# Patent

## Title
Crystallographic structure of TcPRACA and uses therefor

## Abstract

The present invention provides the crystal structure of the Trypanosoma cruzi PRACA proline racemase. Methods of modelling drugs that treat or prevent infection by T. cruzi are also provided, as are the drugs that are identified.

## Background
CROSS-REFERENCE TO RELATED APPLICATIONS
This application is based on and claims the benefit of U.S. Provisional Application No. 60/484,661, filed Jul. 7, 2003 and U.S. Provisional Application No. 60/474,238, filed May 30, 2003. The entire disclosures of these provisional applications are relied upon and incorporated by reference herein. This application is also based on and is a continuation-in-part of application Ser. No. 10/775,339, filed Feb. 11, 2004, now abandoned, which claims the benefit of U.S. Provisional Application No. 60/446,263, filed Feb. 11, 2003.


BACKGROUND OF THE INVENTION
1. Field of the Invention
The present invention relates to the Trypanosoma cruzi proline racemase, a 45 kDa polyclonal activator. More specifically, the present invention relates to the crystal structure of the TcPA45 (TcPRAC) protein of T. cruzi, methods of obtaining crystals and crystal structures of the TcPA45 (TcPRAC) protein of T. cruzi, and methods of using the crystal structure of the TcPA45 (TcPRAC) protein of T. cruzi to identify drugs that affect the pathogenicity of T. cruzi. 
2. Description of the Related Art
D-amino acids have long been described in the cell wall of eubacteria, where they constitute essential elements of the peptidoglycan and act as substitutes of cell wall teichoic acids (4), and in other parts of eubacteria as part of small peptides made by non-ribosomal protein synthesis (3, 4). In contrast, until recently it was believed that only L-amino acid enantiomers were present in eukaryotes (apart from a very low level of D-amino acids from spontaneous racemization due to aging) (1). However, recently an increasing number of studies have reported the presence of various D-amino acids (D-aa) in both protein-bound (5) and free forms (6) in a wide variety of eukaryotes, including mammals. The origin of free D-aa can be exogenous (9) or endogenous (7, 8, 10-12) to the eukaryote.
Proline racemase catalyzes the interconversion of L- and D-proline enantiomers, and has, to date, been described in only two species, Clostridium sticklandii and Trypanosoma cruzi. The enzyme from the eubacterium C. sticklandii contains cysteine residues in the active site, and does not require co-factors or known co-enzymes for activity. As disclosed in U.S. Provisional Patent Application No. 60/446,263, and U.S. patent application Ser. No. 09/725,945, now U.S. Pat. No. 6,713,617, the entire disclosures of which are hereby incorporated by reference, the enzyme from the parasitic eukaryote T. cruzi, which causes Chagas' Disease in humans, exists in two forms, TcPRACA and TcPRACB, encoded by two independent genes, respectively. The T. cruzi TcPRACB enzyme represents an intracellular form of the enzyme that is present in non-infective forms of the organism. The T. cruzi TcPRACA enzyme represents a membrane-bound or secreted form of the enzyme that is present in infective forms of the organism. TcPRACA may also originate an intracellular version of proline racemase by a mechanism of alternative splicing. The two forms of the enzyme share a high level of homology, and appear to be a result of gene duplication. A cysteine at residue 330 of the TcPRACA enzyme is located in the active site of the enzyme. A cysteine at position 160 of the TcPRACA is also involved in the active site of the enzyme. The TcPRACA enzyme is a potent host B-cell mitogen that supports parasite evasion of specific immune responses, and has been implicated in persistence of the parasite through polyclonal lymphocyte activation (10). The mitogenic properties of the T. cruzi proline racemase are dependent on the integrity of the enzyme active site (2).
In view of the importance of both forms of the TcPRAC enzyme (i.e., TcPRACA and TcPRACB) to the growth and infectivity of T. cruzi, structural and biochemical information on the enzyme is needed to provide new drugs and methods for treating T. cruzi infection.
SUMMARY OF THE INVENTION
The present invention addresses the needs of the art for information on the TcPRAC enzyme by providing the three-dimensional structure of the TcPRACA enzyme. The three-dimensional structure of the TcPRACA can be used as a model for rational drug design to design and develop drugs that affect the biological activity of the TcPRACA, and that affect the ability of T. cruzi to establish and perpetuate the process of infection. It also can be used to model drugs that affect proline racemases of other organisms.
In one aspect of the invention, a crystal comprising Trypanosoma cruzi PRACA proline racemase (TcPRACA) is provided. In another aspect, the TcPRACA has the sequence of SEQ ID NO:3, while in a further aspect the TcPRACA is encoded by SEQ ID NO:1. In another aspect of the invention the crystal has a three-dimensional structure defined by the data set listed in Table 2.
The crystal can be provided in multiple forms, including as a component of a composition. Accordingly, in another aspect the invention provides a composition comprising a crystal comprising (TcPRACA) and a salt.
In another aspect, the invention provides a method of making a crystal comprising TcPRACA. In general, the method comprises providing TcPRACA in a solution and at a concentration suitable for the process of crystallization, and allowing the TcPRACA to crystallize from the solution. In one aspect, the method comprises providing TcPRACA at a concentration of 5-6 mg/ml in 25 mM sodium acetate, pH 5.2, to provide a protein solution; mixing the protein solution with an equal volume of a buffer comprising 0.2 M ammonium acetate, 50 mM trisodium citrate dihydrate, pH 5.6, and 15% (w/v) polyethylene glycol 4000; and allowing a crystal comprising TcPRACA to form.
In yet another aspect, the invention provides a method of identifying a substance that affects the biological activity of TcPRACA. The method comprises providing a model of TcPRACA that includes the proline binding site of the TcPRACA, and using the model to determine the structure of a substance that binds to the TcPRACA. In one aspect, the substance interacts with residue Cys160 of TcPRACA. In another aspect, using the model may comprise providing a model of the structure of the substance that binds to the TcPRACA; fitting the model of the structure of the substance into a binding site on the modeled TcPRACA; and selecting a substance whose model structure fits into a binding site on the modeled TcPRACA. In another aspect, the method may further comprise providing the TcPRACA; providing the substance; combining the TcPRACA with the substance; and determining the effect of the substance on the biological activity of the TcPRACA. In a further aspect, determining the effect of the substance on the biological activity of the TcPRACA may comprise modulating TcPRACA activity by means of a molecule being tested in the presence of an equimolar mixture of a L- and D-proline and of TcPRACA to be modulated; oxidatively deaminating the D-proline generated in step (A) by means of a D-amino oxidase with a prosthetic group; and detecting the hydrogen peroxide generated by the oxidative deamination; where modulation of the hydrogen peroxide is indicative of the capability of the tested molecule to modulate TcPRACA activity. In one aspect, the molecule inhibits said racemase activity. In a further aspect, the method identifies a substance that affects the infectivity of T. cruzi. 
In a further aspect, the invention provides a substance that affects the enzymatic activity of the TcPRACA racemase. In one aspect, the substance interacts with residue Cys160 of TcPRACA. The substance that affects the enzymatic activity of the TcPRACA can affect the mitogenicity of the TcPRACA as well. In addition, the substance can affect the parasitic activity or infectivity of T. cruzi. 
In still another aspect, the invention provides a computer readable medium that contains information that can be used to create a model, such as a molecular model, of the TcPRACA. In one aspect, the computer readable medium has recorded thereon the data set listed in Table 2. The computer readable medium may be, for example, a computer diskette, a compact disk, a digital video disk, or a computer hard drive.
In a further aspect, the invention provides a computer system comprising a central processing unit and a video display unit. According to the invention, the computer system, and in particular the combination of the central processing unit and the video display unit, is capable of converting data regarding the positions of atoms in the TcPRACA crystal into a model of TcPRACA. In one aspect, the central processing unit and the video display unit are physically attached. In another aspect, the computer system comprises a central processing unit and a video display unit, where the combination of the central processing unit and the video display unit is capable of converting the data set listed in Table 2 into a model of TcPRACA.
In a still further aspect, the invention provides a method for designing a molecule that affects the biological activity of TcPRACA. The method comprises using the data set listed in Table 2. In another aspect, the invention provides a molecule designed by this method. In another aspect of the method, the method comprises using residue Cys330 as a interaction target for the designed substance.



BRIEF DESCRIPTION OF THE DRAWING
FIG. 1 depicts the active site of the TcPRACA enzyme. In crystallographic studies presented in FIG. 1, the residue Cys330 and the residue Cys160 of the TcPRACA peptide sequence are represented as Cys300 and Cys130, respectively.



DETAILED DESCRIPTION OF VARIOUS EMBODIMENTS
Reference will now be made in detail to specific exemplary embodiments of the invention. The following specific embodiments are not to be construed as limiting the full scope of the invention, but are presented merely to exemplify and explain in detail aspects and embodiments of the invention.
In one aspect of the invention, a crystal comprising Trypanosoma cruzi PRACA proline racemase (TcPRACA) is provided. The crystal can be provided alone, or as part of a composition. If provided as part of a composition, the composition can comprise one or more other components, such as proteins, salts, solvents, etc. The other components can be selected by those of skill in the art based on the intended use of the crystal.
In embodiments of this aspect of the invention, the TcPRACA has the sequence of SEQ ID NO:3. In other embodiments, the TcPRACA has the sequence of SEQ ID NO:2 (GenBank Accession: AAF97423.1). In other embodiments, the TcPRACA is encoded by SEQ ID NO:1 (GenBank Accession: AF195522). In yet other embodiments, the crystal has a three-dimensional structure that can be defined by the data set listed in Table 2.
The TcPRACA proteins that are crystallized can be produced using any known technique. For example, TcPRACA can be overexpressed in E. coli and purified as an excreted protein or from cell lysates. Likewise, it can be expressed in eukaryotic systems, such as a baculovirus system. Those of skill in the art are aware of numerous systems that are suitable for expression of proteins for purification. Thus, the techniques need not be detailed here. Likewise, protein purification techniques are well known to those of skill in the art, and thus need not be detailed here. An exemplary expression and purification scheme is disclosed below in the Examples.
It is now widely recognized that the crystal structure of a protein is a powerful tool for identifying substances that bind to the protein. Indeed, the three-dimensional structure of a protein can be used to model molecular interactions between the protein and various substances, permitting one to design molecules that specifically bind to the protein without having to first chemically synthesize the molecules. The present invention provides such an advantage for the TcPRACA racemase by providing, for the first time, the crystal structure of the racemase. The crystal structure includes the proline binding site, which acts not only as the active site of the enzyme, but whose integrity is involved in the mitogenic activity. Furthermore, the crystal structure provides a plethora of data about the exterior surface of the TcPRACA, which, like the active site, can be used to design and create therapeutic molecules for preventing or treating T. cruzi infection. The crystals of the invention are useful not only for modelling of the racemase and substances that bind to it, but also for modelling the three-dimensional structures of related proteins. Although a powerful use of the crystals of the invention is as a model for drug design, the process of crystallization can also be used as a purification step for the protein.
In a second aspect, the invention provides a method of making a crystal comprising TcPRACA. The method comprises providing TcPRACA at a concentration of 5-6 mg/ml in 25 mM sodium acetate, pH 5.2, to provide a protein solution; mixing the protein solution with an equal volume of a buffer comprising 0.2 M ammonium acetate, 50 mM trisodium citrate dihydrate, pH 5.6, and 15% (w/v) polyethylene glycol 4000; and allowing a crystal to form. It is well within the abilities of those of skill in the art to modify these conditions to obtain crystals according to the invention. For example, the pH of the solutions can be modified within about one unit, the protein can be provided in a concentration that is more or less than 5-6 mg/ml, and the concentrations of the salt components in the protein solution and buffer can be varied. Thus, the invention contemplates crystallization conditions that are not identical to those disclosed herein, but that are similar and result in a crystal of TcPRACA.
Once the crystal forms, it can be analyzed to determine its three-dimensional structure using any number of techniques. For example, the three-dimensional structure of the crystal can be determined using x-ray diffraction using, for example, synchrotron radiation or the sealed tube or rotating anode methods. In addition, neutron diffraction analysis can be used to determine the three-dimensional structure of the crystal. Data can be collected using any suitable technique, including precession photography, oscillation photography, and diffractometer data collection.
Electron density maps can be calculated using programs such as those from the CCP4 computing package (13) and the modelling program O (14). Docking programs, such as GRAM, DOCK, and AUTODOCK (15, 16) are available for identification of substances that interact with TcPRACA. Other well-known computer programs for model building and analysis include HKL, MOSFILM, XDS, SHARP, PHASES, HEAVY, XPLOR, TNT, NMRCOMPASS, NMRPIPE, DIANA, NMRDRAW, FELIX, VNMR, MADIGRAS, BUSTER, SOLVE, FRODO, RASMOL, INSIGHT, MCSS/HOOK, CHARMM, LEAPFROG, CAVEAT (UC Berkeley), CAVEAT (MSI), MODELLER, CATALYST, ISIS, and CHAIN.
In a third aspect, the invention provides a method of identifying a substance that affects the biological activity of TcPRACA. In general, the method comprises providing a model of the TcPRACA, or a portion of the TcPRACA, and using the model to determine the structure of a substance that binds to the TcPRACA. Crystal structure information presented here is useful in designing inhibitors or activators of TcPRACA by modelling their interaction with TcPRACA. In embodiments, the model of TcPRACA includes the proline binding site (the active site). The substance can be a substance having a structure that is designed using the TcPRACA structure, or can be a structure that exists in a computer database. Alternatively, the substance can be identified by first designing a substance using the three-dimensional structure of the TcPRACA, then using the structure of that substance to probe databases for other compounds having similar structures. Those structures can then be modelled with the TcPRACA to determine if they will bind. The method thus can be a method of rational drug design.
The data set disclosed in Table 2 provides a relative set of positions that define a shape in three dimensions. It is to be understood that an entirely different set of positions having a different origin or axes can define a similar three-dimensional shape. Likewise, manipulation of the data set to increase or decrease the distances between various atoms, or to add or subtract solvent molecules, might not significantly alter the overall three-dimensional structure defined by the data set in Table 2. Accordingly, reference to the data set in Table 2 should be understood to include coordinate sets that define the same general structure of TcPRACA, or in which minor variations have been made to the data set. Coordinate sets that are not identical, but define a similar structure as that defined by the data set of Table 2 can be identified using various computer programs, such as the Molecular Similarity application of QUANTA (Molecular Simulations Inc., San Diego, Calif.).
In addition, it is to be understood that the three-dimensional structure defined by the data set in Table 2 encompasses three-dimensional structures of TcPRACA proteins in which one or more amino acids have been altered or deleted, or in which one or more amino acids have been added, without affecting the general three-dimensional structure of the protein. More specifically, it is well known in the art that many changes can be made in a protein's primary amino acid sequence without changing its overall three-dimensional structure or its activity. Such mutations can include a single mutation or multiple mutations within the same primary amino acid sequence. Indeed, with the information provided by the three-dimensional structure of the present invention, those of skill in the art can readily identify numerous amino acids that do not play any apparent role in enzyme activity or folding/structure. It is to be understood that mutants that do not significantly affect the general three-dimensional structure or the activity of the resulting enzyme are encompassed by reference to the data set of Table 2.
In embodiments, the method of identifying a substance also comprises providing the TcPRACA; providing the substance; combining the TcPRACA with the substance; and determining the effect of the substance on the biological activity of the TcPRACA. For example, the method can include contacting the TcPRACA with the substance, assaying the racemase activity of the TcPRACA, and comparing the activity to the activity of an equal amount of TcPRACA assayed under the same conditions, but in the absence of the substance.
An effect of the substance can be an inhibitory effect or an activating effect. In embodiments, the substance inhibits the activity of the TcPRACA at least 80%. That is, the activity of the TcPRACA in the presence of the substance is 20% or less of the activity of the racemase in the absence of the substance, when present at a concentration that provides maximal inhibition. Inhibition can be 80%, 90%, 95%, 98%, or 99% or greater, such as 100%. Alternatively, the activity of the TcPRACA can be activated. For example, it can be 80% more active, 90% more active, 95% more active, or 99% or greater more active. In embodiments, it is twice as active (i.e., 100% more active) or greater.
In embodiments, the method of identifying a substance comprises providing a model of the structure of the substance that binds to the TcPRACA; fitting the model of the structure of the substance into a binding site on the modelled TcPRACA; and selecting a substance whose model structure fits into a binding site on the modelled TcPRACA.
According to the method of identifying a substance, the model of TcPRACA preferably includes the active site of the enzyme. As discussed above, the conformation of the enzyme has been linked to the mitogenic activity of the enzyme, and appears to be involved in the parasitic activity of T. cruzi. The occupation of the active site by a specific inhibitor induces a conformational change affecting completely the mitogenic activity of the protein. Thus, the active site of the enzyme is a logical target for binding of a substance that affects, and in particular, inhibits, the activity of TcPRACA.
However, the invention also includes identifying a substance that binds to a site on the TcPRACA that is not part of the active site. Based on the three-dimensional structure disclosed herein, multiple binding sites for substances can be envisioned. It is well known that binding of a molecule at a site that is distant from an active site of an enzyme can, in some instances, affect the activity of the enzyme by causing a change in the three-dimensional structure of the enzyme, which results in a change in the three-dimensional structure of the active site. Modelling of binding in such a way is encompassed by the present invention. Thus, sites other than those that are part of the active site of the enzyme can be used to identify substances, such as inhibitors, according to the invention.
The method of the invention permits one to identify a substance that affects the enzymatic activity of the TcPRACA racemase. The substance can affect the mitogenicity of the TcPRACA as well. In addition, the substance can affect the parasitic activity of T. cruzi. Further, the substance can affect the infectivity of T. cruzi. Such substances constitute part of the present invention. The effect of the substance can be an inhibiting effect or an activating effect, i.e., it can decrease or increase the activity of the TcPRACA racemase, the mitogenicity of the TcPRACA, and the parasitic activity of T. cruzi, and can decrease or increase the infectivity of T. cruzi. 
When used to affect the mitogenicity, parasitic activity, or infectivity of T. cruzi, the substance is considered to be a drug, in accordance with the broad definition of drug used in the art. The term thus includes antibodies (polyclonal or monoclonal) or fragments of antibodies that are designed using the three-dimensional structure of TcPRACA. The drug can be administered to a subject, such as a human, using any mode of administration that is suitable and that is known in the art for administration of drugs. Thus, for example, the drug can be administered to the subject orally or parenterally, such as by intravenous or intramuscular injection. Other modes of administration can also be employed, such as intrasplenic, intradermal, and mucosal administration (e.g., by inhalation). For purposes of injection, the drug can be prepared in the form of a solution, suspension, or emulsion in vehicles conventionally employed for this purpose. Other dosage forms are well known to those of skill in the art and need not be detailed here.
It is preferred that the drug affect the mitogenicity, or parasitic activity or infectivity by inhibiting or reducing these biological activities. When such a drug is used, it thus can be used to treat or prevent T. cruzi infection. To do so, the drug should be administered in an amount sufficient to reduce, inhibit, or prevent infection or the infectious process of T. cruzi. The amount administered to each individual subject will depend on various physical and physiological traits of the particular individual, including size, absorption, distribution, and clearance by the individual's body.
Thus, the dosage of the drug can vary over wide limits. For example, the dosage of the drug can vary from about 50 ng per kg of body weight to about 1 μg per kg of body weight per dose. Thus, suitable dosages include, but are not limited to, about 100 ng per kg of body weight, and about 500 ng per kg of body weight per dose. Multiple doses can be administered over a suitable time period. Frequency and duration of dosing can also vary depending on such things as the severity of infection, the age of the individual, and the presence or absence of other infections or health problems. Those of skill in the medical art can determine the appropriate dosing regimen using routine techniques without undue experimentation.
The term “about” as used herein in describing dosage ranges means an amount that is equivalent to the numerically stated amount as indicated by the biological effect in the host to whom the drug is administered. It is used to recognize that equivalents, while not necessarily encompassed by the values recited, exist and are included within the spirit and scope of the invention.
The drug can be provided in any suitable form, including, but not limited to, pills, tablets, lozenges, troches, capsules, suppositories, injectable solutions, ingestable solutions, and the like.
Appropriate pharmaceutically acceptable carriers, diluents, and adjuvants can be combined with the drug in order to prepare the drug for use in the treatment or prevention of T. cruzi infection. Such carriers, diluents, and adjuvants are known to those of skill in the art, and need not be detailed here. Thus, drug compositions of this invention can contain the active drug together with a solid or liquid pharmaceutically acceptable nontoxic carrier. Non-limiting examples of pharmaceutical carriers are sterile liquids, such as water and oils, including those of petroleum, animal, vegetable, or synthetic origin. Non-limiting examples of suitable liquids are peanut oil, soybean oil, mineral oil, sesame oil, and the like. Physiological solutions can also be employed as liquid carriers, particularly for injectable solutions.
Suitable pharmaceutical excipients include, but are not limited to, starch, glucose, lactose, sucrose, gelatine, malt, rice, flour, chalk, silica gel, magnesium carbonate, magnesium stearate, sodium stearate, glycerol monostearate, talc, sodium chloride, dried skim milk, glycerol, propylene glycol, water, ethanol, and the like. These compositions can take the form of solutions, suspensions, tablets, pills, capsules, powders, sustained-release formulations, and the like. Suitable pharmaceutical carriers are described in “Remington's Pharmaceutical Sciences” by E. W. Martin.
The subject to whom the drug is administered can be an animal susceptible to infection by T. cruzi. In embodiments, the subject is a mammal. For example, the mammal can be a human, a dog, a cat, a bovine, a pig, or a horse. In particular, the mammal can be a human.
It is to be understood that the drugs identified by practicing this invention can be used in combination with other drugs. For example, mixtures of different drugs can be employed in a single composition. Likewise, multiple compositions comprising one or more drugs can be employed. Indeed, the drugs of the present invention can be administered in conjunction with a vaccine designed to elicit a protective response against T. cruzi. 
In yet another aspect of the invention, a computer readable medium having recorded thereon the data set listed in Table 2, or a portion of the data set listed in Table 2, is provided. By computer readable medium it is meant any media that can be read and accessed directly or indirectly by a computer. An example of a computer readable medium is one that is suitable for use in a computer system, as described below. Non-limiting examples of the computer readable medium include magnetic storage media, such as a computer diskette, a computer hard drive, and a magnetic tape; and optical storage media, such as an optical disk, a compact disk, a digital video disk; and hybrids of these two types of media.
In yet a further aspect, the invention is directed to a computer system comprising at least a central processing unit and a video display unit. The combination of the central processing unit and the video display unit is capable of converting the data set listed in Table 2 into a model of TcPRACA that can be viewed by a person. Likewise, the computer system is capable of converting some, but not all, of the data into a model of a portion of TcPRACA that can be viewed and/or manipulated by a person. It is envisioned that, when less than the entire TcPRACA protein is modelled, a sufficient number of atoms are included in the model to permit a person to determine whether a substance of interest can bind to the TcPRACA. In embodiments, the computer system is used to generate and display a three-dimensional model of TcPRACA, alone or with a model of one or more substances that can bind the TcPRACA. It is preferred that the model or models can be manipulated by a person while being displayed by the computer system.
A computer system according to the invention can comprise hardware, software, and at least one data storage element that are used to collect, store, and analyze information. Hardware includes, but is not limited to, a central processing unit. Software includes all computer programs, whether they be contained within the hardware or provided by way of externally supplied media, that control the activity of the computer system. Data storage elements include, but are not limited to, random access memory (RAM). Computer systems include personal computers, servers, mainframes, and the like, and can be purchased as one unit or in parts from commercial vendors such as Silicon Graphics Inc., Sun Microsystems, and Apple Computer. One particular example of a computer system according to the present invention is a device that is used to analyze atomic coordinate data, including the data set listed in Table 2, or a portion of that data set.
In view of the power of the internet, wide area networks, and local area networks, and the interconnectedness of computers throughout the world, it is not necessary that all of the elements of the computer system be located in physical proximity. Indeed, the elements of the computer system need not be physically connected at all. For example, a central processing unit can be located in one physical location, for example, at a laboratory, while a video display unit can be located in another physical location, for example, an office. The two elements can communicate through any suitable element that is capable of transmitting data, such as electrical, optical, or audio signals.
EXAMPLES
The invention will be further clarified by the following examples, which are intended to be purely exemplary of the invention and should not be construed as limiting the scope of the invention in any way.
Example 1
Recombinant Protein Production and Purification
A TcPRACA gene fragment starting at codon 30 was obtained by PCR using Hi- and Bg-45 primers (17), and cloned in frame with a C-terminal six-histidine tag into the pET28b(+) expression vector, following the protocol described by Reina-San-Martin et al. (10). The sequence of the engineered protein is given as SEQ ID NO:3.
Recombinant TcPRACA was produced in E. coli BL21 (DE3) and purified using Immobilized Metal Affinity Chromatography on nickel columns. Recombinant TcPRACA was purified using an anion exchange column (Mono-Q) and an FPLC system. Elution was performed at a constant flow rate of 0.5 ml/min. Protein fractions of 0.5 ml were collected and the absorbance was monitored at 280 nm. The fraction containing recombinant TcPRACA was recovered and precipitated with 75% ammonium sulfate. The pellet was resuspended in 25 mM NaOAc pH 5.2 with or without 1 mM pyrrole-2-carboxylic acid (PAC). The protein was desalted using PD10 columns previously equilibrated with 25 mM NaOAc pH 5.2. Recombinant TcPRACA was finally submitted to ultra filtration using 25 mM NaOAc pH 5.2.
Example 2
Enzyme Assays
TcPRACA racemization activity was assayed polarimetrically as described previously (10). Briefly, a 500 μl reaction mixture was prepared containing 0.25 μM purified enzyme and 40 mM L-proline in 0.2 M sodium acetate, 20 MM β-mercaptoethanol, pH 6.0. Racemization was assayed at 37EC. The reaction was stopped by incubating for 10 minutes at 80EC and then freezing. Water (1 ml) was then added. The percent racemization was determined by measuring the optical rotation in a polarimeter, such as a model 241 MC, made by Perkin Elmer, Montigny le Bretonneux, France, at a wavelength of 365 nm in a cell with a path length of 10 cm at a precision of 0.001 degree.
Using this assay, compounds that affect the mitogenic activity of TcPRACA can be confirmed, their relative anti-parasite activity determined, and useful in vivo doses identified.
Example 3
Mitogenicity Assays
TcPRACA is a parasite mitogen because it is capable of activating a non-specific polyclonal response in lymphocytes. It is not clear whether TcPRACA itself is a mitogen, whether it acts as a mitogen by binding to host molecules, or whether its enzymatic product is, or constitutes part of, a mitogen. Regardless, the non-specific lymphocyte activation by TcPRACA is a functional result that can be assayed.
As disclosed in co-pending U.S. patent application Ser. No. 09/725,945, now U.S. Pat. No. 6,713,617, TcPRACA mitogenic activity can be assayed in vitro as follows: 5×105 naive spleen cells/well (96 well plate) are stimulated in vitro with different doses of TcPRACA (ranging from about 0.8 to 200 μg/ml final) for 24, 48, and 72 hours at 37EC, 5% CO2. Cultures are pulsed with 3H-thymidine (1 μCi/well) for 16-18 hours before harvesting. 3H-thymidine incorporation is determined by counting using a beta-plate and the ELISPOT technique.
As disclosed in co-pending U.S. patent application Ser. No. 09/725,945, now U.S. Pat. No. 6,713,617, TcPRACA mitogenic activity can be assayed in vivo as follows: BALB/c mice are injected (i.p.) with 50 μg of TcPRACA, and spleen cells assayed day 7 after injection. Results are expressed as total numbers of spleen cells, total number of B cells producing IgM, IgG2a, and IgG2b isotypes, and total number of isotype-producing B cells specific to the TcPRACA. The control run is mice that are not injected with the protein.
Using this assay, compounds that affect the mitogenic activity of TcPRACA can be confirmed, their relative anti-parasite activity determined, and useful in vivo doses identified.
Example 4
Crystallization Buffers
The following buffers can be used to crystallize the TcPRACA protein:

    
    
        Buffer 1: 100 mM NaOAc, pH 5.6-5.8; and 10% polyethylene glycol 1500 with or without 1 mM PAC;
        Buffer 2: 0.2 M ammonium acetate; 50 mM trisodium citrate dihydrate, pH 5.6; 15% (w/v) polyethylene glycol 4000, equilibrated over the buffer;
    
    


Buffer 3: 100 mM ammonium acetate; 50 mM trisodium citrate dihydrate, pH 5.6; and 15% w/v polyethylene glycol 4000 with or without 1 mM PAC.
Example 5
Crystallization of the TcPRACA Protein
A protein drop was set by mixing 2-3 μl (6 μg) of the protein solution obtained in Example 1 with an equal volume of crystallization buffer 2. Crystals grew to a final size of 0.2×0.2×0.05 mm in 3-4 days. For X-ray diffraction experiments, the crystals were frozen in liquid nitrogen using the crystallization buffer plus 30% glycerol (used as a cryoprotectant).
Example 6
Crystallographic Studies
X ray diffraction data sets were collected from single crystals at 110K at the ESRF synchrotron, Grenoble, France, on beamlines BM14 and ID29. Diffraction was isotropic. Data were processed (Table 1) using the programs MOSFLM, SCALA, and TRUNCATE from the CCP4 program suite (13). Crystals proved to be monoclinic (C2) with unit cell dimensions (Å): a=134.0651 Å; b=91.618 Å; c=86.0307 Å; β=123.3735°. No significant non-origin peaks were detected in the native Patterson map.
Initial molecular replacement calculations using low homology models such as diaminopimelate epimerase (PDB1bwz) proved unsuccessful.







TABLE 1







Data collection statistics











Data Set
Native
SAD anomalous peak















Wavelength (Å)
1.0072
0.9795



Dmin (Å)
2.1
2.9



Completeness
98.8
98



(%)



Multiplicity
3.7
6.3



Rsym (%)
6.9
8.9







BEAM-LINE BM14 European Synchrotron Radiation Facility (Grenoble)



Project/Protein name: Proline racemase from Trypanosoma cruzi.



Method of Structure Solution: SAD



MAD/SAD absorption edge: Se SAD Δf′′ peak12.657 KeV



Unit cell dimensions (Å): a = 134.0651 Å; b = 91.618 Å; c = 86.0307 Å; β = 123.3735°



Space group: C2






Example 7
Seleno-Methionine Incorporation
The plasmid expressing the recombinant TcPRACA having the amino acid sequence SEQ ID NO:3 was used to transform strain B834 (DE3) Escherichia coli cells (same genotype as BL21 but met). These transformed bacteria were cultured in M9 minimal medium supplemented with amino acids (seleno-methionine replacing methionine), nucleosides, vitamins, and oligoelements, as described previously (18). Recombinant protein overexpression was induced as usual with IPTG. Cells were harvested, and protein purification was achieved with the same protocols as for the Met wild-type TcPRACA.
The structure was solved by single-wavelength anomalous diffraction methods (highly redundant data set was measured at 12.657 KeV, corresponding to the Se Δf′′ peak) combined with electron density modification strategies that took into account the 2-fold non-crystallographic symmetry. Twenty-two (out of 26) Se sites were determined by direct methods using the program Shake'n'Bake (19), and refined with the program SHARP (20). Electron density improvement was performed with the program SOLOMON (21).
The coordinates of the resulting TcPRACA crystal are given in Table 2.
Example 8
Enzyme Assay
One can use a simple test to rapidly screen putative modulators, such as inhibitors, of TcPRAC. TcPRAC constructs allowing for the production of high amounts of the recombinant active enzyme can be used together with the knowledge of a specific inhibitor of proline racemases (such as, for example, pyrrole carboxylic acid, PAC) to provide a medium/high throughput microplate test to easily screen a high number of inhibitor candidates (i.e. 100-1000). Such a test is based on colorimetric reactions that are a simpler alternative to polarimetry and other time-consuming tests.
More particularly, the test is based on the detection of D-proline originated through racemization of L-proline by TcPRAC, in the presence or in the absence of known concentrations of PAC inhibitor as positive and negative controls of racemization, respectively. For that purpose, this test utilizes another enzyme, D-amino acid oxidase (D-AAO), which has the ability to specifically oxidize D-amino acids in the presence of a donor/acceptor of electrons and yield hydrogen peroxide. The advantage of this strategy is that hydrogen peroxide can be classically quantified by peroxidase in a very sensitive reaction involving ortho-phenylenediamine, for example, ultimately offering a chromogenic reaction that is visualized by colorimetry at 490 nm.
Since D-amino acid oxidase reacts indiscriminately with any “D-amino acid”, and not with their L-stereoisomers, such a test is not only helpful to identify proline racemase inhibitors, but also applicable, if slightly modified, to detect any alterations in levels of free D-aa in various fluids to make a diagnosis of some pathogenic processes.
A. Basics for a D-amino-acid Quantitative Test
The following test allows detection and quantitation of D-Amino acids. A first reaction involves a D-amino-oxidase. This enzyme specifically catalyses an oxidative deamination of D-amino-acids, together with a prosthetic group, either Flavin-Adenin-Dinucleotide (FAD) or Flavin-Mononuclotide (FMN), according to the origin of the Enzyme. (Obs. FAD if the enzyme comes from porcine kidney).
The general reaction is as follows:




    In (1), the D-amino acid is deaminated and oxidized, releasing ammonia and the reduced prosthetic group. If the amino group is not a primary group, the amino group remains untouched and no ammonia is released.
    In (2), the reduced prosthetic group reduces oxygen, and generates hydrogen peroxide.


Either a catalase or a peroxidase can decompose hydrogen peroxide. A catalase activity is written as:




whereas a peroxidase activity is





wherein R′ is any carbon chain.

Thus, detection of hydrogen peroxide can be done with the use of catalase and a reagent sensitive to oxygen, such as by destaining reduced methylene blue, for instance, with oxygen or with the use of peroxidase with a change in color of the reagent indicated by:




B. Application of such a Test for Evaluating the T. Cruzi Racemase Activity and the Modulation of this Racemase.

II-1-Test for Racemase Activity
The T. cruzi racemase activity converts reversibly L-Pro into D-Pro. Since these two forms can induce polarized light deviation, this conversion can be measured by optical polarized light deviation. But the presence of the D-form allows also the use of D-amino-acid oxidase in order to assess the amount of D-Proline in racemase kinetics. In this test, the following reactions are involved:
1) Proline-Racemase activity.




2) D-amino-acid oxidase




(Obs: There is no ammonia formed in the case of Proline, because the nitrogen of Proline is involved in a secondary amine.)





3) Detection of hydrogen peroxide with peroxidase




The chromogenic reagent can be, for example, orthophenylenediamine (OPD), or 3,3′,5,5′ tetramethyl benzidine (TMB), or 5-aminosalicylic acid (ASA).
These reactions can be carried out using the following exemplary, but preferred, materials and methods.










Materials








Materials
Comments





Proline-racemase (TcPRAC) (1 mg/ml



Stock)


L-Proline, Sigma, Ref. P-0380 (1M Stock)
An equimolar of D- and L-Proline is


D-Proline, Aldrich, réf. 85 891-9 (1M
made by mixing equal volumes of 2M


Stock)
D-Proline with 2M L-Proline


Orthophenylenediamine (OPD) Sigma
10 mg tablets. Extemporaneously used


refP-8287 lot 119H8200
as a 20 mg/ml stock solution in water.


D-AAO from swine kidney (Sigma) ref. A-
Powder dissolved into 1 ml Buffer* + 1 ml


5222 lot 102K1287
100% glycerol. The resulting activity is



50 U/ml. Stored at −20° C.


Horse radish peroxidase (HRP) Sigma ref
Powder dissolved into 2.5 ml


P8375 lot 69F95002
Buffer* + 2.5 ml 100% glycerol. The



resulting activity is 5042 U/ml. Stored at



−20° C.


Sodium acetate 0.2M Ph6.0


Flavine-adenine-dinucleotide (FAD)
Stock solution of 10−1M in water.


(Sigma) ref. F-6625
Stored at −20° C. Used as a 10−3M sub-



stock solution.


Sodium pyrophosphate (Pop) 0.235M
Not soluble at a higher concentration.



Must be stored at 4° C. and gently



heated before use in order to solubilize



crystals which may occur.


Buffer* = 10 ml of 0.2M sodium acetate
The final pH is 8.3.


buffer pH6.0 + 680 μl 0.235M Pop


Microplates (96 wells)
With adhesive coverlid


ELISA reader for microplates
With a wavelength filter at 490 nm for



OPD substrate.









Methods
Racemisation in Microplates:
(1) The volumes are indicated for a single well, but duplicates are mandatory. Leave enough raws of the microplate empty for standard and controls to be used in further steps. Distribute the following volumes per well reactions:
a) without inhibitor (Vol=QS 81 μl)
















TcPRAC 1 mg/ml
 2 μl
 2 μl
 2 μl
 2 μl


L-Proline 0.1M
32 μl
16 μl
 8 μl
 4 μl


Proline Final
(40 mM)
(20 mM)
(10 mM)
(5 mM)


concentration


Sodium acetate
47 μl
63 μl
71 μl
75 μl


buffer 0.2M


pH6









b) with inhibitor (Vol=QS 81 μl):
A range of concentrations between 5 mM and 1 mM can be planned for the inhibitor. It should be diluted in sodium acetate buffer 0.2 M pH 6.0. Hence, the volume of inhibitor is substracted from the volume of buffer added in order to reach a final volume of 81 μl. For instance, 50% inhibition of racemisation of 10 mM L-proline is obtained with 45 μM Pyrrole carboxylic acid (PAC, specific inhibitor of proline racemase), when 36.5 μl PAC+44.5 μl buffer are used.
Table 3 is provided for 10 mM L-Proline as a substrate.

















TABLE 3







TcPrac 1 mg/ml
 2 μl
  2 μl
  2 μl
 2 μl
 2 μl
 2 μl
 2 μl
 2 μl
 2 μl
  2 μl


L-Proline 0.1M
 8 μl
  8 μl
  8 μl
 8 μl
 8 μl
 8 μl
 8 μl
 8 μl
 8 μl
  8 μl


PAC 0.1 mM/1 mM**/10 mM***
 0 μl
 5.4 μl
  11 μl
22 μl
43 μl
 9 μl**
 17 μl**
 35 μl**
 69 μl**
 14 μl**


Final concentration (μM)
 0
 6.7
13.5
27
54
107
214
429
858
1715


Sodium acetate buffer 0.2 M
71 μl
65.6 μl
  60 μl
49 μl
28 μl
 62 μl
 54 μl
 36 μl
 2 μl
 57 μl


pH6 QS 81 μl









    (2) Cover the microplate with an adhesive coverlid and leave for 30 nm at 37° C.
    (3) At the end of racemisation, 5.5 μl of 0.235M Pop are added in each reaction well of the microplate in order to shift pH from pH6.0 to pH 8.3.

Quantitation of formed D-Proline: Standards and Controls.



(1) Prepare Standard and Controls:
Standard: An equimolar mixture of L- and D-Proline is used as a standard in a range from 0.05 mM to 50 mM (final concentration in the assay). It is used for assessing the amount of D-Proline formed after racemization. The standard range is made in microtubes, as follows:
In tube 1, mix Proline and buffer according to the described proportions.
Then, add 500 μl of the obtained mixture to 500 μl of buffer in next tube, and so on.

























Negative control: is prepared in an other microtube, as follows:

















L-Proline (1M)
200 μl



Buffer*
800 μl



Final concentration
 40 ml







Blank = Buffer*.






(2) Dispense in the empty wells of the microplate (see step II-1-2.1):
















Buffer*
67 μl



Standard dilutions
20 μl



or negative control







Obs: For the blank dispense 87 μl of Buffer* only:






(3) Prepare a mixture containing the enzymes (D-AAO/HRP Mix), as follows:
The amounts are given for one well, provided that the final volume will be 100 μl with the racemase products or the substrate:















For 13 μl:









Buffer*
 6.5 μl



D-AAO 50 U/ml
 1.7 μl



OPD (20 mg/ml)
 2.5 μl



HRP 5000 U/ml
0.75 μl



FAD 10−3M (4.5 μl 10−1M + 446 μl buffer)
 1.5 μl










This mixture is kept in the ice until use.

(4) The quantitation reaction starts when 13 μl of D-AAO/HRP mix is added to the reaction well.
(5) The microplate is covered with an adhesive coverlid and it is left in the dark at 37° C. between 30 nm and 2 hours. The reaction can be monitored by eye whenever a color gradient matches the D-amino acid concentration of the standard dilutions.
(6) The microplate is read with a microplate spectrophotometer using a filter of at 490 nm.
In conclusion, D-AAO/HRP evaluation is more sensitive than D-Proline quantitation by polarimeter since it can discriminate PAC inhibition at a lower concentration than evaluation with the polarimeter. Furthermore, inhibition is logically conversely proportional to L-Proline concentration, which can be assessed with the D-AAO/HRP method, but not with the polarimeter measurement. Such a test is useful for the screening of new modulators, such as inhibitors, for instance, of TcPRAC in a medium/high throughput test.
A preferred technological platform to perform the above test and to select appropriate inhibitors contains at least the following products:

    
    
        L-Proline, D-Proline, a proline-racemase
        A peroxidase, a substrate of a peroxidase
        A D-amino-acid oxidase
        And optionally a battery of potential inhibitory molecules.
    
    


Example 9
A Medium/High Throughput Test Using the D-AAO Microplate Test
Table 4 is an Example of a medium/high throughput test using the D-AAO microplate test.


















TABLE 4





1













D-Pro


(mM)
2
3
4
5
6
7
8
9
10
11
12







A 10*1
L-Pro*2
T1
T2
T3
T4
T5
T6
T7
T8
T9
T10


B 5*1
L-Pro*2
′′
′′
′′
′′
′′
′′
′′
′′


C 2.5*1
L-Pro + PAC*3
T11
T12
T13
T14
T15
T16
T17
T18
T19
T20


D 1.25*1
L-Pro + PAC*3
′′
′′
′′
′′
′′
′′
′′
′′
′′
′′


E 0.62*1
Blank 1
T21
T22
T23
T24
T25
T26
T27
T28
T29
T30


F 0.31*1
Blank 2
′′
′′
′′
′′
′′
′′
′′
′′
′′


G 0.15*1
L-Pro*4
T31
T32
T33
T34
T35
T36
T37
T38
T39
T40


H 0.07*1
L-Pro*4
′′
′′
′′
′′
′′
′′
′′
′′





*1D-proline standard (column 1)


*2Positive control of racemization using avec 10 mM substate (column 2, line A and B)


*3control for inhibition of racemization reaction by PAC using 10 mM substrate (column 2, line C and D)


Blank 1: mix with racemase (column 2, line E)


Blank 2: mix without racemase (column 2, line F)


*4Negative control for specificity of (without racemase + 40 mM L-proline) (column 2, line G and H)


Other wells: with Inhibitors (T1, T2, T3, . . . T40): in duplicates






The use of a microplate test based on D-amino-acid oxidase together with a peroxidase, such as horseradish peroxidase, can be used to detect and quantitate any D-amino acid in any biological or chemical sample. For example, since D-amino acids are described to be involved in several pathological processes or neurological diseases, such as Alzheimer disease, Parkinson, or renal diseases, their detection can be an important marker or parameter for the diagnosis and the follow-up of these pathologies. This technology can be also extended to the detection and quantification of D-amino acids in eukaryotic organisms, such as plants or fungi, and in bacteria.
The D-AAO/HRP test described here above can also be used for this purpose with slight modifications. For that purpose, the racemase reaction step should be skipped and the microplate test should start straightforward at “Racemisation in microplates” step (2) described above with the following remarks:
1) Standard: It should not be an equimolar mixture of D- and L-amino acid, but rather a serial dilution of D-Amino acids. The choice of amino acid is made according to the interest of the D-amino acid under investigation. The final volume in wells should be of 87 μl.
2) Negative control: It is made with the L-enantiomer of the D-amino acid under investigation. The final volume should be 87 μl.
3) Blank: It is made with 87 μl buffer*. (See paragraph II.1.1 Materials.)
4) Samples: The samples to be tested should be adjusted to pH 8,3 with buffer* and their final volumes should be of 87 μl per well.
Obs: Standards, negative controls, samples to test and blanks should be made in duplicates. They are dispensed into the wells of the microplate.
5) Then, the procedure follows steps 3) to 6), as above.
A preferred platform to search and quantitate the presence of a D-Amino acid in samples contains at least the following products:
A D-amino acid,
A peroxidase and a substrate of a peroxidase
A D-amino-acid oxidase
And optionally, a L-amino acid enantiomer, as control.
Thus, for example, the test for screening a molecule, which can modulate a racemase activity can comprise:

    
    
        (A) modulating a racemase activity by means of a molecule being tested in the presence of an equimolar mixture of a L- and D-amino acid and of a racemase to be modulated;
        (B) oxidatively deaminating the D-amino acid generated in step (A) by means of a D-amino oxidase in a prosthetic group; and
        (C) detecting the hydrogen peroxide generated by the oxidative deamination;

wherein modulation of the hydrogen peroxide is indicative of the capability of the tested molecule to modulate racemase activity. Preferably the molecule inhibits racemase activity, and more preferably the racemase is a proline racemase, for example, Tripanosoma curzi proline racemase.

    
    


The test can include a technological platform and all reagents and devices necessary to perform the test. The technological platform can comprise:

    
    
        a) L-amino acid, D-amino acid, and a racemase;
        b) a peroxydase and a substrate of a peroxydase, or a catalase and a reagent sensitive to oxygen;
        c) a D-amino acid oxidase; and
        d) optionally, one or more molecules to be screened for inhibitory activity of said racemase.
    
    


Preferably, the racemase is a proline racemase and the L-amino acid and D-amino acid are L-proline and D-proline, respectively.
It will be apparent to those skilled in the art that various modifications and other variations can be made in the practice of the present invention without departing from the scope or spirit of the invention. Thus, other embodiments of the invention will be apparent to those skilled in the art from consideration of the specification and practice of the invention disclosed herein. It is intended that the disclosure of specific embodiments be considered as exemplary only, with the true scope and spirit of the invention being indicated by the following claims.







TABLE 2







REMARK coordinates from minimization and B-factor refinement


REMARK refinement resolution: 29 - 2.1 A


REMARK starting r = 0.1896 free_r = 0.2226


REMARK final  r = 0.1742 free_r = 0.2165


REMARK rmsd bonds = 0.016237 rmsd angles = 1.85196


REMARK B rmsd for bonded mainchain atoms = 1.802 target = 1.5


REMARK B rmsd for bonded sidechain atoms = 2.822 target = 2.0


REMARK B rmsd for angle mainchain atoms = 2.613 target = 2.0


REMARK B rmsd for angle sidechain atoms = 3.801 target = 2.5


REMARK target = mlf final wa = 5


REMARK final rweight = 0.1600 (with wa = 5)


REMARK md-method = torsion annealing schedule = slowcool


REMARK starting temperature = 5000 total md steps = 100 * 6


REMARK cycles = 2 coordinate steps = 100 B-factor steps = 50


REMARK sg = C2 a = 131.1528 b = 91.2088 c = 85.9827 alpha = 90 beta = 126.5217


gamma = 90


REMARK topology file 1: CNS_TOPPAR:protein.top


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


REMARK topology file 3: CNS_TOPPAR:water.top


REMARK topology file 4: CNS_TOPPAR:ion.top


REMARK topology file 5: pac.top


REMARK parameter file 1: CNS_TOPPAR:protein_rep.param


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


REMARK parameter file 3: CNS_TOPPAR:water_rep.param


REMARK parameter file 4: CNS_TOPPAR:ion.param


REMARK parameter file 5: pac.par


REMARK molecular structure file: water_pick.mtf


REMARK input coordinates: water_pick.pdb


REMARK reflection file = p45nat_free2.1.hkl


REMARK ncs = none


REMARK B-correction resolution: 6.0 - 2.1


REMARK initial B-factor correction applied to fobs:


REMARK B11 = −6.502 B22 =   4.876 B33 = 1.626


REMARK B12 =   0.000 B13 = −4.520 B23 = 0.000


REMARK B-factor correction applied to coordinate array B: −0.136


REMARK bulk solvent: density level = 0.364053 e/A{circumflex over ( )}3, B-factor = 47.0089 A{circumflex over ( )}2


REMARK reflections with |Fobs|/sigma_F < 0.0 rejected


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








REMARK theoretical total number of refl. in resol. range:
47515 (100.0%)


REMARK number of unobserved reflections (no entry or |F|= 0):
 3534 (7.4%)


REMARK number of reflections rejected:
  0 (0.0%)


REMARK total number of reflections used:
43981 (92.6%)


REMARK number of reflections in working set:
41780 (87.9%)


REMARK number of reflections in test set:
 2201 (4.6%)







CRYST1 131.153 91.209 85.983 90.00 126.52 90.00 C 2


REMARK FILENAME = “/home/da/alebus/Grenoble0207/Nativa/Refine/Cns/refine_ultimo”


REMARK DATE: Nov. 3, 2002 00:23:10  created by user: alebus


REMARK VERSION:1.1


















ATOM
1
CB
LYS
A
44
20.615
6.288
−2.953
1.00
43.29
A


ATOM
2
CG
LYS
A
44
20.649
7.594
−3.721
1.00
45.66
A


ATOM
3
CD
LYS
A
44
20.631
7.304
−5.234
1.00
46.84
A


ATOM
4
CE
LYS
A
44
21.147
8.499
−6.087
1.00
45.34
A


ATOM
5
NZ
LYS
A
44
22.581
8.809
−5.825
1.00
43.53
A


ATOM
6
C
LYS
A
44
19.693
7.028
−0.721
1.00
41.08
A


ATOM
7
O
LYS
A
44
19.606
8.262
−0.567
1.00
42.77
A


ATOM
8
N
LYS
A
44
21.185
5.059
−0.889
1.00
42.83
A


ATOM
9
CA
LYS
A
44
20.898
6.411
−1.463
1.00
41.97
A


ATOM
10
N
SER
A
45
18.770
6.179
−0.277
1.00
35.27
A


ATOM
11
CA
SER
A
45
17.619
6.627
0.499
1.00
32.35
A


ATOM
12
CB
SER
A
45
16.526
7.122
−0.404
1.00
34.26
A


ATOM
13
OG
SER
A
45
16.035
6.043
−1.151
1.00
36.65
A


ATOM
14
C
SER
A
45
17.044
5.514
1.399
1.00
31.37
A


ATOM
15
O
SER
A
45
17.249
4.324
1.150
1.00
29.02
A


ATOM
16
N
PHE
A
46
16.319
5.918
2.442
1.00
27.54
A


ATOM
17
CA
PHE
A
46
15.697
4.986
3.372
1.00
23.33
A


ATOM
18
CB
PHE
A
46
16.461
4.918
4.703
1.00
24.39
A


ATOM
19
CG
PHE
A
46
17.718
4.150
4.631
1.00
24.94
A


ATOM
20
CD1
PHE
A
46
18.903
4.772
4.320
1.00
27.54
A


ATOM
21
CD2
PHE
A
46
17.715
2.786
4.842
1.00
24.61
A


ATOM
22
CE1
PHE
A
46
20.079
4.047
4.218
1.00
28.38
A


ATOM
23
CE2
PHE
A
46
18.871
2.062
4.745
1.00
25.80
A


ATOM
24
CZ
PHE
A
46
20.059
2.687
4.432
1.00
28.78
A


ATOM
25
C
PHE
A
46
14.353
5.561
3.663
1.00
22.42
A


ATOM
26
O
PHE
A
46
14.228
6.766
3.763
1.00
24.31
A


ATOM
27
N
THR
A
47
13.362
4.705
3.831
1.00
20.85
A


ATOM
28
CA
THR
A
47
12.005
5.110
4.145
1.00
19.91
A


ATOM
29
CB
THR
A
47
11.003
4.255
3.323
1.00
23.60
A


ATOM
30
OG1
THR
A
47
11.101
4.621
1.931
1.00
30.92
A


ATOM
31
CG2
THR
A
47
9.602
4.518
3.756
1.00
28.40
A


ATOM
32
C
THR
A
47
11.838
4.847
5.658
1.00
20.08
A


ATOM
33
O
THR
A
47
12.207
3.773
6.147
1.00
17.57
A


ATOM
34
N
CYS
A
48
11.249
5.800
6.373
1.00
18.11
A


ATOM
35
CA
CYS
A
48
11.063
5.691
7.823
1.00
18.60
A


ATOM
36
CB
CYS
A
48
11.954
6.680
8.572
1.00
18.20
A


ATOM
37
SG
CYS
A
48
13.661
6.540
8.248
1.00
32.01
A


ATOM
38
C
CYS
A
48
9.690
6.080
8.235
1.00
18.84
A


ATOM
39
O
CYS
A
48
9.106
7.001
7.652
1.00
17.62
A


ATOM
40
N
ILE
A
49
9.181
5.386
9.249
1.00
17.10
A


ATOM
41
CA
ILE
A
49
7.924
5.761
9.868
1.00
14.94
A


ATOM
42
CB
ILE
A
49
7.060
4.561
10.259
1.00
16.49
A


ATOM
43
CG2
ILE
A
49
5.765
5.056
10.922
1.00
15.09
A


ATOM
44
CG1
ILE
A
49
6.766
3.697
9.018
1.00
19.56
A


ATOM
45
CD1
ILE
A
49
5.714
2.712
9.244
1.00
18.95
A


ATOM
46
C
ILE
A
49
8.523
6.390
11.164
1.00
17.73
A


ATOM
47
O
ILE
A
49
9.053
5.677
12.037
1.00
14.13
A


ATOM
48
N
ASP
A
50
8.503
7.714
11.254
1.00
17.01
A


ATOM
49
CA
ASP
A
50
9.048
8.388
12.440
1.00
17.48
A


ATOM
50
CB
ASP
A
50
9.531
9.822
12.136
1.00
13.12
A


ATOM
51
CG
ASP
A
50
10.953
9.859
11.578
1.00
21.06
A


ATOM
52
OD1
ASP
A
50
11.710
8.846
11.640
1.00
27.30
A


ATOM
53
OD2
ASP
A
50
11.359
10.907
11.055
1.00
24.19
A


ATOM
54
C
ASP
A
50
7.972
8.422
13.491
1.00
18.22
A


ATOM
55
O
ASP
A
50
6.865
8.952
13.293
1.00
20.05
A


ATOM
56
N
MET
A
51
8.277
7.835
14.628
1.00
15.21
A


ATOM
57
CA
MET
A
51
7.299
7.826
15.681
1.00
15.55
A


ATOM
58
CB
MET
A
51
6.834
6.418
15.875
1.00
18.11
A


ATOM
59
CG
MET
A
51
6.226
5.852
14.581
1.00
22.02
A


ATOM
60
SD
MET
A
51
5.667
4.271
14.916
1.00
25.65
A


ATOM
61
CE
MET
A
51
4.098
4.685
15.860
1.00
20.93
A


ATOM
62
C
MET
A
51
7.913
8.301
16.971
1.00
11.93
A


ATOM
63
O
MET
A
51
9.099
8.508
17.027
1.00
13.17
A


ATOM
64
N
HIS
A
52
7.091
8.490
17.989
1.00
10.52
A


ATOM
65
CA
HIS
A
52
7.649
8.765
19.312
1.00
12.27
A


ATOM
66
CB
HIS
A
52
7.710
10.305
19.630
1.00
9.72
A


ATOM
67
CG
HIS
A
52
6.391
10.949
19.953
1.00
12.04
A


ATOM
68
CD2
HIS
A
52
5.489
11.596
19.162
1.00
9.69
A


ATOM
69
ND1
HIS
A
52
5.881
11.001
21.233
1.00
12.85
A


ATOM
70
CE1
HIS
A
52
4.725
11.647
21.222
1.00
11.94
A


ATOM
71
NE2
HIS
A
52
4.466
12.021
19.979
1.00
13.12
A


ATOM
72
C
HIS
A
52
6.724
8.018
20.270
1.00
12.54
A


ATOM
73
O
HIS
A
52
5.535
7.852
20.002
1.00
13.79
A


ATOM
74
N
THR
A
53
7.270
7.533
21.369
1.00
14.00
A


ATOM
75
CA
THR
A
53
6.456
6.881
22.369
1.00
12.69
A


ATOM
76
CB
THR
A
53
7.006
5.499
22.693
1.00
14.08
A


ATOM
77
OG1
THR
A
53
7.018
4.713
21.499
1.00
14.10
A


ATOM
78
CG2
THR
A
53
6.163
4.814
23.776
1.00
11.71
A


ATOM
79
C
THR
A
53
6.562
7.785
23.611
1.00
16.26
A


ATOM
80
O
THR
A
53
7.574
7.728
24.334
1.00
13.58
A


ATOM
81
N
GLU
A
54
5.546
8.628
23.821
1.00
16.02
A


ATOM
82
CA
GLU
A
54
5.474
9.550
24.953
1.00
17.70
A


ATOM
83
CB
GLU
A
54
5.226
8.751
26.257
1.00
17.93
A


ATOM
84
CG
GLU
A
54
3.931
7.897
26.155
1.00
19.27
A


ATOM
85
CD
GLU
A
54
3.605
7.086
27.390
1.00
26.18
A


ATOM
86
OE1
GLU
A
54
3.942
7.555
28.514
1.00
27.93
A


ATOM
87
OE2
GLU
A
54
2.990
5.983
27.250
1.00
23.64
A


ATOM
88
C
GLU
A
54
6.725
10.434
25.044
1.00
20.11
A


ATOM
89
O
GLU
A
54
7.308
10.619
26.117
1.00
19.57
A


ATOM
90
N
GLY
A
55
7.152
10.953
23.892
1.00
16.98
A


ATOM
91
CA
GLY
A
55
8.291
11.848
23.866
1.00
14.52
A


ATOM
92
C
GLY
A
55
9.597
11.265
23.389
1.00
13.92
A


ATOM
93
O
GLY
A
55
10.487
12.010
22.978
1.00
17.15
A


ATOM
94
N
GLU
A
56
9.733
9.947
23.449
1.00
12.64
A


ATOM
95
CA
GLU
A
56
10.957
9.305
23.012
1.00
12.64
A


ATOM
96
CB
GLU
A
56
11.291
8.108
23.926
1.00
12.43
A


ATOM
97
CG
GLU
A
56
12.538
7.340
23.546
1.00
13.31
A


ATOM
98
CD
GLU
A
56
13.833
8.066
23.845
1.00
13.36
A


ATOM
99
OE1
GLU
A
56
13.805
9.147
24.447
1.00
13.61
A


ATOM
100
OE2
GLU
A
56
14.916
7.554
23.465
1.00
15.37
A


ATOM
101
C
GLU
A
56
10.807
8.838
21.575
1.00
13.28
A


ATOM
102
O
GLU
A
56
9.881
8.099
21.242
1.00
14.77
A


ATOM
103
N
ALA
A
57
11.759
9.240
20.759
1.00
12.77
A


ATOM
104
CA
ALA
A
57
11.773
8.933
19.356
1.00
13.88
A


ATOM
105
CB
ALA
A
57
12.899
9.682
18.678
1.00
14.18
A


ATOM
106
C
ALA
A
57
11.924
7.483
19.073
1.00
16.02
A


ATOM
107
O
ALA
A
57
12.583
6.717
19.810
1.00
14.16
A


ATOM
108
N
ALA
A
58
11.326
7.092
17.960
1.00
14.72
A


ATOM
109
CA
ALA
A
58
11.439
5.708
17.519
1.00
14.82
A


ATOM
110
CB
ALA
A
58
10.277
4.899
18.065
1.00
16.68
A


ATOM
111
C
ALA
A
58
11.371
5.783
15.976
1.00
15.38
A


ATOM
112
O
ALA
A
58
10.283
5.714
15.394
1.00
14.57
A


ATOM
113
N
ARG
A
59
12.523
5.992
15.353
1.00
14.25
A


ATOM
114
CA
ARG
A
59
12.630
6.087
13.891
1.00
15.71
A


ATOM
115
CB
ARG
A
59
13.896
6.835
13.534
1.00
14.51
A


ATOM
116
CG
ARG
A
59
14.306
6.885
12.049
1.00
17.75
A


ATOM
117
CD
ARG
A
59
15.248
8.083
11.816
1.00
16.44
A


ATOM
118
NE
ARG
A
59
14.497
9.340
11.944
1.00
18.31
A


ATOM
119
CZ
ARG
A
59
15.055
10.559
12.063
1.00
18.86
A


ATOM
120
NH1
ARG
A
59
16.363
10.721
12.082
1.00
17.30
A


ATOM
121
NH2
ARG
A
59
14.292
11.628
12.146
1.00
19.95
A


ATOM
122
C
ARG
A
59
12.679
4.670
13.314
1.00
14.31
A


ATOM
123
O
ARG
A
59
13.710
4.015
13.359
1.00
11.88
A


ATOM
124
N
ILE
A
60
11.563
4.224
12.761
1.00
12.93
A


ATOM
125
CA
ILE
A
60
11.502
2.876
12.206
1.00
14.14
A


ATOM
126
CB
ILE
A
60
10.145
2.282
12.498
1.00
16.01
A


ATOM
127
CG2
ILE
A
60
10.080
0.837
11.933
1.00
16.40
A


ATOM
128
CG1
ILE
A
60
9.938
2.257
14.030
1.00
14.56
A


ATOM
129
CD1
ILE
A
60
8.512
1.875
14.500
1.00
13.94
A


ATOM
130
C
ILE
A
60
11.817
2.839
10.718
1.00
13.44
A


ATOM
131
O
ILE
A
60
11.047
3.321
9.896
1.00
15.63
A


ATOM
132
N
VAL
A
61
12.959
2.283
10.373
1.00
13.90
A


ATOM
133
CA
VAL
A
61
13.373
2.220
8.986
1.00
18.11
A


ATOM
134
CB
VAL
A
61
14.885
2.099
8.905
1.00
17.61
A


ATOM
135
CG1
VAL
A
61
15.345
2.012
7.447
1.00
16.23
A


ATOM
136
CG2
VAL
A
61
15.508
3.296
9.565
1.00
14.84
A


ATOM
137
C
VAL
A
61
12.698
1.014
8.332
1.00
21.61
A


ATOM
138
O
VAL
A
61
12.988
−0.130
8.681
1.00
22.60
A


ATOM
139
N
THR
A
62
11.787
1.293
7.399
1.00
22.58
A


ATOM
140
CA
THR
A
62
11.016
0.270
6.717
1.00
22.33
A


ATOM
141
CB
THR
A
62
9.602
0.754
6.430
1.00
21.33
A


ATOM
142
OG1
THR
A
62
9.684
1.915
5.617
1.00
26.78
A


ATOM
143
CG2
THR
A
62
8.863
1.088
7.716
1.00
23.19
A


ATOM
144
C
THR
A
62
11.598
−0.231
5.398
1.00
24.06
A


ATOM
145
O
THR
A
62
11.228
−1.321
4.941
1.00
24.17
A


ATOM
146
N
SER
A
63
12.475
0.535
4.773
1.00
21.99
A


ATOM
147
CA
SER
A
63
13.098
0.088
3.527
1.00
23.76
A


ATOM
148
CB
SER
A
63
12.151
0.246
2.312
1.00
26.04
A


ATOM
149
OG
SER
A
63
12.349
1.516
1.696
1.00
33.16
A


ATOM
150
C
SER
A
63
14.367
0.869
3.248
1.00
22.10
A


ATOM
151
O
SER
A
63
14.538
1.983
3.722
1.00
22.92
A


ATOM
152
N
GLY
A
64
15.272
0.252
2.506
1.00
20.57
A


ATOM
153
CA
GLY
A
64
16.499
0.911
2.124
1.00
21.51
A


ATOM
154
C
GLY
A
64
17.704
0.021
2.329
1.00
21.96
A


ATOM
155
O
GLY
A
64
18.740
0.213
1.690
1.00
21.33
A


ATOM
156
N
LEU
A
65
17.591
−0.938
3.248
1.00
21.03
A


ATOM
157
CA
LEU
A
65
18.716
−1.821
3.515
1.00
21.89
A


ATOM
158
CB
LEU
A
65
18.524
−2.545
4.858
1.00
23.31
A


ATOM
159
CG
LEU
A
65
18.805
−1.852
6.195
1.00
21.07
A


ATOM
160
CD1
LEU
A
65
18.461
−2.854
7.286
1.00
18.87
A


ATOM
161
CD2
LEU
A
65
20.274
−1.400
6.286
1.00
17.46
A


ATOM
162
C
LEU
A
65
18.927
−2.906
2.468
1.00
21.41
A


ATOM
163
O
LEU
A
65
17.979
−3.377
1.858
1.00
23.58
A


ATOM
164
N
PRO
A
66
20.182
−3.291
2.227
1.00
23.00
A


ATOM
165
CD
PRO
A
66
21.437
−2.632
2.657
1.00
19.77
A


ATOM
166
CA
PRO
A
66
20.444
−4.372
1.252
1.00
22.04
A


ATOM
167
CB
PRO
A
66
21.933
−4.214
0.960
1.00
21.76
A


ATOM
168
CG
PRO
A
66
22.480
−3.668
2.306
1.00
22.66
A


ATOM
169
C
PRO
A
66
20.197
−5.648
2.076
1.00
25.01
A


ATOM
170
O
PRO
A
66
19.774
−5.562
3.233
1.00
24.41
A


ATOM
171
N
HIS
A
67
20.445
−6.828
1.516
1.00
27.46
A


ATOM
172
CA
HIS
A
67
20.303
−8.042
2.327
1.00
28.25
A


ATOM
173
CB
HIS
A
67
20.597
−9.296
1.506
1.00
30.96
A


ATOM
174
CG
HIS
A
67
20.636
−10.545
2.328
1.00
32.96
A


ATOM
175
CD2
HIS
A
67
19.645
−11.256
2.914
1.00
32.55
A


ATOM
176
ND1
HIS
A
67
21.818
−11.166
2.686
1.00
36.69
A


ATOM
177
CE1
HIS
A
67
21.549
−12.203
3.457
1.00
33.28
A


ATOM
178
NE2
HIS
A
67
20.238
−12.279
3.610
1.00
33.49
A


ATOM
179
C
HIS
A
67
21.367
−7.935
3.430
1.00
27.80
A


ATOM
180
O
HIS
A
67
22.466
−7.496
3.158
1.00
27.68
A


ATOM
181
N
ILE
A
68
21.028
−8.319
4.661
1.00
26.99
A


ATOM
182
CA
ILE
A
68
21.965
−8.285
5.782
1.00
24.94
A


ATOM
183
CB
ILE
A
68
21.404
−7.433
6.968
1.00
22.93
A


ATOM
184
CG2
ILE
A
68
22.319
−7.549
8.147
1.00
19.99
A


ATOM
185
CG1
ILE
A
68
21.261
−5.953
6.543
1.00
20.08
A


ATOM
186
CD1
ILE
A
68
22.594
−5.284
6.161
1.00
20.15
A


ATOM
187
C
ILE
A
68
22.142
−9.747
6.246
1.00
26.15
A


ATOM
188
O
ILE
A
68
21.206
−10.377
6.742
1.00
25.93
A


ATOM
189
N
PRO
A
69
23.347
−10.298
6.103
1.00
26.77
A


ATOM
190
CD
PRO
A
69
24.504
−9.912
5.282
1.00
27.67
A


ATOM
191
CA
PRO
A
69
23.448
−11.683
6.552
1.00
28.58
A


ATOM
192
CB
PRO
A
69
24.800
−12.132
5.989
1.00
28.02
A


ATOM
193
CG
PRO
A
69
25.537
−10.891
5.716
1.00
30.49
A


ATOM
194
C
PRO
A
69
23.301
−11.914
8.064
1.00
28.45
A


ATOM
195
O
PRO
A
69
23.574
−11.031
8.879
1.00
27.11
A


ATOM
196
N
GLY
A
70
22.833
−13.112
8.407
1.00
27.37
A


ATOM
197
CA
GLY
A
70
22.664
−13.499
9.798
1.00
27.72
A


ATOM
198
C
GLY
A
70
21.548
−14.515
9.885
1.00
28.99
A


ATOM
199
O
GLY
A
70
20.503
−14.327
9.251
1.00
29.07
A


ATOM
200
N
SER
A
71
21.723
−15.582
10.661
1.00
28.80
A


ATOM
201
CA
SER
A
71
20.642
−16.564
10.717
1.00
31.13
A


ATOM
202
CB
SER
A
71
21.198
−17.985
10.918
1.00
31.64
A


ATOM
203
OG
SER
A
71
21.813
−18.137
12.189
1.00
37.34
A


ATOM
204
C
SER
A
71
19.581
−16.229
11.766
1.00
31.53
A


ATOM
205
O
SER
A
71
18.564
−16.919
11.863
1.00
31.74
A


ATOM
206
N
ASN
A
72
19.810
−15.170
12.549
1.00
29.98
A


ATOM
207
CA
ASN
A
72
18.818
−14.723
13.532
1.00
27.95
A


ATOM
208
CB
ASN
A
72
18.978
−15.432
14.889
1.00
27.77
A


ATOM
209
CG
ASN
A
72
20.367
−15.274
15.471
1.00
28.15
A


ATOM
210
OD1
ASN
A
72
20.971
−14.222
15.376
1.00
29.74
A


ATOM
211
ND2
ASN
A
72
20.872
−16.327
16.093
1.00
30.36
A


ATOM
212
C
ASN
A
72
18.994
−13.217
13.698
1.00
26.29
A


ATOM
213
O
ASN
A
72
19.937
−12.640
13.182
1.00
25.46
A


ATOM
214
N
MET
A
73
18.084
−12.587
14.421
1.00
25.13
A


ATOM
215
CA
MET
A
73
18.137
−11.145
14.577
1.00
25.69
A


ATOM
216
CB
MET
A
73
16.862
−10.712
15.298
1.00
26.70
A


ATOM
217
CG
MET
A
73
16.066
−9.589
14.629
1.00
31.37
A


ATOM
218
SD
MET
A
73
16.059
−9.539
12.826
1.00
28.71
A


ATOM
219
CE
MET
A
73
14.998
−10.868
12.484
1.00
29.39
A


ATOM
220
C
MET
A
73
19.426
−10.651
15.265
1.00
25.28
A


ATOM
221
O
MET
A
73
19.987
−9.601
14.892
1.00
25.94
A


ATOM
222
N
ALA
A
74
19.929
−11.408
16.235
1.00
23.64
A


ATOM
223
CA
ALA
A
74
21.168
−11.020
16.906
1.00
22.23
A


ATOM
224
CB
ALA
A
74
21.453
−11.956
18.102
1.00
22.03
A


ATOM
225
C
ALA
A
74
22.364
−11.018
15.943
1.00
21.64
A


ATOM
226
O
ALA
A
74
23.283
−10.184
16.063
1.00
21.49
A


ATOM
227
N
GLU
A
75
22.394
−11.940
14.992
1.00
20.77
A


ATOM
228
CA
GLU
A
75
23.532
−11.933
14.071
1.00
22.04
A


ATOM
229
CB
GLU
A
75
23.641
−13.262
13.322
1.00
24.69
A


ATOM
230
CG
GLU
A
75
24.048
−14.407
14.235
1.00
29.64
A


ATOM
231
CD
GLU
A
75
24.196
−15.750
13.502
1.00
36.55
A


ATOM
232
OE1
GLU
A
75
24.396
−16.761
14.214
1.00
35.91
A


ATOM
233
OE2
GLU
A
75
24.109
−15.795
12.238
1.00
36.81
A


ATOM
234
C
GLU
A
75
23.429
−10.794
13.080
1.00
19.77
A


ATOM
235
O
GLU
A
75
24.434
−10.247
12.636
1.00
21.47
A


ATOM
236
N
LYS
A
76
22.212
−10.457
12.711
1.00
19.70
A


ATOM
237
CA
LYS
A
76
21.988
−9.368
11.772
1.00
20.97
A


ATOM
238
CB
LYS
A
76
20.507
−9.326
11.366
1.00
23.57
A


ATOM
239
CG
LYS
A
76
20.093
−10.486
10.463
1.00
26.56
A


ATOM
240
CD
LYS
A
76
18.856
−10.154
9.699
1.00
31.83
A


ATOM
241
CE
LYS
A
76
18.567
−11.228
8.690
1.00
36.06
A


ATOM
242
NZ
LYS
A
76
17.800
−10.601
7.593
1.00
40.32
A


ATOM
243
C
LYS
A
76
22.381
−8.093
12.484
1.00
18.46
A


ATOM
244
O
LYS
A
76
22.919
−7.196
11.878
1.00
21.85
A


ATOM
245
N
LYS
A
77
22.103
−8.015
13.783
1.00
18.56
A


ATOM
246
CA
LYS
A
77
22.488
−6.834
14.562
1.00
20.12
A


ATOM
247
CB
LYS
A
77
21.955
−6.936
15.993
1.00
20.58
A


ATOM
248
CG
LYS
A
77
22.453
−5.820
16.889
1.00
23.41
A


ATOM
249
CD
LYS
A
77
22.270
−6.191
18.374
1.00
27.57
A


ATOM
250
CE
LYS
A
77
23.362
−7.150
18.819
1.00
26.72
A


ATOM
251
NZ
LYS
A
77
23.370
−7.270
20.291
1.00
30.73
A


ATOM
252
C
LYS
A
77
24.013
−6.705
14.599
1.00
21.31
A


ATOM
253
O
LYS
A
77
24.581
−5.607
14.380
1.00
19.27
A


ATOM
254
N
ALA
A
78
24.690
−7.822
14.890
1.00
22.65
A


ATOM
255
CA
ALA
A
78
26.151
−7.824
14.951
1.00
21.66
A


ATOM
256
CB
ALA
A
78
26.681
−9.198
15.437
1.00
20.69
A


ATOM
257
C
ALA
A
78
26.703
−7.506
13.557
1.00
21.46
A


ATOM
258
O
ALA
A
78
27.716
−6.848
13.417
1.00
23.60
A


ATOM
259
N
TYR
A
79
26.044
−7.963
12.515
1.00
23.23
A


ATOM
260
CA
TYR
A
79
26.538
−7.647
11.159
1.00
24.48
A


ATOM
261
CB
TYR
A
79
25.702
−8.347
10.087
1.00
23.95
A


ATOM
262
CG
TYR
A
79
26.324
−8.216
8.723
1.00
27.94
A


ATOM
263
CD1
TYR
A
79
27.183
−9.219
8.230
1.00
30.43
A


ATOM
264
CE1
TYR
A
79
27.825
−9.089
6.991
1.00
32.06
A


ATOM
265
CD2
TYR
A
79
26.110
−7.073
7.943
1.00
26.91
A


ATOM
266
CE2
TYR
A
79
26.739
−6.918
6.706
1.00
29.70
A


ATOM
267
CZ
TYR
A
79
27.597
−7.935
6.231
1.00
33.31
A


ATOM
268
OH
TYR
A
79
28.213
−7.821
5.004
1.00
31.81
A


ATOM
269
C
TYR
A
79
26.476
−6.124
10.925
1.00
22.69
A


ATOM
270
O
TYR
A
79
27.462
−5.504
10.540
1.00
23.34
A


ATOM
271
N
LEU
A
80
25.319
−5.527
11.160
1.00
22.46
A


ATOM
272
CA
LEU
A
80
25.187
−4.078
10.988
1.00
23.85
A


ATOM
273
CB
LEU
A
80
23.801
−3.617
11.455
1.00
22.25
A


ATOM
274
CG
LEU
A
80
22.743
−4.066
10.433
1.00
22.54
A


ATOM
275
CD1
LEU
A
80
21.349
−4.078
11.069
1.00
24.63
A


ATOM
276
CD2
LEU
A
80
22.788
−3.126
9.213
1.00
20.87
A


ATOM
277
C
LEU
A
80
26.278
−3.373
11.773
1.00
22.91
A


ATOM
278
O
LEU
A
80
27.001
−2.522
11.248
1.00
22.48
A


ATOM
279
N
GLN
A
81
26.452
−3.778
13.025
1.00
24.64
A


ATOM
280
CA
GLN
A
81
27.446
−3.137
13.867
1.00
24.12
A


ATOM
281
CB
GLN
A
81
27.336
−3.641
15.297
1.00
26.17
A


ATOM
282
CG
GLN
A
81
28.324
−2.974
16.237
1.00
34.02
A


ATOM
283
CD
GLN
A
81
27.922
−3.169
17.682
1.00
39.76
A


ATOM
284
OE1
GLN
A
81
27.987
−2.243
18.495
1.00
42.80
A


ATOM
285
NE2
GLN
A
81
27.485
−4.384
18.013
1.00
42.11
A


ATOM
286
C
GLN
A
81
28.882
−3.289
13.425
1.00
25.91
A


ATOM
287
O
GLN
A
81
29.688
−2.349
13.545
1.00
24.54
A


ATOM
288
N
GLU
A
82
29.238
−4.477
12.942
1.00
26.23
A


ATOM
289
CA
GLU
A
82
30.621
−4.694
12.547
1.00
27.94
A


ATOM
290
CB
GLU
A
82
30.989
−6.192
12.668
1.00
27.33
A


ATOM
291
CG
GLU
A
82
30.834
−6.750
14.083
1.00
34.38
A


ATOM
292
CD
GLU
A
82
30.963
−8.283
14.165
1.00
37.63
A


ATOM
293
OE1
GLU
A
82
30.675
−8.832
15.253
1.00
40.42
A


ATOM
294
OE2
GLU
A
82
31.348
−8.937
13.159
1.00
38.38
A


ATOM
295
C
GLU
A
82
30.945
−4.206
11.133
1.00
26.64
A


ATOM
296
O
GLU
A
82
32.063
−3.775
10.884
1.00
27.50
A


ATOM
297
N
ASN
A
83
29.977
−4.247
10.224
1.00
24.69
A


ATOM
298
CA
ASN
A
83
30.261
−3.874
8.839
1.00
25.21
A


ATOM
299
CB
ASN
A
83
30.003
−5.089
7.963
1.00
25.28
A


ATOM
300
CG
ASN
A
83
30.679
−6.333
8.514
1.00
27.39
A


ATOM
301
OD1
ASN
A
83
31.901
−6.371
8.646
1.00
28.14
A


ATOM
302
ND2
ASN
A
83
29.879
−7.333
8.888
1.00
27.65
A


ATOM
303
C
ASN
A
83
29.569
−2.677
8.197
1.00
26.32
A


ATOM
304
O
ASN
A
83
29.982
−2.236
7.099
1.00
25.85
A


ATOM
305
N
MET
A
84
28.530
−2.153
8.848
1.00
24.24
A


ATOM
306
CA
MET
A
84
27.776
−1.031
8.278
1.00
23.55
A


ATOM
307
CB
MET
A
84
26.574
−1.583
7.518
1.00
20.89
A


ATOM
308
CG
MET
A
84
26.934
−2.691
6.504
1.00
26.55
A


ATOM
309
SD
MET
A
84
25.498
−3.241
5.536
1.00
30.67
A


ATOM
310
CE
MET
A
84
25.283
−1.794
4.446
1.00
28.24
A


ATOM
311
C
MET
A
84
27.321
−0.045
9.351
1.00
21.14
A


ATOM
312
O
MET
A
84
26.220
0.486
9.320
1.00
22.98
A


ATOM
313
N
ASP
A
85
28.210
0.251
10.271
1.00
21.65
A


ATOM
314
CA
ASP
A
85
27.862
1.114
11.383
1.00
21.92
A


ATOM
315
CB
ASP
A
85
28.939
1.061
12.446
1.00
23.59
A


ATOM
316
CG
ASP
A
85
28.453
1.623
13.754
1.00
26.12
A


ATOM
317
OD1
ASP
A
85
29.172
2.460
14.357
1.00
27.42
A


ATOM
318
OD2
ASP
A
85
27.343
1.223
14.174
1.00
25.97
A


ATOM
319
C
ASP
A
85
27.616
2.548
11.006
1.00
22.06
A


ATOM
320
O
ASP
A
85
26.977
3.275
11.747
1.00
19.57
A


ATOM
321
N
TYR
A
86
28.119
2.951
9.847
1.00
21.34
A


ATOM
322
CA
TYR
A
86
27.915
4.316
9.376
1.00
21.09
A


ATOM
323
CB
TYR
A
86
28.813
4.559
8.144
1.00
22.25
A


ATOM
324
CG
TYR
A
86
28.466
3.685
6.966
1.00
22.22
A


ATOM
325
CD1
TYR
A
86
27.550
4.113
6.012
1.00
21.01
A


ATOM
326
CE1
TYR
A
86
27.170
3.293
4.950
1.00
22.57
A


ATOM
327
CD2
TYR
A
86
29.012
2.398
6.830
1.00
20.83
A


ATOM
328
CE2
TYR
A
86
28.639
1.573
5.773
1.00
22.92
A


ATOM
329
CZ
TYR
A
86
27.713
2.026
4.845
1.00
20.81
A


ATOM
330
OH
TYR
A
86
27.252
1.209
3.858
1.00
24.84
A


ATOM
331
C
TYR
A
86
26.418
4.558
9.046
1.00
20.01
A


ATOM
332
O
TYR
A
86
25.962
5.709
8.997
1.00
19.86
A


ATOM
333
N
LEU
A
87
25.654
3.489
8.841
1.00
18.58
A


ATOM
334
CA
LEU
A
87
24.236
3.635
8.546
1.00
19.32
A


ATOM
335
CB
LEU
A
87
23.601
2.299
8.152
1.00
20.93
A


ATOM
336
CG
LEU
A
87
23.970
1.731
6.753
1.00
23.72
A


ATOM
337
CD1
LEU
A
87
23.110
0.467
6.459
1.00
21.09
A


ATOM
338
CD2
LEU
A
87
23.730
2.798
5.684
1.00
21.56
A


ATOM
339
C
LEU
A
87
23.557
4.168
9.802
1.00
22.57
A


ATOM
340
O
LEU
A
87
22.881
5.219
9.761
1.00
23.70
A


ATOM
341
N
ARG
A
88
23.728
3.446
10.914
1.00
18.66
A


ATOM
342
CA
ARG
A
88
23.178
3.868
12.200
1.00
17.18
A


ATOM
343
CB
ARG
A
88
23.791
3.035
13.340
1.00
16.82
A


ATOM
344
CG
ARG
A
88
23.393
3.500
14.755
1.00
15.73
A


ATOM
345
CD
ARG
A
88
24.192
2.736
15.841
1.00
14.74
A


ATOM
346
NE
ARG
A
88
25.638
2.992
15.790
1.00
14.51
A


ATOM
347
CZ
ARG
A
88
26.248
4.048
16.335
1.00
18.63
A


ATOM
348
NH1
ARG
A
88
25.548
4.977
16.987
1.00
15.86
A


ATOM
349
NH2
ARG
A
88
27.570
4.168
16.236
1.00
16.53
A


ATOM
350
C
ARG
A
88
23.538
5.342
12.444
1.00
17.32
A


ATOM
351
O
ARG
A
88
22.691
6.165
12.773
1.00
17.20
A


ATOM
352
N
ARG
A
89
24.805
5.663
12.275
1.00
18.21
A


ATOM
353
CA
ARG
A
89
25.245
7.011
12.527
1.00
17.70
A


ATOM
354
CB
ARG
A
89
26.752
7.055
12.448
1.00
17.76
A


ATOM
355
CG
ARG
A
89
27.360
6.118
13.470
1.00
23.83
A


ATOM
356
CD
ARG
A
89
28.759
6.521
13.831
1.00
25.48
A


ATOM
357
NE
ARG
A
89
29.600
6.742
12.654
1.00
29.29
A


ATOM
358
CZ
ARG
A
89
30.261
5.795
11.977
1.00
33.21
A


ATOM
359
NH1
ARG
A
89
30.196
4.508
12.339
1.00
31.83
A


ATOM
360
NH2
ARG
A
89
31.023
6.152
10.946
1.00
29.73
A


ATOM
361
C
ARG
A
89
24.597
8.055
11.633
1.00
16.73
A


ATOM
362
O
ARG
A
89
24.228
9.130
12.114
1.00
16.87
A


ATOM
363
N
GLY
A
90
24.405
7.751
10.349
1.00
16.66
A


ATOM
364
CA
GLY
A
90
23.763
8.748
9.489
1.00
15.65
A


ATOM
365
C
GLY
A
90
22.267
8.905
9.742
1.00
16.02
A


ATOM
366
O
GLY
A
90
21.684
9.955
9.519
1.00
17.00
A


ATOM
367
N
ILE
A
91
21.630
7.836
10.207
1.00
16.42
A


ATOM
368
CA
ILE
A
91
20.203
7.833
10.463
1.00
14.69
A


ATOM
369
CB
ILE
A
91
19.684
6.385
10.366
1.00
15.27
A


ATOM
370
CG2
ILE
A
91
18.211
6.313
10.782
1.00
15.69
A


ATOM
371
CG1
ILE
A
91
19.944
5.872
8.937
1.00
17.64
A


ATOM
372
CD1
ILE
A
91
19.610
4.380
8.737
1.00
16.19
A


ATOM
373
C
ILE
A
91
19.869
8.405
11.844
1.00
15.63
A


ATOM
374
O
ILE
A
91
18.827
9.025
12.038
1.00
15.86
A


ATOM
375
N
MET
A
92
20.758
8.178
12.798
1.00
14.75
A


ATOM
376
CA
MET
A
92
20.555
8.611
14.170
1.00
15.17
A


ATOM
377
CB
MET
A
92
21.213
7.624
15.137
1.00
14.47
A


ATOM
378
CG
MET
A
92
20.601
6.219
15.213
1.00
13.01
A


ATOM
379
SD
MET
A
92
18.978
6.209
15.930
1.00
17.19
A


ATOM
380
CE
MET
A
92
17.835
6.183
14.338
1.00
16.35
A


ATOM
381
C
MET
A
92
21.102
9.981
14.525
1.00
15.24
A


ATOM
382
O
MET
A
92
20.505
10.675
15.324
1.00
17.97
A


ATOM
383
N
LEU
A
93
22.236
10.372
13.951
1.00
16.45
A


ATOM
384
CA
LEU
A
93
22.873
11.622
14.359
1.00
17.69
A


ATOM
385
CB
LEU
A
93
24.392
11.427
14.372
1.00
17.36
A


ATOM
386
CG
LEU
A
93
24.907
10.217
15.139
1.00
18.15
A


ATOM
387
CD1
LEU
A
93
26.467
10.218
15.074
1.00
20.38
A


ATOM
388
CD2
LEU
A
93
24.468
10.331
16.617
1.00
19.39
A


ATOM
389
C
LEU
A
93
22.533
12.815
13.483
1.00
18.28
A


ATOM
390
O
LEU
A
93
21.978
12.644
12.398
1.00
16.95
A


ATOM
391
N
GLU
A
94
22.859
14.018
13.966
1.00
16.83
A


ATOM
392
CA
GLU
A
94
22.636
15.231
13.185
1.00
17.55
A


ATOM
393
CB
GLU
A
94
23.241
16.445
13.889
1.00
16.93
A


ATOM
394
CG
GLU
A
94
22.509
16.931
15.139
1.00
15.03
A


ATOM
395
CD
GLU
A
94
23.126
18.232
15.644
1.00
18.68
A


ATOM
396
OE1
GLU
A
94
23.146
19.212
14.874
1.00
14.75
A


ATOM
397
OE2
GLU
A
94
23.594
18.274
16.799
1.00
20.51
A


ATOM
398
C
GLU
A
94
23.397
15.008
11.881
1.00
17.15
A


ATOM
399
O
GLU
A
94
24.399
14.302
11.867
1.00
19.87
A


ATOM
400
N
PRO
A
95
22.981
15.657
10.785
1.00
17.47
A


ATOM
401
CD
PRO
A
95
23.728
15.618
9.500
1.00
13.75
A


ATOM
402
CA
PRO
A
95
21.837
16.587
10.724
1.00
14.31
A


ATOM
403
CB
PRO
A
95
22.173
17.466
9.521
1.00
12.04
A


ATOM
404
CG
PRO
A
95
22.811
16.440
8.547
1.00
14.31
A


ATOM
405
C
PRO
A
95
20.461
15.914
10.569
1.00
14.91
A


ATOM
406
O
PRO
A
95
19.433
16.587
10.759
1.00
13.85
A


ATOM
407
N
ARG
A
96
20.416
14.608
10.255
1.00
14.35
A


ATOM
408
CA
ARG
A
96
19.107
13.939
10.059
1.00
14.78
A


ATOM
409
CB
ARG
A
96
19.226
12.720
9.125
1.00
17.07
A


ATOM
410
CG
ARG
A
96
19.741
13.101
7.724
1.00
16.75
A


ATOM
411
CD
ARG
A
96
20.191
11.906
6.917
1.00
14.98
A


ATOM
412
NE
ARG
A
96
20.844
12.328
5.665
1.00
16.89
A


ATOM
413
CZ
ARG
A
96
22.085
12.801
5.598
1.00
18.63
A


ATOM
414
NH1
ARG
A
96
22.821
12.916
6.701
1.00
15.91
A


ATOM
415
NH2
ARG
A
96
22.599
13.163
4.428
1.00
16.81
A


ATOM
416
C
ARG
A
96
18.460
13.497
11.353
1.00
13.78
A


ATOM
417
O
ARG
A
96
17.250
13.289
11.389
1.00
14.58
A


ATOM
418
N
GLY
A
97
19.267
13.318
12.400
1.00
14.31
A


ATOM
419
CA
GLY
A
97
18.744
12.906
13.706
1.00
10.79
A


ATOM
420
C
GLY
A
97
19.316
13.888
14.739
1.00
15.14
A


ATOM
421
O
GLY
A
97
19.489
15.079
14.429
1.00
7.59
A


ATOM
422
N
HIS
A
98
19.646
13.406
15.941
1.00
10.85
A


ATOM
423
CA
HIS
A
98
20.198
14.288
16.958
1.00
14.07
A


ATOM
424
CB
HIS
A
98
19.178
15.337
17.466
1.00
8.74
A


ATOM
425
CG
HIS
A
98
17.937
14.760
18.073
1.00
13.09
A


ATOM
426
CD2
HIS
A
98
16.764
14.370
17.504
1.00
14.21
A


ATOM
427
ND1
HIS
A
98
17.770
14.604
19.433
1.00
13.11
A


ATOM
428
CE1
HIS
A
98
16.552
14.148
19.677
1.00
14.59
A


ATOM
429
NE2
HIS
A
98
15.921
13.996
18.523
1.00
13.08
A


ATOM
430
C
HIS
A
98
20.712
13.438
18.109
1.00
16.45
A


ATOM
431
O
HIS
A
98
20.539
12.216
18.115
1.00
19.11
A


ATOM
432
N
ASP
A
99
21.320
14.091
19.086
1.00
16.12
A


ATOM
433
CA
ASP
A
99
21.931
13.403
20.203
1.00
17.48
A


ATOM
434
CB
ASP
A
99
22.668
14.418
21.094
1.00
15.66
A


ATOM
435
CG
ASP
A
99
23.915
14.952
20.440
1.00
16.01
A


ATOM
436
OD1
ASP
A
99
24.427
14.349
19.465
1.00
18.90
A


ATOM
437
OD2
ASP
A
99
24.417
15.988
20.899
1.00
23.85
A


ATOM
438
C
ASP
A
99
21.060
12.511
21.052
1.00
18.60
A


ATOM
439
O
ASP
A
99
21.584
11.708
21.823
1.00
19.70
A


ATOM
440
N
ASP
A
100
19.740
12.633
20.918
1.00
17.35
A


ATOM
441
CA
ASP
A
100
18.827
11.814
21.702
1.00
15.56
A


ATOM
442
CB
ASP
A
100
18.090
12.721
22.685
1.00
14.97
A


ATOM
443
CG
ASP
A
100
19.047
13.235
23.761
1.00
19.99
A


ATOM
444
OD1
ASP
A
100
19.281
12.471
24.737
1.00
20.11
A


ATOM
445
OD2
ASP
A
100
19.597
14.355
23.601
1.00
13.67
A


ATOM
446
C
ASP
A
100
17.848
11.000
20.838
1.00
15.48
A


ATOM
447
O
ASP
A
100
16.791
10.568
21.308
1.00
12.21
A


ATOM
448
N
MET
A
101
18.242
10.815
19.581
1.00
15.25
A


ATOM
449
CA
MET
A
101
17.442
10.062
18.621
1.00
15.36
A


ATOM
450
CB
MET
A
101
17.948
10.352
17.200
1.00
14.76
A


ATOM
451
CG
MET
A
101
17.268
9.571
16.033
1.00
13.95
A


ATOM
452
SD
MET
A
101
15.482
9.588
16.014
1.00
13.64
A


ATOM
453
CE
MET
A
101
15.128
11.365
15.913
1.00
12.08
A


ATOM
454
C
MET
A
101
17.566
8.566
18.942
1.00
15.87
A


ATOM
455
O
MET
A
101
18.577
8.063
19.539
1.00
10.67
A


ATOM
456
N
PHE
A
102
16.514
7.851
18.594
1.00
13.47
A


ATOM
457
CA
PHE
A
102
16.529
6.390
18.796
1.00
13.24
A


ATOM
458
CB
PHE
A
102
15.768
6.020
20.059
1.00
11.30
A


ATOM
459
CG
PHE
A
102
15.970
4.596
20.495
1.00
14.49
A


ATOM
460
CD1
PHE
A
102
16.932
4.285
21.443
1.00
17.54
A


ATOM
461
CD2
PHE
A
102
15.250
3.557
19.899
1.00
18.57
A


ATOM
462
CE1
PHE
A
102
17.199
2.936
21.795
1.00
17.59
A


ATOM
463
CE2
PHE
A
102
15.516
2.174
20.246
1.00
14.85
A


ATOM
464
CZ
PHE
A
102
16.494
1.897
21.189
1.00
16.14
A


ATOM
465
C
PHE
A
102
15.792
5.781
17.599
1.00
13.32
A


ATOM
466
O
PHE
A
102
14.898
6.412
17.062
1.00
14.93
A


ATOM
467
N
GLY
A
103
16.130
4.572
17.189
1.00
14.70
A


ATOM
468
CA
GLY
A
103
15.386
3.990
16.074
1.00
16.20
A


ATOM
469
C
GLY
A
103
15.584
2.487
15.907
1.00
18.65
A


ATOM
470
O
GLY
A
103
16.136
1.835
16.784
1.00
17.53
A


ATOM
471
N
ALA
A
104
15.111
1.934
14.790
1.00
15.29
A


ATOM
472
CA
ALA
A
104
15.233
0.522
14.540
1.00
15.59
A


ATOM
473
CB
ALA
A
104
14.145
−0.160
15.241
1.00
11.49
A


ATOM
474
C
ALA
A
104
15.124
0.206
13.042
1.00
19.00
A


ATOM
475
O
ALA
A
104
14.524
0.976
12.265
1.00
19.13
A


ATOM
476
N
PHE
A
105
15.705
−0.925
12.662
1.00
18.37
A


ATOM
477
CA
PHE
A
105
15.618
−1.448
11.295
1.00
18.11
A


ATOM
478
CB
PHE
A
105
16.944
−1.976
10.815
1.00
16.70
A


ATOM
479
CG
PHE
A
105
17.965
−0.921
10.536
1.00
20.05
A


ATOM
480
CD1
PHE
A
105
19.143
−0.871
11.283
1.00
20.65
A


ATOM
481
CD2
PHE
A
105
17.818
−0.046
9.452
1.00
16.06
A


ATOM
482
CE1
PHE
A
105
20.162
0.009
10.950
1.00
20.60
A


ATOM
483
CE2
PHE
A
105
18.838
0.836
9.126
1.00
19.84
A


ATOM
484
CZ
PHE
A
105
20.021
0.865
9.871
1.00
17.14
A


ATOM
485
C
PHE
A
105
14.646
−2.635
11.355
1.00
19.49
A


ATOM
486
O
PHE
A
105
14.778
−3.528
12.210
1.00
18.11
A


ATOM
487
N
LEU
A
106
13.646
−2.622
10.481
1.00
17.64
A


ATOM
488
CA
LEU
A
106
12.699
−3.717
10.375
1.00
19.09
A


ATOM
489
CB
LEU
A
106
11.345
−3.236
9.843
1.00
18.18
A


ATOM
490
CG
LEU
A
106
10.537
−2.315
10.725
1.00
19.53
A


ATOM
491
CD1
LEU
A
106
9.170
−2.039
10.105
1.00
18.35
A


ATOM
492
CD2
LEU
A
106
10.371
−3.012
12.107
1.00
14.58
A


ATOM
493
C
LEU
A
106
13.257
−4.756
9.395
1.00
20.13
A


ATOM
494
O
LEU
A
106
13.975
−4.414
8.447
1.00
21.09
A


ATOM
495
N
PHE
A
107
12.923
−6.025
9.632
1.00
19.65
A


ATOM
496
CA
PHE
A
107
13.364
−7.122
8.774
1.00
19.75
A


ATOM
497
CB
PHE
A
107
14.557
−7.863
9.378
1.00
19.25
A


ATOM
498
CG
PHE
A
107
15.814
−7.081
9.416
1.00
21.72
A


ATOM
499
CD1
PHE
A
107
16.189
−6.397
10.565
1.00
18.65
A


ATOM
500
CD2
PHE
A
107
16.667
−7.075
8.316
1.00
19.05
A


ATOM
501
CE1
PHE
A
107
17.420
−5.718
10.615
1.00
17.88
A


ATOM
502
CE2
PHE
A
107
17.900
−6.405
8.361
1.00
22.07
A


ATOM
503
CZ
PHE
A
107
18.276
−5.723
9.525
1.00
19.88
A


ATOM
504
C
PHE
A
107
12.244
−8.136
8.727
1.00
21.28
A


ATOM
505
O
PHE
A
107
11.313
−8.099
9.569
1.00
20.80
A


ATOM
506
N
ASP
A
108
12.326
−9.077
7.786
1.00
22.42
A


ATOM
507
CA
ASP
A
108
11.318
−10.149
7.779
1.00
23.81
A


ATOM
508
CB
ASP
A
108
11.528
−11.125
6.618
1.00
27.23
A


ATOM
509
CG
ASP
A
108
11.260
−10.502
5.247
1.00
33.34
A


ATOM
510
OD1
ASP
A
108
10.305
−9.698
5.121
1.00
31.69
A


ATOM
511
OD2
ASP
A
108
12.013
−10.852
4.306
1.00
35.16
A


ATOM
512
C
ASP
A
108
11.581
−10.967
9.071
1.00
22.73
A


ATOM
513
O
ASP
A
108
12.729
−11.114
9.500
1.00
21.59
A


ATOM
514
N
PRO
A
109
10.535
−11.534
9.674
1.00
24.11
A


ATOM
515
CD
PRO
A
109
9.125
−11.592
9.235
1.00
27.42
A


ATOM
516
CA
PRO
A
109
10.742
−12.321
10.889
1.00
26.64
A


ATOM
517
CB
PRO
A
109
9.320
−12.626
11.348
1.00
26.54
A


ATOM
518
CG
PRO
A
109
8.574
−12.761
10.062
1.00
27.76
A


ATOM
519
C
PRO
A
109
11.533
−13.582
10.536
1.00
27.91
A


ATOM
520
O
PRO
A
109
11.531
−13.995
9.386
1.00
28.57
A


ATOM
521
N
ILE
A
110
12.278
−14.129
11.496
1.00
27.71
A


ATOM
522
CA
ILE
A
110
13.009
−15.370
11.281
1.00
27.40
A


ATOM
523
CB
ILE
A
110
14.533
−15.210
11.509
1.00
26.59
A


ATOM
524
CG2
ILE
A
110
15.231
−16.579
11.612
1.00
26.12
A


ATOM
525
CG1
ILE
A
110
15.138
−14.452
10.339
1.00
23.91
A


ATOM
526
CD1
ILE
A
110
16.621
−14.185
10.475
1.00
27.88
A


ATOM
527
C
ILE
A
110
12.407
−16.390
12.249
1.00
30.57
A


ATOM
528
O
ILE
A
110
12.054
−17.485
11.836
1.00
33.38
A


ATOM
529
N
GLU
A
111
12.237
−16.044
13.523
1.00
31.37
A


ATOM
530
CA
GLU
A
111
11.668
−17.002
14.455
1.00
34.74
A


ATOM
531
CB
GLU
A
111
11.743
−16.487
15.901
1.00
37.88
A


ATOM
532
CG
GLU
A
111
13.163
−16.199
16.388
1.00
39.88
A


ATOM
533
CD
GLU
A
111
14.150
−17.350
16.125
1.00
43.16
A


ATOM
534
OE1
GLU
A
111
13.790
−18.508
16.449
1.00
41.26
A


ATOM
535
OE2
GLU
A
111
15.284
−17.085
15.613
1.00
41.95
A


ATOM
536
C
GLU
A
111
10.228
−17.362
14.112
1.00
37.26
A


ATOM
537
O
GLU
A
111
9.449
−16.527
13.619
1.00
37.51
A


ATOM
538
N
GLU
A
112
9.878
−18.619
14.365
1.00
37.51
A


ATOM
539
CA
GLU
A
112
8.538
−19.096
14.087
1.00
39.20
A


ATOM
540
CB
GLU
A
112
8.423
−20.618
14.343
1.00
44.94
A


ATOM
541
CG
GLU
A
112
7.136
−21.231
13.740
1.00
52.80
A


ATOM
542
CD
GLU
A
112
7.049
−22.757
13.884
1.00
58.10
A


ATOM
543
OE1
GLU
A
112
6.132
−23.369
13.268
1.00
60.88
A


ATOM
544
OE2
GLU
A
112
7.887
−23.340
14.613
1.00
59.93
A


ATOM
545
C
GLU
A
112
7.554
−18.361
14.969
1.00
35.05
A


ATOM
546
O
GLU
A
112
7.761
−18.229
16.154
1.00
35.71
A


ATOM
547
N
GLY
A
113
6.484
−17.865
14.379
1.00
33.74
A


ATOM
548
CA
GLY
A
113
5.497
−17.146
15.168
1.00
33.22
A


ATOM
549
C
GLY
A
113
5.650
−15.632
15.164
1.00
31.00
A


ATOM
550
O
GLY
A
113
4.718
−14.938
15.561
1.00
30.67
A


ATOM
551
N
ALA
A
114
6.789
−15.111
14.706
1.00
27.90
A


ATOM
552
CA
ALA
A
114
6.968
−13.665
14.707
1.00
27.93
A


ATOM
553
CB
ALA
A
114
8.449
−13.315
14.829
1.00
25.37
A


ATOM
554
C
ALA
A
114
6.377
−13.052
13.446
1.00
30.01
A


ATOM
555
O
ALA
A
114
6.295
−13.708
12.389
1.00
29.87
A


ATOM
556
N
ASP
A
115
5.945
−11.799
13.564
1.00
27.80
A


ATOM
557
CA
ASP
A
115
5.363
−11.085
12.453
1.00
27.62
A


ATOM
558
CB
ASP
A
115
4.201
−10.209
12.928
1.00
29.66
A


ATOM
559
CG
ASP
A
115
3.001
−11.017
13.415
1.00
33.45
A


ATOM
560
OD1
ASP
A
115
2.396
−11.728
12.588
1.00
36.10
A


ATOM
561
OD2
ASP
A
115
2.646
−10.952
14.619
1.00
33.25
A


ATOM
562
C
ASP
A
115
6.416
−10.192
11.859
1.00
27.45
A


ATOM
563
O
ASP
A
115
6.392
−9.888
10.675
1.00
27.18
A


ATOM
564
N
LEU
A
116
7.363
−9.769
12.691
1.00
25.66
A


ATOM
565
CA
LEU
A
116
8.381
−8.846
12.236
1.00
22.36
A


ATOM
566
CB
LEU
A
116
7.955
−7.410
12.513
1.00
22.77
A


ATOM
567
CG
LEU
A
116
7.179
−6.525
11.570
1.00
29.91
A


ATOM
568
CD1
LEU
A
116
6.802
−5.250
12.337
1.00
27.25
A


ATOM
569
CD2
LEU
A
116
8.055
−6.208
10.310
1.00
29.47
A


ATOM
570
C
LEU
A
116
9.690
−8.996
12.949
1.00
21.54
A


ATOM
571
O
LEU
A
116
9.723
−9.166
14.173
1.00
21.94
A


ATOM
572
N
GLY
A
117
10.758
−8.855
12.187
1.00
18.26
A


ATOM
573
CA
GLY
A
117
12.082
−8.884
12.761
1.00
18.36
A


ATOM
574
C
GLY
A
117
12.443
−7.426
12.993
1.00
20.69
A


ATOM
575
O
GLY
A
117
12.034
−6.524
12.212
1.00
17.83
A


ATOM
576
N
ILE
A
118
13.183
−7.172
14.071
1.00
19.56
A


ATOM
577
CA
ILE
A
118
13.582
−5.814
14.401
1.00
19.75
A


ATOM
578
CB
ILE
A
118
12.449
−5.115
15.235
1.00
17.66
A


ATOM
579
CG2
ILE
A
118
12.214
−5.843
16.528
1.00
11.10
A


ATOM
580
CG1
ILE
A
118
12.780
−3.626
15.482
1.00
16.73
A


ATOM
581
CD1
ILE
A
118
11.554
−2.826
15.983
1.00
11.45
A


ATOM
582
C
ILE
A
118
14.950
−5.699
15.082
1.00
20.89
A


ATOM
583
O
ILE
A
118
15.336
−6.523
15.911
1.00
22.69
A


ATOM
584
N
VAL
A
119
15.726
−4.725
14.648
1.00
17.68
A


ATOM
585
CA
VAL
A
119
17.023
−4.479
15.245
1.00
17.73
A


ATOM
586
CB
VAL
A
119
18.156
−4.707
14.245
1.00
18.48
A


ATOM
587
CG1
VAL
A
119
19.470
−4.088
14.786
1.00
16.26
A


ATOM
588
CG2
VAL
A
119
18.360
−6.248
14.024
1.00
17.37
A


ATOM
589
C
VAL
A
119
16.995
−3.007
15.703
1.00
19.67
A


ATOM
590
O
VAL
A
119
16.685
−2.109
14.897
1.00
22.22
A


ATOM
591
N
PHE
A
120
17.264
−2.783
16.990
1.00
17.05
A


ATOM
592
CA
PHE
A
120
17.268
−1.451
17.601
1.00
17.35
A


ATOM
593
CB
PHE
A
120
16.913
−1.575
19.071
1.00
14.79
A


ATOM
594
CG
PHE
A
120
15.575
−2.162
19.296
1.00
14.74
A


ATOM
595
CD1
PHE
A
120
15.446
−3.471
19.743
1.00
18.44
A


ATOM
596
CD2
PHE
A
120
14.431
−1.455
18.942
1.00
11.88
A


ATOM
597
CE1
PHE
A
120
14.205
−4.072
19.822
1.00
17.97
A


ATOM
598
CE2
PHE
A
120
13.184
−2.036
19.024
1.00
8.38
A


ATOM
599
CZ
PHE
A
120
13.065
−3.346
19.461
1.00
16.46
A


ATOM
600
C
PHE
A
120
18.587
−0.704
17.489
1.00
16.31
A


ATOM
601
O
PHE
A
120
19.643
−1.307
17.485
1.00
17.15
A


ATOM
602
N
MET
A
121
18.533
0.607
17.406
1.00
13.89
A


ATOM
603
CA
MET
A
121
19.784
1.373
17.332
1.00
15.68
A


ATOM
604
CB
MET
A
121
20.173
1.653
15.868
1.00
16.03
A


ATOM
605
CG
MET
A
121
19.064
2.347
15.026
1.00
14.51
A


ATOM
606
SD
MET
A
121
19.630
2.803
13.354
1.00
18.48
A


ATOM
607
CE
MET
A
121
17.989
2.729
12.387
1.00
14.43
A


ATOM
608
C
MET
A
121
19.628
2.699
18.085
1.00
15.20
A


ATOM
609
O
MET
A
121
18.511
3.156
18.271
1.00
15.74
A


ATOM
610
N
ASP
A
122
20.738
3.311
18.511
1.00
16.13
A


ATOM
611
CA
ASP
A
122
20.695
4.596
19.228
1.00
15.51
A


ATOM
612
CB
ASP
A
122
20.602
4.380
20.743
1.00
16.13
A


ATOM
613
CG
ASP
A
122
21.662
3.387
21.252
1.00
17.19
A


ATOM
614
OD1
ASP
A
122
21.302
2.301
21.738
1.00
17.17
A


ATOM
615
OD2
ASP
A
122
22.859
3.668
21.110
1.00
18.95
A


ATOM
616
C
ASP
A
122
21.940
5.393
18.875
1.00
16.30
A


ATOM
617
O
ASP
A
122
22.659
5.021
17.927
1.00
16.43
A


ATOM
618
N
THR
A
123
22.232
6.476
19.606
1.00
14.64
A


ATOM
619
CA
THR
A
123
23.405
7.296
19.248
1.00
16.34
A


ATOM
620
CB
THR
A
123
23.377
8.666
19.948
1.00
20.16
A


ATOM
621
OG1
THR
A
123
23.433
8.452
21.359
1.00
20.03
A


ATOM
622
CG2
THR
A
123
22.050
9.420
19.651
1.00
15.91
A


ATOM
623
C
THR
A
123
24.765
6.654
19.543
1.00
18.44
A


ATOM
624
O
THR
A
123
25.788
7.105
19.045
1.00
17.71
A


ATOM
625
N
GLY
A
124
24.783
5.575
20.314
1.00
19.83
A


ATOM
626
CA
GLY
A
124
26.067
4.937
20.620
1.00
19.03
A


ATOM
627
C
GLY
A
124
26.151
3.518
20.111
1.00
20.74
A


ATOM
628
O
GLY
A
124
27.210
3.095
19.684
1.00
23.11
A


ATOM
629
N
GLY
A
125
25.044
2.779
20.111
1.00
21.72
A


ATOM
630
CA
GLY
A
125
25.112
1.398
19.639
1.00
20.92
A


ATOM
631
C
GLY
A
125
23.774
0.755
19.288
1.00
21.20
A


ATOM
632
O
GLY
A
125
22.910
1.390
18.701
1.00
15.13
A


ATOM
633
N
TYR
A
126
23.627
−0.520
19.659
1.00
20.42
A


ATOM
634
CA
TYR
A
126
22.434
−1.309
19.376
1.00
18.95
A


ATOM
635
CB
TYR
A
126
22.769
−2.346
18.304
1.00
18.10
A


ATOM
636
CG
TYR
A
126
23.407
−1.769
17.039
1.00
21.30
A


ATOM
637
CD1
TYR
A
126
24.746
−1.391
17.022
1.00
20.88
A


ATOM
638
CE1
TYR
A
126
25.335
−0.852
15.891
1.00
20.12
A


ATOM
639
CD2
TYR
A
126
22.658
−1.582
15.866
1.00
19.45
A


ATOM
640
CE2
TYR
A
126
23.255
−1.023
14.718
1.00
19.36
A


ATOM
641
CZ
TYR
A
126
24.591
−0.670
14.752
1.00
19.84
A


ATOM
642
OH
TYR
A
126
25.200
−0.139
13.643
1.00
22.55
A


ATOM
643
C
TYR
A
126
21.962
−2.039
20.636
1.00
20.67
A


ATOM
644
O
TYR
A
126
22.664
−2.923
21.122
1.00
21.83
A


ATOM
645
N
LEU
A
127
20.817
−1.668
21.199
1.00
18.90
A


ATOM
646
CA
LEU
A
127
20.333
−2.396
22.378
1.00
19.94
A


ATOM
647
CB
LEU
A
127
19.293
−1.565
23.136
1.00
16.69
A


ATOM
648
CG
LEU
A
127
19.833
−0.296
23.778
1.00
15.15
A


ATOM
649
CD1
LEU
A
127
18.687
0.434
24.454
1.00
15.62
A


ATOM
650
CD2
LEU
A
127
20.917
−0.693
24.813
1.00
14.77
A


ATOM
651
C
LEU
A
127
19.679
−3.714
21.922
1.00
22.15
A


ATOM
652
O
LEU
A
127
19.087
−3.789
20.807
1.00
19.94
A


ATOM
653
N
ASN
A
128
19.729
−4.731
22.784
1.00
19.78
A


ATOM
654
CA
ASN
A
128
19.146
−6.008
22.442
1.00
17.69
A


ATOM
655
CB
ASN
A
128
19.718
−7.129
23.329
1.00
17.30
A


ATOM
656
CG
ASN
A
128
21.132
−7.510
22.910
1.00
20.21
A


ATOM
657
OD1
ASN
A
128
21.321
−8.172
21.911
1.00
21.69
A


ATOM
658
ND2
ASN
A
128
22.130
−7.046
23.653
1.00
20.77
A


ATOM
659
C
ASN
A
128
17.652
−5.951
22.489
1.00
16.66
A


ATOM
660
O
ASN
A
128
16.979
−6.726
21.820
1.00
16.07
A


ATOM
661
N
MET
A
129
17.105
−5.049
23.286
1.00
17.43
A


ATOM
662
CA
MET
A
129
15.644
−4.891
23.293
1.00
17.78
A


ATOM
663
CB
MET
A
129
14.945
−5.836
24.304
1.00
18.80
A


ATOM
664
CG
MET
A
129
13.855
−6.743
23.656
1.00
17.74
A


ATOM
665
SD
MET
A
129
12.478
−5.794
22.876
1.00
19.04
A


ATOM
666
CE
MET
A
129
11.555
−5.342
24.274
1.00
13.77
A


ATOM
667
C
MET
A
129
15.329
−3.450
23.649
1.00
17.45
A


ATOM
668
O
MET
A
129
16.169
−2.749
24.196
1.00
17.29
A


ATOM
669
N
CYS
A
130
14.118
−3.004
23.339
1.00
15.99
A


ATOM
670
CA
CYS
A
130
13.711
−1.636
23.660
1.00
15.23
A


ATOM
671
CB
CYS
A
130
14.154
−0.643
22.570
1.00
15.57
A


ATOM
672
SG
CYS
A
130
13.513
1.020
22.846
1.00
19.18
A


ATOM
673
C
CYS
A
130
12.227
−1.675
23.760
1.00
16.14
A


ATOM
674
O
CYS
A
130
11.503
−2.026
22.790
1.00
15.93
A


ATOM
675
N
GLY
A
131
11.750
−1.357
24.951
1.00
14.58
A


ATOM
676
CA
GLY
A
131
10.337
−1.379
25.170
1.00
12.01
A


ATOM
677
C
GLY
A
131
9.573
−0.282
24.444
1.00
14.99
A


ATOM
678
O
GLY
A
131
8.529
−0.572
23.833
1.00
13.87
A


ATOM
679
N
HIS
A
132
10.047
0.968
24.507
1.00
14.36
A


ATOM
680
CA
HIS
A
132
9.278
2.065
23.885
1.00
13.54
A


ATOM
681
CB
HIS
A
132
9.854
3.463
24.279
1.00
11.91
A


ATOM
682
CG
HIS
A
132
10.898
3.974
23.343
1.00
13.25
A


ATOM
683
CD2
HIS
A
132
10.783
4.677
22.190
1.00
13.24
A


ATOM
684
ND1
HIS
A
132
12.237
3.688
23.486
1.00
9.99
A


ATOM
685
CE1
HIS
A
132
12.898
4.175
22.455
1.00
11.19
A


ATOM
686
NE2
HIS
A
132
12.037
4.776
21.649
1.00
11.37
A


ATOM
687
C
HIS
A
132
9.222
1.914
22.365
1.00
13.22
A


ATOM
688
O
HIS
A
132
8.201
2.253
21.763
1.00
17.33
A


ATOM
689
N
ASN
A
133
10.285
1.399
21.755
1.00
12.92
A


ATOM
690
CA
ASN
A
133
10.317
1.208
20.309
1.00
14.55
A


ATOM
691
CB
ASN
A
133
11.730
1.128
19.793
1.00
15.34
A


ATOM
692
CG
ASN
A
133
11.835
1.479
18.305
1.00
16.38
A


ATOM
693
OD1
ASN
A
133
10.980
1.085
17.438
1.00
20.05
A


ATOM
694
ND2
ASN
A
133
12.879
2.178
17.983
1.00
6.24
A


ATOM
695
C
ASN
A
133
9.560
−0.061
19.895
1.00
18.07
A


ATOM
696
O
ASN
A
133
9.135
−0.173
18.735
1.00
18.98
A


ATOM
697
N
SER
A
134
9.374
−1.011
20.828
1.00
16.69
A


ATOM
698
CA
SER
A
134
8.596
−2.218
20.504
1.00
15.31
A


ATOM
699
CB
SER
A
134
8.807
−3.360
21.507
1.00
10.54
A


ATOM
700
OG
SER
A
134
10.111
−3.909
21.364
1.00
13.79
A


ATOM
701
C
SER
A
134
7.141
−1.785
20.533
1.00
14.52
A


ATOM
702
O
SER
A
134
6.336
−2.230
19.703
1.00
14.42
A


ATOM
703
N
ILE
A
135
6.801
−0.942
21.502
1.00
11.79
A


ATOM
704
CA
ILE
A
135
5.441
−0.420
21.596
1.00
13.50
A


ATOM
705
CB
ILE
A
135
5.332
0.467
22.852
1.00
14.04
A


ATOM
706
CG2
ILE
A
135
4.193
1.501
22.747
1.00
9.42
A


ATOM
707
CG1
ILE
A
135
5.117
−0.450
24.088
1.00
18.53
A


ATOM
708
CD1
ILE
A
135
5.311
0.285
25.427
1.00
17.58
A


ATOM
709
C
ILE
A
135
5.134
0.396
20.301
1.00
14.43
A


ATOM
710
O
ILE
A
135
4.027
0.327
19.742
1.00
15.61
A


ATOM
711
N
ALA
A
136
6.109
1.168
19.826
1.00
13.39
A


ATOM
712
CA
ALA
A
136
5.900
1.957
18.597
1.00
15.96
A


ATOM
713
CB
ALA
A
136
7.045
2.923
18.385
1.00
13.90
A


ATOM
714
C
ALA
A
136
5.766
1.043
17.349
1.00
14.98
A


ATOM
715
O
ALA
A
136
4.943
1.316
16.498
1.00
17.14
A


ATOM
716
N
ALA
A
137
6.606
0.009
17.241
1.00
14.19
A


ATOM
717
CA
ALA
A
137
6.588
−0.926
16.113
1.00
16.25
A


ATOM
718
CB
ALA
A
137
7.739
−1.897
16.211
1.00
12.23
A


ATOM
719
C
ALA
A
137
5.260
−1.692
16.044
1.00
18.92
A


ATOM
720
O
ALA
A
137
4.711
−1.912
14.945
1.00
17.99
A


ATOM
721
N
VAL
A
138
4.735
−2.065
17.213
1.00
18.01
A


ATOM
722
CA
VAL
A
138
3.464
−2.764
17.324
1.00
18.72
A


ATOM
723
CB
VAL
A
138
3.167
−3.135
18.802
1.00
20.11
A


ATOM
724
CG1
VAL
A
138
1.730
−3.592
18.960
1.00
16.49
A


ATOM
725
CG2
VAL
A
138
4.106
−4.290
19.253
1.00
17.41
A


ATOM
726
C
VAL
A
138
2.346
−1.862
16.806
1.00
22.43
A


ATOM
727
O
VAL
A
138
1.467
−2.298
16.033
1.00
21.66
A


ATOM
728
N
THR
A
139
2.370
−0.608
17.269
1.00
19.76
A


ATOM
729
CA
THR
A
139
1.416
0.394
16.874
1.00
17.43
A


ATOM
730
CB
THR
A
139
1.679
1.716
17.613
1.00
17.77
A


ATOM
731
OG1
THR
A
139
1.590
1.501
19.035
1.00
19.95
A


ATOM
732
CG2
THR
A
139
0.622
2.763
17.217
1.00
15.20
A


ATOM
733
C
THR
A
139
1.485
0.649
15.340
1.00
19.71
A


ATOM
734
O
THR
A
139
0.451
0.656
14.676
1.00
17.61
A


ATOM
735
N
ALA
A
140
2.688
0.843
14.807
1.00
16.15
A


ATOM
736
CA
ALA
A
140
2.886
1.115
13.394
1.00
21.42
A


ATOM
737
CB
ALA
A
140
4.344
1.509
13.124
1.00
16.14
A


ATOM
738
C
ALA
A
140
2.488
−0.091
12.509
1.00
24.04
A


ATOM
739
O
ALA
A
140
1.934
0.102
11.430
1.00
23.58
A


ATOM
740
N
ALA
A
141
2.791
−1.315
12.956
1.00
24.46
A


ATOM
741
CA
ALA
A
141
2.435
−2.510
12.198
1.00
26.30
A


ATOM
742
CB
ALA
A
141
2.874
−3.762
12.948
1.00
22.70
A


ATOM
743
C
ALA
A
141
0.907
−2.517
11.954
1.00
28.47
A


ATOM
744
O
ALA
A
141
0.455
−2.817
10.864
1.00
30.58
A


ATOM
745
N
VAL
A
142
0.113
−2.147
12.951
1.00
28.68
A


ATOM
746
CA
VAL
A
142
−1.334
−2.102
12.792
1.00
27.80
A


ATOM
747
CB
VAL
A
142
−1.992
−2.213
14.162
1.00
28.54
A


ATOM
748
CG1
VAL
A
142
−3.496
−2.054
14.046
1.00
28.64
A


ATOM
749
CG2
VAL
A
142
−1.676
−3.598
14.741
1.00
27.60
A


ATOM
750
C
VAL
A
142
−1.844
−0.862
12.031
1.00
29.31
A


ATOM
751
O
VAL
A
142
−2.619
−0.984
11.068
1.00
27.43
A


ATOM
752
N
GLU
A
143
−1.380
0.322
12.422
1.00
26.70
A


ATOM
753
CA
GLU
A
143
−1.783
1.575
11.763
1.00
29.66
A


ATOM
754
CB
GLU
A
143
−1.119
2.802
12.419
1.00
30.43
A


ATOM
755
CG
GLU
A
143
−1.421
2.958
13.895
1.00
33.87
A


ATOM
756
CD
GLU
A
143
−2.592
3.867
14.168
1.00
38.51
A


ATOM
757
OE1
GLU
A
143
−3.334
4.181
13.200
1.00
40.06
A


ATOM
758
OE2
GLU
A
143
−2.782
4.256
15.354
1.00
39.48
A


ATOM
759
C
GLU
A
143
−1.432
1.613
10.279
1.00
29.62
A


ATOM
760
O
GLU
A
143
−2.192
2.155
9.490
1.00
30.72
A


ATOM
761
N
THR
A
144
−0.282
1.068
9.889
1.00
29.09
A


ATOM
762
CA
THR
A
144
0.077
1.112
8.488
1.00
30.43
A


ATOM
763
CB
THR
A
144
1.570
1.450
8.257
1.00
30.25
A


ATOM
764
OG1
THR
A
144
2.395
0.361
8.704
1.00
32.60
A


ATOM
765
CG2
THR
A
144
1.935
2.762
8.951
1.00
28.09
A


ATOM
766
C
THR
A
144
−0.229
−0.179
7.741
1.00
32.73
A


ATOM
767
O
THR
A
144
0.151
−0.328
6.584
1.00
33.67
A


ATOM
768
N
GLY
A
145
−0.872
−1.131
8.405
1.00
33.93
A


ATOM
769
CA
GLY
A
145
−1.244
−2.361
7.722
1.00
35.69
A


ATOM
770
C
GLY
A
145
−0.244
−3.469
7.486
1.00
37.01
A


ATOM
771
O
GLY
A
145
−0.490
−4.326
6.641
1.00
36.31
A


ATOM
772
N
ILE
A
146
0.874
−3.478
8.210
1.00
37.48
A


ATOM
773
CA
ILE
A
146
1.858
−4.541
8.047
1.00
36.37
A


ATOM
774
CB
ILE
A
146
3.141
−4.218
8.819
1.00
36.57
A


ATOM
775
CG2
ILE
A
146
4.073
−5.423
8.822
1.00
34.02
A


ATOM
776
CG1
ILE
A
146
3.829
−3.014
8.180
1.00
34.32
A


ATOM
777
CD1
ILE
A
146
5.092
−2.620
8.908
1.00
32.45
A


ATOM
778
C
ILE
A
146
1.238
−5.825
8.598
1.00
37.65
A


ATOM
779
O
ILE
A
146
1.548
−6.929
8.165
1.00
40.20
A


ATOM
780
N
VAL
A
147
0.348
−5.675
9.558
1.00
38.72
A


ATOM
781
CA
VAL
A
147
−0.330
−6.813
10.154
1.00
40.62
A


ATOM
782
CB
VAL
A
147
0.044
−6.955
11.675
1.00
40.04
A


ATOM
783
CG1
VAL
A
147
−0.821
−8.017
12.352
1.00
39.93
A


ATOM
784
CG2
VAL
A
147
1.520
−7.330
11.815
1.00
38.17
A


ATOM
785
C
VAL
A
147
−1.817
−6.516
9.974
1.00
43.05
A


ATOM
786
O
VAL
A
147
−2.254
−5.374
10.166
1.00
44.56
A


ATOM
787
N
SER
A
148
−2.599
−7.524
9.592
1.00
44.20
A


ATOM
788
CA
SER
A
148
−4.028
−7.310
9.394
1.00
44.71
A


ATOM
789
CB
SER
A
148
−4.600
−8.334
8.427
1.00
46.12
A


ATOM
790
OG
SER
A
148
−4.180
−8.030
7.118
1.00
48.86
A


ATOM
791
C
SER
A
148
−4.834
−7.351
10.649
1.00
44.87
A


ATOM
792
O
SER
A
148
−4.465
−8.000
11.620
1.00
45.30
A


ATOM
793
N
VAL
A
149
−5.960
−6.654
10.604
1.00
46.41
A


ATOM
794
CA
VAL
A
149
−6.884
−6.582
11.716
1.00
48.20
A


ATOM
795
CB
VAL
A
149
−7.392
−5.142
11.916
1.00
46.71
A


ATOM
796
CG1
VAL
A
149
−8.323
−5.094
13.101
1.00
45.64
A


ATOM
797
CG2
VAL
A
149
−6.219
−4.170
12.084
1.00
48.16
A


ATOM
798
C
VAL
A
149
−8.111
−7.454
11.425
1.00
51.06
A


ATOM
799
O
VAL
A
149
−8.984
−7.055
10.659
1.00
53.06
A


ATOM
800
N
PRO
A
150
−8.190
−8.662
12.002
1.00
52.69
A


ATOM
801
CD
PRO
A
150
−7.169
−9.483
12.671
1.00
52.70
A


ATOM
802
CA
PRO
A
150
−9.395
−9.451
11.702
1.00
53.09
A


ATOM
803
CB
PRO
A
150
−9.232
−10.702
12.568
1.00
52.52
A


ATOM
804
CG
PRO
A
150
−8.020
−10.402
13.485
1.00
52.87
A


ATOM
805
C
PRO
A
150
−10.679
−8.670
12.024
1.00
54.69
A


ATOM
806
O
PRO
A
150
−10.787
−8.024
13.072
1.00
54.58
A


ATOM
807
N
ALA
A
151
−11.651
−8.714
11.113
1.00
54.81
A


ATOM
808
CA
ALA
A
151
−12.891
−7.982
11.320
1.00
54.05
A


ATOM
809
CB
ALA
A
151
−13.943
−8.422
10.308
1.00
56.26
A


ATOM
810
C
ALA
A
151
−13.407
−8.179
12.736
1.00
53.12
A


ATOM
811
O
ALA
A
151
−13.345
−9.279
13.296
1.00
51.58
A


ATOM
812
N
ALA
A
152
−13.893
−7.092
13.320
1.00
52.38
A


ATOM
813
CA
ALA
A
152
−14.425
−7.138
14.669
1.00
51.75
A


ATOM
814
CB
ALA
A
152
−15.429
−8.307
14.786
1.00
52.36
A


ATOM
815
C
ALA
A
152
−13.355
−7.247
15.776
1.00
50.34
A


ATOM
816
O
ALA
A
152
−13.688
−7.210
16.956
1.00
50.43
A


ATOM
817
N
ALA
A
153
−12.083
−7.391
15.421
1.00
48.11
A


ATOM
818
CA
ALA
A
153
−11.061
−7.498
16.462
1.00
47.03
A


ATOM
819
CB
ALA
A
153
−9.689
−7.708
15.843
1.00
46.77
A


ATOM
820
C
ALA
A
153
−11.034
−6.271
17.365
1.00
44.94
A


ATOM
821
O
ALA
A
153
−11.250
−5.155
16.917
1.00
45.60
A


ATOM
822
N
THR
A
154
−10.797
−6.505
18.648
1.00
43.39
A


ATOM
823
CA
THR
A
154
−10.688
−5.436
19.630
1.00
42.09
A


ATOM
824
CB
THR
A
154
−11.337
−5.800
20.955
1.00
41.60
A


ATOM
825
OG1
THR
A
154
−12.755
−5.799
20.810
1.00
46.14
A


ATOM
826
CG2
THR
A
154
−10.968
−4.782
21.999
1.00
44.67
A


ATOM
827
C
THR
A
154
−9.200
−5.256
19.924
1.00
39.95
A


ATOM
828
O
THR
A
154
−8.762
−4.189
20.329
1.00
39.27
A


ATOM
829
N
ASN
A
155
−8.449
−6.334
19.737
1.00
37.44
A


ATOM
830
CA
ASN
A
155
−7.013
−6.353
19.985
1.00
36.59
A


ATOM
831
CB
ASN
A
155
−6.708
−7.011
21.339
1.00
34.65
A


ATOM
832
CG
ASN
A
155
−7.267
−6.209
22.498
1.00
35.35
A


ATOM
833
OD1
ASN
A
155
−6.763
−5.151
22.832
1.00
36.67
A


ATOM
834
ND2
ASN
A
155
−8.337
−6.695
23.097
1.00
37.88
A


ATOM
835
C
ASN
A
155
−6.368
−7.124
18.862
1.00
35.69
A


ATOM
836
O
ASN
A
155
−6.966
−8.064
18.319
1.00
37.33
A


ATOM
837
N
VAL
A
156
−5.157
−6.714
18.501
1.00
32.21
A


ATOM
838
CA
VAL
A
156
−4.420
−7.355
17.440
1.00
29.99
A


ATOM
839
CB
VAL
A
156
−4.283
−6.436
16.195
1.00
27.92
A


ATOM
840
CG1
VAL
A
156
−3.633
−7.209
15.063
1.00
24.91
A


ATOM
841
CG2
VAL
A
156
−5.650
−5.859
15.808
1.00
30.14
A


ATOM
842
C
VAL
A
156
−3.012
−7.718
17.893
1.00
29.61
A


ATOM
843
O
VAL
A
156
−2.247
−6.858
18.296
1.00
29.57
A


ATOM
844
N
PRO
A
157
−2.647
−9.000
17.794
1.00
30.55
A


ATOM
845
CD
PRO
A
157
−3.471
−10.155
17.370
1.00
30.65
A


ATOM
846
CA
PRO
A
157
−1.305
−9.415
18.206
1.00
30.07
A


ATOM
847
CB
PRO
A
157
−1.400
−10.954
18.335
1.00
31.51
A


ATOM
848
CG
PRO
A
157
−2.882
−11.276
18.184
1.00
32.25
A


ATOM
849
C
PRO
A
157
−0.260
−9.031
17.171
1.00
28.74
A


ATOM
850
O
PRO
A
157
−0.529
−9.037
15.980
1.00
26.95
A


ATOM
851
N
VAL
A
158
0.932
−8.665
17.641
1.00
25.33
A


ATOM
852
CA
VAL
A
158
2.032
−8.355
16.755
1.00
22.06
A


ATOM
853
CB
VAL
A
158
2.262
−6.855
16.575
1.00
21.96
A


ATOM
854
CG1
VAL
A
158
3.452
−6.653
15.680
1.00
18.31
A


ATOM
855
CG2
VAL
A
158
1.022
−6.171
16.035
1.00
20.19
A


ATOM
856
C
VAL
A
158
3.231
−8.905
17.508
1.00
22.69
A


ATOM
857
O
VAL
A
158
3.607
−8.372
18.559
1.00
23.00
A


ATOM
858
N
VAL
A
159
3.839
−9.948
16.964
1.00
20.54
A


ATOM
859
CA
VAL
A
159
4.986
−10.597
17.576
1.00
20.03
A


ATOM
860
CB
VAL
A
159
4.888
−12.152
17.414
1.00
19.22
A


ATOM
861
CG1
VAL
A
159
6.049
−12.818
18.063
1.00
20.27
A


ATOM
862
CG2
VAL
A
159
3.612
−12.655
18.026
1.00
19.26
A


ATOM
863
C
VAL
A
159
6.287
−10.126
16.978
1.00
20.72
A


ATOM
864
O
VAL
A
159
6.496
−10.302
15.778
1.00
21.19
A


ATOM
865
N
LEU
A
160
7.170
−9.533
17.803
1.00
19.86
A


ATOM
866
CA
LEU
A
160
8.464
−9.068
17.317
1.00
20.29
A


ATOM
867
CB
LEU
A
160
8.854
−7.715
17.953
1.00
19.30
A


ATOM
868
CG
LEU
A
160
7.801
−6.591
17.875
1.00
23.35
A


ATOM
869
CD1
LEU
A
160
8.272
−5.346
18.677
1.00
20.63
A


ATOM
870
CD2
LEU
A
160
7.580
−6.233
16.397
1.00
22.61
A


ATOM
871
C
LEU
A
160
9.594
−10.066
17.590
1.00
20.87
A


ATOM
872
O
LEU
A
160
9.718
−10.608
18.700
1.00
20.58
A


ATOM
873
N
ASP
A
161
10.429
−10.271
16.578
1.00
19.18
A


ATOM
874
CA
ASP
A
161
11.572
−11.151
16.671
1.00
21.03
A


ATOM
875
CB
ASP
A
161
11.640
−11.943
15.360
1.00
23.60
A


ATOM
876
CG
ASP
A
161
12.920
−12.741
15.186
1.00
28.50
A


ATOM
877
OD1
ASP
A
161
13.724
−12.894
16.154
1.00
29.03
A


ATOM
878
OD2
ASP
A
161
13.114
−13.224
14.032
1.00
28.50
A


ATOM
879
C
ASP
A
161
12.756
−10.193
16.874
1.00
21.02
A


ATOM
880
O
ASP
A
161
13.194
−9.514
15.931
1.00
20.75
A


ATOM
881
N
THR
A
162
13.256
−10.126
18.112
1.00
19.55
A


ATOM
882
CA
THR
A
162
14.349
−9.216
18.457
1.00
20.55
A


ATOM
883
CB
THR
A
162
13.913
−8.280
19.605
1.00
20.90
A


ATOM
884
OG1
THR
A
162
14.100
−8.937
20.868
1.00
19.94
A


ATOM
885
CG2
THR
A
162
12.450
−7.937
19.468
1.00
19.99
A


ATOM
886
C
THR
A
162
15.655
−9.910
18.895
1.00
20.99
A


ATOM
887
O
THR
A
162
15.673
−11.097
19.160
1.00
20.21
A


ATOM
888
N
PRO
A
163
16.761
−9.151
18.991
1.00
20.13
A


ATOM
889
CD
PRO
A
163
16.955
−7.743
18.578
1.00
18.75
A


ATOM
890
CA
PRO
A
163
18.020
−9.776
19.399
1.00
18.56
A


ATOM
891
CB
PRO
A
163
19.037
−8.635
19.323
1.00
19.07
A


ATOM
892
CG
PRO
A
163
18.461
−7.736
18.220
1.00
22.15
A


ATOM
893
C
PRO
A
163
17.973
−10.395
20.785
1.00
21.23
A


ATOM
894
O
PRO
A
163
18.817
−11.196
21.127
1.00
20.60
A


ATOM
895
N
ALA
A
164
16.993
−10.023
21.586
1.00
20.11
A


ATOM
896
CA
ALA
A
164
16.911
−10.595
22.912
1.00
23.47
A


ATOM
897
CB
ALA
A
164
16.550
−9.521
23.930
1.00
21.10
A


ATOM
898
C
ALA
A
164
15.877
−11.701
22.971
1.00
22.65
A


ATOM
899
O
ALA
A
164
15.717
−12.322
24.010
1.00
20.35
A


ATOM
900
N
GLY
A
165
15.157
−11.941
21.879
1.00
21.35
A


ATOM
901
CA
GLY
A
165
14.147
−12.994
21.932
1.00
20.84
A


ATOM
902
C
GLY
A
165
12.812
−12.455
21.479
1.00
21.92
A


ATOM
903
O
GLY
A
165
12.700
−11.277
21.111
1.00
20.27
A


ATOM
904
N
LEU
A
166
11.793
−13.299
21.526
1.00
23.31
A


ATOM
905
CA
LEU
A
166
10.457
−12.940
21.065
1.00
23.22
A


ATOM
906
CB
LEU
A
166
9.625
−14.202
20.802
1.00
26.06
A


ATOM
907
CG
LEU
A
166
9.589
−14.876
19.428
1.00
31.69
A


ATOM
908
CD1
LEU
A
166
10.644
−14.308
18.484
1.00
30.71
A


ATOM
909
CD2
LEU
A
166
9.797
−16.382
19.632
1.00
31.54
A


ATOM
910
C
LEU
A
166
9.701
−12.077
22.027
1.00
22.07
A


ATOM
911
O
LEU
A
166
9.557
−12.401
23.204
1.00
21.62
A


ATOM
912
N
VAL
A
167
9.145
−10.993
21.499
1.00
20.99
A


ATOM
913
CA
VAL
A
167
8.376
−10.064
22.301
1.00
18.35
A


ATOM
914
CB
VAL
A
167
8.997
−8.658
22.219
1.00
16.52
A


ATOM
915
CG1
VAL
A
167
8.103
−7.632
22.936
1.00
11.30
A


ATOM
916
CG2
VAL
A
167
10.373
−8.709
22.839
1.00
13.66
A


ATOM
917
C
VAL
A
167
6.969
−10.066
21.740
1.00
19.92
A


ATOM
918
O
VAL
A
167
6.780
−9.713
20.577
1.00
20.81
A


ATOM
919
N
ARG
A
168
5.999
−10.459
22.566
1.00
19.73
A


ATOM
920
CA
ARG
A
168
4.604
−10.562
22.154
1.00
22.66
A


ATOM
921
CB
ARG
A
168
3.967
−11.769
22.841
1.00
25.09
A


ATOM
922
CG
ARG
A
168
4.749
−13.054
22.497
1.00
31.29
A


ATOM
923
CD
ARG
A
168
4.262
−14.314
23.275
1.00
37.67
A


ATOM
924
NE
ARG
A
168
5.111
−15.466
22.927
1.00
46.49
A


ATOM
925
CZ
ARG
A
168
6.304
−15.737
23.476
1.00
50.99
A


ATOM
926
NH1
ARG
A
168
6.808
−14.955
24.440
1.00
52.72
A


ATOM
927
NH2
ARG
A
168
7.038
−16.748
23.014
1.00
51.17
A


ATOM
928
C
ARG
A
168
3.806
−9.315
22.433
1.00
22.76
A


ATOM
929
O
ARG
A
168
3.425
−9.030
23.575
1.00
21.01
A


ATOM
930
N
GLY
A
169
3.525
−8.574
21.369
1.00
22.38
A


ATOM
931
CA
GLY
A
169
2.798
−7.347
21.547
1.00
22.35
A


ATOM
932
C
GLY
A
169
1.357
−7.463
21.195
1.00
23.33
A


ATOM
933
O
GLY
A
169
0.940
−8.401
20.515
1.00
26.69
A


ATOM
934
N
THR
A
170
0.607
−6.483
21.664
1.00
21.16
A


ATOM
935
CA
THR
A
170
−0.809
−6.401
21.438
1.00
22.01
A


ATOM
936
CB
THR
A
170
−1.578
−6.933
22.658
1.00
25.05
A


ATOM
937
OG1
THR
A
170
−1.192
−8.289
22.920
1.00
23.90
A


ATOM
938
CG2
THR
A
170
−3.066
−6.854
22.409
1.00
24.90
A


ATOM
939
C
THR
A
170
−1.219
−4.939
21.209
1.00
21.97
A


ATOM
940
O
THR
A
170
−0.990
−4.069
22.066
1.00
19.17
A


ATOM
941
N
ALA
A
171
−1.818
−4.657
20.055
1.00
19.71
A


ATOM
942
CA
ALA
A
171
−2.270
−3.301
19.798
1.00
19.40
A


ATOM
943
CB
ALA
A
171
−2.161
−2.951
18.302
1.00
18.99
A


ATOM
944
C
ALA
A
171
−3.711
−3.324
20.247
1.00
22.64
A


ATOM
945
O
ALA
A
171
−4.481
−4.181
19.812
1.00
25.12
A


ATOM
946
N
HIS
A
172
−4.072
−2.403
21.124
1.00
22.11
A


ATOM
947
CA
HIS
A
172
−5.433
−2.311
21.646
1.00
26.51
A


ATOM
948
CB
HIS
A
172
−5.392
−1.842
23.100
1.00
26.20
A


ATOM
949
CG
HIS
A
172
−4.564
−2.722
23.976
1.00
28.68
A


ATOM
950
CD2
HIS
A
172
−3.371
−2.513
24.581
1.00
27.13
A


ATOM
951
ND1
HIS
A
172
−4.913
−4.028
24.254
1.00
31.39
A


ATOM
952
CE1
HIS
A
172
−3.968
−4.587
24.989
1.00
31.23
A


ATOM
953
NE2
HIS
A
172
−3.020
−3.688
25.201
1.00
31.70
A


ATOM
954
C
HIS
A
172
−6.109
−1.279
20.762
1.00
28.48
A


ATOM
955
O
HIS
A
172
−5.671
−0.131
20.691
1.00
27.56
A


ATOM
956
N
LEU
A
173
−7.162
−1.691
20.071
1.00
31.72
A


ATOM
957
CA
LEU
A
173
−7.836
−0.800
19.129
1.00
35.72
A


ATOM
958
CB
LEU
A
173
−8.589
−1.621
18.071
1.00
33.82
A


ATOM
959
CG
LEU
A
173
−7.675
−2.540
17.271
1.00
33.81
A


ATOM
960
CD1
LEU
A
173
−8.421
−3.178
16.123
1.00
34.73
A


ATOM
961
CD2
LEU
A
173
−6.513
−1.732
16.744
1.00
33.88
A


ATOM
962
C
LEU
A
173
−8.771
0.231
19.718
1.00
38.58
A


ATOM
963
O
LEU
A
173
−9.358
0.034
20.775
1.00
37.75
A


ATOM
964
N
GLN
A
174
−8.881
1.343
19.006
1.00
42.97
A


ATOM
965
CA
GLN
A
174
−9.759
2.436
19.379
1.00
49.44
A


ATOM
966
CB
GLN
A
174
−9.426
3.662
18.504
1.00
53.22
A


ATOM
967
CG
GLN
A
174
−10.077
4.957
18.944
1.00
57.53
A


ATOM
968
CD
GLN
A
174
−10.144
5.039
20.449
1.00
61.01
A


ATOM
969
OE1
GLN
A
174
−11.148
4.653
21.052
1.00
62.25
A


ATOM
970
NE2
GLN
A
174
−9.057
5.509
21.075
1.00
62.63
A


ATOM
971
C
GLN
A
174
−11.207
1.972
19.123
1.00
51.36
A


ATOM
972
O
GLN
A
174
−11.538
1.544
18.018
1.00
49.38
A


ATOM
973
N
SER
A
175
−12.045
2.051
20.154
1.00
54.64
A


ATOM
974
CA
SER
A
175
−13.454
1.649
20.098
1.00
58.88
A


ATOM
975
CB
SER
A
175
−14.326
2.657
20.839
1.00
58.85
A


ATOM
976
OG
SER
A
175
−14.341
2.355
22.215
1.00
61.88
A


ATOM
977
C
SER
A
175
−14.112
1.385
18.755
1.00
61.01
A


ATOM
978
O
SER
A
175
−14.118
0.253
18.277
1.00
63.42
A


ATOM
979
N
GLY
A
176
−14.683
2.425
18.158
1.00
61.70
A


ATOM
980
CA
GLY
A
176
−15.378
2.240
16.897
1.00
63.37
A


ATOM
981
C
GLY
A
176
−14.584
2.515
15.640
1.00
63.98
A


ATOM
982
O
GLY
A
176
−15.079
3.178
14.725
1.00
64.88
A


ATOM
983
N
THR
A
177
−13.359
2.010
15.578
1.00
63.31
A


ATOM
984
CA
THR
A
177
−12.530
2.232
14.401
1.00
62.57
A


ATOM
985
CB
THR
A
177
−11.271
3.053
14.744
1.00
63.55
A


ATOM
986
OG1
THR
A
177
−10.353
2.239
15.493
1.00
63.78
A


ATOM
987
CG2
THR
A
177
−11.653
4.283
15.564
1.00
62.43
A


ATOM
988
C
THR
A
177
−12.103
0.890
13.839
1.00
61.58
A


ATOM
989
O
THR
A
177
−12.386
−0.153
14.437
1.00
62.24
A


ATOM
990
N
ALA
A
178
−11.419
0.912
12.697
1.00
59.38
A


ATOM
991
CA
ALA
A
178
−10.969
−0.325
12.074
1.00
57.95
A


ATOM
992
CB
ALA
A
178
−11.149
−0.253
10.568
1.00
58.65
A


ATOM
993
C
ALA
A
178
−9.518
−0.660
12.407
1.00
56.56
A


ATOM
994
O
ALA
A
178
−9.220
−1.797
12.771
1.00
57.02
A


ATOM
995
N
SER
A
179
−8.621
0.317
12.273
1.00
53.10
A


ATOM
996
CA
SER
A
179
−7.206
0.091
12.566
1.00
49.87
A


ATOM
997
CB
SER
A
179
−6.421
−0.115
11.261
1.00
49.16
A


ATOM
998
OG
SER
A
179
−6.350
1.075
10.499
1.00
51.02
A


ATOM
999
C
SER
A
179
−6.548
1.205
13.400
1.00
47.04
A


ATOM
1000
O
SER
A
179
−5.323
1.356
13.378
1.00
46.21
A


ATOM
1001
N
GLU
A
180
−7.365
1.975
14.123
1.00
43.11
A


ATOM
1002
CA
GLU
A
180
−6.881
3.060
14.964
1.00
40.75
A


ATOM
1003
CB
GLU
A
180
−7.978
4.094
15.189
1.00
44.55
A


ATOM
1004
CG
GLU
A
180
−8.371
4.823
13.933
1.00
51.79
A


ATOM
1005
CD
GLU
A
180
−7.989
6.270
13.997
1.00
55.40
A


ATOM
1006
OE1
GLU
A
180
−8.486
6.964
14.919
1.00
59.31
A


ATOM
1007
OE2
GLU
A
180
−7.194
6.712
13.135
1.00
58.50
A


ATOM
1008
C
GLU
A
180
−6.447
2.469
16.308
1.00
37.00
A


ATOM
1009
O
GLU
A
180
−7.248
1.846
17.016
1.00
33.16
A


ATOM
1010
N
VAL
A
181
−5.180
2.692
16.649
1.00
33.23
A


ATOM
1011
CA
VAL
A
181
−4.610
2.136
17.872
1.00
28.76
A


ATOM
1012
CB
VAL
A
181
−3.146
1.739
17.625
1.00
24.78
A


ATOM
1013
CG1
VAL
A
181
−2.476
1.316
18.911
1.00
20.13
A


ATOM
1014
CG2
VAL
A
181
−3.110
0.621
16.584
1.00
22.09
A


ATOM
1015
C
VAL
A
181
−4.708
3.057
19.051
1.00
29.35
A


ATOM
1016
O
VAL
A
181
−4.199
4.174
19.020
1.00
30.49
A


ATOM
1017
N
SER
A
182
−5.385
2.592
20.092
1.00
28.63
A


ATOM
1018
CA
SER
A
182
−5.538
3.377
21.309
1.00
28.46
A


ATOM
1019
CB
SER
A
182
−6.674
2.799
22.142
1.00
28.15
A


ATOM
1020
OG
SER
A
182
−6.662
3.370
23.429
1.00
32.23
A


ATOM
1021
C
SER
A
182
−4.219
3.381
22.104
1.00
26.83
A


ATOM
1022
O
SER
A
182
−3.757
4.435
22.539
1.00
26.77
A


ATOM
1023
N
ASN
A
183
−3.626
2.204
22.300
1.00
24.30
A


ATOM
1024
CA
ASN
A
183
−2.337
2.080
22.984
1.00
22.32
A


ATOM
1025
CB
ASN
A
183
−2.416
2.474
24.478
1.00
25.42
A


ATOM
1026
CG
ASN
A
183
−3.214
1.505
25.347
1.00
27.40
A


ATOM
1027
OD1
ASN
A
183
−3.791
0.537
24.892
1.00
31.49
A


ATOM
1028
ND2
ASN
A
183
−3.230
1.787
26.625
1.00
30.03
A


ATOM
1029
C
ASN
A
183
−1.834
0.663
22.736
1.00
23.53
A


ATOM
1030
O
ASN
A
183
−2.501
−0.080
22.038
1.00
21.08
A


ATOM
1031
N
ALA
A
184
−0.651
0.297
23.235
1.00
19.38
A


ATOM
1032
CA
ALA
A
184
−0.113
−1.016
22.963
1.00
19.22
A


ATOM
1033
CB
ALA
A
184
0.819
−0.942
21.791
1.00
18.34
A


ATOM
1034
C
ALA
A
184
0.616
−1.595
24.162
1.00
20.28
A


ATOM
1035
O
ALA
A
184
1.181
−0.863
24.973
1.00
18.76
A


ATOM
1036
N
SER
A
185
0.587
−2.917
24.259
1.00
20.14
A


ATOM
1037
CA
SER
A
185
1.230
−3.636
25.345
1.00
21.79
A


ATOM
1038
CB
SER
A
185
0.190
−4.446
26.151
1.00
21.49
A


ATOM
1039
OG
SER
A
185
−0.692
−3.607
26.891
1.00
26.71
A


ATOM
1040
C
SER
A
185
2.219
−4.617
24.720
1.00
20.64
A


ATOM
1041
O
SER
A
185
2.022
−5.082
23.579
1.00
20.27
A


ATOM
1042
N
ILE
A
186
3.277
−4.905
25.459
1.00
18.13
A


ATOM
1043
CA
ILE
A
186
4.270
−5.880
25.034
1.00
19.89
A


ATOM
1044
CB
ILE
A
186
5.605
−5.261
24.535
1.00
20.55
A


ATOM
1045
CG2
ILE
A
186
5.367
−4.463
23.208
1.00
22.02
A


ATOM
1046
CG1
ILE
A
186
6.190
−4.330
25.593
1.00
22.80
A


ATOM
1047
CD1
ILE
A
186
7.598
−3.839
25.251
1.00
25.83
A


ATOM
1048
C
ILE
A
186
4.584
−6.733
26.243
1.00
20.18
A


ATOM
1049
O
ILE
A
186
4.688
−6.235
27.368
1.00
19.60
A


ATOM
1050
N
ILE
A
187
4.659
−8.037
26.004
1.00
21.83
A


ATOM
1051
CA
ILE
A
187
5.044
−8.987
27.024
1.00
20.11
A


ATOM
1052
CB
ILE
A
187
4.213
−10.226
26.950
1.00
21.79
A


ATOM
1053
CG2
ILE
A
187
4.813
−11.315
27.905
1.00
22.53
A


ATOM
1054
CG1
ILE
A
187
2.776
−9.834
27.345
1.00
21.71
A


ATOM
1055
CD1
ILE
A
187
1.744
−10.923
27.251
1.00
23.99
A


ATOM
1056
C
ILE
A
187
6.494
−9.202
26.625
1.00
19.69
A


ATOM
1057
O
ILE
A
187
6.827
−9.739
25.545
1.00
16.11
A


ATOM
1058
N
ASN
A
188
7.357
−8.692
27.505
1.00
18.39
A


ATOM
1059
CA
ASN
A
188
8.792
−8.673
27.308
1.00
16.27
A


ATOM
1060
CB
ASN
A
188
9.386
−7.742
28.356
1.00
18.81
A


ATOM
1061
CG
ASN
A
188
10.764
−7.272
28.010
1.00
24.47
A


ATOM
1062
OD1
ASN
A
188
11.297
−7.550
26.923
1.00
23.63
A


ATOM
1063
ND2
ASN
A
188
11.368
−6.531
28.934
1.00
23.67
A


ATOM
1064
C
ASN
A
188
9.387
−10.050
27.444
1.00
17.45
A


ATOM
1065
O
ASN
A
188
8.702
−10.982
27.869
1.00
19.16
A


ATOM
1066
N
VAL
A
189
10.653
−10.182
27.065
1.00
17.74
A


ATOM
1067
CA
VAL
A
189
11.369
−11.439
27.255
1.00
18.04
A


ATOM
1068
CB
VAL
A
189
12.759
−11.456
26.539
1.00
17.23
A


ATOM
1069
CG1
VAL
A
189
12.567
−11.291
25.012
1.00
20.32
A


ATOM
1070
CG2
VAL
A
189
13.680
−10.315
27.076
1.00
16.50
A


ATOM
1071
C
VAL
A
189
11.599
−11.574
28.789
1.00
18.92
A


ATOM
1072
O
VAL
A
189
11.461
−10.622
29.567
1.00
19.14
A


ATOM
1073
N
PRO
A
190
11.944
−12.773
29.241
1.00
19.74
A


ATOM
1074
CD
PRO
A
190
12.043
−14.035
28.478
1.00
16.63
A


ATOM
1075
CA
PRO
A
190
12.172
−12.955
30.689
1.00
18.42
A


ATOM
1076
CB
PRO
A
190
12.708
−14.386
30.787
1.00
18.28
A


ATOM
1077
CG
PRO
A
190
11.911
−15.088
29.574
1.00
20.26
A


ATOM
1078
C
PRO
A
190
13.118
−11.943
31.303
1.00
16.46
A


ATOM
1079
O
PRO
A
190
14.227
−11.728
30.809
1.00
18.54
A


ATOM
1080
N
SER
A
191
12.673
−11.338
32.399
1.00
17.82
A


ATOM
1081
CA
SER
A
191
13.452
−10.349
33.101
1.00
19.02
A


ATOM
1082
CB
SER
A
191
12.559
−9.127
33.391
1.00
23.36
A


ATOM
1083
OG
SER
A
191
12.081
−8.520
32.180
1.00
26.09
A


ATOM
1084
C
SER
A
191
13.888
−10.979
34.428
1.00
20.75
A


ATOM
1085
O
SER
A
191
13.208
−11.858
34.916
1.00
19.49
A


ATOM
1086
N
PHE
A
192
15.007
−10.518
34.998
1.00
19.04
A


ATOM
1087
CA
PHE
A
192
15.477
−11.027
36.284
1.00
21.15
A


ATOM
1088
CB
PHE
A
192
16.103
−12.425
36.115
1.00
15.89
A


ATOM
1089
CG
PHE
A
192
17.110
−12.499
35.022
1.00
16.68
A


ATOM
1090
CD1
PHE
A
192
18.431
−12.177
35.247
1.00
12.61
A


ATOM
1091
CD2
PHE
A
192
16.727
−12.890
33.737
1.00
13.86
A


ATOM
1092
CE1
PHE
A
192
19.371
−12.249
34.218
1.00
12.89
A


ATOM
1093
CE2
PHE
A
192
17.642
−12.958
32.727
1.00
13.50
A


ATOM
1094
CZ
PHE
A
192
18.969
−12.644
32.944
1.00
13.74
A


ATOM
1095
C
PHE
A
192
16.498
−10.151
37.011
1.00
19.66
A


ATOM
1096
O
PHE
A
192
17.350
−9.530
36.398
1.00
16.83
A


ATOM
1097
N
LEU
A
193
16.380
−10.091
38.336
1.00
22.72
A


ATOM
1098
CA
LEU
A
193
17.386
−9.398
39.142
1.00
20.58
A


ATOM
1099
CB
LEU
A
193
16.965
−9.418
40.606
1.00
23.85
A


ATOM
1100
CG
LEU
A
193
18.004
−8.909
41.613
1.00
23.40
A


ATOM
1101
CD1
LEU
A
193
18.479
−7.496
41.213
1.00
23.22
A


ATOM
1102
CD2
LEU
A
193
17.346
−8.907
42.999
1.00
22.88
A


ATOM
1103
C
LEU
A
193
18.616
−10.311
38.935
1.00
21.88
A


ATOM
1104
O
LEU
A
193
18.497
−11.549
38.903
1.00
21.21
A


ATOM
1105
N
TYR
A
194
19.786
−9.710
38.756
1.00
22.39
A


ATOM
1106
CA
TYR
A
194
21.004
−10.447
38.518
1.00
22.95
A


ATOM
1107
CB
TYR
A
194
21.616
−9.922
37.229
1.00
21.48
A


ATOM
1108
CG
TYR
A
194
22.869
−10.612
36.795
1.00
19.73
A


ATOM
1109
CD1
TYR
A
194
24.115
−10.095
37.127
1.00
19.48
A


ATOM
1110
CE1
TYR
A
194
25.266
−10.676
36.666
1.00
20.31
A


ATOM
1111
CD2
TYR
A
194
22.813
−11.741
35.984
1.00
16.74
A


ATOM
1112
CE2
TYR
A
194
23.951
−12.322
35.510
1.00
16.40
A


ATOM
1113
CZ
TYR
A
194
25.186
−11.788
35.856
1.00
22.33
A


ATOM
1114
OH
TYR
A
194
26.354
−12.356
35.387
1.00
23.45
A


ATOM
1115
C
TYR
A
194
22.055
−10.413
39.656
1.00
25.99
A


ATOM
1116
O
TYR
A
194
22.700
−11.418
39.935
1.00
23.15
A


ATOM
1117
N
GLN
A
195
22.232
−9.250
40.284
1.00
29.35
A


ATOM
1118
CA
GLN
A
195
23.208
−9.062
41.360
1.00
29.01
A


ATOM
1119
CB
GLN
A
195
24.607
−8.870
40.786
1.00
28.31
A


ATOM
1120
CG
GLN
A
195
25.684
−8.967
41.851
1.00
28.76
A


ATOM
1121
CD
GLN
A
195
27.087
−8.989
41.310
1.00
32.25
A


ATOM
1122
OE1
GLN
A
195
27.375
−9.540
40.229
1.00
33.70
A


ATOM
1123
NE2
GLN
A
195
27.999
−8.417
42.083
1.00
34.02
A


ATOM
1124
C
GLN
A
195
22.822
−7.850
42.188
1.00
31.85
A


ATOM
1125
O
GLN
A
195
22.518
−6.784
41.631
1.00
32.81
A


ATOM
1126
N
GLN
A
196
22.811
−8.008
43.509
1.00
31.55
A


ATOM
1127
CA
GLN
A
196
22.446
−6.914
44.402
1.00
33.01
A


ATOM
1128
CB
GLN
A
196
21.562
−7.388
45.547
1.00
33.40
A


ATOM
1129
CG
GLN
A
196
20.197
−7.792
45.169
1.00
36.87
A


ATOM
1130
CD
GLN
A
196
19.322
−8.018
46.386
1.00
38.23
A


ATOM
1131
OE1
GLN
A
196
18.952
−7.077
47.070
1.00
43.30
A


ATOM
1132
NE2
GLN
A
196
19.000
−9.265
46.663
1.00
41.48
A


ATOM
1133
C
GLN
A
196
23.632
−6.238
45.043
1.00
33.18
A


ATOM
1134
O
GLN
A
196
24.742
−6.772
45.099
1.00
32.67
A


ATOM
1135
N
ASP
A
197
23.347
−5.065
45.583
1.00
34.68
A


ATOM
1136
CA
ASP
A
197
24.320
−4.239
46.278
1.00
37.04
A


ATOM
1137
CB
ASP
A
197
24.393
−4.625
47.758
1.00
39.18
A


ATOM
1138
CG
ASP
A
197
23.035
−4.794
48.375
1.00
43.72
A


ATOM
1139
OD1
ASP
A
197
22.265
−3.802
48.418
1.00
45.93
A


ATOM
1140
OD2
ASP
A
197
22.724
−5.935
48.807
1.00
48.86
A


ATOM
1141
C
ASP
A
197
25.719
−4.272
45.719
1.00
36.93
A


ATOM
1142
O
ASP
A
197
26.672
−4.542
46.455
1.00
35.50
A


ATOM
1143
N
VAL
A
198
25.856
−4.007
44.432
1.00
34.21
A


ATOM
1144
CA
VAL
A
198
27.176
−3.969
43.836
1.00
36.03
A


ATOM
1145
CB
VAL
A
198
27.096
−4.132
42.323
1.00
35.46
A


ATOM
1146
CG1
VAL
A
198
28.473
−3.979
41.716
1.00
35.71
A


ATOM
1147
CG2
VAL
A
198
26.517
−5.498
41.992
1.00
35.80
A


ATOM
1148
C
VAL
A
198
27.735
−2.583
44.161
1.00
38.78
A


ATOM
1149
O
VAL
A
198
27.034
−1.571
44.011
1.00
38.01
A


ATOM
1150
N
VAL
A
199
28.983
−2.523
44.621
1.00
40.43
A


ATOM
1151
CA
VAL
A
199
29.572
−1.222
44.960
1.00
40.95
A


ATOM
1152
CB
VAL
A
199
30.403
−1.279
46.261
1.00
41.60
A


ATOM
1153
CG1
VAL
A
199
29.496
−1.669
47.443
1.00
40.30
A


ATOM
1154
CG2
VAL
A
199
31.554
−2.262
46.094
1.00
43.87
A


ATOM
1155
C
VAL
A
199
30.435
−0.755
43.816
1.00
39.75
A


ATOM
1156
O
VAL
A
199
31.327
−1.465
43.363
1.00
40.53
A


ATOM
1157
N
VAL
A
200
30.132
0.439
43.332
1.00
39.38
A


ATOM
1158
CA
VAL
A
200
30.845
1.004
42.209
1.00
40.37
A


ATOM
1159
CB
VAL
A
200
29.870
1.357
41.036
1.00
40.73
A


ATOM
1160
CG1
VAL
A
200
30.649
1.654
39.771
1.00
40.68
A


ATOM
1161
CG2
VAL
A
200
28.931
0.212
40.780
1.00
38.82
A


ATOM
1162
C
VAL
A
200
31.524
2.258
42.694
1.00
41.59
A


ATOM
1163
O
VAL
A
200
30.902
3.118
43.307
1.00
41.85
A


ATOM
1164
N
VAL
A
201
32.814
2.357
42.418
1.00
44.74
A


ATOM
1165
CA
VAL
A
201
33.567
3.513
42.847
1.00
46.61
A


ATOM
1166
CB
VAL
A
201
34.965
3.106
43.355
1.00
47.23
A


ATOM
1167
CG1
VAL
A
201
35.604
4.274
44.127
1.00
46.39
A


ATOM
1168
CG2
VAL
A
201
34.848
1.883
44.257
1.00
48.12
A


ATOM
1169
C
VAL
A
201
33.711
4.442
41.666
1.00
47.35
A


ATOM
1170
O
VAL
A
201
34.384
4.107
40.704
1.00
46.77
A


ATOM
1171
N
LEU
A
202
33.053
5.594
41.746
1.00
50.34
A


ATOM
1172
CA
LEU
A
202
33.090
6.609
40.695
1.00
53.52
A


ATOM
1173
CB
LEU
A
202
31.669
7.091
40.353
1.00
54.00
A


ATOM
1174
CG
LEU
A
202
30.710
6.236
39.515
1.00
54.72
A


ATOM
1175
CD1
LEU
A
202
30.450
4.928
40.210
1.00
57.57
A


ATOM
1176
CD2
LEU
A
202
29.405
6.963
39.327
1.00
54.51
A


ATOM
1177
C
LEU
A
202
33.905
7.818
41.164
1.00
56.11
A


ATOM
1178
O
LEU
A
202
34.022
8.073
42.368
1.00
55.09
A


ATOM
1179
N
PRO
A
203
34.460
8.591
40.211
1.00
58.37
A


ATOM
1180
CD
PRO
A
203
34.466
8.303
38.762
1.00
59.65
A


ATOM
1181
CA
PRO
A
203
35.262
9.781
40.500
1.00
59.68
A


ATOM
1182
CB
PRO
A
203
35.468
10.407
39.123
1.00
59.41
A


ATOM
1183
CG
PRO
A
203
35.579
9.214
38.239
1.00
59.82
A


ATOM
1184
C
PRO
A
203
34.640
10.759
41.490
1.00
61.14
A


ATOM
1185
O
PRO
A
203
33.433
10.731
41.773
1.00
61.10
A


ATOM
1186
N
LYS
A
204
35.517
11.631
41.983
1.00
63.03
A


ATOM
1187
CA
LYS
A
204
35.243
12.670
42.977
1.00
63.67
A


ATOM
1188
CB
LYS
A
204
36.107
13.911
42.686
1.00
66.51
A


ATOM
1189
CG
LYS
A
204
37.561
13.807
43.182
1.00
70.06
A


ATOM
1190
CD
LYS
A
204
37.661
13.875
44.716
1.00
71.79
A


ATOM
1191
CE
LYS
A
204
39.118
13.815
45.172
1.00
73.07
A


ATOM
1192
NZ
LYS
A
204
39.941
14.903
44.542
1.00
74.42
A


ATOM
1193
C
LYS
A
204
33.828
13.127
43.303
1.00
60.91
A


ATOM
1194
O
LYS
A
204
33.341
12.840
44.398
1.00
64.02
A


ATOM
1195
N
PRO
A
205
33.139
13.818
42.373
1.00
56.45
A


ATOM
1196
CD
PRO
A
205
33.349
13.981
40.925
1.00
53.96
A


ATOM
1197
CA
PRO
A
205
31.792
14.245
42.761
1.00
53.46
A


ATOM
1198
CB
PRO
A
205
31.217
14.849
41.473
1.00
53.48
A


ATOM
1199
CG
PRO
A
205
32.414
15.112
40.611
1.00
53.39
A


ATOM
1200
C
PRO
A
205
30.914
13.121
43.292
1.00
52.72
A


ATOM
1201
O
PRO
A
205
30.146
13.307
44.238
1.00
52.54
A


ATOM
1202
N
TYR
A
206
31.057
11.935
42.713
1.00
51.10
A


ATOM
1203
CA
TYR
A
206
30.183
10.842
43.099
1.00
49.77
A


ATOM
1204
CB
TYR
A
206
29.697
10.147
41.821
1.00
48.49
A


ATOM
1205
CG
TYR
A
206
29.037
11.126
40.858
1.00
46.57
A


ATOM
1206
CD1
TYR
A
206
27.894
11.844
41.234
1.00
45.67
A


ATOM
1207
CE1
TYR
A
206
27.335
12.798
40.387
1.00
43.87
A


ATOM
1208
CD2
TYR
A
206
29.593
11.387
39.609
1.00
45.18
A


ATOM
1209
CE2
TYR
A
206
29.044
12.337
38.762
1.00
44.21
A


ATOM
1210
CZ
TYR
A
206
27.919
13.039
39.154
1.00
44.28
A


ATOM
1211
OH
TYR
A
206
27.393
13.991
38.307
1.00
44.33
A


ATOM
1212
C
TYR
A
206
30.672
9.828
44.124
1.00
49.50
A


ATOM
1213
O
TYR
A
206
29.896
9.412
44.978
1.00
48.83
A


ATOM
1214
N
GLY
A
207
31.935
9.415
44.045
1.00
48.23
A


ATOM
1215
CA
GLY
A
207
32.437
8.458
45.013
1.00
47.40
A


ATOM
1216
C
GLY
A
207
31.848
7.065
44.892
1.00
47.68
A


ATOM
1217
O
GLY
A
207
31.680
6.550
43.780
1.00
49.02
A


ATOM
1218
N
GLU
A
208
31.550
6.445
46.033
1.00
45.57
A


ATOM
1219
CA
GLU
A
208
31.003
5.097
46.043
1.00
43.83
A


ATOM
1220
CB
GLU
A
208
31.457
4.331
47.299
1.00
43.06
A


ATOM
1221
CG
GLU
A
208
32.808
3.661
47.057
1.00
47.39
A


ATOM
1222
CD
GLU
A
208
33.274
2.730
48.167
1.00
48.82
A


ATOM
1223
OE1
GLU
A
208
34.402
2.187
48.026
1.00
49.97
A


ATOM
1224
OE2
GLU
A
208
32.533
2.541
49.162
1.00
48.55
A


ATOM
1225
C
GLU
A
208
29.495
5.088
45.945
1.00
41.80
A


ATOM
1226
O
GLU
A
208
28.818
5.876
46.604
1.00
39.96
A


ATOM
1227
N
VAL
A
209
28.971
4.188
45.113
1.00
40.07
A


ATOM
1228
CA
VAL
A
209
27.525
4.072
44.916
1.00
38.21
A


ATOM
1229
CB
VAL
A
209
27.107
4.779
43.571
1.00
39.80
A


ATOM
1230
CG1
VAL
A
209
27.575
3.956
42.361
1.00
37.58
A


ATOM
1231
CG2
VAL
A
209
25.614
4.989
43.538
1.00
42.93
A


ATOM
1232
C
VAL
A
209
27.158
2.583
44.881
1.00
36.12
A


ATOM
1233
O
VAL
A
209
27.896
1.782
44.317
1.00
37.85
A


ATOM
1234
N
ALA
A
210
26.044
2.212
45.502
1.00
34.67
A


ATOM
1235
CA
ALA
A
210
25.592
0.819
45.530
1.00
34.49
A


ATOM
1236
CB
ALA
A
210
25.119
0.430
46.938
1.00
33.45
A


ATOM
1237
C
ALA
A
210
24.422
0.677
44.539
1.00
33.82
A


ATOM
1238
O
ALA
A
210
23.414
1.365
44.657
1.00
34.77
A


ATOM
1239
N
VAL
A
211
24.547
−0.253
43.606
1.00
32.02
A


ATOM
1240
CA
VAL
A
211
23.529
−0.454
42.596
1.00
29.15
A


ATOM
1241
CB
VAL
A
211
24.070
0.001
41.220
1.00
27.40
A


ATOM
1242
CG1
VAL
A
211
24.705
1.368
41.326
1.00
26.38
A


ATOM
1243
CG2
VAL
A
211
25.095
−0.971
40.724
1.00
24.04
A


ATOM
1244
C
VAL
A
211
23.120
−1.914
42.456
1.00
30.40
A


ATOM
1245
O
VAL
A
211
23.853
−2.820
42.886
1.00
28.98
A


ATOM
1246
N
ASP
A
212
21.948
−2.139
41.858
1.00
28.19
A


ATOM
1247
CA
ASP
A
212
21.483
−3.494
41.566
1.00
28.03
A


ATOM
1248
CB
ASP
A
212
19.999
−3.677
41.919
1.00
29.50
A


ATOM
1249
CG
ASP
A
212
19.752
−3.758
43.431
1.00
31.57
A


ATOM
1250
OD1
ASP
A
212
20.709
−4.058
44.162
1.00
34.76
A


ATOM
1251
OD2
ASP
A
212
18.615
−3.537
43.896
1.00
32.63
A


ATOM
1252
C
ASP
A
212
21.688
−3.686
40.053
1.00
28.82
A


ATOM
1253
O
ASP
A
212
21.599
−2.726
39.262
1.00
28.01
A


ATOM
1254
N
ILE
A
213
22.017
−4.903
39.643
1.00
26.82
A


ATOM
1255
CA
ILE
A
213
22.180
−5.180
38.230
1.00
23.45
A


ATOM
1256
CB
ILE
A
213
23.505
−5.893
37.939
1.00
24.63
A


ATOM
1257
CG2
ILE
A
213
23.567
−6.338
36.450
1.00
20.86
A


ATOM
1258
CG1
ILE
A
213
24.661
−4.928
38.247
1.00
22.68
A


ATOM
1259
CD1
ILE
A
213
26.014
−5.461
37.864
1.00
26.22
A


ATOM
1260
C
ILE
A
213
21.002
−6.073
37.924
1.00
25.43
A


ATOM
1261
O
ILE
A
213
20.742
−7.030
38.668
1.00
24.17
A


ATOM
1262
N
ALA
A
214
20.241
−5.731
36.876
1.00
23.85
A


ATOM
1263
CA
ALA
A
214
19.074
−6.525
36.500
1.00
22.54
A


ATOM
1264
CB
ALA
A
214
17.835
−5.976
37.170
1.00
16.51
A


ATOM
1265
C
ALA
A
214
18.881
−6.559
34.981
1.00
23.53
A


ATOM
1266
O
ALA
A
214
19.274
−5.620
34.259
1.00
24.53
A


ATOM
1267
N
PHE
A
215
18.244
−7.621
34.493
1.00
21.22
A


ATOM
1268
CA
PHE
A
215
18.027
−7.742
33.068
1.00
20.88
A


ATOM
1269
CB
PHE
A
215
18.475
−9.116
32.575
1.00
19.85
A


ATOM
1270
CG
PHE
A
215
18.342
−9.302
31.070
1.00
17.94
A


ATOM
1271
CD1
PHE
A
215
19.241
−8.698
30.201
1.00
18.85
A


ATOM
1272
CD2
PHE
A
215
17.329
−10.076
30.536
1.00
18.21
A


ATOM
1273
CE1
PHE
A
215
19.137
−8.865
28.797
1.00
21.00
A


ATOM
1274
CE2
PHE
A
215
17.212
−10.250
29.125
1.00
18.93
A


ATOM
1275
CZ
PHE
A
215
18.131
−9.635
28.265
1.00
16.86
A


ATOM
1276
C
PHE
A
215
16.541
−7.517
32.774
1.00
19.38
A


ATOM
1277
O
PHE
A
215
15.671
−8.055
33.448
1.00
20.46
A


ATOM
1278
N
GLY
A
216
16.258
−6.673
31.792
1.00
18.98
A


ATOM
1279
CA
GLY
A
216
14.873
−6.415
31.417
1.00
16.50
A


ATOM
1280
C
GLY
A
216
14.826
−6.367
29.881
1.00
17.77
A


ATOM
1281
O
GLY
A
216
13.928
−5.762
29.307
1.00
20.47
A


ATOM
1282
N
GLY
A
217
15.777
−7.023
29.230
1.00
16.37
A


ATOM
1283
CA
GLY
A
217
15.868
−7.004
27.770
1.00
16.96
A


ATOM
1284
C
GLY
A
217
17.268
−6.497
27.468
1.00
16.38
A


ATOM
1285
O
GLY
A
217
17.881
−6.850
26.452
1.00
19.81
A


ATOM
1286
N
ASN
A
218
17.766
−5.641
28.359
1.00
15.91
A


ATOM
1287
CA
ASN
A
218
19.137
−5.137
28.318
1.00
15.62
A


ATOM
1288
CB
ASN
A
218
19.204
−3.642
27.979
1.00
13.15
A


ATOM
1289
CG
ASN
A
218
18.607
−3.327
26.589
1.00
17.85
A


ATOM
1290
OD1
ASN
A
218
19.104
−3.804
25.559
1.00
18.86
A


ATOM
1291
ND2
ASN
A
218
17.554
−2.534
26.575
1.00
14.08
A


ATOM
1292
C
ASN
A
218
19.552
−5.293
29.783
1.00
16.88
A


ATOM
1293
O
ASN
A
218
18.703
−5.367
30.634
1.00
16.76
A


ATOM
1294
N
PHE
A
219
20.844
−5.352
30.061
1.00
17.60
A


ATOM
1295
CA
PHE
A
219
21.278
−5.390
31.445
1.00
20.81
A


ATOM
1296
CB
PHE
A
219
22.693
−5.984
31.547
1.00
20.77
A


ATOM
1297
CG
PHE
A
219
22.706
−7.453
31.800
1.00
21.46
A


ATOM
1298
CD1
PHE
A
219
23.270
−8.325
30.885
1.00
23.13
A


ATOM
1299
CD2
PHE
A
219
22.217
−7.954
32.984
1.00
21.01
A


ATOM
1300
CE1
PHE
A
219
23.352
−9.690
31.151
1.00
24.36
A


ATOM
1301
CE2
PHE
A
219
22.298
−9.311
33.261
1.00
23.60
A


ATOM
1302
CZ
PHE
A
219
22.867
−10.178
32.341
1.00
21.15
A


ATOM
1303
C
PHE
A
219
21.296
−3.948
31.907
1.00
19.22
A


ATOM
1304
O
PHE
A
219
21.817
−3.074
31.230
1.00
21.81
A


ATOM
1305
N
PHE
A
220
20.722
−3.696
33.063
1.00
20.27
A


ATOM
1306
CA
PHE
A
220
20.668
−2.360
33.627
1.00
19.58
A


ATOM
1307
CB
PHE
A
220
19.225
−1.993
33.967
1.00
20.34
A


ATOM
1308
CG
PHE
A
220
18.408
−1.500
32.793
1.00
21.87
A


ATOM
1309
CD1
PHE
A
220
18.187
−0.129
32.610
1.00
20.61
A


ATOM
1310
CD2
PHE
A
220
17.858
−2.410
31.881
1.00
16.67
A


ATOM
1311
CE1
PHE
A
220
17.419
0.340
31.525
1.00
19.99
A


ATOM
1312
CE2
PHE
A
220
17.107
−1.956
30.812
1.00
19.03
A


ATOM
1313
CZ
PHE
A
220
16.885
−0.578
30.633
1.00
19.94
A


ATOM
1314
C
PHE
A
220
21.414
−2.307
34.972
1.00
22.98
A


ATOM
1315
O
PHE
A
220
21.483
−3.313
35.669
1.00
22.94
A


ATOM
1316
N
ALA
A
221
21.968
−1.147
35.309
1.00
21.90
A


ATOM
1317
CA
ALA
A
221
22.528
−0.932
36.641
1.00
22.48
A


ATOM
1318
CB
ALA
A
221
23.891
−0.180
36.590
1.00
21.08
A


ATOM
1319
C
ALA
A
221
21.423
0.001
37.146
1.00
21.09
A


ATOM
1320
O
ALA
A
221
21.142
1.012
36.511
1.00
24.87
A


ATOM
1321
N
ILE
A
222
20.765
−0.347
38.240
1.00
20.84
A


ATOM
1322
CA
ILE
A
222
19.697
0.449
38.816
1.00
23.85
A


ATOM
1323
CB
ILE
A
222
18.521
−0.446
39.155
1.00
23.60
A


ATOM
1324
CG2
ILE
A
222
17.417
0.383
39.799
1.00
21.92
A


ATOM
1325
CG1
ILE
A
222
18.030
−1.159
37.874
1.00
24.75
A


ATOM
1326
CD1
ILE
A
222
16.816
−2.090
38.112
1.00
23.70
A


ATOM
1327
C
ILE
A
222
20.226
1.151
40.088
1.00
25.99
A


ATOM
1328
O
ILE
A
222
20.749
0.489
40.981
1.00
25.47
A


ATOM
1329
N
VAL
A
223
20.076
2.475
40.170
1.00
27.20
A


ATOM
1330
CA
VAL
A
223
20.631
3.272
41.278
1.00
27.77
A


ATOM
1331
CB
VAL
A
223
22.064
3.826
40.861
1.00
30.02
A


ATOM
1332
CG1
VAL
A
223
21.944
4.837
39.708
1.00
30.59
A


ATOM
1333
CG2
VAL
A
223
22.774
4.482
42.038
1.00
29.54
A


ATOM
1334
C
VAL
A
223
19.714
4.430
41.678
1.00
28.94
A


ATOM
1335
O
VAL
A
223
19.151
5.113
40.823
1.00
26.93
A


ATOM
1336
N
PRO
A
224
19.513
4.634
42.993
1.00
28.66
A


ATOM
1337
CD
PRO
A
224
20.022
3.845
44.133
1.00
28.59
A


ATOM
1338
CA
PRO
A
224
18.652
5.725
43.443
1.00
26.78
A


ATOM
1339
CB
PRO
A
224
18.617
5.545
44.965
1.00
27.89
A


ATOM
1340
CG
PRO
A
224
18.954
4.067
45.156
1.00
28.55
A


ATOM
1341
C
PRO
A
224
19.334
7.031
43.066
1.00
26.32
A


ATOM
1342
O
PRO
A
224
20.555
7.101
43.100
1.00
27.49
A


ATOM
1343
N
ALA
A
225
18.587
8.066
42.695
1.00
25.04
A


ATOM
1344
CA
ALA
A
225
19.265
9.331
42.385
1.00
26.13
A


ATOM
1345
CB
ALA
A
225
18.296
10.336
41.857
1.00
23.34
A


ATOM
1346
C
ALA
A
225
19.881
9.875
43.693
1.00
28.41
A


ATOM
1347
O
ALA
A
225
20.928
10.536
43.666
1.00
28.29
A


ATOM
1348
N
ALA
A
226
19.194
9.620
44.806
1.00
30.40
A


ATOM
1349
CA
ALA
A
226
19.635
10.051
46.144
1.00
36.35
A


ATOM
1350
CB
ALA
A
226
18.767
9.354
47.237
1.00
34.64
A


ATOM
1351
C
ALA
A
226
21.135
9.734
46.341
1.00
37.02
A


ATOM
1352
O
ALA
A
226
21.890
10.549
46.843
1.00
41.07
A


ATOM
1353
N
GLN
A
227
21.569
8.564
45.907
1.00
37.05
A


ATOM
1354
CA
GLN
A
227
22.971
8.167
46.016
1.00
36.73
A


ATOM
1355
CB
GLN
A
227
23.120
6.697
45.641
1.00
36.28
A


ATOM
1356
CG
GLN
A
227
22.563
5.732
46.659
1.00
40.94
A


ATOM
1357
CD
GLN
A
227
23.355
4.435
46.638
1.00
44.78
A


ATOM
1358
OE1
GLN
A
227
24.600
4.456
46.745
1.00
48.47
A


ATOM
1359
NE2
GLN
A
227
22.661
3.305
46.495
1.00
40.85
A


ATOM
1360
C
GLN
A
227
23.970
8.956
45.165
1.00
37.38
A


ATOM
1361
O
GLN
A
227
25.174
8.904
45.414
1.00
36.82
A


ATOM
1362
N
LEU
A
228
23.499
9.656
44.139
1.00
35.30
A


ATOM
1363
CA
LEU
A
228
24.407
10.388
43.277
1.00
35.17
A


ATOM
1364
CB
LEU
A
228
23.926
10.329
41.815
1.00
35.67
A


ATOM
1365
CG
LEU
A
228
23.879
8.981
41.087
1.00
36.18
A


ATOM
1366
CD1
LEU
A
228
22.996
9.107
39.838
1.00
36.51
A


ATOM
1367
CD2
LEU
A
228
25.283
8.535
40.728
1.00
36.62
A


ATOM
1368
C
LEU
A
228
24.500
11.842
43.706
1.00
34.19
A


ATOM
1369
O
LEU
A
228
25.261
12.592
43.140
1.00
34.44
A


ATOM
1370
N
GLY
A
229
23.709
12.247
44.688
1.00
35.21
A


ATOM
1371
CA
GLY
A
229
23.779
13.637
45.108
1.00
38.34
A


ATOM
1372
C
GLY
A
229
22.916
14.593
44.294
1.00
41.43
A


ATOM
1373
O
GLY
A
229
22.769
15.770
44.649
1.00
38.76
A


ATOM
1374
N
ILE
A
230
22.337
14.087
43.201
1.00
41.92
A


ATOM
1375
CA
ILE
A
230
21.480
14.899
42.371
1.00
41.59
A


ATOM
1376
CB
ILE
A
230
22.100
15.155
41.016
1.00
42.74
A


ATOM
1377
CG2
ILE
A
230
23.186
16.266
41.165
1.00
45.58
A


ATOM
1378
CG1
ILE
A
230
22.632
13.849
40.436
1.00
42.36
A


ATOM
1379
CD1
ILE
A
230
23.596
14.053
39.267
1.00
40.18
A


ATOM
1380
C
ILE
A
230
20.101
14.318
42.199
1.00
40.92
A


ATOM
1381
O
ILE
A
230
19.895
13.110
42.142
1.00
43.20
A


ATOM
1382
N
ASP
A
231
19.158
15.235
42.143
1.00
39.70
A


ATOM
1383
CA
ASP
A
231
17.731
14.986
42.021
1.00
39.27
A


ATOM
1384
CB
ASP
A
231
17.075
16.210
42.629
1.00
44.87
A


ATOM
1385
CG
ASP
A
231
15.614
16.121
42.667
1.00
51.32
A


ATOM
1386
OD1
ASP
A
231
15.094
15.087
43.149
1.00
55.63
A


ATOM
1387
OD2
ASP
A
231
14.984
17.105
42.228
1.00
55.31
A


ATOM
1388
C
ASP
A
231
17.375
14.816
40.531
1.00
36.01
A


ATOM
1389
O
ASP
A
231
18.099
15.310
39.690
1.00
30.59
A


ATOM
1390
N
ILE
A
232
16.282
14.125
40.198
1.00
34.78
A


ATOM
1391
CA
ILE
A
232
15.930
13.951
38.778
1.00
33.85
A


ATOM
1392
CB
ILE
A
232
15.081
12.664
38.562
1.00
33.96
A


ATOM
1393
CG2
ILE
A
232
14.695
12.543
37.094
1.00
31.54
A


ATOM
1394
CG1
ILE
A
232
15.894
11.426
38.954
1.00
33.28
A


ATOM
1395
CD1
ILE
A
232
15.050
10.137
39.020
1.00
33.21
A


ATOM
1396
C
ILE
A
232
15.158
15.174
38.243
1.00
31.38
A


ATOM
1397
O
ILE
A
232
14.000
15.385
38.586
1.00
33.23
A


ATOM
1398
N
SER
A
233
15.805
15.984
37.413
1.00
31.64
A


ATOM
1399
CA
SER
A
233
15.161
17.185
36.882
1.00
31.46
A


ATOM
1400
CB
SER
A
233
15.226
18.284
37.943
1.00
32.19
A


ATOM
1401
OG
SER
A
233
16.586
18.665
38.122
1.00
31.68
A


ATOM
1402
C
SER
A
233
15.920
17.627
35.651
1.00
30.92
A


ATOM
1403
O
SER
A
233
17.038
17.150
35.423
1.00
31.22
A


ATOM
1404
N
VAL
A
234
15.354
18.555
34.872
1.00
32.37
A


ATOM
1405
CA
VAL
A
234
16.047
19.023
33.667
1.00
32.42
A


ATOM
1406
CB
VAL
A
234
15.132
19.907
32.719
1.00
35.31
A


ATOM
1407
CG1
VAL
A
234
13.800
19.210
32.461
1.00
31.97
A


ATOM
1408
CG2
VAL
A
234
14.929
21.288
33.314
1.00
36.97
A


ATOM
1409
C
VAL
A
234
17.312
19.814
34.000
1.00
32.09
A


ATOM
1410
O
VAL
A
234
18.266
19.844
33.205
1.00
30.77
A


ATOM
1411
N
GLN
A
235
17.326
20.448
35.174
1.00
31.75
A


ATOM
1412
CA
GLN
A
235
18.484
21.223
35.631
1.00
28.16
A


ATOM
1413
CB
GLN
A
235
18.205
21.872
36.986
1.00
33.85
A


ATOM
1414
CG
GLN
A
235
16.998
22.768
37.043
1.00
41.63
A


ATOM
1415
CD
GLN
A
235
15.700
22.061
36.671
1.00
47.44
A


ATOM
1416
OE1
GLN
A
235
15.665
20.837
36.491
1.00
51.31
A


ATOM
1417
NE2
GLN
A
235
14.616
22.835
36.559
1.00
50.11
A


ATOM
1418
C
GLN
A
235
19.645
20.278
35.816
1.00
25.54
A


ATOM
1419
O
GLN
A
235
20.789
20.622
35.559
1.00
22.27
A


ATOM
1420
N
ASN
A
236
19.353
19.060
36.260
1.00
25.06
A


ATOM
1421
CA
ASN
A
236
20.417
18.091
36.510
1.00
27.53
A


ATOM
1422
CB
ASN
A
236
20.042
17.327
37.780
1.00
29.64
A


ATOM
1423
CG
ASN
A
236
20.088
18.223
39.016
1.00
30.18
A


ATOM
1424
OD1
ASN
A
236
19.335
18.042
39.976
1.00
32.72
A


ATOM
1425
ND2
ASN
A
236
20.976
19.203
38.982
1.00
27.69
A


ATOM
1426
C
ASN
A
236
20.725
17.123
35.368
1.00
30.21
A


ATOM
1427
O
ASN
A
236
21.739
16.386
35.387
1.00
29.37
A


ATOM
1428
N
LEU
A
237
19.873
17.153
34.347
1.00
30.39
A


ATOM
1429
CA
LEU
A
237
20.017
16.217
33.229
1.00
29.36
A


ATOM
1430
CB
LEU
A
237
19.094
16.630
32.049
1.00
28.33
A


ATOM
1431
CG
LEU
A
237
18.979
15.614
30.897
1.00
30.71
A


ATOM
1432
CD1
LEU
A
237
18.959
14.171
31.426
1.00
28.27
A


ATOM
1433
CD2
LEU
A
237
17.711
15.936
30.104
1.00
29.89
A


ATOM
1434
C
LEU
A
237
21.448
16.015
32.749
1.00
28.73
A


ATOM
1435
O
LEU
A
237
21.898
14.878
32.609
1.00
25.78
A


ATOM
1436
N
SER
A
238
22.187
17.096
32.518
1.00
26.18
A


ATOM
1437
CA
SER
A
238
23.544
16.918
32.050
1.00
30.73
A


ATOM
1438
CB
SER
A
238
24.145
18.270
31.680
1.00
34.33
A


ATOM
1439
OG
SER
A
238
24.126
19.125
32.823
1.00
41.05
A


ATOM
1440
C
SER
A
238
24.459
16.198
33.088
1.00
31.26
A


ATOM
1441
O
SER
A
238
25.435
15.544
32.714
1.00
31.50
A


ATOM
1442
N
ARG
A
239
24.158
16.310
34.372
1.00
30.67
A


ATOM
1443
CA
ARG
A
239
24.993
15.617
35.354
1.00
32.78
A


ATOM
1444
CB
ARG
A
239
24.910
16.318
36.723
1.00
36.06
A


ATOM
1445
CG
ARG
A
239
25.872
17.529
36.808
1.00
42.05
A


ATOM
1446
CD
ARG
A
239
25.836
18.212
38.173
1.00
49.32
A


ATOM
1447
NE
ARG
A
239
24.558
18.869
38.445
1.00
54.33
A


ATOM
1448
CZ
ARG
A
239
24.156
20.015
37.884
1.00
57.82
A


ATOM
1449
NH1
ARG
A
239
24.941
20.651
37.008
1.00
58.80
A


ATOM
1450
NH2
ARG
A
239
22.959
20.524
38.187
1.00
56.96
A


ATOM
1451
C
ARG
A
239
24.525
14.165
35.420
1.00
30.93
A


ATOM
1452
O
ARG
A
239
25.346
13.233
35.480
1.00
32.56
A


ATOM
1453
N
LEU
A
240
23.212
13.965
35.362
1.00
27.72
A


ATOM
1454
CA
LEU
A
240
22.686
12.606
35.363
1.00
24.97
A


ATOM
1455
CB
LEU
A
240
21.175
12.637
35.222
1.00
23.21
A


ATOM
1456
CG
LEU
A
240
20.491
13.169
36.478
1.00
23.01
A


ATOM
1457
CD1
LEU
A
240
19.064
13.617
36.194
1.00
25.03
A


ATOM
1458
CD2
LEU
A
240
20.476
12.072
37.518
1.00
24.59
A


ATOM
1459
C
LEU
A
240
23.327
11.830
34.238
1.00
25.23
A


ATOM
1460
O
LEU
A
240
23.770
10.694
34.442
1.00
25.65
A


ATOM
1461
N
GLN
A
241
23.426
12.445
33.054
1.00
26.19
A


ATOM
1462
CA
GLN
A
241
24.025
11.783
31.899
1.00
26.22
A


ATOM
1463
CB
GLN
A
241
24.019
12.684
30.635
1.00
26.20
A


ATOM
1464
CG
GLN
A
241
22.633
13.194
30.196
1.00
29.99
A


ATOM
1465
CD
GLN
A
241
22.700
13.888
28.829
1.00
33.73
A


ATOM
1466
OE1
GLN
A
241
23.787
14.192
28.345
1.00
38.34
A


ATOM
1467
NE2
GLN
A
241
21.551
14.136
28.211
1.00
30.09
A


ATOM
1468
C
GLN
A
241
25.454
11.428
32.200
1.00
26.83
A


ATOM
1469
O
GLN
A
241
25.929
10.310
31.903
1.00
25.21
A


ATOM
1470
N
GLU
A
242
26.170
12.402
32.752
1.00
28.33
A


ATOM
1471
CA
GLU
A
242
27.569
12.184
33.088
1.00
29.85
A


ATOM
1472
CB
GLU
A
242
28.204
13.474
33.641
1.00
32.89
A


ATOM
1473
CG
GLU
A
242
28.698
14.392
32.513
1.00
38.22
A


ATOM
1474
CD
GLU
A
242
28.867
15.858
32.950
1.00
41.38
A


ATOM
1475
OE1
GLU
A
242
28.881
16.112
34.185
1.00
40.63
A


ATOM
1476
OE2
GLU
A
242
28.981
16.739
32.047
1.00
40.29
A


ATOM
1477
C
GLU
A
242
27.675
11.063
34.094
1.00
25.98
A


ATOM
1478
O
GLU
A
242
28.465
10.157
33.909
1.00
28.02
A


ATOM
1479
N
ALA
A
243
26.887
11.132
35.154
1.00
25.29
A


ATOM
1480
CA
ALA
A
243
26.903
10.090
36.177
1.00
28.40
A


ATOM
1481
CB
ALA
A
243
25.934
10.452
37.299
1.00
26.78
A


ATOM
1482
C
ALA
A
243
26.545
8.705
35.590
1.00
30.26
A


ATOM
1483
O
ALA
A
243
27.161
7.694
35.947
1.00
28.44
A


ATOM
1484
N
GLY
A
244
25.575
8.675
34.666
1.00
29.10
A


ATOM
1485
CA
GLY
A
244
25.161
7.419
34.071
1.00
27.11
A


ATOM
1486
C
GLY
A
244
26.246
6.817
33.224
1.00
28.29
A


ATOM
1487
O
GLY
A
244
26.398
5.604
33.171
1.00
26.53
A


ATOM
1488
N
GLU
A
245
27.004
7.664
32.537
1.00
31.02
A


ATOM
1489
CA
GLU
A
245
28.101
7.193
31.703
1.00
31.96
A


ATOM
1490
CB
GLU
A
245
28.614
8.325
30.808
1.00
34.93
A


ATOM
1491
CG
GLU
A
245
29.815
7.953
29.956
1.00
40.76
A


ATOM
1492
CD
GLU
A
245
29.499
6.907
28.872
1.00
48.97
A


ATOM
1493
OE1
GLU
A
245
30.455
6.236
28.398
1.00
48.75
A


ATOM
1494
OE2
GLU
A
245
28.303
6.763
28.476
1.00
52.76
A


ATOM
1495
C
GLU
A
245
29.256
6.666
32.590
1.00
32.44
A


ATOM
1496
O
GLU
A
245
29.790
5.581
32.337
1.00
31.01
A


ATOM
1497
N
LEU
A
246
29.649
7.444
33.604
1.00
30.38
A


ATOM
1498
CA
LEU
A
246
30.725
7.041
34.520
1.00
28.75
A


ATOM
1499
CB
LEU
A
246
30.869
8.053
35.666
1.00
26.18
A


ATOM
1500
CG
LEU
A
246
31.392
9.406
35.184
1.00
27.88
A


ATOM
1501
CD1
LEU
A
246
31.292
10.416
36.293
1.00
30.27
A


ATOM
1502
CD2
LEU
A
246
32.817
9.263
34.676
1.00
28.65
A


ATOM
1503
C
LEU
A
246
30.367
5.686
35.106
1.00
28.55
A


ATOM
1504
O
LEU
A
246
31.174
4.765
35.116
1.00
29.12
A


ATOM
1505
N
LEU
A
247
29.129
5.569
35.573
1.00
27.99
A


ATOM
1506
CA
LEU
A
247
28.639
4.331
36.167
1.00
28.99
A


ATOM
1507
CB
LEU
A
247
27.209
4.556
36.628
1.00
29.61
A


ATOM
1508
CG
LEU
A
247
26.536
3.556
37.555
1.00
33.22
A


ATOM
1509
CD1
LEU
A
247
27.526
2.747
38.348
1.00
36.07
A


ATOM
1510
CD2
LEU
A
247
25.669
4.361
38.494
1.00
35.86
A


ATOM
1511
C
LEU
A
247
28.723
3.112
35.246
1.00
29.37
A


ATOM
1512
O
LEU
A
247
29.209
2.047
35.638
1.00
28.84
A


ATOM
1513
N
ARG
A
248
28.285
3.269
34.007
1.00
27.06
A


ATOM
1514
CA
ARG
A
248
28.292
2.163
33.054
1.00
27.52
A


ATOM
1515
CB
ARG
A
248
27.517
2.585
31.784
1.00
24.82
A


ATOM
1516
CG
ARG
A
248
27.552
1.625
30.629
1.00
27.12
A


ATOM
1517
CD
ARG
A
248
27.019
2.387
29.406
1.00
30.53
A


ATOM
1518
NE
ARG
A
248
26.991
1.618
28.180
1.00
33.84
A


ATOM
1519
CZ
ARG
A
248
26.565
2.111
27.018
1.00
36.44
A


ATOM
1520
NH1
ARG
A
248
26.138
3.361
26.948
1.00
34.64
A


ATOM
1521
NH2
ARG
A
248
26.582
1.360
25.924
1.00
36.47
A


ATOM
1522
C
ARG
A
248
29.704
1.730
32.681
1.00
28.74
A


ATOM
1523
O
ARG
A
248
30.001
0.522
32.519
1.00
27.51
A


ATOM
1524
N
THR
A
249
30.575
2.717
32.503
1.00
31.55
A


ATOM
1525
CA
THR
A
249
31.962
2.442
32.138
1.00
33.51
A


ATOM
1526
CB
THR
A
249
32.719
3.758
31.841
1.00
34.55
A


ATOM
1527
OG1
THR
A
249
32.178
4.334
30.640
1.00
33.35
A


ATOM
1528
CG2
THR
A
249
34.225
3.506
31.630
1.00
33.62
A


ATOM
1529
C
THR
A
249
32.641
1.653
33.249
1.00
34.73
A


ATOM
1530
O
THR
A
249
33.190
0.564
33.003
1.00
35.33
A


ATOM
1531
N
GLU
A
250
32.553
2.176
34.469
1.00
36.28
A


ATOM
1532
CA
GLU
A
250
33.153
1.517
35.623
1.00
38.71
A


ATOM
1533
CB
GLU
A
250
33.012
2.379
36.892
1.00
40.35
A


ATOM
1534
CG
GLU
A
250
33.515
1.736
38.224
1.00
42.45
A


ATOM
1535
CD
GLU
A
250
34.964
1.220
38.169
1.00
45.04
A


ATOM
1536
OE1
GLU
A
250
35.751
1.691
37.311
1.00
42.97
A


ATOM
1537
OE2
GLU
A
250
35.319
0.342
39.002
1.00
45.05
A


ATOM
1538
C
GLU
A
250
32.567
0.126
35.846
1.00
38.53
A


ATOM
1539
O
GLU
A
250
33.335
−0.837
35.922
1.00
38.97
A


ATOM
1540
N
ILE
A
251
31.238
−0.015
35.909
1.00
38.19
A


ATOM
1541
CA
ILE
A
251
30.692
−1.357
36.146
1.00
37.75
A


ATOM
1542
CB
ILE
A
251
29.155
−1.406
36.306
1.00
40.00
A


ATOM
1543
CG2
ILE
A
251
28.755
−2.677
37.078
1.00
41.73
A


ATOM
1544
CG1
ILE
A
251
28.681
−0.293
37.215
1.00
41.27
A


ATOM
1545
CD1
ILE
A
251
27.162
−0.244
37.373
1.00
42.50
A


ATOM
1546
C
ILE
A
251
31.080
−2.346
35.064
1.00
35.33
A


ATOM
1547
O
ILE
A
251
31.315
−3.498
35.370
1.00
34.74
A


ATOM
1548
N
ASN
A
252
31.169
−1.935
33.806
1.00
33.30
A


ATOM
1549
CA
ASN
A
252
31.558
−2.917
32.795
1.00
34.49
A


ATOM
1550
CB
ASN
A
252
31.237
−2.440
31.379
1.00
30.83
A


ATOM
1551
CG
ASN
A
252
29.779
−2.642
31.016
1.00
30.63
A


ATOM
1552
OD1
ASN
A
252
29.211
−3.714
31.243
1.00
27.33
A


ATOM
1553
ND2
ASN
A
252
29.167
−1.613
30.425
1.00
30.85
A


ATOM
1554
C
ASN
A
252
33.034
−3.261
32.864
1.00
37.28
A


ATOM
1555
O
ASN
A
252
33.488
−4.238
32.248
1.00
37.49
A


ATOM
1556
N
ARG
A
253
33.796
−2.448
33.599
1.00
41.22
A


ATOM
1557
CA
ARG
A
253
35.230
−2.700
33.727
1.00
44.52
A


ATOM
1558
CB
ARG
A
253
35.998
−1.381
33.940
1.00
45.36
A


ATOM
1559
CG
ARG
A
253
37.516
−1.512
33.955
1.00
49.66
A


ATOM
1560
CD
ARG
A
253
38.162
−0.256
34.552
1.00
52.71
A


ATOM
1561
NE
ARG
A
253
37.788
−0.080
35.966
1.00
57.16
A


ATOM
1562
CZ
ARG
A
253
38.430
−0.629
37.007
1.00
58.29
A


ATOM
1563
NH1
ARG
A
253
39.499
−1.391
36.810
1.00
57.42
A


ATOM
1564
NH2
ARG
A
253
37.988
−0.431
38.252
1.00
58.60
A


ATOM
1565
C
ARG
A
253
35.499
−3.642
34.886
1.00
44.01
A


ATOM
1566
O
ARG
A
253
36.352
−4.504
34.791
1.00
44.73
A


ATOM
1567
N
SER
A
254
34.723
−3.500
35.954
1.00
43.93
A


ATOM
1568
CA
SER
A
254
34.931
−4.272
37.153
1.00
44.32
A


ATOM
1569
CB
SER
A
254
34.937
−3.322
38.329
1.00
47.35
A


ATOM
1570
OG
SER
A
254
33.613
−2.888
38.566
1.00
51.38
A


ATOM
1571
C
SER
A
254
33.959
−5.393
37.470
1.00
44.95
A


ATOM
1572
O
SER
A
254
34.218
−6.181
38.385
1.00
44.40
A


ATOM
1573
N
VAL
A
255
32.844
−5.468
36.741
1.00
42.74
A


ATOM
1574
CA
VAL
A
255
31.836
−6.493
36.986
1.00
40.36
A


ATOM
1575
CB
VAL
A
255
30.548
−5.896
37.561
1.00
41.60
A


ATOM
1576
CG1
VAL
A
255
29.531
−7.011
37.869
1.00
40.22
A


ATOM
1577
CG2
VAL
A
255
30.856
−5.062
38.795
1.00
40.74
A


ATOM
1578
C
VAL
A
255
31.462
−7.102
35.669
1.00
41.39
A


ATOM
1579
O
VAL
A
255
30.865
−6.431
34.840
1.00
41.40
A


ATOM
1580
N
LYS
A
256
31.790
−8.365
35.454
1.00
40.55
A


ATOM
1581
CA
LYS
A
256
31.424
−8.972
34.193
1.00
40.79
A


ATOM
1582
CB
LYS
A
256
32.497
−9.969
33.753
1.00
43.85
A


ATOM
1583
CG
LYS
A
256
33.870
−9.316
33.465
1.00
46.96
A


ATOM
1584
CD
LYS
A
256
33.817
−8.333
32.274
1.00
47.53
A


ATOM
1585
CE
LYS
A
256
35.181
−7.706
32.025
1.00
48.53
A


ATOM
1586
NZ
LYS
A
256
35.655
−7.013
33.257
1.00
50.53
A


ATOM
1587
C
LYS
A
256
30.059
−9.631
34.390
1.00
39.84
A


ATOM
1588
O
LYS
A
256
29.827
−10.326
35.393
1.00
42.78
A


ATOM
1589
N
VAL
A
257
29.138
−9.367
33.471
1.00
33.08
A


ATOM
1590
CA
VAL
A
257
27.817
−9.922
33.593
1.00
28.16
A


ATOM
1591
CB
VAL
A
257
26.742
−8.810
33.564
1.00
30.56
A


ATOM
1592
CG1
VAL
A
257
27.038
−7.774
34.661
1.00
28.05
A


ATOM
1593
CG2
VAL
A
257
26.701
−8.136
32.174
1.00
26.92
A


ATOM
1594
C
VAL
A
257
27.628
−10.859
32.426
1.00
26.46
A


ATOM
1595
O
VAL
A
257
28.268
−10.707
31.400
1.00
25.87
A


ATOM
1596
N
GLN
A
258
26.777
−11.855
32.588
1.00
24.28
A


ATOM
1597
CA
GLN
A
258
26.544
−12.805
31.500
1.00
25.71
A


ATOM
1598
CB
GLN
A
258
27.554
−13.957
31.520
1.00
23.07
A


ATOM
1599
CG
GLN
A
258
27.280
−15.009
30.432
1.00
24.95
A


ATOM
1600
CD
GLN
A
258
27.426
−14.467
29.009
1.00
23.63
A


ATOM
1601
OE1
GLN
A
258
26.467
−14.430
28.221
1.00
26.35
A


ATOM
1602
NE2
GLN
A
258
28.626
−14.073
28.671
1.00
24.37
A


ATOM
1603
C
GLN
A
258
25.146
−13.364
31.589
1.00
24.53
A


ATOM
1604
O
GLN
A
258
24.791
−14.030
32.564
1.00
29.09
A


ATOM
1605
N
HIS
A
259
24.343
−13.053
30.585
1.00
22.69
A


ATOM
1606
CA
HIS
A
259
22.979
−13.524
30.533
1.00
22.57
A


ATOM
1607
CB
HIS
A
259
22.296
−13.070
29.243
1.00
19.75
A


ATOM
1608
CG
HIS
A
259
20.818
−13.316
29.235
1.00
20.16
A


ATOM
1609
CD2
HIS
A
259
19.769
−12.452
29.227
1.00
17.37
A


ATOM
1610
ND1
HIS
A
259
20.272
−14.584
29.179
1.00
19.89
A


ATOM
1611
CE1
HIS
A
259
18.954
−14.493
29.124
1.00
17.62
A


ATOM
1612
NE2
HIS
A
259
18.621
−13.212
29.156
1.00
20.17
A


ATOM
1613
C
HIS
A
259
23.143
−15.025
30.488
1.00
21.89
A


ATOM
1614
O
HIS
A
259
23.808
−15.532
29.588
1.00
21.64
A


ATOM
1615
N
PRO
A
260
22.513
−15.752
31.424
1.00
23.23
A


ATOM
1616
CD
PRO
A
260
21.576
−15.292
32.466
1.00
22.30
A


ATOM
1617
CA
PRO
A
260
22.647
−17.213
31.432
1.00
25.20
A


ATOM
1618
CB
PRO
A
260
22.000
−17.614
32.762
1.00
25.03
A


ATOM
1619
CG
PRO
A
260
20.915
−16.570
32.930
1.00
26.38
A


ATOM
1620
C
PRO
A
260
22.043
−17.957
30.225
1.00
27.63
A


ATOM
1621
O
PRO
A
260
22.445
−19.080
29.966
1.00
27.93
A


ATOM
1622
N
GLN
A
261
21.102
−17.378
29.472
1.00
27.97
A


ATOM
1623
CA
GLN
A
261
20.570
−18.137
28.316
1.00
29.82
A


ATOM
1624
CB
GLN
A
261
19.033
−18.240
28.364
1.00
31.75
A


ATOM
1625
CG
GLN
A
261
18.476
−18.970
29.589
1.00
33.93
A


ATOM
1626
CD
GLN
A
261
18.468
−18.109
30.872
1.00
40.13
A


ATOM
1627
OE1
GLN
A
261
18.531
−18.629
32.008
1.00
38.65
A


ATOM
1628
NE2
GLN
A
261
18.366
−16.795
30.695
1.00
39.37
A


ATOM
1629
C
GLN
A
261
20.985
−17.632
26.940
1.00
30.75
A


ATOM
1630
O
GLN
A
261
20.812
−18.343
25.939
1.00
32.79
A


ATOM
1631
N
LEU
A
262
21.517
−16.404
26.880
1.00
31.46
A


ATOM
1632
CA
LEU
A
262
21.965
−15.784
25.621
1.00
28.88
A


ATOM
1633
CB
LEU
A
262
21.118
−14.549
25.329
1.00
29.37
A


ATOM
1634
CG
LEU
A
262
19.627
−14.879
25.161
1.00
28.53
A


ATOM
1635
CD1
LEU
A
262
18.802
−13.598
25.265
1.00
28.91
A


ATOM
1636
CD2
LEU
A
262
19.406
−15.562
23.819
1.00
27.64
A


ATOM
1637
C
LEU
A
262
23.407
−15.369
25.766
1.00
29.36
A


ATOM
1638
O
LEU
A
262
23.693
−14.333
26.380
1.00
33.16
A


ATOM
1639
N
PRO
A
263
24.347
−16.133
25.175
1.00
29.27
A


ATOM
1640
CD
PRO
A
263
24.175
−17.356
24.377
1.00
28.75
A


ATOM
1641
CA
PRO
A
263
25.773
−15.794
25.285
1.00
28.84
A


ATOM
1642
CB
PRO
A
263
26.467
−16.905
24.487
1.00
28.05
A


ATOM
1643
CG
PRO
A
263
25.495
−18.045
24.616
1.00
30.83
A


ATOM
1644
C
PRO
A
263
26.185
−14.410
24.808
1.00
27.41
A


ATOM
1645
O
PRO
A
263
27.055
−13.771
25.425
1.00
27.57
A


ATOM
1646
N
HIS
A
264
25.558
−13.934
23.740
1.00
25.61
A


ATOM
1647
CA
HIS
A
264
25.921
−12.616
23.194
1.00
26.98
A


ATOM
1648
CB
HIS
A
264
25.252
−12.399
21.816
1.00
28.12
A


ATOM
1649
CG
HIS
A
264
23.783
−12.060
21.868
1.00
29.00
A


ATOM
1650
CD2
HIS
A
264
23.145
−10.860
21.825
1.00
27.83
A


ATOM
1651
ND1
HIS
A
264
22.788
−13.018
21.924
1.00
26.68
A


ATOM
1652
CE1
HIS
A
264
21.607
−12.426
21.910
1.00
26.97
A


ATOM
1653
NE2
HIS
A
264
21.795
−11.117
21.850
1.00
27.70
A


ATOM
1654
C
HIS
A
264
25.622
−11.420
24.110
1.00
26.42
A


ATOM
1655
O
HIS
A
264
26.113
−10.326
23.865
1.00
29.11
A


ATOM
1656
N
ILE
A
265
24.819
−11.614
25.155
1.00
23.38
A


ATOM
1657
CA
ILE
A
265
24.496
−10.520
26.053
1.00
23.73
A


ATOM
1658
CB
ILE
A
265
22.998
−10.500
26.396
1.00
21.86
A


ATOM
1659
CG2
ILE
A
265
22.694
−9.330
27.322
1.00
22.67
A


ATOM
1660
CG1
ILE
A
265
22.176
−10.294
25.106
1.00
23.22
A


ATOM
1661
CD1
ILE
A
265
20.626
−10.297
25.309
1.00
18.57
A


ATOM
1662
C
ILE
A
265
25.359
−10.597
27.304
1.00
26.04
A


ATOM
1663
O
ILE
A
265
25.082
−11.363
28.247
1.00
25.64
A


ATOM
1664
N
ASN
A
266
26.390
−9.755
27.309
1.00
26.84
A


ATOM
1665
CA
ASN
A
266
27.389
−9.742
28.373
1.00
28.18
A


ATOM
1666
CB
ASN
A
266
28.527
−10.684
27.959
1.00
29.99
A


ATOM
1667
CG
ASN
A
266
29.026
−10.392
26.554
1.00
31.62
A


ATOM
1668
OD1
ASN
A
266
29.123
−11.290
25.717
1.00
37.75
A


ATOM
1669
ND2
ASN
A
266
29.328
−9.145
26.286
1.00
29.47
A


ATOM
1670
C
ASN
A
266
27.994
−8.390
28.769
1.00
27.92
A


ATOM
1671
O
ASN
A
266
29.180
−8.325
29.137
1.00
25.80
A


ATOM
1672
N
THR
A
267
27.206
−7.317
28.659
1.00
26.94
A


ATOM
1673
CA
THR
A
267
27.637
−5.997
29.088
1.00
25.81
A


ATOM
1674
CB
THR
A
267
28.156
−5.103
27.938
1.00
26.99
A


ATOM
1675
OG1
THR
A
267
27.180
−5.045
26.894
1.00
24.87
A


ATOM
1676
CG2
THR
A
267
29.452
−5.650
27.386
1.00
29.83
A


ATOM
1677
C
THR
A
267
26.433
−5.311
29.670
1.00
25.85
A


ATOM
1678
O
THR
A
267
25.296
−5.709
29.401
1.00
24.26
A


ATOM
1679
N
VAL
A
268
26.679
−4.306
30.504
1.00
25.30
A


ATOM
1680
CA
VAL
A
268
25.598
−3.528
31.059
1.00
23.45
A


ATOM
1681
CB
VAL
A
268
25.900
−3.048
32.484
1.00
24.54
A


ATOM
1682
CG1
VAL
A
268
24.754
−2.188
32.973
1.00
21.26
A


ATOM
1683
CG2
VAL
A
268
26.056
−4.222
33.429
1.00
22.47
A


ATOM
1684
C
VAL
A
268
25.530
−2.328
30.096
1.00
25.88
A


ATOM
1685
O
VAL
A
268
26.508
−1.572
29.948
1.00
23.19
A


ATOM
1686
N
ASP
A
269
24.381
−2.173
29.433
1.00
23.34
A


ATOM
1687
CA
ASP
A
269
24.184
−1.123
28.421
1.00
22.13
A


ATOM
1688
CB
ASP
A
269
23.485
−1.738
27.182
1.00
24.25
A


ATOM
1689
CG
ASP
A
269
24.340
−2.781
26.487
1.00
29.46
A


ATOM
1690
OD1
ASP
A
269
25.534
−2.837
26.841
1.00
32.96
A


ATOM
1691
OD2
ASP
A
269
23.848
−3.542
25.598
1.00
29.89
A


ATOM
1692
C
ASP
A
269
23.392
0.109
28.870
1.00
19.52
A


ATOM
1693
O
ASP
A
269
23.433
1.145
28.217
1.00
19.36
A


ATOM
1694
N
CYS
A
270
22.665
0.011
29.967
1.00
17.24
A


ATOM
1695
CA
CYS
A
270
21.867
1.142
30.414
1.00
17.72
A


ATOM
1696
CB
CYS
A
270
20.392
0.861
30.112
1.00
16.25
A


ATOM
1697
SG
CYS
A
270
20.107
0.226
28.435
1.00
23.39
A


ATOM
1698
C
CYS
A
270
21.999
1.362
31.914
1.00
18.33
A


ATOM
1699
O
CYS
A
270
22.222
0.406
32.650
1.00
17.53
A


ATOM
1700
N
VAL
A
271
21.797
2.605
32.355
1.00
18.64
A


ATOM
1701
CA
VAL
A
271
21.811
2.955
33.788
1.00
17.75
A


ATOM
1702
CB
VAL
A
271
22.991
3.950
34.145
1.00
16.37
A


ATOM
1703
CG1
VAL
A
271
22.861
4.502
35.546
1.00
14.51
A


ATOM
1704
CG2
VAL
A
271
24.284
3.250
33.981
1.00
18.13
A


ATOM
1705
C
VAL
A
271
20.473
3.623
34.058
1.00
16.20
A


ATOM
1706
O
VAL
A
271
20.128
4.601
33.438
1.00
21.87
A


ATOM
1707
N
GLU
A
272
19.724
3.091
34.998
1.00
17.20
A


ATOM
1708
CA
GLU
A
272
18.417
3.589
35.373
1.00
14.82
A


ATOM
1709
CB
GLU
A
272
17.468
2.384
35.508
1.00
14.38
A


ATOM
1710
CG
GLU
A
272
16.096
2.705
35.949
1.00
14.85
A


ATOM
1711
CD
GLU
A
272
15.239
1.481
36.007
1.00
18.26
A


ATOM
1712
OE1
GLU
A
272
15.439
0.581
35.161
1.00
23.67
A


ATOM
1713
OE2
GLU
A
272
14.361
1.399
36.886
1.00
18.99
A


ATOM
1714
C
GLU
A
272
18.581
4.275
36.715
1.00
20.19
A


ATOM
1715
O
GLU
A
272
18.952
3.621
37.717
1.00
20.75
A


ATOM
1716
N
ILE
A
273
18.334
5.587
36.750
1.00
20.33
A


ATOM
1717
CA
ILE
A
273
18.446
6.365
37.978
1.00
19.63
A


ATOM
1718
CB
ILE
A
273
19.185
7.665
37.698
1.00
20.13
A


ATOM
1719
CG2
ILE
A
273
19.135
8.571
38.944
1.00
18.48
A


ATOM
1720
CG1
ILE
A
273
20.544
7.307
37.107
1.00
17.74
A


ATOM
1721
CD1
ILE
A
273
21.391
8.488
36.553
1.00
17.08
A


ATOM
1722
C
ILE
A
273
17.036
6.659
38.443
1.00
22.46
A


ATOM
1723
O
ILE
A
273
16.252
7.239
37.701
1.00
21.95
A


ATOM
1724
N
TYR
A
274
16.672
6.279
39.663
1.00
20.99
A


ATOM
1725
CA
TYR
A
274
15.296
6.528
40.032
1.00
22.00
A


ATOM
1726
CB
TYR
A
274
14.530
5.197
40.175
1.00
21.54
A


ATOM
1727
CG
TYR
A
274
14.929
4.416
41.395
1.00
24.87
A


ATOM
1728
CD1
TYR
A
274
14.190
4.510
42.590
1.00
26.54
A


ATOM
1729
CE1
TYR
A
274
14.583
3.802
43.737
1.00
26.46
A


ATOM
1730
CD2
TYR
A
274
16.069
3.609
41.372
1.00
26.21
A


ATOM
1731
CE2
TYR
A
274
16.475
2.910
42.497
1.00
29.43
A


ATOM
1732
CZ
TYR
A
274
15.729
3.007
43.674
1.00
29.69
A


ATOM
1733
OH
TYR
A
274
16.159
2.287
44.775
1.00
34.48
A


ATOM
1734
C
TYR
A
274
15.156
7.344
41.285
1.00
23.82
A


ATOM
1735
O
TYR
A
274
16.104
7.506
42.076
1.00
24.77
A


ATOM
1736
N
GLY
A
275
13.945
7.831
41.475
1.00
24.36
A


ATOM
1737
CA
GLY
A
275
13.666
8.655
42.619
1.00
25.88
A


ATOM
1738
C
GLY
A
275
12.171
8.729
42.786
1.00
26.08
A


ATOM
1739
O
GLY
A
275
11.430
8.131
42.023
1.00
25.15
A


ATOM
1740
N
PRO
A
276
11.700
9.481
43.780
1.00
26.94
A


ATOM
1741
CD
PRO
A
276
12.506
10.426
44.574
1.00
27.05
A


ATOM
1742
CA
PRO
A
276
10.274
9.636
44.072
1.00
27.66
A


ATOM
1743
CB
PRO
A
276
10.264
10.579
45.286
1.00
29.39
A


ATOM
1744
CG
PRO
A
276
11.697
10.455
45.868
1.00
29.74
A


ATOM
1745
C
PRO
A
276
9.508
10.226
42.885
1.00
30.26
A


ATOM
1746
O
PRO
A
276
10.034
11.045
42.143
1.00
28.59
A


ATOM
1747
N
PRO
A
277
8.239
9.841
42.727
1.00
31.13
A


ATOM
1748
CD
PRO
A
277
7.480
9.015
43.690
1.00
30.88
A


ATOM
1749
CA
PRO
A
277
7.376
10.308
41.641
1.00
32.26
A


ATOM
1750
CB
PRO
A
277
6.197
9.356
41.713
1.00
31.83
A


ATOM
1751
CG
PRO
A
277
6.017
9.233
43.242
1.00
32.56
A


ATOM
1752
C
PRO
A
277
6.923
11.746
41.815
1.00
35.37
A


ATOM
1753
O
PRO
A
277
6.830
12.249
42.939
1.00
36.26
A


ATOM
1754
N
THR
A
278
6.664
12.409
40.695
1.00
35.39
A


ATOM
1755
CA
THR
A
278
6.169
13.772
40.703
1.00
35.85
A


ATOM
1756
CB
THR
A
278
6.768
14.592
39.570
1.00
37.14
A


ATOM
1757
OG1
THR
A
278
8.189
14.665
39.732
1.00
40.01
A


ATOM
1758
CG2
THR
A
278
6.167
15.980
39.544
1.00
36.22
A


ATOM
1759
C
THR
A
278
4.685
13.568
40.467
1.00
35.62
A


ATOM
1760
O
THR
A
278
3.866
14.107
41.181
1.00
35.55
A


ATOM
1761
N
ASN
A
279
4.338
12.738
39.486
1.00
36.85
A


ATOM
1762
CA
ASN
A
279
2.930
12.468
39.205
1.00
37.04
A


ATOM
1763
CB
ASN
A
279
2.790
11.824
37.837
1.00
37.56
A


ATOM
1764
CG
ASN
A
279
1.367
11.607
37.442
1.00
36.56
A


ATOM
1765
OD1
ASN
A
279
0.550
11.120
38.224
1.00
39.17
A


ATOM
1766
ND2
ASN
A
279
1.053
11.956
36.210
1.00
35.92
A


ATOM
1767
C
ASN
A
279
2.306
11.549
40.259
1.00
40.11
A


ATOM
1768
O
ASN
A
279
2.794
10.442
40.515
1.00
39.15
A


ATOM
1769
N
ALA
A
280
1.209
12.023
40.850
1.00
43.01
A


ATOM
1770
CA
ALA
A
280
0.438
11.306
41.867
1.00
42.19
A


ATOM
1771
CB
ALA
A
280
−0.907
12.034
42.046
1.00
41.76
A


ATOM
1772
C
ALA
A
280
0.172
9.810
41.561
1.00
41.12
A


ATOM
1773
O
ALA
A
280
0.237
8.954
42.453
1.00
41.34
A


ATOM
1774
N
ALA
A
281
−0.133
9.509
40.298
1.00
38.84
A


ATOM
1775
CA
ALA
A
281
−0.456
8.153
39.855
1.00
34.05
A


ATOM
1776
CB
ALA
A
281
−1.221
8.231
38.531
1.00
36.24
A


ATOM
1777
C
ALA
A
281
0.715
7.180
39.714
1.00
32.61
A


ATOM
1778
O
ALA
A
281
0.502
5.978
39.588
1.00
34.54
A


ATOM
1779
N
ALA
A
282
1.938
7.689
39.738
1.00
30.16
A


ATOM
1780
CA
ALA
A
282
3.145
6.872
39.594
1.00
28.98
A


ATOM
1781
CB
ALA
A
282
4.161
7.612
38.771
1.00
24.92
A


ATOM
1782
C
ALA
A
282
3.809
6.441
40.913
1.00
30.47
A


ATOM
1783
O
ALA
A
282
3.811
7.164
41.908
1.00
28.03
A


ATOM
1784
N
ASN
A
283
4.429
5.268
40.870
1.00
28.97
A


ATOM
1785
CA
ASN
A
283
5.105
4.709
42.014
1.00
27.62
A


ATOM
1786
CB
ASN
A
283
5.194
3.194
41.826
1.00
26.90
A


ATOM
1787
CG
ASN
A
283
3.842
2.548
41.886
1.00
29.65
A


ATOM
1788
OD1
ASN
A
283
3.273
2.393
42.982
1.00
32.86
A


ATOM
1789
ND2
ASN
A
283
3.278
2.203
40.724
1.00
22.77
A


ATOM
1790
C
ASN
A
283
6.478
5.338
42.197
1.00
28.79
A


ATOM
1791
O
ASN
A
283
6.897
5.609
43.325
1.00
29.55
A


ATOM
1792
N
TYR
A
284
7.159
5.606
41.085
1.00
27.44
A


ATOM
1793
CA
TYR
A
284
8.500
6.196
41.084
1.00
25.24
A


ATOM
1794
CB
TYR
A
284
9.566
5.107
41.128
1.00
27.49
A


ATOM
1795
CG
TYR
A
284
9.621
4.316
42.400
1.00
31.90
A


ATOM
1796
CD1
TYR
A
284
10.224
4.853
43.547
1.00
33.90
A


ATOM
1797
CE1
TYR
A
284
10.237
4.156
44.742
1.00
36.62
A


ATOM
1798
CD2
TYR
A
284
9.035
3.056
42.481
1.00
31.89
A


ATOM
1799
CE2
TYR
A
284
9.037
2.340
43.670
1.00
36.37
A


ATOM
1800
CZ
TYR
A
284
9.642
2.899
44.806
1.00
39.52
A


ATOM
1801
OH
TYR
A
284
9.641
2.218
46.008
1.00
40.61
A


ATOM
1802
C
TYR
A
284
8.717
6.951
39.789
1.00
24.14
A


ATOM
1803
O
TYR
A
284
7.943
6.821
38.835
1.00
21.53
A


ATOM
1804
N
LYS
A
285
9.818
7.690
39.736
1.00
23.69
A


ATOM
1805
CA
LYS
A
285
10.191
8.422
38.530
1.00
23.08
A


ATOM
1806
CB
LYS
A
285
10.246
9.916
38.815
1.00
26.03
A


ATOM
1807
CG
LYS
A
285
10.760
10.738
37.667
1.00
31.12
A


ATOM
1808
CD
LYS
A
285
11.190
12.168
38.080
1.00
31.68
A


ATOM
1809
CE
LYS
A
285
10.052
13.061
38.489
1.00
33.32
A


ATOM
1810
NZ
LYS
A
285
10.425
14.504
38.222
1.00
30.04
A


ATOM
1811
C
LYS
A
285
11.578
7.937
38.151
1.00
22.32
A


ATOM
1812
O
LYS
A
285
12.337
7.486
39.020
1.00
22.03
A


ATOM
1813
N
ASN
A
286
11.925
7.975
36.870
1.00
17.42
A


ATOM
1814
CA
ASN
A
286
13.275
7.598
36.530
1.00
16.88
A


ATOM
1815
CB
ASN
A
286
13.399
6.079
36.404
1.00
19.06
A


ATOM
1816
CG
ASN
A
286
12.946
5.571
35.029
1.00
18.80
A


ATOM
1817
OD1
ASN
A
286
11.760
5.440
34.756
1.00
19.90
A


ATOM
1818
ND2
ASN
A
286
13.884
5.322
34.182
1.00
14.52
A


ATOM
1819
C
ASN
A
286
13.768
8.201
35.250
1.00
17.89
A


ATOM
1820
O
ASN
A
286
12.996
8.712
34.448
1.00
17.84
A


ATOM
1821
N
VAL
A
287
15.079
8.165
35.060
1.00
20.96
A


ATOM
1822
CA
VAL
A
287
15.629
8.583
33.788
1.00
20.28
A


ATOM
1823
CB
VAL
A
287
16.283
9.987
33.799
1.00
21.60
A


ATOM
1824
CG1
VAL
A
287
17.447
10.041
34.799
1.00
22.48
A


ATOM
1825
CG2
VAL
A
287
16.848
10.275
32.371
1.00
20.79
A


ATOM
1826
C
VAL
A
287
16.672
7.511
33.510
1.00
19.85
A


ATOM
1827
O
VAL
A
287
17.397
7.084
34.406
1.00
20.21
A


ATOM
1828
N
VAL
A
288
16.706
7.016
32.284
1.00
17.36
A


ATOM
1829
CA
VAL
A
288
17.680
6.007
31.901
1.00
14.40
A


ATOM
1830
CB
VAL
A
288
16.981
4.835
31.182
1.00
15.48
A


ATOM
1831
CG1
VAL
A
288
18.009
3.953
30.479
1.00
17.37
A


ATOM
1832
CG2
VAL
A
288
16.147
4.049
32.149
1.00
12.26
A


ATOM
1833
C
VAL
A
288
18.704
6.660
30.959
1.00
18.84
A


ATOM
1834
O
VAL
A
288
18.327
7.341
29.988
1.00
15.71
A


ATOM
1835
N
ILE
A
289
19.989
6.430
31.248
1.00
19.59
A


ATOM
1836
CA
ILE
A
289
21.105
6.942
30.469
1.00
19.86
A


ATOM
1837
CB
ILE
A
289
22.198
7.533
31.390
1.00
22.17
A


ATOM
1838
CG2
ILE
A
289
23.273
8.209
30.563
1.00
22.19
A


ATOM
1839
CG1
ILE
A
289
21.563
8.503
32.394
1.00
23.89
A


ATOM
1840
CD1
ILE
A
289
20.819
9.680
31.767
1.00
25.27
A


ATOM
1841
C
ILE
A
289
21.696
5.775
29.692
1.00
19.13
A


ATOM
1842
O
ILE
A
289
22.042
4.752
30.280
1.00
17.93
A


ATOM
1843
N
PHE
A
290
21.836
5.930
28.373
1.00
18.30
A


ATOM
1844
CA
PHE
A
290
22.357
4.852
27.542
1.00
18.38
A


ATOM
1845
CB
PHE
A
290
21.197
3.883
27.213
1.00
17.27
A


ATOM
1846
CG
PHE
A
290
20.120
4.493
26.342
1.00
16.26
A


ATOM
1847
CD1
PHE
A
290
20.093
4.231
24.965
1.00
14.12
A


ATOM
1848
CD2
PHE
A
290
19.180
5.373
26.882
1.00
13.82
A


ATOM
1849
CE1
PHE
A
290
19.120
4.860
24.125
1.00
15.22
A


ATOM
1850
CE2
PHE
A
290
18.213
5.998
26.065
1.00
18.66
A


ATOM
1851
CZ
PHE
A
290
18.196
5.726
24.665
1.00
14.09
A


ATOM
1852
C
PHE
A
290
22.964
5.426
26.275
1.00
21.43
A


ATOM
1853
O
PHE
A
290
23.087
6.648
26.147
1.00
23.12
A


ATOM
1854
N
GLY
A
291
23.377
4.568
25.347
1.00
22.25
A


ATOM
1855
CA
GLY
A
291
23.956
5.064
24.099
1.00
23.92
A


ATOM
1856
C
GLY
A
291
25.146
5.987
24.330
1.00
25.52
A


ATOM
1857
O
GLY
A
291
25.970
5.682
25.205
1.00
25.30
A


ATOM
1858
N
ASN
A
292
25.276
7.086
23.571
1.00
21.04
A


ATOM
1859
CA
ASN
A
292
26.392
8.032
23.795
1.00
22.18
A


ATOM
1860
CB
ASN
A
292
26.808
8.647
22.457
1.00
25.00
A


ATOM
1861
CG
ASN
A
292
27.985
9.594
22.585
1.00
30.83
A


ATOM
1862
OD1
ASN
A
292
28.708
9.551
23.559
1.00
27.52
A


ATOM
1863
ND2
ASN
A
292
28.171
10.462
21.584
1.00
32.23
A


ATOM
1864
C
ASN
A
292
25.804
9.064
24.802
1.00
23.69
A


ATOM
1865
O
ASN
A
292
25.537
10.238
24.489
1.00
19.53
A


ATOM
1866
N
ARG
A
293
25.643
8.579
26.038
1.00
20.48
A


ATOM
1867
CA
ARG
A
293
24.988
9.281
27.130
1.00
21.42
A


ATOM
1868
CB
ARG
A
293
25.959
10.057
28.070
1.00
22.90
A


ATOM
1869
CG
ARG
A
293
26.918
11.034
27.517
1.00
27.98
A


ATOM
1870
CD
ARG
A
293
27.667
11.715
28.695
1.00
29.22
A


ATOM
1871
NE
ARG
A
293
28.257
12.992
28.297
1.00
30.64
A


ATOM
1872
CZ
ARG
A
293
29.248
13.127
27.413
1.00
27.57
A


ATOM
1873
NH1
ARG
A
293
29.785
12.074
26.828
1.00
23.78
A


ATOM
1874
NH2
ARG
A
293
29.684
14.336
27.079
1.00
30.48
A


ATOM
1875
C
ARG
A
293
23.767
10.122
26.747
1.00
21.38
A


ATOM
1876
O
ARG
A
293
23.639
11.296
27.091
1.00
22.12
A


ATOM
1877
N
GLN
A
294
22.830
9.478
26.049
1.00
19.61
A


ATOM
1878
CA
GLN
A
294
21.574
10.141
25.734
1.00
15.56
A


ATOM
1879
CB
GLN
A
294
21.047
9.649
24.378
1.00
16.96
A


ATOM
1880
CG
GLN
A
294
20.766
8.153
24.240
1.00
12.45
A


ATOM
1881
CD
GLN
A
294
20.403
7.794
22.806
1.00
16.44
A


ATOM
1882
OE1
GLN
A
294
21.250
7.319
22.022
1.00
19.24
A


ATOM
1883
NE2
GLN
A
294
19.130
8.052
22.444
1.00
15.52
A


ATOM
1884
C
GLN
A
294
20.667
9.727
26.899
1.00
16.98
A


ATOM
1885
O
GLN
A
294
21.023
8.831
27.666
1.00
16.47
A


ATOM
1886
N
ALA
A
295
19.522
10.377
27.068
1.00
16.71
A


ATOM
1887
CA
ALA
A
295
18.610
10.055
28.150
1.00
15.79
A


ATOM
1888
CB
ALA
A
295
18.397
11.274
29.040
1.00
14.11
A


ATOM
1889
C
ALA
A
295
17.292
9.703
27.503
1.00
17.48
A


ATOM
1890
O
ALA
A
295
16.907
10.343
26.531
1.00
17.63
A


ATOM
1891
N
ASP
A
296
16.597
8.715
28.058
1.00
16.47
A


ATOM
1892
CA
ASP
A
296
15.311
8.300
27.568
1.00
16.57
A


ATOM
1893
CB
ASP
A
296
14.976
6.921
28.137
1.00
18.10
A


ATOM
1894
CG
ASP
A
296
13.747
6.250
27.473
1.00
22.91
A


ATOM
1895
OD1
ASP
A
296
13.014
6.920
26.684
1.00
18.88
A


ATOM
1896
OD2
ASP
A
296
13.527
5.038
27.776
1.00
21.05
A


ATOM
1897
C
ASP
A
296
14.296
9.314
28.074
1.00
18.63
A


ATOM
1898
O
ASP
A
296
14.295
9.634
29.256
1.00
18.09
A


ATOM
1899
N
ARG
A
297
13.425
9.813
27.186
1.00
14.83
A


ATOM
1900
CA
ARG
A
297
12.357
10.733
27.579
1.00
13.48
A


ATOM
1901
CB
ARG
A
297
11.950
11.644
26.392
1.00
15.86
A


ATOM
1902
CG
ARG
A
297
12.986
12.719
26.071
1.00
13.58
A


ATOM
1903
CD
ARG
A
297
14.068
12.262
25.140
1.00
17.33
A


ATOM
1904
NE
ARG
A
297
14.810
13.446
24.741
1.00
15.75
A


ATOM
1905
CZ
ARG
A
297
15.910
13.909
25.340
1.00
20.23
A


ATOM
1906
NH1
ARG
A
297
16.468
13.261
26.389
1.00
13.67
A


ATOM
1907
NH2
ARG
A
297
16.406
15.081
24.941
1.00
13.96
A


ATOM
1908
C
ARG
A
297
11.148
9.944
28.047
1.00
12.76
A


ATOM
1909
O
ARG
A
297
10.257
10.502
28.686
1.00
12.35
A


ATOM
1910
N
SER
A
298
11.071
8.652
27.690
1.00
12.87
A


ATOM
1911
CA
SER
A
298
9.948
7.820
28.150
1.00
11.04
A


ATOM
1912
CB
SER
A
298
9.624
6.673
27.156
1.00
11.56
A


ATOM
1913
OG
SER
A
298
10.543
5.567
27.271
1.00
13.30
A


ATOM
1914
C
SER
A
298
10.415
7.173
29.445
1.00
13.44
A


ATOM
1915
O
SER
A
298
11.602
7.272
29.804
1.00
15.33
A


ATOM
1916
N
PRO
A
299
9.506
6.485
30.152
1.00
14.80
A


ATOM
1917
CD
PRO
A
299
8.049
6.508
29.913
1.00
11.75
A


ATOM
1918
CA
PRO
A
299
9.826
5.795
31.425
1.00
15.88
A


ATOM
1919
CB
PRO
A
299
8.472
5.337
31.922
1.00
15.36
A


ATOM
1920
CG
PRO
A
299
7.511
6.373
31.306
1.00
17.10
A


ATOM
1921
C
PRO
A
299
10.780
4.601
31.203
1.00
19.82
A


ATOM
1922
O
PRO
A
299
11.376
4.094
32.171
1.00
19.55
A


ATOM
1923
N
CYS
A
300
10.965
4.203
29.935
1.00
15.95
A


ATOM
1924
CA
CYS
A
300
11.850
3.091
29.530
1.00
16.95
A


ATOM
1925
CB
CYS
A
300
13.208
3.147
30.248
1.00
15.86
A


ATOM
1926
SG
CYS
A
300
14.450
2.046
29.512
1.00
20.02
A


ATOM
1927
C
CYS
A
300
11.178
1.763
29.815
1.00
18.14
A


ATOM
1928
O
CYS
A
300
10.962
1.407
30.972
1.00
19.63
A


ATOM
1929
N
GLY
A
301
10.850
1.031
28.754
1.00
15.84
A


ATOM
1930
CA
GLY
A
301
10.142
−0.230
28.893
1.00
14.34
A


ATOM
1931
C
GLY
A
301
11.011
−1.358
29.428
1.00
15.88
A


ATOM
1932
O
GLY
A
301
10.552
−2.130
30.258
1.00
16.82
A


ATOM
1933
N
THR
A
302
12.243
−1.490
28.942
1.00
15.36
A


ATOM
1934
CA
THR
A
302
13.099
−2.539
29.451
1.00
15.43
A


ATOM
1935
CB
THR
A
302
14.307
−2.839
28.488
1.00
14.86
A


ATOM
1936
OG1
THR
A
302
15.120
−1.677
28.299
1.00
13.76
A


ATOM
1937
CG2
THR
A
302
13.793
−3.288
27.066
1.00
14.81
A


ATOM
1938
C
THR
A
302
13.546
−2.140
30.887
1.00
17.35
A


ATOM
1939
O
THR
A
302
13.701
−2.996
31.746
1.00
20.05
A


ATOM
1940
N
GLY
A
303
13.717
−0.851
31.148
1.00
17.14
A


ATOM
1941
CA
GLY
A
303
14.105
−0.408
32.479
1.00
19.74
A


ATOM
1942
C
GLY
A
303
12.953
−0.617
33.436
1.00
20.64
A


ATOM
1943
O
GLY
A
303
13.152
−0.885
34.623
1.00
20.62
A


ATOM
1944
N
THR
A
304
11.723
−0.509
32.929
1.00
17.17
A


ATOM
1945
CA
THR
A
304
10.582
−0.715
33.759
1.00
15.86
A


ATOM
1946
CB
THR
A
304
9.272
−0.241
33.089
1.00
18.98
A


ATOM
1947
OG1
THR
A
304
9.254
1.197
32.985
1.00
17.47
A


ATOM
1948
CG2
THR
A
304
8.097
−0.646
33.901
1.00
16.75
A


ATOM
1949
C
THR
A
304
10.539
−2.216
34.068
1.00
20.55
A


ATOM
1950
O
THR
A
304
10.235
−2.607
35.206
1.00
17.94
A


ATOM
1951
N
SER
A
305
10.861
−3.063
33.088
1.00
19.20
A


ATOM
1952
CA
SER
A
305
10.866
−4.511
33.334
1.00
21.24
A


ATOM
1953
CB
SER
A
305
11.150
−5.325
32.059
1.00
20.30
A


ATOM
1954
OG
SER
A
305
10.160
−5.061
31.113
1.00
25.75
A


ATOM
1955
C
SER
A
305
11.922
−4.914
34.349
1.00
19.43
A


ATOM
1956
O
SER
A
305
11.672
−5.773
35.204
1.00
19.19
A


ATOM
1957
N
ALA
A
306
13.109
−4.324
34.244
1.00
17.52
A


ATOM
1958
CA
ALA
A
306
14.202
−4.676
35.181
1.00
17.97
A


ATOM
1959
CB
ALA
A
306
15.531
−4.017
34.751
1.00
14.00
A


ATOM
1960
C
ALA
A
306
13.813
−4.228
36.564
1.00
19.14
A


ATOM
1961
O
ALA
A
306
14.084
−4.929
37.550
1.00
20.34
A


ATOM
1962
N
LYS
A
307
13.153
−3.070
36.651
1.00
19.53
A


ATOM
1963
CA
LYS
A
307
12.728
−2.549
37.946
1.00
18.39
A


ATOM
1964
CB
LYS
A
307
12.181
−1.125
37.827
1.00
19.79
A


ATOM
1965
CG
LYS
A
307
11.719
−0.476
39.166
1.00
20.72
A


ATOM
1966
CD
LYS
A
307
12.893
−0.148
40.071
1.00
22.15
A


ATOM
1967
CE
LYS
A
307
12.404
0.574
41.320
1.00
26.69
A


ATOM
1968
NZ
LYS
A
307
13.566
1.007
42.204
1.00
29.70
A


ATOM
1969
C
LYS
A
307
11.691
−3.443
38.604
1.00
21.93
A


ATOM
1970
O
LYS
A
307
11.830
−3.746
39.802
1.00
20.75
A


ATOM
1971
N
MET
A
308
10.646
−3.840
37.851
1.00
17.19
A


ATOM
1972
CA
MET
A
308
9.608
−4.708
38.359
1.00
18.29
A


ATOM
1973
CB
MET
A
308
8.438
−4.910
37.357
1.00
16.54
A


ATOM
1974
CG
MET
A
308
7.635
−3.639
37.099
1.00
18.29
A


ATOM
1975
SD
MET
A
308
6.163
−4.045
36.086
1.00
23.99
A


ATOM
1976
CE
MET
A
308
7.003
−4.399
34.684
1.00
17.81
A


ATOM
1977
C
MET
A
308
10.179
−6.080
38.707
1.00
19.02
A


ATOM
1978
O
MET
A
308
9.690
−6.711
39.631
1.00
20.04
A


ATOM
1979
N
ALA
A
309
11.180
−6.558
37.970
1.00
17.72
A


ATOM
1980
CA
ALA
A
309
11.757
−7.855
38.302
1.00
19.75
A


ATOM
1981
CB
ALA
A
309
12.690
−8.311
37.231
1.00
14.38
A


ATOM
1982
C
ALA
A
309
12.539
−7.723
39.634
1.00
21.52
A


ATOM
1983
O
ALA
A
309
12.598
−8.664
40.400
1.00
21.56
A


ATOM
1984
N
THR
A
310
13.189
−6.582
39.852
1.00
22.35
A


ATOM
1985
CA
THR
A
310
13.935
−6.361
41.079
1.00
22.57
A


ATOM
1986
CB
THR
A
310
14.810
−5.107
41.002
1.00
21.10
A


ATOM
1987
OG1
THR
A
310
15.688
−5.259
39.900
1.00
21.25
A


ATOM
1988
CG2
THR
A
310
15.683
−4.934
42.280
1.00
19.81
A


ATOM
1989
C
THR
A
310
12.942
−6.220
42.222
1.00
23.00
A


ATOM
1990
O
THR
A
310
13.130
−6.815
43.278
1.00
25.35
A


ATOM
1991
N
LEU
A
311
11.879
−5.456
42.023
1.00
21.75
A


ATOM
1992
CA
LEU
A
311
10.886
−5.306
43.071
1.00
21.63
A


ATOM
1993
CB
LEU
A
311
9.821
−4.289
42.662
1.00
21.40
A


ATOM
1994
CG
LEU
A
311
10.257
−2.831
42.560
1.00
24.01
A


ATOM
1995
CD1
LEU
A
311
9.065
−2.006
42.131
1.00
21.73
A


ATOM
1996
CD2
LEU
A
311
10.761
−2.319
43.901
1.00
25.88
A


ATOM
1997
C
LEU
A
311
10.208
−6.661
43.406
1.00
25.01
A


ATOM
1998
O
LEU
A
311
9.961
−6.984
44.592
1.00
23.01
A


ATOM
1999
N
TYR
A
312
9.876
−7.428
42.366
1.00
22.08
A


ATOM
2000
CA
TYR
A
312
9.244
−8.724
42.529
1.00
22.17
A


ATOM
2001
CB
TYR
A
312
8.952
−9.366
41.177
1.00
20.80
A


ATOM
2002
CG
TYR
A
312
8.099
−10.600
41.303
1.00
22.27
A


ATOM
2003
CD1
TYR
A
312
6.732
−10.485
41.437
1.00
24.46
A


ATOM
2004
CE1
TYR
A
312
5.927
−11.585
41.595
1.00
26.55
A


ATOM
2005
CD2
TYR
A
312
8.661
−11.879
41.325
1.00
23.25
A


ATOM
2006
CE2
TYR
A
312
7.851
−13.021
41.483
1.00
25.77
A


ATOM
2007
CZ
TYR
A
312
6.485
−12.855
41.617
1.00
27.12
A


ATOM
2008
OH
TYR
A
312
5.617
−13.926
41.776
1.00
30.79
A


ATOM
2009
C
TYR
A
312
10.138
−9.686
43.317
1.00
22.02
A


ATOM
2010
O
TYR
A
312
9.666
−10.431
44.168
1.00
21.42
A


ATOM
2011
N
ALA
A
313
11.420
−9.691
42.998
1.00
23.34
A


ATOM
2012
CA
ALA
A
313
12.357
−10.550
43.702
1.00
24.71
A


ATOM
2013
CB
ALA
A
313
13.746
−10.451
43.074
1.00
21.96
A


ATOM
2014
C
ALA
A
313
12.397
−10.140
45.204
1.00
26.11
A


ATOM
2015
O
ALA
A
313
12.567
−11.006
46.069
1.00
27.03
A


ATOM
2016
N
LYS
A
314
12.210
−8.848
45.509
1.00
24.31
A


ATOM
2017
CA
LYS
A
314
12.248
−8.372
46.911
1.00
26.72
A


ATOM
2018
CB
LYS
A
314
12.788
−6.937
47.016
1.00
23.01
A


ATOM
2019
CG
LYS
A
314
14.216
−6.828
46.576
1.00
23.25
A


ATOM
2020
CD
LYS
A
314
14.797
−5.404
46.643
1.00
24.01
A


ATOM
2021
CE
LYS
A
314
16.179
−5.465
45.999
1.00
25.50
A


ATOM
2022
NZ
LYS
A
314
16.914
−4.157
45.860
1.00
33.57
A


ATOM
2023
C
LYS
A
314
10.913
−8.447
47.619
1.00
26.12
A


ATOM
2024
O
LYS
A
314
10.761
−7.945
48.732
1.00
30.75
A


ATOM
2025
N
GLY
A
315
9.956
−9.089
46.979
1.00
25.97
A


ATOM
2026
CA
GLY
A
315
8.632
−9.242
47.547
1.00
26.25
A


ATOM
2027
C
GLY
A
315
7.717
−8.029
47.544
1.00
29.03
A


ATOM
2028
O
GLY
A
315
6.694
−8.053
48.230
1.00
26.41
A


ATOM
2029
N
GLN
A
316
8.035
−6.990
46.769
1.00
30.10
A


ATOM
2030
CA
GLN
A
316
7.219
−5.777
46.799
1.00
32.61
A


ATOM
2031
CB
GLN
A
316
8.079
−4.517
46.712
1.00
34.46
A


ATOM
2032
CG
GLN
A
316
9.524
−4.682
47.077
1.00
42.07
A


ATOM
2033
CD
GLN
A
316
9.813
−4.340
48.520
1.00
46.90
A


ATOM
2034
OE1
GLN
A
316
8.997
−4.621
49.414
1.00
49.05
A


ATOM
2035
NE2
GLN
A
316
10.993
−3.751
48.769
1.00
45.95
A


ATOM
2036
C
GLN
A
316
6.190
−5.666
45.712
1.00
32.22
A


ATOM
2037
O
GLN
A
316
5.494
−4.669
45.637
1.00
33.69
A


ATOM
2038
N
LEU
A
317
6.064
−6.678
44.879
1.00
30.12
A


ATOM
2039
CA
LEU
A
317
5.109
−6.561
43.814
1.00
30.73
A


ATOM
2040
CB
LEU
A
317
5.884
−6.085
42.574
1.00
31.09
A


ATOM
2041
CG
LEU
A
317
5.307
−5.266
41.433
1.00
28.28
A


ATOM
2042
CD1
LEU
A
317
4.613
−4.070
41.938
1.00
23.24
A


ATOM
2043
CD2
LEU
A
317
6.452
−4.875
40.470
1.00
26.85
A


ATOM
2044
C
LEU
A
317
4.534
−7.942
43.630
1.00
32.43
A


ATOM
2045
O
LEU
A
317
5.285
−8.921
43.624
1.00
31.65
A


ATOM
2046
N
ARG
A
318
3.216
−8.064
43.510
1.00
29.97
A


ATOM
2047
CA
ARG
A
318
2.676
−9.402
43.320
1.00
31.00
A


ATOM
2048
CB
ARG
A
318
1.551
−9.758
44.361
1.00
29.39
A


ATOM
2049
CG
ARG
A
318
0.364
−8.833
44.438
1.00
28.90
A


ATOM
2050
CD
ARG
A
318
−0.689
−9.212
45.524
1.00
22.30
A


ATOM
2051
NE
ARG
A
318
−1.214
−10.593
45.475
1.00
22.48
A


ATOM
2052
CZ
ARG
A
318
−2.299
−10.990
44.793
1.00
25.15
A


ATOM
2053
NH1
ARG
A
318
−2.997
−10.113
44.054
1.00
19.70
A


ATOM
2054
NH2
ARG
A
318
−2.746
−12.250
44.922
1.00
19.22
A


ATOM
2055
C
ARG
A
318
2.166
−9.480
41.909
1.00
30.22
A


ATOM
2056
O
ARG
A
318
1.963
−8.459
41.264
1.00
33.46
A


ATOM
2057
N
ILE
A
319
2.001
−10.693
41.422
1.00
27.73
A


ATOM
2058
CA
ILE
A
319
1.504
−10.931
40.076
1.00
27.20
A


ATOM
2059
CB
ILE
A
319
1.247
−12.448
39.862
1.00
26.32
A


ATOM
2060
CG2
ILE
A
319
0.536
−12.704
38.523
1.00
28.21
A


ATOM
2061
CG1
ILE
A
319
2.560
−13.238
40.010
1.00
30.23
A


ATOM
2062
CD1
ILE
A
319
3.483
−13.203
38.843
1.00
28.53
A


ATOM
2063
C
ILE
A
319
0.190
−10.147
39.798
1.00
26.87
A


ATOM
2064
O
ILE
A
319
−0.769
−10.199
40.568
1.00
27.43
A


ATOM
2065
N
GLY
A
320
0.158
−9.440
38.677
1.00
25.19
A


ATOM
2066
CA
GLY
A
320
−1.036
−8.719
38.284
1.00
24.49
A


ATOM
2067
C
GLY
A
320
−1.101
−7.329
38.835
1.00
21.71
A


ATOM
2068
O
GLY
A
320
−1.921
−6.541
38.409
1.00
22.68
A


ATOM
2069
N
GLU
A
321
−0.237
−7.024
39.787
1.00
21.52
A


ATOM
2070
CA
GLU
A
321
−0.225
−5.702
40.385
1.00
21.14
A


ATOM
2071
CB
GLU
A
321
0.628
−5.688
41.652
1.00
19.03
A


ATOM
2072
CG
GLU
A
321
0.470
−4.405
42.476
1.00
23.27
A


ATOM
2073
CD
GLU
A
321
1.325
−4.412
43.754
1.00
27.85
A


ATOM
2074
OE1
GLU
A
321
1.555
−3.317
44.347
1.00
29.39
A


ATOM
2075
OE2
GLU
A
321
1.763
−5.519
44.151
1.00
27.03
A


ATOM
2076
C
GLU
A
321
0.333
−4.650
39.408
1.00
20.70
A


ATOM
2077
O
GLU
A
321
1.438
−4.785
38.875
1.00
19.53
A


ATOM
2078
N
THR
A
322
−0.411
−3.582
39.206
1.00
20.24
A


ATOM
2079
CA
THR
A
322
0.068
−2.555
38.288
1.00
20.95
A


ATOM
2080
CB
THR
A
322
−1.091
−1.639
37.822
1.00
19.80
A


ATOM
2081
OG1
THR
A
322
−2.014
−2.393
37.016
1.00
21.59
A


ATOM
2082
CG2
THR
A
322
−0.544
−0.455
37.017
1.00
21.75
A


ATOM
2083
C
THR
A
322
1.127
−1.680
38.957
1.00
20.24
A


ATOM
2084
O
THR
A
322
0.922
−1.190
40.054
1.00
22.77
A


ATOM
2085
N
PHE
A
323
2.238
−1.478
38.266
1.00
19.40
A


ATOM
2086
CA
PHE
A
323
3.325
−0.621
38.705
1.00
20.91
A


ATOM
2087
CB
PHE
A
323
4.616
−1.420
38.649
1.00
18.66
A


ATOM
2088
CG
PHE
A
323
5.832
−0.624
38.915
1.00
20.61
A


ATOM
2089
CD1
PHE
A
323
6.154
−0.219
40.223
1.00
20.46
A


ATOM
2090
CD2
PHE
A
323
6.667
−0.265
37.872
1.00
20.38
A


ATOM
2091
CE1
PHE
A
323
7.282
0.522
40.466
1.00
20.48
A


ATOM
2092
CE2
PHE
A
323
7.808
0.494
38.108
1.00
21.91
A


ATOM
2093
CZ
PHE
A
323
8.121
0.889
39.413
1.00
24.48
A


ATOM
2094
C
PHE
A
323
3.340
0.539
37.669
1.00
21.08
A


ATOM
2095
O
PHE
A
323
3.239
0.300
36.460
1.00
19.64
A


ATOM
2096
N
VAL
A
324
3.445
1.784
38.129
1.00
20.22
A


ATOM
2097
CA
VAL
A
324
3.432
2.927
37.211
1.00
17.99
A


ATOM
2098
CB
VAL
A
324
2.215
3.894
37.501
1.00
19.55
A


ATOM
2099
CG1
VAL
A
324
2.198
5.053
36.505
1.00
17.30
A


ATOM
2100
CG2
VAL
A
324
0.881
3.154
37.390
1.00
15.69
A


ATOM
2101
C
VAL
A
324
4.752
3.648
37.371
1.00
20.30
A


ATOM
2102
O
VAL
A
324
5.146
4.066
38.485
1.00
18.30
A


ATOM
2103
N
TYR
A
325
5.472
3.755
36.257
1.00
16.62
A


ATOM
2104
CA
TYR
A
325
6.764
4.419
36.229
1.00
17.19
A


ATOM
2105
CB
TYR
A
325
7.767
3.506
35.549
1.00
16.29
A


ATOM
2106
CG
TYR
A
325
9.116
3.410
36.228
1.00
16.54
A


ATOM
2107
CD1
TYR
A
325
9.451
4.234
37.321
1.00
15.57
A


ATOM
2108
CE1
TYR
A
325
10.690
4.093
37.985
1.00
16.89
A


ATOM
2109
CD2
TYR
A
325
10.035
2.468
35.806
1.00
12.57
A


ATOM
2110
CE2
TYR
A
325
11.252
2.322
36.438
1.00
16.53
A


ATOM
2111
CZ
TYR
A
325
11.577
3.130
37.533
1.00
18.32
A


ATOM
2112
OH
TYR
A
325
12.787
2.924
38.155
1.00
19.91
A


ATOM
2113
C
TYR
A
325
6.649
5.745
35.459
1.00
19.60
A


ATOM
2114
O
TYR
A
325
6.014
5.809
34.382
1.00
16.48
A


ATOM
2115
N
GLU
A
326
7.228
6.810
36.019
1.00
19.56
A


ATOM
2116
CA
GLU
A
326
7.167
8.133
35.398
1.00
17.58
A


ATOM
2117
CB
GLU
A
326
6.672
9.163
36.429
1.00
20.07
A


ATOM
2118
CG
GLU
A
326
6.635
10.622
35.926
1.00
20.89
A


ATOM
2119
CD
GLU
A
326
6.359
11.654
37.019
1.00
25.27
A


ATOM
2120
OE1
GLU
A
326
6.249
11.306
38.223
1.00
26.59
A


ATOM
2121
OE2
GLU
A
326
6.242
12.847
36.679
1.00
27.97
A


ATOM
2122
C
GLU
A
326
8.535
8.506
34.864
1.00
18.25
A


ATOM
2123
O
GLU
A
326
9.536
8.080
35.407
1.00
20.12
A


ATOM
2124
N
SER
A
327
8.596
9.274
33.773
1.00
17.84
A


ATOM
2125
CA
SER
A
327
9.866
9.672
33.201
1.00
17.03
A


ATOM
2126
CB
SER
A
327
9.831
9.564
31.666
1.00
20.28
A


ATOM
2127
OG
SER
A
327
9.168
10.713
31.160
1.00
19.41
A


ATOM
2128
C
SER
A
327
10.174
11.139
33.563
1.00
16.98
A


ATOM
2129
O
SER
A
327
9.347
11.844
34.126
1.00
16.81
A


ATOM
2130
N
ILE
A
328
11.363
11.585
33.177
1.00
19.48
A


ATOM
2131
CA
ILE
A
328
11.796
12.937
33.446
1.00
20.83
A


ATOM
2132
CB
ILE
A
328
13.231
13.102
32.939
1.00
22.78
A


ATOM
2133
CG2
ILE
A
328
13.255
13.263
31.422
1.00
20.86
A


ATOM
2134
CG1
ILE
A
328
13.870
14.329
33.587
1.00
25.35
A


ATOM
2135
CD1
ILE
A
328
15.295
14.540
33.152
1.00
25.98
A


ATOM
2136
C
ILE
A
328
10.846
13.939
32.790
1.00
24.54
A


ATOM
2137
O
ILE
A
328
10.750
15.092
33.186
1.00
25.62
A


ATOM
2138
N
LEU
A
329
10.055
13.467
31.836
1.00
25.46
A


ATOM
2139
CA
LEU
A
329
9.141
14.338
31.112
1.00
25.84
A


ATOM
2140
CB
LEU
A
329
9.212
13.933
29.637
1.00
27.88
A


ATOM
2141
CG
LEU
A
329
8.816
14.822
28.469
1.00
32.12
A


ATOM
2142
CD1
LEU
A
329
9.372
16.220
28.618
1.00
30.41
A


ATOM
2143
CD2
LEU
A
329
9.341
14.147
27.194
1.00
29.12
A


ATOM
2144
C
LEU
A
329
7.731
14.259
31.643
1.00
26.05
A


ATOM
2145
O
LEU
A
329
6.857
15.027
31.237
1.00
25.53
A


ATOM
2146
N
GLY
A
330
7.488
13.331
32.564
1.00
24.08
A


ATOM
2147
CA
GLY
A
330
6.144
13.208
33.110
1.00
21.73
A


ATOM
2148
C
GLY
A
330
5.325
12.127
32.419
1.00
19.70
A


ATOM
2149
O
GLY
A
330
4.159
11.900
32.741
1.00
23.39
A


ATOM
2150
N
SER
A
331
5.923
11.434
31.474
1.00
20.40
A


ATOM
2151
CA
SER
A
331
5.186
10.363
30.778
1.00
22.86
A


ATOM
2152
CB
SER
A
331
5.931
9.876
29.528
1.00
21.11
A


ATOM
2153
OG
SER
A
331
6.431
10.941
28.778
1.00
26.43
A


ATOM
2154
C
SER
A
331
5.098
9.167
31.714
1.00
20.81
A


ATOM
2155
O
SER
A
331
5.999
8.940
32.542
1.00
21.77
A


ATOM
2156
N
LEU
A
332
4.048
8.383
31.530
1.00
18.60
A


ATOM
2157
CA
LEU
A
332
3.825
7.179
32.316
1.00
18.97
A


ATOM
2158
CB
LEU
A
332
2.505
7.301
33.030
1.00
18.99
A


ATOM
2159
CG
LEU
A
332
2.260
8.609
33.745
1.00
19.51
A


ATOM
2160
CD1
LEU
A
332
0.847
8.581
34.238
1.00
21.18
A


ATOM
2161
CD2
LEU
A
332
3.244
8.770
34.924
1.00
17.75
A


ATOM
2162
C
LEU
A
332
3.755
5.887
31.524
1.00
19.35
A


ATOM
2163
O
LEU
A
332
3.188
5.879
30.414
1.00
20.14
A


ATOM
2164
N
PHE
A
333
4.344
4.806
32.061
1.00
17.44
A


ATOM
2165
CA
PHE
A
333
4.203
3.458
31.481
1.00
14.82
A


ATOM
2166
CB
PHE
A
333
5.533
2.761
31.133
1.00
12.51
A


ATOM
2167
CG
PHE
A
333
6.123
3.135
29.778
1.00
13.15
A


ATOM
2168
CD1
PHE
A
333
5.376
3.830
28.824
1.00
15.15
A


ATOM
2169
CD2
PHE
A
333
7.411
2.748
29.460
1.00
8.85
A


ATOM
2170
CE1
PHE
A
333
5.925
4.122
27.571
1.00
14.83
A


ATOM
2171
CE2
PHE
A
333
7.962
3.019
28.233
1.00
14.68
A


ATOM
2172
CZ
PHE
A
333
7.203
3.722
27.266
1.00
14.99
A


ATOM
2173
C
PHE
A
333
3.563
2.653
32.605
1.00
17.99
A


ATOM
2174
O
PHE
A
333
3.831
2.905
33.819
1.00
17.33
A


ATOM
2175
N
GLN
A
334
2.708
1.700
32.231
1.00
16.15
A


ATOM
2176
CA
GLN
A
334
2.073
0.821
33.217
1.00
19.09
A


ATOM
2177
CB
GLN
A
334
0.548
0.748
33.055
1.00
19.52
A


ATOM
2178
CG
GLN
A
334
−0.233
2.077
33.240
1.00
24.47
A


ATOM
2179
CD
GLN
A
334
−0.022
3.042
32.040
1.00
26.93
A


ATOM
2180
OE1
GLN
A
334
−0.116
2.638
30.890
1.00
29.49
A


ATOM
2181
NE2
GLN
A
334
0.251
4.300
32.320
1.00
27.42
A


ATOM
2182
C
GLN
A
334
2.666
−0.578
32.992
1.00
21.41
A


ATOM
2183
O
GLN
A
334
2.788
−1.036
31.842
1.00
22.36
A


ATOM
2184
N
GLY
A
335
3.073
−1.239
34.075
1.00
20.48
A


ATOM
2185
CA
GLY
A
335
3.639
−2.583
33.962
1.00
21.62
A


ATOM
2186
C
GLY
A
335
2.941
−3.553
34.887
1.00
23.01
A


ATOM
2187
O
GLY
A
335
2.341
−3.149
35.905
1.00
22.08
A


ATOM
2188
N
ARG
A
336
2.960
−4.829
34.534
1.00
22.00
A


ATOM
2189
CA
ARG
A
336
2.372
−5.823
35.415
1.00
22.02
A


ATOM
2190
CB
ARG
A
336
0.996
−6.293
34.931
1.00
23.20
A


ATOM
2191
CG
ARG
A
336
−0.120
−5.301
34.988
1.00
27.17
A


ATOM
2192
CD
ARG
A
336
−1.429
−6.013
34.766
1.00
25.93
A


ATOM
2193
NE
ARG
A
336
−1.550
−6.514
33.399
1.00
29.18
A


ATOM
2194
CZ
ARG
A
336
−2.611
−7.179
32.944
1.00
31.96
A


ATOM
2195
NH1
ARG
A
336
−3.626
−7.427
33.765
1.00
28.93
A


ATOM
2196
NH2
ARG
A
336
−2.691
−7.550
31.661
1.00
31.14
A


ATOM
2197
C
ARG
A
336
3.296
−7.016
35.285
1.00
22.85
A


ATOM
2198
O
ARG
A
336
3.805
−7.269
34.187
1.00
19.28
A


ATOM
2199
N
VAL
A
337
3.533
−7.748
36.376
1.00
19.68
A


ATOM
2200
CA
VAL
A
337
4.320
−8.979
36.250
1.00
18.60
A


ATOM
2201
CB
VAL
A
337
5.094
−9.353
37.544
1.00
18.22
A


ATOM
2202
CG1
VAL
A
337
5.790
−10.717
37.352
1.00
16.37
A


ATOM
2203
CG2
VAL
A
337
6.178
−8.328
37.820
1.00
16.50
A


ATOM
2204
C
VAL
A
337
3.227
−9.992
36.024
1.00
17.78
A


ATOM
2205
O
VAL
A
337
2.290
−10.066
36.825
1.00
21.86
A


ATOM
2206
N
LEU
A
338
3.308
−10.786
34.965
1.00
18.50
A


ATOM
2207
CA
LEU
A
338
2.236
−11.755
34.710
1.00
20.96
A


ATOM
2208
CB
LEU
A
338
1.828
−11.751
33.223
1.00
22.53
A


ATOM
2209
CG
LEU
A
338
1.361
−10.403
32.692
1.00
23.74
A


ATOM
2210
CD1
LEU
A
338
1.044
−10.528
31.211
1.00
25.84
A


ATOM
2211
CD2
LEU
A
338
0.183
−9.948
33.503
1.00
23.28
A


ATOM
2212
C
LEU
A
338
2.569
−13.197
35.092
1.00
24.05
A


ATOM
2213
O
LEU
A
338
1.675
−14.037
35.117
1.00
24.40
A


ATOM
2214
N
GLY
A
339
3.838
−13.479
35.369
1.00
24.56
A


ATOM
2215
CA
GLY
A
339
4.231
−14.820
35.743
1.00
23.69
A


ATOM
2216
C
GLY
A
339
5.663
−14.857
36.261
1.00
25.12
A


ATOM
2217
O
GLY
A
339
6.475
−13.968
35.975
1.00
21.74
A


ATOM
2218
N
GLU
A
340
5.965
−15.884
37.042
1.00
23.26
A


ATOM
2219
CA
GLU
A
340
7.294
−16.066
37.575
1.00
26.29
A


ATOM
2220
CB
GLU
A
340
7.311
−15.810
39.081
1.00
25.71
A


ATOM
2221
CG
GLU
A
340
6.533
−16.824
39.921
1.00
30.77
A


ATOM
2222
CD
GLU
A
340
7.177
−16.961
41.293
1.00
34.78
A


ATOM
2223
OE1
GLU
A
340
7.867
−17.970
41.537
1.00
37.88
A


ATOM
2224
OE2
GLU
A
340
7.031
−16.038
42.114
1.00
36.85
A


ATOM
2225
C
GLU
A
340
7.721
−17.493
37.320
1.00
27.28
A


ATOM
2226
O
GLU
A
340
6.885
−18.365
37.101
1.00
27.19
A


ATOM
2227
N
GLU
A
341
9.021
−17.731
37.375
1.00
28.56
A


ATOM
2228
CA
GLU
A
341
9.548
−19.061
37.172
1.00
31.30
A


ATOM
2229
CB
GLU
A
341
9.573
−19.371
35.684
1.00
33.64
A


ATOM
2230
CG
GLU
A
341
9.857
−20.803
35.352
1.00
38.66
A


ATOM
2231
CD
GLU
A
341
9.978
−20.976
33.859
1.00
44.82
A


ATOM
2232
OE1
GLU
A
341
9.148
−20.362
33.141
1.00
47.09
A


ATOM
2233
OE2
GLU
A
341
10.890
−21.699
33.399
1.00
44.78
A


ATOM
2234
C
GLU
A
341
10.967
−19.178
37.719
1.00
30.61
A


ATOM
2235
O
GLU
A
341
11.753
−18.219
37.636
1.00
29.95
A


ATOM
2236
N
ARG
A
342
11.281
−20.348
38.279
1.00
29.23
A


ATOM
2237
CA
ARG
A
342
12.629
−20.642
38.760
1.00
27.84
A


ATOM
2238
CB
ARG
A
342
12.601
−21.110
40.225
1.00
26.45
A


ATOM
2239
CG
ARG
A
342
12.738
−19.878
41.132
1.00
28.80
A


ATOM
2240
CD
ARG
A
342
12.472
−20.089
42.618
1.00
30.93
A


ATOM
2241
NE
ARG
A
342
12.600
−18.845
43.412
1.00
31.05
A


ATOM
2242
CZ
ARG
A
342
13.718
−18.105
43.574
1.00
32.80
A


ATOM
2243
NH1
ARG
A
342
14.884
−18.433
43.004
1.00
29.02
A


ATOM
2244
NH2
ARG
A
342
13.664
−16.996
44.327
1.00
31.86
A


ATOM
2245
C
ARG
A
342
13.157
−21.712
37.821
1.00
27.25
A


ATOM
2246
O
ARG
A
342
12.439
−22.638
37.478
1.00
27.76
A


ATOM
2247
N
ILE
A
343
14.393
−21.555
37.365
1.00
27.87
A


ATOM
2248
CA
ILE
A
343
14.997
−22.496
36.432
1.00
28.78
A


ATOM
2249
CB
ILE
A
343
15.575
−21.745
35.235
1.00
30.53
A


ATOM
2250
CG2
ILE
A
343
15.773
−22.707
34.090
1.00
30.06
A


ATOM
2251
CG1
ILE
A
343
14.606
−20.638
34.774
1.00
30.64
A


ATOM
2252
CD1
ILE
A
343
15.285
−19.655
33.797
1.00
31.26
A


ATOM
2253
C
ILE
A
343
16.120
−23.266
37.185
1.00
29.98
A


ATOM
2254
O
ILE
A
343
17.235
−22.771
37.368
1.00
25.59
A


ATOM
2255
N
PRO
A
344
15.819
−24.503
37.602
1.00
29.90
A


ATOM
2256
CD
PRO
A
344
14.554
−25.191
37.298
1.00
31.23
A


ATOM
2257
CA
PRO
A
344
16.723
−25.382
38.346
1.00
31.90
A


ATOM
2258
CB
PRO
A
344
15.938
−26.690
38.439
1.00
32.97
A


ATOM
2259
CG
PRO
A
344
14.486
−26.202
38.428
1.00
32.84
A


ATOM
2260
C
PRO
A
344
18.078
−25.573
37.726
1.00
32.48
A


ATOM
2261
O
PRO
A
344
18.206
−25.820
36.537
1.00
32.08
A


ATOM
2262
N
GLY
A
345
19.109
−25.439
38.536
1.00
34.45
A


ATOM
2263
CA
GLY
A
345
20.439
−25.664
38.001
1.00
35.77
A


ATOM
2264
C
GLY
A
345
21.028
−24.512
37.219
1.00
36.47
A


ATOM
2265
O
GLY
A
345
22.072
−24.659
36.570
1.00
37.85
A


ATOM
2266
N
VAL
A
346
20.362
−23.371
37.228
1.00
34.13
A


ATOM
2267
CA
VAL
A
346
20.934
−22.235
36.527
1.00
33.93
A


ATOM
2268
CB
VAL
A
346
20.117
−21.836
35.273
1.00
34.56
A


ATOM
2269
CG1
VAL
A
346
20.707
−20.580
34.660
1.00
34.47
A


ATOM
2270
CG2
VAL
A
346
20.096
−22.999
34.251
1.00
31.69
A


ATOM
2271
C
VAL
A
346
20.842
−21.130
37.540
1.00
33.88
A


ATOM
2272
O
VAL
A
346
19.777
−20.915
38.117
1.00
34.02
A


ATOM
2273
N
LYS
A
347
21.952
−20.454
37.798
1.00
33.67
A


ATOM
2274
CA
LYS
A
347
21.893
−19.361
38.744
1.00
34.72
A


ATOM
2275
CB
LYS
A
347
22.362
−19.806
40.129
1.00
37.72
A


ATOM
2276
CG
LYS
A
347
23.748
−20.375
40.194
1.00
43.18
A


ATOM
2277
CD
LYS
A
347
23.809
−21.349
41.386
1.00
47.44
A


ATOM
2278
CE
LYS
A
347
25.239
−21.599
41.817
1.00
49.22
A


ATOM
2279
NZ
LYS
A
347
25.838
−20.326
42.340
1.00
51.49
A


ATOM
2280
C
LYS
A
347
22.668
−18.141
38.297
1.00
32.11
A


ATOM
2281
O
LYS
A
347
23.474
−18.198
37.372
1.00
28.94
A


ATOM
2282
N
VAL
A
348
22.361
−17.023
38.934
1.00
29.06
A


ATOM
2283
CA
VAL
A
348
23.050
−15.779
38.653
1.00
26.24
A


ATOM
2284
CB
VAL
A
348
22.076
−14.770
38.004
1.00
22.25
A


ATOM
2285
CG1
VAL
A
348
21.707
−15.277
36.588
1.00
17.75
A


ATOM
2286
CG2
VAL
A
348
20.830
−14.630
38.840
1.00
19.28
A


ATOM
2287
C
VAL
A
348
23.566
−15.336
40.030
1.00
25.52
A


ATOM
2288
O
VAL
A
348
23.184
−15.928
41.049
1.00
26.03
A


ATOM
2289
N
PRO
A
349
24.433
−14.314
40.079
1.00
24.92
A


ATOM
2290
CD
PRO
A
349
25.154
−13.641
38.987
1.00
24.89
A


ATOM
2291
CA
PRO
A
349
24.953
−13.891
41.377
1.00
26.91
A


ATOM
2292
CB
PRO
A
349
25.723
−12.618
41.046
1.00
26.83
A


ATOM
2293
CG
PRO
A
349
26.354
−13.002
39.715
1.00
26.19
A


ATOM
2294
C
PRO
A
349
23.947
−13.717
42.476
1.00
28.45
A


ATOM
2295
O
PRO
A
349
24.229
−14.074
43.615
1.00
32.28
A


ATOM
2296
N
VAL
A
350
22.757
−13.218
42.191
1.00
25.90
A


ATOM
2297
CA
VAL
A
350
21.852
−13.055
43.314
1.00
25.37
A


ATOM
2298
CB
VAL
A
350
20.731
−12.027
43.017
1.00
25.38
A


ATOM
2299
CG1
VAL
A
350
19.664
−12.641
42.093
1.00
24.57
A


ATOM
2300
CG2
VAL
A
350
20.116
−11.541
44.336
1.00
26.42
A


ATOM
2301
C
VAL
A
350
21.193
−14.334
43.800
1.00
26.89
A


ATOM
2302
O
VAL
A
350
20.578
−14.314
44.860
1.00
27.74
A


ATOM
2303
N
THR
A
351
21.304
−15.432
43.041
1.00
25.74
A


ATOM
2304
CA
THR
A
351
20.649
−16.667
43.426
1.00
27.19
A


ATOM
2305
CB
THR
A
351
20.774
−17.727
42.342
1.00
32.32
A


ATOM
2306
OG1
THR
A
351
20.397
−17.175
41.073
1.00
32.13
A


ATOM
2307
CG2
THR
A
351
19.880
−18.937
42.699
1.00
31.39
A


ATOM
2308
C
THR
A
351
21.240
−17.307
44.689
1.00
26.98
A


ATOM
2309
O
THR
A
351
22.401
−17.699
44.683
1.00
25.39
A


ATOM
2310
N
LYS
A
352
20.427
−17.448
45.731
1.00
27.84
A


ATOM
2311
CA
LYS
A
352
20.882
−18.056
46.994
1.00
31.21
A


ATOM
2312
CB
LYS
A
352
19.981
−17.603
48.129
1.00
30.66
A


ATOM
2313
CG
LYS
A
352
20.109
−16.107
48.292
1.00
34.76
A


ATOM
2314
CD
LYS
A
352
19.066
−15.513
49.184
1.00
38.62
A


ATOM
2315
CE
LYS
A
352
19.451
−14.065
49.440
1.00
41.73
A


ATOM
2316
NZ
LYS
A
352
18.428
−13.358
50.216
1.00
43.53
A


ATOM
2317
C
LYS
A
352
20.951
−19.569
46.971
1.00
30.19
A


ATOM
2318
O
LYS
A
352
20.219
−20.236
46.234
1.00
29.91
A


ATOM
2319
N
ASP
A
353
21.841
−20.085
47.799
1.00
30.00
A


ATOM
2320
CA
ASP
A
353
22.065
−21.507
47.957
1.00
30.30
A


ATOM
2321
CB
ASP
A
353
23.085
−21.745
49.053
1.00
37.47
A


ATOM
2322
CG
ASP
A
353
24.486
−21.427
48.605
1.00
43.97
A


ATOM
2323
OD1
ASP
A
353
24.998
−22.184
47.737
1.00
48.17
A


ATOM
2324
OD2
ASP
A
353
25.060
−20.426
49.113
1.00
48.28
A


ATOM
2325
C
ASP
A
353
20.788
−22.189
48.349
1.00
28.19
A


ATOM
2326
O
ASP
A
353
20.498
−23.292
47.912
1.00
27.41
A


ATOM
2327
N
ALA
A
354
20.014
−21.517
49.176
1.00
26.37
A


ATOM
2328
CA
ALA
A
354
18.770
−22.086
49.623
1.00
28.33
A


ATOM
2329
CB
ALA
A
354
18.238
−21.276
50.837
1.00
26.85
A


ATOM
2330
C
ALA
A
354
17.695
−22.169
48.512
1.00
29.76
A


ATOM
2331
O
ALA
A
354
16.692
−22.844
48.714
1.00
30.31
A


ATOM
2332
N
GLU
A
355
17.891
−21.490
47.371
1.00
28.90
A


ATOM
2333
CA
GLU
A
355
16.887
−21.531
46.282
1.00
32.70
A


ATOM
2334
CB
GLU
A
355
16.807
−20.200
45.488
1.00
30.77
A


ATOM
2335
CG
GLU
A
355
16.979
−18.910
46.264
1.00
38.87
A


ATOM
2336
CD
GLU
A
355
15.681
−18.189
46.581
1.00
41.05
A


ATOM
2337
OE1
GLU
A
355
15.739
−16.946
46.760
1.00
43.22
A


ATOM
2338
OE2
GLU
A
355
14.615
−18.847
46.656
1.00
42.99
A


ATOM
2339
C
GLU
A
355
17.182
−22.618
45.237
1.00
31.53
A


ATOM
2340
O
GLU
A
355
18.340
−22.925
44.954
1.00
31.27
A


ATOM
2341
N
GLU
A
356
16.126
−23.162
44.642
1.00
33.70
A


ATOM
2342
CA
GLU
A
356
16.265
−24.175
43.596
1.00
36.13
A


ATOM
2343
CB
GLU
A
356
15.069
−25.141
43.598
1.00
38.00
A


ATOM
2344
CG
GLU
A
356
15.166
−26.340
44.545
1.00
47.18
A


ATOM
2345
CD
GLU
A
356
16.379
−27.241
44.262
1.00
50.12
A


ATOM
2346
OE1
GLU
A
356
16.697
−27.480
43.069
1.00
51.50
A


ATOM
2347
OE2
GLU
A
356
17.006
−27.720
45.239
1.00
53.20
A


ATOM
2348
C
GLU
A
356
16.234
−23.426
42.273
1.00
36.13
A


ATOM
2349
O
GLU
A
356
15.191
−23.408
41.629
1.00
40.29
A


ATOM
2350
N
GLY
A
357
17.318
−22.774
41.871
1.00
32.38
A


ATOM
2351
CA
GLY
A
357
17.290
−22.089
40.591
1.00
29.57
A


ATOM
2352
C
GLY
A
357
16.995
−20.595
40.570
1.00
26.44
A


ATOM
2353
O
GLY
A
357
16.314
−20.059
41.453
1.00
24.81
A


ATOM
2354
N
MET
A
358
17.514
−19.926
39.537
1.00
25.03
A


ATOM
2355
CA
MET
A
358
17.334
−18.483
39.413
1.00
23.73
A


ATOM
2356
CB
MET
A
358
18.197
−17.912
38.299
1.00
24.66
A


ATOM
2357
CG
MET
A
358
17.740
−18.327
36.886
1.00
23.91
A


ATOM
2358
SD
MET
A
358
18.750
−17.616
35.593
1.00
25.23
A


ATOM
2359
CE
MET
A
358
18.219
−15.909
35.710
1.00
24.07
A


ATOM
2360
C
MET
A
358
15.890
−18.159
39.118
1.00
23.88
A


ATOM
2361
O
MET
A
358
15.205
−18.903
38.417
1.00
26.76
A


ATOM
2362
N
LEU
A
359
15.433
−17.067
39.703
1.00
22.45
A


ATOM
2363
CA
LEU
A
359
14.097
−16.570
39.511
1.00
24.00
A


ATOM
2364
CB
LEU
A
359
13.730
−15.730
40.730
1.00
25.22
A


ATOM
2365
CG
LEU
A
359
12.375
−15.042
40.569
1.00
27.81
A


ATOM
2366
CD1
LEU
A
359
11.251
−16.079
40.469
1.00
23.28
A


ATOM
2367
CD2
LEU
A
359
12.173
−14.123
41.754
1.00
26.78
A


ATOM
2368
C
LEU
A
359
14.052
−15.657
38.229
1.00
22.85
A


ATOM
2369
O
LEU
A
359
14.991
−14.867
37.992
1.00
20.97
A


ATOM
2370
N
VAL
A
360
13.027
−15.806
37.386
1.00
23.44
A


ATOM
2371
CA
VAL
A
360
12.866
−14.922
36.207
1.00
21.29
A


ATOM
2372
CB
VAL
A
360
13.158
−15.590
34.854
1.00
20.64
A


ATOM
2373
CG1
VAL
A
360
14.627
−15.988
34.741
1.00
21.64
A


ATOM
2374
CG2
VAL
A
360
12.200
−16.762
34.618
1.00
20.34
A


ATOM
2375
C
VAL
A
360
11.407
−14.571
36.213
1.00
22.38
A


ATOM
2376
O
VAL
A
360
10.605
−15.336
36.745
1.00
22.65
A


ATOM
2377
N
VAL
A
361
11.039
−13.413
35.664
1.00
20.61
A


ATOM
2378
CA
VAL
A
361
9.623
−13.046
35.645
1.00
20.43
A


ATOM
2379
CB
VAL
A
361
9.294
−11.949
36.708
1.00
21.52
A


ATOM
2380
CG1
VAL
A
361
9.888
−12.362
38.090
1.00
22.78
A


ATOM
2381
CG2
VAL
A
361
9.851
−10.593
36.290
1.00
21.12
A


ATOM
2382
C
VAL
A
361
9.164
−12.565
34.245
1.00
19.89
A


ATOM
2383
O
VAL
A
361
9.973
−12.187
33.408
1.00
16.64
A


ATOM
2384
N
THR
A
362
7.870
−12.630
33.992
1.00
19.31
A


ATOM
2385
CA
THR
A
362
7.342
−12.175
32.729
1.00
21.14
A


ATOM
2386
CB
THR
A
362
6.397
−13.194
32.154
1.00
25.15
A


ATOM
2387
OG1
THR
A
362
7.137
−14.396
31.932
1.00
26.43
A


ATOM
2388
CG2
THR
A
362
5.828
−12.692
30.804
1.00
24.17
A


ATOM
2389
C
THR
A
362
6.621
−10.863
32.964
1.00
18.54
A


ATOM
2390
O
THR
A
362
5.598
−10.816
33.621
1.00
18.66
A


ATOM
2391
N
ALA
A
363
7.214
−9.802
32.446
1.00
18.27
A


ATOM
2392
CA
ALA
A
363
6.699
−8.440
32.591
1.00
21.61
A


ATOM
2393
CB
ALA
A
363
7.868
−7.494
32.802
1.00
22.47
A


ATOM
2394
C
ALA
A
363
5.914
−7.953
31.363
1.00
20.37
A


ATOM
2395
O
ALA
A
363
6.362
−8.116
30.255
1.00
16.27
A


ATOM
2396
N
GLU
A
364
4.761
−7.335
31.590
1.00
20.97
A


ATOM
2397
CA
GLU
A
364
3.970
−6.761
30.510
1.00
21.75
A


ATOM
2398
CB
GLU
A
364
2.510
−7.160
30.626
1.00
21.12
A


ATOM
2399
CG
GLU
A
364
1.622
−6.398
29.619
1.00
23.86
A


ATOM
2400
CD
GLU
A
364
0.148
−6.458
29.974
1.00
25.20
A


ATOM
2401
OE1
GLU
A
364
−0.273
−5.780
30.925
1.00
24.82
A


ATOM
2402
OE2
GLU
A
364
−0.597
−7.197
29.319
1.00
30.79
A


ATOM
2403
C
GLU
A
364
4.084
−5.238
30.699
1.00
21.33
A


ATOM
2404
O
GLU
A
364
3.896
−4.749
31.814
1.00
20.68
A


ATOM
2405
N
ILE
A
365
4.404
−4.521
29.617
1.00
19.59
A


ATOM
2406
CA
ILE
A
365
4.543
−3.059
29.592
1.00
19.18
A


ATOM
2407
CB
ILE
A
365
5.982
−2.617
29.140
1.00
20.31
A


ATOM
2408
CG2
ILE
A
365
6.192
−1.095
29.408
1.00
20.09
A


ATOM
2409
CG1
ILE
A
365
7.036
−3.329
29.991
1.00
20.70
A


ATOM
2410
CD1
ILE
A
365
6.891
−2.938
31.453
1.00
19.70
A


ATOM
2411
C
ILE
A
365
3.535
−2.452
28.605
1.00
19.48
A


ATOM
2412
O
ILE
A
365
3.432
−2.918
27.446
1.00
20.26
A


ATOM
2413
N
THR
A
366
2.807
−1.427
29.060
1.00
17.29
A


ATOM
2414
CA
THR
A
366
1.826
−0.724
28.269
1.00
16.66
A


ATOM
2415
CB
THR
A
366
0.420
−0.835
28.847
1.00
21.20
A


ATOM
2416
OG1
THR
A
366
0.072
−2.212
28.978
1.00
19.38
A


ATOM
2417
CG2
THR
A
366
−0.621
−0.138
27.883
1.00
19.31
A


ATOM
2418
C
THR
A
366
2.145
0.777
28.150
1.00
18.94
A


ATOM
2419
O
THR
A
366
2.510
1.445
29.157
1.00
17.80
A


ATOM
2420
N
GLY
A
367
2.021
1.304
26.920
1.00
18.08
A


ATOM
2421
CA
GLY
A
367
2.253
2.732
26.679
1.00
18.99
A


ATOM
2422
C
GLY
A
367
1.626
3.154
25.365
1.00
19.65
A


ATOM
2423
O
GLY
A
367
1.002
2.310
24.711
1.00
16.56
A


ATOM
2424
N
LYS
A
368
1.799
4.408
24.944
1.00
17.19
A


ATOM
2425
CA
LYS
A
368
1.178
4.854
23.674
1.00
18.96
A


ATOM
2426
CB
LYS
A
368
0.066
5.891
23.956
1.00
20.79
A


ATOM
2427
CG
LYS
A
368
−0.755
6.320
22.720
1.00
19.09
A


ATOM
2428
CD
LYS
A
368
−2.026
7.081
23.166
1.00
26.40
A


ATOM
2429
CE
LYS
A
368
−2.857
7.554
21.980
1.00
25.98
A


ATOM
2430
NZ
LYS
A
368
−2.864
6.515
20.894
1.00
26.43
A


ATOM
2431
C
LYS
A
368
2.201
5.466
22.759
1.00
17.77
A


ATOM
2432
O
LYS
A
368
3.067
6.234
23.218
1.00
18.97
A


ATOM
2433
N
ALA
A
369
2.143
5.126
21.473
1.00
15.93
A


ATOM
2434
CA
ALA
A
369
3.078
5.689
20.500
1.00
15.21
A


ATOM
2435
CB
ALA
A
369
3.881
4.586
19.832
1.00
14.74
A


ATOM
2436
C
ALA
A
369
2.298
6.478
19.435
1.00
18.33
A


ATOM
2437
O
ALA
A
369
1.147
6.169
19.135
1.00
19.74
A


ATOM
2438
N
PHE
A
370
2.938
7.489
18.852
1.00
19.47
A


ATOM
2439
CA
PHE
A
370
2.295
8.291
17.826
1.00
18.39
A


ATOM
2440
CB
PHE
A
370
2.116
9.738
18.283
1.00
18.50
A


ATOM
2441
CG
PHE
A
370
1.005
9.928
19.266
1.00
20.13
A


ATOM
2442
CD1
PHE
A
370
−0.294
10.171
18.825
1.00
25.52
A


ATOM
2443
CD2
PHE
A
370
1.249
9.892
20.611
1.00
20.40
A


ATOM
2444
CE1
PHE
A
370
−1.327
10.389
19.724
1.00
24.88
A


ATOM
2445
CE2
PHE
A
370
0.218
10.107
21.550
1.00
22.40
A


ATOM
2446
CZ
PHE
A
370
−1.065
10.361
21.106
1.00
24.56
A


ATOM
2447
C
PHE
A
370
3.150
8.297
16.591
1.00
17.55
A


ATOM
2448
O
PHE
A
370
4.400
8.302
16.661
1.00
16.04
A


ATOM
2449
N
ILE
A
371
2.497
8.283
15.438
1.00
16.13
A


ATOM
2450
CA
ILE
A
371
3.287
8.398
14.210
1.00
16.03
A


ATOM
2451
CB
ILE
A
371
2.501
7.895
12.984
1.00
17.82
A


ATOM
2452
CG2
ILE
A
371
3.230
8.308
11.715
1.00
15.54
A


ATOM
2453
CG1
ILE
A
371
2.313
6.380
13.049
1.00
17.91
A


ATOM
2454
CD1
ILE
A
371
1.728
5.770
11.704
1.00
21.75
A


ATOM
2455
C
ILE
A
371
3.506
9.929
14.077
1.00
12.83
A


ATOM
2456
O
ILE
A
371
2.562
10.680
14.153
1.00
17.07
A


ATOM
2457
N
MET
A
372
4.724
10.407
13.891
1.00
12.85
A


ATOM
2458
CA
MET
A
372
4.905
11.843
13.776
1.00
13.49
A


ATOM
2459
CB
MET
A
372
5.855
12.380
14.862
1.00
11.09
A


ATOM
2460
CG
MET
A
372
7.214
11.747
14.831
1.00
11.67
A


ATOM
2461
SD
MET
A
372
8.253
12.416
16.231
1.00
15.23
A


ATOM
2462
CE
MET
A
372
9.721
11.802
15.790
1.00
5.94
A


ATOM
2463
C
MET
A
372
5.441
12.215
12.400
1.00
13.02
A


ATOM
2464
O
MET
A
372
5.632
13.377
12.103
1.00
13.88
A


ATOM
2465
N
GLY
A
373
5.732
11.228
11.579
1.00
15.47
A


ATOM
2466
CA
GLY
A
373
6.177
11.541
10.225
1.00
15.39
A


ATOM
2467
C
GLY
A
373
6.390
10.299
9.376
1.00
17.81
A


ATOM
2468
O
GLY
A
373
6.580
9.226
9.938
1.00
13.49
A


ATOM
2469
N
PHE
A
374
6.279
10.438
8.048
1.00
16.92
A


ATOM
2470
CA
PHE
A
374
6.610
9.373
7.097
1.00
18.33
A


ATOM
2471
CB
PHE
A
374
5.454
9.063
6.135
1.00
18.23
A


ATOM
2472
CG
PHE
A
374
4.314
8.350
6.798
1.00
19.51
A


ATOM
2473
CD1
PHE
A
374
4.422
6.997
7.152
1.00
20.79
A


ATOM
2474
CD2
PHE
A
374
3.147
9.020
7.094
1.00
22.02
A


ATOM
2475
CE1
PHE
A
374
3.371
6.328
7.787
1.00
19.41
A


ATOM
2476
CE2
PHE
A
374
2.070
8.352
7.740
1.00
24.08
A


ATOM
2477
CZ
PHE
A
374
2.202
6.994
8.079
1.00
21.87
A


ATOM
2478
C
PHE
A
374
7.739
10.100
6.378
1.00
19.52
A


ATOM
2479
O
PHE
A
374
7.526
11.147
5.757
1.00
20.86
A


ATOM
2480
N
ASN
A
375
8.944
9.567
6.465
1.00
20.28
A


ATOM
2481
CA
ASN
A
375
10.084
10.244
5.885
1.00
21.96
A


ATOM
2482
CB
ASN
A
375
10.959
10.761
7.034
1.00
26.82
A


ATOM
2483
CG
ASN
A
375
12.020
11.752
6.572
1.00
32.64
A


ATOM
2484
OD1
ASN
A
375
11.851
12.438
5.554
1.00
34.71
A


ATOM
2485
ND2
ASN
A
375
13.111
11.851
7.329
1.00
33.11
A


ATOM
2486
C
ASN
A
375
10.943
9.456
4.938
1.00
20.81
A


ATOM
2487
O
ASN
A
375
11.168
8.261
5.105
1.00
22.34
A


ATOM
2488
N
THR
A
376
11.408
10.137
3.910
1.00
20.56
A


ATOM
2489
CA
THR
A
376
12.326
9.535
2.984
1.00
22.95
A


ATOM
2490
CB
THR
A
376
11.884
9.708
1.515
1.00
20.60
A


ATOM
2491
OG1
THR
A
376
10.598
9.103
1.348
1.00
25.54
A


ATOM
2492
CG2
THR
A
376
12.875
9.045
0.595
1.00
22.86
A


ATOM
2493
C
THR
A
376
13.623
10.278
3.224
1.00
22.82
A


ATOM
2494
O
THR
A
376
13.789
11.448
2.838
1.00
21.25
A


ATOM
2495
N
MET
A
377
14.542
9.571
3.869
1.00
23.60
A


ATOM
2496
CA
MET
A
377
15.853
10.075
4.223
1.00
22.90
A


ATOM
2497
CB
MET
A
377
16.317
9.284
5.428
1.00
25.46
A


ATOM
2498
CG
MET
A
377
17.134
10.072
6.412
1.00
32.82
A


ATOM
2499
SD
MET
A
377
17.355
9.160
7.965
1.00
36.16
A


ATOM
2500
CE
MET
A
377
15.837
8.619
8.218
1.00
26.44
A


ATOM
2501
C
MET
A
377
16.835
9.930
3.046
1.00
24.15
A


ATOM
2502
O
MET
A
377
16.950
8.847
2.451
1.00
25.02
A


ATOM
2503
N
LEU
A
378
17.556
11.005
2.736
1.00
21.52
A


ATOM
2504
CA
LEU
A
378
18.492
11.056
1.603
1.00
23.77
A


ATOM
2505
CB
LEU
A
378
18.139
12.237
0.684
1.00
23.01
A


ATOM
2506
CG
LEU
A
378
17.070
11.994
−0.405
1.00
30.05
A


ATOM
2507
CD1
LEU
A
378
16.028
11.009
0.022
1.00
28.18
A


ATOM
2508
CD2
LEU
A
378
16.412
13.323
−0.762
1.00
31.19
A


ATOM
2509
C
LEU
A
378
19.942
11.188
2.003
1.00
21.83
A


ATOM
2510
O
LEU
A
378
20.282
11.911
2.935
1.00
18.59
A


ATOM
2511
N
PHE
A
379
20.787
10.490
1.264
1.00
21.15
A


ATOM
2512
CA
PHE
A
379
22.199
10.474
1.498
1.00
23.32
A


ATOM
2513
CB
PHE
A
379
22.593
9.113
2.087
1.00
23.60
A


ATOM
2514
CG
PHE
A
379
22.074
8.892
3.492
1.00
23.39
A


ATOM
2515
CD1
PHE
A
379
22.764
9.407
4.592
1.00
19.85
A


ATOM
2516
CD2
PHE
A
379
20.883
8.209
3.710
1.00
22.46
A


ATOM
2517
CE1
PHE
A
379
22.263
9.242
5.906
1.00
22.76
A


ATOM
2518
CE2
PHE
A
379
20.375
8.036
5.028
1.00
23.81
A


ATOM
2519
CZ
PHE
A
379
21.085
8.564
6.118
1.00
18.24
A


ATOM
2520
C
PHE
A
379
22.889
10.700
0.148
1.00
26.49
A


ATOM
2521
O
PHE
A
379
22.981
9.794
−0.688
1.00
28.51
A


ATOM
2522
N
ASP
A
380
23.315
11.926
−0.076
1.00
26.30
A


ATOM
2523
CA
ASP
A
380
24.026
12.282
−1.281
1.00
28.29
A


ATOM
2524
CB
ASP
A
380
23.932
13.785
−1.515
1.00
31.26
A


ATOM
2525
CG
ASP
A
380
24.746
14.246
−2.705
1.00
35.78
A


ATOM
2526
OD1
ASP
A
380
25.953
13.901
−2.824
1.00
35.50
A


ATOM
2527
OD2
ASP
A
380
24.170
14.984
−3.520
1.00
40.55
A


ATOM
2528
C
ASP
A
380
25.452
11.916
−0.946
1.00
28.54
A


ATOM
2529
O
ASP
A
380
25.957
12.323
0.087
1.00
28.42
A


ATOM
2530
N
PRO
A
381
26.130
11.170
−1.836
1.00
29.66
A


ATOM
2531
CD
PRO
A
381
25.529
10.736
−3.111
1.00
30.64
A


ATOM
2532
CA
PRO
A
381
27.510
10.686
−1.730
1.00
27.72
A


ATOM
2533
CB
PRO
A
381
27.750
10.023
−3.089
1.00
32.71
A


ATOM
2534
CG
PRO
A
381
26.375
9.552
−3.477
1.00
31.83
A


ATOM
2535
C
PRO
A
381
28.534
11.750
−1.459
1.00
26.44
A


ATOM
2536
O
PRO
A
381
29.579
11.460
−0.872
1.00
23.50
A


ATOM
2537
N
THR
A
382
28.259
12.973
−1.916
1.00
25.73
A


ATOM
2538
CA
THR
A
382
29.192
14.082
−1.714
1.00
26.51
A


ATOM
2539
CB
THR
A
382
29.217
15.026
−2.948
1.00
28.88
A


ATOM
2540
OG1
THR
A
382
27.979
15.742
−3.060
1.00
28.59
A


ATOM
2541
CG2
THR
A
382
29.402
14.187
−4.214
1.00
31.70
A


ATOM
2542
C
THR
A
382
28.896
14.887
−0.449
1.00
25.79
A


ATOM
2543
O
THR
A
382
29.664
15.766
−0.065
1.00
26.15
A


ATOM
2544
N
ASP
A
383
27.773
14.588
0.189
1.00
25.03
A


ATOM
2545
CA
ASP
A
383
27.401
15.239
1.448
1.00
25.26
A


ATOM
2546
CB
ASP
A
383
26.030
14.715
1.883
1.00
25.52
A


ATOM
2547
CG
ASP
A
383
25.499
15.378
3.170
1.00
27.35
A


ATOM
2548
OD1
ASP
A
383
26.289
16.041
3.875
1.00
22.90
A


ATOM
2549
OD2
ASP
A
383
24.276
15.208
3.456
1.00
25.08
A


ATOM
2550
C
ASP
A
383
28.457
14.887
2.508
1.00
23.23
A


ATOM
2551
O
ASP
A
383
28.655
13.721
2.837
1.00
23.43
A


ATOM
2552
N
PRO
A
384
29.130
15.890
3.073
1.00
23.44
A


ATOM
2553
CD
PRO
A
384
28.925
17.327
2.815
1.00
25.02
A


ATOM
2554
CA
PRO
A
384
30.157
15.687
4.096
1.00
22.57
A


ATOM
2555
CB
PRO
A
384
30.661
17.110
4.385
1.00
26.48
A


ATOM
2556
CG
PRO
A
384
30.297
17.885
3.109
1.00
28.16
A


ATOM
2557
C
PRO
A
384
29.627
15.035
5.378
1.00
22.82
A


ATOM
2558
O
PRO
A
384
30.406
14.450
6.140
1.00
23.15
A


ATOM
2559
N
PHE
A
385
28.327
15.161
5.644
1.00
21.40
A


ATOM
2560
CA
PHE
A
385
27.767
14.539
6.848
1.00
21.27
A


ATOM
2561
CB
PHE
A
385
27.139
15.598
7.753
1.00
21.78
A


ATOM
2562
CG
PHE
A
385
28.062
16.738
8.064
1.00
24.99
A


ATOM
2563
CD1
PHE
A
385
29.146
16.563
8.938
1.00
25.29
A


ATOM
2564
CD2
PHE
A
385
27.888
17.974
7.448
1.00
24.36
A


ATOM
2565
CE1
PHE
A
385
30.046
17.618
9.196
1.00
27.96
A


ATOM
2566
CE2
PHE
A
385
28.789
19.043
7.699
1.00
26.41
A


ATOM
2567
CZ
PHE
A
385
29.863
18.868
8.572
1.00
22.72
A


ATOM
2568
C
PHE
A
385
26.754
13.442
6.506
1.00
21.88
A


ATOM
2569
O
PHE
A
385
25.733
13.259
7.215
1.00
22.73
A


ATOM
2570
N
LYS
A
386
27.025
12.731
5.404
1.00
21.03
A


ATOM
2571
CA
LYS
A
386
26.196
11.598
5.006
1.00
22.03
A


ATOM
2572
CB
LYS
A
386
26.667
10.955
3.680
1.00
21.87
A


ATOM
2573
CG
LYS
A
386
28.115
10.474
3.622
1.00
24.75
A


ATOM
2574
CD
LYS
A
386
28.460
10.008
2.182
1.00
25.18
A


ATOM
2575
CE
LYS
A
386
29.840
9.343
2.079
1.00
26.61
A


ATOM
2576
NZ
LYS
A
386
30.174
8.992
0.658
1.00
21.10
A


ATOM
2577
C
LYS
A
386
26.280
10.571
6.119
1.00
20.27
A


ATOM
2578
O
LYS
A
386
25.387
9.739
6.245
1.00
23.80
A


ATOM
2579
N
ASN
A
387
27.332
10.612
6.937
1.00
20.30
A


ATOM
2580
CA
ASN
A
387
27.425
9.639
8.034
1.00
20.44
A


ATOM
2581
CB
ASN
A
387
28.808
8.951
8.069
1.00
21.89
A


ATOM
2582
CG
ASN
A
387
29.079
8.100
6.825
1.00
23.30
A


ATOM
2583
OD1
ASN
A
387
30.240
7.882
6.469
1.00
27.15
A


ATOM
2584
ND2
ASN
A
387
28.010
7.617
6.153
1.00
21.07
A


ATOM
2585
C
ASN
A
387
27.107
10.269
9.383
1.00
21.45
A


ATOM
2586
O
ASN
A
387
27.336
9.658
10.416
1.00
22.31
A


ATOM
2587
N
GLY
A
388
26.577
11.498
9.366
1.00
21.38
A


ATOM
2588
CA
GLY
A
388
26.192
12.196
10.586
1.00
19.34
A


ATOM
2589
C
GLY
A
388
27.321
12.737
11.447
1.00
21.22
A


ATOM
2590
O
GLY
A
388
28.514
12.527
11.146
1.00
23.80
A


ATOM
2591
N
PHE
A
389
26.968
13.467
12.510
1.00
18.74
A


ATOM
2592
CA
PHE
A
389
27.982
13.964
13.434
1.00
17.79
A


ATOM
2593
CB
PHE
A
389
28.649
15.247
12.885
1.00
17.04
A


ATOM
2594
CG
PHE
A
389
27.714
16.432
12.822
1.00
18.32
A


ATOM
2595
CD1
PHE
A
389
27.512
17.232
13.941
1.00
18.28
A


ATOM
2596
CD2
PHE
A
389
27.008
16.733
11.632
1.00
15.12
A


ATOM
2597
CE1
PHE
A
389
26.619
18.346
13.898
1.00
19.48
A


ATOM
2598
CE2
PHE
A
389
26.120
17.832
11.577
1.00
17.11
A


ATOM
2599
CZ
PHE
A
389
25.929
18.638
12.712
1.00
17.18
A


ATOM
2600
C
PHE
A
389
27.359
14.259
14.768
1.00
19.18
A


ATOM
2601
O
PHE
A
389
26.134
14.320
14.909
1.00
21.09
A


ATOM
2602
N
THR
A
390
28.201
14.403
15.781
1.00
19.69
A


ATOM
2603
CA
THR
A
390
27.724
14.797
17.088
1.00
21.13
A


ATOM
2604
CB
THR
A
390
27.584
13.627
18.089
1.00
21.00
A


ATOM
2605
OG1
THR
A
390
27.237
14.175
19.363
1.00
19.82
A


ATOM
2606
CG2
THR
A
390
28.879
12.808
18.217
1.00
22.94
A


ATOM
2607
C
THR
A
390
28.745
15.792
17.635
1.00
24.09
A


ATOM
2608
O
THR
A
390
29.933
15.666
17.365
1.00
22.68
A


ATOM
2609
N
LEU
A
391
28.261
16.782
18.375
1.00
26.12
A


ATOM
2610
CA
LEU
A
391
29.106
17.785
18.984
1.00
28.88
A


ATOM
2611
CB
LEU
A
391
28.552
19.180
18.713
1.00
26.23
A


ATOM
2612
CG
LEU
A
391
28.688
19.677
17.276
1.00
26.31
A


ATOM
2613
CD1
LEU
A
391
28.067
21.014
17.147
1.00
26.01
A


ATOM
2614
CD2
LEU
A
391
30.136
19.788
16.908
1.00
28.41
A


ATOM
2615
C
LEU
A
391
29.122
17.542
20.491
1.00
31.62
A


ATOM
2616
O
LEU
A
391
29.577
18.386
21.252
1.00
32.24
A


ATOM
2617
N
LYS
A
392
28.603
16.394
20.912
1.00
33.34
A


ATOM
2618
CA
LYS
A
392
28.546
16.073
22.323
1.00
34.57
A


ATOM
2619
CB
LYS
A
392
27.766
14.780
22.549
1.00
33.29
A


ATOM
2620
CG
LYS
A
392
27.738
14.379
23.993
1.00
34.77
A


ATOM
2621
CD
LYS
A
392
26.619
13.425
24.307
1.00
34.56
A


ATOM
2622
CE
LYS
A
392
25.318
14.133
24.426
1.00
33.28
A


ATOM
2623
NZ
LYS
A
392
24.299
13.198
24.994
1.00
33.67
A


ATOM
2624
C
LYS
A
392
29.936
15.984
22.947
1.00
38.13
A


ATOM
2625
O
LYS
A
392
30.821
15.272
22.454
1.00
36.18
A


ATOM
2626
N
GLN
A
393
30.090
16.746
24.034
1.00
42.81
A


ATOM
2627
CA
GLN
A
393
31.311
16.868
24.823
1.00
46.40
A


ATOM
2628
CB
GLN
A
393
30.980
17.198
26.304
1.00
49.81
A


ATOM
2629
CG
GLN
A
393
30.051
18.413
26.602
1.00
53.16
A


ATOM
2630
CD
GLN
A
393
28.543
18.152
26.351
1.00
55.09
A


ATOM
2631
OE1
GLN
A
393
28.016
18.484
25.281
1.00
54.47
A


ATOM
2632
NE2
GLN
A
393
27.851
17.558
27.349
1.00
54.52
A


ATOM
2633
C
GLN
A
393
32.110
15.573
24.769
1.00
47.02
A


ATOM
2634
O
GLN
A
393
33.239
15.641
24.241
1.00
47.43
A


ATOM
2635
OXT
GLN
A
393
31.604
14.523
25.259
1.00
46.13
A


ATOM
2636
CB
LYS
B
44
−3.895
17.367
10.930
1.00
40.26
B


ATOM
2637
CG
LYS
B
44
−3.878
15.921
11.439
1.00
44.51
B


ATOM
2638
CD
LYS
B
44
−5.260
15.273
11.545
1.00
43.81
B


ATOM
2639
CE
LYS
B
44
−6.060
15.764
12.744
1.00
45.37
B


ATOM
2640
NZ
LYS
B
44
−6.512
17.191
12.732
1.00
46.86
B


ATOM
2641
C
LYS
B
44
−1.430
17.413
10.215
1.00
37.97
B


ATOM
2642
O
LYS
B
44
−0.781
16.450
10.675
1.00
37.22
B


ATOM
2643
N
LYS
B
44
−2.717
19.537
10.824
1.00
39.54
B


ATOM
2644
CA
LYS
B
44
−2.543
18.082
11.083
1.00
38.58
B


ATOM
2645
N
SER
B
45
−1.181
17.915
8.996
1.00
32.98
B


ATOM
2646
CA
SER
B
45
−0.119
17.359
8.146
1.00
29.60
B


ATOM
2647
CB
SER
B
45
−0.721
16.333
7.204
1.00
31.39
B


ATOM
2648
OG
SER
B
45
0.290
15.796
6.386
1.00
36.45
B


ATOM
2649
C
SER
B
45
0.682
18.394
7.319
1.00
27.30
B


ATOM
2650
O
SER
B
45
0.076
19.151
6.553
1.00
27.94
B


ATOM
2651
N
PHE
B
46
2.021
18.418
7.438
1.00
21.85
B


ATOM
2652
CA
PHE
B
46
2.865
19.370
6.688
1.00
19.64
B


ATOM
2653
CB
PHE
B
46
3.648
20.358
7.592
1.00
20.10
B


ATOM
2654
CG
PHE
B
46
2.812
21.115
8.573
1.00
24.21
B


ATOM
2655
CD1
PHE
B
46
1.500
21.446
8.304
1.00
29.13
B


ATOM
2656
CD2
PHE
B
46
3.346
21.506
9.792
1.00
29.91
B


ATOM
2657
CE1
PHE
B
46
0.728
22.151
9.238
1.00
31.63
B


ATOM
2658
CE2
PHE
B
46
2.569
22.214
10.725
1.00
30.48
B


ATOM
2659
CZ
PHE
B
46
1.268
22.529
10.447
1.00
26.55
B


ATOM
2660
C
PHE
B
46
3.934
18.646
5.903
1.00
20.23
B


ATOM
2661
O
PHE
B
46
4.516
17.661
6.385
1.00
18.88
B


ATOM
2662
N
THR
B
47
4.240
19.169
4.722
1.00
15.03
B


ATOM
2663
CA
THR
B
47
5.281
18.620
3.887
1.00
18.20
B


ATOM
2664
CB
THR
B
47
4.849
18.682
2.362
1.00
20.20
B


ATOM
2665
OG1
THR
B
47
3.830
17.692
2.127
1.00
26.52
B


ATOM
2666
CG2
THR
B
47
5.996
18.358
1.496
1.00
23.55
B


ATOM
2667
C
THR
B
47
6.550
19.450
4.115
1.00
15.89
B


ATOM
2668
O
THR
B
47
6.485
20.669
4.141
1.00
14.37
B


ATOM
2669
N
CYS
B
48
7.700
18.788
4.261
1.00
16.18
B


ATOM
2670
CA
CYS
B
48
8.946
19.488
4.488
1.00
17.12
B


ATOM
2671
CB
CYS
B
48
9.494
19.235
5.926
1.00
18.54
B


ATOM
2672
SG
CYS
B
48
8.389
19.800
7.152
1.00
27.91
B


ATOM
2673
C
CYS
B
48
10.009
18.980
3.573
1.00
17.53
B


ATOM
2674
O
CYS
B
48
10.087
17.774
3.318
1.00
17.05
B


ATOM
2675
N
ILE
B
49
10.862
19.887
3.126
1.00
13.88
B


ATOM
2676
CA
ILE
B
49
12.018
19.448
2.378
1.00
15.60
B


ATOM
2677
CB
ILE
B
49
12.335
20.308
1.152
1.00
14.75
B


ATOM
2678
CG2
ILE
B
49
13.680
19.854
0.596
1.00
11.21
B


ATOM
2679
CG1
ILE
B
49
11.169
20.209
0.137
1.00
15.44
B


ATOM
2680
CD1
ILE
B
49
11.328
21.092
−1.162
1.00
23.66
B


ATOM
2681
C
ILE
B
49
13.073
19.709
3.434
1.00
16.35
B


ATOM
2682
O
ILE
B
49
13.358
20.871
3.735
1.00
16.53
B


ATOM
2683
N
ASP
B
50
13.595
18.636
4.033
1.00
16.66
B


ATOM
2684
CA
ASP
B
50
14.627
18.724
5.068
1.00
19.15
B


ATOM
2685
CB
ASP
B
50
14.600
17.503
6.029
1.00
18.41
B


ATOM
2686
CG
ASP
B
50
13.511
17.608
7.093
1.00
19.55
B


ATOM
2687
OD1
ASP
B
50
12.903
18.676
7.252
1.00
22.93
B


ATOM
2688
OD2
ASP
B
50
13.256
16.636
7.812
1.00
24.62
B


ATOM
2689
C
ASP
B
50
15.988
18.846
4.419
1.00
19.18
B


ATOM
2690
O
ASP
B
50
16.442
18.009
3.610
1.00
20.35
B


ATOM
2691
N
MET
B
51
16.648
19.931
4.746
1.00
19.24
B


ATOM
2692
CA
MET
B
51
17.963
20.137
4.182
1.00
21.10
B


ATOM
2693
CB
MET
B
51
17.902
21.253
3.177
1.00
22.58
B


ATOM
2694
CG
MET
B
51
16.991
20.860
2.013
1.00
29.45
B


ATOM
2695
SD
MET
B
51
16.967
22.192
0.962
1.00
35.46
B


ATOM
2696
CE
MET
B
51
18.548
21.823
0.104
1.00
28.53
B


ATOM
2697
C
MET
B
51
18.912
20.515
5.269
1.00
16.61
B


ATOM
2698
O
MET
B
51
18.490
20.652
6.401
1.00
15.13
B


ATOM
2699
N
HIS
B
52
20.188
20.627
4.905
1.00
15.80
B


ATOM
2700
CA
HIS
B
52
21.213
21.144
5.812
1.00
15.68
B


ATOM
2701
CB
HIS
B
52
21.898
20.048
6.694
1.00
13.58
B


ATOM
2702
CG
HIS
B
52
22.889
19.185
5.971
1.00
12.15
B


ATOM
2703
CD2
HIS
B
52
22.734
18.021
5.281
1.00
10.68
B


ATOM
2704
ND1
HIS
B
52
24.236
19.467
5.950
1.00
12.26
B


ATOM
2705
CE1
HIS
B
52
24.874
18.515
5.281
1.00
13.59
B


ATOM
2706
NE2
HIS
B
52
23.986
17.626
4.866
1.00
14.03
B


ATOM
2707
C
HIS
B
52
22.226
21.909
4.963
1.00
15.91
B


ATOM
2708
O
HIS
B
52
22.485
21.601
3.777
1.00
14.81
B


ATOM
2709
N
THR
B
53
22.769
22.950
5.558
1.00
14.81
B


ATOM
2710
CA
THR
B
53
23.767
23.735
4.859
1.00
16.70
B


ATOM
2711
CB
THR
B
53
23.388
25.216
4.816
1.00
16.27
B


ATOM
2712
OG1
THR
B
53
22.153
25.356
4.102
1.00
17.55
B


ATOM
2713
CG2
THR
B
53
24.489
26.023
4.139
1.00
16.30
B


ATOM
2714
C
THR
B
53
25.034
23.552
5.661
1.00
17.07
B


ATOM
2715
O
THR
B
53
25.173
24.130
6.711
1.00
16.97
B


ATOM
2716
N
GLU
B
54
25.920
22.693
5.175
1.00
19.66
B


ATOM
2717
CA
GLU
B
54
27.171
22.407
5.827
1.00
21.98
B


ATOM
2718
CB
GLU
B
54
28.111
23.606
5.623
1.00
27.55
B


ATOM
2719
CG
GLU
B
54
28.555
23.621
4.135
1.00
29.59
B


ATOM
2720
CD
GLU
B
54
29.305
24.862
3.716
1.00
34.78
B


ATOM
2721
OE1
GLU
B
54
30.255
25.198
4.449
1.00
36.74
B


ATOM
2722
OE2
GLU
B
54
28.952
25.482
2.661
1.00
33.93
B


ATOM
2723
C
GLU
B
54
26.995
22.019
7.277
1.00
22.64
B


ATOM
2724
O
GLU
B
54
27.751
22.458
8.166
1.00
23.61
B


ATOM
2725
N
GLY
B
55
25.978
21.185
7.513
1.00
19.39
B


ATOM
2726
CA
GLY
B
55
25.719
20.725
8.872
1.00
22.16
B


ATOM
2727
C
GLY
B
55
24.588
21.400
9.642
1.00
20.18
B


ATOM
2728
O
GLY
B
55
24.066
20.831
10.612
1.00
21.32
B


ATOM
2729
N
GLU
B
56
24.214
22.612
9.236
1.00
18.08
B


ATOM
2730
CA
GLU
B
56
23.133
23.337
9.910
1.00
17.90
B


ATOM
2731
CB
GLU
B
56
23.387
24.857
9.826
1.00
15.66
B


ATOM
2732
CG
GLU
B
56
22.316
25.716
10.478
1.00
17.78
B


ATOM
2733
CD
GLU
B
56
22.255
25.543
11.992
1.00
19.03
B


ATOM
2734
OE1
GLU
B
56
23.192
24.909
12.526
1.00
19.54
B


ATOM
2735
OE2
GLU
B
56
21.278
26.037
12.655
1.00
17.01
B


ATOM
2736
C
GLU
B
56
21.782
23.002
9.250
1.00
17.16
B


ATOM
2737
O
GLU
B
56
21.610
23.179
8.029
1.00
13.95
B


ATOM
2738
N
ALA
B
57
20.823
22.557
10.050
1.00
17.49
B


ATOM
2739
CA
ALA
B
57
19.529
22.205
9.492
1.00
19.53
B


ATOM
2740
CB
ALA
B
57
18.647
21.565
10.510
1.00
19.15
B


ATOM
2741
C
ALA
B
57
18.789
23.373
8.866
1.00
18.75
B


ATOM
2742
O
ALA
B
57
18.973
24.532
9.222
1.00
16.43
B


ATOM
2743
N
ALA
B
58
17.928
23.012
7.922
1.00
18.84
B


ATOM
2744
CA
ALA
B
58
17.086
23.957
7.204
1.00
17.24
B


ATOM
2745
CB
ALA
B
58
17.824
24.464
5.959
1.00
17.38
B


ATOM
2746
C
ALA
B
58
15.830
23.179
6.812
1.00
14.53
B


ATOM
2747
O
ALA
B
58
15.744
22.640
5.714
1.00
15.00
B


ATOM
2748
N
ARG
B
59
14.862
23.144
7.716
1.00
15.19
B


ATOM
2749
CA
ARG
B
59
13.611
22.437
7.498
1.00
15.97
B


ATOM
2750
CB
ARG
B
59
13.024
21.943
8.847
1.00
13.98
B


ATOM
2751
CG
ARG
B
59
11.585
21.468
8.813
1.00
16.23
B


ATOM
2752
CD
ARG
B
59
11.251
20.594
10.031
1.00
15.13
B


ATOM
2753
NE
ARG
B
59
12.080
19.404
9.963
1.00
15.99
B


ATOM
2754
CZ
ARG
B
59
12.349
18.609
10.979
1.00
19.09
B


ATOM
2755
NH1
ARG
B
59
11.866
18.855
12.199
1.00
21.74
B


ATOM
2756
NH2
ARG
B
59
13.089
17.552
10.760
1.00
18.68
B


ATOM
2757
C
ARG
B
59
12.655
23.378
6.803
1.00
16.30
B


ATOM
2758
O
ARG
B
59
12.084
24.268
7.426
1.00
14.64
B


ATOM
2759
N
ILE
B
60
12.464
23.154
5.502
1.00
17.44
B


ATOM
2760
CA
ILE
B
60
11.589
24.028
4.713
1.00
14.54
B


ATOM
2761
CB
ILE
B
60
12.224
24.302
3.341
1.00
14.79
B


ATOM
2762
CG2
ILE
B
60
11.309
25.206
2.480
1.00
17.69
B


ATOM
2763
CG1
ILE
B
60
13.549
24.991
3.566
1.00
15.38
B


ATOM
2764
CD1
ILE
B
60
14.481
25.009
2.372
1.00
16.72
B


ATOM
2765
C
ILE
B
60
10.199
23.471
4.554
1.00
15.46
B


ATOM
2766
O
ILE
B
60
9.985
22.497
3.844
1.00
15.09
B


ATOM
2767
N
VAL
B
61
9.245
24.109
5.213
1.00
13.03
B


ATOM
2768
CA
VAL
B
61
7.876
23.667
5.155
1.00
16.99
B


ATOM
2769
CB
VAL
B
61
7.113
24.231
6.326
1.00
14.16
B


ATOM
2770
CG1
VAL
B
61
5.642
23.739
6.328
1.00
12.57
B


ATOM
2771
CG2
VAL
B
61
7.836
23.803
7.606
1.00
14.78
B


ATOM
2772
C
VAL
B
61
7.280
24.189
3.834
1.00
17.71
B


ATOM
2773
O
VAL
B
61
7.136
25.401
3.652
1.00
13.04
B


ATOM
2774
N
THR
B
62
6.912
23.267
2.951
1.00
18.07
B


ATOM
2775
CA
THR
B
62
6.392
23.619
1.626
1.00
17.61
B


ATOM
2776
CB
THR
B
62
7.015
22.725
0.556
1.00
17.82
B


ATOM
2777
OG1
THR
B
62
6.807
21.357
0.927
1.00
17.48
B


ATOM
2778
CG2
THR
B
62
8.525
22.970
0.438
1.00
15.38
B


ATOM
2779
C
THR
B
62
4.867
23.556
1.485
1.00
20.81
B


ATOM
2780
O
THR
B
62
4.324
24.050
0.485
1.00
22.90
B


ATOM
2781
N
SER
B
63
4.169
22.913
2.416
1.00
20.20
B


ATOM
2782
CA
SER
B
63
2.717
22.920
2.374
1.00
22.57
B


ATOM
2783
CB
SER
B
63
2.141
22.186
1.146
1.00
24.53
B


ATOM
2784
OG
SER
B
63
2.452
20.829
1.129
1.00
29.31
B


ATOM
2785
C
SER
B
63
2.087
22.378
3.614
1.00
23.17
B


ATOM
2786
O
SER
B
63
2.767
21.814
4.481
1.00
23.98
B


ATOM
2787
N
GLY
B
64
0.781
22.597
3.725
1.00
21.02
B


ATOM
2788
CA
GLY
B
64
0.051
22.105
4.870
1.00
20.80
B


ATOM
2789
C
GLY
B
64
−0.236
23.144
5.925
1.00
19.04
B


ATOM
2790
O
GLY
B
64
−1.079
22.922
6.753
1.00
17.06
B


ATOM
2791
N
LEU
B
65
0.429
24.293
5.873
1.00
21.03
B


ATOM
2792
CA
LEU
B
65
0.172
25.371
6.821
1.00
21.79
B


ATOM
2793
CB
LEU
B
65
1.180
26.492
6.627
1.00
23.81
B


ATOM
2794
CG
LEU
B
65
2.624
26.002
6.721
1.00
31.25
B


ATOM
2795
CD1
LEU
B
65
3.587
27.183
6.412
1.00
33.04
B


ATOM
2796
CD2
LEU
B
65
2.886
25.418
8.131
1.00
31.57
B


ATOM
2797
C
LEU
B
65
−1.183
26.013
6.664
1.00
22.53
B


ATOM
2798
O
LEU
B
65
−1.692
26.147
5.552
1.00
23.83
B


ATOM
2799
N
PRO
B
66
−1.796
26.431
7.779
1.00
23.83
B


ATOM
2800
CD
PRO
B
66
−1.330
26.367
9.184
1.00
22.92
B


ATOM
2801
CA
PRO
B
66
−3.095
27.085
7.670
1.00
20.45
B


ATOM
2802
CB
PRO
B
66
−3.453
27.435
9.116
1.00
23.47
B


ATOM
2803
CG
PRO
B
66
−2.607
26.508
9.946
1.00
22.68
B


ATOM
2804
C
PRO
B
66
−2.816
28.383
6.901
1.00
22.07
B


ATOM
2805
O
PRO
B
66
−1.657
28.831
6.782
1.00
22.24
B


ATOM
2806
N
HIS
B
67
−3.877
29.011
6.423
1.00
22.84
B


ATOM
2807
CA
HIS
B
67
−3.782
30.269
5.696
1.00
24.81
B


ATOM
2808
CB
HIS
B
67
−5.035
30.411
4.849
1.00
25.33
B


ATOM
2809
CG
HIS
B
67
−4.959
29.596
3.600
1.00
24.38
B


ATOM
2810
CD2
HIS
B
67
−5.666
28.522
3.185
1.00
23.83
B


ATOM
2811
ND1
HIS
B
67
−3.984
29.806
2.647
1.00
26.91
B


ATOM
2812
CE1
HIS
B
67
−4.097
28.895
1.695
1.00
24.42
B


ATOM
2813
NE2
HIS
B
67
−5.113
28.106
1.999
1.00
23.01
B


ATOM
2814
C
HIS
B
67
−3.581
31.426
6.684
1.00
26.08
B


ATOM
2815
O
HIS
B
67
−4.302
31.558
7.675
1.00
27.39
B


ATOM
2816
N
ILE
B
68
−2.589
32.242
6.388
1.00
25.17
B


ATOM
2817
CA
ILE
B
68
−2.123
33.364
7.234
1.00
29.31
B


ATOM
2818
CB
ILE
B
68
−0.576
33.114
7.519
1.00
30.05
B


ATOM
2819
CG2
ILE
B
68
0.070
34.226
8.270
1.00
31.44
B


ATOM
2820
CG1
ILE
B
68
−0.424
31.817
8.286
1.00
33.73
B


ATOM
2821
CD1
ILE
B
68
−1.347
31.747
9.448
1.00
32.00
B


ATOM
2822
C
ILE
B
68
−2.281
34.753
6.576
1.00
27.45
B


ATOM
2823
O
ILE
B
68
−1.871
34.926
5.431
1.00
26.19
B


ATOM
2824
N
PRO
B
69
−2.845
35.757
7.296
1.00
27.51
B


ATOM
2825
CD
PRO
B
69
−3.318
35.680
8.689
1.00
28.93
B


ATOM
2826
CA
PRO
B
69
−3.017
37.119
6.758
1.00
24.72
B


ATOM
2827
CB
PRO
B
69
−3.853
37.834
7.820
1.00
28.44
B


ATOM
2828
CG
PRO
B
69
−4.361
36.717
8.724
1.00
30.40
B


ATOM
2829
C
PRO
B
69
−1.661
37.789
6.656
1.00
24.01
B


ATOM
2830
O
PRO
B
69
−0.639
37.181
6.941
1.00
25.75
B


ATOM
2831
N
GLY
B
70
−1.642
39.059
6.276
1.00
27.17
B


ATOM
2832
CA
GLY
B
70
−0.386
39.794
6.213
1.00
24.42
B


ATOM
2833
C
GLY
B
70
−0.143
40.435
4.879
1.00
25.87
B


ATOM
2834
O
GLY
B
70
−0.362
39.789
3.850
1.00
26.98
B


ATOM
2835
N
SER
B
71
0.330
41.682
4.879
1.00
22.99
B


ATOM
2836
CA
SER
B
71
0.575
42.368
3.623
1.00
24.10
B


ATOM
2837
CB
SER
B
71
−0.076
43.770
3.659
1.00
27.25
B


ATOM
2838
OG
SER
B
71
0.501
44.598
4.638
1.00
30.35
B


ATOM
2839
C
SER
B
71
2.052
42.446
3.236
1.00
23.85
B


ATOM
2840
O
SER
B
71
2.420
43.091
2.262
1.00
23.56
B


ATOM
2841
N
ASN
B
72
2.905
41.808
4.028
1.00
21.63
B


ATOM
2842
CA
ASN
B
72
4.330
41.716
3.740
1.00
21.97
B


ATOM
2843
CB
ASN
B
72
5.049
43.073
3.933
1.00
23.34
B


ATOM
2844
CG
ASN
B
72
4.960
43.582
5.333
1.00
25.21
B


ATOM
2845
OD1
ASN
B
72
5.221
42.854
6.284
1.00
24.44
B


ATOM
2846
ND2
ASN
B
72
4.579
44.839
5.479
1.00
27.10
B


ATOM
2847
C
ASN
B
72
4.881
40.574
4.635
1.00
18.79
B


ATOM
2848
O
ASN
B
72
4.203
40.138
5.536
1.00
19.39
B


ATOM
2849
N
MET
B
73
6.053
40.032
4.308
1.00
21.09
B


ATOM
2850
CA
MET
B
73
6.602
38.919
5.037
1.00
20.53
B


ATOM
2851
CB
MET
B
73
7.883
38.409
4.351
1.00
21.73
B


ATOM
2852
CG
MET
B
73
7.660
37.504
3.118
1.00
26.09
B


ATOM
2853
SD
MET
B
73
6.349
36.315
3.372
1.00
24.28
B


ATOM
2854
CE
MET
B
73
7.254
34.956
3.846
1.00
37.90
B


ATOM
2855
C
MET
B
73
6.875
39.241
6.513
1.00
22.95
B


ATOM
2856
O
MET
B
73
6.856
38.327
7.330
1.00
22.05
B


ATOM
2857
N
ALA
B
74
7.155
40.510
6.850
1.00
22.95
B


ATOM
2858
CA
ALA
B
74
7.394
40.888
8.256
1.00
23.73
B


ATOM
2859
CB
ALA
B
74
7.910
42.352
8.374
1.00
22.58
B


ATOM
2860
C
ALA
B
74
6.075
40.734
8.993
1.00
24.38
B


ATOM
2861
O
ALA
B
74
6.063
40.296
10.140
1.00
21.32
B


ATOM
2862
N
GLU
B
75
4.942
41.058
8.350
1.00
22.42
B


ATOM
2863
CA
GLU
B
75
3.671
40.868
9.064
1.00
23.26
B


ATOM
2864
CB
GLU
B
75
2.510
41.632
8.434
1.00
21.51
B


ATOM
2865
CG
GLU
B
75
2.625
43.142
8.648
1.00
30.04
B


ATOM
2866
CD
GLU
B
75
1.533
43.935
7.922
1.00
34.70
B


ATOM
2867
OE1
GLU
B
75
1.561
45.190
8.010
1.00
39.30
B


ATOM
2868
OE2
GLU
B
75
0.660
43.310
7.269
1.00
34.22
B


ATOM
2869
C
GLU
B
75
3.283
39.398
9.158
1.00
21.95
B


ATOM
2870
O
GLU
B
75
2.601
38.998
10.098
1.00
23.57
B


ATOM
2871
N
LYS
B
76
3.685
38.593
8.183
1.00
19.88
B


ATOM
2872
CA
LYS
B
76
3.343
37.159
8.270
1.00
22.05
B


ATOM
2873
CB
LYS
B
76
3.677
36.423
6.960
1.00
21.17
B


ATOM
2874
CG
LYS
B
76
2.664
36.742
5.873
1.00
25.60
B


ATOM
2875
CD
LYS
B
76
2.543
35.595
4.865
1.00
26.77
B


ATOM
2876
CE
LYS
B
76
1.596
35.965
3.764
1.00
26.27
B


ATOM
2877
NZ
LYS
B
76
0.210
35.664
4.200
1.00
28.52
B


ATOM
2878
C
LYS
B
76
4.126
36.531
9.438
1.00
18.93
B


ATOM
2879
O
LYS
B
76
3.584
35.747
10.177
1.00
18.28
B


ATOM
2880
N
LYS
B
77
5.411
36.876
9.561
1.00
20.23
B


ATOM
2881
CA
LYS
B
77
6.227
36.403
10.673
1.00
20.30
B


ATOM
2882
CB
LYS
B
77
7.625
37.008
10.593
1.00
20.58
B


ATOM
2883
CG
LYS
B
77
8.515
36.695
11.805
1.00
24.45
B


ATOM
2884
CD
LYS
B
77
9.762
37.625
11.843
1.00
24.32
B


ATOM
2885
CE
LYS
B
77
9.486
38.814
12.697
1.00
29.37
B


ATOM
2886
NZ
LYS
B
77
10.665
39.704
12.697
1.00
31.25
B


ATOM
2887
C
LYS
B
77
5.568
36.818
11.991
1.00
19.06
B


ATOM
2888
O
LYS
B
77
5.415
35.990
12.891
1.00
22.30
B


ATOM
2889
N
ALA
B
78
5.166
38.085
12.120
1.00
20.24
B


ATOM
2890
CA
ALA
B
78
4.518
38.551
13.351
1.00
18.54
B


ATOM
2891
CB
ALA
B
78
4.301
40.136
13.321
1.00
20.71
B


ATOM
2892
C
ALA
B
78
3.203
37.834
13.637
1.00
19.22
B


ATOM
2893
O
ALA
B
78
2.884
37.496
14.803
1.00
17.38
B


ATOM
2894
N
TYR
B
79
2.418
37.566
12.598
1.00
17.23
B


ATOM
2895
CA
TYR
B
79
1.155
36.866
12.844
1.00
17.32
B


ATOM
2896
CB
TYR
B
79
0.344
36.667
11.553
1.00
18.14
B


ATOM
2897
CG
TYR
B
79
−1.040
36.086
11.796
1.00
19.45
B


ATOM
2898
CD1
TYR
B
79
−2.107
36.915
12.136
1.00
19.81
B


ATOM
2899
CE1
TYR
B
79
−3.335
36.413
12.402
1.00
21.23
B


ATOM
2900
CD2
TYR
B
79
−1.265
34.711
11.733
1.00
21.03
B


ATOM
2901
CE2
TYR
B
79
−2.512
34.185
12.009
1.00
22.82
B


ATOM
2902
CZ
TYR
B
79
−3.542
35.056
12.340
1.00
24.67
B


ATOM
2903
OH
TYR
B
79
−4.800
34.575
12.577
1.00
29.09
B


ATOM
2904
C
TYR
B
79
1.449
35.475
13.425
1.00
16.70
B


ATOM
2905
O
TYR
B
79
0.727
35.030
14.292
1.00
17.53
B


ATOM
2906
N
LEU
B
80
2.484
34.793
12.919
1.00
15.64
B


ATOM
2907
CA
LEU
B
80
2.823
33.437
13.403
1.00
15.86
B


ATOM
2908
CB
LEU
B
80
3.943
32.809
12.554
1.00
13.89
B


ATOM
2909
CG
LEU
B
80
3.541
32.471
11.089
1.00
15.35
B


ATOM
2910
CD1
LEU
B
80
4.787
32.093
10.245
1.00
15.67
B


ATOM
2911
CD2
LEU
B
80
2.530
31.343
11.114
1.00
18.07
B


ATOM
2912
C
LEU
B
80
3.281
33.500
14.857
1.00
17.50
B


ATOM
2913
O
LEU
B
80
2.801
32.737
15.714
1.00
18.00
B


ATOM
2914
N
GLN
B
81
4.204
34.429
15.105
1.00
19.78
B


ATOM
2915
CA
GLN
B
81
4.784
34.660
16.423
1.00
22.99
B


ATOM
2916
CB
GLN
B
81
5.789
35.814
16.343
1.00
24.52
B


ATOM
2917
CG
GLN
B
81
6.309
36.294
17.672
1.00
34.22
B


ATOM
2918
CD
GLN
B
81
7.775
36.672
17.583
1.00
39.07
B


ATOM
2919
OE1
GLN
B
81
8.606
36.156
18.343
1.00
43.27
B


ATOM
2920
NE2
GLN
B
81
8.107
37.556
16.642
1.00
40.22
B


ATOM
2921
C
GLN
B
81
3.722
34.947
17.463
1.00
23.63
B


ATOM
2922
O
GLN
B
81
3.724
34.329
18.525
1.00
23.61
B


ATOM
2923
N
GLU
B
82
2.796
35.850
17.143
1.00
22.09
B


ATOM
2924
CA
GLU
B
82
1.728
36.219
18.059
1.00
23.23
B


ATOM
2925
CB
GLU
B
82
1.226
37.641
17.734
1.00
25.57
B


ATOM
2926
CG
GLU
B
82
2.341
38.721
17.855
1.00
32.60
B


ATOM
2927
CD
GLU
B
82
2.073
40.036
17.076
1.00
35.87
B


ATOM
2928
OE1
GLU
B
82
0.910
40.472
16.988
1.00
39.19
B


ATOM
2929
OE2
GLU
B
82
3.043
40.638
16.565
1.00
38.90
B


ATOM
2930
C
GLU
B
82
0.522
35.308
18.159
1.00
22.18
B


ATOM
2931
O
GLU
B
82
−0.059
35.201
19.226
1.00
25.71
B


ATOM
2932
N
ASN
B
83
0.112
34.648
17.087
1.00
22.06
B


ATOM
2933
CA
ASN
B
83
−1.105
33.808
17.160
1.00
19.46
B


ATOM
2934
CB
ASN
B
83
−2.130
34.327
16.149
1.00
22.79
B


ATOM
2935
CG
ASN
B
83
−2.373
35.819
16.283
1.00
25.14
B


ATOM
2936
OD1
ASN
B
83
−2.885
36.274
17.301
1.00
29.38
B


ATOM
2937
ND2
ASN
B
83
−1.975
36.593
15.268
1.00
28.55
B


ATOM
2938
C
ASN
B
83
−0.950
32.303
16.922
1.00
19.81
B


ATOM
2939
O
ASN
B
83
−1.841
31.535
17.275
1.00
20.66
B


ATOM
2940
N
MET
B
84
0.134
31.864
16.300
1.00
19.13
B


ATOM
2941
CA
MET
B
84
0.267
30.412
16.031
1.00
21.56
B


ATOM
2942
CB
MET
B
84
−0.058
30.108
14.553
1.00
23.06
B


ATOM
2943
CG
MET
B
84
−1.324
30.804
14.080
1.00
30.92
B


ATOM
2944
SD
MET
B
84
−1.914
30.194
12.473
1.00
36.39
B


ATOM
2945
CE
MET
B
84
−3.423
29.460
12.986
1.00
35.29
B


ATOM
2946
C
MET
B
84
1.661
29.921
16.309
1.00
18.45
B


ATOM
2947
O
MET
B
84
2.240
29.181
15.481
1.00
17.30
B


ATOM
2948
N
ASP
B
85
2.222
30.328
17.454
1.00
16.51
B


ATOM
2949
CA
ASP
B
85
3.605
29.948
17.757
1.00
15.72
B


ATOM
2950
CB
ASP
B
85
4.164
30.761
18.944
1.00
13.71
B


ATOM
2951
CG
ASP
B
85
5.652
30.611
19.088
1.00
13.65
B


ATOM
2952
OD1
ASP
B
85
6.092
30.230
20.195
1.00
21.40
B


ATOM
2953
OD2
ASP
B
85
6.407
30.859
18.115
1.00
16.59
B


ATOM
2954
C
ASP
B
85
3.719
28.468
18.027
1.00
14.08
B


ATOM
2955
O
ASP
B
85
4.814
27.920
18.069
1.00
14.59
B


ATOM
2956
N
TYR
B
86
2.599
27.802
18.210
1.00
14.71
B


ATOM
2957
CA
TYR
B
86
2.668
26.360
18.445
1.00
16.89
B


ATOM
2958
CB
TYR
B
86
1.334
25.853
18.968
1.00
17.61
B


ATOM
2959
CG
TYR
B
86
0.181
26.250
18.089
1.00
25.22
B


ATOM
2960
CD1
TYR
B
86
−0.166
25.489
16.997
1.00
22.80
B


ATOM
2961
CE1
TYR
B
86
−1.238
25.850
16.162
1.00
30.23
B


ATOM
2962
CD2
TYR
B
86
−0.557
27.409
18.355
1.00
28.72
B


ATOM
2963
CE2
TYR
B
86
−1.622
27.779
17.539
1.00
31.23
B


ATOM
2964
CZ
TYR
B
86
−1.959
26.988
16.448
1.00
31.51
B


ATOM
2965
OH
TYR
B
86
−3.054
27.310
15.683
1.00
36.09
B


ATOM
2966
C
TYR
B
86
3.085
25.591
17.166
1.00
17.90
B


ATOM
2967
O
TYR
B
86
3.524
24.441
17.261
1.00
17.85
B


ATOM
2968
N
LEU
B
87
2.961
26.205
15.985
1.00
15.55
B


ATOM
2969
CA
LEU
B
87
3.387
25.518
14.747
1.00
16.00
B


ATOM
2970
CB
LEU
B
87
2.914
26.284
13.493
1.00
16.39
B


ATOM
2971
CG
LEU
B
87
1.388
26.390
13.320
1.00
18.77
B


ATOM
2972
CD1
LEU
B
87
1.104
27.272
12.069
1.00
23.28
B


ATOM
2973
CD2
LEU
B
87
0.731
24.991
13.116
1.00
21.10
B


ATOM
2974
C
LEU
B
87
4.910
25.446
14.761
1.00
14.98
B


ATOM
2975
O
LEU
B
87
5.498
24.399
14.512
1.00
16.96
B


ATOM
2976
N
ARG
B
88
5.555
26.566
15.056
1.00
12.31
B


ATOM
2977
CA
ARG
B
88
7.002
26.599
15.131
1.00
12.40
B


ATOM
2978
CB
ARG
B
88
7.505
28.031
15.512
1.00
10.87
B


ATOM
2979
CG
ARG
B
88
9.011
28.105
15.864
1.00
14.15
B


ATOM
2980
CD
ARG
B
88
9.444
29.453
16.494
1.00
11.28
B


ATOM
2981
NE
ARG
B
88
8.833
29.650
17.820
1.00
14.14
B


ATOM
2982
CZ
ARG
B
88
9.340
29.174
18.967
1.00
14.03
B


ATOM
2983
NH1
ARG
B
88
10.480
28.473
18.965
1.00
13.10
B


ATOM
2984
NH2
ARG
B
88
8.696
29.377
20.109
1.00
11.86
B


ATOM
2985
C
ARG
B
88
7.470
25.588
16.183
1.00
11.03
B


ATOM
2986
O
ARG
B
88
8.392
24.795
15.968
1.00
13.86
B


ATOM
2987
N
ARG
B
89
6.828
25.582
17.318
1.00
11.77
B


ATOM
2988
CA
ARG
B
89
7.288
24.664
18.368
1.00
14.54
B


ATOM
2989
CB
ARG
B
89
6.540
24.942
19.669
1.00
11.21
B


ATOM
2990
CG
ARG
B
89
6.949
26.245
20.341
1.00
17.33
B


ATOM
2991
CD
ARG
B
89
6.138
26.435
21.631
1.00
22.04
B


ATOM
2992
NE
ARG
B
89
5.029
27.377
21.482
1.00
31.04
B


ATOM
2993
CZ
ARG
B
89
3.749
27.138
21.819
1.00
31.50
B


ATOM
2994
NH1
ARG
B
89
3.361
25.966
22.321
1.00
31.74
B


ATOM
2995
NH2
ARG
B
89
2.855
28.112
21.709
1.00
29.91
B


ATOM
2996
C
ARG
B
89
7.141
23.191
17.997
1.00
12.87
B


ATOM
2997
O
ARG
B
89
8.042
22.404
18.272
1.00
11.30
B


ATOM
2998
N
GLY
B
90
6.007
22.829
17.390
1.00
10.76
B


ATOM
2999
CA
GLY
B
90
5.806
21.452
17.017
1.00
12.35
B


ATOM
3000
C
GLY
B
90
6.759
21.010
15.942
1.00
11.99
B


ATOM
3001
O
GLY
B
90
7.139
19.847
15.870
1.00
14.46
B


ATOM
3002
N
ILE
B
91
7.165
21.940
15.097
1.00
14.38
B


ATOM
3003
CA
ILE
B
91
8.027
21.614
13.968
1.00
13.92
B


ATOM
3004
CB
ILE
B
91
7.681
22.538
12.774
1.00
17.25
B


ATOM
3005
CG2
ILE
B
91
8.662
22.305
11.592
1.00
18.38
B


ATOM
3006
CG1
ILE
B
91
6.220
22.317
12.352
1.00
16.43
B


ATOM
3007
CD1
ILE
B
91
5.683
23.452
11.384
1.00
19.10
B


ATOM
3008
C
ILE
B
91
9.507
21.717
14.263
1.00
14.95
B


ATOM
3009
O
ILE
B
91
10.330
20.989
13.679
1.00
13.23
B


ATOM
3010
N
MET
B
92
9.867
22.610
15.172
1.00
13.36
B


ATOM
3011
CA
MET
B
92
11.275
22.779
15.503
1.00
14.20
B


ATOM
3012
CB
MET
B
92
11.541
24.255
15.902
1.00
15.14
B


ATOM
3013
CG
MET
B
92
11.381
25.299
14.736
1.00
14.52
B


ATOM
3014
SD
MET
B
92
12.679
25.118
13.560
1.00
17.34
B


ATOM
3015
CE
MET
B
92
11.857
24.037
12.319
1.00
9.40
B


ATOM
3016
C
MET
B
92
11.822
21.886
16.629
1.00
12.93
B


ATOM
3017
O
MET
B
92
12.987
21.435
16.585
1.00
12.02
B


ATOM
3018
N
LEU
B
93
11.002
21.705
17.656
1.00
14.34
B


ATOM
3019
CA
LEU
B
93
11.400
20.981
18.858
1.00
15.78
B


ATOM
3020
CB
LEU
B
93
10.652
21.578
20.070
1.00
13.57
B


ATOM
3021
CG
LEU
B
93
10.690
23.127
20.163
1.00
19.33
B


ATOM
3022
CD1
LEU
B
93
9.924
23.584
21.401
1.00
15.26
B


ATOM
3023
CD2
LEU
B
93
12.170
23.636
20.160
1.00
17.45
B


ATOM
3024
C
LEU
B
93
11.137
19.481
18.832
1.00
17.68
B


ATOM
3025
O
LEU
B
93
10.376
18.942
17.986
1.00
15.62
B


ATOM
3026
N
GLU
B
94
11.738
18.814
19.805
1.00
14.03
B


ATOM
3027
CA
GLU
B
94
11.553
17.381
19.952
1.00
13.77
B


ATOM
3028
CB
GLU
B
94
12.277
16.865
21.221
1.00
12.90
B


ATOM
3029
CG
GLU
B
94
13.778
16.689
21.012
1.00
12.37
B


ATOM
3030
CD
GLU
B
94
14.461
16.007
22.244
1.00
18.93
B


ATOM
3031
OE1
GLU
B
94
14.073
14.847
22.588
1.00
17.09
B


ATOM
3032
OE2
GLU
B
94
15.378
16.644
22.830
1.00
16.53
B


ATOM
3033
C
GLU
B
94
10.067
17.206
20.116
1.00
11.82
B


ATOM
3034
O
GLU
B
94
9.418
18.078
20.654
1.00
12.83
B


ATOM
3035
N
PRO
B
95
9.511
16.045
19.733
1.00
10.57
B


ATOM
3036
CD
PRO
B
95
8.088
15.775
20.028
1.00
11.19
B


ATOM
3037
CA
PRO
B
95
10.192
14.887
19.157
1.00
11.42
B


ATOM
3038
CB
PRO
B
95
9.254
13.710
19.512
1.00
12.72
B


ATOM
3039
CG
PRO
B
95
7.843
14.349
19.422
1.00
11.72
B


ATOM
3040
C
PRO
B
95
10.437
15.004
17.629
1.00
13.53
B


ATOM
3041
O
PRO
B
95
11.260
14.260
17.070
1.00
11.38
B


ATOM
3042
N
ARG
B
96
9.726
15.908
16.953
1.00
12.44
B


ATOM
3043
CA
ARG
B
96
9.921
16.041
15.478
1.00
14.68
B


ATOM
3044
CB
ARG
B
96
8.709
16.765
14.820
1.00
15.11
B


ATOM
3045
CG
ARG
B
96
7.419
15.916
14.917
1.00
10.29
B


ATOM
3046
CD
ARG
B
96
6.173
16.792
14.809
1.00
9.53
B


ATOM
3047
NE
ARG
B
96
4.963
16.064
15.181
1.00
11.15
B


ATOM
3048
CZ
ARG
B
96
4.563
15.836
16.422
1.00
17.72
B


ATOM
3049
NH1
ARG
B
96
5.292
16.296
17.461
1.00
11.24
B


ATOM
3050
NH2
ARG
B
96
3.440
15.139
16.617
1.00
13.64
B


ATOM
3051
C
ARG
B
96
11.196
16.769
15.148
1.00
13.90
B


ATOM
3052
O
ARG
B
96
11.768
16.570
14.075
1.00
11.13
B


ATOM
3053
N
GLY
B
97
11.646
17.647
16.054
1.00
13.62
B


ATOM
3054
CA
GLY
B
97
12.919
18.323
15.797
1.00
12.77
B


ATOM
3055
C
GLY
B
97
13.884
18.116
16.959
1.00
14.62
B


ATOM
3056
O
GLY
B
97
13.925
17.021
17.523
1.00
11.85
B


ATOM
3057
N
HIS
B
98
14.652
19.143
17.332
1.00
11.40
B


ATOM
3058
CA
HIS
B
98
15.579
19.014
18.474
1.00
14.47
B


ATOM
3059
CB
HIS
B
98
16.774
18.067
18.182
1.00
13.56
B


ATOM
3060
CG
HIS
B
98
17.578
18.419
16.965
1.00
9.61
B


ATOM
3061
CD2
HIS
B
98
17.390
18.112
15.651
1.00
10.05
B


ATOM
3062
ND1
HIS
B
98
18.758
19.135
17.019
1.00
9.66
B


ATOM
3063
CE1
HIS
B
98
19.261
19.260
15.800
1.00
11.54
B


ATOM
3064
NE2
HIS
B
98
18.451
18.647
14.951
1.00
12.75
B


ATOM
3065
C
HIS
B
98
16.069
20.396
18.818
1.00
17.08
B


ATOM
3066
O
HIS
B
98
15.750
21.349
18.110
1.00
16.43
B


ATOM
3067
N
ASP
B
99
16.889
20.497
19.866
1.00
16.24
B


ATOM
3068
CA
ASP
B
99
17.345
21.804
20.365
1.00
13.35
B


ATOM
3069
CB
ASP
B
99
18.104
21.628
21.693
1.00
14.50
B


ATOM
3070
CG
ASP
B
99
17.203
21.162
22.820
1.00
17.36
B


ATOM
3071
OD1
ASP
B
99
15.955
21.252
22.727
1.00
19.36
B


ATOM
3072
OD2
ASP
B
99
17.739
20.705
23.841
1.00
21.08
B


ATOM
3073
C
ASP
B
99
18.175
22.673
19.452
1.00
13.04
B


ATOM
3074
O
ASP
B
99
18.403
23.842
19.774
1.00
14.23
B


ATOM
3075
N
ASP
B
100
18.629
22.136
18.329
1.00
12.05
B


ATOM
3076
CA
ASP
B
100
19.445
22.895
17.385
1.00
9.75
B


ATOM
3077
CB
ASP
B
100
20.887
22.343
17.402
1.00
13.53
B


ATOM
3078
CG
ASP
B
100
21.629
22.704
18.752
1.00
19.27
B


ATOM
3079
OD1
ASP
B
100
22.144
23.833
18.871
1.00
15.89
B


ATOM
3080
OD2
ASP
B
100
21.639
21.859
19.686
1.00
17.16
B


ATOM
3081
C
ASP
B
100
18.867
22.883
15.960
1.00
10.00
B


ATOM
3082
O
ASP
B
100
19.586
23.127
14.989
1.00
12.60
B


ATOM
3083
N
MET
B
101
17.572
22.615
15.868
1.00
11.58
B


ATOM
3084
CA
MET
B
101
16.846
22.534
14.602
1.00
11.02
B


ATOM
3085
CB
MET
B
101
15.520
21.786
14.844
1.00
10.22
B


ATOM
3086
CG
MET
B
101
14.521
21.670
13.626
1.00
11.45
B


ATOM
3087
SD
MET
B
101
15.252
21.135
12.093
1.00
15.38
B


ATOM
3088
CE
MET
B
101
15.915
19.442
12.492
1.00
15.52
B


ATOM
3089
C
MET
B
101
16.599
23.974
14.134
1.00
13.90
B


ATOM
3090
O
MET
B
101
16.526
24.919
14.958
1.00
12.10
B


ATOM
3091
N
PHE
B
102
16.483
24.155
12.821
1.00
13.05
B


ATOM
3092
CA
PHE
B
102
16.239
25.481
12.246
1.00
12.65
B


ATOM
3093
CB
PHE
B
102
17.560
26.120
11.815
1.00
13.36
B


ATOM
3094
CG
PHE
B
102
17.427
27.565
11.383
1.00
13.28
B


ATOM
3095
CD1
PHE
B
102
17.757
28.597
12.266
1.00
15.69
B


ATOM
3096
CD2
PHE
B
102
16.869
27.894
10.121
1.00
14.39
B


ATOM
3097
CE1
PHE
B
102
17.536
29.970
11.923
1.00
14.81
B


ATOM
3098
CE2
PHE
B
102
16.629
29.257
9.762
1.00
12.33
B


ATOM
3099
CZ
PHE
B
102
16.967
30.292
10.667
1.00
20.33
B


ATOM
3100
C
PHE
B
102
15.364
25.248
11.001
1.00
12.87
B


ATOM
3101
O
PHE
B
102
15.454
24.190
10.391
1.00
14.63
B


ATOM
3102
N
GLY
B
103
14.537
26.222
10.623
1.00
14.23
B


ATOM
3103
CA
GLY
B
103
13.704
26.010
9.446
1.00
14.68
B


ATOM
3104
C
GLY
B
103
13.023
27.268
8.927
1.00
16.05
B


ATOM
3105
O
GLY
B
103
13.341
28.435
9.319
1.00
14.47
B


ATOM
3106
N
ALA
B
104
12.047
27.044
8.056
1.00
14.15
B


ATOM
3107
CA
ALA
B
104
11.382
28.167
7.426
1.00
13.51
B


ATOM
3108
CB
ALA
B
104
12.315
28.715
6.340
1.00
9.30
B


ATOM
3109
C
ALA
B
104
10.057
27.737
6.834
1.00
14.17
B


ATOM
3110
O
ALA
B
104
9.891
26.581
6.519
1.00
15.19
B


ATOM
3111
N
PHE
B
105
9.124
28.674
6.734
1.00
14.11
B


ATOM
3112
CA
PHE
B
105
7.831
28.432
6.120
1.00
17.87
B


ATOM
3113
CB
PHE
B
105
6.694
29.089
6.891
1.00
20.69
B


ATOM
3114
CG
PHE
B
105
6.550
28.650
8.301
1.00
21.99
B


ATOM
3115
CD1
PHE
B
105
6.938
29.487
9.340
1.00
25.85
B


ATOM
3116
CD2
PHE
B
105
5.902
27.473
8.608
1.00
26.48
B


ATOM
3117
CE1
PHE
B
105
6.651
29.147
10.671
1.00
27.88
B


ATOM
3118
CE2
PHE
B
105
5.608
27.124
9.951
1.00
25.82
B


ATOM
3119
CZ
PHE
B
105
5.970
27.948
10.957
1.00
24.10
B


ATOM
3120
C
PHE
B
105
7.880
29.161
4.770
1.00
19.00
B


ATOM
3121
O
PHE
B
105
8.374
30.312
4.701
1.00
16.48
B


ATOM
3122
N
LEU
B
106
7.399
28.505
3.708
1.00
17.15
B


ATOM
3123
CA
LEU
B
106
7.344
29.157
2.391
1.00
17.40
B


ATOM
3124
CB
LEU
B
106
7.642
28.190
1.252
1.00
15.38
B


ATOM
3125
CG
LEU
B
106
9.056
27.639
1.196
1.00
15.27
B


ATOM
3126
CD1
LEU
B
106
9.212
26.884
−0.090
1.00
13.58
B


ATOM
3127
CD2
LEU
B
106
10.102
28.797
1.300
1.00
13.60
B


ATOM
3128
C
LEU
B
106
5.959
29.727
2.187
1.00
16.51
B


ATOM
3129
O
LEU
B
106
4.979
29.127
2.624
1.00
15.75
B


ATOM
3130
N
PHE
B
107
5.903
30.899
1.541
1.00
17.32
B


ATOM
3131
CA
PHE
B
107
4.651
31.622
1.210
1.00
16.78
B


ATOM
3132
CB
PHE
B
107
4.432
32.840
2.114
1.00
17.59
B


ATOM
3133
CG
PHE
B
107
4.221
32.509
3.568
1.00
21.65
B


ATOM
3134
CD1
PHE
B
107
5.285
32.573
4.478
1.00
19.96
B


ATOM
3135
CD2
PHE
B
107
2.963
32.087
4.022
1.00
21.02
B


ATOM
3136
CE1
PHE
B
107
5.094
32.217
5.817
1.00
17.56
B


ATOM
3137
CE2
PHE
B
107
2.756
31.725
5.386
1.00
19.92
B


ATOM
3138
CZ
PHE
B
107
3.837
31.792
6.280
1.00
18.30
B


ATOM
3139
C
PHE
B
107
4.755
32.207
−0.204
1.00
17.62
B


ATOM
3140
O
PHE
B
107
5.844
32.267
−0.789
1.00
17.80
B


ATOM
3141
N
ASP
B
108
3.618
32.651
−0.739
1.00
15.56
B


ATOM
3142
CA
ASP
B
108
3.621
33.349
−2.004
1.00
17.74
B


ATOM
3143
CB
ASP
B
108
2.201
33.809
−2.370
1.00
18.05
B


ATOM
3144
CG
ASP
B
108
1.372
32.706
−2.988
1.00
20.49
B


ATOM
3145
OD1
ASP
B
108
1.962
31.646
−3.282
1.00
21.20
B


ATOM
3146
OD2
ASP
B
108
0.138
32.907
−3.173
1.00
23.28
B


ATOM
3147
C
ASP
B
108
4.436
34.611
−1.786
1.00
16.97
B


ATOM
3148
O
ASP
B
108
4.354
35.231
−0.723
1.00
16.00
B


ATOM
3149
N
PRO
B
109
5.223
35.019
−2.784
1.00
19.99
B


ATOM
3150
CD
PRO
B
109
5.409
34.433
−4.131
1.00
18.72
B


ATOM
3151
CA
PRO
B
109
6.004
36.246
−2.621
1.00
20.09
B


ATOM
3152
CB
PRO
B
109
6.875
36.255
−3.862
1.00
19.88
B


ATOM
3153
CG
PRO
B
109
5.944
35.592
−4.905
1.00
19.20
B


ATOM
3154
C
PRO
B
109
4.996
37.419
−2.660
1.00
21.67
B


ATOM
3155
O
PRO
B
109
3.939
37.302
−3.294
1.00
21.73
B


ATOM
3156
N
ILE
B
110
5.326
38.527
−1.986
1.00
21.64
B


ATOM
3157
CA
ILE
B
110
4.498
39.741
−1.966
1.00
24.17
B


ATOM
3158
CB
ILE
B
110
4.083
40.152
−0.530
1.00
23.18
B


ATOM
3159
CG2
ILE
B
110
3.425
41.527
−0.553
1.00
22.43
B


ATOM
3160
CG1
ILE
B
110
3.120
39.118
0.047
1.00
23.36
B


ATOM
3161
CD1
ILE
B
110
2.793
39.320
1.514
1.00
24.72
B


ATOM
3162
C
ILE
B
110
5.307
40.895
−2.582
1.00
27.84
B


ATOM
3163
O
ILE
B
110
4.802
41.642
−3.400
1.00
28.68
B


ATOM
3164
N
GLU
B
111
6.576
40.995
−2.207
1.00
29.66
B


ATOM
3165
CA
GLU
B
111
7.474
42.027
−2.686
1.00
32.69
B


ATOM
3166
CB
GLU
B
111
8.796
41.930
−1.932
1.00
35.68
B


ATOM
3167
CG
GLU
B
111
9.693
43.110
−2.117
1.00
41.39
B


ATOM
3168
CD
GLU
B
111
9.005
44.368
−1.668
1.00
44.73
B


ATOM
3169
OE1
GLU
B
111
8.366
44.337
−0.587
1.00
48.52
B


ATOM
3170
OE2
GLU
B
111
9.097
45.380
−2.394
1.00
48.66
B


ATOM
3171
C
GLU
B
111
7.716
41.830
−4.176
1.00
34.14
B


ATOM
3172
O
GLU
B
111
7.962
40.711
−4.638
1.00
32.31
B


ATOM
3173
N
GLU
B
112
7.676
42.924
−4.930
1.00
36.38
B


ATOM
3174
CA
GLU
B
112
7.845
42.845
−6.389
1.00
36.42
B


ATOM
3175
CB
GLU
B
112
7.660
44.239
−7.008
1.00
40.82
B


ATOM
3176
CG
GLU
B
112
7.541
44.237
−8.534
1.00
50.01
B


ATOM
3177
CD
GLU
B
112
6.986
45.567
−9.119
1.00
55.70
B


ATOM
3178
OE1
GLU
B
112
7.033
45.733
−10.364
1.00
56.98
B


ATOM
3179
OE2
GLU
B
112
6.495
46.433
−8.343
1.00
57.59
B


ATOM
3180
C
GLU
B
112
9.193
42.271
−6.783
1.00
33.25
B


ATOM
3181
O
GLU
B
112
10.223
42.692
−6.276
1.00
32.97
B


ATOM
3182
N
GLY
B
113
9.180
41.295
−7.681
1.00
29.97
B


ATOM
3183
CA
GLY
B
113
10.421
40.696
−8.129
1.00
29.24
B


ATOM
3184
C
GLY
B
113
10.854
39.459
−7.356
1.00
27.93
B


ATOM
3185
O
GLY
B
113
11.863
38.842
−7.694
1.00
28.34
B


ATOM
3186
N
ALA
B
114
10.104
39.084
−6.325
1.00
26.08
B


ATOM
3187
CA
ALA
B
114
10.487
37.901
−5.562
1.00
23.73
B


ATOM
3188
CB
ALA
B
114
10.103
38.083
−4.069
1.00
21.16
B


ATOM
3189
C
ALA
B
114
9.826
36.650
−6.120
1.00
20.49
B


ATOM
3190
O
ALA
B
114
8.721
36.711
−6.637
1.00
22.09
B


ATOM
3191
N
ASP
B
115
10.497
35.515
−5.987
1.00
19.60
B


ATOM
3192
CA
ASP
B
115
9.949
34.233
−6.414
1.00
21.22
B


ATOM
3193
CB
ASP
B
115
11.087
33.338
−6.898
1.00
21.99
B


ATOM
3194
CG
ASP
B
115
11.663
33.814
−8.232
1.00
29.33
B


ATOM
3195
OD1
ASP
B
115
10.843
33.917
−9.192
1.00
29.52
B


ATOM
3196
OD2
ASP
B
115
12.894
34.085
−8.329
1.00
27.59
B


ATOM
3197
C
ASP
B
115
9.205
33.531
−5.268
1.00
21.16
B


ATOM
3198
O
ASP
B
115
8.209
32.813
−5.470
1.00
19.61
B


ATOM
3199
N
LEU
B
116
9.700
33.727
−4.056
1.00
18.57
B


ATOM
3200
CA
LEU
B
116
9.124
33.054
−2.902
1.00
20.02
B


ATOM
3201
CB
LEU
B
116
9.956
31.810
−2.530
1.00
18.47
B


ATOM
3202
CG
LEU
B
116
10.015
30.620
−3.484
1.00
23.55
B


ATOM
3203
CD1
LEU
B
116
11.169
29.644
−3.136
1.00
22.45
B


ATOM
3204
CD2
LEU
B
116
8.679
29.929
−3.366
1.00
20.45
B


ATOM
3205
C
LEU
B
116
9.176
33.948
−1.711
1.00
19.28
B


ATOM
3206
O
LEU
B
116
10.174
34.654
−1.526
1.00
19.41
B


ATOM
3207
N
GLY
B
117
8.112
33.895
−0.914
1.00
18.20
B


ATOM
3208
CA
GLY
B
117
8.070
34.612
0.354
1.00
17.03
B


ATOM
3209
C
GLY
B
117
8.601
33.587
1.372
1.00
18.83
B


ATOM
3210
O
GLY
B
117
8.376
32.373
1.211
1.00
16.84
B


ATOM
3211
N
ILE
B
118
9.321
34.037
2.396
1.00
17.91
B


ATOM
3212
CA
ILE
B
118
9.908
33.094
3.366
1.00
17.96
B


ATOM
3213
CB
ILE
B
118
11.299
32.574
2.872
1.00
16.84
B


ATOM
3214
CG2
ILE
B
118
12.346
33.706
2.857
1.00
16.92
B


ATOM
3215
CG1
ILE
B
118
11.804
31.411
3.747
1.00
16.09
B


ATOM
3216
CD1
ILE
B
118
13.066
30.742
3.147
1.00
14.59
B


ATOM
3217
C
ILE
B
118
10.024
33.735
4.731
1.00
18.80
B


ATOM
3218
O
ILE
B
118
10.341
34.934
4.842
1.00
20.74
B


ATOM
3219
N
VAL
B
119
9.663
32.944
5.738
1.00
16.15
B


ATOM
3220
CA
VAL
B
119
9.711
33.291
7.149
1.00
16.03
B


ATOM
3221
CB
VAL
B
119
8.328
33.325
7.756
1.00
15.82
B


ATOM
3222
CG1
VAL
B
119
8.428
33.529
9.281
1.00
15.11
B


ATOM
3223
CG2
VAL
B
119
7.515
34.475
7.115
1.00
18.56
B


ATOM
3224
C
VAL
B
119
10.559
32.219
7.879
1.00
18.50
B


ATOM
3225
O
VAL
B
119
10.267
30.992
7.821
1.00
15.89
B


ATOM
3226
N
PHE
B
120
11.618
32.686
8.541
1.00
16.22
B


ATOM
3227
CA
PHE
B
120
12.536
31.800
9.238
1.00
15.08
B


ATOM
3228
CB
PHE
B
120
13.919
32.413
9.205
1.00
17.53
B


ATOM
3229
CG
PHE
B
120
14.414
32.644
7.833
1.00
14.00
B


ATOM
3230
CD1
PHE
B
120
14.463
33.938
7.307
1.00
14.97
B


ATOM
3231
CD2
PHE
B
120
14.794
31.563
7.044
1.00
14.56
B


ATOM
3232
CE1
PHE
B
120
14.888
34.147
5.989
1.00
16.92
B


ATOM
3233
CE2
PHE
B
120
15.222
31.755
5.709
1.00
15.27
B


ATOM
3234
CZ
PHE
B
120
15.268
33.038
5.186
1.00
18.12
B


ATOM
3235
C
PHE
B
120
12.118
31.536
10.678
1.00
16.02
B


ATOM
3236
O
PHE
B
120
11.491
32.383
11.302
1.00
14.50
B


ATOM
3237
N
MET
B
121
12.476
30.368
11.213
1.00
14.96
B


ATOM
3238
CA
MET
B
121
12.085
30.034
12.597
1.00
14.05
B


ATOM
3239
CB
MET
B
121
10.754
29.263
12.602
1.00
13.80
B


ATOM
3240
CG
MET
B
121
10.803
27.906
11.834
1.00
13.67
B


ATOM
3241
SD
MET
B
121
9.276
26.999
12.007
1.00
22.65
B


ATOM
3242
CE
MET
B
121
9.109
26.208
10.361
1.00
22.43
B


ATOM
3243
C
MET
B
121
13.193
29.190
13.225
1.00
14.84
B


ATOM
3244
O
MET
B
121
14.039
28.649
12.509
1.00
13.98
B


ATOM
3245
N
ASP
B
122
13.219
29.098
14.553
1.00
16.05
B


ATOM
3246
CA
ASP
B
122
14.251
28.285
15.231
1.00
14.56
B


ATOM
3247
CB
ASP
B
122
15.556
29.070
15.385
1.00
16.40
B


ATOM
3248
CG
ASP
B
122
15.338
30.435
16.089
1.00
17.14
B


ATOM
3249
OD1
ASP
B
122
15.593
31.495
15.466
1.00
18.16
B


ATOM
3250
OD2
ASP
B
122
14.877
30.430
17.252
1.00
17.86
B


ATOM
3251
C
ASP
B
122
13.713
27.856
16.587
1.00
13.64
B


ATOM
3252
O
ASP
B
122
12.532
28.005
16.845
1.00
13.72
B


ATOM
3253
N
THR
B
123
14.569
27.357
17.476
1.00
13.54
B


ATOM
3254
CA
THR
B
123
14.060
26.864
18.765
1.00
13.21
B


ATOM
3255
CB
THR
B
123
15.142
26.038
19.482
1.00
13.98
B


ATOM
3256
OG1
THR
B
123
16.294
26.875
19.727
1.00
13.78
B


ATOM
3257
CG2
THR
B
123
15.592
24.911
18.537
1.00
12.57
B


ATOM
3258
C
THR
B
123
13.571
27.945
19.697
1.00
14.90
B


ATOM
3259
O
THR
B
123
12.849
27.644
20.639
1.00
17.35
B


ATOM
3260
N
GLY
B
124
13.921
29.198
19.438
1.00
13.04
B


ATOM
3261
CA
GLY
B
124
13.416
30.232
20.328
1.00
16.04
B


ATOM
3262
C
GLY
B
124
12.435
31.203
19.720
1.00
14.21
B


ATOM
3263
O
GLY
B
124
11.505
31.670
20.394
1.00
15.41
B


ATOM
3264
N
GLY
B
125
12.603
31.507
18.443
1.00
16.96
B


ATOM
3265
CA
GLY
B
125
11.685
32.449
17.825
1.00
14.99
B


ATOM
3266
C
GLY
B
125
11.875
32.551
16.304
1.00
16.45
B


ATOM
3267
O
GLY
B
125
12.004
31.536
15.629
1.00
13.60
B


ATOM
3268
N
TYR
B
126
11.943
33.778
15.781
1.00
14.89
B


ATOM
3269
CA
TYR
B
126
12.001
34.012
14.334
1.00
16.24
B


ATOM
3270
CB
TYR
B
126
10.621
34.491
13.862
1.00
16.59
B


ATOM
3271
CG
TYR
B
126
9.465
33.621
14.327
1.00
17.02
B


ATOM
3272
CD1
TYR
B
126
8.965
33.696
15.657
1.00
15.28
B


ATOM
3273
CE1
TYR
B
126
7.865
32.890
16.067
1.00
15.25
B


ATOM
3274
CD2
TYR
B
126
8.851
32.730
13.429
1.00
16.86
B


ATOM
3275
CE2
TYR
B
126
7.763
31.935
13.822
1.00
14.70
B


ATOM
3276
CZ
TYR
B
126
7.273
32.017
15.118
1.00
16.29
B


ATOM
3277
OH
TYR
B
126
6.176
31.246
15.429
1.00
13.26
B


ATOM
3278
C
TYR
B
126
12.994
35.039
13.888
1.00
16.63
B


ATOM
3279
O
TYR
B
126
12.797
36.206
14.149
1.00
22.61
B


ATOM
3280
N
LEU
B
127
14.048
34.629
13.200
1.00
17.28
B


ATOM
3281
CA
LEU
B
127
15.051
35.577
12.730
1.00
17.83
B


ATOM
3282
CB
LEU
B
127
16.329
34.826
12.412
1.00
15.68
B


ATOM
3283
CG
LEU
B
127
17.085
34.300
13.630
1.00
17.46
B


ATOM
3284
CD1
LEU
B
127
18.245
33.477
13.133
1.00
13.73
B


ATOM
3285
CD2
LEU
B
127
17.619
35.511
14.462
1.00
18.65
B


ATOM
3286
C
LEU
B
127
14.528
36.290
11.465
1.00
21.47
B


ATOM
3287
O
LEU
B
127
13.818
35.674
10.649
1.00
17.85
B


ATOM
3288
N
ASN
B
128
14.894
37.570
11.294
1.00
20.47
B


ATOM
3289
CA
ASN
B
128
14.434
38.334
10.137
1.00
18.68
B


ATOM
3290
CB
ASN
B
128
14.630
39.840
10.391
1.00
17.27
B


ATOM
3291
CG
ASN
B
128
13.611
40.391
11.386
1.00
19.71
B


ATOM
3292
OD1
ASN
B
128
12.443
40.623
11.030
1.00
19.36
B


ATOM
3293
ND2
ASN
B
128
14.038
40.582
12.646
1.00
13.45
B


ATOM
3294
C
ASN
B
128
15.112
37.897
8.837
1.00
19.45
B


ATOM
3295
O
ASN
B
128
14.558
38.096
7.760
1.00
18.70
B


ATOM
3296
N
MET
B
129
16.312
37.314
8.936
1.00
18.45
B


ATOM
3297
CA
MET
B
129
16.992
36.800
7.768
1.00
19.19
B


ATOM
3298
CB
MET
B
129
17.853
37.841
7.060
1.00
19.61
B


ATOM
3299
CG
MET
B
129
17.490
37.948
5.545
1.00
19.46
B


ATOM
3300
SD
MET
B
129
17.672
36.384
4.599
1.00
20.27
B


ATOM
3301
CE
MET
B
129
19.456
36.350
4.406
1.00
13.92
B


ATOM
3302
C
MET
B
129
17.855
35.651
8.229
1.00
20.29
B


ATOM
3303
O
MET
B
129
18.159
35.528
9.436
1.00
16.69
B


ATOM
3304
N
CYS
B
130
18.222
34.793
7.281
1.00
14.53
B


ATOM
3305
CA
CYS
B
130
19.060
33.659
7.600
1.00
13.66
B


ATOM
3306
CB
CYS
B
130
18.245
32.468
8.100
1.00
15.73
B


ATOM
3307
SG
CYS
B
130
19.316
31.057
8.372
1.00
18.46
B


ATOM
3308
C
CYS
B
130
19.785
33.255
6.375
1.00
17.34
B


ATOM
3309
O
CYS
B
130
19.181
32.844
5.354
1.00
18.61
B


ATOM
3310
N
GLY
B
131
21.096
33.364
6.459
1.00
16.94
B


ATOM
3311
CA
GLY
B
131
21.916
33.009
5.330
1.00
18.99
B


ATOM
3312
C
GLY
B
131
21.930
31.539
4.914
1.00
19.83
B


ATOM
3313
O
GLY
B
131
21.733
31.217
3.737
1.00
20.29
B


ATOM
3314
N
HIS
B
132
22.178
30.637
5.844
1.00
17.57
B


ATOM
3315
CA
HIS
B
132
22.294
29.242
5.457
1.00
17.84
B


ATOM
3316
CB
HIS
B
132
22.842
28.401
6.619
1.00
16.45
B


ATOM
3317
CG
HIS
B
132
21.775
27.891
7.528
1.00
14.73
B


ATOM
3318
CD2
HIS
B
132
20.983
26.794
7.438
1.00
18.88
B


ATOM
3319
ND1
HIS
B
132
21.342
28.584
8.637
1.00
18.66
B


ATOM
3320
CE1
HIS
B
132
20.328
27.940
9.191
1.00
17.97
B


ATOM
3321
NE2
HIS
B
132
20.087
26.849
8.482
1.00
16.80
B


ATOM
3322
C
HIS
B
132
20.945
28.703
4.974
1.00
18.44
B


ATOM
3323
O
HIS
B
132
20.890
27.859
4.056
1.00
22.20
B


ATOM
3324
N
ASN
B
133
19.853
29.160
5.570
1.00
17.28
B


ATOM
3325
CA
ASN
B
133
18.544
28.688
5.113
1.00
18.98
B


ATOM
3326
CB
ASN
B
133
17.480
28.949
6.176
1.00
19.66
B


ATOM
3327
CG
ASN
B
133
16.320
27.962
6.062
1.00
22.21
B


ATOM
3328
OD1
ASN
B
133
15.907
27.569
4.951
1.00
22.11
B


ATOM
3329
ND2
ASN
B
133
15.785
27.582
7.174
1.00
15.05
B


ATOM
3330
C
ASN
B
133
18.115
29.305
3.739
1.00
19.26
B


ATOM
3331
O
ASN
B
133
17.297
28.703
2.990
1.00
17.07
B


ATOM
3332
N
SER
B
134
18.650
30.493
3.419
1.00
16.94
B


ATOM
3333
CA
SER
B
134
18.405
31.115
2.120
1.00
17.36
B


ATOM
3334
CB
SER
B
134
18.842
32.574
2.097
1.00
14.74
B


ATOM
3335
OG
SER
B
134
17.987
33.329
2.941
1.00
13.64
B


ATOM
3336
C
SER
B
134
19.197
30.324
1.066
1.00
16.67
B


ATOM
3337
O
SER
B
134
18.685
30.012
−0.008
1.00
18.11
B


ATOM
3338
N
ILE
B
135
20.443
29.997
1.370
1.00
16.41
B


ATOM
3339
CA
ILE
B
135
21.231
29.214
0.460
1.00
17.17
B


ATOM
3340
CB
ILE
B
135
22.623
29.010
1.031
1.00
19.18
B


ATOM
3341
CG2
ILE
B
135
23.301
27.837
0.358
1.00
19.06
B


ATOM
3342
CG1
ILE
B
135
23.410
30.305
0.921
1.00
18.07
B


ATOM
3343
CD1
ILE
B
135
24.775
30.242
1.620
1.00
20.86
B


ATOM
3344
C
ILE
B
135
20.535
27.852
0.252
1.00
19.28
B


ATOM
3345
O
ILE
B
135
20.518
27.296
−0.877
1.00
18.91
B


ATOM
3346
N
ALA
B
136
19.931
27.317
1.313
1.00
17.04
B


ATOM
3347
CA
ALA
B
136
19.215
26.036
1.183
1.00
18.05
B


ATOM
3348
CB
ALA
B
136
18.861
25.447
2.582
1.00
15.60
B


ATOM
3349
C
ALA
B
136
17.913
26.186
0.336
1.00
19.60
B


ATOM
3350
O
ALA
B
136
17.599
25.312
−0.450
1.00
16.66
B


ATOM
3351
N
ALA
B
137
17.136
27.246
0.568
1.00
18.37
B


ATOM
3352
CA
ALA
B
137
15.902
27.484
−0.195
1.00
20.46
B


ATOM
3353
CB
ALA
B
137
15.195
28.724
0.320
1.00
21.00
B


ATOM
3354
C
ALA
B
137
16.156
27.654
−1.717
1.00
21.34
B


ATOM
3355
O
ALA
B
137
15.394
27.134
−2.550
1.00
20.21
B


ATOM
3356
N
VAL
B
138
17.206
28.406
−2.047
1.00
20.85
B


ATOM
3357
CA
VAL
B
138
17.617
28.642
−3.427
1.00
21.90
B


ATOM
3358
CB
VAL
B
138
18.850
29.570
−3.434
1.00
22.55
B


ATOM
3359
CG1
VAL
B
138
19.525
29.595
−4.795
1.00
21.36
B


ATOM
3360
CG2
VAL
B
138
18.401
30.967
−3.012
1.00
18.99
B


ATOM
3361
C
VAL
B
138
17.947
27.292
−4.063
1.00
21.94
B


ATOM
3362
O
VAL
B
138
17.449
26.974
−5.141
1.00
22.22
B


ATOM
3363
N
THR
B
139
18.754
26.490
−3.370
1.00
21.41
B


ATOM
3364
CA
THR
B
139
19.153
25.168
−3.835
1.00
21.36
B


ATOM
3365
CB
THR
B
139
20.113
24.477
−2.818
1.00
21.83
B


ATOM
3366
OG1
THR
B
139
21.265
25.313
−2.622
1.00
23.28
B


ATOM
3367
CG2
THR
B
139
20.589
23.089
−3.328
1.00
16.99
B


ATOM
3368
C
THR
B
139
17.934
24.256
−4.065
1.00
23.71
B


ATOM
3369
O
THR
B
139
17.808
23.601
−5.121
1.00
21.66
B


ATOM
3370
N
ALA
B
140
17.045
24.223
−3.077
1.00
23.43
B


ATOM
3371
CA
ALA
B
140
15.847
23.383
−3.124
1.00
25.06
B


ATOM
3372
CB
ALA
B
140
15.139
23.375
−1.749
1.00
24.09
B


ATOM
3373
C
ALA
B
140
14.868
23.841
−4.195
1.00
26.55
B


ATOM
3374
O
ALA
B
140
14.153
23.016
−4.792
1.00
25.48
B


ATOM
3375
N
ALA
B
141
14.817
25.154
−4.428
1.00
25.06
B


ATOM
3376
CA
ALA
B
141
13.921
25.694
−5.438
1.00
25.64
B


ATOM
3377
CB
ALA
B
141
13.977
27.228
−5.425
1.00
24.92
B


ATOM
3378
C
ALA
B
141
14.320
25.142
−6.825
1.00
24.53
B


ATOM
3379
O
ALA
B
141
13.468
24.722
−7.596
1.00
26.15
B


ATOM
3380
N
VAL
B
142
15.606
25.132
−7.143
1.00
24.67
B


ATOM
3381
CA
VAL
B
142
16.025
24.612
−8.429
1.00
26.83
B


ATOM
3382
CB
VAL
B
142
17.431
25.081
−8.772
1.00
26.68
B


ATOM
3383
CG1
VAL
B
142
17.922
24.382
−10.044
1.00
28.13
B


ATOM
3384
CG2
VAL
B
142
17.435
26.603
−8.937
1.00
28.27
B


ATOM
3385
C
VAL
B
142
15.979
23.084
−8.458
1.00
28.76
B


ATOM
3386
O
VAL
B
142
15.421
22.499
−9.369
1.00
29.04
B


ATOM
3387
N
GLU
B
143
16.547
22.436
−7.452
1.00
27.91
B


ATOM
3388
CA
GLU
B
143
16.556
20.978
−7.417
1.00
29.07
B


ATOM
3389
CB
GLU
B
143
17.328
20.464
−6.213
1.00
29.90
B


ATOM
3390
CG
GLU
B
143
18.693
20.944
−6.181
1.00
34.43
B


ATOM
3391
CD
GLU
B
143
19.635
19.860
−5.892
1.00
37.94
B


ATOM
3392
OE1
GLU
B
143
19.380
19.133
−4.903
1.00
42.35
B


ATOM
3393
OE2
GLU
B
143
20.627
19.737
−6.643
1.00
39.42
B


ATOM
3394
C
GLU
B
143
15.214
20.297
−7.391
1.00
28.14
B


ATOM
3395
O
GLU
B
143
15.090
19.183
−7.889
1.00
31.60
B


ATOM
3396
N
THR
B
144
14.197
20.909
−6.812
1.00
26.25
B


ATOM
3397
CA
THR
B
144
12.927
20.219
−6.790
1.00
25.53
B


ATOM
3398
CB
THR
B
144
12.319
20.183
−5.363
1.00
26.79
B


ATOM
3399
OG1
THR
B
144
11.882
21.499
−4.998
1.00
25.58
B


ATOM
3400
CG2
THR
B
144
13.374
19.670
−4.358
1.00
26.04
B


ATOM
3401
C
THR
B
144
11.915
20.811
−7.737
1.00
27.43
B


ATOM
3402
O
THR
B
144
10.747
20.486
−7.648
1.00
25.42
B


ATOM
3403
N
GLY
B
145
12.350
21.693
−8.631
1.00
30.17
B


ATOM
3404
CA
GLY
B
145
11.430
22.253
−9.613
1.00
33.69
B


ATOM
3405
C
GLY
B
145
10.474
23.358
−9.180
1.00
36.34
B


ATOM
3406
O
GLY
B
145
9.420
23.545
−9.800
1.00
35.36
B


ATOM
3407
N
ILE
B
146
10.803
24.083
−8.113
1.00
36.90
B


ATOM
3408
CA
ILE
B
146
9.930
25.174
−7.694
1.00
37.50
B


ATOM
3409
CB
ILE
B
146
10.228
25.595
−6.225
1.00
37.59
B


ATOM
3410
CG2
ILE
B
146
9.419
26.830
−5.830
1.00
36.67
B


ATOM
3411
CG1
ILE
B
146
9.840
24.424
−5.297
1.00
34.69
B


ATOM
3412
CD1
ILE
B
146
10.078
24.671
−3.841
1.00
35.96
B


ATOM
3413
C
ILE
B
146
10.158
26.287
−8.723
1.00
38.72
B


ATOM
3414
O
ILE
B
146
9.215
26.942
−9.131
1.00
39.42
B


ATOM
3415
N
VAL
B
147
11.396
26.503
−9.160
1.00
40.40
B


ATOM
3416
CA
VAL
B
147
11.614
27.491
−10.216
1.00
43.31
B


ATOM
3417
CB
VAL
B
147
12.561
28.662
−9.825
1.00
41.32
B


ATOM
3418
CG1
VAL
B
147
12.086
29.327
−8.540
1.00
40.94
B


ATOM
3419
CG2
VAL
B
147
13.982
28.178
−9.733
1.00
40.93
B


ATOM
3420
C
VAL
B
147
12.228
26.723
−11.386
1.00
46.54
B


ATOM
3421
O
VAL
B
147
12.945
25.735
−11.196
1.00
46.96
B


ATOM
3422
N
SER
B
148
11.944
27.155
−12.607
1.00
49.75
B


ATOM
3423
CA
SER
B
148
12.497
26.446
−13.751
1.00
51.81
B


ATOM
3424
CB
SER
B
148
11.530
26.508
−14.938
1.00
53.22
B


ATOM
3425
OG
SER
B
148
10.360
25.751
−14.658
1.00
56.25
B


ATOM
3426
C
SER
B
148
13.863
26.956
−14.163
1.00
51.71
B


ATOM
3427
O
SER
B
148
14.230
28.096
−13.864
1.00
50.48
B


ATOM
3428
N
VAL
B
149
14.611
26.088
−14.840
1.00
51.94
B


ATOM
3429
CA
VAL
B
149
15.938
26.426
−15.316
1.00
53.72
B


ATOM
3430
CB
VAL
B
149
16.935
25.276
−15.099
1.00
52.89
B


ATOM
3431
CG1
VAL
B
149
18.334
25.717
−15.520
1.00
51.41
B


ATOM
3432
CG2
VAL
B
149
16.923
24.844
−13.647
1.00
52.99
B


ATOM
3433
C
VAL
B
149
15.892
26.729
−16.807
1.00
55.20
B


ATOM
3434
O
VAL
B
149
15.491
25.880
−17.601
1.00
54.20
B


ATOM
3435
N
PRO
B
150
16.298
27.953
−17.197
1.00
56.79
B


ATOM
3436
CD
PRO
B
150
16.583
29.095
−16.303
1.00
57.13
B


ATOM
3437
CA
PRO
B
150
16.316
28.389
−18.593
1.00
57.79
B


ATOM
3438
CB
PRO
B
150
16.946
29.776
−18.510
1.00
57.92
B


ATOM
3439
CG
PRO
B
150
16.384
30.291
−17.231
1.00
58.94
B


ATOM
3440
C
PRO
B
150
17.097
27.460
−19.502
1.00
58.46
B


ATOM
3441
O
PRO
B
150
17.804
26.564
−19.049
1.00
59.21
B


ATOM
3442
N
ALA
B
151
16.960
27.691
−20.801
1.00
59.07
B


ATOM
3443
CA
ALA
B
151
17.639
26.890
−21.800
1.00
58.12
B


ATOM
3444
CB
ALA
B
151
17.212
27.355
−23.204
1.00
58.67
B


ATOM
3445
C
ALA
B
151
19.159
26.991
−21.640
1.00
57.23
B


ATOM
3446
O
ALA
B
151
19.741
28.082
−21.739
1.00
56.76
B


ATOM
3447
N
ALA
B
152
19.790
25.847
−21.383
1.00
55.66
B


ATOM
3448
CA
ALA
B
152
21.245
25.770
−21.226
1.00
54.69
B


ATOM
3449
CB
ALA
B
152
21.929
26.007
−22.584
1.00
54.88
B


ATOM
3450
C
ALA
B
152
21.834
26.724
−20.175
1.00
53.31
B


ATOM
3451
O
ALA
B
152
23.012
27.084
−20.247
1.00
52.92
B


ATOM
3452
N
ALA
B
153
21.020
27.121
−19.201
1.00
51.83
B


ATOM
3453
CA
ALA
B
153
21.475
28.026
−18.154
1.00
49.75
B


ATOM
3454
CB
ALA
B
153
20.292
28.474
−17.302
1.00
49.39
B


ATOM
3455
C
ALA
B
153
22.508
27.347
−17.276
1.00
48.39
B


ATOM
3456
O
ALA
B
153
22.451
26.139
−17.063
1.00
48.67
B


ATOM
3457
N
THR
B
154
23.466
28.125
−16.787
1.00
46.99
B


ATOM
3458
CA
THR
B
154
24.479
27.595
−15.886
1.00
46.16
B


ATOM
3459
CB
THR
B
154
25.925
27.932
−16.340
1.00
47.69
B


ATOM
3460
OG1
THR
B
154
26.029
29.332
−16.599
1.00
47.71
B


ATOM
3461
CG2
THR
B
154
26.307
27.147
−17.605
1.00
49.85
B


ATOM
3462
C
THR
B
154
24.236
28.234
−14.516
1.00
44.12
B


ATOM
3463
O
THR
B
154
24.826
27.820
−13.524
1.00
43.83
B


ATOM
3464
N
ASN
B
155
23.369
29.245
−14.483
1.00
40.84
B


ATOM
3465
CA
ASN
B
155
23.033
29.949
−13.244
1.00
39.51
B


ATOM
3466
CB
ASN
B
155
23.846
31.234
−13.111
1.00
37.17
B


ATOM
3467
CG
ASN
B
155
25.324
30.957
−12.970
1.00
40.83
B


ATOM
3468
OD1
ASN
B
155
26.128
31.322
−13.836
1.00
44.25
B


ATOM
3469
ND2
ASN
B
155
25.696
30.285
−11.892
1.00
36.63
B


ATOM
3470
C
ASN
B
155
21.557
30.279
−13.225
1.00
37.69
B


ATOM
3471
O
ASN
B
155
21.004
30.736
−14.232
1.00
38.02
B


ATOM
3472
N
VAL
B
156
20.904
30.025
−12.096
1.00
34.36
B


ATOM
3473
CA
VAL
B
156
19.487
30.306
−12.002
1.00
31.70
B


ATOM
3474
CB
VAL
B
156
18.646
29.021
−11.881
1.00
30.36
B


ATOM
3475
CG1
VAL
B
156
17.197
29.387
−12.003
1.00
30.15
B


ATOM
3476
CG2
VAL
B
156
19.034
27.985
−12.953
1.00
30.39
B


ATOM
3477
C
VAL
B
156
19.184
31.177
−10.790
1.00
33.16
B


ATOM
3478
O
VAL
B
156
19.569
30.849
−9.649
1.00
32.35
B


ATOM
3479
N
PRO
B
157
18.516
32.320
−11.028
1.00
32.62
B


ATOM
3480
CD
PRO
B
157
18.341
32.926
−12.361
1.00
32.91
B


ATOM
3481
CA
PRO
B
157
18.134
33.271
−9.980
1.00
29.88
B


ATOM
3482
CB
PRO
B
157
17.789
34.553
−10.748
1.00
29.97
B


ATOM
3483
CG
PRO
B
157
18.521
34.395
−12.040
1.00
34.80
B


ATOM
3484
C
PRO
B
157
16.916
32.723
−9.255
1.00
28.07
B


ATOM
3485
O
PRO
B
157
16.046
32.042
−9.836
1.00
26.47
B


ATOM
3486
N
VAL
B
158
16.881
33.001
−7.964
1.00
25.23
B


ATOM
3487
CA
VAL
B
158
15.793
32.599
−7.083
1.00
21.80
B


ATOM
3488
CB
VAL
B
158
16.129
31.330
−6.326
1.00
20.12
B


ATOM
3489
CG1
VAL
B
158
14.965
31.000
−5.374
1.00
23.71
B


ATOM
3490
CG2
VAL
B
158
16.372
30.163
−7.313
1.00
21.48
B


ATOM
3491
C
VAL
B
158
15.789
33.761
−6.112
1.00
21.25
B


ATOM
3492
O
VAL
B
158
16.755
33.942
−5.367
1.00
20.54
B


ATOM
3493
N
VAL
B
159
14.726
34.557
−6.114
1.00
19.96
B


ATOM
3494
CA
VAL
B
159
14.699
35.736
−5.229
1.00
20.32
B


ATOM
3495
CB
VAL
B
159
14.304
36.989
−6.031
1.00
22.57
B


ATOM
3496
CG1
VAL
B
159
14.359
38.209
−5.167
1.00
18.83
B


ATOM
3497
CG2
VAL
B
159
15.261
37.126
−7.264
1.00
22.85
B


ATOM
3498
C
VAL
B
159
13.747
35.521
−4.079
1.00
21.10
B


ATOM
3499
O
VAL
B
159
12.595
35.127
−4.270
1.00
22.48
B


ATOM
3500
N
LEU
B
160
14.233
35.772
−2.875
1.00
20.03
B


ATOM
3501
CA
LEU
B
160
13.439
35.555
−1.696
1.00
20.10
B


ATOM
3502
CB
LEU
B
160
14.288
34.814
−0.651
1.00
20.63
B


ATOM
3503
CG
LEU
B
160
14.937
33.533
−1.208
1.00
23.47
B


ATOM
3504
CD1
LEU
B
160
15.920
32.951
−0.195
1.00
24.30
B


ATOM
3505
CD2
LEU
B
160
13.833
32.473
−1.500
1.00
22.36
B


ATOM
3506
C
LEU
B
160
12.933
36.840
−1.108
1.00
18.11
B


ATOM
3507
O
LEU
B
160
13.681
37.792
−0.996
1.00
20.65
B


ATOM
3508
N
ASP
B
161
11.659
36.848
−0.732
1.00
16.91
B


ATOM
3509
CA
ASP
B
161
10.997
37.952
−0.075
1.00
18.70
B


ATOM
3510
CB
ASP
B
161
9.540
38.034
−0.591
1.00
21.90
B


ATOM
3511
CG
ASP
B
161
8.732
39.110
0.092
1.00
23.80
B


ATOM
3512
OD1
ASP
B
161
9.331
39.837
0.907
1.00
25.02
B


ATOM
3513
OD2
ASP
B
161
7.500
39.229
−0.171
1.00
23.82
B


ATOM
3514
C
ASP
B
161
11.051
37.565
1.432
1.00
19.10
B


ATOM
3515
O
ASP
B
161
10.319
36.699
1.884
1.00
16.38
B


ATOM
3516
N
THR
B
162
11.946
38.199
2.196
1.00
21.04
B


ATOM
3517
CA
THR
B
162
12.119
37.882
3.628
1.00
19.17
B


ATOM
3518
CB
THR
B
162
13.619
37.604
3.974
1.00
16.98
B


ATOM
3519
OG1
THR
B
162
14.313
38.853
4.099
1.00
16.65
B


ATOM
3520
CG2
THR
B
162
14.318
36.796
2.898
1.00
13.77
B


ATOM
3521
C
THR
B
162
11.673
39.022
4.553
1.00
20.82
B


ATOM
3522
O
THR
B
162
11.456
40.153
4.099
1.00
22.61
B


ATOM
3523
N
PRO
B
163
11.529
38.745
5.870
1.00
21.15
B


ATOM
3524
CD
PRO
B
163
11.458
37.422
6.539
1.00
19.59
B


ATOM
3525
CA
PRO
B
163
11.115
39.819
6.786
1.00
19.48
B


ATOM
3526
CB
PRO
B
163
10.915
39.087
8.119
1.00
18.43
B


ATOM
3527
CG
PRO
B
163
10.426
37.666
7.631
1.00
17.54
B


ATOM
3528
C
PRO
B
163
12.132
40.980
6.891
1.00
19.63
B


ATOM
3529
O
PRO
B
163
11.789
42.060
7.367
1.00
20.79
B


ATOM
3530
N
ALA
B
164
13.362
40.757
6.444
1.00
18.72
B


ATOM
3531
CA
ALA
B
164
14.395
41.802
6.459
1.00
21.68
B


ATOM
3532
CB
ALA
B
164
15.793
41.223
6.888
1.00
17.32
B


ATOM
3533
C
ALA
B
164
14.551
42.460
5.083
1.00
22.84
B


ATOM
3534
O
ALA
B
164
15.340
43.389
4.952
1.00
20.27
B


ATOM
3535
N
GLY
B
165
13.818
41.985
4.068
1.00
21.60
B


ATOM
3536
CA
GLY
B
165
13.982
42.549
2.736
1.00
21.56
B


ATOM
3537
C
GLY
B
165
14.259
41.520
1.635
1.00
22.44
B


ATOM
3538
O
GLY
B
165
14.303
40.309
1.886
1.00
20.06
B


ATOM
3539
N
LEU
B
166
14.460
42.015
0.417
1.00
22.49
B


ATOM
3540
CA
LEU
B
166
14.700
41.188
−0.774
1.00
24.05
B


ATOM
3541
CB
LEU
B
166
14.437
42.023
−2.042
1.00
28.16
B


ATOM
3542
CG
LEU
B
166
13.932
41.314
−3.307
1.00
33.49
B


ATOM
3543
CD1
LEU
B
166
12.568
40.662
−3.005
1.00
31.68
B


ATOM
3544
CD2
LEU
B
166
13.796
42.325
−4.459
1.00
32.73
B


ATOM
3545
C
LEU
B
166
16.117
40.626
−0.791
1.00
23.51
B


ATOM
3546
O
LEU
B
166
17.097
41.360
−0.684
1.00
21.23
B


ATOM
3547
N
VAL
B
167
16.216
39.308
−0.908
1.00
21.21
B


ATOM
3548
CA
VAL
B
167
17.483
38.617
−0.924
1.00
19.79
B


ATOM
3549
CB
VAL
B
167
17.510
37.514
0.221
1.00
20.52
B


ATOM
3550
CG1
VAL
B
167
18.758
36.572
0.050
1.00
21.30
B


ATOM
3551
CG2
VAL
B
167
17.604
38.196
1.592
1.00
16.75
B


ATOM
3552
C
VAL
B
167
17.597
37.968
−2.324
1.00
23.36
B


ATOM
3553
O
VAL
B
167
16.783
37.121
−2.686
1.00
22.28
B


ATOM
3554
N
ARG
B
168
18.596
38.355
−3.107
1.00
22.86
B


ATOM
3555
CA
ARG
B
168
18.722
37.773
−4.446
1.00
26.01
B


ATOM
3556
CB
ARG
B
168
19.123
38.855
−5.459
1.00
25.29
B


ATOM
3557
CG
ARG
B
168
18.017
39.900
−5.600
1.00
29.89
B


ATOM
3558
CD
ARG
B
168
18.397
41.075
−6.511
1.00
36.82
B


ATOM
3559
NE
ARG
B
168
17.202
41.890
−6.756
1.00
44.36
B


ATOM
3560
CZ
ARG
B
168
16.272
41.631
−7.683
1.00
45.86
B


ATOM
3561
NH1
ARG
B
168
16.383
40.581
−8.497
1.00
46.79
B


ATOM
3562
NH2
ARG
B
168
15.197
42.408
−7.768
1.00
49.79
B


ATOM
3563
C
ARG
B
168
19.700
36.623
−4.505
1.00
25.13
B


ATOM
3564
O
ARG
B
168
20.906
36.824
−4.427
1.00
26.32
B


ATOM
3565
N
GLY
B
169
19.173
35.415
−4.664
1.00
23.45
B


ATOM
3566
CA
GLY
B
169
20.042
34.260
−4.732
1.00
24.17
B


ATOM
3567
C
GLY
B
169
20.247
33.741
−6.145
1.00
25.05
B


ATOM
3568
O
GLY
B
169
19.486
34.088
−7.075
1.00
24.68
B


ATOM
3569
N
THR
B
170
21.276
32.908
−6.295
1.00
24.50
B


ATOM
3570
CA
THR
B
170
21.626
32.296
−7.574
1.00
25.20
B


ATOM
3571
CB
THR
B
170
22.833
33.029
−8.273
1.00
25.09
B


ATOM
3572
OG1
THR
B
170
22.546
34.415
−8.404
1.00
25.53
B


ATOM
3573
CG2
THR
B
170
23.097
32.455
−9.684
1.00
26.85
B


ATOM
3574
C
THR
B
170
22.082
30.857
−7.331
1.00
24.77
B


ATOM
3575
O
THR
B
170
23.003
30.620
−6.546
1.00
26.30
B


ATOM
3576
N
ALA
B
171
21.432
29.893
−7.969
1.00
24.50
B


ATOM
3577
CA
ALA
B
171
21.890
28.505
−7.844
1.00
25.22
B


ATOM
3578
CB
ALA
B
171
20.740
27.548
−8.070
1.00
25.22
B


ATOM
3579
C
ALA
B
171
22.916
28.354
−8.969
1.00
27.75
B


ATOM
3580
O
ALA
B
171
22.616
28.723
−10.129
1.00
27.37
B


ATOM
3581
N
HIS
B
172
24.118
27.868
−8.648
1.00
26.80
B


ATOM
3582
CA
HIS
B
172
25.146
27.656
−9.659
1.00
30.31
B


ATOM
3583
CB
HIS
B
172
26.509
28.027
−9.097
1.00
30.88
B


ATOM
3584
CG
HIS
B
172
26.558
29.419
−8.553
1.00
33.46
B


ATOM
3585
CD2
HIS
B
172
26.765
29.885
−7.295
1.00
34.34
B


ATOM
3586
ND1
HIS
B
172
26.361
30.530
−9.345
1.00
34.41
B


ATOM
3587
CE1
HIS
B
172
26.451
31.620
−8.598
1.00
34.92
B


ATOM
3588
NE2
HIS
B
172
26.697
31.256
−7.353
1.00
33.67
B


ATOM
3589
C
HIS
B
172
25.061
26.177
−10.023
1.00
33.61
B


ATOM
3590
O
HIS
B
172
25.249
25.306
−9.179
1.00
32.86
B


ATOM
3591
N
LEU
B
173
24.749
25.893
−11.279
1.00
35.30
B


ATOM
3592
CA
LEU
B
173
24.558
24.511
−11.686
1.00
39.94
B


ATOM
3593
CB
LEU
B
173
23.625
24.473
−12.894
1.00
38.88
B


ATOM
3594
CG
LEU
B
173
22.308
25.249
−12.780
1.00
40.04
B


ATOM
3595
CD1
LEU
B
173
21.597
25.202
−14.130
1.00
40.28
B


ATOM
3596
CD2
LEU
B
173
21.415
24.646
−11.701
1.00
38.11
B


ATOM
3597
C
LEU
B
173
25.797
23.671
−11.961
1.00
43.11
B


ATOM
3598
O
LEU
B
173
26.865
24.176
−12.300
1.00
42.30
B


ATOM
3599
N
GLN
B
174
25.641
22.368
−11.778
1.00
48.56
B


ATOM
3600
CA
GLN
B
174
26.724
21.426
−12.034
1.00
54.90
B


ATOM
3601
CB
GLN
B
174
26.392
20.071
−11.387
1.00
58.00
B


ATOM
3602
CG
GLN
B
174
27.584
19.138
−11.234
1.00
63.64
B


ATOM
3603
CD
GLN
B
174
28.784
19.836
−10.598
1.00
67.39
B


ATOM
3604
OE1
GLN
B
174
29.470
20.640
−11.244
1.00
69.26
B


ATOM
3605
NE2
GLN
B
174
29.033
19.545
−9.319
1.00
68.38
B


ATOM
3606
C
GLN
B
174
26.841
21.285
−13.564
1.00
57.02
B


ATOM
3607
O
GLN
B
174
25.848
20.988
−14.243
1.00
55.17
B


ATOM
3608
N
SER
B
175
28.045
21.529
−14.087
1.00
60.30
B


ATOM
3609
CA
SER
B
175
28.359
21.451
−15.528
1.00
64.34
B


ATOM
3610
CB
SER
B
175
29.707
20.764
−15.738
1.00
65.32
B


ATOM
3611
OG
SER
B
175
30.740
21.450
−15.057
1.00
70.17
B


ATOM
3612
C
SER
B
175
27.346
20.747
−16.421
1.00
65.30
B


ATOM
3613
O
SER
B
175
26.506
21.374
−17.061
1.00
66.46
B


ATOM
3614
N
GLY
B
176
27.440
19.432
−16.485
1.00
66.38
B


ATOM
3615
CA
GLY
B
176
26.515
18.704
−17.327
1.00
68.88
B


ATOM
3616
C
GLY
B
176
25.218
18.276
−16.657
1.00
69.36
B


ATOM
3617
O
GLY
B
176
24.995
17.079
−16.440
1.00
70.97
B


ATOM
3618
N
THR
B
177
24.361
19.232
−16.319
1.00
68.19
B


ATOM
3619
CA
THR
B
177
23.087
18.888
−15.699
1.00
67.44
B


ATOM
3620
CB
THR
B
177
23.196
18.732
−14.158
1.00
68.88
B


ATOM
3621
OG1
THR
B
177
23.520
19.996
−13.562
1.00
68.73
B


ATOM
3622
CG2
THR
B
177
24.268
17.700
−13.792
1.00
69.18
B


ATOM
3623
C
THR
B
177
22.050
19.946
−15.991
1.00
65.83
B


ATOM
3624
O
THR
B
177
22.375
21.065
−16.390
1.00
65.29
B


ATOM
3625
N
ALA
B
178
20.794
19.585
−15.792
1.00
64.55
B


ATOM
3626
CA
ALA
B
178
19.708
20.518
−16.025
1.00
63.40
B


ATOM
3627
CB
ALA
B
178
18.524
19.787
−16.682
1.00
63.43
B


ATOM
3628
C
ALA
B
178
19.277
21.174
−14.702
1.00
62.42
B


ATOM
3629
O
ALA
B
178
18.973
22.370
−14.662
1.00
62.90
B


ATOM
3630
N
SER
B
179
19.268
20.404
−13.615
1.00
59.73
B


ATOM
3631
CA
SER
B
179
18.852
20.962
−12.337
1.00
56.34
B


ATOM
3632
CB
SER
B
179
17.379
20.629
−12.080
1.00
56.87
B


ATOM
3633
OG
SER
B
179
17.118
19.249
−12.291
1.00
56.80
B


ATOM
3634
C
SER
B
179
19.694
20.557
−11.129
1.00
54.13
B


ATOM
3635
O
SER
B
179
19.246
20.694
−9.982
1.00
52.99
B


ATOM
3636
N
GLU
B
180
20.905
20.060
−11.376
1.00
50.55
B


ATOM
3637
CA
GLU
B
180
21.793
19.681
−10.280
1.00
46.87
B


ATOM
3638
CB
GLU
B
180
22.818
18.639
−10.725
1.00
49.20
B


ATOM
3639
CG
GLU
B
180
22.326
17.211
−10.727
1.00
57.97
B


ATOM
3640
CD
GLU
B
180
23.426
16.227
−10.299
1.00
61.97
B


ATOM
3641
OE1
GLU
B
180
24.557
16.301
−10.846
1.00
62.69
B


ATOM
3642
OE2
GLU
B
180
23.154
15.382
−9.408
1.00
64.41
B


ATOM
3643
C
GLU
B
180
22.534
20.945
−9.816
1.00
41.07
B


ATOM
3644
O
GLU
B
180
23.184
21.620
−10.611
1.00
39.10
B


ATOM
3645
N
VAL
B
181
22.455
21.249
−8.533
1.00
34.98
B


ATOM
3646
CA
VAL
B
181
23.109
22.447
−8.019
1.00
31.38
B


ATOM
3647
CB
VAL
B
181
22.172
23.137
−7.021
1.00
29.36
B


ATOM
3648
CG1
VAL
B
181
22.868
24.287
−6.323
1.00
27.12
B


ATOM
3649
CG2
VAL
B
181
20.938
23.589
−7.736
1.00
25.04
B


ATOM
3650
C
VAL
B
181
24.454
22.166
−7.353
1.00
31.06
B


ATOM
3651
O
VAL
B
181
24.522
21.316
−6.453
1.00
29.88
B


ATOM
3652
N
SER
B
182
25.517
22.857
−7.788
1.00
28.94
B


ATOM
3653
CA
SER
B
182
26.833
22.657
−7.167
1.00
31.41
B


ATOM
3654
CB
SER
B
182
27.991
22.966
−8.119
1.00
30.83
B


ATOM
3655
OG
SER
B
182
27.721
24.166
−8.790
1.00
38.77
B


ATOM
3656
C
SER
B
182
26.993
23.500
−5.914
1.00
30.33
B


ATOM
3657
O
SER
B
182
27.660
23.083
−4.978
1.00
31.11
B


ATOM
3658
N
ASN
B
183
26.405
24.689
−5.910
1.00
28.41
B


ATOM
3659
CA
ASN
B
183
26.431
25.574
−4.737
1.00
28.22
B


ATOM
3660
CB
ASN
B
183
27.853
26.033
−4.361
1.00
28.80
B


ATOM
3661
CG
ASN
B
183
28.582
26.720
−5.501
1.00
31.71
B


ATOM
3662
OD1
ASN
B
183
28.246
27.817
−5.885
1.00
31.34
B


ATOM
3663
ND2
ASN
B
183
29.584
26.051
−6.053
1.00
36.11
B


ATOM
3664
C
ASN
B
183
25.514
26.762
−5.043
1.00
27.08
B


ATOM
3665
O
ASN
B
183
24.967
26.885
−6.158
1.00
22.50
B


ATOM
3666
N
ALA
B
184
25.300
27.614
−4.060
1.00
23.13
B


ATOM
3667
CA
ALA
B
184
24.402
28.727
−4.288
1.00
21.08
B


ATOM
3668
CB
ALA
B
184
23.037
28.422
−3.729
1.00
21.32
B


ATOM
3669
C
ALA
B
184
24.976
29.901
−3.566
1.00
22.75
B


ATOM
3670
O
ALA
B
184
25.694
29.761
−2.592
1.00
24.83
B


ATOM
3671
N
SER
B
185
24.625
31.068
−4.041
1.00
22.72
B


ATOM
3672
CA
SER
B
185
25.103
32.284
−3.450
1.00
26.57
B


ATOM
3673
CB
SER
B
185
26.144
32.874
−4.418
1.00
28.05
B


ATOM
3674
OG
SER
B
185
26.220
34.266
−4.248
1.00
41.17
B


ATOM
3675
C
SER
B
185
23.879
33.198
−3.245
1.00
25.15
B


ATOM
3676
O
SER
B
185
22.852
33.042
−3.927
1.00
27.19
B


ATOM
3677
N
ILE
B
186
23.942
34.086
−2.264
1.00
24.64
B


ATOM
3678
CA
ILE
B
186
22.843
35.005
−2.027
1.00
23.33
B


ATOM
3679
CB
ILE
B
186
22.035
34.670
−0.735
1.00
25.15
B


ATOM
3680
CG2
ILE
B
186
21.287
33.323
−0.888
1.00
23.30
B


ATOM
3681
CG1
ILE
B
186
22.965
34.660
0.465
1.00
25.44
B


ATOM
3682
CD1
ILE
B
186
22.267
34.359
1.756
1.00
27.40
B


ATOM
3683
C
ILE
B
186
23.404
36.419
−1.851
1.00
24.37
B


ATOM
3684
O
ILE
B
186
24.489
36.601
−1.290
1.00
23.24
B


ATOM
3685
N
ILE
B
187
22.697
37.403
−2.391
1.00
23.02
B


ATOM
3686
CA
ILE
B
187
23.082
38.798
−2.207
1.00
22.84
B


ATOM
3687
CB
ILE
B
187
22.846
39.621
−3.486
1.00
24.39
B


ATOM
3688
CG2
ILE
B
187
23.191
41.079
−3.214
1.00
24.85
B


ATOM
3689
CG1
ILE
B
187
23.755
39.069
−4.601
1.00
26.00
B


ATOM
3690
CD1
ILE
B
187
23.482
39.621
−6.007
1.00
31.22
B


ATOM
3691
C
ILE
B
187
22.145
39.237
−1.072
1.00
21.88
B


ATOM
3692
O
ILE
B
187
20.928
39.307
−1.244
1.00
18.06
B


ATOM
3693
N
ASN
B
188
22.728
39.500
0.097
1.00
20.03
B


ATOM
3694
CA
ASN
B
188
21.969
39.867
1.298
1.00
20.82
B


ATOM
3695
CB
ASN
B
188
22.924
39.756
2.502
1.00
18.72
B


ATOM
3696
CG
ASN
B
188
22.203
39.619
3.831
1.00
20.78
B


ATOM
3697
OD1
ASN
B
188
20.971
39.545
3.897
1.00
19.18
B


ATOM
3698
ND2
ASN
B
188
22.986
39.565
4.913
1.00
22.75
B


ATOM
3699
C
ASN
B
188
21.362
41.273
1.244
1.00
21.54
B


ATOM
3700
O
ASN
B
188
21.694
42.057
0.361
1.00
23.70
B


ATOM
3701
N
VAL
B
189
20.468
41.583
2.183
1.00
22.12
B


ATOM
3702
CA
VAL
B
189
19.920
42.928
2.298
1.00
21.60
B


ATOM
3703
CB
VAL
B
189
18.761
42.999
3.337
1.00
21.23
B


ATOM
3704
CG1
VAL
B
189
17.710
41.985
2.966
1.00
19.07
B


ATOM
3705
CG2
VAL
B
189
19.298
42.704
4.794
1.00
18.68
B


ATOM
3706
C
VAL
B
189
21.118
43.728
2.800
1.00
21.80
B


ATOM
3707
O
VAL
B
189
22.119
43.162
3.275
1.00
20.03
B


ATOM
3708
N
PRO
B
190
21.058
45.067
2.683
1.00
23.62
B


ATOM
3709
CD
PRO
B
190
19.952
45.927
2.196
1.00
22.76
B


ATOM
3710
CA
PRO
B
190
22.212
45.863
3.149
1.00
20.85
B


ATOM
3711
CB
PRO
B
190
21.714
47.317
2.999
1.00
21.69
B


ATOM
3712
CG
PRO
B
190
20.673
47.221
1.827
1.00
24.78
B


ATOM
3713
C
PRO
B
190
22.659
45.559
4.594
1.00
20.80
B


ATOM
3714
O
PRO
B
190
21.832
45.438
5.495
1.00
18.40
B


ATOM
3715
N
SER
B
191
23.964
45.458
4.799
1.00
20.03
B


ATOM
3716
CA
SER
B
191
24.545
45.211
6.119
1.00
21.28
B


ATOM
3717
CB
SER
B
191
25.562
44.058
6.045
1.00
19.59
B


ATOM
3718
OG
SER
B
191
24.942
42.867
5.651
1.00
24.93
B


ATOM
3719
C
SER
B
191
25.324
46.461
6.602
1.00
20.60
B


ATOM
3720
O
SER
B
191
25.823
47.224
5.792
1.00
21.30
B


ATOM
3721
N
PHE
B
192
25.515
46.609
7.904
1.00
19.63
B


ATOM
3722
CA
PHE
B
192
26.282
47.745
8.393
1.00
21.84
B


ATOM
3723
CB
PHE
B
192
25.417
49.033
8.285
1.00
18.92
B


ATOM
3724
CG
PHE
B
192
23.981
48.865
8.823
1.00
21.72
B


ATOM
3725
CD1
PHE
B
192
23.697
49.027
10.184
1.00
20.59
B


ATOM
3726
CD2
PHE
B
192
22.923
48.545
7.953
1.00
22.45
B


ATOM
3727
CE1
PHE
B
192
22.397
48.885
10.674
1.00
23.50
B


ATOM
3728
CE2
PHE
B
192
21.609
48.394
8.426
1.00
22.94
B


ATOM
3729
CZ
PHE
B
192
21.341
48.568
9.800
1.00
22.39
B


ATOM
3730
C
PHE
B
192
26.795
47.623
9.824
1.00
21.60
B


ATOM
3731
O
PHE
B
192
26.179
46.970
10.672
1.00
20.75
B


ATOM
3732
N
LEU
B
193
27.931
48.254
10.092
1.00
22.13
B


ATOM
3733
CA
LEU
B
193
28.428
48.330
11.459
1.00
22.04
B


ATOM
3734
CB
LEU
B
193
29.835
48.921
11.465
1.00
23.72
B


ATOM
3735
CG
LEU
B
193
30.502
49.181
12.815
1.00
22.77
B


ATOM
3736
CD1
LEU
B
193
30.406
47.931
13.686
1.00
22.50
B


ATOM
3737
CD2
LEU
B
193
31.970
49.572
12.558
1.00
23.46
B


ATOM
3738
C
LEU
B
193
27.418
49.335
12.068
1.00
21.09
B


ATOM
3739
O
LEU
B
193
27.066
50.322
11.423
1.00
22.33
B


ATOM
3740
N
TYR
B
194
26.941
49.064
13.278
1.00
21.78
B


ATOM
3741
CA
TYR
B
194
25.950
49.893
13.970
1.00
22.47
B


ATOM
3742
CB
TYR
B
194
24.784
49.006
14.460
1.00
22.09
B


ATOM
3743
CG
TYR
B
194
23.648
49.707
15.179
1.00
18.54
B


ATOM
3744
CD1
TYR
B
194
23.598
49.765
16.583
1.00
21.22
B


ATOM
3745
CE1
TYR
B
194
22.540
50.430
17.260
1.00
20.11
B


ATOM
3746
CD2
TYR
B
194
22.617
50.312
14.454
1.00
17.85
B


ATOM
3747
CE2
TYR
B
194
21.551
50.955
15.099
1.00
19.87
B


ATOM
3748
CZ
TYR
B
194
21.519
51.025
16.492
1.00
21.49
B


ATOM
3749
OH
TYR
B
194
20.517
51.761
17.098
1.00
21.29
B


ATOM
3750
C
TYR
B
194
26.536
50.659
15.164
1.00
24.91
B


ATOM
3751
O
TYR
B
194
26.299
51.874
15.337
1.00
23.36
B


ATOM
3752
N
GLN
B
195
27.297
49.955
15.987
1.00
26.42
B


ATOM
3753
CA
GLN
B
195
27.875
50.579
17.151
1.00
26.95
B


ATOM
3754
CB
GLN
B
195
26.902
50.511
18.337
1.00
24.84
B


ATOM
3755
CG
GLN
B
195
27.412
51.300
19.549
1.00
26.46
B


ATOM
3756
CD
GLN
B
195
26.353
51.555
20.610
1.00
26.75
B


ATOM
3757
OE1
GLN
B
195
26.684
51.857
21.751
1.00
29.34
B


ATOM
3758
NE2
GLN
B
195
25.085
51.466
20.235
1.00
22.34
B


ATOM
3759
C
GLN
B
195
29.142
49.819
17.409
1.00
28.24
B


ATOM
3760
O
GLN
B
195
29.161
48.605
17.352
1.00
28.82
B


ATOM
3761
N
GLN
B
196
30.196
50.567
17.707
1.00
28.60
B


ATOM
3762
CA
GLN
B
196
31.554
50.075
17.921
1.00
28.90
B


ATOM
3763
CB
GLN
B
196
32.470
51.030
17.156
1.00
32.89
B


ATOM
3764
CG
GLN
B
196
33.820
50.583
16.775
1.00
36.95
B


ATOM
3765
CD
GLN
B
196
34.379
51.519
15.721
1.00
39.73
B


ATOM
3766
OE1
GLN
B
196
34.820
51.077
14.661
1.00
43.26
B


ATOM
3767
NE2
GLN
B
196
34.329
52.828
15.993
1.00
40.01
B


ATOM
3768
C
GLN
B
196
31.974
50.048
19.377
1.00
27.77
B


ATOM
3769
O
GLN
B
196
31.527
50.851
20.161
1.00
27.32
B


ATOM
3770
N
ASP
B
197
32.864
49.129
19.716
1.00
29.24
B


ATOM
3771
CA
ASP
B
197
33.400
48.977
21.066
1.00
33.09
B


ATOM
3772
CB
ASP
B
197
34.616
49.901
21.245
1.00
35.15
B


ATOM
3773
CG
ASP
B
197
35.765
49.521
20.313
1.00
40.80
B


ATOM
3774
OD1
ASP
B
197
36.022
50.230
19.312
1.00
40.71
B


ATOM
3775
OD2
ASP
B
197
36.412
48.486
20.575
1.00
43.69
B


ATOM
3776
C
ASP
B
197
32.424
49.172
22.220
1.00
33.74
B


ATOM
3777
O
ASP
B
197
32.639
50.002
23.104
1.00
31.64
B


ATOM
3778
N
VAL
B
198
31.348
48.399
22.210
1.00
33.10
B


ATOM
3779
CA
VAL
B
198
30.353
48.484
23.253
1.00
33.15
B


ATOM
3780
CB
VAL
B
198
28.989
47.983
22.743
1.00
33.80
B


ATOM
3781
CG1
VAL
B
198
27.971
48.060
23.851
1.00
27.97
B


ATOM
3782
CG2
VAL
B
198
28.557
48.812
21.541
1.00
30.42
B


ATOM
3783
C
VAL
B
198
30.819
47.579
24.382
1.00
35.35
B


ATOM
3784
O
VAL
B
198
31.116
46.405
24.145
1.00
35.20
B


ATOM
3785
N
VAL
B
199
30.896
48.097
25.606
1.00
34.56
B


ATOM
3786
CA
VAL
B
199
31.348
47.229
26.676
1.00
36.32
B


ATOM
3787
CB
VAL
B
199
32.483
47.880
27.528
1.00
38.23
B


ATOM
3788
CG1
VAL
B
199
33.684
48.177
26.644
1.00
40.61
B


ATOM
3789
CG2
VAL
B
199
31.993
49.132
28.197
1.00
39.10
B


ATOM
3790
C
VAL
B
199
30.188
46.854
27.569
1.00
36.00
B


ATOM
3791
O
VAL
B
199
29.429
47.709
28.001
1.00
35.56
B


ATOM
3792
N
VAL
B
200
30.030
45.561
27.806
1.00
34.64
B


ATOM
3793
CA
VAL
B
200
28.982
45.077
28.680
1.00
37.73
B


ATOM
3794
CB
VAL
B
200
27.979
44.195
27.933
1.00
39.32
B


ATOM
3795
CG1
VAL
B
200
27.082
45.059
27.079
1.00
42.45
B


ATOM
3796
CG2
VAL
B
200
28.716
43.198
27.094
1.00
37.56
B


ATOM
3797
C
VAL
B
200
29.622
44.228
29.768
1.00
36.92
B


ATOM
3798
O
VAL
B
200
30.689
43.643
29.580
1.00
37.21
B


ATOM
3799
N
VAL
B
201
28.966
44.156
30.909
1.00
36.03
B


ATOM
3800
CA
VAL
B
201
29.501
43.354
31.973
1.00
35.64
B


ATOM
3801
CB
VAL
B
201
29.529
44.154
33.299
1.00
38.23
B


ATOM
3802
CG1
VAL
B
201
29.931
43.238
34.446
1.00
36.70
B


ATOM
3803
CG2
VAL
B
201
30.501
45.331
33.169
1.00
38.09
B


ATOM
3804
C
VAL
B
201
28.622
42.126
32.111
1.00
34.41
B


ATOM
3805
O
VAL
B
201
27.428
42.237
32.362
1.00
33.60
B


ATOM
3806
N
LEU
B
202
29.213
40.953
31.928
1.00
35.90
B


ATOM
3807
CA
LEU
B
202
28.471
39.703
32.039
1.00
37.78
B


ATOM
3808
CB
LEU
B
202
28.951
38.728
30.971
1.00
35.05
B


ATOM
3809
CG
LEU
B
202
28.793
39.191
29.533
1.00
33.84
B


ATOM
3810
CD1
LEU
B
202
29.425
38.180
28.593
1.00
30.94
B


ATOM
3811
CD2
LEU
B
202
27.336
39.353
29.242
1.00
35.94
B


ATOM
3812
C
LEU
B
202
28.675
39.081
33.431
1.00
40.45
B


ATOM
3813
O
LEU
B
202
29.591
39.473
34.160
1.00
40.07
B


ATOM
3814
N
PRO
B
203
27.804
38.129
33.828
1.00
41.47
B


ATOM
3815
CD
PRO
B
203
26.463
37.810
33.290
1.00
41.41
B


ATOM
3816
CA
PRO
B
203
27.996
37.519
35.147
1.00
43.94
B


ATOM
3817
CB
PRO
B
203
26.958
36.402
35.164
1.00
41.84
B


ATOM
3818
CG
PRO
B
203
25.794
37.075
34.454
1.00
41.27
B


ATOM
3819
C
PRO
B
203
29.426
37.009
35.328
1.00
46.88
B


ATOM
3820
O
PRO
B
203
30.146
36.759
34.355
1.00
46.53
B


ATOM
3821
N
LYS
B
204
29.801
36.861
36.596
1.00
50.44
B


ATOM
3822
CA
LYS
B
204
31.119
36.439
37.043
1.00
52.55
B


ATOM
3823
CB
LYS
B
204
30.980
35.575
38.302
1.00
54.47
B


ATOM
3824
CG
LYS
B
204
30.516
36.350
39.527
1.00
58.74
B


ATOM
3825
CD
LYS
B
204
31.660
36.551
40.532
1.00
62.51
B


ATOM
3826
CE
LYS
B
204
32.839
37.334
39.944
1.00
65.55
B


ATOM
3827
NZ
LYS
B
204
32.432
38.713
39.490
1.00
66.87
B


ATOM
3828
C
LYS
B
204
32.066
35.753
36.070
1.00
53.04
B


ATOM
3829
O
LYS
B
204
33.050
36.357
35.615
1.00
56.07
B


ATOM
3830
N
PRO
B
205
31.776
34.494
35.713
1.00
51.38
B


ATOM
3831
CD
PRO
B
205
30.410
33.932
35.730
1.00
48.40
B


ATOM
3832
CA
PRO
B
205
32.645
33.744
34.795
1.00
48.13
B


ATOM
3833
CB
PRO
B
205
31.692
32.718
34.183
1.00
48.22
B


ATOM
3834
CG
PRO
B
205
30.640
32.549
35.238
1.00
49.33
B


ATOM
3835
C
PRO
B
205
33.337
34.572
33.717
1.00
46.87
B


ATOM
3836
O
PRO
B
205
34.540
34.442
33.476
1.00
48.54
B


ATOM
3837
N
TYR
B
206
32.569
35.450
33.092
1.00
44.86
B


ATOM
3838
CA
TYR
B
206
33.044
36.245
31.967
1.00
41.86
B


ATOM
3839
CB
TYR
B
206
31.966
36.187
30.879
1.00
39.01
B


ATOM
3840
CG
TYR
B
206
31.542
34.761
30.616
1.00
35.04
B


ATOM
3841
CD1
TYR
B
206
32.341
33.912
29.855
1.00
33.92
B


ATOM
3842
CE1
TYR
B
206
32.001
32.591
29.652
1.00
34.84
B


ATOM
3843
CD2
TYR
B
206
30.377
34.250
31.174
1.00
33.09
B


ATOM
3844
CE2
TYR
B
206
30.018
32.918
30.986
1.00
34.92
B


ATOM
3845
CZ
TYR
B
206
30.837
32.096
30.225
1.00
35.22
B


ATOM
3846
OH
TYR
B
206
30.508
30.776
30.064
1.00
36.75
B


ATOM
3847
C
TYR
B
206
33.465
37.679
32.218
1.00
41.31
B


ATOM
3848
O
TYR
B
206
34.363
38.186
31.534
1.00
42.16
B


ATOM
3849
N
GLY
B
207
32.812
38.341
33.165
1.00
40.65
B


ATOM
3850
CA
GLY
B
207
33.171
39.713
33.469
1.00
40.15
B


ATOM
3851
C
GLY
B
207
32.882
40.687
32.341
1.00
41.22
B


ATOM
3852
O
GLY
B
207
31.960
40.496
31.533
1.00
40.83
B


ATOM
3853
N
GLU
B
208
33.688
41.738
32.274
1.00
38.29
B


ATOM
3854
CA
GLU
B
208
33.490
42.758
31.272
1.00
37.17
B


ATOM
3855
CB
GLU
B
208
34.130
44.055
31.744
1.00
38.43
B


ATOM
3856
CG
GLU
B
208
34.041
45.163
30.751
1.00
39.93
B


ATOM
3857
CD
GLU
B
208
34.769
46.413
31.232
1.00
43.29
B


ATOM
3858
OE1
GLU
B
208
34.360
46.979
32.277
1.00
40.64
B


ATOM
3859
OE2
GLU
B
208
35.744
46.814
30.552
1.00
43.54
B


ATOM
3860
C
GLU
B
208
34.064
42.347
29.933
1.00
35.54
B


ATOM
3861
O
GLU
B
208
35.164
41.805
29.859
1.00
35.57
B


ATOM
3862
N
VAL
B
209
33.333
42.645
28.868
1.00
33.17
B


ATOM
3863
CA
VAL
B
209
33.769
42.259
27.534
1.00
33.03
B


ATOM
3864
CB
VAL
B
209
33.029
40.936
27.175
1.00
34.46
B


ATOM
3865
CG1
VAL
B
209
31.710
41.234
26.475
1.00
31.11
B


ATOM
3866
CG2
VAL
B
209
33.937
40.014
26.407
1.00
38.25
B


ATOM
3867
C
VAL
B
209
33.446
43.402
26.544
1.00
31.89
B


ATOM
3868
O
VAL
B
209
32.485
44.128
26.745
1.00
32.72
B


ATOM
3869
N
ALA
B
210
34.256
43.597
25.511
1.00
30.54
B


ATOM
3870
CA
ALA
B
210
33.978
44.657
24.532
1.00
31.33
B


ATOM
3871
CB
ALA
B
210
35.213
45.552
24.332
1.00
29.78
B


ATOM
3872
C
ALA
B
210
33.543
44.036
23.195
1.00
29.61
B


ATOM
3873
O
ALA
B
210
34.167
43.095
22.698
1.00
30.07
B


ATOM
3874
N
VAL
B
211
32.483
44.573
22.607
1.00
27.92
B


ATOM
3875
CA
VAL
B
211
31.962
44.018
21.357
1.00
26.48
B


ATOM
3876
CB
VAL
B
211
30.717
43.108
21.639
1.00
26.81
B


ATOM
3877
CG1
VAL
B
211
30.979
42.152
22.836
1.00
25.54
B


ATOM
3878
CG2
VAL
B
211
29.492
43.974
21.928
1.00
24.69
B


ATOM
3879
C
VAL
B
211
31.506
45.063
20.370
1.00
26.64
B


ATOM
3880
O
VAL
B
211
31.354
46.213
20.721
1.00
28.66
B


ATOM
3881
N
ASP
B
212
31.277
44.651
19.125
1.00
27.44
B


ATOM
3882
CA
ASP
B
212
30.705
45.532
18.098
1.00
24.95
B


ATOM
3883
CB
ASP
B
212
31.474
45.472
16.787
1.00
26.88
B


ATOM
3884
CG
ASP
B
212
32.867
46.064
16.899
1.00
29.89
B


ATOM
3885
OD1
ASP
B
212
33.047
46.951
17.772
1.00
29.64
B


ATOM
3886
OD2
ASP
B
212
33.757
45.655
16.113
1.00
29.19
B


ATOM
3887
C
ASP
B
212
29.299
45.008
17.823
1.00
26.59
B


ATOM
3888
O
ASP
B
212
29.041
43.789
17.956
1.00
25.79
B


ATOM
3889
N
ILE
B
213
28.386
45.909
17.448
1.00
22.74
B


ATOM
3890
CA
ILE
B
213
27.033
45.519
17.135
1.00
21.19
B


ATOM
3891
CB
ILE
B
213
25.999
46.328
17.917
1.00
20.29
B


ATOM
3892
CG2
ILE
B
213
24.548
45.999
17.423
1.00
16.92
B


ATOM
3893
CG1
ILE
B
213
26.142
46.016
19.414
1.00
16.96
B


ATOM
3894
CD1
ILE
B
213
25.177
46.778
20.308
1.00
18.18
B


ATOM
3895
C
ILE
B
213
26.952
45.854
15.649
1.00
25.13
B


ATOM
3896
O
ILE
B
213
27.286
46.989
15.243
1.00
22.61
B


ATOM
3897
N
ALA
B
214
26.551
44.858
14.843
1.00
23.15
B


ATOM
3898
CA
ALA
B
214
26.417
45.032
13.402
1.00
21.58
B


ATOM
3899
CB
ALA
B
214
27.635
44.515
12.724
1.00
22.03
B


ATOM
3900
C
ALA
B
214
25.191
44.295
12.872
1.00
22.41
B


ATOM
3901
O
ALA
B
214
24.798
43.239
13.387
1.00
22.71
B


ATOM
3902
N
PHE
B
215
24.576
44.863
11.844
1.00
20.74
B


ATOM
3903
CA
PHE
B
215
23.406
44.257
11.257
1.00
19.52
B


ATOM
3904
CB
PHE
B
215
22.398
45.338
10.852
1.00
20.22
B


ATOM
3905
CG
PHE
B
215
21.127
44.784
10.222
1.00
17.78
B


ATOM
3906
CD1
PHE
B
215
20.140
44.178
11.025
1.00
18.65
B


ATOM
3907
CD2
PHE
B
215
20.916
44.875
8.848
1.00
16.90
B


ATOM
3908
CE1
PHE
B
215
18.936
43.667
10.463
1.00
18.69
B


ATOM
3909
CE2
PHE
B
215
19.701
44.364
8.248
1.00
14.91
B


ATOM
3910
CZ
PHE
B
215
18.713
43.762
9.066
1.00
18.21
B


ATOM
3911
C
PHE
B
215
23.818
43.484
10.017
1.00
18.87
B


ATOM
3912
O
PHE
B
215
24.532
44.025
9.163
1.00
15.66
B


ATOM
3913
N
GLY
B
216
23.399
42.221
9.924
1.00
18.99
B


ATOM
3914
CA
GLY
B
216
23.710
41.438
8.732
1.00
18.82
B


ATOM
3915
C
GLY
B
216
22.460
40.718
8.223
1.00
20.31
B


ATOM
3916
O
GLY
B
216
22.555
39.722
7.526
1.00
20.48
B


ATOM
3917
N
GLY
B
217
21.291
41.251
8.554
1.00
16.48
B


ATOM
3918
CA
GLY
B
217
20.047
40.595
8.201
1.00
18.41
B


ATOM
3919
C
GLY
B
217
19.377
40.410
9.562
1.00
18.48
B


ATOM
3920
O
GLY
B
217
18.131
40.401
9.691
1.00
16.81
B


ATOM
3921
N
ASN
B
218
20.239
40.252
10.573
1.00
14.32
B


ATOM
3922
CA
ASN
B
218
19.854
40.188
11.992
1.00
17.64
B


ATOM
3923
CB
ASN
B
218
20.047
38.776
12.579
1.00
13.91
B


ATOM
3924
CG
ASN
B
218
19.194
37.751
11.873
1.00
13.87
B


ATOM
3925
OD1
ASN
B
218
17.977
37.878
11.872
1.00
17.25
B


ATOM
3926
ND2
ASN
B
218
19.814
36.757
11.262
1.00
10.85
B


ATOM
3927
C
ASN
B
218
20.900
41.114
12.665
1.00
17.23
B


ATOM
3928
O
ASN
B
218
21.974
41.341
12.079
1.00
19.41
B


ATOM
3929
N
PHE
B
219
20.584
41.654
13.840
1.00
15.60
B


ATOM
3930
CA
PHE
B
219
21.578
42.443
14.596
1.00
16.70
B


ATOM
3931
CB
PHE
B
219
20.932
43.362
15.627
1.00
16.41
B


ATOM
3932
CG
PHE
B
219
20.573
44.717
15.092
1.00
16.73
B


ATOM
3933
CD1
PHE
B
219
19.237
45.101
14.969
1.00
19.82
B


ATOM
3934
CD2
PHE
B
219
21.565
45.616
14.740
1.00
17.46
B


ATOM
3935
CE1
PHE
B
219
18.896
46.383
14.495
1.00
20.17
B


ATOM
3936
CE2
PHE
B
219
21.237
46.899
14.270
1.00
17.52
B


ATOM
3937
CZ
PHE
B
219
19.906
47.275
14.147
1.00
19.68
B


ATOM
3938
C
PHE
B
219
22.392
41.434
15.352
1.00
15.65
B


ATOM
3939
O
PHE
B
219
21.824
40.513
15.960
1.00
16.90
B


ATOM
3940
N
PHE
B
220
23.707
41.579
15.288
1.00
17.38
B


ATOM
3941
CA
PHE
B
220
24.647
40.686
15.990
1.00
17.36
B


ATOM
3942
CB
PHE
B
220
25.669
40.052
15.008
1.00
14.53
B


ATOM
3943
CG
PHE
B
220
25.140
38.895
14.183
1.00
18.08
B


ATOM
3944
CD1
PHE
B
220
25.443
37.571
14.533
1.00
14.69
B


ATOM
3945
CD2
PHE
B
220
24.368
39.130
13.052
1.00
18.82
B


ATOM
3946
CE1
PHE
B
220
24.982
36.499
13.761
1.00
21.99
B


ATOM
3947
CE2
PHE
B
220
23.888
38.049
12.259
1.00
18.50
B


ATOM
3948
CZ
PHE
B
220
24.194
36.737
12.616
1.00
19.93
B


ATOM
3949
C
PHE
B
220
25.535
41.482
16.979
1.00
20.92
B


ATOM
3950
O
PHE
B
220
25.857
42.652
16.740
1.00
21.11
B


ATOM
3951
N
ALA
B
221
25.949
40.814
18.054
1.00
20.42
B


ATOM
3952
CA
ALA
B
221
26.962
41.372
18.950
1.00
21.16
B


ATOM
3953
CB
ALA
B
221
26.652
41.098
20.431
1.00
20.21
B


ATOM
3954
C
ALA
B
221
28.129
40.473
18.492
1.00
20.00
B


ATOM
3955
O
ALA
B
221
28.021
39.259
18.526
1.00
18.54
B


ATOM
3956
N
ILE
B
222
29.218
41.058
18.028
1.00
20.84
B


ATOM
3957
CA
ILE
B
222
30.370
40.284
17.598
1.00
21.05
B


ATOM
3958
CB
ILE
B
222
30.872
40.813
16.270
1.00
19.03
B


ATOM
3959
CG2
ILE
B
222
32.077
39.978
15.827
1.00
21.00
B


ATOM
3960
CG1
ILE
B
222
29.695
40.812
15.258
1.00
19.75
B


ATOM
3961
CD1
ILE
B
222
30.013
41.277
13.822
1.00
21.35
B


ATOM
3962
C
ILE
B
222
31.469
40.380
18.687
1.00
22.59
B


ATOM
3963
O
ILE
B
222
31.852
41.475
19.092
1.00
22.63
B


ATOM
3964
N
VAL
B
223
31.957
39.236
19.163
1.00
23.55
B


ATOM
3965
CA
VAL
B
223
32.949
39.223
20.229
1.00
23.54
B


ATOM
3966
CB
VAL
B
223
32.219
38.970
21.596
1.00
22.80
B


ATOM
3967
CG1
VAL
B
223
31.568
37.621
21.576
1.00
24.59
B


ATOM
3968
CG2
VAL
B
223
33.183
39.048
22.782
1.00
22.04
B


ATOM
3969
C
VAL
B
223
34.060
38.170
20.039
1.00
25.89
B


ATOM
3970
O
VAL
B
223
33.809
37.057
19.534
1.00
24.57
B


ATOM
3971
N
PRO
B
224
35.316
38.513
20.401
1.00
25.09
B


ATOM
3972
CD
PRO
B
224
35.889
39.854
20.644
1.00
24.97
B


ATOM
3973
CA
PRO
B
224
36.363
37.492
20.238
1.00
24.62
B


ATOM
3974
CB
PRO
B
224
37.671
38.282
20.393
1.00
27.03
B


ATOM
3975
CG
PRO
B
224
37.271
39.736
20.045
1.00
27.24
B


ATOM
3976
C
PRO
B
224
36.194
36.457
21.357
1.00
25.91
B


ATOM
3977
O
PRO
B
224
35.868
36.809
22.497
1.00
28.33
B


ATOM
3978
N
ALA
B
225
36.377
35.185
21.029
1.00
25.54
B


ATOM
3979
CA
ALA
B
225
36.274
34.117
21.997
1.00
27.25
B


ATOM
3980
CB
ALA
B
225
36.563
32.762
21.322
1.00
23.58
B


ATOM
3981
C
ALA
B
225
37.303
34.369
23.104
1.00
30.20
B


ATOM
3982
O
ALA
B
225
37.059
34.078
24.286
1.00
28.25
B


ATOM
3983
N
GLU
B
226
38.455
34.897
22.702
1.00
32.53
B


ATOM
3984
CA
GLU
B
226
39.522
35.188
23.637
1.00
36.92
B


ATOM
3985
CB
GLU
B
226
40.712
35.778
22.852
1.00
41.09
B


ATOM
3986
CG
GLU
B
226
41.594
36.739
23.597
1.00
47.67
B


ATOM
3987
CD
GLU
B
226
41.011
38.145
23.613
1.00
52.00
B


ATOM
3988
OE1
GLU
B
226
40.606
38.635
22.517
1.00
54.29
B


ATOM
3989
OE2
GLU
B
226
40.967
38.756
24.713
1.00
53.44
B


ATOM
3990
C
GLU
B
226
39.047
36.090
24.803
1.00
36.91
B


ATOM
3991
O
GLU
B
226
39.537
35.977
25.927
1.00
35.72
B


ATOM
3992
N
GLN
B
227
38.071
36.956
24.552
1.00
35.92
B


ATOM
3993
CA
GLN
B
227
37.572
37.817
25.618
1.00
37.80
B


ATOM
3994
CB
GLN
B
227
36.833
39.006
25.047
1.00
39.77
B


ATOM
3995
CG
GLN
B
227
37.747
40.146
24.734
1.00
43.88
B


ATOM
3996
CD
GLN
B
227
37.050
41.428
24.962
1.00
48.12
B


ATOM
3997
OE1
GLN
B
227
36.188
41.806
24.175
1.00
50.21
B


ATOM
3998
NE2
GLN
B
227
37.378
42.107
26.074
1.00
49.13
B


ATOM
3999
C
GLN
B
227
36.661
37.113
26.599
1.00
36.57
B


ATOM
4000
O
GLN
B
227
36.426
37.605
27.701
1.00
37.01
B


ATOM
4001
N
LEU
B
228
36.131
35.969
26.191
1.00
33.41
B


ATOM
4002
CA
LEU
B
228
35.247
35.204
27.037
1.00
32.10
B


ATOM
4003
CB
LEU
B
228
34.173
34.489
26.189
1.00
30.91
B


ATOM
4004
CG
LEU
B
228
33.275
35.378
25.343
1.00
30.21
B


ATOM
4005
CD1
LEU
B
228
32.395
34.512
24.423
1.00
28.88
B


ATOM
4006
CD2
LEU
B
228
32.422
36.246
26.279
1.00
29.70
B


ATOM
4007
C
LEU
B
228
36.127
34.179
27.720
1.00
31.97
B


ATOM
4008
O
LEU
B
228
35.664
33.425
28.557
1.00
32.83
B


ATOM
4009
N
GLY
B
229
37.400
34.152
27.343
1.00
34.37
B


ATOM
4010
CA
GLY
B
229
38.328
33.193
27.919
1.00
35.86
B


ATOM
4011
C
GLY
B
229
37.923
31.760
27.617
1.00
39.19
B


ATOM
4012
O
GLY
B
229
38.058
30.876
28.470
1.00
39.69
B


ATOM
4013
N
ILE
B
230
37.416
31.540
26.403
1.00
39.34
B


ATOM
4014
CA
ILE
B
230
36.973
30.222
25.946
1.00
39.93
B


ATOM
4015
CB
ILE
B
230
35.424
30.118
25.867
1.00
41.97
B


ATOM
4016
CG2
ILE
B
230
35.008
28.728
25.307
1.00
43.55
B


ATOM
4017
CG1
ILE
B
230
34.789
30.356
27.232
1.00
43.87
B


ATOM
4018
CD1
ILE
B
230
33.258
30.354
27.175
1.00
42.99
B


ATOM
4019
C
ILE
B
230
37.459
30.033
24.512
1.00
39.54
B


ATOM
4020
O
ILE
B
230
37.307
30.927
23.684
1.00
39.70
B


ATOM
4021
N
ASP
B
231
38.042
28.884
24.203
1.00
39.51
B


ATOM
4022
CA
ASP
B
231
38.459
28.656
22.832
1.00
38.89
B


ATOM
4023
CB
ASP
B
231
39.581
27.633
22.765
1.00
45.03
B


ATOM
4024
CG
ASP
B
231
40.869
28.168
23.328
1.00
51.63
B


ATOM
4025
OD1
ASP
B
231
41.325
29.220
22.823
1.00
55.97
B


ATOM
4026
OD2
ASP
B
231
41.429
27.555
24.272
1.00
55.23
B


ATOM
4027
C
ASP
B
231
37.248
28.102
22.118
1.00
35.71
B


ATOM
4028
O
ASP
B
231
36.399
27.453
22.730
1.00
33.16
B


ATOM
4029
N
ILE
B
232
37.157
28.374
20.825
1.00
33.95
B


ATOM
4030
CA
ILE
B
232
36.061
27.860
20.026
1.00
31.83
B


ATOM
4031
CB
ILE
B
232
35.894
28.645
18.732
1.00
30.95
B


ATOM
4032
CG2
ILE
B
232
34.927
27.907
17.808
1.00
27.81
B


ATOM
4033
CG1
ILE
B
232
35.434
30.069
19.057
1.00
26.67
B


ATOM
4034
CD1
ILE
B
232
35.468
31.012
17.875
1.00
28.24
B


ATOM
4035
C
ILE
B
232
36.453
26.440
19.659
1.00
33.88
B


ATOM
4036
O
ILE
B
232
37.388
26.237
18.872
1.00
36.07
B


ATOM
4037
N
SER
B
233
35.754
25.466
20.234
1.00
31.46
B


ATOM
4038
CA
SER
B
233
36.027
24.059
19.976
1.00
32.58
B


ATOM
4039
CB
SER
B
233
37.190
23.566
20.842
1.00
32.17
B


ATOM
4040
OG
SER
B
233
36.779
23.577
22.205
1.00
31.71
B


ATOM
4041
C
SER
B
233
34.782
23.308
20.399
1.00
32.73
B


ATOM
4042
O
SER
B
233
33.949
23.838
21.141
1.00
32.49
B


ATOM
4043
N
VAL
B
234
34.668
22.064
19.964
1.00
32.35
B


ATOM
4044
CA
VAL
B
234
33.510
21.278
20.326
1.00
34.27
B


ATOM
4045
CB
VAL
B
234
33.546
19.948
19.583
1.00
36.16
B


ATOM
4046
CG1
VAL
B
234
32.335
19.078
19.957
1.00
34.94
B


ATOM
4047
CG2
VAL
B
234
33.602
20.248
18.075
1.00
34.29
B


ATOM
4048
C
VAL
B
234
33.407
21.066
21.823
1.00
35.04
B


ATOM
4049
O
VAL
B
234
32.310
21.153
22.398
1.00
37.39
B


ATOM
4050
N
GLN
B
235
34.535
20.825
22.484
1.00
34.17
B


ATOM
4051
CA
GLN
B
235
34.496
20.615
23.928
1.00
35.01
B


ATOM
4052
CB
GLN
B
235
35.912
20.403
24.482
1.00
40.67
B


ATOM
4053
CG
GLN
B
235
36.584
19.102
24.082
1.00
46.21
B


ATOM
4054
CD
GLN
B
235
36.597
18.913
22.580
1.00
52.08
B


ATOM
4055
OE1
GLN
B
235
36.986
19.825
21.826
1.00
53.72
B


ATOM
4056
NE2
GLN
B
235
36.167
17.724
22.123
1.00
53.39
B


ATOM
4057
C
GLN
B
235
33.849
21.759
24.718
1.00
33.35
B


ATOM
4058
O
GLN
B
235
33.304
21.543
25.805
1.00
31.51
B


ATOM
4059
N
ASN
B
236
33.933
22.980
24.191
1.00
33.62
B


ATOM
4060
CA
ASN
B
236
33.405
24.150
24.883
1.00
32.03
B


ATOM
4061
CB
ASN
B
236
34.391
25.300
24.734
1.00
32.81
B


ATOM
4062
CG
ASN
B
236
35.688
25.062
25.500
1.00
33.53
B


ATOM
4063
OD1
ASN
B
236
36.774
25.314
24.997
1.00
33.41
B


ATOM
4064
ND2
ASN
B
236
35.569
24.589
26.723
1.00
34.88
B


ATOM
4065
C
ASN
B
236
32.020
24.655
24.495
1.00
31.94
B


ATOM
4066
O
ASN
B
236
31.602
25.711
24.982
1.00
31.07
B


ATOM
4067
N
LEU
B
237
31.303
23.902
23.666
1.00
30.74
B


ATOM
4068
CA
LEU
B
237
29.991
24.345
23.174
1.00
31.70
B


ATOM
4069
CB
LEU
B
237
29.424
23.294
22.232
1.00
30.14
B


ATOM
4070
CG
LEU
B
237
28.481
23.780
21.135
1.00
35.92
B


ATOM
4071
CD1
LEU
B
237
28.819
25.213
20.688
1.00
32.89
B


ATOM
4072
CD2
LEU
B
237
28.588
22.812
19.965
1.00
34.63
B


ATOM
4073
C
LEU
B
237
28.975
24.735
24.263
1.00
30.38
B


ATOM
4074
O
LEU
B
237
28.288
25.760
24.141
1.00
28.54
B


ATOM
4075
N
SER
B
238
28.870
23.946
25.327
1.00
27.87
B


ATOM
4076
CA
SER
B
238
27.968
24.332
26.398
1.00
30.23
B


ATOM
4077
CB
SER
B
238
27.987
23.307
27.514
1.00
31.81
B


ATOM
4078
OG
SER
B
238
27.245
22.173
27.099
1.00
39.22
B


ATOM
4079
C
SER
B
238
28.344
25.707
26.969
1.00
29.61
B


ATOM
4080
O
SER
B
238
27.473
26.548
27.245
1.00
29.19
B


ATOM
4081
N
ARG
B
239
29.639
25.934
27.137
1.00
29.84
B


ATOM
4082
CA
ARG
B
239
30.106
27.207
27.664
1.00
29.36
B


ATOM
4083
CB
ARG
B
239
31.609
27.143
27.967
1.00
31.87
B


ATOM
4084
CG
ARG
B
239
31.970
26.367
29.232
1.00
38.00
B


ATOM
4085
CD
ARG
B
239
33.474
25.991
29.231
1.00
41.82
B


ATOM
4086
NE
ARG
B
239
34.343
27.165
29.125
1.00
47.34
B


ATOM
4087
CZ
ARG
B
239
35.668
27.133
28.952
1.00
48.64
B


ATOM
4088
NH1
ARG
B
239
36.307
25.975
28.864
1.00
48.73
B


ATOM
4089
NH2
ARG
B
239
36.356
28.273
28.858
1.00
48.08
B


ATOM
4090
C
ARG
B
239
29.834
28.330
26.670
1.00
27.01
B


ATOM
4091
O
ARG
B
239
29.387
29.419
27.043
1.00
24.04
B


ATOM
4092
N
LEU
B
240
30.139
28.077
25.403
1.00
23.94
B


ATOM
4093
CA
LEU
B
240
29.901
29.102
24.397
1.00
23.32
B


ATOM
4094
CB
LEU
B
240
30.448
28.654
23.034
1.00
22.20
B


ATOM
4095
CG
LEU
B
240
31.989
28.602
22.975
1.00
22.16
B


ATOM
4096
CD1
LEU
B
240
32.390
27.645
21.895
1.00
25.36
B


ATOM
4097
CD2
LEU
B
240
32.599
29.958
22.683
1.00
24.14
B


ATOM
4098
C
LEU
B
240
28.421
29.488
24.319
1.00
21.17
B


ATOM
4099
O
LEU
B
240
28.102
30.676
24.179
1.00
22.02
B


ATOM
4100
N
GLN
B
241
27.520
28.515
24.462
1.00
20.36
B


ATOM
4101
CA
GLN
B
241
26.095
28.803
24.407
1.00
22.99
B


ATOM
4102
CB
GLN
B
241
25.256
27.514
24.382
1.00
23.87
B


ATOM
4103
CG
GLN
B
241
25.509
26.532
23.238
1.00
28.86
B


ATOM
4104
CD
GLN
B
241
24.472
25.380
23.265
1.00
31.87
B


ATOM
4105
OE1
GLN
B
241
23.779
25.188
24.273
1.00
35.06
B


ATOM
4106
NE2
GLN
B
241
24.359
24.634
22.171
1.00
30.36
B


ATOM
4107
C
GLN
B
241
25.638
29.652
25.597
1.00
23.20
B


ATOM
4108
O
GLN
B
241
24.793
30.560
25.446
1.00
20.26
B


ATOM
4109
N
GLU
B
242
26.156
29.337
26.792
1.00
22.88
B


ATOM
4110
CA
GLU
B
242
25.788
30.087
27.964
1.00
22.42
B


ATOM
4111
CB
GLU
B
242
26.355
29.421
29.221
1.00
28.71
B


ATOM
4112
CG
GLU
B
242
25.483
28.260
29.702
1.00
36.67
B


ATOM
4113
CD
GLU
B
242
26.188
27.371
30.721
1.00
41.80
B


ATOM
4114
OE1
GLU
B
242
26.823
27.915
31.658
1.00
46.86
B


ATOM
4115
OE2
GLU
B
242
26.101
26.129
30.581
1.00
43.93
B


ATOM
4116
C
GLU
B
242
26.287
31.513
27.823
1.00
21.20
B


ATOM
4117
O
GLU
B
242
25.525
32.440
28.048
1.00
25.61
B


ATOM
4118
N
ALA
B
243
27.541
31.696
27.421
1.00
22.11
B


ATOM
4119
CA
ALA
B
243
28.098
33.043
27.245
1.00
20.87
B


ATOM
4120
CB
ALA
B
243
29.586
32.949
26.834
1.00
20.20
B


ATOM
4121
C
ALA
B
243
27.313
33.824
26.187
1.00
21.83
B


ATOM
4122
O
ALA
B
243
27.019
35.029
26.350
1.00
19.38
B


ATOM
4123
N
GLY
B
244
26.974
33.125
25.099
1.00
19.83
B


ATOM
4124
CA
GLY
B
244
26.220
33.749
24.019
1.00
17.96
B


ATOM
4125
C
GLY
B
244
24.868
34.205
24.520
1.00
16.76
B


ATOM
4126
O
GLY
B
244
24.438
35.301
24.192
1.00
18.51
B


ATOM
4127
N
GLU
B
245
24.187
33.376
25.315
1.00
18.05
B


ATOM
4128
CA
GLU
B
245
22.869
33.731
25.875
1.00
18.68
B


ATOM
4129
CB
GLU
B
245
22.258
32.524
26.600
1.00
18.41
B


ATOM
4130
CG
GLU
B
245
21.001
32.823
27.418
1.00
18.86
B


ATOM
4131
CD
GLU
B
245
19.804
33.258
26.562
1.00
26.70
B


ATOM
4132
OE1
GLU
B
245
19.107
34.218
26.980
1.00
23.58
B


ATOM
4133
OE2
GLU
B
245
19.558
32.635
25.489
1.00
25.59
B


ATOM
4134
C
GLU
B
245
22.972
34.921
26.857
1.00
20.93
B


ATOM
4135
O
GLU
B
245
22.226
35.898
26.744
1.00
19.67
B


ATOM
4136
N
LEU
B
246
23.901
34.837
27.817
1.00
22.15
B


ATOM
4137
CA
LEU
B
246
24.115
35.932
28.791
1.00
21.85
B


ATOM
4138
CB
LEU
B
246
25.220
35.524
29.799
1.00
22.31
B


ATOM
4139
CG
LEU
B
246
24.855
34.275
30.619
1.00
23.50
B


ATOM
4140
CD1
LEU
B
246
25.985
33.932
31.618
1.00
22.59
B


ATOM
4141
CD2
LEU
B
246
23.523
34.524
31.370
1.00
23.93
B


ATOM
4142
C
LEU
B
246
24.523
37.240
28.088
1.00
22.02
B


ATOM
4143
O
LEU
B
246
24.093
38.310
28.477
1.00
22.87
B


ATOM
4144
N
LEU
B
247
25.361
37.172
27.055
1.00
22.12
B


ATOM
4145
CA
LEU
B
247
25.741
38.392
26.361
1.00
21.46
B


ATOM
4146
CB
LEU
B
247
26.939
38.130
25.434
1.00
22.75
B


ATOM
4147
CG
LEU
B
247
27.408
39.192
24.428
1.00
27.31
B


ATOM
4148
CD1
LEU
B
247
27.625
40.552
25.110
1.00
32.23
B


ATOM
4149
CD2
LEU
B
247
28.738
38.730
23.816
1.00
29.23
B


ATOM
4150
C
LEU
B
247
24.541
38.974
25.569
1.00
23.36
B


ATOM
4151
O
LEU
B
247
24.312
40.192
25.569
1.00
24.82
B


ATOM
4152
N
ARG
B
248
23.767
38.131
24.896
1.00
21.35
B


ATOM
4153
CA
ARG
B
248
22.611
38.626
24.151
1.00
18.39
B


ATOM
4154
CB
ARG
B
248
21.886
37.441
23.486
1.00
20.48
B


ATOM
4155
CG
ARG
B
248
20.497
37.773
22.940
1.00
19.16
B


ATOM
4156
CD
ARG
B
248
19.895
36.500
22.342
1.00
18.96
B


ATOM
4157
NE
ARG
B
248
18.614
36.734
21.687
1.00
18.46
B


ATOM
4158
CZ
ARG
B
248
17.891
35.759
21.135
1.00
21.38
B


ATOM
4159
NH1
ARG
B
248
18.352
34.505
21.176
1.00
20.14
B


ATOM
4160
NH2
ARG
B
248
16.734
36.029
20.534
1.00
19.23
B


ATOM
4161
C
ARG
B
248
21.627
39.331
25.112
1.00
19.61
B


ATOM
4162
O
ARG
B
248
21.093
40.403
24.819
1.00
19.89
B


ATOM
4163
N
THR
B
249
21.354
38.721
26.259
1.00
20.63
B


ATOM
4164
CA
THR
B
249
20.411
39.320
27.210
1.00
20.30
B


ATOM
4165
CB
THR
B
249
20.122
38.319
28.354
1.00
23.57
B


ATOM
4166
OG1
THR
B
249
19.580
37.120
27.769
1.00
26.35
B


ATOM
4167
CG2
THR
B
249
19.089
38.881
29.361
1.00
20.63
B


ATOM
4168
C
THR
B
249
20.912
40.662
27.783
1.00
21.90
B


ATOM
4169
O
THR
B
249
20.136
41.622
27.908
1.00
19.98
B


ATOM
4170
N
GLU
B
250
22.214
40.737
28.071
1.00
24.06
B


ATOM
4171
CA
GLU
B
250
22.811
41.935
28.670
1.00
25.90
B


ATOM
4172
CB
GLU
B
250
24.212
41.612
29.214
1.00
25.21
B


ATOM
4173
CG
GLU
B
250
24.940
42.790
29.890
1.00
31.63
B


ATOM
4174
CD
GLU
B
250
24.054
43.574
30.862
1.00
34.21
B


ATOM
4175
OE1
GLU
B
250
23.225
42.970
31.585
1.00
33.95
B


ATOM
4176
OE2
GLU
B
250
24.192
44.812
30.904
1.00
36.59
B


ATOM
4177
C
GLU
B
250
22.873
43.075
27.676
1.00
24.35
B


ATOM
4178
O
GLU
B
250
22.576
44.207
28.024
1.00
22.65
B


ATOM
4179
N
ILE
B
251
23.251
42.754
26.438
1.00
24.24
B


ATOM
4180
CA
ILE
B
251
23.317
43.732
25.366
1.00
25.38
B


ATOM
4181
CB
ILE
B
251
23.776
43.085
24.008
1.00
27.37
B


ATOM
4182
CG2
ILE
B
251
23.246
43.903
22.839
1.00
31.03
B


ATOM
4183
CG1
ILE
B
251
25.297
43.091
23.890
1.00
31.42
B


ATOM
4184
CD1
ILE
B
251
25.879
44.481
23.505
1.00
33.33
B


ATOM
4185
C
ILE
B
251
21.943
44.357
25.166
1.00
22.90
B


ATOM
4186
O
ILE
B
251
21.831
45.570
25.045
1.00
23.83
B


ATOM
4187
N
ASN
B
252
20.888
43.545
25.126
1.00
22.96
B


ATOM
4188
CA
ASN
B
252
19.551
44.101
24.929
1.00
21.88
B


ATOM
4189
CB
ASN
B
252
18.555
42.994
24.574
1.00
23.11
B


ATOM
4190
CG
ASN
B
252
18.746
42.468
23.147
1.00
23.37
B


ATOM
4191
OD1
ASN
B
252
18.661
43.224
22.170
1.00
19.39
B


ATOM
4192
ND2
ASN
B
252
19.013
41.169
23.031
1.00
23.05
B


ATOM
4193
C
ASN
B
252
19.033
44.901
26.133
1.00
21.84
B


ATOM
4194
O
ASN
B
252
18.172
45.765
25.985
1.00
23.05
B


ATOM
4195
N
ARG
B
253
19.543
44.614
27.320
1.00
21.04
B


ATOM
4196
CA
ARG
B
253
19.097
45.349
28.490
1.00
23.58
B


ATOM
4197
CB
ARG
B
253
19.489
44.605
29.779
1.00
24.48
B


ATOM
4198
CG
ARG
B
253
18.836
45.196
31.078
1.00
28.02
B


ATOM
4199
CD
ARG
B
253
19.427
44.592
32.357
1.00
28.97
B


ATOM
4200
NE
ARG
B
253
20.857
44.870
32.483
1.00
32.96
B


ATOM
4201
CZ
ARG
B
253
21.369
46.008
32.981
1.00
37.54
B


ATOM
4202
NH1
ARG
B
253
20.572
46.979
33.425
1.00
35.88
B


ATOM
4203
NH2
ARG
B
253
22.684
46.206
32.990
1.00
36.48
B


ATOM
4204
C
ARG
B
253
19.770
46.727
28.453
1.00
23.77
B


ATOM
4205
O
ARG
B
253
19.126
47.735
28.699
1.00
23.90
B


ATOM
4206
N
SER
B
254
21.061
46.728
28.105
1.00
25.94
B


ATOM
4207
CA
SER
B
254
21.941
47.912
28.049
1.00
29.19
B


ATOM
4208
CB
SER
B
254
23.372
47.469
28.310
1.00
30.04
B


ATOM
4209
OG
SER
B
254
23.418
46.694
29.487
1.00
39.65
B


ATOM
4210
C
SER
B
254
21.976
48.759
26.779
1.00
30.24
B


ATOM
4211
O
SER
B
254
22.292
49.941
26.828
1.00
30.50
B


ATOM
4212
N
VAL
B
255
21.704
48.161
25.629
1.00
29.60
B


ATOM
4213
CA
VAL
B
255
21.746
48.935
24.408
1.00
29.50
B


ATOM
4214
CB
VAL
B
255
22.986
48.578
23.585
1.00
29.07
B


ATOM
4215
CG1
VAL
B
255
23.126
49.537
22.403
1.00
31.55
B


ATOM
4216
CG2
VAL
B
255
24.221
48.628
24.464
1.00
30.70
B


ATOM
4217
C
VAL
B
255
20.509
48.685
23.577
1.00
31.57
B


ATOM
4218
O
VAL
B
255
20.288
47.575
23.100
1.00
31.11
B


ATOM
4219
N
LYS
B
256
19.697
49.718
23.405
1.00
32.36
B


ATOM
4220
CA
LYS
B
256
18.494
49.587
22.601
1.00
33.66
B


ATOM
4221
CB
LYS
B
256
17.462
50.610
23.075
1.00
34.92
B


ATOM
4222
CG
LYS
B
256
17.124
50.390
24.550
1.00
34.93
B


ATOM
4223
CD
LYS
B
256
16.657
48.940
24.760
1.00
33.36
B


ATOM
4224
CE
LYS
B
256
16.491
48.599
26.244
1.00
35.28
B


ATOM
4225
NZ
LYS
B
256
15.997
47.185
26.450
1.00
32.21
B


ATOM
4226
C
LYS
B
256
18.917
49.834
21.157
1.00
33.47
B


ATOM
4227
O
LYS
B
256
19.480
50.875
20.861
1.00
36.27
B


ATOM
4228
N
VAL
B
257
18.704
48.868
20.268
1.00
30.48
B


ATOM
4229
CA
VAL
B
257
19.101
49.064
18.874
1.00
27.66
B


ATOM
4230
CB
VAL
B
257
19.818
47.835
18.305
1.00
26.04
B


ATOM
4231
CG1
VAL
B
257
21.084
47.582
19.097
1.00
27.45
B


ATOM
4232
CG2
VAL
B
257
18.855
46.612
18.321
1.00
27.60
B


ATOM
4233
C
VAL
B
257
17.852
49.286
18.062
1.00
25.25
B


ATOM
4234
O
VAL
B
257
16.789
48.901
18.480
1.00
23.87
B


ATOM
4235
N
GLN
B
258
17.982
49.912
16.907
1.00
22.62
B


ATOM
4236
CA
GLN
B
258
16.818
50.116
16.049
1.00
26.35
B


ATOM
4237
CB
GLN
B
258
16.068
51.403
16.429
1.00
26.85
B


ATOM
4238
CG
GLN
B
258
14.861
51.743
15.554
1.00
29.53
B


ATOM
4239
CD
GLN
B
258
13.767
50.664
15.554
1.00
31.93
B


ATOM
4240
OE1
GLN
B
258
13.594
49.936
14.563
1.00
34.79
B


ATOM
4241
NE2
GLN
B
258
13.026
50.571
16.639
1.00
29.21
B


ATOM
4242
C
GLN
B
258
17.316
50.190
14.615
1.00
23.38
B


ATOM
4243
O
GLN
B
258
18.140
51.039
14.284
1.00
24.45
B


ATOM
4244
N
HIS
B
259
16.860
49.270
13.774
1.00
21.70
B


ATOM
4245
CA
HIS
B
259
17.290
49.302
12.372
1.00
22.97
B


ATOM
4246
CB
HIS
B
259
16.712
48.101
11.603
1.00
21.33
B


ATOM
4247
CG
HIS
B
259
17.203
47.992
10.202
1.00
23.30
B


ATOM
4248
CD2
HIS
B
259
18.065
47.120
9.623
1.00
25.91
B


ATOM
4249
ND1
HIS
B
259
16.830
48.882
9.210
1.00
24.60
B


ATOM
4250
CE1
HIS
B
259
17.445
48.560
8.081
1.00
25.30
B


ATOM
4251
NE2
HIS
B
259
18.199
47.493
8.303
1.00
26.11
B


ATOM
4252
C
HIS
B
259
16.714
50.636
11.859
1.00
23.12
B


ATOM
4253
O
HIS
B
259
15.514
50.878
11.966
1.00
22.20
B


ATOM
4254
N
PRO
B
260
17.562
51.518
11.301
1.00
24.86
B


ATOM
4255
CD
PRO
B
260
19.001
51.404
10.981
1.00
23.76
B


ATOM
4256
CA
PRO
B
260
17.005
52.789
10.831
1.00
27.33
B


ATOM
4257
CB
PRO
B
260
18.250
53.593
10.451
1.00
26.50
B


ATOM
4258
CG
PRO
B
260
19.216
52.535
9.965
1.00
23.82
B


ATOM
4259
C
PRO
B
260
15.954
52.743
9.720
1.00
31.96
B


ATOM
4260
O
PRO
B
260
15.220
53.712
9.522
1.00
32.79
B


ATOM
4261
N
GLN
B
261
15.851
51.651
8.978
1.00
31.37
B


ATOM
4262
CA
GLN
B
261
14.805
51.629
7.950
1.00
34.02
B


ATOM
4263
CB
GLN
B
261
15.430
51.512
6.562
1.00
36.14
B


ATOM
4264
CG
GLN
B
261
16.010
52.837
6.102
1.00
44.20
B


ATOM
4265
CD
GLN
B
261
17.510
52.805
5.906
1.00
48.07
B


ATOM
4266
OE1
GLN
B
261
18.277
52.353
6.773
1.00
50.80
B


ATOM
4267
NE2
GLN
B
261
17.946
53.296
4.755
1.00
51.92
B


ATOM
4268
C
GLN
B
261
13.714
50.570
8.135
1.00
33.51
B


ATOM
4269
O
GLN
B
261
12.715
50.587
7.423
1.00
33.58
B


ATOM
4270
N
LEU
B
262
13.902
49.652
9.092
1.00
31.68
B


ATOM
4271
CA
LEU
B
262
12.918
48.595
9.370
1.00
28.52
B


ATOM
4272
CB
LEU
B
262
13.514
47.210
9.076
1.00
26.54
B


ATOM
4273
CG
LEU
B
262
14.007
47.092
7.632
1.00
28.52
B


ATOM
4274
CD1
LEU
B
262
14.918
45.886
7.483
1.00
26.92
B


ATOM
4275
CD2
LEU
B
262
12.776
47.015
6.669
1.00
26.96
B


ATOM
4276
C
LEU
B
262
12.553
48.706
10.841
1.00
29.00
B


ATOM
4277
O
LEU
B
262
13.271
48.217
11.715
1.00
29.11
B


ATOM
4278
N
PRO
B
263
11.441
49.374
11.137
1.00
28.56
B


ATOM
4279
CD
PRO
B
263
10.544
50.044
10.177
1.00
30.84
B


ATOM
4280
CA
PRO
B
263
10.978
49.562
12.510
1.00
28.36
B


ATOM
4281
CB
PRO
B
263
9.627
50.237
12.325
1.00
29.82
B


ATOM
4282
CG
PRO
B
263
9.836
51.043
11.048
1.00
31.88
B


ATOM
4283
C
PRO
B
263
10.856
48.282
13.342
1.00
28.05
B


ATOM
4284
O
PRO
B
263
11.138
48.313
14.553
1.00
26.36
B


ATOM
4285
N
HIS
B
264
10.455
47.166
12.723
1.00
22.96
B


ATOM
4286
CA
HIS
B
264
10.273
45.926
13.503
1.00
23.58
B


ATOM
4287
CB
HIS
B
264
9.393
44.896
12.736
1.00
22.48
B


ATOM
4288
CG
HIS
B
264
10.043
44.328
11.502
1.00
25.10
B


ATOM
4289
CD2
HIS
B
264
10.634
43.126
11.278
1.00
23.98
B


ATOM
4290
ND1
HIS
B
264
10.206
45.055
10.339
1.00
20.42
B


ATOM
4291
CE1
HIS
B
264
10.878
44.332
9.460
1.00
23.47
B


ATOM
4292
NE2
HIS
B
264
11.150
43.157
10.005
1.00
23.28
B


ATOM
4293
C
HIS
B
264
11.567
45.248
13.989
1.00
21.78
B


ATOM
4294
O
HIS
B
264
11.516
44.331
14.813
1.00
21.79
B


ATOM
4295
N
ILE
B
265
12.730
45.653
13.484
1.00
20.77
B


ATOM
4296
CA
ILE
B
265
13.964
45.031
13.977
1.00
22.53
B


ATOM
4297
CB
ILE
B
265
14.962
44.760
12.837
1.00
21.59
B


ATOM
4298
CG2
ILE
B
265
16.121
43.895
13.380
1.00
20.60
B


ATOM
4299
CG1
ILE
B
265
14.230
44.032
11.680
1.00
23.48
B


ATOM
4300
CD1
ILE
B
265
15.114
43.682
10.468
1.00
23.27
B


ATOM
4301
C
ILE
B
265
14.552
45.978
15.024
1.00
24.24
B


ATOM
4302
O
ILE
B
265
15.095
47.052
14.708
1.00
22.60
B


ATOM
4303
N
ASN
B
266
14.406
45.585
16.284
1.00
26.26
B


ATOM
4304
CA
ASN
B
266
14.862
46.423
17.369
1.00
25.37
B


ATOM
4305
CB
ASN
B
266
13.697
47.307
17.814
1.00
28.78
B


ATOM
4306
CG
ASN
B
266
12.423
46.511
18.044
1.00
29.78
B


ATOM
4307
OD1
ASN
B
266
11.333
46.917
17.636
1.00
34.47
B


ATOM
4308
ND2
ASN
B
266
12.549
45.378
18.705
1.00
30.29
B


ATOM
4309
C
ASN
B
266
15.405
45.632
18.552
1.00
25.99
B


ATOM
4310
O
ASN
B
266
15.225
46.025
19.716
1.00
23.39
B


ATOM
4311
N
THR
B
267
16.053
44.508
18.262
1.00
23.46
B


ATOM
4312
CA
THR
B
267
16.663
43.682
19.319
1.00
20.83
B


ATOM
4313
CB
THR
B
267
15.712
42.555
19.814
1.00
22.37
B


ATOM
4314
OG1
THR
B
267
15.295
41.769
18.684
1.00
25.80
B


ATOM
4315
CG2
THR
B
267
14.473
43.123
20.507
1.00
20.88
B


ATOM
4316
C
THR
B
267
17.871
43.004
18.663
1.00
20.33
B


ATOM
4317
O
THR
B
267
17.905
42.832
17.426
1.00
19.55
B


ATOM
4318
N
VAL
B
268
18.873
42.673
19.468
1.00
18.62
B


ATOM
4319
CA
VAL
B
268
20.051
41.946
19.004
1.00
18.09
B


ATOM
4320
CB
VAL
B
268
21.300
42.304
19.846
1.00
17.35
B


ATOM
4321
CG1
VAL
B
268
22.463
41.417
19.462
1.00
13.08
B


ATOM
4322
CG2
VAL
B
268
21.636
43.771
19.668
1.00
16.71
B


ATOM
4323
C
VAL
B
268
19.650
40.457
19.241
1.00
19.11
B


ATOM
4324
O
VAL
B
268
19.415
40.028
20.385
1.00
17.09
B


ATOM
4325
N
ASP
B
269
19.549
39.687
18.160
1.00
17.98
B


ATOM
4326
CA
ASP
B
269
19.114
38.295
18.242
1.00
20.37
B


ATOM
4327
CB
ASP
B
269
18.050
38.012
17.163
1.00
23.09
B


ATOM
4328
CG
ASP
B
269
16.841
38.912
17.274
1.00
29.74
B


ATOM
4329
OD1
ASP
B
269
16.661
39.532
18.355
1.00
31.79
B


ATOM
4330
OD2
ASP
B
269
16.045
38.994
16.284
1.00
28.20
B


ATOM
4331
C
ASP
B
269
20.179
37.231
18.108
1.00
18.62
B


ATOM
4332
O
ASP
B
269
19.892
36.039
18.297
1.00
18.69
B


ATOM
4333
N
CYS
B
270
21.397
37.633
17.776
1.00
18.19
B


ATOM
4334
CA
CYS
B
270
22.468
36.670
17.568
1.00
16.63
B


ATOM
4335
CB
CYS
B
270
22.682
36.460
16.061
1.00
20.16
B


ATOM
4336
SG
CYS
B
270
21.149
36.098
15.141
1.00
21.54
B


ATOM
4337
C
CYS
B
270
23.783
37.140
18.143
1.00
17.57
B


ATOM
4338
O
CYS
B
270
24.080
38.338
18.129
1.00
17.58
B


ATOM
4339
N
VAL
B
271
24.573
36.196
18.640
1.00
16.48
B


ATOM
4340
CA
VAL
B
271
25.888
36.520
19.149
1.00
16.35
B


ATOM
4341
CB
VAL
B
271
26.021
36.250
20.650
1.00
15.70
B


ATOM
4342
CG1
VAL
B
271
27.469
36.437
21.075
1.00
15.92
B


ATOM
4343
CG2
VAL
B
271
25.132
37.261
21.417
1.00
15.00
B


ATOM
4344
C
VAL
B
271
26.875
35.690
18.382
1.00
16.93
B


ATOM
4345
O
VAL
B
271
26.752
34.468
18.300
1.00
16.84
B


ATOM
4346
N
GLU
B
272
27.853
36.381
17.810
1.00
18.81
B


ATOM
4347
CA
GLU
B
272
28.897
35.797
16.996
1.00
20.90
B


ATOM
4348
CB
GLU
B
272
29.005
36.617
15.703
1.00
21.15
B


ATOM
4349
CG
GLU
B
272
30.112
36.184
14.731
1.00
24.76
B


ATOM
4350
CD
GLU
B
272
30.067
36.995
13.429
1.00
26.53
B


ATOM
4351
OE1
GLU
B
272
28.950
37.366
13.016
1.00
25.44
B


ATOM
4352
OE2
GLU
B
272
31.129
37.252
12.819
1.00
28.19
B


ATOM
4353
C
GLU
B
272
30.224
35.821
17.769
1.00
23.58
B


ATOM
4354
O
GLU
B
272
30.779
36.892
18.040
1.00
22.03
B


ATOM
4355
N
ILE
B
273
30.713
34.642
18.135
1.00
23.04
B


ATOM
4356
CA
ILE
B
273
31.965
34.502
18.873
1.00
21.91
B


ATOM
4357
CB
ILE
B
273
31.777
33.437
19.986
1.00
23.57
B


ATOM
4358
CG2
ILE
B
273
33.066
33.291
20.802
1.00
19.24
B


ATOM
4359
CG1
ILE
B
273
30.580
33.836
20.843
1.00
18.64
B


ATOM
4360
CD1
ILE
B
273
30.153
32.848
21.878
1.00
19.58
B


ATOM
4361
C
ILE
B
273
33.009
34.056
17.837
1.00
23.92
B


ATOM
4362
O
ILE
B
273
32.866
33.003
17.218
1.00
22.57
B


ATOM
4363
N
TYR
B
274
34.041
34.862
17.610
1.00
23.93
B


ATOM
4364
CA
TYR
B
274
35.041
34.521
16.606
1.00
24.62
B


ATOM
4365
CB
TYR
B
274
35.054
35.572
15.502
1.00
25.85
B


ATOM
4366
CG
TYR
B
274
35.797
36.859
15.865
1.00
29.39
B


ATOM
4367
CD1
TYR
B
274
37.135
37.059
15.471
1.00
32.27
B


ATOM
4368
CE1
TYR
B
274
37.805
38.270
15.743
1.00
30.29
B


ATOM
4369
CD2
TYR
B
274
35.153
37.890
16.547
1.00
27.51
B


ATOM
4370
CE2
TYR
B
274
35.804
39.102
16.822
1.00
30.17
B


ATOM
4371
CZ
TYR
B
274
37.128
39.286
16.412
1.00
32.06
B


ATOM
4372
OH
TYR
B
274
37.750
40.500
16.628
1.00
34.51
B


ATOM
4373
C
TYR
B
274
36.444
34.365
17.161
1.00
25.89
B


ATOM
4374
O
TYR
B
274
36.741
34.779
18.280
1.00
27.89
B


ATOM
4375
N
GLY
B
275
37.290
33.742
16.360
1.00
27.45
B


ATOM
4376
CA
GLY
B
275
38.671
33.480
16.734
1.00
29.14
B


ATOM
4377
C
GLY
B
275
39.493
33.009
15.544
1.00
29.69
B


ATOM
4378
O
GLY
B
275
39.004
32.998
14.396
1.00
31.46
B


ATOM
4379
N
PRO
B
276
40.749
32.603
15.779
1.00
30.70
B


ATOM
4380
CD
PRO
B
276
41.391
32.636
17.104
1.00
30.52
B


ATOM
4381
CA
PRO
B
276
41.689
32.119
14.757
1.00
30.59
B


ATOM
4382
CB
PRO
B
276
42.913
31.695
15.571
1.00
30.54
B


ATOM
4383
CG
PRO
B
276
42.858
32.651
16.745
1.00
32.78
B


ATOM
4384
C
PRO
B
276
41.158
30.953
13.980
1.00
29.49
B


ATOM
4385
O
PRO
B
276
40.557
30.060
14.540
1.00
29.97
B


ATOM
4386
N
PRO
B
277
41.400
30.931
12.670
1.00
30.75
B


ATOM
4387
CD
PRO
B
277
42.077
31.968
11.866
1.00
29.65
B


ATOM
4388
CA
PRO
B
277
40.928
29.823
11.828
1.00
31.30
B


ATOM
4389
CB
PRO
B
277
41.189
30.333
10.419
1.00
31.23
B


ATOM
4390
CG
PRO
B
277
42.456
31.205
10.624
1.00
29.77
B


ATOM
4391
C
PRO
B
277
41.744
28.552
12.112
1.00
33.09
B


ATOM
4392
O
PRO
B
277
42.809
28.630
12.714
1.00
32.82
B


ATOM
4393
N
THR
B
278
41.216
27.389
11.735
1.00
31.19
B


ATOM
4394
CA
THR
B
278
41.957
26.152
11.879
1.00
33.37
B


ATOM
4395
CB
THR
B
278
41.140
25.032
12.514
1.00
33.50
B


ATOM
4396
OG1
THR
B
278
40.915
25.337
13.890
1.00
36.07
B


ATOM
4397
CG2
THR
B
278
41.895
23.694
12.403
1.00
34.08
B


ATOM
4398
C
THR
B
278
42.286
25.762
10.450
1.00
34.04
B


ATOM
4399
O
THR
B
278
43.367
25.249
10.155
1.00
36.70
B


ATOM
4400
N
ASN
B
279
41.345
26.001
9.550
1.00
33.97
B


ATOM
4401
CA
ASN
B
279
41.596
25.690
8.173
1.00
34.44
B


ATOM
4402
CB
ASN
B
279
40.302
25.586
7.392
1.00
36.17
B


ATOM
4403
CG
ASN
B
279
40.539
25.170
5.964
1.00
35.93
B


ATOM
4404
OD1
ASN
B
279
41.439
25.683
5.303
1.00
37.59
B


ATOM
4405
ND2
ASN
B
279
39.736
24.242
5.475
1.00
37.18
B


ATOM
4406
C
ASN
B
279
42.450
26.805
7.595
1.00
36.89
B


ATOM
4407
O
ASN
B
279
42.139
27.986
7.719
1.00
35.90
B


ATOM
4408
N
ALA
B
280
43.535
26.410
6.953
1.00
38.37
B


ATOM
4409
CA
ALA
B
280
44.456
27.350
6.366
1.00
38.17
B


ATOM
4410
CB
ALA
B
280
45.602
26.576
5.722
1.00
41.11
B


ATOM
4411
C
ALA
B
280
43.799
28.258
5.338
1.00
37.13
B


ATOM
4412
O
ALA
B
280
44.303
29.326
5.053
1.00
37.57
B


ATOM
4413
N
ALA
B
281
42.671
27.855
4.775
1.00
35.36
B


ATOM
4414
CA
ALA
B
281
42.053
28.702
3.765
1.00
33.49
B


ATOM
4415
CB
ALA
B
281
41.337
27.840
2.735
1.00
32.32
B


ATOM
4416
C
ALA
B
281
41.090
29.741
4.334
1.00
31.88
B


ATOM
4417
O
ALA
B
281
40.647
30.619
3.623
1.00
31.61
B


ATOM
4418
N
ALA
B
282
40.773
29.661
5.616
1.00
30.29
B


ATOM
4419
CA
ALA
B
282
39.836
30.613
6.191
1.00
29.41
B


ATOM
4420
CB
ALA
B
282
38.939
29.913
7.200
1.00
24.10
B


ATOM
4421
C
ALA
B
282
40.508
31.816
6.841
1.00
28.29
B


ATOM
4422
O
ALA
B
282
41.625
31.722
7.302
1.00
29.25
B


ATOM
4423
N
ASN
B
283
39.802
32.934
6.890
1.00
27.61
B


ATOM
4424
CA
ASN
B
283
40.329
34.141
7.523
1.00
29.10
B


ATOM
4425
CB
ASN
B
283
39.570
35.392
7.074
1.00
27.02
B


ATOM
4426
CG
ASN
B
283
39.837
35.744
5.650
1.00
30.78
B


ATOM
4427
OD1
ASN
B
283
40.515
36.732
5.347
1.00
32.73
B


ATOM
4428
ND2
ASN
B
283
39.310
34.940
4.749
1.00
29.57
B


ATOM
4429
C
ASN
B
283
40.144
34.001
9.018
1.00
28.49
B


ATOM
4430
O
ASN
B
283
41.035
34.350
9.778
1.00
27.23
B


ATOM
4431
N
TYR
B
284
38.970
33.503
9.419
1.00
28.27
B


ATOM
4432
CA
TYR
B
284
38.606
33.325
10.836
1.00
29.54
B


ATOM
4433
CB
TYR
B
284
37.879
34.580
11.383
1.00
30.63
B


ATOM
4434
CG
TYR
B
284
38.710
35.859
11.442
1.00
32.81
B


ATOM
4435
CD1
TYR
B
284
39.758
36.000
12.358
1.00
36.40
B


ATOM
4436
CE1
TYR
B
284
40.553
37.141
12.377
1.00
37.48
B


ATOM
4437
CD2
TYR
B
284
38.475
36.902
10.545
1.00
36.01
B


ATOM
4438
CE2
TYR
B
284
39.256
38.049
10.546
1.00
37.71
B


ATOM
4439
CZ
TYR
B
284
40.299
38.165
11.463
1.00
39.96
B


ATOM
4440
OH
TYR
B
284
41.094
39.302
11.440
1.00
41.93
B


ATOM
4441
C
TYR
B
284
37.659
32.143
11.010
1.00
28.79
B


ATOM
4442
O
TYR
B
284
37.183
31.562
10.032
1.00
27.79
B


ATOM
4443
N
LYS
B
285
37.383
31.812
12.265
1.00
26.45
B


ATOM
4444
CA
LYS
B
285
36.453
30.761
12.595
1.00
26.21
B


ATOM
4445
CB
LYS
B
285
37.177
29.612
13.291
1.00
27.59
B


ATOM
4446
CG
LYS
B
285
36.254
28.526
13.695
1.00
27.93
B


ATOM
4447
CD
LYS
B
285
36.844
27.558
14.733
1.00
33.21
B


ATOM
4448
CE
LYS
B
285
38.190
26.954
14.301
1.00
31.02
B


ATOM
4449
NZ
LYS
B
285
38.371
25.617
14.946
1.00
33.66
B


ATOM
4450
C
LYS
B
285
35.425
31.388
13.540
1.00
27.15
B


ATOM
4451
O
LYS
B
285
35.728
32.357
14.242
1.00
28.11
B


ATOM
4452
N
ASN
B
286
34.193
30.903
13.539
1.00
24.35
B


ATOM
4453
CA
ASN
B
286
33.224
31.474
14.458
1.00
24.30
B


ATOM
4454
CB
ASN
B
286
32.550
32.744
13.875
1.00
21.64
B


ATOM
4455
CG
ASN
B
286
31.381
32.421
12.901
1.00
26.71
B


ATOM
4456
OD1
ASN
B
286
31.590
32.106
11.720
1.00
26.63
B


ATOM
4457
ND2
ASN
B
286
30.163
32.481
13.403
1.00
24.63
B


ATOM
4458
C
ASN
B
286
32.134
30.488
14.801
1.00
22.31
B


ATOM
4459
O
ASN
B
286
31.977
29.465
14.121
1.00
21.10
B


ATOM
4460
N
VAL
B
287
31.409
30.792
15.876
1.00
20.11
B


ATOM
4461
CA
VAL
B
287
30.218
30.039
16.231
1.00
18.93
B


ATOM
4462
CB
VAL
B
287
30.459
29.019
17.352
1.00
21.57
B


ATOM
4463
CG1
VAL
B
287
30.971
29.703
18.605
1.00
19.17
B


ATOM
4464
CG2
VAL
B
287
29.161
28.302
17.643
1.00
19.46
B


ATOM
4465
C
VAL
B
287
29.187
31.117
16.619
1.00
20.42
B


ATOM
4466
O
VAL
B
287
29.492
32.061
17.336
1.00
18.29
B


ATOM
4467
N
VAL
B
288
27.973
31.026
16.087
1.00
20.78
B


ATOM
4468
CA
VAL
B
288
26.943
32.022
16.389
1.00
15.95
B


ATOM
4469
CB
VAL
B
288
26.265
32.488
15.063
1.00
15.19
B


ATOM
4470
CG1
VAL
B
288
24.908
33.215
15.353
1.00
14.49
B


ATOM
4471
CG2
VAL
B
288
27.210
33.414
14.276
1.00
11.34
B


ATOM
4472
C
VAL
B
288
25.925
31.362
17.320
1.00
16.29
B


ATOM
4473
O
VAL
B
288
25.488
30.260
17.049
1.00
20.46
B


ATOM
4474
N
ILE
B
289
25.575
32.027
18.418
1.00
14.70
B


ATOM
4475
CA
ILE
B
289
24.622
31.523
19.401
1.00
16.01
B


ATOM
4476
CB
ILE
B
289
25.124
31.740
20.858
1.00
16.66
B


ATOM
4477
CG2
ILE
B
289
24.130
31.086
21.862
1.00
14.71
B


ATOM
4478
CG1
ILE
B
289
26.514
31.130
21.020
1.00
17.58
B


ATOM
4479
CD1
ILE
B
289
26.624
29.695
20.447
1.00
20.06
B


ATOM
4480
C
ILE
B
289
23.355
32.320
19.227
1.00
15.77
B


ATOM
4481
O
ILE
B
289
23.414
33.560
19.222
1.00
15.29
B


ATOM
4482
N
PHE
B
290
22.209
31.636
19.133
1.00
13.94
B


ATOM
4483
CA
PHE
B
290
20.953
32.339
18.883
1.00
14.57
B


ATOM
4484
CB
PHE
B
290
20.832
32.622
17.385
1.00
13.60
B


ATOM
4485
CG
PHE
B
290
20.684
31.345
16.517
1.00
15.09
B


ATOM
4486
CD1
PHE
B
290
19.419
30.964
16.004
1.00
14.57
B


ATOM
4487
CD2
PHE
B
290
21.790
30.558
16.210
1.00
15.36
B


ATOM
4488
CE1
PHE
B
290
19.278
29.822
15.197
1.00
12.71
B


ATOM
4489
CE2
PHE
B
290
21.662
29.374
15.390
1.00
17.26
B


ATOM
4490
CZ
PHE
B
290
20.400
29.021
14.890
1.00
13.79
B


ATOM
4491
C
PHE
B
290
19.821
31.438
19.307
1.00
16.95
B


ATOM
4492
O
PHE
B
290
20.076
30.362
19.843
1.00
17.81
B


ATOM
4493
N
GLY
B
291
18.583
31.842
19.020
1.00
16.05
B


ATOM
4494
CA
GLY
B
291
17.441
31.007
19.389
1.00
17.59
B


ATOM
4495
C
GLY
B
291
17.411
30.764
20.908
1.00
18.74
B


ATOM
4496
O
GLY
B
291
17.616
31.711
21.656
1.00
16.99
B


ATOM
4497
N
ASN
B
292
17.102
29.541
21.364
1.00
18.13
B


ATOM
4498
CA
ASN
B
292
17.126
29.239
22.813
1.00
18.85
B


ATOM
4499
CB
ASN
B
292
16.106
28.147
23.151
1.00
20.25
B


ATOM
4500
CG
ASN
B
292
16.003
27.892
24.639
1.00
23.65
B


ATOM
4501
OD1
ASN
B
292
16.456
28.726
25.429
1.00
19.04
B


ATOM
4502
ND2
ASN
B
292
15.399
26.740
25.036
1.00
19.43
B


ATOM
4503
C
ASN
B
292
18.571
28.751
23.007
1.00
17.43
B


ATOM
4504
O
ASN
B
292
18.849
27.568
23.273
1.00
18.97
B


ATOM
4505
N
ARG
B
293
19.483
29.697
22.844
1.00
15.39
B


ATOM
4506
CA
ARG
B
293
20.920
29.435
22.864
1.00
18.63
B


ATOM
4507
CB
ARG
B
293
21.537
29.478
24.297
1.00
16.99
B


ATOM
4508
CG
ARG
B
293
21.250
28.373
25.269
1.00
19.89
B


ATOM
4509
CD
ARG
B
293
21.912
28.746
26.662
1.00
20.37
B


ATOM
4510
NE
ARG
B
293
21.883
27.627
27.595
1.00
20.93
B


ATOM
4511
CZ
ARG
B
293
20.806
27.213
28.249
1.00
19.26
B


ATOM
4512
NH1
ARG
B
293
19.651
27.841
28.095
1.00
18.57
B


ATOM
4513
NH2
ARG
B
293
20.882
26.132
29.024
1.00
18.49
B


ATOM
4514
C
ARG
B
293
21.356
28.178
22.099
1.00
20.83
B


ATOM
4515
O
ARG
B
293
22.162
27.365
22.588
1.00
20.39
B


ATOM
4516
N
GLN
B
294
20.823
28.013
20.875
1.00
18.85
B


ATOM
4517
CA
GLN
B
294
21.277
26.896
20.049
1.00
15.16
B


ATOM
4518
CB
GLN
B
294
20.224
26.499
18.987
1.00
14.87
B


ATOM
4519
CG
GLN
B
294
19.803
27.618
18.021
1.00
12.74
B


ATOM
4520
CD
GLN
B
294
18.544
27.222
17.208
1.00
12.47
B


ATOM
4521
OE1
GLN
B
294
17.409
27.581
17.567
1.00
13.63
B


ATOM
4522
NE2
GLN
B
294
18.760
26.437
16.137
1.00
9.14
B


ATOM
4523
C
GLN
B
294
22.513
27.483
19.381
1.00
15.29
B


ATOM
4524
O
GLN
B
294
22.750
28.697
19.480
1.00
15.53
B


ATOM
4525
N
ALA
B
295
23.280
26.654
18.679
1.00
14.85
B


ATOM
4526
CA
ALA
B
295
24.494
27.107
18.021
1.00
17.36
B


ATOM
4527
CB
ALA
B
295
25.716
26.422
18.646
1.00
14.59
B


ATOM
4528
C
ALA
B
295
24.421
26.727
16.544
1.00
20.27
B


ATOM
4529
O
ALA
B
295
23.930
25.635
16.203
1.00
19.23
B


ATOM
4530
N
ASP
B
296
24.928
27.616
15.688
1.00
18.98
B


ATOM
4531
CA
ASP
B
296
24.971
27.376
14.246
1.00
18.23
B


ATOM
4532
CB
ASP
B
296
25.088
28.704
13.519
1.00
20.79
B


ATOM
4533
CG
ASP
B
296
24.908
28.578
12.007
1.00
24.56
B


ATOM
4534
OD1
ASP
B
296
24.737
27.449
11.464
1.00
25.61
B


ATOM
4535
OD2
ASP
B
296
24.934
29.638
11.357
1.00
26.22
B


ATOM
4536
C
ASP
B
296
26.195
26.499
13.936
1.00
17.14
B


ATOM
4537
O
ASP
B
296
27.300
26.770
14.387
1.00
17.35
B


ATOM
4538
N
ARG
B
297
25.968
25.421
13.201
1.00
17.43
B


ATOM
4539
CA
ARG
B
297
27.036
24.507
12.807
1.00
17.91
B


ATOM
4540
CB
ARG
B
297
26.479
23.082
12.536
1.00
17.11
B


ATOM
4541
CG
ARG
B
297
26.036
22.327
13.809
1.00
18.89
B


ATOM
4542
CD
ARG
B
297
24.594
22.590
14.265
1.00
20.24
B


ATOM
4543
NE
ARG
B
297
24.264
21.627
15.320
1.00
21.67
B


ATOM
4544
CZ
ARG
B
297
24.447
21.827
16.630
1.00
21.96
B


ATOM
4545
NH1
ARG
B
297
24.927
22.981
17.097
1.00
19.62
B


ATOM
4546
NH2
ARG
B
297
24.206
20.844
17.487
1.00
17.20
B


ATOM
4547
C
ARG
B
297
27.705
25.036
11.552
1.00
18.71
B


ATOM
4548
O
ARG
B
297
28.846
24.639
11.258
1.00
20.92
B


ATOM
4549
N
SER
B
298
26.986
25.902
10.806
1.00
17.13
B


ATOM
4550
CA
SER
B
298
27.507
26.520
9.578
1.00
17.99
B


ATOM
4551
CB
SER
B
298
26.374
26.921
8.612
1.00
18.97
B


ATOM
4552
OG
SER
B
298
25.818
28.216
8.936
1.00
19.93
B


ATOM
4553
C
SER
B
298
28.226
27.793
10.022
1.00
17.47
B


ATOM
4554
O
SER
B
298
28.109
28.183
11.168
1.00
18.59
B


ATOM
4555
N
PRO
B
299
28.997
28.437
9.128
1.00
17.66
B


ATOM
4556
CD
PRO
B
299
29.469
27.971
7.815
1.00
17.65
B


ATOM
4557
CA
PRO
B
299
29.692
29.666
9.556
1.00
18.49
B


ATOM
4558
CB
PRO
B
299
30.693
29.943
8.425
1.00
18.69
B


ATOM
4559
CG
PRO
B
299
30.909
28.547
7.776
1.00
18.31
B


ATOM
4560
C
PRO
B
299
28.725
30.830
9.781
1.00
19.81
B


ATOM
4561
O
PRO
B
299
29.138
31.853
10.306
1.00
23.79
B


ATOM
4562
N
CYS
B
300
27.452
30.668
9.389
1.00
19.74
B


ATOM
4563
CA
CYS
B
300
26.378
31.686
9.549
1.00
17.92
B


ATOM
4564
CB
CYS
B
300
26.418
32.318
10.959
1.00
21.70
B


ATOM
4565
SG
CYS
B
300
24.928
33.340
11.375
1.00
21.58
B


ATOM
4566
C
CYS
B
300
26.468
32.784
8.484
1.00
20.18
B


ATOM
4567
O
CYS
B
300
27.385
33.625
8.479
1.00
21.88
B


ATOM
4568
N
GLY
B
301
25.497
32.794
7.586
1.00
17.72
B


ATOM
4569
CA
GLY
B
301
25.521
33.761
6.504
1.00
19.12
B


ATOM
4570
C
GLY
B
301
25.235
35.192
6.909
1.00
19.66
B


ATOM
4571
O
GLY
B
301
25.846
36.105
6.364
1.00
20.82
B


ATOM
4572
N
THR
B
302
24.282
35.422
7.808
1.00
18.67
B


ATOM
4573
CA
THR
B
302
24.038
36.803
8.232
1.00
18.51
B


ATOM
4574
CB
THR
B
302
22.684
36.998
8.998
1.00
16.35
B


ATOM
4575
OG1
THR
B
302
22.559
36.037
10.043
1.00
16.80
B


ATOM
4576
CG2
THR
B
302
21.510
36.861
8.061
1.00
19.01
B


ATOM
4577
C
THR
B
302
25.220
37.241
9.129
1.00
18.62
B


ATOM
4578
O
THR
B
302
25.599
38.413
9.121
1.00
19.41
B


ATOM
4579
N
GLY
B
303
25.810
36.300
9.863
1.00
18.02
B


ATOM
4580
CA
GLY
B
303
26.950
36.606
10.734
1.00
20.18
B


ATOM
4581
C
GLY
B
303
28.174
36.981
9.908
1.00
23.29
B


ATOM
4582
O
GLY
B
303
28.927
37.888
10.274
1.00
22.50
B


ATOM
4583
N
THR
B
304
28.377
36.287
8.787
1.00
20.83
B


ATOM
4584
CA
THR
B
304
29.480
36.617
7.889
1.00
20.55
B


ATOM
4585
CB
THR
B
304
29.583
35.540
6.756
1.00
19.71
B


ATOM
4586
OG1
THR
B
304
29.811
34.262
7.355
1.00
18.24
B


ATOM
4587
CG2
THR
B
304
30.732
35.826
5.799
1.00
15.10
B


ATOM
4588
C
THR
B
304
29.209
38.039
7.296
1.00
22.24
B


ATOM
4589
O
THR
B
304
30.106
38.890
7.247
1.00
22.60
B


ATOM
4590
N
SER
B
305
27.972
38.319
6.884
1.00
22.31
B


ATOM
4591
CA
SER
B
305
27.669
39.641
6.319
1.00
23.06
B


ATOM
4592
CB
SER
B
305
26.201
39.803
5.958
1.00
21.16
B


ATOM
4593
OG
SER
B
305
25.815
38.801
5.058
1.00
28.01
B


ATOM
4594
C
SER
B
305
27.984
40.660
7.385
1.00
23.82
B


ATOM
4595
O
SER
B
305
28.637
41.650
7.118
1.00
24.28
B


ATOM
4596
N
ALA
B
306
27.490
40.426
8.595
1.00
22.72
B


ATOM
4597
CA
ALA
B
306
27.771
41.342
9.704
1.00
22.21
B


ATOM
4598
CB
ALA
B
306
27.052
40.841
11.005
1.00
19.38
B


ATOM
4599
C
ALA
B
306
29.284
41.504
9.957
1.00
21.86
B


ATOM
4600
O
ALA
B
306
29.799
42.612
10.174
1.00
20.95
B


ATOM
4601
N
LYS
B
307
30.004
40.403
9.952
1.00
21.22
B


ATOM
4602
CA
LYS
B
307
31.437
40.464
10.194
1.00
21.77
B


ATOM
4603
CB
LYS
B
307
31.984
39.039
10.279
1.00
19.90
B


ATOM
4604
CG
LYS
B
307
33.489
38.930
10.355
1.00
24.69
B


ATOM
4605
CD
LYS
B
307
34.023
39.346
11.723
1.00
27.38
B


ATOM
4606
CE
LYS
B
307
35.505
39.124
11.838
1.00
26.03
B


ATOM
4607
NZ
LYS
B
307
35.885
39.513
13.235
1.00
32.57
B


ATOM
4608
C
LYS
B
307
32.120
41.235
9.048
1.00
24.17
B


ATOM
4609
O
LYS
B
307
33.008
42.077
9.290
1.00
24.25
B


ATOM
4610
N
MET
B
308
31.691
40.986
7.800
1.00
22.18
B


ATOM
4611
CA
MET
B
308
32.324
41.690
6.675
1.00
22.84
B


ATOM
4612
CB
MET
B
308
31.918
41.109
5.304
1.00
20.43
B


ATOM
4613
CG
MET
B
308
32.532
39.721
5.037
1.00
21.75
B


ATOM
4614
SD
MET
B
308
32.164
39.133
3.379
1.00
31.01
B


ATOM
4615
CE
MET
B
308
30.453
39.025
3.438
1.00
20.19
B


ATOM
4616
C
MET
B
308
32.013
43.174
6.700
1.00
23.26
B


ATOM
4617
O
MET
B
308
32.856
43.971
6.305
1.00
20.96
B


ATOM
4618
N
ALA
B
309
30.807
43.543
7.146
1.00
22.55
B


ATOM
4619
CA
ALA
B
309
30.454
44.972
7.216
1.00
23.95
B


ATOM
4620
CB
ALA
B
309
29.019
45.157
7.573
1.00
21.81
B


ATOM
4621
C
ALA
B
309
31.328
45.648
8.258
1.00
24.65
B


ATOM
4622
O
ALA
B
309
31.773
46.781
8.047
1.00
25.05
B


ATOM
4623
N
THR
B
310
31.565
44.953
9.370
1.00
23.33
B


ATOM
4624
CA
THR
B
310
32.419
45.462
10.444
1.00
23.58
B


ATOM
4625
CB
THR
B
310
32.398
44.507
11.656
1.00
22.56
B


ATOM
4626
OG1
THR
B
310
31.054
44.427
12.126
1.00
23.56
B


ATOM
4627
CG2
THR
B
310
33.309
45.019
12.824
1.00
21.09
B


ATOM
4628
C
THR
B
310
33.862
45.654
9.947
1.00
23.79
B


ATOM
4629
O
THR
B
310
34.407
46.743
10.042
1.00
24.36
B


ATOM
4630
N
LEU
B
311
34.492
44.595
9.445
1.00
25.69
B


ATOM
4631
CA
LEU
B
311
35.852
44.704
8.918
1.00
24.81
B


ATOM
4632
CB
LEU
B
311
36.273
43.384
8.294
1.00
24.27
B


ATOM
4633
CG
LEU
B
311
36.558
42.204
9.218
1.00
26.60
B


ATOM
4634
CD1
LEU
B
311
36.706
40.935
8.362
1.00
23.71
B


ATOM
4635
CD2
LEU
B
311
37.839
42.476
10.032
1.00
23.33
B


ATOM
4636
C
LEU
B
311
35.966
45.814
7.848
1.00
26.76
B


ATOM
4637
O
LEU
B
311
36.949
46.571
7.801
1.00
25.18
B


ATOM
4638
N
TYR
B
312
34.966
45.888
6.974
1.00
27.78
B


ATOM
4639
CA
TYR
B
312
34.931
46.884
5.896
1.00
28.94
B


ATOM
4640
CB
TYR
B
312
33.673
46.694
5.042
1.00
29.61
B


ATOM
4641
CG
TYR
B
312
33.660
47.576
3.827
1.00
32.01
B


ATOM
4642
CD1
TYR
B
312
34.315
47.182
2.671
1.00
33.32
B


ATOM
4643
CE1
TYR
B
312
34.396
48.004
1.581
1.00
34.26
B


ATOM
4644
CD2
TYR
B
312
33.070
48.830
3.855
1.00
32.13
B


ATOM
4645
CE2
TYR
B
312
33.142
49.676
2.757
1.00
33.45
B


ATOM
4646
CZ
TYR
B
312
33.816
49.249
1.620
1.00
35.84
B


ATOM
4647
OH
TYR
B
312
33.947
50.059
0.515
1.00
31.99
B


ATOM
4648
C
TYR
B
312
34.915
48.299
6.470
1.00
28.47
B


ATOM
4649
O
TYR
B
312
35.602
49.200
5.975
1.00
27.06
B


ATOM
4650
N
ALA
B
313
34.088
48.507
7.487
1.00
26.53
B


ATOM
4651
CA
ALA
B
313
34.005
49.826
8.113
1.00
30.02
B


ATOM
4652
CB
ALA
B
313
32.928
49.836
9.231
1.00
28.00
B


ATOM
4653
C
ALA
B
313
35.373
50.187
8.703
1.00
30.88
B


ATOM
4654
O
ALA
B
313
35.748
51.349
8.722
1.00
30.75
B


ATOM
4655
N
LYS
B
314
36.123
49.182
9.158
1.00
30.56
B


ATOM
4656
CA
LYS
B
314
37.417
49.434
9.744
1.00
31.37
B


ATOM
4657
CB
LYS
B
314
37.714
48.390
10.818
1.00
32.57
B


ATOM
4658
CG
LYS
B
314
36.762
48.467
11.986
1.00
31.09
B


ATOM
4659
CD
LYS
B
314
37.033
47.413
13.046
1.00
30.45
B


ATOM
4660
CE
LYS
B
314
35.925
47.495
14.123
1.00
32.33
B


ATOM
4661
NZ
LYS
B
314
36.157
46.592
15.258
1.00
35.69
B


ATOM
4662
C
LYS
B
314
38.541
49.452
8.730
1.00
31.96
B


ATOM
4663
O
LYS
B
314
39.689
49.586
9.104
1.00
34.08
B


ATOM
4664
N
GLY
B
315
38.223
49.315
7.450
1.00
31.60
B


ATOM
4665
CA
GLY
B
315
39.271
49.320
6.447
1.00
31.25
B


ATOM
4666
C
GLY
B
315
40.020
48.000
6.331
1.00
32.58
B


ATOM
4667
O
GLY
B
315
41.077
47.977
5.715
1.00
32.33
B


ATOM
4668
N
GLN
B
316
39.502
46.905
6.901
1.00
32.50
B


ATOM
4669
CA
GLN
B
316
40.196
45.608
6.838
1.00
32.70
B


ATOM
4670
CB
GLN
B
316
39.925
44.730
8.045
1.00
36.50
B


ATOM
4671
CG
GLN
B
316
39.383
45.414
9.219
1.00
43.19
B


ATOM
4672
CD
GLN
B
316
40.502
45.899
10.014
1.00
46.21
B


ATOM
4673
OE1
GLN
B
316
41.420
46.504
9.456
1.00
49.89
B


ATOM
4674
NE2
GLN
B
316
40.477
45.641
11.321
1.00
45.38
B


ATOM
4675
C
GLN
B
316
39.771
44.739
5.698
1.00
30.10
B


ATOM
4676
O
GLN
B
316
40.277
43.643
5.567
1.00
29.81
B


ATOM
4677
N
LEU
B
317
38.819
45.174
4.902
1.00
29.16
B


ATOM
4678
CA
LEU
B
317
38.352
44.303
3.834
1.00
29.99
B


ATOM
4679
CB
LEU
B
317
37.156
43.466
4.317
1.00
29.43
B


ATOM
4680
CG
LEU
B
317
36.524
42.472
3.354
1.00
32.12
B


ATOM
4681
CD1
LEU
B
317
37.594
41.410
2.967
1.00
30.14
B


ATOM
4682
CD2
LEU
B
317
35.274
41.840
4.029
1.00
29.54
B


ATOM
4683
C
LEU
B
317
37.935
45.202
2.737
1.00
28.56
B


ATOM
4684
O
LEU
B
317
37.328
46.243
3.009
1.00
26.57
B


ATOM
4685
N
ARG
B
318
38.253
44.834
1.496
1.00
26.91
B


ATOM
4686
CA
ARG
B
318
37.872
45.720
0.417
1.00
26.64
B


ATOM
4687
CB
ARG
B
318
39.134
46.180
−0.344
1.00
32.04
B


ATOM
4688
CG
ARG
B
318
40.001
45.085
−0.921
1.00
38.25
B


ATOM
4689
CD
ARG
B
318
41.522
45.382
−0.805
1.00
43.23
B


ATOM
4690
NE
ARG
B
318
41.918
46.658
−1.414
1.00
45.64
B


ATOM
4691
CZ
ARG
B
318
43.134
47.185
−1.302
1.00
42.17
B


ATOM
4692
NH1
ARG
B
318
44.060
46.534
−0.624
1.00
44.82
B


ATOM
4693
NH2
ARG
B
318
43.408
48.377
−1.813
1.00
39.98
B


ATOM
4694
C
ARG
B
318
36.830
45.116
−0.494
1.00
26.71
B


ATOM
4695
O
ARG
B
318
36.567
43.915
−0.457
1.00
25.62
B


ATOM
4696
N
ILE
B
319
36.196
45.954
−1.285
1.00
25.30
B


ATOM
4697
CA
ILE
B
319
35.205
45.462
−2.200
1.00
26.04
B


ATOM
4698
CB
ILE
B
319
34.666
46.601
−3.063
1.00
27.65
B


ATOM
4699
CG2
ILE
B
319
33.928
46.042
−4.275
1.00
26.56
B


ATOM
4700
CG1
ILE
B
319
33.730
47.474
−2.228
1.00
29.26
B


ATOM
4701
CD1
ILE
B
319
33.125
48.635
−2.992
1.00
29.86
B


ATOM
4702
C
ILE
B
319
35.824
44.396
−3.088
1.00
26.25
B


ATOM
4703
O
ILE
B
319
36.952
44.545
−3.541
1.00
25.57
B


ATOM
4704
N
GLY
B
320
35.100
43.308
−3.311
1.00
24.57
B


ATOM
4705
CA
GLY
B
320
35.588
42.251
−4.179
1.00
24.17
B


ATOM
4706
C
GLY
B
320
36.583
41.265
−3.617
1.00
24.87
B


ATOM
4707
O
GLY
B
320
36.854
40.257
−4.243
1.00
24.14
B


ATOM
4708
N
GLU
B
321
37.132
41.547
−2.444
1.00
26.10
B


ATOM
4709
CA
GLU
B
321
38.092
40.660
−1.813
1.00
28.59
B


ATOM
4710
CB
GLU
B
321
38.823
41.434
−0.708
1.00
28.42
B


ATOM
4711
CG
GLU
B
321
39.815
40.640
0.090
1.00
32.87
B


ATOM
4712
CD
GLU
B
321
40.566
41.497
1.123
1.00
35.36
B


ATOM
4713
OE1
GLU
B
321
41.328
40.914
1.926
1.00
33.16
B


ATOM
4714
OE2
GLU
B
321
40.404
42.750
1.120
1.00
36.41
B


ATOM
4715
C
GLU
B
321
37.337
39.439
−1.234
1.00
30.34
B


ATOM
4716
O
GLU
B
321
36.265
39.588
−0.637
1.00
30.59
B


ATOM
4717
N
THR
B
322
37.882
38.237
−1.406
1.00
28.71
B


ATOM
4718
CA
THR
B
322
37.197
37.072
−0.870
1.00
29.64
B


ATOM
4719
CB
THR
B
322
37.495
35.789
−1.676
1.00
29.32
B


ATOM
4720
OG1
THR
B
322
37.031
35.976
−3.019
1.00
27.57
B


ATOM
4721
CG2
THR
B
322
36.720
34.626
−1.097
1.00
29.40
B


ATOM
4722
C
THR
B
322
37.550
36.840
0.582
1.00
27.88
B


ATOM
4723
O
THR
B
322
38.706
36.779
0.924
1.00
30.49
B


ATOM
4724
N
PHE
B
323
36.519
36.751
1.419
1.00
27.87
B


ATOM
4725
CA
PHE
B
323
36.630
36.509
2.863
1.00
24.68
B


ATOM
4726
CB
PHE
B
323
35.765
37.535
3.596
1.00
23.96
B


ATOM
4727
CG
PHE
B
323
35.765
37.373
5.081
1.00
23.54
B


ATOM
4728
CD1
PHE
B
323
36.865
37.767
5.842
1.00
21.76
B


ATOM
4729
CD2
PHE
B
323
34.670
36.788
5.724
1.00
23.45
B


ATOM
4730
CE1
PHE
B
323
36.877
37.579
7.227
1.00
22.68
B


ATOM
4731
CE2
PHE
B
323
34.681
36.596
7.116
1.00
25.05
B


ATOM
4732
CZ
PHE
B
323
35.782
36.990
7.865
1.00
22.57
B


ATOM
4733
C
PHE
B
323
36.100
35.094
3.111
1.00
22.82
B


ATOM
4734
O
PHE
B
323
35.036
34.748
2.648
1.00
23.15
B


ATOM
4735
N
VAL
B
324
36.821
34.278
3.861
1.00
24.13
B


ATOM
4736
CA
VAL
B
324
36.385
32.908
4.071
1.00
22.59
B


ATOM
4737
CB
VAL
B
324
37.479
31.920
3.522
1.00
24.16
B


ATOM
4738
CG1
VAL
B
324
37.079
30.469
3.767
1.00
19.93
B


ATOM
4739
CG2
VAL
B
324
37.667
32.152
2.014
1.00
23.03
B


ATOM
4740
C
VAL
B
324
36.183
32.734
5.564
1.00
23.70
B


ATOM
4741
O
VAL
B
324
37.088
32.981
6.326
1.00
25.46
B


ATOM
4742
N
TYR
B
325
35.007
32.280
5.979
1.00
22.02
B


ATOM
4743
CA
TYR
B
325
34.716
32.129
7.397
1.00
21.09
B


ATOM
4744
CB
TYR
B
325
33.427
32.887
7.724
1.00
21.65
B


ATOM
4745
CG
TYR
B
325
33.431
33.662
9.026
1.00
21.19
B


ATOM
4746
CD1
TYR
B
325
34.496
33.567
9.924
1.00
22.48
B


ATOM
4747
CE1
TYR
B
325
34.516
34.294
11.111
1.00
23.13
B


ATOM
4748
CD2
TYR
B
325
32.361
34.508
9.355
1.00
23.18
B


ATOM
4749
CE2
TYR
B
325
32.361
35.257
10.548
1.00
23.80
B


ATOM
4750
CZ
TYR
B
325
33.461
35.141
11.422
1.00
26.04
B


ATOM
4751
OH
TYR
B
325
33.530
35.908
12.569
1.00
24.25
B


ATOM
4752
C
TYR
B
325
34.523
30.641
7.691
1.00
22.00
B


ATOM
4753
O
TYR
B
325
33.797
29.956
6.953
1.00
18.26
B


ATOM
4754
N
GLU
B
326
35.156
30.160
8.762
1.00
19.41
B


ATOM
4755
CA
GLU
B
326
35.066
28.756
9.139
1.00
20.68
B


ATOM
4756
CB
GLU
B
326
36.469
28.221
9.467
1.00
20.27
B


ATOM
4757
CG
GLU
B
326
36.551
26.727
9.712
1.00
23.54
B


ATOM
4758
CD
GLU
B
326
37.935
26.272
10.251
1.00
27.42
B


ATOM
4759
OE1
GLU
B
326
38.892
27.083
10.273
1.00
25.47
B


ATOM
4760
OE2
GLU
B
326
38.069
25.087
10.641
1.00
29.39
B


ATOM
4761
C
GLU
B
326
34.143
28.574
10.338
1.00
21.06
B


ATOM
4762
O
GLU
B
326
34.138
29.418
11.234
1.00
20.32
B


ATOM
4763
N
SER
B
327
33.363
27.481
10.363
1.00
21.23
B


ATOM
4764
CA
SER
B
327
32.449
27.188
11.488
1.00
21.35
B


ATOM
4765
CB
SER
B
327
31.173
26.465
11.007
1.00
19.86
B


ATOM
4766
OG
SER
B
327
31.467
25.105
10.662
1.00
24.82
B


ATOM
4767
C
SER
B
327
33.166
26.278
12.499
1.00
23.23
B


ATOM
4768
O
SER
B
327
34.269
25.817
12.251
1.00
23.74
B


ATOM
4769
N
ILE
B
328
32.514
26.020
13.627
1.00
24.81
B


ATOM
4770
CA
ILE
B
328
33.054
25.160
14.655
1.00
26.71
B


ATOM
4771
CB
ILE
B
328
32.108
25.170
15.877
1.00
28.57
B


ATOM
4772
CG2
ILE
B
328
30.790
24.456
15.539
1.00
25.55
B


ATOM
4773
CG1
ILE
B
328
32.791
24.519
17.076
1.00
30.14
B


ATOM
4774
CD1
ILE
B
328
32.015
24.681
18.380
1.00
31.36
B


ATOM
4775
C
ILE
B
328
33.218
23.722
14.123
1.00
30.18
B


ATOM
4776
O
ILE
B
328
33.957
22.916
14.703
1.00
29.50
B


ATOM
4777
N
LEU
B
329
32.530
23.402
13.018
1.00
28.53
B


ATOM
4778
CA
LEU
B
329
32.596
22.063
12.420
1.00
27.58
B


ATOM
4779
CB
LEU
B
329
31.250
21.698
11.784
1.00
28.35
B


ATOM
4780
CG
LEU
B
329
30.375
20.622
12.390
1.00
31.33
B


ATOM
4781
CD1
LEU
B
329
30.326
20.831
13.880
1.00
33.26
B


ATOM
4782
CD2
LEU
B
329
29.010
20.660
11.757
1.00
26.48
B


ATOM
4783
C
LEU
B
329
33.647
21.988
11.318
1.00
28.66
B


ATOM
4784
O
LEU
B
329
33.913
20.905
10.794
1.00
28.04
B


ATOM
4785
N
GLY
B
330
34.218
23.129
10.934
1.00
27.29
B


ATOM
4786
CA
GLY
B
330
35.197
23.119
9.867
1.00
24.54
B


ATOM
4787
C
GLY
B
330
34.565
23.478
8.520
1.00
25.24
B


ATOM
4788
O
GLY
B
330
35.261
23.504
7.509
1.00
24.70
B


ATOM
4789
N
SER
B
331
33.254
23.742
8.500
1.00
25.56
B


ATOM
4790
CA
SER
B
331
32.542
24.144
7.257
1.00
25.38
B


ATOM
4791
CB
SER
B
331
31.036
24.246
7.485
1.00
24.64
B


ATOM
4792
OG
SER
B
331
30.506
23.026
7.933
1.00
29.63
B


ATOM
4793
C
SER
B
331
33.017
25.538
6.863
1.00
22.80
B


ATOM
4794
O
SER
B
331
33.348
26.342
7.722
1.00
20.67
B


ATOM
4795
N
LEU
B
332
33.018
25.832
5.569
1.00
22.11
B


ATOM
4796
CA
LEU
B
332
33.453
27.154
5.106
1.00
20.67
B


ATOM
4797
CB
LEU
B
332
34.677
27.015
4.189
1.00
18.98
B


ATOM
4798
CG
LEU
B
332
35.918
26.301
4.734
1.00
21.63
B


ATOM
4799
CD1
LEU
B
332
36.944
26.133
3.604
1.00
19.80
B


ATOM
4800
CD2
LEU
B
332
36.511
27.132
5.893
1.00
18.73
B


ATOM
4801
C
LEU
B
332
32.373
27.865
4.300
1.00
20.52
B


ATOM
4802
O
LEU
B
332
31.623
27.218
3.545
1.00
18.68
B


ATOM
4803
N
PHE
B
333
32.312
29.188
4.445
1.00
19.09
B


ATOM
4804
CA
PHE
B
333
31.410
30.022
3.642
1.00
19.79
B


ATOM
4805
CB
PHE
B
333
30.401
30.834
4.503
1.00
20.49
B


ATOM
4806
CG
PHE
B
333
29.075
30.137
4.746
1.00
22.21
B


ATOM
4807
CD1
PHE
B
333
28.791
28.890
4.162
1.00
22.88
B


ATOM
4808
CD2
PHE
B
333
28.121
30.714
5.594
1.00
20.25
B


ATOM
4809
CE1
PHE
B
333
27.585
28.227
4.418
1.00
19.19
B


ATOM
4810
CE2
PHE
B
333
26.905
30.057
5.858
1.00
20.18
B


ATOM
4811
CZ
PHE
B
333
26.649
28.809
5.261
1.00
23.20
B


ATOM
4812
C
PHE
B
333
32.352
31.022
2.981
1.00
20.58
B


ATOM
4813
O
PHE
B
333
33.373
31.369
3.577
1.00
17.56
B


ATOM
4814
N
GLN
B
334
32.033
31.455
1.754
1.00
21.12
B


ATOM
4815
CA
GLN
B
334
32.826
32.486
1.066
1.00
23.93
B


ATOM
4816
CB
GLN
B
334
33.195
32.093
−0.388
1.00
26.06
B


ATOM
4817
CG
GLN
B
334
34.088
30.833
−0.538
1.00
30.48
B


ATOM
4818
CD
GLN
B
334
33.316
29.542
−0.206
1.00
34.25
B


ATOM
4819
OE1
GLN
B
334
32.215
29.317
−0.732
1.00
33.30
B


ATOM
4820
NE2
GLN
B
334
33.887
28.695
0.666
1.00
33.45
B


ATOM
4821
C
GLN
B
334
31.942
33.742
1.005
1.00
25.04
B


ATOM
4822
O
GLN
B
334
30.758
33.657
0.736
1.00
24.24
B


ATOM
4823
N
GLY
B
335
32.506
34.910
1.268
1.00
25.13
B


ATOM
4824
CA
GLY
B
335
31.696
36.116
1.205
1.00
26.16
B


ATOM
4825
C
GLY
B
335
32.463
37.233
0.510
1.00
25.94
B


ATOM
4826
O
GLY
B
335
33.698
37.262
0.508
1.00
27.60
B


ATOM
4827
N
ARG
B
336
31.758
38.151
−0.101
1.00
25.69
B


ATOM
4828
CA
ARG
B
336
32.451
39.253
−0.740
1.00
28.54
B


ATOM
4829
CB
ARG
B
336
32.640
39.004
−2.234
1.00
29.72
B


ATOM
4830
CG
ARG
B
336
33.508
37.853
−2.617
1.00
41.04
B


ATOM
4831
CD
ARG
B
336
34.016
38.112
−4.041
1.00
45.99
B


ATOM
4832
NE
ARG
B
336
32.926
38.617
−4.875
1.00
50.83
B


ATOM
4833
CZ
ARG
B
336
32.166
37.838
−5.638
1.00
52.45
B


ATOM
4834
NH1
ARG
B
336
32.409
36.527
−5.667
1.00
53.87
B


ATOM
4835
NH2
ARG
B
336
31.161
38.356
−6.339
1.00
49.99
B


ATOM
4836
C
ARG
B
336
31.622
40.506
−0.617
1.00
26.06
B


ATOM
4837
O
ARG
B
336
30.426
40.445
−0.775
1.00
25.98
B


ATOM
4838
N
VAL
B
337
32.246
41.636
−0.333
1.00
25.86
B


ATOM
4839
CA
VAL
B
337
31.485
42.886
−0.318
1.00
25.70
B


ATOM
4840
CB
VAL
B
337
32.180
43.942
0.507
1.00
24.01
B


ATOM
4841
CG1
VAL
B
337
31.429
45.271
0.368
1.00
20.96
B


ATOM
4842
CG2
VAL
B
337
32.228
43.448
1.986
1.00
20.15
B


ATOM
4843
C
VAL
B
337
31.367
43.350
−1.788
1.00
26.87
B


ATOM
4844
O
VAL
B
337
32.368
43.522
−2.483
1.00
27.63
B


ATOM
4845
N
LEU
B
338
30.139
43.505
−2.258
1.00
26.02
B


ATOM
4846
CA
LEU
B
338
29.878
43.910
−3.630
1.00
27.59
B


ATOM
4847
CB
LEU
B
338
28.532
43.326
−4.095
1.00
25.02
B


ATOM
4848
CG
LEU
B
338
28.376
41.786
−3.998
1.00
25.21
B


ATOM
4849
CD1
LEU
B
338
27.080
41.364
−4.729
1.00
24.08
B


ATOM
4850
CD2
LEU
B
338
29.585
41.064
−4.638
1.00
25.18
B


ATOM
4851
C
LEU
B
338
29.891
45.429
−3.833
1.00
29.31
B


ATOM
4852
O
LEU
B
338
30.225
45.910
−4.915
1.00
27.00
B


ATOM
4853
N
GLY
B
339
29.539
46.184
−2.799
1.00
29.30
B


ATOM
4854
CA
GLY
B
339
29.517
47.624
−2.939
1.00
30.47
B


ATOM
4855
C
GLY
B
339
29.139
48.290
−1.635
1.00
32.22
B


ATOM
4856
O
GLY
B
339
28.634
47.635
−0.717
1.00
30.51
B


ATOM
4857
N
GLU
B
340
29.385
49.594
−1.553
1.00
32.95
B


ATOM
4858
CA
GLU
B
340
29.084
50.372
−0.351
1.00
34.26
B


ATOM
4859
CB
GLU
B
340
30.350
50.971
0.257
1.00
33.77
B


ATOM
4860
CG
GLU
B
340
30.999
52.033
−0.627
1.00
38.93
B


ATOM
4861
CD
GLU
B
340
32.342
52.531
−0.099
1.00
41.55
B


ATOM
4862
OE1
GLU
B
340
33.058
53.220
−0.857
1.00
46.29
B


ATOM
4863
OE2
GLU
B
340
32.695
52.241
1.061
1.00
43.41
B


ATOM
4864
C
GLU
B
340
28.178
51.491
−0.781
1.00
35.19
B


ATOM
4865
O
GLU
B
340
27.952
51.690
−1.966
1.00
33.75
B


ATOM
4866
N
GLU
B
341
27.663
52.216
0.198
1.00
37.68
B


ATOM
4867
CA
GLU
B
341
26.771
53.322
−0.064
1.00
39.25
B


ATOM
4868
CB
GLU
B
341
25.484
52.805
−0.678
1.00
42.62
B


ATOM
4869
CG
GLU
B
341
24.465
53.872
−0.951
1.00
47.03
B


ATOM
4870
CD
GLU
B
341
23.247
53.306
−1.619
1.00
51.21
B


ATOM
4871
OE1
GLU
B
341
23.379
52.861
−2.779
1.00
55.60
B


ATOM
4872
OE2
GLU
B
341
22.166
53.285
−0.988
1.00
52.72
B


ATOM
4873
C
GLU
B
341
26.475
54.061
1.230
1.00
39.57
B


ATOM
4874
O
GLU
B
341
26.391
53.450
2.295
1.00
40.02
B


ATOM
4875
N
ARG
B
342
26.379
55.383
1.127
1.00
38.97
B


ATOM
4876
CA
ARG
B
342
26.062
56.252
2.250
1.00
39.68
B


ATOM
4877
CB
ARG
B
342
26.914
57.506
2.188
1.00
40.08
B


ATOM
4878
CG
ARG
B
342
28.346
57.288
2.568
1.00
38.91
B


ATOM
4879
CD
ARG
B
342
28.517
57.312
4.062
1.00
40.93
B


ATOM
4880
NE
ARG
B
342
29.898
57.013
4.430
1.00
40.78
B


ATOM
4881
CZ
ARG
B
342
30.331
56.971
5.683
1.00
40.62
B


ATOM
4882
NH1
ARG
B
342
29.486
57.213
6.682
1.00
39.03
B


ATOM
4883
NH2
ARG
B
342
31.600
56.681
5.933
1.00
39.87
B


ATOM
4884
C
ARG
B
342
24.601
56.644
2.088
1.00
39.85
B


ATOM
4885
O
ARG
B
342
24.206
57.040
0.994
1.00
39.84
B


ATOM
4886
N
ILE
B
343
23.802
56.524
3.153
1.00
38.11
B


ATOM
4887
CA
ILE
B
343
22.388
56.884
3.080
1.00
39.86
B


ATOM
4888
CB
ILE
B
343
21.482
55.833
3.800
1.00
40.57
B


ATOM
4889
CG2
ILE
B
343
20.048
56.325
3.849
1.00
39.53
B


ATOM
4890
CG1
ILE
B
343
21.479
54.500
3.023
1.00
42.58
B


ATOM
4891
CD1
ILE
B
343
22.839
53.867
2.829
1.00
44.12
B


ATOM
4892
C
ILE
B
343
22.248
58.266
3.732
1.00
40.64
B


ATOM
4893
O
ILE
B
343
22.334
58.414
4.956
1.00
39.61
B


ATOM
4894
N
PRO
B
344
22.052
59.304
2.907
1.00
40.68
B


ATOM
4895
CD
PRO
B
344
21.922
59.204
1.441
1.00
40.17
B


ATOM
4896
CA
PRO
B
344
21.912
60.697
3.357
1.00
40.04
B


ATOM
4897
CB
PRO
B
344
21.483
61.416
2.081
1.00
40.93
B


ATOM
4898
CG
PRO
B
344
22.193
60.618
1.000
1.00
42.76
B


ATOM
4899
C
PRO
B
344
20.983
60.994
4.543
1.00
37.82
B


ATOM
4900
O
PRO
B
344
19.808
60.657
4.540
1.00
37.61
B


ATOM
4901
N
GLY
B
345
21.544
61.624
5.568
1.00
40.04
B


ATOM
4902
CA
GLY
B
345
20.767
62.018
6.737
1.00
39.71
B


ATOM
4903
C
GLY
B
345
20.150
60.926
7.582
1.00
39.78
B


ATOM
4904
O
GLY
B
345
19.204
61.178
8.320
1.00
40.82
B


ATOM
4905
N
VAL
B
346
20.682
59.716
7.478
1.00
39.41
B


ATOM
4906
CA
VAL
B
346
20.204
58.565
8.250
1.00
36.79
B


ATOM
4907
CB
VAL
B
346
19.681
57.471
7.309
1.00
38.80
B


ATOM
4908
CG1
VAL
B
346
19.197
56.254
8.108
1.00
35.85
B


ATOM
4909
CG2
VAL
B
346
18.549
58.057
6.440
1.00
38.21
B


ATOM
4910
C
VAL
B
346
21.454
58.086
8.958
1.00
36.54
B


ATOM
4911
O
VAL
B
346
22.408
57.643
8.318
1.00
36.64
B


ATOM
4912
N
LYS
B
347
21.480
58.196
10.278
1.00
34.42
B


ATOM
4913
CA
LYS
B
347
22.661
57.797
10.998
1.00
34.09
B


ATOM
4914
CB
LYS
B
347
23.263
58.997
11.755
1.00
36.17
B


ATOM
4915
CG
LYS
B
347
23.561
60.211
10.886
1.00
38.07
B


ATOM
4916
CD
LYS
B
347
24.358
61.260
11.662
1.00
38.70
B


ATOM
4917
CE
LYS
B
347
24.728
62.460
10.777
1.00
39.52
B


ATOM
4918
NZ
LYS
B
347
26.053
63.049
11.184
1.00
41.11
B


ATOM
4919
C
LYS
B
347
22.348
56.716
11.990
1.00
32.99
B


ATOM
4920
O
LYS
B
347
21.178
56.486
12.317
1.00
32.79
B


ATOM
4921
N
VAL
B
348
23.417
56.065
12.453
1.00
30.95
B


ATOM
4922
CA
VAL
B
348
23.375
55.023
13.472
1.00
29.42
B


ATOM
4923
CB
VAL
B
348
23.626
53.578
12.889
1.00
30.26
B


ATOM
4924
CG1
VAL
B
348
22.372
53.111
12.092
1.00
28.31
B


ATOM
4925
CG2
VAL
B
348
24.902
53.568
12.007
1.00
25.77
B


ATOM
4926
C
VAL
B
348
24.528
55.433
14.396
1.00
30.34
B


ATOM
4927
O
VAL
B
348
25.385
56.217
14.004
1.00
28.38
B


ATOM
4928
N
PRO
B
349
24.569
54.898
15.624
1.00
30.96
B


ATOM
4929
CD
PRO
B
349
23.723
53.791
16.112
1.00
30.71
B


ATOM
4930
CA
PRO
B
349
25.619
55.230
16.600
1.00
30.90
B


ATOM
4931
CB
PRO
B
349
25.505
54.111
17.639
1.00
31.30
B


ATOM
4932
CG
PRO
B
349
24.020
53.776
17.615
1.00
32.51
B


ATOM
4933
C
PRO
B
349
27.035
55.377
16.085
1.00
32.47
B


ATOM
4934
O
PRO
B
349
27.780
56.256
16.530
1.00
32.64
B


ATOM
4935
N
VAL
B
350
27.432
54.523
15.157
1.00
32.92
B


ATOM
4936
CA
VAL
B
350
28.786
54.618
14.662
1.00
33.72
B


ATOM
4937
CB
VAL
B
350
29.258
53.232
14.058
1.00
34.37
B


ATOM
4938
CG1
VAL
B
350
28.802
53.082
12.599
1.00
33.33
B


ATOM
4939
CG2
VAL
B
350
30.772
53.088
14.198
1.00
34.51
B


ATOM
4940
C
VAL
B
350
28.929
55.761
13.638
1.00
34.67
B


ATOM
4941
O
VAL
B
350
30.031
56.147
13.278
1.00
33.68
B


ATOM
4942
N
THR
B
351
27.826
56.332
13.187
1.00
34.78
B


ATOM
4943
CA
THR
B
351
27.954
57.391
12.196
1.00
37.98
B


ATOM
4944
CB
THR
B
351
26.637
57.622
11.496
1.00
36.38
B


ATOM
4945
OG1
THR
B
351
26.122
56.348
11.066
1.00
34.42
B


ATOM
4946
CG2
THR
B
351
26.845
58.520
10.261
1.00
36.20
B


ATOM
4947
C
THR
B
351
28.483
58.698
12.819
1.00
40.94
B


ATOM
4948
O
THR
B
351
27.904
59.222
13.766
1.00
38.36
B


ATOM
4949
N
LYS
B
352
29.611
59.188
12.296
1.00
44.39
B


ATOM
4950
CA
LYS
B
352
30.242
60.418
12.806
1.00
49.45
B


ATOM
4951
CB
LYS
B
352
31.659
60.573
12.243
1.00
51.04
B


ATOM
4952
CG
LYS
B
352
32.650
59.621
12.898
1.00
54.39
B


ATOM
4953
CD
LYS
B
352
33.989
59.628
12.206
1.00
56.49
B


ATOM
4954
CE
LYS
B
352
34.800
58.413
12.625
1.00
58.70
B


ATOM
4955
NZ
LYS
B
352
36.112
58.345
11.911
1.00
62.06
B


ATOM
4956
C
LYS
B
352
29.441
61.673
12.516
1.00
50.40
B


ATOM
4957
O
LYS
B
352
28.717
61.748
11.515
1.00
50.31
B


ATOM
4958
N
ASP
B
353
29.560
62.651
13.410
1.00
52.66
B


ATOM
4959
CA
ASP
B
353
28.844
63.914
13.249
1.00
53.89
B


ATOM
4960
CB
ASP
B
353
29.237
64.890
14.357
1.00
56.77
B


ATOM
4961
CG
ASP
B
353
28.700
64.472
15.703
1.00
59.96
B


ATOM
4962
OD1
ASP
B
353
27.611
63.849
15.703
1.00
61.27
B


ATOM
4963
OD2
ASP
B
353
29.345
64.772
16.744
1.00
60.41
B


ATOM
4964
C
ASP
B
353
29.150
64.531
11.895
1.00
53.00
B


ATOM
4965
O
ASP
B
353
28.253
65.045
11.223
1.00
52.07
B


ATOM
4966
N
ALA
B
354
30.425
64.458
11.510
1.00
52.54
B


ATOM
4967
CA
ALA
B
354
30.909
64.999
10.245
1.00
51.99
B


ATOM
4968
CB
ALA
B
354
32.427
64.961
10.212
1.00
50.93
B


ATOM
4969
C
ALA
B
354
30.352
64.230
9.052
1.00
51.80
B


ATOM
4970
O
ALA
B
354
30.253
64.782
7.949
1.00
53.72
B


ATOM
4971
N
GLU
B
355
30.000
62.961
9.256
1.00
49.04
B


ATOM
4972
CA
GLU
B
355
29.452
62.155
8.172
1.00
46.93
B


ATOM
4973
CB
GLU
B
355
29.638
60.659
8.474
1.00
47.46
B


ATOM
4974
CG
GLU
B
355
31.086
60.183
8.244
1.00
46.52
B


ATOM
4975
CD
GLU
B
355
31.358
58.811
8.825
1.00
46.45
B


ATOM
4976
OE1
GLU
B
355
32.353
58.159
8.410
1.00
45.51
B


ATOM
4977
OE2
GLU
B
355
30.577
58.400
9.709
1.00
43.89
B


ATOM
4978
C
GLU
B
355
27.988
62.499
7.908
1.00
45.36
B


ATOM
4979
O
GLU
B
355
27.164
62.583
8.825
1.00
42.97
B


ATOM
4980
N
GLU
B
356
27.692
62.716
6.633
1.00
45.09
B


ATOM
4981
CA
GLU
B
356
26.358
63.096
6.186
1.00
46.60
B


ATOM
4982
CB
GLU
B
356
26.410
63.582
4.728
1.00
51.78
B


ATOM
4983
CG
GLU
B
356
27.388
64.747
4.443
1.00
59.66
B


ATOM
4984
CD
GLU
B
356
27.003
66.065
5.134
1.00
63.36
B


ATOM
4985
OE1
GLU
B
356
25.796
66.423
5.143
1.00
66.13
B


ATOM
4986
OE2
GLU
B
356
27.915
66.755
5.650
1.00
64.88
B


ATOM
4987
C
GLU
B
356
25.329
61.982
6.281
1.00
43.74
B


ATOM
4988
O
GLU
B
356
24.123
62.256
6.378
1.00
43.78
B


ATOM
4989
N
GLY
B
357
25.808
60.738
6.228
1.00
39.88
B


ATOM
4990
CA
GLY
B
357
24.921
59.586
6.280
1.00
37.14
B


ATOM
4991
C
GLY
B
357
25.615
58.279
6.613
1.00
34.47
B


ATOM
4992
O
GLY
B
357
26.818
58.132
6.447
1.00
34.26
B


ATOM
4993
N
MET
B
358
24.848
57.306
7.090
1.00
33.76
B


ATOM
4994
CA
MET
B
358
25.426
56.015
7.476
1.00
30.05
B


ATOM
4995
CB
MET
B
358
24.364
55.173
8.179
1.00
30.10
B


ATOM
4996
CG
MET
B
358
23.215
54.751
7.295
1.00
28.41
B


ATOM
4997
SD
MET
B
358
21.970
53.810
8.233
1.00
30.92
B


ATOM
4998
CE
MET
B
358
22.892
52.181
8.410
1.00
29.07
B


ATOM
4999
C
MET
B
358
26.007
55.223
6.302
1.00
28.66
B


ATOM
5000
O
MET
B
358
25.545
55.340
5.170
1.00
28.07
B


ATOM
5001
N
LEU
B
359
27.032
54.423
6.582
1.00
26.06
B


ATOM
5002
CA
LEU
B
359
27.640
53.568
5.569
1.00
26.98
B


ATOM
5003
CB
LEU
B
359
29.108
53.355
5.885
1.00
27.21
B


ATOM
5004
CG
LEU
B
359
29.867
52.329
5.045
1.00
27.90
B


ATOM
5005
CD1
LEU
B
359
30.157
52.889
3.655
1.00
29.11
B


ATOM
5006
CD2
LEU
B
359
31.195
52.002
5.746
1.00
30.24
B


ATOM
5007
C
LEU
B
359
26.936
52.198
5.632
1.00
27.27
B


ATOM
5008
O
LEU
B
359
26.710
51.702
6.729
1.00
24.72
B


ATOM
5009
N
VAL
B
360
26.561
51.628
4.477
1.00
26.99
B


ATOM
5010
CA
VAL
B
360
25.948
50.282
4.406
1.00
26.74
B


ATOM
5011
CB
VAL
B
360
24.435
50.277
4.014
1.00
24.35
B


ATOM
5012
CG1
VAL
B
360
23.612
51.065
5.015
1.00
26.85
B


ATOM
5013
CG2
VAL
B
360
24.245
50.821
2.606
1.00
28.14
B


ATOM
5014
C
VAL
B
360
26.700
49.573
3.297
1.00
27.27
B


ATOM
5015
O
VAL
B
360
27.190
50.247
2.387
1.00
28.61
B


ATOM
5016
N
VAL
B
361
26.823
48.241
3.374
1.00
26.68
B


ATOM
5017
CA
VAL
B
361
27.491
47.468
2.318
1.00
25.44
B


ATOM
5018
CB
VAL
B
361
28.864
46.867
2.767
1.00
27.07
B


ATOM
5019
CG1
VAL
B
361
29.862
47.996
3.097
1.00
25.00
B


ATOM
5020
CG2
VAL
B
361
28.684
45.912
3.966
1.00
24.63
B


ATOM
5021
C
VAL
B
361
26.596
46.321
1.854
1.00
26.05
B


ATOM
5022
O
VAL
B
361
25.695
45.903
2.566
1.00
27.10
B


ATOM
5023
N
THR
B
362
26.835
45.824
0.652
1.00
26.26
B


ATOM
5024
CA
THR
B
362
26.055
44.709
0.131
1.00
27.08
B


ATOM
5025
CB
THR
B
362
25.466
45.076
−1.240
1.00
27.95
B


ATOM
5026
OG1
THR
B
362
24.371
45.971
−1.019
1.00
31.35
B


ATOM
5027
CG2
THR
B
362
24.963
43.816
−1.985
1.00
27.89
B


ATOM
5028
C
THR
B
362
26.973
43.494
0.047
1.00
26.27
B


ATOM
5029
O
THR
B
362
27.943
43.502
−0.688
1.00
29.04
B


ATOM
5030
N
ALA
B
363
26.695
42.473
0.845
1.00
24.70
B


ATOM
5031
CA
ALA
B
363
27.506
41.253
0.862
1.00
24.15
B


ATOM
5032
CB
ALA
B
363
27.751
40.812
2.315
1.00
23.75
B


ATOM
5033
C
ALA
B
363
26.840
40.087
0.101
1.00
24.63
B


ATOM
5034
O
ALA
B
363
25.609
39.951
0.072
1.00
23.22
B


ATOM
5035
N
GLU
B
364
27.676
39.273
−0.529
1.00
22.66
B


ATOM
5036
CA
GLU
B
364
27.230
38.093
−1.214
1.00
23.99
B


ATOM
5037
CB
GLU
B
364
27.749
38.055
−2.644
1.00
27.69
B


ATOM
5038
CG
GLU
B
364
27.155
36.902
−3.443
1.00
33.48
B


ATOM
5039
CD
GLU
B
364
27.562
36.936
−4.922
1.00
39.70
B


ATOM
5040
OE1
GLU
B
364
28.779
37.089
−5.183
1.00
42.02
B


ATOM
5041
OE2
GLU
B
364
26.668
36.795
−5.814
1.00
42.01
B


ATOM
5042
C
GLU
B
364
27.876
36.964
−0.402
1.00
23.63
B


ATOM
5043
O
GLU
B
364
29.043
37.073
−0.021
1.00
23.47
B


ATOM
5044
N
ILE
B
365
27.121
35.904
−0.118
1.00
22.05
B


ATOM
5045
CA
ILE
B
365
27.606
34.761
0.659
1.00
20.67
B


ATOM
5046
CB
ILE
B
365
26.777
34.594
1.980
1.00
22.40
B


ATOM
5047
CG2
ILE
B
365
27.274
33.352
2.781
1.00
23.38
B


ATOM
5048
CG1
ILE
B
365
26.847
35.871
2.830
1.00
19.69
B


ATOM
5049
CD1
ILE
B
365
28.257
36.253
3.366
1.00
20.19
B


ATOM
5050
C
ILE
B
365
27.382
33.525
−0.235
1.00
22.67
B


ATOM
5051
O
ILE
B
365
26.338
33.404
−0.913
1.00
21.12
B


ATOM
5052
N
THR
B
366
28.339
32.610
−0.231
1.00
20.74
B


ATOM
5053
CA
THR
B
366
28.233
31.408
−1.062
1.00
22.55
B


ATOM
5054
CB
THR
B
366
29.294
31.424
−2.179
1.00
22.50
B


ATOM
5055
OG1
THR
B
366
29.123
32.605
−2.959
1.00
24.75
B


ATOM
5056
CG2
THR
B
366
29.141
30.232
−3.107
1.00
23.94
B


ATOM
5057
C
THR
B
366
28.475
30.196
−0.181
1.00
22.86
B


ATOM
5058
O
THR
B
366
29.409
30.214
0.604
1.00
22.02
B


ATOM
5059
N
GLY
B
367
27.624
29.177
−0.307
1.00
21.56
B


ATOM
5060
CA
GLY
B
367
27.741
27.951
0.467
1.00
21.48
B


ATOM
5061
C
GLY
B
367
27.050
26.816
−0.284
1.00
22.21
B


ATOM
5062
O
GLY
B
367
26.565
27.017
−1.404
1.00
21.84
B


ATOM
5063
N
LYS
B
368
27.006
25.610
0.283
1.00
22.66
B


ATOM
5064
CA
LYS
B
368
26.347
24.498
−0.423
1.00
20.46
B


ATOM
5065
CB
LYS
B
368
27.398
23.485
−0.916
1.00
24.29
B


ATOM
5066
CG
LYS
B
368
26.833
22.217
−1.637
1.00
27.75
B


ATOM
5067
CD
LYS
B
368
27.990
21.314
−2.153
1.00
29.26
B


ATOM
5068
CE
LYS
B
368
27.466
20.142
−2.982
1.00
30.74
B


ATOM
5069
NZ
LYS
B
368
26.271
20.559
−3.794
1.00
32.01
B


ATOM
5070
C
LYS
B
368
25.362
23.840
0.512
1.00
21.10
B


ATOM
5071
O
LYS
B
368
25.630
23.685
1.708
1.00
23.03
B


ATOM
5072
N
ALA
B
369
24.203
23.468
−0.016
1.00
19.42
B


ATOM
5073
CA
ALA
B
369
23.202
22.825
0.788
1.00
17.75
B


ATOM
5074
CB
ALA
B
369
21.974
23.663
0.878
1.00
19.50
B


ATOM
5075
C
ALA
B
369
22.857
21.487
0.191
1.00
20.13
B


ATOM
5076
O
ALA
B
369
22.956
21.283
−1.028
1.00
19.17
B


ATOM
5077
N
PHE
B
370
22.444
20.576
1.061
1.00
17.05
B


ATOM
5078
CA
PHE
B
370
22.079
19.247
0.630
1.00
18.83
B


ATOM
5079
CB
PHE
B
370
22.992
18.185
1.286
1.00
22.41
B


ATOM
5080
CG
PHE
B
370
24.396
18.173
0.761
1.00
26.25
B


ATOM
5081
CD1
PHE
B
370
24.708
17.482
−0.406
1.00
30.61
B


ATOM
5082
CD2
PHE
B
370
25.395
18.876
1.403
1.00
27.98
B


ATOM
5083
CE1
PHE
B
370
26.006
17.496
−0.921
1.00
32.67
B


ATOM
5084
CE2
PHE
B
370
26.715
18.895
0.888
1.00
28.34
B


ATOM
5085
CZ
PHE
B
370
27.011
18.208
−0.264
1.00
28.75
B


ATOM
5086
C
PHE
B
370
20.688
18.943
1.057
1.00
17.51
B


ATOM
5087
O
PHE
B
370
20.259
19.311
2.172
1.00
16.63
B


ATOM
5088
N
ILE
B
371
19.968
18.243
0.198
1.00
16.90
B


ATOM
5089
CA
ILE
B
371
18.645
17.788
0.602
1.00
18.95
B


ATOM
5090
CB
ILE
B
371
17.781
17.437
−0.627
1.00
21.54
B


ATOM
5091
CG2
ILE
B
371
16.463
16.786
−0.185
1.00
21.62
B


ATOM
5092
CG1
ILE
B
371
17.547
18.720
−1.437
1.00
22.68
B


ATOM
5093
CD1
ILE
B
371
16.438
18.650
−2.554
1.00
27.87
B


ATOM
5094
C
ILE
B
371
18.937
16.512
1.457
1.00
19.48
B


ATOM
5095
O
ILE
B
371
19.709
15.655
1.028
1.00
17.27
B


ATOM
5096
N
MET
B
372
18.401
16.434
2.690
1.00
17.92
B


ATOM
5097
CA
MET
B
372
18.613
15.256
3.506
1.00
18.60
B


ATOM
5098
CB
MET
B
372
19.274
15.623
4.850
1.00
19.34
B


ATOM
5099
CG
MET
B
372
18.419
16.435
5.758
1.00
18.11
B


ATOM
5100
SD
MET
B
372
19.301
16.869
7.267
1.00
19.21
B


ATOM
5101
CE
MET
B
372
18.041
17.789
8.107
1.00
12.91
B


ATOM
5102
C
MET
B
372
17.328
14.445
3.722
1.00
18.21
B


ATOM
5103
O
MET
B
372
17.376
13.308
4.195
1.00
17.66
B


ATOM
5104
N
GLY
B
373
16.184
15.009
3.360
1.00
19.33
B


ATOM
5105
CA
GLY
B
373
14.937
14.276
3.489
1.00
19.69
B


ATOM
5106
C
GLY
B
373
13.702
14.954
2.911
1.00
20.45
B


ATOM
5107
O
GLY
B
373
13.659
16.187
2.793
1.00
18.84
B


ATOM
5108
N
PHE
B
374
12.724
14.157
2.491
1.00
18.91
B


ATOM
5109
CA
PHE
B
374
11.433
14.694
2.051
1.00
21.32
B


ATOM
5110
CB
PHE
B
374
11.031
14.179
0.669
1.00
23.96
B


ATOM
5111
CG
PHE
B
374
11.868
14.742
−0.434
1.00
23.84
B


ATOM
5112
CD1
PHE
B
374
11.773
16.079
−0.773
1.00
25.19
B


ATOM
5113
CD2
PHE
B
374
12.770
13.941
−1.115
1.00
25.02
B


ATOM
5114
CE1
PHE
B
374
12.577
16.605
−1.787
1.00
25.39
B


ATOM
5115
CE2
PHE
B
374
13.568
14.451
−2.120
1.00
24.17
B


ATOM
5116
CZ
PHE
B
374
13.474
15.784
−2.460
1.00
23.47
B


ATOM
5117
C
PHE
B
374
10.544
14.108
3.132
1.00
22.93
B


ATOM
5118
O
PHE
B
374
10.378
12.885
3.208
1.00
23.92
B


ATOM
5119
N
ASN
B
375
9.952
14.961
3.955
1.00
21.77
B


ATOM
5120
CA
ASN
B
375
9.205
14.478
5.104
1.00
22.02
B


ATOM
5121
CB
ASN
B
375
9.982
14.973
6.335
1.00
26.98
B


ATOM
5122
CG
ASN
B
375
9.525
14.358
7.643
1.00
30.89
B


ATOM
5123
OD1
ASN
B
375
8.939
13.266
7.691
1.00
34.61
B


ATOM
5124
ND2
ASN
B
375
9.825
15.061
8.739
1.00
33.14
B


ATOM
5125
C
ASN
B
375
7.764
14.940
5.160
1.00
21.79
B


ATOM
5126
O
ASN
B
375
7.454
16.042
4.729
1.00
25.19
B


ATOM
5127
N
THR
B
376
6.861
14.073
5.603
1.00
18.65
B


ATOM
5128
CA
THR
B
376
5.491
14.481
5.788
1.00
18.70
B


ATOM
5129
CB
THR
B
376
4.528
13.602
5.008
1.00
19.42
B


ATOM
5130
OG1
THR
B
376
4.792
13.773
3.602
1.00
24.49
B


ATOM
5131
CG2
THR
B
376
3.117
14.005
5.292
1.00
20.36
B


ATOM
5132
C
THR
B
376
5.300
14.349
7.294
1.00
18.93
B


ATOM
5133
O
THR
B
376
5.206
13.254
7.846
1.00
20.07
B


ATOM
5134
N
MET
B
377
5.265
15.502
7.936
1.00
18.83
B


ATOM
5135
CA
MET
B
377
5.181
15.654
9.372
1.00
21.66
B


ATOM
5136
CB
MET
B
377
5.888
16.965
9.723
1.00
23.86
B


ATOM
5137
CG
MET
B
377
6.173
17.173
11.177
1.00
28.77
B


ATOM
5138
SD
MET
B
377
7.393
18.508
11.335
1.00
33.73
B


ATOM
5139
CE
MET
B
377
8.597
17.989
10.319
1.00
26.81
B


ATOM
5140
C
MET
B
377
3.745
15.633
9.840
1.00
20.80
B


ATOM
5141
O
MET
B
377
2.909
16.347
9.301
1.00
23.03
B


ATOM
5142
N
LEU
B
378
3.463
14.807
10.847
1.00
18.13
B


ATOM
5143
CA
LEU
B
378
2.122
14.628
11.377
1.00
17.58
B


ATOM
5144
CB
LEU
B
378
1.755
13.145
11.314
1.00
19.64
B


ATOM
5145
CG
LEU
B
378
1.890
12.441
9.960
1.00
23.99
B


ATOM
5146
CD1
LEU
B
378
1.387
11.024
10.095
1.00
25.18
B


ATOM
5147
CD2
LEU
B
378
1.058
13.167
8.929
1.00
22.82
B


ATOM
5148
C
LEU
B
378
1.904
15.123
12.807
1.00
20.28
B


ATOM
5149
O
LEU
B
378
2.805
15.047
13.671
1.00
18.55
B


ATOM
5150
N
PHE
B
379
0.679
15.573
13.060
1.00
19.42
B


ATOM
5151
CA
PHE
B
379
0.293
16.106
14.345
1.00
19.30
B


ATOM
5152
CB
PHE
B
379
0.251
17.642
14.275
1.00
17.57
B


ATOM
5153
CG
PHE
B
379
1.593
18.275
13.988
1.00
18.77
B


ATOM
5154
CD1
PHE
B
379
2.493
18.546
15.035
1.00
16.65
B


ATOM
5155
CD2
PHE
B
379
1.991
18.541
12.669
1.00
20.08
B


ATOM
5156
CE1
PHE
B
379
3.765
19.068
14.776
1.00
16.88
B


ATOM
5157
CE2
PHE
B
379
3.279
19.071
12.386
1.00
18.55
B


ATOM
5158
CZ
PHE
B
379
4.168
19.332
13.465
1.00
14.92
B


ATOM
5159
C
PHE
B
379
−1.095
15.609
14.772
1.00
23.48
B


ATOM
5160
O
PHE
B
379
−2.113
16.153
14.363
1.00
26.02
B


ATOM
5161
N
ASP
B
380
−1.140
14.576
15.590
1.00
23.87
B


ATOM
5162
CA
ASP
B
380
−2.403
14.091
16.101
1.00
24.28
B


ATOM
5163
CB
ASP
B
380
−2.202
12.679
16.640
1.00
27.17
B


ATOM
5164
CG
ASP
B
380
−3.490
12.045
17.131
1.00
29.28
B


ATOM
5165
OD1
ASP
B
380
−4.295
12.692
17.851
1.00
29.00
B


ATOM
5166
OD2
ASP
B
380
−3.671
10.870
16.795
1.00
32.48
B


ATOM
5167
C
ASP
B
380
−2.830
15.044
17.240
1.00
25.93
B


ATOM
5168
O
ASP
B
380
−2.044
15.371
18.112
1.00
25.21
B


ATOM
5169
N
PRO
B
381
−4.088
15.521
17.221
1.00
29.19
B


ATOM
5170
CD
PRO
B
381
−5.069
15.151
16.175
1.00
28.13
B


ATOM
5171
CA
PRO
B
381
−4.686
16.433
18.210
1.00
27.16
B


ATOM
5172
CB
PRO
B
381
−6.153
16.484
17.775
1.00
31.84
B


ATOM
5173
CG
PRO
B
381
−6.089
16.237
16.288
1.00
29.58
B


ATOM
5174
C
PRO
B
381
−4.559
15.894
19.647
1.00
28.24
B


ATOM
5175
O
PRO
B
381
−4.549
16.675
20.634
1.00
26.10
B


ATOM
5176
N
THR
B
382
−4.470
14.563
19.758
1.00
25.53
B


ATOM
5177
CA
THR
B
382
−4.347
13.904
21.065
1.00
26.78
B


ATOM
5178
CB
THR
B
382
−5.109
12.556
21.116
1.00
26.38
B


ATOM
5179
OG1
THR
B
382
−4.537
11.660
20.156
1.00
27.59
B


ATOM
5180
CG2
THR
B
382
−6.575
12.770
20.833
1.00
24.91
B


ATOM
5181
C
THR
B
382
−2.904
13.615
21.491
1.00
25.71
B


ATOM
5182
O
THR
B
382
−2.655
13.143
22.590
1.00
26.08
B


ATOM
5183
N
ASP
B
383
−1.953
13.891
20.622
1.00
23.16
B


ATOM
5184
CA
ASP
B
383
−0.559
13.678
20.951
1.00
22.99
B


ATOM
5185
CB
ASP
B
383
0.256
13.833
19.652
1.00
19.53
B


ATOM
5186
CG
ASP
B
383
1.727
13.629
19.861
1.00
20.29
B


ATOM
5187
OD1
ASP
B
383
2.135
13.563
21.040
1.00
20.01
B


ATOM
5188
OD2
ASP
B
383
2.465
13.548
18.863
1.00
17.16
B


ATOM
5189
C
ASP
B
383
−0.175
14.767
21.987
1.00
23.38
B


ATOM
5190
O
ASP
B
383
−0.247
15.963
21.681
1.00
22.31
B


ATOM
5191
N
PRO
B
384
0.219
14.372
23.229
1.00
24.61
B


ATOM
5192
CD
PRO
B
384
0.601
13.005
23.648
1.00
26.35
B


ATOM
5193
CA
PRO
B
384
0.605
15.362
24.258
1.00
22.33
B


ATOM
5194
CB
PRO
B
384
1.004
14.511
25.489
1.00
27.33
B


ATOM
5195
CG
PRO
B
384
0.534
13.093
25.160
1.00
28.78
B


ATOM
5196
C
PRO
B
384
1.796
16.184
23.805
1.00
19.14
B


ATOM
5197
O
PRO
B
384
2.037
17.230
24.339
1.00
21.49
B


ATOM
5198
N
PHE
B
385
2.560
15.691
22.832
1.00
15.43
B


ATOM
5199
CA
PHE
B
385
3.694
16.430
22.329
1.00
15.93
B


ATOM
5200
CB
PHE
B
385
4.952
15.554
22.436
1.00
18.87
B


ATOM
5201
CG
PHE
B
385
5.260
15.166
23.866
1.00
20.13
B


ATOM
5202
CD1
PHE
B
385
5.581
16.151
24.798
1.00
22.85
B


ATOM
5203
CD2
PHE
B
385
5.120
13.852
24.301
1.00
22.78
B


ATOM
5204
CE1
PHE
B
385
5.760
15.807
26.180
1.00
26.22
B


ATOM
5205
CE2
PHE
B
385
5.290
13.504
25.651
1.00
21.69
B


ATOM
5206
CZ
PHE
B
385
5.608
14.471
26.579
1.00
19.44
B


ATOM
5207
C
PHE
B
385
3.519
16.977
20.918
1.00
16.47
B


ATOM
5208
O
PHE
B
385
4.507
17.204
20.205
1.00
15.60
B


ATOM
5209
N
LYS
B
386
2.270
17.190
20.512
1.00
15.17
B


ATOM
5210
CA
LYS
B
386
1.991
17.765
19.182
1.00
15.53
B


ATOM
5211
CB
LYS
B
386
0.485
17.933
18.935
1.00
16.93
B


ATOM
5212
CG
LYS
B
386
−0.236
18.815
19.932
1.00
17.12
B


ATOM
5213
CD
LYS
B
386
−1.731
18.614
19.828
1.00
20.90
B


ATOM
5214
CE
LYS
B
386
−2.472
19.453
20.810
1.00
24.15
B


ATOM
5215
NZ
LYS
B
386
−3.923
19.103
20.662
1.00
31.40
B


ATOM
5216
C
LYS
B
386
2.666
19.105
19.076
1.00
17.01
B


ATOM
5217
O
LYS
B
386
3.011
19.529
17.974
1.00
16.30
B


ATOM
5218
N
ASN
B
387
2.898
19.778
20.218
1.00
16.85
B


ATOM
5219
CA
ASN
B
387
3.576
21.081
20.166
1.00
16.48
B


ATOM
5220
CB
ASN
B
387
2.787
22.146
20.934
1.00
19.73
B


ATOM
5221
CG
ASN
B
387
1.348
22.312
20.378
1.00
22.02
B


ATOM
5222
OD1
ASN
B
387
0.397
22.510
21.134
1.00
25.02
B


ATOM
5223
ND2
ASN
B
387
1.208
22.225
19.058
1.00
17.56
B


ATOM
5224
C
ASN
B
387
5.021
21.079
20.629
1.00
16.78
B


ATOM
5225
O
ASN
B
387
5.569
22.142
20.944
1.00
15.14
B


ATOM
5226
N
GLY
B
388
5.637
19.896
20.653
1.00
15.66
B


ATOM
5227
CA
GLY
B
388
7.041
19.784
21.032
1.00
13.64
B


ATOM
5228
C
GLY
B
388
7.415
20.031
22.499
1.00
15.26
B


ATOM
5229
O
GLY
B
388
6.596
20.447
23.275
1.00
13.96
B


ATOM
5230
N
PHE
B
389
8.682
19.797
22.847
1.00
16.92
B


ATOM
5231
CA
PHE
B
389
9.185
20.039
24.209
1.00
15.27
B


ATOM
5232
CB
PHE
B
389
8.873
18.849
25.154
1.00
11.75
B


ATOM
5233
CG
PHE
B
389
9.623
17.584
24.800
1.00
14.56
B


ATOM
5234
CD1
PHE
B
389
10.928
17.387
25.228
1.00
16.32
B


ATOM
5235
CD2
PHE
B
389
9.033
16.611
24.004
1.00
14.91
B


ATOM
5236
CE1
PHE
B
389
11.655
16.256
24.883
1.00
14.69
B


ATOM
5237
CE2
PHE
B
389
9.746
15.466
23.643
1.00
15.69
B


ATOM
5238
CZ
PHE
B
389
11.074
15.288
24.090
1.00
16.98
B


ATOM
5239
C
PHE
B
389
10.683
20.181
24.077
1.00
15.32
B


ATOM
5240
O
PHE
B
389
11.263
19.859
23.039
1.00
16.57
B


ATOM
5241
N
THR
B
390
11.303
20.753
25.101
1.00
13.16
B


ATOM
5242
CA
THR
B
390
12.756
20.871
25.158
1.00
15.26
B


ATOM
5243
CB
THR
B
390
13.289
22.292
24.842
1.00
11.40
B


ATOM
5244
OG1
THR
B
390
14.718
22.271
24.938
1.00
14.33
B


ATOM
5245
CG2
THR
B
390
12.764
23.347
25.830
1.00
11.90
B


ATOM
5246
C
THR
B
390
13.128
20.554
26.610
1.00
16.50
B


ATOM
5247
O
THR
B
390
12.373
20.868
27.529
1.00
14.49
B


ATOM
5248
N
LEU
B
391
14.280
19.949
26.796
1.00
20.29
B


ATOM
5249
CA
LEU
B
391
14.768
19.609
28.129
1.00
22.25
B


ATOM
5250
CB
LEU
B
391
15.334
18.195
28.133
1.00
17.40
B


ATOM
5251
CG
LEU
B
391
14.460
17.032
28.635
1.00
21.15
B


ATOM
5252
CD1
LEU
B
391
13.037
17.200
28.424
1.00
18.95
B


ATOM
5253
CD2
LEU
B
391
14.922
15.777
27.985
1.00
19.75
B


ATOM
5254
C
LEU
B
391
15.865
20.624
28.468
1.00
25.38
B


ATOM
5255
O
LEU
B
391
16.522
20.519
29.530
1.00
24.09
B


ATOM
5256
N
LYS
B
392
16.069
21.608
27.579
1.00
21.77
B


ATOM
5257
CA
LYS
B
392
17.087
22.618
27.857
1.00
25.23
B


ATOM
5258
CB
LYS
B
392
17.467
23.442
26.611
1.00
22.83
B


ATOM
5259
CG
LYS
B
392
18.670
24.379
26.879
1.00
25.42
B


ATOM
5260
CD
LYS
B
392
19.140
25.171
25.646
1.00
22.17
B


ATOM
5261
CE
LYS
B
392
19.709
24.248
24.642
1.00
18.21
B


ATOM
5262
NZ
LYS
B
392
20.409
24.920
23.508
1.00
16.92
B


ATOM
5263
C
LYS
B
392
16.553
23.552
28.957
1.00
25.50
B


ATOM
5264
O
LYS
B
392
15.390
23.960
28.930
1.00
22.06
B


ATOM
5265
N
GLN
B
393
17.393
23.891
29.930
1.00
27.99
B


ATOM
5266
CA
GLN
B
393
16.912
24.769
30.987
1.00
31.46
B


ATOM
5267
CB
GLN
B
393
17.537
24.451
32.356
1.00
38.27
B


ATOM
5268
CG
GLN
B
393
18.587
23.361
32.408
1.00
45.31
B


ATOM
5269
CD
GLN
B
393
19.853
23.635
31.584
1.00
51.08
B


ATOM
5270
OE1
GLN
B
393
19.854
23.508
30.330
1.00
48.97
B


ATOM
5271
NE2
GLN
B
393
20.953
23.986
32.287
1.00
50.04
B


ATOM
5272
C
GLN
B
393
17.218
26.202
30.684
1.00
28.44
B


ATOM
5273
O
GLN
B
393
18.222
26.513
30.061
1.00
27.03
B


ATOM
5274
N
TYR
B
394
16.338
27.073
31.145
1.00
29.22
B


ATOM
5275
CA
TYR
B
394
16.520
28.497
30.973
1.00
30.02
B


ATOM
5276
CB
TYR
B
394
15.188
29.211
31.204
1.00
33.65
B


ATOM
5277
CG
TYR
B
394
14.182
28.968
30.082
1.00
38.44
B


ATOM
5278
CD1
TYR
B
394
14.437
29.436
28.783
1.00
40.10
B


ATOM
5279
CE1
TYR
B
394
13.526
29.224
27.731
1.00
39.96
B


ATOM
5280
CD2
TYR
B
394
12.979
28.272
30.308
1.00
39.87
B


ATOM
5281
CE2
TYR
B
394
12.049
28.055
29.242
1.00
41.57
B


ATOM
5282
CZ
TYR
B
394
12.347
28.539
27.964
1.00
40.99
B


ATOM
5283
OH
TYR
B
394
11.497
28.329
26.901
1.00
42.49
B


ATOM
5284
C
TYR
B
394
17.567
28.970
31.969
1.00
28.81
B


ATOM
5285
O
TYR
B
394
17.621
28.495
33.104
1.00
29.44
B


ATOM
5286
N
ILE
B
395
18.415
29.884
31.534
1.00
27.82
B


ATOM
5287
CA
ILE
B
395
19.461
30.445
32.394
1.00
28.78
B


ATOM
5288
CB
ILE
B
395
20.879
30.096
31.895
1.00
27.79
B


ATOM
5289
CG2
ILE
B
395
21.130
28.599
32.026
1.00
27.52
B


ATOM
5290
CG1
ILE
B
395
21.018
30.587
30.449
1.00
27.16
B


ATOM
5291
CD1
ILE
B
395
22.403
30.578
29.928
1.00
28.45
B


ATOM
5292
C
ILE
B
395
19.331
31.961
32.341
1.00
28.96
B


ATOM
5293
O
ILE
B
395
18.778
32.522
31.371
1.00
29.24
B


ATOM
5294
N
TRP
B
396
19.855
32.622
33.374
1.00
26.93
B


ATOM
5295
CA
TRP
B
396
19.815
34.080
33.471
1.00
28.76
B


ATOM
5296
CB
TRP
B
396
18.382
34.526
33.769
1.00
30.11
B


ATOM
5297
CG
TRP
B
396
17.832
34.000
35.089
1.00
32.00
B


ATOM
5298
CD2
TRP
B
396
16.950
32.886
35.274
1.00
31.29
B


ATOM
5299
CE2
TRP
B
396
16.694
32.782
36.662
1.00
32.00
B


ATOM
5300
CE3
TRP
B
396
16.349
31.971
34.406
1.00
31.88
B


ATOM
5301
CD1
TRP
B
396
18.070
34.511
36.344
1.00
32.40
B


ATOM
5302
NE1
TRP
B
396
17.389
33.787
37.287
1.00
31.50
B


ATOM
5303
CZ2
TRP
B
396
15.863
31.794
37.203
1.00
30.40
B


ATOM
5304
CZ3
TRP
B
396
15.519
30.982
34.948
1.00
32.75
B


ATOM
5305
CH2
TRP
B
396
15.287
30.908
36.338
1.00
30.75
B


ATOM
5306
C
TRP
B
396
20.775
34.580
34.577
1.00
30.49
B


ATOM
5307
O
TRP
B
396
21.119
33.835
35.520
1.00
29.07
B


ATOM
5308
N
SER
B
397
21.229
35.823
34.441
1.00
32.27
B


ATOM
5309
CA
SER
B
397
22.139
36.411
35.420
1.00
35.37
B


ATOM
5310
CB
SER
B
397
22.674
37.749
34.908
1.00
37.46
B


ATOM
5311
OG
SER
B
397
21.614
38.595
34.465
1.00
40.94
B


ATOM
5312
C
SER
B
397
21.395
36.643
36.720
1.00
38.16
B


ATOM
5313
O
SER
B
397
20.232
37.050
36.713
1.00
35.33
B


ATOM
5314
N
SER
B
398
22.042
36.364
37.843
1.00
43.16
B


ATOM
5315
CA
SER
B
398
21.375
36.606
39.116
1.00
48.81
B


ATOM
5316
CB
SER
B
398
22.085
35.870
40.247
1.00
50.31
B


ATOM
5317
OG
SER
B
398
23.299
36.531
40.556
1.00
53.01
B


ATOM
5318
C
SER
B
398
21.447
38.126
39.363
1.00
50.81
B


ATOM
5319
O
SER
B
398
20.376
38.786
39.470
1.00
52.12
B


ATOM
5320
OXT
SER
B
398
22.592
38.643
39.431
1.00
53.13
B


ATOM
5321
O7
PYC
A
700
13.481
−0.197
26.759
1.00
19.84
A


ATOM
5322
O8
PYC
A
700
12.170
1.527
26.395
1.00
16.27
A


ATOM
5323
C1
PYC
A
700
13.296
1.007
26.457
1.00
18.42
A


ATOM
5324
C2
PYC
A
700
14.406
1.821
26.182
1.00
22.03
A


ATOM
5325
C3
PYC
A
700
15.773
1.579
26.164
1.00
22.86
A


ATOM
5326
C4
PYC
A
700
16.370
2.779
25.824
1.00
21.80
A


ATOM
5327
C5
PYC
A
700
15.373
3.748
25.630
1.00
23.81
A


ATOM
5328
N6
PYC
A
700
14.204
3.151
25.851
1.00
21.67
A


ATOM
5329
O7
PYC
B
700
22.383
33.722
8.823
1.00
18.59
B


ATOM
5330
O8
PYC
B
700
23.098
31.691
8.287
1.00
18.41
B


ATOM
5331
C1
PYC
B
700
22.534
32.498
9.085
1.00
23.28
B


ATOM
5332
C2
PYC
B
700
22.044
31.993
10.358
1.00
26.44
B


ATOM
5333
C3
PYC
B
700
21.400
32.598
11.433
1.00
29.27
B


ATOM
5334
C4
PYC
B
700
21.173
31.609
12.368
1.00
27.91
B


ATOM
5335
C5
PYC
B
700
21.672
30.396
11.870
1.00
29.09
B


ATOM
5336
N6
PYC
B
700
22.188
30.662
10.674
1.00
27.50
B


ATOM
5337
O
HOH
W
1
19.575
0.730
20.384
1.00
12.54
W


ATOM
5338
O
HOH
W
2
7.711
18.122
17.860
1.00
14.12
W


ATOM
5339
O
HOH
W
3
0.172
3.107
20.802
1.00
16.38
W


ATOM
5340
O
HOH
W
4
17.208
18.178
21.578
1.00
13.22
W


ATOM
5341
O
HOH
W
5
13.548
20.136
21.577
1.00
10.72
W


ATOM
5342
O
HOH
W
6
23.967
14.117
16.596
1.00
15.47
W


ATOM
5343
O
HOH
W
7
29.048
34.506
11.369
1.00
16.68
W


ATOM
5344
O
HOH
W
8
22.689
34.546
21.899
1.00
17.94
W


ATOM
5345
O
HOH
W
9
19.443
−4.117
18.308
1.00
16.92
W


ATOM
5346
O
HOH
W
10
4.639
29.359
14.239
1.00
16.06
W


ATOM
5347
O
HOH
W
11
13.201
25.917
22.886
1.00
15.15
W


ATOM
5348
O
HOH
W
12
13.348
13.237
18.596
1.00
12.85
W


ATOM
5349
O
HOH
W
13
13.920
14.749
15.771
1.00
14.25
W


ATOM
5350
O
HOH
W
14
13.254
2.418
33.519
1.00
19.64
W


ATOM
5351
O
HOH
W
15
9.952
−9.881
31.497
1.00
19.83
W


ATOM
5352
O
HOH
W
16
12.512
13.045
21.227
1.00
13.74
W


ATOM
5353
O
HOH
W
17
14.069
10.773
21.701
1.00
14.26
W


ATOM
5354
O
HOH
W
18
22.009
16.920
18.735
1.00
14.71
W


ATOM
5355
O
HOH
W
19
11.371
34.991
9.992
1.00
18.39
W


ATOM
5356
O
HOH
W
20
18.859
45.956
21.842
1.00
28.04
W


ATOM
5357
O
HOH
W
21
16.980
9.220
23.895
1.00
18.22
W


ATOM
5358
O
HOH
W
22
24.954
6.992
6.611
1.00
18.55
W


ATOM
5359
O
HOH
W
23
19.630
18.720
12.356
1.00
17.14
W


ATOM
5360
O
HOH
W
24
14.717
31.845
12.903
1.00
16.35
W


ATOM
5361
O
HOH
W
25
22.606
12.454
9.699
1.00
19.04
W


ATOM
5362
O
HOH
W
26
17.447
16.403
12.909
1.00
16.47
W


ATOM
5363
O
HOH
W
27
25.555
17.295
18.598
1.00
23.39
W


ATOM
5364
O
HOH
W
28
17.423
41.770
27.801
1.00
21.32
W


ATOM
5365
O
HOH
W
29
3.049
−6.899
39.037
1.00
16.07
W


ATOM
5366
O
HOH
W
30
15.225
33.564
19.567
1.00
26.87
W


ATOM
5367
O
HOH
W
31
17.841
25.008
21.866
1.00
21.46
W


ATOM
5368
O
HOH
W
32
24.759
23.206
19.981
1.00
20.53
W


ATOM
5369
O
HOH
W
33
0.715
−3.226
31.258
1.00
19.12
W


ATOM
5370
O
HOH
W
34
22.550
14.109
1.550
1.00
23.43
W


ATOM
5371
O
HOH
W
35
0.856
31.822
19.591
1.00
23.52
W


ATOM
5372
O
HOH
W
36
1.110
13.342
16.458
1.00
24.25
W


ATOM
5373
O
HOH
W
37
18.003
41.273
15.280
1.00
19.99
W


ATOM
5374
O
HOH
W
38
22.078
19.725
12.381
1.00
16.80
W


ATOM
5375
O
HOH
W
39
13.814
6.768
31.483
1.00
18.36
W


ATOM
5376
O
HOH
W
40
18.317
−8.777
5.412
1.00
28.08
W


ATOM
5377
O
HOH
W
41
21.219
22.343
12.892
1.00
19.62
W


ATOM
5378
O
HOH
W
42
18.656
30.286
26.470
1.00
21.12
W


ATOM
5379
O
HOH
W
43
6.406
23.678
23.186
1.00
21.41
W


ATOM
5380
O
HOH
W
44
20.570
19.256
19.409
1.00
15.70
W


ATOM
5381
O
HOH
W
45
28.511
29.966
13.328
1.00
21.41
W


ATOM
5382
O
HOH
W
46
1.841
9.384
30.007
1.00
21.68
W


ATOM
5383
O
HOH
W
47
29.829
27.435
13.900
1.00
26.70
W


ATOM
5384
O
HOH
W
48
2.476
22.051
16.314
1.00
18.26
W


ATOM
5385
O
HOH
W
49
19.041
14.268
26.973
1.00
22.84
W


ATOM
5386
O
HOH
W
50
7.480
−12.341
24.926
1.00
24.22
W


ATOM
5387
O
HOH
W
51
16.332
39.301
13.526
1.00
16.61
W


ATOM
5388
O
HOH
W
52
16.242
−14.165
15.655
1.00
26.55
W


ATOM
5389
O
HOH
W
53
25.929
2.494
23.401
1.00
29.28
W


ATOM
5390
O
HOH
W
54
15.339
24.525
23.133
1.00
23.56
W


ATOM
5391
O
HOH
W
55
19.012
15.868
21.651
1.00
18.59
W


ATOM
5392
O
HOH
W
56
23.149
52.942
20.995
1.00
33.11
W


ATOM
5393
O
HOH
W
57
7.964
14.521
11.807
1.00
33.54
W


ATOM
5394
O
HOH
W
58
17.164
−13.916
39.473
1.00
21.00
W


ATOM
5395
O
HOH
W
59
24.174
0.430
10.985
1.00
21.07
W


ATOM
5396
O
HOH
W
60
15.268
33.839
16.997
1.00
14.54
W


ATOM
5397
O
HOH
W
61
15.858
−13.374
29.266
1.00
19.95
W


ATOM
5398
O
HOH
W
62
15.585
18.782
24.703
1.00
21.00
W


ATOM
5399
O
HOH
W
63
22.038
14.618
24.718
1.00
21.50
W


ATOM
5400
O
HOH
W
65
7.445
41.308
2.151
1.00
24.44
W


ATOM
5401
O
HOH
W
66
20.460
32.978
22.744
1.00
25.39
W


ATOM
5402
O
HOH
W
67
8.615
42.215
4.941
1.00
28.44
W


ATOM
5403
O
HOH
W
68
22.882
−5.251
28.140
1.00
22.59
W


ATOM
5404
O
HOH
W
69
23.585
1.299
22.927
1.00
22.06
W


ATOM
5405
O
HOH
W
70
14.678
−1.833
7.424
1.00
24.57
W


ATOM
5406
O
HOH
W
71
22.568
36.211
−6.316
1.00
23.20
W


ATOM
5407
O
HOH
W
72
29.977
53.386
17.924
1.00
26.00
W


ATOM
5408
O
HOH
W
73
5.079
30.480
22.852
1.00
30.93
W


ATOM
5409
O
HOH
W
74
10.002
−18.853
43.509
1.00
30.94
W


ATOM
5410
O
HOH
W
75
4.640
26.616
3.081
1.00
28.98
W


ATOM
5411
O
HOH
W
76
2.119
35.716
0.907
1.00
22.45
W


ATOM
5412
O
HOH
W
77
34.942
41.656
0.293
1.00
24.03
W


ATOM
5413
O
HOH
W
78
21.092
17.895
−2.608
1.00
32.20
W


ATOM
5414
O
HOH
W
79
26.638
6.888
3.483
1.00
32.81
W


ATOM
5415
O
HOH
W
80
24.482
−21.567
36.531
1.00
35.97
W


ATOM
5416
O
HOH
W
81
2.934
33.607
20.748
1.00
23.15
W


ATOM
5417
O
HOH
W
82
7.478
3.451
5.218
1.00
30.66
W


ATOM
5418
O
HOH
W
83
−1.102
37.264
2.808
1.00
31.26
W


ATOM
5419
O
HOH
W
84
24.889
4.773
30.816
1.00
25.16
W


ATOM
5420
O
HOH
W
85
19.436
35.034
29.941
1.00
29.97
W


ATOM
5421
O
HOH
W
86
−3.763
−3.330
9.798
1.00
33.95
W


ATOM
5422
O
HOH
W
87
0.070
29.723
−4.420
1.00
20.98
W


ATOM
5423
O
HOH
W
88
21.317
25.487
15.130
1.00
19.92
W


ATOM
5424
O
HOH
W
89
29.507
9.736
12.251
1.00
31.78
W


ATOM
5425
O
HOH
W
90
16.712
38.960
21.105
1.00
21.71
W


ATOM
5426
O
HOH
W
91
−3.537
41.000
5.604
1.00
27.09
W


ATOM
5427
O
HOH
W
92
2.058
28.838
3.074
1.00
30.16
W


ATOM
5428
O
HOH
W
93
22.828
38.394
30.972
1.00
28.01
W


ATOM
5429
O
HOH
W
94
9.284
22.193
26.828
1.00
23.69
W


ATOM
5430
O
HOH
W
95
3.985
−18.017
36.098
1.00
32.32
W


ATOM
5431
O
HOH
W
96
28.767
6.441
17.253
1.00
30.51
W


ATOM
5432
O
HOH
W
97
39.368
35.015
19.824
1.00
34.80
W


ATOM
5433
O
HOH
W
98
19.002
20.208
30.585
1.00
25.43
W


ATOM
5434
O
HOH
W
99
0.860
3.535
41.135
1.00
31.34
W


ATOM
5435
O
HOH
W
100
−3.957
−7.281
36.440
1.00
22.79
W


ATOM
5436
O
HOH
W
101
25.636
11.661
20.100
1.00
23.96
W


ATOM
5437
O
HOH
W
102
14.563
26.171
27.857
1.00
25.50
W


ATOM
5438
O
HOH
W
103
13.033
9.787
31.788
1.00
19.12
W


ATOM
5439
O
HOH
W
104
13.671
−22.210
45.078
1.00
32.32
W


ATOM
5440
O
HOH
W
105
15.309
−1.814
4.838
1.00
25.74
W


ATOM
5441
O
HOH
W
106
23.286
17.123
22.699
1.00
32.55
W


ATOM
5442
O
HOH
W
107
24.172
11.452
22.572
1.00
15.83
W


ATOM
5443
O
HOH
W
108
8.296
7.770
2.718
1.00
43.73
W


ATOM
5444
O
HOH
W
109
2.724
8.988
22.864
1.00
23.77
W


ATOM
5445
O
HOH
W
110
21.667
−4.838
25.392
1.00
18.94
W


ATOM
5446
O
HOH
W
111
19.054
36.694
−8.037
1.00
31.13
W


ATOM
5447
O
HOH
W
112
19.954
42.665
−4.614
1.00
33.84
W


ATOM
5448
O
HOH
W
113
24.939
−8.048
22.820
1.00
30.66
W


ATOM
5449
O
HOH
W
114
3.058
13.336
34.670
1.00
36.40
W


ATOM
5450
O
HOH
W
115
15.948
44.074
27.434
1.00
22.99
W


ATOM
5451
O
HOH
W
116
13.993
23.239
−11.578
1.00
30.94
W


ATOM
5452
O
HOH
W
117
−5.904
25.585
1.138
1.00
28.47
W


ATOM
5453
O
HOH
W
118
35.355
42.252
13.575
1.00
35.41
W


ATOM
5454
O
HOH
W
119
−1.531
5.644
16.680
1.00
39.62
W


ATOM
5455
O
HOH
W
120
26.452
15.032
29.043
1.00
40.51
W


ATOM
5456
O
HOH
W
121
25.201
−5.176
23.848
1.00
32.54
W


ATOM
5457
O
HOH
W
122
−0.624
27.222
3.157
1.00
36.61
W


ATOM
5458
O
HOH
W
123
10.721
−16.970
44.703
1.00
30.04
W


ATOM
5459
O
HOH
W
124
27.180
9.713
19.059
1.00
21.96
W


ATOM
5460
O
HOH
W
125
14.433
−8.850
5.932
1.00
31.47
W


ATOM
5461
O
HOH
W
126
23.876
24.249
−2.724
1.00
21.42
W


ATOM
5462
O
HOH
W
127
−0.948
32.985
−0.899
1.00
24.62
W


ATOM
5463
O
HOH
W
128
7.801
−16.307
33.953
1.00
31.29
W


ATOM
5464
O
HOH
W
129
20.410
20.380
23.747
1.00
33.65
W


ATOM
5465
O
HOH
W
131
14.030
44.772
0.063
1.00
26.62
W


ATOM
5466
O
HOH
W
132
30.159
50.256
−4.517
1.00
32.29
W


ATOM
5467
O
HOH
W
133
26.508
21.268
2.601
1.00
28.60
W


ATOM
5468
O
HOH
W
134
11.823
41.645
14.572
1.00
18.92
W


ATOM
5469
O
HOH
W
135
24.762
42.790
2.730
1.00
23.32
W


ATOM
5470
O
HOH
W
137
22.040
19.987
−4.228
1.00
46.10
W


ATOM
5471
O
HOH
W
138
42.354
44.107
2.423
1.00
43.23
W


ATOM
5472
O
HOH
W
139
−1.546
4.964
19.391
1.00
23.33
W


ATOM
5473
O
HOH
W
140
17.786
34.186
17.907
1.00
21.15
W


ATOM
5474
O
HOH
W
141
23.942
−10.433
44.626
1.00
28.83
W


ATOM
5475
O
HOH
W
142
14.103
−11.214
39.418
1.00
26.66
W


ATOM
5476
O
HOH
W
143
6.494
45.366
−3.941
1.00
37.81
W


ATOM
5477
O
HOH
W
144
1.145
−11.093
21.122
1.00
30.40
W


ATOM
5478
O
HOH
W
145
24.188
−1.703
23.090
1.00
37.48
W


ATOM
5479
O
HOH
W
146
19.956
18.125
42.965
1.00
31.86
W


ATOM
5480
O
HOH
W
147
11.530
38.431
14.796
1.00
37.74
W


ATOM
5481
O
HOH
W
148
34.094
42.825
15.848
1.00
31.85
W


ATOM
5482
O
HOH
W
149
−1.116
21.727
17.827
1.00
25.07
W


ATOM
5483
O
HOH
W
150
36.884
48.719
−1.273
1.00
29.60
W


ATOM
5484
O
HOH
W
151
−0.907
−5.418
45.753
1.00
41.36
W


ATOM
5485
O
HOH
W
153
14.564
36.418
16.445
1.00
32.21
W


ATOM
5486
O
HOH
W
154
25.471
−16.031
34.304
1.00
40.29
W


ATOM
5487
O
HOH
W
155
9.101
−22.454
38.744
1.00
35.78
W


ATOM
5488
O
HOH
W
156
−2.350
−1.857
34.291
1.00
35.57
W


ATOM
5489
O
HOH
W
157
13.668
14.445
11.210
1.00
34.96
W


ATOM
5490
O
HOH
W
158
19.352
41.229
−2.423
1.00
28.29
W


ATOM
5491
O
HOH
W
159
−0.734
−1.890
44.440
1.00
31.74
W


ATOM
5492
O
HOH
W
160
23.964
21.734
−3.660
1.00
31.08
W


ATOM
5493
O
HOH
W
161
−10.017
−8.814
19.418
1.00
40.16
W


ATOM
5494
O
HOH
W
162
17.539
−6.204
4.702
1.00
24.11
W


ATOM
5495
O
HOH
W
163
29.741
−5.988
32.677
1.00
31.42
W


ATOM
5496
O
HOH
W
164
28.001
−9.645
21.744
1.00
33.82
W


ATOM
5497
O
HOH
W
165
0.760
40.602
11.593
1.00
30.23
W


ATOM
5498
O
HOH
W
166
18.668
17.337
25.714
1.00
41.07
W


ATOM
5499
O
HOH
W
168
7.720
41.267
12.098
1.00
26.51
W


ATOM
5500
O
HOH
W
169
4.377
0.505
6.699
1.00
49.69
W


ATOM
5501
O
HOH
W
170
16.156
12.924
6.910
1.00
33.21
W


ATOM
5502
O
HOH
W
171
17.725
43.920
−0.551
1.00
24.17
W


ATOM
5503
O
HOH
W
172
0.459
−12.235
47.031
1.00
33.75
W


ATOM
5504
O
HOH
W
173
30.732
13.058
15.124
1.00
29.90
W


ATOM
5505
O
HOH
W
174
11.356
35.894
17.493
1.00
25.46
W


ATOM
5506
O
HOH
W
175
23.779
25.505
26.926
1.00
39.30
W


ATOM
5507
O
HOH
W
176
−0.665
7.937
15.517
1.00
30.68
W


ATOM
5508
O
HOH
W
177
33.642
17.965
11.163
1.00
49.77
W


ATOM
5509
O
HOH
W
178
12.538
−15.968
22.560
1.00
25.37
W


ATOM
5510
O
HOH
W
179
18.776
−10.986
49.211
1.00
55.81
W


ATOM
5511
O
HOH
W
180
0.483
5.084
28.763
1.00
37.57
W


ATOM
5512
O
HOH
W
181
29.115
60.930
4.087
1.00
56.19
W


ATOM
5513
O
HOH
W
182
9.546
−3.129
6.126
1.00
43.37
W


ATOM
5514
O
HOH
W
183
7.223
−10.154
45.111
1.00
33.68
W


ATOM
5515
O
HOH
W
184
21.609
22.844
22.266
1.00
23.54
W


ATOM
5516
O
HOH
W
185
25.045
40.463
33.659
1.00
43.23
W


ATOM
5517
O
HOH
W
186
2.798
19.840
23.221
1.00
28.72
W


ATOM
5518
O
HOH
W
187
35.149
45.916
19.323
1.00
46.96
W


ATOM
5519
O
HOH
W
188
16.850
45.647
4.603
1.00
36.05
W


ATOM
5520
O
HOH
W
189
31.164
12.579
2.121
1.00
36.80
W


ATOM
5521
O
HOH
W
190
4.482
14.506
36.580
1.00
36.65
W


ATOM
5522
O
HOH
W
191
30.060
21.331
25.530
1.00
28.14
W


ATOM
5523
O
HOH
W
192
0.740
−8.650
24.454
1.00
29.26
W


ATOM
5524
O
HOH
W
193
29.066
49.529
7.946
1.00
25.56
W


ATOM
5525
O
HOH
W
194
15.980
−15.806
30.435
1.00
38.32
W


ATOM
5526
O
HOH
W
195
14.674
−1.144
42.845
1.00
38.18
W


ATOM
5527
O
HOH
W
196
30.078
13.112
22.025
1.00
50.79
W


ATOM
5528
O
HOH
W
197
13.401
−13.755
45.484
1.00
36.75
W


ATOM
5529
O
HOH
W
198
−2.478
−8.276
41.991
1.00
27.69
W


ATOM
5530
O
HOH
W
199
24.180
−4.901
21.333
1.00
27.65
W


ATOM
5531
O
HOH
W
200
30.519
11.752
9.670
1.00
31.30
W


ATOM
5532
O
HOH
W
201
27.815
−1.263
26.975
1.00
34.58
W


ATOM
5533
O
HOH
W
202
39.243
27.120
26.384
1.00
42.73
W


ATOM
5534
O
HOH
W
203
7.031
39.708
−8.535
1.00
43.10
W


ATOM
5535
O
HOH
W
205
26.957
−11.442
11.948
1.00
32.18
W


ATOM
5536
O
HOH
W
206
2.139
25.701
3.586
1.00
24.66
W


ATOM
5537
O
HOH
W
207
−2.639
−5.829
43.496
1.00
20.75
W


ATOM
5538
O
HOH
W
208
10.766
25.886
23.937
1.00
26.10
W


ATOM
5539
O
HOH
W
209
17.856
−15.863
41.163
1.00
24.60
W


ATOM
5540
O
HOH
W
210
29.134
9.212
17.294
1.00
27.68
W


ATOM
5541
O
HOH
W
211
23.343
1.812
25.289
1.00
23.29
W


ATOM
5542
O
HOH
W
212
27.741
54.838
9.595
1.00
24.89
W


ATOM
5543
O
HOH
W
213
33.081
23.635
3.685
1.00
22.39
W


ATOM
5544
O
HOH
W
214
20.368
36.865
31.789
1.00
31.59
W


ATOM
5545
O
HOH
W
215
20.879
18.165
21.790
1.00
29.57
W


ATOM
5546
O
HOH
W
216
1.269
21.473
13.930
1.00
32.04
W


ATOM
5547
O
HOH
W
217
29.881
10.423
14.748
1.00
28.03
W


ATOM
5548
O
HOH
W
218
18.056
−13.596
17.921
1.00
31.04
W


ATOM
5549
O
HOH
W
219
1.991
−12.889
43.464
1.00
35.32
W


ATOM
5550
O
HOH
W
220
15.759
−12.503
41.417
1.00
28.33
W


ATOM
5551
O
HOH
W
221
25.820
5.877
28.354
1.00
28.52
W


ATOM
5552
O
HOH
W
222
4.982
32.970
22.441
1.00
39.46
W


ATOM
5553
O
HOH
W
223
17.476
30.887
28.958
1.00
26.47
W


ATOM
5554
O
HOH
W
224
11.291
41.349
1.417
1.00
37.24
W


ATOM
5555
O
HOH
W
225
29.880
51.712
9.177
1.00
29.75
W


ATOM
5556
O
HOH
W
226
40.211
32.579
20.654
1.00
30.21
W


ATOM
5557
O
HOH
W
227
22.885
5.920
5.241
1.00
41.08
W


ATOM
5558
O
HOH
W
228
−6.490
28.305
6.799
1.00
30.25
W


ATOM
5559
O
HOH
W
229
17.302
−1.431
42.690
1.00
36.18
W


ATOM
5560
O
HOH
W
230
0.125
−11.638
23.724
1.00
35.78
W


ATOM
5561
O
HOH
W
231
8.507
23.950
24.522
1.00
32.56
W


ATOM
5562
O
HOH
W
232
26.160
−1.690
20.722
1.00
29.53
W


ATOM
5563
O
HOH
W
233
13.398
42.760
16.890
1.00
27.10
W


ATOM
5564
O
HOH
W
234
22.357
40.731
32.179
1.00
30.74
W


ATOM
5565
O
HOH
W
235
11.336
−23.140
44.359
1.00
36.30
W


ATOM
5566
O
HOH
W
236
17.508
38.327
−9.628
1.00
35.63
W


ATOM
5567
O
HOH
W
237
8.472
16.550
1.343
1.00
32.74
W


ATOM
5568
O
HOH
W
238
31.364
23.487
27.239
1.00
31.19
W


ATOM
5569
O
HOH
W
239
30.948
6.023
4.210
1.00
37.30
W


ATOM
5570
O
HOH
W
240
26.615
45.872
30.472
1.00
39.41
W


ATOM
5571
O
HOH
W
241
19.326
46.651
5.986
1.00
24.47
W


ATOM
5572
O
HOH
W
242
40.219
38.031
2.750
1.00
41.15
W


ATOM
5573
O
HOH
W
243
7.631
6.447
5.192
1.00
32.07
W


ATOM
5574
O
HOH
W
244
14.947
−4.945
5.698
1.00
46.51
W


ATOM
5575
O
HOH
W
245
29.878
11.916
6.941
1.00
37.43
W


ATOM
5576
O
HOH
W
246
13.119
−15.352
25.333
1.00
31.96
W


ATOM
5577
O
HOH
W
247
26.386
−7.472
25.343
1.00
31.30
W


ATOM
5578
O
HOH
W
248
30.165
34.873
−2.447
1.00
37.59
W


ATOM
5579
O
HOH
W
249
24.264
20.123
21.179
1.00
44.76
W


ATOM
5580
O
HOH
W
250
33.782
14.688
27.127
1.00
48.15
W


ATOM
5581
O
HOH
W
251
15.163
49.239
20.591
1.00
35.54
W


ATOM
5582
O
HOH
W
252
14.290
3.113
0.051
1.00
44.21
W


ATOM
5583
O
HOH
W
253
29.234
14.802
36.478
1.00
37.15
W


ATOM
5584
O
HOH
W
254
1.939
17.834
27.020
1.00
36.48
W


ATOM
5585
O
HOH
W
255
39.232
22.885
9.402
1.00
35.89
W


ATOM
5586
O
HOH
W
256
16.614
47.670
30.134
1.00
30.62
W


ATOM
5587
O
HOH
W
257
32.555
−3.038
6.133
1.00
35.15
W


ATOM
5588
O
HOH
W
258
−2.289
19.140
4.977
1.00
39.69
W


ATOM
5589
O
HOH
W
259
1.553
−17.001
34.997
1.00
42.78
W


ATOM
5590
O
HOH
W
260
15.155
12.430
41.749
1.00
32.11
W


ATOM
5591
O
HOH
W
261
13.134
22.891
29.312
1.00
32.55
W


ATOM
5592
O
HOH
W
262
1.356
29.398
0.186
1.00
39.92
W


ATOM
5593
O
HOH
W
263
15.490
−2.292
1.286
1.00
33.40
W


ATOM
5594
O
HOH
W
264
24.801
−17.578
28.195
1.00
37.92
W


ATOM
5595
O
HOH
W
265
40.969
36.681
18.857
1.00
34.76
W


ATOM
5596
O
HOH
W
266
−0.099
−7.970
26.768
1.00
37.14
W


ATOM
5597
O
HOH
W
267
−5.600
−4.895
36.300
1.00
28.04
W


ATOM
5598
O
HOH
W
268
18.635
53.684
14.149
1.00
39.24
W


ATOM
5599
O
HOH
W
269
21.160
−22.110
44.292
1.00
31.93
W


ATOM
5600
O
HOH
W
270
16.653
8.689
44.684
1.00
35.93
W


ATOM
5601
O
HOH
W
271
8.044
30.381
−7.362
1.00
36.73
W


ATOM
5602
O
HOH
W
272
1.315
11.442
31.274
1.00
36.98
W


ATOM
5603
O
HOH
W
273
8.987
−21.995
41.278
1.00
43.76
W


ATOM
5604
O
HOH
W
274
27.222
−8.171
44.730
1.00
34.99
W


ATOM
5605
O
HOH
W
275
−3.218
10.852
23.922
1.00
38.19
W


ATOM
5606
O
HOH
W
276
16.524
33.011
27.952
1.00
36.27
W


ATOM
5607
O
HOH
W
277
13.566
−15.726
47.855
1.00
39.75
W


ATOM
5608
O
HOH
W
278
9.788
28.090
22.420
1.00
36.95
W


ATOM
5609
O
HOH
W
279
2.038
−0.985
42.549
1.00
29.62
W


ATOM
5610
O
HOH
W
280
−4.926
20.131
22.952
1.00
40.42
W


ATOM
5611
O
HOH
W
281
13.468
39.982
16.142
1.00
40.09
W


ATOM
5612
O
HOH
W
282
30.531
3.268
28.753
1.00
45.55
W


ATOM
5613
O
HOH
W
283
20.900
−19.423
51.054
1.00
38.60
W


ATOM
5614
O
HOH
W
284
31.426
44.515
−6.883
1.00
34.68
W


ATOM
5615
O
HOH
W
285
13.964
35.075
−10.523
1.00
43.27
W


ATOM
5616
O
HOH
W
286
−0.116
39.809
13.953
1.00
34.96
W


ATOM
5617
O
HOH
W
287
21.093
0.363
45.524
1.00
38.08
W


ATOM
5618
O
HOH
W
288
3.056
26.921
0.409
1.00
37.24
W


ATOM
5619
O
HOH
W
289
15.649
14.637
8.810
1.00
41.00
W


ATOM
5620
O
HOH
W
290
10.922
30.495
22.729
1.00
34.18
W


ATOM
5621
O
HOH
W
291
31.775
−6.708
30.429
1.00
43.95
W


ATOM
5622
O
HOH
W
292
−1.428
26.105
1.010
1.00
36.92
W


ATOM
5623
O
HOH
W
293
24.971
−17.752
42.875
1.00
35.76
W


ATOM
5624
O
HOH
W
294
23.232
25.011
29.967
1.00
40.39
W


ATOM
5625
O
HOH
W
295
12.419
35.901
20.319
1.00
38.87
W


ATOM
5626
O
HOH
W
296
11.317
15.747
36.016
1.00
40.10
W


ATOM
5627
O
HOH
W
297
3.160
−3.418
46.260
1.00
42.94
W


ATOM
5628
O
HOH
W
298
−4.846
−3.201
33.946
1.00
41.88
W


ATOM
5629
O
HOH
W
299
1.910
−14.630
12.849
1.00
47.08
W


ATOM
5630
O
HOH
W
300
10.291
−5.920
6.807
1.00
46.76
W


ATOM
5631
O
HOH
W
301
26.461
−10.577
44.997
1.00
36.54
W


ATOM
5632
O
HOH
W
302
−4.047
24.599
4.391
1.00
46.45
W


ATOM
5633
O
HOH
W
303
14.690
25.613
32.659
1.00
51.09
W


ATOM
5634
O
HOH
W
304
8.384
20.073
28.849
1.00
45.29
W


ATOM
5635
O
HOH
W
305
9.442
12.765
10.381
1.00
42.60
W


ATOM
5636
O
HOH
W
306
37.334
24.155
12.850
1.00
34.80
W


ATOM
5637
O
HOH
W
307
23.914
−20.195
27.220
1.00
43.22
W


ATOM
5638
O
HOH
W
308
0.684
−13.695
20.130
1.00
34.10
W


ATOM
5639
O
HOH
W
309
16.030
−13.142
44.203
1.00
38.82
W


ATOM
5640
O
HOH
W
310
20.937
44.215
−1.084
1.00
40.20
W


ATOM
5641
O
HOH
W
311
−3.355
−4.210
38.115
1.00
32.38
W


ATOM
5642
O
HOH
W
312
−0.193
−10.941
13.004
1.00
44.80
W


ATOM
5643
O
HOH
W
313
−1.398
−9.899
9.421
1.00
42.24
W


ATOM
5644
O
HOH
W
314
32.082
54.976
16.970
1.00
43.72
W


ATOM
5645
O
HOH
W
315
10.534
−14.518
25.108
1.00
38.70
W


ATOM
5646
O
HOH
W
316
15.222
−14.044
26.095
1.00
36.31
W


ATOM
5647
O
HOH
W
317
39.673
32.342
23.136
1.00
43.10
W


ATOM
5648
O
HOH
W
318
3.077
−11.273
47.472
1.00
43.71
W


ATOM
5649
O
HOH
W
319
0.005
11.290
14.724
1.00
46.16
W


ATOM
5650
O
HOH
W
320
12.121
14.747
40.180
1.00
43.75
W


ATOM
5651
O
HOH
W
321
16.889
20.109
40.511
1.00
41.01
W


ATOM
5652
O
HOH
W
322
32.369
12.818
17.426
1.00
35.81
W


ATOM
5653
O
HOH
W
323
26.413
13.788
−5.898
1.00
52.65
W


ATOM
5654
O
HOH
W
324
20.779
52.316
24.144
1.00
44.47
W


ATOM
5655
O
HOH
W
325
2.891
11.216
27.584
1.00
39.00
W


ATOM
5656
O
HOH
W
326
17.056
−19.095
14.177
1.00
41.89
W


ATOM
5657
O
HOH
W
327
30.349
−2.177
26.445
1.00
51.16
W


ATOM
5658
O
HOH
W
328
24.569
18.609
−6.806
1.00
41.46
W


ATOM
5659
O
HOH
W
329
8.480
−13.826
27.951
1.00
43.20
W


ATOM
5660
O
HOH
W
330
31.641
9.093
10.231
1.00
41.86
W


ATOM
5661
O
HOH
W
331
10.366
44.118
2.341
1.00
39.86
W


ATOM
5662
O
HOH
W
332
36.931
48.743
3.962
1.00
35.49
W


ATOM
5663
O
HOH
W
333
26.668
19.551
28.746
1.00
45.32
W


ATOM
5664
O
HOH
W
334
16.843
45.042
−3.051
1.00
42.25
W


ATOM
5665
O
HOH
W
335
42.140
50.797
−2.692
1.00
41.41
W


ATOM
5666
O
HOH
W
336
40.032
30.338
30.316
1.00
46.04
W


ATOM
5667
O
HOH
W
337
26.941
16.456
40.201
1.00
42.67
W


ATOM
5668
O
HOH
W
338
3.053
−16.424
17.722
1.00
46.61
W


ATOM
5669
O
HOH
W
339
−2.774
−5.761
28.409
1.00
39.39
W


ATOM
5670
O
HOH
W
340
34.391
42.225
18.425
1.00
36.32
W


ATOM
5671
O
HOH
W
341
34.199
56.068
4.324
1.00
41.66
W


ATOM
5672
O
HOH
W
342
20.148
−7.147
−1.451
1.00
34.79
W


ATOM
5673
O
HOH
W
343
29.115
54.457
19.899
1.00
40.93
W


ATOM
5674
O
HOH
W
344
17.743
43.968
−5.079
1.00
43.89
W


ATOM
5675
O
HOH
W
345
36.280
50.949
−2.561
1.00
42.66
W


ATOM
5676
O
HOH
W
346
7.128
19.648
−1.124
1.00
41.68
W


ATOM
5677
O
HOH
W
347
8.547
14.097
36.084
1.00
36.23
W


ATOM
5678
O
HOH
W
348
37.654
44.030
27.926
1.00
50.15
W


ATOM
5679
O
HOH
W
349
33.172
29.124
30.667
1.00
45.70
W


ATOM
5680
O
HOH
W
350
27.741
27.513
−12.391
1.00
53.77
W


ATOM
5681
O
HOH
W
351
8.225
−0.249
46.162
1.00
41.14
W


END









REFERENCES
The following references are hereby incorporated by reference:

    1. Fisher, G. H., Exs. 85:109-118, 1998.
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    14. Jones et al., Acta Crystallography A47:110-119, 1991.
    15. Walters et al., Drug Discovery Today 3(4):160-178, 1998.
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## Claims

1. A crystal of Trypanosoma cruzi proline racemase form A (TcPRACA) in complex with pyrrole-2-carboxylic acid, wherein the TcPRACA consists of the amino acid sequence of SEQ ID NO:3, except methionine is replaced with selenomethionine, and wherein the crystal has monoclinic space group C2 with unit cell dimensions: a=131.1528 Å, b=91.2088 Å, c=85.9827 Å, and β=126.5217°.

2. A composition comprising the crystal of claim 1 and a salt.

3. The crystal of claim 1, wherein the crystal diffracts X-rays for a determination of structure coordinates of the TcPRACA to a resolution of 2.1 Å.

4. The crystal of claim 3, wherein the structure coordinates of the TcPRACA are defined by the data set of Table 2.

5. A method of making a crystal comprising TcPRACA, said method comprising:
providing TcPRACA at a concentration of 5-6 mg/ml and pyrrole-2-carboxylic acid at a concentration of 1 mM in 25 mM sodium acetate, pH 5.2 to provide a protein solution, wherein the TcPRACA consists of the amino acid sequence of SEQ ID NO:3, except methionine is replaced with selenomethionine;
mixing the protein solution with an equal volume of a buffer comprising 0.2 M ammonium acetate, 50 mM trisodium citrate dihydrate, pH 5.6, and 15% (w/v) polyethylene glycol 4000; and
allowing a crystal comprising the TcPRACA in complex with pyrrole-2-carboxylic acid to form, wherein the crystal has monoclinic space group C2 with unit cell dimensions: a=131.1528 Å, b=91.2088 Å, c=85.9827 Å, and β=126.5217°.

6. A crystal of Trypanosoma cruzi proline racemase form A (TcPRACA), wherein the TcPRACA consists of the amino acid sequence of SEQ ID NO:3, and wherein the crystal has monoclinic space group C2 with unit cell dimensions: a=134.0651 Å, b=91.618 Å, c=86.0307 Å, and β=123.3735°.

7. A composition comprising the crystal of claim 6 and a salt.

8. The crystal of claim 6, wherein the crystal exhibits the diffraction data listed in Table 1.