# Patent

## Title
Design of progesterone receptor ligands

## Abstract

This invention relates to progesterone receptor/ligand complex, and related methods and software systems. Methods for designing and/or selecting ligands of the progesterone receptor using the three-dimensional structural coordinates of the progesterone receptor and/or nonsteroidal ligands are disclosed.

## Background
RELATED APPLICATIONS
This application claims the benefit of U.S. Provisional Application No. 60/603,242, filed Aug. 20, 2004, which is incorporated herein by reference in its entirety


TECHNICAL FIELD
This invention relates to progesterone receptor/ligand complexes, and related methods and software systems.
BACKGROUND
Progesterone is a steroidal hormone that regulates many biological processes. Many of the physiological effects of progesterone are mediated by progesterone receptors (PRs). Interaction of progesterone with progesterone receptor can cause activation of the receptor. This can cause the progesterone receptor to be transported from the cytoplasm into the nucleus. In the nucleus, the progesterone receptor can function as a transcriptional activator, which can cause increased expression of specific gene targets.
SUMMARY
In general, the invention relates to crystalline protein/ligand complexes that include a PR polypeptide bound to a non-steroidal ligand. The PR polypeptide can include the ligand binding domain of the PR, and the non-steroidal ligand can be an agonist or antagonist of the receptor. The invention also relates to methods of using a three-dimensional model of a PR polypeptide/non-steroidal ligand complex to design an agent, such as an agonist or antagonist, that can interact with a PR polypeptide. The invention also features related software methods.
In one aspect, the invention features a crystallized protein-ligand complex that includes a progesterone receptor polypeptide and a non-steroidal ligand. The non-steroidal ligand is an agonist or antagonist of the progesterone receptor polypeptide.
In another aspect, the invention features a crystallized protein-ligand complex that includes a progesterone receptor polypeptide, which includes the amino acid sequence of SEQ ID NO:2, and a non-steroidal ligand. The crystallized protein-ligand complex diffracts X-rays to a resolution of at least about 3.5 Å. The non-steroidal ligand is an agonist or antagonist of the progesterone receptor polypeptide.
In another aspect, the invention features a composition that includes a crystal, which includes a progesterone receptor polypeptide and a non-steroidal ligand. The non-steroidal ligand is an agonist or antagonist of the progesterone receptor polypeptide.
In yet another aspect, the invention features a method that includes using a three-dimensional model to design an agent that interacts with a progesterone receptor polypeptide. The three-dimensional model includes the progesterone receptor polypeptide bound to a non-steroidal ligand that is an agonist or antagonist of the receptor polypeptide.
Another aspect of the invention features a method that includes selecting an agent by performing rational drug design with a three-dimensional structure of a crystalline complex. The complex includes a progesterone receptor polypeptide bound to a non-steroidal ligand that is an agonist or antagonist of the receptor polypeptide, and the method includes contacting the agent with a receptor polypeptide and detecting the ability of the agent to bind the polypeptide.
In another aspect, the invention features a method of growing a crystal that includes a progesterone receptor polypeptide and a non-steroidal ligand that is an agonist or antagonist of the polypeptide. The method includes contacting the receptor polypeptide with the non-steroidal ligand, and the resulting crystal can diffract X-rays to a resolution of at least about 3.5 Å.
Another aspect of the invention features a software system for determining binding characteristics of a candidate agent to a progesterone receptor polypeptide. The software system includes instructions for causing a computer system to accept information relating to the structure of a progesterone receptor polypeptide bound to a non-steroidal ligand that is an agonist or antagonist of the progesterone receptor polypeptide, and to accept information relating to a candidate agent. The determination of binding characteristics is based on the information relating to the structure of the receptor polypeptide and the information relating to the candidate agent.
Another aspect of the invention features a computer program for determining the binding characteristics of a candidate agent to a progesterone receptor polypeptide. The computer program resides on a computer readable medium that includes a plurality of instructions. When executed by one or more processors, the plurality of instructions causes the one or more processors to accept information relating to the structure of a progesterone receptor polypeptide bound to a non-steroidal ligand that is an agonist or antagonist of the progesterone receptor polypeptide, and to accept information relating to a candidate agent. The determination of binding characteristics is based on the information relating to the structure of the receptor polypeptide and the information relating to the candidate agent.
In another aspect, the invention features a method for modeling the binding characteristics of a progesterone receptor polypeptide with a candidate agent. The method includes a software system that models the binding characteristics by accepting information relating to the structure of a progesterone receptor polypeptide bound to a non-steroidal ligand that is an agonist or antagonist of the progesterone receptor polypeptide.
In yet another aspect, the invention features a computer program for modeling the binding characteristics of a progesterone receptor polypeptide with a candidate agent. The computer program resides on a computer readable medium on which is stored a plurality of instructions. When the instructions are executed by one or more processors, the processors accept information relating to the structure of a progesterone receptor polypeptide bound to a non-steroidal ligand that is an agonist or antagonist of the progesterone receptor polypeptide and the processors model the binding characteristics of the receptor polypeptide with the candidate agent.
In another aspect, the invention features a software system for modeling the binding characteristics of a progesterone receptor polypeptide with a candidate agent. The software system includes instructions for causing a computer system to accept information relating to the structure of a progesterone receptor polypeptide bound to a non-steroidal ligand that is an agonist or antagonist of the progesterone receptor polypeptide and to model the binding characteristics of the receptor polypeptide with a candidate agent.
Structural information of a polypeptide can lead to a greater understanding of how the polypeptide functions in vivo. For example, knowledge of the structure of a protein can reveal properties that facilitate the interaction of the protein with its ligands, including other proteins, effector molecules (e.g., hormones), and nucleic acids. In the case of a progesterone receptor, an understanding of such interactions can facilitate the design or selection of ligands (e.g., drugs) that can be useful for modulating the activity of the progesterone receptor in vivo, and can therefore be useful for treating a human. Structure based modeling can be used to identify ligands capable of interacting with a PR polypeptide, thus eliminating the need for screening assays, which can be expensive and time-consuming. Structural information can also be used to direct the modification of a ligand known to interact with a PR polypeptide to generate an alternative ligand with more desirable properties, such as tighter binding or greater specificity.
Unless otherwise defined, all technical and scientific terms used herein have the same meaning as commonly understood by one of ordinary skill in the art to which this invention pertains. Although methods and materials similar or equivalent to those described herein can be used in the practice or testing of the present invention, useful methods and materials are described below. The materials, methods, and examples are illustrative only and not intended to be limiting. Other features and advantages of the invention will be apparent from the accompanying drawings and description, and from the claims. The contents of all references, pending patent applications and published patents, cited throughout this application are hereby expressly incorporated by reference. In case of conflict, the present specification, including definitions, will control.



DESCRIPTION OF DRAWINGS
FIG. 1A is an electron density map showing tanaproget bound to the human PR-LBD. The A, B, and C rings of tanaproget are as designated. The benzoxazine moiety of tanaproget is formed of rings B and C.
FIG. 1B is an electron density map showing tanaproget bound to the human PR-LBD.
FIG. 2A shows the amino acid sequence of the human progesterone receptor ligand binding domain (human PR-LBD) (sequence underlined) fused to glutathione-S-transferase (GST) (sequence not underlined) (SEQ ID NO:1). A thrombin cleavage site (LVPRG (SEQ ID NO:3), marked in bold) occurs at the junction between the GST and PR-LBD sequences.
FIG. 2B shows the amino acid sequence (SEQ ID NO:2) of the human PR-LBD. Amino acids are numbered according to the amino acid sequence of the full-length human progesterone receptor (see FIG. 2C).
FIG. 2C is the full-length sequence of human progesterone receptor (GenBank Accession Number NM—000926; SEQ ID NO:4). Amino acids of the human PR-LBD are underlined.



DETAILED DESCRIPTION
The structure of the human progesterone receptor ligand binding domain (PR-LBD) bound to the non-steroidal hormone tanaproget (IUPAC name: 5-(4,4-dimethyl-2-thioxo-1,4-dihydro-2H-3,1-benzoxazin-6-yl)-1-methyl-1H-pyrrole-2-carbonitrile; tanaproget is the United States Adopted Name (USAN)) was determined by X-ray crystallography and is described herein. FIGS. 1A and 1B are electron density maps illustrating the structure of the PR-LBD/tanaproget complex. The electron density maps provide evidence indicating that the tertiary structure of the human PR-LBD bound to tanaproget is very similar to that of the human PR-LBD bound to its natural ligand, progesterone. It is therefore believed that the crystal structure of the human PR-LBD/tanaproget complex (see Table 2 below) can be useful for designing or identifying other ligands, such as, for example, non-steroidal ligands, that can also interact with a PR-LBD.
FIGS. 2A and 2B provide information regarding the amino acid sequence of the human PR-LBD, and FIG. 2C provides information regarding the full length sequence of human PR.
The chemical structure of tanaproget is shown below:




In general, a complex of the human PR-LBD bound to tanaproget can be prepared as desired. In some embodiments, such a complex can be prepared as follows. The human PR-LBD is expressed from a DNA plasmid. The expression can be driven by a promoter, such as an inducible promoter. The human PR-LBD can be expressed as a fusion protein with a suitable tag, such as a glutathione-S-transferase (GST), myc, HA, hexahistidine (SEQ ID NO:5), or FLAG tag. The tag can facilitate isolation of the human PR-LBD from cells. A fusion protein can be cleaved at a protease site engineered into the fusion protein, such as at or near the site of fusion between the polypeptide and the tag. Following cleavage and purification, the human PR-LBD can be contacted with tanaproget. For example, the human PR-LBD can be mixed with tanaproget prior to purification (e.g., prior to cleavage of a polypeptide tag), or the human PR-LBD can be mixed with tanaproget after purification. In some embodiments, tanaproget can be mixed with the human PR-LBD prior to purification and again following purification.
The human PR-LBD and tanaproget can be combined in a solution for collecting spectral data for the human PR-LBD/tanaproget complex, NMR data for the human PR-LBD/tanaproget complex, or for growing a crystal of the human PR-LBD/tanaproget complex. For example, the human PR-LBD/tanaproget complex can be crystallized in the presence of a salt (e.g., a sodium salt), a polymer (e.g., polyethylene glycol (PEG)), and/or an organic solvent. Crystals can be grown by various methods, such as, for example, sitting or hanging drop vapor diffusion. In general, crystallization can be performed at a temperature of from about 4° C. to about 60° C. (e.g., from about 4° C. to about 45° C., such as at about 4° C., about 15° C., about 18° C., about 20° C., about 25° C., about 30° C., about 32° C., about 35° C., about 37° C.).
In general, a crystal of the human PR-LBD bound to tanaproget can diffract X-rays to a resolution of about 3.5 Å or less (e.g., about 3.2 Å or less, about 3.0 Å or less, about 2.5 Å or less, about 2.4 Å or less, about 2.3 Å or less, about 2.2 Å or less, about 2.1 Å or less, about 2.0 Å or less, about 1.9 Å or less, about 1.8 Å or less, about 1.7 Å or less, about 1.6 Å or less, about 1.5 Å or less, or about 1.4 Å or less). In some embodiments, a crystal of the human PR-LBD bound to tanaproget can diffract X-rays to a resolution of from about 1.6 Å to about 2.5 Å (e.g., from about 1.8 Å to about 2.2 Å).
In some embodiments, a crystal of the human PR-LBD bound to tanaproget belongs to space group P21 with unit cell parameters a=57.52 Å, b=64.50 Å, c=70.41 Å, and b=95.76°. In certain embodiments, a crystal of the human PR-LBD bound to tanaproget can further contain two molecules of the human PR-LBD in the asymmetric unit.
Structural data describing a crystal can be obtained, for example, by X-ray diffraction. X-ray diffraction data can be collected by a variety of sources, X-ray wavelengths and detectors. In some embodiments, rotating anodes and synchrotron sources (e.g., Advanced Light Source (ALS), Berkeley, Calif.; or Advanced Photon Source (APS), Argonne, Ill.) can be used as the source(s) of X-rays. In certain embodiments, X-rays for generating diffraction data can have a wavelength of from about 0.5 Å to about 1.6 Å (e.g., about 0.7 Å, about 0.9 Å, about 1.1 Å, about 1.3 Å, about 1.4 Å, about 1.5 Å, or about 1.6 Å). In some embodiments, area detectors and/or charge-couple devices (CCDs) can be used as the detector(s).
X-ray diffraction data of a crystal of a complex of the human PR-LBD bound to tanaproget can be used to obtain the structural coordinates of the atoms in the complex. The structural coordinates are Cartesian coordinates that describe the location of atoms in three-dimensional space in relation to other atoms in the complex. For example, the structural coordinates listed in Table 2 are the structural coordinates of a crystalline complex of the human PR-LBD bound to tanaproget. These structural coordinates describe the location of atoms of the human PR-LBD in relation to each other, the location of atoms in the human PR-LBD in relation to the atoms in tanaproget, and the location of atoms in tanaproget in relation to each other. The structural coordinates of the complex can be modified by mathematical manipulation, such as by inversion or integer additions or subtractions. As such, structural coordinates are relative coordinates. For example, structural coordinates describing the location of atoms in a PR-LBD bound to tanaproget are not specifically limited by the actual x, y, and z coordinates of Table 2.
The structural coordinates of a complex of the human PR-LBD bound to tanaproget can be used to derive a representation (e.g., a two dimensional representation or three dimensional representation) of the complex, a fragment of the complex, the PR-LBD or a fragment of the PR-LBD. Such a representation can be useful for a number of applications, including, for example, the visualization, identification and characterization of an active site of the polypeptide. In certain embodiments, a three-dimensional representation can include the structural coordinates of the human PR-LBD according to Table 2 ±a root mean square deviation from the alpha carbon atoms of amino acids of not more than about 1.5 Å (e.g., not more than about 1.0 Å, not more than about 0.5 Å). Root mean square deviation is the square root of the arithmetic mean of the squares of the deviations from the mean, and is a way of expressing deviation or variation from structural coordinates. Conservative substitutions (see discussion below) of amino acids can result in a molecular representation having structural coordinates within the stated root mean square deviation. For example, two molecular models of polypeptides that differ from one another by conservative amino acid substitutions can have coordinates of backbone atoms within a stated rms deviation, such as less than about 1.5 Å (e.g., less than about 1.0 Å, less than about 0.5 Å). Backbone atoms of a polypeptide include the alpha carbon (Cα or CA) atoms, carbonyl carbon (C) atoms, and amide nitrogen (N) atoms.
Various software programs allow for the graphical representation of a set of structural coordinates to obtain a representation of a complex of the human PR-LBD bound to tanaproget or a fragment thereof. In general, such a representation should accurately reflect (relatively and/or absolutely) structural coordinates, or information derived from structural coordinates, such as distances or angles between features. In some embodiments, the representation is a two-dimensional figure, such as a stereoscopic two-dimensional figure. In certain embodiments, the representation is an interactive two-dimensional display, such as an interactive stereoscopic two-dimensional display. An interactive two-dimensional display can be, for example, a computer display that can be rotated to show different faces of a polypeptide, a fragment of a polypeptide, a complex and/or a fragment of a complex. In some embodiments, the representation is a three-dimensional representation. As an example, a three-dimensional model can be a physical model of a molecular structure (e.g., a ball-and-stick model). As another example, a three dimensional representation can be a graphical representation of a molecular structure (e.g., a drawing or a figure presented on a computer display). A two-dimensional graphical representation (e.g., a drawing) can correspond to a three-dimensional representation when the two-dimensional representation reflects three-dimensional information, for example, through the use of perspective, shading, or the obstruction of features more distant from the viewer by features closer to the viewer. In some embodiments, a representation can be modeled at more than one level. As an example, when the three-dimensional representation includes a polypeptide, such as a complex of the human PR-LBD bound to tanaproget, the polypeptide can be represented at one or more different levels of structure, such as primary (amino acid sequence), secondary (e.g., α-helices and β-sheets), tertiary (overall fold), and quaternary (oligomerization state) structure.
A representation can include different levels of detail. For example, the representation can include the relative locations of secondary structural features of a protein without specifying the positions of atoms. A more detailed representation could, for example, include the positions of atoms.
In some embodiments, a representation can include information in addition to the structural coordinates of the atoms in a complex of the human PR-LBD bound to tanaproget. For example, a representation can provide information regarding the shape of a solvent accessible surface, the van der Waals radii of the atoms of the model, and the van der Waals radius of a solvent (e.g., water). Other features that can be derived from a representation include, for example, electrostatic potential, the location of voids or pockets within a macromolecular structure, and the location of hydrogen bonds and salt bridges.
An agent that interacts with a human PR-LBD can be identified or designed by a method that includes using a representation of the human PR-LBD or a fragment thereof, or a complex of human PR-LBD bound to tanaproget or a fragment thereof. Exemplary types of representations include the representations discussed above. In some embodiments, the representation can be of an analog polypeptide, polypeptide fragment, complex or fragment of a complex. A candidate agent that interacts with the representation can be designed or identified by performing computer fitting analysis of the candidate agent with the representation. In general, an agent is a molecule. Examples of agents include polypeptides, nucleic acids (including DNA or RNA), steroids and non-steroidal organic compounds. An agent can be a ligand, and can act as an agonist or antagonist. An agent that interacts with a polypeptide (e.g., a PR polypeptide) can interact transiently or stably with the polypeptide. The interaction can be mediated by any of the forces noted herein, including, for example, hydrogen bonding, electrostatic forces, hydrophobic interactions, and van der Waals interactions.
As noted above, X-ray crystallography can be used to obtain structural coordinates of a complex of human PR-LBD bound to tanaproget. However, such structural coordinates can be obtained using other techniques including NMR techniques. Additional structural information can be obtained from spectral techniques (e.g., optical rotary dispersion (ORD), circular dichroism (CD)), homology modeling, and computational methods (e.g., computational methods that can include data from molecular mechanics, computational methods that include data from dynamics assays).
In some embodiments, the X-ray diffraction data can be used to construct an electron density map of a complex of human PR-LBD bound to tanaproget or a fragment thereof, and the electron density map can be used to derive a representation (e.g., a two dimensional representation, a three dimensional representation) of human PR-LBD bound to tanaproget or a fragment thereof. Creation of an electron density map typically involves using information regarding the phase of the X-ray scatter. Phase information can be extracted, for example, either from the diffraction data or from supplementing diffraction experiments to complete the construction of the electron density map. Methods for calculating phase from X-ray diffraction data include, for example, multiwavelength anomalous dispersion (MAD), multiple isomorphous replacement (MIR), multiple isomorphous replacement with anomalous scattering (MIRAS), single isomorphous replacement with anomalous scattering (SIRAS), reciprocal space solvent flattening, molecular replacement, or a combination thereof. These methods generate phase information by making isomorphous structural modifications to the native protein, such as by including a heavy atom or changing the scattering strength of a heavy atom already present, and then measuring the diffraction amplitudes for the native protein and each of the modified cases. If the position of the additional heavy atom or the change in its scattering strength is known, then the phase of each diffracted X-ray can be determined by solving a set of simultaneous phase equations. The location of heavy atom sites can be identified using a computer program, such as SHELXS (Sheldrick, Institut Anorg. Chemie, Gottingen, Germany), and diffraction data can be processed using computer programs such as MOSFLM, SCALA, SOLOMON, and SHARP (“The CCP4 Suite: Programs for Protein Crystallography,” Acta Crystallogr. Sect. D, 54:905-921, 1997; deLa Fortelle and Brigogne, Meth. Enzym. 276:472-494, 1997). Upon determination of the phase, an electron density map of the polypeptide or the complex can be constructed.
The electron density map can be used to derive a representation of a polypeptide or a complex, or a fragment of a polypeptide or complex, by aligning a three-dimensional model of a previously known polypeptide or a previously known complex (e.g., a complex containing a polypeptide bound to a ligand) with the electron density map. This process results in a comparative model that shows the degree to which the calculated electron density map varies from the model of the previously known polypeptide or the previously known complex. The comparative model is then refined over one or more cycles (e.g., two cycles, three cycles, four cycles, five cycles, six cycles, seven cycles, eight cycles, nine cycles, 10 cycles) to generate a better fit with the electron density map. A software program such as CNS (Brunger et al., Acta Crystallogr. D54:905-921, 1998) can be used to refine the model. The quality of fit in the comparative model can be measured by, for example, an Rwork or Rfree value. A smaller value of Rwork or Rfree generally indicates a better fit. Misalignments in the comparative model can be adjusted to provide a modified comparative model and a lower Rwork or Rfree value. The adjustments can be based on information (e.g., sequence information) relating to human PR-LBD, tanaproget, the previously known polypeptide and/or the previously known complex. As an example, in embodiments in which a model of a previously known complex of a polypeptide bound to a ligand is used, an adjustment can include replacing the ligand in the previously known complex with tanaproget. As another example, in certain embodiments, an adjustment can include replacing an amino acid in the previously known polypeptide with the amino acid in the corresponding site of human PR-LBD. When adjustments to the modified comparative model satisfy a best fit to the electron density map, the resulting model is that which is determined to describe the polypeptide or complex from which the X-ray data was derived (e.g., the PR-LBD/tanaproget complex). Methods of such processes are disclosed, for example, in Carter and Sweet, eds., “Macromolecular Crystallography” in Methods in Enzymology, Vol. 277, Part B, New York: Academic Press, 1997, and articles therein, e.g., Jones and Kjeldgaard, “Electron-Density Map Interpretation,” p. 173, and Kleywegt and Jones, “Model Building and Refinement Practice,” p. 208.
In some embodiments, a representation of human PR-LBD bound to tanaproget can be derived by aligning a previously determined structural model of progesterone bound to human PR-LBD (e.g., Protein Databank Identification No. 1a28) with the electron density map of human PR-LBD bound to tanaproget derived from X-ray diffraction data. One adjustment that can be used in the modeling process can include replacing progesterone with tanaproget.
A machine, such as a computer, can be programmed in memory with the structural coordinates of a complex of the human PR-LBD bound to tanaproget, together with a program capable of generating a graphical representation of the structural coordinates on a display connected to the machine. Alternatively or additionally, a software system can be designed and/or utilized to accept and store the structural coordinates. The software system can be capable of generating a graphical representation of the structural coordinates. The software system can also be capable of accessing external databases to identify compounds (e.g., polypeptides) with similar structural features as human PR-LBD, and/or to identify one or more candidate agents with characteristics that may render the candidate agent(s) likely to interact with human PR-LBD.
A machine having a memory containing structure data or a software system containing such data can aid in the rational design or selection of PR agonists and/or PR antagonists. For example, such a machine or software system can aid in the evaluation of the ability of an agent to associate with a complex of the human PR-LBD bound to tanaproget, or can aid in the modeling of compounds or proteins related by structural or sequence homology to a PR-LBD.
The machine can produce a representation (e.g., a two dimensional representation, a three dimensional representation) of a complex of the human PR-LBD bound to tanaproget or a fragment thereof. A software system, for example, can cause the machine to produce such information. The machine can include a machine-readable data storage medium including a data storage material encoded with machine-readable data. The machine-readable data can include structural coordinates of atoms of a complex of the human PR-LBD bound to tanaproget or a fragment thereof. Machine-readable storage media (e.g., data storage material) include, for example, conventional computer hard drives, floppy disks, DAT tape, CD-ROM, DVD, and other magnetic, magneto-optical, optical, and other media which may be adapted for use with a machine (e.g., a computer). The machine can also have a working memory for storing instructions for processing the machine-readable data, as well as a central processing unit (CPU) coupled to the working memory and to the machine-readable data storage medium for the purpose of processing the machine-readable data into the desired three-dimensional representation. A display can be connected to the CPU so that the three-dimensional representation can be visualized by the user. Accordingly, when used with a machine programmed with instructions for using the data (e.g., a computer loaded with one or more programs of the sort described herein) the machine is capable of displaying a graphical representation (e.g., a two dimensional graphical representation, a three-dimensional graphical representation) of any of the polypeptides, polypeptide fragments, complexes, or complex fragments described herein.
A display (e.g., a computer display) can show a representation of a complex of human PR-LBD bound to tanaproget or a fragment thereof. The user can inspect the representation and, using information gained from the representation, generate a model of a complex or fragment thereof that includes an agent other than tanaproget. The model can be generated, for example, by altering a previously existing representation of a human PR-LBD/tanaproget complex. Optionally, the user can superimpose a three-dimensional model of an agent on the representation of human PR-LBD bound to tanaproget. The agent can be an agonist (e.g., a candidate agonist) of human PR-LBD or an antagonist (e.g., a candidate antagonist) of human PR-LBD. In some embodiments, the agent can be a known compound or fragment of a compound. In certain embodiments, the agent can be a previously unknown compound, or a fragment of a previously unknown compound.
It can be desirable for the agent to have a shape that complements the shape of the active site. There can be a preferred distance, or range of distances, between atoms of the agent and atoms of the PR polypeptide. Distances longer than a preferred distance may be associated with a weak interaction between the agent and active site (e.g., human PR-LBD). Distances shorter than a preferred distance may be associated with repulsive forces that can weaken the interaction between the agent and the polypeptide. A steric clash can occur when distances between atoms are too short. A steric clash occurs when the locations of two atoms are unreasonably close together, for example, when two atoms are separated by a distance less than the sum of their van der Waals radii. If a steric clash exists, the user can adjust the position of the agent relative to the PR polypeptide (e.g., a rigid body translation or rotation of the agent), until the steric clash is relieved. The user can adjust the conformation of the agent or of the PR polypeptide in the vicinity of the agent in order to relieve a steric clash. Steric clashes can also be removed by altering the structure of the agent, for example, by changing a “bulky group,” such as an aromatic ring, to a smaller group, such as to a methyl or hydroxyl group, or by changing a rigid group to a flexible group that can accommodate a conformation that does not produce a steric clash. Electrostatic forces can also influence an interaction between an agent and a ligand-binding domain. For example, electrostatic properties can be associated with repulsive forces that can weaken the interaction between the agent and the PR polypeptide. Electrostatic repulsion can be relieved by altering the charge of the agent, e.g., by replacing a positively charged group with a neutral group.
Forces that influence binding strength between tanaproget and human PR-LBD can be evaluated in the polypeptide/agent model. These can include, for example, hydrogen bonding, electrostatic forces, hydrophobic interactions, van der Waals interactions, dipole-dipole interactions, π-stacking forces, and cation-π interactions. The user can evaluate these forces visually, for example by noting a hydrogen bond donor/acceptor pair arranged with a distance and angle suitable for a hydrogen bond. Based on the evaluation, the user can alter the model to find a more favorable interaction between the PR polypeptide and the agent. Altering the model can include changing the three-dimensional structure of the polypeptide without altering its chemical structure, for example by altering the conformation of amino acid side chains or backbone dihedral angles. Altering the model can include altering the position or conformation of the agent, as described above. Altering the model can also include altering the chemical structure of the agent, for example by substituting, adding, or removing groups. For example, if a hydrogen bond donor on the PR polypeptide is located near a hydrogen bond donor on the agent, the user can replace the hydrogen bond donor on the agent with a hydrogen bond acceptor.
The relative locations of an agent and the PR polypeptide, or their conformations, can be adjusted to find an optimized binding geometry for a particular agent to the PR polypeptide. An optimized binding geometry is characterized by, for example, favorable hydrogen bond distances and angles, maximal electrostatic attractions, minimal electrostatic repulsions, the sequestration of hydrophobic moieties away from an aqueous environment, and the absence of steric clashes. The optimized geometry can have the lowest calculated energy of a family of possible geometries for a PR polypeptide/agent complex. An optimized geometry can be determined, for example, through molecular mechanics or molecular dynamics calculations.
A series of representations of complexes of human PR-LBD bound to tanaproget, where tanaproget is replaced or overlaid with different agents, can be generated. A score can be calculated for each representation. The score can describe, for example, an expected strength of interaction between human PR-LBD and the agent. The score can reflect one of the factors described above that influence binding strength. The score can be an aggregate score that reflects more than one of the factors. The different agents can be ranked according to their scores.
Steps in the design of the agent can be carried out in an automated fashion by a machine. For example, a representation of PR-LBD can be programmed in the machine, along with representations of candidate agents. The machine can find an optimized binding geometry for each of the candidate agents to the active site, and calculate a score to determine which of the agents in the series is likely to interact most strongly with human PR-LBD.
A software system can be designed and/or implemented to facilitate these steps. Software systems (e.g., computer programs) used to generate such three-dimensional models or perform the necessary fitting analyses include, but are not limited to: MCSS, Ludi, QUANTA, Insight II, Cerius2, CHARMm, and Modeler from Accelrys, Inc. (San Diego, Calif.); SYBYL, Unity, FleXX, and LEAPFROG from TRIPOS, Inc. (St. Louis, Mo.); AUTODOCK (Scripps Research Institute, La Jolla, Calif.); GRID (Oxford University, Oxford, UK); DOCK (University of California, San Francisco, Calif.); and Flo+ and Flo99 (Thistlesoft, Morris Township, N.J.). Other useful programs include ROCS, ZAP, FRED, Vida, and Szybki from Openeye Scientific Software (Santa Fe, N. Mex.); Maestro, Macromodel, and Glide from Schrodinger, LLC (Portland, Oreg.); MOE (Chemical Computing Group, Montreal, Quebec), Allegrow (Boston De Novo, Boston, Mass.), CNS (Brunger, et al., Acta Crystall. Sect. D 54:905-921, 1997) and GOLD (Jones et al., J. Mol. Biol. 245:43-53, 1995). The structural coordinates can also be used to visualize the three-dimensional structure of PKCθ using MOLSCRIPT, RASTER3D, or PYMOL (Kraulis, J. Appl. Crystallogr. 24: 946-950, 1991; Bacon and Anderson, J. Mol. Graph. 6: 219-220, 1998; DeLano, The PYMOL Molecular Graphics System (2002) DeLano Scientific, San Carlos, Calif.).
The agent, whether an agonist or antagonist, can, for example, be selected by screening an appropriate database, can be designed de novo by analyzing the steric configurations and charge potentials of unbound human PR-LBD in conjunction with the appropriate software systems, and/or can be designed using characteristics of known agonists or antagonists of progesterone receptors or other hormone receptors. The method can be used to design or select agonists or antagonists of human PR-LBD. A software system can be designed and/or implemented to facilitate database searching, and/or agent selection and design.
Once an agent has been designed or identified, it can be obtained or synthesized and further evaluated for its effect on human PR-LBD activity. For example, the agent can be evaluated by contacting it with human PR-LBD and measuring the effect of the agent on polypeptide activity. A method for evaluating the agent can include an activity assay performed in vitro or in vivo. An activity assay can be a cell-based assay, for example. Depending upon the action of the agent on human PR-LBD, the agent can act either as an agonist or antagonist of human PR-LBD activity. The agent also can be contacted with the polypeptide in the presence of progesterone in order to determine whether or not the agent inhibits binding of progesterone to the polypeptide. A crystal containing human PR-LBD bound to the identified agent can be grown and the structure determined by X-ray crystallography. A second agent can be designed or identified based on the interaction of the first agent with human PR-LBD.
Various molecular analysis and rational drug design techniques are further disclosed in, for example, U.S. Pat. Nos. 5,834,228, 5,939,528 and 5,856,116, as well as in PCT Application No. PCT/US98/16879, published as WO 99/09148.
While certain embodiments have been described, other embodiments are also contemplated.
As an example, while embodiments involving the human PR-LBD and tanaproget have been described, the description herein is more generally directed to any PR polypeptide and any non-steroidal ligand.
A PR polypeptide can be a full-length, mature polypeptide, including the full-length amino acid sequence of any isoform of a PR polypeptide. An isoform is any of several multiple forms of a protein that differ in their primary structure. For example, human progesterone receptor exists in at least two isoforms, Pr-B (full-length PR) and Pr-A (N-terminally truncated PR). The two isoforms are transcribed from a single gene, but have different translation start sites. Thus the isoforms are identical except that Pr-B contains an additional 164 N-terminal amino acids. The isoforms have an identical centrally located DNA binding domain, which is flanked at the N-terminus by a transcriptional activation function-1 (AF-1) domain, and at the C-terminus by a hinge region containing nuclear localization signals and a ligand binding domain (PR-LBD). A second transcriptional activation function domain (AF-2) is located in the PR-LBD.
A PR polypeptide can be a fragment of a PR, such as a ligand binding domain, a DNA-binding domain, a protein-interaction domain (e.g., an activation domain), or a combination thereof.
A PR polypeptide can have an active site. In general, an active site can include a site of ligand binding, or a site of phosphorylation, glycosylation, alkylation, acylation, or other covalent modification. A ligand binding site can include accessory binding sites adjacent or proximal to the actual site of binding that may affect activity upon interaction with the ligand. An active site of a PR polypeptide can include amino acids of SEQ ID NO:2. For example, an active site of a PR-polypeptide can include one or more of amino acids Ile699, Ala701, Leu714, Leu715, Leu718, Asn719, Leu721, Gln725, Trp755, Met756, Met759, Val760, Leu763, Arg766, Ser767, Tyr777, Phe778, Ala779, Leu782, Phe794, Leu797, Lys798, Met801, Ile804, Leu887, His888, Tyr890, Cys891, Asn893, Thr894, Phe895, Ser898, Leu901, Val903, Phe905, Met909, Ile913, and Leu917 as defined by SEQ ID NO:2.
The numbering of the amino acids of a PR polypeptide may be different than that set forth herein, and the sequence of the PR polypeptide may contain certain conservative amino acid substitutions that yield the same three-dimensional structure. For example, the numbering of a PR-LBD may be different than that set forth in FIG. 2B, and the sequence of the PR-LBD may contain conservative amino acid substitutions but yield the same structure as that defined by the coordinates of Table 2 and illustrated in FIGS. 1A and 1B. Corresponding amino acids and conservative substitutions in other isoforms or analogs are easily identified by visual inspection of the relevant amino acid sequences or by using commercially available homology software programs (e.g., MODELLAR, MSI, San Diego, Calif.).
An analog is a polypeptide having conservative amino acid substitutions. A conservative substitution can include switching one amino acid for another with similar polarity, steric arrangement, or of the same class (e.g., hydrophobic, acidic or basic), and includes substitutions having an inconsequential effect on the three-dimensional structure of the PR polypeptide with respect to identification and design of agents that interact with the polypeptide (e.g., a PR-LBD), as well as for molecular replacement analyses and/or for homology modeling.
A PR polypeptide can originate from a nonmammalian or mammalian species. A mammalian PR polypeptide can originate from a human, for example. Exemplary nonhuman mammals include, a nonhuman primate (such as a monkey or ape), a mouse, rat, goat, cow, bull, pig, horse, sheep, wild boar, sea otter, cat, and dog. Exemplary nonmammalian species include chicken, turkey, shrimp, alligator, and fish.
As another example, while embodiments have been described in which tanaproget is a ligand, more generally other non-steroidal compounds may also be used as ligands. For example, based on a representation of the human PR-LBD bound to tanaproget derived from the structure of the crystalline complex, without wishing to be bound by theory it is believed that: the carbonitrilo nitrogen of tanaproget forms hydrogen bonds with the side chains of Gln725 and Arg766 of the human PR-LBD; the benzoxazine nitrogen of tanaproget forms hydrogen bonds with the side chain oxygen of Asn719 of the human PR-LBD; hydrophobic interactions occur between Leu797 of the human PR-LBD and the hydrophobic region of the benzoxazine moiety (which includes the pair of methyl substituents in the 4 position) of tanaproget; and an electrostatic interaction occurs between Thr894 of the human PR-LBD and the sulfur of tanaproget.
Based on this information, without wishing to be bound by theory, it is believed that other non-steroidal compounds capable of having one or more similar interactions with the human PR-LBD may also be capable of acting as ligands (e.g., agonists, antagonists) for the human PR-LBD. Such non-steroidal compounds may have the structure:




where A, B and C represent ring systems, B and C are fused rings, and L is a linker moiety.

In general, rings A, B and C are each independently formed of at least four atoms (e.g., five atoms, six atoms, seven atoms, eight atoms, nine atoms, 10 atoms, 11 atoms, 12 atoms, 13 atoms, 14 atoms). One or more atoms (e.g., one atom, two atoms, three atoms, four atoms) in rings A, B and/or C can independently be heteroatoms (e.g., N, S, O). In some embodiments, rings B and C form an indole, an oxindole, a thioindole, a benzothiophene, a benzofuran, a benzothiazole, a benzimidazole, a benzoxazine or a benzthiazine. In one embodiment rings B and C can form a benzoxazine ring that can have at least one hydrophobic substituent at the 4 position. In another embodiment the benzoxazine ring can have at least one hydrophobic substituent near the 4 position e.g. at the 5 position. Benzoxazine derivatives are described, for example, in U.S. Pat. No. 6,562,857, which is hereby incorporated by reference. Ring A can be, for example, a pyrrole, a furan, a thiophene, an imidazole, an oxazole, or a phenyl. In some embodiments, rings A, B and/or C can each independently include one or more (e.g., one, two, three, four) substituents (e.g., one or more substituents that provide favorable interaction with the human PR-LBD, such as, for example, through hydrogen bonding, hydrophobic interaction and/or electrostatic interaction). Examples of substituents include hydroxy substituents, amino substituents, cyano substituents, nitro substituents, oxime substituents, thiol substituents, amido substituents, oxo substituents, alkyl substituents e.g. having 1-6 carbon atoms, alkenyl substituents e.g. having 2-6 carbon atoms, alkynyl substituents e.g. having 2-6 carbon atoms, aryl substituents e.g. an aromatic carbocyclic mono- or polycyclic ring system having from 6-20 ring carbon atoms, cyclyl substituents e.g. a saturated or partially saturated mono- or polycyclic carbocyclic ring system having from 3-14 ring atoms, heteroaryl substituents e.g. an aromatic heterocyclic mono- or polycyclic ring system having from 5-14 ring atoms wherein 1, 2, 3 or 4 of the ring atoms are selected from N, O or S, heterocyclyl substituents e.g. a saturated or partially saturated mono- or polycyclic heterocyclic ring system having from 3-14 ring atoms wherein 1, 2, 3 or 4 of the ring atoms are selected from N, O or S, and halogens (e.g., fluorine, chlorine, bromine, iodine). While in some embodiments, a substituent itself may be a hydrogen bond donor or acceptor with the human PR-LBD, in other embodiments, the substituent may form a hydrogen bond with a portion of the human PR-LBD through one or more solvent molecules such as water.
In general, L can be a direct chemical bond, or L can be formed of a chemical moiety, such as, for example, an alkyl moiety e.g. having 1-6 carbon atoms, an alkenyl moiety e.g. having 2-6 carbon atoms, an alkynyl moiety e.g. having 2-6 carbon atoms, an ether moiety, a thioether moiety, an amido moiety, a carbonyl moiety or a sulfonyl moiety. In some embodiments, L can be formed of multiple moieties (e.g., a sulfonyl moiety bonded to an alkyl moiety).
Although embodiments have been described in which the non-steroidal compound includes rings B and C fused together, in some embodiments, rings B and C can be joined by a chemical linker. Examples of linkers are noted above. In certain embodiments, ring B is not present. For example, ring B can be replaced with a linker moiety that connects ring C with ring A. The linker moiety can, for example, be of sufficient length to allow favorable interactions between ring A and one or both of Glu725 or Arg766 of the human PR-LBD, and between ring C and one or more of Asn719, Thr894, or Cys891 of the human PR-LBD. For example, ring B can be replaced with an alkenyl linker such as a branched alkene, which can provide sufficient length, structural rigidity, and, where desired, bulk (e.g., the linker moiety can include a branched alkenyl moiety).
The following example is illustrative and not intended as limiting.
EXAMPLE
Human progesterone ligand binding domain (PR-LBD) was expressed as an amino terminal glutathione-S-transferase (GST) fusion protein from Escherichia coli BL21 (Stratagene). The PR-LBD domain coding sequence was cloned into the pGEX plasmid (Amersham Pharmacia Biotech) under tac transcriptional control. A thrombin cleavage site (LVPRG, SEQ ID NO:3) R and the G). The sequence of this fusion protein is shown in FIG. 2A. The sequence of the PR-LBD polypeptide following thrombin cleavage is shown in FIG. 2B.
Bacterial growth and protein expression were performed in a Biostat 10 liter fermenter (B. Braun Biotech). A 100 mL preculture was used to inoculate 10 liters of media (fermenter salts, glucose, ampicillin, trace metals and yeast extract media) and expanded overnight at 25° C. Fifteen minutes prior to induction, the vessel temperature was lowered to 15° C. and 5 mls of 66 mM progesterone (Sigma-Aldrich, St. Louis, Mo.) in 100% ethanol was added. The culture was induced at a density of 5.4 OD600 absorbance units with addition of isopropyl-beta-D-thiogalactopyranoside (IPTG, Fisher) to a final concentration of 1.0 mM. Progesterone was again added in 5 ml aliquots of 66 mM at the time of induction and every fifteen minutes thereafter, for the duration of expression (4 hours total, 660 μM final concentration of progesterone). After 4 hours of induction, the culture was harvested yielding 158.76 g of wet cell weight. The protein of interest represented 5-7% of total cell protein, as estimated by SDS-PAGE. Successful isolation of PR-LBD depended strongly on inclusion of a PR ligand during expression (possibly to ensure proper protein folding) and purification. See, for example, Williams and Sigler, Nature 393:392-396, 1998; Tanenbaum et al., Proc. Natl. Acad. Sci. USA 95:5998-6003, 1998; and Matias et al., J. Biol. Chem. 275: 26164-26171, 2000. Tanaproget was exchanged for progesterone during purification.
20 g of frozen cells were suspended in 300 mL of 50 mM HEPES pH 7.3, 150 mM NaCl, 5 mM EDTA, 10% glycerol, 5 mM dithiothreitol (DTT) with 0.33 mM of the protease inhibitor aminoethylbenzenesulfonyl fluoride (AEBSF, Sigma-Aldrich), 0.3 mL of protease inhibitor cocktail (Sigma-Aldrich catalog number 8849) and 5 μM progesterone (Progesterone was stored as a 50 mM stock solution in dimethylsulfoxide). Cells were broken by passage through a microfluidizer (Midrofluidics, Newton, Mass.). Cell debris and aggregated GST/PR-LBD were removed by centrifugation for 2.5 hrs at approximately 40,000 g. CHAPS (Sigma) was added to 1.5% and the solution was passed through a 0.45 micron cellulose nitrate filter and stored overnight.
An initial purification of GST/PR-LBD fusion protein was carried out by affinity chromatography. The filtered solution was passed over two 5 mL columns (in tandem) of GSTrap FF glutathione-Sepharose chromatography media (Amersham Bioscience) at flow rate of about 1 mL/min. Resin was washed with 50 mL of 50 mM HEPES pH 7.3, 150 mM NaCl, 5 mM EDTA, 10% glycerol, then with 50 mL of same solution containing 50 μM tanaproget. GST/PR-LBD was eluted with 12 mM reduced glutathione (Sigma) in 50 mM HEPES pH 7.3, 100 mM NaCl, 10% glycerol, 0.1% octyl-β-glucoside, and 50 μM tanaproget. Fractions of 5 mL were collected. Those fractions containing GST/PR-LBD were identified by SDS-PAGE and pooled. Typically the pooled fractions had a total volume of 30-40 mL. Thrombin was added to 25,000 NIH units/mL. The solution was incubated overnight for specific proteolysis.
The solution was diluted with 4 volumes of 10 mM HEPES pH 7.3, 10% glycerol, 5 mM DTT, 0.1% octyl-β-glucoside, and 50 μM tanaproget. The solution was passed over a 1 mL column of HiTrap SP FF sulfopropyl-Sepharose (Amersham Bioscience) at a flow rate of 1 mL/min. The column was washed with 5 mL of 10 mM HEPES pH 7.3, 20 mM NaCl, 10% glycerol, 0.1% octyl-β-glucoside, and 1 μM tanaproget (tanaproget was stored as a 50 mM stock solution in dimethylsulfoxide). PR-LBD was eluted from the column with a 15 mL gradient of sodium chloride, running from 20 mM to 220 mM (other components as above). Fractions of 1 mL were collected, PR-LBD was located by SDS-PAGE and those fractions containing PR/LBD at a concentration of 1 to 2 mg/mL were used directly for crystallization.
Prior to crystallization, the PR-LBD/tanaproget complex was determined to be homogeneous by SDS-PAGE. The protein had the expected mass as determined by MALDI mass spectrometry ( ̃29,800 Da). The protein behaved as a single species during size-exclusion chromatography. The retention volume, as compared with reference proteins, was consistent with a dimer of PR-LBD. Only those preparations of the PR-LBD/tanaproget complex without any detectable progesterone were used for crystallization. Bound ligand was analyzed by reverse-phase chromatography following protein denaturation in the presence of guanidine-HCl.
Crystals were grown by hanging drop vapor diffusion at 18° C. The drops contained 2.0 μL protein stock solution (5 mg/mL protein, 10 mM HEPES pH 7.3, 10% glycerol, 5 mM DTT,  ̃100 mM NaCl, 0.1% octyl-β-glucoside, 1 μM tanaproget) mixed with 1.0 μL well solution (8% PEG 3350 (Hampton Research), 300 mM MgSO4, 50 mM PIPES pH 6.5, 10% glycerol) and 0.5 μL, 1,3-propanediol (40% v/v, Hampton Research) and equilibrated against a 1 mL well solution. Diamond shaped crystals grew in 2-6 weeks, measuring  ̃50 μm across.
Showers of small crystals grew in the conditions described above with a variety of sulfate salts. The number of nucleation events was reduced by the addition of 1,3-propanediol (40% v/v) to drops, enabling the growth of fewer, larger, single crystals. The crystals belonged to space group P21 with unit cell parameters a=57.52 Å, b=64.50 Å, c=70.41 Å, and β=95.76°, and contained two molecules of PR-LBD in the asymmetric unit, implying a solvent content of 44%. Crystals were drawn through a cryoprotectant solution of 20% ethylene glycol and 80% well solution, and cooled rapidly in liquid nitrogen. Diffraction data were recorded on an R-axis 4 detector. Intensities were integrated and scaled using the programs Denzo and Scalepack (Otwinowski and Minor, Methods Enzymol. 276: 307-326, 1997).
The structure was solved by molecular replacement using the protein model of the PR-LBD/progesterone structure (Williams and Sigler, Nature 393:392-396, 1998) as the search model. After several iterative cycles of refinement using CNS (Brunger et al., Acta Crystallogr. D54:905-921, 1998) and model improvement, tanaproget was placed and refined. The final values of Rwork and Rfree were 19.62% and 23.74%, respectively. Table 1 summarizes the data collection parameters and results.







TABLE 1





Statistics of X-Ray Diffraction Data Collection















Data Collection








Crystal System
monoclinic


Space Group
P21


Unit Cell Dimensions
A = 57.52 Å, b = 64.50 Å,



c = 70.41 Å, β = 95.76°


Data Collection Temperature
−180° C.


Number of crystals
1


Radiation Source
Rigaku rotating anode X-ray



generator


X-ray wavelength
1.54179 Å


Resolution range of data
30.0-2.0 Å


Maximum Resolution
2.0 Å


Rmergea
4.9% (17.6%)


Completeness
100.0% (99.9%)


Total reflections
147,224


Unique reflections
34,825


I/σ(I)
26.9 (8.3)


Phasing and Refinement


Model for molecular refinement
1a28.pdb (PR-LBD/progester-



one)


Construct (aa)
PR-LBD (675-933)


Compound (ligand)
tanaproget


PR-LBD molecules per asymmetric unit
2


Resolution range of refinement
20.0-2.0 Å


Rwork
19.62%


Rfree
23.74%


Number of non-hydrogen protein atoms
4072


Number of water molecules
179


RMS deviations from ideal bond lengths
0.0057 Å


RMS deviations from ideal bond angles
1.132°





aRmerge = |Ih − <Ih>|/Ih, where <Ih> is the average intensity over symmetry equivalents.


Numbers in parentheses reflect statistics for the last shell.


bRwork = ||Fobs| − |Fcalc||/|Fobs|


cRfree is equivalent to Rwork, but calculated for a randomly chosen 5% of reflections omitted from the refinement process.






The refined model included two PR-LBD molecules in the asymmetric unit of the crystal, each bound to one agonist. Tanaproget fit into the buried hydrophobic ligand binding pocket, occupying roughly the same area as progesterone.
The principle features of nuclear receptor ligand binding domains were conserved in the PR-LBD. There were ten helices (following standard steroid receptor nomenclature, helix 2 is missing, and helices 10 and 11 are contiguous), of which helices 3, 5, 7, 11 and 12 contributed to the ligand binding pocket. The two PR-LBD molecules in the crystal formed a dimer centered around interactions between helix 11 of one subunit with helix 12 of the other.
The tertiary structure of PR-LBD/tanaproget was very similar to that of PR-LBD/progesterone. Tanaproget occupied the same binding pocket as progesterone. See FIGS. 1A and 1B, which present views of a 3Fobs-2Fcalc experimental map of tanaproget bound to PR-LBD unbiased by ligand phases and contoured at 1.2 σ. Superposition of the structures of the PR-LBD/tanaproget complex and the PR-LBD/progesterone complex revealed that the 1-methyl-1H-pyrrole-2-carbonitrile ring lay roughly between the A and B rings of progesterone, and the 1,4-dihydro-3,1-benzoxazine-2-thione moiety (“benzoxazine”) lay just above the C and D rings of progesterone in the direction of the protruding methyl groups of progesterone.
Tanaproget mimicked the interaction of progesterone with the ligand binding pocket of PR-LBD in many ways. The nitrile group, positioned approximately 0.6 Å from the 3-keto substituent of the progesterone A ring, formed hydrogen bonds with the side chains of Gln725 and Arg766. Similarly, the progesterone 3-keto group interacted with the side chains of Gln725 and Arg766, and maintained the hydrogen bonding network that provides specificity for steroids with an oxygen atom at the 3-position of the A ring. The benzoxazine moiety occupied approximately the same space as rings C and D of progesterone with similar hydrophobic interactions. The sulfur of the benzoxazine appeared to extend beyond the methyl-ketone substituent at C17 of progesterone. Tanaproget had an additional favorable interaction with the protein in the hydrogen bond formed between the benzoxazine nitrogen and the side chain oxygen of Asn719. The loop between helix 6 and helix 7, including amino acids 788-794, was rearranged with respect to the PR-LBD/progesterone structure. This rearrangement did not appear to be directly due to the different ligand, however, as the shortest distance between tanaproget and PR-LBD in this region is 5 Å, from one tanaproget methyl substituent of the benzoxazine to the side chain of Phe794. The structure indicated that the sulfur atom of tanaproget may form a weak interaction with Thr894 of the PR-LBD, and a hydrophobic region on the benzoxazine molecule forms a favorable hydrophobic interaction with Leu797 of the receptor LBD.
Several side chains were well defined by the experimental electron density in one molecule of the asymmetric unit (molecule “A”), but not in the other (molecule “B”). These side chains include: Met908, Phe794, Trp755, and Leu714. Met908 is somewhat disordered in molecule “A”, with more than one rotamer represented in the electron density.







TABLE 2







Structure coordinates (Table dicloses SEQ ID NO: 6 twice)



















#
Name
Res.
Chain
Res #
X
Y
Z
occ
B
SegID






















ATOM
1
CB
GLN
A
682
−7.348
13.179
57.749
1.00
59.37
A


ATOM
2
CG
GLN
A
682
−6.839
14.229
58.725
1.00
62.50
A


ATOM
3
CD
GLN
A
682
−6.509
13.648
60.089
1.00
64.16
A


ATOM
4
OE1
GLN
A
682
−7.383
13.129
60.785
1.00
65.34
A


ATOM
5
NE2
GLN
A
682
−5.240
13.732
60.476
1.00
64.49
A


ATOM
6
C
GLN
A
682
−6.989
11.007
56.577
1.00
54.95
A


ATOM
7
O
GLN
A
682
−6.920
9.824
56.915
1.00
55.50
A


ATOM
8
N
GLN
A
682
−5.169
12.697
56.667
1.00
58.18
A


ATOM
9
CA
GLN
A
682
−6.321
12.097
57.404
1.00
57.18
A


ATOM
10
N
LEU
A
683
−7.640
11.412
55.493
1.00
51.76
A


ATOM
11
CA
LEU
A
683
−8.315
10.464
54.618
1.00
48.27
A


ATOM
12
CB
LEU
A
683
−9.448
11.156
53.851
1.00
50.10
A


ATOM
13
CG
LEU
A
683
−10.757
11.418
54.603
1.00
52.21
A


ATOM
14
CD1
LEU
A
683
−11.685
12.275
53.749
1.00
52.58
A


ATOM
15
CD2
LEU
A
683
−11.420
10.091
54.945
1.00
51.94
A


ATOM
16
C
LEU
A
683
−7.338
9.846
53.627
1.00
43.82
A


ATOM
17
O
LEU
A
683
−7.630
8.815
53.027
1.00
43.05
A


ATOM
18
N
ILE
A
684
−6.175
10.471
53.470
1.00
39.89
A


ATOM
19
CA
ILE
A
684
−5.173
9.983
52.526
1.00
35.45
A


ATOM
20
CB
ILE
A
684
−4.119
11.060
52.215
1.00
35.60
A


ATOM
21
CG2
ILE
A
684
−3.298
10.633
51.014
1.00
34.67
A


ATOM
22
CG1
ILE
A
684
−4.798
12.400
51.921
1.00
34.80
A


ATOM
23
CD1
ILE
A
684
−5.754
12.361
50.761
1.00
35.65
A


ATOM
24
C
ILE
A
684
−4.435
8.732
52.996
1.00
33.40
A


ATOM
25
O
ILE
A
684
−3.823
8.724
54.063
1.00
32.14
A


ATOM
26
N
PRO
A
685
−4.482
7.657
52.190
1.00
31.08
A


ATOM
27
CD
PRO
A
685
−5.212
7.563
50.914
1.00
29.47
A


ATOM
28
CA
PRO
A
685
−3.823
6.386
52.497
1.00
29.34
A


ATOM
29
CB
PRO
A
685
−4.051
5.566
51.230
1.00
28.42
A


ATOM
30
CG
PRO
A
685
−5.360
6.071
50.745
1.00
29.55
A


ATOM
31
C
PRO
A
685
−2.341
6.604
52.777
1.00
28.94
A


ATOM
32
O
PRO
A
685
−1.685
7.395
52.099
1.00
27.20
A


ATOM
33
N
PRO
A
686
−1.795
5.892
53.776
1.00
28.63
A


ATOM
34
CD
PRO
A
686
−2.499
4.881
54.583
1.00
30.74
A


ATOM
35
CA
PRO
A
686
−0.388
5.983
54.178
1.00
28.46
A


ATOM
36
CB
PRO
A
686
−0.225
4.796
55.122
1.00
29.48
A


ATOM
37
CG
PRO
A
686
−1.565
4.697
55.750
1.00
30.51
A


ATOM
38
C
PRO
A
686
0.615
5.941
53.026
1.00
26.34
A


ATOM
39
O
PRO
A
686
1.448
6.836
52.897
1.00
27.12
A


ATOM
40
N
LEU
A
687
0.538
4.907
52.192
1.00
23.00
A


ATOM
41
CA
LEU
A
687
1.474
4.782
51.077
1.00
21.26
A


ATOM
42
CB
LEU
A
687
1.145
3.552
50.228
1.00
19.41
A


ATOM
43
CG
LEU
A
687
2.091
3.305
49.047
1.00
18.40
A


ATOM
44
CD1
LEU
A
687
3.537
3.370
49.521
1.00
17.99
A


ATOM
45
CD2
LEU
A
687
1.788
1.944
48.420
1.00
17.48
A


ATOM
46
C
LEU
A
687
1.484
6.022
50.194
1.00
21.24
A


ATOM
47
O
LEU
A
687
2.535
6.432
49.700
1.00
21.10
A


ATOM
48
N
ILE
A
688
0.317
6.623
49.994
1.00
20.14
A


ATOM
49
CA
ILE
A
688
0.234
7.818
49.168
1.00
20.01
A


ATOM
50
CB
ILE
A
688
−1.243
8.179
48.845
1.00
20.19
A


ATOM
51
CG2
ILE
A
688
−1.321
9.546
48.196
1.00
19.71
A


ATOM
52
CG1
ILE
A
688
−1.833
7.114
47.907
1.00
20.43
A


ATOM
53
CD1
ILE
A
688
−3.294
7.332
47.534
1.00
20.19
A


ATOM
54
C
ILE
A
688
0.938
8.983
49.862
1.00
20.11
A


ATOM
55
O
ILE
A
688
1.686
9.725
49.225
1.00
20.42
A


ATOM
56
N
ASN
A
689
0.712
9.146
51.164
1.00
21.73
A


ATOM
57
CA
ASN
A
689
1.370
10.227
51.901
1.00
22.53
A


ATOM
58
CB
ASN
A
689
0.967
10.200
53.380
1.00
28.18
A


ATOM
59
CG
ASN
A
689
−0.417
10.782
53.627
1.00
32.46
A


ATOM
60
OD1
ASN
A
689
−1.037
10.513
54.659
1.00
37.47
A


ATOM
61
ND2
ASN
A
689
−0.901
11.594
52.693
1.00
35.14
A


ATOM
62
C
ASN
A
689
2.884
10.040
51.790
1.00
22.06
A


ATOM
63
O
ASN
A
689
3.634
10.997
51.609
1.00
20.86
A


ATOM
64
N
LEU
A
690
3.325
8.793
51.888
1.00
20.88
A


ATOM
65
CA
LEU
A
690
4.746
8.497
51.794
1.00
21.42
A


ATOM
66
CB
LEU
A
690
4.982
7.013
52.057
1.00
21.51
A


ATOM
67
CG
LEU
A
690
6.427
6.547
52.240
1.00
22.35
A


ATOM
68
CD1
LEU
A
690
6.409
5.229
52.969
1.00
26.08
A


ATOM
69
CD2
LEU
A
690
7.129
6.416
50.897
1.00
23.08
A


ATOM
70
C
LEU
A
690
5.259
8.895
50.411
1.00
20.43
A


ATOM
71
O
LEU
A
690
6.299
9.545
50.293
1.00
20.25
A


ATOM
72
N
LEU
A
691
4.523
8.524
49.366
1.00
19.54
A


ATOM
73
CA
LEU
A
691
4.931
8.873
48.008
1.00
18.70
A


ATOM
74
CB
LEU
A
691
3.908
8.357
46.989
1.00
16.88
A


ATOM
75
CG
LEU
A
691
3.852
6.840
46.763
1.00
16.04
A


ATOM
76
CD1
LEU
A
691
2.834
6.533
45.671
1.00
15.95
A


ATOM
77
CD2
LEU
A
691
5.230
6.311
46.355
1.00
16.73
A


ATOM
78
C
LEU
A
691
5.088
10.385
47.868
1.00
19.45
A


ATOM
79
O
LEU
A
691
6.028
10.870
47.238
1.00
18.17
A


ATOM
80
N
MET
A
692
4.166
11.136
48.459
1.00
20.70
A


ATOM
81
CA
MET
A
692
4.243
12.588
48.380
1.00
23.63
A


ATOM
82
CB
MET
A
692
2.998
13.232
49.000
1.00
25.77
A


ATOM
83
CG
MET
A
692
2.988
14.751
48.917
1.00
29.26
A


ATOM
84
SD
MET
A
692
3.036
15.361
47.206
1.00
35.42
A


ATOM
85
CE
MET
A
692
4.716
16.016
47.096
1.00
34.93
A


ATOM
86
C
MET
A
692
5.484
13.105
49.104
1.00
23.94
A


ATOM
87
O
MET
A
692
6.139
14.033
48.636
1.00
22.01
A


ATOM
88
N
SER
A
693
5.804
12.496
50.243
1.00
23.84
A


ATOM
89
CA
SER
A
693
6.953
12.925
51.036
1.00
25.43
A


ATOM
90
CB
SER
A
693
6.960
12.218
52.397
1.00
26.51
A


ATOM
91
OG
SER
A
693
7.373
10.868
52.268
1.00
30.46
A


ATOM
92
C
SER
A
693
8.310
12.716
50.370
1.00
23.96
A


ATOM
93
O
SER
A
693
9.257
13.432
50.677
1.00
22.54
A


ATOM
94
N
ILE
A
694
8.415
11.745
49.465
1.00
22.45
A


ATOM
95
CA
ILE
A
694
9.694
11.492
48.814
1.00
21.42
A


ATOM
96
CB
ILE
A
694
10.001
9.976
48.740
1.00
20.54
A


ATOM
97
CG2
ILE
A
694
10.052
9.393
50.153
1.00
18.76
A


ATOM
98
CG1
ILE
A
694
8.947
9.261
47.896
1.00
20.09
A


ATOM
99
CD1
ILE
A
694
9.257
7.790
47.648
1.00
19.61
A


ATOM
100
C
ILE
A
694
9.828
12.100
47.422
1.00
23.09
A


ATOM
101
O
ILE
A
694
10.756
11.767
46.677
1.00
23.23
A


ATOM
102
N
GLU
A
695
8.904
12.989
47.069
1.00
23.79
A


ATOM
103
CA
GLU
A
695
8.956
13.658
45.773
1.00
24.75
A


ATOM
104
CB
GLU
A
695
7.691
14.489
45.544
1.00
23.00
A


ATOM
105
CG
GLU
A
695
6.538
13.671
45.009
1.00
22.30
A


ATOM
106
CD
GLU
A
695
6.766
13.243
43.574
1.00
22.70
A


ATOM
107
OE1
GLU
A
695
6.637
14.100
42.679
1.00
24.09
A


ATOM
108
OE2
GLU
A
695
7.082
12.060
43.339
1.00
20.49
A


ATOM
109
C
GLU
A
695
10.181
14.563
45.739
1.00
26.09
A


ATOM
110
O
GLU
A
695
10.596
15.097
46.762
1.00
24.44
A


ATOM
111
N
PRO
A
696
10.775
14.746
44.554
1.00
27.98
A


ATOM
112
CD
PRO
A
696
10.513
13.991
43.318
1.00
30.08
A


ATOM
113
CA
PRO
A
696
11.964
15.589
44.402
1.00
29.41
A


ATOM
114
CB
PRO
A
696
12.419
15.286
42.974
1.00
30.04
A


ATOM
115
CG
PRO
A
696
11.895
13.887
42.729
1.00
31.56
A


ATOM
116
C
PRO
A
696
11.692
17.072
44.592
1.00
30.11
A


ATOM
117
O
PRO
A
696
10.561
17.527
44.436
1.00
28.96
A


ATOM
118
N
ASP
A
697
12.737
17.819
44.941
1.00
31.22
A


ATOM
119
CA
ASP
A
697
12.624
19.264
45.093
1.00
32.61
A


ATOM
120
CB
ASP
A
697
13.829
19.834
45.852
1.00
36.05
A


ATOM
121
CG
ASP
A
697
13.550
20.037
47.328
1.00
39.53
A


ATOM
122
OD1
ASP
A
697
12.602
20.786
47.654
1.00
40.51
A


ATOM
123
OD2
ASP
A
697
14.281
19.458
48.160
1.00
40.91
A


ATOM
124
C
ASP
A
697
12.641
19.794
43.661
1.00
32.25
A


ATOM
125
O
ASP
A
697
12.689
19.012
42.712
1.00
29.97
A


ATOM
126
N
VAL
A
698
12.609
21.114
43.506
1.00
32.44
A


ATOM
127
CA
VAL
A
698
12.640
21.722
42.180
1.00
32.25
A


ATOM
128
CB
VAL
A
698
12.444
23.260
42.257
1.00
34.46
A


ATOM
129
CG1
VAL
A
698
12.766
23.896
40.918
1.00
36.09
A


ATOM
130
CG2
VAL
A
698
11.014
23.587
42.653
1.00
35.95
A


ATOM
131
C
VAL
A
698
13.995
21.435
41.543
1.00
30.21
A


ATOM
132
O
VAL
A
698
15.025
21.495
42.217
1.00
30.12
A


ATOM
133
N
ILE
A
699
13.990
21.114
40.253
1.00
27.42
A


ATOM
134
CA
ILE
A
699
15.226
20.835
39.526
1.00
25.67
A


ATOM
135
CB
ILE
A
699
15.239
19.399
38.956
1.00
25.17
A


ATOM
136
CG2
ILE
A
699
16.491
19.190
38.091
1.00
23.70
A


ATOM
137
CG1
ILE
A
699
15.196
18.387
40.102
1.00
23.56
A


ATOM
138
CD1
ILE
A
699
14.904
16.973
39.652
1.00
24.85
A


ATOM
139
C
ILE
A
699
15.384
21.810
38.366
1.00
25.34
A


ATOM
140
O
ILE
A
699
14.507
21.912
37.503
1.00
22.56
A


ATOM
141
N
TYR
A
700
16.504
22.526
38.349
1.00
25.69
A


ATOM
142
CA
TYR
A
700
16.769
23.486
37.286
1.00
26.30
A


ATOM
143
CB
TYR
A
700
17.538
24.689
37.830
1.00
29.84
A


ATOM
144
CG
TYR
A
700
16.802
25.473
38.890
1.00
33.46
A


ATOM
145
CD1
TYR
A
700
16.630
24.956
40.173
1.00
35.57
A


ATOM
146
CE1
TYR
A
700
15.977
25.685
41.161
1.00
36.93
A


ATOM
147
CD2
TYR
A
700
16.296
26.744
38.617
1.00
35.62
A


ATOM
148
CE2
TYR
A
700
15.640
27.484
39.600
1.00
37.08
A


ATOM
149
CZ
TYR
A
700
15.487
26.947
40.868
1.00
37.98
A


ATOM
150
OH
TYR
A
700
14.857
27.677
41.849
1.00
42.60
A


ATOM
151
C
TYR
A
700
17.573
22.845
36.165
1.00
26.05
A


ATOM
152
O
TYR
A
700
18.347
21.911
36.395
1.00
25.35
A


ATOM
153
N
ALA
A
701
17.384
23.352
34.949
1.00
25.26
A


ATOM
154
CA
ALA
A
701
18.092
22.845
33.781
1.00
24.29
A


ATOM
155
CB
ALA
A
701
17.270
23.101
32.518
1.00
24.28
A


ATOM
156
C
ALA
A
701
19.457
23.510
33.650
1.00
25.20
A


ATOM
157
O
ALA
A
701
20.378
22.947
33.053
1.00
23.68
A


ATOM
158
N
GLY
A
702
19.576
24.711
34.212
1.00
26.21
A


ATOM
159
CA
GLY
A
702
20.824
25.453
34.141
1.00
26.56
A


ATOM
160
C
GLY
A
702
20.991
26.136
32.794
1.00
27.49
A


ATOM
161
O
GLY
A
702
22.113
26.367
32.342
1.00
25.92
A


ATOM
162
N
HIS
A
703
19.875
26.456
32.147
1.00
25.65
A


ATOM
163
CA
HIS
A
703
19.911
27.106
30.841
1.00
28.02
A


ATOM
164
CB
HIS
A
703
18.604
26.829
30.090
1.00
26.86
A


ATOM
165
CG
HIS
A
703
18.596
27.332
28.681
1.00
28.60
A


ATOM
166
CD2
HIS
A
703
18.915
26.723
27.515
1.00
27.33
A


ATOM
167
ND1
HIS
A
703
18.233
28.621
28.354
1.00
28.67
A


ATOM
168
CE1
HIS
A
703
18.325
28.782
27.046
1.00
29.35
A


ATOM
169
NE2
HIS
A
703
18.738
27.646
26.513
1.00
29.47
A


ATOM
170
C
HIS
A
703
20.155
28.615
30.961
1.00
29.77
A


ATOM
171
O
HIS
A
703
19.651
29.265
31.873
1.00
27.82
A


ATOM
172
N
ASP
A
704
20.931
29.159
30.027
1.00
32.72
A


ATOM
173
CA
ASP
A
704
21.275
30.579
30.019
1.00
37.35
A


ATOM
174
CB
ASP
A
704
22.110
30.896
28.767
1.00
40.24
A


ATOM
175
CG
ASP
A
704
21.321
30.733
27.468
1.00
42.83
A


ATOM
176
OD1
ASP
A
704
20.357
31.498
27.263
1.00
41.93
A


ATOM
177
OD2
ASP
A
704
21.664
29.847
26.646
1.00
42.26
A


ATOM
178
C
ASP
A
704
20.082
31.542
30.110
1.00
39.25
A


ATOM
179
O
ASP
A
704
19.964
32.310
31.070
1.00
42.51
A


ATOM
180
N
ASN
A
705
19.204
31.487
29.115
1.00
40.19
A


ATOM
181
CA
ASN
A
705
18.023
32.347
29.018
1.00
39.83
A


ATOM
182
CB
ASN
A
705
17.213
32.328
30.318
1.00
39.65
A


ATOM
183
CG
ASN
A
705
16.404
31.052
30.482
1.00
39.53
A


ATOM
184
OD1
ASN
A
705
15.623
30.677
29.602
1.00
38.94
A


ATOM
185
ND2
ASN
A
705
16.582
30.382
31.614
1.00
37.25
A


ATOM
186
C
ASN
A
705
18.358
33.791
28.637
1.00
40.65
A


ATOM
187
O
ASN
A
705
17.479
34.540
28.206
1.00
40.21
A


ATOM
188
N
THR
A
706
19.619
34.186
28.792
1.00
40.22
A


ATOM
189
CA
THR
A
706
20.024
35.542
28.429
1.00
41.37
A


ATOM
190
CB
THR
A
706
21.211
36.046
29.276
1.00
41.45
A


ATOM
191
OG1
THR
A
706
22.376
35.273
28.974
1.00
42.94
A


ATOM
192
CG2
THR
A
706
20.899
35.930
30.760
1.00
42.56
A


ATOM
193
C
THR
A
706
20.449
35.555
26.963
1.00
41.48
A


ATOM
194
O
THR
A
706
20.735
36.609
26.398
1.00
42.00
A


ATOM
195
N
LYS
A
707
20.493
34.373
26.355
1.00
39.94
A


ATOM
196
CA
LYS
A
707
20.882
34.246
24.957
1.00
39.25
A


ATOM
197
CB
LYS
A
707
22.080
33.303
24.805
1.00
40.35
A


ATOM
198
CG
LYS
A
707
23.378
33.794
25.420
1.00
43.83
A


ATOM
199
CD
LYS
A
707
24.534
32.911
24.963
1.00
45.58
A


ATOM
200
CE
LYS
A
707
25.874
33.379
25.514
1.00
48.00
A


ATOM
201
NZ
LYS
A
707
25.993
33.156
26.982
1.00
50.15
A


ATOM
202
C
LYS
A
707
19.727
33.690
24.146
1.00
36.97
A


ATOM
203
O
LYS
A
707
18.858
33.009
24.684
1.00
37.69
A


ATOM
204
N
PRO
A
708
19.703
33.978
22.838
1.00
35.45
A


ATOM
205
CD
PRO
A
708
20.543
34.966
22.141
1.00
36.01
A


ATOM
206
CA
PRO
A
708
18.640
33.487
21.954
1.00
33.79
A


ATOM
207
CB
PRO
A
708
18.937
34.194
20.632
1.00
33.78
A


ATOM
208
CG
PRO
A
708
19.611
35.460
21.065
1.00
35.82
A


ATOM
209
C
PRO
A
708
18.745
31.966
21.824
1.00
32.66
A


ATOM
210
O
PRO
A
708
19.848
31.420
21.802
1.00
31.44
A


ATOM
211
N
ASP
A
709
17.605
31.289
21.738
1.00
30.13
A


ATOM
212
CA
ASP
A
709
17.596
29.835
21.613
1.00
27.78
A


ATOM
213
CB
ASP
A
709
16.164
29.288
21.594
1.00
26.98
A


ATOM
214
CG
ASP
A
709
15.494
29.335
22.941
1.00
26.45
A


ATOM
215
OD1
ASP
A
709
16.180
29.603
23.947
1.00
27.85
A


ATOM
216
OD2
ASP
A
709
14.271
29.086
22.989
1.00
27.12
A


ATOM
217
C
ASP
A
709
18.257
29.357
20.337
1.00
27.24
A


ATOM
218
O
ASP
A
709
18.204
30.026
19.310
1.00
25.71
A


ATOM
219
N
THR
A
710
18.877
28.187
20.413
1.00
25.67
A


ATOM
220
CA
THR
A
710
19.480
27.565
19.245
1.00
26.35
A


ATOM
221
CB
THR
A
710
21.025
27.716
19.195
1.00
26.29
A


ATOM
222
OG1
THR
A
710
21.616
26.958
20.255
1.00
24.75
A


ATOM
223
CG2
THR
A
710
21.433
29.182
19.329
1.00
25.04
A


ATOM
224
C
THR
A
710
19.129
26.097
19.428
1.00
27.11
A


ATOM
225
O
THR
A
710
18.912
25.640
20.555
1.00
26.86
A


ATOM
226
N
SER
A
711
19.052
25.364
18.328
1.00
26.94
A


ATOM
227
CA
SER
A
711
18.725
23.950
18.395
1.00
30.05
A


ATOM
228
CB
SER
A
711
18.857
23.323
17.004
1.00
30.48
A


ATOM
229
OG
SER
A
711
18.600
21.934
17.046
1.00
35.04
A


ATOM
230
C
SER
A
711
19.644
23.227
19.382
1.00
29.29
A


ATOM
231
O
SER
A
711
19.187
22.424
20.197
1.00
30.34
A


ATOM
232
N
SER
A
712
20.937
23.529
19.326
1.00
27.88
A


ATOM
233
CA
SER
A
712
21.891
22.870
20.207
1.00
27.73
A


ATOM
234
CB
SER
A
712
23.322
23.089
19.706
1.00
30.70
A


ATOM
235
OG
SER
A
712
23.692
24.451
19.784
1.00
37.15
A


ATOM
236
C
SER
A
712
21.803
23.264
21.678
1.00
25.40
A


ATOM
237
O
SER
A
712
21.922
22.401
22.544
1.00
23.44
A


ATOM
238
N
SER
A
713
21.593
24.547
21.970
1.00
23.22
A


ATOM
239
CA
SER
A
713
21.519
24.983
23.363
1.00
23.17
A


ATOM
240
CB
SER
A
713
21.554
26.516
23.466
1.00
23.10
A


ATOM
241
OG
SER
A
713
20.364
27.104
22.976
1.00
27.55
A


ATOM
242
C
SER
A
713
20.277
24.442
24.068
1.00
21.24
A


ATOM
243
O
SER
A
713
20.332
24.077
25.246
1.00
20.24
A


ATOM
244
N
LEU
A
714
19.159
24.391
23.351
1.00
20.03
A


ATOM
245
CA
LEU
A
714
17.922
23.871
23.924
1.00
18.97
A


ATOM
246
CB
LEU
A
714
16.734
24.100
22.978
1.00
17.28
A


ATOM
247
CG
LEU
A
714
16.139
25.503
22.873
1.00
20.44
A


ATOM
248
CD1
LEU
A
714
14.961
25.473
21.901
1.00
16.61
A


ATOM
249
CD2
LEU
A
714
15.682
25.978
24.245
1.00
21.04
A


ATOM
250
C
LEU
A
714
18.039
22.378
24.215
1.00
17.72
A


ATOM
251
O
LEU
A
714
17.733
21.927
25.322
1.00
19.37
A


ATOM
252
N
LEU
A
715
18.476
21.610
23.222
1.00
16.17
A


ATOM
253
CA
LEU
A
715
18.611
20.163
23.396
1.00
16.51
A


ATOM
254
CB
LEU
A
715
18.941
19.497
22.054
1.00
15.83
A


ATOM
255
CG
LEU
A
715
17.839
19.637
20.990
1.00
17.05
A


ATOM
256
CD1
LEU
A
715
18.291
19.026
19.668
1.00
17.78
A


ATOM
257
CD2
LEU
A
715
16.566
18.953
21.489
1.00
17.52
A


ATOM
258
C
LEU
A
715
19.676
19.842
24.444
1.00
17.19
A


ATOM
259
O
LEU
A
715
19.526
18.905
25.233
1.00
15.94
A


ATOM
260
N
THR
A
716
20.755
20.618
24.456
1.00
16.23
A


ATOM
261
CA
THR
A
716
21.807
20.405
25.444
1.00
16.41
A


ATOM
262
CB
THR
A
716
23.002
21.353
25.192
1.00
17.33
A


ATOM
263
OG1
THR
A
716
23.719
20.901
24.039
1.00
18.63
A


ATOM
264
CG2
THR
A
716
23.946
21.383
26.393
1.00
18.48
A


ATOM
265
C
THR
A
716
21.254
20.625
26.855
1.00
17.19
A


ATOM
266
O
THR
A
716
21.569
19.873
27.777
1.00
17.56
A


ATOM
267
N
SER
A
717
20.422
21.649
27.025
1.00
17.82
A


ATOM
268
CA
SER
A
717
19.836
21.917
28.334
1.00
17.93
A


ATOM
269
CB
SER
A
717
19.142
23.282
28.349
1.00
18.40
A


ATOM
270
OG
SER
A
717
20.099
24.315
28.459
1.00
20.04
A


ATOM
271
C
SER
A
717
18.840
20.826
28.699
1.00
17.68
A


ATOM
272
O
SER
A
717
18.774
20.399
29.849
1.00
17.99
A


ATOM
273
N
LEU
A
718
18.060
20.372
27.723
1.00
18.63
A


ATOM
274
CA
LEU
A
718
17.092
19.312
27.987
1.00
18.40
A


ATOM
275
CB
LEU
A
718
16.256
19.022
26.733
1.00
18.14
A


ATOM
276
CG
LEU
A
718
15.122
20.027
26.496
1.00
17.83
A


ATOM
277
CD1
LEU
A
718
14.466
19.780
25.139
1.00
18.47
A


ATOM
278
CD2
LEU
A
718
14.096
19.894
27.626
1.00
19.81
A


ATOM
279
C
LEU
A
718
17.835
18.057
28.447
1.00
19.24
A


ATOM
280
O
LEU
A
718
17.357
17.320
29.317
1.00
18.56
A


ATOM
281
N
ASN
A
719
19.012
17.821
27.872
1.00
17.74
A


ATOM
282
CA
ASN
A
719
19.811
16.664
28.259
1.00
18.99
A


ATOM
283
CB
ASN
A
719
20.880
16.359
27.207
1.00
19.92
A


ATOM
284
CG
ASN
A
719
20.300
15.715
25.964
1.00
21.70
A


ATOM
285
OD1
ASN
A
719
19.264
15.051
26.023
1.00
22.14
A


ATOM
286
ND2
ASN
A
719
20.975
15.888
24.834
1.00
21.49
A


ATOM
287
C
ASN
A
719
20.464
16.870
29.625
1.00
19.54
A


ATOM
288
O
ASN
A
719
20.631
15.915
30.383
1.00
18.51
A


ATOM
289
N
GLN
A
720
20.833
18.111
29.946
1.00
20.24
A


ATOM
290
CA
GLN
A
720
21.438
18.383
31.248
1.00
20.89
A


ATOM
291
CB
GLN
A
720
22.024
19.804
31.299
1.00
24.62
A


ATOM
292
CG
GLN
A
720
22.851
20.080
32.562
1.00
29.69
A


ATOM
293
CD
GLN
A
720
23.710
21.344
32.462
1.00
34.45
A


ATOM
294
OE1
GLN
A
720
23.197
22.465
32.431
1.00
36.61
A


ATOM
295
NE2
GLN
A
720
25.024
21.159
32.409
1.00
34.00
A


ATOM
296
C
GLN
A
720
20.345
18.211
32.303
1.00
20.76
A


ATOM
297
O
GLN
A
720
20.571
17.608
33.355
1.00
18.85
A


ATOM
298
N
LEU
A
721
19.156
18.736
32.007
1.00
18.88
A


ATOM
299
CA
LEU
A
721
18.018
18.611
32.909
1.00
19.76
A


ATOM
300
CB
LEU
A
721
16.783
19.313
32.317
1.00
20.61
A


ATOM
301
CG
LEU
A
721
15.529
19.375
33.197
1.00
21.89
A


ATOM
302
CD1
LEU
A
721
15.845
20.126
34.491
1.00
17.83
A


ATOM
303
CD2
LEU
A
721
14.389
20.058
32.435
1.00
17.08
A


ATOM
304
C
LEU
A
721
17.743
17.115
33.063
1.00
18.66
A


ATOM
305
O
LEU
A
721
17.457
16.626
34.157
1.00
18.65
A


ATOM
306
N
GLY
A
722
17.839
16.392
31.953
1.00
18.59
A


ATOM
307
CA
GLY
A
722
17.623
14.959
31.981
1.00
18.69
A


ATOM
308
C
GLY
A
722
18.591
14.261
32.922
1.00
19.59
A


ATOM
309
O
GLY
A
722
18.184
13.426
33.735
1.00
21.70
A


ATOM
310
N
GLU
A
723
19.874
14.598
32.817
1.00
18.22
A


ATOM
311
CA
GLU
A
723
20.898
13.998
33.674
1.00
18.14
A


ATOM
312
CB
GLU
A
723
22.271
14.631
33.400
1.00
18.39
A


ATOM
313
CG
GLU
A
723
23.409
14.008
34.198
1.00
19.11
A


ATOM
314
CD
GLU
A
723
23.922
12.713
33.588
1.00
22.52
A


ATOM
315
OE1
GLU
A
723
23.277
12.184
32.655
1.00
22.75
A


ATOM
316
OE2
GLU
A
723
24.979
12.220
34.040
1.00
22.45
A


ATOM
317
C
GLU
A
723
20.549
14.209
35.145
1.00
18.01
A


ATOM
318
O
GLU
A
723
20.691
13.296
35.967
1.00
16.59
A


ATOM
319
N
ARG
A
724
20.110
15.422
35.474
1.00
17.42
A


ATOM
320
CA
ARG
A
724
19.742
15.756
36.850
1.00
19.72
A


ATOM
321
CB
ARG
A
724
19.551
17.266
36.987
1.00
20.72
A


ATOM
322
CG
ARG
A
724
20.820
18.047
36.693
1.00
21.86
A


ATOM
323
CD
ARG
A
724
20.602
19.549
36.744
1.00
23.18
A


ATOM
324
NE
ARG
A
724
21.855
20.245
36.465
1.00
23.39
A


ATOM
325
CZ
ARG
A
724
22.021
21.563
36.505
1.00
25.86
A


ATOM
326
NH1
ARG
A
724
21.008
22.362
36.813
1.00
24.78
A


ATOM
327
NH2
ARG
A
724
23.217
22.079
36.252
1.00
23.92
A


ATOM
328
C
ARG
A
724
18.476
15.029
37.292
1.00
20.26
A


ATOM
329
O
ARG
A
724
18.383
14.546
38.422
1.00
18.14
A


ATOM
330
N
GLN
A
725
17.493
14.947
36.405
1.00
19.29
A


ATOM
331
CA
GLN
A
725
16.271
14.256
36.762
1.00
21.28
A


ATOM
332
CB
GLN
A
725
15.191
14.504
35.705
1.00
23.07
A


ATOM
333
CG
GLN
A
725
14.691
15.955
35.716
1.00
27.51
A


ATOM
334
CD
GLN
A
725
13.556
16.210
34.743
1.00
30.36
A


ATOM
335
OE1
GLN
A
725
13.084
17.341
34.600
1.00
33.13
A


ATOM
336
NE2
GLN
A
725
13.111
15.161
34.068
1.00
31.54
A


ATOM
337
C
GLN
A
725
16.570
12.769
36.918
1.00
21.14
A


ATOM
338
O
GLN
A
725
15.952
12.087
37.731
1.00
21.59
A


ATOM
339
N
LEU
A
726
17.542
12.276
36.156
1.00
20.47
A


ATOM
340
CA
LEU
A
726
17.919
10.870
36.232
1.00
20.31
A


ATOM
341
CB
LEU
A
726
18.928
10.547
35.126
1.00
21.56
A


ATOM
342
CG
LEU
A
726
19.070
9.108
34.622
1.00
22.31
A


ATOM
343
CD1
LEU
A
726
17.705
8.482
34.346
1.00
20.98
A


ATOM
344
CD2
LEU
A
726
19.908
9.127
33.346
1.00
22.17
A


ATOM
345
C
LEU
A
726
18.512
10.607
37.621
1.00
21.15
A


ATOM
346
O
LEU
A
726
18.190
9.611
38.272
1.00
19.58
A


ATOM
347
N
LEU
A
727
19.375
11.509
38.077
1.00
19.81
A


ATOM
348
CA
LEU
A
727
19.972
11.376
39.400
1.00
20.36
A


ATOM
349
CB
LEU
A
727
20.927
12.535
39.662
1.00
23.93
A


ATOM
350
CG
LEU
A
727
22.304
12.433
39.009
1.00
26.70
A


ATOM
351
CD1
LEU
A
727
23.092
13.712
39.259
1.00
30.45
A


ATOM
352
CD2
LEU
A
727
23.037
11.231
39.586
1.00
27.44
A


ATOM
353
C
LEU
A
727
18.862
11.384
40.455
1.00
18.86
A


ATOM
354
O
LEU
A
727
18.910
10.637
41.437
1.00
17.62
A


ATOM
355
N
SER
A
728
17.863
12.229
40.223
1.00
17.97
A


ATOM
356
CA
SER
A
728
16.724
12.376
41.115
1.00
19.31
A


ATOM
357
CB
SER
A
728
15.836
13.523
40.625
1.00
21.26
A


ATOM
358
OG
SER
A
728
14.794
13.788
41.542
1.00
24.60
A


ATOM
359
C
SER
A
728
15.916
11.083
41.180
1.00
19.09
A


ATOM
360
O
SER
A
728
15.465
10.675
42.251
1.00
18.25
A


ATOM
361
N
VAL
A
729
15.730
10.445
40.027
1.00
18.98
A


ATOM
362
CA
VAL
A
729
14.990
9.190
39.962
1.00
17.54
A


ATOM
363
CB
VAL
A
729
14.814
8.720
38.498
1.00
17.32
A


ATOM
364
CG1
VAL
A
729
14.261
7.312
38.460
1.00
17.30
A


ATOM
365
CG2
VAL
A
729
13.875
9.676
37.770
1.00
19.41
A


ATOM
366
C
VAL
A
729
15.718
8.112
40.765
1.00
17.34
A


ATOM
367
O
VAL
A
729
15.095
7.382
41.537
1.00
16.18
A


ATOM
368
N
VAL
A
730
17.033
8.015
40.590
1.00
15.92
A


ATOM
369
CA
VAL
A
730
17.812
7.024
41.330
1.00
16.21
A


ATOM
370
CB
VAL
A
730
19.321
7.098
40.957
1.00
17.70
A


ATOM
371
CG1
VAL
A
730
20.151
6.236
41.909
1.00
17.59
A


ATOM
372
CG2
VAL
A
730
19.518
6.592
39.533
1.00
19.79
A


ATOM
373
C
VAL
A
730
17.628
7.234
42.840
1.00
18.41
A


ATOM
374
O
VAL
A
730
17.364
6.282
43.582
1.00
20.77
A


ATOM
375
N
LYS
A
731
17.747
8.480
43.290
1.00
18.40
A


ATOM
376
CA
LYS
A
731
17.571
8.809
44.707
1.00
19.11
A


ATOM
377
CB
LYS
A
731
17.806
10.307
44.915
1.00
22.06
A


ATOM
378
CG
LYS
A
731
17.424
10.842
46.297
1.00
26.05
A


ATOM
379
CD
LYS
A
731
18.409
10.437
47.379
1.00
30.61
A


ATOM
380
CE
LYS
A
731
18.029
11.072
48.717
1.00
32.42
A


ATOM
381
NZ
LYS
A
731
19.059
10.845
49.766
1.00
35.26
A


ATOM
382
C
LYS
A
731
16.158
8.435
45.179
1.00
19.62
A


ATOM
383
O
LYS
A
731
15.973
7.778
46.209
1.00
19.40
A


ATOM
384
N
TRP
A
732
15.164
8.873
44.417
1.00
18.65
A


ATOM
385
CA
TRP
A
732
13.767
8.595
44.714
1.00
16.92
A


ATOM
386
CB
TRP
A
732
12.905
9.226
43.617
1.00
18.08
A


ATOM
387
CG
TRP
A
732
11.453
8.863
43.602
1.00
16.59
A


ATOM
388
CD2
TRP
A
732
10.791
8.069
42.612
1.00
18.88
A


ATOM
389
CE2
TRP
A
732
9.412
8.062
42.931
1.00
19.08
A


ATOM
390
CE3
TRP
A
732
11.228
7.366
41.478
1.00
16.99
A


ATOM
391
CD1
TRP
A
732
10.481
9.286
44.469
1.00
19.57
A


ATOM
392
NE1
TRP
A
732
9.250
8.810
44.069
1.00
18.44
A


ATOM
393
CZ2
TRP
A
732
8.467
7.375
42.157
1.00
19.26
A


ATOM
394
CZ3
TRP
A
732
10.289
6.685
40.710
1.00
17.20
A


ATOM
395
CH2
TRP
A
732
8.923
6.697
41.054
1.00
18.84
A


ATOM
396
C
TRP
A
732
13.508
7.090
44.808
1.00
16.34
A


ATOM
397
O
TRP
A
732
12.876
6.611
45.754
1.00
17.11
A


ATOM
398
N
SER
A
733
14.016
6.341
43.838
1.00
16.51
A


ATOM
399
CA
SER
A
733
13.803
4.901
43.813
1.00
18.54
A


ATOM
400
CB
SER
A
733
14.448
4.287
42.561
1.00
18.74
A


ATOM
401
OG
SER
A
733
15.861
4.291
42.643
1.00
18.35
A


ATOM
402
C
SER
A
733
14.319
4.202
45.072
1.00
19.10
A


ATOM
403
O
SER
A
733
13.749
3.196
45.508
1.00
18.34
A


ATOM
404
N
LYS
A
734
15.385
4.741
45.658
1.00
18.85
A


ATOM
405
CA
LYS
A
734
15.958
4.160
46.865
1.00
19.80
A


ATOM
406
CB
LYS
A
734
17.295
4.831
47.200
1.00
22.02
A


ATOM
407
CG
LYS
A
734
18.381
4.547
46.178
1.00
24.28
A


ATOM
408
CD
LYS
A
734
19.678
5.259
46.517
1.00
29.24
A


ATOM
409
CE
LYS
A
734
20.717
5.021
45.429
1.00
30.96
A


ATOM
410
NZ
LYS
A
734
21.974
5.767
45.688
1.00
34.40
A


ATOM
411
C
LYS
A
734
15.012
4.275
48.054
1.00
19.01
A


ATOM
412
O
LYS
A
734
15.107
3.500
49.000
1.00
18.14
A


ATOM
413
N
SER
A
735
14.099
5.240
47.998
1.00
19.77
A


ATOM
414
CA
SER
A
735
13.131
5.445
49.075
1.00
20.89
A


ATOM
415
CB
SER
A
735
13.032
6.931
49.418
1.00
21.77
A


ATOM
416
OG
SER
A
735
14.270
7.412
49.899
1.00
26.19
A


ATOM
417
C
SER
A
735
11.741
4.928
48.735
1.00
18.31
A


ATOM
418
O
SER
A
735
10.864
4.888
49.594
1.00
17.33
A


ATOM
419
N
LEU
A
736
11.544
4.544
47.480
1.00
18.55
A


ATOM
420
CA
LEU
A
736
10.258
4.036
47.007
1.00
16.70
A


ATOM
421
CB
LEU
A
736
10.280
3.936
45.478
1.00
16.07
A


ATOM
422
CG
LEU
A
736
9.049
3.372
44.766
1.00
17.19
A


ATOM
423
CD1
LEU
A
736
7.807
4.227
45.062
1.00
16.11
A


ATOM
424
CD2
LEU
A
736
9.328
3.338
43.270
1.00
12.10
A


ATOM
425
C
LEU
A
736
9.954
2.670
47.622
1.00
16.59
A


ATOM
426
O
LEU
A
736
10.643
1.686
47.341
1.00
14.96
A


ATOM
427
N
PRO
A
737
8.906
2.588
48.461
1.00
16.50
A


ATOM
428
CD
PRO
A
737
7.985
3.652
48.900
1.00
15.57
A


ATOM
429
CA
PRO
A
737
8.564
1.306
49.092
1.00
18.45
A


ATOM
430
CB
PRO
A
737
7.215
1.593
49.753
1.00
18.84
A


ATOM
431
CG
PRO
A
737
7.356
3.040
50.154
1.00
16.58
A


ATOM
432
C
PRO
A
737
8.510
0.127
48.126
1.00
20.18
A


ATOM
433
O
PRO
A
737
7.839
0.181
47.090
1.00
18.72
A


ATOM
434
N
GLY
A
738
9.244
−0.928
48.468
1.00
19.99
A


ATOM
435
CA
GLY
A
738
9.269
−2.122
47.643
1.00
20.37
A


ATOM
436
C
GLY
A
738
10.379
−2.222
46.609
1.00
21.67
A


ATOM
437
O
GLY
A
738
10.883
−3.314
46.344
1.00
22.52
A


ATOM
438
N
PHE
A
739
10.784
−1.094
46.033
1.00
20.61
A


ATOM
439
CA
PHE
A
739
11.807
−1.113
44.988
1.00
19.83
A


ATOM
440
CB
PHE
A
739
12.028
0.300
44.431
1.00
19.10
A


ATOM
441
CG
PHE
A
739
12.605
0.322
43.035
1.00
19.43
A


ATOM
442
CD1
PHE
A
739
11.907
−0.252
41.972
1.00
20.73
A


ATOM
443
CD2
PHE
A
739
13.835
0.925
42.782
1.00
21.00
A


ATOM
444
CE1
PHE
A
739
12.426
−0.225
40.669
1.00
20.34
A


ATOM
445
CE2
PHE
A
739
14.366
0.961
41.482
1.00
20.08
A


ATOM
446
CZ
PHE
A
739
13.653
0.381
40.424
1.00
18.50
A


ATOM
447
C
PHE
A
739
13.154
−1.703
45.404
1.00
20.67
A


ATOM
448
O
PHE
A
739
13.695
−2.555
44.708
1.00
19.78
A


ATOM
449
N
ARG
A
740
13.690
−1.248
46.532
1.00
21.77
A


ATOM
450
CA
ARG
A
740
14.990
−1.716
47.010
1.00
22.39
A


ATOM
451
CB
ARG
A
740
15.355
−1.009
48.321
1.00
21.37
A


ATOM
452
CG
ARG
A
740
14.409
−1.304
49.480
1.00
21.34
A


ATOM
453
CD
ARG
A
740
14.946
−0.719
50.780
1.00
19.50
A


ATOM
454
NE
ARG
A
740
14.050
−0.960
51.908
1.00
20.23
A


ATOM
455
CZ
ARG
A
740
14.351
−0.652
53.165
1.00
20.17
A


ATOM
456
NH1
ARG
A
740
15.520
−0.095
53.442
1.00
18.30
A


ATOM
457
NH2
ARG
A
740
13.488
−0.900
54.144
1.00
19.12
A


ATOM
458
C
ARG
A
740
15.092
−3.225
47.213
1.00
24.06
A


ATOM
459
O
ARG
A
740
16.195
−3.776
47.272
1.00
24.88
A


ATOM
460
N
ASN
A
741
13.953
−3.899
47.308
1.00
24.13
A


ATOM
461
CA
ASN
A
741
13.962
−5.340
47.531
1.00
26.03
A


ATOM
462
CB
ASN
A
741
12.744
−5.736
48.373
1.00
27.83
A


ATOM
463
CG
ASN
A
741
12.650
−4.931
49.660
1.00
29.37
A


ATOM
464
OD1
ASN
A
741
13.637
−4.780
50.381
1.00
29.40
A


ATOM
465
ND2
ASN
A
741
11.464
−4.409
49.952
1.00
30.58
A


ATOM
466
C
ASN
A
741
14.042
−6.172
46.253
1.00
25.13
A


ATOM
467
O
ASN
A
741
14.128
−7.401
46.305
1.00
24.44
A


ATOM
468
N
LEU
A
742
14.012
−5.504
45.104
1.00
22.83
A


ATOM
469
CA
LEU
A
742
14.135
−6.197
43.831
1.00
21.37
A


ATOM
470
CB
LEU
A
742
13.496
−5.384
42.698
1.00
21.88
A


ATOM
471
CG
LEU
A
742
12.009
−5.019
42.812
1.00
21.52
A


ATOM
472
CD1
LEU
A
742
11.613
−4.138
41.624
1.00
21.95
A


ATOM
473
CD2
LEU
A
742
11.159
−6.284
42.840
1.00
19.89
A


ATOM
474
C
LEU
A
742
15.637
−6.311
43.597
1.00
21.92
A


ATOM
475
O
LEU
A
742
16.406
−5.514
44.130
1.00
21.09
A


ATOM
476
N
HIS
A
743
16.057
−7.302
42.818
1.00
23.00
A


ATOM
477
CA
HIS
A
743
17.477
−7.485
42.527
1.00
23.50
A


ATOM
478
CB
HIS
A
743
17.652
−8.612
41.507
1.00
25.73
A


ATOM
479
CG
HIS
A
743
19.071
−9.056
41.328
1.00
29.22
A


ATOM
480
CD2
HIS
A
743
19.697
−10.202
41.690
1.00
29.68
A


ATOM
481
ND1
HIS
A
743
20.025
−8.277
40.708
1.00
28.89
A


ATOM
482
CE1
HIS
A
743
21.177
−8.925
40.694
1.00
31.58
A


ATOM
483
NE2
HIS
A
743
21.005
−10.096
41.283
1.00
31.35
A


ATOM
484
C
HIS
A
743
18.011
−6.170
41.961
1.00
24.00
A


ATOM
485
O
HIS
A
743
17.290
−5.459
41.252
1.00
22.58
A


ATOM
486
N
ILE
A
744
19.260
−5.840
42.276
1.00
22.45
A


ATOM
487
CA
ILE
A
744
19.854
−4.598
41.791
1.00
23.13
A


ATOM
488
CB
ILE
A
744
21.316
−4.437
42.286
1.00
24.13
A


ATOM
489
CG2
ILE
A
744
22.158
−5.623
41.829
1.00
23.77
A


ATOM
490
CG1
ILE
A
744
21.908
−3.128
41.751
1.00
25.51
A


ATOM
491
CD1
ILE
A
744
21.194
−1.865
42.234
1.00
27.84
A


ATOM
492
C
ILE
A
744
19.819
−4.496
40.263
1.00
21.80
A


ATOM
493
O
ILE
A
744
19.639
−3.406
39.715
1.00
19.60
A


ATOM
494
N
ASP
A
745
19.990
−5.622
39.574
1.00
21.91
A


ATOM
495
CA
ASP
A
745
19.945
−5.609
38.112
1.00
21.89
A


ATOM
496
CB
ASP
A
745
20.271
−6.987
37.526
1.00
25.03
A


ATOM
497
CG
ASP
A
745
21.706
−7.415
37.776
1.00
27.05
A


ATOM
498
OD1
ASP
A
745
22.562
−6.546
38.028
1.00
28.56
A


ATOM
499
OD2
ASP
A
745
21.973
−8.632
37.703
1.00
31.09
A


ATOM
500
C
ASP
A
745
18.545
−5.210
37.653
1.00
20.59
A


ATOM
501
O
ASP
A
745
18.386
−4.530
36.637
1.00
19.07
A


ATOM
502
N
ASP
A
746
17.530
−5.656
38.391
1.00
19.31
A


ATOM
503
CA
ASP
A
746
16.154
−5.332
38.043
1.00
18.60
A


ATOM
504
CB
ASP
A
746
15.160
−6.124
38.903
1.00
19.50
A


ATOM
505
CG
ASP
A
746
15.187
−7.620
38.620
1.00
20.87
A


ATOM
506
OD1
ASP
A
746
15.631
−8.029
37.530
1.00
24.46
A


ATOM
507
OD2
ASP
A
746
14.743
−8.391
39.493
1.00
22.73
A


ATOM
508
C
ASP
A
746
15.901
−3.842
38.232
1.00
18.23
A


ATOM
509
O
ASP
A
746
15.283
−3.201
37.383
1.00
16.68
A


ATOM
510
N
GLN
A
747
16.379
−3.294
39.347
1.00
16.31
A


ATOM
511
CA
GLN
A
747
16.196
−1.877
39.635
1.00
16.33
A


ATOM
512
CB
GLN
A
747
16.870
−1.505
40.965
1.00
17.68
A


ATOM
513
CG
GLN
A
747
16.402
−2.330
42.158
1.00
16.41
A


ATOM
514
CD
GLN
A
747
17.039
−1.894
43.471
1.00
19.86
A


ATOM
515
OE1
GLN
A
747
17.270
−2.714
44.361
1.00
21.96
A


ATOM
516
NE2
GLN
A
747
17.307
−0.601
43.605
1.00
13.08
A


ATOM
517
C
GLN
A
747
16.790
−1.025
38.519
1.00
16.94
A


ATOM
518
O
GLN
A
747
16.158
−0.083
38.032
1.00
16.26
A


ATOM
519
N
ILE
A
748
18.011
−1.360
38.119
1.00
17.19
A


ATOM
520
CA
ILE
A
748
18.694
−0.621
37.067
1.00
17.75
A


ATOM
521
CB
ILE
A
748
20.133
−1.136
36.867
1.00
18.93
A


ATOM
522
CG2
ILE
A
748
20.736
−0.537
35.591
1.00
19.15
A


ATOM
523
CG1
ILE
A
748
20.979
−0.780
38.094
1.00
19.91
A


ATOM
524
CD1
ILE
A
748
22.419
−1.268
38.003
1.00
26.17
A


ATOM
525
C
ILE
A
748
17.951
−0.726
35.745
1.00
16.60
A


ATOM
526
O
ILE
A
748
17.801
0.263
35.035
1.00
17.71
A


ATOM
527
N
THR
A
749
17.490
−1.926
35.415
1.00
16.86
A


ATOM
528
CA
THR
A
749
16.772
−2.128
34.166
1.00
17.95
A


ATOM
529
CB
THR
A
749
16.441
−3.618
33.942
1.00
18.55
A


ATOM
530
OG1
THR
A
749
17.657
−4.358
33.776
1.00
19.19
A


ATOM
531
CG2
THR
A
749
15.589
−3.794
32.695
1.00
19.51
A


ATOM
532
C
THR
A
749
15.479
−1.317
34.114
1.00
17.38
A


ATOM
533
O
THR
A
749
15.178
−0.690
33.099
1.00
17.28
A


ATOM
534
N
LEU
A
750
14.720
−1.327
35.206
1.00
16.72
A


ATOM
535
CA
LEU
A
750
13.455
−0.591
35.259
1.00
16.64
A


ATOM
536
CB
LEU
A
750
12.727
−0.887
36.576
1.00
15.87
A


ATOM
537
CG
LEU
A
750
12.229
−2.334
36.712
1.00
17.09
A


ATOM
538
CD1
LEU
A
750
11.660
−2.569
38.111
1.00
13.60
A


ATOM
539
CD2
LEU
A
750
11.166
−2.604
35.642
1.00
15.56
A


ATOM
540
C
LEU
A
750
13.675
0.911
35.097
1.00
17.48
A


ATOM
541
O
LEU
A
750
12.894
1.599
34.423
1.00
16.71
A


ATOM
542
N
ILE
A
751
14.737
1.427
35.706
1.00
16.32
A


ATOM
543
CA
ILE
A
751
15.026
2.850
35.581
1.00
17.20
A


ATOM
544
CB
ILE
A
751
16.123
3.289
36.576
1.00
18.58
A


ATOM
545
CG2
ILE
A
751
16.583
4.694
36.251
1.00
17.18
A


ATOM
546
CG1
ILE
A
751
15.581
3.223
38.010
1.00
17.86
A


ATOM
547
CD1
ILE
A
751
16.642
3.467
39.092
1.00
20.51
A


ATOM
548
C
ILE
A
751
15.464
3.190
34.151
1.00
17.20
A


ATOM
549
O
ILE
A
751
15.093
4.234
33.613
1.00
16.21
A


ATOM
550
N
GLN
A
752
16.241
2.306
33.534
1.00
17.94
A


ATOM
551
CA
GLN
A
752
16.714
2.543
32.169
1.00
18.41
A


ATOM
552
CB
GLN
A
752
17.844
1.571
31.824
1.00
19.20
A


ATOM
553
CG
GLN
A
752
19.052
1.687
32.760
1.00
21.33
A


ATOM
554
CD
GLN
A
752
20.237
0.850
32.311
1.00
22.26
A


ATOM
555
OE1
GLN
A
752
20.075
−0.214
31.717
1.00
21.77
A


ATOM
556
NE2
GLN
A
752
21.439
1.323
32.614
1.00
22.92
A


ATOM
557
C
GLN
A
752
15.600
2.435
31.128
1.00
19.31
A


ATOM
558
O
GLN
A
752
15.657
3.088
30.082
1.00
19.71
A


ATOM
559
N
TYR
A
753
14.594
1.609
31.408
1.00
16.40
A


ATOM
560
CA
TYR
A
753
13.468
1.445
30.488
1.00
17.45
A


ATOM
561
CB
TYR
A
753
12.649
0.189
30.812
1.00
16.91
A


ATOM
562
CG
TYR
A
753
13.220
−1.160
30.420
1.00
18.88
A


ATOM
563
CD1
TYR
A
753
14.312
−1.280
29.560
1.00
19.37
A


ATOM
564
CE1
TYR
A
753
14.775
−2.542
29.158
1.00
19.99
A


ATOM
565
CD2
TYR
A
753
12.609
−2.329
30.874
1.00
20.86
A


ATOM
566
CE2
TYR
A
753
13.058
−3.579
30.483
1.00
19.71
A


ATOM
567
CZ
TYR
A
753
14.134
−3.685
29.628
1.00
21.49
A


ATOM
568
OH
TYR
A
753
14.546
−4.944
29.251
1.00
22.20
A


ATOM
569
C
TYR
A
753
12.480
2.606
30.583
1.00
18.38
A


ATOM
570
O
TYR
A
753
11.925
3.053
29.578
1.00
20.69
A


ATOM
571
N
SER
A
754
12.263
3.080
31.804
1.00
16.00
A


ATOM
572
CA
SER
A
754
11.259
4.108
32.070
1.00
17.01
A


ATOM
573
CB
SER
A
754
10.514
3.731
33.349
1.00
16.69
A


ATOM
574
OG
SER
A
754
11.362
3.939
34.477
1.00
14.48
A


ATOM
575
C
SER
A
754
11.651
5.574
32.195
1.00
16.37
A


ATOM
576
O
SER
A
754
10.774
6.425
32.338
1.00
15.97
A


ATOM
577
N
TRP
A
755
12.934
5.896
32.141
1.00
16.30
A


ATOM
578
CA
TRP
A
755
13.310
7.289
32.333
1.00
16.48
A


ATOM
579
CB
TRP
A
755
14.828
7.468
32.235
1.00
17.08
A


ATOM
580
CG
TRP
A
755
15.389
7.268
30.884
1.00
19.06
A


ATOM
581
CD2
TRP
A
755
15.593
8.276
29.890
1.00
18.43
A


ATOM
582
CE2
TRP
A
755
16.138
7.640
28.757
1.00
18.03
A


ATOM
583
CE3
TRP
A
755
15.364
9.657
29.848
1.00
20.60
A


ATOM
584
CD1
TRP
A
755
15.807
6.093
30.333
1.00
21.01
A


ATOM
585
NE1
TRP
A
755
16.260
6.308
29.053
1.00
21.00
A


ATOM
586
CZ2
TRP
A
755
16.462
8.336
27.590
1.00
20.14
A


ATOM
587
CZ3
TRP
A
755
15.686
10.351
28.687
1.00
23.49
A


ATOM
588
CH2
TRP
A
755
16.229
9.686
27.572
1.00
20.73
A


ATOM
589
C
TRP
A
755
12.608
8.330
31.461
1.00
16.13
A


ATOM
590
O
TRP
A
755
12.208
9.372
31.970
1.00
15.92
A


ATOM
591
N
MET
A
756
12.450
8.073
30.165
1.00
15.54
A


ATOM
592
CA
MET
A
756
11.791
9.066
29.314
1.00
15.68
A


ATOM
593
CB
MET
A
756
11.881
8.677
27.832
1.00
15.94
A


ATOM
594
CG
MET
A
756
11.294
9.720
26.872
1.00
15.93
A


ATOM
595
SD
MET
A
756
12.195
11.300
26.820
1.00
20.03
A


ATOM
596
CE
MET
A
756
13.530
10.864
25.738
1.00
18.29
A


ATOM
597
C
MET
A
756
10.327
9.249
29.710
1.00
15.47
A


ATOM
598
O
MET
A
756
9.837
10.379
29.778
1.00
15.06
A


ATOM
599
N
SER
A
757
9.627
8.150
29.983
1.00
16.31
A


ATOM
600
CA
SER
A
757
8.226
8.258
30.371
1.00
17.31
A


ATOM
601
CB
SER
A
757
7.569
6.872
30.481
1.00
19.17
A


ATOM
602
OG
SER
A
757
8.121
6.111
31.537
1.00
23.52
A


ATOM
603
C
SER
A
757
8.087
9.005
31.690
1.00
16.83
A


ATOM
604
O
SER
A
757
7.166
9.798
31.855
1.00
16.08
A


ATOM
605
N
LEU
A
758
8.998
8.765
32.632
1.00
16.85
A


ATOM
606
CA
LEU
A
758
8.918
9.456
33.915
1.00
15.97
A


ATOM
607
CB
LEU
A
758
9.940
8.899
34.911
1.00
17.47
A


ATOM
608
CG
LEU
A
758
9.748
7.461
35.401
1.00
18.97
A


ATOM
609
CD1
LEU
A
758
10.879
7.100
36.362
1.00
19.01
A


ATOM
610
CD2
LEU
A
758
8.408
7.324
36.094
1.00
18.02
A


ATOM
611
C
LEU
A
758
9.156
10.950
33.730
1.00
15.21
A


ATOM
612
O
LEU
A
758
8.469
11.774
34.333
1.00
14.38
A


ATOM
613
N
MET
A
759
10.131
11.301
32.895
1.00
15.87
A


ATOM
614
CA
MET
A
759
10.424
12.707
32.650
1.00
15.98
A


ATOM
615
CB
MET
A
759
11.675
12.855
31.784
1.00
18.16
A


ATOM
616
CG
MET
A
759
12.968
12.528
32.506
1.00
20.79
A


ATOM
617
SD
MET
A
759
14.388
12.785
31.431
1.00
26.08
A


ATOM
618
CE
MET
A
759
15.672
11.980
32.416
1.00
25.95
A


ATOM
619
C
MET
A
759
9.266
13.441
31.981
1.00
16.81
A


ATOM
620
O
MET
A
759
8.900
14.542
32.392
1.00
18.56
A


ATOM
621
N
VAL
A
760
8.688
12.837
30.949
1.00
17.28
A


ATOM
622
CA
VAL
A
760
7.590
13.483
30.241
1.00
17.08
A


ATOM
623
CB
VAL
A
760
7.290
12.761
28.897
1.00
18.35
A


ATOM
624
CG1
VAL
A
760
6.511
11.486
29.137
1.00
19.74
A


ATOM
625
CG2
VAL
A
760
6.545
13.699
27.964
1.00
20.50
A


ATOM
626
C
VAL
A
760
6.330
13.548
31.111
1.00
18.39
A


ATOM
627
O
VAL
A
760
5.547
14.499
31.017
1.00
19.10
A


ATOM
628
N
PHE
A
761
6.140
12.545
31.963
1.00
16.68
A


ATOM
629
CA
PHE
A
761
4.986
12.523
32.857
1.00
16.45
A


ATOM
630
CB
PHE
A
761
4.897
11.174
33.575
1.00
16.18
A


ATOM
631
CG
PHE
A
761
3.529
10.861
34.130
1.00
15.95
A


ATOM
632
CD1
PHE
A
761
2.420
10.794
33.290
1.00
13.24
A


ATOM
633
CD2
PHE
A
761
3.359
10.588
35.485
1.00
15.65
A


ATOM
634
CE1
PHE
A
761
1.164
10.457
33.791
1.00
14.74
A


ATOM
635
CE2
PHE
A
761
2.104
10.248
35.997
1.00
16.67
A


ATOM
636
CZ
PHE
A
761
1.007
10.183
35.148
1.00
16.46
A


ATOM
637
C
PHE
A
761
5.155
13.651
33.876
1.00
16.84
A


ATOM
638
O
PHE
A
761
4.205
14.377
34.175
1.00
17.63
A


ATOM
639
N
GLY
A
762
6.372
13.798
34.400
1.00
15.02
A


ATOM
640
CA
GLY
A
762
6.644
14.853
35.363
1.00
15.08
A


ATOM
641
C
GLY
A
762
6.480
16.213
34.706
1.00
15.77
A


ATOM
642
O
GLY
A
762
5.978
17.158
35.316
1.00
16.20
A


ATOM
643
N
LEU
A
763
6.920
16.317
33.457
1.00
15.32
A


ATOM
644
CA
LEU
A
763
6.796
17.559
32.706
1.00
17.12
A


ATOM
645
CB
LEU
A
763
7.346
17.373
31.294
1.00
17.85
A


ATOM
646
CG
LEU
A
763
6.960
18.409
30.236
1.00
18.06
A


ATOM
647
CD1
LEU
A
763
7.544
19.779
30.588
1.00
17.06
A


ATOM
648
CD2
LEU
A
763
7.473
17.931
28.878
1.00
16.76
A


ATOM
649
C
LEU
A
763
5.316
17.906
32.627
1.00
17.25
A


ATOM
650
O
LEU
A
763
4.920
19.064
32.795
1.00
16.63
A


ATOM
651
N
GLY
A
764
4.511
16.883
32.365
1.00
17.94
A


ATOM
652
CA
GLY
A
764
3.077
17.067
32.265
1.00
19.00
A


ATOM
653
C
GLY
A
764
2.510
17.652
33.540
1.00
19.54
A


ATOM
654
O
GLY
A
764
1.750
18.621
33.497
1.00
18.93
A


ATOM
655
N
TRP
A
765
2.890
17.073
34.677
1.00
19.11
A


ATOM
656
CA
TRP
A
765
2.408
17.539
35.971
1.00
20.62
A


ATOM
657
CB
TRP
A
765
2.930
16.632
37.092
1.00
21.33
A


ATOM
658
CG
TRP
A
765
2.414
17.012
38.449
1.00
23.29
A


ATOM
659
CD2
TRP
A
765
1.078
16.833
38.937
1.00
23.57
A


ATOM
660
CE2
TRP
A
765
1.034
17.368
40.242
1.00
25.22
A


ATOM
661
CE3
TRP
A
765
−0.088
16.272
38.396
1.00
25.69
A


ATOM
662
CD1
TRP
A
765
3.107
17.630
39.449
1.00
24.56
A


ATOM
663
NE1
TRP
A
765
2.284
17.848
40.532
1.00
25.99
A


ATOM
664
CZ2
TRP
A
765
−0.132
17.362
41.016
1.00
27.48
A


ATOM
665
CZ3
TRP
A
765
−1.248
16.266
39.166
1.00
24.65
A


ATOM
666
CH2
TRP
A
765
−1.259
16.808
40.460
1.00
25.43
A


ATOM
667
C
TRP
A
765
2.794
18.988
36.255
1.00
19.81
A


ATOM
668
O
TRP
A
765
1.928
19.812
36.546
1.00
19.54
A


ATOM
669
N
ARG
A
766
4.087
19.299
36.174
1.00
19.47
A


ATOM
670
CA
ARG
A
766
4.556
20.666
36.421
1.00
19.40
A


ATOM
671
CB
ARG
A
766
6.080
20.763
36.247
1.00
18.97
A


ATOM
672
CG
ARG
A
766
6.882
20.041
37.320
1.00
19.48
A


ATOM
673
CD
ARG
A
766
8.363
20.419
37.252
1.00
17.56
A


ATOM
674
NE
ARG
A
766
8.984
20.012
35.994
1.00
18.67
A


ATOM
675
CZ
ARG
A
766
9.269
18.755
35.666
1.00
20.53
A


ATOM
676
NH1
ARG
A
766
8.996
17.761
36.502
1.00
19.81
A


ATOM
677
NH2
ARG
A
766
9.822
18.488
34.492
1.00
17.68
A


ATOM
678
C
ARG
A
766
3.884
21.687
35.505
1.00
19.03
A


ATOM
679
O
ARG
A
766
3.505
22.774
35.944
1.00
19.25
A


ATOM
680
N
SER
A
767
3.741
21.348
34.229
1.00
18.79
A


ATOM
681
CA
SER
A
767
3.108
22.265
33.281
1.00
18.18
A


ATOM
682
CB
SER
A
767
3.140
21.671
31.875
1.00
19.63
A


ATOM
683
OG
SER
A
767
4.472
21.475
31.433
1.00
20.37
A


ATOM
684
C
SER
A
767
1.662
22.507
33.708
1.00
20.50
A


ATOM
685
O
SER
A
767
1.156
23.638
33.670
1.00
17.64
A


ATOM
686
N
TYR
A
768
1.008
21.427
34.123
1.00
21.00
A


ATOM
687
CA
TYR
A
768
−0.375
21.465
34.579
1.00
22.52
A


ATOM
688
CB
TYR
A
768
−0.845
20.027
34.853
1.00
24.84
A


ATOM
689
CG
TYR
A
768
−2.213
19.874
35.490
1.00
26.80
A


ATOM
690
CD1
TYR
A
768
−3.330
20.524
34.968
1.00
27.94
A


ATOM
691
CE1
TYR
A
768
−4.601
20.319
35.505
1.00
28.43
A


ATOM
692
CD2
TYR
A
768
−2.401
19.012
36.577
1.00
28.57
A


ATOM
693
CE2
TYR
A
768
−3.672
18.799
37.119
1.00
29.44
A


ATOM
694
CZ
TYR
A
768
−4.765
19.455
36.575
1.00
30.55
A


ATOM
695
OH
TYR
A
768
−6.024
19.238
37.092
1.00
32.27
A


ATOM
696
C
TYR
A
768
−0.545
22.328
35.834
1.00
23.30
A


ATOM
697
O
TYR
A
768
−1.411
23.202
35.884
1.00
23.03
A


ATOM
698
N
LYS
A
769
0.296
22.100
36.836
1.00
24.38
A


ATOM
699
CA
LYS
A
769
0.195
22.834
38.097
1.00
25.93
A


ATOM
700
CB
LYS
A
769
0.828
22.013
39.228
1.00
29.02
A


ATOM
701
CG
LYS
A
769
0.293
20.591
39.364
1.00
33.47
A


ATOM
702
CD
LYS
A
769
−1.225
20.546
39.541
1.00
36.41
A


ATOM
703
CE
LYS
A
769
−1.671
21.179
40.850
1.00
37.62
A


ATOM
704
NZ
LYS
A
769
−3.160
21.214
40.952
1.00
38.42
A


ATOM
705
C
LYS
A
769
0.759
24.255
38.155
1.00
25.94
A


ATOM
706
O
LYS
A
769
0.248
25.085
38.908
1.00
25.87
A


ATOM
707
N
HIS
A
770
1.799
24.549
37.380
1.00
25.10
A


ATOM
708
CA
HIS
A
770
2.405
25.881
37.425
1.00
25.51
A


ATOM
709
CB
HIS
A
770
3.928
25.770
37.294
1.00
28.44
A


ATOM
710
CG
HIS
A
770
4.572
24.979
38.389
1.00
32.15
A


ATOM
711
CD2
HIS
A
770
5.154
23.755
38.383
1.00
33.76
A


ATOM
712
ND1
HIS
A
770
4.641
25.427
39.691
1.00
36.27
A


ATOM
713
CE1
HIS
A
770
5.236
24.515
40.439
1.00
35.37
A


ATOM
714
NE2
HIS
A
770
5.557
23.490
39.670
1.00
34.58
A


ATOM
715
C
HIS
A
770
1.893
26.879
36.390
1.00
25.25
A


ATOM
716
O
HIS
A
770
1.779
28.073
36.679
1.00
25.06
A


ATOM
717
N
VAL
A
771
1.601
26.404
35.185
1.00
22.32
A


ATOM
718
CA
VAL
A
771
1.132
27.300
34.134
1.00
22.97
A


ATOM
719
CB
VAL
A
771
2.213
27.486
33.043
1.00
23.19
A


ATOM
720
CG1
VAL
A
771
3.326
28.385
33.575
1.00
23.98
A


ATOM
721
CG2
VAL
A
771
2.786
26.134
32.630
1.00
23.30
A


ATOM
722
C
VAL
A
771
−0.179
26.869
33.491
1.00
21.91
A


ATOM
723
O
VAL
A
771
−0.411
27.101
32.305
1.00
23.10
A


ATOM
724
N
SER
A
772
−1.036
26.247
34.291
1.00
20.67
A


ATOM
725
CA
SER
A
772
−2.340
25.796
33.825
1.00
22.11
A


ATOM
726
CB
SER
A
772
−3.226
27.012
33.532
1.00
23.44
A


ATOM
727
OG
SER
A
772
−3.245
27.902
34.643
1.00
22.81
A


ATOM
728
C
SER
A
772
−2.222
24.923
32.583
1.00
21.42
A


ATOM
729
O
SER
A
772
−3.157
24.830
31.781
1.00
21.19
A


ATOM
730
N
GLY
A
773
−1.060
24.292
32.426
1.00
21.10
A


ATOM
731
CA
GLY
A
773
−0.820
23.415
31.292
1.00
19.40
A


ATOM
732
C
GLY
A
773
−0.654
24.099
29.944
1.00
20.22
A


ATOM
733
O
GLY
A
773
−0.603
23.426
28.911
1.00
21.05
A


ATOM
734
N
GLN
A
774
−0.541
25.423
29.935
1.00
19.35
A


ATOM
735
CA
GLN
A
774
−0.422
26.144
28.669
1.00
19.19
A


ATOM
736
CB
GLN
A
774
−1.335
27.372
28.703
1.00
19.43
A


ATOM
737
CG
GLN
A
774
−2.793
26.987
28.931
1.00
19.08
A


ATOM
738
CD
GLN
A
774
−3.187
25.750
28.136
1.00
18.95
A


ATOM
739
OE1
GLN
A
774
−3.122
25.739
26.904
1.00
18.16
A


ATOM
740
NE2
GLN
A
774
−3.590
24.697
28.842
1.00
18.81
A


ATOM
741
C
GLN
A
774
0.992
26.527
28.224
1.00
18.56
A


ATOM
742
O
GLN
A
774
1.178
27.356
27.337
1.00
18.81
A


ATOM
743
N
MET
A
775
1.981
25.911
28.855
1.00
19.20
A


ATOM
744
CA
MET
A
775
3.385
26.105
28.520
1.00
19.64
A


ATOM
745
CB
MET
A
775
4.009
27.253
29.323
1.00
20.86
A


ATOM
746
CG
MET
A
775
3.522
28.652
28.959
1.00
21.16
A


ATOM
747
SD
MET
A
775
4.507
29.907
29.799
1.00
25.84
A


ATOM
748
CE
MET
A
775
3.216
30.919
30.610
1.00
25.72
A


ATOM
749
C
MET
A
775
4.061
24.803
28.921
1.00
18.35
A


ATOM
750
O
MET
A
775
3.516
24.050
29.727
1.00
20.32
A


ATOM
751
N
LEU
A
776
5.224
24.521
28.349
1.00
17.82
A


ATOM
752
CA
LEU
A
776
5.955
23.317
28.721
1.00
18.54
A


ATOM
753
CB
LEU
A
776
6.723
22.741
27.526
1.00
18.50
A


ATOM
754
CG
LEU
A
776
5.844
22.027
26.490
1.00
19.83
A


ATOM
755
CD1
LEU
A
776
6.711
21.491
25.367
1.00
19.70
A


ATOM
756
CD2
LEU
A
776
5.068
20.890
27.149
1.00
18.31
A


ATOM
757
C
LEU
A
776
6.912
23.762
29.813
1.00
18.66
A


ATOM
758
O
LEU
A
776
7.886
24.471
29.551
1.00
19.30
A


ATOM
759
N
TYR
A
777
6.611
23.354
31.040
1.00
16.71
A


ATOM
760
CA
TYR
A
777
7.401
23.719
32.203
1.00
17.38
A


ATOM
761
CB
TYR
A
777
6.459
23.907
33.405
1.00
18.98
A


ATOM
762
CG
TYR
A
777
7.056
24.636
34.591
1.00
22.23
A


ATOM
763
CD1
TYR
A
777
7.970
24.008
35.439
1.00
23.96
A


ATOM
764
CE1
TYR
A
777
8.500
24.670
36.550
1.00
25.16
A


ATOM
765
CD2
TYR
A
777
6.689
25.954
34.878
1.00
22.47
A


ATOM
766
CE2
TYR
A
777
7.216
26.626
35.984
1.00
24.25
A


ATOM
767
CZ
TYR
A
777
8.118
25.978
36.816
1.00
25.97
A


ATOM
768
OH
TYR
A
777
8.632
26.629
37.918
1.00
25.81
A


ATOM
769
C
TYR
A
777
8.440
22.641
32.500
1.00
16.79
A


ATOM
770
O
TYR
A
777
8.290
21.867
33.443
1.00
16.14
A


ATOM
771
N
PHE
A
778
9.479
22.575
31.675
1.00
17.41
A


ATOM
772
CA
PHE
A
778
10.533
21.590
31.890
1.00
18.04
A


ATOM
773
CB
PHE
A
778
11.592
21.668
30.780
1.00
17.18
A


ATOM
774
CG
PHE
A
778
11.076
21.299
29.414
1.00
19.92
A


ATOM
775
CD1
PHE
A
778
10.664
22.284
28.520
1.00
19.96
A


ATOM
776
CD2
PHE
A
778
11.017
19.967
29.016
1.00
18.19
A


ATOM
777
CE1
PHE
A
778
10.206
21.946
27.244
1.00
20.84
A


ATOM
778
CE2
PHE
A
778
10.561
19.620
27.745
1.00
20.50
A


ATOM
779
CZ
PHE
A
778
10.155
20.611
26.855
1.00
19.47
A


ATOM
780
C
PHE
A
778
11.178
21.873
33.245
1.00
17.23
A


ATOM
781
O
PHE
A
778
11.393
20.961
34.049
1.00
15.16
A


ATOM
782
N
ALA
A
779
11.479
23.149
33.486
1.00
17.50
A


ATOM
783
CA
ALA
A
779
12.091
23.588
34.738
1.00
18.81
A


ATOM
784
CB
ALA
A
779
13.599
23.329
34.708
1.00
16.57
A


ATOM
785
C
ALA
A
779
11.816
25.083
34.940
1.00
20.23
A


ATOM
786
O
ALA
A
779
11.372
25.771
34.021
1.00
18.79
A


ATOM
787
N
PRO
A
780
12.068
25.603
36.151
1.00
22.34
A


ATOM
788
CD
PRO
A
780
12.432
24.933
37.411
1.00
22.01
A


ATOM
789
CA
PRO
A
780
11.815
27.031
36.373
1.00
23.57
A


ATOM
790
CB
PRO
A
780
12.236
27.232
37.825
1.00
25.03
A


ATOM
791
CG
PRO
A
780
11.911
25.906
38.448
1.00
23.19
A


ATOM
792
C
PRO
A
780
12.610
27.911
35.406
1.00
23.67
A


ATOM
793
O
PRO
A
780
12.154
28.982
35.018
1.00
22.71
A


ATOM
794
N
ASP
A
781
13.795
27.442
35.017
1.00
23.34
A


ATOM
795
CA
ASP
A
781
14.657
28.182
34.098
1.00
21.94
A


ATOM
796
CB
ASP
A
781
16.107
28.136
34.594
1.00
21.93
A


ATOM
797
CG
ASP
A
781
16.646
26.718
34.718
1.00
23.63
A


ATOM
798
OD1
ASP
A
781
15.843
25.769
34.856
1.00
22.19
A


ATOM
799
OD2
ASP
A
781
17.883
26.554
34.693
1.00
24.73
A


ATOM
800
C
ASP
A
781
14.569
27.676
32.653
1.00
21.19
A


ATOM
801
O
ASP
A
781
15.390
28.032
31.806
1.00
20.19
A


ATOM
802
N
LEU
A
782
13.572
26.847
32.369
1.00
19.89
A


ATOM
803
CA
LEU
A
782
13.385
26.343
31.013
1.00
20.33
A


ATOM
804
CB
LEU
A
782
14.151
25.028
30.802
1.00
18.43
A


ATOM
805
CG
LEU
A
782
14.176
24.494
29.361
1.00
19.40
A


ATOM
806
CD1
LEU
A
782
14.784
25.536
28.434
1.00
20.75
A


ATOM
807
CD2
LEU
A
782
14.981
23.203
29.300
1.00
19.07
A


ATOM
808
C
LEU
A
782
11.895
26.139
30.768
1.00
19.43
A


ATOM
809
O
LEU
A
782
11.377
25.027
30.848
1.00
18.09
A


ATOM
810
N
ILE
A
783
11.211
27.240
30.486
1.00
19.42
A


ATOM
811
CA
ILE
A
783
9.779
27.208
30.233
1.00
20.01
A


ATOM
812
CB
ILE
A
783
9.036
28.186
31.172
1.00
20.25
A


ATOM
813
CG2
ILE
A
783
7.536
28.162
30.877
1.00
23.95
A


ATOM
814
CG1
ILE
A
783
9.298
27.803
32.632
1.00
20.97
A


ATOM
815
CD1
ILE
A
783
8.914
28.885
33.646
1.00
21.41
A


ATOM
816
C
ILE
A
783
9.531
27.614
28.786
1.00
19.86
A


ATOM
817
O
ILE
A
783
9.954
28.686
28.352
1.00
18.73
A


ATOM
818
N
LEU
A
784
8.861
26.752
28.032
1.00
18.35
A


ATOM
819
CA
LEU
A
784
8.577
27.073
26.642
1.00
18.52
A


ATOM
820
CB
LEU
A
784
9.040
25.946
25.709
1.00
18.59
A


ATOM
821
CG
LEU
A
784
10.420
25.291
25.813
1.00
20.62
A


ATOM
822
CD1
LEU
A
784
10.716
24.600
24.479
1.00
19.63
A


ATOM
823
CD2
LEU
A
784
11.496
26.306
26.120
1.00
21.85
A


ATOM
824
C
LEU
A
784
7.090
27.303
26.389
1.00
18.16
A


ATOM
825
O
LEU
A
784
6.290
26.373
26.513
1.00
17.61
A


ATOM
826
N
ASN
A
785
6.714
28.536
26.058
1.00
18.24
A


ATOM
827
CA
ASN
A
785
5.323
28.809
25.708
1.00
18.38
A


ATOM
828
CB
ASN
A
785
4.970
30.302
25.866
1.00
19.86
A


ATOM
829
CG
ASN
A
785
5.922
31.220
25.127
1.00
21.17
A


ATOM
830
OD1
ASN
A
785
6.473
30.861
24.091
1.00
22.33
A


ATOM
831
ND2
ASN
A
785
6.104
32.428
25.654
1.00
21.27
A


ATOM
832
C
ASN
A
785
5.257
28.377
24.242
1.00
18.94
A


ATOM
833
O
ASN
A
785
6.286
28.051
23.655
1.00
19.11
A


ATOM
834
N
GLU
A
786
4.077
28.376
23.637
1.00
20.82
A


ATOM
835
CA
GLU
A
786
3.974
27.919
22.256
1.00
20.94
A


ATOM
836
CB
GLU
A
786
2.513
27.923
21.792
1.00
23.70
A


ATOM
837
CG
GLU
A
786
2.345
27.424
20.366
1.00
24.17
A


ATOM
838
CD
GLU
A
786
0.935
26.968
20.058
1.00
26.71
A


ATOM
839
OE1
GLU
A
786
−0.012
27.549
20.630
1.00
20.59
A


ATOM
840
OE2
GLU
A
786
0.781
26.037
19.235
1.00
23.53
A


ATOM
841
C
GLU
A
786
4.839
28.649
21.239
1.00
22.11
A


ATOM
842
O
GLU
A
786
5.375
28.023
20.330
1.00
21.62
A


ATOM
843
N
GLN
A
787
4.978
29.963
21.370
1.00
22.98
A


ATOM
844
CA
GLN
A
787
5.799
30.702
20.417
1.00
24.73
A


ATOM
845
CB
GLN
A
787
5.738
32.207
20.698
1.00
26.16
A


ATOM
846
CG
GLN
A
787
6.457
33.064
19.652
1.00
29.65
A


ATOM
847
CD
GLN
A
787
5.977
32.785
18.233
1.00
34.00
A


ATOM
848
OE1
GLN
A
787
4.771
32.732
17.967
1.00
35.14
A


ATOM
849
NE2
GLN
A
787
6.920
32.613
17.313
1.00
35.97
A


ATOM
850
C
GLN
A
787
7.251
30.218
20.487
1.00
25.27
A


ATOM
851
O
GLN
A
787
7.916
30.078
19.457
1.00
23.55
A


ATOM
852
N
ARG
A
788
7.740
29.957
21.696
1.00
24.46
A


ATOM
853
CA
ARG
A
788
9.113
29.488
21.856
1.00
23.62
A


ATOM
854
CB
ARG
A
788
9.512
29.486
23.332
1.00
23.38
A


ATOM
855
CG
ARG
A
788
11.013
29.406
23.555
1.00
22.19
A


ATOM
856
CD
ARG
A
788
11.371
29.462
25.035
1.00
22.56
A


ATOM
857
NE
ARG
A
788
12.817
29.466
25.241
1.00
21.14
A


ATOM
858
CZ
ARG
A
788
13.410
29.478
26.433
1.00
25.92
A


ATOM
859
NH1
ARG
A
788
14.737
29.481
26.514
1.00
26.50
A


ATOM
860
NH2
ARG
A
788
12.682
29.482
27.546
1.00
26.08
A


ATOM
861
C
ARG
A
788
9.224
28.081
21.270
1.00
23.70
A


ATOM
862
O
ARG
A
788
10.282
27.683
20.769
1.00
23.15
A


ATOM
863
N
MET
A
789
8.122
27.335
21.331
1.00
23.02
A


ATOM
864
CA
MET
A
789
8.072
25.987
20.776
1.00
23.37
A


ATOM
865
CB
MET
A
789
6.746
25.298
21.124
1.00
23.06
A


ATOM
866
CG
MET
A
789
6.543
24.933
22.592
1.00
21.04
A


ATOM
867
SD
MET
A
789
4.957
24.068
22.811
1.00
21.30
A


ATOM
868
CE
MET
A
789
4.293
24.917
24.247
1.00
21.48
A


ATOM
869
C
MET
A
789
8.185
26.074
19.255
1.00
25.50
A


ATOM
870
O
MET
A
789
8.940
25.325
18.636
1.00
25.04
A


ATOM
871
N
LYS
A
790
7.423
26.992
18.664
1.00
27.11
A


ATOM
872
CA
LYS
A
790
7.408
27.190
17.214
1.00
29.59
A


ATOM
873
CB
LYS
A
790
6.447
28.322
16.833
1.00
32.00
A


ATOM
874
CG
LYS
A
790
4.976
27.980
16.967
1.00
37.02
A


ATOM
875
CD
LYS
A
790
4.103
29.124
16.456
1.00
38.59
A


ATOM
876
CE
LYS
A
790
2.628
28.840
16.698
1.00
41.04
A


ATOM
877
NZ
LYS
A
790
1.753
29.958
16.236
1.00
42.99
A


ATOM
878
C
LYS
A
790
8.770
27.498
16.609
1.00
30.18
A


ATOM
879
O
LYS
A
790
9.068
27.073
15.493
1.00
28.32
A


ATOM
880
N
GLU
A
791
9.591
28.251
17.330
1.00
30.15
A


ATOM
881
CA
GLU
A
791
10.908
28.597
16.813
1.00
33.53
A


ATOM
882
CB
GLU
A
791
11.149
30.101
16.988
1.00
34.94
A


ATOM
883
CG
GLU
A
791
10.733
30.663
18.334
1.00
37.89
A


ATOM
884
CD
GLU
A
791
10.597
32.179
18.320
1.00
38.69
A


ATOM
885
OE1
GLU
A
791
9.722
32.700
17.596
1.00
40.52
A


ATOM
886
OE2
GLU
A
791
11.366
32.851
19.035
1.00
39.54
A


ATOM
887
C
GLU
A
791
12.048
27.790
17.435
1.00
33.31
A


ATOM
888
O
GLU
A
791
13.198
28.230
17.440
1.00
34.67
A


ATOM
889
N
SER
A
792
11.726
26.595
17.926
1.00
32.17
A


ATOM
890
CA
SER
A
792
12.710
25.722
18.572
1.00
32.29
A


ATOM
891
CB
SER
A
792
12.011
24.823
19.595
1.00
31.21
A


ATOM
892
OG
SER
A
792
11.197
23.862
18.942
1.00
25.26
A


ATOM
893
C
SER
A
792
13.514
24.827
17.624
1.00
33.43
A


ATOM
894
O
SER
A
792
14.676
24.512
17.902
1.00
34.87
A


ATOM
895
N
SER
A
793
12.871
24.417
16.531
1.00
32.81
A


ATOM
896
CA
SER
A
793
13.421
23.528
15.495
1.00
31.80
A


ATOM
897
CB
SER
A
793
14.955
23.396
15.571
1.00
34.40
A


ATOM
898
OG
SER
A
793
15.367
22.397
16.494
1.00
32.53
A


ATOM
899
C
SER
A
793
12.774
22.151
15.648
1.00
30.98
A


ATOM
900
O
SER
A
793
12.882
21.299
14.764
1.00
32.51
A


ATOM
901
N
PHE
A
794
12.101
21.933
16.775
1.00
27.80
A


ATOM
902
CA
PHE
A
794
11.408
20.669
17.012
1.00
26.68
A


ATOM
903
CB
PHE
A
794
12.221
19.764
17.954
1.00
24.25
A


ATOM
904
CG
PHE
A
794
12.685
20.437
19.221
1.00
21.22
A


ATOM
905
CD1
PHE
A
794
11.961
20.308
20.400
1.00
23.19
A


ATOM
906
CD2
PHE
A
794
13.870
21.166
19.241
1.00
21.45
A


ATOM
907
CE1
PHE
A
794
12.412
20.893
21.586
1.00
24.05
A


ATOM
908
CE2
PHE
A
794
14.333
21.756
20.420
1.00
20.76
A


ATOM
909
CZ
PHE
A
794
13.606
21.619
21.593
1.00
23.61
A


ATOM
910
C
PHE
A
794
9.996
20.928
17.552
1.00
26.57
A


ATOM
911
O
PHE
A
794
9.566
20.356
18.555
1.00
26.01
A


ATOM
912
N
TYR
A
795
9.285
21.803
16.847
1.00
25.69
A


ATOM
913
CA
TYR
A
795
7.920
22.192
17.191
1.00
24.51
A


ATOM
914
CB
TYR
A
795
7.382
23.150
16.120
1.00
24.31
A


ATOM
915
CG
TYR
A
795
5.983
23.675
16.365
1.00
27.22
A


ATOM
916
CD1
TYR
A
795
5.605
24.166
17.619
1.00
27.70
A


ATOM
917
CE1
TYR
A
795
4.331
24.688
17.834
1.00
27.85
A


ATOM
918
CD2
TYR
A
795
5.048
23.718
15.330
1.00
27.80
A


ATOM
919
CE2
TYR
A
795
3.771
24.239
15.534
1.00
29.91
A


ATOM
920
CZ
TYR
A
795
3.419
24.723
16.788
1.00
30.25
A


ATOM
921
OH
TYR
A
795
2.159
25.242
16.988
1.00
30.87
A


ATOM
922
C
TYR
A
795
6.991
20.993
17.336
1.00
23.82
A


ATOM
923
O
TYR
A
795
6.283
20.872
18.335
1.00
21.37
A


ATOM
924
N
SER
A
796
7.001
20.100
16.349
1.00
23.12
A


ATOM
925
CA
SER
A
796
6.132
18.928
16.385
1.00
23.80
A


ATOM
926
CB
SER
A
796
6.296
18.106
15.104
1.00
27.03
A


ATOM
927
OG
SER
A
796
7.659
17.796
14.869
1.00
30.34
A


ATOM
928
C
SER
A
796
6.372
18.043
17.605
1.00
24.28
A


ATOM
929
O
SER
A
796
5.430
17.470
18.163
1.00
23.18
A


ATOM
930
N
LEU
A
797
7.631
17.927
18.014
1.00
22.88
A


ATOM
931
CA
LEU
A
797
7.973
17.124
19.176
1.00
22.93
A


ATOM
932
CB
LEU
A
797
9.492
17.019
19.327
1.00
26.10
A


ATOM
933
CG
LEU
A
797
9.992
15.840
20.163
1.00
27.87
A


ATOM
934
CD1
LEU
A
797
9.676
14.545
19.430
1.00
28.16
A


ATOM
935
CD2
LEU
A
797
11.491
15.966
20.392
1.00
27.90
A


ATOM
936
C
LEU
A
797
7.386
17.809
20.407
1.00
20.98
A


ATOM
937
O
LEU
A
797
6.837
17.151
21.287
1.00
20.95
A


ATOM
938
N
CYS
A
798
7.513
19.133
20.461
1.00
20.57
A


ATOM
939
CA
CYS
A
798
6.973
19.903
21.579
1.00
20.61
A


ATOM
940
CB
CYS
A
798
7.265
21.399
21.404
1.00
20.74
A


ATOM
941
SG
CYS
A
798
8.989
21.866
21.726
1.00
21.60
A


ATOM
942
C
CYS
A
798
5.469
19.690
21.678
1.00
20.72
A


ATOM
943
O
CYS
A
798
4.926
19.504
22.773
1.00
19.17
A


ATOM
944
N
LEU
A
799
4.793
19.722
20.533
1.00
19.90
A


ATOM
945
CA
LEU
A
799
3.349
19.526
20.518
1.00
21.06
A


ATOM
946
CB
LEU
A
799
2.798
19.688
19.099
1.00
21.78
A


ATOM
947
CG
LEU
A
799
2.933
21.096
18.505
1.00
21.95
A


ATOM
948
CD1
LEU
A
799
2.376
21.100
17.093
1.00
24.69
A


ATOM
949
CD2
LEU
A
799
2.194
22.114
19.377
1.00
21.59
A


ATOM
950
C
LEU
A
799
3.007
18.146
21.060
1.00
22.12
A


ATOM
951
O
LEU
A
799
2.035
17.984
21.797
1.00
23.00
A


ATOM
952
N
THR
A
800
3.813
17.153
20.698
1.00
21.35
A


ATOM
953
CA
THR
A
800
3.593
15.789
21.170
1.00
22.13
A


ATOM
954
CB
THR
A
800
4.621
14.818
20.539
1.00
22.94
A


ATOM
955
OG1
THR
A
800
4.413
14.770
19.124
1.00
22.16
A


ATOM
956
CG2
THR
A
800
4.469
13.414
21.116
1.00
24.15
A


ATOM
957
C
THR
A
800
3.696
15.727
22.693
1.00
20.94
A


ATOM
958
O
THR
A
800
2.861
15.125
23.361
1.00
21.14
A


ATOM
959
N
MET
A
801
4.723
16.356
23.247
1.00
21.63
A


ATOM
960
CA
MET
A
801
4.890
16.363
24.691
1.00
20.90
A


ATOM
961
CB
MET
A
801
6.251
16.960
25.059
1.00
21.60
A


ATOM
962
CG
MET
A
801
7.439
16.115
24.604
1.00
22.22
A


ATOM
963
SD
MET
A
801
9.029
16.740
25.194
1.00
24.57
A


ATOM
964
CE
MET
A
801
9.415
17.955
23.949
1.00
24.02
A


ATOM
965
C
MET
A
801
3.770
17.165
25.363
1.00
22.02
A


ATOM
966
O
MET
A
801
3.265
16.786
26.421
1.00
21.68
A


ATOM
967
N
TRP
A
802
3.373
18.259
24.720
1.00
21.19
A


ATOM
968
CA
TRP
A
802
2.337
19.155
25.232
1.00
21.40
A


ATOM
969
CB
TRP
A
802
2.214
20.360
24.290
1.00
20.55
A


ATOM
970
CG
TRP
A
802
1.627
21.606
24.910
1.00
21.30
A


ATOM
971
CD2
TRP
A
802
1.238
22.802
24.219
1.00
21.96
A


ATOM
972
CE2
TRP
A
802
0.797
23.727
25.193
1.00
20.55
A


ATOM
973
CE3
TRP
A
802
1.225
23.182
22.869
1.00
22.42
A


ATOM
974
CD1
TRP
A
802
1.409
21.847
26.239
1.00
21.16
A


ATOM
975
NE1
TRP
A
802
0.910
23.121
26.416
1.00
20.99
A


ATOM
976
CZ2
TRP
A
802
0.343
25.011
24.860
1.00
21.73
A


ATOM
977
CZ3
TRP
A
802
0.775
24.461
22.536
1.00
23.05
A


ATOM
978
CH2
TRP
A
802
0.342
25.359
23.531
1.00
23.08
A


ATOM
979
C
TRP
A
802
0.974
18.479
25.419
1.00
21.76
A


ATOM
980
O
TRP
A
802
0.126
18.973
26.168
1.00
21.60
A


ATOM
981
N
GLN
A
803
0.766
17.350
24.747
1.00
21.02
A


ATOM
982
CA
GLN
A
803
−0.496
16.619
24.856
1.00
21.96
A


ATOM
983
CB
GLN
A
803
−0.488
15.404
23.921
1.00
23.91
A


ATOM
984
CG
GLN
A
803
−0.267
15.756
22.447
1.00
27.15
A


ATOM
985
CD
GLN
A
803
−0.209
14.537
21.537
1.00
31.34
A


ATOM
986
OE1
GLN
A
803
0.116
14.648
20.352
1.00
35.35
A


ATOM
987
NE2
GLN
A
803
−0.526
13.372
22.084
1.00
32.57
A


ATOM
988
C
GLN
A
803
−0.759
16.152
26.289
1.00
23.03
A


ATOM
989
O
GLN
A
803
−1.898
16.173
26.759
1.00
21.44
A


ATOM
990
N
ILE
A
804
0.299
15.736
26.980
1.00
21.25
A


ATOM
991
CA
ILE
A
804
0.170
15.242
28.344
1.00
22.31
A


ATOM
992
CB
ILE
A
804
1.532
14.758
28.891
1.00
21.58
A


ATOM
993
CG2
ILE
A
804
1.381
14.289
30.331
1.00
22.10
A


ATOM
994
CG1
ILE
A
804
2.051
13.609
28.020
1.00
25.42
A


ATOM
995
CD1
ILE
A
804
3.379
13.044
28.464
1.00
28.79
A


ATOM
996
C
ILE
A
804
−0.432
16.270
29.297
1.00
21.32
A


ATOM
997
O
ILE
A
804
−1.415
15.984
29.981
1.00
21.18
A


ATOM
998
N
PRO
A
805
0.153
17.476
29.366
1.00
21.85
A


ATOM
999
CD
PRO
A
805
1.379
17.971
28.716
1.00
19.76
A


ATOM
1000
CA
PRO
A
805
−0.409
18.484
30.270
1.00
22.32
A


ATOM
1001
CB
PRO
A
805
0.439
19.718
29.981
1.00
23.10
A


ATOM
1002
CG
PRO
A
805
1.758
19.134
29.593
1.00
24.27
A


ATOM
1003
C
PRO
A
805
−1.880
18.716
29.932
1.00
22.86
A


ATOM
1004
O
PRO
A
805
−2.726
18.842
30.820
1.00
21.86
A


ATOM
1005
N
GLN
A
806
−2.178
18.767
28.637
1.00
21.67
A


ATOM
1006
CA
GLN
A
806
−3.549
18.991
28.199
1.00
24.13
A


ATOM
1007
CB
GLN
A
806
−3.601
19.119
26.669
1.00
25.09
A


ATOM
1008
CG
GLN
A
806
−2.740
20.270
26.116
1.00
25.65
A


ATOM
1009
CD
GLN
A
806
−3.241
21.661
26.516
1.00
29.07
A


ATOM
1010
OE1
GLN
A
806
−3.896
21.832
27.546
1.00
26.16
A


ATOM
1011
NE2
GLN
A
806
−2.914
22.666
25.701
1.00
30.40
A


ATOM
1012
C
GLN
A
806
−4.481
17.882
28.696
1.00
23.92
A


ATOM
1013
O
GLN
A
806
−5.624
18.152
29.062
1.00
23.37
A


ATOM
1014
N
GLU
A
807
−3.998
16.640
28.726
1.00
24.30
A


ATOM
1015
CA
GLU
A
807
−4.818
15.532
29.215
1.00
25.08
A


ATOM
1016
CB
GLU
A
807
−4.175
14.180
28.893
1.00
27.80
A


ATOM
1017
CG
GLU
A
807
−4.461
13.676
27.495
1.00
32.53
A


ATOM
1018
CD
GLU
A
807
−5.951
13.489
27.238
1.00
34.70
A


ATOM
1019
OE1
GLU
A
807
−6.570
12.623
27.893
1.00
35.52
A


ATOM
1020
OE2
GLU
A
807
−6.501
14.211
26.381
1.00
36.62
A


ATOM
1021
C
GLU
A
807
−5.025
15.641
30.723
1.00
24.42
A


ATOM
1022
O
GLU
A
807
−6.056
15.222
31.251
1.00
22.60
A


ATOM
1023
N
PHE
A
808
−4.034
16.189
31.418
1.00
23.73
A


ATOM
1024
CA
PHE
A
808
−4.143
16.357
32.860
1.00
23.36
A


ATOM
1025
CB
PHE
A
808
−2.818
16.857
33.443
1.00
24.21
A


ATOM
1026
CG
PHE
A
808
−1.785
15.774
33.622
1.00
25.04
A


ATOM
1027
CD1
PHE
A
808
−2.118
14.433
33.439
1.00
26.18
A


ATOM
1028
CD2
PHE
A
808
−0.490
16.091
34.010
1.00
26.53
A


ATOM
1029
CE1
PHE
A
808
−1.173
13.422
33.648
1.00
27.84
A


ATOM
1030
CE2
PHE
A
808
0.462
15.088
34.222
1.00
27.25
A


ATOM
1031
CZ
PHE
A
808
0.119
13.754
34.040
1.00
25.53
A


ATOM
1032
C
PHE
A
808
−5.264
17.349
33.150
1.00
22.79
A


ATOM
1033
O
PHE
A
808
−6.074
17.142
34.057
1.00
22.62
A


ATOM
1034
N
VAL
A
809
−5.312
18.418
32.359
1.00
22.34
A


ATOM
1035
CA
VAL
A
809
−6.345
19.440
32.512
1.00
22.35
A


ATOM
1036
CB
VAL
A
809
−6.140
20.590
31.500
1.00
21.96
A


ATOM
1037
CG1
VAL
A
809
−7.325
21.541
31.545
1.00
22.83
A


ATOM
1038
CG2
VAL
A
809
−4.863
21.346
31.818
1.00
20.25
A


ATOM
1039
C
VAL
A
809
−7.734
18.844
32.285
1.00
23.40
A


ATOM
1040
O
VAL
A
809
−8.658
19.059
33.073
1.00
22.44
A


ATOM
1041
N
LYS
A
810
−7.880
18.088
31.204
1.00
24.89
A


ATOM
1042
CA
LYS
A
810
−9.168
17.493
30.873
1.00
26.91
A


ATOM
1043
CB
LYS
A
810
−9.105
16.836
29.491
1.00
29.69
A


ATOM
1044
CG
LYS
A
810
−8.893
17.826
28.355
1.00
33.08
A


ATOM
1045
CD
LYS
A
810
−8.741
17.116
27.014
1.00
38.27
A


ATOM
1046
CE
LYS
A
810
−8.498
18.114
25.881
1.00
40.99
A


ATOM
1047
NZ
LYS
A
810
−8.286
17.433
24.568
1.00
43.19
A


ATOM
1048
C
LYS
A
810
−9.663
16.486
31.907
1.00
27.41
A


ATOM
1049
O
LYS
A
810
−10.855
16.444
32.214
1.00
26.62
A


ATOM
1050
N
LEU
A
811
−8.753
15.677
32.440
1.00
24.95
A


ATOM
1051
CA
LEU
A
811
−9.123
14.683
33.438
1.00
25.56
A


ATOM
1052
CB
LEU
A
811
−8.217
13.458
33.318
1.00
25.67
A


ATOM
1053
CG
LEU
A
811
−8.421
12.595
32.078
1.00
26.38
A


ATOM
1054
CD1
LEU
A
811
−7.289
11.591
31.949
1.00
26.98
A


ATOM
1055
CD2
LEU
A
811
−9.760
11.893
32.186
1.00
26.29
A


ATOM
1056
C
LEU
A
811
−9.044
15.220
34.863
1.00
24.44
A


ATOM
1057
O
LEU
A
811
−9.522
14.579
35.793
1.00
24.86
A


ATOM
1058
N
GLN
A
812
−8.458
16.401
35.026
1.00
25.33
A


ATOM
1059
CA
GLN
A
812
−8.288
16.989
36.351
1.00
26.61
A


ATOM
1060
CB
GLN
A
812
−9.635
17.477
36.905
1.00
30.42
A


ATOM
1061
CG
GLN
A
812
−10.100
18.777
36.256
1.00
35.79
A


ATOM
1062
CD
GLN
A
812
−11.386
19.328
36.849
1.00
40.76
A


ATOM
1063
OE1
GLN
A
812
−11.736
20.489
36.621
1.00
45.20
A


ATOM
1064
NE2
GLN
A
812
−12.099
18.499
37.608
1.00
42.16
A


ATOM
1065
C
GLN
A
812
−7.655
15.950
37.281
1.00
24.37
A


ATOM
1066
O
GLN
A
812
−8.185
15.625
38.348
1.00
22.99
A


ATOM
1067
N
VAL
A
813
−6.513
15.423
36.846
1.00
22.72
A


ATOM
1068
CA
VAL
A
813
−5.776
14.422
37.607
1.00
20.15
A


ATOM
1069
CB
VAL
A
813
−4.501
13.989
36.853
1.00
21.18
A


ATOM
1070
CG1
VAL
A
813
−3.707
12.977
37.694
1.00
19.93
A


ATOM
1071
CG2
VAL
A
813
−4.882
13.388
35.506
1.00
19.31
A


ATOM
1072
C
VAL
A
813
−5.380
14.998
38.958
1.00
20.32
A


ATOM
1073
O
VAL
A
813
−4.906
16.134
39.042
1.00
18.09
A


ATOM
1074
N
SER
A
814
−5.579
14.220
40.016
1.00
18.44
A


ATOM
1075
CA
SER
A
814
−5.235
14.690
41.353
1.00
20.30
A


ATOM
1076
CB
SER
A
814
−6.143
14.057
42.408
1.00
18.76
A


ATOM
1077
OG
SER
A
814
−5.858
12.674
42.549
1.00
17.92
A


ATOM
1078
C
SER
A
814
−3.794
14.348
41.687
1.00
21.13
A


ATOM
1079
O
SER
A
814
−3.173
13.496
41.050
1.00
21.63
A


ATOM
1080
N
GLN
A
815
−3.276
15.024
42.700
1.00
21.79
A


ATOM
1081
CA
GLN
A
815
−1.916
14.807
43.164
1.00
23.69
A


ATOM
1082
CB
GLN
A
815
−1.648
15.736
44.349
1.00
27.86
A


ATOM
1083
CG
GLN
A
815
−0.226
15.755
44.851
1.00
34.98
A


ATOM
1084
CD
GLN
A
815
−0.029
16.804
45.927
1.00
38.93
A


ATOM
1085
OE1
GLN
A
815
1.084
17.036
46.386
1.00
42.97
A


ATOM
1086
NE2
GLN
A
815
−1.120
17.448
46.333
1.00
42.31
A


ATOM
1087
C
GLN
A
815
−1.748
13.348
43.585
1.00
21.52
A


ATOM
1088
O
GLN
A
815
−0.710
12.729
43.325
1.00
21.53
A


ATOM
1089
N
GLU
A
816
−2.782
12.794
44.215
1.00
19.19
A


ATOM
1090
CA
GLU
A
816
−2.744
11.410
44.682
1.00
19.04
A


ATOM
1091
CB
GLU
A
816
−3.946
11.116
45.582
1.00
20.60
A


ATOM
1092
CG
GLU
A
816
−3.983
11.908
46.885
1.00
22.06
A


ATOM
1093
CD
GLU
A
816
−4.344
13.374
46.692
1.00
24.05
A


ATOM
1094
OE1
GLU
A
816
−4.903
13.729
45.632
1.00
21.48
A


ATOM
1095
OE2
GLU
A
816
−4.078
14.171
47.615
1.00
26.29
A


ATOM
1096
C
GLU
A
816
−2.720
10.408
43.534
1.00
18.03
A


ATOM
1097
O
GLU
A
816
−2.003
9.409
43.586
1.00
16.07
A


ATOM
1098
N
GLU
A
817
−3.516
10.664
42.503
1.00
17.72
A


ATOM
1099
CA
GLU
A
817
−3.553
9.772
41.352
1.00
18.37
A


ATOM
1100
CB
GLU
A
817
−4.700
10.163
40.413
1.00
19.36
A


ATOM
1101
CG
GLU
A
817
−6.089
10.025
41.036
1.00
18.88
A


ATOM
1102
CD
GLU
A
817
−7.186
10.619
40.164
1.00
20.98
A


ATOM
1103
OE1
GLU
A
817
−6.934
11.652
39.510
1.00
19.85
A


ATOM
1104
OE2
GLU
A
817
−8.305
10.067
40.143
1.00
20.28
A


ATOM
1105
C
GLU
A
817
−2.214
9.869
40.615
1.00
17.45
A


ATOM
1106
O
GLU
A
817
−1.654
8.859
40.203
1.00
18.12
A


ATOM
1107
N
PHE
A
818
−1.710
11.092
40.464
1.00
17.39
A


ATOM
1108
CA
PHE
A
818
−0.443
11.339
39.778
1.00
17.67
A


ATOM
1109
CB
PHE
A
818
−0.108
12.836
39.820
1.00
18.87
A


ATOM
1110
CG
PHE
A
818
1.307
13.158
39.396
1.00
20.11
A


ATOM
1111
CD1
PHE
A
818
1.697
13.039
38.065
1.00
21.04
A


ATOM
1112
CD2
PHE
A
818
2.255
13.551
40.337
1.00
22.59
A


ATOM
1113
CE1
PHE
A
818
3.018
13.306
37.673
1.00
21.13
A


ATOM
1114
CE2
PHE
A
818
3.577
13.821
39.961
1.00
22.38
A


ATOM
1115
CZ
PHE
A
818
3.959
13.696
38.624
1.00
21.87
A


ATOM
1116
C
PHE
A
818
0.690
10.543
40.423
1.00
17.61
A


ATOM
1117
O
PHE
A
818
1.426
9.828
39.745
1.00
17.85
A


ATOM
1118
N
LEU
A
819
0.820
10.668
41.739
1.00
17.17
A


ATOM
1119
CA
LEU
A
819
1.857
9.966
42.476
1.00
16.75
A


ATOM
1120
CB
LEU
A
819
1.712
10.259
43.972
1.00
17.20
A


ATOM
1121
CG
LEU
A
819
2.030
11.713
44.349
1.00
17.53
A


ATOM
1122
CD1
LEU
A
819
1.682
11.970
45.816
1.00
18.42
A


ATOM
1123
CD2
LEU
A
819
3.509
11.989
44.089
1.00
18.88
A


ATOM
1124
C
LEU
A
819
1.844
8.456
42.217
1.00
18.00
A


ATOM
1125
O
LEU
A
819
2.890
7.864
41.954
1.00
17.24
A


ATOM
1126
N
CYS
A
820
0.665
7.840
42.273
1.00
16.25
A


ATOM
1127
CA
CYS
A
820
0.549
6.400
42.034
1.00
16.35
A


ATOM
1128
CB
CYS
A
820
−0.851
5.911
42.419
1.00
13.68
A


ATOM
1129
SG
CYS
A
820
−1.192
5.999
44.186
1.00
18.53
A


ATOM
1130
C
CYS
A
820
0.837
6.027
40.580
1.00
17.21
A


ATOM
1131
O
CYS
A
820
1.516
5.027
40.305
1.00
16.67
A


ATOM
1132
N
MET
A
821
0.318
6.826
39.652
1.00
15.37
A


ATOM
1133
CA
MET
A
821
0.530
6.573
38.234
1.00
16.27
A


ATOM
1134
CB
MET
A
821
−0.265
7.573
37.392
1.00
17.92
A


ATOM
1135
CG
MET
A
821
−1.771
7.383
37.460
1.00
17.69
A


ATOM
1136
SD
MET
A
821
−2.643
8.818
36.774
1.00
19.79
A


ATOM
1137
CE
MET
A
821
−2.555
8.439
35.021
1.00
15.33
A


ATOM
1138
C
MET
A
821
2.015
6.677
37.897
1.00
15.93
A


ATOM
1139
O
MET
A
821
2.531
5.902
37.097
1.00
14.16
A


ATOM
1140
N
LYS
A
822
2.707
7.628
38.515
1.00
14.88
A


ATOM
1141
CA
LYS
A
822
4.130
7.774
38.239
1.00
16.59
A


ATOM
1142
CB
LYS
A
822
4.698
9.016
38.936
1.00
16.10
A


ATOM
1143
CG
LYS
A
822
6.140
9.301
38.551
1.00
16.38
A


ATOM
1144
CD
LYS
A
822
6.486
10.792
38.596
1.00
17.94
A


ATOM
1145
CE
LYS
A
822
6.423
11.366
40.004
1.00
16.34
A


ATOM
1146
NZ
LYS
A
822
7.308
10.632
40.944
1.00
18.00
A


ATOM
1147
C
LYS
A
822
4.892
6.516
38.664
1.00
15.81
A


ATOM
1148
O
LYS
A
822
5.834
6.104
37.992
1.00
14.75
A


ATOM
1149
N
VAL
A
823
4.487
5.894
39.772
1.00
16.36
A


ATOM
1150
CA
VAL
A
823
5.160
4.672
40.203
1.00
14.72
A


ATOM
1151
CB
VAL
A
823
4.703
4.200
41.613
1.00
15.84
A


ATOM
1152
CG1
VAL
A
823
5.305
2.824
41.917
1.00
15.64
A


ATOM
1153
CG2
VAL
A
823
5.167
5.197
42.684
1.00
14.56
A


ATOM
1154
C
VAL
A
823
4.889
3.550
39.204
1.00
14.32
A


ATOM
1155
O
VAL
A
823
5.776
2.753
38.899
1.00
13.04
A


ATOM
1156
N
LEU
A
824
3.668
3.484
38.684
1.00
13.35
A


ATOM
1157
CA
LEU
A
824
3.340
2.437
37.725
1.00
14.01
A


ATOM
1158
CB
LEU
A
824
1.834
2.433
37.434
1.00
13.91
A


ATOM
1159
CG
LEU
A
824
0.993
2.089
38.671
1.00
16.39
A


ATOM
1160
CD1
LEU
A
824
−0.493
2.176
38.350
1.00
15.94
A


ATOM
1161
CD2
LEU
A
824
1.360
0.683
39.158
1.00
15.40
A


ATOM
1162
C
LEU
A
824
4.152
2.572
36.437
1.00
11.71
A


ATOM
1163
O
LEU
A
824
4.466
1.573
35.792
1.00
13.59
A


ATOM
1164
N
LEU
A
825
4.497
3.800
36.062
1.00
12.33
A


ATOM
1165
CA
LEU
A
825
5.301
4.012
34.862
1.00
12.91
A


ATOM
1166
CB
LEU
A
825
5.418
5.507
34.542
1.00
12.32
A


ATOM
1167
CG
LEU
A
825
4.228
6.126
33.799
1.00
14.73
A


ATOM
1168
CD1
LEU
A
825
4.491
7.612
33.545
1.00
16.34
A


ATOM
1169
CD2
LEU
A
825
4.023
5.389
32.478
1.00
12.28
A


ATOM
1170
C
LEU
A
825
6.698
3.407
35.058
1.00
13.79
A


ATOM
1171
O
LEU
A
825
7.252
2.791
34.147
1.00
13.59
A


ATOM
1172
N
LEU
A
826
7.262
3.583
36.251
1.00
12.61
A


ATOM
1173
CA
LEU
A
826
8.576
3.027
36.554
1.00
14.11
A


ATOM
1174
CB
LEU
A
826
8.977
3.375
37.994
1.00
14.02
A


ATOM
1175
CG
LEU
A
826
10.211
2.635
38.531
1.00
17.91
A


ATOM
1176
CD1
LEU
A
826
11.464
3.153
37.824
1.00
16.45
A


ATOM
1177
CD2
LEU
A
826
10.333
2.838
40.038
1.00
17.97
A


ATOM
1178
C
LEU
A
826
8.526
1.501
36.391
1.00
14.93
A


ATOM
1179
O
LEU
A
826
9.505
0.875
35.995
1.00
15.99
A


ATOM
1180
N
LEU
A
827
7.364
0.918
36.676
1.00
15.65
A


ATOM
1181
CA
LEU
A
827
7.168
−0.528
36.590
1.00
15.35
A


ATOM
1182
CB
LEU
A
827
6.430
−1.000
37.848
1.00
15.51
A


ATOM
1183
CG
LEU
A
827
6.949
−0.493
39.202
1.00
16.57
A


ATOM
1184
CD1
LEU
A
827
5.966
−0.846
40.304
1.00
15.59
A


ATOM
1185
CD2
LEU
A
827
8.320
−1.110
39.486
1.00
18.43
A


ATOM
1186
C
LEU
A
827
6.350
−0.952
35.362
1.00
17.65
A


ATOM
1187
O
LEU
A
827
5.749
−2.031
35.361
1.00
16.15
A


ATOM
1188
N
ASN
A
828
6.346
−0.131
34.314
1.00
18.51
A


ATOM
1189
CA
ASN
A
828
5.520
−0.424
33.141
1.00
16.99
A


ATOM
1190
CB
ASN
A
828
4.881
0.877
32.649
1.00
17.83
A


ATOM
1191
CG
ASN
A
828
3.418
0.703
32.307
1.00
20.51
A


ATOM
1192
OD1
ASN
A
828
2.743
−0.175
32.858
1.00
17.90
A


ATOM
1193
ND2
ASN
A
828
2.912
1.541
31.411
1.00
17.96
A


ATOM
1194
C
ASN
A
828
6.126
−1.180
31.958
1.00
17.76
A


ATOM
1195
O
ASN
A
828
5.448
−1.412
30.960
1.00
17.82
A


ATOM
1196
N
THR
A
829
7.391
−1.566
32.066
1.00
16.44
A


ATOM
1197
CA
THR
A
829
8.056
−2.318
31.013
1.00
16.99
A


ATOM
1198
CB
THR
A
829
8.866
−1.396
30.056
1.00
18.11
A


ATOM
1199
OG1
THR
A
829
8.008
−0.394
29.494
1.00
17.42
A


ATOM
1200
CG2
THR
A
829
9.474
−2.219
28.920
1.00
20.30
A


ATOM
1201
C
THR
A
829
9.031
−3.292
31.673
1.00
17.73
A


ATOM
1202
O
THR
A
829
9.717
−2.930
32.629
1.00
17.99
A


ATOM
1203
N
ILE
A
830
9.071
−4.531
31.189
1.00
17.90
A


ATOM
1204
CA
ILE
A
830
10.002
−5.519
31.724
1.00
18.71
A


ATOM
1205
CB
ILE
A
830
9.311
−6.520
32.685
1.00
19.83
A


ATOM
1206
CG2
ILE
A
830
8.568
−5.753
33.781
1.00
20.83
A


ATOM
1207
CG1
ILE
A
830
8.338
−7.423
31.922
1.00
18.24
A


ATOM
1208
CD1
ILE
A
830
7.762
−8.554
32.782
1.00
19.69
A


ATOM
1209
C
ILE
A
830
10.661
−6.278
30.572
1.00
19.02
A


ATOM
1210
O
ILE
A
830
10.193
−6.224
29.434
1.00
18.72
A


ATOM
1211
N
PRO
A
831
11.771
−6.981
30.849
1.00
19.69
A


ATOM
1212
CD
PRO
A
831
12.515
−7.077
32.118
1.00
17.13
A


ATOM
1213
CA
PRO
A
831
12.451
−7.725
29.789
1.00
20.61
A


ATOM
1214
CB
PRO
A
831
13.691
−8.289
30.491
1.00
20.77
A


ATOM
1215
CG
PRO
A
831
13.920
−7.336
31.637
1.00
19.58
A


ATOM
1216
C
PRO
A
831
11.555
−8.830
29.256
1.00
21.97
A


ATOM
1217
O
PRO
A
831
10.610
−9.247
29.922
1.00
21.43
A


ATOM
1218
N
LEU
A
832
11.855
−9.297
28.051
1.00
23.36
A


ATOM
1219
CA
LEU
A
832
11.082
−10.371
27.448
1.00
25.72
A


ATOM
1220
CB
LEU
A
832
11.617
−10.676
26.047
1.00
26.92
A


ATOM
1221
CG
LEU
A
832
11.334
−9.596
25.003
1.00
28.15
A


ATOM
1222
CD1
LEU
A
832
12.033
−9.942
23.699
1.00
30.17
A


ATOM
1223
CD2
LEU
A
832
9.827
−9.476
24.801
1.00
28.94
A


ATOM
1224
C
LEU
A
832
11.180
−11.619
28.318
1.00
26.21
A


ATOM
1225
O
LEU
A
832
10.217
−12.373
28.447
1.00
25.46
A


ATOM
1226
N
GLU
A
833
12.348
−11.822
28.918
1.00
25.70
A


ATOM
1227
CA
GLU
A
833
12.592
−12.982
29.770
1.00
27.45
A


ATOM
1228
CB
GLU
A
833
14.083
−13.354
29.741
1.00
29.43
A


ATOM
1229
CG
GLU
A
833
15.009
−12.303
30.357
1.00
32.13
A


ATOM
1230
CD
GLU
A
833
15.437
−11.215
29.378
1.00
33.98
A


ATOM
1231
OE1
GLU
A
833
14.668
−10.884
28.454
1.00
33.06
A


ATOM
1232
OE2
GLU
A
833
16.550
−10.675
29.545
1.00
36.26
A


ATOM
1233
C
GLU
A
833
12.156
−12.739
31.219
1.00
27.20
A


ATOM
1234
O
GLU
A
833
12.334
−13.599
32.081
1.00
27.90
A


ATOM
1235
N
GLY
A
834
11.583
−11.569
31.480
1.00
25.12
A


ATOM
1236
CA
GLY
A
834
11.153
−11.246
32.827
1.00
24.64
A


ATOM
1237
C
GLY
A
834
12.292
−10.725
33.687
1.00
23.57
A


ATOM
1238
O
GLY
A
834
13.425
−10.611
33.225
1.00
23.20
A


ATOM
1239
N
LEU
A
835
11.992
−10.409
34.941
1.00
22.62
A


ATOM
1240
CA
LEU
A
835
12.994
−9.896
35.868
1.00
23.78
A


ATOM
1241
CB
LEU
A
835
12.384
−8.781
36.718
1.00
21.76
A


ATOM
1242
CG
LEU
A
835
11.886
−7.540
35.965
1.00
22.76
A


ATOM
1243
CD1
LEU
A
835
11.025
−6.680
36.888
1.00
21.31
A


ATOM
1244
CD2
LEU
A
835
13.072
−6.745
35.448
1.00
21.97
A


ATOM
1245
C
LEU
A
835
13.517
−11.011
36.772
1.00
23.97
A


ATOM
1246
O
LEU
A
835
12.925
−12.085
36.847
1.00
23.94
A


ATOM
1247
N
ARG
A
836
14.632
−10.761
37.451
1.00
25.83
A


ATOM
1248
CA
ARG
A
836
15.198
−11.760
38.352
1.00
27.17
A


ATOM
1249
CB
ARG
A
836
16.594
−11.346
38.828
1.00
30.08
A


ATOM
1250
CG
ARG
A
836
17.643
−11.247
37.733
1.00
36.54
A


ATOM
1251
CD
ARG
A
836
19.056
−11.242
38.313
1.00
41.84
A


ATOM
1252
NE
ARG
A
836
19.633
−12.586
38.408
1.00
48.33
A


ATOM
1253
CZ
ARG
A
836
19.195
−13.552
39.214
1.00
50.99
A


ATOM
1254
NH1
ARG
A
836
18.164
−13.342
40.021
1.00
53.00
A


ATOM
1255
NH2
ARG
A
836
19.783
−14.741
39.205
1.00
52.15
A


ATOM
1256
C
ARG
A
836
14.286
−11.915
39.565
1.00
26.30
A


ATOM
1257
O
ARG
A
836
14.091
−13.021
40.068
1.00
25.88
A


ATOM
1258
N
SER
A
837
13.735
−10.797
40.029
1.00
23.15
A


ATOM
1259
CA
SER
A
837
12.840
−10.797
41.181
1.00
23.00
A


ATOM
1260
CB
SER
A
837
13.198
−9.644
42.128
1.00
23.75
A


ATOM
1261
OG
SER
A
837
14.548
−9.705
42.557
1.00
23.11
A


ATOM
1262
C
SER
A
837
11.403
−10.628
40.693
1.00
22.34
A


ATOM
1263
O
SER
A
837
10.647
−9.822
41.233
1.00
19.84
A


ATOM
1264
N
GLN
A
838
11.035
−11.398
39.671
1.00
23.15
A


ATOM
1265
CA
GLN
A
838
9.698
−11.326
39.081
1.00
24.26
A


ATOM
1266
CB
GLN
A
838
9.527
−12.422
38.020
1.00
25.27
A


ATOM
1267
CG
GLN
A
838
8.289
−12.273
37.134
1.00
22.45
A


ATOM
1268
CD
GLN
A
838
8.307
−10.999
36.290
1.00
25.56
A


ATOM
1269
OE1
GLN
A
838
9.336
−10.627
35.725
1.00
24.82
A


ATOM
1270
NE2
GLN
A
838
7.157
−10.338
36.187
1.00
23.08
A


ATOM
1271
C
GLN
A
838
8.565
−11.423
40.094
1.00
24.82
A


ATOM
1272
O
GLN
A
838
7.569
−10.706
39.983
1.00
23.75
A


ATOM
1273
N
THR
A
839
8.702
−12.314
41.074
1.00
26.33
A


ATOM
1274
CA
THR
A
839
7.662
−12.474
42.088
1.00
26.16
A


ATOM
1275
CB
THR
A
839
8.004
−13.597
43.088
1.00
28.64
A


ATOM
1276
OG1
THR
A
839
8.256
−14.816
42.378
1.00
30.75
A


ATOM
1277
CG2
THR
A
839
6.845
−13.817
44.050
1.00
26.66
A


ATOM
1278
C
THR
A
839
7.475
−11.179
42.873
1.00
25.53
A


ATOM
1279
O
THR
A
839
6.358
−10.681
43.010
1.00
25.17
A


ATOM
1280
N
GLN
A
840
8.576
−10.637
43.385
1.00
24.47
A


ATOM
1281
CA
GLN
A
840
8.526
−9.404
44.157
1.00
24.83
A


ATOM
1282
CB
GLN
A
840
9.912
−9.072
44.721
1.00
26.45
A


ATOM
1283
CG
GLN
A
840
10.482
−10.137
45.663
1.00
30.94
A


ATOM
1284
CD
GLN
A
840
11.324
−11.185
44.951
1.00
33.60
A


ATOM
1285
OE1
GLN
A
840
10.894
−11.795
43.966
1.00
32.51
A


ATOM
1286
NE2
GLN
A
840
12.534
−11.405
45.456
1.00
35.22
A


ATOM
1287
C
GLN
A
840
8.010
−8.242
43.307
1.00
23.05
A


ATOM
1288
O
GLN
A
840
7.231
−7.417
43.780
1.00
23.69
A


ATOM
1289
N
PHE
A
841
8.447
−8.180
42.052
1.00
21.65
A


ATOM
1290
CA
PHE
A
841
8.006
−7.123
41.145
1.00
20.44
A


ATOM
1291
CB
PHE
A
841
8.640
−7.311
39.763
1.00
19.26
A


ATOM
1292
CG
PHE
A
841
8.031
−6.441
38.697
1.00
18.62
A


ATOM
1293
CD1
PHE
A
841
8.448
−5.125
38.528
1.00
18.04
A


ATOM
1294
CD2
PHE
A
841
7.021
−6.932
37.877
1.00
19.63
A


ATOM
1295
CE1
PHE
A
841
7.865
−4.314
37.569
1.00
17.16
A


ATOM
1296
CE2
PHE
A
841
6.428
−6.123
36.913
1.00
18.19
A


ATOM
1297
CZ
PHE
A
841
6.855
−4.811
36.758
1.00
17.63
A


ATOM
1298
C
PHE
A
841
6.489
−7.195
41.007
1.00
20.37
A


ATOM
1299
O
PHE
A
841
5.790
−6.186
41.078
1.00
15.98
A


ATOM
1300
N
GLU
A
842
5.987
−8.405
40.797
1.00
20.47
A


ATOM
1301
CA
GLU
A
842
4.557
−8.607
40.635
1.00
23.77
A


ATOM
1302
CB
GLU
A
842
4.274
−10.091
40.400
1.00
27.79
A


ATOM
1303
CG
GLU
A
842
3.228
−10.343
39.345
1.00
32.65
A


ATOM
1304
CD
GLU
A
842
3.644
−9.861
37.961
1.00
32.93
A


ATOM
1305
OE1
GLU
A
842
4.434
−10.554
37.291
1.00
36.77
A


ATOM
1306
OE2
GLU
A
842
3.179
−8.786
37.542
1.00
33.52
A


ATOM
1307
C
GLU
A
842
3.800
−8.095
41.866
1.00
23.22
A


ATOM
1308
O
GLU
A
842
2.794
−7.399
41.740
1.00
22.93
A


ATOM
1309
N
GLU
A
843
4.293
−8.429
43.053
1.00
23.18
A


ATOM
1310
CA
GLU
A
843
3.658
−7.982
44.290
1.00
24.02
A


ATOM
1311
CB
GLU
A
843
4.334
−8.640
45.499
1.00
27.96
A


ATOM
1312
CG
GLU
A
843
3.980
−10.118
45.676
1.00
33.63
A


ATOM
1313
CD
GLU
A
843
4.660
−10.752
46.880
1.00
37.86
A


ATOM
1314
OE1
GLU
A
843
4.585
−10.176
47.986
1.00
41.00
A


ATOM
1315
OE2
GLU
A
843
5.265
−11.833
46.725
1.00
41.92
A


ATOM
1316
C
GLU
A
843
3.713
−6.457
44.426
1.00
21.45
A


ATOM
1317
O
GLU
A
843
2.748
−5.825
44.848
1.00
20.19
A


ATOM
1318
N
MET
A
844
4.842
−5.869
44.055
1.00
19.19
A


ATOM
1319
CA
MET
A
844
5.005
−4.418
44.143
1.00
19.24
A


ATOM
1320
CB
MET
A
844
6.454
−4.032
43.832
1.00
19.91
A


ATOM
1321
CG
MET
A
844
6.747
−2.542
43.974
1.00
19.06
A


ATOM
1322
SD
MET
A
844
8.449
−2.108
43.505
1.00
21.31
A


ATOM
1323
CE
MET
A
844
8.364
−0.338
43.669
1.00
16.72
A


ATOM
1324
C
MET
A
844
4.064
−3.703
43.172
1.00
18.33
A


ATOM
1325
O
MET
A
844
3.332
−2.793
43.558
1.00
17.42
A


ATOM
1326
N
ARG
A
845
4.087
−4.121
41.910
1.00
18.70
A


ATOM
1327
CA
ARG
A
845
3.230
−3.511
40.894
1.00
19.90
A


ATOM
1328
CB
ARG
A
845
3.474
−4.180
39.539
1.00
20.02
A


ATOM
1329
CG
ARG
A
845
2.649
−3.614
38.385
1.00
21.73
A


ATOM
1330
CD
ARG
A
845
3.201
−4.107
37.053
1.00
24.38
A


ATOM
1331
NE
ARG
A
845
2.496
−3.542
35.903
1.00
28.68
A


ATOM
1332
CZ
ARG
A
845
1.308
−3.950
35.474
1.00
29.80
A


ATOM
1333
NH1
ARG
A
845
0.677
−4.939
36.096
1.00
31.71
A


ATOM
1334
NH2
ARG
A
845
0.750
−3.369
34.419
1.00
32.30
A


ATOM
1335
C
ARG
A
845
1.754
−3.631
41.284
1.00
19.74
A


ATOM
1336
O
ARG
A
845
1.004
−2.657
41.227
1.00
18.83
A


ATOM
1337
N
SER
A
846
1.341
−4.824
41.692
1.00
18.87
A


ATOM
1338
CA
SER
A
846
−0.044
−5.025
42.083
1.00
19.72
A


ATOM
1339
CB
SER
A
846
−0.275
−6.491
42.452
1.00
21.67
A


ATOM
1340
OG
SER
A
846
−0.127
−7.322
41.306
1.00
21.71
A


ATOM
1341
C
SER
A
846
−0.420
−4.107
43.247
1.00
20.41
A


ATOM
1342
O
SER
A
846
−1.524
−3.563
43.291
1.00
19.34
A


ATOM
1343
N
SER
A
847
0.506
−3.923
44.184
1.00
19.04
A


ATOM
1344
CA
SER
A
847
0.247
−3.063
45.329
1.00
18.35
A


ATOM
1345
CB
SER
A
847
1.408
−3.137
46.323
1.00
20.48
A


ATOM
1346
OG
SER
A
847
1.220
−2.210
47.372
1.00
24.25
A


ATOM
1347
C
SER
A
847
0.016
−1.612
44.918
1.00
17.69
A


ATOM
1348
O
SER
A
847
−0.853
−0.938
45.465
1.00
16.70
A


ATOM
1349
N
TYR
A
848
0.794
−1.120
43.960
1.00
16.16
A


ATOM
1350
CA
TYR
A
848
0.615
0.258
43.525
1.00
16.48
A


ATOM
1351
CB
TYR
A
848
1.873
0.740
42.804
1.00
16.12
A


ATOM
1352
CG
TYR
A
848
2.954
1.112
43.796
1.00
15.32
A


ATOM
1353
CD1
TYR
A
848
2.862
2.292
44.541
1.00
15.55
A


ATOM
1354
CE1
TYR
A
848
3.817
2.616
45.507
1.00
15.99
A


ATOM
1355
CD2
TYR
A
848
4.031
0.264
44.040
1.00
16.08
A


ATOM
1356
CE2
TYR
A
848
4.993
0.579
45.005
1.00
15.10
A


ATOM
1357
CZ
TYR
A
848
4.878
1.756
45.733
1.00
17.33
A


ATOM
1358
OH
TYR
A
848
5.825
2.076
46.682
1.00
16.56
A


ATOM
1359
C
TYR
A
848
−0.643
0.428
42.674
1.00
16.19
A


ATOM
1360
O
TYR
A
848
−1.233
1.509
42.636
1.00
16.16
A


ATOM
1361
N
ILE
A
849
−1.060
−0.640
42.003
1.00
16.12
A


ATOM
1362
CA
ILE
A
849
−2.286
−0.588
41.209
1.00
17.53
A


ATOM
1363
CB
ILE
A
849
−2.487
−1.883
40.375
1.00
16.60
A


ATOM
1364
CG2
ILE
A
849
−3.915
−1.928
39.806
1.00
11.46
A


ATOM
1365
CG1
ILE
A
849
−1.443
−1.943
39.255
1.00
16.24
A


ATOM
1366
CD1
ILE
A
849
−1.505
−3.204
38.413
1.00
17.37
A


ATOM
1367
C
ILE
A
849
−3.419
−0.459
42.232
1.00
17.52
A


ATOM
1368
O
ILE
A
849
−4.350
0.331
42.062
1.00
19.29
A


ATOM
1369
N
ARG
A
850
−3.327
−1.237
43.306
1.00
18.62
A


ATOM
1370
CA
ARG
A
850
−4.337
−1.179
44.356
1.00
19.04
A


ATOM
1371
CB
ARG
A
850
−4.081
−2.252
45.425
1.00
17.63
A


ATOM
1372
CG
ARG
A
850
−4.325
−3.677
44.942
1.00
20.04
A


ATOM
1373
CD
ARG
A
850
−4.508
−4.651
46.104
1.00
19.34
A


ATOM
1374
NE
ARG
A
850
−3.302
−4.816
46.905
1.00
21.22
A


ATOM
1375
CZ
ARG
A
850
−2.261
−5.569
46.558
1.00
23.77
A


ATOM
1376
NH1
ARG
A
850
−2.266
−6.246
45.413
1.00
20.56
A


ATOM
1377
NH2
ARG
A
850
−1.202
−5.641
47.360
1.00
23.31
A


ATOM
1378
C
ARG
A
850
−4.333
0.206
45.002
1.00
18.72
A


ATOM
1379
O
ARG
A
850
−5.384
0.717
45.410
1.00
17.53
A


ATOM
1380
N
GLU
A
851
−3.158
0.825
45.080
1.00
17.58
A


ATOM
1381
CA
GLU
A
851
−3.049
2.154
45.687
1.00
16.80
A


ATOM
1382
CB
GLU
A
851
−1.580
2.476
45.987
1.00
17.63
A


ATOM
1383
CG
GLU
A
851
−1.378
3.485
47.117
1.00
18.50
A


ATOM
1384
CD
GLU
A
851
−1.946
2.995
48.444
1.00
17.77
A


ATOM
1385
OE1
GLU
A
851
−2.123
1.767
48.597
1.00
17.44
A


ATOM
1386
OE2
GLU
A
851
−2.198
3.834
49.340
1.00
18.22
A


ATOM
1387
C
GLU
A
851
−3.657
3.222
44.768
1.00
16.79
A


ATOM
1388
O
GLU
A
851
−4.258
4.200
45.235
1.00
20.29
A


ATOM
1389
N
LEU
A
852
−3.497
3.040
43.462
1.00
15.37
A


ATOM
1390
CA
LEU
A
852
−4.063
3.973
42.493
1.00
16.55
A


ATOM
1391
CB
LEU
A
852
−3.708
3.554
41.063
1.00
15.51
A


ATOM
1392
CG
LEU
A
852
−4.438
4.310
39.941
1.00
16.71
A


ATOM
1393
CD1
LEU
A
852
−4.188
5.810
40.076
1.00
14.65
A


ATOM
1394
CD2
LEU
A
852
−3.972
3.807
38.582
1.00
16.68
A


ATOM
1395
C
LEU
A
852
−5.576
3.934
42.666
1.00
17.16
A


ATOM
1396
O
LEU
A
852
−6.251
4.959
42.593
1.00
17.80
A


ATOM
1397
N
ILE
A
853
−6.102
2.734
42.890
1.00
17.86
A


ATOM
1398
CA
ILE
A
853
−7.535
2.563
43.078
1.00
18.24
A


ATOM
1399
CB
ILE
A
853
−7.898
1.061
43.173
1.00
17.18
A


ATOM
1400
CG2
ILE
A
853
−9.353
0.880
43.639
1.00
18.01
A


ATOM
1401
CG1
ILE
A
853
−7.700
0.415
41.797
1.00
15.66
A


ATOM
1402
CD1
ILE
A
853
−7.798
−1.103
41.795
1.00
15.60
A


ATOM
1403
C
ILE
A
853
−8.003
3.322
44.316
1.00
18.88
A


ATOM
1404
O
ILE
A
853
−9.065
3.946
44.294
1.00
20.72
A


ATOM
1405
N
LYS
A
854
−7.207
3.290
45.385
1.00
19.21
A


ATOM
1406
CA
LYS
A
854
−7.559
4.009
46.609
1.00
19.73
A


ATOM
1407
CB
LYS
A
854
−6.574
3.697
47.739
1.00
19.29
A


ATOM
1408
CG
LYS
A
854
−6.560
2.276
48.255
1.00
23.21
A


ATOM
1409
CD
LYS
A
854
−5.459
2.177
49.304
1.00
25.78
A


ATOM
1410
CE
LYS
A
854
−5.237
0.771
49.787
1.00
27.22
A


ATOM
1411
NZ
LYS
A
854
−4.022
0.746
50.645
1.00
27.63
A


ATOM
1412
C
LYS
A
854
−7.530
5.517
46.352
1.00
18.40
A


ATOM
1413
O
LYS
A
854
−8.353
6.267
46.882
1.00
17.47
A


ATOM
1414
N
ALA
A
855
−6.559
5.956
45.554
1.00
18.32
A


ATOM
1415
CA
ALA
A
855
−6.414
7.371
45.216
1.00
19.46
A


ATOM
1416
CB
ALA
A
855
−5.177
7.574
44.332
1.00
18.11
A


ATOM
1417
C
ALA
A
855
−7.668
7.854
44.486
1.00
20.08
A


ATOM
1418
O
ALA
A
855
−8.194
8.931
44.771
1.00
20.31
A


ATOM
1419
N
ILE
A
856
−8.138
7.054
43.535
1.00
21.87
A


ATOM
1420
CA
ILE
A
856
−9.341
7.393
42.779
1.00
22.21
A


ATOM
1421
CB
ILE
A
856
−9.663
6.312
41.720
1.00
21.32
A


ATOM
1422
CG2
ILE
A
856
−11.043
6.574
41.106
1.00
22.81
A


ATOM
1423
CG1
ILE
A
856
−8.591
6.318
40.626
1.00
21.10
A


ATOM
1424
CD1
ILE
A
856
−8.721
5.169
39.625
1.00
17.78
A


ATOM
1425
C
ILE
A
856
−10.525
7.495
43.739
1.00
23.75
A


ATOM
1426
O
ILE
A
856
−11.333
8.417
43.651
1.00
23.51
A


ATOM
1427
N
GLY
A
857
−10.617
6.539
44.657
1.00
24.69
A


ATOM
1428
CA
GLY
A
857
−11.712
6.531
45.611
1.00
25.96
A


ATOM
1429
C
GLY
A
857
−11.791
7.754
46.508
1.00
27.36
A


ATOM
1430
O
GLY
A
857
−12.818
7.993
47.145
1.00
25.78
A


ATOM
1431
N
LEU
A
858
−10.713
8.533
46.566
1.00
28.12
A


ATOM
1432
CA
LEU
A
858
−10.687
9.733
47.400
1.00
29.63
A


ATOM
1433
CB
LEU
A
858
−9.275
10.330
47.437
1.00
28.28
A


ATOM
1434
CG
LEU
A
858
−8.196
9.521
48.153
1.00
27.33
A


ATOM
1435
CD1
LEU
A
858
−6.867
10.264
48.070
1.00
27.66
A


ATOM
1436
CD2
LEU
A
858
−8.611
9.294
49.606
1.00
27.32
A


ATOM
1437
C
LEU
A
858
−11.663
10.807
46.921
1.00
32.53
A


ATOM
1438
O
LEU
A
858
−12.139
11.621
47.714
1.00
31.16
A


ATOM
1439
N
ARG
A
859
−11.956
10.816
45.626
1.00
35.00
A


ATOM
1440
CA
ARG
A
859
−12.864
11.814
45.076
1.00
40.11
A


ATOM
1441
CB
ARG
A
859
−12.079
12.810
44.218
1.00
41.59
A


ATOM
1442
CG
ARG
A
859
−10.950
13.477
44.983
1.00
45.19
A


ATOM
1443
CD
ARG
A
859
−10.168
14.479
44.149
1.00
46.94
A


ATOM
1444
NE
ARG
A
859
−9.060
15.024
44.929
1.00
49.30
A


ATOM
1445
CZ
ARG
A
859
−8.256
16.000
44.524
1.00
50.75
A


ATOM
1446
NH1
ARG
A
859
−8.426
16.560
43.333
1.00
52.23
A


ATOM
1447
NH2
ARG
A
859
−7.278
16.418
45.317
1.00
50.68
A


ATOM
1448
C
ARG
A
859
−13.964
11.169
44.251
1.00
43.10
A


ATOM
1449
O
ARG
A
859
−15.145
11.469
44.429
1.00
43.32
A


ATOM
1450
N
GLN
A
860
−13.568
10.282
43.346
1.00
45.83
A


ATOM
1451
CA
GLN
A
860
−14.521
9.592
42.493
1.00
48.83
A


ATOM
1452
CB
GLN
A
860
−13.782
8.786
41.424
1.00
49.90
A


ATOM
1453
CG
GLN
A
860
−12.820
9.633
40.604
1.00
50.95
A


ATOM
1454
CD
GLN
A
860
−13.514
10.785
39.901
1.00
51.85
A


ATOM
1455
OE1
GLN
A
860
−12.874
11.756
39.498
1.00
52.01
A


ATOM
1456
NE2
GLN
A
860
−14.829
10.677
39.742
1.00
52.02
A


ATOM
1457
C
GLN
A
860
−15.386
8.682
43.346
1.00
50.16
A


ATOM
1458
O
GLN
A
860
−15.055
7.519
43.580
1.00
51.05
A


ATOM
1459
N
LYS
A
861
−16.496
9.235
43.821
1.00
50.99
A


ATOM
1460
CA
LYS
A
861
−17.425
8.497
44.657
1.00
51.23
A


ATOM
1461
CB
LYS
A
861
−18.081
9.450
45.657
1.00
52.22
A


ATOM
1462
CG
LYS
A
861
−17.072
10.173
46.543
1.00
53.62
A


ATOM
1463
CD
LYS
A
861
−17.738
11.203
47.441
1.00
56.57
A


ATOM
1464
CE
LYS
A
861
−18.380
12.322
46.629
1.00
57.51
A


ATOM
1465
NZ
LYS
A
861
−19.063
13.320
47.501
1.00
57.72
A


ATOM
1466
C
LYS
A
861
−18.469
7.844
43.763
1.00
50.75
A


ATOM
1467
O
LYS
A
861
−19.079
8.499
42.917
1.00
51.25
A


ATOM
1468
N
GLY
A
862
−18.660
6.544
43.950
1.00
48.78
A


ATOM
1469
CA
GLY
A
862
−19.614
5.815
43.139
1.00
46.59
A


ATOM
1470
C
GLY
A
862
−18.891
4.728
42.371
1.00
45.09
A


ATOM
1471
O
GLY
A
862
−17.832
4.966
41.789
1.00
42.61
A


ATOM
1472
N
VAL
A
863
−19.464
3.532
42.367
1.00
43.94
A


ATOM
1473
CA
VAL
A
863
−18.859
2.401
41.678
1.00
44.09
A


ATOM
1474
CB
VAL
A
863
−19.721
1.130
41.853
1.00
44.83
A


ATOM
1475
CG1
VAL
A
863
−19.897
0.829
43.334
1.00
46.10
A


ATOM
1476
CG2
VAL
A
863
−21.074
1.319
41.193
1.00
45.96
A


ATOM
1477
C
VAL
A
863
−18.624
2.641
40.186
1.00
42.90
A


ATOM
1478
O
VAL
A
863
−17.542
2.357
39.671
1.00
43.15
A


ATOM
1479
N
VAL
A
864
−19.628
3.168
39.493
1.00
40.87
A


ATOM
1480
CA
VAL
A
864
−19.506
3.414
38.061
1.00
39.53
A


ATOM
1481
CB
VAL
A
864
−20.878
3.775
37.430
1.00
39.71
A


ATOM
1482
CG1
VAL
A
864
−21.395
5.075
38.002
1.00
40.62
A


ATOM
1483
CG2
VAL
A
864
−20.745
3.874
35.921
1.00
41.26
A


ATOM
1484
C
VAL
A
864
−18.500
4.519
37.748
1.00
37.88
A


ATOM
1485
O
VAL
A
864
−17.720
4.403
36.806
1.00
37.34
A


ATOM
1486
N
SER
A
865
−18.518
5.585
38.540
1.00
35.74
A


ATOM
1487
CA
SER
A
865
−17.598
6.696
38.338
1.00
35.39
A


ATOM
1488
CB
SER
A
865
−17.972
7.865
39.251
1.00
37.79
A


ATOM
1489
OG
SER
A
865
−17.071
8.943
39.081
1.00
41.84
A


ATOM
1490
C
SER
A
865
−16.153
6.283
38.614
1.00
33.45
A


ATOM
1491
O
SER
A
865
−15.262
6.529
37.800
1.00
31.58
A


ATOM
1492
N
SER
A
866
−15.927
5.654
39.764
1.00
30.19
A


ATOM
1493
CA
SER
A
866
−14.584
5.224
40.136
1.00
29.83
A


ATOM
1494
CB
SER
A
866
−14.567
4.714
41.584
1.00
30.55
A


ATOM
1495
OG
SER
A
866
−15.330
3.528
41.733
1.00
35.07
A


ATOM
1496
C
SER
A
866
−14.073
4.142
39.186
1.00
28.90
A


ATOM
1497
O
SER
A
866
−12.871
4.046
38.925
1.00
26.65
A


ATOM
1498
N
SER
A
867
−14.991
3.338
38.661
1.00
28.37
A


ATOM
1499
CA
SER
A
867
−14.634
2.268
37.732
1.00
30.83
A


ATOM
1500
CB
SER
A
867
−15.815
1.313
37.549
1.00
32.58
A


ATOM
1501
OG
SER
A
867
−15.419
0.156
36.834
1.00
39.29
A


ATOM
1502
C
SER
A
867
−14.214
2.845
36.376
1.00
30.15
A


ATOM
1503
O
SER
A
867
−13.253
2.376
35.760
1.00
29.63
A


ATOM
1504
N
GLN
A
868
−14.940
3.857
35.912
1.00
29.59
A


ATOM
1505
CA
GLN
A
868
−14.616
4.501
34.643
1.00
30.50
A


ATOM
1506
CB
GLN
A
868
−15.735
5.459
34.225
1.00
33.42
A


ATOM
1507
CG
GLN
A
868
−17.027
4.768
33.798
1.00
40.79
A


ATOM
1508
CD
GLN
A
868
−18.021
5.727
33.160
1.00
44.38
A


ATOM
1509
OE1
GLN
A
868
−17.714
6.387
32.164
1.00
48.14
A


ATOM
1510
NE2
GLN
A
868
−19.219
5.806
33.729
1.00
47.00
A


ATOM
1511
C
GLN
A
868
−13.306
5.279
34.780
1.00
28.76
A


ATOM
1512
O
GLN
A
868
−12.501
5.339
33.847
1.00
28.37
A


ATOM
1513
N
ARG
A
869
−13.106
5.875
35.952
1.00
25.54
A


ATOM
1514
CA
ARG
A
869
−11.904
6.651
36.239
1.00
23.93
A


ATOM
1515
CB
ARG
A
869
−12.001
7.257
37.643
1.00
24.14
A


ATOM
1516
CG
ARG
A
869
−10.842
8.165
38.026
1.00
24.38
A


ATOM
1517
CD
ARG
A
869
−10.865
9.446
37.230
1.00
26.98
A


ATOM
1518
NE
ARG
A
869
−9.901
10.419
37.734
1.00
26.60
A


ATOM
1519
CZ
ARG
A
869
−9.722
11.624
37.209
1.00
27.32
A


ATOM
1520
NH1
ARG
A
869
−10.443
12.002
36.159
1.00
27.79
A


ATOM
1521
NH2
ARG
A
869
−8.831
12.453
37.734
1.00
26.20
A


ATOM
1522
C
ARG
A
869
−10.667
5.760
36.142
1.00
21.71
A


ATOM
1523
O
ARG
A
869
−9.640
6.159
35.589
1.00
21.09
A


ATOM
1524
N
PHE
A
870
−10.767
4.553
36.689
1.00
20.52
A


ATOM
1525
CA
PHE
A
870
−9.657
3.607
36.649
1.00
21.95
A


ATOM
1526
CB
PHE
A
870
−10.030
2.313
37.380
1.00
23.09
A


ATOM
1527
CG
PHE
A
870
−8.945
1.273
37.361
1.00
23.44
A


ATOM
1528
CD1
PHE
A
870
−7.878
1.342
38.252
1.00
24.31
A


ATOM
1529
CD2
PHE
A
870
−8.975
0.237
36.432
1.00
23.49
A


ATOM
1530
CE1
PHE
A
870
−6.858
0.391
38.215
1.00
23.31
A


ATOM
1531
CE2
PHE
A
870
−7.960
−0.717
36.388
1.00
23.17
A


ATOM
1532
CZ
PHE
A
870
−6.902
−0.639
37.281
1.00
22.88
A


ATOM
1533
C
PHE
A
870
−9.316
3.290
35.192
1.00
22.30
A


ATOM
1534
O
PHE
A
870
−8.145
3.189
34.818
1.00
19.13
A


ATOM
1535
N
TYR
A
871
−10.346
3.131
34.367
1.00
22.40
A


ATOM
1536
CA
TYR
A
871
−10.132
2.835
32.957
1.00
23.09
A


ATOM
1537
CB
TYR
A
871
−11.466
2.628
32.234
1.00
25.44
A


ATOM
1538
CG
TYR
A
871
−11.291
2.436
30.743
1.00
29.50
A


ATOM
1539
CD1
TYR
A
871
−10.944
1.192
30.216
1.00
31.45
A


ATOM
1540
CE1
TYR
A
871
−10.709
1.027
28.846
1.00
34.54
A


ATOM
1541
CD2
TYR
A
871
−11.404
3.516
29.865
1.00
30.74
A


ATOM
1542
CE2
TYR
A
871
−11.168
3.362
28.499
1.00
33.34
A


ATOM
1543
CZ
TYR
A
871
−10.821
2.117
27.998
1.00
34.38
A


ATOM
1544
OH
TYR
A
871
−10.579
1.966
26.650
1.00
38.83
A


ATOM
1545
C
TYR
A
871
−9.388
3.986
32.285
1.00
21.64
A


ATOM
1546
O
TYR
A
871
−8.399
3.778
31.587
1.00
20.89
A


ATOM
1547
N
GLN
A
872
−9.881
5.200
32.501
1.00
21.08
A


ATOM
1548
CA
GLN
A
872
−9.295
6.394
31.899
1.00
21.63
A


ATOM
1549
CB
GLN
A
872
−10.088
7.627
32.309
1.00
23.97
A


ATOM
1550
CG
GLN
A
872
−11.548
7.594
31.907
1.00
29.50
A


ATOM
1551
CD
GLN
A
872
−12.270
8.844
32.344
1.00
32.02
A


ATOM
1552
OE1
GLN
A
872
−12.344
9.148
33.536
1.00
35.43
A


ATOM
1553
NE2
GLN
A
872
−12.800
9.585
31.381
1.00
36.11
A


ATOM
1554
C
GLN
A
872
−7.833
6.626
32.263
1.00
20.95
A


ATOM
1555
O
GLN
A
872
−6.998
6.879
31.392
1.00
17.56
A


ATOM
1556
N
LEU
A
873
−7.533
6.557
33.553
1.00
18.12
A


ATOM
1557
CA
LEU
A
873
−6.175
6.791
34.007
1.00
19.84
A


ATOM
1558
CB
LEU
A
873
−6.145
6.878
35.538
1.00
19.94
A


ATOM
1559
CG
LEU
A
873
−6.994
8.036
36.083
1.00
20.53
A


ATOM
1560
CD1
LEU
A
873
−6.851
8.145
37.598
1.00
20.93
A


ATOM
1561
CD2
LEU
A
873
−6.551
9.336
35.417
1.00
23.05
A


ATOM
1562
C
LEU
A
873
−5.221
5.724
33.500
1.00
20.65
A


ATOM
1563
O
LEU
A
873
−4.110
6.033
33.062
1.00
19.40
A


ATOM
1564
N
THR
A
874
−5.656
4.468
33.542
1.00
20.04
A


ATOM
1565
CA
THR
A
874
−4.811
3.382
33.077
1.00
20.77
A


ATOM
1566
CB
THR
A
874
−5.361
2.017
33.538
1.00
20.85
A


ATOM
1567
OG1
THR
A
874
−6.725
1.878
33.126
1.00
21.70
A


ATOM
1568
CG2
THR
A
874
−5.279
1.905
35.062
1.00
20.63
A


ATOM
1569
C
THR
A
874
−4.689
3.425
31.553
1.00
22.66
A


ATOM
1570
O
THR
A
874
−3.623
3.132
30.992
1.00
23.26
A


ATOM
1571
N
LYS
A
875
−5.773
3.806
30.885
1.00
22.44
A


ATOM
1572
CA
LYS
A
875
−5.752
3.915
29.431
1.00
23.45
A


ATOM
1573
CB
LYS
A
875
−7.129
4.316
28.890
1.00
24.25
A


ATOM
1574
CG
LYS
A
875
−7.208
4.331
27.369
1.00
27.73
A


ATOM
1575
CD
LYS
A
875
−6.942
2.944
26.792
1.00
30.15
A


ATOM
1576
CE
LYS
A
875
−6.923
2.964
25.270
1.00
31.96
A


ATOM
1577
NZ
LYS
A
875
−6.757
1.594
24.705
1.00
35.36
A


ATOM
1578
C
LYS
A
875
−4.722
4.976
29.047
1.00
22.41
A


ATOM
1579
O
LYS
A
875
−3.984
4.810
28.079
1.00
23.26
A


ATOM
1580
N
LEU
A
876
−4.679
6.066
29.813
1.00
22.49
A


ATOM
1581
CA
LEU
A
876
−3.728
7.149
29.565
1.00
22.37
A


ATOM
1582
CB
LEU
A
876
−3.914
8.264
30.606
1.00
22.36
A


ATOM
1583
CG
LEU
A
876
−3.128
9.579
30.483
1.00
24.28
A


ATOM
1584
CD1
LEU
A
876
−3.717
10.604
31.439
1.00
24.81
A


ATOM
1585
CD2
LEU
A
876
−1.654
9.362
30.796
1.00
23.97
A


ATOM
1586
C
LEU
A
876
−2.305
6.589
29.640
1.00
22.30
A


ATOM
1587
O
LEU
A
876
−1.469
6.875
28.777
1.00
19.88
A


ATOM
1588
N
LEU
A
877
−2.033
5.788
30.668
1.00
20.81
A


ATOM
1589
CA
LEU
A
877
−0.708
5.198
30.814
1.00
20.51
A


ATOM
1590
CB
LEU
A
877
−0.609
4.409
32.125
1.00
18.01
A


ATOM
1591
CG
LEU
A
877
−0.722
5.272
33.391
1.00
19.57
A


ATOM
1592
CD1
LEU
A
877
−0.644
4.381
34.623
1.00
19.95
A


ATOM
1593
CD2
LEU
A
877
0.397
6.318
33.422
1.00
19.10
A


ATOM
1594
C
LEU
A
877
−0.404
4.300
29.614
1.00
20.50
A


ATOM
1595
O
LEU
A
877
0.714
4.322
29.085
1.00
17.23
A


ATOM
1596
N
ASP
A
878
−1.389
3.518
29.177
1.00
20.16
A


ATOM
1597
CA
ASP
A
878
−1.191
2.651
28.014
1.00
21.77
A


ATOM
1598
CB
ASP
A
878
−2.474
1.885
27.657
1.00
22.61
A


ATOM
1599
CG
ASP
A
878
−2.712
0.658
28.530
1.00
24.90
A


ATOM
1600
OD1
ASP
A
878
−1.883
0.338
29.408
1.00
20.69
A


ATOM
1601
OD2
ASP
A
878
−3.756
−0.002
28.323
1.00
27.24
A


ATOM
1602
C
ASP
A
878
−0.802
3.518
26.813
1.00
21.54
A


ATOM
1603
O
ASP
A
878
0.132
3.194
26.076
1.00
22.58
A


ATOM
1604
N
ASN
A
879
−1.524
4.620
26.625
1.00
21.91
A


ATOM
1605
CA
ASN
A
879
−1.275
5.529
25.509
1.00
24.62
A


ATOM
1606
CB
ASN
A
879
−2.361
6.612
25.432
1.00
23.63
A


ATOM
1607
CG
ASN
A
879
−3.730
6.054
25.063
1.00
26.89
A


ATOM
1608
OD1
ASN
A
879
−3.840
4.973
24.486
1.00
26.87
A


ATOM
1609
ND2
ASN
A
879
−4.781
6.807
25.381
1.00
26.39
A


ATOM
1610
C
ASN
A
879
0.098
6.203
25.549
1.00
25.62
A


ATOM
1611
O
ASN
A
879
0.593
6.658
24.517
1.00
26.49
A


ATOM
1612
N
LEU
A
880
0.711
6.276
26.727
1.00
24.07
A


ATOM
1613
CA
LEU
A
880
2.028
6.900
26.838
1.00
25.83
A


ATOM
1614
CB
LEU
A
880
2.456
7.033
28.298
1.00
25.52
A


ATOM
1615
CG
LEU
A
880
1.906
8.225
29.081
1.00
29.53
A


ATOM
1616
CD1
LEU
A
880
2.583
8.268
30.450
1.00
27.82
A


ATOM
1617
CD2
LEU
A
880
2.170
9.524
28.315
1.00
28.47
A


ATOM
1618
C
LEU
A
880
3.112
6.146
26.078
1.00
25.34
A


ATOM
1619
O
LEU
A
880
4.035
6.760
25.549
1.00
25.19
A


ATOM
1620
N
HIS
A
881
3.007
4.818
26.038
1.00
26.40
A


ATOM
1621
CA
HIS
A
881
3.987
3.995
25.335
1.00
26.00
A


ATOM
1622
CB
HIS
A
881
3.520
2.532
25.290
1.00
27.74
A


ATOM
1623
CG
HIS
A
881
3.805
1.765
26.548
1.00
29.80
A


ATOM
1624
CD2
HIS
A
881
4.934
1.656
27.289
1.00
29.97
A


ATOM
1625
ND1
HIS
A
881
2.866
0.962
27.162
1.00
31.29
A


ATOM
1626
CE1
HIS
A
881
3.404
0.391
28.226
1.00
30.71
A


ATOM
1627
NE2
HIS
A
881
4.659
0.796
28.325
1.00
32.87
A


ATOM
1628
C
HIS
A
881
4.235
4.508
23.916
1.00
26.38
A


ATOM
1629
O
HIS
A
881
5.379
4.641
23.483
1.00
25.86
A


ATOM
1630
N
ASP
A
882
3.159
4.816
23.203
1.00
25.87
A


ATOM
1631
CA
ASP
A
882
3.267
5.303
21.835
1.00
25.66
A


ATOM
1632
CB
ASP
A
882
1.891
5.273
21.179
1.00
31.45
A


ATOM
1633
CG
ASP
A
882
1.262
3.900
21.238
1.00
35.82
A


ATOM
1634
OD1
ASP
A
882
1.688
3.017
20.460
1.00
37.06
A


ATOM
1635
OD2
ASP
A
882
0.359
3.699
22.081
1.00
39.76
A


ATOM
1636
C
ASP
A
882
3.853
6.706
21.757
1.00
23.14
A


ATOM
1637
O
ASP
A
882
4.692
6.990
20.904
1.00
23.94
A


ATOM
1638
N
LEU
A
883
3.412
7.583
22.648
1.00
20.96
A


ATOM
1639
CA
LEU
A
883
3.914
8.950
22.671
1.00
20.25
A


ATOM
1640
CB
LEU
A
883
3.146
9.759
23.719
1.00
20.75
A


ATOM
1641
CG
LEU
A
883
3.408
11.260
23.836
1.00
23.11
A


ATOM
1642
CD1
LEU
A
883
2.206
11.911
24.517
1.00
24.84
A


ATOM
1643
CD2
LEU
A
883
4.692
11.525
24.624
1.00
24.63
A


ATOM
1644
C
LEU
A
883
5.414
8.925
22.989
1.00
19.01
A


ATOM
1645
O
LEU
A
883
6.209
9.615
22.354
1.00
16.78
A


ATOM
1646
N
VAL
A
884
5.794
8.116
23.971
1.00
18.69
A


ATOM
1647
CA
VAL
A
884
7.193
7.987
24.370
1.00
16.95
A


ATOM
1648
CB
VAL
A
884
7.301
7.148
25.666
1.00
17.81
A


ATOM
1649
CG1
VAL
A
884
8.753
6.772
25.953
1.00
15.34
A


ATOM
1650
CG2
VAL
A
884
6.724
7.954
26.831
1.00
15.89
A


ATOM
1651
C
VAL
A
884
8.061
7.377
23.261
1.00
17.62
A


ATOM
1652
O
VAL
A
884
9.264
7.631
23.189
1.00
17.21
A


ATOM
1653
N
LYS
A
885
7.458
6.585
22.384
1.00
18.89
A


ATOM
1654
CA
LYS
A
885
8.227
5.995
21.296
1.00
19.66
A


ATOM
1655
CB
LYS
A
885
7.388
4.976
20.532
1.00
22.16
A


ATOM
1656
CG
LYS
A
885
8.142
4.308
19.388
1.00
24.56
A


ATOM
1657
CD
LYS
A
885
7.292
3.222
18.738
1.00
27.97
A


ATOM
1658
CE
LYS
A
885
7.977
2.647
17.506
1.00
30.89
A


ATOM
1659
NZ
LYS
A
885
7.178
1.532
16.917
1.00
33.14
A


ATOM
1660
C
LYS
A
885
8.741
7.078
20.341
1.00
19.41
A


ATOM
1661
O
LYS
A
885
9.855
6.976
19.820
1.00
17.34
A


ATOM
1662
N
GLN
A
886
7.943
8.117
20.114
1.00
20.30
A


ATOM
1663
CA
GLN
A
886
8.368
9.208
19.237
1.00
20.05
A


ATOM
1664
CB
GLN
A
886
7.214
10.175
18.982
1.00
24.07
A


ATOM
1665
CG
GLN
A
886
6.098
9.593
18.119
1.00
31.54
A


ATOM
1666
CD
GLN
A
886
4.942
10.566
17.914
1.00
36.15
A


ATOM
1667
OE1
GLN
A
886
3.995
10.271
17.188
1.00
41.20
A


ATOM
1668
NE2
GLN
A
886
5.016
11.728
18.557
1.00
38.67
A


ATOM
1669
C
GLN
A
886
9.546
9.963
19.863
1.00
20.53
A


ATOM
1670
O
GLN
A
886
10.483
10.365
19.168
1.00
17.99
A


ATOM
1671
N
LEU
A
887
9.495
10.153
21.178
1.00
18.09
A


ATOM
1672
CA
LEU
A
887
10.568
10.849
21.880
1.00
17.27
A


ATOM
1673
CB
LEU
A
887
10.163
11.118
23.336
1.00
17.29
A


ATOM
1674
CG
LEU
A
887
8.846
11.886
23.520
1.00
19.30
A


ATOM
1675
CD1
LEU
A
887
8.660
12.252
24.997
1.00
16.99
A


ATOM
1676
CD2
LEU
A
887
8.850
13.137
22.661
1.00
16.70
A


ATOM
1677
C
LEU
A
887
11.835
9.999
21.825
1.00
16.42
A


ATOM
1678
O
LEU
A
887
12.927
10.507
21.574
1.00
18.79
A


ATOM
1679
N
HIS
A
888
11.678
8.700
22.048
1.00
15.31
A


ATOM
1680
CA
HIS
A
888
12.799
7.771
22.006
1.00
15.69
A


ATOM
1681
CB
HIS
A
888
12.316
6.343
22.279
1.00
13.45
A


ATOM
1682
CG
HIS
A
888
12.170
6.018
23.733
1.00
16.95
A


ATOM
1683
CD2
HIS
A
888
12.609
6.662
24.840
1.00
16.73
A


ATOM
1684
ND1
HIS
A
888
11.553
4.869
24.180
1.00
18.43
A


ATOM
1685
CE1
HIS
A
888
11.622
4.816
25.498
1.00
19.06
A


ATOM
1686
NE2
HIS
A
888
12.259
5.892
25.924
1.00
19.99
A


ATOM
1687
C
HIS
A
888
13.546
7.802
20.677
1.00
14.55
A


ATOM
1688
O
HIS
A
888
14.776
7.862
20.654
1.00
15.76
A


ATOM
1689
N
LEU
A
889
12.807
7.751
19.571
1.00
14.95
A


ATOM
1690
CA
LEU
A
889
13.426
7.763
18.247
1.00
15.66
A


ATOM
1691
CB
LEU
A
889
12.371
7.551
17.146
1.00
15.15
A


ATOM
1692
CG
LEU
A
889
12.885
7.571
15.693
1.00
16.45
A


ATOM
1693
CD1
LEU
A
889
13.998
6.548
15.523
1.00
14.91
A


ATOM
1694
CD2
LEU
A
889
11.751
7.283
14.712
1.00
15.91
A


ATOM
1695
C
LEU
A
889
14.171
9.069
18.000
1.00
16.20
A


ATOM
1696
O
LEU
A
889
15.296
9.061
17.498
1.00
15.72
A


ATOM
1697
N
TYR
A
890
13.544
10.189
18.353
1.00
15.89
A


ATOM
1698
CA
TYR
A
890
14.167
11.497
18.165
1.00
15.42
A


ATOM
1699
CB
TYR
A
890
13.181
12.612
18.545
1.00
16.23
A


ATOM
1700
CG
TYR
A
890
13.720
14.017
18.336
1.00
19.79
A


ATOM
1701
CD1
TYR
A
890
14.631
14.580
19.232
1.00
17.47
A


ATOM
1702
CE1
TYR
A
890
15.146
15.863
19.026
1.00
20.88
A


ATOM
1703
CD2
TYR
A
890
13.336
14.775
17.225
1.00
20.09
A


ATOM
1704
CE2
TYR
A
890
13.851
16.059
17.009
1.00
20.17
A


ATOM
1705
CZ
TYR
A
890
14.754
16.593
17.912
1.00
21.65
A


ATOM
1706
OH
TYR
A
890
15.283
17.846
17.694
1.00
22.11
A


ATOM
1707
C
TYR
A
890
15.432
11.604
19.022
1.00
14.92
A


ATOM
1708
O
TYR
A
890
16.451
12.143
18.584
1.00
15.02
A


ATOM
1709
N
CYS
A
891
15.355
11.092
20.246
1.00
13.56
A


ATOM
1710
CA
CYS
A
891
16.488
11.125
21.164
1.00
13.38
A


ATOM
1711
CB
CYS
A
891
16.060
10.621
22.549
1.00
15.61
A


ATOM
1712
SG
CYS
A
891
17.401
10.546
23.778
1.00
17.44
A


ATOM
1713
C
CYS
A
891
17.634
10.272
20.625
1.00
12.47
A


ATOM
1714
O
CYS
A
891
18.789
10.704
20.604
1.00
14.79
A


ATOM
1715
N
LEU
A
892
17.322
9.061
20.178
1.00
13.99
A


ATOM
1716
CA
LEU
A
892
18.366
8.190
19.646
1.00
13.42
A


ATOM
1717
CB
LEU
A
892
17.802
6.798
19.325
1.00
14.16
A


ATOM
1718
CG
LEU
A
892
18.817
5.779
18.779
1.00
16.50
A


ATOM
1719
CD1
LEU
A
892
19.976
5.645
19.750
1.00
17.30
A


ATOM
1720
CD2
LEU
A
892
18.146
4.430
18.564
1.00
15.85
A


ATOM
1721
C
LEU
A
892
19.035
8.786
18.408
1.00
13.65
A


ATOM
1722
O
LEU
A
892
20.259
8.745
18.286
1.00
14.68
A


ATOM
1723
N
ASN
A
893
18.244
9.331
17.486
1.00
13.74
A


ATOM
1724
CA
ASN
A
893
18.817
9.921
16.284
1.00
15.86
A


ATOM
1725
CB
ASN
A
893
17.726
10.436
15.337
1.00
18.00
A


ATOM
1726
CG
ASN
A
893
17.040
9.322
14.578
1.00
19.28
A


ATOM
1727
OD1
ASN
A
893
17.694
8.407
14.081
1.00
20.97
A


ATOM
1728
ND2
ASN
A
893
15.716
9.403
14.465
1.00
21.13
A


ATOM
1729
C
ASN
A
893
19.733
11.071
16.663
1.00
16.82
A


ATOM
1730
O
ASN
A
893
20.837
11.205
16.124
1.00
14.75
A


ATOM
1731
N
THR
A
894
19.273
11.898
17.600
1.00
14.78
A


ATOM
1732
CA
THR
A
894
20.061
13.037
18.046
1.00
16.39
A


ATOM
1733
CB
THR
A
894
19.258
13.912
19.033
1.00
18.69
A


ATOM
1734
OG1
THR
A
894
18.055
14.371
18.394
1.00
18.55
A


ATOM
1735
CG2
THR
A
894
20.091
15.113
19.484
1.00
18.34
A


ATOM
1736
C
THR
A
894
21.359
12.566
18.715
1.00
17.20
A


ATOM
1737
O
THR
A
894
22.425
13.153
18.501
1.00
15.61
A


ATOM
1738
N
PHE
A
895
21.269
11.501
19.509
1.00
14.74
A


ATOM
1739
CA
PHE
A
895
22.435
10.947
20.199
1.00
16.10
A


ATOM
1740
CB
PHE
A
895
22.004
9.768
21.080
1.00
18.24
A


ATOM
1741
CG
PHE
A
895
23.129
9.135
21.849
1.00
17.59
A


ATOM
1742
CD1
PHE
A
895
23.674
9.767
22.964
1.00
19.36
A


ATOM
1743
CD2
PHE
A
895
23.637
7.900
21.464
1.00
18.77
A


ATOM
1744
CE1
PHE
A
895
24.712
9.173
23.691
1.00
19.72
A


ATOM
1745
CE2
PHE
A
895
24.676
7.295
22.181
1.00
20.89
A


ATOM
1746
CZ
PHE
A
895
25.214
7.933
23.298
1.00
19.53
A


ATOM
1747
C
PHE
A
895
23.470
10.472
19.170
1.00
17.01
A


ATOM
1748
O
PHE
A
895
24.665
10.740
19.300
1.00
16.55
A


ATOM
1749
N
ILE
A
896
22.993
9.754
18.157
1.00
16.61
A


ATOM
1750
CA
ILE
A
896
23.843
9.243
17.084
1.00
18.06
A


ATOM
1751
CB
ILE
A
896
22.997
8.447
16.052
1.00
18.72
A


ATOM
1752
CG2
ILE
A
896
23.783
8.231
14.758
1.00
20.23
A


ATOM
1753
CG1
ILE
A
896
22.575
7.106
16.649
1.00
18.11
A


ATOM
1754
CD1
ILE
A
896
21.537
6.382
15.811
1.00
19.50
A


ATOM
1755
C
ILE
A
896
24.542
10.394
16.360
1.00
18.68
A


ATOM
1756
O
ILE
A
896
25.724
10.310
16.029
1.00
19.12
A


ATOM
1757
N
GLN
A
897
23.807
11.477
16.132
1.00
17.29
A


ATOM
1758
CA
GLN
A
897
24.349
12.637
15.427
1.00
19.03
A


ATOM
1759
CB
GLN
A
897
23.305
13.146
14.427
1.00
19.67
A


ATOM
1760
CG
GLN
A
897
22.667
12.039
13.596
1.00
21.81
A


ATOM
1761
CD
GLN
A
897
21.462
12.510
12.804
1.00
22.65
A


ATOM
1762
OE1
GLN
A
897
20.568
11.720
12.483
1.00
23.76
A


ATOM
1763
NE2
GLN
A
897
21.434
13.793
12.476
1.00
21.56
A


ATOM
1764
C
GLN
A
897
24.743
13.780
16.366
1.00
18.17
A


ATOM
1765
O
GLN
A
897
24.892
14.922
15.925
1.00
17.24
A


ATOM
1766
N
SER
A
898
24.927
13.475
17.646
1.00
19.29
A


ATOM
1767
CA
SER
A
898
25.256
14.498
18.641
1.00
19.48
A


ATOM
1768
CB
SER
A
898
25.482
13.857
20.016
1.00
19.59
A


ATOM
1769
OG
SER
A
898
26.612
13.015
20.014
1.00
23.61
A


ATOM
1770
C
SER
A
898
26.431
15.428
18.321
1.00
20.34
A


ATOM
1771
O
SER
A
898
26.339
16.629
18.563
1.00
19.85
A


ATOM
1772
N
ARG
A
899
27.528
14.892
17.790
1.00
20.10
A


ATOM
1773
CA
ARG
A
899
28.679
15.736
17.468
1.00
23.31
A


ATOM
1774
CB
ARG
A
899
29.880
14.876
17.052
1.00
27.16
A


ATOM
1775
CG
ARG
A
899
30.420
13.995
18.169
1.00
33.57
A


ATOM
1776
CD
ARG
A
899
31.727
13.320
17.775
1.00
39.72
A


ATOM
1777
NE
ARG
A
899
32.308
12.568
18.885
1.00
45.23
A


ATOM
1778
CZ
ARG
A
899
33.516
12.013
18.862
1.00
48.88
A


ATOM
1779
NH1
ARG
A
899
33.963
11.345
19.919
1.00
50.43
A


ATOM
1780
NH2
ARG
A
899
34.282
12.126
17.784
1.00
49.70
A


ATOM
1781
C
ARG
A
899
28.359
16.743
16.363
1.00
24.46
A


ATOM
1782
O
ARG
A
899
28.630
17.938
16.497
1.00
23.89
A


ATOM
1783
N
ALA
A
900
27.781
16.254
15.271
1.00
23.66
A


ATOM
1784
CA
ALA
A
900
27.424
17.113
14.150
1.00
25.41
A


ATOM
1785
CB
ALA
A
900
26.821
16.276
13.022
1.00
24.80
A


ATOM
1786
C
ALA
A
900
26.436
18.198
14.576
1.00
25.89
A


ATOM
1787
O
ALA
A
900
26.536
19.341
14.141
1.00
24.07
A


ATOM
1788
N
LEU
A
901
25.496
17.836
15.446
1.00
24.94
A


ATOM
1789
CA
LEU
A
901
24.471
18.765
15.908
1.00
25.72
A


ATOM
1790
CB
LEU
A
901
23.180
17.993
16.198
1.00
26.87
A


ATOM
1791
CG
LEU
A
901
22.684
17.065
15.088
1.00
26.25
A


ATOM
1792
CD1
LEU
A
901
21.458
16.312
15.569
1.00
26.78
A


ATOM
1793
CD2
LEU
A
901
22.361
17.869
13.841
1.00
28.03
A


ATOM
1794
C
LEU
A
901
24.852
19.587
17.139
1.00
26.55
A


ATOM
1795
O
LEU
A
901
24.058
20.402
17.610
1.00
25.12
A


ATOM
1796
N
SER
A
902
26.058
19.374
17.660
1.00
25.57
A


ATOM
1797
CA
SER
A
902
26.526
20.094
18.846
1.00
25.20
A


ATOM
1798
CB
SER
A
902
26.683
21.589
18.549
1.00
26.76
A


ATOM
1799
OG
SER
A
902
27.664
21.806
17.552
1.00
32.11
A


ATOM
1800
C
SER
A
902
25.595
19.922
20.042
1.00
24.98
A


ATOM
1801
O
SER
A
902
25.303
20.874
20.768
1.00
22.85
A


ATOM
1802
N
VAL
A
903
25.121
18.702
20.247
1.00
23.89
A


ATOM
1803
CA
VAL
A
903
24.244
18.430
21.375
1.00
22.49
A


ATOM
1804
CB
VAL
A
903
22.960
17.712
20.917
1.00
21.00
A


ATOM
1805
CG1
VAL
A
903
22.100
17.373
22.115
1.00
20.35
A


ATOM
1806
CG2
VAL
A
903
22.190
18.601
19.942
1.00
21.63
A


ATOM
1807
C
VAL
A
903
25.004
17.551
22.357
1.00
22.22
A


ATOM
1808
O
VAL
A
903
25.462
16.468
22.004
1.00
22.99
A


ATOM
1809
N
GLU
A
904
25.149
18.023
23.588
1.00
22.49
A


ATOM
1810
CA
GLU
A
904
25.863
17.261
24.605
1.00
22.99
A


ATOM
1811
CB
GLU
A
904
26.494
18.201
25.636
1.00
26.54
A


ATOM
1812
CG
GLU
A
904
27.496
19.191
25.070
1.00
32.93
A


ATOM
1813
CD
GLU
A
904
27.985
20.166
26.123
1.00
35.69
A


ATOM
1814
OE1
GLU
A
904
28.416
19.703
27.203
1.00
38.41
A


ATOM
1815
OE2
GLU
A
904
27.939
21.390
25.872
1.00
36.80
A


ATOM
1816
C
GLU
A
904
24.947
16.294
25.344
1.00
22.46
A


ATOM
1817
O
GLU
A
904
23.801
16.624
25.660
1.00
21.31
A


ATOM
1818
N
PHE
A
905
25.467
15.102
25.621
1.00
19.52
A


ATOM
1819
CA
PHE
A
905
24.736
14.088
26.370
1.00
20.13
A


ATOM
1820
CB
PHE
A
905
24.483
12.833
25.521
1.00
17.67
A


ATOM
1821
CG
PHE
A
905
23.378
12.993
24.517
1.00
20.01
A


ATOM
1822
CD1
PHE
A
905
23.611
13.625
23.299
1.00
18.40
A


ATOM
1823
CD2
PHE
A
905
22.095
12.519
24.795
1.00
16.55
A


ATOM
1824
CE1
PHE
A
905
22.589
13.785
22.373
1.00
18.70
A


ATOM
1825
CE2
PHE
A
905
21.066
12.675
23.877
1.00
18.48
A


ATOM
1826
CZ
PHE
A
905
21.311
13.309
22.660
1.00
18.42
A


ATOM
1827
C
PHE
A
905
25.604
13.715
27.565
1.00
19.48
A


ATOM
1828
O
PHE
A
905
26.663
13.115
27.395
1.00
18.97
A


ATOM
1829
N
PRO
A
906
25.179
14.083
28.786
1.00
19.52
A


ATOM
1830
CD
PRO
A
906
24.084
15.010
29.128
1.00
20.38
A


ATOM
1831
CA
PRO
A
906
25.963
13.756
29.981
1.00
19.87
A


ATOM
1832
CB
PRO
A
906
25.157
14.397
31.108
1.00
19.03
A


ATOM
1833
CG
PRO
A
906
24.561
15.594
30.442
1.00
20.40
A


ATOM
1834
C
PRO
A
906
26.147
12.252
30.170
1.00
20.93
A


ATOM
1835
O
PRO
A
906
25.532
11.448
29.471
1.00
19.74
A


ATOM
1836
N
GLU
A
907
26.982
11.892
31.138
1.00
22.35
A


ATOM
1837
CA
GLU
A
907
27.317
10.504
31.435
1.00
23.45
A


ATOM
1838
CB
GLU
A
907
28.243
10.457
32.656
1.00
28.12
A


ATOM
1839
CG
GLU
A
907
29.018
9.154
32.788
1.00
34.86
A


ATOM
1840
CD
GLU
A
907
29.942
9.140
33.993
1.00
38.06
A


ATOM
1841
OE1
GLU
A
907
30.637
10.154
34.220
1.00
41.07
A


ATOM
1842
OE2
GLU
A
907
29.978
8.114
34.706
1.00
38.81
A


ATOM
1843
C
GLU
A
907
26.166
9.517
31.646
1.00
21.79
A


ATOM
1844
O
GLU
A
907
26.042
8.543
30.908
1.00
21.49
A


ATOM
1845
N
MET
A
908
25.344
9.742
32.665
1.00
22.08
A


ATOM
1846
CA
MET
A
908
24.241
8.822
32.937
1.00
23.28
A


ATOM
1847
CB
MET
A
908
23.538
9.193
34.245
1.00
27.12
A


ATOM
1848
CG
MET
A
908
24.346
8.860
35.489
1.00
34.62
A


ATOM
1849
SD
MET
A
908
23.440
9.197
37.025
1.00
43.74
A


ATOM
1850
CE
MET
A
908
22.199
7.897
36.981
1.00
38.86
A


ATOM
1851
C
MET
A
908
23.230
8.757
31.799
1.00
20.83
A


ATOM
1852
O
MET
A
908
22.700
7.686
31.504
1.00
20.86
A


ATOM
1853
N
MET
A
909
22.967
9.898
31.166
1.00
18.93
A


ATOM
1854
CA
MET
A
909
22.036
9.958
30.041
1.00
19.79
A


ATOM
1855
CB
MET
A
909
21.883
11.402
29.542
1.00
21.27
A


ATOM
1856
CG
MET
A
909
20.947
12.269
30.359
1.00
20.34
A


ATOM
1857
SD
MET
A
909
19.199
11.802
30.150
1.00
26.91
A


ATOM
1858
CE
MET
A
909
18.993
12.166
28.374
1.00
23.59
A


ATOM
1859
C
MET
A
909
22.576
9.087
28.910
1.00
19.04
A


ATOM
1860
O
MET
A
909
21.854
8.282
28.330
1.00
19.89
A


ATOM
1861
N
SER
A
910
23.858
9.251
28.604
1.00
18.89
A


ATOM
1862
CA
SER
A
910
24.484
8.469
27.546
1.00
20.47
A


ATOM
1863
CB
SER
A
910
25.938
8.908
27.364
1.00
20.19
A


ATOM
1864
OG
SER
A
910
25.998
10.249
26.900
1.00
20.62
A


ATOM
1865
C
SER
A
910
24.427
6.976
27.869
1.00
21.20
A


ATOM
1866
O
SER
A
910
24.210
6.153
26.982
1.00
19.29
A


ATOM
1867
N
GLU
A
911
24.610
6.638
29.142
1.00
22.27
A


ATOM
1868
CA
GLU
A
911
24.587
5.244
29.578
1.00
24.86
A


ATOM
1869
CB
GLU
A
911
24.965
5.149
31.060
1.00
29.31
A


ATOM
1870
CG
GLU
A
911
24.950
3.736
31.626
1.00
35.80
A


ATOM
1871
CD
GLU
A
911
25.165
3.700
33.136
1.00
40.80
A


ATOM
1872
OE1
GLU
A
911
26.207
4.204
33.609
1.00
45.47
A


ATOM
1873
OE2
GLU
A
911
24.290
3.166
33.854
1.00
43.61
A


ATOM
1874
C
GLU
A
911
23.231
4.574
29.347
1.00
23.81
A


ATOM
1875
O
GLU
A
911
23.164
3.493
28.756
1.00
22.59
A


ATOM
1876
N
VAL
A
912
22.151
5.202
29.807
1.00
20.88
A


ATOM
1877
CA
VAL
A
912
20.827
4.613
29.623
1.00
22.23
A


ATOM
1878
CB
VAL
A
912
19.718
5.404
30.374
1.00
22.28
A


ATOM
1879
CG1
VAL
A
912
20.025
5.441
31.868
1.00
23.61
A


ATOM
1880
CG2
VAL
A
912
19.602
6.807
29.819
1.00
23.21
A


ATOM
1881
C
VAL
A
912
20.454
4.535
28.149
1.00
20.96
A


ATOM
1882
O
VAL
A
912
19.876
3.546
27.699
1.00
21.47
A


ATOM
1883
N
ILE
A
913
20.794
5.571
27.392
1.00
20.47
A


ATOM
1884
CA
ILE
A
913
20.477
5.589
25.969
1.00
21.45
A


ATOM
1885
CB
ILE
A
913
20.875
6.949
25.330
1.00
21.91
A


ATOM
1886
CG2
ILE
A
913
20.829
6.862
23.810
1.00
21.47
A


ATOM
1887
CG1
ILE
A
913
19.926
8.042
25.830
1.00
19.94
A


ATOM
1888
CD1
ILE
A
913
20.320
9.446
25.420
1.00
23.22
A


ATOM
1889
C
ILE
A
913
21.188
4.448
25.249
1.00
22.68
A


ATOM
1890
O
ILE
A
913
20.570
3.694
24.503
1.00
23.60
A


ATOM
1891
N
ALA
A
914
22.486
4.313
25.492
1.00
23.11
A


ATOM
1892
CA
ALA
A
914
23.276
3.270
24.857
1.00
24.55
A


ATOM
1893
CB
ALA
A
914
24.757
3.453
25.203
1.00
24.17
A


ATOM
1894
C
ALA
A
914
22.823
1.878
25.268
1.00
24.85
A


ATOM
1895
O
ALA
A
914
22.738
0.973
24.441
1.00
24.84
A


ATOM
1896
N
ALA
A
915
22.532
1.715
26.551
1.00
26.25
A


ATOM
1897
CA
ALA
A
915
22.119
0.425
27.077
1.00
27.16
A


ATOM
1898
CB
ALA
A
915
22.155
0.460
28.602
1.00
26.43
A


ATOM
1899
C
ALA
A
915
20.759
−0.093
26.616
1.00
27.28
A


ATOM
1900
O
ALA
A
915
20.627
−1.277
26.315
1.00
28.47
A


ATOM
1901
N
GLN
A
916
19.754
0.773
26.526
1.00
24.56
A


ATOM
1902
CA
GLN
A
916
18.429
0.272
26.178
1.00
23.88
A


ATOM
1903
CB
GLN
A
916
17.529
0.337
27.418
1.00
23.68
A


ATOM
1904
CG
GLN
A
916
18.134
−0.202
28.704
1.00
25.94
A


ATOM
1905
CD
GLN
A
916
18.337
−1.704
28.688
1.00
28.66
A


ATOM
1906
OE1
GLN
A
916
17.808
−2.408
27.828
1.00
29.30
A


ATOM
1907
NE2
GLN
A
916
19.101
−2.206
29.654
1.00
29.87
A


ATOM
1908
C
GLN
A
916
17.622
0.830
25.011
1.00
21.93
A


ATOM
1909
O
GLN
A
916
16.766
0.119
24.496
1.00
20.48
A


ATOM
1910
N
LEU
A
917
17.856
2.073
24.588
1.00
21.01
A


ATOM
1911
CA
LEU
A
917
17.030
2.639
23.518
1.00
21.54
A


ATOM
1912
CB
LEU
A
917
17.484
4.062
23.150
1.00
24.24
A


ATOM
1913
CG
LEU
A
917
16.864
5.165
24.010
1.00
27.14
A


ATOM
1914
CD1
LEU
A
917
17.113
6.536
23.371
1.00
25.74
A


ATOM
1915
CD2
LEU
A
917
15.367
4.913
24.147
1.00
27.44
A


ATOM
1916
C
LEU
A
917
16.846
1.826
22.243
1.00
21.71
A


ATOM
1917
O
LEU
A
917
15.717
1.662
21.771
1.00
22.26
A


ATOM
1918
N
PRO
A
918
17.939
1.315
21.656
1.00
20.55
A


ATOM
1919
CD
PRO
A
918
19.368
1.494
21.970
1.00
21.89
A


ATOM
1920
CA
PRO
A
918
17.764
0.530
20.429
1.00
20.41
A


ATOM
1921
CB
PRO
A
918
19.190
0.106
20.082
1.00
21.03
A


ATOM
1922
CG
PRO
A
918
20.017
1.247
20.622
1.00
21.48
A


ATOM
1923
C
PRO
A
918
16.851
−0.670
20.683
1.00
19.91
A


ATOM
1924
O
PRO
A
918
15.918
−0.932
19.924
1.00
18.25
A


ATOM
1925
N
LYS
A
919
17.132
−1.386
21.766
1.00
19.57
A


ATOM
1926
CA
LYS
A
919
16.356
−2.561
22.154
1.00
19.46
A


ATOM
1927
CB
LYS
A
919
16.944
−3.152
23.436
1.00
22.54
A


ATOM
1928
CG
LYS
A
919
16.263
−4.419
23.930
1.00
27.11
A


ATOM
1929
CD
LYS
A
919
16.667
−4.723
25.374
1.00
28.80
A


ATOM
1930
CE
LYS
A
919
18.180
−4.789
25.536
1.00
29.86
A


ATOM
1931
NZ
LYS
A
919
18.598
−4.886
26.971
1.00
33.98
A


ATOM
1932
C
LYS
A
919
14.882
−2.213
22.375
1.00
20.15
A


ATOM
1933
O
LYS
A
919
13.986
−2.941
21.944
1.00
19.14
A


ATOM
1934
N
ILE
A
920
14.631
−1.099
23.057
1.00
20.31
A


ATOM
1935
CA
ILE
A
920
13.262
−0.669
23.321
1.00
18.33
A


ATOM
1936
CB
ILE
A
920
13.242
0.552
24.267
1.00
20.86
A


ATOM
1937
CG2
ILE
A
920
11.820
1.098
24.402
1.00
22.14
A


ATOM
1938
CG1
ILE
A
920
13.781
0.138
25.640
1.00
18.33
A


ATOM
1939
CD1
ILE
A
920
13.903
1.284
26.619
1.00
23.66
A


ATOM
1940
C
ILE
A
920
12.540
−0.328
22.025
1.00
19.54
A


ATOM
1941
O
ILE
A
920
11.424
−0.788
21.788
1.00
19.13
A


ATOM
1942
N
LEU
A
921
13.180
0.472
21.179
1.00
20.13
A


ATOM
1943
CA
LEU
A
921
12.585
0.851
19.904
1.00
20.63
A


ATOM
1944
CB
LEU
A
921
13.503
1.829
19.167
1.00
21.68
A


ATOM
1945
CG
LEU
A
921
13.416
3.266
19.680
1.00
22.69
A


ATOM
1946
CD1
LEU
A
921
14.462
4.139
18.995
1.00
21.07
A


ATOM
1947
CD2
LEU
A
921
12.005
3.796
19.409
1.00
20.56
A


ATOM
1948
C
LEU
A
921
12.304
−0.362
19.022
1.00
21.94
A


ATOM
1949
O
LEU
A
921
11.324
−0.386
18.280
1.00
24.08
A


ATOM
1950
N
ALA
A
922
13.162
−1.372
19.107
1.00
20.43
A


ATOM
1951
CA
ALA
A
922
12.989
−2.578
18.305
1.00
21.49
A


ATOM
1952
CB
ALA
A
922
14.294
−3.354
18.243
1.00
20.05
A


ATOM
1953
C
ALA
A
922
11.889
−3.466
18.866
1.00
22.02
A


ATOM
1954
O
ALA
A
922
11.546
−4.489
18.274
1.00
21.77
A


ATOM
1955
N
GLY
A
923
11.342
−3.075
20.012
1.00
21.48
A


ATOM
1956
CA
GLY
A
923
10.286
−3.860
20.629
1.00
21.95
A


ATOM
1957
C
GLY
A
923
10.794
−5.142
21.266
1.00
21.42
A


ATOM
1958
O
GLY
A
923
10.031
−6.092
21.456
1.00
22.31
A


ATOM
1959
N
MET
A
924
12.080
−5.179
21.601
1.00
19.45
A


ATOM
1960
CA
MET
A
924
12.658
−6.364
22.215
1.00
20.79
A


ATOM
1961
CB
MET
A
924
14.091
−6.580
21.722
1.00
22.02
A


ATOM
1962
CG
MET
A
924
14.178
−6.895
20.238
1.00
25.40
A


ATOM
1963
SD
MET
A
924
13.141
−8.295
19.764
1.00
28.65
A


ATOM
1964
CE
MET
A
924
14.164
−9.661
20.270
1.00
27.15
A


ATOM
1965
C
MET
A
924
12.631
−6.293
23.737
1.00
20.36
A


ATOM
1966
O
MET
A
924
13.603
−6.635
24.404
1.00
20.04
A


ATOM
1967
N
VAL
A
925
11.499
−5.829
24.259
1.00
20.45
A


ATOM
1968
CA
VAL
A
925
11.235
−5.718
25.689
1.00
19.83
A


ATOM
1969
CB
VAL
A
925
11.571
−4.319
26.262
1.00
19.54
A


ATOM
1970
CG1
VAL
A
925
13.067
−4.040
26.133
1.00
18.25
A


ATOM
1971
CG2
VAL
A
925
10.745
−3.252
25.555
1.00
17.24
A


ATOM
1972
C
VAL
A
925
9.730
−5.924
25.773
1.00
20.81
A


ATOM
1973
O
VAL
A
925
9.053
−5.958
24.739
1.00
17.16
A


ATOM
1974
N
LYS
A
926
9.206
−6.052
26.986
1.00
20.03
A


ATOM
1975
CA
LYS
A
926
7.776
−6.271
27.157
1.00
22.62
A


ATOM
1976
CB
LYS
A
926
7.532
−7.544
27.977
1.00
24.15
A


ATOM
1977
CG
LYS
A
926
6.062
−7.903
28.123
1.00
27.68
A


ATOM
1978
CD
LYS
A
926
5.884
−9.233
28.839
1.00
32.47
A


ATOM
1979
CE
LYS
A
926
4.412
−9.611
28.927
1.00
33.32
A


ATOM
1980
NZ
LYS
A
926
4.224
−10.923
29.603
1.00
35.99
A


ATOM
1981
C
LYS
A
926
7.037
−5.103
27.803
1.00
22.57
A


ATOM
1982
O
LYS
A
926
7.076
−4.921
29.026
1.00
22.63
A


ATOM
1983
N
PRO
A
927
6.367
−4.280
26.986
1.00
23.30
A


ATOM
1984
CD
PRO
A
927
6.374
−4.224
25.516
1.00
23.83
A


ATOM
1985
CA
PRO
A
927
5.629
−3.149
27.551
1.00
23.76
A


ATOM
1986
CB
PRO
A
927
5.220
−2.339
26.316
1.00
24.30
A


ATOM
1987
CG
PRO
A
927
6.229
−2.751
25.265
1.00
25.51
A


ATOM
1988
C
PRO
A
927
4.417
−3.750
28.253
1.00
24.23
A


ATOM
1989
O
PRO
A
927
3.801
−4.686
27.740
1.00
22.94
A


ATOM
1990
N
LEU
A
928
4.081
−3.241
29.427
1.00
22.92
A


ATOM
1991
CA
LEU
A
928
2.930
−3.773
30.132
1.00
24.28
A


ATOM
1992
CB
LEU
A
928
3.200
−3.825
31.640
1.00
22.59
A


ATOM
1993
CG
LEU
A
928
4.419
−4.655
32.060
1.00
24.35
A


ATOM
1994
CD1
LEU
A
928
4.460
−4.776
33.579
1.00
23.99
A


ATOM
1995
CD2
LEU
A
928
4.350
−6.038
31.426
1.00
26.06
A


ATOM
1996
C
LEU
A
928
1.726
−2.896
29.824
1.00
25.03
A


ATOM
1997
O
LEU
A
928
1.826
−1.666
29.812
1.00
27.49
A


ATOM
1998
N
LEU
A
929
0.596
−3.533
29.549
1.00
24.29
A


ATOM
1999
CA
LEU
A
929
−0.627
−2.809
29.234
1.00
24.19
A


ATOM
2000
CB
LEU
A
929
−1.107
−3.163
27.825
1.00
25.39
A


ATOM
2001
CG
LEU
A
929
−0.272
−2.680
26.640
1.00
23.43
A


ATOM
2002
CD1
LEU
A
929
−0.739
−3.371
25.363
1.00
23.68
A


ATOM
2003
CD2
LEU
A
929
−0.397
−1.166
26.520
1.00
23.94
A


ATOM
2004
C
LEU
A
929
−1.722
−3.150
30.226
1.00
25.66
A


ATOM
2005
O
LEU
A
929
−1.820
−4.286
30.699
1.00
23.46
A


ATOM
2006
N
PHE
A
930
−2.541
−2.152
30.535
1.00
26.75
A


ATOM
2007
CA
PHE
A
930
−3.657
−2.315
31.451
1.00
28.37
A


ATOM
2008
CB
PHE
A
930
−3.949
−0.987
32.151
1.00
25.94
A


ATOM
2009
CG
PHE
A
930
−2.857
−0.545
33.093
1.00
24.34
A


ATOM
2010
CD1
PHE
A
930
−2.662
−1.198
34.306
1.00
24.73
A


ATOM
2011
CD2
PHE
A
930
−2.015
0.511
32.758
1.00
22.44
A


ATOM
2012
CE1
PHE
A
930
−1.641
−0.802
35.175
1.00
24.82
A


ATOM
2013
CE2
PHE
A
930
−0.994
0.914
33.617
1.00
23.39
A


ATOM
2014
CZ
PHE
A
930
−0.805
0.256
34.828
1.00
23.89
A


ATOM
2015
C
PHE
A
930
−4.880
−2.776
30.660
1.00
30.68
A


ATOM
2016
O
PHE
A
930
−5.794
−3.391
31.215
1.00
29.02
A


ATOM
2017
N
HIS
A
931
−4.881
−2.476
29.362
1.00
33.18
A


ATOM
2018
CA
HIS
A
931
−5.976
−2.856
28.475
1.00
38.68
A


ATOM
2019
CB
HIS
A
931
−6.909
−1.666
28.238
1.00
39.02
A


ATOM
2020
CG
HIS
A
931
−7.356
−0.994
29.497
1.00
40.32
A


ATOM
2021
CD2
HIS
A
931
−7.249
0.292
29.906
1.00
40.17
A


ATOM
2022
ND1
HIS
A
931
−7.976
−1.674
30.523
1.00
40.39
A


ATOM
2023
CE1
HIS
A
931
−8.229
−0.836
31.513
1.00
40.76
A


ATOM
2024
NE2
HIS
A
931
−7.798
0.363
31.164
1.00
41.79
A


ATOM
2025
C
HIS
A
931
−5.439
−3.341
27.134
1.00
41.55
A


ATOM
2026
O
HIS
A
931
−4.304
−3.045
26.762
1.00
41.94
A


ATOM
2027
N
LYS
A
932
−6.264
−4.087
26.409
1.00
45.37
A


ATOM
2028
CA
LYS
A
932
−5.871
−4.607
25.107
1.00
49.31
A


ATOM
2029
CB
LYS
A
932
−6.553
−5.953
24.850
1.00
51.25
A


ATOM
2030
CG
LYS
A
932
−8.041
−5.969
25.159
1.00
53.19
A


ATOM
2031
CD
LYS
A
932
−8.607
−7.375
25.030
1.00
55.91
A


ATOM
2032
CE
LYS
A
932
−10.000
−7.477
25.642
1.00
57.08
A


ATOM
2033
NZ
LYS
A
932
−10.971
−6.540
25.010
1.00
58.49
A


ATOM
2034
C
LYS
A
932
−6.219
−3.625
23.997
1.00
50.69
A


ATOM
2035
O
LYS
A
932
−6.726
−2.528
24.316
1.00
51.64
A


ATOM
2036
OXT
LYS
A
932
−5.971
−3.965
22.820
1.00
53.42
A


ATOM
2037
CB
GLN
B
682
18.994
−21.280
−25.886
1.00
64.64
B


ATOM
2038
CG
GLN
B
682
20.304
−21.103
−26.640
1.00
67.42
B


ATOM
2039
CD
GLN
B
682
20.213
−21.557
−28.085
1.00
69.58
B


ATOM
2040
OE1
GLN
B
682
19.707
−22.642
−28.379
1.00
70.69
B


ATOM
2041
NE2
GLN
B
682
20.711
−20.728
−28.997
1.00
70.72
B


ATOM
2042
C
GLN
B
682
17.739
−20.948
−23.741
1.00
60.54
B


ATOM
2043
O
GLN
B
682
16.624
−20.450
−23.891
1.00
61.01
B


ATOM
2044
N
GLN
B
682
20.194
−20.628
−23.821
1.00
62.94
B


ATOM
2045
CA
GLN
B
682
18.922
−20.478
−24.585
1.00
62.30
B


ATOM
2046
N
LEU
B
683
17.986
−21.915
−22.863
1.00
57.86
B


ATOM
2047
CA
LEU
B
683
16.949
−22.424
−21.976
1.00
54.52
B


ATOM
2048
CB
LEU
B
683
17.296
−23.831
−21.481
1.00
56.05
B


ATOM
2049
CG
LEU
B
683
17.347
−24.973
−22.497
1.00
56.91
B


ATOM
2050
CD1
LEU
B
683
17.763
−26.253
−21.789
1.00
57.17
B


ATOM
2051
CD2
LEU
B
683
15.988
−25.149
−23.158
1.00
57.28
B


ATOM
2052
C
LEU
B
683
16.906
−21.464
−20.797
1.00
51.41
B


ATOM
2053
O
LEU
B
683
15.849
−21.218
−20.214
1.00
51.78
B


ATOM
2054
N
ILE
B
684
18.074
−20.923
−20.458
1.00
46.89
B


ATOM
2055
CA
ILE
B
684
18.197
−19.974
−19.360
1.00
42.41
B


ATOM
2056
CB
ILE
B
684
19.665
−19.802
−18.918
1.00
42.31
B


ATOM
2057
CG2
ILE
B
684
19.742
−18.819
−17.754
1.00
41.95
B


ATOM
2058
CG1
ILE
B
684
20.259
−21.152
−18.516
1.00
43.99
B


ATOM
2059
CD1
ILE
B
684
19.612
−21.778
−17.297
1.00
44.53
B


ATOM
2060
C
ILE
B
684
17.685
−18.616
−19.825
1.00
38.54
B


ATOM
2061
O
ILE
B
684
18.255
−18.010
−20.729
1.00
36.91
B


ATOM
2062
N
PRO
B
685
16.598
−18.123
−19.213
1.00
35.60
B


ATOM
2063
CD
PRO
B
685
15.838
−18.725
−18.103
1.00
35.69
B


ATOM
2064
CA
PRO
B
685
16.032
−16.824
−19.587
1.00
33.16
B


ATOM
2065
CB
PRO
B
685
15.030
−16.555
−18.469
1.00
33.62
B


ATOM
2066
CG
PRO
B
685
14.553
−17.922
−18.121
1.00
34.50
B


ATOM
2067
C
PRO
B
685
17.134
−15.763
−19.652
1.00
30.56
B


ATOM
2068
O
PRO
B
685
18.029
−15.738
−18.808
1.00
29.11
B


ATOM
2069
N
PRO
B
686
17.081
−14.880
−20.658
1.00
28.12
B


ATOM
2070
CD
PRO
B
686
16.116
−14.858
−21.772
1.00
28.97
B


ATOM
2071
CA
PRO
B
686
18.083
−13.823
−20.822
1.00
27.69
B


ATOM
2072
CB
PRO
B
686
17.532
−13.010
−21.990
1.00
28.13
B


ATOM
2073
CG
PRO
B
686
16.862
−14.063
−22.820
1.00
29.95
B


ATOM
2074
C
PRO
B
686
18.321
−12.967
−19.575
1.00
25.10
B


ATOM
2075
O
PRO
B
686
19.464
−12.648
−19.247
1.00
25.19
B


ATOM
2076
N
LEU
B
687
17.252
−12.601
−18.878
1.00
22.87
B


ATOM
2077
CA
LEU
B
687
17.396
−11.771
−17.685
1.00
22.31
B


ATOM
2078
CB
LEU
B
687
16.025
−11.372
−17.141
1.00
20.28
B


ATOM
2079
CG
LEU
B
687
16.037
−10.547
−15.848
1.00
21.32
B


ATOM
2080
CD1
LEU
B
687
16.936
−9.323
−16.015
1.00
21.04
B


ATOM
2081
CD2
LEU
B
687
14.616
−10.132
−15.501
1.00
22.03
B


ATOM
2082
C
LEU
B
687
18.207
−12.467
−16.592
1.00
21.06
B


ATOM
2083
O
LEU
B
687
19.025
−11.840
−15.921
1.00
23.05
B


ATOM
2084
N
ILE
B
688
17.974
−13.760
−16.409
1.00
21.09
B


ATOM
2085
CA
ILE
B
688
18.702
−14.512
−15.399
1.00
20.07
B


ATOM
2086
CB
ILE
B
688
18.120
−15.927
−15.252
1.00
21.05
B


ATOM
2087
CG2
ILE
B
688
19.059
−16.808
−14.438
1.00
21.46
B


ATOM
2088
CG1
ILE
B
688
16.741
−15.831
−14.594
1.00
20.53
B


ATOM
2089
CD1
ILE
B
688
15.968
−17.135
−14.567
1.00
20.95
B


ATOM
2090
C
ILE
B
688
20.166
−14.572
−15.804
1.00
21.10
B


ATOM
2091
O
ILE
B
688
21.056
−14.491
−14.960
1.00
18.80
B


ATOM
2092
N
ASN
B
689
20.411
−14.696
−17.104
1.00
21.37
B


ATOM
2093
CA
ASN
B
689
21.776
−14.743
−17.613
1.00
24.08
B


ATOM
2094
CB
ASN
B
689
21.770
−14.963
−19.132
1.00
28.04
B


ATOM
2095
CG
ASN
B
689
23.165
−15.126
−19.700
1.00
34.12
B


ATOM
2096
OD1
ASN
B
689
23.885
−16.064
−19.350
1.00
37.11
B


ATOM
2097
ND2
ASN
B
689
23.560
−14.210
−20.582
1.00
37.70
B


ATOM
2098
C
ASN
B
689
22.451
−13.415
−17.288
1.00
22.87
B


ATOM
2099
O
ASN
B
689
23.612
−13.370
−16.873
1.00
23.07
B


ATOM
2100
N
LEU
B
690
21.712
−12.332
−17.482
1.00
22.51
B


ATOM
2101
CA
LEU
B
690
22.232
−11.000
−17.200
1.00
21.77
B


ATOM
2102
CB
LEU
B
690
21.199
−9.942
−17.587
1.00
21.00
B


ATOM
2103
CG
LEU
B
690
21.628
−8.481
−17.421
1.00
24.94
B


ATOM
2104
CD1
LEU
B
690
20.798
−7.601
−18.349
1.00
26.36
B


ATOM
2105
CD2
LEU
B
690
21.469
−8.047
−15.963
1.00
23.11
B


ATOM
2106
C
LEU
B
690
22.570
−10.893
−15.715
1.00
20.64
B


ATOM
2107
O
LEU
B
690
23.637
−10.395
−15.347
1.00
20.56
B


ATOM
2108
N
LEU
B
691
21.666
−11.376
−14.866
1.00
20.00
B


ATOM
2109
CA
LEU
B
691
21.882
−11.331
−13.421
1.00
18.30
B


ATOM
2110
CB
LEU
B
691
20.669
−11.906
−12.675
1.00
14.83
B


ATOM
2111
CG
LEU
B
691
19.385
−11.068
−12.715
1.00
16.41
B


ATOM
2112
CD1
LEU
B
691
18.292
−11.772
−11.925
1.00
14.23
B


ATOM
2113
CD2
LEU
B
691
19.648
−9.672
−12.136
1.00
16.13
B


ATOM
2114
C
LEU
B
691
23.145
−12.097
−13.029
1.00
18.65
B


ATOM
2115
O
LEU
B
691
23.826
−11.728
−12.079
1.00
17.99
B


ATOM
2116
N
MET
B
692
23.450
−13.167
−13.757
1.00
19.64
B


ATOM
2117
CA
MET
B
692
24.646
−13.956
−13.470
1.00
21.71
B


ATOM
2118
CB
MET
B
692
24.676
−15.237
−14.319
1.00
23.95
B


ATOM
2119
CG
MET
B
692
23.620
−16.280
−13.983
1.00
28.81
B


ATOM
2120
SD
MET
B
692
23.860
−17.830
−14.932
1.00
34.88
B


ATOM
2121
CE
MET
B
692
22.791
−17.547
−16.333
1.00
34.64
B


ATOM
2122
C
MET
B
692
25.887
−13.130
−13.793
1.00
20.55
B


ATOM
2123
O
MET
B
692
26.827
−13.062
−13.003
1.00
19.66
B


ATOM
2124
N
SER
B
693
25.872
−12.490
−14.959
1.00
20.66
B


ATOM
2125
CA
SER
B
693
27.003
−11.691
−15.417
1.00
22.33
B


ATOM
2126
CB
SER
B
693
26.811
−11.303
−16.888
1.00
24.97
B


ATOM
2127
OG
SER
B
693
25.751
−10.374
−17.040
1.00
29.96
B


ATOM
2128
C
SER
B
693
27.298
−10.430
−14.609
1.00
21.68
B


ATOM
2129
O
SER
B
693
28.428
−9.938
−14.623
1.00
21.77
B


ATOM
2130
N
ILE
B
694
26.305
−9.891
−13.912
1.00
20.69
B


ATOM
2131
CA
ILE
B
694
26.559
−8.674
−13.141
1.00
20.69
B


ATOM
2132
CB
ILE
B
694
25.397
−7.667
−13.264
1.00
19.13
B


ATOM
2133
CG2
ILE
B
694
25.199
−7.291
−14.732
1.00
19.95
B


ATOM
2134
CG1
ILE
B
694
24.115
−8.262
−12.685
1.00
18.02
B


ATOM
2135
CD1
ILE
B
694
22.973
−7.256
−12.567
1.00
16.95
B


ATOM
2136
C
ILE
B
694
26.833
−8.939
−11.667
1.00
20.67
B


ATOM
2137
O
ILE
B
694
27.035
−8.009
−10.888
1.00
20.17
B


ATOM
2138
N
GLU
B
695
26.840
−10.212
−11.288
1.00
21.75
B


ATOM
2139
CA
GLU
B
695
27.104
−10.583
−9.908
1.00
24.75
B


ATOM
2140
CB
GLU
B
695
27.027
−12.100
−9.745
1.00
24.51
B


ATOM
2141
CG
GLU
B
695
27.077
−12.547
−8.310
1.00
28.80
B


ATOM
2142
CD
GLU
B
695
25.739
−12.415
−7.615
1.00
28.02
B


ATOM
2143
OE1
GLU
B
695
24.997
−11.445
−7.898
1.00
25.16
B


ATOM
2144
OE2
GLU
B
695
25.436
−13.288
−6.776
1.00
29.89
B


ATOM
2145
C
GLU
B
695
28.502
−10.086
−9.541
1.00
26.27
B


ATOM
2146
O
GLU
B
695
29.416
−10.100
−10.368
1.00
25.29
B


ATOM
2147
N
PRO
B
696
28.681
−9.625
−8.296
1.00
29.47
B


ATOM
2148
CD
PRO
B
696
27.624
−9.400
−7.293
1.00
31.49
B


ATOM
2149
CA
PRO
B
696
29.968
−9.116
−7.812
1.00
30.81
B


ATOM
2150
CB
PRO
B
696
29.662
−8.727
−6.366
1.00
30.96
B


ATOM
2151
CG
PRO
B
696
28.228
−8.311
−6.433
1.00
32.91
B


ATOM
2152
C
PRO
B
696
31.122
−10.113
−7.891
1.00
30.70
B


ATOM
2153
O
PRO
B
696
30.926
−11.327
−7.848
1.00
29.38
B


ATOM
2154
N
ASP
B
697
32.331
−9.578
−8.005
1.00
31.64
B


ATOM
2155
CA
ASP
B
697
33.531
−10.396
−8.051
1.00
32.72
B


ATOM
2156
CB
ASP
B
697
34.676
−9.592
−8.668
1.00
37.63
B


ATOM
2157
CG
ASP
B
697
35.443
−10.374
−9.710
1.00
41.79
B


ATOM
2158
OD1
ASP
B
697
34.805
−10.892
−10.655
1.00
43.16
B


ATOM
2159
OD2
ASP
B
697
36.684
−10.464
−9.585
1.00
44.61
B


ATOM
2160
C
ASP
B
697
33.833
−10.722
−6.587
1.00
29.84
B


ATOM
2161
O
ASP
B
697
33.262
−10.101
−5.693
1.00
28.09
B


ATOM
2162
N
VAL
B
698
34.706
−11.694
−6.344
1.00
28.32
B


ATOM
2163
CA
VAL
B
698
35.069
−12.083
−4.981
1.00
27.02
B


ATOM
2164
CB
VAL
B
698
36.205
−13.140
−4.974
1.00
28.37
B


ATOM
2165
CG1
VAL
B
698
36.747
−13.323
−3.560
1.00
28.43
B


ATOM
2166
CG2
VAL
B
698
35.682
−14.470
−5.502
1.00
28.67
B


ATOM
2167
C
VAL
B
698
35.532
−10.881
−4.168
1.00
25.36
B


ATOM
2168
O
VAL
B
698
36.328
−10.076
−4.639
1.00
25.06
B


ATOM
2169
N
ILE
B
699
35.030
−10.767
−2.944
1.00
24.97
B


ATOM
2170
CA
ILE
B
699
35.397
−9.658
−2.071
1.00
22.14
B


ATOM
2171
CB
ILE
B
699
34.156
−8.823
−1.679
1.00
20.66
B


ATOM
2172
CG2
ILE
B
699
34.545
−7.726
−0.690
1.00
20.23
B


ATOM
2173
CG1
ILE
B
699
33.545
−8.188
−2.931
1.00
21.51
B


ATOM
2174
CD1
ILE
B
699
32.271
−7.432
−2.666
1.00
19.96
B


ATOM
2175
C
ILE
B
699
36.089
−10.142
−0.800
1.00
21.77
B


ATOM
2176
O
ILE
B
699
35.546
−10.957
−0.044
1.00
16.92
B


ATOM
2177
N
TYR
B
700
37.296
−9.636
−0.579
1.00
20.63
B


ATOM
2178
CA
TYR
B
700
38.069
−9.988
0.602
1.00
23.86
B


ATOM
2179
CB
TYR
B
700
39.566
−10.003
0.285
1.00
26.68
B


ATOM
2180
CG
TYR
B
700
39.969
−11.095
−0.676
1.00
32.41
B


ATOM
2181
CD1
TYR
B
700
39.640
−11.018
−2.027
1.00
34.57
B


ATOM
2182
CE1
TYR
B
700
39.979
−12.036
−2.909
1.00
38.16
B


ATOM
2183
CD2
TYR
B
700
40.651
−12.224
−0.228
1.00
33.94
B


ATOM
2184
CE2
TYR
B
700
40.993
−13.251
−1.104
1.00
37.69
B


ATOM
2185
CZ
TYR
B
700
40.652
−13.149
−2.442
1.00
38.33
B


ATOM
2186
OH
TYR
B
700
40.974
−14.165
−3.315
1.00
43.13
B


ATOM
2187
C
TYR
B
700
37.798
−8.979
1.706
1.00
23.63
B


ATOM
2188
O
TYR
B
700
37.501
−7.816
1.439
1.00
24.64
B


ATOM
2189
N
ALA
B
701
37.892
−9.427
2.949
1.00
23.12
B


ATOM
2190
CA
ALA
B
701
37.664
−8.541
4.080
1.00
23.90
B


ATOM
2191
CB
ALA
B
701
37.177
−9.345
5.276
1.00
21.97
B


ATOM
2192
C
ALA
B
701
38.947
−7.795
4.439
1.00
25.27
B


ATOM
2193
O
ALA
B
701
38.907
−6.764
5.117
1.00
23.66
B


ATOM
2194
N
GLY
B
702
40.078
−8.316
3.971
1.00
26.40
B


ATOM
2195
CA
GLY
B
702
41.361
−7.706
4.282
1.00
30.27
B


ATOM
2196
C
GLY
B
702
41.693
−7.977
5.740
1.00
33.57
B


ATOM
2197
O
GLY
B
702
42.346
−7.170
6.410
1.00
32.31
B


ATOM
2198
N
HIS
B
703
41.238
−9.130
6.229
1.00
35.31
B


ATOM
2199
CA
HIS
B
703
41.441
−9.529
7.616
1.00
39.69
B


ATOM
2200
CB
HIS
B
703
40.355
−10.529
8.021
1.00
39.47
B


ATOM
2201
CG
HIS
B
703
40.516
−11.070
9.406
1.00
40.61
B


ATOM
2202
CD2
HIS
B
703
39.934
−10.715
10.575
1.00
41.64
B


ATOM
2203
ND1
HIS
B
703
41.390
−12.092
9.707
1.00
42.57
B


ATOM
2204
CE1
HIS
B
703
41.338
−12.345
11.003
1.00
42.52
B


ATOM
2205
NE2
HIS
B
703
40.462
−11.523
11.553
1.00
42.74
B


ATOM
2206
C
HIS
B
703
42.824
−10.107
7.909
1.00
43.10
B


ATOM
2207
O
HIS
B
703
43.437
−10.747
7.058
1.00
42.57
B


ATOM
2208
N
ASP
B
704
43.301
−9.876
9.130
1.00
48.46
B


ATOM
2209
CA
ASP
B
704
44.613
−10.353
9.561
1.00
53.34
B


ATOM
2210
CB
ASP
B
704
45.215
−9.389
10.588
1.00
55.90
B


ATOM
2211
CG
ASP
B
704
45.145
−7.941
10.147
1.00
59.16
B


ATOM
2212
OD1
ASP
B
704
44.020
−7.417
9.988
1.00
60.18
B


ATOM
2213
OD2
ASP
B
704
46.219
−7.326
9.963
1.00
61.84
B


ATOM
2214
C
ASP
B
704
44.552
−11.745
10.187
1.00
55.32
B


ATOM
2215
O
ASP
B
704
44.445
−11.872
11.407
1.00
55.54
B


ATOM
2216
N
ASN
B
705
44.619
−12.785
9.362
1.00
57.68
B


ATOM
2217
CA
ASN
B
705
44.593
−14.148
9.881
1.00
60.68
B


ATOM
2218
CB
ASN
B
705
44.482
−15.162
8.738
1.00
60.99
B


ATOM
2219
CG
ASN
B
705
43.096
−15.201
8.126
1.00
61.69
B


ATOM
2220
OD1
ASN
B
705
42.623
−14.215
7.561
1.00
61.90
B


ATOM
2221
ND2
ASN
B
705
42.434
−16.345
8.241
1.00
62.70
B


ATOM
2222
C
ASN
B
705
45.878
−14.391
10.665
1.00
62.22
B


ATOM
2223
O
ASN
B
705
45.965
−15.311
11.478
1.00
62.97
B


ATOM
2224
N
THR
B
706
46.870
−13.544
10.410
1.00
63.73
B


ATOM
2225
CA
THR
B
706
48.166
−13.629
11.069
1.00
64.99
B


ATOM
2226
CB
THR
B
706
49.068
−12.445
10.655
1.00
64.95
B


ATOM
2227
OG1
THR
B
706
50.196
−12.373
11.534
1.00
65.67
B


ATOM
2228
CG2
THR
B
706
48.293
−11.132
10.710
1.00
65.66
B


ATOM
2229
C
THR
B
706
48.064
−13.652
12.591
1.00
65.48
B


ATOM
2230
O
THR
B
706
48.428
−14.636
13.233
1.00
65.69
B


ATOM
2231
N
LYS
B
707
47.559
−12.561
13.158
1.00
66.27
B


ATOM
2232
CA
LYS
B
707
47.419
−12.424
14.604
1.00
66.72
B


ATOM
2233
CB
LYS
B
707
47.443
−10.944
14.983
1.00
67.27
B


ATOM
2234
CG
LYS
B
707
48.563
−10.151
14.333
1.00
68.66
B


ATOM
2235
CD
LYS
B
707
48.407
−8.666
14.617
1.00
69.39
B


ATOM
2236
CE
LYS
B
707
49.468
−7.847
13.901
1.00
69.82
B


ATOM
2237
NZ
LYS
B
707
49.310
−6.392
14.181
1.00
70.19
B


ATOM
2238
C
LYS
B
707
46.127
−13.043
15.125
1.00
66.65
B


ATOM
2239
O
LYS
B
707
45.153
−13.186
14.385
1.00
66.82
B


ATOM
2240
N
PRO
B
708
46.106
−13.422
16.414
1.00
66.47
B


ATOM
2241
CD
PRO
B
708
47.218
−13.402
17.381
1.00
66.43
B


ATOM
2242
CA
PRO
B
708
44.908
−14.019
17.011
1.00
65.90
B


ATOM
2243
CB
PRO
B
708
45.291
−14.151
18.482
1.00
66.34
B


ATOM
2244
CG
PRO
B
708
46.763
−14.410
18.413
1.00
66.16
B


ATOM
2245
C
PRO
B
708
43.727
−13.075
16.799
1.00
64.68
B


ATOM
2246
O
PRO
B
708
43.917
−11.868
16.654
1.00
64.70
B


ATOM
2247
N
ASP
B
709
42.514
−13.615
16.781
1.00
63.45
B


ATOM
2248
CA
ASP
B
709
41.341
−12.781
16.563
1.00
62.09
B


ATOM
2249
CB
ASP
B
709
40.410
−13.430
15.527
1.00
64.40
B


ATOM
2250
CG
ASP
B
709
39.736
−14.691
16.047
1.00
65.90
B


ATOM
2251
OD1
ASP
B
709
40.448
−15.647
16.421
1.00
67.51
B


ATOM
2252
OD2
ASP
B
709
38.487
−14.726
16.079
1.00
66.80
B


ATOM
2253
C
ASP
B
709
40.565
−12.493
17.841
1.00
59.94
B


ATOM
2254
O
ASP
B
709
40.223
−13.405
18.595
1.00
60.20
B


ATOM
2255
N
THR
B
710
40.300
−11.212
18.081
1.00
56.60
B


ATOM
2256
CA
THR
B
710
39.538
−10.786
19.247
1.00
52.69
B


ATOM
2257
CB
THR
B
710
40.152
−9.532
19.901
1.00
53.13
B


ATOM
2258
OG1
THR
B
710
40.264
−8.488
18.925
1.00
52.57
B


ATOM
2259
CG2
THR
B
710
41.527
−9.843
20.466
1.00
52.58
B


ATOM
2260
C
THR
B
710
38.125
−10.460
18.781
1.00
50.35
B


ATOM
2261
O
THR
B
710
37.880
−10.302
17.586
1.00
48.41
B


ATOM
2262
N
SER
B
711
37.196
−10.361
19.721
1.00
48.24
B


ATOM
2263
CA
SER
B
711
35.816
−10.060
19.376
1.00
46.44
B


ATOM
2264
CB
SER
B
711
34.943
−10.057
20.634
1.00
47.23
B


ATOM
2265
OG
SER
B
711
33.572
−9.910
20.303
1.00
49.85
B


ATOM
2266
C
SER
B
711
35.709
−8.711
18.668
1.00
43.95
B


ATOM
2267
O
SER
B
711
34.900
−8.544
17.757
1.00
43.72
B


ATOM
2268
N
SER
B
712
36.531
−7.753
19.081
1.00
41.06
B


ATOM
2269
CA
SER
B
712
36.502
−6.429
18.475
1.00
38.56
B


ATOM
2270
CB
SER
B
712
37.143
−5.402
19.417
1.00
39.63
B


ATOM
2271
OG
SER
B
712
38.524
−5.659
19.593
1.00
42.74
B


ATOM
2272
C
SER
B
712
37.207
−6.400
17.117
1.00
35.92
B


ATOM
2273
O
SER
B
712
36.779
−5.695
16.201
1.00
33.99
B


ATOM
2274
N
SER
B
713
38.285
−7.167
16.983
1.00
32.54
B


ATOM
2275
CA
SER
B
713
39.025
−7.200
15.728
1.00
30.34
B


ATOM
2276
CB
SER
B
713
40.357
−7.934
15.904
1.00
31.13
B


ATOM
2277
OG
SER
B
713
40.161
−9.335
15.964
1.00
31.92
B


ATOM
2278
C
SER
B
713
38.186
−7.912
14.673
1.00
28.11
B


ATOM
2279
O
SER
B
713
38.265
−7.607
13.487
1.00
24.98
B


ATOM
2280
N
LEU
B
714
37.380
−8.864
15.125
1.00
26.38
B


ATOM
2281
CA
LEU
B
714
36.517
−9.626
14.240
1.00
26.52
B


ATOM
2282
CB
LEU
B
714
35.972
−10.848
14.986
1.00
29.55
B


ATOM
2283
CG
LEU
B
714
35.155
−11.892
14.226
1.00
31.86
B


ATOM
2284
CD1
LEU
B
714
35.842
−12.254
12.917
1.00
34.03
B


ATOM
2285
CD2
LEU
B
714
34.997
−13.129
15.106
1.00
32.83
B


ATOM
2286
C
LEU
B
714
35.373
−8.746
13.745
1.00
25.49
B


ATOM
2287
O
LEU
B
714
35.045
−8.749
12.557
1.00
22.75
B


ATOM
2288
N
LEU
B
715
34.770
−7.982
14.652
1.00
23.34
B


ATOM
2289
CA
LEU
B
715
33.679
−7.101
14.266
1.00
22.41
B


ATOM
2290
CB
LEU
B
715
33.040
−6.480
15.509
1.00
23.20
B


ATOM
2291
CG
LEU
B
715
32.283
−7.511
16.358
1.00
25.47
B


ATOM
2292
CD1
LEU
B
715
31.802
−6.887
17.658
1.00
25.60
B


ATOM
2293
CD2
LEU
B
715
31.110
−8.056
15.551
1.00
24.95
B


ATOM
2294
C
LEU
B
715
34.203
−6.021
13.318
1.00
21.60
B


ATOM
2295
O
LEU
B
715
33.537
−5.655
12.346
1.00
20.68
B


ATOM
2296
N
THR
B
716
35.406
−5.527
13.595
1.00
19.50
B


ATOM
2297
CA
THR
B
716
36.021
−4.513
12.750
1.00
18.98
B


ATOM
2298
CB
THR
B
716
37.385
−4.066
13.337
1.00
18.83
B


ATOM
2299
OG1
THR
B
716
37.155
−3.304
14.531
1.00
20.73
B


ATOM
2300
CG2
THR
B
716
38.156
−3.220
12.345
1.00
18.41
B


ATOM
2301
C
THR
B
716
36.210
−5.059
11.330
1.00
20.03
B


ATOM
2302
O
THR
B
716
35.944
−4.365
10.350
1.00
18.15
B


ATOM
2303
N
SER
B
717
36.657
−6.306
11.217
1.00
20.54
B


ATOM
2304
CA
SER
B
717
36.857
−6.901
9.898
1.00
21.70
B


ATOM
2305
CB
SER
B
717
37.588
−8.241
10.010
1.00
23.38
B


ATOM
2306
OG
SER
B
717
38.960
−8.031
10.299
1.00
28.56
B


ATOM
2307
C
SER
B
717
35.533
−7.090
9.168
1.00
20.61
B


ATOM
2308
O
SER
B
717
35.466
−6.914
7.952
1.00
20.71
B


ATOM
2309
N
LEU
B
718
34.484
−7.449
9.905
1.00
18.62
B


ATOM
2310
CA
LEU
B
718
33.164
−7.638
9.306
1.00
18.51
B


ATOM
2311
CB
LEU
B
718
32.193
−8.240
10.321
1.00
18.50
B


ATOM
2312
CG
LEU
B
718
32.302
−9.746
10.585
1.00
19.89
B


ATOM
2313
CD1
LEU
B
718
31.510
−10.098
11.833
1.00
20.48
B


ATOM
2314
CD2
LEU
B
718
31.781
−10.517
9.369
1.00
18.28
B


ATOM
2315
C
LEU
B
718
32.625
−6.294
8.826
1.00
18.13
B


ATOM
2316
O
LEU
B
718
31.889
−6.220
7.837
1.00
16.53
B


ATOM
2317
N
ASN
B
719
32.985
−5.229
9.534
1.00
18.23
B


ATOM
2318
CA
ASN
B
719
32.528
−3.902
9.144
1.00
17.99
B


ATOM
2319
CB
ASN
B
719
32.704
−2.907
10.292
1.00
19.22
B


ATOM
2320
CG
ASN
B
719
31.682
−3.107
11.390
1.00
20.19
B


ATOM
2321
OD1
ASN
B
719
30.611
−3.667
11.156
1.00
20.66
B


ATOM
2322
ND2
ASN
B
719
31.997
−2.632
12.593
1.00
19.69
B


ATOM
2323
C
ASN
B
719
33.294
−3.432
7.915
1.00
19.00
B


ATOM
2324
O
ASN
B
719
32.745
−2.727
7.067
1.00
16.93
B


ATOM
2325
N
GLN
B
720
34.562
−3.834
7.820
1.00
17.58
B


ATOM
2326
CA
GLN
B
720
35.391
−3.463
6.679
1.00
18.94
B


ATOM
2327
CB
GLN
B
720
36.851
−3.859
6.925
1.00
19.50
B


ATOM
2328
CG
GLN
B
720
37.736
−3.733
5.695
1.00
22.84
B


ATOM
2329
CD
GLN
B
720
37.784
−2.318
5.149
1.00
23.37
B


ATOM
2330
OE1
GLN
B
720
37.894
−2.117
3.941
1.00
21.74
B


ATOM
2331
NE2
GLN
B
720
37.711
−1.332
6.038
1.00
22.07
B


ATOM
2332
C
GLN
B
720
34.846
−4.200
5.463
1.00
19.76
B


ATOM
2333
O
GLN
B
720
34.714
−3.636
4.372
1.00
15.95
B


ATOM
2334
N
LEU
B
721
34.526
−5.474
5.665
1.00
18.87
B


ATOM
2335
CA
LEU
B
721
33.973
−6.293
4.599
1.00
18.03
B


ATOM
2336
CB
LEU
B
721
33.763
−7.726
5.102
1.00
18.09
B


ATOM
2337
CG
LEU
B
721
33.182
−8.735
4.113
1.00
19.65
B


ATOM
2338
CD1
LEU
B
721
34.094
−8.844
2.893
1.00
16.27
B


ATOM
2339
CD2
LEU
B
721
33.033
−10.090
4.810
1.00
18.08
B


ATOM
2340
C
LEU
B
721
32.643
−5.660
4.204
1.00
17.35
B


ATOM
2341
O
LEU
B
721
32.301
−5.592
3.027
1.00
17.63
B


ATOM
2342
N
GLY
B
722
31.901
−5.188
5.202
1.00
16.11
B


ATOM
2343
CA
GLY
B
722
30.622
−4.547
4.942
1.00
17.12
B


ATOM
2344
C
GLY
B
722
30.780
−3.281
4.109
1.00
19.60
B


ATOM
2345
O
GLY
B
722
29.948
−2.985
3.239
1.00
17.68
B


ATOM
2346
N
GLU
B
723
31.847
−2.526
4.366
1.00
17.38
B


ATOM
2347
CA
GLU
B
723
32.095
−1.296
3.612
1.00
17.59
B


ATOM
2348
CB
GLU
B
723
33.322
−0.563
4.162
1.00
16.95
B


ATOM
2349
CG
GLU
B
723
33.590
0.782
3.490
1.00
16.70
B


ATOM
2350
CD
GLU
B
723
32.710
1.898
4.032
1.00
18.40
B


ATOM
2351
OE1
GLU
B
723
31.667
1.582
4.637
1.00
18.46
B


ATOM
2352
OE2
GLU
B
723
33.057
3.092
3.847
1.00
15.57
B


ATOM
2353
C
GLU
B
723
32.340
−1.629
2.143
1.00
17.94
B


ATOM
2354
O
GLU
B
723
31.844
−0.946
1.241
1.00
18.69
B


ATOM
2355
N
ARG
B
724
33.122
−2.679
1.910
1.00
18.32
B


ATOM
2356
CA
ARG
B
724
33.451
−3.099
0.555
1.00
18.63
B


ATOM
2357
CB
ARG
B
724
34.591
−4.125
0.586
1.00
18.71
B


ATOM
2358
CG
ARG
B
724
35.845
−3.613
1.289
1.00
19.29
B


ATOM
2359
CD
ARG
B
724
36.992
−4.604
1.193
1.00
20.38
B


ATOM
2360
NE
ARG
B
724
38.173
−4.123
1.903
1.00
22.22
B


ATOM
2361
CZ
ARG
B
724
39.355
−4.728
1.892
1.00
23.91
B


ATOM
2362
NH1
ARG
B
724
39.526
−5.849
1.205
1.00
22.36
B


ATOM
2363
NH2
ARG
B
724
40.372
−4.205
2.568
1.00
26.01
B


ATOM
2364
C
ARG
B
724
32.230
−3.683
−0.148
1.00
18.31
B


ATOM
2365
O
ARG
B
724
32.021
−3.465
−1.339
1.00
16.69
B


ATOM
2366
N
GLN
B
725
31.414
−4.422
0.590
1.00
17.60
B


ATOM
2367
CA
GLN
B
725
30.227
−5.000
−0.011
1.00
18.87
B


ATOM
2368
CB
GLN
B
725
29.637
−6.073
0.908
1.00
17.78
B


ATOM
2369
CG
GLN
B
725
30.538
−7.305
1.030
1.00
23.54
B


ATOM
2370
CD
GLN
B
725
29.853
−8.468
1.714
1.00
25.93
B


ATOM
2371
OE1
GLN
B
725
30.443
−9.532
1.901
1.00
29.72
B


ATOM
2372
NE2
GLN
B
725
28.599
−8.274
2.088
1.00
28.88
B


ATOM
2373
C
GLN
B
725
29.195
−3.920
−0.332
1.00
18.08
B


ATOM
2374
O
GLN
B
725
28.440
−4.036
−1.298
1.00
18.14
B


ATOM
2375
N
LEU
B
726
29.172
−2.855
0.459
1.00
18.05
B


ATOM
2376
CA
LEU
B
726
28.227
−1.777
0.203
1.00
18.04
B


ATOM
2377
CB
LEU
B
726
28.323
−0.727
1.314
1.00
20.54
B


ATOM
2378
CG
LEU
B
726
27.263
0.376
1.383
1.00
20.94
B


ATOM
2379
CD1
LEU
B
726
25.859
−0.216
1.325
1.00
19.79
B


ATOM
2380
CD2
LEU
B
726
27.472
1.171
2.681
1.00
21.03
B


ATOM
2381
C
LEU
B
726
28.551
−1.172
−1.167
1.00
18.14
B


ATOM
2382
O
LEU
B
726
27.658
−0.933
−1.986
1.00
17.87
B


ATOM
2383
N
LEU
B
727
29.836
−0.950
−1.426
1.00
16.39
B


ATOM
2384
CA
LEU
B
727
30.259
−0.401
−2.706
1.00
18.19
B


ATOM
2385
CB
LEU
B
727
31.775
−0.179
−2.715
1.00
19.81
B


ATOM
2386
CG
LEU
B
727
32.387
0.233
−4.060
1.00
22.06
B


ATOM
2387
CD1
LEU
B
727
31.828
1.578
−4.498
1.00
24.00
B


ATOM
2388
CD2
LEU
B
727
33.905
0.309
−3.932
1.00
24.38
B


ATOM
2389
C
LEU
B
727
29.868
−1.334
−3.860
1.00
18.39
B


ATOM
2390
O
LEU
B
727
29.457
−0.872
−4.929
1.00
18.62
B


ATOM
2391
N
SER
B
728
29.986
−2.644
−3.646
1.00
17.14
B


ATOM
2392
CA
SER
B
728
29.643
−3.598
−4.696
1.00
19.54
B


ATOM
2393
CB
SER
B
728
30.125
−5.013
−4.343
1.00
20.37
B


ATOM
2394
OG
SER
B
728
29.369
−5.558
−3.280
1.00
27.70
B


ATOM
2395
C
SER
B
728
28.138
−3.610
−4.943
1.00
17.78
B


ATOM
2396
O
SER
B
728
27.698
−3.747
−6.079
1.00
18.32
B


ATOM
2397
N
VAL
B
729
27.352
−3.476
−3.880
1.00
17.66
B


ATOM
2398
CA
VAL
B
729
25.895
−3.446
−4.020
1.00
18.18
B


ATOM
2399
CB
VAL
B
729
25.201
−3.329
−2.642
1.00
19.59
B


ATOM
2400
CG1
VAL
B
729
23.712
−3.029
−2.816
1.00
19.79
B


ATOM
2401
CG2
VAL
B
729
25.381
−4.630
−1.869
1.00
22.69
B


ATOM
2402
C
VAL
B
729
25.467
−2.261
−4.888
1.00
18.00
B


ATOM
2403
O
VAL
B
729
24.630
−2.402
−5.781
1.00
18.81
B


ATOM
2404
N
VAL
B
730
26.040
−1.092
−4.624
1.00
16.70
B


ATOM
2405
CA
VAL
B
730
25.694
0.092
−5.401
1.00
18.31
B


ATOM
2406
CB
VAL
B
730
26.364
1.364
−4.822
1.00
17.54
B


ATOM
2407
CG1
VAL
B
730
25.962
2.587
−5.646
1.00
20.82
B


ATOM
2408
CG2
VAL
B
730
25.940
1.561
−3.363
1.00
20.52
B


ATOM
2409
C
VAL
B
730
26.102
−0.086
−6.865
1.00
17.87
B


ATOM
2410
O
VAL
B
730
25.331
0.230
−7.770
1.00
21.04
B


ATOM
2411
N
LYS
B
731
27.303
−0.598
−7.108
1.00
17.34
B


ATOM
2412
CA
LYS
B
731
27.739
−0.803
−8.485
1.00
18.71
B


ATOM
2413
CB
LYS
B
731
29.190
−1.289
−8.527
1.00
22.00
B


ATOM
2414
CG
LYS
B
731
30.213
−0.192
−8.223
1.00
23.19
B


ATOM
2415
CD
LYS
B
731
31.632
−0.719
−8.378
1.00
28.30
B


ATOM
2416
CE
LYS
B
731
32.657
0.390
−8.185
1.00
30.48
B


ATOM
2417
NZ
LYS
B
731
34.053
−0.126
−8.247
1.00
34.47
B


ATOM
2418
C
LYS
B
731
26.825
−1.808
−9.183
1.00
19.77
B


ATOM
2419
O
LYS
B
731
26.421
−1.605
−10.331
1.00
17.95
B


ATOM
2420
N
TRP
B
732
26.509
−2.887
−8.473
1.00
17.50
B


ATOM
2421
CA
TRP
B
732
25.630
−3.937
−8.975
1.00
17.41
B


ATOM
2422
CB
TRP
B
732
25.438
−4.996
−7.883
1.00
16.91
B


ATOM
2423
CG
TRP
B
732
24.321
−5.985
−8.112
1.00
15.88
B


ATOM
2424
CD2
TRP
B
732
23.100
−6.073
−7.371
1.00
15.43
B


ATOM
2425
CE2
TRP
B
732
22.388
−7.191
−7.863
1.00
16.91
B


ATOM
2426
CE3
TRP
B
732
22.539
−5.317
−6.331
1.00
14.91
B


ATOM
2427
CD1
TRP
B
732
24.299
−7.019
−9.011
1.00
16.77
B


ATOM
2428
NE1
TRP
B
732
23.140
−7.751
−8.863
1.00
16.21
B


ATOM
2429
CZ2
TRP
B
732
21.140
−7.571
−7.350
1.00
16.15
B


ATOM
2430
CZ3
TRP
B
732
21.299
−5.694
−5.818
1.00
14.22
B


ATOM
2431
CH2
TRP
B
732
20.614
−6.813
−6.330
1.00
16.68
B


ATOM
2432
C
TRP
B
732
24.279
−3.350
−9.378
1.00
16.02
B


ATOM
2433
O
TRP
B
732
23.783
−3.617
−10.472
1.00
16.45
B


ATOM
2434
N
SER
B
733
23.699
−2.541
−8.495
1.00
16.26
B


ATOM
2435
CA
SER
B
733
22.390
−1.939
−8.749
1.00
17.13
B


ATOM
2436
CB
SER
B
733
21.945
−1.105
−7.543
1.00
15.29
B


ATOM
2437
OG
SER
B
733
22.713
0.081
−7.434
1.00
16.35
B


ATOM
2438
C
SER
B
733
22.365
−1.068
−10.009
1.00
18.91
B


ATOM
2439
O
SER
B
733
21.318
−0.901
−10.633
1.00
18.17
B


ATOM
2440
N
LYS
B
734
23.519
−0.524
−10.383
1.00
18.91
B


ATOM
2441
CA
LYS
B
734
23.612
0.329
−11.564
1.00
21.91
B


ATOM
2442
CB
LYS
B
734
24.952
1.073
−11.576
1.00
26.10
B


ATOM
2443
CG
LYS
B
734
25.042
2.153
−10.518
1.00
30.52
B


ATOM
2444
CD
LYS
B
734
26.320
2.954
−10.644
1.00
35.02
B


ATOM
2445
CE
LYS
B
734
26.159
4.306
−9.974
1.00
37.63
B


ATOM
2446
NZ
LYS
B
734
25.095
5.122
−10.632
1.00
39.56
B


ATOM
2447
C
LYS
B
734
23.444
−0.447
−12.863
1.00
21.73
B


ATOM
2448
O
LYS
B
734
23.125
0.133
−13.905
1.00
19.82
B


ATOM
2449
N
SER
B
735
23.659
−1.758
−12.798
1.00
19.96
B


ATOM
2450
CA
SER
B
735
23.517
−2.616
−13.969
1.00
19.76
B


ATOM
2451
CB
SER
B
735
24.748
−3.519
−14.126
1.00
19.35
B


ATOM
2452
OG
SER
B
735
25.918
−2.756
−14.356
1.00
23.17
B


ATOM
2453
C
SER
B
735
22.267
−3.488
−13.878
1.00
18.19
B


ATOM
2454
O
SER
B
735
21.932
−4.189
−14.833
1.00
17.56
B


ATOM
2455
N
LEU
B
736
21.589
−3.446
−12.731
1.00
17.46
B


ATOM
2456
CA
LEU
B
736
20.375
−4.239
−12.503
1.00
16.58
B


ATOM
2457
CB
LEU
B
736
19.991
−4.193
−11.017
1.00
16.96
B


ATOM
2458
CG
LEU
B
736
18.736
−4.939
−10.547
1.00
19.34
B


ATOM
2459
CD1
LEU
B
736
18.886
−6.439
−10.793
1.00
18.13
B


ATOM
2460
CD2
LEU
B
736
18.525
−4.679
−9.058
1.00
18.75
B


ATOM
2461
C
LEU
B
736
19.230
−3.680
−13.344
1.00
17.27
B


ATOM
2462
O
LEU
B
736
18.776
−2.562
−13.111
1.00
16.74
B


ATOM
2463
N
PRO
B
737
18.738
−4.458
−14.322
1.00
18.08
B


ATOM
2464
CD
PRO
B
737
19.117
−5.847
−14.643
1.00
17.66
B


ATOM
2465
CA
PRO
B
737
17.643
−4.005
−15.188
1.00
18.21
B


ATOM
2466
CB
PRO
B
737
17.247
−5.275
−15.943
1.00
18.86
B


ATOM
2467
CG
PRO
B
737
18.556
−6.022
−16.035
1.00
17.53
B


ATOM
2468
C
PRO
B
737
16.470
−3.390
−14.438
1.00
18.80
B


ATOM
2469
O
PRO
B
737
15.890
−4.013
−13.544
1.00
19.03
B


ATOM
2470
N
GLY
B
738
16.145
−2.152
−14.800
1.00
18.43
B


ATOM
2471
CA
GLY
B
738
15.031
−1.455
−14.187
1.00
17.85
B


ATOM
2472
C
GLY
B
738
15.338
−0.574
−12.991
1.00
16.86
B


ATOM
2473
O
GLY
B
738
14.678
0.444
−12.791
1.00
15.62
B


ATOM
2474
N
PHE
B
739
16.350
−0.932
−12.205
1.00
15.96
B


ATOM
2475
CA
PHE
B
739
16.662
−0.163
−11.010
1.00
14.50
B


ATOM
2476
CB
PHE
B
739
17.791
−0.829
−10.216
1.00
14.29
B


ATOM
2477
CG
PHE
B
739
17.917
−0.307
−8.818
1.00
14.77
B


ATOM
2478
CD1
PHE
B
739
17.021
−0.712
−7.832
1.00
17.58
B


ATOM
2479
CD2
PHE
B
739
18.916
0.601
−8.483
1.00
16.38
B


ATOM
2480
CE1
PHE
B
739
17.116
−0.217
−6.528
1.00
19.63
B


ATOM
2481
CE2
PHE
B
739
19.022
1.102
−7.187
1.00
18.02
B


ATOM
2482
CZ
PHE
B
739
18.120
0.689
−6.205
1.00
15.95
B


ATOM
2483
C
PHE
B
739
17.031
1.296
−11.247
1.00
15.95
B


ATOM
2484
O
PHE
B
739
16.554
2.180
−10.532
1.00
15.43
B


ATOM
2485
N
ARG
B
740
17.893
1.542
−12.233
1.00
14.92
B


ATOM
2486
CA
ARG
B
740
18.336
2.898
−12.546
1.00
18.27
B


ATOM
2487
CB
ARG
B
740
19.414
2.868
−13.631
1.00
20.12
B


ATOM
2488
CG
ARG
B
740
18.933
2.276
−14.956
1.00
20.07
B


ATOM
2489
CD
ARG
B
740
19.951
2.489
−16.074
1.00
20.49
B


ATOM
2490
NE
ARG
B
740
19.432
2.001
−17.347
1.00
21.32
B


ATOM
2491
CZ
ARG
B
740
20.021
2.190
−18.524
1.00
22.16
B


ATOM
2492
NH1
ARG
B
740
21.164
2.862
−18.601
1.00
20.37
B


ATOM
2493
NH2
ARG
B
740
19.460
1.704
−19.625
1.00
20.63
B


ATOM
2494
C
ARG
B
740
17.185
3.783
−13.013
1.00
18.64
B


ATOM
2495
O
ARG
B
740
17.324
5.001
−13.090
1.00
18.88
B


ATOM
2496
N
ASN
B
741
16.048
3.167
−13.315
1.00
18.88
B


ATOM
2497
CA
ASN
B
741
14.883
3.904
−13.786
1.00
19.14
B


ATOM
2498
CB
ASN
B
741
14.088
3.015
−14.742
1.00
22.68
B


ATOM
2499
CG
ASN
B
741
14.904
2.633
−15.964
1.00
23.46
B


ATOM
2500
OD1
ASN
B
741
14.743
1.551
−16.533
1.00
25.91
B


ATOM
2501
ND2
ASN
B
741
15.798
3.530
−16.371
1.00
22.56
B


ATOM
2502
C
ASN
B
741
14.001
4.448
−12.666
1.00
18.84
B


ATOM
2503
O
ASN
B
741
13.090
5.241
−12.906
1.00
18.36
B


ATOM
2504
N
LEU
B
742
14.282
4.034
−11.436
1.00
16.78
B


ATOM
2505
CA
LEU
B
742
13.529
4.532
−10.293
1.00
17.18
B


ATOM
2506
CB
LEU
B
742
13.660
3.583
−9.090
1.00
17.93
B


ATOM
2507
CG
LEU
B
742
13.275
2.111
−9.273
1.00
19.23
B


ATOM
2508
CD1
LEU
B
742
13.651
1.333
−8.019
1.00
20.55
B


ATOM
2509
CD2
LEU
B
742
11.782
1.993
−9.554
1.00
21.11
B


ATOM
2510
C
LEU
B
742
14.125
5.886
−9.919
1.00
17.11
B


ATOM
2511
O
LEU
B
742
15.287
6.171
−10.219
1.00
16.40
B


ATOM
2512
N
HIS
B
743
13.323
6.720
−9.273
1.00
17.11
B


ATOM
2513
CA
HIS
B
743
13.779
8.030
−8.826
1.00
20.34
B


ATOM
2514
CB
HIS
B
743
12.670
8.667
−7.981
1.00
22.04
B


ATOM
2515
CG
HIS
B
743
12.930
10.087
−7.590
1.00
26.50
B


ATOM
2516
CD2
HIS
B
743
12.372
11.244
−8.018
1.00
28.30
B


ATOM
2517
ND1
HIS
B
743
13.842
10.439
−6.617
1.00
27.58
B


ATOM
2518
CE1
HIS
B
743
13.832
11.751
−6.461
1.00
28.99
B


ATOM
2519
NE2
HIS
B
743
12.948
12.263
−7.299
1.00
27.82
B


ATOM
2520
C
HIS
B
743
15.046
7.777
−7.990
1.00
20.44
B


ATOM
2521
O
HIS
B
743
15.121
6.782
−7.264
1.00
18.79
B


ATOM
2522
N
ILE
B
744
16.041
8.652
−8.109
1.00
20.57
B


ATOM
2523
CA
ILE
B
744
17.289
8.483
−7.365
1.00
19.99
B


ATOM
2524
CB
ILE
B
744
18.279
9.638
−7.666
1.00
21.19
B


ATOM
2525
CG2
ILE
B
744
19.513
9.538
−6.760
1.00
19.18
B


ATOM
2526
CG1
ILE
B
744
18.701
9.569
−9.138
1.00
20.37
B


ATOM
2527
CD1
ILE
B
744
19.690
10.646
−9.566
1.00
25.65
B


ATOM
2528
C
ILE
B
744
17.086
8.352
−5.857
1.00
20.50
B


ATOM
2529
O
ILE
B
744
17.802
7.595
−5.196
1.00
20.10
B


ATOM
2530
N
ASP
B
745
16.114
9.073
−5.304
1.00
19.58
B


ATOM
2531
CA
ASP
B
745
15.857
8.974
−3.868
1.00
21.19
B


ATOM
2532
CB
ASP
B
745
14.768
9.952
−3.416
1.00
24.33
B


ATOM
2533
CG
ASP
B
745
15.233
11.387
−3.413
1.00
27.99
B


ATOM
2534
OD1
ASP
B
745
16.458
11.622
−3.380
1.00
30.68
B


ATOM
2535
OD2
ASP
B
745
14.364
12.280
−3.426
1.00
30.97
B


ATOM
2536
C
ASP
B
745
15.400
7.566
−3.517
1.00
19.87
B


ATOM
2537
O
ASP
B
745
15.752
7.044
−2.462
1.00
20.15
B


ATOM
2538
N
ASP
B
746
14.591
6.971
−4.389
1.00
19.04
B


ATOM
2539
CA
ASP
B
746
14.097
5.618
−4.152
1.00
18.78
B


ATOM
2540
CB
ASP
B
746
13.055
5.201
−5.197
1.00
18.11
B


ATOM
2541
CG
ASP
B
746
11.817
6.078
−5.191
1.00
21.37
B


ATOM
2542
OD1
ASP
B
746
11.580
6.816
−4.207
1.00
19.54
B


ATOM
2543
OD2
ASP
B
746
11.065
6.004
−6.188
1.00
22.68
B


ATOM
2544
C
ASP
B
746
15.261
4.631
−4.213
1.00
17.19
B


ATOM
2545
O
ASP
B
746
15.319
3.689
−3.423
1.00
18.41
B


ATOM
2546
N
GLN
B
747
16.176
4.836
−5.157
1.00
16.73
B


ATOM
2547
CA
GLN
B
747
17.320
3.936
−5.282
1.00
16.32
B


ATOM
2548
CB
GLN
B
747
18.227
4.357
−6.439
1.00
16.06
B


ATOM
2549
CG
GLN
B
747
17.570
4.282
−7.815
1.00
14.64
B


ATOM
2550
CD
GLN
B
747
18.478
4.787
−8.916
1.00
16.67
B


ATOM
2551
OE1
GLN
B
747
18.021
5.411
−9.874
1.00
18.54
B


ATOM
2552
NE2
GLN
B
747
19.775
4.518
−8.789
1.00
12.03
B


ATOM
2553
C
GLN
B
747
18.116
3.929
−3.984
1.00
15.90
B


ATOM
2554
O
GLN
B
747
18.426
2.870
−3.445
1.00
15.22
B


ATOM
2555
N
ILE
B
748
18.441
5.119
−3.486
1.00
15.67
B


ATOM
2556
CA
ILE
B
748
19.199
5.247
−2.250
1.00
14.76
B


ATOM
2557
CB
ILE
B
748
19.447
6.726
−1.901
1.00
17.21
B


ATOM
2558
CG2
ILE
B
748
20.131
6.831
−0.544
1.00
18.09
B


ATOM
2559
CG1
ILE
B
748
20.314
7.376
−2.981
1.00
16.97
B


ATOM
2560
CD1
ILE
B
748
20.562
8.874
−2.767
1.00
19.77
B


ATOM
2561
C
ILE
B
748
18.459
4.588
−1.094
1.00
15.63
B


ATOM
2562
O
ILE
B
748
19.046
3.826
−0.320
1.00
15.86
B


ATOM
2563
N
THR
B
749
17.166
4.884
−0.984
1.00
14.70
B


ATOM
2564
CA
THR
B
749
16.336
4.323
0.072
1.00
14.94
B


ATOM
2565
CB
THR
B
749
14.891
4.858
−0.037
1.00
16.72
B


ATOM
2566
OG1
THR
B
749
14.894
6.268
0.218
1.00
18.70
B


ATOM
2567
CG2
THR
B
749
13.974
4.173
0.969
1.00
17.71
B


ATOM
2568
C
THR
B
749
16.320
2.793
0.055
1.00
14.91
B


ATOM
2569
O
THR
B
749
16.499
2.151
1.096
1.00
15.12
B


ATOM
2570
N
LEU
B
750
16.117
2.204
−1.122
1.00
13.93
B


ATOM
2571
CA
LEU
B
750
16.073
0.745
−1.232
1.00
14.49
B


ATOM
2572
CB
LEU
B
750
15.667
0.327
−2.654
1.00
14.19
B


ATOM
2573
CG
LEU
B
750
14.214
0.702
−2.987
1.00
16.47
B


ATOM
2574
CD1
LEU
B
750
13.922
0.449
−4.476
1.00
16.09
B


ATOM
2575
CD2
LEU
B
750
13.272
−0.115
−2.101
1.00
14.27
B


ATOM
2576
C
LEU
B
750
17.407
0.108
−0.853
1.00
14.83
B


ATOM
2577
O
LEU
B
750
17.437
−0.924
−0.177
1.00
15.56
B


ATOM
2578
N
ILE
B
751
18.508
0.719
−1.277
1.00
14.16
B


ATOM
2579
CA
ILE
B
751
19.824
0.179
−0.942
1.00
16.07
B


ATOM
2580
CB
ILE
B
751
20.952
0.904
−1.719
1.00
15.86
B


ATOM
2581
CG2
ILE
B
751
22.326
0.534
−1.138
1.00
15.95
B


ATOM
2582
CG1
ILE
B
751
20.874
0.525
−3.202
1.00
15.28
B


ATOM
2583
CD1
ILE
B
751
21.803
1.311
−4.093
1.00
20.05
B


ATOM
2584
C
ILE
B
751
20.077
0.298
0.561
1.00
16.75
B


ATOM
2585
O
ILE
B
751
20.543
−0.650
1.196
1.00
16.19
B


ATOM
2586
N
GLN
B
752
19.763
1.454
1.136
1.00
17.86
B


ATOM
2587
CA
GLN
B
752
19.976
1.646
2.567
1.00
18.49
B


ATOM
2588
CB
GLN
B
752
19.788
3.120
2.950
1.00
17.93
B


ATOM
2589
CG
GLN
B
752
20.754
4.049
2.212
1.00
19.72
B


ATOM
2590
CD
GLN
B
752
20.823
5.449
2.800
1.00
21.05
B


ATOM
2591
OE1
GLN
B
752
19.825
5.986
3.282
1.00
22.57
B


ATOM
2592
NE2
GLN
B
752
22.006
6.056
2.742
1.00
20.90
B


ATOM
2593
C
GLN
B
752
19.067
0.748
3.407
1.00
19.34
B


ATOM
2594
O
GLN
B
752
19.457
0.315
4.488
1.00
19.27
B


ATOM
2595
N
TYR
B
753
17.865
0.461
2.909
1.00
17.95
B


ATOM
2596
CA
TYR
B
753
16.919
−0.407
3.616
1.00
16.98
B


ATOM
2597
CB
TYR
B
753
15.519
−0.316
2.994
1.00
19.29
B


ATOM
2598
CG
TYR
B
753
14.634
0.837
3.424
1.00
18.86
B


ATOM
2599
CD1
TYR
B
753
15.116
1.891
4.204
1.00
19.58
B


ATOM
2600
CE1
TYR
B
753
14.275
2.973
4.552
1.00
20.49
B


ATOM
2601
CD2
TYR
B
753
13.304
0.884
3.007
1.00
20.96
B


ATOM
2602
CE2
TYR
B
753
12.472
1.943
3.342
1.00
20.37
B


ATOM
2603
CZ
TYR
B
753
12.956
2.980
4.106
1.00
19.88
B


ATOM
2604
OH
TYR
B
753
12.108
4.021
4.401
1.00
21.79
B


ATOM
2605
C
TYR
B
753
17.318
−1.888
3.574
1.00
18.67
B


ATOM
2606
O
TYR
B
753
17.142
−2.612
4.555
1.00
17.27
B


ATOM
2607
N
SER
B
754
17.845
−2.327
2.431
1.00
17.61
B


ATOM
2608
CA
SER
B
754
18.198
−3.736
2.215
1.00
17.75
B


ATOM
2609
CB
SER
B
754
17.769
−4.150
0.807
1.00
16.13
B


ATOM
2610
OG
SER
B
754
18.566
−3.484
−0.156
1.00
17.94
B


ATOM
2611
C
SER
B
754
19.659
−4.129
2.392
1.00
17.86
B


ATOM
2612
O
SER
B
754
20.004
−5.303
2.253
1.00
17.64
B


ATOM
2613
N
TRP
B
755
20.513
−3.157
2.678
1.00
17.38
B


ATOM
2614
CA
TRP
B
755
21.941
−3.410
2.853
1.00
19.81
B


ATOM
2615
CB
TRP
B
755
22.569
−2.169
3.497
1.00
24.07
B


ATOM
2616
CG
TRP
B
755
23.816
−2.413
4.246
1.00
30.04
B


ATOM
2617
CD2
TRP
B
755
23.997
−2.283
5.656
1.00
31.44
B


ATOM
2618
CE2
TRP
B
755
25.333
−2.639
5.942
1.00
33.80
B


ATOM
2619
CE3
TRP
B
755
23.159
−1.900
6.709
1.00
30.73
B


ATOM
2620
CD1
TRP
B
755
25.013
−2.826
3.739
1.00
33.58
B


ATOM
2621
NE1
TRP
B
755
25.934
−2.966
4.754
1.00
35.50
B


ATOM
2622
CZ2
TRP
B
755
25.850
−2.625
7.239
1.00
34.63
B


ATOM
2623
CZ3
TRP
B
755
23.673
−1.886
7.998
1.00
31.07
B


ATOM
2624
CH2
TRP
B
755
25.007
−2.247
8.251
1.00
32.77
B


ATOM
2625
C
TRP
B
755
22.263
−4.683
3.662
1.00
18.91
B


ATOM
2626
O
TRP
B
755
22.919
−5.599
3.160
1.00
18.50
B


ATOM
2627
N
MET
B
756
21.794
−4.745
4.903
1.00
16.98
B


ATOM
2628
CA
MET
B
756
22.054
−5.902
5.765
1.00
16.75
B


ATOM
2629
CB
MET
B
756
21.488
−5.652
7.169
1.00
15.08
B


ATOM
2630
CG
MET
B
756
21.834
−6.735
8.207
1.00
18.13
B


ATOM
2631
SD
MET
B
756
23.609
−6.843
8.597
1.00
21.78
B


ATOM
2632
CE
MET
B
756
23.790
−5.506
9.806
1.00
22.86
B


ATOM
2633
C
MET
B
756
21.477
−7.205
5.205
1.00
16.39
B


ATOM
2634
O
MET
B
756
22.135
−8.243
5.236
1.00
16.19
B


ATOM
2635
N
SER
B
757
20.251
−7.155
4.694
1.00
15.29
B


ATOM
2636
CA
SER
B
757
19.619
−8.349
4.150
1.00
17.08
B


ATOM
2637
CB
SER
B
757
18.174
−8.055
3.728
1.00
20.88
B


ATOM
2638
OG
SER
B
757
18.141
−7.124
2.662
1.00
28.77
B


ATOM
2639
C
SER
B
757
20.401
−8.895
2.960
1.00
17.10
B


ATOM
2640
O
SER
B
757
20.589
−10.101
2.846
1.00
17.47
B


ATOM
2641
N
LEU
B
758
20.861
−8.013
2.078
1.00
17.47
B


ATOM
2642
CA
LEU
B
758
21.620
−8.452
0.911
1.00
17.62
B


ATOM
2643
CB
LEU
B
758
21.922
−7.270
−0.018
1.00
17.52
B


ATOM
2644
CG
LEU
B
758
20.713
−6.633
−0.715
1.00
21.15
B


ATOM
2645
CD1
LEU
B
758
21.172
−5.516
−1.651
1.00
21.27
B


ATOM
2646
CD2
LEU
B
758
19.964
−7.696
−1.500
1.00
21.66
B


ATOM
2647
C
LEU
B
758
22.922
−9.103
1.356
1.00
16.78
B


ATOM
2648
O
LEU
B
758
23.342
−10.114
0.795
1.00
16.30
B


ATOM
2649
N
MET
B
759
23.556
−8.529
2.373
1.00
14.76
B


ATOM
2650
CA
MET
B
759
24.808
−9.077
2.863
1.00
17.48
B


ATOM
2651
CB
MET
B
759
25.458
−8.126
3.863
1.00
19.24
B


ATOM
2652
CG
MET
B
759
26.046
−6.892
3.211
1.00
25.62
B


ATOM
2653
SD
MET
B
759
27.036
−5.967
4.372
1.00
30.32
B


ATOM
2654
CE
MET
B
759
27.629
−4.686
3.275
1.00
31.96
B


ATOM
2655
C
MET
B
759
24.659
−10.452
3.494
1.00
16.79
B


ATOM
2656
O
MET
B
759
25.465
−11.344
3.229
1.00
17.13
B


ATOM
2657
N
VAL
B
760
23.639
−10.626
4.329
1.00
16.12
B


ATOM
2658
CA
VAL
B
760
23.429
−11.912
4.980
1.00
16.70
B


ATOM
2659
CB
VAL
B
760
22.425
−11.788
6.163
1.00
18.09
B


ATOM
2660
CG1
VAL
B
760
21.012
−11.598
5.652
1.00
18.30
B


ATOM
2661
CG2
VAL
B
760
22.524
−13.005
7.059
1.00
18.55
B


ATOM
2662
C
VAL
B
760
22.945
−12.966
3.972
1.00
17.46
B


ATOM
2663
O
VAL
B
760
23.260
−14.146
4.098
1.00
16.23
B


ATOM
2664
N
PHE
B
761
22.195
−12.533
2.963
1.00
15.44
B


ATOM
2665
CA
PHE
B
761
21.700
−13.451
1.938
1.00
15.94
B


ATOM
2666
CB
PHE
B
761
20.686
−12.732
1.040
1.00
13.58
B


ATOM
2667
CG
PHE
B
761
19.770
−13.657
0.281
1.00
15.45
B


ATOM
2668
CD1
PHE
B
761
18.904
−14.516
0.957
1.00
15.98
B


ATOM
2669
CD2
PHE
B
761
19.745
−13.643
−1.110
1.00
14.81
B


ATOM
2670
CE1
PHE
B
761
18.028
−15.343
0.261
1.00
16.60
B


ATOM
2671
CE2
PHE
B
761
18.867
−14.470
−1.815
1.00
15.63
B


ATOM
2672
CZ
PHE
B
761
18.009
−15.319
−1.125
1.00
14.90
B


ATOM
2673
C
PHE
B
761
22.907
−13.922
1.116
1.00
15.74
B


ATOM
2674
O
PHE
B
761
23.038
−15.110
0.812
1.00
15.94
B


ATOM
2675
N
GLY
B
762
23.788
−12.986
0.767
1.00
14.42
B


ATOM
2676
CA
GLY
B
762
24.979
−13.330
0.003
1.00
15.82
B


ATOM
2677
C
GLY
B
762
25.858
−14.267
0.822
1.00
15.85
B


ATOM
2678
O
GLY
B
762
26.462
−15.198
0.293
1.00
15.53
B


ATOM
2679
N
LEU
B
763
25.934
−14.005
2.123
1.00
13.94
B


ATOM
2680
CA
LEU
B
763
26.709
−14.838
3.033
1.00
14.37
B


ATOM
2681
CB
LEU
B
763
26.599
−14.290
4.460
1.00
14.34
B


ATOM
2682
CG
LEU
B
763
26.948
−15.255
5.596
1.00
13.19
B


ATOM
2683
CD1
LEU
B
763
28.420
−15.626
5.511
1.00
13.63
B


ATOM
2684
CD2
LEU
B
763
26.631
−14.599
6.948
1.00
14.36
B


ATOM
2685
C
LEU
B
763
26.163
−16.270
2.985
1.00
13.49
B


ATOM
2686
O
LEU
B
763
26.921
−17.244
2.939
1.00
13.17
B


ATOM
2687
N
GLY
B
764
24.841
−16.392
2.992
1.00
13.47
B


ATOM
2688
CA
GLY
B
764
24.230
−17.708
2.943
1.00
15.22
B


ATOM
2689
C
GLY
B
764
24.621
−18.453
1.677
1.00
16.83
B


ATOM
2690
O
GLY
B
764
24.932
−19.647
1.718
1.00
14.60
B


ATOM
2691
N
TRP
B
765
24.615
−17.747
0.550
1.00
15.62
B


ATOM
2692
CA
TRP
B
765
24.974
−18.360
−0.729
1.00
16.29
B


ATOM
2693
CB
TRP
B
765
24.776
−17.364
−1.877
1.00
17.83
B


ATOM
2694
CG
TRP
B
765
25.067
−17.960
−3.226
1.00
19.06
B


ATOM
2695
CD2
TRP
B
765
24.298
−18.961
−3.901
1.00
21.11
B


ATOM
2696
CE2
TRP
B
765
24.981
−19.278
−5.097
1.00
22.22
B


ATOM
2697
CE3
TRP
B
765
23.099
−19.625
−3.610
1.00
20.70
B


ATOM
2698
CD1
TRP
B
765
26.149
−17.711
−4.017
1.00
21.91
B


ATOM
2699
NE1
TRP
B
765
26.107
−18.500
−5.146
1.00
21.48
B


ATOM
2700
CZ2
TRP
B
765
24.504
−20.231
−6.003
1.00
20.86
B


ATOM
2701
CZ3
TRP
B
765
22.625
−20.574
−4.515
1.00
21.28
B


ATOM
2702
CH2
TRP
B
765
23.331
−20.866
−5.695
1.00
20.63
B


ATOM
2703
C
TRP
B
765
26.413
−18.863
−0.727
1.00
14.88
B


ATOM
2704
O
TRP
B
765
26.676
−20.009
−1.079
1.00
14.96
B


ATOM
2705
N
ARG
B
766
27.350
−18.010
−0.329
1.00
15.86
B


ATOM
2706
CA
ARG
B
766
28.755
−18.414
−0.293
1.00
15.20
B


ATOM
2707
CB
ARG
B
766
29.645
−17.219
0.059
1.00
15.13
B


ATOM
2708
CG
ARG
B
766
29.681
−16.130
−1.027
1.00
14.72
B


ATOM
2709
CD
ARG
B
766
30.770
−15.102
−0.715
1.00
17.05
B


ATOM
2710
NE
ARG
B
766
30.520
−14.418
0.553
1.00
15.75
B


ATOM
2711
CZ
ARG
B
766
29.649
−13.424
0.706
1.00
17.31
B


ATOM
2712
NH1
ARG
B
766
28.939
−12.992
−0.327
1.00
14.99
B


ATOM
2713
NH2
ARG
B
766
29.499
−12.847
1.889
1.00
15.66
B


ATOM
2714
C
ARG
B
766
29.031
−19.569
0.678
1.00
14.85
B


ATOM
2715
O
ARG
B
766
29.819
−20.463
0.371
1.00
15.12
B


ATOM
2716
N
SER
B
767
28.396
−19.556
1.846
1.00
14.72
B


ATOM
2717
CA
SER
B
767
28.605
−20.623
2.826
1.00
15.93
B


ATOM
2718
CB
SER
B
767
27.876
−20.284
4.128
1.00
16.70
B


ATOM
2719
OG
SER
B
767
28.307
−19.035
4.638
1.00
17.22
B


ATOM
2720
C
SER
B
767
28.071
−21.941
2.253
1.00
16.52
B


ATOM
2721
O
SER
B
767
28.680
−23.007
2.397
1.00
17.28
B


ATOM
2722
N
TYR
B
768
26.918
−21.842
1.604
1.00
16.21
B


ATOM
2723
CA
TYR
B
768
26.255
−22.969
0.966
1.00
15.35
B


ATOM
2724
CB
TYR
B
768
24.914
−22.476
0.405
1.00
16.96
B


ATOM
2725
CG
TYR
B
768
24.224
−23.359
−0.615
1.00
17.34
B


ATOM
2726
CD1
TYR
B
768
23.962
−24.707
−0.358
1.00
16.25
B


ATOM
2727
CE1
TYR
B
768
23.226
−25.481
−1.263
1.00
16.76
B


ATOM
2728
CD2
TYR
B
768
23.742
−22.811
−1.805
1.00
17.37
B


ATOM
2729
CE2
TYR
B
768
23.009
−23.569
−2.705
1.00
17.14
B


ATOM
2730
CZ
TYR
B
768
22.749
−24.896
−2.432
1.00
16.64
B


ATOM
2731
OH
TYR
B
768
21.970
−25.608
−3.309
1.00
17.70
B


ATOM
2732
C
TYR
B
768
27.148
−23.536
−0.140
1.00
17.02
B


ATOM
2733
O
TYR
B
768
27.427
−24.737
−0.174
1.00
16.79
B


ATOM
2734
N
LYS
B
769
27.627
−22.665
−1.021
1.00
14.67
B


ATOM
2735
CA
LYS
B
769
28.474
−23.086
−2.132
1.00
16.86
B


ATOM
2736
CB
LYS
B
769
28.599
−21.944
−3.151
1.00
16.98
B


ATOM
2737
CG
LYS
B
769
27.302
−21.576
−3.852
1.00
18.50
B


ATOM
2738
CD
LYS
B
769
26.917
−22.586
−4.943
1.00
19.38
B


ATOM
2739
CE
LYS
B
769
27.840
−22.500
−6.161
1.00
17.86
B


ATOM
2740
NZ
LYS
B
769
27.399
−23.425
−7.249
1.00
15.11
B


ATOM
2741
C
LYS
B
769
29.885
−23.579
−1.782
1.00
18.73
B


ATOM
2742
O
LYS
B
769
30.337
−24.590
−2.318
1.00
18.48
B


ATOM
2743
N
HIS
B
770
30.577
−22.874
−0.889
1.00
17.78
B


ATOM
2744
CA
HIS
B
770
31.961
−23.219
−0.546
1.00
18.94
B


ATOM
2745
CB
HIS
B
770
32.750
−21.937
−0.241
1.00
20.02
B


ATOM
2746
CG
HIS
B
770
32.825
−20.982
−1.391
1.00
21.63
B


ATOM
2747
CD2
HIS
B
770
32.090
−19.883
−1.685
1.00
21.95
B


ATOM
2748
ND1
HIS
B
770
33.712
−21.142
−2.434
1.00
22.29
B


ATOM
2749
CE1
HIS
B
770
33.517
−20.183
−3.324
1.00
23.77
B


ATOM
2750
NE2
HIS
B
770
32.539
−19.407
−2.894
1.00
23.71
B


ATOM
2751
C
HIS
B
770
32.214
−24.202
0.592
1.00
19.97
B


ATOM
2752
O
HIS
B
770
33.203
−24.935
0.564
1.00
19.99
B


ATOM
2753
N
VAL
B
771
31.341
−24.212
1.592
1.00
19.79
B


ATOM
2754
CA
VAL
B
771
31.532
−25.080
2.746
1.00
20.09
B


ATOM
2755
CB
VAL
B
771
31.993
−24.242
3.968
1.00
21.67
B


ATOM
2756
CG1
VAL
B
771
33.355
−23.626
3.691
1.00
21.97
B


ATOM
2757
CG2
VAL
B
771
30.988
−23.132
4.246
1.00
22.98
B


ATOM
2758
C
VAL
B
771
30.274
−25.864
3.110
1.00
19.76
B


ATOM
2759
O
VAL
B
771
30.047
−26.194
4.280
1.00
20.09
B


ATOM
2760
N
SER
B
772
29.465
−26.162
2.099
1.00
17.17
B


ATOM
2761
CA
SER
B
772
28.225
−26.903
2.294
1.00
18.29
B


ATOM
2762
CB
SER
B
772
28.539
−28.381
2.525
1.00
18.92
B


ATOM
2763
OG
SER
B
772
29.220
−28.907
1.397
1.00
20.36
B


ATOM
2764
C
SER
B
772
27.370
−26.361
3.433
1.00
17.67
B


ATOM
2765
O
SER
B
772
26.645
−27.116
4.092
1.00
17.83
B


ATOM
2766
N
GLY
B
773
27.448
−25.049
3.651
1.00
16.98
B


ATOM
2767
CA
GLY
B
773
26.665
−24.407
4.700
1.00
18.02
B


ATOM
2768
C
GLY
B
773
27.068
−24.727
6.134
1.00
19.19
B


ATOM
2769
O
GLY
B
773
26.385
−24.322
7.080
1.00
19.19
B


ATOM
2770
N
GLN
B
774
28.181
−25.436
6.307
1.00
18.16
B


ATOM
2771
CA
GLN
B
774
28.637
−25.820
7.640
1.00
18.57
B


ATOM
2772
CB
GLN
B
774
29.293
−27.200
7.579
1.00
18.50
B


ATOM
2773
CG
GLN
B
774
28.375
−28.248
6.987
1.00
22.02
B


ATOM
2774
CD
GLN
B
774
27.010
−28.250
7.647
1.00
26.61
B


ATOM
2775
OE1
GLN
B
774
26.879
−28.545
8.841
1.00
27.59
B


ATOM
2776
NE2
GLN
B
774
25.980
−27.907
6.875
1.00
28.16
B


ATOM
2777
C
GLN
B
774
29.566
−24.817
8.328
1.00
19.18
B


ATOM
2778
O
GLN
B
774
29.995
−25.033
9.460
1.00
18.70
B


ATOM
2779
N
MET
B
775
29.879
−23.730
7.634
1.00
17.50
B


ATOM
2780
CA
MET
B
775
30.705
−22.653
8.176
1.00
18.41
B


ATOM
2781
CB
MET
B
775
32.182
−22.814
7.790
1.00
19.65
B


ATOM
2782
CG
MET
B
775
32.922
−23.895
8.558
1.00
23.25
B


ATOM
2783
SD
MET
B
775
34.702
−23.859
8.249
1.00
27.85
B


ATOM
2784
CE
MET
B
775
35.070
−25.630
8.200
1.00
29.77
B


ATOM
2785
C
MET
B
775
30.159
−21.370
7.569
1.00
16.57
B


ATOM
2786
O
MET
B
775
29.460
−21.414
6.559
1.00
15.67
B


ATOM
2787
N
LEU
B
776
30.452
−20.233
8.189
1.00
16.83
B


ATOM
2788
CA
LEU
B
776
29.976
−18.963
7.657
1.00
15.86
B


ATOM
2789
CB
LEU
B
776
29.558
−18.022
8.797
1.00
15.81
B


ATOM
2790
CG
LEU
B
776
28.302
−18.480
9.556
1.00
15.03
B


ATOM
2791
CD1
LEU
B
776
27.886
−17.440
10.586
1.00
16.94
B


ATOM
2792
CD2
LEU
B
776
27.167
−18.709
8.565
1.00
17.07
B


ATOM
2793
C
LEU
B
776
31.089
−18.355
6.817
1.00
16.39
B


ATOM
2794
O
LEU
B
776
32.086
−17.856
7.342
1.00
16.45
B


ATOM
2795
N
TYR
B
777
30.907
−18.421
5.502
1.00
15.59
B


ATOM
2796
CA
TYR
B
777
31.885
−17.923
4.544
1.00
14.70
B


ATOM
2797
CB
TYR
B
777
31.792
−18.764
3.264
1.00
16.31
B


ATOM
2798
CG
TYR
B
777
32.970
−18.650
2.316
1.00
18.23
B


ATOM
2799
CD1
TYR
B
777
33.118
−17.544
1.476
1.00
19.16
B


ATOM
2800
CE1
TYR
B
777
34.175
−17.469
0.559
1.00
19.47
B


ATOM
2801
CD2
TYR
B
777
33.910
−19.676
2.222
1.00
19.79
B


ATOM
2802
CE2
TYR
B
777
34.969
−19.610
1.307
1.00
18.50
B


ATOM
2803
CZ
TYR
B
777
35.091
−18.509
0.480
1.00
18.83
B


ATOM
2804
OH
TYR
B
777
36.109
−18.463
−0.446
1.00
19.32
B


ATOM
2805
C
TYR
B
777
31.662
−16.441
4.236
1.00
16.02
B


ATOM
2806
O
TYR
B
777
31.095
−16.089
3.200
1.00
13.24
B


ATOM
2807
N
PHE
B
778
32.098
−15.578
5.149
1.00
15.22
B


ATOM
2808
CA
PHE
B
778
31.950
−14.141
4.953
1.00
16.74
B


ATOM
2809
CB
PHE
B
778
32.370
−13.377
6.217
1.00
14.02
B


ATOM
2810
CG
PHE
B
778
31.427
−13.571
7.382
1.00
16.42
B


ATOM
2811
CD1
PHE
B
778
31.654
−14.568
8.328
1.00
17.13
B


ATOM
2812
CD2
PHE
B
778
30.282
−12.784
7.504
1.00
16.49
B


ATOM
2813
CE1
PHE
B
778
30.752
−14.779
9.382
1.00
17.43
B


ATOM
2814
CE2
PHE
B
778
29.374
−12.986
8.553
1.00
17.31
B


ATOM
2815
CZ
PHE
B
778
29.612
−13.987
9.493
1.00
16.02
B


ATOM
2816
C
PHE
B
778
32.798
−13.719
3.758
1.00
16.59
B


ATOM
2817
O
PHE
B
778
32.343
−12.974
2.887
1.00
18.01
B


ATOM
2818
N
ALA
B
779
34.028
−14.216
3.714
1.00
17.78
B


ATOM
2819
CA
ALA
B
779
34.940
−13.918
2.620
1.00
19.19
B


ATOM
2820
CB
ALA
B
779
35.589
−12.556
2.833
1.00
18.30
B


ATOM
2821
C
ALA
B
779
36.010
−15.004
2.550
1.00
20.69
B


ATOM
2822
O
ALA
B
779
36.133
−15.832
3.456
1.00
19.06
B


ATOM
2823
N
PRO
B
780
36.790
−15.028
1.462
1.00
22.12
B


ATOM
2824
CD
PRO
B
780
36.645
−14.287
0.196
1.00
22.83
B


ATOM
2825
CA
PRO
B
780
37.834
−16.050
1.353
1.00
22.26
B


ATOM
2826
CB
PRO
B
780
38.468
−15.747
−0.004
1.00
23.89
B


ATOM
2827
CG
PRO
B
780
37.306
−15.222
−0.795
1.00
25.92
B


ATOM
2828
C
PRO
B
780
38.838
−15.949
2.502
1.00
22.45
B


ATOM
2829
O
PRO
B
780
39.424
−16.950
2.916
1.00
22.14
B


ATOM
2830
N
ASP
B
781
39.014
−14.740
3.029
1.00
21.57
B


ATOM
2831
CA
ASP
B
781
39.954
−14.512
4.126
1.00
21.92
B


ATOM
2832
CB
ASP
B
781
40.814
−13.282
3.820
1.00
23.49
B


ATOM
2833
CG
ASP
B
781
39.991
−12.017
3.661
1.00
24.54
B


ATOM
2834
OD1
ASP
B
781
38.772
−12.117
3.393
1.00
22.71
B


ATOM
2835
OD2
ASP
B
781
40.571
−10.920
3.795
1.00
24.49
B


ATOM
2836
C
ASP
B
781
39.267
−14.340
5.476
1.00
21.74
B


ATOM
2837
O
ASP
B
781
39.888
−13.917
6.451
1.00
22.77
B


ATOM
2838
N
LEU
B
782
37.979
−14.664
5.526
1.00
20.36
B


ATOM
2839
CA
LEU
B
782
37.210
−14.557
6.756
1.00
19.59
B


ATOM
2840
CB
LEU
B
782
36.619
−13.151
6.893
1.00
20.63
B


ATOM
2841
CG
LEU
B
782
35.970
−12.802
8.232
1.00
22.29
B


ATOM
2842
CD1
LEU
B
782
36.949
−13.088
9.370
1.00
25.24
B


ATOM
2843
CD2
LEU
B
782
35.567
−11.325
8.237
1.00
21.90
B


ATOM
2844
C
LEU
B
782
36.095
−15.603
6.761
1.00
19.08
B


ATOM
2845
O
LEU
B
782
34.954
−15.320
6.389
1.00
15.84
B


ATOM
2846
N
ILE
B
783
36.452
−16.815
7.179
1.00
18.17
B


ATOM
2847
CA
ILE
B
783
35.525
−17.941
7.257
1.00
17.98
B


ATOM
2848
CB
ILE
B
783
36.062
−19.142
6.446
1.00
17.80
B


ATOM
2849
CG2
ILE
B
783
35.093
−20.311
6.551
1.00
20.50
B


ATOM
2850
CG1
ILE
B
783
36.282
−18.723
4.988
1.00
18.65
B


ATOM
2851
CD1
ILE
B
783
37.092
−19.720
4.155
1.00
20.07
B


ATOM
2852
C
ILE
B
783
35.407
−18.340
8.725
1.00
19.08
B


ATOM
2853
O
ILE
B
783
36.402
−18.697
9.358
1.00
19.55
B


ATOM
2854
N
LEU
B
784
34.200
−18.289
9.269
1.00
19.91
B


ATOM
2855
CA
LEU
B
784
34.021
−18.618
10.676
1.00
22.66
B


ATOM
2856
CB
LEU
B
784
33.276
−17.490
11.401
1.00
21.59
B


ATOM
2857
CG
LEU
B
784
33.858
−16.076
11.358
1.00
24.80
B


ATOM
2858
CD1
LEU
B
784
32.937
−15.138
12.135
1.00
23.29
B


ATOM
2859
CD2
LEU
B
784
35.257
−16.062
11.941
1.00
24.21
B


ATOM
2860
C
LEU
B
784
33.291
−19.917
10.953
1.00
24.35
B


ATOM
2861
O
LEU
B
784
32.305
−20.251
10.300
1.00
22.70
B


ATOM
2862
N
ASN
B
785
33.799
−20.645
11.939
1.00
26.14
B


ATOM
2863
CA
ASN
B
785
33.186
−21.885
12.376
1.00
28.52
B


ATOM
2864
CB
ASN
B
785
34.158
−23.058
12.240
1.00
30.54
B


ATOM
2865
CG
ASN
B
785
35.509
−22.761
12.841
1.00
31.69
B


ATOM
2866
OD1
ASN
B
785
35.606
−22.104
13.875
1.00
33.80
B


ATOM
2867
ND2
ASN
B
785
36.564
−23.253
12.204
1.00
34.71
B


ATOM
2868
C
ASN
B
785
32.835
−21.648
13.843
1.00
29.93
B


ATOM
2869
O
ASN
B
785
33.155
−20.597
14.409
1.00
28.08
B


ATOM
2870
N
GLU
B
785
32.190
−22.625
14.458
1.00
31.08
B


ATOM
2871
CA
GLU
B
786
31.771
−22.516
15.845
1.00
33.20
B


ATOM
2872
CB
GLU
B
786
31.169
−23.849
16.286
1.00
37.40
B


ATOM
2873
CG
GLU
B
786
30.217
−23.750
17.455
1.00
42.11
B


ATOM
2874
CD
GLU
B
786
29.476
−25.050
17.696
1.00
46.15
B


ATOM
2875
OE1
GLU
B
786
28.841
−25.555
16.743
1.00
46.80
B


ATOM
2876
OE2
GLU
B
786
29.529
−25.563
18.836
1.00
48.79
B


ATOM
2877
C
GLU
B
786
32.862
−22.088
16.830
1.00
32.26
B


ATOM
2878
O
GLU
B
786
32.624
−21.246
17.696
1.00
31.14
B


ATOM
2879
N
GLN
B
787
34.058
−22.651
16.692
1.00
32.38
B


ATOM
2880
CA
GLN
B
787
35.151
−22.332
17.604
1.00
34.18
B


ATOM
2881
CB
GLN
B
787
36.353
−23.235
17.327
1.00
37.31
B


ATOM
2882
CG
GLN
B
787
37.302
−22.693
16.275
1.00
41.80
B


ATOM
2883
CD
GLN
B
787
38.555
−23.530
16.137
1.00
45.28
B


ATOM
2884
OE1
GLN
B
787
39.524
−23.116
15.497
1.00
47.58
B


ATOM
2885
NE2
GLN
B
787
38.542
−24.722
16.733
1.00
48.17
B


ATOM
2886
C
GLN
B
787
35.609
−20.876
17.558
1.00
34.13
B


ATOM
2887
O
GLN
B
787
36.198
−20.377
18.518
1.00
33.23
B


ATOM
2888
N
ARG
B
788
35.355
−20.200
16.441
1.00
32.22
B


ATOM
2889
CA
ARG
B
788
35.767
−18.810
16.294
1.00
31.78
B


ATOM
2890
CB
ARG
B
788
36.169
−18.528
14.842
1.00
31.05
B


ATOM
2891
CG
ARG
B
788
37.322
−19.393
14.343
1.00
32.23
B


ATOM
2892
CD
ARG
B
788
37.772
−18.988
12.938
1.00
32.79
B


ATOM
2893
NE
ARG
B
788
38.365
−17.652
12.923
1.00
33.62
B


ATOM
2894
CZ
ARG
B
788
38.815
−17.036
11.831
1.00
35.26
B


ATOM
2895
NH1
ARG
B
788
38.742
−17.630
10.643
1.00
32.75
B


ATOM
2896
NH2
ARG
B
788
39.349
−15.824
11.929
1.00
33.61
B


ATOM
2897
C
ARG
B
788
34.670
−17.847
16.733
1.00
31.36
B


ATOM
2898
O
ARG
B
788
34.773
−16.637
16.532
1.00
32.48
B


ATOM
2899
N
MET
B
789
33.621
−18.398
17.334
1.00
30.68
B


ATOM
2900
CA
MET
B
789
32.490
−17.613
17.824
1.00
31.24
B


ATOM
2901
CB
MET
B
789
31.200
−18.116
17.178
1.00
29.02
B


ATOM
2902
CG
MET
B
789
31.266
−18.136
15.660
1.00
29.15
B


ATOM
2903
SD
MET
B
789
29.905
−19.023
14.891
1.00
27.19
B


ATOM
2904
CE
MET
B
789
30.378
−18.882
13.161
1.00
27.27
B


ATOM
2905
C
MET
B
789
32.430
−17.787
19.339
1.00
31.40
B


ATOM
2906
O
MET
B
789
31.528
−18.433
19.870
1.00
31.70
B


ATOM
2907
N
LYS
B
790
33.404
−17.197
20.023
1.00
33.04
B


ATOM
2908
CA
LYS
B
790
33.520
−17.297
21.474
1.00
34.21
B


ATOM
2909
CB
LYS
B
790
34.887
−16.759
21.894
1.00
33.75
B


ATOM
2910
CG
LYS
B
790
36.030
−17.429
21.141
1.00
34.59
B


ATOM
2911
CD
LYS
B
790
37.368
−16.763
21.407
1.00
35.73
B


ATOM
2912
CE
LYS
B
790
38.469
−17.425
20.588
1.00
37.42
B


ATOM
2913
NZ
LYS
B
790
39.785
−16.747
20.754
1.00
39.03
B


ATOM
2914
C
LYS
B
790
32.407
−16.605
22.262
1.00
36.08
B


ATOM
2915
O
LYS
B
790
31.732
−17.241
23.070
1.00
35.56
B


ATOM
2916
N
GLU
B
791
32.222
−15.308
22.033
1.00
37.31
B


ATOM
2917
CA
GLU
B
791
31.186
−14.545
22.728
1.00
39.12
B


ATOM
2918
CB
GLU
B
791
31.231
−13.080
22.288
1.00
41.76
B


ATOM
2919
CG
GLU
B
791
31.625
−12.115
23.390
1.00
47.66
B


ATOM
2920
CD
GLU
B
791
30.594
−12.053
24.508
1.00
50.47
B


ATOM
2921
OE1
GLU
B
791
29.437
−11.657
24.237
1.00
51.08
B


ATOM
2922
OE2
GLU
B
791
30.942
−12.401
25.659
1.00
52.17
B


ATOM
2923
C
GLU
B
791
29.804
−15.128
22.445
1.00
38.82
B


ATOM
2924
O
GLU
B
791
29.383
−15.221
21.292
1.00
39.17
B


ATOM
2925
N
SER
B
792
29.099
−15.513
23.504
1.00
37.75
B


ATOM
2926
CA
SER
B
792
27.770
−16.102
23.373
1.00
37.53
B


ATOM
2927
CB
SER
B
792
27.191
−16.390
24.760
1.00
39.01
B


ATOM
2928
OG
SER
B
792
27.172
−15.215
25.549
1.00
41.88
B


ATOM
2929
C
SER
B
792
26.803
−15.220
22.587
1.00
36.19
B


ATOM
2930
O
SER
B
792
25.936
−15.720
21.869
1.00
35.18
B


ATOM
2931
N
SER
B
793
26.955
−13.908
22.736
1.00
35.25
B


ATOM
2932
CA
SER
B
793
26.102
−12.948
22.046
1.00
34.13
B


ATOM
2933
CB
SER
B
793
26.415
−11.535
22.542
1.00
35.74
B


ATOM
2934
OG
SER
B
793
25.504
−10.594
22.006
1.00
40.72
B


ATOM
2935
C
SER
B
793
26.339
−13.033
20.539
1.00
32.40
B


ATOM
2936
O
SER
B
793
25.397
−13.100
19.749
1.00
30.32
B


ATOM
2937
N
PHE
B
794
27.611
−13.029
20.158
1.00
31.57
B


ATOM
2938
CA
PHE
B
794
28.010
−13.111
18.759
1.00
31.79
B


ATOM
2939
CB
PHE
B
794
29.517
−12.856
18.636
1.00
33.58
B


ATOM
2940
CG
PHE
B
794
30.024
−12.869
17.222
1.00
36.88
B


ATOM
2941
CD1
PHE
B
794
29.579
−11.926
16.300
1.00
37.56
B


ATOM
2942
CD2
PHE
B
794
30.950
−13.825
16.812
1.00
38.13
B


ATOM
2943
CE1
PHE
B
794
30.048
−11.932
14.986
1.00
38.39
B


ATOM
2944
CE2
PHE
B
794
31.426
−13.841
15.500
1.00
39.25
B


ATOM
2945
CZ
PHE
B
794
30.973
−12.890
14.585
1.00
39.67
B


ATOM
2946
C
PHE
B
794
27.664
−14.487
18.194
1.00
30.57
B


ATOM
2947
O
PHE
B
794
27.281
−14.615
17.030
1.00
29.77
B


ATOM
2948
N
TYR
B
795
27.794
−15.516
19.026
1.00
29.44
B


ATOM
2949
CA
TYR
B
795
27.490
−16.876
18.606
1.00
27.92
B


ATOM
2950
CB
TYR
B
795
27.872
−17.872
19.709
1.00
31.37
B


ATOM
2951
CG
TYR
B
795
27.579
−19.317
19.357
1.00
33.31
B


ATOM
2952
CD1
TYR
B
795
28.001
−19.860
18.141
1.00
34.81
B


ATOM
2953
CE1
TYR
B
795
27.732
−21.185
17.807
1.00
35.57
B


ATOM
2954
CD2
TYR
B
795
26.878
−20.142
20.237
1.00
35.46
B


ATOM
2955
CE2
TYR
B
795
26.603
−21.473
19.913
1.00
36.78
B


ATOM
2956
CZ
TYR
B
795
27.032
−21.984
18.697
1.00
36.92
B


ATOM
2957
OH
TYR
B
795
26.752
−23.288
18.365
1.00
39.48
B


ATOM
2958
C
TYR
B
795
26.008
−17.008
18.267
1.00
26.49
B


ATOM
2959
O
TYR
B
795
25.644
−17.624
17.268
1.00
23.95
B


ATOM
2960
N
SER
B
796
25.150
−16.423
19.095
1.00
25.20
B


ATOM
2961
CA
SER
B
796
23.716
−16.492
18.847
1.00
26.93
B


ATOM
2962
CB
SER
B
796
22.941
−15.864
20.006
1.00
28.16
B


ATOM
2963
OG
SER
B
796
23.161
−16.592
21.200
1.00
30.73
B


ATOM
2964
C
SER
B
796
23.374
−15.770
17.548
1.00
25.62
B


ATOM
2965
O
SER
B
796
22.499
−16.195
16.795
1.00
25.30
B


ATOM
2966
N
LEU
B
797
24.074
−14.673
17.296
1.00
24.05
B


ATOM
2967
CA
LEU
B
797
23.851
−13.893
16.088
1.00
25.18
B


ATOM
2968
CB
LEU
B
797
24.720
−12.638
16.112
1.00
24.29
B


ATOM
2969
CG
LEU
B
797
24.429
−11.600
15.027
1.00
27.01
B


ATOM
2970
CD1
LEU
B
797
23.024
−11.043
15.197
1.00
27.55
B


ATOM
2971
CD2
LEU
B
797
25.447
−10.491
15.128
1.00
28.99
B


ATOM
2972
C
LEU
B
797
24.196
−14.744
14.870
1.00
22.79
B


ATOM
2973
O
LEU
B
797
23.429
−14.809
13.907
1.00
23.34
B


ATOM
2974
N
CYS
B
798
25.354
−15.397
14.920
1.00
22.06
B


ATOM
2975
CA
CYS
B
798
25.792
−16.253
13.826
1.00
21.40
B


ATOM
2976
CB
CYS
B
798
27.205
−16.777
14.102
1.00
22.48
B


ATOM
2977
SG
CYS
B
798
28.482
−15.490
14.048
1.00
23.41
B


ATOM
2978
C
CYS
B
798
24.817
−17.414
13.613
1.00
21.32
B


ATOM
2979
O
CYS
B
798
24.535
−17.793
12.473
1.00
20.28
B


ATOM
2980
N
LEU
B
799
24.306
−17.981
14.702
1.00
19.81
B


ATOM
2981
CA
LEU
B
799
23.341
−19.069
14.588
1.00
19.74
B


ATOM
2982
CB
LEU
B
799
22.899
−19.559
15.970
1.00
23.55
B


ATOM
2983
CG
LEU
B
799
23.890
−20.438
16.740
1.00
24.38
B


ATOM
2984
CD1
LEU
B
799
23.279
−20.850
18.077
1.00
26.86
B


ATOM
2985
CD2
LEU
B
799
24.226
−21.674
15.911
1.00
26.58
B


ATOM
2986
C
LEU
B
799
22.135
−18.550
13.818
1.00
20.29
B


ATOM
2987
O
LEU
B
799
21.563
−19.255
12.990
1.00
20.26
B


ATOM
2988
N
THR
B
800
21.756
−17.304
14.086
1.00
20.04
B


ATOM
2989
CA
THR
B
800
20.629
−16.703
13.387
1.00
20.32
B


ATOM
2990
CB
THR
B
800
20.289
−15.308
13.967
1.00
21.13
B


ATOM
2991
OG1
THR
B
800
19.814
−15.453
15.312
1.00
19.83
B


ATOM
2992
CG2
THR
B
800
19.218
−14.620
13.131
1.00
21.16
B


ATOM
2993
C
THR
B
800
20.937
−16.574
11.893
1.00
19.37
B


ATOM
2994
O
THR
B
800
20.098
−16.882
11.049
1.00
20.15
B


ATOM
2995
N
MET
B
801
22.140
−16.119
11.564
1.00
18.98
B


ATOM
2996
CA
MET
B
801
22.518
−15.969
10.160
1.00
20.07
B


ATOM
2997
CB
MET
B
801
23.854
−15.229
10.042
1.00
20.74
B


ATOM
2998
CG
MET
B
801
23.833
−13.802
10.575
1.00
20.42
B


ATOM
2999
SD
MET
B
801
25.357
−12.924
10.203
1.00
24.80
B


ATOM
3000
CE
MET
B
801
26.385
−13.408
11.562
1.00
25.72
B


ATOM
3001
C
MET
B
801
22.636
−17.336
9.489
1.00
19.47
B


ATOM
3002
O
MET
B
801
22.326
−17.491
8.310
1.00
17.79
B


ATOM
3003
N
TRP
B
802
23.075
−18.321
10.264
1.00
20.79
B


ATOM
3004
CA
TRP
B
802
23.266
−19.690
9.792
1.00
21.60
B


ATOM
3005
CB
TRP
B
802
23.788
−20.550
10.942
1.00
22.91
B


ATOM
3006
CG
TRP
B
802
24.985
−21.360
10.590
1.00
24.57
B


ATOM
3007
CD2
TRP
B
802
26.211
−21.434
11.323
1.00
25.80
B


ATOM
3008
CE2
TRP
B
802
27.069
−22.304
10.613
1.00
25.69
B


ATOM
3009
CE3
TRP
B
802
26.670
−20.847
12.511
1.00
26.80
B


ATOM
3010
CD1
TRP
B
802
25.140
−22.168
9.497
1.00
25.78
B


ATOM
3011
NE1
TRP
B
802
26.390
−22.738
9.506
1.00
25.97
B


ATOM
3012
CZ2
TRP
B
802
28.365
−22.603
11.053
1.00
27.76
B


ATOM
3013
CZ3
TRP
B
802
27.962
−21.145
12.949
1.00
26.64
B


ATOM
3014
CH2
TRP
B
802
28.792
−22.015
12.219
1.00
27.43
B


ATOM
3015
C
TRP
B
802
22.005
−20.345
9.227
1.00
21.64
B


ATOM
3016
O
TRP
B
802
22.085
−21.309
8.463
1.00
20.67
B


ATOM
3017
N
GLN
B
803
20.842
−19.835
9.617
1.00
21.08
B


ATOM
3018
CA
GLN
B
803
19.575
−20.396
9.161
1.00
20.48
B


ATOM
3019
CB
GLN
B
803
18.416
−19.663
9.824
1.00
21.39
B


ATOM
3020
CG
GLN
B
803
18.558
−19.535
11.323
1.00
23.58
B


ATOM
3021
CD
GLN
B
803
17.428
−18.743
11.932
1.00
27.19
B


ATOM
3022
OE1
GLN
B
803
16.344
−19.274
12.181
1.00
29.06
B


ATOM
3023
NE2
GLN
B
803
17.666
−17.460
12.159
1.00
28.68
B


ATOM
3024
C
GLN
B
803
19.412
−20.321
7.651
1.00
21.76
B


ATOM
3025
O
GLN
B
803
18.786
−21.191
7.039
1.00
21.16
B


ATOM
3026
N
ILE
B
804
19.964
−19.274
7.048
1.00
20.31
B


ATOM
3027
CA
ILE
B
804
19.849
−19.107
5.611
1.00
19.18
B


ATOM
3028
CB
ILE
B
804
20.336
−17.704
5.184
1.00
18.04
B


ATOM
3029
CG2
ILE
B
804
20.227
−17.550
3.674
1.00
17.29
B


ATOM
3030
CG1
ILE
B
804
19.478
−16.633
5.875
1.00
19.81
B


ATOM
3031
CD1
ILE
B
804
19.859
−15.195
5.524
1.00
20.17
B


ATOM
3032
C
ILE
B
804
20.602
−20.206
4.849
1.00
20.03
B


ATOM
3033
O
ILE
B
804
20.019
−20.884
4.005
1.00
21.05
B


ATOM
3034
N
PRO
B
805
21.901
−20.400
5.137
1.00
20.99
B


ATOM
3035
CD
PRO
B
805
22.753
−19.671
6.094
1.00
20.74
B


ATOM
3036
CA
PRO
B
805
22.667
−21.446
4.440
1.00
21.50
B


ATOM
3037
CB
PRO
B
805
24.037
−21.390
5.117
1.00
22.20
B


ATOM
3038
CG
PRO
B
805
24.136
−19.979
5.600
1.00
22.08
B


ATOM
3039
C
PRO
B
805
21.998
−22.807
4.649
1.00
22.88
B


ATOM
3040
O
PRO
B
805
21.897
−23.624
3.730
1.00
22.43
B


ATOM
3041
N
GLN
B
806
21.547
−23.041
5.877
1.00
22.24
B


ATOM
3042
CA
GLN
B
806
20.886
−24.291
6.227
1.00
22.01
B


ATOM
3043
CB
GLN
B
806
20.511
−24.280
7.712
1.00
23.12
B


ATOM
3044
CG
GLN
B
806
21.732
−24.418
8.616
1.00
27.21
B


ATOM
3045
CD
GLN
B
806
21.452
−24.120
10.079
1.00
31.98
B


ATOM
3046
OE1
GLN
B
806
22.295
−24.379
10.939
1.00
37.38
B


ATOM
3047
NE2
GLN
B
806
20.276
−23.569
10.370
1.00
32.65
B


ATOM
3048
C
GLN
B
806
19.656
−24.528
5.356
1.00
23.33
B


ATOM
3049
O
GLN
B
806
19.443
−25.639
4.872
1.00
23.30
B


ATOM
3050
N
GLU
B
807
18.855
−23.487
5.144
1.00
21.25
B


ATOM
3051
CA
GLU
B
807
17.662
−23.611
4.306
1.00
21.78
B


ATOM
3052
CB
GLU
B
807
16.770
−22.375
4.441
1.00
25.31
B


ATOM
3053
CG
GLU
B
807
15.931
−22.353
5.698
1.00
29.26
B


ATOM
3054
CD
GLU
B
807
14.962
−23.520
5.762
1.00
32.50
B


ATOM
3055
OE1
GLU
B
807
14.077
−23.606
4.887
1.00
33.09
B


ATOM
3056
OE2
GLU
B
807
15.092
−24.353
6.684
1.00
32.53
B


ATOM
3057
C
GLU
B
807
18.043
−23.805
2.843
1.00
20.58
B


ATOM
3058
O
GLU
B
807
17.354
−24.519
2.108
1.00
19.42
B


ATOM
3059
N
PHE
B
808
19.129
−23.159
2.418
1.00
19.70
B


ATOM
3060
CA
PHE
B
808
19.602
−23.292
1.042
1.00
18.77
B


ATOM
3061
CB
PHE
B
808
20.832
−22.408
0.785
1.00
16.63
B


ATOM
3062
CG
PHE
B
808
20.510
−20.951
0.577
1.00
18.24
B


ATOM
3063
CD1
PHE
B
808
19.195
−20.495
0.604
1.00
15.60
B


ATOM
3064
CD2
PHE
B
808
21.529
−20.030
0.369
1.00
17.34
B


ATOM
3065
CE1
PHE
B
808
18.905
−19.133
0.431
1.00
17.14
B


ATOM
3066
CE2
PHE
B
808
21.248
−18.672
0.196
1.00
18.78
B


ATOM
3067
CZ
PHE
B
808
19.929
−18.227
0.228
1.00
17.21
B


ATOM
3068
C
PHE
B
808
19.964
−24.751
0.802
1.00
17.37
B


ATOM
3069
O
PHE
B
808
19.610
−25.322
−0.225
1.00
17.11
B


ATOM
3070
N
VAL
B
809
20.673
−25.346
1.756
1.00
18.79
B


ATOM
3071
CA
VAL
B
809
21.054
−26.756
1.655
1.00
19.69
B


ATOM
3072
CB
VAL
B
809
21.955
−27.190
2.846
1.00
21.10
B


ATOM
3073
CG1
VAL
B
809
22.113
−28.704
2.855
1.00
23.52
B


ATOM
3074
CG2
VAL
B
809
23.330
−26.536
2.742
1.00
19.39
B


ATOM
3075
C
VAL
B
809
19.800
−27.640
1.646
1.00
21.36
B


ATOM
3076
O
VAL
B
809
19.685
−28.560
0.830
1.00
21.94
B


ATOM
3077
N
LYS
B
810
18.864
−27.364
2.551
1.00
21.13
B


ATOM
3078
CA
LYS
B
810
17.634
−28.152
2.630
1.00
23.80
B


ATOM
3079
CB
LYS
B
810
16.748
−27.674
3.786
1.00
27.42
B


ATOM
3080
CG
LYS
B
810
17.228
−28.037
5.182
1.00
31.68
B


ATOM
3081
CD
LYS
B
810
16.184
−27.605
6.205
1.00
35.53
B


ATOM
3082
CE
LYS
B
810
16.667
−27.793
7.632
1.00
39.05
B


ATOM
3083
NZ
LYS
B
810
15.639
−27.331
8.608
1.00
38.71
B


ATOM
3084
C
LYS
B
810
16.801
−28.115
1.355
1.00
23.30
B


ATOM
3085
O
LYS
B
810
16.407
−29.157
0.829
1.00
20.94
B


ATOM
3086
N
LEU
B
811
16.514
−26.910
0.871
1.00
22.91
B


ATOM
3087
CA
LEU
B
811
15.700
−26.747
−0.331
1.00
21.97
B


ATOM
3088
CB
LEU
B
811
15.015
−25.374
−0.315
1.00
21.71
B


ATOM
3089
CG
LEU
B
811
14.081
−25.064
0.861
1.00
22.02
B


ATOM
3090
CD1
LEU
B
811
13.701
−23.588
0.851
1.00
22.31
B


ATOM
3091
CD2
LEU
B
811
12.837
−25.939
0.779
1.00
25.00
B


ATOM
3092
C
LEU
B
811
16.507
−26.900
−1.619
1.00
22.54
B


ATOM
3093
O
LEU
B
811
15.938
−26.954
−2.714
1.00
21.82
B


ATOM
3094
N
GLN
B
812
17.828
−26.980
−1.483
1.00
21.57
B


ATOM
3095
CA
GLN
B
812
18.720
−27.097
−2.633
1.00
21.27
B


ATOM
3096
CB
GLN
B
812
18.561
−28.472
−3.308
1.00
20.69
B


ATOM
3097
CG
GLN
B
812
19.021
−29.621
−2.404
1.00
22.08
B


ATOM
3098
CD
GLN
B
812
19.074
−30.985
−3.097
1.00
26.58
B


ATOM
3099
OE1
GLN
B
812
19.622
−31.944
−2.550
1.00
26.47
B


ATOM
3100
NE2
GLN
B
812
18.501
−31.076
−4.290
1.00
25.48
B


ATOM
3101
C
GLN
B
812
18.466
−25.963
−3.627
1.00
20.82
B


ATOM
3102
O
GLN
B
812
18.251
−26.189
−4.815
1.00
21.92
B


ATOM
3103
N
VAL
B
813
18.495
−24.736
−3.114
1.00
19.44
B


ATOM
3104
CA
VAL
B
813
18.287
−23.537
−3.923
1.00
19.33
B


ATOM
3105
CB
VAL
B
813
18.438
−22.268
−3.045
1.00
18.90
B


ATOM
3106
CG1
VAL
B
813
18.280
−21.007
−3.890
1.00
20.26
B


ATOM
3107
CG2
VAL
B
813
17.412
−22.297
−1.921
1.00
18.94
B


ATOM
3108
C
VAL
B
813
19.287
−23.466
−5.086
1.00
18.64
B


ATOM
3109
O
VAL
B
813
20.486
−23.680
−4.903
1.00
18.83
B


ATOM
3110
N
SER
B
814
18.793
−23.157
−6.281
1.00
18.80
B


ATOM
3111
CA
SER
B
814
19.652
−23.061
−7.459
1.00
18.35
B


ATOM
3112
CB
SER
B
814
18.863
−23.440
−8.715
1.00
18.95
B


ATOM
3113
OG
SER
B
814
17.833
−22.498
−8.946
1.00
17.40
B


ATOM
3114
C
SER
B
814
20.186
−21.638
−7.616
1.00
19.62
B


ATOM
3115
O
SER
B
814
19.624
−20.695
−7.060
1.00
19.00
B


ATOM
3116
N
GLN
B
815
21.266
−21.477
−8.375
1.00
21.03
B


ATOM
3117
CA
GLN
B
815
21.815
−20.142
−8.589
1.00
22.06
B


ATOM
3118
CB
GLN
B
815
23.037
−20.177
−9.513
1.00
24.38
B


ATOM
3119
CG
GLN
B
815
23.720
−18.810
−9.642
1.00
29.34
B


ATOM
3120
CD
GLN
B
815
24.757
−18.746
−10.754
1.00
30.23
B


ATOM
3121
OE1
GLN
B
815
25.384
−17.709
−10.968
1.00
35.37
B


ATOM
3122
NE2
GLN
B
815
24.937
−19.850
−11.468
1.00
32.87
B


ATOM
3123
C
GLN
B
815
20.758
−19.250
−9.228
1.00
21.09
B


ATOM
3124
O
GLN
B
815
20.639
−18.073
−8.889
1.00
20.44
B


ATOM
3125
N
GLU
B
816
19.988
−19.813
−10.153
1.00
19.51
B


ATOM
3126
CA
GLU
B
816
18.955
−19.038
−10.837
1.00
21.06
B


ATOM
3127
CB
GLU
B
816
18.333
−19.862
−11.970
1.00
21.97
B


ATOM
3128
CG
GLU
B
816
19.327
−20.221
−13.073
1.00
23.03
B


ATOM
3129
CD
GLU
B
816
20.038
−21.547
−12.836
1.00
26.52
B


ATOM
3130
OE1
GLU
B
816
20.073
−22.025
−11.681
1.00
23.85
B


ATOM
3131
OE2
GLU
B
816
20.575
−22.109
−13.813
1.00
28.20
B


ATOM
3132
C
GLU
B
816
17.877
−18.529
−9.880
1.00
19.82
B


ATOM
3133
O
GLU
B
816
17.435
−17.383
−9.993
1.00
19.18
B


ATOM
3134
N
GLU
B
817
17.463
−19.367
−8.932
1.00
17.39
B


ATOM
3135
CA
GLU
B
817
16.457
−18.956
−7.956
1.00
18.18
B


ATOM
3136
CB
GLU
B
817
15.983
−20.159
−7.126
1.00
18.59
B


ATOM
3137
CG
GLU
B
817
15.397
−21.297
−7.966
1.00
22.22
B


ATOM
3138
CD
GLU
B
817
15.064
−22.531
−7.145
1.00
23.48
B


ATOM
3139
OE1
GLU
B
817
15.892
−22.936
−6.296
1.00
22.86
B


ATOM
3140
OE2
GLU
B
817
13.976
−23.106
−7.363
1.00
25.72
B


ATOM
3141
C
GLU
B
817
17.063
−17.906
−7.030
1.00
17.11
B


ATOM
3142
O
GLU
B
817
16.422
−16.912
−6.700
1.00
16.65
B


ATOM
3143
N
PHE
B
818
18.305
−18.142
−6.618
1.00
16.93
B


ATOM
3144
CA
PHE
B
818
19.018
−17.239
−5.723
1.00
16.13
B


ATOM
3145
CB
PHE
B
818
20.435
−17.769
−5.456
1.00
16.83
B


ATOM
3146
CG
PHE
B
818
21.349
−16.761
−4.791
1.00
16.89
B


ATOM
3147
CD1
PHE
B
818
21.199
−16.445
−3.442
1.00
15.26
B


ATOM
3148
CD2
PHE
B
818
22.345
−16.115
−5.526
1.00
17.05
B


ATOM
3149
CE1
PHE
B
818
22.027
−15.499
−2.830
1.00
16.92
B


ATOM
3150
CE2
PHE
B
818
23.182
−15.164
−4.927
1.00
17.15
B


ATOM
3151
CZ
PHE
B
818
23.022
−14.855
−3.576
1.00
16.27
B


ATOM
3152
C
PHE
B
818
19.122
−15.818
−6.278
1.00
16.33
B


ATOM
3153
O
PHE
B
818
18.840
−14.849
−5.569
1.00
15.00
B


ATOM
3154
N
LEU
B
819
19.538
−15.706
−7.538
1.00
14.54
B


ATOM
3155
CA
LEU
B
819
19.716
−14.404
−8.177
1.00
16.83
B


ATOM
3156
CB
LEU
B
819
20.311
−14.581
−9.582
1.00
16.07
B


ATOM
3157
CG
LEU
B
819
21.722
−15.189
−9.612
1.00
18.18
B


ATOM
3158
CD1
LEU
B
819
22.082
−15.583
−11.026
1.00
18.54
B


ATOM
3159
CD2
LEU
B
819
22.737
−14.192
−9.056
1.00
16.82
B


ATOM
3160
C
LEU
B
819
18.424
−13.597
−8.245
1.00
16.62
B


ATOM
3161
O
LEU
B
819
18.436
−12.385
−8.027
1.00
18.04
B


ATOM
3162
N
CYS
B
820
17.314
−14.266
−8.541
1.00
16.17
B


ATOM
3163
CA
CYS
B
820
16.021
−13.596
−8.616
1.00
16.66
B


ATOM
3164
CB
CYS
B
820
14.983
−14.509
−9.271
1.00
16.58
B


ATOM
3165
SG
CYS
B
820
15.294
−14.853
−11.023
1.00
18.85
B


ATOM
3166
C
CYS
B
820
15.551
−13.197
−7.223
1.00
16.30
B


ATOM
3167
O
CYS
B
820
15.032
−12.094
−7.023
1.00
14.96
B


ATOM
3168
N
MET
B
821
15.737
−14.099
−6.263
1.00
16.45
B


ATOM
3169
CA
MET
B
821
15.342
−13.843
−4.880
1.00
15.29
B


ATOM
3170
CB
MET
B
821
15.607
−15.074
−4.011
1.00
16.65
B


ATOM
3171
CG
MET
B
821
14.675
−16.244
−4.269
1.00
17.53
B


ATOM
3172
SD
MET
B
821
15.242
−17.726
−3.411
1.00
19.94
B


ATOM
3173
CE
MET
B
821
14.783
−17.351
−1.762
1.00
15.63
B


ATOM
3174
C
MET
B
821
16.110
−12.661
−4.299
1.00
15.82
B


ATOM
3175
O
MET
B
821
15.564
−11.868
−3.535
1.00
14.99
B


ATOM
3176
N
LYS
B
822
17.381
−12.549
−4.663
1.00
16.67
B


ATOM
3177
CA
LYS
B
822
18.212
−11.473
−4.148
1.00
16.99
B


ATOM
3178
CB
LYS
B
822
19.679
−11.705
−4.526
1.00
18.26
B


ATOM
3179
CG
LYS
B
822
20.635
−10.691
−3.906
1.00
19.96
B


ATOM
3180
CD
LYS
B
822
22.044
−11.256
−3.763
1.00
20.99
B


ATOM
3181
CE
LYS
B
822
22.696
−11.541
−5.110
1.00
23.13
B


ATOM
3182
NZ
LYS
B
822
22.880
−10.302
−5.919
1.00
23.24
B


ATOM
3183
C
LYS
B
822
17.728
−10.117
−4.644
1.00
17.98
B


ATOM
3184
O
LYS
B
822
17.814
−9.128
−3.922
1.00
17.23
B


ATOM
3185
N
VAL
B
823
17.220
−10.066
−5.872
1.00
17.29
B


ATOM
3186
CA
VAL
B
823
16.698
−8.814
−6.404
1.00
15.85
B


ATOM
3187
CB
VAL
B
823
16.379
−8.919
−7.905
1.00
17.02
B


ATOM
3188
CG1
VAL
B
823
15.756
−7.603
−8.397
1.00
15.78
B


ATOM
3189
CG2
VAL
B
823
17.650
−9.228
−8.685
1.00
15.65
B


ATOM
3190
C
VAL
B
823
15.412
−8.467
−5.653
1.00
15.49
B


ATOM
3191
O
VAL
B
823
15.155
−7.306
−5.340
1.00
14.04
B


ATOM
3192
N
LEU
B
824
14.603
−9.478
−5.356
1.00
14.47
B


ATOM
3193
CA
LEU
B
824
13.361
−9.240
−4.631
1.00
15.65
B


ATOM
3194
CB
LEU
B
824
12.525
−10.523
−4.584
1.00
15.79
B


ATOM
3195
CG
LEU
B
824
11.928
−10.911
−5.942
1.00
18.34
B


ATOM
3196
CD1
LEU
B
824
11.245
−12.262
−5.835
1.00
17.24
B


ATOM
3197
CD2
LEU
B
824
10.933
−9.842
−6.393
1.00
16.65
B


ATOM
3198
C
LEU
B
824
13.667
−8.730
−3.223
1.00
16.46
B


ATOM
3199
O
LEU
B
824
12.907
−7.931
−2.662
1.00
17.28
B


ATOM
3200
N
LEU
B
825
14.781
−9.184
−2.656
1.00
16.24
B


ATOM
3201
CA
LEU
B
825
15.190
−8.721
−1.324
1.00
17.69
B


ATOM
3202
CB
LEU
B
825
16.463
−9.419
−0.861
1.00
17.38
B


ATOM
3203
CG
LEU
B
825
16.366
−10.560
0.141
1.00
23.00
B


ATOM
3204
CD1
LEU
B
825
17.767
−10.795
0.695
1.00
19.06
B


ATOM
3205
CD2
LEU
B
825
15.396
−10.217
1.276
1.00
21.23
B


ATOM
3206
C
LEU
B
825
15.472
−7.227
−1.360
1.00
15.92
B


ATOM
3207
O
LEU
B
825
15.111
−6.492
−0.441
1.00
15.49
B


ATOM
3208
N
LEU
B
826
16.151
−6.793
−2.416
1.00
15.55
B


ATOM
3209
CA
LEU
B
826
16.477
−5.380
−2.587
1.00
15.43
B


ATOM
3210
CB
LEU
B
826
17.235
−5.179
−3.906
1.00
13.00
B


ATOM
3211
CG
LEU
B
826
17.367
−3.755
−4.447
1.00
17.08
B


ATOM
3212
CD1
LEU
B
826
18.309
−2.932
−3.565
1.00
15.15
B


ATOM
3213
CD2
LEU
B
826
17.880
−3.813
−5.893
1.00
15.84
B


ATOM
3214
C
LEU
B
826
15.192
−4.552
−2.605
1.00
15.22
B


ATOM
3215
O
LEU
B
826
15.159
−3.417
−2.123
1.00
15.10
B


ATOM
3216
N
LEU
B
827
14.134
−5.146
−3.148
1.00
14.61
B


ATOM
3217
CA
LEU
B
827
12.835
−4.487
−3.287
1.00
17.58
B


ATOM
3218
CB
LEU
B
827
12.261
−4.795
−4.678
1.00
16.81
B


ATOM
3219
CG
LEU
B
827
13.201
−4.610
−5.872
1.00
19.46
B


ATOM
3220
CD1
LEU
B
827
12.564
−5.176
−7.146
1.00
18.89
B


ATOM
3221
CD2
LEU
B
827
13.519
−3.131
−6.032
1.00
15.57
B


ATOM
3222
C
LEU
B
827
11.827
−4.961
−2.253
1.00
16.56
B


ATOM
3223
O
LEU
B
827
10.625
−4.866
−2.487
1.00
18.58
B


ATOM
3224
N
ASN
B
828
12.299
−5.438
−1.106
1.00
15.56
B


ATOM
3225
CA
ASN
B
828
11.380
−5.998
−0.125
1.00
17.84
B


ATOM
3226
CB
ASN
B
828
11.992
−7.291
0.421
1.00
19.91
B


ATOM
3227
CG
ASN
B
828
10.986
−8.423
0.503
1.00
24.26
B


ATOM
3228
OD1
ASN
B
828
10.082
−8.524
−0.328
1.00
24.73
B


ATOM
3229
ND2
ASN
B
828
11.153
−9.294
1.495
1.00
24.40
B


ATOM
3230
C
ASN
B
828
10.894
−5.105
1.022
1.00
17.27
B


ATOM
3231
O
ASN
B
828
10.137
−5.558
1.879
1.00
16.66
B


ATOM
3232
N
THR
B
829
11.323
−3.848
1.037
1.00
14.98
B


ATOM
3233
CA
THR
B
829
10.896
−2.903
2.063
1.00
18.37
B


ATOM
3234
CB
THR
B
829
11.914
−2.802
3.232
1.00
18.06
B


ATOM
3235
OG1
THR
B
829
12.146
−4.102
3.789
1.00
17.88
B


ATOM
3236
CG2
THR
B
829
11.372
−1.889
4.321
1.00
20.06
B


ATOM
3237
C
THR
B
829
10.775
−1.523
1.426
1.00
18.82
B


ATOM
3238
O
THR
B
829
11.607
−1.151
0.595
1.00
17.50
B


ATOM
3239
N
ILE
B
830
9.736
−0.775
1.792
1.00
17.45
B


ATOM
3240
CA
ILE
B
830
9.548
0.572
1.258
1.00
19.79
B


ATOM
3241
CB
ILE
B
830
8.523
0.594
0.089
1.00
20.43
B


ATOM
3242
CG2
ILE
B
830
8.982
−0.346
−1.019
1.00
19.43
B


ATOM
3243
CG1
ILE
B
830
7.133
0.200
0.592
1.00
21.42
B


ATOM
3244
CD1
ILE
B
830
6.083
0.164
−0.493
1.00
22.07
B


ATOM
3245
C
ILE
B
830
9.084
1.522
2.366
1.00
19.09
B


ATOM
3246
O
ILE
B
830
8.680
1.080
3.440
1.00
21.03
B


ATOM
3247
N
PRO
B
831
9.159
2.840
2.126
1.00
19.68
B


ATOM
3248
CD
PRO
B
831
9.738
3.505
0.949
1.00
18.90
B


ATOM
3249
CA
PRO
B
831
8.738
3.828
3.129
1.00
21.03
B


ATOM
3250
CB
PRO
B
831
9.057
5.164
2.460
1.00
20.87
B


ATOM
3251
CG
PRO
B
831
10.192
4.821
1.528
1.00
22.56
B


ATOM
3252
C
PRO
B
831
7.252
3.696
3.428
1.00
22.30
B


ATOM
3253
O
PRO
B
831
6.498
3.183
2.608
1.00
22.00
B


ATOM
3254
N
LEU
B
832
6.827
4.161
4.597
1.00
23.69
B


ATOM
3255
CA
LEU
B
832
5.413
4.088
4.957
1.00
26.10
B


ATOM
3256
CB
LEU
B
832
5.190
4.686
6.351
1.00
26.82
B


ATOM
3257
CG
LEU
B
832
5.745
3.874
7.529
1.00
26.56
B


ATOM
3258
CD1
LEU
B
832
5.599
4.667
8.820
1.00
28.10
B


ATOM
3259
CD2
LEU
B
832
5.002
2.551
7.628
1.00
27.65
B


ATOM
3260
C
LEU
B
832
4.550
4.823
3.929
1.00
26.82
B


ATOM
3261
O
LEU
B
832
3.442
4.392
3.614
1.00
26.75
B


ATOM
3262
N
GLU
B
833
5.070
5.928
3.403
1.00
27.88
B


ATOM
3263
CA
GLU
B
833
4.347
6.719
2.414
1.00
29.18
B


ATOM
3264
CB
GLU
B
833
4.808
8.180
2.461
1.00
31.58
B


ATOM
3265
CG
GLU
B
833
6.300
8.368
2.212
1.00
33.80
B


ATOM
3266
CD
GLU
B
833
7.141
8.184
3.467
1.00
34.56
B


ATOM
3267
OE1
GLU
B
833
6.840
7.282
4.272
1.00
34.98
B


ATOM
3268
OE2
GLU
B
833
8.119
8.938
3.643
1.00
36.68
B


ATOM
3269
C
GLU
B
833
4.559
6.163
1.007
1.00
29.05
B


ATOM
3270
O
GLU
B
833
4.009
6.682
0.032
1.00
30.18
B


ATOM
3271
N
GLY
B
834
5.354
5.104
0.901
1.00
25.32
B


ATOM
3272
CA
GLY
B
834
5.616
4.520
−0.398
1.00
23.75
B


ATOM
3273
C
GLY
B
834
6.766
5.233
−1.087
1.00
24.18
B


ATOM
3274
O
GLY
B
834
7.334
6.179
−0.547
1.00
22.28
B


ATOM
3275
N
LEU
B
835
7.106
4.779
−2.288
1.00
23.91
B


ATOM
3276
CA
LEU
B
835
8.196
5.368
−3.049
1.00
24.07
B


ATOM
3277
CB
LEU
B
835
8.885
4.283
−3.871
1.00
23.41
B


ATOM
3278
CG
LEU
B
835
9.564
3.167
−3.074
1.00
22.91
B


ATOM
3279
CD1
LEU
B
835
9.954
2.031
−4.003
1.00
21.52
B


ATOM
3280
CD2
LEU
B
835
10.778
3.732
−2.361
1.00
22.16
B


ATOM
3281
C
LEU
B
835
7.697
6.465
−3.982
1.00
25.22
B


ATOM
3282
O
LEU
B
835
6.494
6.599
−4.214
1.00
23.05
B


ATOM
3283
N
ARG
B
836
8.625
7.250
−4.518
1.00
25.18
B


ATOM
3284
CA
ARG
B
836
8.251
8.305
−5.450
1.00
27.41
B


ATOM
3285
CB
ARG
B
836
9.410
9.289
−5.629
1.00
29.23
B


ATOM
3286
CG
ARG
B
836
9.790
9.972
−4.326
1.00
33.63
B


ATOM
3287
CD
ARG
B
836
10.699
11.168
−4.531
1.00
39.98
B


ATOM
3288
NE
ARG
B
836
11.086
11.742
−3.244
1.00
46.27
B


ATOM
3289
CZ
ARG
B
836
11.726
12.897
−3.091
1.00
48.81
B


ATOM
3290
NH1
ARG
B
836
12.032
13.327
−1.873
1.00
50.05
B


ATOM
3291
NH2
ARG
B
836
12.059
13.623
−4.152
1.00
50.02
B


ATOM
3292
C
ARG
B
836
7.874
7.644
−6.774
1.00
25.29
B


ATOM
3293
O
ARG
B
836
6.886
8.015
−7.405
1.00
25.23
B


ATOM
3294
N
SER
B
837
8.652
6.641
−7.174
1.00
23.28
B


ATOM
3295
CA
SER
B
837
8.387
5.906
−8.408
1.00
21.91
B


ATOM
3296
CB
SER
B
837
9.696
5.609
−9.138
1.00
22.60
B


ATOM
3297
OG
SER
B
837
10.416
6.806
−9.380
1.00
24.64
B


ATOM
3298
C
SER
B
837
7.693
4.597
−8.046
1.00
21.70
B


ATOM
3299
O
SER
B
837
8.145
3.518
−8.427
1.00
19.42
B


ATOM
3300
N
GLN
B
838
6.593
4.707
−7.307
1.00
21.26
B


ATOM
3301
CA
GLN
B
838
5.831
3.544
−6.862
1.00
22.08
B


ATOM
3302
CB
GLN
B
838
4.618
4.004
−6.040
1.00
22.63
B


ATOM
3303
CG
GLN
B
838
3.915
2.893
−5.259
1.00
26.54
B


ATOM
3304
CD
GLN
B
838
4.822
2.234
−4.226
1.00
26.15
B


ATOM
3305
OE1
GLN
B
838
5.562
2.909
−3.513
1.00
27.61
B


ATOM
3306
NE2
GLN
B
838
4.755
0.911
−4.135
1.00
27.61
B


ATOM
3307
C
GLN
B
838
5.368
2.647
−8.012
1.00
21.61
B


ATOM
3308
O
GLN
B
838
5.515
1.427
−7.949
1.00
20.05
B


ATOM
3309
N
THR
B
839
4.812
3.249
−9.062
1.00
22.33
B


ATOM
3310
CA
THR
B
839
4.336
2.479
−10.207
1.00
22.29
B


ATOM
3311
CB
THR
B
839
3.694
3.386
−11.276
1.00
24.97
B


ATOM
3312
OG1
THR
B
839
2.579
4.077
−10.702
1.00
27.76
B


ATOM
3313
CG2
THR
B
839
3.206
2.555
−12.460
1.00
24.83
B


ATOM
3314
C
THR
B
839
5.463
1.690
−10.855
1.00
20.46
B


ATOM
3315
O
THR
B
839
5.321
0.498
−11.118
1.00
21.42
B


ATOM
3316
N
GLN
B
840
6.582
2.354
−11.111
1.00
19.38
B


ATOM
3317
CA
GLN
B
840
7.725
1.690
−11.722
1.00
21.53
B


ATOM
3318
CB
GLN
B
840
8.831
2.702
−12.013
1.00
25.28
B


ATOM
3319
CG
GLN
B
840
10.059
2.081
−12.661
1.00
33.27
B


ATOM
3320
CD
GLN
B
840
9.737
1.408
−13.983
1.00
37.68
B


ATOM
3321
OE1
GLN
B
840
9.410
2.073
−14.968
1.00
41.19
B


ATOM
3322
NE2
GLN
B
840
9.818
0.078
−14.009
1.00
41.64
B


ATOM
3323
C
GLN
B
840
8.259
0.599
−10.793
1.00
20.93
B


ATOM
3324
O
GLN
B
840
8.638
−0.477
−11.242
1.00
22.03
B


ATOM
3325
N
PHE
B
841
8.287
0.891
−9.498
1.00
18.17
B


ATOM
3326
CA
PHE
B
841
8.764
−0.065
−8.499
1.00
17.96
B


ATOM
3327
CB
PHE
B
841
8.654
0.540
−7.097
1.00
16.53
B


ATOM
3328
CG
PHE
B
841
8.826
−0.464
−5.982
1.00
17.42
B


ATOM
3329
CD1
PHE
B
841
10.092
−0.912
−5.612
1.00
19.52
B


ATOM
3330
CD2
PHE
B
841
7.718
−0.953
−5.296
1.00
16.29
B


ATOM
3331
CE1
PHE
B
841
10.250
−1.832
−4.570
1.00
15.82
B


ATOM
3332
CE2
PHE
B
841
7.867
−1.877
−4.253
1.00
18.30
B


ATOM
3333
CZ
PHE
B
841
9.139
−2.313
−3.893
1.00
16.42
B


ATOM
3334
C
PHE
B
841
7.938
−1.341
−8.554
1.00
18.36
B


ATOM
3335
O
PHE
B
841
8.474
−2.447
−8.625
1.00
16.92
B


ATOM
3336
N
GLU
B
842
6.624
−1.181
−8.524
1.00
18.46
B


ATOM
3337
CA
GLU
B
842
5.742
−2.333
−8.552
1.00
20.40
B


ATOM
3338
CB
GLU
B
842
4.300
−1.874
−8.320
1.00
22.60
B


ATOM
3339
CG
GLU
B
842
3.992
−1.716
−6.831
1.00
28.47
B


ATOM
3340
CD
GLU
B
842
2.778
−0.855
−6.553
1.00
33.41
B


ATOM
3341
OE1
GLU
B
842
1.849
−0.848
−7.387
1.00
35.95
B


ATOM
3342
OE2
GLU
B
842
2.748
−0.194
−5.490
1.00
34.10
B


ATOM
3343
C
GLU
B
842
5.885
−3.159
−9.824
1.00
19.29
B


ATOM
3344
O
GLU
B
842
5.856
−4.388
−9.769
1.00
18.69
B


ATOM
3345
N
GLU
B
843
6.053
−2.492
−10.962
1.00
19.28
B


ATOM
3346
CA
GLU
B
843
6.234
−3.194
−12.229
1.00
20.40
B


ATOM
3347
CB
GLU
B
843
6.279
−2.195
−13.391
1.00
23.21
B


ATOM
3348
CG
GLU
B
843
4.908
−1.670
−13.817
1.00
26.48
B


ATOM
3349
CD
GLU
B
843
4.993
−0.619
−14.912
1.00
28.27
B


ATOM
3350
OE1
GLU
B
843
5.906
−0.710
−15.761
1.00
31.59
B


ATOM
3351
OE2
GLU
B
843
4.140
0.289
−14.933
1.00
30.69
B


ATOM
3352
C
GLU
B
843
7.542
−3.984
−12.180
1.00
21.13
B


ATOM
3353
O
GLU
B
843
7.600
−5.147
−12.580
1.00
20.25
B


ATOM
3354
N
MET
B
844
8.594
−3.339
−11.684
1.00
20.24
B


ATOM
3355
CA
MET
B
844
9.892
−3.984
−11.574
1.00
21.25
B


ATOM
3356
CB
MET
B
844
10.920
−3.004
−11.001
1.00
21.39
B


ATOM
3357
CG
MET
B
844
12.315
−3.597
−10.878
1.00
21.13
B


ATOM
3358
SD
MET
B
844
13.560
−2.448
−10.248
1.00
19.73
B


ATOM
3359
CE
MET
B
844
14.982
−3.557
−10.182
1.00
17.38
B


ATOM
3360
C
MET
B
844
9.787
−5.222
−10.679
1.00
21.40
B


ATOM
3361
O
MET
B
844
10.238
−6.309
−11.045
1.00
21.49
B


ATOM
3362
N
ARG
B
845
9.183
−5.056
−9.509
1.00
21.07
B


ATOM
3363
CA
ARG
B
845
9.026
−6.170
−8.584
1.00
22.63
B


ATOM
3364
CB
ARG
B
845
8.320
−5.683
−7.317
1.00
23.95
B


ATOM
3365
CG
ARG
B
845
8.324
−6.666
−6.164
1.00
27.11
B


ATOM
3366
CD
ARG
B
845
7.705
−6.032
−4.922
1.00
25.54
B


ATOM
3367
NE
ARG
B
845
7.297
−7.039
−3.953
1.00
27.61
B


ATOM
3368
CZ
ARG
B
845
8.134
−7.751
−3.208
1.00
30.27
B


ATOM
3369
NH1
ARG
B
845
7.654
−8.651
−2.359
1.00
32.12
B


ATOM
3370
NH2
ARG
B
845
9.447
−7.552
−3.295
1.00
28.99
B


ATOM
3371
C
ARG
B
845
8.250
−7.329
−9.236
1.00
23.19
B


ATOM
3372
O
ARG
B
845
8.662
−8.485
−9.139
1.00
22.55
B


ATOM
3373
N
SER
B
846
7.144
−7.021
−9.912
1.00
21.82
B


ATOM
3374
CA
SER
B
846
6.349
−8.057
−10.572
1.00
23.07
B


ATOM
3375
CB
SER
B
846
5.115
−7.449
−11.252
1.00
24.12
B


ATOM
3376
OG
SER
B
846
4.220
−6.922
−10.293
1.00
26.05
B


ATOM
3377
C
SER
B
846
7.184
−8.791
−11.614
1.00
22.04
B


ATOM
3378
O
SER
B
846
7.058
−10.003
−11.777
1.00
24.09
B


ATOM
3379
N
SER
B
847
8.028
−8.048
−12.324
1.00
21.69
B


ATOM
3380
CA
SER
B
847
8.888
−8.629
−13.345
1.00
22.04
B


ATOM
3381
CB
SER
B
847
9.734
−7.545
−14.020
1.00
24.55
B


ATOM
3382
OG
SER
B
847
8.929
−6.652
−14.771
1.00
31.05
B


ATOM
3383
C
SER
B
847
9.816
−9.682
−12.748
1.00
20.47
B


ATOM
3384
O
SER
B
847
9.948
−10.781
−13.281
1.00
21.10
B


ATOM
3385
N
TYR
B
848
10.468
−9.343
−11.644
1.00
19.70
B


ATOM
3386
CA
TYR
B
848
11.379
−10.279
−11.010
1.00
18.31
B


ATOM
3387
CB
TYR
B
848
12.288
−9.526
−10.043
1.00
19.17
B


ATOM
3388
CG
TYR
B
848
13.362
−8.765
−10.800
1.00
19.76
B


ATOM
3389
CD1
TYR
B
848
14.496
−9.425
−11.279
1.00
18.70
B


ATOM
3390
CE1
TYR
B
848
15.462
−8.756
−12.026
1.00
16.37
B


ATOM
3391
CD2
TYR
B
848
13.218
−7.407
−11.088
1.00
18.08
B


ATOM
3392
CE2
TYR
B
848
14.182
−6.726
−11.839
1.00
17.62
B


ATOM
3393
CZ
TYR
B
848
15.301
−7.409
−12.302
1.00
19.15
B


ATOM
3394
OH
TYR
B
848
16.272
−6.751
−13.028
1.00
17.87
B


ATOM
3395
C
TYR
B
848
10.641
−11.431
−10.338
1.00
18.15
B


ATOM
3396
O
TYR
B
848
11.180
−12.529
−10.214
1.00
18.25
B


ATOM
3397
N
ILE
B
849
9.411
−11.191
−9.903
1.00
18.38
B


ATOM
3398
CA
ILE
B
849
8.631
−12.274
−9.316
1.00
20.21
B


ATOM
3399
CB
ILE
B
849
7.286
−11.758
−8.723
1.00
21.49
B


ATOM
3400
CG2
ILE
B
849
6.368
−12.929
−8.395
1.00
21.35
B


ATOM
3401
CG1
ILE
B
849
7.557
−10.955
−7.446
1.00
22.56
B


ATOM
3402
CD1
ILE
B
849
6.316
−10.343
−6.811
1.00
21.72
B


ATOM
3403
C
ILE
B
849
8.375
−13.255
−10.474
1.00
21.64
B


ATOM
3404
O
ILE
B
849
8.468
−14.471
−10.309
1.00
22.27
B


ATOM
3405
N
ARG
B
850
8.080
−12.724
−11.659
1.00
22.31
B


ATOM
3406
CA
ARG
B
850
7.849
−13.588
−12.813
1.00
24.41
B


ATOM
3407
CB
ARG
B
850
7.375
−12.781
−14.030
1.00
26.21
B


ATOM
3408
CG
ARG
B
850
5.921
−12.320
−13.957
1.00
28.80
B


ATOM
3409
CD
ARG
B
850
5.417
−11.832
−15.319
1.00
29.74
B


ATOM
3410
NE
ARG
B
850
5.971
−10.537
−15.710
1.00
30.41
B


ATOM
3411
CZ
ARG
B
850
5.629
−9.378
−15.152
1.00
31.78
B


ATOM
3412
NH1
ARG
B
850
4.733
−9.348
−14.175
1.00
33.98
B


ATOM
3413
NH2
ARG
B
850
6.178
−8.247
−15.571
1.00
29.88
B


ATOM
3414
C
ARG
B
850
9.128
−14.329
−13.181
1.00
25.13
B


ATOM
3415
O
ARG
B
850
9.090
−15.501
−13.568
1.00
26.48
B


ATOM
3416
N
GLU
B
851
10.263
−13.649
−13.058
1.00
22.96
B


ATOM
3417
CA
GLU
B
851
11.541
−14.258
−13.402
1.00
22.01
B


ATOM
3418
CB
GLU
B
851
12.647
−13.196
−13.394
1.00
22.35
B


ATOM
3419
CG
GLU
B
851
13.838
−13.513
−14.289
1.00
21.41
B


ATOM
3420
CD
GLU
B
851
13.454
−13.712
−15.756
1.00
25.43
B


ATOM
3421
OE1
GLU
B
851
12.520
−13.035
−16.241
1.00
25.41
B


ATOM
3422
OE2
GLU
B
851
14.103
−14.540
−16.435
1.00
26.71
B


ATOM
3423
C
GLU
B
851
11.856
−15.386
−12.423
1.00
22.31
B


ATOM
3424
O
GLU
B
851
12.408
−16.416
−12.814
1.00
22.61
B


ATOM
3425
N
LEU
B
852
11.497
−15.196
−11.155
1.00
22.07
B


ATOM
3426
CA
LEU
B
852
11.718
−16.226
−10.140
1.00
21.52
B


ATOM
3427
CB
LEU
B
852
11.274
−15.724
−8.759
1.00
19.90
B


ATOM
3428
CG
LEU
B
852
11.214
−16.726
−7.598
1.00
18.71
B


ATOM
3429
CD1
LEU
B
852
12.577
−17.352
−7.373
1.00
20.12
B


ATOM
3430
CD2
LEU
B
852
10.747
−16.017
−6.331
1.00
19.80
B


ATOM
3431
C
LEU
B
852
10.910
−17.468
−10.520
1.00
22.67
B


ATOM
3432
O
LEU
B
852
11.369
−18.602
−10.354
1.00
20.55
B


ATOM
3433
N
ILE
B
853
9.699
−17.248
−11.023
1.00
22.76
B


ATOM
3434
CA
ILE
B
853
8.852
−18.360
−11.429
1.00
23.15
B


ATOM
3435
CB
ILE
B
853
7.472
−17.855
−11.899
1.00
23.96
B


ATOM
3436
CG2
ILE
B
853
6.652
−19.005
−12.471
1.00
22.33
B


ATOM
3437
CG1
ILE
B
853
6.741
−17.212
−10.714
1.00
22.16
B


ATOM
3438
CD1
ILE
B
853
5.362
−16.673
−11.052
1.00
24.56
B


ATOM
3439
C
ILE
B
853
9.559
−19.127
−12.542
1.00
22.87
B


ATOM
3440
O
ILE
B
853
9.636
−20.357
−12.505
1.00
22.24
B


ATOM
3441
N
LYS
B
854
10.097
−18.401
−13.519
1.00
23.12
B


ATOM
3442
CA
LYS
B
854
10.828
−19.033
−14.612
1.00
23.82
B


ATOM
3443
CB
LYS
B
854
11.408
−17.987
−15.567
1.00
24.73
B


ATOM
3444
CG
LYS
B
854
10.411
−17.073
−16.253
1.00
27.55
B


ATOM
3445
CD
LYS
B
854
11.172
−16.123
−17.173
1.00
29.14
B


ATOM
3446
CE
LYS
B
854
10.282
−15.067
−17.796
1.00
30.68
B


ATOM
3447
NZ
LYS
B
854
11.116
−14.097
−18.571
1.00
30.20
B


ATOM
3448
C
LYS
B
854
11.990
−19.839
−14.025
1.00
24.39
B


ATOM
3449
O
LYS
B
854
12.232
−20.987
−14.417
1.00
23.69
B


ATOM
3450
N
ALA
B
855
12.712
−19.223
−13.089
1.00
22.20
B


ATOM
3451
CA
ALA
B
855
13.851
−19.872
−12.446
1.00
21.90
B


ATOM
3452
CB
ALA
B
855
14.454
−18.949
−11.371
1.00
20.12
B


ATOM
3453
C
ALA
B
855
13.430
−21.197
−11.825
1.00
22.62
B


ATOM
3454
O
ALA
B
855
14.129
−22.199
−11.954
1.00
22.66
B


ATOM
3455
N
ILE
B
856
12.284
−21.196
−11.152
1.00
24.17
B


ATOM
3456
CA
ILE
B
856
11.765
−22.401
−10.511
1.00
26.32
B


ATOM
3457
CB
ILE
B
856
10.527
−22.063
−9.646
1.00
25.90
B


ATOM
3458
CG2
ILE
B
856
9.780
−23.332
−9.263
1.00
26.41
B


ATOM
3459
CG1
ILE
B
856
10.962
−21.282
−8.402
1.00
25.34
B


ATOM
3460
CD1
ILE
B
856
9.812
−20.728
−7.575
1.00
23.16
B


ATOM
3461
C
ILE
B
856
11.385
−23.455
−11.558
1.00
28.99
B


ATOM
3462
O
ILE
B
856
11.572
−24.655
−11.342
1.00
29.74
B


ATOM
3463
N
GLY
B
857
10.864
−22.989
−12.692
1.00
29.48
B


ATOM
3464
CA
GLY
B
857
10.446
−23.883
−13.761
1.00
30.13
B


ATOM
3465
C
GLY
B
857
11.580
−24.580
−14.482
1.00
31.17
B


ATOM
3466
O
GLY
B
857
11.366
−25.568
−15.188
1.00
30.36
B


ATOM
3467
N
LEU
B
858
12.792
−24.071
−14.312
1.00
30.74
B


ATOM
3468
CA
LEU
B
858
13.944
−24.676
−14.954
1.00
33.55
B


ATOM
3469
CB
LEU
B
858
15.199
−23.831
−14.713
1.00
30.85
B


ATOM
3470
CG
LEU
B
858
15.263
−22.461
−15.392
1.00
29.83
B


ATOM
3471
CD1
LEU
B
858
16.541
−21.749
−14.968
1.00
29.15
B


ATOM
3472
CD2
LEU
B
858
15.222
−22.628
−16.914
1.00
29.41
B


ATOM
3473
C
LEU
B
858
14.163
−26.090
−14.424
1.00
36.01
B


ATOM
3474
O
LEU
B
858
14.733
−26.933
−15.114
1.00
34.89
B


ATOM
3475
N
ARG
B
859
13.697
−26.344
−13.204
1.00
38.73
B


ATOM
3476
CA
ARG
B
859
13.862
−27.652
−12.585
1.00
43.94
B


ATOM
3477
CB
ARG
B
859
14.929
−27.562
−11.490
1.00
45.40
B


ATOM
3478
CG
ARG
B
859
16.243
−27.004
−12.026
1.00
47.91
B


ATOM
3479
CD
ARG
B
859
17.346
−26.903
−10.988
1.00
50.31
B


ATOM
3480
NE
ARG
B
859
18.531
−26.277
−11.574
1.00
53.12
B


ATOM
3481
CZ
ARG
B
859
19.713
−26.166
−10.973
1.00
54.97
B


ATOM
3482
NH1
ARG
B
859
19.895
−26.641
−9.746
1.00
55.64
B


ATOM
3483
NH2
ARG
B
859
20.718
−25.573
−11.605
1.00
54.67
B


ATOM
3484
C
ARG
B
859
12.555
−28.221
−12.032
1.00
46.55
B


ATOM
3485
O
ARG
B
859
12.298
−29.420
−12.159
1.00
47.71
B


ATOM
3486
N
GLN
B
860
11.730
−27.369
−11.427
1.00
49.36
B


ATOM
3487
CA
GLN
B
860
10.444
−27.812
−10.884
1.00
51.49
B


ATOM
3488
CB
GLN
B
860
9.925
−26.819
−9.842
1.00
53.00
B


ATOM
3489
CG
GLN
B
860
10.879
−26.585
−8.679
1.00
56.02
B


ATOM
3490
CD
GLN
B
860
11.123
−27.832
−7.849
1.00
57.66
B


ATOM
3491
OE1
GLN
B
860
11.981
−27.843
−6.963
1.00
59.53
B


ATOM
3492
NE2
GLN
B
860
10.367
−28.888
−8.125
1.00
58.86
B


ATOM
3493
C
GLN
B
860
9.453
−27.913
−12.036
1.00
52.06
B


ATOM
3494
O
GLN
B
860
8.769
−26.945
−12.370
1.00
52.54
B


ATOM
3495
N
LYS
B
861
9.384
−29.097
−12.633
1.00
52.72
B


ATOM
3496
CA
LYS
B
861
8.514
−29.353
−13.775
1.00
53.52
B


ATOM
3497
CB
LYS
B
861
8.954
−30.648
−14.463
1.00
54.01
B


ATOM
3498
CG
LYS
B
861
10.407
−30.634
−14.922
1.00
54.24
B


ATOM
3499
CD
LYS
B
861
10.654
−29.511
−15.920
1.00
55.39
B


ATOM
3500
CE
LYS
B
861
12.105
−29.470
−16.371
1.00
55.75
B


ATOM
3501
NZ
LYS
B
861
12.329
−28.410
−17.394
1.00
54.73
B


ATOM
3502
C
LYS
B
861
7.017
−29.415
−13.470
1.00
53.18
B


ATOM
3503
O
LYS
B
861
6.199
−28.967
−14.272
1.00
54.01
B


ATOM
3504
N
GLY
B
862
6.657
−29.969
−12.318
1.00
53.04
B


ATOM
3505
CA
GLY
B
862
5.250
−30.072
−11.968
1.00
52.10
B


ATOM
3506
C
GLY
B
862
4.610
−28.753
−11.577
1.00
51.07
B


ATOM
3507
O
GLY
B
862
5.248
−27.909
−10.952
1.00
50.08
B


ATOM
3508
N
VAL
B
863
3.345
−28.574
−11.946
1.00
50.57
B


ATOM
3509
CA
VAL
B
863
2.620
−27.352
−11.615
1.00
50.24
B


ATOM
3510
CB
VAL
B
863
1.237
−27.312
−12.305
1.00
50.56
B


ATOM
3511
CG1
VAL
B
863
1.411
−27.323
−13.814
1.00
50.62
B


ATOM
3512
CG2
VAL
B
863
0.392
−28.498
−11.859
1.00
51.12
B


ATOM
3513
C
VAL
B
863
2.419
−27.254
−10.104
1.00
49.58
B


ATOM
3514
O
VAL
B
863
2.575
−26.184
−9.512
1.00
48.75
B


ATOM
3515
N
VAL
B
864
2.073
−28.379
−9.486
1.00
48.74
B


ATOM
3516
CA
VAL
B
864
1.858
−28.430
−8.044
1.00
47.66
B


ATOM
3517
CB
VAL
B
864
1.255
−29.784
−7.619
1.00
47.83
B


ATOM
3518
CG1
VAL
B
864
1.003
−29.793
−6.120
1.00
49.12
B


ATOM
3519
CG2
VAL
B
864
−0.036
−30.036
−8.376
1.00
48.15
B


ATOM
3520
C
VAL
B
864
3.201
−28.248
−7.346
1.00
46.26
B


ATOM
3521
O
VAL
B
864
3.312
−27.514
−6.363
1.00
45.73
B


ATOM
3522
N
SER
B
865
4.216
−28.928
−7.869
1.00
44.35
B


ATOM
3523
CA
SER
B
865
5.566
−28.850
−7.331
1.00
42.44
B


ATOM
3524
CB
SER
B
865
6.481
−29.811
−8.097
1.00
43.32
B


ATOM
3525
OG
SER
B
865
7.814
−29.753
−7.619
1.00
46.42
B


ATOM
3526
C
SER
B
865
6.089
−27.414
−7.455
1.00
40.83
B


ATOM
3527
O
SER
B
865
6.677
−26.873
−6.519
1.00
38.94
B


ATOM
3528
N
SER
B
866
5.866
−26.807
−8.617
1.00
39.03
B


ATOM
3529
CA
SER
B
866
6.302
−25.440
−8.875
1.00
38.13
B


ATOM
3530
CB
SER
B
866
5.976
−25.041
−10.315
1.00
39.12
B


ATOM
3531
OG
SER
B
866
6.795
−25.745
−11.230
1.00
42.05
B


ATOM
3532
C
SER
B
866
5.655
−24.447
−7.922
1.00
37.24
B


ATOM
3533
O
SER
B
866
6.320
−23.545
−7.408
1.00
36.71
B


ATOM
3534
N
SER
B
867
4.357
−24.610
−7.690
1.00
35.62
B


ATOM
3535
CA
SER
B
867
3.635
−23.716
−6.794
1.00
35.02
B


ATOM
3536
CB
SER
B
867
2.132
−23.979
−6.875
1.00
35.17
B


ATOM
3537
OG
SER
B
867
1.654
−23.704
−8.180
1.00
38.33
B


ATOM
3538
C
SER
B
867
4.116
−23.882
−5.361
1.00
34.04
B


ATOM
3539
O
SER
B
867
4.285
−22.900
−4.640
1.00
33.31
B


ATOM
3540
N
GLN
B
868
4.335
−25.124
−4.945
1.00
31.60
B


ATOM
3541
CA
GLN
B
868
4.810
−25.373
−3.592
1.00
32.33
B


ATOM
3542
CB
GLN
B
868
4.856
−26.871
−3.308
1.00
34.57
B


ATOM
3543
CG
GLN
B
868
3.502
−27.494
−3.071
1.00
39.81
B


ATOM
3544
CD
GLN
B
868
3.579
−28.998
−2.949
1.00
42.53
B


ATOM
3545
OE1
GLN
B
868
4.411
−29.530
−2.213
1.00
45.19
B


ATOM
3546
NE2
GLN
B
868
2.709
−29.696
−3.670
1.00
43.84
B


ATOM
3547
C
GLN
B
868
6.202
−24.779
−3.417
1.00
29.48
B


ATOM
3548
O
GLN
B
868
6.537
−24.260
−2.355
1.00
28.85
B


ATOM
3549
N
ARG
B
869
7.003
−24.868
−4.470
1.00
27.65
B


ATOM
3550
CA
ARG
B
869
8.364
−24.345
−4.463
1.00
28.67
B


ATOM
3551
CB
ARG
B
869
9.067
−24.720
−5.766
1.00
27.99
B


ATOM
3552
CG
ARG
B
869
10.514
−24.264
−5.852
1.00
29.69
B


ATOM
3553
CD
ARG
B
869
11.378
−25.038
−4.883
1.00
28.24
B


ATOM
3554
NE
ARG
B
869
12.798
−24.771
−5.076
1.00
30.16
B


ATOM
3555
CZ
ARG
B
869
13.765
−25.430
−4.446
1.00
28.86
B


ATOM
3556
NH1
ARG
B
869
13.452
−26.393
−3.588
1.00
26.30
B


ATOM
3557
NH2
ARG
B
869
15.040
−25.130
−4.672
1.00
24.34
B


ATOM
3558
C
ARG
B
869
8.327
−22.825
−4.322
1.00
27.76
B


ATOM
3559
O
ARG
B
869
9.083
−22.240
−3.548
1.00
29.39
B


ATOM
3560
N
PHE
B
870
7.437
−22.195
−5.080
1.00
26.99
B


ATOM
3561
CA
PHE
B
870
7.286
−20.749
−5.045
1.00
26.48
B


ATOM
3562
CB
PHE
B
870
6.215
−20.309
−6.041
1.00
26.94
B


ATOM
3563
CG
PHE
B
870
6.003
−18.824
−6.085
1.00
26.83
B


ATOM
3564
CD1
PHE
B
870
6.902
−17.999
−6.755
1.00
28.19
B


ATOM
3565
CD2
PHE
B
870
4.905
−18.246
−5.450
1.00
27.94
B


ATOM
3566
CE1
PHE
B
870
6.711
−16.616
−6.796
1.00
27.85
B


ATOM
3567
CE2
PHE
B
870
4.704
−16.862
−5.483
1.00
28.37
B


ATOM
3568
CZ
PHE
B
870
5.612
−16.048
−6.161
1.00
27.70
B


ATOM
3569
C
PHE
B
870
6.889
−20.328
−3.636
1.00
26.34
B


ATOM
3570
O
PHE
B
870
7.401
−19.344
−3.101
1.00
25.56
B


ATOM
3571
N
TYR
B
871
5.974
−21.078
−3.032
1.00
26.21
B


ATOM
3572
CA
TYR
B
871
5.542
−20.763
−1.682
1.00
27.42
B


ATOM
3573
CB
TYR
B
871
4.494
−21.767
−1.193
1.00
30.77
B


ATOM
3574
CG
TYR
B
871
4.073
−21.517
0.234
1.00
33.19
B


ATOM
3575
CD1
TYR
B
871
3.055
−20.613
0.532
1.00
35.86
B


ATOM
3576
CE1
TYR
B
871
2.717
−20.318
1.853
1.00
36.85
B


ATOM
3577
CD2
TYR
B
871
4.743
−22.126
1.293
1.00
34.60
B


ATOM
3578
CE2
TYR
B
871
4.416
−21.837
2.615
1.00
36.18
B


ATOM
3579
CZ
TYR
B
871
3.405
−20.933
2.888
1.00
37.44
B


ATOM
3580
OH
TYR
B
871
3.092
−20.633
4.196
1.00
39.18
B


ATOM
3581
C
TYR
B
871
6.747
−20.818
−0.751
1.00
26.36
B


ATOM
3582
O
TYR
B
871
6.972
−19.913
0.049
1.00
25.94
B


ATOM
3583
N
GLN
B
872
7.518
−21.895
−0.865
1.00
25.60
B


ATOM
3584
CA
GLN
B
872
8.691
−22.091
−0.026
1.00
25.57
B


ATOM
3585
CB
GLN
B
872
9.364
−23.421
−0.359
1.00
27.35
B


ATOM
3586
CG
GLN
B
872
8.531
−24.643
−0.039
1.00
30.68
B


ATOM
3587
CD
GLN
B
872
9.221
−25.925
−0.453
1.00
31.86
B


ATOM
3588
OE1
GLN
B
872
9.552
−26.112
−1.624
1.00
34.33
B


ATOM
3589
NE2
GLN
B
872
9.444
−26.815
0.505
1.00
34.20
B


ATOM
3590
C
GLN
B
872
9.713
−20.978
−0.164
1.00
23.41
B


ATOM
3591
O
GLN
B
872
10.177
−20.430
0.830
1.00
21.76
B


ATOM
3592
N
LEU
B
873
10.066
−20.644
−1.398
1.00
22.08
B


ATOM
3593
CA
LEU
B
873
11.061
−19.605
−1.608
1.00
21.86
B


ATOM
3594
CB
LEU
B
873
11.508
−19.595
−3.074
1.00
18.40
B


ATOM
3595
CG
LEU
B
873
12.160
−20.916
−3.522
1.00
20.29
B


ATOM
3596
CD1
LEU
B
873
12.594
−20.822
−4.972
1.00
17.60
B


ATOM
3597
CD2
LEU
B
873
13.369
−21.236
−2.632
1.00
19.06
B


ATOM
3598
C
LEU
B
873
10.576
−18.228
−1.162
1.00
21.93
B


ATOM
3599
O
LEU
B
873
11.348
−17.461
−0.584
1.00
22.49
B


ATOM
3600
N
THR
B
874
9.304
−17.917
−1.404
1.00
22.76
B


ATOM
3601
CA
THR
B
874
8.767
−16.621
−0.999
1.00
23.91
B


ATOM
3602
CB
THR
B
874
7.423
−16.299
−1.702
1.00
24.32
B


ATOM
3603
OG1
THR
B
874
6.458
−17.318
−1.412
1.00
25.03
B


ATOM
3604
CG2
THR
B
874
7.626
−16.203
−3.209
1.00
26.12
B


ATOM
3605
C
THR
B
874
8.576
−16.560
0.516
1.00
25.18
B


ATOM
3606
O
THR
B
874
8.635
−15.483
1.113
1.00
26.18
B


ATOM
3607
N
LYS
B
875
8.359
−17.713
1.142
1.00
24.45
B


ATOM
3608
CA
LYS
B
875
8.194
−17.753
2.592
1.00
23.83
B


ATOM
3609
CB
LYS
B
875
7.659
−19.116
3.046
1.00
25.61
B


ATOM
3610
CG
LYS
B
875
7.292
−19.162
4.522
1.00
28.99
B


ATOM
3611
CD
LYS
B
875
6.156
−18.190
4.830
1.00
33.42
B


ATOM
3612
CE
LYS
B
875
5.855
−18.135
6.321
1.00
35.92
B


ATOM
3613
NZ
LYS
B
875
4.702
−17.238
6.602
1.00
37.34
B


ATOM
3614
C
LYS
B
875
9.558
−17.506
3.230
1.00
23.31
B


ATOM
3615
O
LYS
B
875
9.664
−16.887
4.287
1.00
21.67
B


ATOM
3616
N
LEU
B
876
10.604
−17.999
2.580
1.00
21.64
B


ATOM
3617
CA
LEU
B
876
11.957
−17.808
3.088
1.00
22.58
B


ATOM
3618
CB
LEU
B
876
12.966
−18.543
2.198
1.00
21.81
B


ATOM
3619
CG
LEU
B
876
14.434
−18.534
2.645
1.00
22.37
B


ATOM
3620
CD1
LEU
B
876
15.194
−19.641
1.927
1.00
23.69
B


ATOM
3621
CD2
LEU
B
876
15.059
−17.179
2.358
1.00
22.29
B


ATOM
3622
C
LEU
B
876
12.248
−16.308
3.100
1.00
21.74
B


ATOM
3623
O
LEU
B
876
12.800
−15.782
4.061
1.00
21.27
B


ATOM
3624
N
LEU
B
877
11.863
−15.625
2.028
1.00
21.67
B


ATOM
3625
CA
LEU
B
877
12.072
−14.183
1.935
1.00
21.91
B


ATOM
3626
CB
LEU
B
877
11.643
−13.669
0.556
1.00
20.68
B


ATOM
3627
CG
LEU
B
877
12.504
−14.111
−0.631
1.00
22.24
B


ATOM
3628
CD1
LEU
B
877
11.906
−13.568
−1.916
1.00
22.05
B


ATOM
3629
CD2
LEU
B
877
13.941
−13.609
−0.466
1.00
20.37
B


ATOM
3630
C
LEU
B
877
11.287
−13.476
3.040
1.00
20.65
B


ATOM
3631
O
LEU
B
877
11.817
−12.593
3.709
1.00
19.22
B


ATOM
3632
N
ASP
B
878
10.028
−13.869
3.233
1.00
19.37
B


ATOM
3633
CA
ASP
B
878
9.202
−13.283
4.289
1.00
20.36
B


ATOM
3634
CB
ASP
B
878
7.866
−14.022
4.415
1.00
21.34
B


ATOM
3635
CG
ASP
B
878
6.822
−13.532
3.438
1.00
23.18
B


ATOM
3636
OD1
ASP
B
878
7.165
−12.760
2.516
1.00
24.47
B


ATOM
3637
OD2
ASP
B
878
5.649
−13.933
3.597
1.00
24.18
B


ATOM
3638
C
ASP
B
878
9.918
−13.391
5.631
1.00
20.20
B


ATOM
3639
O
ASP
B
878
10.034
−12.413
6.371
1.00
18.45
B


ATOM
3640
N
ASN
B
879
10.397
−14.593
5.940
1.00
19.35
B


ATOM
3641
CA
ASN
B
879
11.080
−14.836
7.203
1.00
21.08
B


ATOM
3642
CB
ASN
B
879
11.361
−16.332
7.380
1.00
23.62
B


ATOM
3643
CG
ASN
B
879
10.099
−17.166
7.343
1.00
27.77
B


ATOM
3644
OD1
ASN
B
879
9.044
−16.740
7.819
1.00
29.01
B


ATOM
3645
ND2
ASN
B
879
10.200
−18.368
6.787
1.00
29.13
B


ATOM
3646
C
ASN
B
879
12.379
−14.062
7.377
1.00
21.21
B


ATOM
3647
O
ASN
B
879
12.904
−13.972
8.487
1.00
21.00
B


ATOM
3648
N
LEU
B
880
12.910
−13.501
6.297
1.00
20.95
B


ATOM
3649
CA
LEU
B
880
14.152
−12.752
6.424
1.00
21.38
B


ATOM
3650
CB
LEU
B
880
14.770
−12.486
5.052
1.00
20.58
B


ATOM
3651
CG
LEU
B
880
15.371
−13.739
4.406
1.00
24.77
B


ATOM
3652
CD1
LEU
B
880
16.034
−13.370
3.100
1.00
24.40
B


ATOM
3653
CD2
LEU
B
880
16.386
−14.364
5.346
1.00
24.56
B


ATOM
3654
C
LEU
B
880
13.981
−11.445
7.188
1.00
19.74
B


ATOM
3655
O
LEU
B
880
14.925
−10.972
7.809
1.00
20.66
B


ATOM
3656
N
HIS
B
881
12.786
−10.861
7.154
1.00
19.70
B


ATOM
3657
CA
HIS
B
881
12.562
−9.613
7.876
1.00
19.35
B


ATOM
3658
CB
HIS
B
881
11.121
−9.123
7.680
1.00
20.71
B


ATOM
3659
CG
HIS
B
881
10.856
−8.537
6.323
1.00
20.01
B


ATOM
3660
CD2
HIS
B
881
11.379
−7.452
5.704
1.00
17.82
B


ATOM
3661
ND1
HIS
B
881
9.942
−9.076
5.443
1.00
21.77
B


ATOM
3662
CE1
HIS
B
881
9.909
−8.345
4.341
1.00
18.83
B


ATOM
3663
NE2
HIS
B
881
10.772
−7.353
4.475
1.00
21.49
B


ATOM
3664
C
HIS
B
881
12.855
−9.806
9.368
1.00
20.98
B


ATOM
3665
O
HIS
B
881
13.581
−9.018
9.974
1.00
18.74
B


ATOM
3666
N
ASP
B
882
12.299
−10.858
9.958
1.00
22.20
B


ATOM
3667
CA
ASP
B
882
12.525
−11.130
11.377
1.00
22.92
B


ATOM
3668
CB
ASP
B
882
11.698
−12.329
11.842
1.00
27.90
B


ATOM
3669
CG
ASP
B
882
10.216
−12.047
11.853
1.00
33.60
B


ATOM
3670
OD1
ASP
B
882
9.816
−10.997
12.399
1.00
34.59
B


ATOM
3671
OD2
ASP
B
882
9.449
−12.884
11.327
1.00
39.23
B


ATOM
3672
C
ASP
B
882
13.987
−11.418
11.666
1.00
22.16
B


ATOM
3673
O
ASP
B
882
14.532
−10.963
12.670
1.00
21.45
B


ATOM
3674
N
LEU
B
883
14.617
−12.189
10.785
1.00
20.81
B


ATOM
3675
CA
LEU
B
883
16.018
−12.554
10.953
1.00
18.58
B


ATOM
3676
CB
LEU
B
883
16.425
−13.551
9.853
1.00
19.75
B


ATOM
3677
CG
LEU
B
883
17.801
−14.225
9.926
1.00
22.35
B


ATOM
3678
CD1
LEU
B
883
17.821
−15.438
8.994
1.00
22.84
B


ATOM
3679
CD2
LEU
B
883
18.896
−13.235
9.550
1.00
22.64
B


ATOM
3680
C
LEU
B
883
16.918
−11.322
10.912
1.00
18.56
B


ATOM
3681
O
LEU
B
883
17.753
−11.114
11.795
1.00
17.89
B


ATOM
3682
N
VAL
B
884
16.733
−10.506
9.882
1.00
17.78
B


ATOM
3683
CA
VAL
B
884
17.523
−9.295
9.702
1.00
18.13
B


ATOM
3684
CB
VAL
B
884
17.191
−8.640
8.354
1.00
19.53
B


ATOM
3685
CG1
VAL
B
884
17.891
−7.298
8.230
1.00
21.68
B


ATOM
3686
CG2
VAL
B
884
17.618
−9.576
7.227
1.00
18.29
B


ATOM
3687
C
VAL
B
884
17.329
−8.287
10.826
1.00
18.10
B


ATOM
3688
O
VAL
B
884
18.237
−7.520
11.145
1.00
18.80
B


ATOM
3689
N
LYS
B
885
16.151
−8.290
11.436
1.00
18.09
B


ATOM
3690
CA
LYS
B
885
15.889
−7.370
12.530
1.00
19.60
B


ATOM
3691
CB
LYS
B
885
14.469
−7.565
13.054
1.00
23.11
B


ATOM
3692
CG
LYS
B
885
14.118
−6.649
14.219
1.00
25.74
B


ATOM
3693
CD
LYS
B
885
12.706
−6.924
14.689
1.00
31.18
B


ATOM
3694
CE
LYS
B
885
12.381
−6.163
15.961
1.00
31.73
B


ATOM
3695
NZ
LYS
B
885
11.051
−6.599
16.474
1.00
38.15
B


ATOM
3696
C
LYS
B
885
16.898
−7.582
13.667
1.00
19.50
B


ATOM
3697
O
LYS
B
885
17.378
−6.618
14.265
1.00
17.26
B


ATOM
3698
N
GLN
B
886
17.225
−8.842
13.955
1.00
19.54
B


ATOM
3699
CA
GLN
B
886
18.184
−9.149
15.015
1.00
19.86
B


ATOM
3700
CB
GLN
B
886
18.248
−10.660
15.273
1.00
25.01
B


ATOM
3701
CG
GLN
B
886
16.941
−11.267
15.755
1.00
31.58
B


ATOM
3702
CD
GLN
B
886
16.480
−10.710
17.098
1.00
36.35
B


ATOM
3703
OE1
GLN
B
886
15.365
−10.988
17.540
1.00
40.85
B


ATOM
3704
NE2
GLN
B
886
17.337
−9.930
17.754
1.00
38.26
B


ATOM
3705
C
GLN
B
886
19.572
−8.639
14.634
1.00
18.79
B


ATOM
3706
O
GLN
B
886
20.328
−8.171
15.491
1.00
16.94
B


ATOM
3707
N
LEU
B
887
19.910
−8.736
13.352
1.00
17.04
B


ATOM
3708
CA
LEU
B
887
21.205
−8.259
12.881
1.00
16.54
B


ATOM
3709
CB
LEU
B
887
21.445
−8.685
11.427
1.00
18.52
B


ATOM
3710
CG
LEU
B
887
21.471
−10.184
11.104
1.00
23.04
B


ATOM
3711
CD1
LEU
B
887
21.992
−10.382
9.682
1.00
22.45
B


ATOM
3712
CD2
LEU
B
887
22.358
−10.920
12.080
1.00
24.74
B


ATOM
3713
C
LEU
B
887
21.245
−6.733
12.988
1.00
15.32
B


ATOM
3714
O
LEU
B
887
22.251
−6.156
13.396
1.00
16.15
B


ATOM
3715
N
HIS
B
888
20.142
−6.085
12.620
1.00
14.69
B


ATOM
3716
CA
HIS
B
888
20.047
−4.631
12.678
1.00
14.50
B


ATOM
3717
CB
HIS
B
888
18.684
−4.164
12.144
1.00
15.66
B


ATOM
3718
CG
HIS
B
888
18.605
−4.093
10.649
1.00
14.62
B


ATOM
3719
CD2
HIS
B
888
19.574
−4.009
9.706
1.00
15.13
B


ATOM
3720
ND1
HIS
B
888
17.406
−4.038
9.971
1.00
15.95
B


ATOM
3721
CE1
HIS
B
888
17.638
−3.919
8.675
1.00
13.80
B


ATOM
3722
NE2
HIS
B
888
18.945
−3.900
8.487
1.00
17.55
B


ATOM
3723
C
HIS
B
888
20.226
−4.141
14.112
1.00
15.95
B


ATOM
3724
O
HIS
B
888
20.995
−3.215
14.368
1.00
18.20
B


ATOM
3725
N
LEU
B
889
19.518
−4.762
15.049
1.00
16.97
B


ATOM
3726
CA
LEU
B
889
19.617
−4.360
16.449
1.00
17.38
B


ATOM
3727
CB
LEU
B
889
18.647
−5.176
17.306
1.00
16.53
B


ATOM
3728
CG
LEU
B
889
18.667
−4.889
18.814
1.00
18.28
B


ATOM
3729
CD1
LEU
B
889
18.420
−3.402
19.077
1.00
18.15
B


ATOM
3730
CD2
LEU
B
889
17.604
−5.737
19.494
1.00
19.21
B


ATOM
3731
C
LEU
B
889
21.042
−4.528
16.971
1.00
17.72
B


ATOM
3732
O
LEU
B
889
21.590
−3.622
17.597
1.00
17.23
B


ATOM
3733
N
TYR
B
890
21.642
−5.687
16.708
1.00
18.99
B


ATOM
3734
CA
TYR
B
890
23.007
−5.947
17.160
1.00
20.22
B


ATOM
3735
CB
TYR
B
890
23.442
−7.360
16.747
1.00
21.39
B


ATOM
3736
CG
TYR
B
890
24.807
−7.772
17.266
1.00
24.48
B


ATOM
3737
CD1
TYR
B
890
25.974
−7.278
16.688
1.00
23.63
B


ATOM
3738
CE1
TYR
B
890
27.230
−7.639
17.172
1.00
26.80
B


ATOM
3739
CD2
TYR
B
890
24.926
−8.646
18.348
1.00
25.44
B


ATOM
3740
CE2
TYR
B
890
26.180
−9.016
18.842
1.00
28.35
B


ATOM
3741
CZ
TYR
B
890
27.326
−8.508
18.247
1.00
27.86
B


ATOM
3742
OH
TYR
B
890
28.568
−8.865
18.726
1.00
30.29
B


ATOM
3743
C
TYR
B
890
23.951
−4.905
16.563
1.00
18.18
B


ATOM
3744
O
TYR
B
890
24.798
−4.346
17.260
1.00
18.16
B


ATOM
3745
N
CYS
B
891
23.796
−4.640
15.270
1.00
17.50
B


ATOM
3746
CA
CYS
B
891
24.646
−3.667
14.596
1.00
16.55
B


ATOM
3747
CB
CYS
B
891
24.309
−3.612
13.101
1.00
16.50
B


ATOM
3748
SG
CYS
B
891
25.362
−2.476
12.150
1.00
18.64
B


ATOM
3749
C
CYS
B
891
24.517
−2.268
15.211
1.00
16.80
B


ATOM
3750
O
CYS
B
891
25.522
−1.628
15.511
1.00
17.68
B


ATOM
3751
N
LEU
B
892
23.291
−1.794
15.402
1.00
15.23
B


ATOM
3752
CA
LEU
B
892
23.097
−0.466
15.978
1.00
16.77
B


ATOM
3753
CB
LEU
B
892
21.610
−0.100
16.003
1.00
16.01
B


ATOM
3754
CG
LEU
B
892
21.265
1.332
16.428
1.00
15.16
B


ATOM
3755
CD1
LEU
B
892
22.059
2.342
15.586
1.00
15.59
B


ATOM
3756
CD2
LEU
B
892
19.769
1.557
16.262
1.00
15.56
B


ATOM
3757
C
LEU
B
892
23.693
−0.343
17.384
1.00
17.79
B


ATOM
3758
O
LEU
B
892
24.342
0.659
17.696
1.00
19.65
B


ATOM
3759
N
ASN
B
893
23.482
−1.351
18.228
1.00
17.78
B


ATOM
3760
CA
ASN
B
893
24.030
−1.323
19.585
1.00
19.02
B


ATOM
3761
CB
ASN
B
893
23.685
−2.604
20.357
1.00
19.78
B


ATOM
3762
CG
ASN
B
893
22.266
−2.613
20.870
1.00
22.60
B


ATOM
3763
OD1
ASN
B
893
21.705
−1.563
21.187
1.00
25.14
B


ATOM
3764
ND2
ASN
B
893
21.679
−3.804
20.976
1.00
23.61
B


ATOM
3765
C
ASN
B
893
25.543
−1.189
19.532
1.00
20.12
B


ATOM
3766
O
ASN
B
893
26.137
−0.380
20.242
1.00
22.59
B


ATOM
3767
N
THR
B
894
26.167
−2.000
18.690
1.00
19.05
B


ATOM
3768
CA
THR
B
894
27.612
−1.974
18.547
1.00
19.44
B


ATOM
3769
CB
THR
B
894
28.076
−3.079
17.586
1.00
19.42
B


ATOM
3770
OG1
THR
B
894
27.549
−4.338
18.030
1.00
17.10
B


ATOM
3771
CG2
THR
B
894
29.595
−3.149
17.545
1.00
18.92
B


ATOM
3772
C
THR
B
894
28.076
−0.616
18.023
1.00
21.22
B


ATOM
3773
O
THR
B
894
29.073
−0.071
18.491
1.00
20.90
B


ATOM
3774
N
PHE
B
895
27.348
−0.079
17.047
1.00
20.38
B


ATOM
3775
CA
PHE
B
895
27.677
1.215
16.460
1.00
22.73
B


ATOM
3776
CB
PHE
B
895
26.662
1.558
15.363
1.00
22.12
B


ATOM
3777
CG
PHE
B
895
26.933
2.856
14.664
1.00
21.75
B


ATOM
3778
CD1
PHE
B
895
28.068
3.014
13.874
1.00
23.50
B


ATOM
3779
CD2
PHE
B
895
26.043
3.917
14.779
1.00
23.49
B


ATOM
3780
CE1
PHE
B
895
28.312
4.210
13.206
1.00
23.87
B


ATOM
3781
CE2
PHE
B
895
26.276
5.121
14.113
1.00
24.35
B


ATOM
3782
CZ
PHE
B
895
27.414
5.268
13.326
1.00
23.84
B


ATOM
3783
C
PHE
B
895
27.643
2.279
17.557
1.00
23.93
B


ATOM
3784
O
PHE
B
895
28.533
3.121
17.653
1.00
23.95
B


ATOM
3785
N
ILE
B
896
26.606
2.223
18.384
1.00
26.93
B


ATOM
3786
CA
ILE
B
896
26.435
3.160
19.488
1.00
31.13
B


ATOM
3787
CB
ILE
B
896
25.090
2.900
20.213
1.00
31.72
B


ATOM
3788
CG2
ILE
B
896
25.012
3.701
21.497
1.00
34.14
B


ATOM
3789
CG1
ILE
B
896
23.927
3.230
19.277
1.00
33.07
B


ATOM
3790
CD1
ILE
B
896
24.014
4.596
18.654
1.00
30.60
B


ATOM
3791
C
ILE
B
896
27.577
3.066
20.508
1.00
33.19
B


ATOM
3792
O
ILE
B
896
27.986
4.073
21.085
1.00
35.25
B


ATOM
3793
N
GLN
B
897
28.089
1.859
20.727
1.00
34.17
B


ATOM
3794
CA
GLN
B
897
29.169
1.654
21.692
1.00
35.56
B


ATOM
3795
CB
GLN
B
897
28.817
0.494
22.624
1.00
35.80
B


ATOM
3796
CG
GLN
B
897
27.338
0.369
22.930
1.00
36.67
B


ATOM
3797
CD
GLN
B
897
27.000
−0.946
23.601
1.00
38.80
B


ATOM
3798
OE1
GLN
B
897
25.836
−1.350
23.657
1.00
39.12
B


ATOM
3799
NE2
GLN
B
897
28.019
−1.624
24.121
1.00
40.79
B


ATOM
3800
C
GLN
B
897
30.484
1.337
20.990
1.00
36.74
B


ATOM
3801
O
GLN
B
897
31.406
0.795
21.605
1.00
36.87
B


ATOM
3802
N
SER
B
898
30.569
1.681
19.706
1.00
37.12
B


ATOM
3803
CA
SER
B
898
31.756
1.407
18.902
1.00
37.09
B


ATOM
3804
CB
SER
B
898
31.655
2.110
17.544
1.00
36.71
B


ATOM
3805
OG
SER
B
898
31.802
3.513
17.674
1.00
35.33
B


ATOM
3806
C
SER
B
898
33.061
1.812
19.575
1.00
38.11
B


ATOM
3807
O
SER
B
898
34.007
1.028
19.636
1.00
36.29
B


ATOM
3808
N
ARG
B
899
33.116
3.039
20.074
1.00
39.88
B


ATOM
3809
CA
ARG
B
899
34.325
3.521
20.724
1.00
42.35
B


ATOM
3810
CB
ARG
B
899
34.180
5.000
21.069
1.00
45.76
B


ATOM
3811
CG
ARG
B
899
35.338
5.530
21.873
1.00
50.91
B


ATOM
3812
CD
ARG
B
899
35.349
7.042
21.919
1.00
55.56
B


ATOM
3813
NE
ARG
B
899
36.392
7.501
22.825
1.00
59.98
B


ATOM
3814
CZ
ARG
B
899
36.755
8.767
22.979
1.00
61.92
B


ATOM
3815
NH1
ARG
B
899
37.716
9.067
23.839
1.00
63.21
B


ATOM
3816
NH2
ARG
B
899
36.166
9.727
22.274
1.00
62.81
B


ATOM
3817
C
ARG
B
899
34.689
2.731
21.978
1.00
41.68
B


ATOM
3818
O
ARG
B
899
35.858
2.418
22.202
1.00
41.52
B


ATOM
3819
N
ALA
B
900
33.686
2.407
22.787
1.00
40.82
B


ATOM
3820
CA
ALA
B
900
33.909
1.657
24.018
1.00
40.31
B


ATOM
3821
CB
ALA
B
900
32.679
1.750
24.910
1.00
39.86
B


ATOM
3822
C
ALA
B
900
34.246
0.191
23.752
1.00
40.02
B


ATOM
3823
O
ALA
B
900
34.876
−0.469
24.581
1.00
39.73
B


ATOM
3824
N
LEU
B
901
33.823
−0.317
22.599
1.00
38.18
B


ATOM
3825
CA
LEU
B
901
34.081
−1.706
22.241
1.00
37.31
B


ATOM
3826
CB
LEU
B
901
32.867
−2.299
21.518
1.00
37.48
B


ATOM
3827
CG
LEU
B
901
31.545
−2.292
22.285
1.00
38.53
B


ATOM
3828
CD1
LEU
B
901
30.441
−2.875
21.416
1.00
38.07
B


ATOM
3829
CD2
LEU
B
901
31.698
−3.095
23.572
1.00
38.86
B


ATOM
3830
C
LEU
B
901
35.310
−1.826
21.348
1.00
35.77
B


ATOM
3831
O
LEU
B
901
35.714
−2.929
20.981
1.00
35.59
B


ATOM
3832
N
SER
B
902
35.901
−0.685
21.009
1.00
34.11
B


ATOM
3833
CA
SER
B
902
37.073
−0.645
20.144
1.00
33.24
B


ATOM
3834
CB
SER
B
902
38.234
−1.415
20.779
1.00
35.64
B


ATOM
3835
OG
SER
B
902
38.654
−0.802
21.982
1.00
39.63
B


ATOM
3836
C
SER
B
902
36.762
−1.230
18.765
1.00
31.15
B


ATOM
3837
O
SER
B
902
37.620
−1.853
18.137
1.00
29.62
B


ATOM
3838
N
VAL
B
903
35.532
−1.026
18.301
1.00
28.43
B


ATOM
3839
CA
VAL
B
903
35.112
−1.525
16.992
1.00
26.89
B


ATOM
3840
CB
VAL
B
903
33.725
−2.198
17.059
1.00
26.31
B


ATOM
3841
CG1
VAL
B
903
33.320
−2.700
15.668
1.00
25.67
B


ATOM
3842
CG2
VAL
B
903
33.756
−3.350
18.058
1.00
28.50
B


ATOM
3843
C
VAL
B
903
35.037
−0.377
15.994
1.00
26.42
B


ATOM
3844
O
VAL
B
903
34.369
0.625
16.243
1.00
26.76
B


ATOM
3845
N
GLU
B
904
35.720
−0.524
14.865
1.00
24.57
B


ATOM
3846
CA
GLU
B
904
35.712
0.513
13.848
1.00
25.03
B


ATOM
3847
CB
GLU
B
904
37.073
0.595
13.160
1.00
28.92
B


ATOM
3848
CG
GLU
B
904
38.204
0.987
14.094
1.00
38.82
B


ATOM
3849
CD
GLU
B
904
39.490
1.288
13.355
1.00
43.68
B


ATOM
3850
OE1
GLU
B
904
39.987
0.395
12.633
1.00
47.38
B


ATOM
3851
OE2
GLU
B
904
40.004
2.419
13.497
1.00
48.28
B


ATOM
3852
C
GLU
B
904
34.633
0.300
12.797
1.00
23.04
B


ATOM
3853
O
GLU
B
904
34.418
−0.821
12.326
1.00
19.12
B


ATOM
3854
N
PHE
B
905
33.957
1.394
12.448
1.00
20.12
B


ATOM
3855
CA
PHE
B
905
32.912
1.395
11.431
1.00
20.96
B


ATOM
3856
CB
PHE
B
905
31.575
1.886
12.006
1.00
20.87
B


ATOM
3857
CG
PHE
B
905
30.861
0.877
12.856
1.00
21.25
B


ATOM
3858
CD1
PHE
B
905
31.284
0.613
14.156
1.00
18.95
B


ATOM
3859
CD2
PHE
B
905
29.761
0.187
12.354
1.00
19.31
B


ATOM
3860
CE1
PHE
B
905
30.621
−0.327
14.946
1.00
19.88
B


ATOM
3861
CE2
PHE
B
905
29.094
−0.751
13.132
1.00
22.00
B


ATOM
3862
CZ
PHE
B
905
29.526
−1.010
14.438
1.00
20.34
B


ATOM
3863
C
PHE
B
905
33.340
2.356
10.325
1.00
19.65
B


ATOM
3864
O
PHE
B
905
33.518
3.550
10.574
1.00
20.10
B


ATOM
3865
N
PRO
B
906
33.525
1.851
9.096
1.00
19.13
B


ATOM
3866
CD
PRO
B
906
33.677
0.436
8.715
1.00
19.13
B


ATOM
3867
CA
PRO
B
906
33.933
2.733
7.994
1.00
18.54
B


ATOM
3868
CB
PRO
B
906
34.170
1.762
6.842
1.00
18.01
B


ATOM
3869
CG
PRO
B
906
34.661
0.526
7.560
1.00
21.07
B


ATOM
3870
C
PRO
B
906
32.853
3.767
7.687
1.00
17.77
B


ATOM
3871
O
PRO
B
906
31.698
3.614
8.102
1.00
17.22
B


ATOM
3872
N
GLU
B
907
33.230
4.800
6.938
1.00
17.56
B


ATOM
3873
CA
GLU
B
907
32.330
5.909
6.609
1.00
17.42
B


ATOM
3874
CB
GLU
B
907
33.106
6.988
5.856
1.00
15.83
B


ATOM
3875
CG
GLU
B
907
34.261
7.598
6.643
1.00
16.09
B


ATOM
3876
CD
GLU
B
907
33.823
8.322
7.906
1.00
18.31
B


ATOM
3877
OE1
GLU
B
907
32.677
8.821
7.962
1.00
17.52
B


ATOM
3878
OE2
GLU
B
907
34.643
8.414
8.842
1.00
19.06
B


ATOM
3879
C
GLU
B
907
31.026
5.634
5.864
1.00
17.19
B


ATOM
3880
O
GLU
B
907
29.981
6.177
6.227
1.00
16.76
B


ATOM
3881
N
MET
B
908
31.066
4.819
4.819
1.00
15.73
B


ATOM
3882
CA
MET
B
908
29.840
4.561
4.076
1.00
17.55
B


ATOM
3883
CB
MET
B
908
30.165
3.859
2.755
1.00
17.66
B


ATOM
3884
CG
MET
B
908
31.054
4.709
1.842
1.00
18.47
B


ATOM
3885
SD
MET
B
908
31.344
4.017
0.197
1.00
19.83
B


ATOM
3886
CE
MET
B
908
32.363
2.584
0.608
1.00
20.34
B


ATOM
3887
C
MET
B
908
28.854
3.756
4.912
1.00
19.27
B


ATOM
3888
O
MET
B
908
27.654
4.057
4.944
1.00
18.84
B


ATOM
3889
N
MET
B
909
29.374
2.741
5.597
1.00
20.63
B


ATOM
3890
CA
MET
B
909
28.586
1.884
6.477
1.00
21.59
B


ATOM
3891
CB
MET
B
909
29.498
0.849
7.140
1.00
26.31
B


ATOM
3892
CG
MET
B
909
29.928
−0.280
6.249
1.00
31.81
B


ATOM
3893
SD
MET
B
909
28.744
−1.626
6.369
1.00
41.30
B


ATOM
3894
CE
MET
B
909
29.012
−2.122
8.117
1.00
35.86
B


ATOM
3895
C
MET
B
909
27.952
2.732
7.573
1.00
19.52
B


ATOM
3896
O
MET
B
909
26.767
2.603
7.873
1.00
16.91
B


ATOM
3897
N
SER
B
910
28.765
3.594
8.178
1.00
19.62
B


ATOM
3898
CA
SER
B
910
28.300
4.456
9.254
1.00
18.66
B


ATOM
3899
CB
SER
B
910
29.438
5.358
9.740
1.00
19.13
B


ATOM
3900
OG
SER
B
910
30.424
4.602
10.423
1.00
21.89
B


ATOM
3901
C
SER
B
910
27.108
5.308
8.840
1.00
18.32
B


ATOM
3902
O
SER
B
910
26.168
5.483
9.610
1.00
17.55
B


ATOM
3903
N
GLU
B
911
27.146
5.829
7.618
1.00
18.37
B


ATOM
3904
CA
GLU
B
911
26.068
6.669
7.112
1.00
17.93
B


ATOM
3905
CB
GLU
B
911
26.467
7.267
5.759
1.00
18.99
B


ATOM
3906
CG
GLU
B
911
25.386
8.098
5.091
1.00
23.81
B


ATOM
3907
CD
GLU
B
911
24.898
9.231
5.965
1.00
26.02
B


ATOM
3908
OE1
GLU
B
911
25.737
9.851
6.656
1.00
29.85
B


ATOM
3909
OE2
GLU
B
911
23.681
9.506
5.954
1.00
28.42
B


ATOM
3910
C
GLU
B
911
24.769
5.877
6.971
1.00
18.59
B


ATOM
3911
O
GLU
B
911
23.695
6.353
7.343
1.00
17.69
B


ATOM
3912
N
VAL
B
912
24.867
4.668
6.433
1.00
17.22
B


ATOM
3913
CA
VAL
B
912
23.682
3.837
6.255
1.00
18.22
B


ATOM
3914
CB
VAL
B
912
24.032
2.532
5.502
1.00
18.83
B


ATOM
3915
CG1
VAL
B
912
22.898
1.531
5.628
1.00
21.35
B


ATOM
3916
CG2
VAL
B
912
24.283
2.850
4.027
1.00
18.17
B


ATOM
3917
C
VAL
B
912
23.053
3.503
7.599
1.00
17.16
B


ATOM
3918
O
VAL
B
912
21.831
3.551
7.760
1.00
16.31
B


ATOM
3919
N
ILE
B
913
23.899
3.165
8.565
1.00
15.65
B


ATOM
3920
CA
ILE
B
913
23.435
2.821
9.899
1.00
17.18
B


ATOM
3921
CB
ILE
B
913
24.614
2.320
10.770
1.00
17.40
B


ATOM
3922
CG2
ILE
B
913
24.183
2.186
12.225
1.00
16.84
B


ATOM
3923
CG1
ILE
B
913
25.116
0.972
10.232
1.00
16.47
B


ATOM
3924
CD1
ILE
B
913
26.470
0.544
10.786
1.00
20.34
B


ATOM
3925
C
ILE
B
913
22.769
4.030
10.555
1.00
19.14
B


ATOM
3926
O
ILE
B
913
21.637
3.946
11.028
1.00
20.38
B


ATOM
3927
N
ALA
B
914
23.455
5.166
10.555
1.00
20.59
B


ATOM
3928
CA
ALA
B
914
22.905
6.366
11.175
1.00
21.55
B


ATOM
3929
CB
ALA
B
914
23.956
7.472
11.191
1.00
20.73
B


ATOM
3930
C
ALA
B
914
21.635
6.868
10.495
1.00
23.12
B


ATOM
3931
O
ALA
B
914
20.707
7.327
11.157
1.00
24.41
B


ATOM
3932
N
ALA
B
915
21.582
6.766
9.174
1.00
24.15
B


ATOM
3933
CA
ALA
B
915
20.427
7.263
8.438
1.00
23.02
B


ATOM
3934
CB
ALA
B
915
20.813
7.496
6.979
1.00
23.13
B


ATOM
3935
C
ALA
B
915
19.148
6.432
8.498
1.00
22.96
B


ATOM
3936
O
ALA
B
915
18.052
6.992
8.515
1.00
23.53
B


ATOM
3937
N
GLN
B
916
19.268
5.111
8.548
1.00
20.89
B


ATOM
3938
CA
GLN
B
916
18.074
4.282
8.535
1.00
22.00
B


ATOM
3939
CB
GLN
B
916
18.010
3.481
7.223
1.00
24.20
B


ATOM
3940
CG
GLN
B
916
18.095
4.282
5.923
1.00
27.17
B


ATOM
3941
CD
GLN
B
916
17.030
5.345
5.801
1.00
29.02
B


ATOM
3942
OE1
GLN
B
916
15.925
5.205
6.324
1.00
28.23
B


ATOM
3943
NE2
GLN
B
916
17.353
6.417
5.087
1.00
33.25
B


ATOM
3944
C
GLN
B
916
17.812
3.292
9.667
1.00
21.39
B


ATOM
3945
O
GLN
B
916
16.651
3.008
9.959
1.00
22.64
B


ATOM
3946
N
LEU
B
917
18.849
2.742
10.295
1.00
19.37
B


ATOM
3947
CA
LEU
B
917
18.588
1.727
11.317
1.00
18.64
B


ATOM
3948
CB
LEU
B
917
19.895
1.152
11.885
1.00
18.07
B


ATOM
3949
CG
LEU
B
917
20.687
0.240
10.936
1.00
20.90
B


ATOM
3950
CD1
LEU
B
917
21.614
−0.666
11.741
1.00
17.81
B


ATOM
3951
CD2
LEU
B
917
19.739
−0.612
10.115
1.00
20.60
B


ATOM
3952
C
LEU
B
917
17.635
2.090
12.450
1.00
17.99
B


ATOM
3953
O
LEU
B
917
16.745
1.303
12.777
1.00
19.33
B


ATOM
3954
N
PRO
B
918
17.793
3.270
13.068
1.00
17.70
B


ATOM
3955
CD
PRO
B
918
18.853
4.290
12.994
1.00
18.75
B


ATOM
3956
CA
PRO
B
918
16.848
3.575
14.148
1.00
18.53
B


ATOM
3957
CB
PRO
B
918
17.285
4.966
14.596
1.00
19.15
B


ATOM
3958
CG
PRO
B
918
18.779
4.916
14.375
1.00
17.58
B


ATOM
3959
C
PRO
B
918
15.400
3.538
13.636
1.00
18.88
B


ATOM
3960
O
PRO
B
918
14.521
2.939
14.257
1.00
15.75
B


ATOM
3961
N
LYS
B
919
15.176
4.173
12.490
1.00
18.61
B


ATOM
3962
CA
LYS
B
919
13.860
4.234
11.852
1.00
20.51
B


ATOM
3963
CB
LYS
B
919
13.960
5.063
10.569
1.00
24.87
B


ATOM
3964
CG
LYS
B
919
12.673
5.155
9.765
1.00
29.78
B


ATOM
3965
CD
LYS
B
919
12.926
5.776
8.402
1.00
34.28
B


ATOM
3966
CE
LYS
B
919
13.531
7.168
8.525
1.00
37.85
B


ATOM
3967
NZ
LYS
B
919
13.932
7.713
7.194
1.00
42.01
B


ATOM
3968
C
LYS
B
919
13.317
2.842
11.515
1.00
19.41
B


ATOM
3969
O
LYS
B
919
12.146
2.540
11.766
1.00
19.67
B


ATOM
3970
N
ILE
B
920
14.164
2.002
10.925
1.00
17.71
B


ATOM
3971
CA
ILE
B
920
13.764
0.644
10.573
1.00
17.37
B


ATOM
3972
CB
ILE
B
920
14.887
−0.077
9.796
1.00
17.05
B


ATOM
3973
CG2
ILE
B
920
14.474
−1.515
9.497
1.00
17.48
B


ATOM
3974
CG1
ILE
B
920
15.171
0.670
8.486
1.00
16.02
B


ATOM
3975
CD1
ILE
B
920
16.351
0.143
7.705
1.00
15.95
B


ATOM
3976
C
ILE
B
920
13.411
−0.172
11.825
1.00
17.73
B


ATOM
3977
O
ILE
B
920
12.357
−0.801
11.891
1.00
19.73
B


ATOM
3978
N
LEU
B
921
14.290
−0.153
12.821
1.00
18.28
B


ATOM
3979
CA
LEU
B
921
14.048
−0.894
14.058
1.00
17.30
B


ATOM
3980
CB
LEU
B
921
15.256
−0.761
14.991
1.00
17.29
B


ATOM
3981
CG
LEU
B
921
16.506
−1.550
14.568
1.00
19.30
B


ATOM
3982
CD1
LEU
B
921
17.685
−1.192
15.458
1.00
20.25
B


ATOM
3983
CD2
LEU
B
921
16.212
−3.049
14.650
1.00
18.96
B


ATOM
3984
C
LEU
B
921
12.779
−0.405
14.759
1.00
18.82
B


ATOM
3985
O
LEU
B
921
12.060
−1.189
15.386
1.00
18.43
B


ATOM
3986
N
ALA
B
922
12.506
0.891
14.650
1.00
18.13
B


ATOM
3987
CA
ALA
B
922
11.316
1.475
15.260
1.00
20.31
B


ATOM
3988
CB
ALA
B
922
11.459
2.994
15.329
1.00
18.87
B


ATOM
3989
C
ALA
B
922
10.062
1.102
14.468
1.00
21.56
B


ATOM
3990
O
ALA
B
922
8.958
1.530
14.799
1.00
21.69
B


ATOM
3991
N
GLY
B
923
10.240
0.312
13.415
1.00
21.30
B


ATOM
3992
CA
GLY
B
923
9.111
−0.104
12.600
1.00
22.52
B


ATOM
3993
C
GLY
B
923
8.491
1.015
11.784
1.00
23.20
B


ATOM
3994
O
GLY
B
923
7.301
0.977
11.474
1.00
24.52
B


ATOM
3995
N
MET
B
924
9.289
2.010
11.421
1.00
23.73
B


ATOM
3996
CA
MET
B
924
8.778
3.134
10.651
1.00
24.27
B


ATOM
3997
CB
MET
B
924
9.433
4.424
11.137
1.00
26.89
B


ATOM
3998
CG
MET
B
924
9.330
4.611
12.645
1.00
29.64
B


ATOM
3999
SD
MET
B
924
7.622
4.544
13.234
1.00
36.14
B


ATOM
4000
CE
MET
B
924
7.016
6.119
12.590
1.00
32.22
B


ATOM
4001
C
MET
B
924
8.968
2.973
9.141
1.00
22.97
B


ATOM
4002
O
MET
B
924
9.237
3.939
8.434
1.00
24.86
B


ATOM
4003
N
VAL
B
925
8.834
1.737
8.669
1.00
22.70
B


ATOM
4004
CA
VAL
B
925
8.945
1.394
7.254
1.00
20.11
B


ATOM
4005
CB
VAL
B
925
10.357
0.879
6.873
1.00
21.32
B


ATOM
4006
CG1
VAL
B
925
11.396
1.961
7.137
1.00
18.72
B


ATOM
4007
CG2
VAL
B
925
10.681
−0.404
7.648
1.00
19.44
B


ATOM
4008
C
VAL
B
925
7.951
0.269
7.008
1.00
20.72
B


ATOM
4009
O
VAL
B
925
7.427
−0.317
7.958
1.00
17.16
B


ATOM
4010
N
LYS
B
926
7.698
−0.039
5.740
1.00
20.24
B


ATOM
4011
CA
LYS
B
926
6.756
−1.096
5.405
1.00
22.19
B


ATOM
4012
CB
LYS
B
926
5.693
−0.583
4.431
1.00
23.49
B


ATOM
4013
CG
LYS
B
926
4.697
−1.663
4.034
1.00
27.62
B


ATOM
4014
CD
LYS
B
926
3.735
−1.209
2.948
1.00
29.56
B


ATOM
4015
CE
LYS
B
926
2.774
−2.338
2.595
1.00
32.37
B


ATOM
4016
NZ
LYS
B
926
1.833
−1.961
1.507
1.00
35.72
B


ATOM
4017
C
LYS
B
926
7.419
−2.320
4.789
1.00
22.27
B


ATOM
4018
O
LYS
B
926
7.812
−2.300
3.620
1.00
20.78
B


ATOM
4019
N
PRO
B
927
7.555
−3.405
5.568
1.00
23.59
B


ATOM
4020
CD
PRO
B
927
7.287
−3.541
7.009
1.00
23.58
B


ATOM
4021
CA
PRO
B
927
8.177
−4.619
5.035
1.00
23.23
B


ATOM
4022
CB
PRO
B
927
8.399
−5.481
6.280
1.00
24.23
B


ATOM
4023
CG
PRO
B
927
8.372
−4.483
7.429
1.00
26.39
B


ATOM
4024
C
PRO
B
927
7.156
−5.251
4.095
1.00
23.54
B


ATOM
4025
O
PRO
B
927
5.968
−5.295
4.417
1.00
23.62
B


ATOM
4026
N
LEU
B
928
7.598
−5.723
2.935
1.00
21.25
B


ATOM
4027
CA
LEU
B
928
6.672
−6.343
2.000
1.00
21.62
B


ATOM
4028
CB
LEU
B
928
7.083
−6.038
0.553
1.00
20.54
B


ATOM
4029
CG
LEU
B
928
7.097
−4.547
0.191
1.00
19.73
B


ATOM
4030
CD1
LEU
B
928
7.385
−4.376
−1.299
1.00
19.70
B


ATOM
4031
CD2
LEU
B
928
5.751
−3.916
0.530
1.00
19.69
B


ATOM
4032
C
LEU
B
928
6.635
−7.845
2.250
1.00
22.19
B


ATOM
4033
O
LEU
B
928
7.670
−8.481
2.447
1.00
20.86
B


ATOM
4034
N
LEU
B
929
5.431
−8.404
2.255
1.00
22.00
B


ATOM
4035
CA
LEU
B
929
5.252
−9.828
2.499
1.00
21.93
B


ATOM
4036
CB
LEU
B
929
4.480
−10.042
3.804
1.00
20.94
B


ATOM
4037
CG
LEU
B
929
5.072
−9.503
5.105
1.00
20.69
B


ATOM
4038
CD1
LEU
B
929
4.053
−9.654
6.233
1.00
21.83
B


ATOM
4039
CD2
LEU
B
929
6.350
−10.255
5.429
1.00
18.32
B


ATOM
4040
C
LEU
B
929
4.498
−10.517
1.370
1.00
23.95
B


ATOM
4041
O
LEU
B
929
3.556
−9.961
0.799
1.00
22.92
B


ATOM
4042
N
PHE
B
930
4.923
−11.736
1.058
1.00
25.00
B


ATOM
4043
CA
PHE
B
930
4.280
−12.533
0.025
1.00
27.93
B


ATOM
4044
CB
PHE
B
930
5.275
−13.520
−0.571
1.00
26.70
B


ATOM
4045
CG
PHE
B
930
6.283
−12.887
−1.474
1.00
27.33
B


ATOM
4046
CD1
PHE
B
930
5.979
−12.641
−2.807
1.00
26.64
B


ATOM
4047
CD2
PHE
B
930
7.531
−12.521
−0.989
1.00
26.19
B


ATOM
4048
CE1
PHE
B
930
6.910
−12.042
−3.650
1.00
28.73
B


ATOM
4049
CE2
PHE
B
930
8.470
−11.920
−1.822
1.00
27.94
B


ATOM
4050
CZ
PHE
B
930
8.158
−11.680
−3.154
1.00
28.06
B


ATOM
4051
C
PHE
B
930
3.120
−13.302
0.645
1.00
29.58
B


ATOM
4052
O
PHE
B
930
2.159
−13.651
−0.039
1.00
30.87
B


ATOM
4053
N
HIS
B
931
3.220
−13.560
1.944
1.00
31.13
B


ATOM
4054
CA
HIS
B
931
2.190
−14.303
2.660
1.00
34.65
B


ATOM
4055
CB
HIS
B
931
2.738
−15.668
3.070
1.00
33.95
B


ATOM
4056
CG
HIS
B
931
3.394
−16.408
1.948
1.00
35.58
B


ATOM
4057
CD2
HIS
B
931
4.685
−16.765
1.751
1.00
35.09
B


ATOM
4058
ND1
HIS
B
931
2.704
−16.827
0.831
1.00
35.08
B


ATOM
4059
CE1
HIS
B
931
3.543
−17.408
−0.008
1.00
36.03
B


ATOM
4060
NE2
HIS
B
931
4.751
−17.384
0.526
1.00
35.91
B


ATOM
4061
C
HIS
B
931
1.703
−13.556
3.892
1.00
37.35
B


ATOM
4062
O
HIS
B
931
2.457
−12.824
4.532
1.00
36.89
B


ATOM
4063
N
LYS
B
932
0.433
−13.753
4.221
1.00
41.41
B


ATOM
4064
CA
LYS
B
932
−0.177
−13.105
5.376
1.00
45.14
B


ATOM
4065
CB
LYS
B
932
−1.702
−13.161
5.241
1.00
46.49
B


ATOM
4066
CG
LYS
B
932
−2.196
−14.436
4.585
1.00
47.98
B


ATOM
4067
CD
LYS
B
932
−3.679
−14.370
4.259
1.00
50.28
B


ATOM
4068
CE
LYS
B
932
−4.073
−15.492
3.306
1.00
50.95
B


ATOM
4069
NZ
LYS
B
932
−3.678
−16.832
3.824
1.00
51.90
B


ATOM
4070
C
LYS
B
932
0.261
−13.748
6.690
1.00
45.88
B


ATOM
4071
O
LYS
B
932
0.973
−14.774
6.641
1.00
46.33
B


ATOM
4072
OXT
LYS
B
932
−0.114
−13.213
7.755
1.00
47.76
B


ATOM
4073
S
SO4
Z
1
17.414
−1.312
−17.993
1.00
31.48
Z


ATOM
4074
O1
SO4
Z
1
18.530
−2.281
−17.932
1.00
35.16
Z


ATOM
4075
O2
SO4
Z
1
17.425
−0.473
−16.787
1.00
32.29
Z


ATOM
4076
O3
SO4
Z
1
17.593
−0.480
−19.187
1.00
31.61
Z


ATOM
4077
O4
SO4
Z
1
16.139
−2.038
−18.069
1.00
33.87
Z


ATOM
4078
O
HOH
W
1
9.851
−0.179
33.299
1.00
14.73
W


ATOM
4079
O
HOH
W
2
22.939
−10.562
−9.981
1.00
15.38
W


ATOM
4080
O
HOH
W
3
2.083
29.100
25.389
1.00
20.40
W


ATOM
4081
O
HOH
W
4
14.086
−2.560
0.315
1.00
17.07
W


ATOM
4082
O
HOH
W
5
27.328
−10.890
1.331
1.00
18.73
W


ATOM
4083
O
HOH
W
6
13.331
5.641
28.674
1.00
19.86
W


ATOM
4084
O
HOH
W
7
13.186
1.399
47.673
1.00
13.95
W


ATOM
4085
O
HOH
W
8
32.971
−11.715
0.505
1.00
14.94
W


ATOM
4086
O
HOH
W
9
18.332
−4.869
5.470
1.00
18.48
W


ATOM
4087
O
HOH
W
10
12.895
−0.329
56.919
1.00
18.21
W


ATOM
4088
O
HOH
W
11
39.458
−17.312
7.769
1.00
30.23
W


ATOM
4089
O
HOH
W
12
26.010
−12.904
−3.995
1.00
34.91
W


ATOM
4090
O
HOH
W
13
10.307
23.211
14.451
1.00
24.90
W


ATOM
4091
O
HOH
W
14
33.794
−3.491
−3.298
1.00
24.71
W


ATOM
4092
O
HOH
W
15
−7.542
−1.149
46.176
1.00
17.56
W


ATOM
4093
O
HOH
W
16
10.481
5.430
28.973
1.00
16.76
W


ATOM
4094
O
HOH
W
17
9.010
1.461
31.392
1.00
20.19
W


ATOM
4095
O
HOH
W
18
0.442
−1.822
32.126
1.00
27.35
W


ATOM
4096
O
HOH
W
19
20.106
−2.758
6.202
1.00
22.10
W


ATOM
4097
O
HOH
W
20
6.858
5.226
−11.172
1.00
19.86
W


ATOM
4098
O
HOH
W
21
3.112
31.643
22.889
1.00
22.74
W


ATOM
4099
O
HOH
W
22
10.057
15.524
34.676
1.00
20.39
W


ATOM
4100
O
HOH
W
23
28.343
−13.760
−2.951
1.00
27.79
W


ATOM
4101
O
HOH
W
24
5.302
8.903
42.508
1.00
17.97
W


ATOM
4102
O
HOH
W
25
12.929
28.598
20.593
1.00
23.80
W


ATOM
4103
O
HOH
W
26
−4.534
17.192
43.743
1.00
28.92
W


ATOM
4104
O
HOH
W
27
9.676
3.409
22.849
1.00
14.96
W


ATOM
4105
O
HOH
W
28
13.824
−6.363
9.101
1.00
24.33
W


ATOM
4106
O
HOH
W
29
19.783
−1.498
23.163
1.00
21.54
W


ATOM
4107
O
HOH
W
30
7.516
21.308
40.840
1.00
39.46
W


ATOM
4108
O
HOH
W
31
20.250
−8.806
18.170
1.00
22.74
W


ATOM
4109
O
HOH
W
32
20.825
−10.938
−8.107
1.00
23.11
W


ATOM
4110
O
HOH
W
33
−1.545
−0.716
48.089
1.00
19.38
W


ATOM
4111
O
HOH
W
34
3.305
−1.599
49.132
1.00
34.02
W


ATOM
4112
O
HOH
W
35
40.480
−6.360
12.399
1.00
27.56
W


ATOM
4113
O
HOH
W
36
11.493
20.832
38.950
1.00
38.71
W


ATOM
4114
O
HOH
W
37
9.120
1.197
21.414
1.00
23.98
W


ATOM
4115
O
HOH
W
38
−1.682
3.281
52.013
1.00
22.24
W


ATOM
4116
O
HOH
W
39
−11.086
22.915
35.681
1.00
32.42
W


ATOM
4117
O
HOH
W
40
12.002
7.533
−1.688
1.00
30.69
W


ATOM
4118
O
HOH
W
41
14.518
−13.452
−19.077
1.00
26.25
W


ATOM
4119
O
HOH
W
42
18.500
30.309
24.738
1.00
37.66
W


ATOM
4120
O
HOH
W
43
14.005
−7.837
26.712
1.00
24.93
W


ATOM
4121
O
HOH
W
44
2.873
−1.026
35.419
1.00
35.46
W


ATOM
4122
O
HOH
W
45
19.791
−5.878
22.089
1.00
24.74
W


ATOM
4123
O
HOH
W
46
36.617
−7.101
−5.193
1.00
27.22
W


ATOM
4124
O
HOH
W
47
17.997
16.706
17.050
1.00
23.35
W


ATOM
4125
O
HOH
W
48
12.818
29.647
30.373
1.00
34.99
W


ATOM
4126
O
HOH
W
49
35.741
2.637
0.675
1.00
29.22
W


ATOM
4127
O
HOH
W
50
−0.698
−9.676
42.142
1.00
30.67
W


ATOM
4128
O
HOH
W
51
−0.525
29.866
21.575
1.00
19.53
W


ATOM
4129
O
HOH
W
52
18.379
−2.516
47.069
1.00
27.04
W


ATOM
4130
O
HOH
W
53
8.722
0.737
27.146
1.00
31.04
W


ATOM
4131
O
HOH
W
54
20.510
8.743
13.356
1.00
23.93
W


ATOM
4132
O
HOH
W
55
12.649
20.284
36.357
1.00
16.97
W


ATOM
4133
O
HOH
W
56
−8.042
11.472
43.548
1.00
24.46
W


ATOM
4134
O
HOH
W
57
−11.476
3.549
43.258
1.00
25.26
W


ATOM
4135
O
HOH
W
58
7.056
−16.459
−15.106
1.00
23.80
W


ATOM
4136
O
HOH
W
59
21.350
−22.318
13.143
1.00
34.05
W


ATOM
4137
O
HOH
W
60
28.062
12.099
16.977
1.00
26.29
W


ATOM
4138
O
HOH
W
61
−22.171
4.158
40.700
1.00
28.15
W


ATOM
4139
O
HOH
W
62
22.437
24.881
26.553
1.00
20.93
W


ATOM
4140
O
HOH
W
63
28.474
13.733
32.727
1.00
30.22
W


ATOM
4141
O
HOH
W
64
1.626
−6.963
38.739
1.00
22.58
W


ATOM
4142
O
HOH
W
65
5.955
33.007
28.845
1.00
42.67
W


ATOM
4143
O
HOH
W
66
7.548
3.514
24.485
1.00
25.19
W


ATOM
4144
O
HOH
W
67
28.084
10.733
25.158
1.00
32.12
W


ATOM
4145
O
HOH
W
68
14.819
−4.756
10.909
1.00
22.88
W


ATOM
4146
O
HOH
W
69
12.512
−3.850
11.912
1.00
30.27
W


ATOM
4147
O
HOH
W
70
23.580
−16.334
5.829
1.00
22.52
W


ATOM
4148
O
HOH
W
71
10.565
−11.166
−16.058
1.00
23.71
W


ATOM
4149
O
HOH
W
72
2.064
13.163
18.256
1.00
38.01
W


ATOM
4150
O
HOH
W
73
24.352
27.565
20.778
1.00
29.09
W


ATOM
4151
O
HOH
W
74
13.534
11.655
46.723
1.00
29.05
W


ATOM
4152
O
HOH
W
75
−3.751
1.854
53.213
1.00
24.50
W


ATOM
4153
O
HOH
W
76
14.249
−6.307
6.318
1.00
33.71
W


ATOM
4154
O
HOH
W
77
8.346
20.512
13.638
1.00
29.91
W


ATOM
4155
O
HOH
W
78
10.659
−27.801
−3.102
1.00
25.66
W


ATOM
4156
O
HOH
W
79
29.300
−5.213
−7.941
1.00
27.88
W


ATOM
4157
O
HOH
W
80
23.744
15.309
11.455
1.00
36.84
W


ATOM
4158
O
HOH
W
81
26.341
−4.131
−16.979
1.00
37.38
W


ATOM
4159
O
HOH
W
82
−5.101
−2.239
21.176
1.00
49.05
W


ATOM
4160
O
HOH
W
83
8.948
−10.743
1.764
1.00
25.57
W


ATOM
4161
O
HOH
W
84
22.426
8.856
3.497
1.00
30.12
W


ATOM
4162
O
HOH
W
85
15.590
−6.464
2.357
1.00
20.20
W


ATOM
4163
O
HOH
W
86
22.984
−28.399
7.053
1.00
43.09
W


ATOM
4164
O
HOH
W
87
35.903
−1.727
10.279
1.00
24.30
W


ATOM
4165
O
HOH
W
88
7.456
3.549
31.583
1.00
22.42
W


ATOM
4166
O
HOH
W
89
7.855
−6.471
46.303
1.00
30.69
W


ATOM
4167
O
HOH
W
90
43.114
−4.754
5.804
1.00
31.47
W


ATOM
4168
O
HOH
W
91
23.688
18.339
28.249
1.00
35.33
W


ATOM
4169
O
HOH
W
92
8.671
30.830
26.750
1.00
25.23
W


ATOM
4170
O
HOH
W
93
21.069
9.806
42.796
1.00
22.22
W


ATOM
4171
O
HOH
W
94
34.235
3.943
13.825
1.00
29.92
W


ATOM
4172
O
HOH
W
95
4.325
−12.649
42.865
1.00
33.49
W


ATOM
4173
O
HOH
W
96
4.905
−14.665
5.831
1.00
30.26
W


ATOM
4174
O
HOH
W
97
17.850
0.612
51.901
1.00
26.30
W


ATOM
4175
O
HOH
W
98
29.845
−26.714
−0.530
1.00
32.22
W


ATOM
4176
O
HOH
W
99
21.826
3.590
34.558
1.00
30.54
W


ATOM
4177
O
HOH
W
100
8.730
5.195
6.121
1.00
31.99
W


ATOM
4178
O
HOH
W
101
−12.510
−0.569
35.114
1.00
39.35
W


ATOM
4179
O
HOH
W
102
9.974
18.335
15.716
1.00
30.38
W


ATOM
4180
O
HOH
W
103
−20.727
6.780
40.198
1.00
31.21
W


ATOM
4181
O
HOH
W
104
17.245
3.775
27.753
1.00
23.95
W


ATOM
4182
O
HOH
W
105
12.204
31.282
32.900
1.00
47.25
W


ATOM
4183
O
HOH
W
106
30.849
−13.455
−10.120
1.00
44.05
W


ATOM
4184
O
HOH
W
107
31.232
−11.424
−3.737
1.00
34.09
W


ATOM
4185
O
HOH
W
108
0.616
0.645
30.187
1.00
19.02
W


ATOM
4186
O
HOH
W
109
9.969
10.406
39.896
1.00
41.21
W


ATOM
4187
O
HOH
W
110
4.951
−13.348
36.812
1.00
25.64
W


ATOM
4188
O
HOH
W
111
24.217
0.126
32.380
1.00
42.27
W


ATOM
4189
O
HOH
W
112
7.760
3.239
27.484
1.00
31.56
W


ATOM
4190
O
HOH
W
113
−13.150
10.929
35.305
1.00
37.37
W


ATOM
4191
O
HOH
W
114
14.414
10.760
49.023
1.00
25.40
W


ATOM
4192
O
HOH
W
115
9.753
12.679
37.102
1.00
37.47
W


ATOM
4193
O
HOH
W
116
−4.457
0.109
25.639
1.00
31.43
W


ATOM
4194
O
HOH
W
117
31.098
5.122
20.729
1.00
32.11
W


ATOM
4195
O
HOH
W
118
9.748
22.778
39.579
1.00
29.38
W


ATOM
4196
O
HOH
W
119
15.530
−4.123
52.634
1.00
29.51
W


ATOM
4197
O
HOH
W
120
14.408
−3.786
6.247
1.00
35.75
W


ATOM
4198
O
HOH
W
121
3.061
16.521
16.785
1.00
25.91
W


ATOM
4199
O
HOH
W
122
39.801
−19.133
1.482
1.00
26.72
W


ATOM
4200
O
HOH
W
123
37.378
−1.402
24.102
1.00
39.79
W


ATOM
4201
O
HOH
W
124
14.576
12.610
44.487
1.00
30.08
W


ATOM
4202
O
HOH
W
125
4.145
16.097
43.565
1.00
34.79
W


ATOM
4203
O
HOH
W
126
7.682
25.781
13.009
1.00
45.48
W


ATOM
4204
O
HOH
W
127
9.845
−12.141
9.020
1.00
29.42
W


ATOM
4205
O
HOH
W
128
15.739
10.997
−9.996
1.00
27.09
W


ATOM
4206
O
HOH
W
129
6.716
10.052
44.773
1.00
20.65
W


ATOM
4207
O
HOH
W
130
14.744
−8.445
4.732
1.00
23.00
W


ATOM
4208
O
HOH
W
131
21.909
24.767
16.946
1.00
31.22
W


ATOM
4209
O
HOH
W
132
33.120
−12.601
−1.941
1.00
27.91
W


ATOM
4210
O
HOH
W
133
23.283
3.901
−16.585
1.00
40.81
W


ATOM
4211
O
HOH
W
134
27.581
13.334
14.368
1.00
31.58
W


ATOM
4212
O
HOH
W
135
23.546
−8.108
−4.594
1.00
38.50
W


ATOM
4213
O
HOH
W
136
3.316
−6.614
1.955
1.00
31.34
W


ATOM
4214
O
HOH
W
137
17.363
1.926
49.485
1.00
28.70
W


ATOM
4215
O
HOH
W
138
38.393
−7.509
−2.153
1.00
31.36
W


ATOM
4216
O
HOH
W
139
14.920
−4.060
2.471
1.00
31.77
W


ATOM
4217
O
HOH
W
140
38.118
−0.901
8.667
1.00
31.86
W


ATOM
4218
O
HOH
W
141
26.383
5.332
2.546
1.00
34.89
W


ATOM
4219
O
HOH
W
142
35.405
3.798
3.233
1.00
34.38
W


ATOM
4220
O
HOH
W
143
11.409
−21.800
−16.697
1.00
35.84
W


ATOM
4221
O
HOH
W
144
39.725
−6.596
7.646
1.00
38.73
W


ATOM
4222
O
HOH
W
145
17.070
6.806
11.706
1.00
34.49
W


ATOM
4223
O
HOH
W
146
3.371
3.664
29.494
1.00
39.22
W


ATOM
4224
O
HOH
W
147
13.400
6.010
35.121
1.00
36.31
W


ATOM
4225
O
HOH
W
148
11.012
18.450
40.465
1.00
37.80
W


ATOM
4226
O
HOH
W
149
35.666
−17.196
−3.005
1.00
33.54
W


ATOM
4227
O
HOH
W
150
27.587
−15.335
−11.411
1.00
32.63
W


ATOM
4228
O
HOH
W
151
24.903
−9.920
−1.819
1.00
37.55
W


ATOM
4229
O
HOH
W
152
15.833
8.081
−12.357
1.00
42.37
W


ATOM
4230
O
HOH
W
153
28.438
16.821
21.396
1.00
44.90
W


ATOM
4231
O
HOH
W
154
21.332
29.602
23.542
1.00
39.67
W


ATOM
4232
O
HOH
W
155
12.772
−9.868
3.678
1.00
36.84
W


ATOM
4233
O
HOH
W
156
16.961
−7.689
35.260
1.00
44.42
W


ATOM
4234
O
HOH
W
157
10.499
10.751
16.433
1.00
34.39
W


ATOM
4235
O
HOH
W
158
28.327
−5.237
−10.882
1.00
45.84
W


ATOM
4236
O
HOH
W
159
36.087
4.558
6.039
1.00
28.34
W


ATOM
4237
O
HOH
W
160
−0.994
29.266
35.756
1.00
35.83
W


ATOM
4238
O
HOH
W
161
0.695
−6.498
29.582
1.00
33.46
W


ATOM
4239
O
HOH
W
162
26.373
21.757
15.011
1.00
43.14
W


ATOM
4240
O
HOH
W
163
15.148
32.436
21.985
1.00
36.34
W


ATOM
4241
O
HOH
W
164
−3.288
−2.573
49.020
1.00
37.67
W


ATOM
4242
O
HOH
W
165
−1.628
26.470
37.063
1.00
33.28
W


ATOM
4243
O
HOH
W
166
27.897
14.312
24.143
1.00
35.59
W


ATOM
4244
O
HOH
W
167
7.738
17.438
39.142
1.00
46.82
W


ATOM
4245
O
HOH
W
168
10.899
4.880
52.240
1.00
32.86
W


ATOM
4246
O
HOH
W
169
10.635
−22.038
3.450
1.00
43.02
W


ATOM
4247
O
HOH
W
170
25.343
2.041
28.575
1.00
43.36
W


ATOM
4248
O
HOH
W
171
4.243
6.461
−2.841
1.00
33.86
W


ATOM
4249
O
HOH
W
172
4.073
6.130
−9.321
1.00
37.81
W


ATOM
4250
O
HOH
W
173
7.805
−22.135
−12.033
1.00
33.34
W


ATOM
4251
O
HOH
W
174
13.170
−15.783
10.760
1.00
40.16
W


ATOM
4252
O
HOH
W
175
15.268
−15.546
12.623
1.00
39.35
W


ATOM
4253
O
HOH
W
176
8.067
−4.029
50.607
1.00
41.24
W


ATOM
4254
O
HOH
W
177
−2.564
26.998
20.110
1.00
40.38
W


ATOM
4255
O
HOH
W
178
20.599
−7.598
44.029
1.00
35.32
W


ATOM
4256
O
HOH
W
179
7.493
−14.259
8.323
1.00
45.07
W


ATOM
4257
N1
989
C
701
12.950
16.155
29.632
1.00
25.58
C


ATOM
4258
C2
989
C
701
12.751
15.346
28.400
1.00
26.75
C


ATOM
4259
C3
989
C
701
11.423
15.061
28.357
1.00
25.91
C


ATOM
4260
C4
989
C
701
10.740
15.698
29.489
1.00
26.53
C


ATOM
4261
C5
989
C
701
11.639
16.305
30.277
1.00
24.85
C


ATOM
4262
C6
989
C
701
11.345
17.031
31.471
1.00
25.38
C


ATOM
4263
N7
989
C
701
11.135
17.620
32.434
1.00
28.13
C


ATOM
4264
C8
989
C
701
14.187
16.785
30.127
1.00
23.90
C


ATOM
4265
C12
989
C
701
13.748
15.000
27.362
1.00
26.02
C


ATOM
4266
C13
989
C
701
15.088
14.717
27.732
1.00
26.27
C


ATOM
4267
C14
989
C
701
16.102
14.633
26.756
1.00
27.92
C


ATOM
4268
C15
989
C
701
15.772
14.704
25.388
1.00
28.20
C


ATOM
4269
C16
989
C
701
14.419
14.901
24.980
1.00
26.87
C


ATOM
4270
C17
989
C
701
13.419
15.084
25.984
1.00
27.22
C


ATOM
4271
N18
989
C
701
16.760
14.547
24.458
1.00
30.23
C


ATOM
4272
C19
989
C
701
16.515
14.415
23.126
1.00
31.26
C


ATOM
4273
O20
989
C
701
15.208
14.452
22.722
1.00
31.21
C


ATOM
4274
C21
989
C
701
14.108
14.960
23.483
1.00
29.70
C


ATOM
4275
C22
989
C
701
12.917
14.062
23.101
1.00
28.20
C


ATOM
4276
C26
989
C
701
13.888
16.419
23.039
1.00
27.96
C


ATOM
4277
S30
989
C
701
17.846
14.580
22.146
1.00
28.30
C


ATOM
4278
N1
989
D
701
28.639
−9.086
6.656
1.00
28.57
D


ATOM
4279
C2
989
D
701
27.632
−8.815
7.706
1.00
29.39
D


ATOM
4280
C3
989
D
701
26.668
−9.755
7.546
1.00
27.96
D


ATOM
4281
C4
989
D
701
26.974
−10.590
6.385
1.00
28.44
D


ATOM
4282
C5
989
D
701
28.128
−10.194
5.838
1.00
28.00
D


ATOM
4283
C6
989
D
701
28.775
−10.812
4.721
1.00
29.08
D


ATOM
4284
N7
989
D
701
29.314
−11.293
3.826
1.00
32.15
D


ATOM
4285
C8
989
D
701
30.021
−8.594
6.590
1.00
27.50
D


ATOM
4286
C12
989
D
701
27.714
−7.844
8.821
1.00
29.66
D


ATOM
4287
C13
989
D
701
28.293
−6.561
8.626
1.00
30.33
D


ATOM
4288
C14
989
D
701
28.500
−5.693
9.723
1.00
32.12
D


ATOM
4289
C15
989
D
701
28.076
−6.071
11.018
1.00
31.15
D


ATOM
4290
C16
989
D
701
27.461
−7.340
11.226
1.00
31.11
D


ATOM
4291
C17
989
D
701
27.287
−8.212
10.117
1.00
30.39
D


ATOM
4292
N18
989
D
701
28.293
−5.221
12.072
1.00
33.73
D


ATOM
4293
C19
989
D
701
27.907
−5.501
13.348
1.00
34.14
D


ATOM
4294
O20
989
D
701
27.191
−6.652
13.554
1.00
33.18
D


ATOM
4295
C21
989
D
701
26.998
−7.721
12.626
1.00
32.21
D


ATOM
4296
C22
989
D
701
25.485
−8.011
12.650
1.00
32.12
D


ATOM
4297
C26
989
D
701
27.816
−8.917
13.151
1.00
34.10
D


ATOM
4298
S30
989
D
701
28.475
−4.462
14.528
1.00
34.00
D









OTHER EMBODIMENTS
A number of embodiments of the invention have been described. Nevertheless, it will be understood that various modifications may be made. For example, a structure of progesterone receptor can be determined where progesterone receptor is bound to a non-steroidal agent other than tanaproget. Accordingly, other embodiments are within the scope of the following claims.

## Claims

1. A method of designing or selecting a non-steroidal candidate agent that interacts with a progesterone receptor, comprising:
(a) utilizing the three-dimensional structural coordinates of the progesterone receptor ligand binding domain:non-steroidal ligand complex of Table 2 ± a root mean square deviation for alpha carbon atoms of not more than 1.5 Å, to generate a three-dimensional model wherein said non-steroidal ligand from Table 2 forms a favorable hydrogen bond, hydrophobic and/or electrostatic interaction between said non-steroid ligand and Asn719 and Gln725, and between one or more of Leu797, Arg766, Thr894 or Cys891;
(b) identifying the amino acid residues forming a non-steroidal ligand binding pocket of the progesterone receptor ligand binding domain from the three-dimensional model in step (a) in order to generate a three-dimensional representation of the non-steroidal ligand binding pocket, wherein the non-steroidal ligand binding pocket comprises amino acids Ile699, Ala701, Leu714, Leu715, Leu718, Asn719, Leu721, Gln725, Trp755, Met756, Met759, Val760, Leu763, Arg766, Ser767, Tyr777, Phe778, Ala779, Leu782, Phe794, Leu797, Cys798, Met801, Ile804, Leu887, His888, Tyr890, Cys891, Asn893, Thr894, Phe895, Ser898, Leu901, Val903, Phe905, Met909, Ile913, and Leu917 according to Table 2, ± a root mean square deviation for alpha carbon atoms of not more than 1.5 Å, and wherein said three-dimensional representation of the non-steroidal ligand binding pocket optionally has the non-steroidal ligand from step (a) present or absent;
(c) employing said three dimensional representation from step (b) to design or select said candidate agent such that the favorable interactions from step (a) are maintained between the candidate non-steroidal ligand and the progesterone receptor ligand binding pocket;
(d) synthesizing said candidate agent; and
(e) contacting said candidate agent with said progesterone receptor ligand binding domain to determine the ability of said candidate agent to interact or bind said progesterone receptor ligand binding domain;
whereby the detection of the ability of said candidate agent to interact or bind said progesterone receptor ligand binding domain thereby identifies said candidate agent as an agent that interacts with the progesterone receptor.

2. A method of designing or selecting a non-steroidal candidate agent that interacts with a progesterone receptor, comprising:
(a) utilizing the three-dimensional structural coordinates of the progesterone receptor ligand binding domain:non-steroidal ligand complex of Table 2± a root mean square deviation for alpha carbon atoms of not more than 1.5 Å, to generate a three-dimensional model wherein said non-steroidal ligand from Table 2 forms a favorable hydrogen bond, hydrophobic and/or electrostatic interaction between said non-steroid ligand and Asn719 and Gln725, and between one or more of Leu797, Arg766, Thr894 or Cys891;
(b) identifying the amino acid residues forming a non-steroidal ligand binding pocket of the progesterone receptor ligand binding domain from the three-dimensional model in step (a) in order to generate a three-dimensional representation of the non-steroidal ligand binding pocket, wherein the non-steroidal ligand binding pocket comprises amino acids Ile699, Ala701, Leu714, Leu715, Leu718, Asn719, Leu721, Gln725, Trp755, Met756, Met759, Val760, Leu763, Arg766, Ser767, Tyr777, Phe778, Ala779, Leu782, Phe794, Leu797, Cys798, Met801, Ile804, Leu887, His888, Tyr890, Cys891, Asn893, Thr894, Phe895, Ser898, Leu901, Val903, Phe905, Met909, Ile913, and Leu917, according to Table 2, ± a root mean square deviation for alpha carbon atoms of not more than 1.5 Å and wherein said three-dimensional representation of the non-steroidal ligand binding pocket optionally has the non-steroidal ligand from step(a) present or absent;
(c) employing said three dimensional representation from step (b) to design or select said candidate agent such that the favorable interactions from step (a) are maintained between the candidate non-steroidal ligand and the progesterone receptor ligand binding pocket;
(d) obtaining said candidate agent; and
(e) contacting in vitro or in vivo said candidate agent with a polypeptide comprising said progesterone receptor ligand binding domain to determine the ability of said candidate agent to interact or bind said progesterone receptor ligand binding domain;
whereby the detection of the ability of said candidate agent to interact or bind said progesterone receptor ligand binding domain thereby identifies said candidate agent as an agent that interacts with the progesterone receptor.

3. The method of claim 1 or 2, wherein the progesterone receptor ligand binding domain comprises amino acids Gln682 to Lys932 of SEQ ID NO:4.

4. The method of claim 1 or 2, wherein the non-steroidal ligand is tanaproget.

5. The method of claim 1 or 2, wherein the three dimensional model of step (a) comprises structural coordinates of atoms of the candidate agent.

6. The method of claim 1 or 2, wherein the structural coordinates of the progesterone receptor ligand binding domain: non-steroidal ligand complex are according to Table 2, ± a root mean square deviation for alpha carbon atoms of not more than 1.0 Å.

7. The method of claim 1 or 2, wherein the structural coordinates of the progesterone receptor ligand binding domain:non-steroidal ligand complex are according to Table 2, ± a root mean square deviation for alpha carbon atoms of not more than 0.5 Å.

8. The method of claim 1 or 2, further comprising altering a computer-displayed representation of the non-steroidal ligand in the three dimensional model of step (a) or (b).

9. The method of claim 8, wherein altering the computer-displayed representation of the non-steroidal ligand comprises changing the structural coordinates of the non-steroidal ligand.

10. The method of claim 8, wherein altering the computer-displayed representation of the non-steroidal ligand comprises changing the chemical structure of the non-steroidal ligand.

11. The method of claim 8, wherein altering the computer-displayed representation of the non-steroidal ligand comprises superimposing a three dimensional structure of the candidate agent over the computer-displayed representation of the non-steroidal ligand.

12. The method of claim 1 or 2, further comprising determining a fit between the structural coordinates of the amino acids of the non-steroidal ligand binding pocket and a three-dimensional structure of the candidate agent.

13. The method of claim 12, wherein determining the fit comprises calculating a distance between an atom of the non-steroidal binding pocket and an atom of the candidate agent.

14. The method of claim 1, further comprising comparing a predicted interaction between the candidate agent and the non-steroidal ligand binding pocket progesterone receptor with the interaction between the non-steroidal ligand and the non-steroidal ligand binding pocket progesterone receptor.

15. The method of claim 12, wherein determining the fit comprises docking a three-dimensional model of the candidate agent to the three-dimensional model of the ligand binding domain of the progesterone receptor.

16. The method of claim 14, further comprising comparing the interaction of the candidate agent with the progesterone receptor to an interaction of a second agent with the progesterone receptor.

17. The method of claim 2, wherein the step of obtaining the agent comprises synthesizing the agent.

18. A method of designing or selecting an agent that interacts with a progesterone receptor, comprising:
(a) providing a three-dimensional structure of a complex comprising a human progesterone receptor ligand binding domain (hPR-LBD) and tanoproget, said three-dimensional structure being obtained by subjecting a co-crystal comprising the hPR-LBD in complex with tanoproget, wherein said hPR-LBD consists of SEQ ID NO:2 and said co-crystal is characterized by space group P21, with dimensions a=57.52 Å, b=64.50 Å, c=70.41 Å and β3=95.76, to X- ray diffraction and collecting data sufficient to determine the three-dimensional structure of said complex;
(b) generating a three-dimensional model from the three-dimensional structure of said complex;
(c) identifying the amino acid residues forming a non-steroidal ligand binding pocket of the progesterone receptor ligand binding domain from the three-dimensional model in step (b) in order to generate a three-dimensional representation of the non-steroidal ligand binding pocket, wherein the non-steroidal ligand binding pocket comprises amino acids Ile699, Ala701, Leu714, Leu715, Leu718, Asn719, Leu721, Gln725, Trp755, Met756, Met759, Val76O, Leu763, Arg766, Ser767, Tyr777, Phe778, Ala779, Leu782, Phe794, Leu797, Cys798, Met801, Ile804, Leu887, His888, Tyr890, Cys891, Asn893, Thr894, Phe895, Ser898, Leu901, Val903, Phe905, Met909, Ile913, and Leu917 of SEQ ID NO:4, according to Table 2, ± a root mean square deviation for alpha carbon atoms of not more than 1.5 Å and wherein said three-dimensional representation of the non-steroidal ligand binding pocket optionally has the non-steroidal ligand from step(b) present or absent;
(d) employing said three dimensional representation from step (c) to design or select said candidate agent;
(e) synthesizing said candidate agent; and
(f) contacting said candidate agent with said progesterone receptor ligand binding domain to determine the ability of said candidate agent to interact or bind said progesterone receptor ligand binding domain;
whereby the detection of the ability of said candidate agent to interact or bind said progesterone receptor ligand binding domain thereby identifies said candidate agent as an agent that interacts with the progesterone receptor.