
N
LEU D
377
135.616
−14.081
24.555
1.00
31.19
D

ATOM
6593
CA
LEU D
377
136.916
−13.701
24.001
1.00
33.04
D

ATOM
6594
CS
LEU D
377
136.888
−12.242
23.558
1.00
31.62
D

ATOM
6595
CG
LEU D
377
135.621
−11.843
22.793
1.00
32.74
D

ATOM
6596
CD1
LEU D
377
135.718
−10.396
22.376
1.00
32.01
D

ATOM
6597
CD2
LEU D
377
135.430
−12.735
21.590
1.00
32.02
D

ATOM
6598
C
LEU D
377
138.006
−13.907
25.044
1.00
35.05
D

ATOM
6599
O
LEU D
377
137.733
−13.877
26.241
1.00
36.55
D

ATOM
6600
N
ARG D
378
139.238
−14.122
24.590
1.00
37.30
D

ATOM
6601
CA
ARG D
378
140.381
−14.341
25.487
1.00
38.75
D

ATOM
6602
CS
ARG D
378
141.620
−14.732
24.661
1.00
41.44
D

ATOM
6603
CG
ARG D
378
142.735
−15.467
25.412
1.00
45.29
D

ATOM
6604
CD
ARG D
378
143.962
−15.705
24.499
1.00
49.27
D

ATOM
6605
NE
ARG D
378
144.615
−14.445
24.116
1.00
53.86
D

ATOM
6606
CZ
ARG D
378
145.636
−14.322
23.260
1.00
55.92
D

ATOM
6607
NH1
ARG D
378
146.147
−15.400
22.666
1.00
55.78
D

ATOM
6608
NH2
ARG D
378
146.152
−13.109
23.009
1.00
55.08
D

ATOM
6609
C
ARG D
378
140.663
−13.056
26.259
1.00
38.43
D

ATOM
6610
O
ARG D
378
140.498
−11.956
25.723
1.00
37.88
D

ATOM
6611
N
GLY D
379
141.098
−13.206
27.510
1.00
38.54
D

ATOM
6612
CA
GLY D
379
141.408
−12.058
28.349
1.00
38.37
D

ATOM
6613
C
GLY D
379
142.901
−11.817
28.563
1.00
38.46
D

ATOM
6614
O
GLY D
379
143.704
−12.014
27.646
1.00
39.93
D

ATOM
6615
N
HIS
D380
143.270
−11.390
29.771
1.00
36.54
D

ATOM
6616
CA
HIS D
380
144.663
−11.116
30.118
1.00
35.40
D

ATOM
6617
CB
HIS D
380
144.735
−10.098
31.259
1.00
32.54
D

ATOM
6618
CG
HIS D
380
144.169
−8.762
30.910
1.00
29.64
D

ATOM
6619
CD2
HIS D
380
144.748
−7.541
30.837
1.00
29.11
D

ATOM
6620
ND1
HIS D
380
142.845
−8.580
30.581
1.00
28.66
D

ATOM
6621
CE1
HIS D
380
142.630
−7.302
30.323
1.00
26.84
D

ATOM
6622
NE2
HIS D
380
143.768
−6.650
30.470
1.00
28.50
D

ATOM
6623
C
HIS D
380
145.400
−12.389
30.524
1.00
35.86
D

ATOM
6624
O
HIS D
380
144.796
−13.450
30.606
1.00
35.08
D

ATOM
6625
N
MSE D
381
146.699
−12.287
30.790
1.00
37.57
D

ATOM
6626
CA
MSE D
381
147.467
−13.465
31.172
1.00
40.68
D

ATOM
6627
CS
MSE D
381
148.937
−13.253
30.850
1.00
42.82
D

ATOM
6628
CG
MSE D
381
149.177
−13.111
29.372
1.00
45.44
D

ATOM
6629
SE
MSE D
381
150.909
−12.445
28.929
1.00
55.08
D

ATOM
6630
CE
MSE D
381
150.582
−10.533
29.001
1.00
48.67
D

ATOM
6631
C
MSE D
381
147.306
−13.812
32.645
1.00
41.59
D

ATOM
6632
O
MSE D
381
147.979
−14.701
33.169
1.00
40.94
D

ATOM
6633
N
THR D
382
146.392
−13.103
33.296
1.00
42.55
D

ATOM
6634
CA
THR D
382
146.091
−13.286
34.704
1.00
42.91
D

ATOM
6635
CB
THR D
382
146.571
−12.035
35.487
1.00
42.87
D

ATOM
6636
OG1
THR D
382
146.096
−12.083
36.838
1.00
47.41
D

ATOM
6637
CG2
THR D
382
146.091
−10.770
34.806
1.00
42.47
D

ATOM
6638
C
THR D
382
144.566
−13.490
34.809
1.00
42.80
D

ATOM
6639
O
THR D
382
143.799
−12.695
34.280
1.00
45.02
D

ATOM
6640
N
SER D
383
144.129
−14.559
35.466
1.00
41.05
D

ATOM
6641
CA
SER D
383
142.708
−14.855
35.590
1.00
40.03
D

ATOM
6642
CB
SER D
383
142.527
−16.201
36.285
1.00
41.63
D

ATOM
6643
OG
SER D
383
143.273
−16.252
37.491
1.00
42.67
D

ATOM
6644
C
SER D
383
141.888
−13.806
36.323
1.00
38.85
D

ATOM
6645
O
SER D
383
140.701
−14.007
36.569
1.00
39.35
D

ATOM
6646
N
VAL D
384
142.514
−12.689
36.665
1.00
37.95
D

ATOM
6647
CA
VAL D
384
141.829
−11.620
37.382
1.00
37.40
D

ATOM
6648
CB
VAL D
384
142.471
−11.414
38.777
1.00
39.34
D

ATOM
6649
CG1
VAL D
384
141.606
−10.515
39.638
1.00
39.21
D

ATOM
6650
CG2
VAL D
384
142.672
−12.756
39.451
1.00
41.87
D

ATOM
6651
C
VAL D
384
141.899
−10.302
36.615
1.00
35.77
D

ATOM
6652
O
VAL D
384
142.987
−9.824
36.282
1.00
35.80
D

ATOM
6653
N
ILE D
385
140.741
−9.719
36.330
1.00
33.56
D

ATOM
6654
CA
ILE D
385
140.697
−8.445
35.627
1.00
31.75
D

ATOM
6655
CB
ILE D
385
139.503
−8.347
34.670
1.00
32.21
D

ATOM
6656
CG2
ILE D
385
139.566
−7.028
33.924
1.00
31.42
D

ATOM
6657
CG1
ILE D
385
139.528
−9.506
33.673
1.00
34.12
D

ATOM
6658
CD1
ILE D
385
140.728
−9.519
32.787
1.00
31.79
D

ATOM
6659
C
ILE D
385
140.524
−7.369
36.681
1.00
29.87
D

ATOM
6660
O
ILE D
385
139.636
−7.468
37.523
1.00
29.33
D

ATOM
6661
N
THR D
386
141.364
−6.341
36.631
1.00
28.00
D

ATOM
6662
CA
THR D
386
141.284
−5.262
37.603
1.00
26.59
D

ATOM
6663
CB
THR D
386
142.665
−4.709
37.933
1.00
28.33
D

ATOM
6664
OG1
THR D
386
143.147
−3.965
36.810
1.00
33.14
D

ATOM
6665
CG2
THR D
386
143.629
−5.847
38.258
1.00
27.95
D

ATOM
6666
C
THR D
386
140.370
−4.095
37.219
1.00
23.96
D

ATOM
6667
O
THR D
386
140.049
−3.258
38.057
1.00
23.82
D

ATOM
6668
N
CYS D
387
139.969
−4.000
35.959
1.00
21.99
D

ATOM
6669
CA
CYS D
387
139.032
−2.946
35.583
1.00
21.32
D

ATOM
6670
CB
CYS D
387
139.593
−1.554
35.810
1.00
21.52
D

ATOM
6671
SG
CYS D
387
141.286
−1.370
35.494
1.00
24.48
D

ATOM
6672
C
CYS D
387
138.522
−3.058
34.185
1.00
20.32
D

ATOM
6673
O
CYS D
387
139.180
−3.609
33.309
1.00
20.62
D

ATOM
6674
N
LEU D
388
137.313
−2.554
33.993
1.00
21.13
D

ATOM
6675
CA
LEU D
388
136.666
−2.620
32.699
1.00
21.99
D

ATOM
6676
CB
LEU D
388
135.720
−3.811
32.699
1.00
19.44
D

ATOM
6677
CG
LEU D
388
134.666
−3.896
31.603
1.00
17.83
D

ATOM
6678
CD1
LEU D
388
134.369
−5.364
31.382
1.00
19.58
D

ATOM
6679
CD2
LEU D
388
133.406
−3.172
32.009
1.00
17.27
D

ATOM
6680
C
LEU D
388
135.910
−1.349
32.307
1.00
23.54
D

ATOM
6681
O
LEU D
388
135.262
−0.724
33.136
1.00
24.86
D

ATOM
6682
N
GLN D
389
136.011
−0.965
31.038
1.00
25.33
D

ATOM
6683
CA
GLN D
389
135.302
0.203
30.521
1.00
25.28
D

ATOM
6684
CB
GLN D
389
136.275
1.296
30.073
1.00
25.97
D

ATOM
6685
CG
GLN D
389
137.029
2.071
31.150
1.00
25.10
D

ATOM
6686
CD
GLN D
389
136.179
3.114
31.877
1.00
26.41
D

ATOM
6687
OE1
GLN D
389
135.673
2.850
32.949
1.00
26.25
D

ATOM
6688
NE2
GLN D
389
136.031
4.304
31.293
1.00
27.94
D

ATOM
6689
C
GLN D
389
134.477
−0.233
29.303
1.00
26.25
D

ATOM
6690
O
GLN D
389
134.917
−1.076
28.515
1.00
26.39
D

ATOM
6691
N
PHE D
390
133.284
0.340
29.153
1.00
27.94
D

ATOM
6692
CA
PHE D
390
132.415
0.045
28.015
1.00
28.91
D

ATOM
6693
CB
PHE D
390
131.364
−0.995
28.424
1.00
26.05
D

ATOM
6694
CG
PHE D
390
130.416
−1.381
27.322
1.00
26.58
D

ATOM
6695
CD1
PHE D
390
130.826
−1.411
25.998
1.00
27.31
D

ATOM
6696
CD2
PHE D
390
129.087
−1.675
27.609
1.00
27.25
D

ATOM
6697
CE1
PHE D
390
129.921
−1.716
24.978
1.00
26.45
D

ATOM
6698
CE2
PHE D
390
128.179
−1.982
26.595
1.00
26.66
D

ATOM
6699
CZ
PHE D
390
128.597
−1.999
25.284
1.00
25.88
D

ATOM
6700
C
PHE D
390
131.800
1.375
27.521
1.00
31.17
D

ATOM
6701
O
PHE D
390
130.844
1.911
28.095
1.00
31.73
D

ATOM
6702
N
GLU D
391
132.404
1.908
26.460
1.00
33.23
D

ATOM
6703
CA
GLU D
391
132.004
3.172
25.842
1.00
36.52
D

ATOM
6704
CB
GLU D
391
132.752
4.335
26.494
1.00
37.25
D

ATOM
6705
CG
GLU D
391
131.870
5.425
27.041
1.00
38.77
D

ATOM
6706
CD
GLU D
391
131.258
5.032
28.354
1.00
39.09
D

ATOM
6707
OE1
GLU D
391
132.023
4.888
29.322
1.00
40.49
D

ATOM
6708
OE2
GLU D
391
130.024
4.859
28.417
1.00
39.48
D

ATOM
6709
C
GLU D
391
132.377
3.150
24.360
1.00
37.92
D

ATOM
6710
O
GLU D
391
133.293
2.426
23.956
1.00
39.21
D

ATOM
6711
N
ASP D
392
131.704
3.971
23.557
1.00
38.58
D

ATOM
6712
CA
ASP D
392
131.986
4.053
22.112
1.00
38.07
D

ATOM
6713
CB
ASP D
392
133.157
5.009
21.858
1.00
37.43
D

ATOM
6714
CG
ASP D
392
132.716
6.428
21.778
1.00
39.32
D

ATOM
6715
OD1
ASP D
392
131.501
6.650
21.954
1.00
40.76
D

ATOM
6716
OD2
ASP D
392
133.557
7.317
21.530
1.00
40.53
D

ATOM
6717
C
ASP D
392
132.253
2.725
21.400
1.00
36.82
D

ATOM
6718
O
ASP D
392
133.221
2.589
20.647
1.00
36.96
D

ATOM
6719
N
ASN D
393
131.381
1.753
21.631
1.00
35.81
D

ATOM
6720
CA
ASN D
393
131.513
0.448
21.000
1.00
36.51
D

ATOM
6721
CB
ASN D
393
131.410
0.572
19.471
1.00
37.62
D

ATOM
6722
CG
ASN D
393
130.111
1.264
19.001
1.00
39.78
D

ATOM
6723
OD1
ASN D
393
130.023
1.696
17.846
1.00
41.53
D

ATOM
6724
ND2
ASN D
393
129.111
1.362
19.881
1.00
38.28
D

ATOM
6725
C
ASN D
393
132.829
−0.215
21.366
1.00
34.65
D

ATOM
6726
O
ASN D
393
133.249
−1.163
20.710
1.00
34.87
D

ATOM
6727
N
TYR D
394
133.477
0.292
22.409
1.00
33.42
D

ATOM
6728
CA
TYR D
394
134.742
−0.264
22.884
1.00
32.37
D

ATOM
6729
CB
TYR D
394
135.783
0.838
23.102
1.00
32.07
D

ATOM
6730
CG
TYR D
394
136.458
1.349
21.860
1.00
32.95
D

ATOM
6731
CD1
TYR D
394
137.124
0.479
20.992
1.00
32.58
D

ATOM
6732
CE1
TYR D
394
137.777
0.953
19.858
1.00
31.50
D

ATOM
6733
CD2
TYR D
394
136.459
2.704
21.565
1.00
31.89
D

ATOM
6734
CE2
TYR D
394
137.104
3.189
20.445
1.00
33.06
D

ATOM
6735
CZ
TYR D
394
137.762
2.316
19.594
1.00
33.32
D

ATOM
6736
OH
TYR D
394
138.406
2.827
18.492
1.00
33.69
D

ATOM
6737
C
TYR D
394
134.554
−0.956
24.224
1.00
32.16
D

ATOM
6738
O
TYR D
394
133.692
−0.582
25.016
1.00
33.01
D

ATOM
6739
N
VAL D
395
135.359
−1.970
24.481
1.00
31.18
D

ATOM
6740
CA
VAL D
395
135.307
−2.636
25.767
1.00
30.34
D

ATOM
6741
CB
VAL D
395
134.724
−4.036
25.689
1.00
32.30
D

ATOM
6742
CG1
VAL D
395
134.537
−4.571
27.092
1.00
30.09
D

ATOM
6743
CG2
VAL D
395
133.388
−4.017
24.945
1.00
32.97
D

ATOM
6744
C
VAL D
395
136.751
−2.752
26.150
1.00
29.50
D

ATOM
6745
O
VAL D
395
137.469
−3.592
25.608
1.00
30.47
D

ATOM
6746
N
ILE D
396
137.190
−1.895
27.061
1.00
27.33
D

ATOM
6747
CA
ILE D
396
138.579
−1.929
27.471
1.00
24.79
D

ATOM
6748
CB
ILE D
396
139.202
−0.529
27.477
1.00
20.54
D

ATOM
6749
CG2
ILE D
396
140.724
−0.654
27.607
1.00
18.18
D

ATOM
6750
CG1
ILE D
396
138.779
0.231
26.222
1.00
19.10
D

ATOM
6751
CD1
ILE D
396
137.698
1.261
26.480
1.00
15.50
D

ATOM
6752
C
ILE D
396
138.721
−2.532
28.860
1.00
25.91
D

ATOM
6753
O
ILE D
396
137.839
−2.371
29.709
1.00
25.28
D

ATOM
6754
N
THR D
397
139.839
−3.228
29.075
1.00
25.38
D

ATOM
6755
CA
THR D
397
140.133
−3.867
30.352
1.00
24.35
D

ATOM
6756
CB
THR D
397
139.734
−5.353
30.367
1.00
23.41
D

ATOM
6757
OG1
THR D
397
140.542
−6.067
29.425
1.00
22.79
D

ATOM
6758
CG2
THR D
397
138.280
−5.530
30.010
1.00
22.25
D

ATOM
6759
C
THR D
397
141.610
−3.834
30.732
1.00
25.66
D

ATOM
6760
O
THR D
397
142.492
−3.945
29.876
1.00
25.23
D

ATOM
6761
N
GLY D
398
141.871
−3.715
32.032
1.00
26.89
D

ATOM
6762
CA
GLY D
398
143.239
−3.717
32.535
1.00
27.00
D

ATOM
6763
C
GLY D
398
143.440
−4.892
33.487
1.00
26.90
D

ATOM
6764
O
GLY D
398
142.464
−5.481
33.951
1.00
26.42
D

ATOM
6765
N
ALA D
399
144.692
−5.250
33.776
1.00
28.42
D

ATOM
6766
CA
ALA D
399
144.977
−6.367
34.694
1.00
29.91
D

ATOM
6767
CB
ALA D
399
144.889
−7.701
33.945
1.00
28.40
D

ATOM
6768
C
ALA D
399
146.335
−6.265
35.410
1.00
31.06
D

ATOM
6769
O
ALA D
399
147.208
−5.469
35.041
1.00
29.92
D

ATOM
6770
N
ASP D
400
146.511
−7.083
36.444
1.00
33.65
D

ATOM
6771
CA
ASP D
400
147.767
−7.066
37.178
1.00
35.36
D

ATOM
6772
CB
ASP D
400
147.670
−7.891
38.473
1.00
37.51
D

ATOM
6773
CG
ASP D
400
148.845
−7.626
39.429
1.00
42.78
D

ATOM
6774
OD1
ASP D
400
149.073
−6.446
39.813
1.00
42.00
D

ATOM
6775
OD2
ASP D
400
149.544
−8.603
39.802
1.00
45.77
D

ATOM
6776
C
ASP D
400
148.818
−7.639
36.237
1.00
34.42
D

ATOM
6777
O
ASP D
400
149.996
−7.735
36.579
1.00
34.18
D

ATOM
6778
N
ASP D
401
148.379
−8.014
35.037
1.00
33.68
D

ATOM
6779
CA
ASP D
401
149.293
−8.550
34.047
1.00
32.54
D

ATOM
6780
CB
ASP D
401
148.571
−9.554
33.118
1.00
31.92
D

ATOM
6781
CG
ASP D
401
147.897
−8.910
31.909
1.00
31.59
D

ATOM
6782
OD1
ASP D
401
147.579
−7.704
31.945
1.00
30.42
D

ATOM
6783
OD2
ASP D
401
147.671
−9.645
30.916
1.00
31.10
D

ATOM
6784
C
ASP D
401
149.901
−7.372
33.293
1.00
32.98
D

ATOM
6785
O
ASP D
401
150.551
−7.539
32.266
1.00
33.47
D

ATOM
6786
N
LYS D
402
149.699
−6.180
33.854
1.00
33.97
D

ATOM
6787
CA
LYS D
402
150.215
−4.921
33.319
1.00
34.64
D

ATOM
6788
CB
LYS D
402
151.735
−4.825
33.568
1.00
33.75
D

ATOM
6789
CG
LYS D
402
152.545
−5.988
33.073
1.00
33.34
D

ATOM
6790
CD
LYS D
402
153.625
−6.377
34.058
1.00
34.65
D

ATOM
6791
CE
LYS D
402
154.661
−5.300
34.221
1.00
35.08
D

ATOM
6792
NZ
LYS D
402
155.714
−5.811
35.142
1.00
34.72
D

ATOM
6793
C
LYS D
402
149.895
−4.650
31.846
1.00
35.07
D

ATOM
6794
O
LYS D
402
150.606
−3.907
31.167
1.00
35.57
D

ATOM
6795
N
MSE D
403
148.809
−5.238
31.360
1.00
37.46
D

ATOM
6796
CA
MSE D
403
148.389
−5.066
29.966
1.00
39.42
D

ATOM
6797
CB
MSE D
403
148.429
−6.405
29.210
1.00
40.61
D

ATOM
6798
CG
MSE D
403
149.792
−7.054
29.119
1.00
42.82
D

ATOM
6799
SE
MSE D
403
150.956
−5.997
28.018
1.00
47.96
D

ATOM
6800
CE
MSE D
403
152.415
−5.649
29.261
1.00
46.83
D

ATOM
6801
C
MSE D
403
146.970
−4.518
29.882
1.00
39.22
D

ATOM
6802
O
MSE D
403
146.140
−4.767
30.761
1.00
41.64
D

ATOM
6803
N
ILE D
404
146.691
−3.797
28.802
1.00
37.92
D

ATOM
6804
CA
ILE D
404
145.372
−3.216
28.582
1.00
35.96
O

ATOM
6805
CB
ILE D
404
145.455
−1.675
28.574
1.00
34.69
O

ATOM
6806
CG2
ILE D
404
144.114
−1.082
28.156
1.00
33.19
D

ATOM
6807
CG1
ILE D
404
145.880
−1.186
29.962
1.00
33.10
D

ATOM
6808
CO1
ILE D
404
146.272
0.266
29.999
1.00
31.33
O

ATOM
6809
C
ILE D
404
144.788
−3.709
27.251
1.00
35.14
D

ATOM
6810
O
ILE D
404
145.304
−3.392
26.193
1.00
34.48
O

ATOM
6811
N
ARG D
405
143.709
−4.482
27.325
1.00
34.81
D

ATOM
6812
CA
ARG D
405
143.046
−5.027
26.151
1.00
34.51
O

ATOM
6813
CB
ARG D
405
142.428
−6.373
26.494
1.00
34.25
O

ATOM
6814
CG
ARG D
405
143.353
−7.285
27.227
1.00
34.29
O

ATOM
6815
CD
ARG D
405
144.147
−8.101
26.302
1.00
33.92
O

ATOM
6816
NE
ARG D
405
143.362
−9.187
25.745
1.00
34.85
O

ATOM
6817
CZ
ARG D
405
143.844
−10.076
24.882
1.00
37.01
D

ATOM
6818
NH1
ARG D
405
145.110
−9.992
24.481
1.00
32.55
D

ATOM
6819
NH2
ARG D
405
143.069
−11.063
24.436
1.00
38.58
D

ATOM
6820
C
ARG D
405
141.931
−4.099
25.668
1.00
35.40
O

ATOM
6821
O
ARG D
405
141.238
−3.474
26.479
1.00
36.54
D

ATOM
6822
N
VAL D
406
141.749
−4.041
24.349
1.00
35.29
D

ATOM
6823
CA
VAL D
406
140.719
−3.214
23.719
1.00
34.73
D

ATOM
6824
CB
VAL D
406
141.332
−2.093
22.879
1.00
35.48
D

ATOM
6825
CG1
VAL D
406
140.229
−1.244
22.275
1.00
35.19
D

ATOM
6826
CG2
VAL D
406
142.275
−1.253
23.737
1.00
35.51
O

ATOM
6827
C
VAL D
406
139.921
−4.085
22.780
1.00
34.43
O

ATOM
6828
O
VAL D
406
140.500
−4.664
21.874
1.00
34.33
D

ATOM
6829
N
TYR D
407
138.603
−4.160
22.977
1.00
34.53
D

ATOM
6830
CA
TYR D
407
137.739
−4.985
22.124
1.00
34.18
D

ATOM
6831
CB
TYR D
407
137.059
−6.091
22.937
1.00
33.29
D

ATOM
6832
CG
TYR D
407
137.966
−6.948
23.781
1.00
33.16
D

ATOM
6833
CD1
TYR D
407
138.423
−6.509
25.026
1.00
32.93
D

ATOM
6834
CE1
TYR D
407
139.255
−7.313
25.802
1.00
33.43
D

ATOM
6835
CD2
TYR D
407
138.362
−8.206
23.335
1.00
31.85
D

ATOM
6836
CE2
TYR D
407
139.189
−9.013
24.091
1.00
31.74
D

ATOM
6837
CZ
TYR D
407
139.637
−8.572
25.320
1.00
33.54
O

ATOM
6838
OH
TYR D
407
140.485
−9.378
26.052
1.00
34.77
D

ATOM
6839
C
TYR D
407
136.635
−4.194
21.417
1.00
34.58
D

ATOM
6840
O
TYR D
407
136.246
−3.117
21.864
1.00
35.32
D

ATOM
6841
N
ASP D
408
136.122
−4.775
20.332
1.00
35.38
D

ATOM
6842
CA
ASP D
408
135.043
−4.221
19.501
1.00
35.74
D

ATOM
6843
CB
ASP D
408
135.302
−4.625
18.038
1.00
38.38
D

ATOM
6844
CG
ASP D
408
134.214
−4.143
17.066
1.00
40.45
D

ATOM
6845
OD1
ASP D
408
133.015
−4.143
17.433
1.00
41.61
D

ATOM
6846
OD2
ASP D
408
134.563
−3.781
15.917
1.00
39.05
D

ATOM
6847
C
ASP D
408
133.685
−4.788
19.965
1.00
35.67
D

ATOM
6848
O
ASP D
408
133.413
−5.980
19.799
1.00
35.45
D

ATOM
6849
N
SER D
409
132.829
−3.934
20.519
1.00
36.24
D

ATOM
6850
CA
SER D
409
131.510
−4.351
21.021
1.00
37.97
D

ATOM
6851
CB
SER D
409
130.779
−3.160
21.623
1.00
39.00
D

ATOM
6852
OG
SER D
409
131.590
−2.452
22.533
1.00
42.40
D

ATOM
6853
C
SER D
409
130.594
−4.953
19.968
1.00
39.04
D

ATOM
6854
O
SER D
409
129.915
−5.958
20.216
1.00
38.64
D

ATOM
6855
N
ILE D
410
130.565
−4.295
18.807
1.00
40.27
D

ATOM
6856
CA
ILE D
410
129.740
−4.695
17.658
1.00
41.19
D

ATOM
6857
CB
ILE D
410
129.743
−3.613
16.553
1.00
42.29
D

ATOM
6858
CG2
ILE D
410
128.654
−3.904
15.539
1.00
41.48
D

ATOM
6859
CG1
ILE D
410
129.507
−2.227
17.162
1.00
43.94
D

ATOM
6860
CD1
ILE D
410
129.838
−1.089
16.202
1.00
43.04
D

ATOM
6861
C
ILE D
410
130.244
−5.996
17.038
1.00
40.21
D

ATOM
6862
O
ILE D
410
129.616
−7.041
17.170
1.00
40.47
D

ATOM
6863
N
ASN D
411
131.385
−5.945
16.370
1.00
38.97
D

ATOM
6864
CA
ASN D
411
131.900
−7.153
15.769
1.00
39.16
D

ATOM
6865
CB
ASN D
411
133.158
−6.848
14.985
1.00
41.69
D

ATOM
6866
CG
ASN D
411
132.943
−5.731
13.995
1.00
43.77
D

ATOM
6867
OD1
ASN D
411
131.889
−5.649
13.355
1.00
43.07
D

ATOM
6868
ND2
ASN D
411
133.938
−4.866
13.855
1.00
45.58
D

ATOM
6869
C
ASN D
411
132.178
−8.213
16.805
1.00
38.20
D

ATOM
6870
O
ASN D
411
132.364
−9.377
16.458
1.00
36.34
D

ATOM
6871
N
LYS D
412
132.197
−7.800
18.074
1.00
37.74
D

ATOM
6872
CA
LYS D
412
132.451
−8.693
19.211
1.00
36.63
D

ATOM
6873
CB
LYS D
412
131.300
−9.690
19.338
1.00
35.83
D

ATOM
6874
CG
LYS D
412
129.936
−9.018
19.314
1.00
35.16
D

ATOM
6875
CD
LYS D
412
128.805
−10.011
19.175
1.00
34.88
D

ATOM
6876
CE
LYS D
412
127.483
−9.278
19.119
1.00
36.26
D

ATOM
6877
NZ
LYS D
412
126.321
−10.211
19.101
1.00
37.05
D

ATOM
6878
C
LYS D
412
133.776
−9.442
19.066
1.00
36.14
D

ATOM
6879
O
LYS D
412
133.828
−10.659
19.227
1.00
35.34
D

ATOM
6880
N
LYS D
413
134.845
−8.707
18.772
1.00
36.48
D

ATOM
6881
CA
LYS D
413
136.161
−9.314
18.597
1.00
38.12
D

ATOM
6882
CB
LYS D
413
136.440
−9.573
17.118
1.00
37.83
D

ATOM
6883
CG
LYS D
413
136.378
−8.322
16.257
1.00
41.43
D

ATOM
6884
CD
LYS D
413
136.964
−8.566
14.853
1.00
44.72
D

ATOM
6885
CE
LYS D
413
136.674
−7.400
13.885
1.00
46.65
D

ATOM
6886
NZ
LYS D
413
137.132
−6.056
14.371
1.00
47.55
D

ATOM
6887
C
LYS D
413
137.303
−8.471
19.159
1.00
38.78
D

ATOM
6888
O
LYS D
413
137.244
−7.242
19.151
1.00
38.60
D

ATOM
6889
N
PHE D
414
138.348
−9.149
19.630
1.00
38.98
D

ATOM
6890
CA
PHE D
414
139.520
−8.489
20.191
1.00
38.98
D

ATOM
6891
CB
PHE D
414
140.513
−9.528
20.715
1.00
39.56
D

ATOM
6892
CG
PHE D
414
141.908
−8.997
20.902
1.00
41.07
D

ATOM
6893
CD1
PHE D
414
142.184
−8.046
21.874
1.00
43.51
D

ATOM
6894
CD2
PHE D
414
142.949
−9.454
20.110
1.00
41.71
D

ATOM
6895
CE1
PHE D
414
143.488
−7.557
22.058
1.00
44.32
D

ATOM
6896
CE2
PHE D
414
144.251
−8.973
20.287
1.00
43.60
D

ATOM
6897
CZ
PHE D
414
144.519
−8.022
21.264
1.00
42.78
D

ATOM
6898
C
PHE D
414
140.208
−7.620
19.157
1.00
39.17
D

ATOM
6899
O
PHE D
414
140.529
−8.083
18.068
1.00
40.84
D

ATOM
6900
N
LEU D
415
140.430
−6.359
19.506
1.00
38.34
D

ATOM
6901
CA
LEU D
415
141.099
−5.434
18.617
1.00
37.48
D

ATOM
6902
CB
LEU D
415
140.555
−4.026
18.815
1.00
37.15
D

ATOM
6903
CG
LEU D
415
139.163
−3.792
18.224
1.00
38.52
D

ATOM
6904
CD1
LEU D
415
138.737
−2.351
18.453
1.00
39.38
D

ATOM
6905
CD2
LEU D
415
139.191
−4.091
16.736
1.00
39.17
D

ATOM
6906
C
LEU D
415
142.611
−5.451
18.832
1.00
37.67
D

ATOM
6907
O
LEU D
415
143.328
−6.171
18.138
1.00
38.98
D

ATOM
6908
N
LEU D
416
143.097
−4.681
19.799
1.00
35.95
D

ATOM
6909
CA
LEU D
416
144.528
−4.611
20.052
1.00
34.61
D

ATOM
6910
CB
LEU D
416
145.102
−3.394
19.317
1.00
32.51
D

ATOM
6911
CG
LEU D
416
144.656
−2.045
19.880
1.00
30.50
D

ATOM
6912
CD1
LEU D
416
145.700
−1.579
20.853
1.00
31.53
D

ATOM
6913
CD2
LEU D
416
144.470
−1.017
18.789
1.00
30.55
D

ATOM
6914
C
LEU D
416
144.865
−4.519
21.545
1.00
35.53
D

ATOM
6915
O
LEU D
416
144.013
−4.200
22.364
1.00
36.55
D

ATOM
6916
N
GLN D
417
146.116
−4.791
21.891
1.00
35.81
D

ATOM
6917
CA
GLN D
417
146.547
−4.716
23.271
1.00
35.57
D

ATOM
6918
CB
GLN D
417
147.254
−6.007
23.671
1.00
37.43
D

ATOM
6919
CG
GLN D
417
147.625
−6.074
25.145
1.00
39.62
D

ATOM
6920
CD
GLN D
417
148.512
−7.253
25.464
1.00
41.04
D

ATOM
6921
OE1
CLN D
417
149.615
−7.378
24.914
1.00
43.24
D

ATOM
6922
NE2
GLN D
417
148.046
−8.128
26.358
1.00
40.41
D

ATOM
6923
C
GLN D
417
147.506
−3.532
23.450
1.00
35.61
D

ATOM
6924
O
GLN D
417
148.374
−3.297
22.605
1.00
35.43
D

ATOM
6925
N
LEU D
418
147.337
−2.798
24.551
1.00
35.15
D

ATOM
6926
CA
LEU D
418
148.166
−1.644
24.885
1.00
33.41
D

ATOM
6927
CB
LEU D
418
147.315
−0.523
25.429
1.00
31.33
D

ATOM
6928
CG
LEU D
418
146.413
0.034
24.359
1.00
31.84
D

ATOM
6929
CD1
LEU D
418
145.508
1.119
24.943
1.00
33.02
D

ATOM
6930
CD2
LEU D
418
147.293
0.595
23.253
1.00
33.13
D

ATOM
6931
C
LEU D
418
149.180
−2.006
25.939
1.00
33.92
D

ATOM
6932
O
LEU D
418
148.811
−2.281
27.076
1.00
33.63
D

ATOM
6933
N
SER D
419
150.458
−1.991
25.572
1.00
35.50
D

ATOM
6934
CA
SER D
419
151.529
−2.323
26.518
1.00
35.75
D

ATOM
6935
CB
SER D
419
152.504
−3.304
25.889
1.00
36.24
D

ATOM
6936
OG
SER D
419
153.366
−2.611
25.006
1.00
39.10
D

ATOM
6937
C
SER D
419
152.286
−1.060
26.903
1.00
34.65
D

ATOM
6938
O
SER D
419
152.148
−0.036
26.243
1.00
35.71
D

ATOM
6939
N
GLY D
420
153.082
−1.132
27.969
1.00
34.21
D

ATOM
6940
CA
GLY D
420
153.845
0.030
28.407
1.00
32.81
D

ATOM
6941
C
GLY D
420
154.127
0.063
29.904
1.00
32.19
D

ATOM
6942
O
GLY D
420
155.277
0.111
30.334
1.00
32.95
D

ATOM
6943
N
HIS D
421
153.057
0.038
30.690
1.00
32.53
D

ATOM
6944
CA
HIS D
421
153.116
0.056
32.142
1.00
31.89
D

ATOM
6945
CB
HIS D
421
151.744
−0.233
32.728
1.00
28.17
D

ATOM
6946
CG
HIS D
421
150.862
0.972
32.856
1.00
26.59
D

ATOM
6947
CD2
HIS D
421
149.677
1.270
32.274
1.00
23.86
D

ATOM
6948
ND1
HIS D
421
151.123
1.998
33.738
1.00
24.07
D

ATOM
6949
CE1
HIS D
421
150.133
2.872
33.699
1.00
24.39
D

ATOM
6950
NE2
HIS D
421
149.243
2.454
32.818
1.00
22.81
D

ATOM
6951
C
HIS D
421
154.082
−0.966
32.714
1.00
34.84
D

ATOM
6952
O
HIS D
421
154.005
−2.162
32.399
1.00
35.95
D

ATOM
6953
N
ASP D
422
154.973
−0.487
33.580
1.00
37.06
D

ATOM
6954
CA
ASP D
422
155.969
−1.328
34.241
1.00
37.22
D

ATOM
6955
CB
ASP D
422
157.181
−0.481
34.655
1.00
37.19
D

ATOM
6956
CG
ASP D
422
157.811
0.261
33.479
1.00
38.07
D

ATOM
6957
OD1
ASP D
422
158.398
−0.414
32.605
1.00
36.97
D

ATOM
6958
OD2
ASP D
422
157.716
1.519
33.426
1.00
39.00
D

ATOM
6959
C
ASP D
422
155.331
−1.974
35.468
1.00
37.57
D

ATOM
6960
O
ASP D
422
155.947
−2.791
36.155
1.00
38.18
D

ATOM
6961
N
GLY D
423
154.089
−1.584
35.735
1.00
38.03
D

ATOM
6962
CA
GLY D
423
153.357
−2.135
36.862
1.00
37.36
D

ATOM
6963
C
GLY D
423
151.963
−2.599
36.451
1.00
36.40
D

ATOM
6964
O
GLY D
423
151.496
−2.282
35.358
1.00
37.00
D

ATOM
6965
N
GLY D
424
151.297
−3.361
37.311
1.00
35.05
D

ATOM
6966
CA
GLY D
424
149.965
−3.823
36.984
1.00
33.45
D

ATOM
6967
C
GLY D
424
149.032
−2.637
36.920
1.00
33.03
D

ATOM
6968
O
GLY D
424
149.183
−1.692
37.687
1.00
32.43
D

ATOM
6969
N
VAL D
425
148.074
−2.685
36.004
1.00
33.29
D

ATOM
6970
CA
VAL D
425
147.112
−1.602
35.826
1.00
34.26
D

ATOM
6971
CB
VAL D
425
146.545
−1.623
34.420
1.00
34.93
D

ATOM
6972
CG1
VAL D
425
145.785
−0.328
34.150
1.00
37.13
D

ATOM
6973
CG2
VAL D
425
147.661
−1.843
33.433
1.00
34.83
D

ATOM
6974
C
VAL D
425
145.955
−1.776
36.795
1.00
33.41
D

ATOM
6975
O
VAL D
425
145.473
−2.880
36.975
1.00
33.61
D

ATOM
6976
N
TRP D
426
145.493
−0.700
37.410
1.00
32.49
D

ATOM
6977
CA
TRP D
426
144.395
−0.837
38.343
1.00
32.03
D

ATOM
6978
CB
TRP D
426
144.952
−0.866
39.774
1.00
30.72
D

ATOM
6979
CG
TRP D
426
145.618
−2.192
40.132
1.00
29.46
D

ATOM
6980
CD2
TRP D
426
145.011
−3.288
40.834
1.00
27.59
D

ATOM
6981
CE2
TRP D
426
145.982
−4.311
40.937
1.00
25.67
D

ATOM
6982
CE3
TRP D
426
143.738
−3.502
41.390
1.00
27.62
D

ATOM
6983
CD1
TRP D
426
146.903
−2.592
39.838
1.00
28.36
D

ATOM
6984
NE1
TRP D
426
147.122
−3.863
40.321
1.00
26.42
D

ATOM
6985
CZ2
TRP D
426
145.720
−5.527
41.572
1.00
23.76
D

ATOM
6986
CZ3
TRP D
426
143.477
−4.712
42.021
1.00
25.66
D

ATOM
6987
CH2
TRP D
426
144.467
−5.711
42.108
1.00
24.10
D

ATOM
6988
C
TRP D
426
143.291
0.224
38.190
1.00
32.39
D

ATOM
6989
O
TRP D
426
142.270
0.182
38.876
1.00
32.60
D

ATOM
6990
N
ALA D
427
143.483
1.164
37.275
1.00
31.70
D

ATOM
6991
CA
ALA D
427
142.489
2.201
37.060
1.00
32.14
D

ATOM
6992
CB
ALA D
427
142.699
3.330
38.059
1.00
30.77
D

ATOM
6993
C
ALA D
427
142.544
2.749
35.631
1.00
32.54
D

ATOM
6994
O
ALA D
427
143.610
3.128
35.148
1.00
33.11
D

ATOM
6995
N
LEU D
428
141.403
2.763
34.949
1.00
31.96
D

ATOM
6996
CA
LEU D
428
141.362
3.298
33.605
1.00
31.52
D

ATOM
6997
CB
LEU D
428
141.879
2.273
32.591
1.00
30.47
D

ATOM
6998
CG
LEU D
428
141.523
0.793
32.619
1.00
25.70
D

ATOM
6999
CD1
LEU D
428
140.061
0.566
32.426
1.00
26.95
D

ATOM
7000
CD2
LEU D
428
142.302
0.127
31.520
1.00
26.15
D

ATOM
7001
C
LEU D
428
139.998
3.823
33.185
1.00
32.41
D

ATOM
7002
O
LEU D
428
139.015
3.092
33.159
1.00
31.99
D

ATOM
7003
N
LYS D
429
139.970
5.117
32.874
1.00
34.44
D

ATOM
7004
CA
LYS D
429
138.779
5.846
32.441
1.00
36.04
D

ATOM
7005
CE
LYS D
429
138.655
7.149
33.247
1.00
36.79
D

ATOM
7006
CG
LYS D
429
137.379
7.954
33.000
1.00
41.16
D

ATOM
7007
CD
LYS D
429
136.228
7.499
33.914
1.00
44.67
D

ATOM
7008
CE
LYS D
429
134.828
7.936
33.399
1.00
47.43
D

ATOM
7009
NZ
LYS D
429
134.385
7.223
32.133
1.00
49.62
D

ATOM
7010
C
LYS D
429
138.944
6.184
30.951
1.00
35.80
D

ATOM
7011
O
LYS D
429
139.982
6.698
30.531
1.00
35.22
D

ATOM
7012
N
TYR D
430
137.926
5.888
30.152
1.00
36.71
D

ATOM
7013
CA
TYR D
430
137.962
6.183
28.719
1.00
38.50
D

ATOM
7014
CE
TYR D
430
137.142
5.152
27.936
1.00
38.31
D

ATOM
7015
CG
TYR D
430
136.840
5.560
26.501
1.00
38.68
D

ATOM
7016
CD1
TYR D
430
135.713
6.331
26.192
1.00
38.18
D

ATOM
7017
CE1
TYR D
430
135.427
6.702
24.875
1.00
37.22
D

ATOM
7018
CD2
TYR D
430
137.680
5.173
25.449
1.00
39.59
D

ATOM
7019
CE2
TYR D
430
137.403
5.542
24.126
1.00
38.38
D

ATOM
7020
CZ
TYR D
430
136.275
6.303
23.853
1.00
38.21
D

ATOM
7021
OH
TYR D
430
135.983
6.646
22.557
1.00
37.82
D

ATOM
7022
C
TYR D
430
137.401
7.574
28.427
1.00
39.86
D

ATOM
7023
O
TYR D
430
136.344
7.931
28.934
1.00
39.99
D

ATOM
7024
N
ALA D
431
138.109
8.349
27.607
1.00
40.69
D

ATOM
7025
CA
ALA D
431
137.660
9.688
27.227
1.00
41.42
D

ATOM
7026
CB
ALA D
431
138.790
10.695
27.407
1.00
40.10
D

ATOM
7027
C
ALA D
431
137.208
9.641
25.763
1.00
43.09
D

ATOM
7028
O
ALA D
431
137.842
8.998
24.916
1.00
43.69
D

ATOM
7029
N
HIS D
432
136.108
10.321
25.465
1.00
42.71
D

ATOM
7030
CA
HIS D
432
135.584
10.340
24.102
1.00
43.16
D

ATOM
7031
CB
HIS D
432
134.468
11.383
23.966
1.00
47.95
D

ATOM
7032
CG
HIS D
432
133.942
11.523
22.566
1.00
53.08
D

ATOM
7033
CD2
HIS D
432
133.728
12.622
21.801
1.00
53.58
D

ATOM
7034
ND1
HIS D
432
133.594
10.439
21.787
1.00
53.70
D

ATOM
7035
CE1
HIS D
432
133.192
10.865
20.601
1.00
54.74
D

ATOM
7036
NE2
HIS D
432
133.265
12.184
20.584
1.00
54.71
D

ATOM
7037
C
HIS D
432
136.646
10.636
23.052
1.00
40.32
D

ATOM
7038
O
HIS D
432
137.420
11.573
23.201
1.00
40.89
D

ATOM
7039
N
GLY D
433
136.669
9.852
21.980
1.00
37.59
D

ATOM
7040
CA
GLY D
433
137.640
10.095
20.926
1.00
36.16
D

ATOM
7041
C
GLY D
433
138.701
9.029
20.850
1.00
34.81
D

ATOM
7042
O
GLY D
433
139.697
9.177
20.143
1.00
32.92
D

ATOM
7043
N
GLY D
434
138.474
7.948
21.588
1.00
36.25
D

ATOM
7044
CA
GLY D
434
139.412
6.841
21.617
1.00
36.22
D

ATOM
7045
C
GLY D
434
140.580
7.079
22.557
1.00
36.76
D

ATOM
7046
O
GLY D
434
141.559
6.338
22.493
1.00
37.12
D

ATOM
7047
N
ILE D
435
140.469
8.106
23.411
1.00
37.42
D

ATOM
7048
CA
ILE D
435
141.501
8.478
24.397
1.00
37.95
D

ATOM
7049
CB
ILE D
435
141.424
9.992
24.784
1.00
39.16
D

ATOM
7050
CG2
ILE D
435
142.684
10.430
25.539
1.00
37.49
D

ATOM
7051
CG1
ILE D
435
141.328
10.839
23.519
1.00
39.15
D

ATOM
7052
CD1
ILE D
435
142.476
10.580
22.572
1.00
38.06
D

ATOM
7053
C
ILE D
435
141.273
7.662
25.658
1.00
37.16
D

ATOM
7054
O
ILE D
435
140.130
7.426
26.059
1.00
36.94
D

ATOM
7055
N
LEU D
436
142.360
7.251
26.297
1.00
35.58
D

ATOM
7056
CA
LEU D
436
142.243
6.427
27.481
1.00
34.59
D

ATOM
7057
CB
LEU D
436
142.354
4.980
27.046
1.00
35.11
D

ATOM
7058
CG
LEU D
436
141.894
3.866
27.965
1.00
35.32
D

ATOM
7059
CD1
LEU D
436
142.000
2.560
27.178
1.00
34.07
D

ATOM
7060
CD2
LEU D
436
142.727
3.819
29.234
1.00
35.01
D

ATOM
7061
C
LEU D
436
143.309
6.742
28.511
1.00
34.64
D

ATOM
7062
O
LEU D
436
144.495
6.786
28.195
1.00
35.84
D

ATOM
7063
N
VAL D
437
142.891
6.960
29.750
1.00
33.63
D

ATOM
7064
CA
VAL D
437
143.854
7.244
30.801
1.00
32.09
D

ATOM
7065
CB
VAL D
437
143.484
8.519
31.575
1.00
31.66
D

ATOM
7066
CG1
VAL D
437
144.624
8.902
32.506
1.00
32.49
D

ATOM
7067
CG2
VAL D
437
143.172
9.650
30.608
1.00
31.31
D

ATOM
7068
C
VAL D
437
143.887
6.058
31.764
1.00
31.94
D

ATOM
7069
O
VAL D
437
142.845
5.454
32.047
1.00
31.55
D

ATOM
7070
N
SER D
438
145.080
5.707
32.246
1.00
29.85
D

ATOM
7071
CA
SER D
438
145.201
4.597
33.189
1.00
26.33
D

ATOM
7072
CB
SER D
438
145.601
3.302
32.480
1.00
25.65
D

ATOM
7073
OG
SER D
438
146.858
3.426
31.852
1.00
26.66
D

ATOM
7074
C
SER D
438
146.156
4.853
34.336
1.00
23.90
D

ATOM
7075
O
SER D
438
146.977
5.765
34.294
1.00
21.89
D

ATOM
7076
N
GLY D
439
146.019
4.025
35.366
1.00
23.29
D

ATOM
7077
CA
GLY D
439
146.835
4.130
36.563
1.00
23.55
D

ATOM
7078
C
GLY D
439
147.396
2.783
36.962
1.00
23.12
D

ATOM
7079
O
GLY D
439
146.725
1.748
36.883
1.00
22.22
D

ATOM
7080
N
SER D
440
148.634
2.800
37.429
1.00
23.85
D

ATOM
7081
CA
SER D
440
149.302
1.562
37.786
1.00
25.71
D

ATOM
7082
CB
SER D
440
150.244
1.169
36.630
1.00
24.70
D

ATOM
7083
OG
SER D
440
151.145
0.129
36.979
1.00
23.47
D

ATOM
7084
C
SER D
440
150.078
1.620
39.099
1.00
26.18
D

ATOM
7085
O
SER D
440
150.112
2.651
39.793
1.00
26.21
D

ATOM
7086
N
THR D
441
150.695
0.481
39.413
1.00
27.38
D

ATOM
7087
CA
THR D
441
151.521
0.308
40.593
1.00
27.39
D

ATOM
7088
CB
THR D
441
151.676
−1.165
40.968
1.00
28.12
D

ATOM
7089
OG1
THR D
441
152.519
−1.810
40.004
1.00
27.63
D

ATOM
7090
CG2
THR D
441
150.310
−1.858
41.003
1.00
28.73
D

ATOM
7091
C
THR D
441
152.903
0.847
40.237
1.00
28.31
D

ATOM
7092
O
THR D
441
153.768
0.906
41.090
1.00
29.00
D

ATOM
7093
N
ASP D
442
153.116
1.234
38.980
1.00
29.46
D

ATOM
7094
CA
ASP D
442
154.402
1.796
38.603
1.00
31.38
D

ATOM
7095
CB
ASP D
442
154.724
1.551
37.126
1.00
33.65
D

ATOM
7096
CG
ASP D
442
153.695
2.167
36.185
1.00
35.87
D

ATOM
7097
OD1
ASP D
442
152.845
2.962
36.680
1.00
35.07
D

ATOM
7098
OD2
ASP D
442
153.753
1.860
34.959
1.00
34.85
D

ATOM
7099
C
ASP D
442
154.351
3.287
38.857
1.00
31.58
D

ATOM
7100
O
ASP D
442
155.161
4.049
38.334
1.00
31.31
D

ATOM
7101
N
ARG D
443
153.360
3.700
39.635
1.00
31.79
D

ATOM
7102
CA
ARG D
443
153.191
5.100
39.983
1.00
31.82
D

ATOM
7103
CB
ARG D
443
154.413
5.569
40.760
1.00
28.96
D

ATOM
7104
CG
ARG D
443
154.805
4.604
41.846
1.00
26.68
D

ATOM
7105
CD
ARG D
443
156.056
5.065
42.541
1.00
25.25
D

ATOM
7106
NE
ARG D
443
156.496
4.111
43.541
1.00
26.33
D

ATOM
7107
CZ
ARG D
443
157.552
4.303
44.319
1.00
27.22
D

ATOM
7108
NH1
ARG D
443
158.250
5.419
44.192
1.00
28.58
D

ATOM
7109
NH2
ARG D
443
157.916
3.388
45.213
1.00
26.32
D

ATOM
7110
C
ARG D
443
152.955
6.016
38.783
1.00
32.05
D

ATOM
7111
O
ARG D
443
152.975
7.243
38.917
1.00
32.48
D

ATOM
7112
N
THR D
444
152.705
5.439
37.616
1.00
31.82
D

ATOM
7113
CA
THR D
444
152.486
6.283
36.459
1.00
32.99
D

ATOM
7114
CB
THR D
444
153.335
5.824
35.246
1.00
32.98
D

ATOM
7115
OG1
THR D
444
152.768
4.643
34.657
1.00
30.88
D

ATOM
7116
CG2
THR D
444
154.757
5.549
35.680
1.00
31.91
D

ATOM
7117
C
THR D
444
151.036
6.451
36.000
1.00
34.38
D

ATOM
7118
O
THR D
444
150.182
5.570
36.164
1.00
34.02
D

ATOM
7119
N
VAL D
445
150.784
7.623
35.432
1.00
35.02
D

ATOM
7120
CA
VAL D
445
149.492
7.992
34.888
1.00
35.88
D

ATOM
7121
CB
VAL D
445
149.049
9.384
35.406
1.00
34.38
D

ATOM
7122
CG1
VAL D
445
147.839
9.871
34.640
1.00
33.91
D

ATOM
7123
CG2
VAL D
445
148.747
9.312
36.893
1.00
33.31
D

ATOM
7124
C
VAL D
445
149.787
8.067
33.392
1.00
38.00
D

ATOM
7125
O
VAL D
445
150.648
8.841
32.969
1.00
40.09
D

ATOM
7126
N
ARG D
446
149.116
7.256
32.583
1.00
38.70
D

ATOM
7127
CA
ARG D
446
149.390
7.299
31.152
1.00
40.25
D

ATOM
7128
CB
ARG D
446
150.102
6.016
30.707
1.00
40.97
D

ATOM
7129
CG
ARG D
446
151.387
5.796
31.448
1.00
42.38
D

ATOM
7130
CD
ARG D
446
152.190
4.636
30.925
1.00
44.42
D

ATOM
7131
NE
ARG D
446
153.302
4.360
31.835
1.00
48.85
D

ATOM
7132
CZ
ARG D
446
154.291
3.506
31.588
1.00
50.95
D

ATOM
7133
NH1
ARG D
446
154.316
2.834
30.442
1.00
52.13
D

ATOM
7134
NH2
ARG D
446
155.251
3.320
32.490
1.00
51.46
D

ATOM
7135
C
ARG D
446
148.155
7.527
30.296
1.00
40.71
D

ATOM
7136
O
ARG D
446
147.050
7.083
30.635
1.00
39.57
D

ATOM
7137
N
VAL D
447
148.357
8.253
29.195
1.00
40.90
D

ATOM
7138
CA
VAL D
447
147.293
8.552
28.237
1.00
41.54
D

ATOM
7139
CB
VAL D
447
147.260
10.037
27.849
1.00
40.47
D

ATOM
7140
CG1
VAL D
447
146.043
10.306
26.981
1.00
38.69
D

ATOM
7141
CG2
VAL D
447
147.226
10.895
29.100
1.00
40.93
D

ATOM
7142
C
VAL D
447
147.566
7.735
26.991
1.00
42.31
D

ATOM
7143
O
VAL D
447
148.689
7.712
26.501
1.00
43.98
D

ATOM
7144
N
TRP D
448
146.549
7.055
26.481
1.00
42.01
D

ATOM
7145
CA
TRP D
448
146.730
6.234
25.296
1.00
42.06
D

ATOM
7146
CB
TRP D
448
146.416
4.769
25.625
1.00
40.93
D

ATOM
7147
CG
TRP D
448
147.108
4.254
26.849
1.00
40.06
D

ATOM
7148
CD2
TRP D
448
148.167
3.294
26.890
1.00
39.39
D

ATOM
7149
CE2
TRP D
448
148.529
3.127
28.247
1.00
39.74
D

ATOM
7150
CE3
TRP D
448
148.846
2.555
25.911
1.00
37.93
D

ATOM
7151
CD1
TRP D
448
146.871
4.621
28.145
1.00
39.85
D

ATOM
7152
NE1
TRP D
448
147.720
3.949
28.992
1.00
39.87
D

ATOM
7153
CZ2
TRP D
448
149.552
2.247
28.653
1.00
38.84
D

ATOM
7154
CZ3
TRP D
448
149.860
1.680
26.314
1.00
38.08
D

ATOM
7155
CH2
TRP D
448
150.203
1.537
27.679
1.00
37.48
D

ATOM
7156
C
TRP D
448
145.825
6.705
24.156
1.00
42.74
D

ATOM
7157
O
TRP D
448
144.933
7.537
24.349
1.00
42.62
D

ATOM
7158
N
ASP D
449
146.067
6.165
22.967
1.00
43.66
D

ATOM
7159
CA
ASP D
449
145.265
6.485
21.797
1.00
44.36
D

ATOM
7160
CB
ASP D
449
146.062
7.368
20.836
1.00
45.33
D

ATOM
7161
CG
ASP D
449
145.256
7.782
19.616
1.00
46.25
D

ATOM
7162
OD1
ASP D
449
145.791
8.522
18.771
1.00
46.26
D

ATOM
7163
OD2
ASP D
449
144.088
7.370
19.494
1.00
47.22
D

ATOM
7164
C
ASP D
449
144.899
5.169
21.119
1.00
44.82
D

ATOM
7165
O
ASP D
449
145.735
4.551
20.468
1.00
44.81
D

ATOM
7166
N
ILE D
450
143.653
4.740
21.280
1.00
45.73
D

ATOM
7167
CA
ILE D
450
143.205
3.484
20.687
1.00
47.64
D

ATOM
7168
CB
ILE D
450
141.711
3.215
21.000
1.00
46.91
D

ATOM
7169
CG2
ILE D
450
141.335
1.820
20.527
1.00
45.80
D

ATOM
7170
CG1
ILE D
450
141.455
3.357
22.507
1.00
46.32
D

ATOM
7171
CD1
ILE D
450
140.009
3.138
22.920
1.00
46.07
D

ATOM
7172
C
ILE D
450
143.395
3.516
19.173
1.00
49.71
D

ATOM
7173
O
ILE D
450
143.890
2.556
18.573
1.00
49.74
D

ATOM
7174
N
LYS D
451
142.984
4.631
18.571
1.00
51.95
D

ATOM
7175
CA
LYS D
451
143.092
4.859
17.130
1.00
52.66
D

ATOM
7176
CB
LYS D
451
142.789
6.329
16.815
1.00
54.03
D

ATOM
7177
CG
LYS D
451
141.425
6.825
17.283
1.00
54.77
D

ATOM
7178
CD
LYS D
451
140.315
6.348
16.362
1.00
56.08
D

ATOM
7179
CE
LYS D
451
138.958
6.853
16.829
1.00
58.40
D

ATOM
7180
NZ
LYS D
451
138.564
6.293
18.170
1.00
60.81
D

ATOM
7181
C
LYS D
451
144.519
4.534
16.687
1.00
53.12
D

ATOM
7182
O
LYS D
451
144.743
3.637
15.875
1.00
52.92
D

ATOM
7183
N
LYS D
452
145.478
5.279
17.236
1.00
53.06
D

ATOM
7184
CA
LYS D
452
146.889
5.081
16.922
1.00
53.16
D

ATOM
7185
CB
LYS D
452
147.727
6.274
17.405
1.00
54.65
D

ATOM
7186
CG
LYS D
452
147.432
7.608
16.705
1.00
55.78
D

ATOM
7187
CD
LYS D
452
148.434
8.689
17.106
1.00
54.91
D

ATOM
7188
CE
LYS D
452
148.269
9.952
16.262
1.00
56.24
D

ATOM
7189
NZ
LYS D
452
146.931
10.592
16.394
1.00
55.58
D

ATOM
7190
C
LYS D
452
147.426
3.801
17.565
1.00
52.16
D

ATOM
7191
O
LYS D
452
148.530
3.352
17.257
1.00
52.14
D

ATOM
7192
N
GLY D
453
146.646
3.221
18.466
1.00
51.03
D

ATOM
7193
CA
GLY D
453
147.070
2.000
19.119
1.00
48.98
D

ATOM
7194
C
GLY D
453
148.425
2.076
19.795
1.00
47.55
D

ATOM
7195
O
GLY D
453
149.268
1.206
19.598
1.00
48.41
D

ATOM
7196
N
CYS D
454
148.643
3.111
20.595
1.00
45.89
D

ATOM
7197
CA
CYS D
454
149.903
3.252
21.306
1.00
45.10
D

ATOM
7198
CB
CYS D
454
151.007
3.764
20.371
1.00
45.35
D

ATOM
7199
SG
CYS D
454
151.016
5.592
20.180
1.00
46.05
D

ATOM
7200
C
CYS D
454
149.733
4.246
22.445
1.00
45.09
D

ATOM
7201
O
CYS D
454
148.660
4.827
22.632
1.00
43.95
D

ATOM
7202
N
CYS D
455
150.815
4.443
23.191
1.00
45.72
D

ATOM
7203
CA
CYS D
455
150.831
5.373
24.307
1.00
46.22
D

ATOM
7204
CB
CYS D
455
151.663
4.818
25.461
1.00
46.14
D

ATOM
7205
SG
CYS D
455
151.652
5.917
26.902
1.00
44.91
D

ATOM
7206
C
CYS D
455
151.412
6.717
23.880
1.00
45.90
D

ATOM
7207
O
CYS D
455
152.504
6.787
23.328
1.00
45.72
D

ATOM
7208
N
THR D
456
150.674
7.778
24.160
1.00
46.41
D

ATOM
7209
CA
THR D
456
151.089
9.114
23.807
1.00
47.30
D

ATOM
7210
CB
THR D
456
149.878
9.947
23.316
1.00
47.67
D

ATOM
7211
OG1
THR D
456
150.170
11.344
23.454
1.00
49.91
D

ATOM
7212
CG2
THR D
456
148.633
9.623
24.124
1.00
48.32
D

ATOM
7213
C
THR D
456
151.767
9.870
24.953
1.00
47.34
D

ATOM
7214
O
THR D
456
152.722
10.614
24.729
1.00
47.57
D

ATOM
7215
N
HIS D
457
151.280
9.691
26.177
1.00
46.90
D

ATOM
7216
CA
HIS D
457
151.850
10.407
27.315
1.00
46.66
D

ATOM
7217
CB
HIS D
457
150.935
11.569
27.708
1.00
48.78
D

ATOM
7218
CG
HIS D
457
150.781
12.608
26.639
1.00
52.07
D

ATOM
7219
CD2
HIS D
457
149.752
12.884
25.802
1.00
53.00
D

ATOM
7220
ND1
HIS D
457
151.768
13.525
26.349
1.00
51.90
D

ATOM
7221
CE1
HIS D
457
151.351
14.324
25.383
1.00
53.55
D

ATOM
7222
NE2
HIS D
457
150.131
13.957
25.033
1.00
53.69
D

ATOM
7223
C
HIS D
457
152.101
9.534
28.529
1.00
45.09
D

ATOM
7224
O
HIS D
457
151.360
8.591
28.797
1.00
46.21
D

ATOM
7225
N
VAL D
458
153.163
9.864
29.255
1.00
43.08
D

ATOM
7226
CA
VAL D
458
153.544
9.142
30.462
1.00
40.12
D

ATOM
7227
CB
VAL D
458
154.847
8.350
30.247
1.00
38.48
D

ATOM
7228
CG1
VAL D
458
155.106
7.437
31.430
1.00
36.35
D

ATOM
7229
CG2
VAL D
458
154.758
7.554
28.954
1.00
37.80
D

ATOM
7230
C
VAL D
458
153.761
10.197
31.535
1.00
38.68
D

ATOM
7231
O
VAL D
458
154.733
10.942
31.474
1.00
38.06
D

ATOM
7232
N
PHE D
459
152.834
10.267
32.491
1.00
37.03
D

ATOM
7233
CA
PHE D
459
152.902
11.230
33.588
1.00
35.98
D

ATOM
7234
CB
PHE D
459
151.526
11.848
33.859
1.00
35.38
D

ATOM
7235
CG
PHE D
459
151.009
12.705
32.729
1.00
36.52
D

ATOM
7236
CD1
PHE D
459
149.643
12.975
32.603
1.00
35.53
D

ATOM
7237
CD2
PHE D
459
151.882
13.228
31.773
1.00
36.02
D

ATOM
7238
CE1
PHE D
459
149.160
13.748
31.542
1.00
33.32
D

ATOM
7239
CE2
PHE D
459
151.404
13.999
30.715
1.00
34.61
D

ATOM
7240
CZ
PHE D
459
150.040
14.258
30.599
1.00
33.14
D

ATOM
7241
C
PHE D
459
153.421
10.583
34.858
1.00
35.63
D

ATOM
7242
O
PHE D
459
152.927
9.540
35.286
1.00
36.76
D

ATOM
7243
N
GLU D
460
154.436
11.210
35.443
1.00
34.40
D

ATOM
7244
CA
GLU D
460
155.042
10.731
36.669
1.00
32.85
D

ATOM
7245
CB
GLD D
460
156.541
10.572
36.501
1.00
31.50
D

ATOM
7246
CG
GLU D
460
156.912
9.591
35.436
1.00
34.06
D

ATOM
7247
CD
GLU D
460
158.340
9.146
35.561
1.00
34.99
D

ATOM
7248
OE1
GLU D
460
159.177
9.996
35.916
1.00
38.06
D

ATOM
7249
OE2
GLU D
460
158.634
7.959
35.305
1.00
34.49
D

ATOM
7250
C
GLU D
460
154.754
11.770
37.717
1.00
32.81
D

ATOM
7251
O
GLU D
460
154.506
12.927
37.387
1.00
33.34
D

ATOM
7252
N
GLY D
461
154.788
11.364
38.982
1.00
33.03
D

ATOM
7253
CA
GLY D
461
154.503
12.295
40.057
1.00
31.23
D

ATOM
7254
C
GLY D
461
154.150
11.600
41.354
1.00
30.79
D

ATOM
7255
O
GLY D
461
154.770
11.857
42.383
1.00
31.55
D

ATOM
7256
N
HIS D
462
153.151
10.727
41.318
1.00
30.63
D

ATOM
7257
CA
HIS D
462
152.744
10.016
42.522
1.00
30.77
D

ATOM
7258
CB
HIS D
462
151.580
9.065
42.209
1.00
30.12
D

ATOM
7259
CG
HIS D
462
150.254
9.754
42.066
1.00
29.59
D

ATOM
7260
CD2
HIS D
462
149.387
9.814
41.026
1.00
29.20
D

ATOM
7261
ND1
HIS D
462
149.701
10.520
43.070
1.00
27.98
D

ATOM
7262
CE1
HIS D
462
148.555
11.027
42.652
1.00
29.48
D

ATOM
7263
NE2
HIS D
462
148.342
10.615
41.415
1.00
29.45
D

ATOM
7264
C
HIS D
462
153.935
9.233
43.032
1.00
31.13
D

ATOM
7265
O
HIS D
462
154.687
8.672
42.240
1.00
32.76
D

ATOM
7266
N
ASN D
463
154.113
9.195
44.349
1.00
31.08
D

ATOM
7267
CA
ASN D
463
155.239
8.473
44.929
1.00
30.79
D

ATOM
7268
CB
ASN D
463
155.764
9.212
46.155
1.00
31.33
D

ATOM
7269
CG
ASN D
463
156.351
10.572
45.806
1.00
33.80
D

ATOM
7270
OD1
ASN D
463
156.669
11.368
46.700
1.00
36.56
D

ATOM
7271
ND2
ASN D
463
156.500
10.848
44.511
1.00
31.92
D

ATOM
7272
C
ASN D
463
154.863
7.058
45.300
1.00
30.83
D

ATOM
7273
O
ASN D
463
155.678
6.319
45.843
1.00
32.01
D

ATOM
7274
N
SER D
464
153.623
6.685
44.996
1.00
30.09
D

ATOM
7275
CA
SER D
464
153.099
5.346
45.292
1.00
29.60
D

ATOM
7276
CB
SER D
464
152.364
5.358
46.630
1.00
31.07
D

ATOM
7277
OG
SER D
464
153.073
4.621
47.611
1.00
34.87
D

ATOM
7278
C
SER D
464
152.125
4.900
44.203
1.00
28.55
D

ATOM
7279
O
SER D
464
151.814
5.656
43.289
1.00
29.29
D

ATOM
7280
N
THR D
465
151.625
3.676
44.313
1.00
27.12
D

ATOM
7281
CA
THR D
465
150.675
3.153
43.331
1.00
25.67
D

ATOM
7282
CB
THR D
465
150.036
1.828
43.817
1.00
23.85
D

ATOM
7283
OG1
THR D
465
151.057
0.894
44.197
1.00
24.69
D

ATOM
7284
CG2
THR D
465
149.169
1.234
42.742
1.00
22.12
D

ATOM
7285
C
THR D
465
149.536
4.150
43.089
1.00
26.17
D

ATOM
7286
O
THR D
465
149.122
4.872
44.001
1.00
27.21
D

ATOM
7287
N
VAL D
466
149.041
4.197
41.856
1.00
25.63
D

ATOM
7288
CA
VAL D
466
147.933
5.078
41.506
1.00
24.45
D

ATOM
7289
CB
VAL D
466
148.003
5.484
39.994
1.00
26.90
D

ATOM
7290
CG1
VAL D
466
146.795
6.351
39.597
1.00
27.11
D

ATOM
7291
CG2
VAL D
466
149.300
6.240
39.732
1.00
27.75
D

ATOM
7292
C
VAL D
466
146.740
4.165
41.783
1.00
22.49
D

ATOM
7293
O
VAL D
466
146.604
3.130
41.148
1.00
19.72
D

ATOM
7294
N
ARG D
467
145.894
4.543
42.737
1.00
21.80
D

ATOM
7295
CA
ARG D
467
144.764
3.713
43.121
1.00
21.09
D

ATOM
7296
CB
ARG D
467
144.529
3.828
44.637
1.00
21.63
D

ATOM
7297
CG
ARG D
467
143.582
2.778
45.221
1.00
24.03
D

ATOM
7298
CD
ARG D
467
144.190
1.398
45.033
1.00
25.89
D

ATOM
7299
NE
ARG D
467
143.247
0.294
45.158
1.00
27.91
D

ATOM
7300
CZ
ARG D
467
142.283
0.013
44.288
1.00
30.10
D

ATOM
7301
NH1
ARG D
467
142.117
0.776
43.214
1.00
32.22
D

ATOM
7302
NH2
ARG D
467
141.515
−1.064
44.469
1.00
28.51
D

ATOM
7303
C
ARG D
467
143.463
3.984
42.370
1.00
21.53
D

ATOM
7304
O
ARG D
467
142.666
3.071
42.152
1.00
21.18
D

ATOM
7305
N
CYS D
468
143.240
5.225
41.960
1.00
21.08
D

ATOM
7306
CA
CYS D
468
142.008
5.538
41.259
1.00
22.04
D

ATOM
7307
CB
CYS D
468
140.874
5.672
42.282
1.00
22.73
D

ATOM
7308
SG
CYS D
468
141.036
7.052
43.480
1.00
26.78
D

ATOM
7309
C
CYS D
468
142.141
6.807
40.433
1.00
22.89
D

ATOM
7310
O
CYS D
468
143.034
7.617
40.672
1.00
24.06
D

ATOM
7311
N
LEU D
469
141.247
6.995
39.466
1.00
23.65
D

ATOM
7312
CA
LEU D
469
141.321
8.189
38.614
1.00
25.22
D

ATOM
7313
CB
LEU D
469
142.382
7.997
37.512
1.00
25.67
D

ATOM
7314
CG
LEU D
469
142.191
6.914
36.441
1.00
25.46
D

ATOM
7315
CD1
LEU D
469
140.965
7.170
35.605
1.00
24.47
D

ATOM
7316
CD2
LEU D
469
143.428
6.891
35.560
1.00
26.81
D

ATOM
7317
C
LEU D
469
140.005
8.574
37.960
1.00
24.60
D

ATOM
7318
O
LEU D
469
139.162
7.729
37.690
1.00
24.12
D

ATOM
7319
N
ASP D
470
139.818
9.853
37.693
1.00
24.30
D

ATOM
7320
CA
ASP D
470
138.584
10.242
37.043
1.00
24.73
D

ATOM
7321
CB
ASP D
470
137.540
10.594
38.118
1.00
24.80
D

ATOM
7322
CG
ASP D
470
136.109
10.685
37.571
1.00
24.84
D

ATOM
7323
OD1
ASP D
470
135.842
10.240
36.441
1.00
25.89
D

ATOM
7324
OD2
ASP D
470
135.242
11.197
38.296
1.00
23.60
D

ATOM
7325
C
ASP D
470
138.857
11.409
36.091
1.00
24.57
D

ATOM
7326
O
ASP D
470
139.863
12.118
36.214
1.00
23.14
D

ATOM
7327
N
ILE D
471
137.988
11.584
35.110
1.00
24.45
D

ATOM
7328
CA
ILE D
471
138.184
12.684
34.197
1.00
26.31
D

ATOM
7329
CB
ILE D
471
138.389
12.210
32.737
1.00
24.06
D

ATOM
7330
CG2
ILE D
471
138.861
13.393
31.915
1.00
24.13
D

ATOM
7331
CG1
ILE D
471
139.454
11.097
32.656
1.00
22.43
D

ATOM
7332
CD1
ILE D
471
139.553
10.449
31.293
1.00
18.18
D

ATOM
7333
C
ILE D
471
136.971
13.600
34.271
1.00
28.56
D

ATOM
7334
O
ILE D
471
135.833
13.135
34.280
1.00
30.74
D

ATOM
7335
N
VAL D
472
137.222
14.901
34.358
1.00
30.47
D

ATOM
7336
CA
VAL D
472
136.157
15.892
34.433
1.00
31.86
D

ATOM
7337
CB
VAL D
472
136.105
16.544
35.857
1.00
31.83
D

ATOM
7338
CG1
VAL D
472
135.793
15.474
36.896
1.00
30.28
D

ATOM
7339
CG2
VAL D
472
137.427
17.231
36.193
1.00
27.41
D

ATOM
7340
C
VAL D
472
136.369
16.966
33.358
1.00
33.87
D

ATOM
7341
O
VAL D
472
137.474
17.119
32.826
1.00
34.57
D

ATOM
7342
N
GLU D
473
135.304
17.692
33.026
1.00
35.69
D

ATOM
7343
CA
GLU D
473
135.354
18.747
32.004
1.00
37.97
D

ATOM
7344
CE
GLU D
473
134.565
18.321
30.751
1.00
39.26
D

ATOM
7345
CG
GLU D
473
134.587
19.326
29.567
1.00
41.82
D

ATOM
7346
CD
GLU D
473
133.581
18.966
28.455
1.00
41.92
D

ATOM
7347
OE1
GLU D
473
133.651
17.853
27.893
1.00
41.68
D

ATOM
7348
OE2
GLU D
473
132.712
19.801
28.145
1.00
42.75
D

ATOM
7349
C
GLU D
473
134.722
19.983
32.620
1.00
38.63
D

ATOM
7350
O
GLU D
473
133.585
19.944
33.084
1.00
39.66
D

ATOM
7351
N
TYR D
474
135.464
21.077
32.651
1.00
39.16
D

ATOM
7352
CA
TYR D
474
134.952
22.311
33.231
1.00
39.98
D

ATOM
7353
CB
TYR D
474
135.534
22.496
34.630
1.00
39.54
D

ATOM
7354
CG
TYR D
474
135.126
23.777
35.311
1.00
40.62
D

ATOM
7355
CD1
TYR D
474
133.802
24.002
35.686
1.00
40.93
D

ATOM
7356
CE1
TYR D
474
133.432
25.174
36.332
1.00
40.40
D

ATOM
7357
CD2
TYR D
474
136.072
24.761
35.601
1.00
40.52
D

ATOM
7358
CE2
TYR D
474
135.714
25.933
36.243
1.00
40.34
D

ATOM
7359
CZ
TYR D
474
134.393
26.134
36.604
1.00
40.71
D

ATOM
7360
OH
TYR D
474
134.025
27.300
37.224
1.00
41.79
D

ATOM
7361
C
TYR D
474
135.422
23.394
32.277
1.00
39.99
D

ATOM
7362
O
TYR D
474
136.550
23.339
31.784
1.00
40.02
D

ATOM
7363
N
LYS D
475
134.551
24.357
31.998
1.00
40.09
D

ATOM
7364
CA
LYE D
475
134.868
25.438
31.069
1.00
42.55
D

ATOM
7365
CE
LYE D
475
135.796
26.471
31.723
1.00
43.10
D

ATOM
7366
CG
LYS D
475
135.185
27.292
32.864
1.00
43.55
D

ATOM
7367
CD
LYS D
475
136.276
28.148
33.502
1.00
46.85
D

ATOM
7368
CE
LYE D
475
135.765
29.052
34.623
1.00
48.93
D

ATOM
7369
NZ
LYE D
475
134.765
30.077
34.181
1.00
49.55
D

ATOM
7370
C
LYE D
475
135.529
24.888
29.804
1.00
43.23
D

ATOM
7371
O
LYE D
475
136.556
25.401
29.352
1.00
43.08
D

ATOM
7372
N
ASN D
476
134.943
23.831
29.248
1.00
44.27
D

ATOM
7373
CA
ASN D
476
135.449
23.202
28.024
1.00
44.54
D

ATOM
7374
CB
ASN D
476
135.383
24.180
26.850
1.00
44.94
D

ATOM
7375
CG
ASN D
476
134.054
24.135
26.140
1.00
44.85
D

ATOM
7376
OD1
ASN D
476
133.040
24.596
26.665
1.00
44.09
D

ATOM
7377
ND2
ASN D
476
134.048
23.565
24.934
1.00
45.89
D

ATOM
7378
C
ASN D
476
136.841
22.591
28.077
1.00
44.03
D

ATOM
7379
O
ASN D
476
137.403
22.230
27.036
1.00
44.45
D

ATOM
7380
N
ILE D
477
137.400
22.474
29.280
1.00
43.98
D

ATOM
7381
CA
ILE D
477
138.722
21.860
29.459
1.00
42.39
D

ATOM
7382
CB
ILE D
477
139.681
22.744
30.260
1.00
42.82
D

ATOM
7383
CG2
ILE D
477
141.024
22.052
30.387
1.00
43.06
D

ATOM
7384
CG1
ILE D
477
139.842
24.097
29.583
1.00
42.36
D

ATOM
7385
CD1
ILE D
477
140.465
25.135
30.486
1.00
41.94
D

ATOM
7386
C
ILE D
477
138.528
20.578
30.249
1.00
41.19
D

ATOM
7387
O
ILE D
477
137.805
20.560
31.253
1.00
40.43
D

ATOM
7388
N
LYS D
478
139.166
19.511
29.777
1.00
38.84
D

ATOM
7389
CA
LYS D
478
139.078
18.212
30.428
1.00
36.96
D

ATOM
7390
CB
LYS D
478
139.070
17.085
29.394
1.00
35.75
D

ATOM
7391
CG
LYS D
478
137.740
16.932
28.687
1.00
35.23
D

ATOM
7392
CD
LYS D
478
137.557
15.519
28.160
1.00
32.30
D

ATOM
7393
CE
LYS D
478
136.120
15.312
27.725
1.00
31.88
D

ATOM
7394
NZ
LYS D
478
135.743
13.871
27.552
1.00
32.71
D

ATOM
7395
C
LYS D
478
140.218
17.984
31.402
1.00
36.46
D

ATOM
7396
O
LYS D
478
141.381
18.009
31.015
1.00
36.77
D

ATOM
7397
N
TYR D
479
139.884
17.749
32.666
1.00
35.14
D

ATOM
7398
CA
TYR D
479
140.906
17.514
33.675
1.00
34.37
D

ATOM
7399
CB
TYR D
479
140.674
18.442
34.875
1.00
33.93
D

ATOM
7400
CG
TYR D
479
140.847
19.914
34.543
1.00
34.98
D

ATOM
7401
CD1
TYR D
479
142.108
20.529
34.614
1.00
33.05
D

ATOM
7402
CE1
TYR D
479
142.264
21.880
34.300
1.00
32.76
D

ATOM
7403
CD2
TYR D
479
139.753
20.691
34.147
1.00
33.92
D

ATOM
7404
CE2
TYR D
479
139.901
22.037
33.830
1.00
34.11
D

ATOM
7405
CZ
TYR D
479
141.152
22.624
33.907
1.00
34.22
D

ATOM
7406
OH
TYR D
479
141.270
23.952
33.573
1.00
37.80
D

ATOM
7407
C
TYR D
479
140.936
16.061
34.134
1.00
32.92
D

ATOM
7408
O
TYR D
479
139.903
15.404
34.218
1.00
32.94
D

ATOM
7409
N
ILE D
480
142.138
15.569
34.412
1.00
31.23
D

ATOM
7410
CA
ILE D
480
142.344
14.213
34.910
1.00
30.00
D

ATOM
7411
CB
ILE D
480
143.568
13.528
34.236
1.00
30.27
D

ATOM
7412
CG2
ILE D
480
143.826
12.150
34.879
1.00
31.07
D

ATOM
7413
CG1
ILE D
480
143.335
13.334
32.741
1.00
31.12
D

ATOM
7414
CD1
ILE D
480
144.440
12.531
32.060
1.00
26.66
D

ATOM
7415
C
ILE D
480
142.674
14.314
36.417
1.00
29.96
D

ATOM
7416
O
ILE D
480
143.583
15.063
36.808
1.00
29.34
D

ATOM
7417
N
VAL D
481
141.944
13.582
37.263
1.00
28.07
D

ATOM
7418
CA
VAL D
481
142.234
13.590
38.702
1.00
26.17
D

ATOM
7419
CB
VAL D
481
141.048
14.099
39.550
1.00
25.50
D

ATOM
7420
CG1
VAL D
481
141.533
14.438
40.943
1.00
25.80
D

ATOM
7421
CG2
VAL D
481
140.431
15.338
38.910
1.00
26.04
D

ATOM
7422
C
VAL D
481
142.587
12.166
39.110
1.00
26.07
D

ATOM
7423
O
VAL D
481
141.848
11.232
38.812
1.00
26.50
D

ATOM
7424
N
THR D
482
143.734
12.006
39.766
1.00
26.06
D

ATOM
7425
CA
THR D
482
144.217
10.691
40.184
1.00
26.60
D

ATOM
7426
CB
THR D
482
145.520
10.324
39.440
1.00
25.75
D

ATOM
7427
OG1
THR D
482
146.452
11.402
39.568
1.00
23.78
D

ATOM
7428
CG2
THR D
482
145.252
10.057
37.971
1.00
26.32
D

ATOM
7429
C
THR D
482
144.496
10.591
41.688
1.00
27.46
D

ATOM
7430
O
THR D
482
145.180
11.444
42.267
1.00
29.29
D

ATOM
7431
N
GLY D
483
143.977
9.530
42.303
1.00
25.97
D

ATOM
7432
CA
GLY D
483
144.176
9.303
43.724
1.00
24.32
D

ATOM
7433
C
GLY D
483
145.201
8.206
43.922
1.00
23.49
D

ATOM
7434
O
GLY D
483
145.156
7.171
43.236
1.00
23.98
D

ATOM
7435
N
SER D
484
146.106
8.428
44.877
1.00
22.04
D

ATOM
7436
CA
SER D
484
147.208
7.503
45.153
1.00
21.89
D

ATOM
7437
CB
SER D
484
148.540
8.193
44.820
1.00
19.14
D

ATOM
7438
OG
SER D
484
149.640
7.324
45.038
1.00
17.25
D

ATOM
7439
C
SER D
484
147.266
7.012
46.582
1.00
22.62
D

ATOM
7440
O
SER D
484
146.488
7.433
47.426
1.00
25.82
D

ATOM
7441
N
ARG D
485
148.193
6.100
46.837
1.00
24.32
D

ATOM
7442
CA
ARG D
485
148.412
5.585
48.179
1.00
26.12
D

ATOM
7443
CB
ARG D
485
149.052
4.206
48.134
1.00
27.36
D

ATOM
7444
CG
ARG D
485
148.168
3.160
47.556
1.00
28.76
D

ATOM
7445
CD
ARG D
485
148.786
1.809
47.722
1.00
29.11
D

ATOM
7446
NE
ARG D
485
147.768
0.784
47.543
1.00
31.30
D

ATOM
7447
CZ
ARG D
485
148.031
−0.500
47.350
1.00
31.33
D

ATOM
7448
NH1
ARG D
485
149.283
−0.931
47.304
1.00
30.94
D

ATOM
7449
NH2
ARG D
485
147.039
−1.353
47.214
1.00
31.96
D

ATOM
7450
C
ARG D
485
149.367
6.534
48.886
1.00
27.46
D

ATOM
7451
O
ARG D
485
149.712
6.329
50.045
1.00
28.74
D

ATOM
7452
N
ASP D
486
149.822
7.561
48.186
1.00
27.88
D

ATOM
7453
CA
ASP D
486
150.722
8.487
48.819
1.00
27.38
D

ATOM
7454
CB
ASP D
486
151.631
9.137
47.789
1.00
29.39
D

ATOM
7455
CG
ASP D
486
150.858
9.822
46.695
1.00
30.30
D

ATOM
7456
OD1
ASP D
486
149.693
10.190
46.951
1.00
28.83
D

ATOM
7457
OD2
ASP D
486
151.410
10.006
45.591
1.00
33.15
D

ATOM
7458
C
ASP D
486
149.947
9.547
49.566
1.00
26.08
D

ATOM
7459
O
ASP D
486
150.524
10.533
49.997
1.00
26.51
D

ATOM
7460
N
ASN D
487
148.643
9.343
49.727
1.00
26.47
D

ATOM
7461
CA
ASN D
487
147.778
10.295
50.449
1.00
28.03
D

ATOM
7462
CB
ASN D
487
148.466
10.859
51.720
1.00
24.22
D

ATOM
7463
CG
ASN D
487
149.130
9.783
52.608
1.00
25.85
D

ATOM
7464
OD1
ASN D
487
150.077
10.094
53.357
1.00
25.75
D

ATOM
7465
ND2
ASN D
487
148.639
8.536
52.543
1.00
23.88
D

ATOM
7466
C
ASN D
487
147.331
11.492
49.578
1.00
29.17
D

ATOM
7467
O
ASN D
487
146.419
12.233
49.958
1.00
30.88
D

ATOM
7468
N
THR D
488
147.959
11.686
48.419
1.00
30.51
D

ATOM
7469
CA
THR D
488
147.599
12.817
47.574
1.00
31.76
D

ATOM
7470
CB
THR D
488
148.867
13.590
47.044
1.00
32.19
D

ATOM
7471
OG1
THR D
488
149.361
12.984
45.841
1.00
30.87
D

ATOM
7472
CG2
THR D
488
149.968
13.586
48.078
1.00
32.86
D

ATOM
7473
C
THR D
488
146.708
12.444
46.387
1.00
33.20
D

ATOM
7474
O
THR D
488
146.374
11.267
46.172
1.00
32.98
D

ATOM
7475
N
LEU D
489
146.310
13.480
45.650
1.00
34.03
D

ATOM
7476
CA
LEU D
489
145.468
13.377
44.465
1.00
34.19
D

ATOM
7477
CS
LEU D
489
144.056
13.869
44.779
1.00
34.15
D

ATOM
7478
CG
LEU D
489
143.138
12.961
45.589
1.00
34.12
D

ATOM
7479
CD1
LEU D
489
142.459
13.747
46.710
1.00
33.50
D

ATOM
7480
CD2
LEU D
489
142.102
12.369
44.642
1.00
32.16
D

ATOM
7481
C
LEU D
489
146.084
14.320
43.448
1.00
33.40
D

ATOM
7482
O
LEU D
489
145.854
15.519
43.533
1.00
34.39
D

ATOM
7483
N
HIS D
490
146.876
13.818
42.506
1.00
32.48
D

ATOM
7484
CA
HIS D
490
147.465
14.727
41.522
1.00
31.60
D

ATOM
7485
CB
HIS D
490
148.744
14.136
40.909
1.00
31.07
D

ATOM
7486
CG
HIS D
490
149.914
14.125
41.846
1.00
31.65
D

ATOM
7487
CD2
HIS D
490
149.977
14.042
43.197
1.00
32.29
D

ATOM
7488
ND1
HIS D
490
151.219
14.191
41.407
1.00
33.73
D

ATOM
7489
CE1
HIS D
490
152.036
14.152
42.446
1.00
33.37
D

ATOM
7490
NE2
HIS D
490
151.306
14.061
43.543
1.00
32.68
D

ATOM
7491
C
HIS D
490
146.456
15.034
40.429
1.00
30.39
D

ATOM
7492
O
HIS D
490
145.735
14.149
39.983
1.00
31.27
D

ATOM
7493
N
VAL D
491
146.391
16.296
40.022
1.00
29.80
D

ATOM
7494
CA
VAL D
491
145.466
16.726
38.977
1.00
31.12
D

ATOM
7495
CB
VAL D
491
144.610
17.941
39.472
1.00
30.67
D

ATOM
7496
CG1
VAL D
491
143.683
18.442
38.365
1.00
29.26
D

ATOM
7497
CG2
VAL D
491
143.798
17.544
40.683
1.00
29.19
D

ATOM
7498
C
VAL D
491
146.256
17.127
37.712
1.00
32.27
D

ATOM
7499
O
VAL D
491
147.249
17.850
37.802
1.00
33.21
D

ATOM
7500
N
TRP D
492
145.829
16.647
36.545
1.00
32.46
D

ATOM
7501
CA
TRP D
492
146.501
16.975
35.285
1.00
33.55
D

ATOM
7502
CB
TRP D
492
147.308
15.798
34.759
1.00
33.18
D

ATOM
7503
CG
TRP D
492
147.697
14.828
35.788
1.00
34.51
D

ATOM
7504
CD2
TRP D
492
149.014
14.604
36.288
1.00
35.06
D

ATOM
7505
CE2
TRP D
492
148.930
13.552
37.224
1.00
34.88
D

ATOM
7506
CE3
TRP D
492
150.263
15.189
36.034
1.00
33.09
D

ATOM
7507
CD1
TRP D
492
146.884
13.936
36.423
1.00
34.18
D

ATOM
7508
NE1
TRP D
492
147.617
13.161
37.285
1.00
34.58
D

ATOM
7509
CZ2
TRP D
492
150.048
13.073
37.906
1.00
34.36
D

ATOM
7510
CZ3
TRP D
492
151.371
14.715
36.710
1.00
32.50
D

ATOM
7511
CH2
TRP D
492
151.258
13.667
37.634
1.00
33.38
D

ATOM
7512
C
TRP D
492
145.475
17.318
34.226
1.00
34.32
D

ATOM
7513
O
TRP D
492
144.338
16.864
34.292
1.00
35.53
D

ATOM
7514
N
LYS D
493
145.859
18.110
33.236
1.00
34.28
D

ATOM
7515
CA
LYS D
493
144.900
18.433
32.202
1.00
35.06
D

ATOM
7516
CB
LYS D
493
145.116
19.860
31.694
1.00
35.38
D

ATOM
7517
CG
LYS D
493
146.531
20.133
31.281
1.00
37.78
D

ATOM
7518
CD
LYS D
493
146.739
21.563
30.810
1.00
39.13
D

ATOM
7519
CE
LYS D
493
146.643
22.588
31.928
1.00
37.56
D

ATOM
7520
NZ
LYS D
493
147.094
23.906
31.410
1.00
35.80
D

ATOM
7521
C
LYS D
493
145.075
17.408
31.084
1.00
34.97
D

ATOM
7522
O
LYS D
493
146.182
17.192
30.600
1.00
33.77
D

ATOM
7523
N
LEU D
494
143.981
16.753
30.706
1.00
36.70
D

ATOM
7524
CA
LEU D
494
144.018
15.744
29.659
1.00
39.45
D

ATOM
7525
CB
LEU D
494
142.630
15.126
29.458
1.00
39.18
D

ATOM
7526
CG
LEU D
494
142.458
14.046
28.380
1.00
38.09
D

ATOM
7527
CD1
LEU D
494
143.506
12.972
28.552
1.00
36.77
D

ATOM
7528
CD2
LEU D
494
141.043
13.442
28.448
1.00
36.96
D

ATOM
7529
C
LEU D
494
144.493
16.382
28.366
1.00
42.52
D

ATOM
7530
O
LEU D
494
143.928
17.387
27.912
1.00
42.98
D

ATOM
7531
N
PRO D
495
145.559
15.819
27.764
1.00
45.09
D

ATOM
7532
CD
PRO D
495
146.315
14.686
28.330
1.00
45.01
D

ATOM
7533
CA
PRO D
495
146.168
16.287
26.505
1.00
45.59
D

ATOM
7534
CB
PRO D
495
147.255
15.253
26.241
1.00
45.10
D

ATOM
7535
CG
PRO D
495
147.633
14.802
27.619
1.00
45.87
D

ATOM
7536
C
PRO D
495
145.146
16.324
25.365
1.00
46.50
D

ATOM
7537
O
PRO D
495
144.334
15.409
25.243
1.00
47.18
D

ATOM
7538
N
LYS D
496
145.194
17.360
24.525
1.00
47.14
D

ATOM
7539
CA
LYS D
496
144.254
17.491
23.400
1.00
47.35
D

ATOM
7540
CB
LYS D
496
143.768
18.942
23.268
1.00
47.30
D

ATOM
7541
CG
LYS D
496
143.109
19.501
24.520
0.00
47.88
D

ATOM
7542
CD
LYS D
496
141.811
18.778
24.840
0.00
48.23
D

ATOM
7543
CE
LYS D
496
141.133
19.370
26.065
0.00
48.50
D

ATOM
7544
NZ
LYS D
496
139.817
18.722
26.331
0.00
48.74
D

ATOM
7545
C
LYS D
496
144.853
17.046
22.064
1.00
47.41
D

ATOM
7546
O
LYS D
496
145.277
15.898
21.895
1.00
46.92
D

ATOM
7547
N
ASP D
508
157.546
8.144
18.136
1.00
82.08
D

ATOM
7548
CA
ASP D
508
158.190
8.937
19.182
1.00
81.66
D

ATOM
7549
CB
ASP D
508
158.981
10.090
18.569
1.00
82.86
D

ATOM
7550
CG
ASP D
508
158.086
11.249
18.168
1.00
83.90
D

ATOM
7551
OD1
ASP D
508
157.135
11.025
17.381
1.00
83.92
D

ATOM
7552
OD2
ASP D
508
158.334
12.378
18.644
1.00
83.63
D

ATOM
7553
C
ASP D
508
157.121
9.528
20.096
1.00
80.44
D

ATOM
7554
O
ASP D
508
157.419
10.346
20.972
1.00
80.05
D

ATOM
7555
N
TYR D
509
155.874
9.120
19.884
1.00
78.72
D

ATOM
7556
CA
TYR D
509
154.768
9.631
20.678
1.00
76.03
D

ATOM
7557
CB
TYR D
509
153.454
8.997
20.254
1.00
76.05
D

ATOM
7558
CG
TYR D
509
152.443
10.025
19.841
1.00
77.13
D

ATOM
7559
CD1
TYR D
509
152.268
11.195
20.579
1.00
77.84
D

ATOM
7560
CE1
TYR D
509
151.324
12.147
20.205
1.00
79.73
D

ATOM
7561
CD2
TYR D
509
151.653
9.830
18.719
1.00
78.10
D

ATOM
7562
CE2
TYR D
509
150.709
10.769
18.335
1.00
79.97
D

ATOM
7563
CZ
TYR D
509
150.543
11.923
19.080
1.00
80.67
D

ATOM
7564
OH
TYR D
509
149.570
12.832
18.715
1.00
82.17
D

ATOM
7565
C
TYR D
509
154.938
9.440
22.170
1.00
73.80
D

ATOM
7566
O
TYR D
509
154.457
10.253
22.960
1.00
75.57
D

ATOM
7567
N
PRO D
510
155.602
8.352
22.588
1.00
70.29
D

ATOM
7568
CD
PRO D
510
156.084
7.160
21.860
1.00
68.38
D

ATOM
7569
CA
PRO D
510
155.758
8.194
24.039
1.00
66.01
D

ATOM
7570
CB
PRO D
510
156.600
6.929
24.150
1.00
66.48
D

ATOM
7571
CG
PRO D
510
156.132
6.128
22.949
1.00
68.27
D

ATOM
7572
C
PRO D
510
156.446
9.424
24.644
1.00
62.34
D

ATOM
7573
O
PRO D
510
157.667
9.504
24.676
1.00
62.17
D

ATOM
7574
N
LEU D
511
155.655
10.392
25.096
1.00
58.50
D

ATOM
7575
CA
LEU D
511
156.197
11.603
25.700
1.00
54.92
D

ATOM
7576
CB
LEU D
511
155.354
12.806
25.313
1.00
54.10
D

ATOM
7577
CG
LEU D
511
155.130
12.940
23.807
1.00
52.83
D

ATOM
7578
CD1
LEU D
511
154.228
14.114
23.521
1.00
51.33
D

ATOM
7579
CD2
LEU D
511
156.467
13.102
23.107
1.00
52.54
D

ATOM
7580
C
LEU D
511
156.188
11.451
27.211
1.00
53.49
D

ATOM
7581
O
LEU D
511
155.145
11.576
27.847
1.00
53.00
D

ATOM
7582
N
VAL D
512
157.359
11.184
27.778
1.00
52.14
D

ATOM
7583
CA
VAL D
512
157.506
10.992
29.213
1.00
49.88
D

ATOM
7584
CB
VAL D
512
158.576
9.937
29.498
1.00
48.71
D

ATOM
7585
CG1
VAL D
512
158.654
9.664
30.992
1.00
49.81
D

ATOM
7586
CG2
VAL D
512
158.262
8.666
28.725
1.00
47.64
D

ATOM
7587
C
VAL D
512
157.889
12.265
29.954
1.00
49.28
D

ATOM
7588
O
VAL D
512
158.855
12.925
29.592
1.00
48.19
D

ATOM
7589
N
PHE D
513
157.126
12.598
30.994
1.00
50.24
D

ATOM
7590
CA
PHE D
513
157.397
13.778
31.823
1.00
51.82
D

ATOM
7591
CB
PHE D
513
156.158
14.671
31.950
1.00
51.83
D

ATOM
7592
CG
PHE D
513
155.565
15.091
30.632
1.00
52.04
D

ATOM
7593
CD1
PHE D
513
154.849
14.187
29.856
1.00
52.52
D

ATOM
7594
CD2
PHE D
513
155.724
16.392
30.164
1.00
51.87
D

ATOM
7595
CE1
PHE D
513
154.305
14.571
28.635
1.00
52.41
D

ATOM
7596
CE2
PHE D
513
155.182
16.785
28.944
1.00
51.44
D

ATOM
7597
CZ
PHE D
513
154.472
15.873
28.181
1.00
51.72
D

ATOM
7598
C
PHE D
513
157.807
13.318
33.225
1.00
52.58
D

ATOM
7599
O
PHE D
513
156.957
13.164
34.100
1.00
53.73
D

ATOM
7600
N
HIS D
514
159.107
13.108
33.427
1.00
52.88
D

ATOM
7601
CA
HIS D
514
159.649
12.656
34.707
1.00
52.63
D

ATOM
7602
CB
HIS D
514
161.150
12.425
34.577
1.00
52.45
D

ATOM
7603
CG
HIS D
514
161.495
11.297
33.662
1.00
53.43
D

ATOM
7604
CD2
HIS D
514
161.857
11.285
32.358
1.00
53.76
D

ATOM
7605
ND1
HIS D
514
161.411
9.977
34.049
1.00
54.13
D

ATOM
7606
CE1
HIS D
514
161.705
9.199
33.023
1.00
54.22
D

ATOM
7607
NE2
HIS D
514
161.979
9.968
31.985
1.00
55.05
D

ATOM
7608
C
HIS D
514
159.388
13.615
35.855
1.00
53.18
D

ATOM
7609
O
HIS D
514
159.096
13.204
36.986
1.00
54.06
D

ATOM
7610
N
THR D
515
159.494
14.901
35.569
1.00
52.64
D

ATOM
7611
CA
THR D
515
159.281
15.888
36.597
1.00
52.40
D

ATOM
7612
CB
THR D
515
160.524
16.788
36.742
1.00
52.48
D

ATOM
7613
OG1
THR D
515
160.166
17.996
37.420
1.00
52.59
D

ATOM
7614
CG2
THR D
515
161.126
17.093
35.381
1.00
52.87
D

ATOM
7615
C
THR D
515
158.029
16.705
36.322
1.00
52.17
D

ATOM
7616
O
THR D
515
157.858
17.269
35.245
1.00
51.18
D

ATOM
7617
N
PRO D
516
157.114
16.736
37.304
1.00
53.39
D

ATOM
7618
CD
PRO D
516
157.164
15.841
38.478
1.00
53.89
D

ATOM
7619
CA
PRO D
516
155.835
17.449
37.271
1.00
52.84
D

ATOM
7620
CB
PRO D
516
155.231
17.119
38.632
1.00
52.59
D

ATOM
7621
CG
PRO D
516
155.703
15.729
38.851
1.00
52.83
D

ATOM
7622
C
PRO D
516
155.976
18.939
37.057
1.00
51.67
D

ATOM
7623
O
PRO D
516
155.238
19.533
36.279
1.00
52.06
D

ATOM
7624
N
GLU D
517
156.925
19.545
37.751
1.00
51.53
D

ATOM
7625
CA
GLD D
517
157.115
20.974
37.615
1.00
51.30
D

ATOM
7626
CB
GLU D
517
158.171
21.456
38.611
1.00
53.01
D

ATOM
7627
CG
GLU D
517
157.783
21.225
40.076
1.00
55.65
D

ATOM
7628
CD
GLU D
517
156.339
21.648
40.384
1.00
57.61
D

ATOM
7629
OE1
GLU D
517
155.899
22.718
39.901
1.00
58.27
D

ATOM
7630
OE2
GLU D
517
155.641
20.911
41.115
1.00
58.41
D

ATOM
7631
C
GLU D
517
157.482
21.376
36.180
1.00
50.73
D

ATOM
7632
O
GLD D
517
157.417
22.549
35.824
1.00
50.38
D

ATOM
7633
N
GLU D
518
157.853
20.408
35.350
1.00
49.94
D

ATOM
7634
CA
GLU D
518
158.200
20.707
33.964
1.00
48.95
D

ATOM
7635
CB
GLU D
518
159.552
20.081
33.613
1.00
49.87
D

ATOM
7636
CG
GLU D
518
160.741
20.801
34.239
1.00
51.31
D

ATOM
7637
CD
GLU D
518
162.074
20.125
33.945
1.00
52.52
D

ATOM
7638
OE1
GLU D
518
162.225
19.579
32.823
1.00
53.98
D

ATOM
7639
OE2
GLU D
518
162.971
20.153
34.826
1.00
50.01
D

ATOM
7640
C
GLU D
518
157.119
20.209
33.003
1.00
47.92
D

ATOM
7641
O
GLU D
518
157.143
20.496
31.808
1.00
47.01
D

ATOM
7642
N
ASN D
519
156.164
19.465
33.541
1.00
47.59
D

ATOM
7643
CA
ASN D
519
155.071
18.933
32.746
1.00
46.99
D

ATOM
7644
CB
ASN D
519
154.490
17.710
33.459
1.00
45.93
D

ATOM
7645
CG
ASN D
519
153.454
16.995
32.633
1.00
45.28
D

ATOM
7646
OD1
ASN D
519
152.907
15.970
33.055
1.00
45.38
D

ATOM
7647
ND2
ASN D
519
153.173
17.526
31.445
1.00
42.56
D

ATOM
7648
C
ASN D
519
153.998
20.023
32.551
1.00
46.69
D

ATOM
7649
O
ASN D
519
153.408
20.516
33.524
1.00
46.92
D

ATOM
7650
N
PRO D
520
153.758
20.431
31.291
1.00
45.28
D

ATOM
7651
CD
PRO D
520
154.544
20.037
30.110
1.00
43.44
D

ATOM
7652
CA
PRO D
520
152.769
21.460
30.937
1.00
44.93
D

ATOM
7653
CB
PRO D
520
152.965
21.621
29.431
1.00
43.10
D

ATOM
7654
CG
PRO D
520
154.396
21.232
29.234
1.00
43.83
D

ATOM
7655
C
PRO D
520
151.328
21.058
31.265
1.00
44.42
D

ATOM
7656
O
PRO D
520
150.430
21.899
31.341
1.00
45.05
D

ATOM
7657
N
TYR D
521
151.126
19.764
31.465
1.00
43.22
D

ATOM
7658
CA
TYR D
521
149.808
19.216
31.733
1.00
42.86
D

ATOM
7659
CB
TYR D
521
149.707
17.885
31.017
1.00
42.46
D

ATOM
7660
CG
TYR D
521
150.006
17.994
29.543
1.00
41.84
D

ATOM
7661
CD1
TYR D
521
149.117
18.639
28.684
1.00
43.00
D

ATOM
7662
CE1
TYR D
521
149.330
18.673
27.315
1.00
42.26
D

ATOM
7663
CD2
TYR D
521
151.135
17.395
28.996
1.00
42.03
D

ATOM
7664
CE2
TYR D
521
151.363
17.422
27.625
1.00
42.28
D

ATOM
7665
CZ
TYR D
521
150.445
18.058
26.788
1.00
43.30
D

ATOM
7666
OH
TYR D
521
150.592
18.015
25.418
1.00
44.00
D

ATOM
7667
C
TYR D
521
149.444
19.047
33.211
1.00
42.72
D

ATOM
7668
O
TYR D
521
148.267
18.922
33.567
1.00
42.06
D

ATOM
7669
N
PHE D
522
150.459
19.030
34.065
1.00
41.61
D

ATOM
7670
CA
PHE D
522
150.263
18.902
35.500
1.00
40.23
D

ATOM
7671
CB
PHE D
522
151.606
18.630
36.163
1.00
40.93
D

ATOM
7672
CG
PHE D
522
151.580
18.761
37.646
1.00
41.77
D

ATOM
7673
CD1
PHE D
522
150.784
17.923
38.415
1.00
42.70
D

ATOM
7674
CD2
PHE D
522
152.362
19.716
38.280
1.00
42.48
D

ATOM
7675
CE1
PHE D
522
150.770
18.030
39.800
1.00
43.11
D

ATOM
7676
CE2
PHE D
522
152.357
19.835
39.665
1.00
43.56
D

ATOM
7677
CZ
PHE D
522
151.559
18.989
40.427
1.00
44.10
D

ATOM
7678
C
PHE D
522
149.682
20.218
36.013
1.00
38.95
D

ATOM
7679
O
PHE D
522
149.994
21.271
35.470
1.00
38.64
D

ATOM
7680
N
VAL D
523
148.823
20.169
37.028
1.00
38.34
D

ATOM
7681
CA
VAL D
523
148.256
21.407
37.559
1.00
38.44
D

ATOM
7682
CB
VAL D
523
146.720
21.500
37.351
1.00
37.33
D

ATOM
7683
CG1
VAL D
523
146.352
21.189
35.900
1.00
35.81
D

ATOM
7684
CG2
VAL D
523
146.020
20.585
38.298
1.00
39.53
D

ATOM
7685
C
VAL D
523
148.543
21.590
39.044
1.00
38.09
D

ATOM
7686
O
VAL D
523
148.774
22.712
39.510
1.00
38.38
D

ATOM
7687
N
GLY D
524
148.543
20.484
39.780
1.00
36.48
D

ATOM
7688
CA
GLY D
524
148.798
20.567
41.203
1.00
35.67
D

ATOM
7689
C
GLY D
524
148.389
19.349
42.012
1.00
34.74
D

ATOM
7690
O
GLY D
524
147.705
18.446
41.512
1.00
36.14
D

ATOM
7691
N
VAL D
525
148.812
19.351
43.276
1.00
32.26
D

ATOM
7692
CA
VAL D
525
148.563
18.270
44.224
1.00
28.84
D

ATOM
7693
CB
VAL D
525
149.834
17.940
44.980
1.00
28.68
D

ATOM
7694
CG1
VAL D
525
149.536
16.914
46.060
1.00
28.23
D

ATOM
7695
CG2
VAL D
525
150.913
17.467
43.993
1.00
27.71
D

ATOM
7696
C
VAL D
525
147.522
18.613
45.261
1.00
27.86
D

ATOM
7697
O
VAL D
525
147.686
19.580
45.985
1.00
29.26
D

ATOM
7698
N
LEU D
526
146.469
17.807
45.349
1.00
26.79
D

ATOM
7699
CA
LEU D
526
145.421
18.028
46.341
1.00
24.97
D

ATOM
7700
CB
LEU D
526
144.082
17.539
45.796
1.00
24.09
D

ATOM
7701
CG
LEU D
526
143.105
18.496
45.072
1.00
25.53
D

ATOM
7702
CD1
LEU D
526
143.706
19.861
44.714
1.00
21.96
D

ATOM
7703
CD2
LEU D
526
142.600
17.770
43.842
1.00
24.82
D

ATOM
7704
C
LEU D
526
145.771
17.305
47.659
1.00
25.98
D

ATOM
7705
O
LEU D
526
145.389
16.153
47.865
1.00
26.01
D

ATOM
7706
N
ARG D
527
146.507
18.008
48.533
1.00
26.45
D

ATOM
7707
CA
ARG D
527
146.953
17.504
49.839
1.00
27.15
D

ATOM
7708
CB
ARG D
527
148.068
18.359
50.423
1.00
29.53
D

ATOM
7709
CG
ARG D
527
149.136
18.793
49.481
1.00
30.78
D

ATOM
7710
CD
ARG D
527
150.199
17.750
49.353
1.00
29.79
D

ATOM
7711
NE
ARG D
527
151.289
18.254
48.534
1.00
28.82
D

ATOM
7712
CZ
ARG D
527
152.426
17.609
48.341
1.00
28.06
D

ATOM
7713
NH1
ARG D
527
152.621
16.424
48.913
1.00
27.74
D

ATOM
7714
NH2
ARG D
527
153.361
18.156
47.578
1.00
28.96
D

ATOM
7715
C
ARG D
527
145.833
17.583
50.854
1.00
27.48
D

ATOM
7716
O
ARG D
527
145.198
18.625
50.982
1.00
28.10
D

ATOM
7717
N
GLY D
528
145.643
16.511
51.618
1.00
27.13
D

ATOM
7718
CA
GLY D
528
144.593
16.502
52.618
1.00
25.97
D

ATOM
7719
C
GLY D
528
144.378
15.186
53.350
1.00
27.12
D

ATOM
7720
O
GLY D
528
144.222
15.170
54.573
1.00
26.85
D

ATOM
7721
N
HIS D
529
144.349
14.076
52.619
1.00
28.35
D

ATOM
7722
CA
HIS D
529
144.148
12.771
53.242
1.00
28.78
D

ATOM
7723
CB
HIS D
529
143.686
11.747
52.197
1.00
29.36
D

ATOM
7724
CG
HIS D
529
142.272
11.942
51.729
1.00
31.01
D

ATOM
7725
CD2
HIS D
529
141.776
12.234
50.502
1.00
32.50
D

ATOM
7726
ND1
HIS D
529
141.181
11.808
52.562
1.00
29.94
D

ATOM
7727
CE1
HIS D
529
140.074
12.010
51.864
1.00
32.77
D

ATOM
7728
NE2
HIS D
529
140.409
12.270
50.613
1.00
31.73
D

ATOM
7729
C
HIS D
529
145.428
12.293
53.922
1.00
29.06
D

ATOM
7730
O
HIS D
529
146.525
12.716
53.562
1.00
29.97
D

ATOM
7731
N
MSE D
530
145.278
11.412
54.906
1.00
30.41
D

ATOM
7732
CA
MSE D
530
146.411
10.872
55.662
1.00
31.44
D

ATOM
7733
CB
MSE D
530
146.116
10.979
57.163
1.00
36.54
D

ATOM
7734
CG
MSE D
530
145.727
12.383
57.647
1.00
40.77
D

ATOM
7735
SE
MSE D
530
147.225
13.555
57.992
1.00
48.72
D

ATOM
7736
CE
MSE D
530
147.747
12.886
59.726
1.00
44.45
D

ATOM
7737
C
MSE D
530
146.708
9.409
55.286
1.00
30.15
D

ATOM
7738
O
MSE D
530
147.663
8.804
55.770
1.00
31.06
D

ATOM
7739
N
ALA D
531
145.872
8.837
54.433
1.00
27.91
D

ATOM
7740
CA
ALA D
531
146.077
7.470
53.983
1.00
25.52
D

ATOM
7741
CB
ALA D
531
145.322
6.506
54.863
1.00
23.17
D

ATOM
7742
C
ALA D
531
145.634
7.329
52.528
1.00
25.05
D

ATOM
7743
O
ALA D
531
145.166
8.283
51.903
1.00
25.19
D

ATOM
7744
N
SER D
532
145.778
6.126
52.004
1.00
24.01
D

ATOM
7745
CA
SER D
532
145.431
5.834
50.635
1.00
23.62
D

ATOM
7746
CB
SER D
532
145.452
4.332
50.427
1.00
23.66
D

ATOM
7747
OG
SER D
532
145.044
4.009
49.120
1.00
24.72
D

ATOM
7748
C
SER D
532
144.093
6.391
50.161
1.00
24.24
D

ATOM
7749
O
SER D
532
143.059
6.249
50.835
1.00
23.67
D

ATOM
7750
N
VAL D
533
144.131
7.028
48.987
1.00
22.26
D

ATOM
7751
CA
VAL D
533
142.930
7.588
48.383
1.00
21.80
D

ATOM
7752
CB
VAL D
533
143.238
8.790
47.509
1.00
19.37
D

ATOM
7753
CG1
VAL D
533
141.973
9.225
46.786
1.00
19.14
D

ATOM
7754
CG2
VAL D
533
143.757
9.912
48.367
1.00
16.33
D

ATOM
7755
C
VAL D
533
142.311
6.476
47.564
1.00
23.09
D

ATOM
7756
O
VAL D
533
142.740
6.181
46.464
1.00
24.67
D

ATOM
7757
N
ARG D
534
141.281
5.865
48.125
1.00
23.37
D

ATOM
7758
CA
ARG D
534
140.630
4.734
47.514
1.00
21.94
D

ATOM
7759
CB
ARG D
534
139.887
3.966
48.588
1.00
22.94
D

ATOM
7760
CG
ARG D
534
139.334
2.660
48.104
1.00
20.89
D

ATOM
7761
CD
ARG D
534
140.460
1.735
47.688
1.00
20.13
D

ATOM
7762
NE
ARG D
534
139.934
0.404
47.470
1.00
22.05
D

ATOM
7763
CZ
ARG D
534
139.177
0.061
46.435
1.00
21.88
D

ATOM
7764
NH1
ARG D
534
138.859
0.955
45.499
1.00
16.38
D

ATOM
7765
NH2
ARG D
534
138.723
−1.184
46.354
1.00
21.24
D

ATOM
7766
C
ARG D
534
139.687
4.934
46.350
1.00
21.77
D

ATOM
7767
O
ARG D
534
139.630
4.082
45.464
1.00
23.87
D

ATOM
7768
N
THR
0535
138.944
6.029
46.328
1.00
21.46
D

ATOM
7769
CA
THR D
535
137.976
6.186
45.252
1.00
23.21
D

ATOM
7770
CB
THR D
535
136.630
5.607
45.693
1.00
22.72
D

ATOM
7771
OG1
THR D
535
135.615
5.908
44.728
1.00
24.25
D

ATOM
7772
CG2
THR D
535
136.255
6.189
47.038
1.00
21.59
D

ATOM
7773
C
THR D
535
137.785
7.623
44.871
1.00
22.36
D

ATOM
7774
O
THR D
535
138.010
8.494
45.692
1.00
22.27
D

ATOM
7775
N
VAL D
536
137.383
7.869
43.627
1.00
23.47
D

ATOM
7776
CA VAL D
536
137.154
9.240
43.178
1.00
26.56
D

ATOM
7777
CB
VAL D
536
138.340
9.805
42.381
1.00
27.30
D

ATOM
7778
CG1
VAL D
536
138.152
11.303
42.178
1.00
27.76
D

ATOM
7779
CG2
VAL D
536
139.615
9.573
43.126
1.00
29.04
D

ATOM
7780
C
VAL D
536
135.907
9.379
42.330
1.00
26.74
D

ATOM
7781
O
VAL D
536
135.550
8.486
41.558
1.00
28.31
D

ATOM
7782
N
SER D
537
135.248
10.517
42.473
1.00
26.29
D

ATOM
7783
CA
SER D
537
134.019
10.759
41.741
1.00
25.58
D

ATOM
7784
CB
SER D
537
132.832
10.197
42.529
1.00
23.69
D

ATOM
7785
OC
SER D
537
131.605
10.436
41.878
1.00
19.22
D

ATOM
7786
C
SER D
537
133.859
12.252
41.547
1.00
26.69
D

ATOM
7787
O
SER D
537
133.697
13.000
42.517
1.00
27.22
D

ATOM
7788
N
GLY D
538
133.923
12.684
40.294
1.00
26.82
D

ATOM
7789
CA
GLY D
538
133.794
14.096
40.020
1.00
28.64
D

ATOM
7790
C
GLY D
538
133.027
14.446
38.766
1.00
28.83
D

ATOM
7791
O
GLY D
538
132.961
13.666
37.820
1.00
29.17
D

ATOM
7792
N
HIS D
539
132.450
15.645
38.790
1.00
29.15
D

ATOM
7793
CA
HIS D
539
131.679
16.226
37.696
1.00
27.88
D

ATOM
7794
CB
HIS D
539
130.179
16.025
37.911
1.00
27.43
D

ATOM
7795
CG
HIS D
539
129.333
16.567
36.799
1.00
28.11
D

ATOM
7796
CD2
HIS D
539
128.736
17.772
36.637
1.00
30.46
D

ATOM
7797
ND1
HIS D
539
129.046
15.843
35.662
1.00
27.67
D

ATOM
7798
CE1
HIS D
539
128.307
16.577
34.848
1.00
29.05
D

ATOM
7799
NE2
HIS D
539
128.105
17.753
35.415
1.00
30.92
D

ATOM
7800
C
HIS D
539
131.959
17.735
37.697
1.00
29.12
D

ATOM
7801
O
HIS D
539
131.791
18.409
38.728
1.00
28.57
D

ATOM
7802
N
GLY D
540
132.376
18.261
36.546
1.00
28.54
D

ATOM
7803
CA
GLY D
540
132.650
19.682
36.436
1.00
27.08
D

ATOM
7804
C
GLY D
540
133.872
20.122
37.215
1.00
27.09
D

ATOM
7805
O
GLY D
540
134.904
19.454
37.179
1.00
28.54
D

ATOM
7806
N
ASN D
541
133.777
21.245
37.920
1.00
25.16
D

ATOM
7807
CA
ASN D
541
134.924
21.706
38.679
1.00
24.86
D

ATOM
7808
CB
ASN D
541
134.907
23.237
38.816
1.00
26.35
D

ATOM
7809
CG
ASN D
541
133.889
23.726
39.851
1.00
29.47
D

ATOM
7810
OD1
ASN D
541
132.706
23.341
39.803
1.00
29.21
D

ATOM
7811
ND2
ASN D
541
134.341
24.575
40.792
1.00
26.35
D

ATOM
7812
C
ASN D
541
134.915
21.062
40.056
1.00
24.63
D

ATOM
7813
O
ASN D
541
135.803
21.308
40.864
1.00
25.54
D

ATOM
7814
N
ILE D
542
133.921
20.220
40.321
1.00
22.93
D

ATOM
7815
CA
ILE D
542
133.821
19.574
41.629
1.00
22.46
D

ATOM
7816
CB
ILE D
542
132.361
19.724
42.186
1.00
20.91
D

ATOM
7817
CG2
ILE D
542
132.215
18.977
43.497
1.00
22.05
D

ATOM
7818
CG1
ILE D
542
132.001
21.215
42.385
1.00
19.70
D

ATOM
7819
CD1
ILE D
542
132.866
22.016
43.388
1.00
10.85
D

ATOM
7820
C
ILE D
542
134.258
18.085
41.663
1.00
24.27
D

ATOM
7821
O
ILE D
542
133.841
17.258
40.832
1.00
23.68
D

ATOM
7822
N
VAL D
543
135.108
17.738
42.624
1.00
24.95
D

ATOM
7823
CA
VAL D
543
135.565
16.350
42.735
1.00
26.33
D

ATOM
7824
CB
VAL D
543
137.023
16.176
42.199
1.00
28.00
D

ATOM
7825
CG1
VAL D
543
137.492
14.742
42.406
1.00
27.16
D

ATOM
7826
CG2
VAL D
543
137.073
16.515
40.716
1.00
30.18
D

ATOM
7827
C
VAL D
543
135.509
15.864
44.174
1.00
25.02
D

ATOM
7828
O
VAL D
543
135.893
16.601
45.079
1.00
24.45
D

ATOM
7829
N
VAL D
544
135.017
14.639
44.388
1.00
24.93
D

ATOM
7830
CA
VAL D
544
134.939
14.093
45.748
1.00
25.31
D

ATOM
7831
CB
VAL D
544
133.495
13.783
46.197
1.00
24.60
D

ATOM
7832
CG1
VAL D
544
133.507
13.509
47.679
1.00
24.71
D

ATOM
7833
CG2
VAL D
544
132.553
14.940
45.889
1.00
25.25
D

ATOM
7834
C
VAL D
544
135.750
12.814
45.910
1.00
25.25
D

ATOM
7835
O
VAL D
544
135.662
11.903
45.082
1.00
26.67
D

ATOM
7836
N
SER D
545
136.534
12.745
46.985
1.00
24.15
D

ATOM
7837
CA
SER D
545
137.367
11.566
47.236
1.00
24.66
D

ATOM
7838
CB
SER D
545
138.835
11.960
47.213
1.00
22.85
D

ATOM
7839
OG
SER D
545
139.110
12.914
48.221
1.00
26.17
D

ATOM
7840
C
SER D
545
137.105
10.777
48.525
1.00
26.03
D

ATOM
7841
O
SER D
545
136.609
11.315
49.516
1.00
27.76
D

ATOM
7842
N
GLY D
546
137.467
9.497
48.495
1.00
25.26
D

ATOM
7843
CA
GLY D
546
137.292
8.642
49.647
1.00
24.44
D

ATOM
7844
C
GLY D
546
138.637
8.073
50.039
1.00
24.54
D

ATOM
7845
O
GLY D
546
139.318
7.450
49.220
1.00
23.24
D

ATOM
7846
N
SER D
547
139.038
8.282
51.288
1.00
25.20
D

ATOM
7847
CA
SER D
547
140.339
7.773
51.730
1.00
27.40
D

ATOM
7848
CB
SER D
547
141.235
8.897
52.239
1.00
25.06
D

ATOM
7849
OG
SER D
547
142.424
8.333
52.763
1.00
23.13
D

ATOM
7850
C
SER D
547
140.286
6.723
52.816
1.00
28.75
D

ATOM
7851
O
SER D
547
139.260
6.520
53.462
1.00
32.39
D

ATOM
7852
N
TYR D
548
141.411
6.062
53.031
1.00
27.35
D

ATOM
7853
CA
TYR D
548
141.457
5.071
54.078
1.00
24.34
D

ATOM
7854
CB
TYR D
548
142.588
4.085
53.835
1.00
21.23
D

ATOM
7855
CG
TYR D
548
142.185
2.933
52.964
1.00
18.24
D

ATOM
7856
CD1
TYR D
548
140.975
2.940
52.267
1.00
17.37
D

ATOM
7857
CE1
TYR D
548
140.631
1.894
51.426
1.00
15.22
D

ATOM
7858
CD2
TYR D
548
143.030
1.850
52.802
1.00
18.07
D

ATOM
7859
CE2
TYR D
548
142.701
0.796
51.969
1.00
15.33
D

ATOM
7860
CZ
TYR D
548
141.507
0.825
51.283
1.00
17.35
D

ATOM
7861
OH
TYR D
548
141.195
−0.213
50.435
1.00
18.41
D

ATOM
7862
C
TYR D
548
141.637
5.742
55.428
1.00
25.52
D

ATOM
7863
O
TYR D
548
141.897
5.060
56.401
1.00
24.80
D

ATOM
7864
N
ASP D
549
141.517
7.070
55.496
1.00
26.28
D

ATOM
7865
CA
ASP D
549
141.637
7.739
56.789
1.00
26.66
D

ATOM
7866
CB
ASP D
549
142.332
9.114
56.693
1.00
28.11
D

ATOM
7867
CG
ASP D
549
141.761
10.006
55.611
1.00
28.18
D

ATOM
7868
OD1
ASP D
549
140.580
9.822
55.227
1.00
30.65
D

ATOM
7869
OD2
ASP D
549
142.507
10.909
55.167
1.00
25.41
D

ATOM
7870
C
ASP D
549
140.239
7.884
57.363
1.00
26.46
D

ATOM
7871
O
ASP D
549
140.014
8.634
58.311
1.00
26.79
D

ATOM
7872
N
ASN D
550
139.309
7.157
56.742
1.00
26.14
D

ATOM
7873
CA
ASN D
550
137.906
7.115
57.139
1.00
24.53
D

ATOM
7874
CB
ASN D
550
137.825
6.849
58.633
1.00
23.45
D

ATOM
7875
CG
ASN D
550
138.484
5.542
59.012
1.00
23.88
D

ATOM
7876
OD1
ASN D
550
139.126
4.894
58.190
1.00
24.66
D

ATOM
7877
ND2
ASN D
550
138.319
5.143
60.253
1.00
25.10
D

ATOM
7878
C
ASN D
550
137.162
8.374
56.796
1.00
23.51
D

ATOM
7879
O
ASN D
550
136.006
8.534
57.146
1.00
23.99
D

ATOM
7880
N
THR D
551
137.811
9.237
56.038
1.00
24.61
D

ATOM
7881
CA
THR D
551
137.221
10.510
55.706
1.00
24.98
D

ATOM
7882
CB
THR D
551
138.155
11.584
56.208
1.00
25.84
D

ATOM
7883
OG1
THR D
551
137.402
12.640
56.803
1.00
26.76
D

ATOM
7884
CG2
THR D
551
139.015
12.107
55.053
1.00
24.97
D

ATOM
7885
C
THR D
551
136.993
10.725
54.206
1.00
25.92
D

ATOM
7886
O
THR D
551
137.535
9.996
53.376
1.00
24.99
D

ATOM
7887
N
LEU D
552
136.173
11.719
53.868
1.00
26.68
D

ATOM
7888
CA
LEU D
552
135.934
12.079
52.471
1.00
26.79
D

ATOM
7889
CB
LEU D
552
134.508
11.771
52.031
1.00
24.86
D

ATOM
7890
CG
LEU D
552
134.189
10.328
51.665
1.00
23.77
D

ATOM
7891
CD1
LEU D
552
133.215
9.804
52.689
1.00
23.78
D

ATOM
7892
CD2
LEU D
552
133.597
10.237
50.257
1.00
22.54
D

ATOM
7893
C
LEU D
552
136.180
13.572
52.308
1.00
27.51
D

ATOM
7894
O
LEU D
552
135.792
14.366
53.170
1.00
28.40
D

ATOM
7895
N
ILE D
553
136.828
13.955
51.206
1.00
27.13
D

ATOM
7896
CA
ILE D
553
137.102
15.372
50.939
1.00
25.65
D

ATOM
7897
CE
ILE D
553
138.623
15.686
50.957
1.00
24.82
D

ATOM
7898
CG2
ILE D
553
138.854
17.153
50.606
1.00
24.33
D

ATOM
7899
CG1
ILE D
553
139.212
15.444
52.355
1.00
25.26
D

ATOM
7900
CD1
ILE D
553
140.725
15.613
52.413
1.00
24.18
D

ATOM
7901
C
ILE D
553
136.531
15.869
49.606
1.00
25.82
D

ATOM
7902
O
ILE D
553
136.664
15.210
48.561
1.00
24.35
D

ATOM
7903
N
VAL D
554
135.889
17.038
49.672
1.00
24.96
D

ATOM
7904
CA
VAL D
554
135.299
17.704
48.503
1.00
24.79
D

ATOM
7905
CB
VAL D
554
133.964
18.425
48.858
1.00
21.69
D

ATOM
7906
CG1
VAL D
554
133.366
19.041
47.620
1.00
19.43
D

ATOM
7907
CG2
VAL D
554
133.000
17.455
49.480
1.00
21.35
D

ATOM
7908
C
VAL D
554
136.308
18.753
48.016
1.00
26.46
D

ATOM
7909
O
VAL D
554
136.646
19.689
48.746
1.00
26.64
D

ATOM
7910
N
TRP D
555
136.812
18.574
46.797
1.00
27.69
D

ATOM
7911
CA
TRP D
555
137.784
19.500
46.233
1.00
28.09
D

ATOM
7912
CB
TRP D
555
139.026
18.767
45.703
1.00
28.18
D

ATOM
7913
CG
TRP D
555
139.593
17.681
46.576
1.00
29.63
D

ATOM
7914
CD2
TRP D
555
140.695
17.795
47.487
1.00
30.60
D

ATOM
7915
CE2
TRP D
555
140.948
16.505
48.003
1.00
30.79
D

ATOM
7916
CE3
TRP D
555
141.492
18.862
47.915
1.00
30.24
D

ATOM
7917
CD1
TRP D
555
139.228
16.365
46.587
1.00
29.55
D

ATOM
7918
NE1
TRP D
555
140.041
15.652
47.436
1.00
30.90
D

ATOM
7919
CZ2
TRP D
555
141.968
16.253
48.921
1.00
31.50
D

ATOM
7920
CZ3
TRP D
555
142.510
18.608
48.832
1.00
31.00
D

ATOM
7921
CH2
TRP D
555
142.736
17.314
49.323
1.00
31.35
D

ATOM
7922
C
TRP D
555
137.210
20.306
45.075
1.00
27.75
D

ATOM
7923
O
TRP D
555
136.392
19.807
44.297
1.00
26.08
D

ATOM
7924
N
ASP D
556
137.658
21.556
44.981
1.00
29.07
D

ATOM
7925
CA
ASP D
556
137.274
22.463
43.904
1.00
29.82
D

ATOM
7926
CB
ASP D
556
136.917
23.849
44.425
1.00
33.43
D

ATOM
7927
CG
ASP D
556
136.336
24.762
43.335
1.00
36.51
D

ATOM
7928
OD1
ASP D
556
136.913
24.864
42.216
1.00
35.80
D

ATOM
7929
OD2
ASP D
556
135.285
25.388
43.609
1.00
39.49
D

ATOM
7930
C
ASP D
556
138.539
22.591
43.095
1.00
28.83
D

ATOM
7931
O
ASP D
556
139.440
23.337
43.463
1.00
25.39
D

ATOM
7932
N
VAL D
557
138.596
21.858
41.995
1.00
31.59
D

ATOM
7933
CA
VAL D
557
139.756
21.853
41.123
1.00
34.16
D

ATOM
7934
CE
VAL D
557
139.592
20.840
40.007
1.00
34.22
D

ATOM
7935
CG1
VAL D
557
140.777
20.942
39.064
1.00
36.74
D

ATOM
7936
CG2
VAL D
557
139.460
19.444
40.582
1.00
31.24
D

ATOM
7937
C
VAL D
557
140.021
23.183
40.466
1.00
35.74
D

ATOM
7938
O
VAL D
557
141.168
23.535
40.244
1.00
37.94
D

ATOM
7939
N
ALA D
558
138.959
23.906
40.133
1.00
37.02
D

ATOM
7940
CA
ALA D
558
139.107
25.196
39.485
1.00
37.13
D

ATOM
7941
CB
ALA D
558
137.747
25.730
39.065
1.00
39.25
D

ATOM
7942
C
ALA D
558
139.784
26.167
40.430
1.00
36.58
D

ATOM
7943
O
ALA D
558
140.342
27.168
39.997
1.00
37.02
D

ATOM
7944
N
GLN D
559
139.729
25.857
41.722
1.00
37.85
D

ATOM
7945
CA
GLN D
559
140.327
26.688
42.763
1.00
37.56
D

ATOM
7946
CB
GLN D
559
139.248
27.110
43.750
1.00
37.90
D

ATOM
7947
CG
GLN D
559
139.672
28.264
44.624
1.00
43.44
D

ATOM
7948
CD
GLN D
559
138.523
28.874
45.444
1.00
45.28
D

ATOM
7949
OE1
GLN D
559
137.375
28.927
44.987
1.00
46.49
D

ATOM
7950
NE2
GLN D
559
138.839
29.354
46.655
1.00
45.82
D

ATOM
7951
C
GLN D
559
141.419
25.896
43.479
1.00
37.70
D

ATOM
7952
O
GLN D
559
142.131
26.428
44.336
1.00
36.85
D

ATOM
7953
N
MSE D
560
141.535
24.624
43.094
1.00
38.22
D

ATOM
7954
CA
MSE D
560
142.505
23.687
43.645
1.00
37.94
D

ATOM
7955
CB
MSE D
560
143.870
23.912
42.984
1.00
37.36
D

ATOM
7956
CG
MSE D
560
144.681
22.648
42.719
1.00
37.70
D

ATOM
7957
SE
MSE D
560
143.786
21.540
41.377
1.00
39.17
D

ATOM
7958
CE
MSE D
560
143.835
22.738
39.886
1.00
41.26
D

ATOM
7959
C
MSE D
560
142.597
23.865
45.164
1.00
37.81
D

ATOM
7960
O
MSE D
560
143.675
24.035
45.710
1.00
39.53
D

ATOM
7961
N
LYS D
561
141.449
23.844
45.832
1.00
37.74
D

ATOM
7962
CA
LYS D
561
141.384
23.995
47.279
1.00
38.73
D

ATOM
7963
CB
LYS D
561
141.037
25.452
47.638
1.00
39.81
D

ATOM
7964
CG
LYS D
561
142.191
26.428
47.399
0.00
40.07
D

ATOM
7965
CD
LYS D
561
143.372
26.124
48.318
0.00
40.65
D

ATOM
7966
CE
LYS D
561
142.998
26.355
49.774
0.00
41.01
D

ATOM
7967
NZ
LYS D
561
144.024
25.827
50.715
0.00
41.29
D

ATOM
7968
C
LYS D
561
140.356
23.022
47.887
1.00
39.22
D

ATOM
7969
O
LYS D
561
139.419
22.584
47.208
1.00
38.84
D

ATOM
7970
N
CYS D
562
140.556
22.670
49.159
1.00
38.90
D

ATOM
7971
CA
CYS D
562
139.668
21.759
49.885
1.00
38.52
D

ATOM
7972
CB
CYS D
562
140.360
21.270
51.164
1.00
38.67
D

ATOM
7973
SG
CYS D
562
139.309
20.275
52.277
1.00
44.51
D

ATOM
7974
C
CYS D
562
138.402
22.521
50.260
1.00
37.58
D

ATOM
7975
O
CYS D
562
138.494
23.572
50.888
1.00
40.09
D

ATOM
7976
N
LEU D
563
137.223
22.015
49.895
1.00
34.69
D

ATOM
7977
CA
LEU D
563
135.981
22.726
50.232
1.00
31.60
D

ATOM
7978
CB
LEU D
563
134.924
22.550
49.132
1.00
28.39
D

ATOM
7979
CG
LEU D
563
135.214
23.279
47.820
1.00
25.92
D

ATOM
7980
CD1
LEU D
563
133.986
23.317
46.939
1.00
24.65
D

ATOM
7981
CD2
LEU D
563
135.679
24.670
48.139
1.00
23.99
D

ATOM
7982
C
LEU D
563
135.388
22.281
51.552
1.00
30.82
D

ATOM
7983
O
LEU D
563
135.012
23.099
52.388
1.00
29.72
D

ATOM
7984
N
TYR D
564
135.320
20.968
51.723
1.00
31.20
D

ATOM
7985
CA
TYR D
564
134.768
20.358
52.915
1.00
29.79
D

ATOM
7986
CB
TYR D
564
133.276
20.087
52.705
1.00
31.53
D

ATOM
7987
CG
TYR D
564
132.415
21.316
52.480
1.00
35.18
D

ATOM
7988
CD1
TYR D
564
132.216
22.250
53.503
1.00
35.47
D

ATOM
7989
CE1
TYR D
564
131.381
23.356
53.321
1.00
37.11
D

ATOM
7990
CD2
TYR D
564
131.757
21.522
51.257
1.00
35.79
D

ATOM
7991
CE2
TYR D
564
130.918
22.626
51.064
1.00
37.32
D

ATOM
7992
CZ
TYR D
564
130.733
23.539
52.100
1.00
37.56
D

ATOM
7993
OH
TYR D
564
129.901
24.625
51.926
1.00
37.99
D

ATOM
7994
C
TYR D
564
135.464
19.028
53.213
1.00
28.42
D

ATOM
7995
O
TYR D
564
135.998
18.357
52.323
1.00
29.93
D

ATOM
7996
N
ILE D
565
135.448
18.655
54.482
1.00
26.22
D

ATOM
7997
CA
ILE D
565
136.001
17.389
54.916
1.00
24.23
D

ATOM
7998
CB
ILE D
565
137.222
17.574
55.861
1.00
24.90
D

ATOM
7999
CG2
ILE D
565
137.641
16.232
56.471
1.00
22.64
D

ATOM
8000
CG1
ILE D
565
138.389
18.173
55.066
1.00
23.83
D

ATOM
8001
CD1
ILE D
565
139.596
18.476
55.898
1.00
22.10
D

ATOM
8002
C
ILE D
565
134.853
16.708
55.654
1.00
24.14
D

ATOM
8003
O
ILE D
565
134.436
17.123
56.745
1.00
24.92
D

ATOM
8004
N
LEU D
566
134.319
15.674
55.022
1.00
23.68
D

ATOM
8005
CA
LEU D
566
133.209
14.910
55.567
1.00
21.44
D

ATOM
8006
CB
LEU D
566
132.498
14.204
54.433
1.00
18.60
D

ATOM
8007
CG
LEU D
566
132.249
15.108
53.240
1.00
16.04
D

ATOM
8008
CD1
LEU D
566
131.493
14.312
52.195
1.00
18.64
D

ATOM
8009
CD2
LEU D
566
131.471
16.327
53.661
1.00
11.95
D

ATOM
8010
C
LEU D
566
133.725
13.876
56.532
1.00
20.93
D

ATOM
8011
O
LEU D
566
134.448
12.975
56.126
1.00
21.77
D

ATOM
8012
N
SER D
567
133.345
13.980
57.800
1.00
22.31
D

ATOM
8013
CA
SER D
567
133.806
12.995
58.783
1.00
23.94
D

ATOM
8014
CB
SER D
567
134.810
13.630
59.731
1.00
23.34
D

ATOM
8015
OG
SER D
567
135.808
14.311
58.987
1.00
24.18
D

ATOM
8016
C
SER D
567
132.676
12.349
59.568
1.00
24.28
D

ATOM
8017
O
SER D
567
131.586
12.904
59.663
1.00
24.81
D

ATOM
8018
N
GLY D
568
132.950
11.166
60.113
1.00
25.74
D

ATOM
8019
CA
GLY D
568
131.953
10.416
60.858
1.00
25.21
D

ATOM
8020
C
GLY D
568
132.134
8.906
60.681
1.00
26.37
D

ATOM
8021
O
GLY D
568
132.130
8.163
61.664
1.00
27.73
D

ATOM
8022
N
HIS D
569
132.288
8.440
59.437
1.00
25.07
D

ATOM
8023
CA
HIS D
569
132.500
7.007
59.175
1.00
23.33
D

ATOM
8024
CB
HIS D
569
132.949
6.749
57.730
1.00
22.22
D

ATOM
8025
CG
HIS D
569
131.839
6.801
56.725
1.00
21.96
D

ATOM
8026
CD2
HIS D
569
131.594
7.675
55.720
1.00
21.82
D

ATOM
8027
ND1
HIS D
569
130.827
5.865
56.671
1.00
20.28
D

ATOM
8028
CE1
HIS D
569
130.009
6.160
55.676
1.00
20.59
D

ATOM
8029
NE2
HIS D
569
130.452
7.254
55.083
1.00
20.12
D

ATOM
8030
C
HIS D
569
133.590
6.520
60.129
1.00
24.25
D

ATOM
8031
O
HIS D
569
134.625
7.176
60.291
1.00
24.38
D

ATOM
8032
N
THR D
570
133.357
5.371
60.759
1.00
25.24
D

ATOM
8033
CA
THR D
570
134.296
4.806
61.724
1.00
25.54
D

ATOM
8034
CE
THR D
570
133.508
4.097
62.867
1.00
26.19
D

ATOM
8035
OG1
THR D
570
132.385
3.381
62.321
1.00
27.58
D

ATOM
8036
CG2
THR D
570
133.008
5.120
63.869
1.00
23.79
D

ATOM
8037
C
THR D
570
135.355
3.864
61.114
1.00
25.50
D

ATOM
8038
O
THR D
570
136.225
3.349
61.812
1.00
26.67
D

ATOM
8039
N
ASP D
571
135.279
3.628
59.811
1.00
26.22
D

ATOM
8040
CA
ASP D
571
136.284
2.804
59.141
1.00
25.18
D

ATOM
8041
CB
ASP D
571
135.810
1.365
58.999
1.00
26.72
D

ATOM
8042
CG
ASP D
571
136.956
0.386
59.009
1.00
28.41
D

ATOM
8043
OD1
ASP D
571
138.011
0.726
58.447
1.00
30.11
D

ATOM
8044
OD2
ASP D
571
136.818
−0.715
59.575
1.00
29.31
D

ATOM
8045
C
ASP D
571
136.590
3.382
57.759
1.00
24.07
D

ATOM
8046
O
ASP D
571
135.917
4.303
57.281
1.00
22.39
D

ATOM
8047
N
ARG D
572
137.593
2.825
57.101
1.00
23.27
D

ATOM
8048
CA
ARG D
572
137.976
3.314
55.781
1.00
22.84
D

ATOM
8049
CB
ARG D
572
139.153
2.491
55.250
1.00
21.15
D

ATOM
8050
CG
ARG D
572
138.981
1.032
55.408
1.00
19.04
D

ATOM
8051
CD
ARG D
572
140.058
0.268
54.705
1.00
20.64
D

ATOM
8052
NE
ARG D
572
141.341
0.249
55.393
1.00
22.31
D

ATOM
8053
CZ
ARG D
572
142.293
−0.649
55.130
1.00
23.14
D

ATOM
8054
NH1
ARG D
572
142.071
−1.571
54.198
1.00
17.78
D

ATOM
8055
NH2
ARG D
572
143.449
−0.646
55.799
1.00
23.35
D

ATOM
8056
C
ARG D
572
136.820
3.300
54.789
1.00
22.51
D

ATOM
8057
O
ARG D
572
135.914
2.475
54.922
1.00
22.42
D

ATOM
8058
N
ILE D
573
136.825
4.241
53.837
1.00
23.14
D

ATOM
8059
CA
ILE D
573
135.779
4.301
52.809
1.00
24.51
D

ATOM
8060
CB
ILE D
573
135.449
5.739
52.295
1.00
27.12
D

ATOM
8061
CG2
ILE D
573
134.618
5.643
51.025
0.00
26.23
D

ATOM
8062
CG1
ILE D
573
134.652
6.536
53.333
1.00
26.27
D

ATOM
8063
CD1
ILE D
573
135.472
7.060
54.419
1.00
25.64
D

ATOM
8064
C
ILE D
573
136.330
3.577
51.601
1.00
24.11
D

ATOM
8065
O
ILE D
573
137.517
3.724
51.270
1.00
23.80
D

ATOM
8066
N
TYR D
574
135.459
2.830
50.927
1.00
22.78
D

ATOM
8067
CA
TYR D
574
135.849
2.071
49.742
1.00
22.23
D

ATOM
8068
CB
TYR D
574
135.498
0.583
49.951
1.00
21.98
D

ATOM
8069
CG
TYR D
574
136.588
−0.242
50.619
1.00
24.35
D

ATOM
8070
CD1
TYR D
574
137.503
−0.992
49.853
1.00
22.37
D

ATOM
8071
CE1
TYR D
574
138.524
−1.729
50.463
1.00
23.23
D

ATOM
8072
CD2
TYR D
574
136.723
−0.254
52.019
1.00
24.83
D

ATOM
8073
CE2
TYR D
574
137.736
−0.982
52.641
1.00
26.35
D

ATOM
8074
CZ
TYR D
574
138.639
−1.719
51.862
1.00
25.64
D

ATOM
8075
OH
TYR D
574
139.650
−2.423
52.493
1.00
26.87
D

ATOM
8076
C
TYR D
574
135.245
2.570
48.402
1.00
21.18
D

ATOM
8077
O
TYR D
574
135.716
2.188
47.325
1.00
22.28
D

ATOM
8078
N
SER D
575
134.231
3.432
48.464
1.00
19.10
D

ATOM
8079
CA
SER D
575
133.556
3.933
47.258
1.00
18.07
D

ATOM
8080
CB
SER D
575
132.559
2.872
46.756
1.00
18.09
D

ATOM
8081
OG
SER D
575
131.552
3.435
45.926
1.00
17.37
D

ATOM
8082
C
SER D
575
132.814
5.255
47.504
1.00
17.95
D

ATOM
8083
O
SER D
575
132.312
5.515
48.599
1.00
17.19
D

ATOM
8084
N
THR D
576
132.731
6.105
46.498
1.00
17.64
D

ATOM
8085
CA
THR D
576
132.009
7.334
46.737
1.00
19.01
D

ATOM
8086
CB
THR D
576
132.936
8.441
47.285
1.00
17.27
D

ATOM
8087
OG1
THR D
576
132.145
9.575
47.662
1.00
15.53
D

ATOM
8088
CG2
THR D
576
133.968
8.869
46.228
1.00
20.28
D

ATOM
8089
C
THR D
576
131.369
7.808
45.454
1.00
19.84
D

ATOM
8090
O
THR D
576
131.878
7.565
44.358
1.00
20.54
D

ATOM
8091
N
ILE D
577
130.228
8.461
45.571
1.00
18.92
D

ATOM
8092
CA
ILE D
577
129.622
8.959
44.366
1.00
20.24
D

ATOM
8093
CB
ILE D
577
128.395
8.161
43.984
1.00
19.47
D

ATOM
8094
CG2
ILE D
577
127.588
8.938
42.958
1.00
17.51
D

ATOM
8095
CG1
ILE D
577
128.818
6.790
43.456
1.00
19.93
D

ATOM
8096
CD1
ILE D
577
127.641
5.922
43.008
1.00
20.62
D

ATOM
8097
C
ILE D
577
129.232
10.403
44.528
1.00
21.53
D

ATOM
8098
O
ILE D
577
128.603
10.777
45.530
1.00
23.56
D

ATOM
8099
N
TYR D
578
129.615
11.223
43.551
1.00
20.82
D

ATOM
8100
CA
TYR D
578
129.264
12.644
43.593
1.00
21.04
D

ATOM
8101
CB
TYR D
578
130.384
13.509
42.982
1.00
21.65
D

ATOM
8102
CG
TYR D
578
130.022
14.975
42.792
1.00
22.52
D

ATOM
8103
CD1
TYR D
578
129.168
15.625
43.690
1.00
22.16
D

ATOM
8104
CE1
TYR D
578
128.795
16.960
43.506
1.00
21.60
D

ATOM
8105
CD2
TYR D
578
130.510
15.702
41.701
1.00
21.12
D

ATOM
8106
CE2
TYR D
578
130.147
17.038
41.506
1.00
21.36
D

ATOM
8107
CZ
TYR D
578
129.286
17.663
42.410
1.00
21.53
D

ATOM
8108
OH
TYR D
578
128.900
18.977
42.212
1.00
21.71
D

ATOM
8109
C
TYR D
578
127.955
12.883
42.851
1.00
20.91
D

ATOM
8110
O
TYR D
578
127.939
12.885
41.633
1.00
21.83
D

ATOM
8111
N
ASP D
579
126.866
13.094
43.596
1.00
22.68
D

ATOM
8112
CA
ASP D
579
125.534
13.342
43.017
1.00
24.76
D

ATOM
8113
CB
ASP D
579
124.440
13.037
44.054
1.00
25.04
D

ATOM
8114
CG
ASP D
579
123.029
12.930
43.443
1.00
27.17
D

ATOM
8115
OD1
ASP D
579
122.790
13.506
42.363
1.00
26.43
D

ATOM
8116
OD2
ASP D
579
122.144
12.271
44.061
1.00
27.38
D

ATOM
8117
C
ASP D
579
125.435
14.808
42.583
1.00
26.38
D

ATOM
8118
O
ASP D
579
124.715
15.590
43.200
1.00
25.82
D

ATOM
8119
N
HIS D
580
126.148
15.172
41.513
1.00
28.39
D

ATOM
8120
CA
HIS D
580
126.145
16.555
41.028
1.00
31.78
D

ATOM
8121
CB
HIS D
580
127.029
16.692
39.794
1.00
33.03
D

ATOM
8122
CG
HIS D
580
126.607
15.830
38.654
1.00
37.41
D

ATOM
8123
CD2
HIS D
580
125.611
15.973
37.750
1.00
38.10
D

ATOM
8124
ND1
HIS D
580
127.244
14.648
38.342
1.00
39.09
D

ATOM
8125
CE1
HIS D
580
126.660
14.102
37.292
1.00
38.85
D

ATOM
8126
NE2
HIS D
580
125.666
14.885
36.913
1.00
39.22
D

ATOM
8127
C
HIS D
580
124.745
17.113
40.723
1.00
33.01
D

ATOM
8128
O
HIS D
580
124.484
18.313
40.890
1.00
34.71
D

ATOM
8129
N
GLU D
581
123.836
16.251
40.292
1.00
33.24
D

ATOM
8130
CA
GLU D
581
122.486
16.693
39.995
1.00
32.71
D

ATOM
8131
CB
GLU D
581
121.700
15.544
39.375
1.00
35.03
D

ATOM
8132
CG
GLU D
581
120.463
15.978
38.652
1.00
39.07
D

ATOM
8133
CD
GLU D
581
119.702
14.818
38.092
1.00
41.55
D

ATOM
8134
OE1
GLU D
581
120.332
14.026
37.350
1.00
43.80
D

ATOM
8135
OE2
GLU D
581
118.485
14.712
38.394
1.00
41.52
D

ATOM
8136
C
GLU D
581
121.788
17.202
41.266
1.00
31.80
D

ATOM
8137
O
GLU D
581
121.244
18.306
41.260
1.00
31.97
D

ATOM
8138
N
ARG D
582
121.808
16.414
42.348
1.00
29.57
D

ATOM
8139
CA
ARG D
582
121.177
16.825
43.616
1.00
29.36
D

ATOM
8140
CB
ARG D
582
120.622
15.607
44.390
1.00
26.09
D

ATOM
8141
CG
ARG D
582
119.558
14.822
43.650
1.00
22.04
D

ATOM
8142
CD
ARG D
582
118.850
13.766
44.496
1.00
20.11
D

ATOM
8143
NE
ARG D
582
118.024
12.908
43.636
1.00
19.38
D

ATOM
8144
CZ
ARG D
582
118.506
12.137
42.658
1.00
20.74
D

ATOM
8145
NH1
ARG D
582
119.808
12.105
42.415
1.00
22.11
D

ATOM
8146
NH2
ARG D
582
117.695
11.398
41.908
1.00
19.51
D

ATOM
8147
C
ARG D
582
122.160
17.598
44.531
1.00
31.40
D

ATOM
8148
O
ARG D
582
121.796
18.063
45.622
1.00
29.69
D

ATOM
8149
N
LYS D
583
123.401
17.747
44.074
1.00
33.89
D

ATOM
8150
CA
LYS D
583
124.433
18.436
44.849
1.00
35.05
D

ATOM
8151
CB
LYS D
583
124.069
19.912
45.068
1.00
38.08
D

ATOM
8152
CG
LYS D
583
124.348
20.830
43.882
1.00
40.35
D

ATOM
8153
CD
LYS D
583
125.842
20.963
43.611
1.00
42.80
D

ATOM
8154
CE
LYS D
583
126.103
21.734
42.310
1.00
42.80
D

ATOM
8155
NZ
LYS D
583
125.618
23.153
42.366
1.00
43.25
D

ATOM
8156
C
LYS D
583
124.627
17.755
46.202
1.00
34.05
D

ATOM
8157
O
LYS D
583
124.524
18.401
47.241
1.00
35.02
D

ATOM
8158
N
ARG D
584
124.898
16.449
46.172
1.00
33.23
D

ATOM
8159
CA
ARG D
584
125.128
15.634
47.370
1.00
31.46
D

ATOM
8160
CB
ARG D
584
123.854
14.861
47.768
1.00
29.44
D

ATOM
8161
CG
ARG D
584
122.595
15.702
47.938
1.00
30.45
D

ATOM
8162
CD
ARG D
584
121.369
14.815
48.175
1.00
30.86
D

ATOM
8163
NE
ARG D
584
120.098
15.542
48.113
1.00
31.46
D

ATOM
8164
CZ
ARG D
584
118.904
14.965
48.229
1.00
32.25
D

ATOM
8165
NH1
ARG D
584
118.820
13.653
48.414
1.00
29.52
D

ATOM
8166
NH2
ARG D
584
117.793
15.697
48.156
1.00
30.64
D

ATOM
8167
C
ARG D
584
126.247
14.622
47.065
1.00
31.14
D

ATOM
8168
O
ARG D
584
126.668
14.466
45.916
1.00
30.87
D

ATOM
8169
N
CYS D
585
126.732
13.961
48.111
1.00
30.50
D

ATOM
8170
CA
CYS D
585
127.762
12.937
48.009
1.00
29.49
D

ATOM
8171
CB
CYS D
585
129.086
13.427
48.598
1.00
32.51
D

ATOM
8172
SG
CYS D
585
130.268
12.081
49.098
1.00
36.50
D

ATOM
8173
C
CYS D
585
127.298
11.719
48.809
1.00
28.24
D

ATOM
8174
O
CYS D
585
126.814
11.850
49.943
1.00
28.12
D

ATOM
8175
N
ILE D
586
127.434
10.546
48.193
1.00
25.25
D

ATOM
8176
CA
ILE D
586
127.094
9.266
48.806
1.00
22.27
D

ATOM
8177
CB
ILE D
586
126.394
8.304
47.804
1.00
21.75
D

ATOM
8178
CG2
ILE D
586
126.164
6.967
48.464
1.00
18.50
D

ATOM
8179
CG1
ILE D
586
125.070
8.900
47.279
1.00
21.75
D

ATOM
8180
CD1
ILE D
586
125.217
9.902
46.122
1.00
19.83
D

ATOM
8181
C
ILE D
586
128.460
8.670
49.123
1.00
22.41
D

ATOM
8182
O
ILE D
586
129.400
8.875
48.359
1.00
24.24
D

ATOM
8183
N
SER D
587
128.586
7.955
50.236
1.00
21.77
D

ATOM
8184
CA
SER D
587
129.856
7.319
50.595
1.00
19.65
D

ATOM
8185
CB
SER D
587
130.644
8.217
51.548
1.00
18.81
D

ATOM
8186
OC
SER D
587
129.942
8.436
52.758
1.00
17.09
D

ATOM
8187
C
SER D
587
129.579
5.968
51.255
1.00
19.73
D

ATOM
8188
O
SER D
587
128.676
5.867
52.082
1.00
20.77
D

ATOM
8189
N
ALA D
588
130.334
4.936
50.874
1.00
19.14
D

ATOM
8190
CA
ALA D
588
130.169
3.595
51.436
1.00
18.83
D

ATOM
8191
CB
ALA D
588
129.817
2.586
50.342
1.00
17.57
D

ATOM
8192
C
ALA D
588
131.483
3.220
52.105
1.00
18.48
D

ATOM
8193
O
ALA D
588
132.549
3.280
51.482
1.00
18.12
D

ATOM
8194
N
SER D
589
131.387
2.829
53.375
1.00
19.29
D

ATOM
8195
CA
SER D
589
132.546
2.500
54.224
1.00
20.33
D

ATOM
8196
CB
SER D
589
132.552
3.487
55.416
1.00
21.31
D

ATOM
8197
OG
SER D
589
133.427
3.106
56.474
1.00
19.54
D

ATOM
8198
C
SER D
589
132.633
1.058
54.749
1.00
20.03
D

ATOM
8199
O
SER D
589
131.638
0.322
54.743
1.00
20.59
D

ATOM
8200
N
MSE D
590
133.837
0.677
55.189
1.00
22.56
D

ATOM
8201
CA
MSE D
590
134.089
−0.644
55.760
1.00
25.48
D

ATOM
8202
CB
MSE D
590
135.578
−0.827
56.067
1.00
28.07
D

ATOM
8203
CG
MSE D
590
135.932
−2.225
56.531
1.00
30.40
D

ATOM
8204
SE
MSE D
590
137.843
−2.501
56.672
1.00
39.74
D

ATOM
8205
CE
MSE D
590
138.123
−3.610
55.120
1.00
33.01
D

ATOM
8206
C
MSE D
590
133.271
−0.777
57.053
1.00
26.26
D

ATOM
8207
O
MSE D
590
133.045
−1.883
57.540
1.00
27.96
D

ATOM
8208
N
ASP D
591
132.806
0.352
57.587
1.00
24.74
D

ATOM
8209
CA
ASP D
591
131.999
0.333
58.790
1.00
24.47
D

ATOM
8210
CB
ASP D
591
131.931
1.722
59.447
1.00
25.09
D

ATOM
8211
CG
ASP D
591
131.115
2.730
58.635
1.00
26.02
D

ATOM
8212
OD1
ASP D
591
130.116
2.338
57.987
1.00
23.16
D

ATOM
8213
OD2
ASP D
591
131.461
3.930
58.668
1.00
28.61
D

ATOM
8214
C
ASP D
591
130.575
−0.167
58.535
1.00
25.63
D

ATOM
8215
O
ASP D
591
129.731
−0.111
59.435
1.00
27.48
D

ATOM
8216
N
THR D
592
130.280
−0.612
57.315
1.00
24.13
D

ATOM
8217
CA
THR D
592
128.953
−1.144
57.027
1.00
23.60
D

ATOM
8218
CB
THR D
592
128.479
−2.010
58.217
1.00
23.93
D

ATOM
8219
OG1
THR D
592
129.276
−3.197
58.290
1.00
24.58
D

ATOM
8220
CG2
THR D
592
127.032
−2.388
58.071
1.00
25.94
D

ATOM
8221
C
THR D
592
127.858
−0.117
56.694
1.00
23.10
D

ATOM
8222
O
THR D
592
126.814
−0.466
56.131
1.00
23.01
D

ATOM
8223
N
THR D
593
128.086
1.146
57.020
1.00
21.17
D

ATOM
8224
CA
THR D
593
127.084
2.164
56.743
1.00
20.07
D

ATOM
8225
CB
THR D
593
127.097
3.238
57.829
1.00
19.96
D

ATOM
8226
OG1
THR D
593
128.317
3.981
57.736
1.00
20.19
D

ATOM
8227
CG2
THR D
593
127.012
2.601
59.205
1.00
20.49
D

ATOM
8228
C
THR D
593
127.303
2.861
55.400
1.00
20.54
D

ATOM
8229
O
THR D
593
128.282
2.602
54.705
1.00
20.50
D

ATOM
8230
N
ILE D
594
126.360
3.728
55.039
1.00
19.85
D

ATOM
8231
CA
ILE D
594
126.422
4.520
53.823
1.00
18.48
D

ATOM
8232
CB
ILE D
594
125.423
4.012
52.749
1.00
17.96
D

ATOM
8233
CG2
ILE D
594
125.476
4.931
51.512
1.00
16.27
D

ATOM
8234
CG1
ILE D
594
125.763
2.564
52.352
1.00
17.94
D

ATOM
8235
CD1
ILE D
594
124.874
1.976
51.244
1.00
13.75
D

ATOM
8236
C
ILE D
594
126.013
5.920
54.297
1.00
20.05
D

ATOM
8237
O
ILE D
594
125.125
6.060
55.147
1.00
19.44
D

ATOM
8238
N
ARG D
595
126.661
6.961
53.787
1.00
21.73
D

ATOM
8239
CA
ARG D
595
126.294
8.304
54.229
1.00
24.25
D

ATOM
8240
CE
ARG D
595
127.380
8.898
55.133
1.00
26.38
D

ATOM
8241
CG
ARG D
595
127.485
8.261
56.508
1.00
27.19
D

ATOM
8242
CD
ARG D
595
128.489
9.003
57.373
1.00
29.27
D

ATOM
8243
NE
ARG D
595
128.184
8.848
58.797
1.00
33.82
D

ATOM
8244
CZ
ARG D
595
128.465
9.753
59.732
1.00
34.00
D

ATOM
8245
NH1
ARG D
595
129.068
10.889
59.398
1.00
34.40
D

ATOM
8246
NH2
ARG D
595
128.125
9.528
60.998
1.00
33.02
D

ATOM
8247
C
ARG D
595
125.999
9.282
53.108
1.00
24.90
D

ATOM
8248
O
ARG D
595
126.702
9.329
52.102
1.00
25.43
D

ATOM
8249
N
ILE D
596
124.939
10.056
53.294
1.00
25.81
D

ATOM
8250
CA
ILE D
596
124.540
11.056
52.319
1.00
27.39
D

ATOM
8251
CB
ILE D
596
123.000
11.093
52.138
1.00
27.40
D

ATOM
8252
CG2
ILE D
596
122.646
11.950
50.935
1.00
27.77
D

ATOM
8253
CG1
ILE D
596
122.459
9.681
51.891
1.00
27.13
D

ATOM
8254
CD1
ILE D
596
122.953
9.062
50.590
1.00
26.64
D

ATOM
8255
C
ILE D
596
125.013
12.392
52.870
1.00
28.16
D

ATOM
8256
O
ILE D
596
124.637
12.787
53.976
1.00
28.61
D

ATOM
8257
N
TRP D
597
125.862
13.078
52.118
1.00
28.67
D

ATOM
8258
CA
TRP D
597
126.368
14.368
52.568
1.00
28.04
D

ATOM
8259
CE
TRP D
597
127.893
14.391
52.515
1.00
29.61
D

ATOM
8260
CG
TRP D
597
128.562
13.228
53.155
1.00
28.57
D

ATOM
8261
CD2
TRP D
597
129.116
13.186
54.470
1.00
27.43
D

ATOM
8262
CE2
TRP D
597
129.707
11.918
54.634
1.00
27.37
D

ATOM
8263
CE3
TRP D
597
129.172
14.103
55.529
1.00
27.46
D

ATOM
8264
CD1
TRP D
597
128.822
12.016
52.589
1.00
29.00
D

ATOM
8265
NE1
TRP D
597
129.516
11.221
53.469
1.00
27.32
D

ATOM
8266
CZ2
TRP D
597
130.349
11.541
55.817
1.00
27.76
D

ATOM
8267
CZ3
TRP D
597
129.810
13.729
56.703
1.00
27.02
D

ATOM
8268
CR2
TRP D
597
130.389
12.457
56.838
1.00
27.58
D

ATOM
8269
C
TRP D
597
125.838
15.486
51.684
1.00
27.75
D

ATOM
8270
O
TRP D
597
125.729
15.326
50.472
1.00
27.73
D

ATOM
8271
N
ASP D
598
125.519
16.624
52.284
1.00
28.69
D

ATOM
8272
CA
ASP D
598
125.012
17.773
51.527
1.00
29.82
D

ATOM
8273
CB
ASP D
598
123.966
18.511
52.381
1.00
29.96
D

ATOM
8274
CG
ASP D
598
123.483
19.816
51.749
1.00
30.01
D

ATOM
8275
OD1
ASP D
598
123.889
20.118
50.601
1.00
29.40
D

ATOM
8276
OD2
ASP D
598
122.700
20.537
52.417
1.00
28.15
D

ATOM
8277
C
ASP D
598
126.197
18.694
51.177
1.00
28.75
D

ATOM
8278
O
ASP D
598
126.880
19.192
52.067
1.00
26.58
D

ATOM
8279
N
LEU D
599
126.442
18.912
49.884
1.00
29.62
D

ATOM
8280
CA
LEU D
599
127.567
19.753
49.466
1.00
32.72
D

ATOM
8281
CB
LEU D
599
128.148
19.244
48.141
1.00
30.82
D

ATOM
8282
CG
LEU D
599
128.646
17.780
48.141
1.00
31.03
D

ATOM
8283
CD1
LEU D
599
129.360
17.472
46.822
1.00
29.75
D

ATOM
8284
CD2
LEU D
599
129.579
17.529
49.309
1.00
28.77
D

ATOM
8285
C
LEU D
599
127.238
21.246
49.383
1.00
35.04
D

ATOM
8286
O
LEU D
599
127.899
22.009
48.686
1.00
34.05
D

ATOM
8287
N
GLU D
600
126.228
21.651
50.145
1.00
39.89
D

ATOM
8288
CA
GLU D
600
125.793
23.041
50.205
1.00
42.71
D

ATOM
8289
CB
GLU D
600
124.279
23.118
49.998
1.00
43.83
D

ATOM
8290
CG
GLU D
600
123.818
22.578
48.659
1.00
49.15
D

ATOM
8291
CD
GLU D
600
124.057
23.565
47.524
1.00
52.47
D

ATOM
8292
OE1
GLU D
600
123.836
23.205
46.340
1.00
54.37
D

ATOM
8293
OE2
GLU D
600
124.462
24.710
47.820
1.00
53.81
D

ATOM
8294
C
GLU D
600
126.154
23.614
51.581
1.00
43.08
D

ATOM
8295
O
GLU D
600
125.956
24.799
51.847
1.00
44.92
D

ATOM
8296
N
ASN D
605
126.681
22.769
52.461
1.00
42.60
D

ATOM
8297
CA
ASN D
605
127.049
23.217
53.798
1.00
41.25
D

ATOM
8298
CB
ASN D
605
125.787
23.392
54.640
1.00
41.21
D

ATOM
8299
CG
ASN D
605
125.003
22.105
54.794
1.00
42.82
D

ATOM
8300
OD1
ASN D
605
124.753
21.383
53.830
1.00
41.44
D

ATOM
8301
ND2
ASN D
605
124.599
21.819
56.024
1.00
44.97
D

ATOM
8302
C
ASN D
605
128.006
22.222
54.440
1.00
40.16
D

ATOM
8303
O
ASN D
605
128.507
22.442
55.544
1.00
39.89
D

ATOM
8304
N
GLY D
606
128.259
21.135
53.712
1.00
39.38
D

ATOM
8305
CA
GLY D
606
129.165
20.091
54.156
1.00
36.83
D

ATOM
8306
C
GLY D
606
128.629
19.279
55.311
1.00
35.89
D

ATOM
8307
O
GLY D
606
129.336
18.446
55.865
1.00
35.05
D

ATOM
8308
N
GLU D
607
127.378
19.523
55.675
1.00
35.04
D

ATOM
8309
CA
GLU D
607
126.771
18.814
56.779
1.00
35.34
D

ATOM
8310
CB
GLU D
607
125.624
19.635
57.350
1.00
38.59
D

ATOM
8311
CG
GLU D
607
126.032
20.652
58.401
1.00
44.13
D

ATOM
8312
CD
GLU D
607
124.828
21.150
59.183
1.00
49.69
D

ATOM
8313
OE1
GLU D
607
124.093
20.289
59.749
1.00
51.01
D

ATOM
8314
OE2
GLU D
607
124.608
22.394
59.227
1.00
52.33
D

ATOM
8315
C
GLU D
607
126.271
17.415
56.411
1.00
33.71
D

ATOM
8316
O
GLU D
607
125.991
17.144
55.247
1.00
33.25
D

ATOM
8317
N
LEU D
608
126.175
16.521
57.397
1.00
31.85
D

ATOM
8318
CA
LEU D
608
125.686
15.175
57.125
1.00
30.51
D

ATOM
8319
CE
LEU D
608
126.052
14.216
58.253
1.00
27.96
D

ATOM
8320
CG
LEU D
608
125.557
12.778
58.041
1.00
28.56
D

ATOM
8321
CD1
LEU D
608
126.456
12.051
57.046
1.00
24.69
D

ATOM
8322
CD2
LEU D
608
125.531
12.032
59.394
1.00
28.82
D

ATOM
8323
C
LEU D
608
124.169
15.253
56.971
1.00
30.57
D

ATOM
8324
O
LEU D
608
123.532
16.124
57.573
1.00
31.18
D

ATOM
8325
N
MEE D
625
123.605
14.363
56.150
1.00
29.87
D

ATOM
8326
CA
MSE D
625
122.153
14.303
55.888
1.00
30.31
D

ATOM
8327
CB
MSE D
625
121.846
14.367
54.381
1.00
31.08
D

ATOM
8328
CG
MSE D
625
122.016
15.737
53.754
1.00
33.02
D

ATOM
8329
SE
MSE D
625
121.598
15.802
51.862
1.00
38.72
D

ATOM
8330
CE
MSE D
625
119.705
15.354
51.962
1.00
32.55
D

ATOM
8331
C
MSE D
625
121.523
13.022
56.410
1.00
27.88
D

ATOM
8332
O
MSE D
625
120.538
13.032
57.145
1.00
28.06
D

ATOM
8333
N
TYR D
626
122.073
11.901
55.993
1.00
25.99
D

ATOM
8334
CA
TYR D
626
121.505
10.670
56.444
1.00
24.99
D

ATOM
8335
CB
TYR D
626
120.453
10.176
55.461
1.00
25.25
D

ATOM
8336
CG
TYR D
626
119.434
11.186
54.999
1.00
24.62
D

ATOM
8337
CD1
TYR D
626
118.409
11.612
55.842
1.00
21.86
D

ATOM
8338
CE1
TYR D
626
117.391
12.424
55.363
1.00
23.49
D

ATOM
8339
CD2
TYR D
626
119.426
11.615
53.669
1.00
24.69
D

ATOM
8340
CE2
TYR D
626
118.421
12.421
53.179
1.00
24.51
D

ATOM
8341
CZ
TYR D
626
117.396
12.820
54.023
1.00
24.72
D

ATOM
8342
OH
TYR D
626
116.346
13.555
53.502
1.00
25.76
D

ATOM
8343
C
TYR D
626
122.555
9.597
56.565
1.00
23.88
D

ATOM
8344
O
TYR D
626
123.605
9.652
55.923
1.00
23.89
D

ATOM
8345
N
THR D
627
122.255
8.616
57.406
1.00
23.42
D

ATOM
8346
CA
THR D
627
123.122
7.472
57.564
1.00
20.62
D

ATOM
8347
CE
THR D
627
123.589
7.271
58.987
1.00
19.43
D

ATOM
8348
OG1
THR D
627
124.268
8.447
59.440
1.00
20.14
D

ATOM
8349
CG2
THR D
627
124.535
6.066
59.050
1.00
17.31
D

ATOM
8350
C
THR D
627
122.235
6.308
57.191
1.00
19.41
D

ATOM
8351
O
THR D
627
121.244
6.050
57.859
1.00
18.63
D

ATOM
8352
N
LEU D
628
122.577
5.640
56.095
1.00
19.47
D

ATOM
8353
CA
LEU D
628
121.821
4.485
55.626
1.00
19.11
D

ATOM
8354
CE
LEU D
628
121.755
4.469
54.108
1.00
17.80
D

ATOM
8355
CG
LEU D
628
121.117
5.669
53.396
1.00
16.59
D

ATOM
8356
CD1
LEU D
628
121.092
5.364
51.890
1.00
16.34
D

ATOM
8357
CD2
LEU D
628
119.712
5.929
53.916
1.00
13.86
D

ATOM
8358
C
LEU D
628
122.523
3.227
56.111
1.00
19.57
D

ATOM
8359
O
LEU D
628
123.674
2.966
55.744
1.00
20.61
D

ATOM
8360
N
GLN D
629
121.817
2.456
56.936
1.00
19.21
D

ATOM
8361
CA
GLN D
629
122.331
1.216
57.512
1.00
19.59
D

ATOM
8362
CE
GLN D
629
122.142
1.262
59.031
1.00
18.99
D

ATOM
8363
CG
GLN D
629
122.640
0.047
59.795
1.00
19.95
D

ATOM
8364
CD
GLN D
629
124.155
−0.088
59.756
1.00
21.73
D

ATOM
8365
OE1
GLN D
629
124.709
−0.697
58.841
1.00
21.66
D

ATOM
8366
NE2
GLN D
629
124.834
0.492
60.751
1.00
21.48
D

ATOM
8367
C
GLN D
629
121.565
0.034
56.922
1.00
19.26
D

ATOM
8368
O
GLN D
629
120.435
−0.224
57.313
1.00
22.24
D

ATOM
8369
N
GLY D
630
122.178
−0.689
55.993
1.00
18.64
D

ATOM
8370
CA
GLY D
630
121.480
−1.802
55.386
1.00
19.70
D

ATOM
8371
C
GLY D
630
122.361
−2.917
54.860
1.00
21.44
D

ATOM
8372
O
GLY D
630
122.068
−3.533
53.844
1.00
22.81
D

ATOM
8373
N
HIS D
631
123.459
−3.179
55.544
1.00
22.39
D

ATOM
8374
CA
HIS D
631
124.368
−4.236
55.143
1.00
23.12
D

ATOM
8375
CB
HIS D
631
125.425
−3.720
54.169
1.00
26.25
D

ATOM
8376
CG
HIS D
631
124.856
−3.144
52.915
1.00
28.65
D

ATOM
8377
CD2
HIS D
631
124.544
−1.870
52.586
1.00
28.78
D

ATOM
8378
ND1
HIS D
631
124.504
−3.920
51.833
1.00
29.43
D

ATOM
8379
CE1
HIS D
631
124.002
−3.146
50.887
1.00
28.34
D

ATOM
8380
NE2
HIS D
631
124.015
−1.898
51.319
1.00
28.49
D

ATOM
8381
C
HIS D
631
125.030
−4.618
56.440
1.00
22.81
D

ATOM
8382
O
HIS D
631
125.008
−3.860
57.402
1.00
25.35
D

ATOM
8383
N
THR D
632
125.661
−5.774
56.455
1.00
21.41
D

ATOM
8384
CA
THR D
632
126.288
−6.261
57.663
1.00
20.28
D

ATOM
8385
CB
THR D
632
125.646
−7.591
58.047
1.00
18.49
D

ATOM
8386
OG1
THR D
632
125.767
−8.524
56.957
1.00
18.30
D

ATOM
8387
CG2
THR D
632
124.173
−7.371
58.349
1.00
13.99
D

ATOM
8388
C
THR D
632
127.771
−6.466
57.509
1.00
20.33
D

ATOM
8389
O
THR D
632
128.427
−6.983
58.405
1.00
22.76
D

ATOM
8390
N
ALA D
633
128.291
−6.053
56.367
1.00
19.78
D

ATOM
8391
CA
ALA D
633
129.695
−6.224
56.061
1.00
18.83
D

ATOM
8392
CB
ALA D
633
129.877
−7.469
55.239
1.00
17.26
D

ATOM
8393
C
ALA D
633
130.169
−5.029
55.282
1.00
19.55
D

ATOM
8394
O
ALA D
633
129.385
−4.126
54.991
1.00
19.68
D

ATOM
8395
N
LEU D
634
131.455
−5.024
54.951
1.00
20.72
D

ATOM
8396
CA
LEU D
634
132.051
−3.944
54.175
1.00
20.81
D

ATOM
8397
CB
LEU D
634
133.478
−4.347
53.790
1.00
21.47
D

ATOM
8398
CG
LEU D
634
134.286
−3.752
52.639
1.00
22.59
D

ATOM
8399
CD1
LEU D
634
133.982
−4.534
51.395
1.00
25.22
D

ATOM
8400
CD2
LEU D
634
133.968
−2.263
52.448
1.00
26.73
D

ATOM
8401
C
LEU D
634
131.211
−3.634
52.940
1.00
21.70
D

ATOM
8402
O
LEU D
634
130.889
−4.523
52.138
1.00
22.37
D

ATOM
8403
N
VAL D
635
130.822
−2.371
52.807
1.00
21.89
D

ATOM
8404
CA
VAL D
635
130.038
−1.957
51.646
1.00
23.38
D

ATOM
8405
CB
VAL D
635
128.929
−0.951
52.019
1.00
23.26
D

ATOM
8406
CG1
VAL D
635
128.136
−0.574
50.771
1.00
25.04
D

ATOM
8407
CG2
VAL D
635
128.008
−1.545
53.048
1.00
21.55
D

ATOM
8408
C
VAL D
635
131.019
−1.303
50.670
1.00
24.61
D

ATOM
8409
O
VAL D
635
131.455
−0.164
50.878
1.00
22.67
D

ATOM
8410
N
GLY D
636
131.352
−2.036
49.607
1.00
25.64
D

ATOM
8411
CA
GLY D
636
132.320
−1.552
48.641
1.00
26.53
D

ATOM
8412
C
GLY D
636
131.874
−1.151
47.254
1.00
26.66
D

ATOM
8413
O
GLY D
636
132.687
−0.595
46.509
1.00
27.11
D

ATOM
8414
N
LEU D
637
130.612
−1.418
46.906
1.00
26.43
D

ATOM
8415
CA
LEU D
637
130.077
−1.089
45.582
1.00
24.26
D

ATOM
8416
CB
LEU D
637
129.705
−2.367
44.825
1.00
22.49
D

ATOM
8417
CG
LEU D
637
130.896
−3.277
44.542
1.00
21.34
D

ATOM
8418
CD1
LEU D
637
132.028
−2.399
44.003
1.00
18.59
D

ATOM
8419
CD2
LEU D
637
131.352
−3.982
45.809
1.00
23.19
D

ATOM
8420
C
LEU D
637
128.868
−0.163
45.606
1.00
25.18
D

ATOM
8421
O
LEU D
637
127.843
−0.503
46.182
1.00
26.31
D

ATOM
8422
N
LEU D
638
129.009
1.004
44.970
1.00
26.27
D

ATOM
8423
CA
LEU D
638
127.959
2.021
44.854
1.00
25.24
D

ATOM
8424
CB
LEU D
638
128.335
3.308
45.579
1.00
25.17
D

ATOM
8425
CG
LEU D
638
128.217
3.292
47.092
1.00
26.38
D

ATOM
8426
CD1
LEU D
638
128.445
4.708
47.617
1.00
25.29
D

ATOM
8427
CD2
LEU D
638
126.827
2.778
47.484
1.00
23.90
D

ATOM
8428
C
LEU D
638
127.772
2.372
43.396
1.00
25.47
D

ATOM
8429
O
LEU D
638
128.746
2.427
42.638
1.00
24.74
D

ATOM
8430
N
ARG D
639
126.515
2.639
43.029
1.00
25.82
D

ATOM
8431
CA
ARG D
639
126.101
2.999
41.661
1.00
24.67
D

ATOM
8432
CB
ARG D
639
125.735
1.733
40.875
1.00
24.23
D

ATOM
8433
CG
ARG D
639
126.472
1.524
39.569
1.00
24.13
D

ATOM
8434
CD
ARG D
639
127.923
1.341
39.843
1.00
24.24
D

ATOM
8435
NE
ARG D
639
128.539
0.275
39.061
1.00
25.29
D

ATOM
8436
CZ
ARG D
639
129.345
0.488
38.027
1.00
26.83
D

ATOM
8437
NH1
ARG D
639
129.609
1.735
37.658
1.00
22.95
D

ATOM
8438
NH2
ARG D
639
129.909
−0.538
37.387
1.00
27.61
D

ATOM
8439
C
ARG D
639
124.857
3.877
41.777
1.00
24.76
D

ATOM
8440
O
ARG D
639
123.942
3.540
42.519
1.00
24.70
D

ATOM
8441
N
LEU D
640
124.821
4.991
41.046
1.00
25.49
D

ATOM
8442
CA
LEU D
640
123.668
5.908
41.066
1.00
23.58
D

ATOM
8443
CB
LEU D
640
124.142
7.354
41.250
1.00
20.68
D

ATOM
8444
CG
LEU D
640
123.301
8.220
42.178
1.00
21.27
D

ATOM
8445
CD1
LEU D
640
123.483
9.698
41.849
1.00
19.99
D

ATOM
8446
CD2
LEU D
640
121.854
7.834
42.058
1.00
21.23
D

ATOM
8447
C
LEU D
640
122.888
5.800
39.753
1.00
23.09
D

ATOM
8448
O
LEU D
640
123.464
5.886
38.677
1.00
25.33
D

ATOM
8449
N
SER D
641
121.582
5.598
39.846
1.00
22.47
D

ATOM
8450
CA
SER D
641
120.741
5.498
38.668
1.00
21.80
D

ATOM
8451
CB
SER D
641
119.920
4.212
38.713
1.00
23.05
D

ATOM
8452
OC
SER D
641
118.628
4.399
38.170
1.00
26.20
D

ATOM
8453
C
SER D
641
119.837
6.712
38.706
1.00
22.79
D

ATOM
8454
O
SER D
641
119.697
7.344
39.743
1.00
21.44
D

ATOM
8455
N
ASP D
642
119.206
7.052
37.596
1.00
25.87
D

ATOM
8456
CA
ASP D
642
118.361
8.230
37.631
1.00
29.02
D

ATOM
8457
CB
ASP D
642
117.753
8.507
36.258
1.00
32.11
D

ATOM
8458
CG
ASP D
642
117.066
9.854
36.206
1.00
35.97
D

ATOM
8459
OD1
ASP D
642
117.782
10.877
36.333
1.00
38.30
D

ATOM
8460
OD2
ASP D
642
115.817
9.904
36.059
1.00
37.81
D

ATOM
8461
C
ASP D
642
117.247
8.077
38.655
1.00
28.71
D

ATOM
8462
O
ASP D
642
116.649
9.055
39.098
1.00
28.83
D

ATOM
8463
N
LYS D
643
116.975
6.847
39.047
1.00
29.24
D

ATOM
8464
CA
LYS D
643
115.903
6.626
39.989
1.00
29.96
D

ATOM
8465
CB
LYS D
643
114.760
5.934
39.241
1.00
31.36
D

ATOM
8466
CG
LYS D
643
113.626
5.382
40.076
1.00
36.57
D

ATOM
8467
CD
LYS D
643
112.491
4.792
39.183
1.00
38.95
D

ATOM
8468
CE
LYS D
643
111.899
5.844
38.222
1.00
40.27
D

ATOM
8469
NZ
LYS D
643
110.719
5.330
37.453
1.00
40.99
D

ATOM
8470
C
LYS D
643
116.325
5.831
41.222
1.00
29.02
D

ATOM
8471
O
LYS D
643
115.628
5.832
42.234
1.00
29.30
D

ATOM
8472
N
PHE D
644
117.483
5.187
41.160
1.00
27.45
D

ATOM
8473
CA
PHE D
644
117.924
4.370
42.276
1.00
25.90
D

ATOM
8474
CB
PHE D
644
117.822
2.889
41.918
1.00
23.62
D

ATOM
8475
CG
PHE D
644
116.428
2.416
41.670
1.00
22.94
D

ATOM
8476
CD1
PHE D
644
116.097
1.784
40.480
1.00
23.53
D

ATOM
8477
CD2
PHE D
644
115.448
2.567
42.632
1.00
21.03
D

ATOM
8478
CE1
PHE D
644
114.807
1.309
40.266
1.00
21.81
D

ATOM
8479
CE2
PHE D
644
114.164
2.094
42.416
1.00
18.29
D

ATOM
8480
CZ
PHE D
644
113.847
1.467
41.237
1.00
17.27
D

ATOM
8481
C
PHE D
644
119.337
4.618
42.735
1.00
26.43
D

ATOM
8482
O
PHE D
644
120.164
5.136
41.989
1.00
25.68
D

ATOM
8483
N
LEU D
645
119.589
4.238
43.988
1.00
27.14
D

ATOM
8484
CA
LEU D
645
120.911
4.318
44.608
1.00
26.31
D

ATOM
8485
CB
LEU D
645
120.914
5.234
45.828
1.00
27.08
D

ATOM
8486
CG
LEU D
645
122.217
5.194
46.640
1.00
27.94
D

ATOM
8487
CD1
LEU D
645
123.290
5.975
45.918
1.00
29.78
D

ATOM
8488
CD2
LEU D
645
121.994
5.766
48.028
1.00
27.68
D

ATOM
8489
C
LEU D
645
121.152
2.890
45.059
1.00
24.69
D

ATOM
8490
O
LEU D
645
120.758
2.514
46.146
1.00
26.35
D

ATOM
8491
N
VAL D
646
121.786
2.100
44.206
1.00
23.16
D

ATOM
8492
CA
VAL D
646
122.056
0.706
44.499
1.00
21.12
D

ATOM
8493
CB
VAL D
646
122.116
−0.101
43.212
1.00
20.50
D

ATOM
8494
CG1
VAL D
646
122.047
−1.583
43.514
1.00
21.04
D

ATOM
8495
CG2
VAL D
646
120.997
0.334
42.283
1.00
20.61
D

ATOM
8496
C
VAL D
646
123.384
0.523
45.211
1.00
20.80
D

ATOM
8497
O
VAL D
646
124.375
1.159
44.857
1.00
21.52
D

ATOM
8498
N
SER D
647
123.408
−0.356
46.208
1.00
20.76
D

ATOM
8499
CA
SER D
647
124.637
−0.643
46.936
1.00
19.72
D

ATOM
8500
CB
SER D
647
124.706
0.166
48.231
1.00
19.38
D

ATOM
8501
OG
SER D
647
123.594
−0.100
49.071
1.00
20.83
D

ATOM
8502
C
SER D
647
124.723
−2.140
47.249
1.00
19.78
D

ATOM
8503
O
SER D
647
123.694
−2.816
47.373
1.00
18.23
D

ATOM
8504
N
ALA D
648
125.950
−2.654
47.344
1.00
18.94
D

ATOM
8505
CA
ALA D
648
126.175
−4.060
47.646
1.00
19.09
D

ATOM
8506
CB
ALA D
648
126.463
−4.850
46.377
1.00
15.72
D

ATOM
8507
C
ALA D
648
127.337
−4.180
48.618
1.00
20.74
D

ATOM
8508
O
ALA D
648
128.279
−3.399
48.547
1.00
22.53
D

ATOM
8509
N
ALA D
649
127.253
−5.148
49.533
1.00
21.16
D

ATOM
8510
CA
ALA D
649
128.301
−5.372
50.514
1.00
20.36
D

ATOM
8511
CB
ALA D
649
127.774
−5.097
51.911
1.00
23.59
D

ATOM
8512
C
ALA D
649
128.912
−6.772
50.457
1.00
20.64
D

ATOM
8513
O
ALA D
649
128.453
−7.663
49.723
1.00
19.52
D

ATOM
8514
N
ALA D
650
129.951
−6.944
51.271
1.00
18.79
D

ATOM
8515
CA
ALA D
650
130.703
−8.192
51.372
1.00
17.83
D

ATOM
8516
CB
ALA D
650
131.839
−8.012
52.334
1.00
17.25
D

ATOM
8517
C
ALA D
650
129.889
−9.409
51.786
1.00
17.38
D

ATOM
8518
O
ALA D
650
130.337
−10.545
51.626
1.00
16.75
D

ATOM
8519
N
ASP D
651
128.699
−9.190
52.329
1.00
18.32
D

ATOM
8520
CA
ASP D
651
127.880
−10.323
52.748
1.00
19.29
D

ATOM
8521
CB
ASP D
651
126.982
−9.930
53.920
1.00
21.96
D

ATOM
8522
CG
ASP D
651
126.027
−8.804
53.568
1.00
26.40
D

ATOM
8523
OD1
ASP D
651
125.508
−8.816
52.425
1.00
28.33
D

ATOM
8524
OD2
ASP D
651
125.781
−7.924
54.436
1.00
25.72
D

ATOM
8525
C
ASP D
651
127.026
−10.856
51.609
1.00
19.07
D

ATOM
8526
O
ASP D
651
126.244
−11.789
51.787
1.00
20.37
D

ATOM
8527
N
GLY D
652
127.164
−10.256
50.437
1.00
19.11
D

ATOM
8528
CA
GLY D
652
126.370
−10.711
49.315
1.00
18.71
D

ATOM
8529
C
GLY D
652
125.024
−10.018
49.213
1.00
18.78
D

ATOM
8530
O
GLY D
652
124.142
−10.475
48.479
1.00
17.99
D

ATOM
8531
N
SER D
653
124.841
−8.926
49.950
1.00
20.24
D

ATOM
8532
CA
SER D
653
123.575
−8.198
49.864
1.00
21.58
D

ATOM
8533
CB
SER D
653
123.133
−7.678
51.236
1.00
21.54
D

ATOM
8534
OG
SER D
653
124.037
−6.731
51.772
1.00
22.98
D

ATOM
8535
C
SER D
653
123.665
−7.033
48.881
1.00
22.14
D

ATOM
8536
O
SER D
653
124.742
−6.510
48.598
1.00
21.79
D

ATOM
8537
N
ILE D
654
122.515
−6.652
48.350
1.00
23.25
D

ATOM
8538
CA
ILE D
654
122.418
−5.554
47.409
1.00
25.80
D

ATOM
8539
CB
ILE D
654
122.165
−6.055
45.982
1.00
26.21
D

ATOM
8540
CG2
ILE D
654
122.297
−4.918
45.003
1.00
26.27
D

ATOM
8541
CG1
ILE D
654
123.154
−7.158
45.616
1.00
28.16
D

ATOM
8542
CD1
ILE D
654
122.870
−7.785
44.254
1.00
28.37
D

ATOM
8543
C
ILE D
654
121.197
−4.754
47.836
1.00
26.75
D

ATOM
8544
O
ILE D
654
120.122
−5.323
48.064
1.00
27.01
D

ATOM
8545
N
ARG D
655
121.346
−3.443
47.951
1.00
27.07
D

ATOM
8546
CA
ARG D
655
120.216
−2.626
48.356
1.00
27.67
D

ATOM
8547
CB
ARG D
655
120.467
−2.029
49.737
1.00
28.04
D

ATOM
8548
CG
ARG D
655
120.592
−3.062
50.832
1.00
29.00
D

ATOM
8549
CD
ARG D
655
119.901
−2.605
52.103
1.00
31.71
D

ATOM
8550
NE
ARG D
655
118.574
−3.199
52.240
1.00
33.84
D

ATOM
8551
CZ
ARG D
655
118.328
−4.314
52.914
1.00
33.80
D

ATOM
8552
NH1
ARG D
655
119.314
−4.960
53.527
1.00
33.02
D

ATOM
8553
NH2
ARG D
655
117.094
−4.787
52.953
1.00
36.00
D

ATOM
8554
C
ARG D
655
119.903
−1.524
47.358
1.00
27.31
D

ATOM
8555
O
ARG D
655
120.797
−0.985
46.706
1.00
26.04
D

ATOM
8556
N
GLY D
656
118.620
−1.203
47.237
1.00
27.56
D

ATOM
8557
CA
GLY D
656
118.206
−0.164
46.315
1.00
28.15
D

ATOM
8558
C
GLY D
656
117.482
0.916
47.087
1.00
27.66
D

ATOM
8559
O
GLY D
656
116.514
0.621
47.775
1.00
28.41
D

ATOM
8560
N
TRP D
657
117.944
2.158
46.996
1.00
27.78
D

ATOM
8561
CA
TRP D
657
117.299
3.256
47.715
1.00
28.29
D

ATOM
8562
CB
TRP D
657
118.296
3.913
48.699
1.00
26.47
D

ATOM
8563
CG
TRP D
657
119.251
2.947
49.419
1.00
24.99
D

ATOM
8564
CD2
TRP D
657
119.136
2.448
50.768
1.00
23.38
D

ATOM
8565
CE2
TRP D
657
120.215
1.554
50.972
1.00
22.65
D

ATOM
8566
CE3
TRP D
657
118.226
2.664
51.818
1.00
22.66
D

ATOM
8567
CD1
TRP D
657
120.369
2.352
48.891
1.00
22.06
D

ATOM
8568
NE1
TRP D
657
120.947
1.520
49.815
1.00
21.92
D

ATOM
8569
CZ2
TRP D
657
120.407
0.875
52.180
1.00
20.78
D

ATOM
8570
CZ3
TRP D
657
118.423
1.979
53.026
1.00
22.09
D

ATOM
8571
CR2
TRP D
657
119.505
1.098
53.187
1.00
22.26
D

ATOM
8572
C
TRP D
657
116.777
4.313
46.705
1.00
29.51
D

ATOM
8573
O
TRP D
657
117.304
4.422
45.592
1.00
29.88
D

ATOM
8574
N
ASP D
658
115.744
5.076
47.075
1.00
29.21
D

ATOM
8575
CA
ASP D
658
115.223
6.104
46.174
1.00
29.96
D

ATOM
8576
CB
ASP D
658
113.977
6.790
46.757
1.00
28.48
D

ATOM
8577
CG
ASP D
658
113.460
7.923
45.868
1.00
28.43
D

ATOM
8578
OD1
ASP D
658
112.888
7.650
44.793
1.00
28.91
D

ATOM
8579
OD2
ASP D
658
113.628
9.101
46.236
1.00
27.59
D

ATOM
8580
C
ASP D
658
116.354
7.113
46.026
1.00
31.50
D

ATOM
8581
O
ASP D
658
116.978
7.503
47.017
1.00
32.96
D

ATOM
8582
N
ALA D
659
116.621
7.526
44.791
1.00
31.88
D

ATOM
8583
CA
ALA D
659
117.694
8.468
44.499
1.00
32.44
D

ATOM
8584
CB
ALA D
659
117.811
8.649
43.010
1.00
32.07
D

ATOM
8585
C
ALA D
659
117.541
9.829
45.162
1.00
33.56
D

ATOM
8586
O
ALA D
659
118.463
10.634
45.141
1.00
34.05
D

ATOM
8587
N
ASN D
660
116.387
10.091
45.761
1.00
36.44
D

ATOM
8588
CA
ASN D
660
116.155
11.379
46.400
1.00
37.59
D

ATOM
8589
CB
ASN D
660
115.061
12.130
45.645
1.00
39.91
D

ATOM
8590
CG
ASN D
660
114.872
13.542
46.149
1.00
43.39
D

ATOM
8591
OD1
ASN D
660
114.382
13.764
47.264
1.00
44.43
D

ATOM
8592
ND2
ASN D
660
115.274
14.515
45.334
1.00
45.95
D

ATOM
8593
C
ASN D
660
115.791
11.248
47.876
1.00
36.76
D

ATOM
8594
O
ASN D
660
116.233
12.050
48.689
1.00
38.43
D

ATOM
8595
N
ASP D
661
114.991
10.239
48.214
1.00
35.26
D

ATOM
8596
CA
ASP D
661
114.566
9.984
49.592
1.00
33.16
D

ATOM
8597
CB
ASP D
661
113.165
9.393
49.620
1.00
34.45
D

ATOM
8598
CG
ASP D
661
112.144
10.331
49.104
1.00
38.11
D

ATOM
8599
OD1
ASP D
661
112.280
11.540
49.419
1.00
40.95
D

ATOM
8600
OD2
ASP D
661
111.200
9.876
48.409
1.00
39.95
D

ATOM
8601
C
ASP D
661
115.458
8.980
50.292
1.00
31.13
D

ATOM
8602
O
ASP D
661
115.569
9.004
51.505
1.00
31.79
D

ATOM
8603
N
TYR D
662
116.023
8.062
49.517
1.00
26.92
D

ATOM
8604
CA
TYR D
662
116.885
7.016
50.027
1.00
25.03
D

ATOM
8605
CB
TYR D
662
118.028
7.615
50.876
1.00
23.52
D

ATOM
8606
CG
TYR D
662
118.839
8.622
50.075
1.00
24.99
D

ATOM
8607
CD1
TYR D
662
119.614
8.201
48.999
1.00
23.45
D

ATOM
8608
CE1
TYR D
662
120.257
9.099
48.181
1.00
23.80
D

ATOM
8609
CD2
TYR D
662
118.739
9.996
50.317
1.00
23.15
D

ATOM
8610
CE2
TYR D
662
119.384
10.914
49.497
1.00
24.08
D

ATOM
8611
CZ
TYR D
662
120.143
10.459
48.424
1.00
25.80
D

ATOM
8612
OH
TYR D
662
120.770
11.367
47.581
1.00
25.60
D

ATOM
8613
C
TYR D
662
116.090
5.979
50.808
1.00
24.80
D

ATOM
8614
O
TYR D
662
116.663
5.210
51.590
1.00
25.89
D

ATOM
8615
N
SER D
663
114.777
5.946
50.575
1.00
21.66
D

ATOM
8616
CA
SER D
663
113.886
4.981
51.228
1.00
21.07
D

ATOM
8617
CB
SER D
663
112.432
5.460
51.165
1.00
20.52
D

ATOM
8618
OG
SER D
663
111.987
5.642
49.838
1.00
19.13
D

ATOM
8619
C
SER D
663
113.996
3.610
50.564
1.00
20.63
D

ATOM
8620
O
SER D
663
114.182
3.530
49.357
1.00
20.77
D

ATOM
8621
N
ARG D
664
113.901
2.537
51.353
1.00
21.12
D

ATOM
8622
CA
ARG D
664
114.022
1.180
50.819
1.00
20.22
D

ATOM
8623
CB
ARG D
664
113.564
0.125
51.849
1.00
22.66
D

ATOM
8624
CG
ARG D
664
114.575
−0.302
52.980
1.00
25.13
D

ATOM
8625
CD
ARG D
664
114.860
0.821
53.987
1.00
27.71
D

ATOM
8626
NE
ARG D
664
115.573
0.440
55.219
1.00
29.68
D

ATOM
8627
CZ
ARG D
664
116.626
−0.373
55.291
1.00
31.69
D

ATOM
8628
NH1
ARG D
664
117.114
−0.935
54.200
1.00
34.72
D

ATOM
8629
NH2
ARG D
664
117.226
−0.597
56.456
1.00
30.46
D

ATOM
8630
C
ARG D
664
113.196
1.037
49.552
1.00
18.91
D

ATOM
8631
O
ARG D
664
112.013
1.393
49.525
1.00
19.59
D

ATOM
8632
N
LYS D
665
113.833
0.544
48.496
1.00
17.43
D

ATOM
8633
CA
LYS D
665
113.144
0.320
47.238
1.00
16.40
D

ATOM
8634
CB
LYS D
665
113.729
1.204
46.148
1.00
14.06
D

ATOM
8635
CG
LYS D
665
113.132
2.582
46.190
1.00
13.78
D

ATOM
8636
CD
LYS D
665
111.661
2.434
45.960
1.00
14.84
D

ATOM
8637
CE
LYS D
665
110.875
3.713
46.115
1.00
14.42
D

ATOM
8638
NZ
LYS D
665
109.447
3.311
45.873
1.00
17.38
D

ATOM
8639
C
LYS D
665
113.202
−1.149
46.868
1.00
15.50
D

ATOM
8640
O
LYS D
665
112.216
−1.709
46.413
1.00
18.21
D

ATOM
8641
N
PHE D
666
114.352
−1.778
47.069
1.00
15.94
D

ATOM
8642
CA
PHE D
666
114.492
−3.207
46.810
1.00
16.38
D

ATOM
8643
CB
PHE D
666
114.453
−3.531
45.291
1.00
12.81
D

ATOM
8644
CG
PHE D
666
115.613
−2.980
44.477
1.00
13.72
D

ATOM
8645
CD1
PHE D
666
116.914
−3.428
44.676
1.00
14.32
D

ATOM
8646
CD2
PHE D
666
115.386
−2.051
43.460
1.00
16.32
D

ATOM
8647
CE1
PHE D
666
117.963
−2.962
43.881
1.00
12.43
D

ATOM
8648
CE2
PEE D
666
116.433
−1.579
42.659
1.00
14.70
D

ATOM
8649
CZ
PHE D
666
117.716
−2.039
42.873
1.00
15.14
D

ATOM
8650
C
PHE D
666
115.764
−3.767
47.482
1.00
17.88
D

ATOM
8651
O
PHE D
666
116.618
−3.017
47.971
1.00
18.62
D

ATOM
8652
N
SER D
667
115.869
−5.088
47.533
1.00
19.07
D

ATOM
8653
CA
SER D
667
117.021
−5.736
48.127
1.00
20.16
D

ATOM
8654
CE
SER D
667
116.971
−5.646
49.661
1.00
21.18
D

ATOM
8655
OG
SER D
667
115.778
−6.192
50.188
1.00
21.36
D

ATOM
8656
C
SER D
667
117.089
−7.188
47.675
1.00
19.78
D

ATOM
8657
O
SER D
667
116.093
−7.907
47.662
1.00
18.38
D

ATOM
8658
N
TYR D
668
118.280
−7.596
47.274
1.00
20.33
D

ATOM
8659
CA
TYR D
668
118.499
−8.946
46.807
1.00
21.29
D

ATOM
8660
CE
TYR D
668
118.756
−8.936
45.293
1.00
21.18
D

ATOM
8661
CG
TYR D
668
117.595
−8.369
44.470
1.00
20.55
D

ATOM
8662
CD1
TYR D
668
116.495
−9.171
44.114
1.00
18.14
D

ATOM
8663
CE1
TYR D
668
115.423
−8.647
43.403
1.00
18.24
D

ATOM
8664
CD2
TYR D
668
117.584
−7.020
44.084
1.00
18.54
D

ATOM
8665
CE2
TYR D
668
116.522
−6.484
43.379
1.00
18.25
D

ATOM
8666
CZ
TYR D
668
115.437
−7.293
43.044
1.00
19.79
D

ATOM
8667
OH
TYR D
668
114.343
−6.732
42.410
1.00
18.58
D

ATOM
8668
C
TYR D
668
119.709
−9.445
47.560
1.00
21.68
D

ATOM
8669
O
TYR D
668
120.525
−8.650
48.008
1.00
24.28
D

ATOM
8670
N
HIS D
669
119.802
−10.757
47.718
1.00
23.30
D

ATOM
8671
CA
HIS D
669
120.904
−11.398
48.413
1.00
23.12
D

ATOM
8672
CB
HIS D
669
120.433
−11.895
49.771
1.00
23.33
D

ATOM
8673
CG
HIS D
669
121.343
−11.528
50.897
1.00
26.89
D

ATOM
8674
CD2
HIS D
669
121.187
−10.654
51.921
1.00
25.28
D

ATOM
8675
ND1
HIS D
669
122.608
−12.060
51.034
1.00
26.65
D

ATOM
8676
CE1
HIS D
669
123.193
−11.529
52.093
1.00
27.24
D

ATOM
8677
NE2
HIS D
669
122.353
−10.673
52.649
1.00
27.53
D

ATOM
8678
C
HIS D
669
121.274
−12.587
47.535
1.00
24.51
D

ATOM
8679
O
HIS D
669
120.399
−13.313
47.036
1.00
24.95
D

ATOM
8680
N
HIS D
670
122.569
−12.779
47.335
1.00
24.99
D

ATOM
8681
CA
HIS D
670
123.045
−13.882
46.521
1.00
25.59
D

ATOM
8682
CE
HIS D
670
124.501
−13.642
46.121
1.00
26.37
D

ATOM
8683
CG
HIS D
670
124.666
−12.905
44.823
1.00
29.01
D

ATOM
8684
CD2
HIS D
670
125.637
−12.971
43.881
1.00
27.78
D

ATOM
8685
ND1
HIS D
670
123.779
−11.942
44.387
1.00
28.88
D

ATOM
8686
CE1
HIS D
670
124.199
−11.450
43.236
1.00
26.47
D

ATOM
8687
NE2
HIS D
670
125.324
−12.055
42.907
1.00
25.99
D

ATOM
8688
C
HIS D
670
122.918
−15.176
47.326
1.00
27.14
D

ATOM
8689
O
HIS D
670
123.583
−15.346
48.362
1.00
25.08
D

ATOM
8690
N
THR D
671
122.059
−16.080
46.840
1.00
28.13
D

ATOM
8691
CA
THR D
671
121.796
−17.381
47.473
1.00
27.79
D

ATOM
8692
CB
THR D
671
121.180
−18.369
46.454
1.00
26.12
D

ATOM
8693
OG1
THR D
671
119.789
−18.069
46.289
1.00
23.95
D

ATOM
8694
CG2
THR D
671
121.312
−19.791
46.930
1.00
26.83
D

ATOM
8695
C
THR D
671
122.992
−18.034
48.162
1.00
29.31
D

ATOM
8696
O
THR D
671
122.854
−18.547
49.271
1.00
29.25
D

ATOM
8697
N
ASN D
672
124.156
−18.025
47.516
1.00
31.23
D

ATOM
8698
CA
ASN D
672
125.354
−18.627
48.116
1.00
33.42
D

ATOM
8699
CB
ASN D
672
126.498
−18.738
47.089
1.00
35.89
D

ATOM
8700
CG
ASN D
672
126.323
−19.911
46.105
1.00
40.95
D

ATOM
8701
OD1
ASN D
672
125.241
−20.116
45.535
1.00
42.75
D

ATOM
8702
ND2
ASN D
672
127.406
−20.672
45.887
1.00
42.55
D

ATOM
8703
C
ASN D
672
125.861
−17.813
49.317
1.00
33.48
D

ATOM
8704
O
ASN D
672
126.666
−18.302
50.105
1.00
35.72
D

ATOM
8705
N
LEU D
673
125.405
−16.574
49.455
1.00
31.40
D

ATOM
8706
CA
LEU D
673
125.864
−15.722
50.549
1.00
30.75
D

ATOM
8707
CB
LEU D
673
125.631
−16.410
51.901
1.00
30.83
D

ATOM
8708
CG
LEU D
673
124.165
−16.514
52.344
1.00
31.99
D

ATOM
8709
CD1
LEU D
673
124.059
−17.284
53.649
1.00
32.25
D

ATOM
8710
CD2
LEU D
673
123.580
−15.115
52.510
1.00
33.43
D

ATOM
8711
C
LEU D
673
127.346
−15.337
50.420
1.00
28.49
D

ATOM
8712
O
LEU D
673
128.045
−15.214
51.429
1.00
29.31
D

ATOM
8713
N
SER D
674
127.812
−15.145
49.185
1.00
24.89
D

ATOM
8714
CA
SER D
674
129.201
−14.771
48.911
1.00
23.72
D

ATOM
8715
CB
SER D
674
129.764
−15.608
47.764
1.00
23.54
D

ATOM
8716
OG
SER D
674
128.969
−15.454
46.598
1.00
27.66
D

ATOM
8717
C
SER D
674
129.289
−13.287
48.546
1.00
22.55
D

ATOM
8718
O
SER D
674
128.336
−12.721
48.035
1.00
22.93
D

ATOM
8719
N
ALA D
675
130.431
−12.657
48.796
1.00
21.17
D

ATOM
8720
CA
ALA D
675
130.580
−11.240
48.498
1.00
20.35
D

ATOM
8721
CB
ALA D
675
132.002
−10.779
48.814
1.00
16.29
D

ATOM
8722
C
ALA D
675
130.215
−10.836
47.075
1.00
20.97
D

ATOM
8723
O
ALA D
675
130.528
−11.527
46.095
1.00
22.46
D

ATOM
8724
N
ILE D
676
129.538
−9.703
46.972
1.00
21.38
D

ATOM
8725
CA
ILE D
676
129.180
−9.194
45.667
1.00
23.44
D

ATOM
8726
CB
ILE D
676
128.051
−8.132
45.734
1.00
24.56
D

ATOM
8727
CG2
ILE D
676
127.897
−7.484
44.377
1.00
23.13
D

ATOM
8728
CG1
ILE D
676
126.727
−8.776
46.197
1.00
25.69
D

ATOM
8729
CD1
ILE D
676
126.316
−10.018
45.386
1.00
25.28
D

ATOM
8730
C
ILE D
676
130.470
−8.526
45.202
1.00
23.09
D

ATOM
8731
O
ILE D
676
130.971
−7.613
45.853
1.00
23.97
D

ATOM
8732
N
THR D
677
131.012
−9.000
44.091
1.00
21.72
D

ATOM
8733
CA
THR D
677
132.250
−8.474
43.554
1.00
21.86
D

ATOM
8734
CB
THR D
677
133.096
−9.589
42.896
1.00
25.37
D

ATOM
8735
OG1
THR D
677
133.515
−10.542
43.884
1.00
25.75
D

ATOM
8736
CG2
THR D
677
134.328
−8.977
42.219
1.00
27.86
D

ATOM
8737
C
THR D
677
132.001
−7.420
42.488
1.00
20.83
D

ATOM
8738
O
THR D
677
132.880
−6.605
42.208
1.00
17.53
D

ATOM
8739
N
THR D
678
130.818
−7.457
41.876
1.00
20.52
D

ATOM
8740
CA
THR D
678
130.492
−6.512
40.821
1.00
19.25
D

ATOM
8741
CB
THR D
678
131.294
−6.864
39.512
1.00
20.24
D

ATOM
8742
OG1
THR D
678
131.093
−5.842
38.533
1.00
19.49
D

ATOM
8743
CG2
THR D
678
130.834
−8.193
38.927
1.00
17.27
D

ATOM
8744
C
THR D
678
129.001
−6.490
40.495
1.00
18.40
D

ATOM
8745
O
THR D
678
128.308
−7.497
40.627
1.00
17.73
D

ATOM
8746
N
PHE D
679
128.521
−5.336
40.044
1.00
19.50
D

ATOM
8747
CA
PHE D
679
127.119
−5.179
39.653
1.00
20.10
D

ATOM
8748
CB
PHE D
679
126.212
−5.151
40.896
1.00
19.62
D

ATOM
8749
CG
PHE D
679
126.072
−3.794
41.546
1.00
20.58
D

ATOM
8750
CD1
PHE D
679
125.187
−2.838
41.036
1.00
19.81
D

ATOM
8751
CD2
PHE D
679
126.786
−3.493
42.708
1.00
22.11
D

ATOM
8752
CE1
PHE D
679
125.008
−1.595
41.679
1.00
19.56
D

ATOM
8753
CE2
PHE D
679
126.622
−2.255
43.369
1.00
21.42
D

ATOM
8754
CZ
PHE D
679
125.730
−1.305
42.855
1.00
20.49
D

ATOM
8755
C
PHE D
679
126.967
−3.908
38.836
1.00
18.56
D

ATOM
8756
O
PHE D
679
127.824
−3.040
38.902
1.00
18.64
D

ATOM
8757
N
TYR D
680
125.900
−3.826
38.038
1.00
18.73
D

ATOM
8758
CA
TYR D
680
125.610
−2.640
37.216
1.00
18.62
D

ATOM
8759
CB
TYR D
680
126.140
−2.818
35.776
1.00
19.64
D

ATOM
8760
CG
TYR D
680
126.416
−1.498
35.070
1.00
21.94
D

ATOM
8761
CD1
TYR D
680
127.503
−0.704
35.447
1.00
21.42
D

ATOM
8762
CE1
TYR D
680
127.691
0.578
34.917
1.00
21.58
D

ATOM
8763
CD2
TYR D
680
125.525
−0.982
34.123
1.00
21.80
D

ATOM
8764
CE2
TYR D
680
125.702
0.304
33.585
1.00
21.45
D

ATOM
8765
CZ
TYR D
680
126.780
1.083
33.992
1.00
21.61
D

ATOM
8766
OH
TYR D
680
126.891
2.384
33.541
1.00
21.38
D

ATOM
8767
C
TYR D
680
124.087
−2.429
37.194
1.00
18.89
D

ATOM
8768
O
TYR D
680
123.326
−3.394
37.244
1.00
21.29
D

ATOM
8769
N
VAL D
681
123.635
−1.182
37.148
1.00
18.55
D

ATOM
8770
CA
VAL D
681
122.202
−0.952
37.112
1.00
20.06
D

ATOM
8771
CB
VAL D
681
121.588
−0.612
38.502
1.00
19.46
D

ATOM
8772
CG1
VAL D
681
121.748
−1.770
39.427
1.00
23.82
D

ATOM
8773
CG2
VAL D
681
122.219
0.634
39.080
1.00
18.66
D

ATOM
8774
C
VAL D
681
121.699
0.134
36.196
1.00
21.12
D

ATOM
8775
O
VAL D
681
122.429
1.030
35.748
1.00
19.50
D

ATOM
8776
N
SER D
682
120.404
0.039
35.956
1.00
22.21
D

ATOM
8777
CA
SER D
682
119.698
0.991
35.147
1.00
21.87
D

ATOM
8778
CB
SER D
682
119.633
0.520
33.703
1.00
20.44
D

ATOM
8779
OG
SER D
682
118.589
−0.410
33.525
1.00
21.95
D

ATOM
8780
C
SER D
682
118.331
0.950
35.783
1.00
23.11
D

ATOM
8781
O
SER D
682
118.048
0.053
36.582
1.00
22.65
D

ATOM
8782
N
ASP D
683
117.483
1.910
35.457
1.00
23.07
D

ATOM
8783
CA
ASP D
683
116.165
1.901
36.050
1.00
23.72
D

ATOM
8784
CB
ASP D
683
115.359
3.107
35.591
1.00
26.85
D

ATOM
8785
CG
ASP D
683
115.822
4.384
36.224
1.00
30.20
D

ATOM
8786
OD1
ASP D
683
116.151
4.341
37.431
1.00
35.54
D

ATOM
8787
OD2
ASP D
683
115.840
5.421
35.521
1.00
28.97
D

ATOM
8788
C
ASP D
683
115.381
0.631
35.728
1.00
22.90
D

ATOM
8789
O
ASP D
683
114.466
0.281
36.458
1.00
22.58
D

ATOM
8790
N
ASN D
684
115.717
−0.072
34.653
1.00
21.68
D

ATOM
8791
CA
ASN D
684
114.937
−1.257
34.335
1.00
21.96
D

ATOM
8792
CB
ASN D
684
114.568
−1.291
32.842
1.00
20.91
D

ATOM
8793
CG
ASN D
684
113.639
−0.138
32.417
1.00
22.88
D

ATOM
8794
OD1
ASN D
684
112.685
0.229
33.132
1.00
20.08
D

ATOM
8795
ND2
ASN D
684
113.907
0.423
31.231
1.00
21.27
D

ATOM
8796
C
ASN D
684
115.561
−2.597
34.705
1.00
22.28
D

ATOM
8797
O
ASN D
684
114.840
−3.557
34.983
1.00
21.62
D

ATOM
8798
N
ILE D
685
116.890
−2.659
34.735
1.00
22.22
D

ATOM
8799
CA
ILE D
685
117.592
−3.906
35.022
1.00
24.26
D

ATOM
8800
CB
ILE D
685
118.241
−4.431
33.725
1.00
25.72
D

ATOM
8801
CG2
ILE D
685
119.014
−5.722
33.987
1.00
28.28
D

ATOM
8802
CG1
ILE D
685
117.181
−4.607
32.646
1.00
26.62
D

ATOM
8803
CD1
ILE D
685
117.527
−3.851
31.344
1.00
32.32
D

ATOM
8804
C
ILE D
685
118.701
−3.830
36.081
1.00
25.44
D

ATOM
8805
O
ILE D
685
119.291
−2.771
36.300
1.00
25.75
D

ATOM
8806
N
LEU D
686
118.989
−4.964
36.717
1.00
25.66
D

ATOM
8807
CA
LEU D
686
120.069
−5.041
37.689
1.00
26.90
D

ATOM
8808
CB
LEU D
686
119.530
−5.089
39.127
1.00
26.08
D

ATOM
8809
CG
LEU D
686
120.472
−5.572
40.262
1.00
23.99
D

ATOM
8810
CD1
LEU D
686
121.709
−4.699
40.345
1.00
23.40
D

ATOM
8811
CD2
LEU D
686
119.740
−5.567
41.585
1.00
21.28
D

ATOM
8812
C
LEU D
686
120.859
−6.317
37.412
1.00
28.01
D

ATOM
8813
O
LEU D
686
120.275
−7.397
37.340
1.00
28.42
D

ATOM
8814
N
VAL D
687
122.170
−6.194
37.226
1.00
26.81
D

ATOM
8815
CA
VAL D
687
122.995
−7.371
37.019
1.00
28.16
D

ATOM
8816
CB
VAL D
687
123.648
−7.401
35.629
1.00
28.88
D

ATOM
8817
CG1
VAL D
687
124.496
−8.669
35.484
1.00
27.76
D

ATOM
8818
CG2
VAL D
687
122.562
−7.383
34.553
1.00
29.55
D

ATOM
8819
C
VAL D
687
124.064
−7.347
38.098
1.00
29.32
D

ATOM
8820
O
VAL D
687
124.744
−6.331
38.291
1.00
29.09
D

ATOM
8821
N
SER D
688
124.200
−8.465
38.813
1.00
28.34
D

ATOM
8822
CA
SER D
688
125.166
−8.570
39.910
1.00
27.42
D

ATOM
8823
CB
SER D
688
124.419
−8.567
41.247
1.00
26.52
D

ATOM
8824
OG
SER D
688
123.505
−9.651
41.304
1.00
25.52
D

ATOM
8825
C
SER D
688
125.990
−9.853
39.808
1.00
27.67
D

ATOM
8826
O
SER D
688
125.518
−10.870
39.304
1.00
28.15
D

ATOM
8827
N
GLY D
689
127.217
−9.818
40.299
1.00
25.88
D

ATOM
8828
CA
GLY D
689
128.012
−11.016
40.228
1.00
25.97
D

ATOM
8829
C
GLY D
689
128.901
−11.218
41.422
1.00
27.10
D

ATOM
8830
O
GLY D
689
129.549
−10.285
41.890
1.00
29.72
D

ATOM
8831
N
SER D
690
128.914
−12.445
41.922
1.00
27.15
D

ATOM
8832
CA
SER D
690
129.752
−12.819
43.042
1.00
27.45
D

ATOM
8833
CB
SER D
690
128.918
−13.015
44.300
1.00
26.48
D

ATOM
8834
OG
SER D
690
127.975
−14.044
44.099
1.00
25.71
D

ATOM
8835
C
SER D
690
130.376
−14.145
42.630
1.00
28.76
D

ATOM
8836
O
SER D
690
130.435
−14.457
41.444
1.00
28.74
D

ATOM
8837
N
GLU D
691
130.829
−14.925
43.609
1.00
29.69
D

ATOM
8838
CA
GLU D
691
131.446
−16.210
43.320
1.00
29.80
D

ATOM
8839
CB
GLU D
691
132.241
−16.711
44.532
1.00
30.89
D

ATOM
8840
CG
GLU D
691
132.740
−18.153
44.426
1.00
34.76
D

ATOM
8841
CD
GLU D
691
133.806
−18.516
45.469
1.00
37.18
D

ATOM
8842
OE1
GLU D
691
134.895
−17.901
45.448
1.00
39.22
D

ATOM
8843
OE2
GLU D
691
133.564
−19.420
46.305
1.00
38.14
D

ATOM
8844
C
GLD D
691
130.409
−17.239
42.888
1.00
29.94
D

ATOM
8845
O
GLU D
691
129.441
−17.507
43.596
1.00
28.81
D

ATOM
8846
N
ASN D
692
130.621
−17.784
41.693
1.00
30.68
D

ATOM
8847
CA
ASN D
692
129.756
−18.800
41.122
1.00
30.63
D

ATOM
8848
CB
ASN D
692
129.854
−20.070
41.975
1.00
32.82
D

ATOM
8849
CG
ASN D
692
131.019
−20.951
41.562
1.00
34.81
D

ATOM
8850
OD1
ASN D
692
130.832
−21.908
40.812
1.00
39.00
D

ATOM
8851
ND2
ASN D
692
132.231
−20.614
42.016
1.00
34.40
D

ATOM
8852
C
ASN D
692
128.313
−18.370
40.941
1.00
30.73
D

ATOM
8853
O
ASN D
692
127.395
−19.187
40.996
1.00
31.82
D

ATOM
8854
N
GLN D
693
128.113
−17.081
40.711
1.00
30.83
D

ATOM
8855
CA
GLN D
693
126.774
−16.564
40.496
1.00
30.85
D

ATOM
8856
CB
GLN D
693
126.127
−16.215
41.837
1.00
32.95
D

ATOM
8857
CG
GLN D
693
125.494
−17.398
42.562
1.00
36.48
D

ATOM
8858
CD
CLN D
693
124.636
−16.949
43.741
1.00
39.48
D

ATOM
8859
OE1
GLN D
693
123.650
−16.222
43.571
1.00
40.51
D

ATOM
8860
NE2
GLN D
693
125.014
−17.371
44.941
1.00
40.67
D

ATOM
8861
C
GLN D
693
126.771
−15.350
39.560
1.00
30.20
D

ATOM
8862
O
GLN D
693
127.694
−14.533
39.586
1.00
28.95
D

ATOM
8863
N
PHE D
694
125.729
−15.268
38.728
1.00
28.92
D

ATOM
8864
CA
PHE D
694
125.534
−14.189
37.758
1.00
27.46
D

ATOM
8865
CB
PHE D
694
126.183
−14.549
36.404
1.00
26.85
D

ATOM
8866
CG
PHE D
694
126.212
−13.402
35.413
1.00
27.99
D

ATOM
8867
CD1
PHE D
694
127.027
−12.290
35.626
1.00
28.31
D

ATOM
8868
CD2
PHE D
694
125.387
−13.411
34.291
1.00
28.25
D

ATOM
8869
CE1
PHE D
694
127.011
−11.201
34.734
1.00
25.87
D

ATOM
8870
CE2
PHE D
694
125.365
−12.329
33.397
1.00
26.35
D

ATOM
8871
CZ
PHE D
694
126.175
−11.226
33.620
1.00
24.43
D

ATOM
8872
C
PHE D
694
124.018
−14.020
37.600
1.00
26.65
D

ATOM
8873
O
PHE D
694
123.360
−14.804
36.923
1.00
27.90
D

ATOM
8874
N
ASN D
695
123.462
−12.997
38.235
1.00
25.11
D

ATOM
8875
CA
ASN D
695
122.033
−12.784
38.169
1.00
22.66
D

ATOM
8876
CE
ASN D
695
121.462
−12.735
39.570
1.00
21.74
D

ATOM
8877
CG
ASN D
695
121.802
−13.948
40.351
1.00
22.53
D

ATOM
8878
OD1
ASN D
695
122.469
−13.863
41.381
1.00
25.44
D

ATOM
8879
ND2
ASN D
695
121.369
−15.102
39.866
1.00
21.60
D

ATOM
8880
C
ASN D
695
121.586
−11.557
37.431
1.00
22.56
D

ATOM
8881
O
ASN D
695
122.283
−10.537
37.402
1.00
24.25
D

ATOM
8882
N
ILE D
696
120.407
−11.675
36.828
1.00
20.27
D

ATOM
8883
CA
ILE D
696
119.785
−10.570
36.112
1.00
18.17
D

ATOM
8884
CB
ILE D
696
119.741
−10.848
34.598
1.00
13.96
D

ATOM
8885
CG2
ILE D
696
119.173
−9.631
33.874
1.00
12.40
D

ATOM
8886
CG1
ILE D
696
121.165
−11.096
34.095
1.00
11.96
D

ATOM
8887
CD1
ILE D
696
121.278
−11.411
32.627
1.00
10.15
D

ATOM
8888
C
ILE D
696
118.375
−10.387
36.708
1.00
19.43
D

ATOM
8889
O
ILE D
696
117.558
−11.307
36.714
1.00
19.49
D

ATOM
8890
N
TYR D
697
118.130
−9.194
37.236
1.00
18.77
D

ATOM
8891
CA
TYR D
697
116.878
−8.867
37.881
1.00
17.94
D

ATOM
8892
CB
TYR D
697
117.167
−8.295
39.280
1.00
19.60
D

ATOM
8893
CG
TYR D
697
118.014
−9.185
40.171
1.00
19.57
D

ATOM
8894
CD1
TYR D
697
117.428
−10.186
40.962
1.00
20.99
D

ATOM
8895
CE1
TYR D
697
118.204
−11.012
41.789
1.00
18.57
D

ATOM
8896
CD2
TYR D
697
119.397
−9.031
40.223
1.00
18.67
D

ATOM
8897
CE2
TYR D
697
120.179
−9.840
41.035
1.00
19.21
D

ATOM
8898
CZ
TYR D
697
119.581
−10.832
41.820
1.00
20.43
D

ATOM
8899
OH
TYR D
697
120.372
−11.634
42.627
1.00
20.44
D

ATOM
8900
C
TYR D
697
116.059
−7.843
37.104
1.00
18.57
D

ATOM
8901
O
TYR D
697
116.604
−6.934
36.456
1.00
18.53
D

ATOM
8902
N
ASN D
698
114.746
−7.975
37.208
1.00
16.25
D

ATOM
8903
CA
ASN D
698
113.826
−7.049
36.575
1.00
16.13
D

ATOM
8904
CB
ASN D
698
112.594
−7.832
36.111
1.00
16.70
D

ATOM
8905
CG
ASN D
698
111.516
−6.939
35.508
1.00
18.93
D

ATOM
8906
OD1
ASN D
698
111.253
−5.822
36.004
1.00
16.72
D

ATOM
8907
ND2
ASN D
698
110.873
−7.428
34.443
1.00
16.48
D

ATOM
8908
C
ASN D
698
113.441
−6.032
37.682
1.00
15.83
D

ATOM
8909
O
ASN D
698
112.568
−6.301
38.499
1.00
14.84
D

ATOM
8910
N
LEU D
699
114.078
−4.874
37.735
1.00
14.22
D

ATOM
8911
CA
LEU D
699
113.725
−3.948
38.796
1.00
15.47
D

ATOM
8912
CB
LEU D
699
114.549
−2.673
38.704
1.00
11.67
D

ATOM
8913
CG
LEU D
699
115.818
−2.596
39.541
1.00
12.58
D

ATOM
8914
CD
LEU D
699
116.357
−4.000
39.957
1.00
9.17
D

ATOM
8915
CD2
LEU D
699
116.822
−1.809
38.724
1.00
9.81
D

ATOM
8916
C
LEU D
699
112.260
−3.560
38.883
1.00
18.10
D

ATOM
8917
O
LEU D
699
111.836
−3.053
39.914
1.00
21.11
D

ATOM
8918
N
ARG D
700
111.479
−3.765
37.826
1.00
19.06
D

ATOM
8919
CA
ARG D
700
110.063
−3.382
37.889
1.00
18.41
D

ATOM
8920
CB
ARG D
700
109.474
−3.190
36.481
1.00
16.13
D

ATOM
8921
CG
ARG D
700
110.078
−2.053
35.660
1.00
18.32
D

ATOM
8922
CD
ARG D
700
109.605
−2.100
34.188
1.00
19.47
D

ATOM
8923
NE
ARG D
700
110.340
−1.195
33.295
1.00
19.60
D

ATOM
8924
CZ
ARG D
700
109.881
−0.738
32.127
1.00
20.84
D

ATOM
8925
NH1
ARG D
700
108.678
−1.085
31.693
1.00
19.16
D

ATOM
8926
NH2
ARG D
700
110.633
0.057
31.378
1.00
20.52
D

ATOM
8927
C
ARG D
700
109.211
−4.411
38.652
1.00
19.19
D

ATOM
8928
O
ARG D
700
108.440
−4.069
39.546
1.00
20.01
D

ATOM
8929
N
SER D
701
109.344
−5.673
38.286
1.00
18.61
D

ATOM
8930
CA
SER D
701
108.580
−6.719
38.919
1.00
18.99
D

ATOM
8931
CB
SER D
701
108.403
−7.907
37.960
1.00
17.26
D

ATOM
8932
OG
SER D
701
109.627
−8.299
37.350
1.00
16.41
D

ATOM
8933
C
SER D
701
109.317
−7.179
40.154
1.00
21.34
D

ATOM
8934
O
SER D
701
108.758
−7.881
40.983
1.00
21.67
D

ATOM
8935
N
GLY D
702
110.577
−6.782
40.277
1.00
23.17
D

ATOM
8936
CA
GLY D
702
111.367
−7.189
41.420
1.00
25.46
D

ATOM
8937
C
GLY D
702
111.916
−8.601
41.338
1.00
26.82
D

ATOM
8938
O
GLY D
702
112.676
−9.008
42.208
1.00
28.70
D

ATOM
8939
N
LYS D
703
111.580
−9.346
40.290
1.00
28.39
D

ATOM
8940
CA
LYS D
703
112.040
−10.734
40.187
1.00
29.97
D

ATOM
8941
CE
LYS D
703
110.926
−11.616
39.609
1.00
30.86
D

ATOM
8942
CG
LYS D
703
109.566
−11.294
40.211
1.00
34.24
D

ATOM
8943
CD
LYS D
703
108.553
−12.393
40.031
1.00
36.04
D

ATOM
8944
CE
LYS D
703
108.971
−13.657
40.786
1.00
38.38
D

ATOM
8945
NZ
LYS D
703
107.900
−14.711
40.780
1.00
39.62
D

ATOM
8946
C
LYS D
703
113.319
−11.022
39.428
1.00
30.16
D

ATOM
8947
O
LYS D
703
113.822
−10.202
38.665
1.00
33.16
D

ATOM
8948
N
LEU D
704
113.824
−12.227
39.655
1.00
31.22
D

ATOM
8949
CA
LEU D
704
115.037
−12.717
39.024
1.00
31.13
D

ATOM
8950
CE
LEU D
704
115.655
−13.799
39.894
1.00
28.59
D

ATOM
8951
CG
LEU D
704
116.959
−14.425
39.433
1.00
29.39
D

ATOM
8952
CD1
LEU D
704
118.092
−13.385
39.446
1.00
31.25
D

ATOM
8953
CD2
LEU D
704
117.298
−15.548
40.368
1.00
27.62
D

ATOM
8954
C
LEU D
704
114.663
−13.302
37.668
1.00
32.42
D

ATOM
8955
O
LEU D
704
113.791
−14.167
37.585
1.00
34.11
D

ATOM
8956
N
VAL D
705
115.308
−12.827
36.607
1.00
32.96
D

ATOM
8957
CA
VAL D
705
115.014
−13.329
35.275
1.00
33.27
D

ATOM
8958
CB
VAL D
705
115.052
−12.240
34.214
1.00
31.84
D

ATOM
8959
CG1
VAL D
705
114.710
−12.853
32.866
1.00
33.49
D

ATOM
8960
CG2
VAL D
705
114.079
−11.142
34.544
1.00
30.65
D

ATOM
8961
C
VAL D
705
116.011
−14.389
34.841
1.00
35.05
D

ATOM
8962
O
VAL D
705
115.632
−15.501
34.504
1.00
37.11
D

ATOM
8963
N
HIS D
706
117.291
−14.041
34.827
1.00
36.45
D

ATOM
8964
CA
HIS D
706
118.316
−14.991
34.426
1.00
36.74
D

ATOM
8965
CB
HIS D
706
119.007
−14.539
33.137
1.00
37.71
D

ATOM
8966
CG
HIS D
706
118.064
−14.142
32.042
1.00
40.20
D

ATOM
8967
CD2
HIS D
706
117.901
−12.964
31.392
1.00
41.01
D

ATOM
8968
ND1
HIS D
706
117.172
−15.022
31.468
1.00
40.45
D

ATOM
8969
CE1
HIS D
706
116.504
−14.404
30.509
1.00
41.40
D

ATOM
8970
NE2
HIS D
706
116.927
−13.155
30.441
1.00
41.00
D

ATOM
8971
C
HIS D
706
119.361
−15.155
35.527
1.00
37.89
D

ATOM
8972
O
HIS D
706
119.869
−14.174
36.096
1.00
38.65
D

ATOM
8973
N
ALA D
707
119.686
−16.414
35.805
1.00
37.80
D

ATOM
8974
CA
ALA D
707
120.660
−16.757
36.828
1.00
36.66
D

ATOM
8975
CB
ALA D
707
119.935
−17.223
38.075
1.00
33.53
D

ATOM
8976
C
ALA D
707
121.651
−17.828
36.367
1.00
36.44
D

ATOM
8977
O
ALA D
707
122.608
−18.138
37.079
1.00
36.66
D

ATOM
8978
N
ASN D
708
121.446
−18.382
35.177
1.00
36.37
D

ATOM
8979
CA
ASN D
708
122.347
−19.431
34.710
1.00
37.18
D

ATOM
8980
CB
ASN D
708
121.553
−20.739
34.521
1.00
37.73
D

ATOM
8981
CG
ASN D
708
120.893
−21.212
35.821
1.00
38.57
D

ATOM
8982
OD1
ASN D
708
119.667
−21.227
35.947
1.00
38.35
D

ATOM
8983
ND2
ASN D
708
121.712
−21.588
36.794
1.00
37.37
D

ATOM
8984
C
ASN D
708
123.137
−19.084
33.443
1.00
36.59
D

ATOM
8985
O
ASN D
708
123.856
−19.927
32.907
1.00
35.29
D

ATOM
8986
N
ILE D
709
123.019
−17.839
32.986
1.00
35.82
D

ATOM
8987
CA
ILE D
709
123.709
−17.402
31.781
1.00
34.43
D

ATOM
8988
CB
ILE D
709
123.349
−15.928
31.408
1.00
32.34
D

ATOM
8989
CG2
ILE D
709
124.151
−15.460
30.221
1.00
30.43
D

ATOM
8990
CG1
ILE D
709
121.875
−15.836
31.017
1.00
30.65
D

ATOM
8991
CD1
ILE D
709
121.444
−14.459
30.565
1.00
28.79
D

ATOM
8992
C
ILE D
709
125.216
−17.552
31.873
1.00
34.88
D

ATOM
8993
O
ILE D
709
125.863
−17.878
30.882
1.00
36.86
D

ATOM
8994
N
LEU D
710
125.785
−17.336
33.051
1.00
34.63
D

ATOM
8995
CA
LEU D
710
127.232
−17.454
33.186
1.00
32.46
D

ATOM
8996
CB
LEU D
710
127.837
−16.058
33.402
1.00
28.39
D

ATOM
8997
CG
LEU D
710
128.450
−15.306
32.208
1.00
25.87
D

ATOM
8998
CD1
LEU D
710
127.798
−15.707
30.894
1.00
24.33
D

ATOM
8999
CD2
LEU D
710
128.331
−13.810
32.443
1.00
23.04
D

ATOM
9000
C
LEU D
710
127.683
−18.434
34.269
1.00
33.52
D

ATOM
9001
O
LEU D
710
128.730
−18.246
34.882
1.00
34.43
D

ATOM
9002
N
LYS D
711
126.902
−19.494
34.480
1.00
34.36
D

ATOM
9003
CA
LYS D
711
127.230
−20.518
35.481
1.00
35.44
D

ATOM
9004
CB
LYS D
711
126.238
−21.670
35.389
1.00
34.96
D

ATOM
9005
CG
LYS D
711
125.872
−22.006
33.980
1.00
36.79
D

ATOM
9006
CD
LYS D
711
124.620
−22.834
33.940
1.00
38.39
D

ATOM
9007
CE
LYS D
711
124.936
−24.285
34.192
1.00
40.21
D

ATOM
9008
NZ
LYS D
711
125.841
−24.794
33.104
1.00
42.27
D

ATOM
9009
C
LYS D
711
128.645
−21.068
35.350
1.00
36.53
D

ATOM
9010
O
LYS D
711
129.284
−21.427
36.341
1.00
36.63
D

ATOM
9011
N
ASP D
712
129.130
−21.126
34.121
1.00
37.64
D

ATOM
9012
CA
ASP D
712
130.457
−21.629
33.836
1.00
39.74
D

ATOM
9013
CB
ASP D
712
130.688
−21.555
32.336
1.00
44.17
D

ATOM
9014
CG
ASP D
712
129.490
−22.032
31.558
1.00
49.91
D

ATOM
9015
OD1
ASP D
712
129.338
−23.276
31.408
1.00
53.21
D

ATOM
9016
OD2
ASP D
712
128.684
−21.163
31.122
1.00
51.40
D

ATOM
9017
C
ASP D
712
131.548
−20.856
34.551
1.00
39.02
D

ATOM
9018
O
ASP D
712
132.528
−21.439
34.992
1.00
39.79
D

ATOM
9019
N
ALA D
713
131.398
−19.542
34.647
1.00
37.44
D

ATOM
9020
CA
ALA D
713
132.427
−18.740
35.295
1.00
37.31
D

ATOM
9021
CB
ALA D
713
132.131
−17.254
35.119
1.00
37.40
D

ATOM
9022
C
ALA D
713
132.603
−19.055
36.775
1.00
36.89
D

ATOM
9023
O
ALA D
713
131.693
−19.535
37.437
1.00
37.66
D

ATOM
9024
N
ASP D
714
133.785
−18.782
37.296
1.00
35.36
D

ATOM
9025
CA
ASP D
714
134.018
−19.033
38.693
1.00
34.87
D

ATOM
9026
CB
ASP D
714
135.384
−19.678
38.893
1.00
33.94
D

ATOM
9027
CG
ASP D
714
135.484
−21.038
38.244
1.00
32.23
D

ATOM
9028
OD1
ASP D
714
134.599
−21.877
38.477
1.00
32.51
D

ATOM
9029
OD2
ASP D
714
136.456
−21.279
37.505
1.00
34.54
D

ATOM
9030
C
ASP D
714
133.946
−17.705
39.433
1.00
35.72
D

ATOM
9031
O
ASP D
714
133.610
−17.651
40.616
1.00
35.20
D

ATOM
9032
N
GLN D
715
134.238
−16.629
38.714
1.00
35.93
D

ATOM
9033
CA
GLN D
715
134.233
−15.293
39.284
1.00
36.18
D

ATOM
9034
CE
GLN D
715
135.648
−14.938
39.750
1.00
37.10
D

ATOM
9035
CG
GLN D
715
136.260
−15.951
40.716
1.00
39.05
D

ATOM
9036
CD
GLN D
715
135.897
−15.672
42.165
1.00
40.12
D

ATOM
9037
OE1
GLN D
715
134.751
−15.380
42.472
1.00
42.68
D

ATOM
9038
NE2
GLN D
715
136.874
−15.763
43.057
1.00
39.97
D

ATOM
9039
C
GLN D
715
133.756
−14.264
38.254
1.00
35.81
D

ATOM
9040
O
GLN D
715
133.993
−14.407
37.054
1.00
35.76
D

ATOM
9041
N
ILE D
716
133.073
−13.232
38.736
1.00
34.56
D

ATOM
9042
CA
ILE D
716
132.582
−12.149
37.888
1.00
32.51
D

ATOM
9043
CB
ILE D
716
131.061
−11.982
38.032
1.00
31.79
D

ATOM
9044
CG2
ILE D
716
130.547
−11.006
36.996
1.00
30.49
D

ATOM
9045
CG1
ILE D
716
130.363
−13.336
37.890
1.00
33.24
D

ATOM
9046
CD1
ILE D
716
130.638
−14.060
36.579
1.00
34.30
D

ATOM
9047
C
ILE D
716
133.285
−10.863
38.375
1.00
32.59
D

ATOM
9048
O
ILE D
716
132.797
−10.160
39.264
1.00
33.77
D

ATOM
9049
N
TRP D
717
134.444
−10.580
37.795
1.00
30.84
D

ATOM
9050
CA
TRP D
717
135.252
−9.429
38.162
1.00
29.11
D

ATOM
9051
CE
TRP D
717
136.558
−9.454
37.379
1.00
32.71
D

ATOM
9052
CG
TRP D
717
137.348
−10.687
37.596
1.00
35.43
D

ATOM
9053
CD2
TRP D
717
137.669
−11.278
38.855
1.00
35.53
D

ATOM
9054
CE2
TRP D
717
138.462
−12.416
38.589
1.00
36.83
D

ATOM
9055
CE3
TRP D
717
137.364
−10.960
40.185
1.00
35.83
D

ATOM
9056
CD1
TRP D
717
137.940
−11.464
36.640
1.00
36.35
D

ATOM
9057
NE1
TRP D
717
138.612
−12.504
37.230
1.00
37.07
D

ATOM
9058
CZ2
TRP D
717
138.956
−13.237
39.605
1.00
38.32
D

ATOM
9059
CZ3
TRP D
717
137.855
−11.780
41.193
1.00
37.12
D

ATOM
9060
CH2
TRP D
717
138.641
−12.904
40.896
1.00
37.38
D

ATOM
9061
C
TRP D
717
134.583
−8.102
37.930
1.00
26.79
D

ATOM
9062
O
TRP D
717
134.507
−7.262
38.825
1.00
24.62
D

ATOM
9063
N
SER D
718
134.110
−7.899
36.713
1.00
24.96
D

ATOM
9064
CA
SER D
718
133.473
−6.639
36.403
1.00
23.33
D

ATOM
9065
CB
SER D
718
134.499
−5.674
35.830
1.00
21.39
D

ATOM
9066
OG
SER D
718
133.898
−4.420
35.620
1.00
24.14
D

ATOM
9067
C
SER D
718
132.347
−6.825
35.421
1.00
22.63
D

ATOM
9068
O
SER D
718
132.481
−7.549
34.443
1.00
25.60
D

ATOM
9069
N
VAL D
719
131.228
−6.175
35.679
1.00
21.31
D

ATOM
9070
CA
VAL D
719
130.095
−6.286
34.784
1.00
23.17
D

ATOM
9071
CB
VAL D
719
128.900
−6.926
35.517
1.00
23.18
D

ATOM
9072
CG1
VAL D
719
128.244
−5.916
36.483
1.00
23.48
D

ATOM
9073
CG2
VAL D
719
127.915
−7.427
34.517
1.00
24.77
D

ATOM
9074
C
VAL D
719
129.703
−4.887
34.255
1.00
24.78
D

ATOM
9075
O
VAL D
719
130.024
−3.864
34.872
1.00
25.63
D

ATOM
9076
N
ASN D
720
129.005
−4.835
33.125
1.00
25.17
D

ATOM
9077
CA
ASN D
720
128.604
−3.547
32.543
1.00
25.66
D

ATOM
9078
CB
ASN D
720
129.844
−2.787
31.999
1.00
25.58
D

ATOM
9079
CG
ASN D
720
129.627
−1.256
31.853
1.00
26.08
D

ATOM
9080
OD1
ASN D
720
128.697
−0.790
31.193
1.00
24.37
D

ATOM
9081
ND2
ASN D
720
130.527
−0.484
32.456
1.00
24.14
D

ATOM
9082
C
ASN D
720
127.665
−3.882
31.397
1.00
25.69
D

ATOM
9083
O
ASN D
720
127.961
−4.770
30.601
1.00
24.75
D

ATOM
9084
N
PHE D
721
126.524
−3.209
31.324
1.00
25.70
D

ATOM
9085
CA
PHE D
721
125.610
−3.473
30.226
1.00
25.92
D

ATOM
9086
CB
PHE D
721
124.486
−4.426
30.663
1.00
24.85
D

ATOM
9087
CG
PHE D
721
123.483
−3.803
31.566
1.00
23.85
D

ATOM
9088
CD1
PHE D
721
122.441
−3.052
31.043
1.00
22.92
D

ATOM
9089
CD2
PHE D
721
123.588
−3.938
32.941
1.00
22.57
D

ATOM
9090
CE1
PHE D
721
121.525
−2.442
31.877
1.00
21.91
D

ATOM
9091
CE2
PHE D
721
122.675
−3.328
33.777
1.00
22.55
D

ATOM
9092
CZ
PHE D
721
121.640
−2.579
33.243
1.00
21.48
D

ATOM
9093
C
PHE D
721
125.076
−2.145
29.706
1.00
26.21
D

ATOM
9094
O
PHE D
721
125.149
−1.120
30.402
1.00
25.17
D

ATOM
9095
N
LYS D
722
124.564
−2.166
28.473
1.00
26.41
D

ATOM
9096
CA
LYS D
722
124.046
−0.966
27.801
1.00
25.77
D

ATOM
9097
CB
LYS D
722
125.230
−0.140
27.287
1.00
25.66
D

ATOM
9098
CG
LYS D
722
125.220
1.340
27.627
1.00
26.55
D

ATOM
9099
CD
LYS D
722
124.193
2.106
26.828
1.00
28.07
D

ATOM
9100
CE
LYS D
722
124.609
3.586
26.571
1.00
31.04
D

ATOM
9101
NZ
LYS D
722
125.623
3.789
25.462
1.00
31.59
D

ATOM
9102
C
LYS D
722
123.152
−1.376
26.621
1.00
25.54
D

ATOM
9103
O
LYS D
722
123.556
−2.161
25.765
1.00
24.73
D

ATOM
9104
N
GLY D
723
121.936
−0.851
26.580
1.00
25.69
D

ATOM
9105
CA
GLY D
723
121.044
−1.201
25.497
1.00
25.26
D

ATOM
9106
C
GLY D
723
120.804
−2.694
25.431
1.00
27.03
D

ATOM
9107
O
GLY D
723
120.226
−3.287
26.342
1.00
28.21
D

ATOM
9108
N
LYS D
724
121.262
−3.313
24.350
1.00
28.66
D

ATOM
9109
CA
LYS D
724
121.087
−4.752
24.144
1.00
29.79
D

ATOM
9110
CB
LYS D
724
120.590
−4.978
22.732
1.00
30.45
D

ATOM
9111
CG
LYS D
724
121.344
−4.146
21.713
1.00
32.48
D

ATOM
9112
CD
LYS D
724
122.379
−4.944
20.947
1.00
34.54
D

ATOM
9113
CE
LYS D
724
122.796
−4.163
19.693
1.00
36.42
D

ATOM
9114
NZ
LYS D
724
123.789
−4.878
18.817
1.00
36.97
D

ATOM
9115
C
LYS D
724
122.373
−5.535
24.346
1.00
29.03
D

ATOM
9116
O
LYS D
724
122.417
−6.749
24.142
1.00
28.40
D

ATOM
9117
N
THR D
725
123.409
−4.820
24.759
1.00
28.23
D

ATOM
9118
CA
THR D
725
124.720
−5.400
24.964
1.00
27.95
D

ATOM
9119
CB
THR D
725
125.784
−4.578
24.178
1.00
27.43
D

ATOM
9120
OG1
THR D
725
125.351
−4.417
22.821
1.00
26.72
D

ATOM
9121
CG2
THR D
725
127.134
−5.273
24.189
1.00
25.82
D

ATOM
9122
C
THR D
725
125.106
−5.460
26.443
1.00
27.90
D

ATOM
9123
O
THR D
725
124.891
−4.505
27.199
1.00
28.70
D

ATOM
9124
N
LEU D
726
125.682
−6.591
26.842
1.00
26.83
D

ATOM
9125
CA
LEU D
726
126.119
−6.806
28.213
1.00
24.94
D

ATOM
9126
CB
LEU D
726
125.126
−7.703
28.937
1.00
27.71
D

ATOM
9127
CG
LEU D
726
125.632
−8.393
30.211
1.00
29.98
D

ATOM
9128
CD1
LEU D
726
126.114
−7.390
31.271
1.00
30.93
D

ATOM
9129
CD2
LEU D
726
124.478
−9.202
30.758
1.00
31.05
D

ATOM
9130
C
LEU D
726
127.485
−7.441
28.245
1.00
22.94
D

ATOM
9131
O
LEU D
726
127.673
−8.537
27.741
1.00
24.07
D

ATOM
9132
N
VAL D
727
128.436
−6.753
28.856
1.00
23.62
D

ATOM
9133
CA
VAL D
727
129.798
−7.256
28.940
1.00
23.62
D

ATOM
9134
CB
VAL D
727
130.766
−6.218
28.377
1.00
24.57
D

ATOM
9135
CG1
VAL D
727
132.189
−6.737
28.490
1.00
28.26
D

ATOM
9136
CG2
VAL D
727
130.414
−5.939
26.896
1.00
22.22
D

ATOM
9137
C
VAL D
727
130.214
−7.625
30.360
1.00
21.59
D

ATOM
9138
O
VAL D
727
129.738
−7.034
31.333
1.00
20.77
D

ATOM
9139
N
ALA D
728
131.106
−8.608
30.461
1.00
21.47
D

ATOM
9140
CA
ALA D
728
131.597
−9.084
31.751
1.00
21.74
D

ATOM
9141
CB
ALA D
728
130.593
−10.057
32.371
1.00
23.07
D

ATOM
9142
C
ALA D
728
132.952
−9.749
31.692
1.00
21.99
D

ATOM
9143
O
ALA D
728
133.199
−10.624
30.846
1.00
17.98
D

ATOM
9144
N
ALA D
729
133.823
−9.315
32.605
1.00
24.10
D

ATOM
9145
CA
ALA D
729
135.175
−9.868
32.740
1.00
25.79
D

ATOM
9146
CB
ALA D
729
136.139
−8.792
33.225
1.00
26.49
D

ATOM
9147
C
ALA D
729
135.036
−10.980
33.770
1.00
26.20
D

ATOM
9148
O
ALA D
729
134.619
−10.736
34.900
1.00
24.79
D

ATOM
9149
N
VAL D
730
135.363
−12.199
33.351
1.00
27.91
D

ATOM
9150
CA
VAL D
730
135.224
−13.396
34.182
1.00
28.52
D

ATOM
9151
CB
VAL D
730
134.162
−14.349
33.578
1.00
25.65
D

ATOM
9152
CD1
VAL D
730
132.846
−13.619
33.401
1.00
21.69
D

ATOM
9153
CD2
VAL D
730
134.667
−14.910
32.251
1.00
23.86
D

ATOM
9154
C
VAL D
730
136.496
−14.215
34.373
1.00
30.60
D

ATOM
9155
O
VAL D
730
137.544
−13.945
33.773
1.00
29.25
D

ATOM
9156
N
GLU D
731
136.373
−15.227
35.224
1.00
34.05
D

ATOM
9157
CA
GLU D
731
137.468
−16.136
35.507
1.00
38.43
D

ATOM
9158
CB
GLU D
731
138.069
−15.875
36.877
1.00
39.08
D

ATOM
9159
CG
GLU D
731
139.163
−16.851
37.195
1.00
41.06
D

ATOM
9160
CD
GLU D
731
139.469
−16.908
38.664
1.00
44.19
D

ATOM
9161
OE1
GLU D
731
139.986
−15.898
39.204
1.00
43.94
D

ATOM
9162
OE2
GLU D
731
139.184
−17.969
39.275
1.00
45.15
D

ATOM
9163
C
GLU D
731
136.915
−17.541
35.481
1.00
39.52
D

ATOM
9164
O
GLU D
731
136.003
−17.862
36.239
1.00
38.90
D

ATOM
9165
N
LYS D
732
137.464
−18.375
34.606
1.00
42.02
D

ATOM
9166
CA
LYS D
732
137.000
−19.744
34.487
1.00
44.14
D

ATOM
9167
CB
LYS D
732
136.079
−19.864
33.279
1.00
45.79
D

ATOM
9168
CG
LYS D
732
135.263
−21.130
33.269
1.00
48.52
D

ATOM
9169
CD
LYS D
732
134.329
−21.169
32.074
1.00
48.95
D

ATOM
9170
CE
LYS D
732
133.753
−22.555
31.897
1.00
50.73
D

ATOM
9171
NZ
LYS D
732
132.777
−22.576
30.795
1.00
53.14
D

ATOM
9172
C
LYS D
732
138.155
−20.724
34.366
1.00
45.13
D

ATOM
9173
O
LYS D
732
139.012
−20.593
33.491
1.00
46.00
D

ATOM
9174
N
ASP D
733
138.179
−21.702
35.263
1.00
45.68
D

ATOM
9175
CA
ASP D
733
139.227
−22.710
35.263
1.00
45.99
D

ATOM
9176
CE
ASP D
733
139.114
−23.590
34.013
1.00
47.96
D

ATOM
9177
CG
ASP D
733
137.759
−24.322
33.917
1.00
51.97
D

ATOM
9178
OD1
ASP D
733
137.355
−24.977
34.905
1.00
55.70
D

ATOM
9179
OD2
ASP D
733
137.095
−24.256
32.855
1.00
50.55
D

ATOM
9180
C
ASP D
733
140.603
−22.066
35.311
1.00
45.97
D

ATOM
9181
O
ASP D
733
141.493
−22.456
34.565
1.00
46.45
D

ATOM
9182
N
GLY D
734
140.778
−21.075
36.182
1.00
45.60
D

ATOM
9183
CA
GLY D
734
142.072
−20.420
36.295
1.00
44.79
D

ATOM
9184
C
GLY D
734
142.438
−19.447
35.182
1.00
44.98
D

ATOM
9185
O
GLY D
734
143.607
−19.089
35.012
1.00
44.45
D

ATOM
9186
N
GLN D
735
141.453
−19.010
34.411
1.00
43.41
D

ATOM
9187
CA
GLN D
735
141.747
−18.067
33.349
1.00
42.41
D

ATOM
9188
CB
GLN D
735
141.935
−18.820
32.034
1.00
44.33
D

ATOM
9189
CG
GLN D
735
143.185
−19.679
32.036
1.00
46.62
D

ATOM
9190
CD
GLN D
735
143.303
−20.555
30.810
1.00
48.33
D

ATOM
9191
OE1
GLN D
735
143.228
−20.076
29.670
1.00
49.33
D

ATOM
9192
NE2
GLN D
735
143.495
−21.853
31.035
1.00
48.62
D

ATOM
9193
C
GLN D
735
140.647
−17.025
33.243
1.00
40.32
D

ATOM
9194
O
GLN D
735
139.504
−17.282
33.609
1.00
40.35
D

ATOM
9195
N
SER D
736
141.001
−15.841
32.765
1.00
37.70
D

ATOM
9196
CA
SER D
736
140.033
−14.770
32.630
1.00
35.67
D

ATOM
9197
CB
SER D
736
140.664
−13.454
33.051
1.00
35.55
D

ATOM
9198
OG
SER D
736
141.815
−13.209
32.262
1.00
33.28
D

ATOM
9199
C
SER D
736
139.580
−14.656
31.191
1.00
35.08
D

ATOM
9200
O
SER D
736
140.375
−14.823
30.273
1.00
35.01
D

ATOM
9201
N
PHE D
737
138.299
−14.370
30.998
1.00
35.00
D

ATOM
9202
CA
PHE D
737
137.749
−14.215
29.662
1.00
34.26
D

ATOM
9203
CB
PHE D
737
136.928
−15.436
29.259
1.00
34.41
D

ATOM
9204
CG
PHE D
737
137.736
−16.689
29.121
1.00
34.85
D

ATOM
9205
CD1
PHE D
737
138.122
−17.416
30.243
1.00
34.24
D

ATOM
9206
CD2
PHE D
737
138.120
−17.140
27.864
1.00
34.84
D

ATOM
9207
CE1
PHE D
737
138.871
−18.574
30.108
1.00
34.16
D

ATOM
9208
CE2
PHE D
737
138.868
−18.293
27.724
1.00
33.97
D

ATOM
9209
CZ
PHE D
737
139.246
−19.012
28.845
1.00
34.14
D

ATOM
9210
C
PHE D
737
136.869
−12.992
29.611
1.00
33.97
D

ATOM
9211
O
PHE D
737
136.627
−12.359
30.639
1.00
34.16
D

ATOM
9212
N
LEU D
738
136.387
−12.673
28.411
1.00
32.98
D

ATOM
9213
CA
LEU D
738
135.526
−11.514
28.199
1.00
33.21
D

ATOM
9214
CB
LEU D
738
136.222
−10.527
27.255
1.00
32.13
D

ATOM
9215
CG
LEU D
738
135.744
−9.075
27.237
1.00
32.97
D

ATOM
9216
CD1
LEU D
738
134.465
−8.962
26.461
1.00
33.24
D

ATOM
9217
CD2
LEU D
738
135.574
−8.569
28.668
1.00
33.16
D

ATOM
9218
C
LEU D
738
134.180
−11.955
27.620
1.00
33.76
D

ATOM
9219
O
LEU D
738
134.110
−12.360
26.473
1.00
36.66
D

ATOM
9220
N
GLU D
739
133.114
−11.870
28.410
1.00
33.64
D

ATOM
9221
CA
GLU D
739
131.793
−12.292
27.959
1.00
32.51
D

ATOM
9222
CB
GLU D
739
131.000
−12.884
29.121
1.00
33.25
D

ATOM
9223
CG
GLU D
739
131.529
−14.166
29.668
1.00
34.95
D

ATOM
9224
CD
GLU D
739
131.644
−15.235
28.602
1.00
38.68
D

ATOM
9225
OE1
GLU D
739
130.731
−15.323
27.733
1.00
38.32
D

ATOM
9226
OE2
GLU D
739
132.651
−15.991
28.646
1.00
39.63
D

ATOM
9227
C
GLU D
739
130.961
−11.163
27.377
1.00
32.88
D

ATOM
9228
O
GLU D
739
130.735
−10.144
28.044
1.00
33.94
D

ATOM
9229
N
ILE D
740
130.487
−11.329
26.147
1.00
31.70
D

ATOM
9230
CA
ILE D
740
129.641
−10.301
25.568
1.00
29.64
D

ATOM
9231
CB
ILE D
740
130.288
−9.670
24.299
1.00
28.27
D

ATOM
9232
CG2
ILE D
740
129.461
−8.484
23.831
1.00
27.08
D

ATOM
9233
CG1
ILE D
740
131.663
−9.093
24.620
1.00
24.97
D

ATOM
9234
CD1
ILE D
740
132.282
−8.385
23.424
1.00
24.47
D

ATOM
9235
C
ILE D
740
128.275
−10.906
25.252
1.00
29.65
D

ATOM
9236
O
ILE D
740
128.174
−11.845
24.470
1.00
30.71
D

ATOM
9237
N
LEU D
741
127.226
−10.388
25.885
1.00
30.03
D

ATOM
9238
CA
LEU D
741
125.872
−10.903
25.659
1.00
30.25
D

ATOM
9239
CB
LEU D
741
125.209
−11.213
26.994
1.00
30.19
D

ATOM
9240
CG
LEU D
741
126.016
−12.176
27.872
1.00
30.17
D

ATOM
9241
CD1
LEU D
741
125.458
−12.120
29.284
1.00
31.69
D

ATOM
9242
CD2
LEU D
741
125.969
−13.591
27.323
1.00
26.90
D

ATOM
9243
C
LEU D
741
125.012
−9.935
24.863
1.00
29.80
D

ATOM
9244
O
LEU D
741
124.939
−8.750
25.176
1.00
28.77
D

ATOM
9245
N
ASP D
742
124.354
−10.462
23.837
1.00
31.56
D

ATOM
9246
CA
ASP D
742
123.513
−9.664
22.948
1.00
32.74
D

ATOM
9247
CB
ASP D
742
123.917
−9.906
21.492
1.00
33.83
D

ATOM
9248
CG
ASP D
742
123.601
−8.730
20.592
1.00
34.30
D

ATOM
9249
OD1
ASP D
742
122.422
−8.315
20.526
1.00
33.76
D

ATOM
9250
OD2
ASP D
742
124.550
−8.223
19.952
1.00
34.48
D

ATOM
9251
C
ASP D
742
122.046
−10.021
23.110
1.00
33.39
D

ATOM
9252
O
ASP D
742
121.617
−11.102
22.713
1.00
33.45
D

ATOM
9253
N
PHE D
743
121.283
−9.097
23.685
1.00
34.50
D

ATOM
9254
CA
PHE D
743
119.858
−9.296
23.905
1.00
34.56
D

ATOM
9255
CB
PHE D
743
119.422
−8.544
25.161
1.00
32.05
D

ATOM
9256
CG
PHE D
743
119.627
−9.324
26.400
1.00
29.59
D

ATOM
9257
CD1
PHE D
743
120.893
−9.462
26.941
1.00
27.43
D

ATOM
9258
CD2
PHE D
743
118.579
−10.058
26.935
1.00
28.98
D

ATOM
9259
CE1
PHE D
743
121.116
−10.332
27.987
1.00
26.97
D

ATOM
9260
CE2
PHE D
743
118.787
−10.933
27.980
1.00
27.93
D

ATOM
9261
CZ
PHE D
743
120.059
−11.077
28.507
1.00
26.94
D

ATOM
9262
C
PHE D
743
118.973
−8.895
22.734
1.00
35.12
D

ATOM
9263
O
PHE D
743
117.746
−8.889
22.849
1.00
35.80
D

ATOM
9264
N
SER D
744
119.594
−8.592
21.600
1.00
35.35
D

ATOM
9265
CA
SER D
744
118.854
−8.176
20.416
1.00
35.76
D

ATOM
9266
CB
SER D
744
119.823
−7.612
19.381
1.00
36.40
D

ATOM
9267
OG
SER D
744
119.126
−6.857
18.417
1.00
40.54
D

ATOM
9268
C
SER D
744
118.029
−9.301
19.793
1.00
35.75
D

ATOM
9269
O
SER D
744
118.433
−10.488
19.873
1.00
36.28
D

ATOM
9270
OXT
SER D
744
116.984
−8.972
19.209
1.00
34.82
D

ATOM
9271
CB
LEU E
2
57.203
−3.013
76.696
1.00
93.40
E

ATOM
9272
CG
LEU E
2
56.802
−2.909
78.154
1.00
92.64
E

ATOM
9273
CD1
LEU E
2
56.089
−4.209
78.494
1.00
92.62
E

ATOM
9274
CD2
LEU E
2
58.002
−2.716
79.063
1.00
91.70
E

ATOM
9275
C
LEU E
2
58.910
−2.837
74.950
1.00
94.06
E

ATOM
9276
O
LEU E
2
59.052
−4.056
75.064
1.00
94.80
E

ATOM
9277
N
LEU E
2
57.498
−0.813
75.549
1.00
93.79
E

ATOM
9278
CA
LEU E
2
58.180
−2.054
76.029
1.00
93.74
E

ATOM
9279
N
LEU E
3
59.349
−2.162
73.890
1.00
93.32
E

ATOM
9280
CA
LEU E
3
60.093
−2.853
72.840
1.00
91.84
E

ATOM
9281
CS
LEU E
3
60.099
−2.030
71.539
1.00
90.21
E

ATOM
9282
CG
LEU E
3
58.738
−2.011
70.818
1.00
88.51
E

ATOM
9283
CD1
LEU E
3
58.863
−1.419
69.431
1.00
86.61
E

ATOM
9284
CD2
LEU E
3
58.194
−3.426
70.729
1.00
87.78
E

ATOM
9285
C
LEU E
3
61.504
−3.132
73.355
1.00
91.93
E

ATOM
9286
O
LEU E
3
62.459
−2.428
73.011
1.00
92.22
E

ATOM
9287
N
TPO E
4
61.634
−4.171
74.204
1.00
91.56
E

ATOM
9288
CA
TPO E
4
62.536
−4.975
75.032
1.00
90.52
E

ATOM
9289
CE
TPO E
4
62.853
−4.058
76.249
1.00
89.37
E

ATOM
9290
CG2
TPO E
4
63.717
−4.740
77.314
1.00
89.39
E

ATOM
9291
OG1
TPO E
4
63.546
−2.864
75.833
1.00
86.87
E

ATOM
9292
P
TPO E
4
65.016
−2.884
75.092
1.00
83.35
E

ATOM
9293
O1P
TPO E
4
64.849
−3.624
73.731
1.00
83.36
E

ATOM
9294
O2P
TPO E
4
66.088
−3.641
76.006
1.00
83.80
E

ATOM
9295
O3P
TPO E
4
65.359
−1.340
74.831
1.00
84.80
E

ATOM
9296
C
TPO E
4
61.804
−6.259
75.507
1.00
91.34
E

ATOM
9297
O
TPO E
4
60.467
−6.316
75.619
1.00
91.46
E

ATOM
9298
N
PRO E
5
63.256
−5.997
71.948
1.00
83.51
E

ATOM
9299
CD
PRO E
5
63.441
−4.606
71.529
1.00
83.14
E

ATOM
9300
CA
PRO E
5
63.931
−6.885
71.003
1.00
84.53
E

ATOM
9301
CE
PRO E
5
65.159
−6.089
70.575
1.00
83.61
E

ATOM
9302
OG
PRO E
5
64.831
−4.637
70.919
1.00
83.06
E

ATOM
9303
C
PRO E
5
64.316
−8.236
71.564
1.00
85.50
E

ATOM
9304
O
PRO E
5
64.916
−8.330
72.628
1.00
85.67
E

ATOM
9305
N
PRO E
6
63.969
−9.312
70.847
1.00
86.93
E

ATOM
9306
CD
PRO E
6
63.085
−9.303
69.669
1.00
87.22
E

ATOM
9307
CA
PRO E
6
64.267
−10.690
71.255
1.00
88.33
E

ATOM
9308
CE
PRO E
6
63.629
−11.522
70.149
1.00
87.80
E

ATOM
9309
CG
PRO E
6
62.478
−10.688
69.722
1.00
87.62
E

ATOM
9310
C
PRO E
6
65.765
−10.988
71.384
1.00
89.85
E

ATOM
9311
O
PRO E
6
66.575
−10.544
70.557
1.00
90.61
E

ATOM
9312
N
GLN E
7
66.126
−11.745
72.421
1.00
90.83
E

ATOM
9313
CA
GLN E
7
67.515
−12.125
72.626
1.00
91.45
E

ATOM
9314
CE
GLN E
7
68.006
−11.682
73.992
1.00
91.16
E

ATOM
9315
CG
GLN E
7
68.555
−10.282
73.957
1.00
91.12
E

ATOM
9316
CD
GLN E
7
69.842
−10.165
74.739
1.00
91.14
E

ATOM
9317
OE1
GLN E
7
69.851
−10.287
75.975
1.00
92.25
E

ATOM
9318
NB2
GLN E
7
70.950
−9.958
74.025
1.00
89.30
E

ATOM
9319
C
GLN E
7
67.666
−13.631
72.485
1.00
91.90
E

ATOM
9320
0
GLN E
7
67.429
−14.383
73.431
1.00
92.11
E

ATOM
9321
N
SER E
8
68.051
−14.055
71.282
1.00
92.25
E

ATOM
9322
CA
SER E
8
68.235
−15.467
70.933
1.00
92.14
E

ATOM
9323
CE
SER E
8
67.113
−15.896
69.981
1.00
92.25
E

ATOM
9324
OG
SER E
8
66.978
−17.305
69.938
1.00
92.67
E

ATOM
9325
C
SER E
8
69.603
−15.640
70.258
1.00
92.02
E

ATOM
9326
O
SER E
8
70.638
−15.398
70.879
1.00
91.94
E

ATOM
9327
N
GLY E
9
69.602
−16.057
68.994
1.00
91.78
E

ATOM
9328
CA
GLY E
9
70.854
−16.235
68.277
1.00
91.39
E

ATOM
9329
C
GLY E
9
70.848
−15.537
66.928
1.00
91.23
E

ATOM
9330
O
GLY E
9
69.743
−15.212
66.445
1.00
90.99
E

ATOM
9331
OXT
GLY E
9
71.939
−15.322
66.346
1.00
90.21
E

ATOM
9332
CE
LEU F
2
137.489
−5.702
48.818
1.00
79.71
F

ATOM
9333
CG
LEU F
2
138.842
−5.743
49.546
1.00
80.18
F

ATOM
9334
CD1
LEU F
2
139.667
−4.549
49.099
1.00
79.66
F

ATOM
9335
CD2
LEU F
2
138.661
−5.730
51.075
1.00
78.72
F

ATOM
9336
C
LEU F
2
138.487
−6.493
46.630
1.00
78.95
F

ATOM
9337
O
LEU F
2
138.336
−7.720
46.632
1.00
77.64
F

ATOM
9338
N
LEU F
2
136.056
−5.715
46.790
1.00
79.28
F

ATOM
9339
CA
LEU F
2
137.454
−5.545
47.286
1.00
79.36
F

ATOM
9340
N
LEU F
3
139.520
−5.871
46.060
1.00
78.25
F

ATOM
9341
CA
LEU F
3
140.670
−6.502
45.403
1.00
76.54
F

ATOM
9342
CB
LEU F
3
140.433
−6.740
43.915
1.00
77.32
F

ATOM
9343
CG
LEU F
3
139.459
−7.802
43.429
1.00
78.88
F

ATOM
9344
CD1
LEU F
3
138.100
−7.190
43.081
1.00
80.14
F

ATOM
9345
CD2
LEU F
3
140.065
−8.449
42.204
1.00
78.71
F

ATOM
9346
C
LEU F
3
141.723
−5.415
45.530
1.00
75.20
F

ATOM
9347
O
LEU F
3
141.444
−4.264
45.195
1.00
75.82
F

ATOM
9348
N
TPO F
4
142.936
−5.746
46.012
1.00
72.87
F

ATOM
9349
CA
TPO F
4
144.008
−4.734
46.163
1.00
70.82
F

ATOM
9350
CB
TPO F
4
144.161
−4.534
47.709
1.00
68.53
F

ATOM
9351
CG2
TPO F
4
145.393
−3.748
48.146
1.00
70.46
F

ATOM
9352
OG1
TPO F
4
142.965
−3.903
48.203
1.00
65.51
F

ATOM
9353
P
TPO F
4
142.778
−2.260
48.081
1.00
60.19
F

ATOM
9354
O1P
TPO F
4
142.871
−1.889
46.565
1.00
64.16
F

ATOM
9355
O2P
TPO F
4
143.905
−1.501
48.889
1.00
62.63
F

ATOM
9356
O3P
TPO F
4
141.319
−1.975
48.672
1.00
64.49
F

ATOM
9357
C
TPO F
4
145.311
−5.244
45.579
1.00
70.94
F

ATOM
9358
O
TPO F
4
145.629
−6.541
45.562
1.00
71.31
F

ATOM
9359
N
PRO F
5
146.116
−4.278
45.081
1.00
71.04
F

ATOM
9360
CD
PRO F
5
145.651
−2.886
44.895
1.00
69.22
F

ATOM
9361
CA
PRO F
5
147.434
−4.439
44.468
1.00
71.37
F

ATOM
9362
CB
PRO F
5
147.722
−3.051
43.898
1.00
70.57
F

ATOM
9363
CG
PRO F
5
146.379
−2.473
43.673
1.00
68.58
F

ATOM
9364
C
PRO F
5
148.447
−4.823
45.533
1.00
72.63
F

ATOM
9365
O
PRO F
5
148.273
−4.524
46.709
1.00
72.26
F

ATOM
9366
N
PRO F
6
149.531
−5.484
45.133
1.00
74.58
F

ATOM
9367
CD
PRO F
6
149.883
−5.888
43.760
1.00
74.65
F

ATOM
9368
CA
PRO F
6
150.563
−5.898
46.087
1.00
76.44
F

ATOM
9369
CB
PRO F
6
151.636
−6.499
45.180
1.00
76.17
F

ATOM
9370
CG
PRO F
6
150.843
−7.015
44.005
1.00
75.36
F

ATOM
9371
C
PRO F
6
151.108
−4.721
46.907
1.00
78.12
F

ATOM
9372
O
PRO F
6
151.745
−3.827
46.351
1.00
78.87
F

ATOM
9373
N
GLN F
7
150.858
−4.699
48.213
1.00
79.62
F

ATOM
9374
CA
GLN F
7
151.397
−3.605
49.020
1.00
81.37
F

ATOM
9375
CB
GLN F
7
150.607
−3.435
50.333
1.00
81.68
F

ATOM
9376
CG
GLN F
7
151.014
−2.213
51.171
1.00
82.68
F

ATOM
9377
CD
GLN F
7
150.936
−0.896
50.397
1.00
83.36
F

ATOM
9378
OE1
GLN F
7
151.562
−0.740
49.343
1.00
84.22
F

ATOM
9379
NE2
GLN F
7
150.175
0.061
50.927
1.00
82.82
F

ATOM
9380
C
GLN F
7
152.866
−3.939
49.299
1.00
82.45
F

ATOM
9381
O
GLN F
7
153.186
−4.607
50.282
1.00
82.78
F

ATOM
9382
N
SER F
8
153.745
−3.472
48.411
1.00
83.82
F

ATOM
9383
CA
SER F
8
155.196
−3.704
48.479
1.00
85.47
F

ATOM
9384
CB
SER F
8
155.937
−2.583
47.732
1.00
84.24
F

ATOM
9385
OG
SER F
8
155.277
−2.236
46.527
1.00
83.28
F

ATOM
9386
C
SER F
8
155.813
−3.857
49.887
1.00
86.86
F

ATOM
9387
O
SER F
8
156.285
−2.881
50.482
1.00
87.36
F

ATOM
9388
N
GLY F
9
155.830
−5.093
50.390
1.00
87.52
F

ATOM
9389
CA
GLY F
9
156.387
−5.374
51.708
1.00
87.82
F

ATOM
9390
C
GLY F
9
155.445
−6.117
52.646
1.00
87.94
F

ATOM
9391
O
GLY F
9
154.243
−6.240
52.319
1.00
88.07
F

ATOM
9392
OXT
GLY F
9
155.901
−6.573
53.717
1.00
87.76
F

END

[0525]

8

TABLE 7

Oligonucleotides used in Example 2

MTO#
Oligo name
Sequence

MTO 1146
LP6DelA-FWD
gccttcgcgaactgatgtacactttgcagggtcatacagc

MTO 1147
LP6DelA-REV
gccttggccattttctagatcccaaattctaatagtggtatccatac

MTO 1254
CDC4-BNSH-F
gtaggatccatatgggcgccgcaagctttcccttagctgagtttcc

MTO 1367
V384N-C
catatgacgagtaatattacgtgcttgc

MTO 1368
V384N3
caagcacgtaatattactcgtcatatg

MTO 1369
K402A-C
ggggctgatgacgcaatgatcagag

MTO 1370
K402A-N
ctctgatcattgcgtcatcagcccc

MTO 1371
W426A 5′
gatggtggggttgcggcgctgaagtatgcccatg

MTO 1372
DN426A
catgggcatacttcagcgccgcaaccccaccatc

MTO 1373
R443D-C
ggttctacagacgacacggtccgagtttggg

MTO 1374
R443D
tatcccaaactcggaccgtgtcgtcgtctgtagaaccg

MTO 1375
Y548F
cagtgtattatcaaagcttccactaacgac

MTO 1376
Y548F-C
gtcgttagtggaagctttgataatacactg

MTO 1377
Y574F-N
gtagattgtcgaaaatattcgatccgtatg

MTO 1378
Y574F-C
catacggatcgaatattttcgacaatctac

MTO 1379
W717N Hpa
ttgcccttaaagttaaccgagttaatctgatcag

MTO 1380
W717N-C
ctgatcagattaactcggttaactttaagggcaa

MTO 1381
2Flex359 5′
tcttttctggagcccgggccaattttaaaaaattggtac

MTO 1382
2Flex359 3′
gtaccaattttttaaaattggcccgggctccagaaaaga

MTO 1383
H5 Dest 5′
ggttttaattctctcggcccgggaccctcccaaaaatacccaaaactc

MTO 1384
H5 Dest 3′
gagttttgggtatttttgggagggtcccgggccgagagaattaaaacc

MTO 1385
H5 del 5′
gtgagcccaaagggtccaaagctttcacaacaagatcgc

MTO 1386
H5 del 3′
gcgatcttgttgtgaaagctttggaccctttgggctcac

MTO 1387
H5 + Dest 5′
gtggaaaaaacttctgatattcattttaaaaaattggtacaatcc

MTO 1388
H5 + Dest 3′
ggattgtaccaattttttaaaatgaatatcagaagttttttccac

MTO 1389
Ala1-3
ccaattttttaaaatgaatgcaatattctccagaaaag

MTO 1390
Ala2-3
ccaattttttaaaatgaatgctgcaatattctccagaaaag

MTO 1391
Ala3-3
ccaatttttttaaaatgaaagcggctgcaatattctccagaaaag

MTO 1392
Ala4-3
ccaattttttaaaatgaaggctgcagctgcaatattctccagaaaag

MTO 1393
Ala8 5′
gccgcgcgcgctaaagctgcagcgttcattttaaaaaattggtacaatcc

MTO 1394
Ala8 3′
cgctgcagctttagcgcgcgcggctatattctccagaaaagataatc

MTO 1395
Ala12 5′
gccgcgcgcgctaaagctgcagcgcgcgcgaaagccttcattttaaaaaattggtacaatcc

MTO 1396
Al12 3′
ggctttcgcgcgcgctgcagctttagcgcgcgcggctatattctccagaaaagataatc

[0526]

9

TABLE 8

Plasmids used in Example 2

Plasmid
Relevant Characteristic
Source

pMT 3169
pProEx Hta-CDC4 LP6DelA GST-Skp1
This study

pMT 3055
pProEx Hta-CDC4 263-744 GST-Skp1
Nash et. al.

pMT 3000
pProEx Hta-CDC4 1-744 GST-Skp1
This study

pMT 3217
pRS 314 CDC4-BNSH/Eco
This study

pMT 3001
pMT 3055 V384N
This study

pMT 3002
pMT 3055 K402A
This study

pMT 3385
pMT 3055 W426A
This study

pMT 3058
pMT 3055 R443A
Nash et. al

pMT 3003
pMT 3055 R443D
This study

pMT 3059
pMT 3055 R467A
Nash et. al

pMT 3060
pMT 3055 R485A
Nash et. al

pMT 3061
pMT 3055 R534A
Nash et. al

pMT 3004
pMT 3055 Y548F
This study

pMT 3005
pMT 3055 Y574F
This study

pMT 3006
pMT 3055 W717N
This study

pMT 3007
pMT 3055 V384N + W717N
This study

pMT 3008
pMT 3055 K402 + R443D
This study

pMT 3010
pMT 3000 R443D
This study

pMT 3011
pMT 3000 R443A
This study

pMT 3012
pMT 3000 W717N
This study

pMT 3013
pMT 3000 K402A + R443D
This study

pMT 3014
pMT 3000 V384N + W717N
This study

pMT 3015
pMT 3217 V384N
This study

pMT 3016
pMT 3217 K402A
This study

pMT 3386
pMT 3217 W426A
This study

pMT 3017
pMT 3217 R443D
This study

pMT 3058
PRS 314-CDC4 R443A
Nash et. al.

pMT 3018
pMT 3217 Y548F
This study

pMT 3068
PRS 314-CDC4 R572A
Nash et. al

pMT 3019
pMT 3217 Y574F
This study

pMT 3020
pMT 3217 W717N
This study

pMT 3021
pMT 3217 V384N + W717N
This study

pMT 3022
pMT 3217 K402A + R443D
This study

pMT 3024
pMT 3000 Helix 5 Δ 330-443
This study

pMT 3025
pMT 3000 Helix 5 breaker
This study

pMT 3026
pMT 3000 Helix 5 Δ 321-360
This study

pMT 3027
pMT 3000 Helix 6 breaker
This study

pMT 3028
pMT 3000 Ala1 insert
This study

pMT 3029
pMT 3000 Ala2 insert
This study

pMT 3030
pMT 3000 Ala3 insert
This study

pMT 3031
pMT 3000 Ala4 insert
This study

pMT 3032
pMT 3000 Ala8 insert
This study

pMT 3033
pMT 3000 Ala12 insert
This study

pMT 3034
pMT 3217 Helix 5 Δ 330-443
This study

pMT 3035
pMT 3217 Helix 5 breaker
This study

pMT 3036
pMT 3217 Helix 5 Δ 321-360
This study

pMT 3037
pMT 3217 Helix 6 breaker
This study

pMT 3038
pMT 3217 Ala1 insert
This study

pMT 3039
pMT 3217 Ala2 insert
This study

pMT 3040
pMT 3217 Ala3 insert
This study

pMT 3041
pMT 3217 Ala4 insert
This study

pMT 3042
pMT 3217 Ala8 insert
This study

pMT 3043
pMT 3217 Ala12 insert
This study

pMT 1571
Pet16b-Sic1
Previous study

MDM 152
pGALl1 SIC1 LEU2 CEN ARS
M. Mendenhall

MDM202
pGAL1 SIC1T33V LEU2 CEN ARS
M. Mendenhall

LIST OF REFERENCES

[0527] 1. Amati, B., and Vlach, J. (1999). Kip1 meets SKP2: new links in cell-cycle control [news], Nat Cell Biol 1, E91-3.

[0528] 2. Bai, C., Sen, P., Hofmann, K., Ma, L., Goebl, M., Harper, J. W., and Elledge, S. J. (1996). SKP1 connects cell cycle regulators to the ubiquitin proteolysis machinery through a novel motif, the F-box, Cell 86, 263-74.

[0529] 3. Brunger, A. T., Adams, P. D., Clore, G. M., Gros, P., Grosse-Kuntsleve, Jiang, R. W., Kuszewski, J., Nilges, M., Pannu, N. S., Read, R. J., and al., e. (1998). Crystallography and NMR system: a new software suite for macromolecular structure determination. Acta Cryst. D54, 905-921.

[0530] 4. Carson, M. (1991). Ribbons 2.0. J. Appl. Crystallgr. 24, 958-961.

[0531] 5. Chi, Y., Huddleston, M. J., Zhang, X., Young, R. A., Annan, R. S., Carr, S. A., and Deshaies, R. J. (2001). Negative regulation of Gcn4 and Msn2 transcription factors by Srb10 cyclin-dependent kinase. Genes. Dev. 15, 1078-1092.

[0532] 6. Cohen, P. (2000). The regulation of protein function by multisite phosphorylation: a 25 year update. Trends Biochem. Sci. 25, 596-601.

[0533] 7. de La Fortelle, E., and Bricogne, G. (1997). Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods. Methods Enzymol. 276, 472-494.

[0534] 8. Deshaies, R. J. (1999). SCF and Cullin/Ring H2-based ubiquitin ligases, Annu Rev Cell Dev Biol 15, 435-67.

[0535] 9. Deshaies, R. J., and Ferrell, J. E., Jr. (2001). Multisite phosphorylation and the countdown to S phase, Cell 107, 819-22.

[0536] 10. Drury, L. S., Perkins, G., and Diffley, J. F. (1997). The Cdc4/34/53 pathway targets Cdc6p for proteolysis in budding yeast, Embo J 16, 5966-76.

[0537] 11. Eck, M. J., Pluskey, S., Trub, T., Harrison, S. C., and Shoelson, S. E. (1996). Spatial constraints on the recognition of phosphoproteins by the tandem SH2 domains of the phosphatase SH-PTP2, Nature 379, 277-80.

[0538] 12. Endicott, J. A., Noble, M. E., and Tucker, J. A. (1999). Cyclin-dependent kinases: inhibition and substrate recognition. Curr. Opin. Struct. Biol. 9, 738-744.

[0539] 13. Feldman, R. M., Correll, C. C., Kaplan, K. B., and Deshaies, R. J. (1997). A complex of Cdc4p, Skp1p, and Cdc53p/cullin catalyzes ubiquitination of the phosphorylated CDK inhibitor Sic1p, Cell 91, 221-30.

[0540] 14. Ferrell, J. E. (1996). Tripping the switch fantastic: how a protein kinase cascade can convert graded inputs into switch-like outputs, Trends Biochem Sci 21, 460-466.

[0541] 15. Fulop, V., and Jones, D. T. (1999). Beta propellers: structural rigidity and functional diversity, Curr Opin Struct Biol 9, 715-721.

[0542] 16. Gstaiger, M., Jordan, R., Lim, M., Catzavelos, C., Mestan, J., Slingerland, J., and Krek, W. (2001). Skp2 is oncogenic and overexpressed in human cancers, Proc Natl Acad Sci USA 98, 5043-8.

[0543] 17. Gupta-Rossi, N., Le Bail, O., Gonen, H., Brou, C., Logeat, F., Six, E., Ciechanover, A., and Israel, A. (2002). Functional interaction between SEL-10, an F-box protein, and the nuclear form of activated Notch1 receptor, J Biol Chem 276, 34371-34378.

[0544] 18. Hamilton, K. S., Ellison, M. J., Barber, K. R., Williams, R. S., Huzil, J. T., McKenna, S., Ptak, C., Glover, M., and Shaw, G. S. (2001). Structure of a conjugating enzyme-ubiquitin thiolester intermediate reveals a novel role for the ubiquitin tail. Structure 9, 897-904.

[0545] 19. Harper, J. W. (2001). Protein destruction: adapting roles for Cks proteins. Curr Biol 11, R431-435.

[0546] 20. Harper, J. W. (2002). A phosphorylation-driven ubiquitination switch for cell-cycle control, Trends Cell Biol 12, 104-7.

[0547] 21. Hershko, A., and Ciechanover, A. (1998). The ubiquitin system, Annu Rev Biochem 67, 425-79.

[0548] 22. Hershko, D., Bornstein, G., Ben-Izhak, O., Carrano, A., Pagano, M., Krausz, M. M., and Hershko, A. (2001). Inverse relation between levels of p27(Kip1) and of its ubiquitin ligase subunit Skp2 in colorectal carcinomas, Cancer 91, 1745-51.

[0549] 23. Hsiung, Y. G., Chang, H. C., Pellequer, J. L., La Valle, R., Lanker, S., and Wittenberg, C. (2001). F-box protein Grr1 interacts with phosphorylated targets via the cationic surface of its leucine-rich repeat, Mol Cell Biol 21, 2506-20.

[0550] 24. Huang, L., Kinnucan, E., Wang, G., Beaudenon, S., Howley, P. M., Huibregtse, J. M., and Pavletich, N. P. (1999). Structure of an E6AP-UbCH7 complex: insights into ubiquitination by the E2-E3 enzyme cascade, Science 286, 1321-6.

[0551] 25. Hubbard, E. J., Wu, G., Kitajewski, J., and Greenwald, I. (1997). sel-10, a negative regulator of lin-12 activity in Caenorhabditis elegans, encodes a member of the CDC4 family of proteins, Genes Dev 11, 3182-93.

[0552] 26. Jones, T. A., Zou, J. Y., Cowan, S. W., and Kjeldgaard, M. (1991). Improved methods for binding protein models in electron density maps and the localization of errors in these models. Acta Cryst. A47, 110-119.

[0553] 27. Kaelin, W. G., Jr. (2002). Molecular basis of the VHL hereditary cancer syndrome. Nat. Rev. Cancer 2, 673-682.

[0554] 28. Keyomarsi, K., Tucker, S. L., Buchholz, T. A., Callister, M., Ding, Y., Hortobagyi, G. N., Bedrosian, I., Knickerbocker, C., Toyofuku, W., Lowe, M., et al. (2002). Cyclin E and survival in patients with breast cancer. N. Engl. J. Med. 347, 1566-1575.

[0555] 29. Koepp, D. M., Harper, J. W., and Elledge, S. J. (1999). How the cyclin became a cyclin: regulated proteolysis in the cell cycle, Cell 97, 431-4.

[0556] 30. Koepp, D. M., Schaefer, L. K., Ye, X., Keyomarsi, K., Chu, C., Harper, J. W., and Elledge, S. J. (2001). Phosphorylation-dependent ubiquitination of cyclin E by the SCFFbw7 ubiquitin ligase, Science 294, 173-7.

[0557] 31. Kominami, K., Ochotorena, I., and Toda, T. (1998). Two F-box/WD-repeat proteins Pop1 and Pop2 form hetero- and homo-complexes together with cullin-1 in the fission yeast SCF (Skp1-Cullin-1-F-box) ubiquitin ligase, Genes Cells 3, 721-35.

[0558] 32. Lai, E. C. (2002). Protein degradation: four E3s for the notch pathway. Curr. Biol. 12, R74-78.

[0559] 33. Lanker, S., Valdivieso, M. H., and Wittenberg, C. (1996). Rapid degradation of the G1 cyclin Cln2 induced by CDK-dependent phosphorylation, Science 271, 1597-601.

[0560] 34. Lai, E. C. (2002). Protein degradation: four E3s for the notch pathway. Curr. Biol. 12, R74-78.

[0561] 35. Lengronne, A., and Schwob, E. (2002). The yeast CDK inhibitor Sic1 prevents genomic instability by promoting replication origin licensing in late G1. Mol. Cell. 9, 1067-1078.

[0562] 36. Mammen, M., Choi, S.-K., and Whitesides, G. M. (1998). Polyvalent interactions in biological systems: implications for design and use of multivalent ligands and inhibitors. Angew. Chem. 37, 2754-2794.

[0563] 37. Maniatis, T. (1999). A ubiquitin ligase complex essential for the NF-kappaB, Wnt/Wingless, and hedgehog signaling pathways, Genes Dev 13, 505-510.

[0564] 38. Margottin, F., Bour, S. P., Durand, H., Selig, L., Benichou, S., Richard, V., Thomas, D., Strebel, K., and Benarous, R. (1998). A novel human WD protein, h-beta TrCp, that interacts with HIV-1 Vpu connects CD4 to the ER degradation pathway through an F-box motif, Mol Cell 1, 565-74.

[0565] 39. Meimoun, A., Holtzman, T., Weissman, Z., McBride, H. J., Stillman, D. J., Fink, G. R., and Kornitzer, D. (2000). Degradation of the transcription factor Gcn4 requires the kinase Pho85 and the SCFCDC4 ubiquitin-ligase complex. Mol. Biol. Cell. 11, 915-927.

[0566] 40. Miller, R., Gallo, S. M., Khalak, H. G., and Weeks, C. M. (1994). SnB: crystal structure determination via Shake-and-Bake. J. Appl. Crystallgr. 27, 613-621.

[0567] 41. Moberg, K. H., Bell, D. W., Wahrer, D. C., Haber, D. A., and Hariharan, I. K. (2001). Archipelago regulates Cyclin E levels in Drosophila and is mutated in human cancer cell lines, Nature 413, 311-6.

[0568] 42. Nash, P., Tang, X., Orlicky, S., Chen, Q., Gertler, F. B., Mendenhall, M. D., Sicheri, F., Pawson, T., and Tyers, M. (2001). Multisite phosphorylation of a CDK inhibitor sets a threshold for the onset of DNA replication, Nature 414, 514-21.

[0569] 43. Nicholls, A., Sharp, K. A., and Honig, B. (1991). Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins Struct. Funct. Genet. 11, 281-296.

[0570] 44. Nugroho, T. T., and Mendenhall, M. D. (1994). An inhibitor of yeast cyclin-dependent protein kinase plays an important role in ensuring the genomic integrity of daughter cells, Mol Cell Biol 14, 3320-3328.

[0571] 45. Otwinowski, Z., and Minor, W. (1997). Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326.

[0572] 46. Patton, E. E., Willems, A. R., and Tyers, M. (1998). Combinatorial control in ubiquitin-dependent proteolysis: don't Skp the F-box hypothesis, Trends Genet 14, 236-43.

[0573] 47. Pawson, T., and Nash, P. (2000). Protein-protein interactions define specificity in signal transduction., Genes Dev 14, 1027-47.

[0574] 48. Pickart, C. M. (2001). Mechanisms underlying ubiquitination, Annu Rev Biochem 70, 503-33.

[0575] 49. Sakamoto, K. M., Kim, K. B., Kumagai, A., Mercurio, F., Crews, C. M., and Deshaies, R. J. (2001). Protacs: chimeric molecules that target proteins to the Skp1-Cullin-F box complex for ubiquitination and degradation, Proc Natl Acad Sci USA 98, 8554-9.

[0576] 50. Schneider, B. L., Yang, Q. H., and Futcher, A. B. (1996). Linkage of replication to start by the Cdk inhibitor Sic1, Science 272, 560-2.

[0577] 51. Schulman, B. A., Carrano, A. C., Jeffrey, P. D., Bowen, Z., Kinnucan, E. R., Finnin, M. S., Elledge, S. J., Harper, J. W., Pagano, M., and Pavletich, N. P. (2000). Insights into SCF ubiquitin ligases from the structure of the Skp1-Skp2 complex, Nature 408, 381-6.

[0578] 52. Schwob, E., Bohm, T., Mendenhall, M. D., and Nasmyth, K. (1994). The B-type cyclin kinase inhibitor p40SIC1 controls the G1 to S transition in S. cerevisiae, Cell 79, 233-44.

[0579] 53. Selkoe, D. J. (2001). Presenilin, Notch, and the genesis and treatment of Alzheimer's disease, Proc Natl Acad Sci USA 98, 11039-41.

[0580] 54. Signoretti, S., Di Marcotulio, L., Richardson, A., Ramaswamy, S., Isaac, B., Rue, M., Monti, F., Loda, M., and Pagano, M. (2002). Oncogenic role of the ubiquitin ligase subunit Skp2 in human breast cancer, J Clin Invest 110, 633-41.

[0581] 55. Skowyra, D., Craig, K. L., Tyers, M., Elledge, S. J., and Harper, J. W. (1997). F-box proteins are receptors that recruit phosphorylated substrates to the SCF ubiquitin-ligase complex, Cell 91, 209-19.

[0582] 56. Sprague, E. R., Redd, M. J., Johnson, A. D., and Wolberger, C. (2000). Structure of the C-terminal domain of Tup1, a corepressor of transcription in yeast, Embo J 19, 3016-27.

[0583] 57. Spruck, C. H., Strohmaier, H., Sangfelt, O., Muller, H. M., Hubalek, M., Muller-Holzner, E., Marth, C., Widschwendter, M., and Reed, S. 1. (2002). hCDC4 gene mutations in endometrial cancer, Cancer Res 62, 4535-9.

[0584] 58. Spruck, C. H., Won, K. A., and Reed, S. I. (1999). Deregulated cyclin E induces chromosome instability, Nature 401, 297-300.

[0585] 59. Strohmaier, H., Spruck, C. H., Kaiser, P., Won, K. A., Sangfelt, O., and Reed, S. I. (2001). Human F-box protein hCdc4 targets cyclin E for proteolysis and is mutated in a breast cancer cell line, Nature 413, 316-22.

[0586] 60. Suzuki, H., Chiba, T., Suzuki, T., Fujita, T., Ikenoue, T., Omata, M., Furuichi, K., Shikama, H., and Tanaka, K. (2000). Homodimer of two F-box proteins beta TrCP1 or betaTrCP2 binds to IkappaBalpha for signal-dependent ubiquitination, J Biol Chem 275, 2877-84.

[0587] 61. ter Haar, E., Harrison, S. C., and Kirchhausen, T. (2000). Peptide-in-groove interactions link target proteins to the beta-propeller of clathrin., Proc Natl Acad Sci USA 97, 1096-100.

[0588] 62. Tong, A. H., Evangelista, M., Parsons, A. B., Xu, H., Bader, G. D., Page, N., Robinson, M., Raghibizadeh, S., Hogue, C. W., Bussey, H., et al. (2001). Systematic genetic analysis with ordered arrays of yeast deletion mutants, Science 294, 2364-8.

[0589] 63. Tyers, M., and Jorgensen, P. (2000). Proteolysis and the cell cycle: with this RING I do thee destroy, Curr Opin Genet Dev 10, 54-64.

[0590] 64. Varshavsky, A. (1991). Naming a targeting signal, Cell 64, 13-5.

[0591] 65. Verdecia, M. A., Bowman, M. E., Lu, K. P., Hunter, T., and Noel, J. P. (2000). Structural basis for phosphoserine-proline recognition by group IV WW domains. Nat. Struct. Biol. 7, 639-643.

[0592] 66. Verma, R., Annan, R. S., Huddleston, M. J., Carr, S. A., Reynard, G., and Deshaies, R. J. (1997). Phosphorylation of Sic1p by G1 Cdk required for its degradation and entry into S phase, Science 278, 455-460.

[0593] 67. Wall, M. A., Coleman, D. E., Lee, E. I.-L., J. A., Posner, B. A., Gilman, A. G., and Sprang, S. R. (1995). The structure of the G protein heterotrimer G1 alpha 1 beta 1 gamma 2, Cell 83, 1047-58.

[0594] 68. Wolf, D. A., McKeon, F., and Jackson, P. K. (1999). F-box/WD-repeat proteins Pop1p and Sud1p/Pop2p form complexes that bind and direct the proteolysis of Cdcl8p. Curr. Biol. 9, 373-376.

[0595] 69. Wu, G., Hubbard, E. J., Kitajewski, J. K., and Greenwald, I. (1998). Evidence for functional and physical association between Caenorhabditis elegans SEL-10, a Cdc4p-related protein, and SEL-12 presenilin., Proc Natl Acad Sci USA 95, 15787-15891.

[0596] 70. Wu, G., Lyapina, S., Das, I., Li, J., Gurney, M., Pauley, A., Chui, I., Deshaies, R. J., and Kitajewski, J. (2001). SEL-10 is an inhibitor of notch signaling that targets notch for ubiquitin-mediated protein degradation, Mol Cell Biol 21, 7403-15.

[0597] 71. Yaffe, M. B., and Elia, A. E. (2001). Phosphoserine/threonine-binding domains, Curr Opin Cell Biol 13, 131-8.

[0598] 72. Yaffe, M. B., Rittinger, K., Volinia, S., Caron, P. R., Aitken, A., Leffers, H., Gamblin, S. J., Smerdon, S. J., and Cantley, L. C. (1997). The structural basis for 14-3-3:phosphopeptide binding specificity, Cell 91, 961-71.

[0599] 73. Zachariae, W., and Nasmyth, K. (1999). Whose end is destruction: cell division and the anaphase-promoting complex, Genes Dev 13, 2039-58.

[0600] 74. Zheng, N., Schulman, B. A., Song, L., Miller, J. J., Jeffrey, P. D., Wang, P., Chu, C., Koepp, D. M., Elledge, S. J., Pagano, M., et al. (2002). Structure of the Cull-Rbx1-Skp1-F boxSkp2 SCF ubiquitin ligase complex, Nature 416, 703-9.

[0601] 75. Zheng, N., Wang, P., Jeffrey, P. D., and Pavletich, N. P. (2000). Structure of a c-Cb1-UbCH7 complex: RING domain function in ubiquitin-protein ligases, Cell 102, 533-9.

Structures of substrate binding pockets of SCF complexes

Information

Publication Number

Date Filed

Date Published

Inventors

Original Assignees

CPC

US Classifications

International Classifications

Abstract

Description

Claims

Provisional Applications (1)