# Patent

## Title
Small molecules modulator of epigenetic regulation and their therapeutic applications

## Abstract

Disclosed are methods and compositions for modulating the function of transcription factors, especially transcription factors that recruit epigenetic regulators (histone modifying enzymes) to specific DNA promoters. The targeted transcription factors include but are not limited to the myocyte enhancing factor (MEF2), the forkhead/winged helix transcription factor FOXP3 and the transcription factor GATA3. Also disclosed are small molecule modulators of MEF2 and its associated factors that include but not limited to histone deacetylases (HDACs), p300/CBP and Cabin1 and the therapeutic applications thereof.

## Background
CROSS-REFERENCE TO RELATED APPLICATIONS
This application is a continuation of U.S. Non-provisional application Ser. No. 13/801,380, filed on Mar. 13, 2013, which is a divisional of U.S. Non-provisional application Ser. No. 12/613,521, filed on Nov. 5, 2009, now U.S. Pat. No. 8,697,729, issued on Apr. 15, 2014 which claims the benefit of U.S. Provisional Application No. 61/111,189, filed on Nov. 5, 2008, and Provisional Application No. 61/246,934, filed on Sep. 29, 2009. The above provisional applications are hereby incorporated herein by reference.


STATEMENT REGARDING FEDERALLY SPONSORED RESEARCH AND DEVELOPMENT
This invention was made with support in part by the following grants from NIH R21AI49905, RO1HL076334, and RC1DA028790. Therefore, the U.S. government has certain rights.


FIELD OF THE INVENTION
The invention relates generally to the field of molecular medicine. In particular, the invention pertains to methods and compositions for modulating the function of transcription factors, especially transcription factors that recruit epigenetic regulators (histone modifying enzymes) to specific DNA promoters. The targeted transcription factors include but are not limited to the myocyte enhancing factor (MEF2), the forkhead/winged helix transcription factor FOXP3 and the transcription factor GATA3. More particularly, the invention pertains to small molecule modulators of MEF2 and its associated factors that include but not limited to histone deacetylases (HDACs), p300/CBP and Cabin1 and the therapeutic applications thereof.
BACKGROUND OF THE INVENTION
This invention relates to the use of small molecules for modulating the functions of transcription factors that are associated with certain diseases. Transcription factors are proteins that bind to specific DNA sequences and regulate gene expression either directly or through associated proteins such as co-activators and co-repressors, or by recruiting histone modifying enzymes such as histone acetyltransferases (HATs) and histone deacetylases (HDACs). Transcription factors play key roles in many biological processes by ensuring the appropriate level of gene expression. They can also be associated with certain disease states, if their ability to regulate transcription is aberrantly modified. The identification and development of small molecules that can selectively modulate the function of certain transcription factors, therefore, can lead to potentially new therapeutic applications. This invention is based on two basic ideas. One is to develop small molecules that bind a specific transcription factors such as MEF2, FOXP3 and GATA3 and modulate its interaction with transcription co-activators and co-repressors. The other is to develop small molecules to block the recruitment of HAT (such as p300 and CBP) and HDACs and other histone modifying enzymes (such as histone methyltransferases, and demethylases, DNA methyltransferases) and chromatin remodeling machineries to specific regions of chromatin.
In particular, this invention relates to the myocyte enhancer factor-2 (MEF2) which plays critical roles in the development and adaptive responses of the muscle, immune and nervous systems (Flavell et al., 2006; Kim et al., 2008; Mao et al., 1999; McKinsey et al., 2002; Pan et al., 2004; Potthoff and Olson, 2007; Youn and Liu, 2000; Youn et al., 1999). MEF2 has been implicated as a key regulator of hypertrophic responses in heart muscle cells. Heart hypertrophy induced by pathological stimuli can lead to heart failure in many forms of cardiovascular diseases.
MEF2 generally defines a family of transcription factors with four members: MEF2A, MEF2B, MEF2C and MEF2D. The importance of their function has been demonstrated in detail through the use of murine and Drosophila genetics (Potthoff and Olson, 2007). MEF2, in skeletal muscles where it was initially identified, together with myogenic basic helix-loop-helix transcription factors such as MyoD, promotes and maintains myogenesis (Molkentin and Olson, 1996). MEF2A, one member of the MEF2 family, has recently been coined as the “heart attack gene” because a mutation in this protein is linked to coronary artery disease (CAD) and myocardial infarction (MI) (Wang et al., 2003). These findings underlie a critical role of MEF2 in human heart diseases (Kim et al., 2008; Wei et al., 2008; Zhang et al., 2002).
MEF2 is now known to be a general transcriptional factor in many other cell types. For instance, MEF2 is one of the important transcriptional factors for mediating calcium signaling in lymph system development}(Pan et al., 2004; Youn and Liu, 2000; Youn et al., 1999). MEF2 regulates cytokine expression and immune responses. MEF2 also regulates transcription programs underlying neuronal survival and synaptic remodeling (Chen and Cepko, 2009; Flavell et al., 2006; Flavell and Greenberg, 2008; Flavell et al., 2008; Mao et al., 1999; Morrow et al., 2008; Shalizi et al., 2006; Shalizi and Bonni, 2005; Yang et al., 2009). These observations suggest that small molecules that modulate MEF2 function could have therapeutic effect in cardiac hypertrophy and heart failure, autoimmune diseases and transplant rejection, neurodegenerative diseases and pathological impairment of learning and memory (Fischer et al., 2007; Stefanko et al., 2009).
Inside cells, the action of MEF2 includes three distinct steps: (i) transcriptional repression; (ii) calcium-dependent de-repression; and (iii) transcription activation. Transcriptional repression by MEF2 depends on its association with a variety of transcriptional co-repressors with intrinsic or associated histone deacetylase (HDAC) activity. In T cells, MEF2 bind Cabin1, which in turn associate with class I HDACs such as HDAC1, HADC2 and HDAC3 (Youn and Liu, 2000). In muscle cells, MEF2 binds directly to class II HDACs such as HDAC4, HDAC5, and HDAC9 and inhibits the expression of specific genes involved in the development and adaptive responses of muscle (Chan et al., 2003; Gregoire et al., 2006; Gregoire and Yang, 2005; McKinsey et al., 2001, 2002; Miska et al., 1999; Sparrow et al., 1999). Mice whose HDAC5 or HDAC9 has been knocked out showed increased sensitivity to hypertrophic stimuli, suggesting important roles of class II HDACs in heart hypertrophy (Potthoff and Olson, 2007). These and other data indicate that MEF2 and Class II histone deacetylases (HDACs), and particularly HDAC5 and HDAC9, are key mediators of hypertrophic signals in cardiomyocytes. Ample data have suggested that the MEF2/class II HDAC pathway is potential therapeutic target for heart hypertrophy.
In response to specific calcium signals, Cabin1 and HDACs are removed from MEF2 (Potthoff and Olson, 2007). MEF2 then recruits co-activators such as p300 and CBP to turn on distinct programs by association with a variety of transcriptional activators and co-activators (McKinsey et al., 2001; Sartorelli et al., 1997; Slepak et al., 2001; Wei et al., 2008). A small increase of p300 has been shown to be necessary and sufficient to induce MEF2-dependent cardiac hypertrophy. MEF2 has a highly conserved N-terminal region (residues 2-93), consisting of the well-characterized MADS-box and a MEF2-specific domain (Shore and Sharrocks, 1995). The MADS-box/MEF2 domain is remarkably rich in function, mediating DNA binding, dimerization, and protein-protein interactions with a myriad of MEF2 transcription partners (McKinsey et al., 2001, 2002), including Cabin1, Class IIa HDACs and p300/CBP. It has been shown that the MADS-box/MEF2 domain in MEF2 is necessary and sufficient to bind with a small motif conserved in class II HDACs and Cabin1. The CH3 domain of p300 and CBP is also shown to bind the MADS-box/MEF2 domain.
Despite the extensive knowledge about MEF2's involvement in various cellular processes available in the art, it has heretofore been impossible to capitalize on the knowledge due the lack of suitable molecular tools. In particular, how to modulate the activity of MEF2 by small molecules has been a long standing challenge. This is because MEF2 is a relatively small transcription factor without any apparent enzymatic activity; its main function is to bind specific DNA and recruit transcription co-regulators such as Cabin1, class II HDACs and p300/CBP to specific promoters. This mode of function is generally considered not druggable or at least very difficult to target by small molecules. Discovery or creation of such molecules will facilitate further advances in this field and can lead to new mechanism-based and structure-based therapeutic applications for MEF2-associated diseases, including inflammation, autoimmune diseases, neurodegenerative diseases, cancer, and cardiovascular disease.
The invention described in this application can also be extended to modulating the activity of other transcription factors such as the forkhead/winged helix transcription factor FOXP3 (Bennett et al., 2001; Fontenot et al., 2003; Hori et al., 2003; Wu et al., 2006; Zheng and Rudensky, 2007). FOXP3 is a key transcription factor critical to the development and function of regulator T cells (Tregs). Tregs are a special population of T cells required for suppressing the excessive activation of the immune system. Loss of function of FOXP3 by mutations and other mechanisms lead to fetal autoimmune diseases such as IPEX whereas enhanced expression of FOXP3 or its activity can confer suppression function. Elevated FOXP3 function can be beneficial in treating autoimmune diseases and transplant rejection while strategic down regulation of FOXP3 activity can be used to develop immune-based anti-tumor therapies (Zuo et al., 2007a; Zuo et al., 2007b). Thus, small molecules that bind FOXP3 and modulate its interaction with co-repressors and co-activators could have therapeutic application in autoimmune diseases, transplant rejection and cancer therapy.
Similarly to MEF2, the function of FOXP3 is tightly regulated by transcription co-regulators that include HAT (such as TIP60) and HDACs (including class I and class II HDACs) (Li et al., 2007). Thus, small molecules could be developed by methods described in this invention that binds FOXP3 and blocks its interaction with co-regulators including epigenetic regulators such as histone modifying enzymes and chromatin remodeling machines.
Similarly, targeting transcription co-regulators has also met its share of challenges.
Among the transcription co-regulators of transcription factors such as MEF2, class II HDACs are the best studied group.
Histone deacetylases (HDACs) (EC number 3.5.1) are a class of enzymes that remove acetyl groups from an ε-N-acetyl lysine amino acid on a histone. Its action is opposite to that of histone acetyltransferases (HATs). HDACs proteins are now also being referred to as lysine deacetylases (KDAC) to more precisely describe their activity rather than their target, which also includes numerous non-histone proteins.
As their name suggests, one of HDACs main functions is to remove acetyl groups from histone proteins. Histone proteins are the chief protein components of chromatin. They act as spools around which DNA winds and play an important role in gene regulation and DNA packaging Histone proteins have tails that are normally positively charged due to the amine groups present on their lysine and arginine amino acids. These positive charges help the histone tails to interact with and bind to the negatively charged phosphate groups on the DNA backbone.
The association between DNA and histone acts as a vital control mechanism in regulating the ability of transcription factors to access DNA. Strong association between DNA and histones restricts access by transcription factors and therefore represses gene transcription (Morrison et al., 2007). Modification of histones or DNA can alter the strength of their association and thus modulate transcriptional activity (Morrison et al., 2007). Covalent addition of methyl, phosphate, or acetyl moieties has been shown to alter the nucleosome state and consequently affect transcription. Acetylation results from the addition of an acetyl group to the ε-amino group of conserved N-terminal lysine residues on histones. Addition of acetyl groups to histones reduces the attractive force between positively charged histone proteins and the negatively charged DNA phosphate backbone, resulting in a more relaxed and accessible chromatin structure. HATs facilitate histone acetylation and are thus believed to be transcriptional activators. Conversely, HDACs serve to remove acetyl groups from histones and thereby repress transcription. Thus, it is the interplay between HATs and HDACs activity that primarily governs local chromatin structure and gene expression. HDACs alter global gene transcription through the deacetylation of chromatin. It should be noted that HDACs do not directly bind DNA sequence and require additional factors for target gene recognition (Morrison et al., 2007).
There are 4 recognized subtypes of HDAC proteins (class I-IV) based on function and DNA sequence similarities. The first two subtypes are considered “classical” HDACs whose activity are inhibited by trichostatin A (TSA). Class I HDACs includes HDACs 1, 2, 3 and 8, which are expressed ubiquitously (Zhang and Olsen, 2000). Class II HDACs has two subgroups, IIa that includes 4, 5, 7 and 9, and IIb that includes HDAC6 and HDAC10. Class IIa share a common structural organization, with carboxyl-terminal catalytic domain and an amino-terminal extension that mediates interactions with members of the myocyte enhancer factor 2 (MEF2) family of transcription factors. HDACs also differ in terms of their subcellular localization with class I generally found in the nucleus, class IIb are located mostly in the cytoplasm, while class IIa shuttle between the nucleus and the cytoplasm. Unlike class I HDACs, class IIa HDACs are tissue-restricted, with especially high levels of expression in heart, skeletal muscle, and brain (Zhang et al., 2002). Class III is a family of NAD+-dependent proteins not affected by TSA and class IV is considered an atypical category of its own. HDAC11 is grouped in class V.
Given the important roles that HDACs play in cellular processes, the medical applications of HDAC inhibitors (HDACi) is an intense area of research. However, many uses of HDACi in medicine were discovered without knowledge of the underlying mechanism. For example, in psychiatry and neurology, there is a long history of using valproic acid as mood stabilizers and anti-epileptics. The anticonvulsant property of valproic acid was accidentally discovered when it was being used as a vehicle for a number of other compounds that were being investigated as anticonvulsant. It was not until later that valproic acid was identified as a HDACi. In recent years, HDACi are being actively studied as a mitigator or treatment for neurodegenerative diseases. There has also been extensive effort to develop HDACi for cancer therapy. For example, Vorinostat (SAHA) has recently been approved for treatment of cutaneous T-cell lymphoma (CTCL). An alternative agent under clinical evaluation for CTCL is the cyclic depsipeptide natural product FK228 (Romidepsin) which is a potent inhibitor of class I HDACs. In addition, a clinical trial is studying the effects of valproic acid on the latent pools of HIV in infected persons. Despite the growing interest in the medicinal applications of HDACi, the exact mechanisms by which these compounds work are still not well understood. Thus, these efforts are largely guided by guesswork and trial-and-error experiments.
One particular problem with the use of HDACi is that most of the known small molecules that inhibit HDAC activity are designed to function by targeting the catalytic activity of HDACs. However, since the active site is a conserved feature shared by a large number of different HDAC isoforms, it is inherently difficult to identify isoform-selective HDACi. Therefore, most HDACi have low specificity and are incapable of specific targeting of any particular species of HDAC. For example, trichostatin A (TSA) is among the most potent reversible HDACi currently known, with an IC50 in low nanomolar range. TSA with its hydroxamic acid group and its five-carbon atom linker to the phenyl group, has the optimal conformation to fit into the active site of HDAC (de Ruijter et al., 2003; Somoza et al., 2004). All HDACs are thought to be approximately equally sensitive to inhibition by TSA (de Ruijter et al., 2003).
A major impediment, therefore, for the discovery of small molecules that inhibit the function of HDACs and thereby modulate the activity of related transcription factors, is that the current state of the art is focused on the discovery and optimization of HDACi that are identified and evaluated through their ability to bind to the active site of the HDAC enzymes. Typically, these HDACi have the general structure R-L-Z, where R is a protein surface recognition group connected via a short fatty linker L to a Zn2+-chelating group Z that binds to the active site zinc atom. The most common chelating groups (Z) featured in the known HDACi are: hydroxamic acids (TSA, vorinostat, LAQ824, belinostat), thiol derivatives (FK228, largazole) or electrophilic ketones (trapoxin A). A potential drawback of such groups that bind tightly to metal cations like Zn2+ is that they may lack sufficient selectivity for a particular protein, resulting in various side effects.
Another class of known HDACi are the benzamides that feature an ortho-aminoanilide (2-aminoanilide) moiety, including MS-725, MGCD0103, pimeloylanilide ortho-aminoanilide (PAOA) and compound 106 (N1-(2-aminophenyl)-N7-p-tolylheptanediamide) which was investigated as a potential therapeutic for neurodegenerative diseases including Friedreich's ataxia and Huntington disease (Chou et al., 2008; Herman et al., 2006; Paris et al., 2008; Rai et al., 2008; Thomas et al., 2008; Wong et al., 2003). Although the detailed molecular mechanism of action of this class of HDACi is not known, these molecules were postulated to involve binding of the o-aminoanilide group to the zinc atom of the HDAC active site, despite the lack of any direct evidence regarding such binding motif. Moreover, such molecules were found to exhibit biological activity implicating inhibition of HDAC function, even though other non-selective HDACi did not show similar activity. For example compound 106 was shown to be very active for the induction of frataxin, despite weak HDAC inhibition, while closely related HDACi such as SAHA did not have this type of activity. Consequently, in light of the absence of a molecular mechanism for the actions of this class of compounds, the optimization of their therapeutic potential has been hampered.
Several additional factors resulting from the well-regulated biological roles of the various HDAC isoforms, impose further challenges for the conventional approaches to the design of HDACi. Experiments have shown that the amount of acetylated histones increases in the presence of HDACi. Yet, recruitment of HATs and HDACs by DNA-bound transcription factors results in the formation of multi-protein transcription regulatory complexes that confer cell type specificity and signal dependent regulation to arrays of subordinate genes. Using HDACi that inhibit HDACs indiscriminately is akin to throwing a monkey ranch into a complicated and delicately balanced machine. This explains the numerous undesirable side-effects observed in many of the trials involving HDACi.
The problems encountered in investigating medicinal uses of HDACi are also shared by researchers investigating epigenetic regulation. Epigenetic regulation is the establishment of inheritable gene expression patterns without permanently changing the DNA sequence. It has emerged as a key mechanism for regulating cellular function.
Alteration of epigenetic regulation is a hallmark of many diseases, especially cancer. Small molecules that are being developed as drugs in treating these diseases, typically found via phenotypic screening, act by modulating the epigenetic control of cellular process. As such, the fundamental mechanisms of epigenetic regulation is an area of intense interest. At the same time, the search for small molecule epigenetic regulators is becoming a very promising area for drug discovery.
Because epigenetic regulation is achieved largely through chemical modifications of chromatin structure by enzymes that act upon DNA (e.g. DNA cytosine methyltransferase) or proteins (e.g. HATs, HDACs, histone methylases, and histone demethylases), in this context, HDACs' role in regulating DNA transcription can be viewed as a component of epigenetic regulation. Similar to HDACi, the majority of current chemical modulators of epigenetic regulators inhibit these enzymes by binding to their catalytic site, which is often shared by multiple enzymes with distinct cellular roles.
Despite recent advances regarding the role of transcription factors such as MEF2, and its implication in several major diseases, it has not been possible to identify small molecules that are capable of modulating the function of MEF2. Such molecules would facilitate further advances in this field and can lead to new mechanism-based and structure-based therapeutic applications for MEF2-associated diseases, including inflammation, autoimmune diseases, neurodegenerative diseases, cancer, and cardiovascular disease.
Therefore, a general problem in this area of research has been the lack of small molecules that can target a specific epigenetic regulator enzyme or protein. A further problem has also been the lack of methods for the design, evaluation and optimization of such small molecules, in a manner that bestows the required selectivity without the associated drawbacks resulting from broad-spectrum activities across entire enzyme or protein classes. Such molecules will have important applications as molecular tools in studying the basic mechanism of epigenetic regulation as well as therapeutic agents for targeted therapeutic interventions.
SUMMARY OF THE INVENTION
Through extensive biochemical and structural studies (Guo et al., 2007; Han et al., 2005; Han et al., 2003), the inventors have unexpectedly discovered a unique structural feature of MEF2 that made it possible to modulate its activity using small molecules. This discovery lies at the core of the invention as it goes against conventional wisdom and opens up a new door of possibilities. Based on this unexpected discovery, inventors have devised a general strategy for modulating cellular processes by blocking the interactions between transcription factors and their co-factors via an interfacial inhibitor. Accordingly, this invention also provides methods for identifying, screening, assaying, and synthesizing small molecule modulators that are capable of binding to a site lying in the interfacial surface of the factor-cofactor complex, thereby, disrupting the formation of the complex.
Thus, this invention has solved the long standing problem of targeting the heretofore “undrugable” transcription factors such as MEF2.
With respect to the specificity problem faced by HDACi, this invention provides an alternative approach for the development of small molecule modulators of HDAC function. Rather than targeting the active site of a particular HDAC, the present invention targets the binding site of the HDAC with an associated transcription factor which is required for regulating transcription. Because different HDAC subtype will have different binding surface to different transcription factor, by targeting the interface of these protein-protein interactions, the specificity issue posed by the conservative active site is resolved.
In particular, the present invention targets the interaction between the transcription factor MEF2 and class IIa HDACs. The activity of MEF2 is controlled by class IIa HDACs that bind MEF2 on specific promoters to repress target gene expression (Potthoff and Olson, 2007). Some small molecule inhibitors of HDACs (HDACi) that are being developed for the treatment of a variety of cancers also show therapeutic potential in diseases where deregulation of MEF2 and HDACs activity is implicated, including cardiac hypertrophy, neurodegenerative disorders, and immune dysfunction (Morrison et al., 2007; Paris et al., 2008). These observations suggest that small molecules blocking class IIa HDAC:MEF2 interaction might offer similar clinical benefits as member-specific HDACi (Guo et al., 2007; Han et al., 2005; Han et al., 2003).
Class IIa HDACs function closely with MEF2 in muscle, neurons and T cells. Class IIa HDACs do not bind DNA but depend on its interaction with DNA-bound MEF2 for promoter targeting. This interaction is mediated by a short amphipathic helix conserved in class IIa HDACs but not other HDACs that binds to a hydrophobic groove on the MADS-box/MEF2 domain of MEF2 (Guo et al., 2007; Han et al., 2005; Han et al., 2003). Such a ligand/receptor like binding mechanism suggests that it might be possible to use small molecules to block the recruitment of class IIa HDACs to MEF2-specific promoters (Guo et al., 2007; Han et al., 2005; Han et al., 2003).
The invention is based on systematic structure and biochemical studies (Guo et al., 2007; Han et al., 2005; Han et al., 2003) suggesting that small molecules binding to MEF2 can modulate its activity in the recruitment of transcription co-regulator such as Cabin1, class IIa HADCS and p300/CBP. Most of the these co-regulators have intrinsic function to modify chromatin (e.g. HDACs, p300 and CBP) or the ability to recruit chromatin modifying enzymes and machinery (e.g. mSin3A that binds Cabin1, HP1, CtBP, 14-3-3 that binds class IIa HDACs). Thus, small molecules that bind MEF2 and modulate its interactions with other transcription co-regulators can serve as epigenetic modulators in tissues where MEF2 play key regulatory roles. These small molecules can therefore be used to treat diseases where the activity of MEF2-dependent gene expression is dysregulated. The dysregulation could result from genetic mutations of MEF2 and its associated factors, diminished or excessive signals leading to the reduced or overly activated MEF2 function, abnormal under- or over-expression of co-factors that bind and interact with MEF2. Potential clinical applications of the MEF2-binding small molecules include but not limited to diseases from the muscle, immune and nervous systems. In the muscle system are cardiac hypertrophy, muscle fiber type remodeling, and other muscle related diseases resulting from imbalanced MEF2 function. In the immune system are a variety of autoimmune diseases or immune deficiency that result from excessive or too little MEF2-dependent gene expression. MEF2-binding small molecules can also be used to manipulate the function of regulatory T cells and the overall immune response for preventing transplant rejection. Since MEF2-dependent gene expression is intimately linked to synapses remodeling and neuronal survival, MEF2-binding small molecules can also be used treat a variety of neurodegenerative diseases (e g Alzheimer's disease and Huntington disease etc), autism, psychiatric disorders, and impaired learning and memory that result from deregulated MEF2 function.
Because small molecule modulators of this invention operate by targeting binding sites located at the protein-protein interaction interface of the transcription factors and their co-factors, they are also referred to herein as interfacial inhibitors.
Having explained the basic principles of this invention, we now summarize the various aspects and embodiments of the invention below:
In a first aspect, the invention provides an assay for screening, identifying, or optimizing a candidate interfacial inhibitor. Assays in accordance with this aspect of the invention will generally include the steps of contacting the candidate interfacial inhibitor to an evaluating element comprising a molecular surface defined by a protein-protein interface, which includes beta strands S1, S2 and S3 and helix H2 of each MEF2 monomer and the short helix motif from Cabin1 and HDAC4 and HDAC 9. In some preferred embodiments, the evaluating element is operatively coupled with a reporting element that provides information about the candidate inhibitor. In a preferred embodiment, the assay is a cell-based luciferase assay that allow rapid and high throughput screen and optimization of small molecules that bind MEF2 and modulate its binding to transcription co-regulators. This assay is developed based on more than 10 years of structural and biochemical studies of MEF2 complexes by the inventor's laboratory. This invention claims that the protein-protein interface, first identified by crystallography studies, and further demonstrated by structure-guided mutation studies in the invention, could serve as the molecular basis for a highly specific and sensitive screen for MEF2-binding small molecules. In other embodiments, the evaluating element of the assay may be implemented with physical assays that include but are not limited to pull down, coimmunoprecipitation or fluorescence quenching and anisotropy or any in vitro binding assays and cell-based luciferase reporter assay, transgenic reporter assay that are based on the protein-protein interface identified by this invention.
In a second aspect, this invention also provides compounds useful as epigenetic modulators of MEF2-dependent transcription in a variety of mammalian tissues that include but are not limited to muscle, immune and nervous systems. In some preferred embodiments, compounds in accordance with this aspect of the invention may include but are not limited to the previously published compounds (Chou et al., 2008; Herman et al., 2006; Paris et al., 2008; Rai et al., 2008; Thomas et al., 2008; Wong et al., 2003), pimeloylanilide orthoaminoanilide PAOA, and the commercially available homolog suberoylanilide orthoaminoanilide, or BML-210, as well as their structurally related derivatives.
In a third aspect, this invention also provides a molecular framework defined by the BML-210 binding site on MEF2 derived from the structural frame work established by the crystal structure of BML-210 bound to MEF2, as set forth in the crystal structure coordinates in Table 1. We co-crystallized BML-210 with a MEF2A (1-78) dimer bound to DNA. The crystals diffracted to 2.4 Å, and the structure was solved by molecular replacement using the MEF2A (1-78):DNA complex as the search model (Santelli and Richmond, 2000). BML-210 adopts an extended conformation to bind into the hydrophobic pocket of the MEF2 (FIG. 1d). One end of the molecule, the phenylamide group, is surrounded by a number of hydrophobic residues including Leu66, Leu67, Thr70, Leu66′ (prime sign denote residues from the other monomer) and Thr70′. The amide group at this end is also in position to engage in hydrogen bonding interactions with Thr70 and Thr70′, respectively. At the other end of the BML-210, the ring-link electron density is in a more hydrophilic environment surrounded by Asn73, Gln56′, Asp61′ and Asp63′. This region correspond to the ortho-aminoanilide group. Here the ortho-aminoanilide moiety with its amide group make extensive van der waals contacts and potential hydrogen bonding interactions with residues of MEF2 (FIG. 1d). The methylene groups of the octanediamide fit snugly between helix H2 of the two MEF2 molecules, making numerous contacts to the main chain and side chain of MEF2 residues, mostly of hydrophobic nature (FIG. 1d). Based on the crystal structure of BML-210 bound to MEF2, we claim that the surface residues that contact or are close proximity to contact BML-210 and PAOA can be used to guide the design and screen of small molecules to MEF2 by experimental and computational based approaches. These residues include all the residues on strand S1, S2 and S3 and helix H2 of MEF2 that are exposed. This structural frame, coupled with the high throughput, specific and sensitive assay described in the present invention will allow rapid design and optimization MEF2-binding small molecules that include BML210 and PAOA derivatives and molecules based on novel molecular scaffolds. The crystal structure of BML-210 bound to MEF2 disclosed in this invention, in addition to defining the small molecule MEF2-binding site as described herein, it also reveals for the first time a likely binding site for the ortho-aminoanilide moiety present in BML-210 and in other benzamide-containing HDAC inhibitors. Notably, this binding site is different from the HDAC enzyme's active site as has been postulated previously for this class of HDAC inhibitors.
In a fourth aspect, the invention provides MEF2-binding small molecules useful for binding to the interfacial binding site defined by the molecular framework in the third aspect above. In one embodiment the provided molecules are MEF2-binding small molecules with a general structural formula derived from the identified binding site derived from the crystal structure of BML-210 bound to MEF2. The provided small molecules are designed to bind to the described structural fold and would potentially bind MEF2 with high affinity and selectivity. The compounds provided under this embodiment of the invention include compounds of the general formula Ra-L-Rb that bind to the MEF2 binding site, wherein:

    
    
        Ra is a recognition group that binds to the hydrophobic region of the MEF2 binding site selected from a group that includes lower alkyl, alkenyl, alkynyl, aryl, heteroaryl, alkoxy, aryloxy, alkylthio, arylthio, or RcRdNC(═O)—, RcRdN(SO2)—, wherein:
        
            Rc and Rd are independently selected from a group consisting of hydrogen, alkyl, alkenyl, alkynyl, alkoxy, aryl, heteroaryl, alkylamino, dialkylamino, arylamino or heteroarylamino.
        
        
        L is a linker consisting of a chain of up to 20 carbon atoms, provided that up to three carbon atoms can be replaced with an oxygen, nitrogen or sulfur atom, and further provided that it can include substituents selected from a group consisting of:
        
            alkyl, alkenyl, alkynyl, aryl, heteroaryl, benzo, hydroxy, alkoxy, aryloxy, oxa, keto, amido, sulfonamido, or fluoro
        
        
        Rb is a recognition group that binds to the hydrophilic region of the MEF2 binding site selected from a group that includes lower alkyl, alkenyl, alkynyl, aryl, heteroaryl, alkoxy, aryloxy, alkylthio, arylthio, or RcRdNC(═O)—, RcRdN(SO2), wherein:
        
            Rc and Rd are independently selected from a group consisting of hydrogen, alkyl, alkenyl, alkynyl, alkoxy, aryl, heteroaryl, alkylamino, dialkylamino, arylamino or heteroarylamino.
        
        
    
    


In a preferred embodiment the provided compounds have the general structure Ar1-L1-L2-L3-Ar2 wherein:

    
    
        Ar1 and Are are aromatic rings independently selected from a group consisting of benzene, naphthalene, pyridine, pyrimidine, pyrazine, quinoline, isoquinoline, pyrrole, furan, thiophene, imidazole, pyrazole, oxazole, thiazole, isoxazole, indole, benzimidazole, benzothiazole, benzoxazole, provided that the aromatic ring may contain up to seven substituents selected from a group consisting of: hydrogen, alkyl, alkenyl, alkynyl, alkoxy, aryl, heteroaryl, amino, alkylamino, dialkylamino, arylamino, heteroarylamino, hydroxy, or halo. The substituents can also join together to form a ring of up to 12 atoms,
        L1 and L3 are linking groups independently selected from a group consisting of amino, alkylamino, arylamino, oxa, keto, NHC(═O), NR(C═O), S(═O) or —S(═O)2—
        L2 is a linking group selected from a group consisting of a chain of up to 10 carbon atoms, provided that up to three atoms can be replaced with an oxygen, nitrogen or sulfur atom, and further provided that these atoms can contain substituents selected from a group consisting of:
        
            alkyl, alkenyl, alkynyl, aryl, heteroaryl, benzo, hydroxy, alkoxy, aryloxy, oxa, keto, amido, sulfonamido, or fluoro
        
        
    
    


In a further preferred embodiment, the provided compounds have the general formula:




wherein:

    
    
        R1-R10 are independently selected from the group consisting of hydrogen, alkyl, alkenyl, alkynyl, alkoxy, aryl, heteroaryl, amino, alkylamino, dialkylamino, arylamino, heteroarylamino, hydroxy, and halo; and
        L4 is a linking group selected from a group consisting of a chain of up to 10 carbon atoms, provided that up to three atoms can be replaced with an oxygen, nitrogen or sulfur atom, and further provided that these atoms can contain substituents selected from a group consisting of: alkyl, alkenyl, alkynyl, aryl, heteroaryl, benzo, hydroxy, alkoxy, aryloxy, oxa, keto, amido, sulfonamido, and fluoro.
    
    


In a further preferred embodiment, the provided compounds are selected from the following list of compounds (FIG. 2)
These compounds showed a wide range of affinity in binding to MEF2 in vitro and in vivo, and could be used as lead to develop MEF2-based therapeutics in muscle, immune and nervous systems as mentioned above. The compounds indeed showed effect in promoting regulatory T cell functions in vitro and in mouse model, and are therefore potential drug leads for autoimmune diseases and preventing transplant rejection.
Methods for the preparation of the provided MEF2-binding molecules are also provided in this invention.
In a fifth aspect, the invention also provides compounds and compositions useful for treating diseases that result from deregulation of MEF2-dependent transcription. Compositions in accordance with this aspect of the invention will include one or more of a compound capable of blocking binding of MEF2 and its co-factors. The provided compounds and compositions can be used in therapeutic applications involving the modulation of epigenetic regulation associated with the interaction of transcription factors and their recruited histone-modifying enzymes. In particular, the provided MEF2-binding small molecules can be used to treat a variety of diseases resulting from deregulation of MEF2-dependent transcription, which include but not limited to cardiac hypertrophy, muscle fiber type remodeling, and other muscle-related diseases resulting from imbalanced MEF2 function; autoimmune diseases or immune deficiency that result from excessive or too little MEF2-dependent gene expression, and transplant rejection; a variety of neurodegenerative diseases (e.g. Alzheimer's disease and Huntington disease etc), autism, psychiatric disorders, and impaired learning and memory that result from deregulated MEF2 function. A further application of this embodiment of the invention involves small molecules that modulate the function of the FOXP3 transcription factor that can be used to treat a variety of diseases that result from deregulation of FOXP3-dependent transcription. These diseases include but not limited to autoimmune diseases, transplant rejection and cancer.
The sixth embodiment of this invention involves the preparation of the drug:MEF2 complex and its crystallization for structure determination. This protocol define the specific protein fragment of MEF2A (2-78) and the range of buffer conditions to obtain high quality of crystals of compounds bound to MEF2. This method of complex preparation and crystallization is essential for structural characterization of current and future small molecules bound to MEF2 and use the structure to guide the optimization of the lead compounds.
The above-mentioned and other features of this invention and the manner of obtaining and using them will become more apparent, and will be best understood, by reference to the following description, taken in conjunction with the accompanying drawings. The drawings depict only typical embodiments of the invention and do not therefore limit its scope
Other aspects and advantages of the invention will be apparent from the following description and the appended claims.



BRIEF DESCRIPTION OF THE DRAWINGS
FIGS. 1A-1D FIGS. 1A-1C show three different depictions of a crystal structure of MEF2 and the identified ligand binding site; FIG. 1D shown is BML-210 bound to MEF2A (1-78) at 2.4 Å resolution, including the amino acids involved in binding interactions with BML-210. In FIG. 1a the top DNA sequence (i.e., AAGCTACTATATTTAGC) is SEQ ID NO:1 and the bottom DNA sequence (i.e., CGATGATATAAATCGTT) is SEQ ID NO:2. In FIG. 1c XX(V/T)KXY(L)YXX(V/I/L)(L)XX is SEQ ID NO:3.
FIG. 2 shows the structures of BML-210, PAOA and related exemplary MEF2-binding molecules.
FIGS. 3A-3B show a schematic diagram of MEF2-HDAC luciferase reporter assay for HDACi.
FIG. 4 shows normalized response for luciferase activity in MEF2-HDAC luciferase reporter assay 24 hrs after treatment with BML-210. The luciferase activity decreased in a dose dependent manner.
FIGS. 5A-5B FIG. 5A shows competitive inhibition of MEF2 binding to HDAC after incubation with BML-210 in Biacore assay; FIG. 5B Structural analysis showing that BML-210 and HDAC9 bind overlap regions on MEF2.



DETAILED DESCRIPTION
Having summarized the various aspects of this invention, we now describe in detail the various exemplary embodiments to further illustrate the invention.
Specific Interfacial Inhibitors of HDACs and Uses Thereof
As mentioned above, what makes the study of epigenetic regulators challenging is the fact that there are a large number of enzyme isoforms, many of which have distinct functions. For example, among the four HDAC enzyme super families, class I (HDAC 1, 2, 3, and 8) and class II (HDAC 4, 5, 6, 7, 9, and 10) are the two major classes implicated in cancer. Although the unique function of each individual member can be studies by molecular biology approaches such as knockout or knockdown, their roles in drug-based therapy cannot be assessed because most current HDAC inhibitors target the catalytic domain common to most HDACs (class I and II). In fact, it is often observed that a given HDAC inhibitor induces what appears to be opposing effects in different cellular conditions, presumably by affecting the activity of different HDAC isoforms. Thus, the lack of isoform specificity of current HDACi presents a major barrier to rational mechanistic studies of drug effects and the individual function of specific HDACs. Also, it is not clear if it is more pharmacologically beneficial to inhibit a large number of HDACs or a small subset or even a specific member. It is possible that certain clinical applications (e.g. cancer therapy) may require the former, whereas others (e.g. neurodegeneration and inflammation) may benefit from the latter.
Currently available inhibitors of class I and class II HDACs can be grouped into six categories based on the key features of their chemical structures: (1) hydroxamic acids; (2) thiol-containing molecules; (3) electrophilic ketones; (4) short-chain fatty acids; (5) benzamides (ortho-aminoanilides); and (6) cyclic depsipeptides. While it is well established that some of these molecules, including hydroxamic acids, thiols, and electrophilic ketones, work by binding to the zinc ion of the HDAC active site, the inhibitory mechanism of the other categories are not well defined. Different HDAC inhibitors have shown different activities on different classes of HDACs. For example, while members of the hydroxamic acids category, such as TSA and SAHA, are potent inhibitors across the entire class I and class II HDACs, some members of the benzamide family (e.g. pimeloylanilide ortho-aminoanilide (PAOA), MS-275, CI-994, MGCD-0103), and the cyclic peptide family (e.g. FK228), showed modest selectivity toward certain HDAC members or subclasses. However, because of the general lack of understanding of the molecular mechanisms of HDAC inhibitors, how this selectivity is achieved is not clear. Consequently, the empirical observations of selectivity in some HDAC inhibitors could not guide rational design of subtype-specific HDAC inhibitors. While crystal structures of the catalytic domain of several class I (HDAC8) and class II (HDAC4 and HDAC7) members and their complexes with different inhibitors have been solved, these structures and the structure-based sequence-alignments of class I and class II HDACs suggest that the active site is highly conserved and show only minor differences in the surrounding region. Therefore, they also fail to provide any insights with regard to potential mechanisms of selectivity. Given this background, rational design of subtype-specific inhibitors against the highly conserved catalytic domain is widely considered to be highly challenging.
Observing that HDACs often exist in large multi-protein complexes with specific co-regulators and other chromatin modifying enzymes, inventors of this invention postulated that a mechanism-based approach may offer a better pathway to identifying and optimizing novel HDAC-based small molecule epigenetic regulators. That is, instead of targeting the active site of the enzyme as dictated by conventional approaches of drug design, one would develop small-molecules targeting the protein-protein interactions between HDACs and their relevant functional partners.
Accordingly, in one aspect, this invention provides a method of modulating HDAC function by blocking the binding of HDAC to an associated transcription factor. In general, methods according to this aspect of the invention will have the steps of: contacting the transcription factor with interfacial inhibitor, wherein the interfacial inhibitor is capable of selectively binding to a site within the interfacial surface between the transcription factor and HDAC, thereby preventing this HDAC from performing its catalytic activity at protein sites that are located in the vicinity of the DNA-binding site of the transcription factor.
The HDAC may be any HDAC isoform from a classical HDAC or a subset thereof. Exemplary HDAC may include HDAC 4, 5, 6, 7, 9 and 10, or any subset thereof. In a preferred embodiment, the HDAC is a class IIa HDACs, and in a further preferred embodiment the HDAC is either HDAC4 or HDAC9.
The transcription factor may be any transcription factor known to bind to the HDAC. Exemplary transcription factors may include MEF2, FOXP3, GATA3, and Cabin1 but are not limited thereto. In a preferred embodiment, the transcription factor is MEF2.
The interfacial inhibitor may be a small molecule.
Methods described herein above may be used in a research setting for obtaining information regarding the function and mechanisms of a HDACs and the counterpart transcription factor in vivo or in vitro. They may also be used in a clinical setting for treating diseases.
Diseases that may be treated with methods of this invention are generally those involving cardiac hypertrophy, muscle fiber type remodeling, and other muscle-related diseases resulting from imbalanced MEF2 function; autoimmune diseases or immune deficiency that result from excessive or too little MEF2-dependent gene expression, and transplant rejection; a variety of neurodegenerative diseases (e.g. Friedrich's ataxia, Alzheimer's disease and Huntington disease etc), autism, psychiatric disorders, and impaired learning and memory that result from deregulated MEF2 function. Exemplary diseases may include neurodegenerative diseases, heart diseases, autoimmune diseases, inflammation, and cancer, but are not limited thereto.
When used in a clinical setting, methods in accordance with this aspect of the invention will include the general steps of: administering to a patient a pharmaceutically effective amount of a blocking agent, in which the blocking agent is capable of blocking the binding of a HDAC to a transcription factor.
When used in a different clinical setting, methods in accordance with this aspect of the invention will include the general steps of: administering to a patient a pharmaceutically effective amount of a blocking agent, in which the blocking agent is capable of blocking the binding of a Cabin1 to MEF2. Cabin1 is a transcription co-repressor of calcineurin-dependent transcription program. It is highly expressed in T cells and neuronal cells.
When used in yet a different clinical setting, methods in accordance with this aspect of the invention will include the general steps of: administering to a patient a pharmaceutically effective amount of a blocking agent, in which the blocking agent is capable of blocking the binding of a p300 to MEF2.
When used in yet a different clinical setting, methods in accordance with this aspect of the invention will include the general steps of: administering to a patient a pharmaceutically effective amount of a blocking agent, in which the blocking agent is capable of blocking the binding of a CBP to MEF2.
In a more general setting, methods in accordance with this aspect of the invention will include the general steps of: administering to a patient a pharmaceutically effective amount of a blocking agent, in which the blocking agent is capable of blocking the binding of any transcription co-regulators that bind MEF2.
As set forth above, the HDAC may be any classical HDAC or a subset thereof. The blocking agent may be a small molecule, a helical peptidomimetic, or a combination thereof, so long as the blocking agent is capable of selectively binding to a site located on the interfacial surface between the HDAC and the transcription factor. In a preferred embodiment, the transcription factor is MEF2.
Methods and Tools for Developing Interfacial Inhibitors
In another aspect, this invention also provides an assay for identifying an interfacial inhibitor capable of binding to an interfacial site between HDAC and a transcription factor so as to block the interactions thereof.
Assays in accordance with this aspect of the invention will generally have the steps of introducing a test compound to an evaluation element, wherein said evaluation element comprises an interfacial binding site on a MEF2 dimer defined by the interface between a first group of structural elements on the MEF2 dimer and a second group of structural elements. The first group of structural elements include the beta strands S1, S2, S3, and the helix H2 of each of the MEF2 monomer (The secondary structural elements and corresponding residue ranges are as described in Han et al., Nature 2003). The second group include the short helix motif from Cabin1, HDAC4, HDAC9, HDAC5, HDAC7, p300 and CBP. The evaluation element may also be operatively coupled with a reporter element for reporting information related to the binding or non-binding of the test compound.
In a preferred embodiment, there is disclosed herein a two-hybrid system based assay includes a binding domain fused with a bait, an activating domain fused with a prey, and a reporter gene; and determining a reporter signal level. The binding domain comprises a MEF2D fused with GAL4 DNA (GAL4-MEF2); the activating domain comprises MEF2 binding motif of HDAC4 fused with VP-16 (HDAC4-VP16). The reporter gene is a GAL4-driven reporter plasmid (GAL4Luc), all hosted in a cell host.
This preferred embodiment of this invention is a cell-based luciferase assay that allows rapid and high throughput screening and optimization of small molecules that bind to a transcription factor such as MEF2 and modulate its binding to transcription co-regulators. The assay is developed based on more than 10 years of structural and biochemical studies of MEF2 complexes by the inventor's laboratory. This exemplary embodiment based that the protein-protein interface, first identified by crystallography studies, and further demonstrated by structure-guided mutation studies in the invention, could serve as the molecular basis for a highly specific and sensitive screen for MEF2-binding small molecules.
Any assay that based on this protein-protein interface, which include beta strands S1, S2 and S3 and helix H2 of each MEF2 monomer and the short helix motif from Cabin1 and HDAC4 and HDAC 9 are considered to be within the scope of this invention. Other exemplary assay implementations may include any physical assay techniques such as, but not limited to, pull-down, co-immunoprecipitation; fluorescence-based binding assays and functional assays including, but not limited to, luciferase reporter assay, and transgenic reporter assay that are based on the protein-protein interface identified by this invention.
In particular, in order to establish if a provided compound can indeed disrupt the binding of class IIa HDAC inside cells, several types of assays can be used, including the Chromatin Immunoprecipitation (ChIP) assay. HDAC4 plasmid construct is transiently transfected into Hela Cells. HDAC4 occupation on MEF2 mediated promoters are detected by ChIP using appropriate specific antibodies and PCR primers in the presence of the tested compound and buffer control. A fluorescence imaging based method as an alternative approach to ChIP analysis can also be used. GFP-fused MEF2C and HDAC4 is transfected into HeLa or C2C12 cells to study their interaction. When expressed alone, GFP-HDAC4 localizes in the cytoplasm in a diffusive manner, whereas GFP-MEF2 localizes in the nucleus, also in a diffusive pattern. When co-expressed, HDAC4 and MEF2 form punctate bodies inside the nucleus. Although the nature of these punctate nuclear bodies is unknown, their formation is apparently dependent on MEF2:HDAC4 interaction, as a HDAC4 mutant lacking a functional MEF2-binding motif fails to target MEF2 to nuclear bodies. Finally, a genome-wide analysis of MEF2 target genes by mRNA profiling (microarray) and binding location (ChIP-on-chip) can further facilitate this method, by selecting well-known MEF2 target genes that show large responses to MEF2-dependent repression or activation in the resting or activated (e.g. with calcium signal turned on) state. Using this method it can be established if these genes are potentially regulated by class II HDACs or other MEF2 co-repressors (e.g. Cabin1) by detecting the promoter presence of class IIa HDAC using ChIP and by monitoring expression changes upon drug treatment or after siRNA knockdown of HDAC4, 5, 7 or 9 (expression changes due to siRNA are evaluated first). Overall this method can be used to evaluate a compound at a genome-wide level by analyzing gene expression using microarray and by detecting genome-wide binding of class IIa HDACs in the presence of various concentrations of the provided compound.
To facilitate performing the assay, this invention also provides a high throughput, highly sensitive and specific screen platform for searching MEF2-binding small molecules. This platform comprises stably transformed cell lines containing the GAL4-driven reporter plasmid (GAL4Luc), MEF2D fused with GAL4 DNA-binding domain (GAL4-MEF2), the MEF2-binding motif of HDAC4 fused with VP-16 (HDAC4-VP16), GAL4 DNA-binding domain fused with VP-16 (positive control) and various compounds as negative and positive controls. A kit consistent of the above stable cell lines, plasmids, and control compounds can be made for the screen by users searching for new MEF2-binding molecules and for optimizing existing leading compounds. By switching MEF2D to MEF2A, MEF2B and MEF2C, one can also use this method to search for compounds that bind selectively to an isoform of the MEF2 family. Such compounds can be used to study the function and involvement of specific MEF2 family members in diseases and can be employed in the development of diagnostic agents and for the identification of more specific therapeutic agents for MEF2-associated diseases.
In yet another aspect, the invention also provides a method for identifying a subtype-specific HDAC inhibitor/modulator by targeting their regulatory and functional complexes. Methods in accordance with this aspect of the invention generally includes the steps of: (1) solving the structure or substructure that contains functionally important interfaces; (2) applying docking analysis to the solved structures by computationally docking test molecules selected from existing or new potential HDAC inhibitors; (3) developing an assay for screening compounds that can disrupt the protein-protein interactions between the HDAC complex of interest; (4) characterizing the compound identified in step (3); (5) optimizing the compound computationally; and (6) synthesizing the optimized compound and validating the compound using the assay of step (3).
For step 1, the structure can be solved by molecular replacement using existing structure as the search model. If necessary, experimental phases can be obtained MAD or MIR. For step 2, docking can be performed using standard package such as AutoDock. Step 3 is as described above and will most be based on mammalian two-hybrid assay. The rest of the steps will depend on the nature of the compounds using methods known in the art.
In still another aspect, the invention also provides compounds useful as blocking agents for blocking the binding between a HDAC and a transcription factor. The HDAC may be any classical HDAC or a subset thereof. The transcription factor may be any transcription factor known to bind to HDAC, including but not limited to MEF2, FOXP3 and GATA3.
In a preferred embodiment, the transcription factor is MEF2.
Compounds according to this aspect of the invention include small organic molecules and helical peptidomimetics.
MEF2-binding small molecules can be identified using the method provided herein, by utilizing the disclosed MEF2 binding site as a guide. The provided small molecules have a general structural formula derived from the identified binding site revealed from the crystal structure of BML-210 bound to MEF2. The provided small molecules are designed to bind to the described structural fold and would potentially bind MEF2 with high affinity and selectivity. In order to identify more potent and selective compounds using this approach, methods known in the art can be utilized, including but not limited to: computer-aided structure-based design combined with in-silico screening, combinatorial library design combined with high-throughput screening, and fragment-based drug discovery for lead identification followed by lead optimization.
In a preferred embodiment, the compounds provided under this invention include compounds that bind to the MEF2 binding site with the general formula:

Ra-L-Rb, wherein:

    
    
        Ra is a recognition group that binds to the hydrophobic region of the MEF2 binding site selected from a group that includes lower alkyl, alkenyl, alkynyl, aryl, heteroaryl, alkoxy, aryloxy, alkylthio, arylthio, or RcRdNC(═O)—, RcRdN(SO2), wherein:
        
            Rc and Rd are independently selected from a group consisting of hydrogen, alkyl, alkenyl, alkynyl, alkoxy, aryl, heteroaryl, alkylamino, dialkylamino, arylamino or heteroarylamino.
        
        
        L is a linker consisting of a chain of up to 20 carbon atoms, provided that up to three carbon atoms can be replaced with an oxygen, nitrogen or sulfur atom, and further provided that it can include substituents selected from a group consisting of:
        
            alkyl, alkenyl, alkynyl, aryl, heteroaryl, benzo, hydroxy, alkoxy, aryloxy, oxa, keto, amido, sulfonamido, or fluoro;
        
        
        Rb is a recognition group that binds to the hydrophilic region of the MEF2 binding site selected from a group that includes lower alkyl, alkenyl, alkynyl, aryl, heteroaryl, alkoxy, aryloxy, alkylthio, arylthio, or RcRdNC(═O)—, RcRdN(SO2), wherein:
        
            Rc and Rd are independently selected from a group consisting of hydrogen, alkyl, alkenyl, alkynyl, alkoxy, aryl, heteroaryl, alkylamino, dialkylamino, arylamino or heteroarylamino.
        
        
    
    


In a preferred embodiment the provided compounds have the general structure Ar1-L1-L2-L3-Ar2 wherein:

    
    
        Ar1 and Ar2 are aromatic rings independently selected from a group consisting of benzene, naphthalene, pyridine, pyrimidine, pyrazine, quinoline, isoquinoline, pyrrole, furan, thiophene, imidazole, pyrazole, oxazole, thiazole, isoxazole, indole, benzimidazole, benzothiazole, benzoxazole, provided that the aromatic ring may contain up to seven substituents selected from a group consisting of: hydrogen, alkyl, alkenyl, alkynyl, alkoxy, aryl, heteroaryl, amino, alkylamino, dialkylamino, arylamino, heteroarylamino, hydroxy, or halo. The substituents can also join together to form a ring of up to 12 atoms,
        L1 and L3 are linking groups independently selected from a group consisting of amino, alkylamino, arylamino, oxa, keto, NHC(═O), NR(C═O), S(═O) or —S(═O)2—
        L2 is a linking group selected from a group consisting of a chain of up to 10 carbon atoms, provided that up to three atoms can be replaced with an oxygen, nitrogen or sulfur atom, and further provided that these atoms can contain substituents selected from a group consisting of:
        
            alkyl, alkenyl, alkynyl, aryl, heteroaryl, benzo, hydroxy, alkoxy, aryloxy, oxa, keto, amido, sulfonamido, or fluoro
        
        
    
    


In a further preferred embodiment, the provided compounds have the general formula:




wherein:

    
    
        R1—R10 are independently selected from a group consisting of hydrogen, alkyl, alkenyl, alkynyl, alkoxy, aryl, heteroaryl, amino, alkylamino, dialkylamino, arylamino, heteroarylamino, hydroxy, and halo; and
        L4 is a linking group selected from a group consisting of a chain of up to 10 carbon atoms, provided that up to three atoms can be replaced with an oxygen, nitrogen or sulfur atom, and further provided that these atoms can contain substituents selected from a group consisting of: alkyl, alkenyl, alkynyl, aryl, heteroaryl, benzo, hydroxy, alkoxy, aryloxy, oxa, keto, amido, sulfonamido, and fluoro.
    
    


In a further preferred embodiment, the provided compounds are selected from the following list of compounds (FIG. 2)







further facilitate a complete understanding of the various aspects and ramifications of this invention, the following illustrative examples are provided.

EXAMPLES
Example 1
Strategy for Identifying Subtype-specific HDAC Inhibitors/Modulators
This invention provides a novel strategy for identifying lead compounds that may act as subtype-specific HDAC inhibitor/modulators. The strategy consists of several iterative steps:
Step 1: for a given HDAC complex of interest, the structure or substructure of the HDAC bound to its associated regulatory protein is solved or its structure or substructure that contains functionally important interfaces is obtained.
Step 2: the structure is used for docking analysis of existing or new potential HDAC inhibitors that may bind the protein-protein interface. The virtual screen will be guided by functional data such as if the HDAC inhibitor showed effect in cellular processes involving the target HDAC complex and if the HDAC inhibitor seems to act through mechanisms other than active site inhibition.
Step 3: the structure and related biochemical information is also used to guide the development of assays that can be used to screen compounds that can disrupt the intended protein-protein interface.
Step 4: once such leads are found, their complexes with the protein target is characterized using the structural study system established in Step1.
Step 5: the structural information, in combination with relevant chemistry methodologies is used to guide the design of analogs that can bind the target protein with higher affinity and specificity. The methods used are similar to that of Step 2.
Step 6: the designed analogs are synthesized and analyzed by assays established in Step 3. Finally, the optimized compounds are used for in vivo studies to test if they can mimic the effects of the parent compound but with higher potency and less non-specific/side effects.
Utilizing the above mechanism-based approach, inventors have demonstrated that a previous known HDAC inhibitor, PAOA, was identified as a lead compound that can specifically disrupt the function of class IIa HDACs by serving as a MEF2 inhibitor (MEF2i). Moreover, representative structural analogs of PAOA were also designed, synthesized and evaluated with the method described herein, and several more potent MEF2i were identified (FIG. 2), thereby demonstrating further aspects of this approach.
Example 2
Uses of Subtype-specific HDAC Inhibitors in Therapeutic Applications
Class IIa HDACs play crucial roles in neuronal survival/synapse formation, T cell selection/activation, and muscle remodeling. Dysregulation of these activities are implicated in a number of diseases, including neurodegeneration, inflammation and cardiac hypertrophy. Some HDACi developed for cancer therapy showed beneficial effects against these disorders. Although the non-specific nature of these HDAC inhibitors prevent their clinical applications in these diseases, these observations raise an intriguing question whether the observed therapeutic effects were related to class IIa HDACs, and whether selected disruption of class IIa HDAC function could be a viable strategy for treating these diseases. To address these questions, small molecules that can specifically disrupt the function of class IIa HDACs are needed.
Based on the known cellular functions of MEF2 and class IIa HDACs and the effects of some HDAC inhibitors in muscle, immune and neuronal systems, we propose methods and compounds of this invention could be used to treat cardiac hypertrophy, muscle fiber type remodeling, and other muscle-related diseases resulting from imbalanced MEF2 function; autoimmune diseases or immune deficiency that result from excessive or too little MEF2-dependent gene expression, and transplant rejection; a variety of neurodegenerative diseases (e.g. Friedrich's ataxia, Alzheimer's disease and Huntington disease etc), autism, psychiatric disorders, and impaired learning and memory that result from deregulated MEF2 function.
The MEF2-binding molecules developed for treating various human diseases mentioned above could be administered orally, intramuscular, intraperitoneal, subcutaneous, intravenous injections. Other delivery methods are also possible, and the exact protocol will depend on the conditions that are being treated. The dose could also vary according to specific clinical applications. But the standard assays at which the compound shows effect in vitro is around 0.1-10 μM in vitro and 1-10 mg per KG of body mass in animal model studies.
Preferred compounds provided under this invention shown in FIG. 2 exhibited a wide range of affinity in binding to MEF2 in vitro and in vivo, and could serve as lead compounds to develop MEF2-based therapeutics in muscle, immune and nervous systems as mentioned above. The compounds indeed showed effect in promoting regulatory T cell functions in vitro and in mouse model, and are therefore potential drug leads for autoimmune diseases and preventing transplant rejection. For example, the MEF2-binding molecule NKL30 at 0.15 μM greatly enhanced regulatory T cell function as evident by the enhanced suppression activity in vivo. In an mouse model of homeostatic proliferation assay, the compound at 1 mg/KG body mass administered by intravenous injection also greatly enhanced the Treg function in vivo. These data strongly suggest that MEF2-binding molecules provided by this invention could be used to treat autoimmune diseases and for preventing transplant rejection.
Example 3
Targeting Class IIa HDACs for Functional Modulation
Compared with other HDACs, the class IIa family is unique in several aspects of function and regulation. First, class IIa HDACs are selectively expressed in muscle, brain and T cells, consistent with their functions in these tissues. Second, the activity of class IIa HDACs is tightly regulated by the calcium signal, a predominant second messenger in tissues where class IIa HDACs are expressed. Third, class II HDACs contain a large regulatory domain N-terminal to the catalytic domain, which confers unique properties to this subclass of HDACs. The N-terminal regulatory region contains domains and motifs that interact with a variety of proteins, including those regulating the calcium responsiveness of class II HDACs, such as CaM, CaMK and 14-3-3, and those targeting class II HDACs to specific promoters such as MEF2 and BCL-6, and other epigenetic regulators and effectors such as class I HDACs, CtBP and HP-1 that function cooperatively with class IIa HDACs. The structures of a number of these complexes are investigated as potential targets for specific disruption.
Among the many complexes involved in the regulation and function of class IIa HDACs, the best characterized is the MEF2 complex in terms of biochemistry and structure. MEF2 is a family of sequence-specific transcription factors (MEF2A-D) that has the same expression pattern as class IIa HDACs and is also implicated in neurodegeneration, inflammation and cardiac diseases. The MEF2 family of transcription factors share a highly conserved N-terminal region, referred to as the MADS-box/MEF2S domain, that mediates DNA binding, dimerization and protein-protein interactions with a variety of transcription factors and co-regulators. Class IIa HDACs do not bind DNA but depend on interaction with MEF2 to target specific chromatin regions for deacetylation. Blocking this interaction is selected as a potential way to disrupt the function of class IIa HDACs.
The interaction between class IIa HDACs and MEF2 has been the subject of extensive functional and biochemical analyses, which reveal that a short sequence motif (MEF2-binding motif) conserved in class IIa HDACs and the MADS-box/MEF2S domain of MEF2 are necessary and sufficient for their binding. Systematic structural and biophysical studies were conducted on the interaction between MEF2 and class IIa HDACs and a related transcription repression (Cabin1) that contain a similar MEF2-binding motif. The crystal structures reveal that the MEF2-binding motif adopts a short amphipathic helix structure to bind a hydrophobic groove on the MADS-box/MEF2 domain of MEF2. Such a ligand/receptor like binding mechanism suggests that it might be possible to use small molecules to block the recruitment of class IIa HDACs to MEF2-specific promoters (refs Han Nature and 2005).
Example 4
Development of a Sub-class Specific HDAC Inhibition Assay
A series of MEF2-dependent luciferase reporter assays with transiently transfected MEF2D, HDAC4 and the co-activator p300 were used initially to screen various compounds. But these assays gave weak signal and high frequency of false positives, probably due to the complex transcription activation mechanisms of MEF2 and interference from endogenous factors. Through these observations, it was discovered that a highly sensitive and specific assay that can recapitulate the molecular interaction between HDAC4 and MEF2 inside cells is essential. To solve this problem, the inventors devised a mammalian two-hybrid system that is capable of detecting the interaction between HDAC4 and MEF2D with minimal interference from endogenous factors (FIG. 3).
In this assay system, MEF2D is fused with GAL4 DNA binding domain (GAL4-MEF2D) and the MEF2-binding motif of HDAC4 (aa 155-220) fused with VP-16 (HDAC4-VP16). Preliminary analysis showed that Hela Cells transiently transfected with both constructs and the GAL4-driven reporter plasmid (GAL4Luc) produced a strong signal comparable to that generated by the positive control of GAL4-VP16, whereas a MEF2D mutant Leu67Asp (L67D) that is previously shown to be defective in binding to HDAC4 failed to activate the reporter (data not shown). Protein expression levels in all luciferase reporter assays were confirmed by western blot.
Taking advantage of the structural insights, in addition to the MEF2D L67D mutant mentioned above, we introduced a number mutations in HDAC4 that had been previously shown to disrupt HDAC4:MEF2 interaction in vitro. These mutations also diminished the luciferase signal in the cell-based assay (FIG. 3b). Most interestingly, mutation of Val180Lys on HDCA4, which weakened the binding of MEF2 by  ̃60% in vitro (Kd of MEF2 binding by the wild type and the mutant HDAC4 are 0.47 μM and 0.81 μM, respectively), partially reduced the luciferase signal in the cell-based assay (FIG. 3b). These observations demonstrate that the signal from the mammalian two-hybrid assay correlates very well with the molecular interaction between HDAC4 and MEF2. These results not only provide further support for the structural model of the HDAC4:MEF2 interaction but also establish a sensitive and specific method for detecting the HADC4:MEF2 interaction inside the cells.
Example 5
Identifying Selective Inhibitors of the MEF2/HDAC Interaction
To reduce the complexity of the screening, the vast amount of functional data on existing HDAC inhibitors was utilized. Although most of the these inhibitors target the catalytic domain, some of the compounds discovered through the cell based histone acetylation assays may affect other aspects of HDAC function, including the binding of class IIa HDACs to MEF2. With this in mind, we performed virtual screen (3D docking) against a small molecule database using a pharmacophore model derived from the crystal structure of the HDAC9:MEF2 complex. Although this search did not yield a novel target, it did show that the hydrophobic pocket of MEF2 prefers compounds with two aromatic rings connected by a linker of certain length. This result is consistent with crystallographic analysis showing that the MEF2 dimer contains two symmetry-related sites that can bind a phenylalanine from HDAC9 (refs Han et Nature and JMB). We therefore searched for known HDAC inhibitors that bear such structural features and tested their effect on HDAC4:MEF2 interaction using the mammalian two-hybrid assay.
Screening a pool of selected HDAC inhibitors using the mammalian two-hybrid assay revealed that PAOA (FIG. 2), a previously studied compound inhibited the reporter signal in a dose dependent manner (FIG. 4). PAOA did not affect the expression of HDAC4-VP16 but reduced the reporter signal driven by GAL4-VP16 by 5.6 fold at 10 μM (data not shown), indicating non-specific inhibition by this compound on the expression of luciferase activity under our experimental conditions. However, the same concentration of PAOA decreased the reporter signal driven by GAL4-MEF2D and HDAC4-VP16 by about 26 fold, suggesting that PAOA have specific effect on disrupting the HDAC4:MEF2 interaction beyond its general inhibitory effect. By contrast, trichostatin A (TSA), a potent HDAC inhibitor that targets the zinc active site, showed similar inhibitory effect on the reporter signals driven by GAL4-VP 16 and GAL4-MEF2D/HDAC4-VP16 (data not shown). These results suggest that PAOA but not TSA can disrupt the interaction between HDAC4 and MEF2D.
The IC50 of PAOA on HDAC4:MEF2 interaction is around 5 μM based on the mammalian two-hybrid assay, similar to that determined using histone acetylation inhibition assay. The Kd for HDAC4 binding to MEF2 was previously determined to be 0.47 μM. If we assume the equilibrium concentration of HDAC4 is  ̃0.5 μM under our assay condition, the Kd for the binding of PAOA to MEF2 is estimated to be 5 μM. However, the estimated Kd could be larger if the free HDAC4 concentration is lower in the cell-based assay.
Whether PAOA binds MEF2 competitively with HDAC4 was also assessed in vitro using surface Plasmon resonance (SPR) on Biacore T-100. Here HDAC4 (aa 155-220) was immobilized on a CM5 sensor chip and purified MEF2A (1-95) was used as the analyte. The binding of MEF2A to HDAC4 at various concentrations generated a series of well-defined sensorgrams (data not shown). MEF2A incubated with increasing concentrations of PAOA showed dose dependent decrease of binding to the immobilized HDAC4 (FIG. 5). Analysis of the Biacore data indicates that the competitive binding reaction is complex, whereas direct binding of BML-210 to MEF2 was beyond the detection limit of the instrument. These technical limitations made it difficult to obtain a quantitative binding constant. Nevertheless, the preliminary data suggest that BML-210 indeed bind MEF2 competitively with HDAC4 in vitro.
PAOA was originally discovered as part of a group of compounds that selectively induce acetylation of histone but not tubulin, presumably through inhibition of HDACs other than HDAC6, a tubulin-specific HDAC. PAOA binds MEF2 competitively with HDAC4 in vitro. The inserts on the right illustrate the assay by Biacore. HDAC4: red helix; MEF2: green cross. deacetylase. Although the molecular basis of this selectivity is not known, it is noteworthy that HDAC6, which belongs to the class IIb subfamily, does not have the MEF2-binding motif conserved in class IIa and does seem to require MEF2 for function. PAOA and its derivatives have been recently shown to enhance the expression of frataxin in Friedreich's ataxia. Although the mechanism seems to involve induced histone acetylation, more potent but less specific HDAC inhibitors such as TSA and SAHA showed no effect on frataxin expression despite being able to induce higher level total histone acetylation in cells than PAOA. These observations suggest that PAOA and its derivatives possess a unique function to inhibit a specific HDAC or HDAC complex involved in frataxin silencing. Furthermore, the molecular basis for the action of PAOA can be further clarified with the crystal structure of BML-210 bound to MEF2 disclosed in this invention. In addition to defining the small molecule MEF2-binding site as described herein, this structure also reveals for the first time a likely binding site for the ortho-aminoanilide moiety present in BML-210, as well as PAOA and in other benzamide-containing HDAC inhibitors. Notably, this binding site is different from the HDAC enzyme's active site as has been postulated previously for this class of HDAC inhibitors.
Example 5
Preparation of Complexes of BML-210 Bound to MEF2 on DNA and the Crystals of the BML-210:MEF2:DNA Complex and the Atomic Details of the Complex Structure
In order to characterize the detailed interaction of BML-210 bound to MEF2 and use the structural information to guide the design of more potent MEF2 binding molecules, we have determined the crystal structure of the BML-210 bound to MEF2 on DNA. The gene coding MEF2A1-78 was created by PCR amplification from MEF2AFL and cloning into the pET30b expression vector. Protein was expressed in E. coli strain BL21(DE3)pLysS, 25 C, overnight and was purified by successive chromatographic steps on Sp-Sepharose, and gel filtration run at 4 C in 250 mM NaCl, 10 mM Hepes (pH7.6), 1 mM EDTA, 1 mM DTT to give a final yield of 0.6 mg/l. Oligonucleotides (Santelli and Richmond, 2000) were purchased from IDT DNA technologies, purified using MonoQ FPLC column followed by dialysis, lyophylization and annealing using thermal cycler.
 1/10th protein sample volume of 10 mM BML 210 was added to the protein samples at 0.5 mg/ml and concentrated to approximately 17 mg/ml (0.9 mM). and DNA duplex was added at 1:1 ratio prior to setting trays (10% DMSO end concentration). Plate like crystals were obtained by hanging drop vapor diffusion conditions at 18 C using 24% PEG4000, 140 mM NaCl, 5 mM MgCl2, 10 mM CaCl2, 0.004% NaN3, 3.3% glycerol, 50 mM TrisHCl (pH 5.8-pH8.18). Crystals with drug density were obtained at pH 8.18. The crystal diffracted to 2.4 Å resolution and belongs to space group P1 (a=41.567 Å, b=61.622 Åc=61.478 Å α=114.12° β=89.99° γ=89.95°. The structure is solved by molecular replacement using 1TQE.pdb as search model (refs Richmond 2000). The final model has an Rfree of 26% and Rw of 23%. The coordinates are attached (11.1_001_nr_nh_bml.pdb).
Example 6
Lead Optimization Using Structure-guided Design and Chemical Methodologies
Most HDAC inhibitors discovered by functional screen have modest potency with IC50 in the micromolar or even millimolar range. Lead optimization is typically done by systematic modifications of the chemical structure and structure-activity relationships (SAR) studies. However, without knowing the target and the detailed binding interactions between the compound and its target, such an empirical approach is often labor intensive and of limited effectiveness. This is in fact the case for PAOA where a series of analogs were synthesized to search for more potent compounds that may be used for treating Friedreich's ataxia. Although some PAOA analogs did show higher activity than the parent compound, the effect was very modest and the mechanism of improvement was not clear.
Remarkably, the ability by which these PAOA derivatives activate frataxin expression did not correlate with their HDAC inhibition activity. For example, some of the derivatives were very weak in histone deacetylation inhibition assay and yet very active in frataxin induction. Our preliminary findings that PAOA binds MEF2 and block the recruitment of class IIa HDACs provide a potential molecular mechanism for these intriguing results. Class IIa HDAC can repress transcription independent of the deacetylase activity. For example, a naturally occurring splicing variant of HDAC9 that lacks the entire C-terminal catalytic domain, also known as MITR, is a potent transcription repressor of MEF2-dependent gene expression, presumably by recruiting other epigenetic effectors such as HP1 and CtBP. In this sense, small molecule inhibitors that target the catalytic domain of class IIa HDACs cannot eliminate the full epigenetic silencing potential of these proteins, which may explain the ineffectiveness of TSA and SAHA in reactivating frataxin expression. PAOA, on the other hand, can block the recruitment of HDAC activity and other transcription repressors together. Although MEF2 is also involved in gene activation by recruiting transcription activators such as CBP/p300, current data suggest that the main effect of PAOA on MEF2 dependent gene expression is alleviating the silencing effect of class IIa HDACs and other transcription repressors.
By relying on the above analysis and the disclosed structure of BML-210:MEF2:DNA, and by employing docking solutions of PAOA to MEF2A it is shown that this drug molecule can fit preferably into the experimentally observed electron density, demonstrating the relative effectiveness of the ICM-Docking protocol (Molsoft L.L.C) for the design of new PAOA-like compounds for MEF2 binding. This docking approach can be used to design and analyze new PAOA analogues with potentially greater affinity and selectivity. Some of the features of the structure are briefly described below to illustrate the principles to be used in designing new molecules that may bind MEF2 with higher affinity.
BML-210 adopts an extended conformation to bind into the hydrophobic pocket of MEF2 (FIG. 1). This is also the binding site for the MEF2-binding motif conserved in class IIa HDACs and Cabin1. Since one end of the electron density resembles a simple aromatic ring and is surrounded by a number of hydrophobic residues including Leu66, Leu67, Thr70, Leu66′, Leu67′ and Thr70′ (prime sign denote residues from the other monomer), we assigned this density to the phenyl group. The carbonyl group at this end is also in position to engage in hydrogen bonding interactions with Thr70′ (FIG. 1).
The structure-based design of new and optimized MEF2-binding small molecules can be achieved using several known structures of MEF2. We have now solved the crystal structures of three MEF2 complexes. Two of them contain a peptide derived from the MEF2-binding motif of Cabin1 and HDAC9, respectively (Guo et al., 2007; Han et al., 2005; Han et al., 2003), whereas the third one is the BML-210 complex described herein, which is the first structure showing how a small molecule can bind to MEF2. In all three complexes, the small molecule ligand, whether naturally occurring peptide or synthetic molecule, binds to the deep groove on the surface of MEF2 dimer (FIG. 1). Our previous studies show that Cabin1 and HDAC9 bind MEF2 through similar as well as distinct protein-protein interactions (FIG. 1) Interestingly, BML-210 seems to mimic some aspects of natural ligands in binding to MEF2. For example, the binding of the phenyl ring of PAOA to the central hydrophobic pocket formed by Leu66, Leu67, Thr70, Leu66′, Leu67′ and Thr70′ is reminiscent of that of Leu147 in HDAC9 (FIG. 1). Through detailed analyses of the three structures, we have identified a variety of structural features on the MEF2 groove that may be explored for small molecule binding, including a number of discrete hydrophobic pockets, hydrogen bond donors and acceptors, and several charged residues. We plan to utilize this structural information to design and optimize new series of small molecules that can bind selectively to MEF2.
Example 7
Structure-guided Design of Small Molecule Inhibitors of the MEF2/HDAC Interaction
Using the crystal structures as guide, a large number of PAOA analogs that can provide the basis for identifying new MEF2-active small molecules was designed. The first group of analogs were designed to explore two general elements of the PAOA structure. First is the length and rigidity of the linker. Second are the functional groups and their positions on the two aromatic binding units. The electron density of the linker indicates that it adopts multiple conformations, suggesting non-optimal binding between PAOA and MEF2 in this region. In HDAC9, on the other hand, the aliphatic side chain of Lys144 and Val143 fill up the groove of MEF2 nicely to establish extensive Van der Waals contact and a hydrogen bond. Functional groups introduced at the PAOA linker to mimic/improve these natural interactions may enhance the binding affinity. The designed compounds were subjected to docking analysis mentioned above to filter out energetically unfavorable ones. The remaining molecules were synthesized using standard techniques and subjected to in vitro and in vivo analysis as described previously.
A first series of potential inhibitors (FIG. 2) was synthesized, and already found that different compounds showed significantly different activity in their ability to inhibit the reporter signal in the mammalian two-hybrid assay. Most interestingly, one of these, compound 4, showed similar activity as PAOA but with no effect on the control signal driven by GAL-VP-16, suggesting that this new derivative is more specific than PAOA. The ortho-aminoanilide moiety in PAOA has previously been postulated to be a zinc chelating group that can bind to the active site of class I and class II HDACs, but direct evidence for this mode of action is yet to be obtained. In compound 4, this Zinc chelating group is eliminated by moving the amino group to the meta position. Yet this derivative is as active as PAOA with less nonspecific effect, suggesting that the observed effect of PAOA inside cells, under our assay condition, is mainly due to its ability to disrupt MEF2:HDAC4 interaction rather than inhibiting the catalytic activity.
Example 8
Synthesis of Compound 10
The provided compounds can be prepared by adaptation of methods known in the art. For example, the synthesis of compound 10:




was prepared by the following steps:

    
    
        Step 1: Pimelic acid (1 equiv) and 3-bromoaniline (1 equiv) were added to flask and stirred at 130° C. overnight. The reaction mixture was diluted in EtOAc and extracted with 10% potassium hydroxide. The aqueous layer was acidified to pH ̃2 with conc. HCl and extracted with ethyl acetate. The organic layer was reduced under vacuum and recrystallized with acetonitrile/water.
        Step 2. To a solution of phenylenediamine in dichloromethane was added (Boc)2O (1 equiv) at rt and the mixture was stirred overnight. The reaction was concentrated under vacuum, diluted with ethyl acetate, and was extracted with three times with water and brine. The organic layer was reduced under vacuum and recrystallized chloroform/hexanes.
        Step 3. The product of Step 1 (100 mg) was dissolved in DMSO (3 mL) and to this solution was added Hunig's base (1 equiv), HBTU (1 equiv), and the monoprotected phenylenediamine product of Step 2. The resulting solution was stirred overnight at rt. The solution was diluted with ethyl acetate and extracted with three times with brine. The organic layer was reduced under vacuum and purified by column chromatography (hexanes/ethyl acetate gradient). The isolated product was dissolved in dichloromethane, cooled to ° C. and treated with trifluoroacetic acid (1 mL) The solution was allowed to warm to rt and stirred overnight. The reaction was neutralized with sodium bicarbonate and concentrated under vacuum. The resulting solid was dissolved in ethyl acetate and extracted with a saturated sodium chloride solution. The organic layer was dried with magnesium sulfate, filtered, concentrated under vacuum, and purified by column chromatography (hexanes/ethyl acetate and dichloromethane/methanol gradient). Evaporation of the solvents under vacuum, provided the pure product 10, whose structure and purity was verified by NMR spectroscopy.
    
    


Although the present invention has been described in terms of specific exemplary embodiments and examples, it will be appreciated that the embodiments disclosed herein are for illustrative purposes only and various modifications and alterations might be made by those skilled in the art without departing from the spirit and scope of the invention as set forth in the following claims.
The protein sequence Gly Arg Lys Lys Ile Gln Ile Thr Arg Ile Met Asp Glx Arg Asn Arg Gln Val Thr Phe Thr Lys Arg Lys Phe Gly Leu Met Lys Lys Ala Tyr Glx Leu Ser Val Leu Cys Asp Cys Gly Ile Ala Leu Ile Ile Phe Asn Ser Ser Asn Lys Leu Phe Gln Tyr Ala Ser Thr Asp Met Asp Lys Val Leu Leu Lys Tyr Thr Glx Tyr in Table 1 is SEQ ID NO:4. The protein sequence Gly Arg Lys Lys Ile Gln Ile Thr Arg Ile Met Asp Glx Arg Asn Arg Gln Val Thr Phe Thr Lys Arg Lys Phe Gly Leu Met Lys Lys Ala Tyr Glx Leu Ser Val Leu Cys Asp Cys Gly Ile Ala Leu Ile Ile Phe Asn Ser Ser Asn Lys Leu Phe Gln Tyr Ala Ser Thr Asp Met Asp Lys Val Leu Leu Lys Tyr Thr Glx Tyr Asn in Table 1 is SEQ ID NO:5. The DNA sequence AAAGCTATTATTAGCTT in Table 1 is SEQ ID NO:6. The DNA sequence TAAGCTAATAATAGCTT in Table 1 is SEQ ID NO:7.








TABLE 1







REMARK
Date 2009-01-07 Time 10:43:15 PST -0800 (1231353795.26 s)


REMARK
PHENIX refinement


REMARK


REMARK
****************** INPUT FILES AND LABELS *******************************


REMARK
Reflections:









REMARK
file name
: 3set-bm30-p1.mtz


REMARK
labels
: [′F_nat,SIGF_nat’]








REMARK
R-free flags:









REMARK
file name
: 3set-bm30-p1.mtz


REMARK
label
: FreeR_flag


REMARK
test_flag_value
: 0








REMARK
Model file name(s):


REMARK
/Users/rajadey/bml30/phenix/11.1_001_nr_h_001.pdb_modified.pdb


REMARK


REMARK
******************** REFINEMENT SUMMARY: QUICK FACTS *******************


REMARK
Start: r_work = 0.2261 r_free = 0.2662 bonds = 0.010 angles = 1.585


REMARK
Final: r_work = 0.2300 r_free = 0.2625 bonds = 0.004 angles = 0.999


REMARK
***********************************************************************


REMARK


REMARK
****************** REFINEMENT STATISTICS STEP BY STEP ******************


REMARK
leading digit, like 1_, means number of macro-cycle


REMARK
0  : statistics at the very beginning when nothing is done yet


REMARK
1_bss: bulk solvent correction and/or (anisotropic) scaling


REMARK
1_xyz: refinement of coordinates


REMARK
1_sar: simulated annealing refinement of x,y,z


REMARK
1_gbr: group B-factor refinement


REMARK
------------------------------------------------------------------------








REMARK
R-factors, x-ray target values and norm of gradient of x-ray target












REMARK
stage
r-work
r-free
xray_target_w
xray_target_t












REMARK
0  :
0.3724
0.4597
4.600657e+00
4.693864e+00


REMARK
1_bss:
0.2261
0.2662
4.353757e+00
4.511409e+00


REMARK
1_sar:
0.2304
0.2635
4.369227e+00
4.510175e+00


REMARK
1_xyz:
0.2300
0.2624
4.366691e+00
4.507881e+00


REMARK
1_adp:
0.2313
0.2633
4.364563e+00
4.506710e+00


REMARK
1_bss:
0.2300
0.2625
4.363161e+00
4.505319e+00








REMARK
------------------------------------------------------------------------
















REMARK
stage
k_sol
b_sol
b11
b22
b33
b12
b13
b23
















REMARK
0  :
0.000
0.000
0.000
0.000
0.000
0.000
0.000
0.000


REMARK
1_bss:
0.364
20.242
−6.805
6.192
−3.021
−0.487
0.775
−11.187


REMARK
1_sar:
0.364
20.242
−6.805
6.192
−3.021
−0.487
0.775
−11.187


REMARK
1_xyz:
0.364
20.242
−6.805
6.192
−3.021
−0.487
0.775
−11.187


REMARK
1_adp:
0.364
20.242
−6.805
6.192
−3.021
−0.487
0.775
−11.187


REMARK
1_bss:
0.365
21.349
−5.565
7.438
−1.873
−0.502
0.768
−11.282








REMARK
------------------------------------------------------------------------












REMARK
stage
<pher>
fom
alpha
beta












REMARK
0  :
38.723
0.6722
0.4429
3605.155


REMARK
1_bss:
29.255
0.7800
0.4779
1636.075


REMARK
1_sar:
29.008
0.7829
0.4789
1613.168


REMARK
1_xyz:
29.000
0.7829
0.4786
1605.471


REMARK
1_adp:
28.879
0.7844
0.4600
1604.065


REMARK
1_bss:
28.857
0.7846
0.4744
1600.058








REMARK
------------------------------------------------------------------------















REMARK
stage
angl
bond
chir
dihe
plan
repu
geom_target















REMARK
0  :
1.585
0.010
0.062
24.116
0.004
4.102
1.0603e−01


REMARK
1_bss:
1.585
0.010
0.062
24.116
0.004
4.102
1.0603e−01


REMARK
1_sar:
1.491
0.016
0.080
22.841
0.006
4.104
1.3573e−01


REMARK
1_xyz:
0.999
0.004
0.052
22.782
0.002
4.103
5.3401e−02


REMARK
1_adp:
0.999
0.004
0.052
22.782
0.002
4.103
5.3401e−02


REMARK
1_bss:
0.999
0.004
0.052
22.782
0.002
4.103
5.3401e−02








REMARK
------------------------------------------------------------------------








REMARK
Maximal deviations:















REMARK
stage
angl
bond
chir
dihe
plan
repu
|grad|















REMARK
0  :
19.277
0.072
0.199
87.514
0.017
2.477
7.1857e−02


REMARK
1_bss:
19.277
0.072
0.199
87.514
0.017
2.477
7.1857e−02


REMARK
1_sar:
13.759
0.149
0.349
82.939
0.024
2.483
2.0037e−01


REMARK
1_xyz:
5.840
0.026
0.193
83.107
0.009
2.480
2.2669e−02


REMARK
1_adp:
5.840
0.026
0.193
83.107
0.009
2.480
2.2669e−02


REMARK
1_bss:
5.840
0.026
0.193
83.107
0.009
2.480
2.2669e−02








REMARK
------------------------------------------------------------------------











REMARK
stage
b_max
b_min
b_ave











REMARK
0  :
98.49
10.66
34.81


REMARK
1_bss:
98.49
10.66
34.81


REMARK
1_sar:
98.49
10.66
34.81


REMARK
1_xyz:
98.49
10.66
34.81


REMARK
1_adp:
97.61
8.23
33.04


REMARK
1_bss:
97.70
8.32
33.12








REMARK
------------------------------------------------------------------------









REMARK
stage
Deviation of refined


REMARK

model from start model











REMARK

max
min
mean


REMARK
0  :
0.000
0.000
0.000


REMARK
1_bss:
0.000
0.000
0.000


REMARK
1_sar:
0.779
0.002
0.073


REMARK
1_xyz:
0.781
0.003
0.069


REMARK
1_adp:
0.781
0.003
0.069


REMARK
1_bss:
0.781
0.003
0.069








REMARK
------------------------------------------------------------------------


REMARK
MODEL CONTENT.










REMARK
ELEMENT
ATOM RECORD COUNT
OCCUPANCY SUM


REMARK
P
64
64.00


REMARK
C
2188
2188.00


REMARK
S
20
20.00


REMARK
O
824
824.00


REMARK
N
654
654.00


REMARK
TOTAL
3750
3750.00








REMARK
-----------------------------------------------------------------------


REMARK
r_free_flags.md5.hexdigest c7ab61ecd5d91bd96f477e00cb52bbd9


REMARK


REMARK
IF THIS FILE IS FOR PDB DEPOSITION: REMOVE ALL FROM THIS LINE UP.








REMARK
3









REMARK
3
REFINEMENT.










REMARK
3
PROGRAM
: PHENIX (phenix,refine)


REMARK
3
AUTHORS
: Paul Adams, Pavel Afonine, Vincent Chen, Ian


REMARK
3

: Davis, Kreshna Gopal, Ralf Grosse-Kunstleve,


REMARK
3

: Jeffrey Headd, Li-Wei Hung, Robert


REMARK
3

: Immormino, Tom Ioerger, Airlie McCoy, Erik


REMARK
3

: McKee, Nigel Moriarty, Reetal Pai, Randy


REMARK
3

: Read, Jane Richardson, David Richardson, Tod


REMARK
3

: Romo, Jim Sacchettini, Nicholas Sauter,


REMARK
3

: Jacob Smith, Laurent Storoni, Tom


REMARK
3

: Terwilliger, Peter Zwart


REMARK
3









REMARK
3
REFINEMENT TARGET : ML


REMARK
3



REMARK
3
DATA USED IN REFINEMENT.










REMARK
3
RESOLUTION RANGE HIGH (ANGSTROMS)
: 2.434


REMARK
3
RESOLUTION RANGE LOW (ANGSTROMS)
: 33.444


REMARK
3
MIN(FOBS/SIGMA_FOBS)
: 2.00











REMARK
3
COMPLETENESS FOR RANGE
(%)
: 94.76










REMARK
3
NUMBER OF REFLECTIONS
: 19820


REMARK
3












REMARK
3
FIT TO DATA USED IN REFINEMENT.











REMARK
3
R VALUE (WORKING + TEST SET)
: 0.2318











REMARK
3
R VALUE
 (WORKING SET)
: 0.2300










REMARK
3
FREE R VALUE
: 0.2625











REMARK
3
FREE R VALUE TEST SET SIZE
(%)
: 5.18










REMARK
3
FREE R VALUE TEST SET COUNT
: 1026


REMARK
3









REMARK
3
FIT TO DATA USED IN REFINEMENT (IN BINS).















REMARK
3
BIN
RESOLUTION RANGE
COMPL.
NWORK
NFREE
RWORK
RFREE


REMARK
3
1
33.4475 - 4.6528
0.98
2734
158
0.1822
0.2100


REMARK
3
2
4.6528 - 3.6946
0.96
2695
176
0.1877
0.2158


REMARK
3
3
3.6946 - 3.2280
0.96
2707
127
0.2008
0.2520


REMARK
3
4
3.2280 - 2.9331
0.95
2707
141
0.2463
0.2810


REMARK
3
5
2.9331 - 2.7229
0.95
2703
142
0.2703
0.3447


REMARK
3
6
2.7229 - 2.5624
0.95
2664
142
0.2602
0.2953


REMARK
3
7
2.5624 - 2.4342
0.89
2584
140
0.2774
0.3272


REMARK
3









REMARK
3
BULK SOLVENT MODELLING.










REMARK
3
METHOD USED
: FLAT BULK SOLVENT MODEL


REMARK
3
SOLVENT RADIUS
: 1.11


REMARK
3
SHRINKAGE RADIUS
: 0.90


REMARK
3
GRID STEP FACTOR
: 4.00


REMARK
3
K_SOL
: 0.365


REMARK
3
B_SOL
: 21.349









REMARK
3



REMARK
3
ERROR ESTIMATES.









REMARK
3
COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)  : 0.40


REMARK
3
PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.86


REMARK
3









REMARK
3
OVERALL SCALE FACTORS.









REMARK
3
SCALE = SUM(|F_OBS|*|F_MODEL|)/SUM(|F_MODEL|**2) : 0.5328


REMARK
3
ANISOTROPIC SCALE MATRIX ELEMENTS (IN CARTESIAN BASIS).









REMARK
3
B11 : −5.5649


REMARK
3
B22 : 7.4379


REMARK
3
B33 : −1.8730


REMARK
3
B12 : −0.5019


REMARK
3
B13 : 0.7684


REMARK
3
B23 : −11.2823


REMARK
3









REMARK
3
R FACTOR FORMULA.









REMARK
3
R = SUM(||F_OBS|−SCALE*|F_MODEL||)/SUM(|F_OBS|)


REMARK
3









REMARK
3
TOTAL MODEL STRUCTURE FACTOR (F_MODEL).









REMARK
3
F_MODEL = FB_CART * (F_CALC_ATOMS + F_BULK)









REMARK
3
F_BULK = K_SOL * EXP(−B_SOL * S**2 / 4) * F_MASK


REMARK
3
F_CALC_ATOMS = ATOMIC MODEL STRUCTURE FACTORS


REMARK
3
FB_CART = EXP(−H(t) * A(−1) * B * A(−1t) * H)









REMARK
3
A = orthogonalization matrix, H = MILLER INDEX









REMARK
3
(t) = TRANSPOSE, (−1) = INVERSE


REMARK
3









REMARK
3
STRUCTURE FACTORS CALCULATION ALGORITHM : FFT


REMARK
3


REMARK
3
DEVIATIONS FROM IDEAL VALUES.












REMARK
3

RMSD
MAX
COUNT


REMARK
3
BOND
: 0.004
0.026
3944


REMARK
3
ANGLE
: 0.999
5.840
5574


REMARK
3
CHIRALITY
: 0.052
0.193
630


REMARK
3
PLANARITY
: 0.002
0.009
458


REMARK
3
DIHEDRAL
: 22.782
83.107
1588









REMARK
3
MIN NONBONDED DISTANCE : 2.480


REMARK
3









REMARK
3
ATOMIC DISPLACEMENT PARAMETERS.









REMARK
3
WILSON B : 32.79


REMARK
3
RMS(B_ISO_OR_EQUIVALENT_BONDED) : 5.16










REMARK
3
ATOMS
NUMBER OF ATOMS











REMARK
3

ISO.
ANISO.


REMARK
3
ALL
: 3750
0


REMARK
3
ALL (NO H)
: 3750
0


REMARK
3
SOLVENT
: 0
0


REMARK
3
NON-SOLVENT
: 3750
0


REMARK
3
HYDROGENS
: 0
0


REMARK
3














CRYST1
41.567
61.622
61.478
114.12
89.99
89.95
P 1











SCALE1
0.024058
−0.000021
−0.000013
0.00000


SCALE2
0.000000
0.016228
0.007267
0.00000


SCALE3
0.000000
0.000000
0.017822
0.00000


















ATOM
1
N
GLY A
2
5.558
9.665
−0.148
1.00
40.48
A
N


ATOM
2
CA
GLY A
2
6.598
10.216
0.701
1.00
40.72
A
C


ATOM
3
C
GLY A
2
7.400
11.294
−0.003
1.00
44.33
A
C


ATOM
4
O
GLY A
2
7.374
11.395
−1.230
1.00
46.18
A
O


ATOM
5
N
ARG A
3
8.110
12.105
0.774
1.00
36.20
A
N


ATOM
6
CA
ARG A
3
8.920
13.177
0.212
1.00
36.54
A
C


ATOM
7
C
ARG A
3
9.915
12.608
−0.791
1.00
39.57
A
C


ATOM
8
O
ARG A
3
10.208
13.222
−1.818
1.00
41.96
A
O


ATOM
9
CB
ARG A
3
9.649
13.937
1.320
1.00
35.42
A
C


ATOM
10
CG
ARG A
3
8.729
14.765
2.204
1.00
35.12
A
C


ATOM
11
CD
ARG A
3
7.761
15.588
1.364
1.00
39.80
A
C


ATOM
12
NE
ARG A
3
6.939
16.479
2.177
1.00
35.64
A
N


ATOM
13
CZ
ARG A
3
7.340
17.668
2.620
1.00
40.68
A
C


ATOM
14
NH1
ARG A
3
8.558
18.111
2.336
1.00
32.06
A
N


ATOM
15
NH2
ARG A
3
6.522
18.412
3.353
1.00
37.63
A
N


ATOM
16
N
LYS A
4
10.426
11.423
−0.481
1.00
34.29
A
N


ATOM
17
CA
LYS A
4
11.319
10.710
−1.377
1.00
36.15
A
C


ATOM
18
C
LYS A
4
10.906
9.247
−1.456
1.00
40.15
A
C


ATOM
19
O
LYS A
4
10.372
8.689
−0.494
1.00
32.40
A
O


ATOM
20
CB
LYS A
4
12.772
10.822
−0.901
1.00
37.35
A
C


ATOM
21
CG
LYS A
4
13.368
12.214
−1.063
1.00
39.95
A
C


ATOM
22
CD
LYS A
4
13.177
12.709
−2.489
1.00
40.70
A
C


ATOM
23
CE
LYS A
4
13.272
14.224
−2.579
1:00
54.15
A
C


ATOM
24
NZ
LYS A
4
12.727
14.727
−3.875
1.00
47.90
A
N


ATOM
25
N
LYS A
5
11.141
8.633
−2.609
1.00
47.06
A
N


ATOM
26
CA
LYS A
5
10.950
7.199
−2.740
1.00
44.41
A
C


ATOM
27
C
LYS A
5
12.022
6.496
−1.927
1.00
46.84
A
C


ATOM
28
O
LYS A
5
13.159
6.963
−1.860
1.00
51.80
A
O


ATOM
29
CB
LYS A
5
11.037
6.767
−4.203
1.00
41.74
A
C


ATOM
30
CG
LYS A
5
11.031
5.260
−4.387
1.00
49.22
A
C


ATOM
31
CD
LYS A
5
10.524
4.863
−5.762
1.00
45.09
A
C


ATOM
32
CE
LYS A
5
10.369
3.358
−5.865
1.00
49.10
A
C


ATOM
33
NZ
LYS A
5
9.791
2.946
−7.171
1.00
54.49
A
N


ATOM
34
N
ILE A
6
11.661
5.385
−1.296
1.00
40.65
A
N


ATOM
35
CA
ILE A
6
12.634
4.589
−0.561
1.00
38.64
A
C


ATOM
36
C
ILE A
6
12.794
3.198
−1.156
1.00
44.27
A
C


ATOM
37
O
ILE A
6
11.989
2.759
−1.979
1.00
45.26
A
O


ATOM
38
CB
ILE A
6
12.258
4.448
0.920
1.00
41.86
A
C


ATOM
39
CG1
ILE A
6
11.049
3.527
1.083
1.00
37.25
A
C


ATOM
40
CG2
ILE A
6
11.993
5.811
1.527
1.00
44.72
A
C


ATOM
41
CD1
ILE A
6
10.760
3.169
2.524
1.00
38.36
A
C


ATOM
42
N
GLN A
7
13.848
2.512
−0.740
1.00
46.69
A
N


ATOM
43
CA
GLN A
7
14.063
1.137
−1.149
1.00
45.95
A
C


ATOM
44
C
GLN A
7
13.629
0.232
−0.017
1.00
44.14
A
C


ATOM
45
O
GLN A
7
13.755
0.587
1.154
1.00
43.70
A
O


ATOM
46
CB
GLN A
7
15.533
0.894
−1.493
1.00
54.70
A
C


ATOM
47
CG
GLN A
7
15.980
1.567
−2.781
1.00
56.91
A
C


ATOM
48
CD
GLN A
7
15.079
1.227
−3.957
1.00
73.33
A
C


ATOM
49
OE1
GLN A
7
14.583
0.104
−4.071
1.00
77.38
A
O


ATOM
50
NE2
GLN A
7
14.865
2.199
−4.840
1.00
72.72
A
N


ATOM
51
N
ILE A
8
13.100
−0.933
−0.363
1.00
29.95
A
N


ATOM
52
CA
ILE A
8
12.650
−1.870
0.650
1.00
22.66
A
C


ATOM
53
C
ILE A
8
13.831
−2.654
1.210
1.00
25.91
A
C


ATOM
54
O
ILE A
8
14.156
−3.748
0.749
1.00
26.66
A
O


ATOM
55
CB
ILE A
8
11.550
−2.801
0.113
1.00
22.42
A
C


ATOM
56
CG1
ILE A
8
10.316
−1.972
−0.262
1.00
28.59
A
C


ATOM
57
CG2
ILE A
8
11.171
−3.841
1.145
1.00
19.64
A
C


ATOM
58
CD1
ILE A
8
9.862
−1.025
0.835
1.00
23.12
A
C


ATOM
59
N
THR A
9
14.483
−2.072
2.208
1.00
25.29
A
N


ATOM
60
CA
THR A
9
15.574
−2.752
2.889
1.00
25.71
A
C


ATOM
61
C
THR A
9
15.621
−2.310
4.343
1.00
23.18
A
C


ATOM
62
O
THR A
9
15.241
−1.185
4.669
1.00
26.78
A
O


ATOM
63
CB
THR A
9
16.930
−2.491
2.204
1.00
29.73
A
C


ATOM
64
OG1
THR A
9
17.943
−3.307
2.811
1.00
36.44
A
O


ATOM
65
CG2
THR A
9
17.316
−1.019
2.312
1.00
22.13
A
C


ATOM
66
N
ARG A
10
16.078
−3.209
5.209
1.00
22.93
A
N


ATOM
67
CA
ARG A
10
16.159
−2.950
6.642
1.00
28.37
A
C


ATOM
68
C
ARG A
10
16.693
−1.557
6.955
1.00
26.68
A
C


ATOM
69
O
ARG A
10
17.735
−1.148
6.443
1.00
27.49
A
O


ATOM
70
CB
ARG A
10
17.023
−4.007
7.327
1.00
26.07
A
C


ATOM
71
CG
ARG A
10
16.937
−3.984
8.836
1.00
25.73
A
C


ATOM
72
CD
ARG A
10
17.825
−5.050
9.458
1.00
26.43
A
C


ATOM
73
NE
ARG A
10
17.850
−4.937
10.912
1.00
42.58
A
N


ATOM
74
CZ
ARG A
10
18.617
−4.080
11.579
1.00
36.16
A
C


ATOM
75
NH1
ARG A
10
19.426
−3.263
10.917
1.00
40.67
A
N


ATOM
76
NH2
ARG A
10
18.578
−4.039
12.906
1.00
33.57
A
N


ATOM
77
N
ILE A
11
15.952
−0.833
7.785
1.00
16.41
A
N


ATOM
78
CA
ILE A
11
16.335
0.494
8.233
1.00
19.58
A
C


ATOM
79
C
ILE A
11
17.336
0.359
9.378
1.00
23.29
A
C


ATOM
80
O
ILE A
11
17.026
−0.225
10.420
1.00
24.17
A
O


ATOM
81
CB
ILE A
11
15.093
1.288
8.695
1.00
24.31
A
C


ATOM
82
CG1
ILE A
11
14.176
1.563
7.502
1.00
17.73
A
C


ATOM
83
CG2
ILE A
11
15.493
2.592
9.378
1.00
17.50
A
C


ATOM
84
CD1
ILE A
11
12.849
2.159
7.874
1.00
19.62
A
C


ATOM
85
N
MET A
12
18.540
0.887
9.176
1.00
25.66
A
N


ATOM
86
CA
MET A
12
19.642
0.655
10.103
1.00
32.46
A
C


ATOM
87
C
MET A
12
19.527
1.503
11.367
1.00
32.06
A
C


ATOM
88
O
MET A
12
20.041
1.130
12.419
1.00
31.35
A
O


ATOM
89
CB
MET A
12
20.989
0.904
9.414
1.00
27.61
A
C


ATOM
90
CG
MET A
12
21.231
0.039
8.175
1.00
32.68
A
C


ATOM
91
SD
MET A
12
21.173
−1.741
8.497
1.00
34.64
A
S


ATOM
92
CE
MET A
12
22.666
−1.967
9.473
1.00
28.81
A
C


ATOM
93
N
ASP A
13
18.851
2.643
11.249
1.00
53.42
A
N


ATOM
94
CA
ASP A
13
18.670
3.570
12.363
1.00
55.93
A
C


ATOM
95
C
ASP A
13
17.489
3.150
13.238
1.00
51.35
A
C


ATOM
96
O
ASP A
13
16.336
3.215
12.809
1.00
49.36
A
O


ATOM
97
CB
ASP A
13
18.460
4.991
11.826
1.00
56.02
A
C


ATOM
98
CG
ASP A
13
17.848
5.929
12.857
1.00
72.21
A
C


ATOM
99
OD1
ASP A
13
18.235
5.856
14.043
1.00
78.94
A
O


ATOM
100
OD2
ASP A
13
16.982
6.749
12.477
1.00
67.36
A
O


ATOM
101
N
GLU A
14
17.786
2.721
14.462
1.00
23.30
A
N


ATOM
102
CA
GLU A
14
16.768
2.257
15.407
1.00
28.94
A
C


ATOM
103
C
GLU A
14
15.663
3.287
15.636
1.00
34.28
A
C


ATOM
104
O
GLU A
14
14.500
2.934
15.842
1.00
26.54
A
O


ATOM
105
CB
GLU A
14
17.416
1.898
16.746
1.00
26.47
A
C


ATOM
106
CG
GLU A
14
16.449
1.557
17.868
1.00
28.84
A
C


ATOM
107
CD
GLU A
14
17.134
1.534
19.235
1.00
56.72
A
C


ATOM
108
OE1
GLU A
14
17.945
2.448
19.516
1.00
62.38
A
O


ATOM
109
OE2
GLU A
14
16.862
0.607
20.031
1.00
47.25
A
O


ATOM
110
N
ARG A
15
16.028
4.562
15.600
1.00
47.85
A
N


ATOM
111
CA
ARG A
15
15.056
5.624
15.804
1.00
40.56
A
C


ATOM
112
C
ARG A
15
14.036
5.672
14.670
1.00
36.17
A
C


ATOM
113
O
ARG A
15
12.834
5.592
14.914
1.00
32.41
A
O


ATOM
114
CB
ARG A
15
15.755
6.974
15.963
1.00
49.45
A
C


ATOM
115
CG
ARG A
15
14.860
8.051
16.537
1.00
54.99
A
C


ATOM
116
CD
ARG A
15
15.619
8.954
17.492
1.00
65.98
A
C


ATOM
117
NE
ARG A
15
14.821
9.226
18.684
1.00
72.44
A
N


ATOM
118
CZ
ARG A
15
14.831
8.464
19.774
1.00
68.90
A
C


ATOM
119
NH1
ARG A
15
15.607
7.387
19.827
1.00
77.09
A
N


ATOM
120
NH2
ARG A
15
14.067
8.778
20.813
1.00
50.97
A
N


ATOM
121
N
ASN A
16
14.511
5.798
13.433
1.00
34.37
A
N


ATOM
122
CA
ASN A
16
13.610
5.821
12.282
1.00
30.83
A
C


ATOM
123
C
ASN A
16
12.915
4.478
12.068
1.00
26.73
A
C


ATOM
124
O
ASN A
16
11.836
4.417
11.485
1.00
25.88
A
O


ATOM
125
CB
ASN A
16
14.340
6.245
11.000
1.00
36.12
A
C


ATOM
126
CG
ASN A
16
13.409
6.283
9.777
1.00
44.40
A
C


ATOM
127
OD1
ASN A
16
12.378
6.962
9.784
1.00
34.71
A
O


ATOM
128
ND2
ASN A
16
13.776
5.552
8.725
1.00
30.96
A
N


ATOM
129
N
ARG A
17
13.530
3.399
12.535
1.00
19.72
A
N


ATOM
130
CA
ARG A
17
12.931
2.088
12.349
1.00
22.57
A
C


ATOM
131
C
ARG A
17
11.716
1.960
13.253
1.00
23.83
A
C


ATOM
132
O
ARG A
17
10.688
1.407
12.862
1.00
22.36
A
O


ATOM
133
CB
ARG A
17
13.935
0.969
12.626
1.00
19.23
A
C


ATOM
134
CG
ARG A
17
13.410
−0.412
12.279
1.00
19.82
A
C


ATOM
135
CD
ARG A
17
14.508
−1.472
12.340
1.00
23.69
A
C


ATOM
136
NE
ARG A
17
15.061
−1.590
13.683
1.00
27.46
A
N


ATOM
137
CZ
ARG A
17
16.306
−1.263
14.017
1.00
30.61
A
C


ATOM
138
NH1
ARG A
17
17.159
−0.816
13.097
1.00
23.50
A
N


ATOM
139
NH2
ARG A
17
16.701
−1.399
15.276
1.00
31.20
A
N


ATOM
140
N
GLN A
18
11.842
2.487
14.465
1.00
28.12
A
N


ATOM
141
CA
GLN A
18
10.745
2.492
15.423
1.00
29.50
A
C


ATOM
142
C
GLN A
18
9.583
3.356
14.921
1.00
25.82
A
C


ATOM
143
O
GLN A
18
8.423
2.952
14.994
1.00
21.13
A
O


ATOM
144
CB
GLN A
18
11.245
2.984
16.787
1.00
25.64
A
C


ATOM
145
CG
GLN A
18
10.148
3.365
17.764
1.00
26.78
A
C


ATOM
146
CD
GLN A
18
9.184
2.227
18.041
1.00
41.07
A
C


ATOM
147
OE1
GLN A
18
9.474
1.063
17.760
1.00
49.03
A
O


ATOM
148
NE2
GLN A
18
8.024
2.562
18.601
1.00
51.07
A
N


ATOM
149
N
VAL A
19
9.910
4.541
14.410
1.00
27.77
A
N


ATOM
150
CA
VAL A
19
8.916
5.456
13.861
1.00
26.66
A
C


ATOM
151
C
VAL A
19
8.195
4.853
12.660
1.00
30.61
A
C


ATOM
152
O
VAL A
19
6.964
4.827
12.610
1.00
30.39
A
O


ATOM
153
CB
VAL A
19
9.561
6.781
13.424
1.00
29.19
A
C


ATOM
154
CG1
VAL A
19
8.619
7.558
12.511
1.00
27.30
A
C


ATOM
155
CG2
VAL A
19
9.944
7.606
14.640
1.00
27.00
A
C


ATOM
156
N
THR A
20
8.965
4.376
11.689
1.00
24.75
A
N


ATOM
157
CA
THR A
20
8.387
3.772
10.501
1.00
25.94
A
C


ATOM
158
C
THR A
20
7.502
2.592
10.884
1.00
25.46
A
C


ATOM
159
O
THR A
20
6.453
2.356
10.277
1.00
23.02
A
O


ATOM
160
CB
THR A
20
9.473
3.280
9.537
1.00
28.24
A
C


ATOM
161
OG1
THR A
20
10.148
4.405
8.961
1.00
26.89
A
O


ATOM
162
CG2
THR A
20
8.850
2.434
8.430
1.00
23.49
A
C


ATOM
163
N
PHE A
21
7.930
1.853
11.898
1.00
22.67
A
N


ATOM
164
CA
PHE A
21
7.191
0.675
12.326
1.00
25.01
A
C


ATOM
165
C
PHE A
21
5.824
1.033
12.904
1.00
23.93
A
C


ATOM
166
O
PHE A
21
4.838
0.345
12.545
1.00
23.30
A
O


ATOM
167
CB
PHE A
21
7.996
−0.136
13.339
1.00
20.65
A
C


ATOM
168
CG
PHE A
21
7.201
−1.214
14.011
1.00
22.59
A
C


ATOM
169
CD1
PHE A
21
7.028
−2.448
13.400
1.00
17.85
A
C


ATOM
170
CD2
PHE A
21
6.616
−0.993
15.249
1.00
22.78
A
C


ATOM
171
CE1
PHE A
21
6.300
−3.446
14.014
1.00
20.66
A
C


ATOM
172
CE2
PHE A
21
5.876
−1.989
15.872
1.00
23.04
A
C


ATOM
173
CZ
PHE A
21
5.720
−3.218
15.255
1.00
27.67
A
C


ATOM
174
N
THR A
22
5.767
2.102
13.690
1.00
17.65
A
N


ATOM
175
CA
THR A
22
4.503
2.537
14.271
1.00
18.23
A
C


ATOM
176
C
THR A
22
3.548
3.066
13.196
1.00
16.79
A
C


ATOM
177
O
THR A
22
2.354
2.772
13.221
1.00
17.70
A
O


ATOM
178
CB
THR A
22
4.703
3.611
15.378
1.00
19.42
A
C


ATOM
179
OG1
THR A
22
5.340
3.023
16.521
1.00
16.50
A
O


ATOM
180
CG2
THR A
22
3.365
4.185
15.803
1.00
13.05
A
C


ATOM
181
N
LYS A
23
4.070
3.850
12.258
1.00
21.15
A
N


ATOM
182
CA
LYS A
23
3.245
4.375
11.177
1.00
22.13
A
C


ATOM
183
C
LYS A
23
2.692
3.252
10.312
1.00
21.52
A
C


ATOM
184
O
LYS A
23
1.487
3.165
10.100
1.00
22.00
A
O


ATOM
185
CB
LYS A
23
4.032
5.350
10.300
1.00
25.46
A
C


ATOM
186
CG
LYS A
23
4.247
6.727
10.908
1.00
31.78
A
C


ATOM
187
CD
LYS A
23
5.175
7.556
10.019
1.00
35.00
A
C


ATOM
188
CE
LYS A
23
5.361
8.963
10.558
1.00
38.42
A
C


ATOM
189
NZ
LYS A
23
6.455
9.677
9.844
1.00
36.46
A
N


ATOM
190
N
ARG A
24
3.578
2.393
9.818
1.00
18.04
A
N


ATOM
191
CA
ARG A
24
3.181
1.335
8.887
1.00
17.50
A
C


ATOM
192
C
ARG A
24
2.380
0.210
9.547
1.00
19.35
A
C


ATOM
193
O
ARG A
24
1.571
−0.436
8.878
1.00
18.00
A
O


ATOM
194
CB
ARG A
24
4.395
0.765
8.149
1.00
14.94
A
C


ATOM
195
CG
ARG A
24
4.892
1.624
6.987
1.00
16.36
A
C


ATOM
196
CD
ARG A
24
6.120
0.999
6.313
1.00
15.51
A
C


ATOM
197
NE
ARG A
24
6.453
1.675
5.062
1.00
17.77
A
N


ATOM
198
CZ
ARG A
24
6.091
1.244
3.855
1.00
19.55
A
C


ATOM
199
NH1
ARG A
24
5.388
0.122
3.722
1.00
19.36
A
N


ATOM
200
NH2
ARG A
24
6.430
1.934
2.778
1.00
14.87
A
N


ATOM
201
N
LYS A
25
2.600
−0.029
10.843
1.00
19.64
A
N


ATOM
202
CA
LYS A
25
1.820
−1.041
11.560
1.00
20.34
A
C


ATOM
203
C
LYS A
25
0.370
−0.608
11.601
1.00
20.24
A
C


ATOM
204
O
LYS A
25
−0.537
−1.397
11.351
1.00
20.44
A
O


ATOM
205
CB
LYS A
25
2.326
−1.257
12.987
1.00
26.21
A
C


ATOM
206
CG
LYS A
25
1.347
−2.046
13.867
1.00
22.43
A
C


ATOM
207
CD
LYS A
25
2.031
−2.639
15.101
1.00
28.10
A
C


ATOM
208
CE
LYS A
25
2.524
−1.564
16.083
1.00
24.12
A
C


ATOM
209
NZ
LYS A
25
1.411
−0.839
16.761
1.00
21.37
A
N


ATOM
210
N
PHE A
26
0.160
0.661
11.917
1.00
16.23
A
N


ATOM
211
CA
PHE A
26
−1.165
1.248
11.835
1.00
18.62
A
C


ATOM
212
C
PHE A
26
−1.732
1.076
10.415
1.00
18.38
A
C


ATOM
213
O
PHE A
26
−2.837
0.573
10.234
1.00
19.75
A
O


ATOM
214
CB
PHE A
26
−1.101
2.727
12.213
1.00
15.46
A
C


ATOM
215
CG
PHE A
26
−2.443
3.384
12.314
1.00
19.64
A
C


ATOM
216
CD1
PHE A
26
−3.053
3.558
13.548
1.00
22.13
A
C


ATOM
217
CD2
PHE A
26
−3.095
3.834
11.177
1.00
17.94
A
C


ATOM
218
CE1
PHE A
26
−4.290
4.168
13.645
1.00
23.01
A
C


ATOM
219
CE2
PHE A
26
−4.329
4.440
11.266
1.00
21.01
A
C


ATOM
220
CZ
PHE A
26
−4.929
4.609
12.505
1.00
27.60
A
C


ATOM
221
N
GLY A
27
−0.962
1.487
9.413
1.00
27.12
A
N


ATOM
222
CA
GLY A
27
−1.369
1.366
8.024
1.00
25.34
A
C


ATOM
223
C
GLY A
27
−1.735
−0.049
7.618
1.00
23.53
A
C


ATOM
224
O
GLY A
27
−2.658
−0.250
6.832
1.00
25.30
A
O


ATOM
225
N
LEU A
28
−1.017
−1.032
8.154
1.00
20.30
A
N


ATOM
226
CA
LEU A
28
−1.255
−2.431
7.800
1.00
20.79
A
C


ATOM
227
C
LEU A
28
−2.542
−2.957
8.432
1.00
19.85
A
C


ATOM
228
O
LEU A
28
−3.313
−3.672
7.790
1.00
17.99
A
O


ATOM
229
CB
LEU A
28
−0.070
−3.310
8.210
1.00
23.59
A
C


ATOM
230
CG
LEU A
28
−0.132
−4.788
7.794
1.00
20.17
A
C


ATOM
231
CD1
LEU A
28
−0.146
−4.926
6.293
1.00
16.98
A
C


ATOM
232
CD2
LEU A
28
1.026
−5.582
8.385
1.00
17.88
A
C


ATOM
233
N
MET A
29
−2.774
−2.585
9.690
1.00
23.01
A
N


ATOM
234
CA
MET A
29
−3.980
−3.002
10.395
1.00
20.12
A
C


ATOM
235
C
MET A
29
−5.208
−2.346
9.777
1.00
18.22
A
C


ATOM
236
O
MET A
29
−6.250
−2.976
9.629
1.00
16.78
A
O


ATOM
237
CB
MET A
29
−3.889
−2.672
11.887
1.00
20.50
A
C


ATOM
238
CG
MET A
29
−2.792
−3.423
12.641
1.00
20.16
A
C


ATOM
239
SD
MET A
29
−3.158
−3.552
14.417
1.00
22.93
A
S


ATOM
240
CE
MET A
29
−1.718
−4.473
14.963
1.00
25.26
A
C


ATOM
241
N
LYS A
30
−5.082
−1.079
9.406
1.00
21.44
A
N


ATOM
242
CA
LYS A
30
−6.195
−0.385
8.770
1.00
22.10
A
C


ATOM
243
C
LYS A
30
−6.676
−1.145
7.529
1.00
21.81
A
C


ATOM
244
O
LYS A
30
−7.861
−1.459
7.403
1.00
24.17
A
O


ATOM
245
CB
LYS A
30
−5.813
1.053
8.416
1.00
20.87
A
C


ATOM
246
CG
LYS A
30
−6.980
1.885
7.914
1.00
29.30
A
C


ATOM
247
CD
LYS A
30
−6.575
3.329
7.647
1.00
29.06
A
C


ATOM
248
CE
LYS A
30
−7.756
4.132
7.118
1.00
35.72
A
C


ATOM
249
NZ
LYS A
30
−7.340
5.436
6.528
1.00
30.83
A
N


ATOM
250
N
LYS A
31
−5.756
−1.460
6.623
1.00
18.84
A
N


ATOM
251
CA
LYS A
31
−6.119
−2.177
5.399
1.00
22.05
A
C


ATOM
252
C
LYS A
31
−6.644
−3.592
5.653
1.00
17.61
A
C


ATOM
253
O
LYS A
31
−7.568
−4.043
4.985
1.00
21.05
A
O


ATOM
254
CB
LYS A
31
−4.951
−2.188
4.412
1.00
18.86
A
C


ATOM
255
CG
LYS A
31
−4.954
−0.991
3.476
1.00
20.01
A
C


ATOM
256
CD
LYS A
31
−3.565
−0.685
2.946
1.00
22.22
A
C


ATOM
257
CE
LYS A
31
−3.641
0.064
1.623
1.00
21.55
A
C


ATOM
258
NZ
LYS A
31
−4.901
0.856
1.487
1.00
21.23
A
N


ATOM
259
N
ALA A
32
−6.069
−4.283
6.630
1.00
13.45
A
N


ATOM
260
CA
ALA A
32
−6.528
−5.624
6.967
1.00
13.40
A
C


ATOM
261
C
ALA A
32
−7.983
−5.576
7.417
1.00
17.70
A
C


ATOM
262
O
ALA A
32
−8.813
−6.346
6.928
1.00
17.45
A
O


ATOM
263
CB
ALA A
32
−5.645
−6.244
8.043
1.00
12.68
A
C


ATOM
264
N
TYR A
33
−8.285
−4.664
8.343
1.00
22.08
A
N


ATOM
265
CA
TYR A
33
−9.655
−4.417
8.791
1.00
21.79
A
C


ATOM
266
C
TYR A
33
−10.596
−4.066
7.633
1.00
24.76
A
C


ATOM
267
O
TYR A
33
−11.714
−4.577
7.554
1.00
25.28
A
O


ATOM
268
CB
TYR A
33
−9.682
−3.303
9.848
1.00
26.33
A
C


ATOM
269
CG
TYR A
33
−11.001
−2.557
9.934
1.00
24.65
A
C


ATOM
270
CD1
TYR A
33
−12.060
−3.060
10.676
1.00
28.98
A
C


ATOM
271
CD2
TYR A
33
−11.184
−1.349
9.271
1.00
26.32
A
C


ATOM
272
CE1
TYR A
33
−13.266
−2.382
10.757
1.00
30.58
A
C


ATOM
273
CE2
TYR A
33
−12.389
−0.664
9.341
1.00
25.98
A
C


ATOM
274
CZ
TYR A
33
−13.424
−1.185
10.087
1.00
31.84
A
C


ATOM
275
OH
TYR A
33
−14.621
−0.509
10.165
1.00
30.84
A
O


ATOM
276
N
GLU A
34
−10.146
−3.187
6.744
1.00
23.16
A
N


ATOM
277
CA
GLU A
34
−10.947
−2.799
5.589
1.00
21.92
A
C


ATOM
278
C
GLU A
34
−11.227
−3.986
4.675
1.00
22.46
A
C


ATOM
279
O
GLU A
34
−12.328
−4.113
4.129
1.00
22.16
A
O


ATOM
280
CB
GLU A
34
−10.266
−1.673
4.810
1.00
21.12
A
C


ATOM
281
CG
GLU A
34
−10.229
−0.344
5.557
1.00
20.36
A
C


ATOM
282
CD
GLU A
34
−9.648
0.778
4.718
1.00
21.90
A
C


ATOM
283
OE1
GLU A
34
−9.002
0.483
3.690
1.00
23.00
A
O


ATOM
284
OE2
GLU A
34
−9.836
1.956
5.081
1.00
19.62
A
O


ATOM
285
N
LEU A
35
−10.244
−4.867
4.520
1.00
19.11
A
N


ATOM
286
CA
LEU A
35
−10.450
−6.059
3.696
1.00
19.55
A
C


ATOM
287
C
LEU A
35
−11.446
−7.026
4.342
1.00
20.70
A
C


ATOM
288
O
LEU A
35
−12.263
−7.643
3.652
1.00
22.13
A
O


ATOM
289
CB
LEU A
35
−9.129
−6.769
3.392
1.00
16.66
A
C


ATOM
290
CG
LEU A
35
−9.271
−8.010
2.511
1.00
19.14
A
C


ATOM
291
CD1
LEU A
35
−9.903
−7.645
1.173
1.00
17.50
A
C


ATOM
292
CD2
LEU A
35
−7.933
−8.701
2.306
1.00
18.21
A
C


ATOM
293
N
SER A
36
−11.379
−7.157
5.662
1.00
22.42
A
N


ATOM
294
CA
SER A
36
−12.327
−8.001
6.379
1.00
27.64
A
C


ATOM
295
C
SER A
36
−13.764
−7.538
6.134
1.00
24.59
A
C


ATOM.
296
O
SER A
36
−14.650
−8.346
5.866
1.00
26.35
A
O


ATOM
297
CB
SER A
36
−12.026
−8.000
7.879
1.00
29.01
A
C


ATOM
298
OG
SER A
36
−12.983
−8.771
8.588
1.00
28.5I
A
O


ATOM
299
N
VAL A
37
−13.983
−6.230
6.217
1.00
20.31
A
N


ATOM
300
CA
VAL A
37
−15.321
−5.664
6.084
1.00
19.68
A
C


ATOM
301
C
VAL A
37
−15.815
−5.656
4.637
1.00
21.49
A
C


ATOM
302
O
VAL A
37
−16.905
−6.141
4.344
1.00
21.28
A
O


ATOM
303
CB
VAL A
37
−15.382
−4.229
6.643
1.00
20.47
A
C


ATOM
304
CG1
VAL A
37
−16.750
−3.610
5.387
1.00
17.32
A
C


ATOM
305
CG2
VAL A
37
−15.060
−4.228
8.124
1.00
21.67
A
C


ATOM
306
N
LEU A
38
−15.016
−5.093
3.738
1.00
24.67
A
N


ATOM
307
CA
LEU A
38
−15.401
−4.971
2.338
1.00
20.97
A
C


ATOM
308
C
LEU A
38
−15.745
−6.319
1.717
1.00
22.62
A
C


ATOM
309
O
LEU A
38
−16.724
−6.438
0.975
1.00
24.77
A
O


ATOM
310
CB
LEU A
38
−14.274
−4.327
1.527
1.00
20.39
A
C


ATOM
311
CG
LEU A
38
−13.936
−2.859
1.771
1.00
18.81
A
C


ATOM
312
CD1
LEU A
38
−12.570
−2.532
1.177
1.00
16.96
A
C


ATOM
313
CD2
LEU A
38
−15.017
−1.951
1.204
1.00
19.42
A
C


ATOM
314
N
CYS A
39
−14.937
−7.331
2.013
1.00
21.00
A
N


ATOM
315
CA
CYS A
39
−15.071
−8.615
1.330
1.00
22.90
A
C


ATOM
316
C
CYS A
39
−15.531
−9.750
2.239
1.00
24.81
A
C


ATOM
317
O
CYS A
39
−15.504
−10.915
1.847
1.00
28.63
A
O


ATOM
318
CB
CYS A
39
−13.757
−8.989
0.640
1.00
18.48
A
C


ATOM
319
SG
CYS A
39
−13.163
−7.706
−0.472
1.00
18.20
A
S


ATOM
320
N
ASP A
40
−15.944
−9.413
3.455
1.00
28.63
A
N


ATOM
321
CA
ASP A
40
−16.503
−10.417
4.351
1.00
30.28
A
C


ATOM
322
C
ASP A
40
−15.583
−11.631
4.483
1.00
31.00
A
C


ATOM
323
O
ASP A
40
−15.878
−12.695
3.944
1.00
30.22
A
O


ATOM
324
CB
ASP A
40
−17.876
−10.858
3.831
1.00
27.25
A
C


ATOM
325
CG
ASP A
40
−18.585
−11.821
4.770
1.00
31.14
A
C


ATOM
326
OD1
ASP A
40
−18.189
−11.932
5.948
1.00
32.84
A
O


ATOM
327
OD2
ASP A
40
−19.552
−12.472
4.318
1.00
47.25
A
O


ATOM
328
N
CYS A
41
−14.469
−11.472
5.192
1.00
28.67
A
N


ATOM
329
CA
CYS A
41
−13.600
−12.611
5.476
1.00
34.11
A
C


ATOM
330
C
CYS A
41
−12.962
−12.566
6.867
1.00
33.64
A
C


ATOM
331
O
CYS A
41
−12.839
−11.500
7.470
1.00
32.01
A
O


ATOM
332
CB
CYS A
41
−12.530
−12.771
4.390
1.00
34.49
A
C


ATOM
333
SG
CYS A
41
−11.901
−11.242
3.695
1.00
42.38
A
S


ATOM
334
N
GLU A
42
−12.589
−13.739
7.377
1.00
35.13
A
N


ATOM
335
CA
GLU A
42
−11.835
−13.837
8.617
1.00
31.41
A
C


ATOM
336
C
GLU A
42
−10.393
−13.499
8.312
1.00
31.12
A
C


ATOM
337
O
GLU A
42
−9.852
−13.934
7.299
1.00
34.59
A
O


ATOM
338
CB
GLU A
42
−11.864
−15.258
9.177
1.00
36.09
A
C


ATOM
339
CG
GLU A
42
−13.223
−15.801
9.546
1.00
50.30
A
C


ATOM
340
CD
GLU A
42
−13.107
−17.105
10.310
1.00
48.91
A
C


ATOM
341
OE1
GLU A
42
−13.992
−17.973
10.160
1.00
69.71
A
O


ATOM
342
OE2
GLU A
42
−12.118
−17.264
11.053
1.00
39.96
A
O


ATOM
343
N
ILE A
43
−9.760
−12.740
9.196
1.00
22.52
A
N


ATOM
344
CA
ILE A
43
−8.359
−12.401
9.012
1.00
18.82
A
C


ATOM
345
C
ILE A
43
−7.604
−12.413
10.333
1.00
18.26
A
C


ATOM
346
O
ILE A
43
−8.152
−12.074
11.378
1.00
19.33
A
O


ATOM
347
CB
ILE A
43
−8.204
−11.046
8.308
1.00
18.81
A
C


ATOM
348
CG1
ILE A
43
−8.579
−11.199
6.828
1.00
19.26
A
C


ATOM
349
CG2
ILE A
43
−6.774
−10.523
8.471
1.00
14.71
A
C


ATOM
350
CD1
ILE A
43
−8.902
−9.910
6.115
1.00
17.63
A
C


ATOM
351
N
ALA A
44
−6.347
−12.832
10.282
1.00
20.70
A
N


ATOM
352
CA
ALA A
44
−5.490
−12.809
11.456
1.00
22.51
A
C


ATOM
353
C
ALA A
44
−4.138
−12.232
11.077
1.00
21.54
A
C


ATOM
354
O
ALA A
44
−3.557
−12.601
10.061
1.00
24.49
A
O


ATOM
355
CB
ALA A
44
−5.335
−14.210
12.044
1.00
20.18
A
C


ATOM
356
N
LEU A
45
−3.645
−11.321
11.902
1.00
17.20
A
N


ATOM
357
CA
LEU A
45
−2.373
−10.673
11.656
1.00
15.17
A
C


ATOM
358
C
LEU A
45
−1.574
−10.679
12.949
1.00
18.70
A
C


ATOM
359
O
LEU A
45
−1.992
−10.088
13.944
1.00
18.56
A
O


ATOM
360
CB
LEU A
45
−2.605
−9.233
11.184
1.00
17.70
A
C


ATOM
361
CG
LEU A
45
−1.376
−8.343
10.969
1.00
18.97
A
C


ATOM
362
CD1
LEU A
45
−0.350
−9.045
10.095
1.00
13.61
A
C


ATOM
363
CD2
LEU A
45
−1.769
−6.995
10.371
1.00
15.25
A
C


ATOM
364
N
ILE A
46
−0.435
−11.361
12.938
1.00
26.22
A
N


ATOM
365
CA
ILE A
46
0.447
−11.399
14.100
1.00
28.53
A
C


ATOM
366
C
ILE A
46
1.785
−10.754
13.769
1.00
28.91
A
C


ATOM
367
O
ILE A
46
2.450
−11.141
12.804
1.00
26.44
A
O


ATOM
368
CB
ILE A
46
0.683
−12.842
14.585
1.00
31.11
A
C


ATOM
369
CG1
ILE A
46
−0.604
−13.416
15.186
1.00
29.74
A
C


ATOM
370
CG2
ILE A
46
1.810
−12.883
15.600
1.00
27.36
A
C


ATOM
371
CD1
ILE A
46
−0.564
−14.908
15.418
1.00
29.20
A
C


ATOM
372
N
ILE A
47
2.179
−9.771
14.572
1.00
23.77
A
N


ATOM
373
CA
ILE A
47
3.412
−9.032
14.328
1.00
24.05
A
C


ATOM
374
C
ILE A
47
4.284
−8.942
15.572
1.00
24.16
A
C


ATOM
375
O
ILE A
47
3.843
−8.444
16.608
1.00
27.34
A
O


ATOM
376
CB
ILE A
47
3.118
−7.585
13.884
1.00
24.61
A
C


ATOM
377
CG1
ILE A
47
2.161
−7.561
12.691
1.00
22.79
A
C


ATOM
378
CG2
ILE A
47
4.420
−6.847
13.569
1.00
25.34
A
C


ATOM
379
CD1
ILE A
47
1.725
−6.168
12.318
1.00
20.83
A
C


ATOM
380
N
PHE A
48
5.521
−9.410
15.467
1.00
22.85
A
N


ATOM
381
CA
PHE A
48
6.512
−9.211
16.518
1.00
22.42
A
C


ATOM
382
C
PHE A
48
7.548
−8.240
15.990
1.00
25.30
A
C


ATOM
383
O
PHE A
48
8.218
−8.543
15.007
1.00
29.18
A
O


ATOM
384
CB
PHE A
48
7.226
−10.522
16.859
1.00
25.20
A
C


ATOM
385
CG
PHE A
48
6.317
−11.609
17.348
1.00
23.66
A
C


ATOM
386
CD1
PHE A
48
5.817
−12.556
16.471
1.00
22.65
A
C


ATOM
387
CD2
PHE A
48
5.979
−11.699
18.888
1.00
27.45
A
C


ATOM
388
CE1
PHE A
48
4.982
−13.567
16.920
1.00
23.46
A
C


ATOM
389
CE2
PHE A
48
5.147
−12.709
19.142
1.00
29.13
A
C


ATOM
390
CZ
PHE A
48
4.649
−13.645
18.251
1.00
24.78
A
C


ATOM
391
N
ASN A
49
7.701
−7.086
16.631
1.00
25.18
A
N


ATOM
392
CA
ASN A
49
8.713
−6.132
16.184
1.00
24.60
A
C


ATOM
393
C
ASN A
49
10.116
−6.668
16.455
1.00
25.56
A
C


ATOM
394
O
ASN A
49
10.268
−7.771
16.984
1.00
25.60
A
O


ATOM
395
CB
ASN A
49
8.504
−4.745
16.807
1.00
22.23
A
C


ATOM
396
CG
ASN A
49
8.835
−4.702
18.290
1.00
28.49
A
C


ATOM
397
OD1
ASN A
49
9.250
−5.702
18.884
1.00
28.05
A
O


ATOM
398
ND2
ASN A
49
8.654
−3.532
18.895
1.00
25.55
A
N


ATOM
399
N
SER A
50
11.135
−5.899
16.081
1.00
25.43
A
N


ATOM
400
CA
SER A
50
12.519
−6.333
16.254
1.00
31.36
A
C


ATOM
401
C
SER A
50
12.881
−6.563
17.719
1.00
35.94
A
C


ATOM
402
O
SER A
50
13.703
−7.423
18.026
1.00
40.93
A
O


ATOM
403
CB
SER A
50
13.492
−5.338
15.610
1.00
31.21
A
C


ATOM
404
OG
SER A
50
13.188
−4.003
15.972
1.00
36.34
A
O


ATOM
405
N
SER A
51
12.263
−5.801
18.618
1.00
40.78
A
N


ATOM
406
CA
SER A
51
12.503
−5.959
20.055
1.00
40.97
A
C


ATOM
407
C
SER A
51
11.650
−7.080
20.648
1.00
44.26
A
C


ATOM
408
O
SER A
51
11.588
−7.245
21.867
1.00
37.55
A
O


ATOM
409
CB
SER A
51
12.231
−4.650
20.801
1.00
35.21
A
C


ATOM
410
OG
SER A
51
12.982
−3.582
20.252
1.00
42.54
A
O


ATOM
411
N
ASN A
52
10.978
−7.827
19.775
1.00
42.32
A
N


ATOM
412
CA
ASN A
52
10.240
−9.032
20.156
1.00
39.65
A
C


ATOM
413
C
ASN A
52
8.901
−8.797
20.870
1.00
39.57
A
C


ATOM
414
O
ASN A
52
8.307
−9.735
21.406
1.00
40.20
A
O


ATOM
415
CB
ASN A
52
11.123
−9.962
20.990
1.00
40.53
A
C


ATOM
416
CG
ASN A
52
11.150
−11.379
20.449
1.00
54.19
A
C


ATOM
417
OD1
ASN A
52
11.503
−11.606
19.288
1.00
47.98
A
O


ATOM
418
ND2
ASN A
52
10.787
−12.343
21.290
1.00
54.16
A
N


ATOM
419
N
LYS A
53
8.420
−7.558
20.880
1.00
28.18
A
N


ATOM
420
CA
LYS A
53
7.092
−7.297
21.431
1.00
31.87
A
C


ATOM
421
C
LYS A
53
5.992
−7.674
20.436
1.00
29.62
A
C


ATOM
422
O
LYS A
53
6.091
−7.392
19.242
1.00
24.49
A
O


ATOM
423
CB
LYS A
53
6.927
−5.841
21.878
1.00
29.10
A
C


ATOM
424
CG
LYS A
53
5.561
−5.579
22.522
1.00
36.89
A
C


ATOM
425
CD
LYS A
53
5.352
−4.114
22.898
1.00
32.62
A
C


ATOM
426
CE
LYS A
53
3.962
−3.900
23.489
1.00
35.52
A
C


ATOM
427
NZ
LYS A
53
3.638
−2.459
23.700
1.00
34.56
A
N


ATOM
428
N
LEU A
54
4.941
−8.303
20.951
1.00
30.84
A
N


ATOM
429
CA
LEU A
54
3.848
−8.811
20.135
1.00
25.96
A
C


ATOM
430
C
LEU A
54
2.779
−7.753
19.832
1.00
24.55
A
C


ATOM
431
O
LEU A
54
2.358
−7.010
20.711
1.00
32.55
A
O


ATOM
432
CB
LEU A
54
3.212
−10.008
20.844
1.00
30.00
A
C


ATOM
433
CG
LEU A
54
1.897
−10.574
20.308
1.00
33.18
A
C


ATOM
434
CD1
LEU A
54
2.067
−11.111
18.891
1.00
23.66
A
C


ATOM
435
CD2
LEU A
54
1.372
−11.655
21.245
1.00
28.80
A
C


ATOM
436
N
PHE A
55
2.358
−7.687
18.574
1.00
25.64
A
N


ATOM
437
CA
PHE A
55
1.218
−6.867
18.175
1.00
25.15
A
C


ATOM
438
C
PHE A
55
0.298
−7.729
17.324
1.00
23.57
A
C


ATOM
439
O
PHE A
55
0.767
−8.560
16.554
1.00
29.95
A
O


ATOM
440
CB
PHE A
55
1.673
−5.645
17.378
1.00
25.44
A
C


ATOM
441
CG
PHE A
55
2.542
−4.702
18.157
1.00
20.82
A
C


ATOM
442
CD1
PHE A
55
3.918
−4.851
18.163
1.00
23.48
A
C


ATOM
443
CD2
PHE A
55
1.980
−3.663
18.880
1.00
24.05
A
C


ATOM
444
CE1
PHE A
55
4.723
−3.984
18.881
1.00
28.55
A
C


ATOM
445
CE2
PHE A
55
2.776
−2.786
19.602
1.00
27.58
A
C


ATOM
446
CZ
PHE A
55
4.152
−2.945
19.601
1.00
31.46
A
C


ATOM
447
N
GLN A
56
−1.008
−7.542
17.456
1.00
24.49
A
N


ATOM
448
CA
GLN A
56
−1.934
−8.428
16.774
1.00
25.21
A
C


ATOM
449
C
GLN A
56
−3.247
−7.778
16.369
1.00
27.21
A
C


ATOM
450
O
GLN A
56
−3.723
−6.842
17.009
1.00
29.58
A
O


ATOM
451
CB
GLN A
56
−2.216
−9.658
17.641
1.00
31.95
A
C


ATOM
452
CG
GLN A
56
−2.730
−9.336
19.035
1.00
28.95
A
C


ATOM
453
CD
GLN A
56
−2.850
−10.574
19.914
1.00
40.70
A
C


ATOM
454
OE1
GLN A
56
−3.506
−11.554
19.547
1.00
35.84
A
O


ATOM
455
NE2
GLN A
56
−2.216
−10.532
21.084
1.00
38.27
A
N


ATOM
456
N
TYR A
57
−3.819
−8.294
15.287
1.00
24.23
A
N


ATOM
457
CA
TYR A
57
−5.164
−7.950
14.866
1.00
23.97
A
C


ATOM
458
C
TYR A
57
−5.876
−9.216
14.415
1.00
25.38
A
C


ATOM
459
O
TYR A
57
−5.253
−10.121
13.855
1.00
29.08
A
O


ATOM
460
CB
TYR A
57
−5.164
−6.947
13.708
1.00
28.41
A
C


ATOM
461
CG
TYR A
57
−6.492
−6.947
12.975
1.00
26.05
A
C


ATOM
462
CD1
TYR A
57
−7.586
−6.260
13.483
1.00
25.02
A
C


ATOM
463
CD2
TYR A
57
−6.665
−7.675
11.806
1.00
22.16
A
C


ATOM
464
CE1
TYR A
57
−8.809
−6279
12.836
1.00
23.65
A
C


ATOM
465
CE2
TYR A
57
−7.883
−7.699
11.150
1.00
21.67
A
C


ATOM
466
CZ
TYR A
57
−8.952
−7.002
11.669
1.00
25.56
A
C


ATOM
467
OH
TYR A
57
−10.168
−7.017
11.021
1.00
25.78
A
O


ATOM
468
N
ALA A
58
−7.183
−9.270
14.645
1.00
13.45
A
N


ATOM
469
CA
ALA A
58
−8.001
−10.369
14.156
1.00
18.60
A
C


ATOM
470
C
ALA A
58
−9.446
−9.907
13.982
1.00
17.25
A
C


ATOM
471
O
ALA A
58
−9.962
−9.165
14.810
1.00
18.31
A
O


ATOM
472
CB
ALA A
56
−7918
−11.548
15.100
1.00
19.29
A
C


ATOM
473
N
SER A
59
−10.092
−10.341
12.902
1.00
19.89
A
N


ATOM
474
CA
SER A
59
−11.471
−9.942
12.632
1.00
23.73
A
C


ATOM
475
C
SER A
59
−12.451
−10.641
13.572
1.00
25.80
A
C


ATOM
476
O
SER A
59
−13.630
−10.306
13.605
1.00
26.75
A
O


ATOM
477
CB
SER A
59
−11.849
−10.200
11.170
1.00
21.23
A
C


ATOM
478
OG
SER A
59
−11.812
−11.582
10.859
1.00
20.25
A
O


ATOM
479
N
THR A
60
−11.952
−11.625
14.318
1.00
40.12
A
N


ATOM
480
CA
THR A
60
−12.699
−12.265
15.398
1.00
40.61
A
C


ATOM
481
C
THR A
60
−11.684
−12.718
16.431
1.00
43.22
A
C


ATOM
482
O
THR A
60
−10.506
−12.388
16.322
1.00
43.35
A
O


ATOM
483
CB
THR A
60
−13.469
−13.508
14.926
1.00
49.84
A
C


ATOM
484
OG1
THR A
60
−12.545
−14.580
14.689
1.00
54.22
A
O


ATOM
485
CG2
THR A
60
−14.257
−13.220
13.655
1.00
57.35
A
C


ATOM
486
N
ASP A
61
−12.126
−13.481
17.426
1.00
31.10
A
N


ATOM
487
CA
ASP A
61
−11.191
−14.035
18.405
1.00
35.26
A
C


ATOM
488
C
ASP A
61
−10.038
−14.736
17.691
1.00
35.75
A
C


ATOM
489
O
ASP A
61
−10.254
−15.609
16.839
1.00
32.83
A
O


ATOM
490
CB
ASP A
61
−11.891
−15.008
19.363
1.00
37.37
A
C


ATOM
491
CG
ASP A
61
−12.676
−14.296
20.454
1.00
40.45
A
C


ATOM
492
OD1
ASP A
61
−13.084
−13.137
20.237
1.00
42.00
A
O


ATOM
493
OD2
ASP A
61
−12.883
−14.895
21.530
1.00
47.45
A
O


ATOM
494
N
MET A
62
−8.817
−14.343
18.038
1.00
45.71
A
N


ATOM
495
CA
MET A
62
−7.619
−14.912
17.430
1.00
39.27
A
C


ATOM
496
C
MET A
62
−7.597
−16.434
17.508
1.00
42.49
A
C


ATOM
497
O
MET A
62
−7.261
−17.105
16.534
1.00
45.64
A
O


ATOM
498
CB
MET A
62
−6.363
−14.350
18.092
1.00
31.62
A
C


ATOM
499
CG
MET A
62
−5.077
−14.872
17.479
1.00
41.13
A
C


ATOM
500
SD
MET A
62
−4.955
−14.470
15.724
1.00
33.45
A
S


ATOM
501
CE
MET A
62
−4.563
−12.724
15.799
1.00
30.51
A
C


ATOM
502
N
ASP A
63
−7.956
−16.971
18.670
1.00
50.73
A
N


ATOM
503
CA
ASP A
63
−7.911
−18.411
18.898
1.00
51.32
A
C


ATOM
504
C
ASP A
63
−8.782
−19.163
17.898
1.00
45.54
A
C


ATOM
505
O
ASP A
63
−8.557
−20.342
17.631
1.00
52.73
A
O


ATOM
506
CB
ASP A
63
−8.338
−18.744
20.334
1.00
56.83
A
C


ATOM
507
CG
ASP A
63
−9.849
−18.803
20.499
1.00
68.01
A
C


ATOM
508
OD1
ASP A
63
−10.443
−19.866
20.207
1.00
61.02
A
O


ATOM
509
OD2
ASP A
63
−10.442
−17.792
20.934
1.00
68.32
A
O


ATOM
510
N
LYS A
64
−9.775
−18.478
17.344
1.00
35.97
A
N


ATOM
511
CA
LYS A
64
−10.681
−19.107
16.389
1.00
37.94
A
C


ATOM
512
C
LYS A
64
−10.058
−19.207
14.997
1.00
40.31
A
C


ATOM
513
O
LYS A
64
−10.062
−20.276
14.385
1.00
29.12
A
O


ATOM
514
CB
LYS A
64
−12.016
−18.358
16.331
1.00
36.49
A
C


ATOM
515
CG
LYS A
64
−12.829
−18.456
17.611
1.00
43.90
A
C


ATOM
516
CD
LYS A
64
−14.061
−17.571
17.552
1.00
45.07
A
C


ATOM
517
CE
LYS A
64
−14.886
−17.686
18.824
1.00
46.12
A
C


ATOM
518
NZ
LYS A
64
−15.996
−16.690
18.845
1.00
53.34
A
N


ATOM
519
N
VAL A
65
−9.524
−18.091
14.504
1.00
37.32
A
N


ATOM
520
CA
VAL A
65
−8.883
−18.071
13.194
1.00
34.82
A
C


ATOM
521
C
VAL A
65
−7.770
−19.110
13.153
1.00
34.94
A
C


ATOM
522
O
VAL A
65
−7.611
−19.830
12.163
1.00
32.76
A
O


ATOM
523
CB
VAL A
65
−8.287
−16.687
12.863
1.00
33.26
A
C


ATOM
524
CG1
VAL A
65
−7.703
−16.687
11.461
1.00
25.32
A
C


ATOM
525
CG2
VAL A
65
−9.337
−15.602
13.000
1.00
31.07
A
C


ATOM
526
N
LEU A
66
−7.013
−19.191
14.245
1.00
33.50
A
N


ATOM
527
CA
LEU A
66
−5.907
−20.131
14.346
1.00
34.39
A
C


ATOM
528
C
LEU A
66
−6.369
−21.582
14.224
1.00
43.02
A
C


ATOM
529
O
LEU A
66
−5.812
−22.356
13.437
1.00
40.25
A
O


ATOM
530
CB
LEU A
66
−5.142
−19.924
15.653
1.00
37.57
A
C


ATOM
531
CG
LEU A
66
−4.360
−18.614
15.753
1.00
41.06
A
C


ATOM
532
CD1
LEU A
66
−3.493
−18.610
16.994
1.00
40.01
A
C


ATOM
533
CD2
LEU A
66
−3.513
−18.409
14.508
1.00
34.50
A
C


ATOM
534
N
LEU A
67
−7.385
−21.950
14.998
1.00
44.58
A
N


ATOM
535
CA
LEU A
67
−7.897
−23.315
14.961
1.00
45.52
A
C


ATOM
536
C
LEU A
67
−8.462
−23.658
13.590
1.00
44.52
A
C


ATOM
537
O
LEU A
67
−8.327
−24.782
13.122
1.00
46.24
A
O


ATOM
538
CB
LEU A
67
−8.947
−23.542
16.051
1.00
49.95
A
C


ATOM
539
CG
LEU A
67
−8.367
−23.854
17.434
1.00
58.40
A
C


ATOM
540
CD1
LEU A
67
−9.474
−24.163
18.430
1.00
62.44
A
C


ATOM
541
CD2
LEU A
67
−7.373
−25.009
17.354
1.00
52.35
A
C


ATOM
542
N
LYS A
68
−9.087
−22.677
12.951
1.00
28.77
A
N


ATOM
543
CA
LYS A
68
−9.634
−22.855
11.616
1.00
30.29
A
C


ATOM
544
C
LYS A
68
−8.490
−23.109
10.637
1.00
33.93
A
C


ATOM
545
O
LYS A
68
−8.659
−23.794
9.624
1.00
33.71
A
O


ATOM
546
CB
LYS A
68
−10.441
−21.616
11.218
1.00
32.94
A
C


ATOM
547
CG
LYS A
68
−11.349
−21.788
10.010
1.00
35.71
A
C


ATOM
548
CD
LYS A
68
−12.588
−20.911
10.149
1.00
33.52
A
C


ATOM
549
CE
LYS A
68
−13.498
−21.001
8.930
1.00
31.15
A
C


ATOM
550
NZ
LYS A
68
−13.079
−20.050
7.866
1.00
35.48
A
N


ATOM
551
N
TYR A
69
−7.321
−22.563
10.959
1.00
40.79
A
N


ATOM
552
CA
TYR A
69
−6.119
−22.772
10.155
1.00
42.75
A
C


ATOM
553
C
TYR A
69
−5.551
−24.177
10.350
1.00
43.67
A
C


ATOM
554
O
TYR A
69
−5.195
−24.849
9.381
1.00
39.63
A
O


ATOM
555
CB
TYR A
69
−5.049
−21.726
10.495
1.00
35.20
A
C


ATOM
556
CG
TYR A
69
−3.719
−21.966
9.812
1.00
29.77
A
C


ATOM
557
CD1
TYR A
69
−3.504
−21.552
8.504
1.00
30.89
A
C


ATOM
558
CD2
TYR A
69
−2.682
−22.608
10.472
1.00
31.32
A
C


ATOM
559
CE1
TYR A
69
−2.295
−21.768
7.875
1.00
27.04
A
C


ATOM
560
CE2
TYR A
69
−1.465
−22.831
9.848
1.00
28.93
A
C


ATOM
561
CZ
TYR A
69
−1.280
−22.409
8.550
1.00
29.92
A
C


ATOM
562
OH
TYR A
69
−0.075
−22.628
7.922
1.00
31.31
A
O


ATOM
563
N
THR A
70
−5.459
−24.613
11.605
1.00
35.69
A
N


ATOM
564
CA
THR A
70
−4.898
−25.928
11.906
1.00
43.59
A
C


ATOM
565
C
THR A
70
−5.838
−27.048
11.470
1.00
45.00
A
C


ATOM
566
O
THR A
70
−5.397
−28.043
10.894
1.00
48.92
A
O


ATOM
567
CB
THR A
70
−4.529
−26.084
13.403
1.00
41.16
A
C


ATOM
568
OG1
THR A
70
−5.627
−25.665
14.221
1.00
56.03
A
O


ATOM
569
CG2
THR A
70
−3.305
−25.240
13.741
1.00
41.46
A
C


ATOM
570
N
GLU A
71
−7.130
−26.877
11.732
1.00
71.37
A
N


ATOM
571
CA
GLU A
71
−8.130
−27.853
11.308
1.00
82.63
A
C


ATOM
572
C
GLU A
71
−8.173
−27.949
9.786
1.00
76.61
A
C


ATOM
573
O
GLU A
71
−8.610
−28.954
9.229
1.00
81.40
A
O


ATOM
574
CB
GLU A
71
−9.521
−27.478
11.838
1.00
78.47
A
C


ATOM
575
CG
GLU A
71
−9.607
−27.275
13.348
1.00
86.35
A
C


ATOM
576
CD
GLU A
71
−9.479
−28.566
14.132
1.00
90.69
A
C


ATOM
577
OE1
GLU A
71
−9.615
−29.650
13.525
1.00
97.70
A
O


ATOM
578
OE2
GLU A
71
−9.249
−28.494
15.359
1.00
83.58
A
O


ATOM
579
N
TYR A
72
−7.713
−26.894
9.120
1.00
49.20
A
N


ATOM
580
CA
TYR A
72
−7.800
−26.799
7.667
1.00
47.92
A
C


ATOM
581
C
TYR A
72
−7.085
−27.958
6.983
1.00
45.30
A
C


ATOM
582
O
TYR A
72
−7.519
−28.423
5.930
1.00
42.68
A
O


ATOM
583
CB
TYR A
72
−7.225
−25.464
7.187
1.00
44.29
A
C


ATOM
584
CG
TYR A
72
−7.659
−25.054
5.794
1.00
41.13
A
C


ATOM
585
CD1
TYR A
72
−8.875
−24.416
5.586
1.00
35.47
A
C


ATOM
586
CD2
TYR A
72
−6.845
−25.291
4.689
1.00
43.90
A
C


ATOM
587
CE1
TYR A
72
−9.277
−24.030
4.316
1.00
34.32
A
C


ATOM
588
CE2
TYR A
72
−7.235
−24.906
3.414
1.00
38.74
A
C


ATOM
589
CZ
TYR A
72
−8.453
−24.275
3.234
1.00
42.36
A
C


ATOM
590
OH
TYR A
72
−8.852
−23.888
1.972
1.00
38.66
A
O


TER


ATOM
591
N
GLY B
2
−9.188
5.872
−5.539
1.00
35.93
B
N


ATOM
592
CA
GLY B
2
−9.888
5.453
−6.741
1.00
41.50
B
C


ATOM
593
C
GLY B
2
−10.704
6.574
−7.356
1.00
43.98
B
C


ATOM
594
O
GLY B
2
−10.628
7.722
−6.907
1.00
39.60
B
O


ATOM
595
N
ARG B
3
−11.484
6.244
−8.384
1.00
34.91
B
N


ATOM
596
CA
ARG B
3
−12.303
7.235
−9.080
1.00
36.90
B
C


ATOM
597
C
ARG B
3
−13.303
7.899
−8.138
1.00
39.43
B
C


ATOM
598
O
ARG B
3
−13.661
9.065
−8.311
1.00
43.98
B
O


ATOM
599
CB
ARG B
3
−13.029
6.601
−10.267
1.00
37.34
B
C


ATOM
600
CG
ARG B
3
−12.101
6.102
−11.369
1.00
39.68
B
C


ATOM
601
CD
ARG B
3
−11.130
7.187
−11.823
1.00
42.23
B
C


ATOM
602
NE
ARG B
3
−10.365
6.783
−13.000
1.00
38.79
B
N


ATOM
603
CZ
ARG B
3
−10.840
6.808
−14.242
1.00
44.35
5
C


ATOM
604
NH1
ARG B
3
−12.084
7.212
−14.474
1.00
33.55
B
N


ATOM
605
NH2
ARG B
3
−10.073
6.423
−15.253
1.00
43.80
B
N


ATOM
606
N
LYS B
4
−13.753
7.144
−7.143
1.00
32.66
B
N


ATOM
607
CA
LYS B
4
−14.606
7.679
−6.094
1.00
32.76
B
C


ATOM
608
C
LYS B
4
−14.195
7.094
−4.752
1.00
36.67
B
C


ATOM
609
O
LYS B
4
−13.841
5.915
−4.658
1.00
31.80
B
O


ATOM
610
CB
LYS B
4
−16.075
7.341
−6.357
1.00
35.54
B
C


ATOM
611
CG
LYS B
4
−16.670
7.976
−7.605
1.00
39.71
B
C


ATOM
612
CD
LYS B
4
−18.000
7.320
−7.949
1.00
35.56
B
C


ATOM
613
CE
LYS B
4
−18.425
7.630
−9.371
1.00
47.36
B
C


ATOM
614
NZ
LYS B
4
−19.420
6.635
−9.876
1.00
51.32
B
N


ATOM
615
N
LYS B
5
−14.235
7.922
−3.716
1.00
40.04
B
N


ATOM
616
CA
LYS B
5
−14.081
7.426
−2.362
1.00
37.87
B
C


ATOM
617
C
LYS B
5
−15.249
6.499
−2.081
1.00
39.79
B
C


ATOM
618
O
LYS B
5
−16.384
6.802
−2.449
1.00
40.95
B
O


ATOM
619
CB
LYS B
5
−14.082
8.583
−1.359
1.00
35.44
B
C


ATOM
620
CG
LYS B
5
−14.292
8.145
0.087
1.00
40.32
B
C


ATOM
621
CD
LYS B
5
−13.906
9.244
1.069
1.00
36.82
B
C


ATOM
622
CE
LYS B
5
−13.884
8.717
2.494
1.00
46.24
B
C


ATOM
623
NZ
LYS B
5
−13.497
9.771
3.476
1.00
52.66
B
N


ATOM
624
N
ILE B
6
−14.972
5.363
−1.449
1.00
39.51
B
N


ATOM
625
CA
ILE B
6
−16.037
4.465
−1.020
1.00
39.10
B
C


ATOM.
626
C
ILE B
6
−16.194
4.479
0.495
1.00
44.95
B
C


ATOM
627
O
ILE B
6
−15.428
5.129
1.207
1.00
43.30
B
O


ATOM
628
CE
ILE B
6
−15.795
3.017
−1.473
1.00
43.66
B
C


ATOM
629
CG1
ILE B
6
−14.604
2.411
−0.728
1.00
41.77
B
C


ATOM
630
CG2
ILE B
6
−15.606
2.954
−2.982
1.00
47.69
B
C


ATOM
631
CD1
ILE B
6
−14.433
0.923
−0.970
1.00
39.73
B
C


ATOM
632
N
GLN B
7
−17.203
3.765
0.977
1.00
36.28
B
N


ATOM
633
CA
GLN B
7
−17.422
3.616
2.405
1.00
37.59
B
C


ATOM
634
C
GLN B
7
−17.066
2.196
2.786
1.00
33.90
B
C


ATOM
635
O
GLN B
7
−17.264
1.269
2.000
1.00
33.84
B
O


ATOM
636
CB
GLN B
7
−18.880
3.911
2.765
1.00
47.49
B
C


ATOM
637
CG
GLN B
7
−19.228
5.391
2.796
1.00
45.21
B
C


ATOM
638
CD
GLN B
7
−18.721
6.085
4.048
1.00
62.62
B
C


ATOM
639
OE1
GLN B
7
−19.133
5.760
5.164
1.00
65.96
B
O


ATOM
640
NE2
GLN B
7
−17.829
7.054
3.866
1.00
64.78
B
N


ATOM
641
N
ILE B
8
−16.534
2.025
3.990
1.00
28.89
B
N


ATOM
642
CA
ILE B
8
−16.087
0.712
4.435
1.00
24.06
B
C


ATOM
643
C
ILE B
8
−17.257
−0.135
4.929
1.00
26.92
B
C


ATOM
644
O
ILE B
8
−17.536
−0.209
6.128
1.00
26.19
B
O


ATOM
645
CB
ILE B
8
−14.965
0.823
5.495
1.00
20.79
B
C


ATOM
646
CG1
ILE B
8
−13.755
1.528
4.882
1.00
20.90
B
C


ATOM
647
CG2
ILE B
8
−14.556
−0.546
6.017
1.00
18.34
B
C


ATOM
648
CD1
ILE B
8
−13.387
1.003
3.506
1.00
20.40
B
C


ATOM
649
N
THR B
9
−17.947
−0.767
3.984
1.00
28.04
B
N


ATOM
650
CA
THR B
9
−19.038
−1.677
4.313
1.00
28.46
B
C


ATOM
651
C
THR B
9
−19.055
−2.860
3.344
1.00
24.67
B
C


ATOM
652
O
THR B
9
−18.658
−2.724
2.186
1.00
28.00
B
O


ATOM
653
CB
THR B
9
−20.399
−0.949
4.311
1.00
34.72
B
C


ATOM
654
OG1
THR B
9
−21.408
−1.809
4.860
1.00
36.57
B
O


ATOM
655
CG2
THR B
9
−20.784
−0.520
2.894
1.00
26.37
B
C


ATOM
656
N
ARG B
10
−19.502
−4.015
3.830
1.00
23.22
B
N


ATOM
657
CA
ARG B
10
−19.521
−5.249
3.041
1.00
27.96
B
C


ATOM
658
C
ARG B
10
−20.109
−5.073
1.644
1.00
27.22
B
C


ATOM
659
O
ARG B
10
−21.267
−4.682
1.491
1.00
29.90
B
O


ATOM
660
CB
ARG B
10
−20.283
−6.353
3.777
1.00
27.06
B
C


ATOM
661
CG
ARG B
10
−20.326
−7.678
3.024
1.00
27.66
B
C


ATOM
662
CD
ARG B
10
−21.227
−8.687
3.728
1.00
30.60
B
C


ATOM
663
NE
ARG B
10
−21.283
−9.974
3.035
1.00
44.23
B
N


ATOM
664
CZ
ARG B
10
−22.086
−10.242
2.007
1.00
41.38
B
C


ATOM
665
NH1
ARG B
10
−22.905
−9.309
1.539
1.00
42.70
B
N


ATOM
666
NH2
ARG B
10
−22.070
−11.443
1.442
1.00
34.97
B
N


ATOM
667
N
ILE B
11
−19.299
−5.367
0.632
1.00
18.77
B
N


ATOM
668
CA
ILE B
11
−19.735
−5.298
−0.756
1.00
19.25
B
C


ATOM
669
C
ILE B
11
−20.735
−6.417
−1.041
1.00
25.50
B
C


ATOM
670
O
ILE B
11
−20.462
−7.592
−0.773
1.00
23.75
B
O


ATOM
671
CB
ILE B
11
−18.539
−5.406
−1.714
1.00
20.42
B
C


ATOM
672
CG1
ILE B
11
−17.639
−4.181
−1.565
1.00
15.67
B
C


ATOM
673
CG2
ILE B
11
−19.009
−5.539
−3.154
1.00
18.62
B
C


ATOM
674
CD1
ILE B
11
−16.254
−4.380
−2.103
1.00
17.71
B
C


ATOM
675
N
MET B
12
−21.893
−6.047
−1.579
1.00
22.5I
B
N


ATOM
676
CA
MET B
12
−23.000
−6.985
−1.720
1.00
24.87
B
C


ATOM
677
C
MET B
12
−22.909
−7.816
−2.996
1.00
31.08
B
C


ATOM
678
O
MET B
12
−23.373
−8.955
−3.032
1.00
25.68
B
O


ATOM
679
CB
MET B
12
−24.341
−6.246
−1.657
1.00
25.38
B
C


ATOM
680
CG
MET B
12
−24.564
−5.470
−0.358
1.00
30.39
B
C


ATOM
681
SD
MET B
12
−24.573
−6.517
1.118
1.00
35.66
B
S


ATOM
682
CE
MET B
12
−26.117
−7.406
0.874
1.00
22.73
B
C


ATOM
683
N
ASP B
13
−22.315
−7.242
−4.039
1.00
38.07
B
N


ATOM
684
CA
ASP B
13
−22.152
−7.942
−5.311
1.00
39.19
B
C


ATOM
685
C
ASP B
13
−20.988
−8.931
−5.246
1.00
41.47
B
C


ATOM
686
O
ASP B
13
−19.841
−8.536
−5.025
1.00
36.72
B
O


ATOM
687
CB
ASP B
13
−21.925
−6.939
−6.448
1.00
39.47
B
C


ATOM
688
CG
ASP B
13
−21.667
−7.617
−7.790
1.00
59.19
B
C


ATOM
689
OD1
ASP B
13
−22.367
−8.603
−8.109
1.00
58.53
B
O


ATOM
690
OD2
ASP B
13
−20.767
−7.158
−8.530
1.00
56.17
B
O


ATOM
691
N
GLU B
14
−21.290
−10.212
−5.433
1.00
29.13
B
N


ATOM
692
CA
GLU B
14
−20.272
−11.262
−5.425
1.00
30.70
B
C


ATOM
693
C
GLU B
14
−19.154
−10.996
−6.431
1.00
35.92
B
C


ATOM
694
O
GLU B
14
−17.984
−11.262
−6.157
1.00
32.47
B
O


ATOM
695
CB
GLU B
14
−20.906
−12.622
−5.718
1.00
29.50
B
C


ATOM
696
CG
GLU B
14
−19.928
−13.785
−5.799
1.00
35.92
B
C


ATOM
697
CD
GLU B
14
−20.584
−15.052
−6.339
1.00
61.30
B
C


ATOM
698
OE1
GLU B
14
−21.212
−14.986
−7.421
1.00
65.75
B
O


ATOM
699
OE2
GLU B
14
−20.475
−16.112
−5.683
1.00
53.89
B
O


ATOM
700
N
ARG B
15
−19.511
−10.473
−7.597
1.00
46.25
B
N


ATOM
701
CA
ARG B
15
−18.516
−10.214
−8.631
1.00
39.81
B
C


ATOM
702
C
ARG B
15
−17.541
−9.116
−8.215
1.00
34.94
B
C


ATOM
703
O
ARG B
15
−16.337
−9.348
−8.165
1.00
30.98
B
O


ATOM
704
CB
ARG B
15
−19.184
−9.880
−9.965
1.00
47.87
B
C


ATOM
705
CG
ARG B
15
−18.255
−9.253
−10.988
1.00
53.75
B
C


ATOM
706
CD
ARG B
15
−18.624
−9.678
−12.403
1.00
61.36
B
C


ATOM
707
NE
ARG B
15
−18.159
−11.032
−12.697
1.00
67.24
B
N


ATOM
708
CZ
ARG B
15
−18.907
−12.127
−12.584
1.00
69.40
B
C


ATOM
709
NH1
ARG B
15
−20.170
−12.036
−12.188
1.00
74.25
B
N


ATOM
710
NH2
ARG B
15
−18.389
−13.317
−12.873
1.00
47.80
B
N


ATOM
711
N
ASN B
16
−18.057
−7.927
−7.916
1.00
38.39
B
N


ATOM
712
CA
ASN B
16
−17.201
−6.832
−7.467
1.00
33.29
B
C


ATOM
713
C
ASN B
16
−16.510
−7.157
−6.144
1.00
30.20
B
C


ATOM
714
O
ASN B
16
−15.475
−6.580
−5.820
1.00
31.16
B
O


ATOM
715
CB
ASN B
16
−17.980
−5.514
−7.344
1.00
38.21
B
C


ATOM
716
CG
ASN B
16
−17.124
−4.371
−6.764
1.00
46.55
B
C


ATOM
717
OD1
ASN B
16
−15.983
−4.145
−7.190
1.00
31.35
B
O


ATOM
718
ND2
ASN B
16
−17.681
−3.646
−5.790
1.00
34.92
B
N


ATOM
719
N
ARG B
17
−17.079
−8.077
−5.374
1.00
21.31
B
N


ATOM
720
CA
ARG B
17
−16.484
−8.412
−4.091
1.00
25.28
B
C


ATOM
721
C
ARG B
17
−15.244
−9.251
−4.316
1.00
27.07
B
C


ATOM
722
O
ARG B
17
−14.212
−9.041
−3.675
1.00
27.84
B
O


ATOM
723
CB
ARG B
17
−17.464
−9.151
−3.184
1.00
24.01
B
C


ATOM
724
CG
ARG B
17
−16.867
−9.515
−1.834
1.00
23.82
B
C


ATOM
725
CD
ARG B
17
−17.926
−9.981
−0.842
1.00
26.00
B
C


ATOM
726
NE
ARG B
17
−18.536
−11.237
−1.258
1.00
32.53
B
N


ATOM
727
CZ
ARG B
17
−19.797
−11.363
−1.661
1.00
33.84
B
C


ATOM
728
NH1
ARG B
17
−20.604
−10.306
−1.687
1.00
26.61
B
N


ATOM
729
NH2
ARG B
17
−20.251
−12.553
−2.031
1.00
33.93
B
N


ATOM
730
N
GLN B
18
−15.350
−10.202
−5.236
1.00
29.00
B
N


ATOM
731
CA
GLN B
18
−14.225
−11.058
−5.573
1.00
30.09
B
C


ATOM
732
C
GLN B
18
−13.091
−10.247
−6.192
1.00
25.53
B
C


ATOM
733
O
GLN B
18
−11.921
−10.457
−5.868
1.00
22.89
B
O


ATOM
734
CB
GLN B
18
−14.669
−12.182
−6.513
1.00
28.95
B
C


ATOM
735
CG
GLN B
18
−13.522
−12.988
−7.104
1.00
29.28
B
C


ATOM
736
CD
GLN B
18
−12.610
−13.585
−6.048
1.00
33.30
B
C


ATOM
737
OE1
GLN B
18
−12.886
−13.510
−4.850
1.00
38.50
B
O


ATOM
738
NE2
GLN B
18
−11.508
−14.184
−6.492
1.00
42.99
B
N


ATOM
739
N
VAL B
19
−13.448
−9.313
−7.070
1.00
25.06
B
N


ATOM
740
CA
VAL B
19
−12.472
−8.442
−7.718
1.00
28.61
B
C


ATOM
741
C
VAL B
19
−11.723
−7.571
−6.710
1.00
29.35
B
C


ATOM
742
O
VAL B
19
−10.495
−7.502
−6.728
1.00
30.32
B
O


ATOM
743
CB
VAL B
19
−13.136
−7.529
−8.765
1.00
27.95
B
C


ATOM
744
CG1
VAL B
19
−12.285
−6.291
−9.013
1.00
28.44
B
C


ATOM
745
CG2
VAL B
19
−13.361
−8.288
−10.053
1.00
31.41
B
C


ATOM
746
N
THR B
20
−12.469
−6.905
−5.836
1.00
28.91
B
N


ATOM
747
CA
THR B
20
−11.866
−6.061
−4.815
1.00
26.07
B
C


ATOM
748
C
THR B
20
−11.017
−6.903
−3.875
1.00
27.75
B
C


ATOM
749
O
THR B
20
−9.937
−6.488
−3.453
1.00
24.01
B
O


ATOM
750
CB
THR B
20
−12.928
−5.306
−4.012
1.00
27.80
B
C


ATOM
751
OG1
THR B
20
−13.454
−4.244
−4.814
1.00
29.96
B
O


ATOM
752
CG2
THR B
20
−12.324
−4.722
−2.735
1.00
24.77
B
C


ATOM
753
N
PHE B
21
−11.503
−8.096
−3.556
1.00
22.15
B
N


ATOM
754
CA
PHE B
21
−10.746
−8.998
−2.698
1.00
21.89
B
C


ATOM
755
C
PHE B
21
−9.365
−9.324
−3.272
1.00
18.93
B
C


ATOM
756
O
PHE B
21
−8.367
−9.306
−2.553
1.00
19.66
B
O


ATOM
757
CB
PHE B
21
−11.523
−10.287
−2.446
1.00
19.40
B
C


ATOM
758
CG
PHE B
21
−10.707
−11.361
−1.796
1.00
19.58
B
C


ATOM
759
CD1
PHE B
21
−10.525
−11.374
−0.424
1.00
17.26
B
C


ATOM
760
CD2
PHE B
21
−10.116
−12.353
−2.557
1.00
19.84
B
C


ATOM
761
CE1
PHE B
21
−9.774
−12.358
0.180
1.00
20.45
B
C


ATOM
762
CE2
PHE B
21
−9.360
−13.343
−1.960
1.00
22.00
B
C


ATOM
763
CZ
PHE B
21
−9.190
−13.348
−0.589
1.00
25.35
B
C


ATOM.
764
N
THR B
22
−9.312
−9.628
−4.563
1.00
21.88
B
N


ATOM
765
CA
THR B
22
−8.054
−9.996
−5.202
1.00
20.53
B
C


ATOM
766
C
THR B
22
−7.093
−8.808
−5.230
1.00
19.42
B
C


ATOM
767
O
THR B
22
−5.899
−8.960
−4.967
1.00
20.21
B
O


ATOM
768
CB
THR B
22
−8.267
−10.561
−6.640
1.00
24.17
B
C


ATOM
769
OG1
THR B
22
−8.869
−11.862
−6.570
1.00
23.68
B
O


ATOM
770
CG2
THR B
22
−6.945
−10.675
−7.377
1.00
15.72
B
C


ATOM
771
N
LYS B
23
−7.607
−7.622
−5.542
1.00
17.48
B
N


ATOM
772
CA
LYS B
23
−6.756
−6.437
−5.542
1.00
19.24
B
C


ATOM
773
C
LYS B
23
−6.181
−6.175
−4.149
1.00
18.39
B
C


ATOM
774
O
LYS B
23
−4.962
−6.144
−3.971
1.00
18.07
B
O


ATOM
775
CB
LYS B
23
−7.511
−5.203
−6.050
1.00
20.59
B
C


ATOM
776
CG
LYS B
23
−7.846
−5.236
−7.535
1.00
26.67
B
C


ATOM
777
CD
LYS B
23
−8.583
−3.964
−7.961
1.00
28.62
B
C


ATOM
778
CE
LYS B
23
−8.978
−4.026
−9.431
1.00
28.02
B
C


ATOM
779
NZ
LYS B
23
−9.916
−2.935
−9.814
1.00
32.81
B
N


ATOM
780
N
ARG B
24
−7.061
−6.009
−3.165
1.00
16.09
B
N


ATOM
781
CA
ARG B
24
−6.640
−5.635
−1.812
1.00
16.07
B
C


ATOM
782
C
ARG B
24
−5.836
−6.711
−1.072
1.00
18.15
B
C


ATOM
783
O
ARG B
24
−5.008
−6.378
−0.218
1.00
15.59
B
O


ATOM
784
CB
ARG B
24
−7.832
−5.174
−0.969
1.00
13.10
B
C


ATOM
785
CG
ARG B
24
−8.234
−3.717
−1.203
1.00
14.76
B
C


ATOM
786
CD
ARG B
24
−9.495
−3.357
−0.424
1.00
14.27
B
C


ATOM
787
ME
ARG B
24
−9.879
−1.954
−0.584
1.00
15.73
B
N


ATOM
788
CZ
ARG B
24
−9.536
−0.980
0.258
1.00
18.12
B
C


ATOM
789
NH1
ARG B
24
−8.797
−1.247
1.331
1.00
16.01
B
N


ATOM
790
NH2
ARG B
24
−9.933
0.263
0.028
1.00
16.88
B
N


ATOM
791
N
LYS B
25
−6.064
−7.987
−1.394
1.00
19.04
B
N


ATOM
792
CA
LYS B
25
−5.278
−9.061
−0.779
1.00
19.08
B
C


ATOM
793
C
LYS B
25
−3.822
−8.901
−1.164
1.00
18.45
B
C


ATOM
794
O
LYS B
25
−2.930
−8.970
−0.328
1.00
19.20
B
O


ATOM
795
CB
LYS B
25
−5.762
−10.447
−1.214
1.00
23.30
B
C


ATOM
796
CG
LYS B
25
−4.782
−11.570
−0.853
1.00
19.47
B
C


ATOM
797
CD
LYS B
25
−5.469
−12.936
−0.772
1.00
22.91
B
C


ATOM
798
CE
LYS B
25
−5.988
−13.411
−2.138
1.00
26.31
B
C


ATOM
799
NZ
LYS B
25
−4.897
−13.779
−3.087
1.00
20.74
B
N


ATOM
800
N
PHE B
26
−3.594
−8.692
−2.451
1.00
16.72
B
N


ATOM
801
CA
PHE B
26
−2.260
−8.430
−2.954
1.00
17.53
B
C


ATOM
802
C
PHE B
26
−1.655
−7.216
−2.226
1.00
19.47
B
C


ATOM
803
O
PHE B
26
−0.552
−7.285
−1.684
1.00
20.99
B
O


ATOM
804
CB
PHE B
26
−2.336
−8.184
−4.460
1.00
17.86
B
C


ATOM
805
CG
PHE B
26
−1.005
−8.004
−5.109
1.00
21.69
B
C


ATOM
806
CD1
PHE B
26
−0.379
−9.073
−5.732
1.00
25.97
B
C


ATOM
807
CD2
PHE B
26
−0.386
−6.768
−5.110
1.00
18.89
B
C


ATOM
808
CE1
PHE B
26
0.853
−8.913
−6.342
1.00
25.80
B
C


ATOM
809
CE2
PHE B
26
0.848
−6.602
−5.718
1.00
25.93
B
C


ATOM
810
CZ
PHE B
26
1.467
−7.676
−6.333
1.00
23.95
B
C


ATOM
811
N
GLY B
27
−2.395
−6.111
−2.213
1.00
19.53
B
N


ATOM
812
CA
GLY B
27
−1.966
−4.896
−1.548
1.00
18.26
B
C


ATOM
813
C
GLY B
27
−1.679
−5.073
−0.069
1.00
17.11
B
C


ATOM
814
O
GLY B
27
−0.796
−4.415
0.474
1.00
15.96
B
O


ATOM
815
N
LEU B
28
−2.423
−5.959
0.589
1.00
18.00
B
N


ATOM
816
CA
LEU B
28
−2.214
−6.213
2.016
1.00
18.51
B
C


ATOM
817
C
LEU B
28
−0.923
−6.999
2.259
1.00
18.19
B
C


ATOM
818
O
LEU B
28
−0.141
−6.670
3.156
1.00
15.92
B
O


ATOM
819
CB
LEU B
28
−3.406
−6.962
2.619
1.00
18.03
B
C


ATOM
820
CG
LEU B
28
−3.321
−7.263
4.123
1.00
17.44
B
C


ATOM
821
CD1
LEU B
28
−3.250
−5.981
4.924
1.00
15.32
B
C


ATOM
822
CD2
LEU B
28
−4.506
−8.112
4.579
1.00
16.82
B
C


ATOM
823
N
MET B
29
−0.710
−8.034
1.450
1.00
20.23
B
N


ATOM
824
CA
MET B
29
0.502
−8.845
1.525
1.00
19.85
B
C


ATOM
825
C
MET B
29
1.733
−8.013
1.190
1.00
17.85
B
C


ATOM
826
O
MET B
29
2.770
−8.150
1.823
1.00
17.90
B
O


ATOM
827
CB
MET B
29
0.410
−10.050
0.585
1.00
21.04
B
C


ATOM
828
CG
MET B
29
−0.699
−11.045
0.936
1.00
20.57
B
C


ATOM
829
SD
MET B
29
−0.410
−12.688
0.227
1.00
25.22
B
S


ATOM
830
CE
MET B
29
−1.808
−13.585
0.911
1.00
25.68
B
C


ATOM
831
N
LYS B
30
1.612
−7.141
0.198
1.00
21.15
B
N


ATOM
832
CA
LYS B
30
2.733
−6.297
−0.199
1.00
23.46
B
C


ATOM
833
C
LYS B
30
3.208
−5.420
0.963
1.00
22.21
B
C


ATOM
834
O
LYS B
30
4.409
−5.327
1.230
1.00
22.98
B
O


ATOM
835
CB
LYS B
30
2.380
−5.439
−1.418
1.00
22.85
B
C


ATOM
836
CG
LYS B
30
3.597
−4.786
−2.066
1.00
31.19
B
C


ATOM
837
CD
LYS B
30
3.233
−3.940
−3.284
1.00
30.28
B
C


ATOM
838
CE
LYS B
30
4.410
−3.069
−3.708
1.00
32.21
B
C


ATOM
839
NZ
LYS B
30
3.999
−1.884
−4.515
1.00
32.92
B
N


ATOM
840
N
LYS B
31
2.269
−4.785
1.661
1.00
18.51
B
N


ATOM
841
CA
LYS B
31
2.629
−3.953
2.810
1.00
19.94
B
C


ATOM
842
C
LYS B
31
3.135
−4.774
4.002
1.00
17.10
B
C


ATOM
843
O
LYS B
31
4.045
−4.354
4.707
1.00
19.53
B
O


ATOM
844
CB
LYS B
31
1.474
−3.025
3.202
1.00
16.96
B
C


ATOM
845
CG
LYS B
31
1.285
−1.885
2.214
1.00
16.08
B
C


ATOM
846
CD
LYS B
31
0.282
−0.855
2.704
1.00
22.23
B
C


ATOM
847
CE
LYS B
31
0.246
0.355
1.779
1.00
22.27
B
C


ATOM
848
NZ
LYS B
31
1.595
0.974
1.641
1.00
23.12
B
N


ATOM
849
N
ALA B
32
2.560
−5.953
4.206
1.00
11.50
B
N


ATOM
850
CA
ALA B
32
3.033
−6860
5.242
1.00
12.27
B
C


ATOM
851
C
ALA B
32
4.503
−7.208
4.998
1.00
15.88
B
C


ATOM
852
O
ALA B
32
5.327
−7.137
5.913
1.00
13.80
B
O


ATOM
853
CB
ALA B
32
2.182
−8.123
5.269
1.00
11.97
B
C


ATOM
854
N
TYR B
33
4.819
−7.581
3.757
1.00
22.53
B
N


ATOM
855
CA
TYR B
33
6.189
−7.880
3.346
1.00
21.55
B
C


ATOM
856
C
TYR B
33
7.141
−6.692
3.554
1.00
23.48
B
C


ATOM
857
O
TYR B
33
8.224
−6.843
4.124
1.00
24.87
B
O


ATOM
858
CB
TYR B
33
6.214
−8.336
1.880
1.00
26.95
B
C


ATOM
859
CG
TYR B
33
7.560
−8.179
1.202
1.00
25.09
B
C


ATOM
860
CD1
TYR B
33
8.596
−9.064
1.460
−1.00
27.42
B
C


ATOM
861
CD2
TYR B
33
7.794
−7.140
0.306
1.00
25.48
B
C


ATOM
862
CE1
TYR B
33
9.831
−8.922
0.848
1.00
29.33
B
C


ATOM
863
CE2
TYR B
33
9.027
−6.986
−0.308
1.00
25.23
B
C


ATOM
864
CZ
TYR B
33
10.040
−7.881
−0.033
1.00
29.66
B
C


ATOM
865
OH
TYR B
33
11.269
−7.743
−0.642
1.00
32.89
B
O


ATOM
866
N
GLU B
34
6.735
−5.517
3.086
1.00
17.81
B
N


ATOM
867
CA
GLU B
34
7.539
−4.308
3.231
1.00
19.60
B
C


ATOM
868
C
GLU B
34
7.810
−3.965
4.696
1.00
20.91
B
C


ATOM
869
O
GLU B
34
8.931
−3.579
5.054
1.00
17.67
B
O


ATOM
870
CB
GLU B
34
6.876
−3.126
2.518
1.00
18.42
B
C


ATOM
871
CG
GLU B
34
6.846
−3.262
0.997
1.00
19.82
B
C


ATOM
872
CD
GLU B
34
6.199
−2.067
0.310
1.00
25.58
B
C


ATOM
873
OE1
GLU B
34
5.545
−1.255
1.004
1.00
22.87
B
O


ATOM
874
OE2
GLU B
34
6.345
−1.939
−0.926
1.00
21.30
B
O


ATOM
875
N
LEU B
35
6.793
−4.115
5.544
1.00
16.91
B
N


ATOM
876
CA
LEU B
35
6.966
−3.847
6.972
1.00
16.29
B
C


ATOM
877
C
LEU B
35
7.932
−4.845
7.619
1.00
16.61
B
C


ATOM
878
O
LEU B
35
8.731
−4.482
8.487
1.00
18.25
B
O


ATOM
879
CB
LEU B
35
5.626
−3.850
7.708
1.00
13.34
B
C


ATOM
880
CG
LEU B
35
5.763
−3.654
9.219
1.00
14.59
B
C


ATOM
881
CD1
LEU B
35
6.310
−2.272
9.516
1.00
14.93
B
C


ATOM
882
CD2
LEU B
35
4.451
−3.882
9.940
1.00
14.02
B
C


ATOM
883
N
SER B
36
7.860
−6.102
7.204
1.00
17.19
B
N


ATOM
884
CA
SER B
36
5.792
−7.102
7.716
1.00
26.25
B
C


ATOM
885
C
SER B
36
10.251
−6.770
7.364
1.00
21.13
B
C


ATOM
886
O
SER B
36
11.153
−6.935
8.183
1.00
23.34
B
O


ATOM
887
CB
SER B
36
8.431
−8.494
7.199
1.00
23.09
B
C


ATOM
888
OG
SER B
36
9.402
−9.438
7.616
1.00
27.07
B
O


ATOM
889
N
VAL B
37
10.473
−6.299
6.143
1.00
20.97
B
N


ATOM
890
CA
VAL B
37
11.820
−5.988
5.678
1.00
21.94
B
C


ATOM
891
C
VAL B
37
12.328
−4.665
6.247
1.00
22.41
B
C


ATOM
892
O
VAL B
37
13.440
−4.588
6.769
1.00
22.46
B
O


ATOM
893
CB
VAL B
37
11.877
−5.935
4.139
1.00
21.78
B
C


ATOM
894
CG1
VAL E
37
13.164
−5.273
3.667
1.00
17.34
B
C


ATOM
895
CG2
VAL B
37
11.742
−7.336
3.562
1.00
22.73
B
C


ATOM
896
N
LEU B
38
11.509
−3.625
6.139
1.00
29.65
B
N


ATOM
897
CA
LEU B
38
11.895
−2.302
6.606
1.00
29.22
B
C


ATOM
898
C
LEU B
38
12.222
−2.292
8.095
1.00
29.43
B
C


ATOM
899
O
LEU B
38
13.176
−1.639
8.527
1.00
29.26
B
O


ATOM
900
CB
LEU B
38
10.781
−1.294
6.326
1.00
27.68
B
C


ATOM
901
CG
LEU B
38
10.564
−0.877
4.875
1.00
27.08
B
C


ATOM
902
CD1
LEU B
38
9.277
−0.077
4.758
1.00
23.22
B
C


ATOM
903
CD2
LEU B
38
11.756
−0.083
4.363
1.00
24.95
B
C


ATOM
904
N
CYS B
39
11.432
−3.015
8.880
1.00
17.61
b
N


ATOM
905
CA
CYS B
39
11.579
−2.941
10.330
1.00
22.07
B
C


ATOM
906
C
CYS B
39
12.059
−4.238
10.992
1.00
21.34
B
C


ATOM
907
O
CYS B
39
12.094
−4.338
12.216
1.00
24.49
B
O


ATOM
908
CB
CYS B
39
10.276
−2.448
10.968
1.00
15.92
B
C


ATOM
909
SG
CYS B
39
9.701
−0.901
10.239
1.00
19.75
B
S


ATOM
910
N
ASP B
40
12.433
−5.226
10.191
1.00
31.69
B
N


ATOM
911
CA
ASP B
40
12.981
−6.454
10.754
1.00
37.68
B
C


ATOM
912
C
ASP B
40
12.040
−7.040
11.810
1.00
37.06
B
C


ATOM
913
O
ASP B
40
12.325
−6.975
13.006
1.00
34.46
B
O


ATOM
914
CB
ASP B
40
14.351
−6.169
11.382
1.00
33.34
B
C


ATOM
915
CG
ASP B
40
15.076
−7.432
11.824
1.00
41.25
B
C


ATOM
916
OD1
ASP B
40
14.704
−8.540
11.380
1.00
43.90
B
O


ATOM
917
OD2
ASP B
40
16.031
−7.312
12.621
1.00
52.43
B
O


ATOM
918
N
CYS B
41
10.919
−7.603
11.370
1.00
28.73
B
N


ATOM
919
CA
CYS B
41
9.996
−8.257
12.289
1.00
33.22
B
C


ATOM
920
C
CYS B
41
9.336
−9.506
11.693
1.00
31.42
B
C


ATOM
921
O
CYS B
41
9.191
−9.620
10.477
1.00
31.49
B
O


ATOM
922
CB
CYS B
41
8.943
−7.266
12.798
1.00
30.60
B
C


ATOM
923
SG
CYS B
41
8.329
−6.093
11.583
1.00
39.58
B
S


ATOM
924
N
GLU B
42
8.966
−10.446
12.561
1.00
32.53
B
N


ATOM
925
CA
GLU B
42
8.232
−11.638
12.153
1.00
34.28
B
C


ATOM
926
C
GLU B
42
6.772
−11.284
11.955
1.00
31.82
B
C


ATOM
927
O
GLU B
42
6.133
−10.739
12.853
1.00
32.57
B
O


ATOM
928
CB
GLU B
42
8.303
−12.725
13.225
1.00
36.20
B
C


ATOM
929
CG
GLU B
42
9.646
−13.393
13.405
1.00
46.15
B
C


ATOM
930
CD
GLU B
42
9.568
−14.549
14.382
1.00
47.22
B
C


ATOM
931
OE1
GLU B
42
10.523
−14.734
15.167
1.00
64.02
B
O


ATOM
932
OE2
GLU B
42
8.542
−15.265
14.372
1.00
37.09
B
O


ATOM
933
N
ILE B
43
6.232
−11.615
10.792
1.00
20.98
B
N


ATOM
934
CA
ILE B
43
4.832
−11.335
10.524
1.00
20.90
B
C


ATOM
935
C
ILE B
43
4.116
−12.561
9.975
1.00
20.19
B
C


ATOM
936
O
ILE B
43
4.693
−13.344
9.223
1.00
21.90
B
O


ATOM
937
CB
ILE B
43
4.678
−10.128
9.578
1.00
21.58
B
C


ATOM
938
CG1
ILE B
43
5.102
−8.848
10.310
1.00
18.84
B
C


ATOM
939
CG2
ILE B
43
3.244
−10.033
9.056
1.00
14.53
B
C


ATOM
940
CD1
ILE B
43
5.145
−7.608
9.446
1.00
16.56
B
C


ATOM
941
N
ALA B
44
2.865
−12.735
10.381
1.00
22.30
B
N


ATOM
942
CA
ALA B
44
2.028
−13.607
9.861
1.00
22.53
B
C


ATOM
943
C
ALA B
44
0.660
−13.234
9.523
1.00
20.25
B
C


ATOM
944
O
ALA B
44
0.123
−12.420
10.266
1.00
22.18
B
O


ATOM
945
CB
ALA B
44
1.907
−14.946
10.878
1.00
20.13
B
C


ATOM
346
N
LEU B
45
0.102
−13.660
8.398
1.00
21.92
B
N


ATOM
947
CA
LEU B
45
−1.165
−13.124
7.928
1.00
18.74
B
C


ATOM
948
C
LEU B
45
−2.013
−14.241
7.342
1.00
22.81
B
C


ATOM
949
O
LEU B
45
−1.791
−14.662
6.210
1.00
25.91
B
O


ATOM
950
CB
LEU B
45
−0.908
−12.046
6.869
1.00
21.14
B
C


ATOM
951
CG
LEU B
45
−2.098
−11.413
6.139
1.00
21.33
B
C


ATOM
952
CD1
LEU B
45
−3.034
−10.714
7.115
1.00
18.73
B
C


ATOM
953
CD2
LEU B
45
−1.623
−10.441
5.059
1.00
15.76
B
C


ATOM
954
N
ILE B
46
−2.980
−14.726
8.112
1.00
28.56
B
N


ATOM
955
CA
ILE B
46
−3.894
−15.759
7.627
1.00
28.46
B
C


ATOM
956
C
ILE B
46
−5.221
−15.148
7.187
1.00
27.91
B
C


ATOM
957
O
ILE B
46
−5.828
−14.367
7.922
1.00
28.37
B
O


ATOM
958
CB
ILE B
46
−4.152
−16.829
8.704
1.00
29.75
B
C


ATOM
959
CG1
ILE B
46
−2.865
−17.601
8.999
1.00
27.86
B
C


ATOM
960
CG2
ILE B
46
−5.243
−17.774
8.258
1.00
29.11
B
C


ATOM
961
CD1
ILE B
46
−2.877
−18.332
10.321
1.00
30.75
B
C


ATOM
962
N
ILE B
47
−5.668
−15.509
5.988
1.00
24.78
B
N


ATOM
963
CA
ILE B
47
−6.883
−14.943
5.405
1.00
22.12
B
C


ATOM
964
C
ILE B
47
−7.777
−16.006
4.768
1.00
25.06
B
C


ATOM
965
O
ILE B
47
−7.330
−16.774
3.914
1.00
28.66
B
O


ATOM
966
CB
ILE B
47
−6.544
−13.927
4.299
1.00
25.90
B
C


ATOM
967
CG1
ILE B
47
−5.569
−12.864
4.805
1.00
25.54
B
C


ATOM
968
CG2
ILE B
47
−7.815
−13.286
3.747
1.00
28.25
B
C


ATOM
969
CD1
ILE B
47
−5.081
−11.952
3.706
1.00
22.33
B
C


ATOM
970
N
PHE B
48
−9.044
−16.035
5.172
1.00
23.95
B
N


ATOM
971
CA
PHE B
48
−10.031
−16.927
4.574
1.00
25.54
B
C


ATOM
972
C
PHE B
48
−11.088
−16.077
3.887
1.00
30.58
B
C


ATOM
973
O
PHE B
48
−11.813
−15.347
4.556
1.00
29.00
B
O


ATOM
974
CB
PHE B
48
−10.725
−17.782
5.646
1.00
25.36
B
C


ATOM
975
CG
PHE B
48
−9.798
−18.674
6.429
1.00
26.77
B
C


ATOM
976
CD1
PHE B
48
−9.260
−18.251
7.636
1.00
24.64
B
C


ATOM
977
CD2
PHE B
48
−9.487
−19.946
5.974
1.00
28.62
B
C


ATOM
978
CE1
PHE B
48
−8.412
−19.074
8.366
1.00
23.95
B
C


ATOM
979
CE2
PHE B
48
−8.645
−20.775
6.700
1.00
28.73
B
C


ATOM
980
CZ
PHE B
48
−8.107
−20.335
7.898
1.00
25.90
B
C


ATOM
981
N
ASN B
49
−11.197
−16.170
2.565
1.00
23.38
B
N


ATOM
982
CA
ASN B
49
−12.209
−15.384
1.863
1.00
27.57
B
C


ATOM
983
C
ASN B
49
−13.626
−15.824
2.242
1.00
27.92
B
C


ATOM
984
O
ASN B
49
−13.801
−16.750
3.038
1.00
28.71
B
O


ATOM
985
CB
ASN B
49
−11.995
−15.419
0.346
1.00
22.94
B
C


ATOM
986
CG
ASN B
49
−12.275
−16.780
−0.257
1.00
32.75
B
C


ATOM
987
OD1
ASN B
49
−12.822
−17.671
0.403
1.00
30.86
B
O


ATOM
988
ND2
ASN B
49
−11.902
−16.949
−1.523
1.00
25.20
B
N


ATOM
989
N
SER B
50
−14.631
−15.158
1.683
1.00
33.24
B
N


ATOM
990
CA
SER B
50
−16.019
−15.449
2.039
1.00
40.75
B
C


ATOM
991
C
SER B
50
−16.472
−16.818
1.540
1.00
40.36
B
C


ATOM
992
O
SER B
50
−17.562
−17.272
1.877
1.00
41.94
B
O


ATOM
993
CB
SER B
50
−16.960
−14.355
1.524
1.00
38.64
B
C


ATOM
994
OG
SER B
50
−16.843
−14.194
0.122
1.00
41.82
B
O


ATOM
995
N
SER B
51
−15.632
−17.468
0.738
1.00
49.72
B
N


ATOM
996
CA
SER B
51
−15.915
−18.819
0.251
1.00
48.33
B
C


ATOM
997
C
SER B
51
−15.090
−19.846
1.015
1.00
48.30
B
C


ATOM
998
O
SER B
51
−14.964
−20.992
0.587
1.00
39.41
B
O


ATOM
999
CB
SER B
51
−15.619
−18.938
−1.247
1.00
44.33
B
C


ATOM
1000
OG
SER B
51
−16.500
−18.134
−2.010
1.00
55.02
B
O


ATOM
1001
N
ASN B
52
−14.514
−19.416
2.135
1.00
47.00
B
N


ATOM
1002
CA
ASN B
52
−13.750
−20.302
3.013
1.00
42.12
B
C


ATOM
1003
C
ASN B
52
−12.414
−20.795
2.464
1.00
41.08
B
C


ATOM
1004
O
ASN B
52
−11.768
−21.645
3.080
1.00
42.93
B
O


ATOM
1005
CB
ASN B
52
−14.604
−21.489
3.462
1.00
49.34
B
C


ATOM
1006
CG
ASN B
52
−15.199
−21.287
4.840
1.00
56.21
B
C


ATOM
1007
OD1
ASN B
52
−16.408
−21.114
4.993
1.00
46.14
B
O


ATOM
1008
ND2
ASN B
52
−14.344
−21.299
5.854
1.00
54.50
B
N


ATOM
1009
N
LYS B
53
−11.996
−20.273
1.315
1.00
31.71
B
N


ATOM
1010
CA
LYS B
53
−10.663
−20.590
0.811
1.00
33.29
B
C


ATOM
1011
C
LYS B
53
−9.585
−19.861
1.621
1.00
33.31
B
C


ATOM
1012
O
LYS B
53
−9.771
−18.720
2.044
1.00
27.43
B
O


ATOM
1013
CB
LYS B
53
−10.517
−20.266
−0.679
1.00
27.59
B
C


ATOM
1014
CG
LYS B
53
−9.121
−20.606
−1.208
1.00
36.54
B
C


ATOM
1015
CD
LYS B
53
−9.032
−20.560
−2.730
1.00
42.26
B
C


ATOM
1016
CE
LYS B
53
−7.659
−21.035
−3.201
1.00
35.17
B
C


ATOM
1017
NZ
LYS B
53
−7.479
−20.908
−4.672
1.00
35.78
B
N


ATOM
1018
N
LEU B
54
−8.461
−20.537
1.829
1.00
33.51
B
N


ATOM
1019
CA
LEU B
54
−7.380
−20.017
2.652
1.00
27.32
B
C


ATOM
1020
C
LEU B
54
−6.290
−19.334
1.820
1.00
29.53
B
C


ATOM
1021
O
LEU B
54
−5.893
−19.830
0.767
1.00
36.19
B
O


ATOM
1022
CB
LEU B
54
−6.781
−21.156
3.480
1.00
31.38
B
C


ATOM
1023
CG
LEU B
54
−5.476
−20.910
4.237
1.00
33.67
B
C


ATOM
1024
CD1
LEU B
54
−5.650
−19.818
5.278
1.00
27.50
B
C


ATOM
1025
CD2
LEU B
54
−4.986
−22.199
4.882
1.00
32.84
B
C


ATOM
1026
N
PHE B
55
−5.824
−18.185
2.297
1.00
28.75
B
N


ATOM
1027
CA
PHE B
55
−4.682
−17.494
1.708
1.00
27.50
B
C


ATOM
1028
C
PHE B
55
−3.775
−17.062
2.846
1.00
25.87
B
C


ATOM
1029
O
PHE B
55
−4.255
−16.629
3.884
1.00
32.23
B
O


ATOM
1030
CB
PHE B
55
−5.131
−16.261
0.921
1.00
27.64
B
C


ATOM
1031
CG
PHE B
55
−6.026
−16.572
−0.244
1.00
22.94
B
C


ATOM
1032
CD1
PHE B
55
−7.399
−16.567
−0.096
1.00
22.20
B
C


ATOM
1033
CD2
PHE B
55
−5.488
−16.854
−1.491
1.00
27.58
B
C


ATOM
1034
CE1
PHE B
55
−8.226
−16.847
−1.165
1.00
30.38
B
C


ATOM
1035
CE2
PHE B
55
−6.306
−17.135
−2.572
1.00
26.44
B
C


ATOM
1036
CZ
PHE B
55
−7.681
−17.130
−2.408
1.00
32.90
B
C


ATOM.
1037
N
GLN B
55
−2.467
−17.172
2.668
1.00
28.02
B
N


ATOM
1038
CA
GLN B
56
−1.576
−16.878
3.773
1.00
27.44
B
C


ATOM
1039
C
GLN B
56
−0.267
−16.221
3.363
1.00
31.46
B
C


ATOM
1040
O
GLN B
56
0.192
−16.362
2.231
1.00
37.98
B
O


ATOM
1041
CB
GLN B
56
−1.301
−18.151
4.576
1.00
33.26
B
C


ATOM
1042
CG
GLN B
56
−0.939
−19.360
3.730
1.00
32.44
B
C


ATOM
1043
CD
GLN B
56
−0.622
−20.589
4.571
1.00
41.26
B
C


ATOM
1044
OE1
GLN B
56
0.246
−20.552
5.445
1.00
40.41
B
O


ATOM
1045
NE2
GLN B
56
−1.325
−21.687
4.305
1.00
39.56
B
N


ATOM
1046
N
TYR B
57
0.317
−15.487
4.302
1.00
21.88
B
N


ATOM
1047
CA
TYR B
57
1.658
−14.946
4.150
1.00
22.42
B
C


ATOM
1048
C
TYR B
57
2.390
−15.047
5.480
1.00
22.08
B
C


ATOM
1049
O
TYR B
57
1.793
−14.877
6.539
1.00
23.51
B
O


ATOM
1050
CB
TYR B
57
1.638
−13.479
3.701
1.00
24.62
B
C


ATOM
1051
CG
TYR B
57
2.957
−12.787
3.985
1.00
23.21
B
C


ATOM
1052
CD1
TYR B
57
4.037
−12.924
3.120
1.00
24.26
B
C


ATOM
1053
CD2
TYR B
57
3.137
−12.036
5.140
1.00
21.52
B
C


ATOM
1054
CE1
TYR B
57
5.252
−12.318
3.387
1.00
22.38
B
C


ATOM
1055
CE2
TYR B
57
4.348
−11.422
5.416
1.00
20.47
B
C


ATOM
1056
CZ
TYR B
57
5.402
−11.565
4.537
1.00
25.24
B
C


ATOM
1057
OH
TYR B
57
6.609
−10.950
4.805
1.00
20.23
B
O


ATOM
1058
N
ALA B
58
3.689
−15.308
5.424
1.00
21.77
B
N


ATOM
1059
CA
ALA B
58
4.499
−15.335
6.631
1.00
24.55
B
C


ATOM
1060
C
ALA B
58
5.950
−14.993
6.308
1.00
20.16
B
C


ATOM
1061
O
ALA B
58
6.479
−15.431
5.294
1.00
20.99
B
O


ATOM
1062
CB
ALA B
58
4.393
−16.689
7.302
1.00
27.40
B
C


ATOM
1063
N
SER B
59
6.585
−14.199
7.188
1.00
24.98
B
N


ATOM
1064
CA
SER B
59
7.967
−13.781
6.941
1.00
26.54
B
C


ATOM
1065
C
SER B
59
8.948
−14.926
7.182
1.00
30.03
B
C


ATOM
1066
O
SER B
59
10.132
−14.809
6.877
1.00
21.34
B
O


ATOM
1067
CB
SER B
59
8.327
−12.559
7.794
1.00
22.90
B
C


ATOM
1068
OG
SER B
59
8.172
−12.824
9.179
1.00
25.51
B
O


ATOM
1069
N
THR B
60
8.439
−16.020
7.748
1.00
48.65
B
N


ATOM
1070
CA
THR B
60
9.151
−17.296
7.827
1.00
46.35
B
C


ATOM
1071
C
THR B
60
8.101
−18.397
7.770
1.00
52.29
B
C


ATOM
1072
O
THR B
60
6.948
−18.134
7.434
1.00
49.50
B
O


ATOM
1073
CB
THR B
60
9.948
−17.458
9.134
1.00
54.49
B
C


ATOM
1074
OG1
THR B
60
9.042
−17.536
10.243
1.00
57.06
B
O


ATOM
1075
CG2
THR B
60
10.910
−16.295
9.340
1.00
65.06
B
C


ATOM
1076
N
ASP B
61
8.486
−19.625
8.104
1.00
37.07
B
N


ATOM
1077
CA
ASP B
61
7.527
−20.726
8.124
1.00
35.62
B
C


ATOM
1078
C
ASP B
61
6.343
−20.347
9.009
1.00
40.19
B
C


ATOM
1079
O
ASP B
61
6.513
−19.998
10.183
1.00
36.11
B
O


ATOM
1080
CB
ASP B
61
8.173
−22.024
8.623
1.00
41.27
B
C


ATOM
1081
CG
ASP B
61
9.375
−22.440
7.792
1.00
49.43
B
C


ATOM
1082
OD1
ASP B
61
10.392
−21.707
7.787
1.00
53.39
B
O


ATOM
1083
OD2
ASP B
61
9.320
−23.512
7.156
1.00
44.21
B
O


ATOM
1084
N
MET B
62
5.146
−20.409
8.432
1.00
43.31
B
N


ATOM
1085
CA
MET B
62
3.926
−20.014
9.128
1.00
38.52
B
C


ATOM
1086
C
MET B
62
3.808
−20.643
10.511
1.00
42.96
B
C


ATOM
1087
O
MET B
62
3.315
−20.015
11.451
1.00
41.37
B
O


ATOM
1088
CB
MET B
62
2.696
−20.381
8.301
1.00
31.75
B
C


ATOM
1089
CG
MET B
62
1.390
−20.116
9.027
1.00
37.30
B
C


ATOM
1090
SD
MET B
62
1.265
−18.411
9.606
1.00
31.33
B
S


ATOM
1091
CE
MET B
62
0.980
−17.545
8.070
1.00
24.54
B
C


ATOM
1092
N
ASP B
63
4.265
−21.884
10.629
1.00
49.42
B
N


ATOM
1093
CA
ASP B
63
4.104
−22.643
11.862
1.00
47.63
B
C


ATOM
1094
C
ASP B
63
5.076
−22.198
12.950
1.00
44.15
B
C


ATOM
1095
O
ASP B
63
4.859
−22.462
14.127
1.00
46.49
B
O


ATOM
1096
CB
ASP B
63
4.250
−24.140
11.587
1.00
59.12
B
C


ATOM
1097
CG
ASP B
63
3.201
−24.656
10.616
1.00
66.90
B
C


ATOM
1098
OD1
ASP B
63
2.006
−24.684
10.985
1.00
59.57
B
O


ATOM
1099
OD2
ASP B
63
3.576
−25.034
9.483
1.00
67.57
B
O


ATOM
1100
N
LYS B
64
6.147
−21.520
12.558
1.00
41.21
B
N


ATOM
1101
CA
LYS B
64
7.111
−21.032
13.536
1.00
39.98
B
C


ATOM
1102
C
LYS B
64
6.595
−19.774
14.237
1.00
39.97
B
C


ATOM
1103
O
LYS B
64
6.717
−19.639
15.454
1.00
33.04
B
O


ATOM
1104
CB
LYS B
64
8.471
−20.785
12.880
1.00
44.04
B
C


ATOM
1105
CG
LYS B
64
9.091
−22.046
12.290
1.00
54.30
B
C


ATOM
1106
CD
LYS B
64
10.492
−21.798
11.749
1.00
57.87
B
C


ATOM
1107
CE
LYS B
64
11.106
−23.085
11.213
1.00
56.54
B
C


ATOM
1108
NZ
LYS B
64
12.416
−22.845
10.554
1.00
57.68
B
N


ATOM
1109
N
VAL B
65
6.011
−18.862
13.464
1.00
35.84
B
H


ATOM
1110
CA
VAL B
65
5.418
−17.651
14.022
1.00
32.80
B
C


ATOM
1111
C
VAL B
65
4.295
−18.006
14.994
1.00
32.81
B
C


ATOM
1112
O
VAL B
65
4.166
−17.406
16.067
1.00
29.45
B
O


ATOM
1113
CB
VAL B
6S
4.836
−16.746
12.919
1.00
30.22
B
C


ATOM
1114
CG1
VAL B
65
4.343
−15.435
13.517
1.00
25.45
B
C


ATOM
1115
CG2
VAL B
65
5.868
−16.493
11.835
1.00
34.33
B
C


ATOM
1116
N
LEU B
66
3.488
−18.990
14.610
1.00
29.80
B
N


ATOM
1117
CA
LEU B
66
2.369
−19.424
15.430
1.00
34.20
B
C


ATOM
1118
C
LEU B
66
2.828
−19.990
16.773
1.00
41.26
B
C


ATOM
1119
O
LEU B
66
−2.331
−19.586
17.827
1.00
39.01
B
O


ATOM
1120
CB
LEU B
66
1.517
−20.443
14.673
1.00
35.53
B
C


ATOM
1121
CG
LEU B
66
0.792
−19.857
13.460
1.00
36.37
B
C


ATOM
1122
CD1
LEU B
66
−0.167
−20.870
12.864
1.00
31.71
B
C


ATOM
1123
CD2
LEU B
66
0.056
−18.584
13.861
1.00
31.61
B
C


ATOM
1124
N
LEU B
67
3.779
−20.917
16.737
1.00
41.41
B
N


ATOM
1125
CA
LEU B
67
4.285
−21.510
17.967
1.00
41.65
B
C


ATOM
1126
C
LEU B
67
4.886
−20.442
18.870
1.00
41.31
B
C


ATOM
1127
O
LEU B
67
4.796
−20.532
20.093
1.00
44.99
B
O


ATOM
1128
CB
LEU B
67
5.309
−22.611
17.672
1.00
44.98
B
C


ATOM
1129
CG
LEU B
67
4.740
−24.028
17.518
1.00
46.47
B
C


ATOM
1130
CD1
LEU B
67
3.909
−24.399
18.741
1.00
51.36
B
C


ATOM
1131
CD2
LEU B
67
3.910
−24.170
16.247
1.00
47.13
B
C


ATOM
1132
N
LYS B
68
5.490
−19.429
18.260
1.00
30.15
B
N


ATOM
1133
CA
LYS B
68
6.064
−18.321
19.007
1.00
28.49
B
C


ATOM
1134
C
LYS B
68
4.952
−17.512
19.664
1.00
36.89
B
C


ATOM
1135
O
LYS B
68
5.133
−16.932
20.736
1.00
38.72
B
O


ATOM
1136
CB
LYS B
68
6.905
−17.433
18.087
1.00
31.22
B
C


ATOM
1137
CG
LYS B
68
7.590
−16.276
18.794
1.00
36.27
B
C


ATOM
1138
CD
LYS B
68
8.714
−15.695
17.952
1.00
41.13
B
C


ATOM
1139
CE
LYS B
68
9.450
−14.598
18.705
1.00
38.43
B
C


ATOM
1140
NZ
LYS B
68
10.588
−14.050
17.922
1.00
37.80
B
N


ATOM
1141
N
TYR B
69
3.794
−17.486
19.013
1.00
39.71
B
N


ATOM
1142
CA
TYR B
69
2.631
−16.793
19.547
1.00
41.49
B
C


ATOM
1143
C
TYR B
69
2.057
−17.534
20.750
1.00
40.39
B
C


ATOM
1144
O
TYR B
69
1.821
−16.941
21.803
1.00
39.82
B
O


ATOM
1145
CB
TYR B
69
1.561
−16.645
18.464
1.00
36.39
B
C


ATOM
1146
CG
TYR B
69
0.250
−16.092
18.968
1.00
31.52
B
C


ATOM
1147
CD1
TYR B
69
0.068
−14.727
19.125
1.00
28.35
B
C


ATOM
1148
CD2
TYR B
69
−0.805
−16.935
19.284
1.00
32.82
B
C


ATOM
1149
CE1
TYR B
69
−1.126
−14.217
19.581
1.00
26.39
B
C


ATOM
1150
CE2
TYR B
69
−2.006
−16.432
19.744
1.00
26.38
B
C


ATOM
1151
CZ
TYR B
69
−2.160
−15.072
19.889
1.00
27.61
B
C


ATOM
1152
OH
TYR B
69
−3.352
−14.558
20.349
1.00
30.19
B
O


ATOM
1153
N
THR B
70
1.828
−18.832
20.586
1.00
34.49
B
N


ATOM
1154
CA
THR B
70
1.244
−19.635
21.652
1.00
40.30
B
C


ATOM
1155
C
THR B
70
2.209
−19.763
22.824
1.00
43.81
B
C


ATOM
1156
O
THR B
70
1.792
−19.786
23.982
1.00
52.58
B
O


ATOM
1157
CB
THR B
70
0.812
−21.030
21152
1.00
41.92
B
C


ATOM
1158
OG1
THR B
70
1.903
−21.656
20.466
1.00
51.10
B
O


ATOM
1159
CG2
THR B
70
−0.368
−20.909
20.198
1.00
38.12
B
C


ATOM
1160
N
GLU B
71
3.501
−19.835
22.521
1.00
44.26
B
N


ATOM
1161
CA
GLU B
71
4.524
−19.856
23.561
1.00
52.17
B
C


ATOM
1162
C
GLU B
71
4.573
−18.509
24.278
1.00
47.45
B
C


ATOM
1163
O
GLU B
71
4.934
−18.430
25.452
1.00
51.35
B
O


ATOM
1164
CB
GLU B
71
5.899
−20.193
22.970
1.00
41.33
B
C


ATOM
1165
N
TYR B
72
4.206
−17.453
23.557
1.00
47.78
B
N


ATOM
1166
CA
TYR B
72
4.186
−16.103
24.107
1.00
49.37
B
C


ATOM
1167
C
TYR B
72
3.136
−16.007
25.205
1.00
57.87
B
C


ATOM
1168
O
TYR B
72
3.440
−15.631
26.340
1.00
57.55
B
O


ATOM
1169
CB
TYR B
72
3.871
−15.097
22.997
1.00
50.17
B
C


ATOM
1170
CG
TYR B
72
4.235
−13.657
23.302
1.00
46.16
B
C


ATOM
1171
CD1
TYR B
72
5.430
−13.114
22.846
1.00
41.62
B
C


ATOM
1172
CD2
TYR B
72
3.374
−12.833
24.024
1.00
47.37
B
C


ATOM
1173
CE1
TYR B
72
5.768
−11.798
23.107
1.00
38.98
B
C


ATOM
1174
CE2
TYR B
72
3.702
−11.509
24.291
1.00
41.15
B
C


ATOM
1175
CZ
TYR B
72
4.903
−11.000
23.828
1.00
46.34
B
C


ATOM
1176
OH
TYR B
72
5.246
−9.691
24.081
1.00
48.06
B
O


ATOM
1177
N
ASN B
73
1.900
−16.354
24.854
1.00
73.31
B
N


ATOM
1178
CA
ASN B
73
0.776
−16.302
25.784
1.00
74.49
B
C


ATOM
1179
C
ASN B
73
0.903
−17.343
26.894
1.00
82.99
B
C


ATOM
1180
O
ASN B
73
0.162
−18.328
26.926
1.00
80.74
B
O


ATOM
1181
CB
ASN B
73
−0.557
−16.487
25.042
1.00
71.38
B
C


ATOM
1182
CG
ASN B
73
−0.860
−15.349
24.071
1.00
61.49
B
C


ATOM
1183
OD1
ASN B
73
−1.840
−14.621
24.237
1.00
64.97
B
O


ATOM
1184
ND2
ASN B
73
−0.023
−15.198
23.053
1.00
53.52
B
N


TER


ATOM
1185
O5′
ADE E
1
−18.730
−9.736
−18.656
1.00
29.47
E
O


ATOM
1186
C5′
ADE E
1
−18.988
−11.075
−19.073
1.00
30.92
E
C


ATOM
1187
C4′
ADE E
1
−17.709
−11.792
−19.477
1.00
31.56
E
C


ATOM
1188
O4′
ADE E
1
−17.094
−11.116
−20.606
1.00
28.61
E
O


ATOM
1189
C3′
ADE E
1
−16.621
−11.853
−18.406
1.00
35.77
E
C


ATOM
1190
O3′
ADE E
1
−15.887
−13.057
−18.533
1.00
31.63
E
O


ATOM
1191
C2′
ADE E
1
−15.739
−10.670
−18.779
1.00
36.34
E
C


ATOM
1192
C1′
ADE E
1
−15.738
−10.885
−20.284
1.00
30.42
E
C


ATOM
1193
N9
ADE E
1
−15.256
−9.747
−21.050
1.00
30.35
E
N


ATOM
1194
C8
ADE E
1
−14.044
−9.644
−21.669
1.00
31.25
E
C


ATOM
1195
N7
ADE E
1
−13.867
−8.508
−22.293
1.00
29.12
E
N


ATOM
1196
C5
ADE E
1
−15.041
−7.823
−22.062
1.00
24.57
E
C


ATOM
1197
C6
ADE E
1
−15.465
−6.552
−22.461
1.00
26.42
E
C


ATOM
1198
N6
ADE E
1
−14.705
−5.753
−23.207
1.00
29.08
E
N


ATOM
1199
N1
ADE E
1
−16.693
−6.147
−22.069
1.00
32.94
E
N


ATOM
1200
C2
ADE E
1
−17.434
−6.980
−21.321
1.00
32.52
E
C


ATOM
1201
N3
ADE E
1
−17.138
−8.206
−20.882
1.00
29.17
E
N


ATOM
1202
C4
ADE E
1
−15.913
−8.567
−21.297
1.00
28.60
E
C


ATOM
1203
P
ADE E
2
−14.980
−13.540
−17.328
1.00
39.32
E
P


ATOM
1204
OP1
ADE E
2
−14.609
−14.955
−17.546
1.00
40.48
E
O


ATOM
1205
OP2
ADE E
2
−15.600
−13.127
−16.063
1.00
34.58
E
O


ATOM
1206
O5′
ADE E
2
−13.642
−12.657
−17.522
1.00
46.72
E
O


ATOM
1207
C5′
ADE E
2
−12.623
−13.009
−18.459
1.00
35.44
E
C


ATOM
1208
C4′
ADE E
2
−11.485
−12.005
−18.354
1.00
37.56
E
C


ATOM
1209
O4′
ADE E
2
−11.957
−10.700
−18.795
1.00
40.64
E
O


ATOM
1210
C3′
ADE E
2
−10.967
−11.762
−16.938
1.00
35.93
E
C


ATOM
1211
O3′
ADE E
2
−9.635
−11.291
−16.984
1.00
43.80
E
O


ATOM
1212
C2′
ADE E
2
−11.869
−10.630
−16.474
1.00
37.03
E
C


ATOM
1213
C1′
ADE E
2
−11.769
−9.786
−17.734
1.00
32.46
E
C


ATOM
1214
N9
ADE E
2
−12.739
−8.703
−17.801
1.00
30.38
E
N


ATOM
1215
CB
ADE E
2
−13.795
−8.479
−16.959
1.00
33.19
E
C


ATOM
1216
N7
ADE E
2
−14.493
−7.404
−17.259
1.00
31.00
E
N


ATOM
1217
C5
ADE E
2
−13.843
−6.893
−18.372
1.00
30.47
E
C


ATOM
1218
C6
ADE E
2
−14.084
−5.764
−19.174
1.00
29.69
E
C


ATOM
1219
N6
ADE E
2
−15.097
−4.919
−18.959
1.00
30.34
E
N


ATOM
1220
N1
ADE E
2
−13.242
−5.537
−20.202
1.00
27.90
E
N


ATOM
1221
C2
ADE E
2
−12.230
−6.383
−20.416
1.00
27.22
E
C


ATOM
1222
N3
ADE E
2
−11.905
−7.479
−19.735
1.00
27.95
E
N


ATOM
1223
C4
ADE E
2
−12.760
−7.679
−18.718
1.00
29.70
E
C


ATOM
1224
P
ADE E
3
−8.398
−12.239
−16.627
1.00
42.48
E
P


ATOM
1225
OP1
ADE E
3
−8.627
−13.552
−17.273
1.00
38.14
E
O


ATOM
1226
OP2
ADE E
3
−8.173
−12.152
−15.165
1.00
39.30
E
O


ATOM
1227
O5′
ADE E
3
−7.186
−11.486
−17.357
1.00
35.22
E
O


ATOM
1228
C5′
ADE E
3
−7.251
−11.226
−18.752
1.00
29.83
E
C


ATOM
1229
C4′
ADE E
3
−6.680
−9.856
−19.079
1.00
33.29
E
C


ATOM
1230
O4′
ADE E
3
−7.724
−8.849
−19.015
1.00
30.41
E
O


ATOM
1231
C3′
ADE E
3
−5.555
−9.369
−18.163
1.00
40.46
E
C


ATOM
1232
O3′
ADE E
3
−4.525
−8.798
−18.955
1.00
37.31
E
O


ATOM
1233
C2′
ADE E
3
−6.237
−8.316
−17.280
1.00
34.29
E
C


ATOM
1234
C1′
ADE E
3
−7.283
−7.751
−18.235
1.00
37.00
E
C


ATOM
1235
N9
ADE E
3
−8.454
−7.181
−17.576
1.00
31.30
E
N


ATOM
1236
C8
ADE E
3
−9.136
−7.698
−16.508
1.00
30.32
E
C


ATOM
1237
N7
ADE E
3
−10.162
−6.971
−16.133
1.00
31.10
E
N


ATOM
1238
C5
ADE E
3
−10.153
−5.905
−17.019
1.00
29.56
E
C


ATOM
1239
C6
ADE E
3
−10.988
−4.779
−17.159
1.00
28.07
E
C


ATOM
1240
N6
ADE E
3
−12.036
−4.540
−16.363
1.00
32.00
E
N


ATOM
1241
N1
ADE E
3
−10.700
−3.905
−18.150
1.00
32.19
E
N


ATOM
1242
C2
ADE E
3
−9.650
−4.146
−18.946
1.00
29.48
E
C


ATOM
1243
N3
ADE E
3
−8.799
−5.172
−18.911
1.00
29.41
E
N


ATOM
1244
C4
ADE E
3
−9.108
−6.019
−17.917
1.00
28.05
E
C


ATOM
1245
P
GUA E
4
−3.192
−8.251
−18.255
1.00
44.81
E
P


ATOM
1246
OP1
GUA E
4
−2.061
−8.508
−19.174
1.00
26.47
E
O


ATOM
1247
OP2
GUA E
4
−3.173
−8.771
−16.867
1.00
42.97
E
O


ATOM
1248
O5′
GUA E
4
−3.445
−6.670
−18.204
1.00
41.54
E
O


ATOM
1249
C5′
GUA E
4
−3.525
−5.970
−19.443
1.00
41.38
E
C


ATOM
1250
C4′
GUA E
4
−4.139
−4.590
−19.282
1.00
40.49
E
C


ATOM
1251
O4′
GUA E
4
−5.362
−4.659
−18.507
1.00
41.29
E
O


ATOM
1252
C3′
GUA E
4
−3.273
−3.548
−18.579
1.00
49.70
E
C


ATOM
1253
O3′
GUA E
4
−3.057
−2.496
−19.513
1.00
51.54
E
O


ATOM
1254
C2′
GUA E
4
−4.099
−3.111
−17.362
1.00
40.72
E
C


ATOM
1255
C1′
GUA E
4
−5.513
−3.432
−17.833
1.00
35.99
E
C


ATOM
1256
N9
GUA E
4
−6.536
−3.626
−16.805
100
35.36
E
N


ATOM
1257
C8
GUA E
4
−6.606
−4.633
−15.869
1.00
31.20
E
C


ATOM
1258
N7
GUA E
4
−7.657
−4.550
−15.094
1.00
30.27
E
N


ATOM
1259
C5
GUA E
4
−8.334
−3.418
−15.544
1.00
31.07
E
C


ATOM
1260
C6
GUA E
4
−9.545
−2.824
−15.091
1.00
29/65
E
C


ATOM
1261
O6
GUA E
4
−10.299
−3.183
−14.166
1.00
25.90
E
O


ATOM
1252
N1
GUA E
4
−9.863
−1.693
−15.837
1.00
27.69
E
N


ATOM
1263
C2
GUA E
4
−9.114
−1.197
−16.878
1.00
32.22
E
C


ATOM
1264
N2
GUA E
4
−9.586
−0.090
−17.471
1.00
36.73
E
N


ATOM
1265
N3
GUA E
4
−7.981
−1.739
−17.312
1.00
30.68
E
N


ATOM
1266
C4
GUA E
4
−7.655
−2.844
−16.601
1.00
32.71
E
C


ATOM
1267
P
CYT E
5
−2.178
−1.210
−19.151
1.00
55.63
E
P


ATOM
1268
OP1
CYT E
5
−1.471
−0.815
−20.393
1.00
38.22
E
O


ATOM
1269
OP2
CYT E
5
−1.446
−1.473
−17.889
1.00
40.16
E
O


ATOM
1270
O5′
CYT E
5
−3.303
−0.112
−18.855
1.00
37.38
E
O


ATOM
1271
C5′
CYT E
5
−4.265
0.131
−19.866
1.00
33.01
E
C


ATOM
1272
C4′
CYT E
5
−5.032
1.402
−19.579
1.00
33.11
E
C


ATOM
1273
O4′
CYT E
5
−6.050
1.157
−18.576
1.00
30.77
E
O


ATOM
1274
C3′
CYT E
5
−4.180
2.557
−19.075
1.00
34.24
E
C


ATOM
1275
O3′
CYT E
5
−4.639
3.713
−19.760
1.00
39.20
E
O


ATOM
1276
C2′
CYT E
5
−4.446
2.561
−17.565
1.00
31.20
E
C


ATOM
1277
C1′
CYT E
5
−5.863
2.000
−17.463
1.00
28.63
E
C


ATOM
1278
N1
CYT E
5
−6.146
1.145
−16.274
1.00
29.46
E
N


ATOM
1279
C2
CYT E
5
−7.212
1.483
−15.439
1.00
26.08
E
C


ATOM
1280
O2
CYT E
5
−7.885
2.490
−15.698
1.00
28.38
E
O


ATOM
1281
N3
CYT E
5
−7.479
0.700
−14.367
1.00
26.72
E
N


ATOM
1282
C4
CYT E
5
−6.735
−0.378
−14.115
1.00
25.28
E
C


ATOM
1283
N4
CYT E
5
−7.053
−1.106
−13.036
1.00
22.58
E
N


ATOM
1284
C5
CYT E
5
−5.642
−0.745
−14.956
1.00
25.38
E
C


ATOM
1285
C6
CYT E
5
−5.390
0.038
−16.014
1.00
30.65
E
C


ATOM
1286
P
THY E
6
−4.170
5.191
−19.383
1.00
60.37
E
P


ATOM
1287
OP1
THY E
6
−4.538
6.060
−20.525
1.00
54.22
E
O


ATOM
1288
OP2
THY E
6
−2.773
5.142
−18.892
1.00
49.93
E
O


ATOM
1289
O5′
THY E
6
−5.109
5.566
−18.140
1.00
47.68
E
O


ATOM
1290
C5′
THY E
6
−6.386
6.162
−18.345
1.00
46.46
E
C


ATOM
1291
C4′
THY E
6
−6.806
6.961
−17.125
1.00
38.37
E
C


ATOM
1292
O4′
THY E
6
−7.109
6.050
−16.035
1.00
39.69
E
O


ATOM
1293
C3′
THY E
6
−5.735
7.892
−16.572
1.00
43.33
E
C


ATOM
1294
O3′
THY E
6
−6.340
8.950
−15.857
1.00
49.28
E
O


ATOM
1295
C2′
THY E
6
−5.027
6.982
−15.582
1.00
39.84
E
C


ATOM
1296
C1′
THY E
6
−6.267
6.372
−14.942
1.00
44.31
E
C


ATOM
1297
N1
THY E
6
−5.997
5.155
−14.132
1.00
36.55
E
N


ATOM
1298
C2
THY E
6
−6.920
4.771
−13.188
1.00
34.38
E
C


ATOM
1299
O2
THY E
6
−7.955
5.383
−12.988
1.00
33.38
E
O


ATOM
1300
N3
THY E
6
−6.584
3.638
−12.489
1.00
29.23
E
N


ATOM
1301
C4
THY E
6
−5.440
2.878
−12.640
1.00
30.85
E
C


ATOM
1302
O4
THY E
6
−5.220
1.878
−11.967
1.00
34.06
E
O


ATOM
1303
C5
THY E
6
−4.515
3.343
−13.642
1.00
32.80
E
C


ATOM
1304
C7
THY E
6
−3.238
2.592
−13.883
1.00
27.26
E
C


ATOM
1305
C6
THY E
6
−4.831
4.446
−14.332
1.00
30.87
E
C


ATOM
1306
P
ADE E
7
−6.618
10.359
−16.554
1.00
45.58
E
P


ATOM
1307
OP1
ADE E
7
−7.118
10.099
−17.923
1.00
48.75
E
O


ATOM
1308
OP2
ADE E
7
−5.421
11.205
−16.345
1.00
50.29
E
O


ATOM
1309
O5′
ADE E
7
−7.804
10.955
−15.662
1.00
37.42
E
O


ATOM
1310
C5′
ADE E
7
−9.051
10.284
−15.612
1.00
40.53
E
C


ATOM
1311
C4′
ADE E
7
−9.601
10.242
−14.196
1.00
40.88
E
C


ATOM
1312
O4′
ADE E
7
−8.962
9.183
−13.434
1.00
42.29
E
O


ATOM
1313
C3′
ADE E
7
−9.423
11.515
−13.380
1.00
43.86
E
C


ATOM
1314
O3′
ADE E
7
−10.618
11.704
−12.623
1.00
46.18
E
O


ATOM
1315
C2′
ADE E
7
−8.191
11.211
−12.518
1.00
38.63
E
C


ATOM
1316
C1′
ADE E
7
−8.329
9.708
−12.280
1.00
40.37
E
C


ATOM
1317
N9
ADE E
7
−7.083
8.955
−12.110
1.00
35.39
E
N


ATOM
1318
CB
ADE E
7
−5.878
9.165
−12.724
1.00
38.43
E
C


ATOM
1319
N7
ADE E
7
−4.946
8.303
−12.375
1.00
38.83
E
N


ATOM
1320
C5
ADE E
7
−5.583
7.461
−11.475
1.00
32.45
E
C


ATOM
1321
C6
ADE E
7
−5.153
6.335
−10.738
1.00
28.45
E
C


ATOM
1322
N6
ADE E
7
−3.917
5.831
−10.788
1.00
23.96
e
N


ATOM
1323
N1
ADE E
7
−6.052
5.733
−9.930
1.00
28.10
E
N


ATOM
1324
C2
ADE E
7
−7.293
6.222
−9.866
1.00
28.25
E
C


ATOM
1325
N3
ADE E
7
−7.814
7.266
−10.509
1.00
34.76
E
N


ATOM
1326
C4
ADE E
7
−6.901
7.849
−11.306
1.00
35.01
E
C


ATOM
1327
P
THY E
8
−10.849
13.012
−11.730
1.00
56.64
E
P


ATOM
1328
OP1
THY E
8
−12.282
13.371
−11.831
1.00
50.90
E
O


ATOM
1329
OP2
THY E
8
−9.782
13.995
−12.048
1.00
41.51
E
O


ATOM
1330
O5′
THY E
8
−10.591
12.465
−10.254
1.00
37.60
E
O


ATOM
1331
C5′
THY E
8
−11.256
11.287
−9.857
1.00
37.93
E
C


ATOM
1332
C4′
THY E
8
−10.552
10.694
−8.657
1.00
38.57
E
C


ATOM
1333
O4′
THY E
8
−9.292
10.106
−9.047
1.00
40.12
E
O


ATOM
1334
C3′
THY E
8
−10.174
11.692
−7.570
1.00
30.77
E
C


ATOM
1335
O3′
THY E
8
−11.212
11.693
−6.602
1.00
31.18
E
O


ATOM
1336
C2′
THY E
8
−8.839
11.161
−7.031
1.00
28.75
E
C


ATOM
1337
C1′
THY E
8
−8.637
9.870
−7.823
1.00
31.57
E
C


ATOM
1338
N1
THY E
8
−7.211
9.446
−8.069
1.00
30.96
E
N


ATOM
1339
C2
THY E
8
−6.738
8.325
−7.418
1.00
29.46
E
C


ATOM
1340
O2
THY E
8
−7.411
7.658
−6.647
1.00
28.41
E
O


ATOM
1341
N3
THY E
8
−5.434
8.008
−7.696
1.00
25.51
E
N


ATOM
1342
C4
THY E
8
−4.573
8.678
−8.543
1.00
28.41
E
C


ATOM
1343
O4
THY E
8
−3.414
8.304
−8.725
1.00
24.27
E
O


ATOM
1344
C5
THY E
8
−5.133
9.838
−9.195
1.00
28.63
E
C


ATOM
1345
C7
THY E
8
−4.291
10.650
−10.138
1.00
36.79
E
C


ATOM
1346
C6
THY E
8
−6.405
10.163
−8.930
1.00
26.96
E
C


ATOM
1347
P
THY E
8
−11.056
12.419
−5.183
1.00
42.41
E
P


ATOM
1348
OP1
THY E
9
−12.415
12.694
−4.663
1.00
31.14
E
O


ATOM
1349
OP2
THY E
9
−10.054
13.502
−5.314
1.00
35.31
E
O


ATOM
1350
O5′
THY E
9
−10.434
11.264
−4.279
1.00
37.55
E
O


ATOM
1351
C5′
THY E
9
−11.266
10.160
−3.990
1.00
35.57
E
C


ATOM
1352
C4′
THY E
9
−10.478
9.121
−3.227
1.00
33.83
E
C


ATOM
1353
O4′
THY E
9
−9.220
8.899
−3.906
1.00
29.86
E
O


ATOM
1354
C3′
THY E
9
−10.144
9.494
−1.786
1.00
28.03
E
C


ATOM
1355
O3′
THY E
9
−10.370
8.323
−1.022
1.00
31.20
E
O


ATOM
1356
C2′
THY E
9
−8.675
9.907
−1.859
1.00
27.45
E
C


ATOM
1357
C1′
THY E
9
−8.172
8.985
−2.967
1.00
31.01
E
C


ATOM
1358
N1
THY E
9
−6.962
9.450
−3.704
1.00
28.12
E
N


ATOM
1359
C2
THY E
9
−5.909
8.582
−3.811
1.00
25.18
E
C


ATOM
1360
O2
THY E
9
−5.927
7.464
−3.328
1.00
26.89
E
O


ATOM
1361
N3
THY E
9
−4.838
9.074
−4.507
1.00
26.79
E
N


ATOM
1362
C4
THY E
9
−4.717
10.316
−5.095
1.00
24.43
E
C


ATOM
1363
O4
THY E
9
−3.708
10.664
−5.700
1.00
27.08
E
O


ATOM
1364
C5
THY E
9
−5.853
11.178
−4.945
1.00
26.20
E
C


ATOM
1365
C7
THY E
9
−5.819
12.553
−5.545
1.00
26.68
E
C


ATOM
1366
C6
THY E
9
−6.911
10.711
−4.266
1.00
30.99
E
C


ATOM
1367
P
ADE E
10
−10.116
8.233
0.551
1.00
27.69
E
P


ATOM
1368
OP1
ADE E
10
−10.999
7.180
1.102
1.00
25.31
E
O


ATOM
1369
OP2
ADE E
10
−10.161
9.594
1123
1.00
31.49
E
O


ATOM
1370
O5′
ADE E
10
−8.616
7.674
0.595
1.00
37.35
E
O


ATOM
1371
C5′
ADE E
10
−8.361
6.335
0.171
1.00
23.82
E
C


ATOM
1372
C4′
ADE E
10
−6.969
5.856
0.564
1.00
22.72
E
C


ATOM
1373
O4′
ADE E
10
−5.977
6.502
−0.266
1.00
23.11
E
O


ATOM
1374
C3′
ADE E
10
−6.531
6.128
2.002
1.00
25.58
E
C


ATOM
1375
O3′
ADE E
10
−5.853
4.975
2.479
1.00
22.92
E
O


ATOM
1376
C2′
ADE E
10
−5.596
7.330
1.881
1.00
19.12
E
C


ATOM
1377
C1′
ADE E
10
−4.945
7.047
0.533
1.00
23.66
E
C


ATOM
1378
N9
ADE E
10
−4.450
8.219
−0.185
1.00
23.63
E
N


ATOM
1379
C8
ADE E
10
−5.137
9.377
−0.427
1.00
20.43
E
C


ATOM
1380
N7
ADE E
10
−4.449
10.259
−1.116
1.00
21.56
E
N


ATOM
1381
C5
ADE E
10
−3.232
9.637
−1.348
1.00
20.27
E
C


ATOM
1382
C6
ADE E
10
−2.065
10.050
−2.026
1.00
23.27
E
C


ATOM
1383
N6
ADE E
10
−1.935
11.243
−2.621
1.00
22.55
E
N


ATOM
1384
N1
ADE E
10
−1.028
9.186
−2.072
1.00
21.68
E
N


ATOM
1385
C2
ADE E
10
−1.159
7.995
−1.473
1.00
20.08
E
C


ATOM
1386
N3
ADE E
10
−2.204
7.498
−0.811
1.00
21.84
E
N


ATOM
1387
C4
ADE E
10
−3.218
8.376
−0.783
1.00
20.33
E
C


ATOM
1368
P
THY E
11
−5.251
4.906
3.959
1.00
30.15
E
P


ATOM
1389
OP1
THY E
11
−5.489
3.533
4.453
1.00
30.86
E
O


ATOM
1390
OP2
THY E
11
−5.725
6.061
4.753
1.00
22.38
E
O


ATOM
1391
O5′
THY E
11
−3.686
5.080
3.667
1.00
31.02
E
O


ATOM
1392
C5′
THY E
11
−3.054
4.141
2.808
1.00
24.15
E
C


ATOM
1393
C4′
THY E
11
−1.576
4.434
2.624
1.00
27.89
E
C


ATOM
1394
O4′
THY E
11
−1.390
5.686
1.914
1.00
25.80
E
O


ATOM
1395
C3′
THY E
11
−0.762
4.531
3.910
1.00
29.91
E
C


ATOM
1396
O3′
THY E
11
0.381
3.686
3.729
1.00
26.16
E
O


ATOM
1397
C2′
THY E
11
−0.441
6.029
4.018
1.00
26.53
E
C


ATOM
1398
C1′
THY E
11
−0.387
6.444
2.547
1.00
25.90
E
C


ATOM
1399
N1
THY E
11
−0.686
7.873
2.192
1.00
23.31
E
N


ATOM
1400
C2
THY E
11
0.223
8.558
1.409
1.00
24.11
E
C


ATOM
1401
O2
THY E
11
1.270
8.088
1.011
1.00
29.11
E
O


ATOM
1402
N3
THY E
11
−0.121
9.841
1.100
1.00
22.87
E
N


ATOM
1403
C4
THY E
11
−1.265
10.498
1.485
1.00
28.65
E
C


ATOM
1404
O4
THY E
11
−1.474
11.662
1.151
1.00
36.71
E
O


ATOM
1405
C5
THY E
11
−2.185
9.732
2.295
1.00
24.77
E
C


ATOM
1406
C7
THY E
11
−3/464
10.372
2.759
1.00
24.15
E
C


ATOM
1407
C6
THY E
11
−1.862
8.466
2.606
1.00
22.01
E
C


ATOM
1408
P
THY E
12
1.421
3.356
4.904
1.00
25.44
E
P


ATOM
1409
OP1
THY E
12
2.065
2.075
4.536
1.00
24.55
E
O


ATOM
1410
OP2
THY E
12
0.765
3.505
6.222
1.00
32.62
E
O


ATOM
1411
O5′
THY E
12
2.496
4.537
4.755
1.00
26.81
E
O


ATOM
1412
C5′
THY E
12
3.296
4.563
3.566
1.00
21.48
E
C


ATOM
1413
C4′
THY E
12
4.129
5.825
3.493
1.00
23.82
E
C


ATOM
1414
O4′
THY E
12
3.290
6.969
3.188
1.00
23.67
E
O


ATOM
1415
C3′
THY E
12
4.867
6.182
4.783
1.00
24.81
E
C


ATOM
1416
O3′
THY E
12
6.206
6.506
4.466
1.00
25.36
E
O


ATOM
1417
C2′
THY E
12
4.120
7.416
5.290
1.00
18.68
E
C


ATOM
1418
C1′
THY E
12
3.788
8.050
3.948
1.00
20.51
E
C


ATOM
1419
N1
THY E
12
2.771
9.121
3.988
1.00
21.40
E
N


ATOM
1420
C2
THY E
12
2.955
10.241
3.198
1.00
22.05
E
C


ATOM
1421
O2
THY E
12
3.910
10.394
2.460
1.00
21.47
E
O


ATOM
1422
N3
THY E
12
1.967
11.186
3.304
1.00
18.78
E
N


ATOM
1423
C4
THY E
12
0.843
11.109
4.096
1.00
19.13
E
C


ATOM
1424
O4
THY E
12
0.012
12.009
4.111
1.00
26.75
E
O


ATOM
1425
C5
THY E
12
0.713
9.915
4.898
1.00
18.25
E
C


ATOM
1426
C7
THY E
12
−0.472
9.735
5.805
1.00
19.51
E
C


ATOM
1427
C6
THY E
12
1.670
8.989
4.811
1.00
19.46
E
C


ATOM
1428
P
ADE E
13
7.377
5.414
4.483
1.00
30.98
E
P


ATOM
1429
OP1
ADE E
13
7.071
4.389
3.460
1.00
28.50
E
O


ATOM
1430
OP2
ADE E
13
7.606
5.022
5.896
1.00
23.43
E
O


ATOM
1431
O5′
ADE E
13
8.623
6.284
3.975
1.00
29.72
E
O


ATOM
1432
C5′
ADE E
13
8.538
6.922
2.706
1.00
26.78
E
C


ATOM
1433
C4′
ADE E
13
9.483
8.111
2.612
1.00
31.36
E
C


ATOM
1434
O4′
ADE E
13
8.780
9.358
2.850
1.00
26.91
E
O


ATOM
1435
C3′
ADE E
13
10.671
8.113
3.567
1.00
24.84
E
C


ATOM
1436
O3′
ADE E
13
11.755
8.715
2.871
1.00
25.02
E
O


ATOM .
1437
C2′
ADE E
13
10.168
8.953
4.739
1.00
24.93
E
C


ATOM
1438
C1′
ADE E
13
9.149
9.897
4.101
1.00
28.31
E
C


ATOM
1439
N9
ADE E
13
7.913
10.036
4.860
1.00
22.96
E
N


ATOM
1440
C8
ADE E
13
7.461
9.213
5.849
1.00
20.48
E
C


ATOM
1441
N7
ADE E
13
6.310
9.588
6.352
1.00
21.80
E
N


ATOM
1442
C5
ADE E
13
5.977
10.724
5.631
1.00
19.63
E
C


ATOM
1443
C6
ADE E
13
4.867
11.590
5.680
1.00
20.30
E
C


ATOM
1444
N6
ADE E
13
3.845
11.428
6.529
1.00
19.00
E
N


ATOM
1445
N1
APE E
13
4.852
12.631
4.819
1.00
21.87
E
N


ATOM
1446
C2
ADE E
13
5.879
12.785
3.971
1.00
21.40
E
C


ATOM
1447
N3
ADE E
13
6.973
12.039
3.838
1.00
20.80
E
N


ATOM
1448
C4
ADE E
13
6.958
11.014
4.703
1.00
21.32
E
C


ATOM
1449
P
GUA E
14
13.159
9.030
3.570
1.00
31.66
E
P


ATOM
1450
OP1
GUA E
14
14.216
8.918
2.535
1.00
31.34
E
O


ATOM
1451
OP2
GUA E
14
13.251
8.231
4.813
1.00
22.94
E
O


ATOM
1452
O5
GUA E
14
13.004
10.579
3.943
1.00
25.42
E
O


ATOM
1453
C5′
GUA E
14
12.824
11.512
2.891
1.00
25.99
E
C


ATOM
1454
C4′
GUA E
14
12.492
12.896
3.415
1.00
34.31
E
C


ATOM
1455
O4′
GUA E
14
11.188
12.895
4.055
1.00
34.27
E
O


ATOM
1456
C3′
GUA E
14
13.485
13.460
4.429
1.00
37.50
E
C


ATOM
1457
O3′
GUA E
14
13.899
14.742
3.973
1.00
41.76
E
O


ATOM
1458
C2′
GUA E
14
12.698
13.526
5.738
1.00
34.47
E
C


ATOM
1459
C1′
GUA E
14
11.253
13.627
5.258
1.00
31.30
E
C


ATOM
1460
N9
GUA E
14
10.291
13.055
6.194
1.00
29.91
E
N


ATOM
1461
CB
GUA E
14
10.424
11.900
6.934
1.00
30.46
E
C


ATOM
1462
N7
GUA E
14
9.388
11.644
7.689
1.00
28.53
E
N


ATOM
1463
C5
GUA E
14
8.513
12.695
7.432
1.00
24.42
E
C


ATOM
1464
C6
GUA E
14
7.230
12.965
7.955
1.00
24.43
E
C


ATOM
1465
O6
GUA E
14
6.586
12.305
8.777
1.00
28.12
E
O


ATOM
1466
N1
GUA E
14
6.687
14.137
7.435
1.00
24.65
E
N


ATOM
1467
C2
GUA E
14
7.309
14.949
6.517
1.00
28.51
E
C


ATOM
1468
N2
GUA E
14
6.629
16.039
6.125
1.00
28.83
E
N


ATOM
1469
N3
GUA E
14
8.513
14.708
6.013
1.00
30.78
E
N


ATOM
1470
C4
GUA E
14
9.053
13.570
6.515
1.00
29.53
E
C


ATOM
1471
P
CYT E
15
14.736
15.739
4.898
1.00
56.84
E
P


ATOM
1472
OP1
CYT E
15
15.666
16.475
4.014
1.00
65.29
E
O


ATOM
1473
OP2
CYT E
15
15.262
14.989
6.062
1.00
49.85
E
O


ATOM
1474
O5′
CYT E
15
13.603
16.748
5.406
1.00
55.19
E
O


ATOM
1475
C5′
CYT E
15
12.708
17.324
4.454
1.00
56.18
E
C


ATOM
1476
O4′
CYT E
15
11.542
18.176
5.128
1.00
61.42
E
C


ATOM
1477
O4′
CYT E
15
10.704
17.348
5.868
1.00
54.03
E
O


ATOM
1478
C3′
CYT E
15
12.169
19.200
6.129
1.00
63.66
E
C


ATOM
1479
O3′
CYT E
15
11.386
20.389
6.042
1.00
69.99
E
O


ATOM
1480
C2′
CYT E
15
11.981
18.488
7.465
1.00
52.85
E
C


ATOM
1481
C1′
CYT E
15
10.653
17.784
7.212
1.00
49.35
E
C


ATOM
1482
N1
CYT E
15
10.426
16.603
8.090
1.00
42.67
E
N


ATOM
1483
C2
CYT E
15
9.266
16.548
8.872
1.00
37.19
E
C


ATOM
1484
O2
CYT E
15
8.458
17.484
8.812
1.00
38.83
E
O


ATOM
1485
N3
CYT E
15
9.062
15.470
9.671
1.00
31.91
E
N


ATOM
1486
C4
CYT E
15
9.963
14.484
9.704
1.00
35.66
E
C


ATOM
1487
N4
CYT E
15
9.715
13.443
10.508
1.00
33.17
E
N


ATOM
1488
C5
CYT E
15
11.156
14.526
8.915
1.00
37.46
E
C


ATOM
1489
C6
CYT E
15
11.346
15.593
8.129
1.00
38.60
E
C


ATOM
1490
P
THY E
16
11.995
21.808
6.469
1.00
78.44
E
P


ATOM
1491
OP1
THY E
16
11.959
22.665
5.264
1.00
50.40
E
O


ATOM
1492
OP2
THY E
16
13.261
21.586
7.212
1.00
63.19
E
O


ATOM
1493
O5′
THY E
16
10.923
22.349
7.524
1.00
70.06
E
O


ATOM
1494
C5′
THY E
16
9.533
22.263
7.241
1.00
65.61
E
C


ATOM
1495
C4′
THY E
16
8.750
22.391
8.533
1.00
64.41
E
C


ATOM
1496
O4′
THY E
16
8.692
21.120
9.230
1.00
56.65
E
O


ATOM
1497
C3′
THY E
16
9.346
23.382
9.527
1.00
64.90
E
C


ATOM
1498
O3′
THY E
16
8.281
24.127
10.092
1.00
70.01
E
O


ATOM
1499
C2′
THY E
16
10.035
22.482
10.552
1.00
55.44
E
C


ATOM
1500
C1′
THY E
16
9.040
21.330
10.583
1.00
49.98
E
C


ATOM
1501
N1
THY E
16
9.550
20.043
11.132
1.00
46.89
E
N


ATOM
1502
C2
THY E
16
8.698
19.308
11.926
1.00
41.72
E
C


ATOM
1503
O2
THY E
16
7.565
19.677
12.194
1.00
36.25
E
O


ATOM
1504
N3
THY E
16
9.225
18.128
12.392
1.00
36.45
E
N


ATOM
1505
C4
THY E
16
10.491
17.628
12.146
1.00
38.15
E
C


ATOM
1506
O4
THY E
16
10.882
16.559
12.606
1.00
36.21
E
O


ATOM
1507
C5
THY E
16
11.327
18.448
11.309
1.00
39.53
E
C


ATOM
1508
C7
THY E
16
12.717
17.982
10.988
1.00
36.66
E
C


ATOM
1509
C6
THY E
16
10.828
19.603
10.843
1.00
43.44
E
C


ATOM
1510
P
THY E
17
8.549
25.581
10.689
1.00
78.30
E
P


ATOM
1511
OP1
THY E
17
7.626
26.522
10.012
1.00
60.38
E
O


ATOM
1512
OP2
THY E
17
10.012
25.813
10.672
1.00
73.87
E
O


ATOM
1513
O5′
THY E
17
8.116
25.415
12.218
1.00
73.56
E
O


ATOM
1514
C5′
THY E
17
6.754
25.202
12.576
1.00
68.05
E
C


ATOM
1515
C4′
THY E
17
6.683
24.775
14.030
l.00
68.97
E
C


ATOM
1516
O4′
THY E
17
7.266
23.452
14.157
1.00
64.24
E
O


ATOM
1517
C3′
THY E
17
7.449
25.680
14.994
1.00
65.70
E
C


ATOM
1518
O3′
THY E
17
6.707
25.874
16.192
1.00
71.08
E
O


ATOM
1519
C2′
THY E
17
8.741
24.910
15.254
1.00
65.84
E
C


ATOM
1520
C1′
THY E
17
8.250
23.470
15.169
1.00
71.79
E
C


ATOM
1521
N1
THY E
17
9.320
22.512
14.802
1.00
62.90
E
N


ATOM
1522
C2
THY E
17
9.211
21.191
15.192
1.00
55.41
E
C


ATOM
1523
O2
THY E
17
8.264
20.754
I5.830
1.00
43.12
E
O


ATOM
1524
N3
THY E
17
10.263
20.397
14.798
1.00
44.40
E
N


ATOM
1525
C4
THY E
17
11.380
20.789
14.081
1.00
46.62
E
C


ATOM
1526
O4
THY E
17
12.273
20.005
13.779
1.00
49.59
E
O


ATOM
1527
C5
THY E
17
11.425
22.183
13.711
1.00
62.54
E
C


ATOM
1528
C7
THY E
17
12.591
22.718
12.930
1.00
69.77
E
C


ATOM
1529
C6
THY E
17
10.407
22.970
14.086
1.00
59.82
E
C


TER


ATOM
1530
O5′
THY F
1
15.151
15.405
19.847
1.00
35.44
F
O


ATOM
1531
C5′
THY F
1
15.320
14.944
21.178
1.00
28.60
F
C


ATOM
1532
C4′
THY F
1
13.978
14.889
21.887
1.00
27.43
F
C


ATOM
1533
O4′
THY F
1
13.339
16.188
21.818
1.00
29.22
F
O


ATOM
1534
C3′
THY F
1
12.977
13.892
21.316
1.00
28.97
F
C


ATOM
1535
O3′
THY F
1
12.248
13.304
22.386
1.00
29.78
F
O


ATOM
1536
C2′
THY F
1
12.095
14.750
20.407
1.00
32.74
F
C


ATOM
1537
C1′
THY F
1
12.142
16.129
21.065
1.00
29.02
F
C


ATOM
1538
N1
THY F
1
12.145
17.296
20.117
1.00
27.55
F
N


ATOM
1539
C2
THY F
1
11.029
18.102
20.029
1.00
26.62
F
C


ATOM
1540
O2
THY F
1
10.018
17.923
20.677
1.00
32.29
F
O


ATOM
1541
N3
THY F
1
11.126
19.142
19.148
1.00
24.47
F
N


ATOM
1542
C4
THY F
1
12.206
19.455
18.356
1.00
27.28
F
C


ATOM
1543
O4
THY F
1
12.186
20.415
17.595
1.00
32.91
F
O


ATOM
1544
C5
THY F
1
13.344
18.577
18.487
1.00
26.29
F
C


ATOM
1545
C7
THY F
1
14.575
18.823
17.668
1.00
33.04
F
C


ATOM
1546
C6
THY F
1
13.265
17.553
19.348
1.00
27.16
F
C


ATOM
1547
P
ADE F
2
11.449
11.931
22.178
1.00
39.94
F
P


ATOM
1548
OP1
ADE F
2
11.319
11.249
23.481
1.00
40.24
F
O


ATOM
1549
OP2
ADE F
2
12.049
11.216
21.034
1.00
31.49
F
O


ATOM
1550
O5′
ADE F
2
10.007
12.422
21.708
1.00
39.09
F
O


ATOM
1551
C5′
ADE F
2
9.242
13.377
22.427
1.00
26.83
F
C


ATOM
1552
C4′
ADE F
2
8.068
13.787
21.551
1.00
33.76
F
C


ATOM
1553
O4′
ADE F
2
8.510
14.720
20.526
1.00
38.96
F
O


ATOM
1554
C3′
ADE F
2
7.419
12.650
20.766
1.00
35.68
F
C


ATOM
1555
O3′
ADE F
2
6.097
13.018
20.473
1.00
42.23
F
O


ATOM
1556
C2′
ADE F
2
8.221
12.663
19.471
1.00
30.26
F
C


ATOM
1557
C1′
ADE F
2
8.209
14.169
19.255
1.00
30.49
F
C


ATOM
1558
N9
ADE F
2
9.163
14.657
18.268
1.00
26.53
F
N


ATOM
1559
C8
ADE F
2
10.195
13.977
17.681
1.00
28.86
F
C


ATOM
1560
N7
ADE F
2
10.879
14.698
16.815
1.00
28.94
F
N


ATOM
1561
C5
ADE F
2
10.251
15.934
16.841
1.00
27.05
F
C


ATOM
1562
C6
ADE F
2
10.482
17.144
16.157
1.00
25.84
F
C


ATOM
1563
N6
ADE F
2
11.464
17.322
15.272
1.00
28.80
F
N


ATOM
1564
N1
ADE F
2
9.662
18.179
16.421
1.00
25.80
F
N


ATOM
1565
C2
ADE F
2
8.678
18.020
17.310
1.00
24.88
F
C


ATOM
1566
N3
ADE F
2
8.363
16.936
18.012
1.00
26.79
F
N


ATOM
1567
C4
ADE F
2
9.192
15.922
17.731
1.00
27.44
F
C


ATOM
1568
P
ADE F
3
4.853
12.162
20.988
1.00
39.47
F
P


ATOM
1569
OP1
ADE F
3
4.873
12.164
22.468
1.00
40.90
F
O


ATOM
1570
OP2
ADE F
3
4.808
10.885
20.235
1.00
38.47
F
O


ATOM
1571
O5′
ADE F
3
3.662
13.097
20.486
1.00
32.45
F
O


ATOM
1572
C5′
ADE F
3
3.672
14.458
20.891
1.00
32.40
F
C


ATOM
1573
C4′
ADE F
3
3.160
15.342
19.773
1.00
28.86
F
C


ATOM
1574
O4′
ADE F
3
4.231
15.629
18.842
1.00
28.94
F
O


ATOM
1575
C3′
ADE F
3
2.036
14.721
18.953
1.00
39.96
F
C


ATOM
1576
O3′
ADE F
3
0.991
15.679
18.813
1.00
36.97
F
O


ATOM
1577
C2′
ADE F
3
2.694
14.359
17.614
1.00
33.14
F
C


ATOM
1578
C1′
ADE F
3
3.792
15.414
17.514
1.00
36.24
F
C


ATOM
1579
N9
ADE F
3
4.967
15.021
16.739
1.00
28.30
F
N


ATOM
1580
C8
ADE F
3
5.621
13.819
16.767
1.00
29.94
F
C


ATOM
1581
N7
ADE F
3
6.663
13.762
15.969
1.00
29.86
F
N


ATOM
1582
C5
ADE F
3
6.697
15.018
15.379
1.00
29.66
F
C


ATOM
1583
C6
ADE F
3
7.562
15.605
14.433
1.00
26.28
F
C


ATOM
1584
N6
APE F
3
8.605
14.972
13.892
1.00
30.60
F
N


ATOM
1585
N1
ADE F
3
7.314
16.879
14.061
1.00
28.86
F
N


ATOM
1586
C2
ADE F
3
6.267
17.520
14.600
1.00
28.38
F
C


ATOM
1587
N3
ADE F
3
5.387
17.076
15.499
1.00
30.45
F
N


ATOM
1588
C4
ADE F
3
5.660
15.807
15.848
1.00
30.12
F
C


ATOM
1589
P
GUA F
4
−0.306
15.279
17.977
1.00
36.44
F
P


ATOM
1590
OP1
GUA F
4
−1.461
15.980
18.572
1.00
30.12
F
O


ATOM
1591
OP2
GUA F
4
−0.313
13.800
17.840
1.00
37.68
F
O


ATOM
1592
O5′
GUA F
4
0.019
15.913
16.539
1.00
38.14
F
O


ATOM
1593
C5′
GUA F
4
0.319
17.304
16.457
1.00
34.43
F
C


ATOM
1594
C4′
GUA F
4
0.845
17.689
15.083
1.00
37.40
F
C


ATOM
1595
O4′
GUA F
4
2.082
16.992
14.785
1.00
40.03
F
O


ATOM
1596
C3′
GUA F
4
−0.082
17.399
13.905
1.00
48.37
F
C


ATOM
1597
O3′
GUA F
4
−0.224
18.621
13.194
1.00
50.22
F
O


ATOM
1598
C2′
GUA F
4
0.650
16.322
13.096
1.00
37.79
F
C


ATOM
1599
C1′
GUA F
4
2.096
16.693
13.404
1.00
35.99
F
C


ATOM
1600
N9
GUA F
4
3.113
15.662
13.184
1.00
32.40
F
N


ATOM
1601
C8
GUA F
4
3.178
14.408
13.743
1.00
30.83
F
C


ATOM
1602
N7
GUA F
4
4.226
13.724
13.367
1.00
30.41
F
N


ATOM
1603
C5
GUA F
4
4.907
14.581
12.507
1.00
30.17
F
C


ATOM
1604
C6
GUA F
4
6.116
14.396
11.787
1.00
27.54
F
C


ATOM
1605
O6
GUA F
4
6.864
13.403
11.757
1.00
25.09
F
O


ATOM
1606
N1
GUA F
4
6.442
15.526
11.041
1.00
28.44
F
N


ATOM
1607
C2
GUA F
4
5.697
16.679
10.991
1.00
31.59
F
C


ATOM
1608
N2
GUA F
4
6.176
17.660
10.212
1.00
36.28
F
N


ATOM
1609
N3
GUA F
4
4.567
16.866
11.657
1.00
30.17
F
N


ATOM
1610
C4
GUA F
4
4.234
15.778
12.391
1.00
31.30
F
C


ATOM
1611
P
CYT F
5
−1.174
18.766
11.913
1.00
55.22
F
P


ATOM
1612
OP1
CYT F
5
−1.967
20.000
12.116
1.00
35.41
F
O


ATOM
1613
OP2
CYT F
5
−1.818
17.463
11.625
1.00
41.84
F
O


ATOM
1614
O5′
CYT F
5
−0.117
19.042
10.750
1.00
45.09
F
O


ATOM
1615
C5′
CYT F
5
0.805
20.099
10.935
1.00
36.95
F
C


ATOM
1616
C4′
CYT F
5
1.679
20.233
9.710
1.00
34.80
F
C


ATOM
1617
O4′
CYT F
5
2.599
19.115
9.620
1.00
30.71
F
O


ATOM
1618
C3′
CYT F
5
0.917
20.269
8.395
1.00
32.81
F
C


ATOM
1619
O3′
CYT F
5
1.552
21.256
7.611
1.00
38.98
F
O


ATOM
1620
C2′
CYT F
5
1.090
18.847
7.850
1.00
30.04
F
C


ATOM
1621
C1′
CYT F
5
2.483
18.494
8.360
1.00
30.96
F
C


ATOM
1622
N1
CYT F
5
2.763
17.057
8.621
1.00
32.68
F
N


ATOM
1623
C2
CYT F
5
3.866
16.455
8.007
1.00
28.42
F
C


ATOM
1624
O2
CYT F
5
4.574
17.122
7.239
1.00
30.64
F
O


ATOM
1625
N3
CYT F
5
4.129
15.152
8.271
1.00
29.28
F
N


ATOM
1626
C4
CYT F
5
3.344
14.461
9.101
1.00
28.82
F
C


ATOM
1627
N4
CYT F
5
3.652
13.176
9.319
1.00
26.68
F
N


ATOM
1628
C5
CYT F
5
2.218
15.058
9.741
1.00
26.50
F
C


ATOM
1629
C6
CYT F
5
1.973
16.347
9.477
1.00
34.18
F
C


ATOM
1630
P
THY F
6
0.911
21.797
6.257
1.00
45.82
F
P


ATOM
1631
OP1
THY F
6
1.340
23.204
6.087
1.00
50.17
F
O


ATOM
1632
OP2
THY F
6
−0.527
21.445
6.242
1.00
48.70
F
O


ATOM
1633
O5′
THY F
6
1.645
20.899
5.156
1.00
45.06
F
O


ATOM
1634
C5′
THY F
6
2.993
21.162
4.785
1.00
41.65
F
C


ATOM
1635
C4′
THY F
6
3.362
20.354
3.556
1.00
37.82
F
C


ATOM
1636
O4′
THY F
6
3.682
18.997
3.962
1.00
40.57
F
O


ATOM
1637
C3′
THY F
6
2.234
20.213
2.540
1.00
38.89
F
C


ATOM
1638
O3′
THY F
6
2.758
19.997
1.240
1.00
45.07
F
O


ATOM
1639
C2′
THY F
6
1.555
18.940
3.018
1.00
39.65
F
C


ATOM
1640
C1′
THY F
6
2.810
18.118
3.277
1.00
40.46
F
C


ATOM
1641
N1
THY F
6
2.575
16.902
4.089
1.00
33.12
F
N


ATOM
1642
C2
THY F
6
3.531
15.917
4.063
1.00
33.34
F
C


ATOM
1643
O2
THY F
6
4.553
16.018
3.409
1.00
36.26
F
O


ATOM
1644
N3
THY F
6
3.244
14.819
4.836
1.00
29.65
F
N


ATOM
1645
C4
THY F
6
2.113
14.623
5.607
1.00
30.16
F
C


ATOM
1646
O4
THY F
6
1.944
13.601
6.265
1.00
28.94
F
O


ATOM
1647
C5
THY F
6
1.146
15.697
5.580
1.00
31.04
F
C


ATOM
1648
C7
THY F
6
−0.125
15.596
6.376
1.00
27.30
F
C


ATOM
1649
C6
THY F
6
1.420
16.773
4.831
1.00
29.41
F
C


ATOM
1650
P
ADE F
7
3.087
21.237
0.286
1.00
43.24
F
P


ATOM
1651
OP1
ADE F
7
3.511
22.361
1.152
1.00
39.52
F
O


ATOM
1652
OP2
ADE F
7
1.946
21.410
−0.641
1.00
43.23
F
O


ATOM
1653
O5′
ADE F
7
4.337
20.696
−0.558
1.00
31.77
F
O


ATOM
1654
C5′
ADE F
7
5.573
20.439
0.091
1.00
31.76
F
C


ATOM
1655
C4′
ADE F
7
6.250
19.186
−0.442
1.00
34.10
F
C


ATOM
1656
O4′
ADE F
7
5.668
17.997
0.158
1.00
36.40
F
O


ATOM
1657
C3′
ADE F
7
6.159
18.965
−1.945
1.00
37.37
F
C


ATOM
1658
O3′
ADE F
7
7.365
18.325
−2.375
1.00
37.11
F
O


ATOM
1659
C2′
ADE F
7
4.922
18.068
−2.076
1.00
34.22
F
C


ATOM
1660
C1′
ADE F
7
5.045
17.190
−0.831
1.00
36.46
F
C


ATOM
1661
N9
ADE F
7
3.796
16.716
−0.234
1.00
29.12
F
N


ATOM
1662
C8
ADE F
7
2.603
17.380
−0.136
1.00
31.32
F
C


ATOM
1663
N7
ADE F
7
1.664
16.695
0.484
1.00
32.25
F
N


ATOM
1664
C5
ADE F
7
2.284
15.502
0.826
1.00
26.57
F
C


ATOM
1665
C6
ADE F
7
1.838
14.346
1.503
1.00
22.11
F
C


ATOM
1666
N6
ADE F
7
0.599
14.190
1.983
1.00
20.31
F
N


ATOM
1667
N1
ADE F
7
2.723
13.340
1.670
1.00
22.14
F
N


ATOM
1668
C2
ADE F
7
3.964
13.483
1.198
1.00
23.50
F
C


ATOM
1669
N3
ADE F
7
4.500
14.518
0.551
1.00
28.66
F
N


ATOM
1670
C4
ADE F
7
3.601
15.505
0.395
1.00
30.88
F
C


ATOM
1671
P
ADE F
8
7.584
17.995
−3.924
1.00
57.47
F
P


ATOM
1672
OP1
ADE F
8
9.025
18.154
−4.225
1.00
44.64
F
O


ATOM
1673
OP2
ADE F
8
6.546
18.735
−4.687
1.00
39.39
F
O


ATOM
1674
O5′
ADE F
8
7.234
16.441
−4.011
1.00
40.95
F
O


ATOM
1675
C5′
ADE F
8
7.986
15.526
−3.241
1.00
40.65
F
C


ATOM
1676
C4′
ADE F
8
7.318
14.166
−3.261
1.00
42.55
F
C


ATOM
1677
O4′
ADE F
8
6.068
14.237
−2.542
1.00
43.82
F
O


ATOM
1678
C3′
ADE F
8
6.962
13.635
−4.648
1.00
37.24
F
C


ATOM
1679
O3′
ADE F
8
7.876
12.598
−4.962
1.00
36.02
F
O


ATOM
1680
C2′
ADE F
8
5.523
13.126
−4.513
1.00
34.48
F
C


ATOM
1681
C1′
ADE F
8
5.279
13.168
−3.007
1.00
36.61
F
C


ATOM
1682
N9
ADE F
8
3.897
13.418
−2.605
1.00
35.16
F
N


ATOM
1683
C8
ADE F
8
3.136
14.523
−2.874
1.00
34.63
F
C


ATOM
1684
N7
ADE F
8
1.924
14.470
−2.372
1.00
33.52
F
N


ATOM
1685
C5
ADE F
8
1.890
13.243
−1.730
1.00
30.78
F
C


ATOM
1686
C6
ADE F
8
0.881
12.586
−1.000
1.00
36.08
F
C


ATOM
1687
N6
ADE F
8
−0.330
13.117
−0.802
1.00
31.29
F
N


ATOM
1686
N1
ADE F
8
1.168
11.366
−0.482
1.00
34.00
F
N


ATOM
1689
C2
ADE F
8
2.390
10.849
−0.691
1.00
37.64
F
C


ATOM
1690
N3
ADE F
8
3.421
11.372
−1.364
1.00
31.88
F
N


ATOM
1691
C4
ADE F
8
3.099
12.581
−1.860
1.00
32.34
F
C


ATOM
1692
P
THY F
9
7.678
11.637
−6.223
1.00
38.24
F
P


ATOM
1693
OP1
THY F
9
9.021
11.281
−6.729
1.00
31.02
F
O


ATOM
1694
OP2
THY F
9
6.669
12.226
−7.135
1.00
36.79
F
O


ATOM
1695
O5′
THY F
9
7.060
10.340
−5.528
1.00
35.06
F
O


ATOM
1696
C5′
THY F
9
7.848
9.687
−4.551
1.00
35.57
F
C


ATOM
1697
C4′
THY F
9
7.066
8.560
−3.913
1.00
34.01
F
C


ATOM
1698
O4′
THY F
9
5.808
9.079
−3.419
1.00
27.93
F
O


ATOM
1699
C3′
THY F
9
6.722
7.390
−4.832
1.00
28.47
F
C


ATOM
1700
O3′
THY F
9
6.955
6.202
−4.082
1.00
28.04
F
O


ATOM
1701
C2′
THY F
9
5.248
7.620
−5.164
1.00
26.35
F
C


ATOM
1702
C1′
THY F
9
4.753
8.259
−3.869
1.00
27.34
F
C


ATOM
1703
N1
THY F
9
3.561
9.140
−3.995
1.00
25.52
F
N


ATOM
1704
C2
THY F
9
2.512
8.921
−3.143
1.00
27.45
F
C


ATOM
1705
O2
THY F
9
2.528
8.038
−2.306
1.00
29.33
F
O


ATOM
1706
N3
THY F
9
1.451
9.776
−3.308
1.00
28.84
F
N


ATOM
1707
C4
THY F
9
1.345
10.805
−4.226
1.00
26.17
F
C


ATOM
1708
O4
THY F
9
0.357
11.526
−4.310
1.00
27.50
F
O


ATOM
1709
C5
THY F
9
2.477
10.978
−5.088
1.00
27.41
F
C


ATOM
1710
C7
THY F
9
2.450
12.071
−6.119
1.00
26.72
F
C


ATOM
1711
C6
THY F
9
3.522
10.151
−4.933
1.00
27.85
F
C


ATOM
1712
P
ADE F
10
6.614
4.738
−4.629
1.00
23.93
F
P


ATOM
1713
OP1
ADE F
10
7.397
3.770
−3.830
1.00
23.75
F
O


ATOM
1714
OP2
ADE F
10
6.742
4.742
−6.104
1.00
31.81
F
O


ATOM
1715
O5′
ADE F
10
5.071
4.571
−4.220
1.00
35.82
F
O


ATOM
1716
C5′
APE F
10
4.732
4.500
−2.835
1.00
25.94
F
C


ATOM
1717
C4′
ADE F
10
3.369
3.873
−2.576
1.00
20.59
F
C


ATOM
1718
O4′
ADE F
10
2.313
4.838
−2.795
1.00
22.02
F
O


ATOM
1719
C3′
ADE F
10
2.998
2.665
−3428
1.00
25.03
F
C


ATOM
1720
O3′
ADE F
10
2.352
1.741
−2.564
1.00
21.68
F
O


ATOM
1721
C2′
ADE F
10
2.059
3.247
−4.486
1.00
20.64
F
C


ATOM
1722
C1′
ADE F
10
1.340
4.328
−3.686
1.00
21.60
F
C


ATOM
1723
N9
ADE F
10
0.878
5.487
−4.447
1.00
24.05
F
N


ATOM
1724
C8
ADE F
10
1.593
6.194
−5.377
1.00
20.24
F
C


ATOM
1725
N7
ADE F
10
0.930
7.207
−5.882
1.00
22.47
F
N


ATOM
1726
C5
ADE F
10
−0.296
7.166
−5.240
1.00
19.26
F
C


ATOM
1727
C6
ADE F
10
−1.445
7.976
−5337
1.00
21.91
F
C


ATOM
1728
N6
ADE F
10
−1.537
9.028
−6.159
1.00
22.42
F
N


ATOM
1729
N1
ADE F
10
−2.502
7.663
−4.556
1.00
20.46
F
N


ATOM
1730
C2
ADE F
10
−2.404
6.608
−3.738
1.00
21.25
F
C


ATOM
1731
N3
ADE F
10
−1.373
5.777
−3.557
1.00
21.22
F
N


ATOM
1732
C4
ADE F
10
−0.343
6.115
−4.348
1.00
18.15
F
C


ATOM
1733
P
ADE F
11
1.831
0.323
−3.073
1.00
26.26
F
P


ATOM
1734
OP1
ADE F
11
2.148
−0.677
−2.034
1.00
33.89
F
O


ATOM
1735
OP2
ADE F
11
2.267
0.111
−4.472
1.00
23.71
F
O


ATOM
1736
O5′
ADE F
11
0.251
0.571
−3.069
1.00
30.04
F
O


ATOM
1737
C5′
ADE F
11
−0.359
1.033
−1.884
1.00
23.86
F
C


ATOM
1738
C4′
ADE F
11
−1.850
1.245
−2.067
1.00
25.98
F
C


ATOM
1739
O4′
ADE F
11
−2.088
2.375
−2.942
1.00
21.87
F
O


ATOM
1740
C3′
ADE F
11
−2.629
0.077
−2.661
1.00
27.40
F
C


ATOM
1741
O3′
ADE F
11
−3.869
0.048
−1.963
1.00
27.22
F
O


ATOM
1742
C2′
ADE F
11
−2.785
0.484
−4.126
1.00
22.69
F
C


ATOM
1743
C1′
ADE F
11
−2.949
1.997
−3.991
1.00
25.23
F
C


ATOM
1744
N9
ADE F
11
−2.484
2.813
−5.103
1.00
25.79
F
N


ATOM
1745
C8
ADE F
11
−1.310
2.670
−5.794
1.00
25.41
F
C


ATOM
1746
N7
ADE F
11
−1.138
3.568
−6.736
1.00
26.27
F
N


ATOM
1747
C5
ADE F
11
−2.274
4.357
−6.639
1.00
24.40
F
C


ATOM
1748
C6
ADE F
11
−2.693
5.484
−7.361
1.00
26.97
F
C


ATOM
1749
N6
ADE F
11
−1.962
6.001
−8.355
1.00
30.79
F
N


ATOM
1750
N1
ADE F
11
−3.880
6.043
−7.028
1.00
26.76
F
N


ATOM
1751
C2
ADE F
11
−4.594
5.498
−6.030
1.00
27.39
F
C


ATOM
1752
N3
ADE F
11
−4.296
4.433
−5.279
1.00
24.26
F
N


ATOM
1753
C4
ADE F
11
−3.113
3.912
−5.638
1.00
22.08
F
C


ATOM
1754
P
THY F
12
−4.857
−1.211
−1.981
1.00
26.75
F
P


ATOM
1755
OP1
THY F
12
−5.433
−1.311
−0.619
1.00
27.03
F
O


ATOM
1756
OP2
THY F
12
−4.163
−2.383
−2.556
1.00
22.77
F
O


ATOM
1757
O5′
THY F
12
−5.993
−0.716
−2.998
1.00
26.06
F
O


ATOM
1758
C5′
THY F
12
−6.803
0.411
−2.603
1.00
24.65
F
C


ATOM
1759
C4′
THY F
12
−7.609
0.986
−3.754
1.00
27.12
F
C


ATOM
1760
O4′
THY F
12
−6.751
1.762
−4.633
1.00
24.99
F
O


ATOM
1761
C3′
THY F
12
−8.307
−0.047
−4.646
1.00
27.27
F
C


ATOM
1762
O3′
THY F
12
−9.654
0.322
−4.869
1.00
26.89
F
O


ATOM
1763
C2′
THY F
12
−7.524
0.037
−5.955
1.00
22.09
F
C


ATOM
1764
C1′
THY F
12
−7.222
1.528
−5.945
1.00
23.77
F
C


ATOM
1765
N1
THY F
12
−6.198
1.950
−6.926
1.00
23.74
F
N


ATOM
1766
C2
THY F
12
−6.346
3.165
−7.564
1.00
24.23
F
C


ATOM
1767
O2
THY F
12
−7.277
3.925
−7.363
1.00
22.95
F
O


ATOM
1768
N3
THY F
12
−5.346
3.463
−8.452
1.00
21.71
F
N


ATOM
1769
C4
THY F
12
−4.250
2.684
−8.753
1.00
21.38
F
C


ATOM
1770
O4
THY F
12
−3.416
3.055
−9.568
1.00
26.86
F
O


ATOM
1771
C5
THY F
12
−4.161
1.425
−8.051
1.00
19.72
F
C


ATOM
1772
C7
THY F
12
−3.013
0.485
−8.294
1.00
20.68
F
C


ATOM
1773
C6
THY F
12
−5.128
1.120
−7.183
1.00
19.97
F
C


ATOM
1774
P
ADE F
13
−10.808
0.035
−3.799
1.00
37.17
F
P


ATOM
1775
OP1
ADE F
13
−10.428
0.709
−2.533
1.00
31.49
F
O


ATOM
1776
OP2
ADE F
13
−11.117
−1.414
−3.821
1.00
25.92
F
O


ATOM
1777
O5′
ADE F
13
−12.042
0.827
−4.445
1.00
33.97
F
O


ATOM
1778
C5′
ADE F
13
−12.010
2.251
−4.451
1.00
31.66
F
C


ATOM
1779
C4′
APE F
13
−12.914
2.837
−5.523
1.00
36.86
F
C


ATOM
1780
O4′
AGE F
13
−12.183
3.096
−6.750
1.00
31.85
F
O


ATOM
1781
C3′
ADE F
13
−14.115
1.994
−5.925
1.00
27.27
F
C


ATOM
1782
O3′
ADE F
13
−15.155
2.910
−6.228
1.00
29.73
F
O


ATOM
1783
C2′
ADE F
13
−13.604
1.237
−7.148
1.00
26.25
F
C


ATOM
1784
CR′
ADE F
13
−12.558
2.173
−7.754
1.00
29.08
F
C


ATOM
1785
N9
ADE F
13
−11.324
1.523
−8.187
1.00
25.69
F
N


ATOM
1786
C8
ADE F
13
−10.877
0.272
−7.861
1.00
22.17
F
C


ATOM
1787
N7
ADE F
13
−9.718
−0.031
−8.405
1.00
23.97
F
N


ATOM
1788
C5
ADE F
13
−9.372
1.106
−9.123
1.00
22.53
F
C


ATOM
1789
C6
ADE F
13
−8.249
1.433
−9.914
1.00
23.42
F
C


ATOM
1790
N6
ADE F
13
−7.222
0.600
−10.129
1.00
20.47
F
N


ATOM
1791
N1
ADE F
13
−8.224
2.655
−10.485
1.00
23.63
F
N


ATOM
1792
C2
ADE F
13
−9.251
3.487
−10.274
1.00
24.20
F
C


ATOM
1793
N3
ADE F
13
−10.355
3.295
−9.551
1.00
24.43
F
N


ATOM
1794
C4
ADE F
13
−10.352
2.074
−8.994
1.00
23.99
F
C


ATOM
1795
P
GUA F
14
−16.572
2.450
−6.800
1.00
30.58
F
P


ATOM
1796
OP1
GUA F
14
−17.581
3.404
−6.283
1.00
29.22
F
O


ATOM
1797
OP2
GUA F
14
−16.732
0.996
−6.558
1.00
28.14
F
O


ATOM
1798
O5′
GUA F
14
−16.417
2.710
−8.369
1.00
21.73
F
O


ATOM
1799
C5′
GUA F
14
−16.239
4.053
−8.799
1.00
28.86
F
C


ATOM
1800
C4′
GUA F
14
−15.866
4.106
−10.267
1.00
35.27
F
C


ATOM
1801
O4′
GUA F
14
−14.568
3.491
−10.468
1.00
32.56
F
O


ATOM
1802
C3′
GUA F
14
−16.849
3.401
−11.197
1.00
41.42
F
C


ATOM
1803
O3′
GUA F
14
−17.292
4.357
−12.165
1.00
50.72
F
O


ATOM
1804
C2′
GUA F
14
−16.046
2.239
−11.786
1.00
35.19
F
C


ATOM
1805
C1′
GUA F
14
−14.601
2.711
−11.636
1.00
28.95
F
C


ATOM
1806
N9
GUA F
14
−13.629
1.628
−11.502
1.00
28.65
F
N


ATOM
1807
C8
GUA F
14
−13.734
0.478
−10.751
1.00
27.50
F
C


ATOM
1808
N7
GUA F
14
−12.690
−0.305
−10.845
1.00
25.21
F
N


ATOM
1809
C5
GUA F
14
−11.835
0.372
−11.706
1.00
22.23
F
C


ATOM
1810
C6
GUA F
14
−10.554
0.025
−12.185
1.00
23.99
F
C


ATOM
1811
O6
GUA F
14
−9.894
−0.990
−11.930
1.00
26.66
F
O


ATOM
1812
N1
GUA F
14
−10.039
0.991
−13.050
1.00
23.15
F
N


ATOM
1813
C2
GUA F
14
−10.683
2.153
−13.402
1.00
27.10
F
C


ATOM
1814
N2
GUA F
14
−10.040
2.977
−14.244
1.00
27.62
F
N


ATOM
1815
N3
GUA F
14
−11.882
2.492
−12.955
1.00
29.89
F
N


ATOM
1816
C4
GUA F
14
−12.397
1.559
−12.118
1.00
28.73
F
C


ATOM
1817
P
CYT F
15
−17.994
3.944
−13.540
1.00
57.53
F
P


ATOM
1818
OP1
CYT F
15
−18.880
5.065
−13.912
1.00
66.77
F
O


ATOM
1819
OP2
CYT F
15
−18.533
2.569
−13.429
1.00
45.10
F
O


ATOM
1820
O5′
CYT F
15
−16.765
3.919
−14.561
1.00
61.13
F
O


ATOM
1821
C5′
CYT F
15
−16.011
5.107
−14.774
1.00
60.71
F
C


ATOM
1822
C4′
CYT F
15
−14.957
4.886
−15.844
1.00
63.70
F
C


ATOM
1823
O4′
CYT F
15
−14.016
3.870
−15.408
1.00
56.35
F
O


ATOM
1824
C3′
CYT F
15
−15.507
4.415
−17.186
1.00
63.78
F
C


ATOM
1825
O3′
CYT F
15
−14.833
5.094
−18.244
1.00
69.14
F
O


ATOM
1826
C2′
CYT F
15
−15.220
2.915
−17.180
1.00
54.75
F
C


ATOM
1827
C1′
CYT F
15
−13.525
2.848
−16.379
1.00
50.07
F
C


ATOM
1828
N1
CYT F
15
−13.730
1.550
−15.671
1.00
42.12
F
N


ATOM
1829
C2
CYT F
15
−12.553
0.820
−15.884
1.00
38.81
F
C


ATOM
1830
O2
CYT F
15
−11.691
1.262
−16.660
1.00
38.49
F
O


ATOM
1831
N3
CYT F
15
−12.390
−0.357
−15.231
1.00
32.50
F
N


ATOM
1832
C4
CYT F
15
−13.338
−0.803
−14.404
1.00
36.68
F
C


ATOM
1833
N4
CYT F
15
−13.119
−1.972
−13.789
1.00
32.28
F
N


ATOM
1834
C5
CYT F
15
−14.546
−0.071
−14.174
1.00
36.00
F
C


ATOM
1835
C6
CYT F
15
−14.696
1.089
−14.822
1.00
37.43
F
C


ATOM
1836
P
THY F
16
−15.377
5.023
−19.751
1.00
80.16
F
P


ATOM
1837
OP1
THY F
16
−15.380
6.409
−20.269
1.00
68.74
F
O


ATOM
1838
OP2
THY F
16
−16.614
4.202
−19.786
1.00
59.17
F
O


ATOM
1839
O5′
THY F
16
−14.242
4.186
−20.504
1.00
74.20
F
O


ATOM
1840
C5′
THY F
16
−12.868
4.527
−20.356
1.00
64.50
F
C


ATOM
1841
C4′
THY F
16
−12.005
3.433
−20.959
1.00
61.48
F
C


ATOM
1842
O4′
THY F
16
−11.933
2.288
−20.071
1.00
56.08
F
O


ATOM
1843
C3′
THY F
16
−12.522
2.903
−22.292
1.00
64.84
F
C


ATOM
1844
O3′
THY F
16
−11.448
2.856
−23.218
1.00
65.11
F
O


ATOM
1845
C2′
THY F
16
−13.065
1.514
−21.959
1.00
58.52
F
C


ATOM
1846
C1′
THY F
16
−12.146
1.106
−20.816
1.00
48.55
F
C


ATOM
1847
N1
THY F
16
−12.712
0.088
−19.887
1.00
44.56
F
N


ATOM
1848
C2
THY F
16
−11.930
−0.987
−19.523
1.00
41.93
F
C


ATOM
1849
O2
THY F
16
−10.789
−1.154
−19.928
1.00
36.72
F
O


ATOM
1850
N3
THY F
16
−12.540
−1.862
−18.658
1.00
37.33
F
N


ATOM
1851
C4
THY F
16
−13.817
−1.771
−18.138
1.00
38.23
F
C


ATOM
1852
O4
THY F
16
−14.279
−2.606
−17.367
1.00
38.67
F
O


ATOM
1853
C5
THY F
16
−14.576
−0.625
−18.564
1.00
39.50
F
C


ATOM
1854
C7
THY F
16
−15.975
−0.438
−18.059
1.00
37.21
F
C


ATOM
1855
C6
THY F
16
−13.998
0.241
−19.406
1.00
43.36
F
C


ATOM
1856
P
THY F
17
−11.767
2.951
−24.778
1.00
81.71
F
P


ATOM
1857
OP1
THY F
17
−10.777
3.861
−25.394
1.00
56.22
F
O


ATOM
1858
OP2
THY F
17
−13.218
3.216
−24.919
1.00
75.03
F
O


ATOM
1859
O5′
THY F
17
−11.493
1.459
−25.283
1.00
76.85
F
O


ATOM
1860
C5′
THY F
17
−10.171
0.932
−25.289
1.00
71.22
F
C


ATOM
1861
C4′
THY F
17
−10.213
−0.575
−25.471
1.00
71.63
F
C


ATOM
1862
O4′
THY F
17
−10.789
−1.183
−24.287
1.00
63.05
F
O


ATOM
1863
C3′
THY F
17
−11.042
−1.060
−26.661
1.00
64.78
F
C


ATOM
1864
O3′
THY F
17
−10.284
−1.985
−27.435
1.00
63.87
F
O


ATOM
1865
C2′
THY F
17
−12.265
−1.721
−26.025
1.00
64.01
F
C


ATOM
1866
C1′
THY F
17
−11.714
−2.172
−24.678
1.00
67.24
F
C


ATOM
1867
N1
THY F
17
−12.743
−2.246
−23.624
1.00
64.24
F
N


ATOM
1868
C2
THY F
17
−12.611
−3.176
−22.614
1.00
58.85
F
C


ATOM
1869
O2
THY F
17
−11.674
−3.955
−22.540
1.00
48.20
F
O


ATOM
1870
N3
THY F
17
−13.627
−3.153
−21.689
1.00
46.71
F
N


ATOM
1871
C4
THY F
17
−14.726
−2.314
−21.681
1.00
48.10
F
C


ATOM
1872
O4
THY F
17
−15.585
−2.370
−20.808
1.00
54.41
F
O


ATOM
1873
C5
THY F
17
−14.795
−1.367
−22.768
1.00
57.18
F
C


ATOM
1874
C7
THY F
17
−15.944
−0.406
−22.864
1.00
61.07
F
C


ATOM
1875
C6
THY F
17
−13.813
−1.379
−23.678
1.00
62.83
F
C


TER


ATOM
1876
N
GLY C
2
26.102
−30.410
−22.106
1.00
37.16
C
N


ATOM
1877
CA
GLY C
2
27.225
−30.891
−22.889
1.00
37.40
C
C


ATOM
1878
C
GLY C
2
27.997
−31.989
−22.183
1.00
41.01
C
C


ATOM
1879
O
GLY C
2
27.938
−32.110
−20.958
1.00
42.86
C
O


ATOM
1880
N
ARG C
3
28.721
−32.793
−22.956
1.00
39.84
C
N


ATOM
1881
CA
ARG C
3
29.520
−33.876
−22.393
1.00
40.18
C
C


ATOM
1882
C
ARG C
3
30.538
−33.327
−21.398
1.00
43.21
C
C


ATOM
1883
O
ARG C
3
30.820
−33.945
−20.369
1.00
45.60
C
O


ATOM
1884
CB
ARG C
3
30.219
−34.661
−23.504
1.00
39.06
C
C


ATOM
1885
CG
ARG C
3
29.272
−35.479
−24.372
1.00
38.76
C
C


ATOM
1866
CD
ARG C
3
28.414
−36.403
−23.522
1.00
43.44
C
C


ATOM
1887
NE
ARG C
3
27.577
−37.286
−24.330
1.00
39.28
C
N


ATOM
1888
CZ
ARG C
3
27.994
−38.428
−24.868
1.00
44.32
C
C


ATOM
1889
NH1
ARG C
3
29.247
−38.828
−24.698
1.00
35.70
C
N


ATOM
1890
NH2
ARG C
3
27.159
−39.167
−25.583
1.00
41.27
C
N


ATOM
1891
N
LYS C
4
31.082
−32.159
−21.716
1.00
38.21
C
N


ATOM
1892
CA
LYS C
4
31.986
−31.455
−20.817
1.00
40.07
C
C


ATOM
1893
C
LYS C
4
31.589
−29.985
−20.733
1.00
44.07
C
C


ATOM
1894
O
LYS C
4
31.123
−29.404
−21.713
1.00
36.32
C
O


ATOM
1895
CB
LYS C
4
33.437
−31.575
−21.299
1.00
41.27
C
C


ATOM
1896
CG
LYS C
4
34.023
−32.977
−21.180
1.00
43.87
C
C


ATOM
1897
CD
LYS C
4
33.886
−33.497
−19.754
1.00
44.62
C
C


ATOM
1898
CE
LYS C
4
33.899
−35.016
−19.705
1.00
58.07
C
C


ATOM
1899
NZ
LYS C
4
33.253
−35.524
−18.459
1.00
51.82
C
N


ATOM
1900
N
LYS C
5
31.768
−29.387
−19.561
1.00
44.47
C
N


ATOM
1901
CA
LYS C
5
31.606
−27.947
−19.433
1.00
41.82
C
C


ATOM
1902
C
LYS C
5
32.702
−27.261
−20.233
1.00
44.25
C
C


ATOM
1903
O
LYS C
5
33.806
−27.791
−20.359
1.00
49.21
C
O


ATOM
1904
CB
LYS C
5
31.682
−27.513
−17.971
1.00
39.15
C
C


ATOM
1905
CG
LYS C
5
31.691
−26.002
−17.792
1.00
46.63
C
C


ATOM
1906
CD
LYS C
5
31.374
−25.594
−16.363
1.00
42.50
C
C


ATOM
1907
CE
LYS C
5
31.225
−24.090
−16.258
1.00
46.51
C
C


ATOM
1908
N2
LYS C
5
30.818
−23.663
−14.892
1.00
51.90
C
N


ATOM
1909
N
ILE C
6
32.398
−26.089
−20.782
1.00
37.05
C
N


ATOM
1910
CA
ILE C
6
33.394
−25.321
−21.521
1.00
35.04
C
C


ATOM
1911
C
ILE C
6
33.581
−23.914
−20.958
1.00
40.67
C
C


ATOM
1912
O
ILE C
6
32.791
−23.446
−20.136
1.00
41.66
C
O


ATOM
1913
CB
ILE C
6
33.041
−25.223
−23.013
1.00
38.26
C
C


ATOM
1914
CG1
ILE C
6
31.877
−24.255
−23.235
1.00
33.65
C
C


ATOM
1915
CG2
ILE C
6
32.721
−26.603
−23.569
1.00
41.12
C
C


ATOM
1916
CD1
ILE C
6
31.712
−23.841
−24.682
1.00
34.76
C
C


ATOM
1917
N
GLN C
7
34.644
−23.249
−21.396
1.00
46.96
C
N


ATOM
1918
CA
GLN C
7
34.892
−21.873
−20.999
1.00
46.22
C
C


ATOM
1919
C
GLN C
7
34.452
−20.956
−22.120
1.00
44.41
C
C


ATOM
1920
O
GLN C
7
34.662
−21.257
−23.296
1.00
43.97
C
O


ATOM
1921
CB
GLN C
7
36.374
−21.649
−20.687
1.00
54.97
C
C


ATOM
1922
CG
GLN C
7
36.843
−22.323
−19.409
1.00
57.18
C
C


ATOM
1923
CD
GLN C
7
35.980
−21.963
−18.213
1.00
73.60
C
C


ATOM
1924
OE1
GLN C
7
35.636
−20.797
−18.008
1.00
77.65
C
O


ATOM
1925
NE2
GLN C
7
35.629
−22.966
−17.413
1.00
72.99
C
N


ATOM
1926
N
ILE C
8
33.830
−19.839
−21.761
1.00
28.39
C
N


ATOM
1927
CA
ILE C
8
33.363
−18.899
−22.767
1.00
21.10
C
C


ATOM
1928
C
ILE C
8
34.548
−18.138
−23.353
1.00
24.35
C
C


ATOM
1929
O
ILE C
8
34.920
−17.062
−22.879
1.00
25.10
C
O


ATOM
1930
CB
ILE C
8
32.292
−17.944
−22.211
1.00
20.86
C
C


ATOM
1931
CG1
ILE C
8
31.062
−18.743
−21.773
1.00
27.03
C
C


ATOM
1932
CG2
ILE C
8
31.895
−16.916
−23.249
1.00
18.08
C
C


ATOM
1933
CD1
ILE C
8
30.547
−19.712
−22.835
1.00
21.56
C
C


ATOM
1934
N
THR C
9
35.149
−18.718
−24.386
1.00
18.31
C
N


ATOM
1935
CA
THR C
9
36.265
−18.074
−25.064
1.00
18.73
C
C


ATOM
1936
C
THR C
9
36.330
−18.510
−26.528
1.00
16.20
C
C


ATOM
1937
O
THR C
9
35.998
−19.652
−26.885
1.00
19.80
C
O


ATOM
1938
CB
THR C
9
37.604
−18.337
−24.335
1.00
22.75
C
C


ATOM
1939
OG1
THR C
9
38.643
−17.538
−24.920
1.00
29.46
C
O


ATOM
1940
CG2
THR C
9
37.976
−19.817
−24.395
1.00
15.15
C
C


ATOM
1941
N
ARG C
10
36.736
−17.577
−27.385
1.00
22.69
C
N


ATOM
1942
CA
ARG C
10
36.805
−17.797
−28.828
1.00
28.13
C
C


ATOM
1943
C
ARG C
10
37.364
−19.165
−29.205
1.00
26.44
C
C


ATOM
1944
O
ARG C
10
38.497
−19.501
−28.866
1.00
27.25
C
O


ATOM
1945
CB
ARG C
10
37.635
−16.698
−29.496
1.00
25.83
C
C


ATOM
1946
CG
ARG C
10
37.636
−16.769
−31.009
1.00
25.49
C
C


ATOM
1947
CD
ARG C
10
38.512
−15.685
−31.619
1.00
26.19
C
C


ATOM
1948
NE
ARG C
10
38.533
−15.776
−33.077
1.00
42.34
C
N


ATOM
1949
CZ
ARG C
10
39.313
−16.606
−33.764
1.00
35.92
C
C


ATOM
1950
NH1
ARG C
10
40.138
−17.421
−33.123
1.00
40.43
C
N


ATOM
1951
NH2
ARG C
10
39.269
−16.620
−35.089
1.00
33.33
C
N


ATOM
1952
N
ILE C
11
36.546
−19.948
−29.898
1.00
13.48
C
N


ATOM
1953
CA
ILE C
11
36.954
−21.246
−30.411
1.00
16.65
C
C


ATOM
1954
C
ILE C
11
37.985
−21.029
−31.516
1.00
20.36
C
C


ATOM
1955
O
ILE C
11
37.745
−20.268
−32.458
1.00
21.24
C
O


ATOM
1956
CB
ILE C
11
35.741
−22.022
−30.952
1.00
21.38
C
C


ATOM
1957
CG1
ILE C
11
34.750
−22.296
−29.816
1.00
14.80
C
C


ATOM
1958
CG2
ILE C
11
36.177
−23.320
−31.635
1.00
14.57
C
C


ATOM
1959
CD1
ILE C
11
33.463
−22.954
−30.264
1.00
16.69
C
C


ATOM
1960
N
MET C
12
39.138
−21.678
−31.382
1.00
22.82
C
N


ATOM
1961
CA
MET C
12
40.267
−21.407
−32.262
1.00
29.62
C
C


ATOM
1962
C
MET C
12
40.202
−22.231
−33.544
1.00
29.22
C
C


ATOM
1963
O
MET C
12
40.707
−21.810
−34.581
1.00
28.51
C
O


ATOM
1964
CB
MET C
12
41.594
−21.653
−31.533
1.00
24.77
C
C


ATOM
1965
CG
MET C
12
41.796
−20.801
−30.272
1.00
29.84
C
C


ATOM
1566
SD
MET C
12
41.935
−19.026
−30.587
1.00
31.60
C
S


ATOM
1967
CE
MET C
12
43.472
−18.972
−31.519
1.00
25.97
C
C


ATOM
1968
N
ASP C
13
39.577
−23.401
−33.461
1.00
47.38
C
N


ATOM
1969
CA
ASP C
13
39.448
−24.301
−34.604
1.00
49.89
C
C


ATOM
1970
C
ASP C
13
38.251
−23.913
−35.472
1.00
45.31
C
C


ATOM
1971
O
ASP C
13
37.102
−24.017
−35.041
1.00
43.32
C
O


ATOM
1972
CB
ASP C
13
39.301
−25.745
−34.114
1.00
49.98
C
C


ATOM
1973
CG
ASP C
13
38.903
−26.707
−35.223
1.00
66.17
C
C


ATOM
1974
OD1
ASP C
13
39.467
−26.610
−36.335
1.00
72.90
C
O


ATOM
1975
OD2
ASP C
13
38.030
−27.571
−34.979
1.00
61.32
C
O


ATOM
1976
N
GLU C
14
38.530
−23.461
−36.690
1.00
27.77
C
N


ATOM
1977
CA
GLU C
14
37.488
−23.055
−37.629
1.00
33.41
C
C


ATOM
1978
C
GLU C
14
36.413
−24.122
−37.807
1.00
38.75
C
C


ATOM
1979
O
GLU C
14
35.233
−23.808
−37.960
1.00
31.01
C
O


ATOM
1980
CB
GLU C
14
38.096
−22.710
−38.991
1.00
30.94
C
C


ATOM
1981
CG
GLU C
14
37.079
−22.438
−40.088
1.00
33.31
C
C


ATOM
1982
CD
GLU C
14
37.732
−22.114
−41.426
1.00
61.19
C
C


ATOM
1983
OE1
GLU C
14
38.831
−22.642
−41.705
1.00
66.85
C
O


ATOM
1984
OE2
GLU C
14
37.144
−21.333
−42.204
1.00
51.72
C
O


ATOM
1985
N
ARG C
15
36.816
−25.386
−37.785
1.00
49.66
C
N


ATOM
1986
CA
ARG C
15
35.856
−26.464
−37.972
1.00
42.37
C
C


ATOM
1987
C
ARG C
15
34.830
−26.496
−36.843
1.00
37.98
C
C


ATOM
1988
O
ARG C
15
33.637
−26.352
−37.088
1.00
34.22
C
O


ATOM
1989
CB
ARG C
15
36.562
−27.814
−38.111
1.00
51.26
C
C


ATOM
1990
CG
ARG C
15
35.704
−28.875
−38.771
1.00
56.80
C
C


ATOM
1991
CD
ARG C
15
36.503
−29.690
−39.775
1.00
67.79
C
C


ATOM
1992
NE
ARG C
15
35.708
−29.979
−40.966
1.00
74.25
C
N


ATOM
1993
CZ
ARG C
15
35.568
−29.141
−41.990
1.00
70.71
C
C


ATOM
1994
NH1
ARG C
15
36.173
−27.959
−41.971
1.00
78.90
C
N


ATOM
1995
NH2
ARG C
15
34.822
−29.481
−43.035
1.00
52.78
C
N


ATOM
1996
N
ASN C
16
35.292
−26.677
−35.608
1.00
39.27
C
N


ATOM
1997
CA
ASN C
16
34.381
−26.706
−34.469
1.00
35.73
C
C


ATOM
1998
C
ASN C
16
33.650
−25.380
−34.274
1.00
31.63
C
C


ATOM
1999
O
ASN C
16
32.565
−25.346
−33.705
1.00
30.78
C
O


ATOM
2000
CB
ASN C
16
35.103
−27.106
−33.173
1.00
41.02
C
C


ATOM
2001
CG
ASN C
16
34.151
−27.172
−31.964
1.00
49.30
C
C


ATOM
2002
OD1
ASN C
16
33.053
−27.730
−32.049
1.00
39.61
C
O


ATOM
2003
ND2
ASN C
16
34.576
−26.601
−30.838
1.00
35.86
C
N


ATOM
2004
N
ARG C
17
34.237
−24.287
−34.745
1.00
19.12
C
N


ATOM
2005
CA
ARG C
17
33.618
−22.985
−34.552
1.00
21.97
C
C


ATOM
2006
C
ARG C
17
32.409
−22.833
−35.466
1.00
23.23
C
C


ATOM
2007
O
ARG C
17
31.385
−22.271
−35.074
1.00
21.76
C
O


ATOM
2008
CB
ARG C
17
34.618
−21.851
−34.783
1.00
18.63
C
C


ATOM
2009
CG
ARG C
17
34.048
−20.470
−34.495
1.00
19.22
C
C


ATOM
2010
CD
ARG C
17
35.129
−19.388
−34.498
1.00
23.09
C
C


ATOM
2011
NE
ARG C
17
35.704
−19.201
−35.826
1.00
26.86
C
N


ATOM
2012
CZ
ARG C
17
36.947
−19.533
−36.164
1.00
30.01
C
C


ATOM
2013
NH1
ARG C
17
37.775
−20.055
−35.261
1.00
22.90
C
N


ATOM
2014
NH2
ARG C
17
37.366
−19.328
−37.409
1.00
30.60
C
N


ATOM
2015
N
GLN C
18
32.531
−23.336
−36.687
1.00
26.75
C
N


ATOM
2016
CA
GLN C
18
31.417
−23.314
−37.621
1.00
28.13
C
C


ATOM
2017
C
GLN C
18
30.264
−24.158
−37.079
1.00
24.45
C
C


ATOM
2018
O
GLN C
18
29.106
−23.745
−37.125
1.00
19.76
C
O


ATOM
2019
CB
GLN C
18
31.855
−23.839
−38.990
1.00
24.27
C
C


ATOM
2020
CG
GLN C
18
30.779
−23.713
−40.054
1.00
25.41
C
C


ATOM
2021
CD
GLN C
18
30.429
−22.266
−40.352
1.00
39.70
C
C


ATOM
2022
OE1
GLN C
18
31.245
−21.517
−40.894
1.00
47.66
C
O


ATOM
2023
NE2
GLN C
18
29.211
−21.867
−40.004
1.00
49.70
C
N


ATOM
2024
N
VAL C
19
30.603
−25.338
−36.566
1.00
29.15
C
N


ATOM
2025
CA
VAL C
10
29.631
−26.274
−36.016
1.00
28.04
C
C


ATOM
2026
C
VAL C
19
28.932
−25.697
−34.789
1.00
31.99
C
C


ATOM
2027
O
VAL C
19
27.708
−25.733
−34.679
1.00
31.77
C
O


ATOM
2028
CB
VAL C
19
30.314
−27.597
−35.621
1.00
30.57
C
C


ATOM
2029
CG1
VAL C
19
29.381
−28.459
−34.788
1.00
28.68
C
C


ATOM
2030
CG2
VAL C
19
30.767
−28.337
−36.856
1.00
28.38
C
C


ATOM
2031
N
THR C
20
29.718
−25.167
−33.863
1.00
23.43
C
N


ATOM
2032
CA
THR C
20
29.167
−24.575
−32.659
1.00
24.62
C
C


ATOM
2033
C
THR C
20
28.283
−23.392
−33.022
1.00
24.14
C
C


ATOM
2034
O
THR C
20
27.247
−23.149
−32.391
1.00
21.70
C
O


ATOM
2035
CB
THR C
20
30.279
−24.114
−31.717
1.00
26.92
C
C


ATOM
2036
OG1
THR C
20
30.934
−25.264
−31.172
1.00
25.57
C
O


ATOM
2037
CG2
THR C
20
29.705
−23.271
−30.584
1.00
22.17
C
C


ATOM
2038
N
PHE C
21
28.693
−22.665
−34.053
1.00
21.78
C
N


ATOM
2039
CA
PHE C
21
27.948
−21.492
−34.491
1.00
24.12
C
C


ATOM
2040
C
PHE C
21
26.587
−21.851
−35.081
1.00
23.04
C
C


ATOM
2041
O
PHE C
21
25.603
−21.162
−34.832
1.00
22.41
C
O


ATOM
2042
CB
PHE C
21
28.757
−20.679
−35.501
1.00
19.76
C
C


ATOM
2043
CG
PHE C
21
27.948
−19.642
−36.219
1.00
21.70
C
C


ATOM
2044
CD1
PHE C
21
27.773
−18.379
−35.672
1.00
16.96
C
C


ATOM
2045
CD2
PHE C
21
27.349
−19.932
−37.438
1.00
21.89
C
C


ATOM
2046
CE1
PHE C
21
27.027
−17.419
−36.328
1.00
19.77
C
C


ATOM
2047
CE2
PHE C
21
26.594
−18.976
−38.100
1.00
22.15
C
C


ATOM
2048
CZ
PHE C
21
26.434
−17.719
−37.549
1.00
26.78
C
C


ATOM
2049
N
THR C
22
26.531
−22.919
−35.869
1.00
17.14
C
N


ATOM
2050
CA
THR C
22
25.265
−23.334
−36.471
1.00
17.72
C
C


ATOM
2051
C
THR C
22
24.301
−23.861
−35.409
1.00
16.28
C
C


ATOM
2052
O
THR C
22
23.096
−23.613
−35.476
1.00
17.19
C
O


ATOM
2053
CB
THR C
22
25.455
−24.402
−37.590
1.00
18.91
C
C


ATOM
2054
OG1
THR C
22
26.031
−23.796
−38.757
1.00
15.99
C
O


ATOM
2055
CG2
THR C
22
24.121
−25.011
−37.968
1.00
12.54
C
C


ATOM
2056
N
LYS C
23
24.831
−24.589
−34.428
1.00
18.67
C
N


ATOM
2057
CA
LYS C
23
23.995
−25.125
−33.359
1.00
19.65
C
C


ATOM
2058
C
LYS C
23
23.422
−24.010
−32.493
1.00
19.04
C
C


ATOM
2059
O
LYS C
23
22.209
−23.923
−32.305
1.00
19.52
C
O


ATOM
2060
CB
LYS C
23
24.775
−26.114
−32.488
1.00
22.98
C
C


ATOM
2061
CG
LYS C
23
25.091
−27.443
−33.169
1.00
29.30
C
C


ATOM
2062
CD
LYS C
23
25.900
−28.341
−32.235
1.00
32.52
C
C


ATOM
2063
CE
LYS C
23
26.088
−29.726
−32.813
1.00
35.94
C
C


ATOM
2064
NZ
LYS C
23
27.012
−30.536
−31.973
1.00
33.98
C
N


ATOM
2065
N
ARG C
24
24.302
−23.153
−31.980
1.00
16.23
C
N


ATOM
2066
CA
ARG C
24
23.895
−22.083
−31.072
1.00
15.69
C
C


ATOM
2067
C
ARG C
24
23.079
−20.973
−31.746
1.00
17.54
C
C


ATOM
2068
O
ARG C
24
22.246
−20.339
−31.088
1.00
16.19
C
O


ATOM
2069
CB
ARG C
24
25.106
−21.494
−30.346
1.00
13.13
C
C


ATOM
2070
CG
ARG C
24
25.567
−22.316
−29.145
1.00
14.55
C
C


ATOM
2071
CD
ARG C
24
26.824
−21.735
−28.509
1.00
13.70
C
C


ATOM
2072
NE
ARG C
24
27.168
−22.430
−27.273
1.00
15.96
C
N


ATOM
2073
CZ
ARG C
24
26.860
−21.988
−26.055
1.00
17.74
C
C


ATOM
2074
NH1
ARG C
24
26.203
−20.842
−25.901
1.00
17.55
C
N


ATOM
2075
NH2
ARG C
24
27.209
−22.690
−24.990
1.00
13.06
C
N


ATOM
2076
N
LYS C
25
23.313
−20.732
−33.040
1.00
20.57
C
N


ATOM
2077
CA
LYS C
25
22.542
−19.711
−33.763
1.00
21.27
C
C


ATOM
2078
C
LYS C
25
21.087
−20.126
−33.788
1.00
21.17
C
C


ATOM
2079
O
LYS C
25
20.188
−19.314
−33.581
1.00
21.37
C
O


ATOM
2080
CB
LYS C
25
23.040
−19.522
−35.196
1.00
27.14
C
C


ATOM
2081
CG
LYS C
25
22.094
−18.694
−36.068
1.00
23.36
C
C


ATOM
2082
CD
LYS C
25
22.799
−18.097
−37.285
1.00
29.03
C
C


ATOM
2083
CE
LYS C
25
23.198
−19.165
−38.317
1.00
25.05
C
C


ATOM
2084
NZ
LYS C
25
22.025
−19.796
−38.986
1.00
22.30
C
N


ATOM
2085
N
PHE C
26
20.870
−21.407
−34.050
1.00
16.86
C
N


ATOM
2086
CA
PHE C
26
19.541
−21.989
−33.996
1.00
19.25
C
C


ATOM
2087
C
PHE C
26
18.942
−21.777
−32.593
1.00
19.01
C
C


ATOM
2088
O
PHE C
26
17.915
−21.115
−32.435
1.00
20.38
C
O


ATOM
2089
CB
PHE C
26
19.629
−23.478
−34.344
1.00
16.09
C
C


ATOM
2090
CG
PHE C
26
18.300
−24.149
−34.472
1.00
20.27
C
C


ATOM
2091
CD1
PHE C
26
17.753
−24.395
−35.723
1.00
22.76
C
C


ATOM
2092
CD2
PHE C
26
17.595
−24.539
−33.343
1.00
18.57
C
C


ATOM
2093
CE1
PHE C
26
16.525
−25.014
−35.846
1.00
23.64
C
C


ATOM
2094
CE2
PHEC
26
16.369
−25.160
−33.458
1.00
21.64
C
C


ATOM
2095
CZ
PHE C
26
15.831
−25.398
−34.714
1.00
28.23
C
C


ATOM
2096
N
GLY C
27
19.606
−22.329
−31.579
1.00
21.08
C
N


ATOM
2097
CA
GLY C
27
19.207
−22.147
−30.196
1.00
19.30
C
C


ATOM
2098
C
GLY C
27
18.916
−20.709
−29.804
1.00
17.49
C
C


ATOM
2099
O
GLY C
27
18.010
−20.459
−29.013
1.00
19.26
C
O


ATOM
2100
N
LEU C
28
19.676
−19.760
−30.346
1.00
18.92
C
N


ATOM
2101
CA
LEU C
28
19.486
−18.351
−29.999
1.00
19.41
C
C


ATOM
2102
C
LEU C
28
18.215
−17.781
−30.627
1.00
18.47
C
C


ATOM
2103
O
LEU C
28
17.478
−17.031
−29.983
1.00
16.61
C
O


ATOM
2104
CB
LEU C
28
20.697
−17.513
−30.410
1.00
22.21
C
C


ATOM
2105
CG
LEU C
28
20.668
−16.026
−30.026
1.00
18.79
C
C


ATOM
2106
CD1
LEU C
28
20.508
−15.853
−28.534
1.00
15.60
C
C


ATOM
2107
CD2
LEU C
28
21.923
−15.305
−30.508
1.00
16.50
C
C


ATOM
2108
N
MET C
29
17.965
−18.147
−31.883
1.00
24.79
C
N


ATOM
2109
CA
MET C
29
16.753
−17.736
−32.583
1.00
21.90
C
C


ATOM
2110
C
MET C
29
15.530
−18.403
−31.971
1.00
20.00
C
C


ATOM
2111
O
MET C
29
14.478
−17.790
−31.847
1.00
18.56
C
O


ATOM
2112
CB
MET C
29
16.838
−18.074
−34.075
1.00
22.28
C
C


ATOM
2113
CG
MET C
29
17.931
−17.326
−34.839
1.00
21.94
C
C


ATOM
2114
SD
MET C
29
17.603
−17.288
−36.625
1.00
24.71
C
S


ATOM
2115
CE
MET C
29
19.065
−16.419
−37.197
1.00
27.04
C
C


ATOM
2116
N
LYS C
30
15.672
−19.664
−31.585
1.00
18.86
C
N


ATOM
2117
CA
LYS C
30
14.565
−20.375
−30.958
1.00
19.52
C
C


ATOM
2118
C
LYS C
30
14.080
−19.611
−29.701
1.00
19.23
C
C


ATOM
2119
O
LYS C
30
12.881
−19.397
−29.537
1.00
21.59
C
O


ATOM
2120
CB
LYS C
30
14.945
−21.821
−30.627
1.00
18.29
C
C


ATOM
2121
CG
LYS C
30
13.752
−22.660
−30.193
1.00
26.72
C
C


ATOM
2122
CD
LYS C
30
14.138
−24.070
−29.781
1.00
26.48
C
C


ATOM
2123
CE
LYS C
30
12.902
−24.862
−29.372
1.00
33.14
C
C


ATOM
2124
NZ
LYS C
30
13.230
−26.088
−28.587
1.00
28.25
C
N


ATOM
2125
N
LYS C
31
15.010
−19.277
−28.823
1.00
18.87
C
N


ATOM
2126
CA
LYS C
31
14.640
−18.561
−27.600
1.00
22.08
C
C


ATOM
2127
C
LYS C
31
14.141
−17.141
−27.870
1.00
17.64
C
C


ATOM
2128
O
LYS C
31
13.226
−16.662
−27.209
1.00
21.08
C
O


ATOM
2129
CB
LYS C
31
15.790
−18.571
−26.590
1.00
18.89
C
C


ATOM
2130
CG
LYS C
31
15.972
−19.926
−25.938
1.00
20.04
C
C


ATOM
2131
CD
LYS C
31
17.018
−19.903
−24.839
1.00
22.25
C
C


ATOM
2132
CE
LYS C
31
17.024
−21.223
−24.079
1.00
21.58
C
C


ATOM
2133
NZ
LYS C
31
15.661
−21.584
−23.593
1.00
21.26
C
N


ATOM
2134
N
ALA C
32
14.725
−16.476
−28.856
1.00
9.09
C
N


ATOM
2135
CA
ALA C
32
14.263
−15.148
−29.228
1.00
9.04
C
C


ATOM
2136
C
ALA C
32
12.793
−15.201
−29.651
1.00
13.34
C
C


ATOM
2137
O
ALA C
32
11.980
−14.402
−29.184
1.00
13.09
C
O


ATOM
2138
CB
ALA C
32
15.130
−14.569
−30.337
1.00
8.32
C
C


ATOM
2139
N
TYR C
33
12.464
−16.154
−30.524
1.00
19.25
C
N


ATOM
2140
CA
TYR C
33
11.089
−16.391
−30.975
1.00
18.96
C
C


ATOM
2141
C
TYR C
33
10.127
−16.715
−29.822
1.00
21.93
C
C


ATOM
2142
O
TYR C
33
9.026
−16.162
−29.745
1.00
22.45
C
O


ATOM
2143
CB
TYR C
33
11.062
−17.513
−32.026
1.00
23.50
C
C


ATOM
2144
CG
TYR C
33
9.731
−18.234
−32.146
1.00
21.82
C
C


ATOM
2145
CD1
TYR C
33
8.658
−17.646
−32.804
1.00
26.15
C
C


ATOM
2146
CD2
TYR C
33
9.551
−19.500
−31.599
1.00
23.49
C
C


ATOM
2147
CE1
TYR C
33
7.439
−18.297
−32.916
1.00
27.75
C
C


ATOM
2148
CE2
TYR C
33
8.331
−20.163
−31.700
1.00
23.15
C
C


ATOM
2149
CZ
TYR C
33
7.281
−19.555
−32.362
1.00
29.01
C
C


ATOM
2150
OH
TYR C
33
6.069
−20.198
−32.475
1.00
28.01
C
O


ATOM
2151
N
GLU C
34
10.546
−17.613
−28.934
1.00
21.34
C
N


ATOM
2152
CA
GLU C
34
9.741
−17.988
−27.772
1.00
20.10
C
C


ATOM
2153
C
GLU C
34
9.478
−16.799
−26.852
1.00
20.64
C
C


ATOM
2154
O
GLU C
34
8.376
−16.653
−26.312
1.00
20.34
C
O


ATOM
2155
CB
GLU C
34
10.410
−19.120
−26.989
1.00
19.30
C
C


ATOM
2156
CG
GLU C
34
10.422
−20.458
−27.724
1.00
18.54
C
C


ATOM
2157
CD
GLU C
34
11.121
−21.552
−26.934
1.00
20.08
C
C


ATOM
2158
OE1
GLU C
34
11.829
−21.227
−25.954
1.00
21.18
C
O


ATOM
2159
OE2
GLU C
34
10.966
−22.738
−27.292
1.00
17.80
C
O


ATOM
2160
N
LEU C
35
10.485
−15.947
−26.673
1.00
18.35
C
N


ATOM
2161
CA
LEU C
35
10.300
−14.753
−25.852
1.00
18.79
C
C


ATOM
2162
C
LEU C
35
9.309
−13.789
−26.505
1.00
19.94
C
C


ATOM
2163
O
LEU C
35
8.488
−13.171
−25.824
1.00
21.37
C
O


ATOM
2164
CB
LEU C
35
11.627
−14.050
−25.582
1.00
15.90
C
C


ATOM
2165
CG
LEU C
35
11.519
−12.771
−24.750
1.00
18.38
C
C


ATOM
2166
CD1
LEU C
35
10.931
−13.071
−23.382
1.00
16.74
C
C


ATOM
2167
CD2
LEU C
35
12.871
−12.089
−24.618
1.00
17.45
C
C


ATOM
2168
N
SER C
36
9.385
−13.661
−27.823
1.00
25.87
C
N


ATOM
2169
CA
SER C
36
8.449
−12.811
−28.548
1.00
31.09
C
C


ATOM
2170
C
SER C
36
6.995
−13.257
−28.326
1.00
28.04
C
C


ATOM
2171
O
SER C
36
6.123
−12.443
−28.038
1.00
29.80
C
O


ATOM
2172
CB
SER C
36
8.778
−12.805
−30.043
1.00
32.46
C
C


ATOM
2173
OG
SER C
36
7.835
−12.024
−30.756
1.00
31.96
C
O


ATOM
2174
N
VAL C
37
6.749
−14.557
−28.450
1.00
20.90
C
N


ATOM
2175
CA
VAL C
37
5.406
−I5.109
−28.320
1.00
20.27
C
C


ATOM
2176
C
VAL C
37
4.903
−15.111
−26.873
1.00
22.08
C
C


ATOM
2177
O
VAL C
37
3.773
−14.706
−26.602
1.00
21.87
C
O


ATOM
2178
CB
VAL C
37
5.332
−16.546
−28.876
1.00
21.06
C
C


ATOM
2179
CG1
VAL C
37
4.025
−17.211
−28.469
1.00
17.91
C
C


ATOM
2180
CG2
VAL C
37
5.488
−16.541
−30.392
1.00
22.26
C
C


ATOM
2181
N
LEU C
38
5.738
−15.579
−25.952
1.00
28.66
C
N


ATOM
2182
CA
LEU C
38
5.337
−15.712
−24.557
1.00
24.96
C
C


ATOM
2183
C
LEU C
38
4.994
−14.367
−23.933
1.00
26.61
C
C


ATOM
2184
O
LEU C
38
4.017
−14.247
−23.189
1.00
28.76
C
O


ATOM
2185
CB
LEU C
38
6.454
−16.364
−23.739
1.00
24.38
C
C


ATOM
2186
CG
LEU C
38
6.792
−17.832
−23.978
1.00
22.80
C
C


ATOM
2187
CD1
LEU C
38
8.138
−16.157
−23.352
1.00
20.95
C
C


ATOM
2188
CD2
LEU C
38
5.703
−18.741
−23.431
1.00
23.41
C
C


ATOM
2189
N
CYS C
39
5.807
−13.359
−24.231
1.00
22.88
C
N


ATOM
2190
CA
CYS C
39
5.695
−12.077
−23.543
1.00
24.78
C
C


ATOM
2191
C
CYS C
39
5.249
−10.941
−24.458
1.00
26.69
C
C


ATOM
2192
O
CYS C
39
5.319
−9.770
−24.089
1.00
30.51
C
O


ATOM
2193
CB
CYS C
39
7.020
−11.733
−22.861
1.00
20.36
C
C


ATOM
2194
SG
CYS C
39
7.564
−13.026
−21.730
1.00
20.08
C
S


ATOM
2195
N
ASP C
40
4.789
−11.294
−25.653
1.00
29.36
C
N


ATOM
2196
CA
ASP C
40
4.248
−10.299
−26.565
1.00
31.01
C
C


ATOM
2197
C
ASP C
40
5.191
−9.102
−26.685
1.00
31.73
C
C


ATOM
2198
O
ASP C
40
4.928
−8.041
−26.125
1.00
30.95
C
O


ATOM
2199
CB
ASP C
40
2.870
−9.845
−26.070
1.00
27.98
C
C


ATOM
2200
CG
ASP C
40
2.188
−8.875
−27.017
1.00
31.87
C
C


ATOM
2201
OD1
ASP C
40
2.552
−8.826
−28.211
1.00
33.57
C
O


ATOM
2202
OD2
ASP C
40
1.274
−8.154
−26.559
1.00
47.98
C
O


ATOM
2203
N
CYS C
41
6.298
−9.276
−27.402
1.00
26.23
C
N


ATOM
2204
CA
CYS C
41
7.198
−8.153
−27.658
1.00
31.67
C
C


ATOM
2205
C
CYS C
41
7.834
−8.179
−29.047
1.00
31.20
C
C


ATOM
2206
O
CYS C
41
7.889
−9.224
−29.700
1.00
29.57
C
O


ATOM
2207
CB
CYS C
41
8.264
−8.029
−26.561
1.00
32.05
C
C


ATOM
2208
SG
CYS C
41
8.786
−9.569
−25.798
1.00
39.94
C
S


ATOM
2209
N
GLU C
42
8.279
−7.010
−29.501
1.00
36.27
C
N


ATOM
2210
CA
GLU C
42
9.014
−6.898
−30.751
1.00
32.55
C
C


ATOM
2211
C
GLU C
42
10.475
−7.202
−30.488
1.00
32.26
C
C


ATOM
2212
O
GLU C
42
11.072
−6.659
−29.560
1.00
35.73
C
O


ATOM
2213
CB
GLU C
42
8.912
−5.487
−31.328
1.00
37.23
C
C


ATOM
2214
CG
GLU C
42
7.590
−5.143
−31.974
1.00
51.44
C
C


ATOM
2215
CD
GLU C
42
7.655
−3.824
−32.718
1.00
50.05
C
C


ATOM
2216
OE1
GLU C
42
6.711
−3.016
−32.585
1.00
70.85
C
O


ATOM
2217
OE2
GLU C
42
8.658
−3.592
−33.426
1.00
41.10
C
O


ATOM
2218
N
ILE C
43
11.058
−8.056
−31.316
1.00
23.83
C
N


ATOM
2219
CA
ILE C
43
12.456
−8.416
−31.144
1.00
20.13
C
C


ATOM
2220
C
ILE C
43
13.185
−8.409
−32.473
1.00
19.57
C
C


ATOM
2221
O
ILE C
43
12.628
−8.793
−33.498
1.00
20.64
C
O


ATOM
2222
CB
ILE C
43
12.597
−9.788
−30.461
1.00
20.12
C
C


ATOM
2223
CG1
ILE C
43
12.116
−9.689
−29.009
1.00
20.57
C
C


ATOM
2224
CG2
ILE C
43
14.038
−10.284
−30.546
1.00
16.02
C
C


ATOM
2225
CD1
ILE C
43
12.008
−11.011
−28.293
1.00
18.94
C
C


ATOM
2226
N
ALA C
44
14.428
−7.949
−32.454
1.00
23.50
C
N


ATOM
2227
CA
ALA C
44
15.268
−7.984
−33.639
1.00
25.31
C
C


ATOM
2228
C
ALA C
44
16.633
−8.531
−33.268
1.00
24.34
C
C


ATOM
2229
O
ALA C
44
17.238
−8.106
−32.286
1.00
27.29
C
O


ATOM
2230
CB
ALA C
44
15.393
−6.593
−34.259
1.00
22.98
C
C


ATOM
2231
N
LEU C
45
17.115
−9.478
−34.059
1.00
20.02
C
N


ATOM
2232
CA
LEU C
45
18.407
−10.093
−33.815
1.00
17.99
C
C


ATOM
2233
C
LEU C
45
19.197
−10.106
−35.112
1.00
21.52
C
C


ATOM
2234
O
LEU C
45
18.795
−10.747
−36.080
1.00
21.38
C
O


ATOM
2235
CB
LEU C
45
18.217
−11.525
−33.304
1.00
20.52
C
C


ATOM
2236
CG
LEU C
45
19.472
−12.387
−33.136
1.00
21.79
C
C


ATOM
2237
CD1
LEU C
45
20.440
−11.730
−32.161
1.00
16.43
C
C


ATOM
2238
CD2
LEU C
45
19.118
−13.805
−32.685
1.00
18.07
C
C


ATOM
2239
N
ILE C
46
20.315
−9.389
−35.133
1.00
23.15
C
N


ATOM
2240
CA
ILE C
46
21.194
−9.369
−36.300
1.00
25.46
C
C


ATOM
2241
C
ILE C
46
22.539
−10.013
−35.976
1.00
25.84
C
C


ATOM
2242
O
ILE C
46
23.200
−9.636
−35.007
1.00
23.37
C
O


ATOM
2243
CB
ILE C
46
21.422
−7.932
−36.808
1.00
28.04
C
C


ATOM
2244
CG1
ILE C
46
20.168
−7.419
−37.522
1.00
26.67
C
C


ATOM
2245
CG2
ILE C
46
22.621
−7.884
−37.733
1.00
24.29
C
C


ATOM
2246
CD1
ILE C
46
20.059
−5.907
−37.569
1.00
26.13
C
C


ATOM
2247
N
ILE C
47
22.937
−10.983
−36.793
1.00
21.24
C
N


ATOM
2248
CA
ILE C
47
24.164
−11.736
−36.563
1.00
21.52
C
C


ATOM
2249
C
ILE C
47
25.027
−11.833
−37.816
1.00
21.63
C
C


ATOM
2250
O
ILE C
47
24.573
−12.316
−38.852
1.00
24.81
C
O


ATOM
2251
CB
ILE C
47
23.857
−13.181
−36.123
1.00
22.08
C
C


ATOM
2252
CG1
ILE C
47
22.955
−13.203
−34.890
1.00
20.26
C
C


ATOM
2253
CG2
ILE C
47
25.152
−13.946
−35.860
1.00
22.81
C
C


ATOM
2254
CD1
ILE C
47
22.536
−14.600
−34.492
1.00
18.30
C
C


ATOM
2255
N
PHE C
48
26.272
−11.384
−37.717
1.00
20.46
C
N


ATOM
2256
CA
PHE C
48
27.259
−11.603
−38.767
1.00
20.03
C
C


ATOM
2257
C
PHE C
48
28.281
−12.567
−38.203
1.00
22.91
C
C


ATOM
2258
O
PHE C
48
28.837
−12.306
−37.143
1.00
26.79
C
O


ATOM
2259
CB
PHE C
48
27.979
−10.300
−39.133
1.00
22.81
C
C


ATOM
2260
CG
PHE C
48
27.063
−9.188
−39.565
1.00
21.27
C
C


ATOM
2251
CD1
PHE C
48
26.574
−8.277
−38.643
1.00
20.26
C
C


ATOM
2252
CD2
PHE C
48
26.711
−9.040
−40.899
1.00
25.06
C
C


ATOM
2253
CE1
PHE C
48
25.737
−7.245
−39.041
1.00
21.07
C
C


ATOM
2264
O2
PHE C
48
25.878
−8.009
−41.301
1.00
25.74
C
C


ATOM
2265
CZ
PHE C
48
25.390
−7.111
−40.367
1.00
22.39
C
C


ATOM
2266
N
ASN C
49
28.541
−13.671
−38.893
1.00
26.25
C
N


ATOM
2267
CA
ASN C
49
29.561
−14.607
−38.428
1.00
25.67
C
C


ATOM
2268
C
ASN C
49
30.963
−14.054
−38.686
1.00
26.63
C
C


ATOM
2269
O
ASN C
49
31.107
−12.932
−39.174
1.00
26.67
C
O


ATOM
2270
CB
ASN C
49
29.384
−15.987
−39.070
1.00
23.30
C
C


ATOM
2271
CG
ASN C
49
29.646
−15.976
−40.566
1.00
29.56
C
C


ATOM
2272
OD1
ASN C
49
30.164
−14.999
−41.118
1.00
29.12
C
O


ATOM
2273
ND2
ASN C
49
29.288
−17.071
−41.234
1.00
26.62
C
N


ATOM
2274
N
SER C
50
31.989
−14.834
−38.359
1.00
28.75
C
N


ATOM
2275
CA
SER C
50
33.368
−14.384
−38.534
1.00
34.68
C
C


ATOM
2276
C
SER C
50
33.729
−14.177
−40.001
1.00
39.26
C
C


ATOM
2277
O
SER C
50
34.583
−13.354
−40.321
1.00
44.25
C
O


ATOM
2278
CB
SER C
50
34.354
−15.354
−37.872
1.00
34.53
C
C


ATOM
2279
OG
SER C
50
34.054
−16.698
−38.196
1.00
39.66
C
O


ATOM
2280
N
SER C
51
33.076
−14.922
−40.889
1.00
4485
C
N


ATOM
2281
CA
SER C
51
33.291
−14.765
−42.326
1.00
45.04
C
C


ATOM
2282
C
SER C
51
32.420
−13.647
−42.888
1.00
48.33
C
C


ATOM
2283
O
SER C
51
32.322
−13.478
−44.103
1.00
41.62
C
O


ATOM
2284
CB
SER C
51
33.005
−16.070
−43.066
1.00
39.28
C
C


ATOM
2285
OG
SER C
51
33.839
−17.113
−42.593
1.00
46.61
C
O


ATOM
2286
N
ASN C
52
31.771
−12.911
−41.991
1.00
49.99
C
N


ATOM
2287
CA
ASN C
52
31.033
−11.700
−42.347
1.00
47.32
C
C


ATOM
2288
C
ASN C
52
29.686
−11.923
−43.042
1.00
47.24
C
C


ATOM
2289
O
ASN C
52
29.085
−10.976
−43.552
1.00
47.87
C
O


ATOM
2290
CB
ASN C
52
31.907
−10.776
−43.197
1.00
48.20
C
C


ATOM
2291
CG
ASN C
52
31.878
−9.343
−42.714
1.00
61.86
C
C


ATOM
2292
OD1
ASN C
52
32.478
−9.010
−41.690
1.00
55.65
C
O


ATOM
2293
ND2
ASN C
52
31.187
−8.482
−43.453
1.00
61.83
C
N


ATOM
2294
N
LYS C
53
29.210
−13.165
−43.066
1.00
29.68
C
N


ATOM
2295
CA
LYS C
53
27.879
−13.440
−43.605
1.00
33.37
C
C


ATOM
2296
C
LYS C
53
26.774
−13.075
−42.608
1.00
31.12
C
C


ATOM
2297
O
LYS C
53
26.885
−13.342
−41.412
1.00
25.99
C
O


ATOM
2298
CB
LYS C
53
27.735
−14.901
−44.037
1.00
30.60
C
C


ATOM
2299
OG
LYS C
53
26.328
−15.237
−44.537
1.00
38.39
C
C


ATOM
2300
CD
LYS C
53
26.237
−15.650
−45.112
1.00
34.12
C
C


ATOM
2301
CE
LYS C
53
24.811
−16.980
−45.534
1.00
37.02
C
C


ATOM
2302
NZ
LYS C
53
24.680
−18.380
−46.033
1.00
36.06
C
N


ATOM
2303
N
LEU C
54
25.704
−12.475
−43.122
1.00
30.45
C
N


ATOM
2304
CA
LEU C
54
24.601
−11.989
−42.301
1.00
25.57
C
C


ATOM
2305
C
UEU C
54
23.541
−13.053
−41.998
1.00
24.16
C
C


ATOM
2306
O
LEU C
54
23.134
−13.807
−42.875
1.00
32.16
C
O


ATOM
2307
CB
LEU C
54
23.945
−10.794
−42.995
1.00
29.61
C
C


ATOM
2308
CG
LEU C
54
22.636
−10.252
−42.418
1.00
32.79
C
C


ATOM
2309
CD1
LEU C
54
22.840
−9.712
−41.006
1.00
23.27
C
C


ATOM
2310
CD2
LEU C
54
22.049
−9.182
−43.336
1.00
28.41
C
C


ATOM
2311
N
PHE C
55
23.103
−13.106
−40.745
1.00
28.59
C
N


ATOM
2312
CA
PHE C
55
21.941
−13.900
−40.355
1.00
28.10
C
C


ATOM
2313
C
PHE C
55
21.915
−13.020
−39.526
1.00
26.52
C
C


ATOM
2314
O
PHE C
55
21.479
−12.122
−38.824
1.00
32.90
C
O


ATOM
2315
CB
PHE C
55
22.358
−15.131
−39.550
1.00
28.39
C
C


ATOM
2316
CG
PHE C
55
23.239
−16.080
−40.307
1.00
23.77
C
C


ATOM
2317
CD1
PHE C
55
24.614
−15.973
−40.234
1.00
26.43
C
C


ATOM
2318
CD2
PHE C
55
22.689
−17.081
−41.085
1.00
27.00
C
C


ATOM
2319
CE1
PHE C
55
25.430
−16.845
−40.927
1.00
31.50
C
C


ATOM
2320
CE2
PHE C
55
23.496
−17.963
−41.783
1.00
30.53
C
C


ATOM
2321
CZ
PHE C
55
24.569
−17.845
−41.705
1.00
34.41
C
C


ATOM
2322
N
GLN C
56
19.718
−13.263
−39.599
1.00
25.53
C
N


ATOM
2323
CA
GLN C
56
18.785
−12.363
−38.948
1.00
26.25
C
C


ATOM
2324
C
GLN C
56
17.465
−13.010
−38.553
1.00
28.25
C
C


ATOM
2325
O
GLN C
56
17.007
−13.966
−39.181
1.00
30.62
C
O


ATOM
2326
CB
GLN C
56
18.523
−11.149
−39.843
1.00
32.99
C
C


ATOM
2327
CG
GLN C
56
17.979
−11.493
−41.221
1.00
29.99
C
C


ATOM
2328
CD
GLN C
56
17.877
−10.276
−42.131
1.00
41.74
C
C


ATOM
2329
OE1
GLN C
56
17.110
−9.348
−41.868
1.00
36.88
C
O


ATOM
2330
NE2
GLN C
56
18.651
−10.279
−43.210
1.00
39.31
C
N


ATOM
2331
N
TYR C
57
16.874
−12.472
−37.491
1.00
20.89
C
N


ATOM
2332
CA
TYR C
57
15.526
−12.814
−37.068
1.00
20.63
C
C


ATOM
2333
C
TYR C
57
14.833
−11.554
−36.575
1.00
22.04
C
C


ATOM
2334
O
TYR C
57
15.459
−10.704
−35.940
1.00
25.74
C
O


ATOM
2335
CB
TYR C
57
15.533
−13.839
−35.929
1.00
25.07
C
C


ATOM
2336
CG
TYR C
57
14.213
−13.867
−35.181
1.00
22.71
C
C


ATOM
2337
CD1
TYR C
57
13.146
−14.623
−35.644
1.00
21.68
C
C


ATOM
2338
CD2
TYR C
57
14.020
−13.099
−34.041
1.00
18.82
C
C


ATOM
2339
CE1
TYR C
57
11.930
−14.635
−34.983
1.00
20.31
C
C


ATOM
2340
CE2
TYR C
57
12.807
−13.102
−33.369
1.00
18.33
C
C


ATOM
2341
CZ
TYR C
57
11.766
−13.872
−33.844
1.00
22.22
C
C


ATOM
2342
OH
TYR C
57
10.560
−13.885
−33.180
1.00
22.44
C
O


ATOM
2343
N
ALA C
58
13.537
−11.441
−36.852
1.00
20.58
C
N


ATOM
2344
CA
ALA C
58
12.730
−10.359
−36.304
1.00
25.73
C
C


ATOM
2345
C
ALA C
58
11.279
−10.807
−36.148
1.00
24.38
C
C


ATOM
2346
O
ALA C
58
10.775
−11.565
−36.971
1.00
25.44
C
O


ATOM
2347
CB
ALA C
58
12.826
−9.129
−37.178
1.00
26.42
C
C


ATOM
2348
N
SER C
59
10.615
−10.340
−35.091
1.00
22.34
C
N


ATOM
2349
CA
SER C
59
9.232
−10.730
−34.829
1.00
26.18
C
C


ATOM
2350
C
SER C
59
8.270
−10.052
−35.799
1.00
28.25
C
C


ATOM
2351
O
SER C
59
7.095
−10.402
−35.857
1.00
29.20
C
O


ATOM
2352
CB
SER C
59
8.833
−10.444
−33.377
1.00
23.68
C
C


ATOM
2353
OG
SER C
59
9.017
−9.078
−33.047
1.00
22.70
C
O


ATOM
2354
N
THR C
60
8.786
−9.076
−36.547
1.00
41.26
C
N


ATOM
2355
CA
THR C
60
8.072
−8.461
−37.666
1.00
41.75
C
C


ATOM
2356
C
THR C
60
9.098
−8.045
−38.707
1.00
44.36
C
C


ATOM
2357
O
THR C
60
10.258
−8.453
−38.633
1.00
44.49
C
O


ATOM
2358
CB
THR C
60
7.283
−7.209
−37.247
1.00
50.98
C
C


ATOM
2359
OG1
THR C
60
8.143
−6.318
−36.524
1.00
55.36
C
O


ATOM
2360
CG2
THR C
60
6.088
−7.582
−36.380
1.00
58.49
C
C


ATOM
2361
N
ASP C
61
8.677
−7.235
−39.674
1.00
33.65
C
N


ATOM
2362
CA
ASP C
61
9.611
−6.694
−40.657
1.00
37.81
C
C


ATOM
2363
C
ASP C
61
10.768
−6.016
−39.933
1.00
38.30
C
C


ATOM
2364
O
ASP C
61
10.559
−5.141
−39.082
1.00
35.38
C
O


ATOM
2365
CB
ASP C
61
8.922
−5.688
−41.585
1.00
39.92
C
C


ATOM
2366
CG
ASP C
61
8.070
−6.356
−42.654
1.00
43.00
C
C


ATOM
2367
OD1
ASP C
61
7.600
−7.491
−42.434
1.00
44.55
C
O


ATOM
2368
OD2
ASP C
61
7.865
−5.735
−43.718
1.00
50.00
C
O


ATOM
2369
N
MET C
62
11.987
−6.429
−40.269
1.00
47.81
C
N


ATOM
2370
CA
MET C
62
13.183
−5.871
−39.65O
1.00
41.37
C
C


ATOM
2371
C
MET C
62
13.177
−4.343
−39.681
1.00
44.59
C
C


ATOM
2372
O
MET C
62
13.376
−3.695
−38.654
1.00
47.74
C
O


ATOM
2373
CB
MET C
62
14.443
−6.406
−40.332
1.00
33.72
C
C


ATOM
2374
CG
MET C
62
15.737
−5.950
−39.669
1.00
43.23
C
C


ATOM
2375
SD
MET C
62
15.850
−6.454
−37.936
1.00
35.55
C
S


ATOM
2376
CE
MET C
62
16.116
−8.214
−38.110
1.00
32.61
C
C


ATOM
2377
N
ASP C
63
12.938
−3.777
−40.861
1.00
57.74
C
N


ATOM
2378
CA
ASP C
63
12.975
−2.328
−41.044
1.00
58.33
C
C


ATOM
2379
C
ASP C
63
12.066
−1.600
−40.057
1.00
52.55
C
C


ATOM
2380
O
ASP C
63
12.293
−0.434
−39.738
1.00
59.74
C
O


ATOM
2381
CB
ASP C
63
12.592
−1.952
−42.480
1.00
63.84
C
C


ATOM
2382
CG
ASP C
63
11.092
−2.020
−42.723
1.00
75.02
C
C


ATOM
2383
OD1
ASP C
63
10.476
−0.956
−42.961
1.00
68.03
C
O


ATOM
2384
OD2
ASP C
63
10.526
−3.134
−42.664
1.00
75.33
C
O


ATOM
2385
N
LYS C
64
11.035
−2.286
−39.578
1.00
39.30
C
N


ATOM
2386
CA
LYS C
64
10.108
−1.681
−38.629
1.00
41.27
C
C


ATOM
2387
C
LYS C
64
10.700
−1.602
−37.220
1.00
43.64
C
C


ATOM
2388
O
LYS C
64
10.672
−0.543
−36.588
1.00
32.45
C
O


ATOM
2389
CB
LYS C
64
8.772
−2.427
−38.623
1.00
39.82
C
C


ATOM
2390
CG
LYS C
64
7.983
−2.266
−39.916
1.00
47.23
C
C


ATOM
2391
CD
LYS C
64
6.671
−3.034
−39.884
1.00
48.40
C
C


ATOM
2392
CE
LYS C
64
5.854
−2.764
−41.138
1.00
49.45
C
C


ATOM
2393
NZ
LYS C
64
4.682
−3.676
−41.241
1.00
56.67
C
N


ATOM
2394
N
VAL C
65
11.242
−2.719
−36.735
1.00
36.46
C
N


ATOM
2395
CA
VAL C
65
11.875
−2.743
−35.421
1.00
33.96
C
C


ATOM
2396
C
VAL C
65
13.000
−1.716
−35.377
1.00
34.08
C
C


ATOM
2397
O
VAL C
65
13.153
−0.983
−34.398
1.00
31.90
C
O


ATOM
2398
CB
VAL C
65
12.461
−4.127
−35.083
1.00
32.40
C
C


ATOM
2399
CG1
VAL C
65
12.862
−4.181
−33.616
1.00
24.46
C
C


ATOM
2400
CG2
VAL C
65
11.463
−5.226
−35.406
1.00
30.21
C
C


ATOM
2401
N
LEU C
66
13.783
−1.669
−36.451
1.00
33.80
C
N


ATOM
2402
CA
LEU C
66
14.885
−0.726
−36.546
1.00
34.69
C
C


ATOM
2403
C
LEU C
66
14.385
0.714
−36.476
1.00
43.32
C
C


ATOM
2404
O
LEU C
66
14.915
1.529
−35.717
1.00
40.55
C
O


ATOM
2405
CB
LEU C
66
15.684
−0.958
−37.829
1.00
37.87
C
C


ATOM
2406
CG
LEU C
66
16.467
−2.272
−37.880
1.00
41.36
C
C


ATOM
2407
CD1
LEU C
66
17.377
−2.307
−39.094
1.00
40.31
C
C


ATOM
2408
CD2
LEU C
66
17.268
−2.463
−36.599
1.00
34.80
C
C


ATOM
2409
N
LEU C
67
13.358
1.023
−37.258
1.00
41.33
C
N


ATOM
2410
CA
LEU C
67
12.827
2.379
−37.292
1.00
42.27
C
C


ATOM
2411
C
LEU C
67
12.264
2.795
−35.938
1.00
41.27
C
C


ATOM
2412
O
LEU C
67
12.381
3.950
−35.542
1.00
42.99
C
O


ATOM
2413
CB
LEU C
67
11.780
2.530
−38.397
1.00
46.70
C
C


ATOM
2414
CG
LEU C
67
12.391
2.585
−39.802
1.00
55.15
C
C


ATOM
2415
CD1
LEU C
67
11.316
2.649
−40.878
1.00
59.19
C
C


ATOM
2416
CD2
LEU C
67
13.357
3.762
−39.926
1.00
49.10
C
C


ATOM
2417
N
LYS C
68
11.664
1.844
−35.230
1.00
31.65
C
N


ATOM
2418
CA
LYS C
68
11.140
2.100
−33.900
1.00
33.17
C
C


ATOM
2419
C
LYS C
68
12.294
2.425
−32.959
1.00
36.81
C
C


ATOM
2420
O
LYS C
68
12.152
3.226
−32.032
1.00
36.59
C
O


ATOM
2421
CB
LYS C
68
10.362
0.882
−33.394
1.00
35.82
C
C


ATOM
2422
CG
LYS C
68
9.523
1.146
−32.148
1.00
38.59
C
C


ATOM
2423
CD
LYS C
68
8.716
−0.082
−31.741
1.00
36.40
C
C


ATOM
2424
CE
LYS C
68
7.671
0.265
−30.686
1.00
34.03
C
C


ATOM
2425
NZ
LYS C
68
6.999
−0.939
−30.118
1.00
38.36
C
N


ATOM
2426
N
TYR C
69
13.442
1.804
−33.212
1.00
40.52
C
N


ATOM
2427
CA
TYR C
69
14.630
2.003
−32.387
1.00
42.48
C
C


ATOM
2428
C
TYR C
69
15.267
3.372
−32.615
1.00
43.40
C
C


ATOM
2429
O
TYR C
69
15.696
4.030
−31.666
1.00
39.36
C
O


ATOM
2430
CB
TYR C
69
15.657
0.900
−32.658
1.00
34.93
C
C


ATOM
2431
CG
TYR C
69
16.992
1.127
−31.984
1.00
29.50
C
C


ATOM
2432
CD1
TYR C
69
17.206
0.731
−30.671
1.00
30.62
C
C


ATOM
2433
CD2
TYR C
69
18.037
1.736
−32.662
1.00
31.05
C
C


ATOM
2434
CE1
TYR C
69
18.423
0.936
−30.055
1.00
26.77
C
C


ATOM
2435
CE2
TYR C
69
19.258
1.945
−32.053
1.00
28.66
C
C


ATOM
2436
CZ
TYR C
69
19.446
1.543
−30.752
1.00
29.65
C
C


ATOM
2437
OH
TYR C
69
20.664
1.754
−30.143
1.00
31.04
C
O


ATOM
2438
N
THR C
70
15.336
3.791
−33.876
1.00
34.09
C
N


ATOM
2439
CA
THR C
70
15.916
5.086
−34.214
1.00
40.99
C
C


ATOM
2440
C
THR C
70
15.029
6.237
−33.744
1.00
42.40
C
C


ATOM
2441
O
THR C
70
15.524
7.234
−33.212
1.00
46.32
C
O


ATOM
2442
CB
THR C
70
16.226
5.215
−35.726
1.00
38.56
C
C


ATOM
2443
OG1
THR C
70
15.097
4.777
−36.493
1.00
53.43
C
O


ATOM
2444
CG2
THR C
70
17.437
4.362
−36.097
1.00
38.86
C
C


ATOM
2445
N
GLU C
71
13.719
6.091
−33.924
1.00
65.54
C
N


ATOM
2446
CA
GLU C
71
12.772
7.104
−33.465
1.00
76.80
C
C


ATOM
2447
C
GLU C
71
12.743
7.167
−31.940
1.00
70.78
C
C


ATOM
2448
O
GLU C
71
12.413
8.200
−31.358
1.00
75.57
C
O


ATOM
2449
CB
GLU C
71
11.359
6.816
−33.992
1.00
72.64
C
C


ATOM
2450
CG
GLU C
71
11.274
6.464
−35.473
1.00
80.52
C
C


ATOM
2451
CD
GLU C
71
11.482
7.652
−36.391
1.00
84.86
C
C


ATOM
2452
OE1
GLU C
71
11.645
8.782
−35.883
1.00
91.87
C
O


ATOM
2453
OE2
GLU C
71
11.478
7.453
−37.625
1.00
77.75
C
O


ATOM
2454
N
TYR C
72
13.090
6.054
−31.301
1.00
47.88
C
N


ATOM
2455
CA
TYR C
72
12.996
5.936
−29.849
1.00
46.60
C
C


ATOM
2456
C
TYR C
72
13.701
7.082
−29.129
1.00
43.98
C
C


ATOM
2457
O
TYR C
72
13.248
7.533
−28.074
1.00
41.36
C
O


ATOM
2458
CB
TYR C
72
13.559
4.591
−29.384
1.00
42.97
C
C


ATOM
2459
CG
TYR C
72
13.130
4.183
−27.989
1.00
39.81
C
C


ATOM
2460
CD1
TYR C
72
11.898
3.577
−27.769
1.00
34.15
C
C


ATOM
2461
CD2
TYR C
72
13.960
4.398
−26.892
1.00
42.58
C
C


ATOM
2462
CE1
TYR C
72
11.500
3.195
−26.496
1.00
33.00
C
C


ATOM
2463
CE2
TYR C
72
13.574
4.019
−25.614
1.00
37.42
C
C


ATOM
2464
CZ
TYR C
72
12.342
3.417
−25.423
1.00
41.04
C
C


ATOM
2465
OH
TYR C
72
11.949
3.037
−24.156
1.00
37.34
C
O


TER


ATOM
2466
N
GLY D
2
11.562
−26.613
−16.682
1.00
44.76
D
N


ATOM
2467
CA
GLY D
2
10.788
−26.142
−15.547
1.00
50.33
D
C


ATOM
2468
C
GLY D
2
10.001
−27.255
−14.883
1.00
52.81
D
C


ATOM
2469
O
GLY D
2
10.106
−28.416
−15.283
1.00
48.43
D
O


ATOM
2470
N
ARG D
3
9.213
−26.906
−13.868
1.00
33.83
D
N


ATOM
2471
CA
ARG D
3
8.433
−27.898
−13.132
1.00
35.82
D
C


ATOM
2472
C
ARG D
3
7.466
−28.629
−14.056
1.00
38.35
D
C


ATOM
2473
O
ARG D
3
7.232
−29.830
−13.909
1.00
42.90
D
O


ATOM
2474
CB
ARG D
3
7.679
−27.246
−11.973
1.00
36.26
D
C


ATOM
2475
CG
ARG D
3
8.573
−26.827
−10.813
1.00
38.60
D
C


ATOM
2476
CD
ARG D
3
9.475
−27.974
−10.376
1.00
41.15
D
C


ATOM
2477
NE
ARG D
3
10.365
−27.594
−9.283
1.00
37.71
D
N


ATOM
2478
CZ
ARG D
3
10.010
−27.581
−8.002
1.00
43.27
D
C


ATOM
2479
NH1
ARG D
3
8.777
−27.919
−7.647
1.00
32.47
D
N


ATOM
2480
NH2
ARG D
3
10.890
−27.223
−7.076
1.00
42.72
D
N


ATOM
2481
N
LYS D
4
6.907
−27.891
−15.007
1.00
31.39
D
N


ATOM
2482
CA
LYS D
4
6.073
−28.468
−16.048
1.00
31.49
D
C


ATOM
2483
C
LYS D
4
6.503
−27.912
−17.394
1.00
35.40
D
C


ATOM
2484
O
LYS D
4
6.887
−26.745
−17.500
1.00
30.53
D
O


ATOM
2485
CB
LYS D
4
4.598
−28.134
−15.815
1.00
34.27
D
C


ATOM
2486
CG
LYS D
4
3.970
−28.821
−14.615
1.00
38.44
D
C


ATOM
2487
CD
LYS D
4
2.695
−28.101
−14.200
1.00
34.29
D
C


ATOM
2488
CE
LYS D
4
2.224
−28.546
−12.829
1.00
46.09
D
C


ATOM
2489
NZ
LYS D
4
1.259
−27.570
−12.237
1.00
50.05
D
N


ATOM
2490
N
LYS D
5
6.449
−28.751
−18.421
1.00
40.77
D
N


ATOM
2491
CA
LYS D
5
6.620
−28.270
−19.779
1.00
38.60
D
C


ATOM
2492
C
LYS D
5
5.462
−27.339
−20.087
1.00
40.52
D
C


ATOM
2493
O
LYS D
5
4.311
−27.649
−19.774
1.00
41.68
D
O


ATOM
2494
CB
LYS D
5
6.630
−29.431
−20.776
1.00
36.17
D
C


ATOM
2495
CG
LYS D
5
6.437
−28.994
−22.224
1.00
41.05
D
C


ATOM
2496
CD
LYS D
5
6.857
−30.075
−23.210
1.00
37.55
D
C


ATOM
2497
CE
LYS D
5
6.782
−29.563
−24.640
1.00
46.97
D
C


ATOM
2498
NZ
LYS D
5
7.086
−30.620
−25.646
1.00
53.39
D
N


ATOM
2499
N
ILE D
6
5.765
−26.189
−20.678
1.00
41.72
D
N


ATOM
2500
CA
ILE D
6
4.721
−25.288
−21.141
1.00
41.31
D
C


ATOM
2501
C
ILE D
6
4.618
−25.333
−22.655
1.00
47.16
D
C


ATOM
2502
O
ILE D
6
5.421
−25.980
−23.331
1.00
45.51
D
O


ATOM
2503
CB
ILE D
6
4.988
−23.837
−20.726
1.00
45.87
D
C


ATOM
2504
CG1
ILE D
6
6.267
−23.317
−21.388
1.00
43.98
D
C


ATOM
2505
CG2
ILE D
6
5.053
−23.716
−19.210
1.00
49.90
D
C


ATOM
2506
CD1
ILE D
6
6.495
−21.833
−21.180
1.00
41.94
D
C


ATOM
2507
N
GLN D
7
3.617
−24.645
−23.184
1.00
39.50
D
N


ATOM
2508
CA
GLN D
7
3.496
−24.480
−24.619
1.00
40.81
D
C


ATOM
2509
C
GLN D
7
3.747
−23.028
−24.966
1.00
37.12
D
C


ATOM
2510
O
GLN D
7
3.531
−22.138
−24.145
1.00
37.06
D
O


ATOM
2511
CB
GLN D
7
2.122
−24.930
−25.117
1.00
50.71
D
C


ATOM
2512
CG
GLN D
7
2.064
−26.395
−25.528
1.00
48.43
D
C


ATOM
2513
CD
GLN D
7
2.945
−26.703
−26.734
1.00
65.84
D
C


ATOM
2514
OE1
GLN D
7
3.680
−25.840
−27.223
1.00
69.18
D
O


ATOM
2515
NE2
GLN D
7
2.870
−27.940
−27.220
1.00
68.00
D
N


ATOM
2516
N
ILE D
8
4.214
−22.794
−26.185
1.00
28.04
D
N


ATOM
2517
CA
ILE D
8
4.606
−21.461
−26.605
1.00
23.21
D
C


ATOM
2518
C
ILE D
8
3.411
−20.664
−27.112
1.00
26.07
D
C


ATOM
2519
O
ILE D
8
3.090
−20.678
−28.299
1.00
25.34
D
O


ATOM
2520
CB
ILE D
8
5.734
−21.519
−27.662
1.00
19.94
D
C


ATOM
2521
CG1
ILE D
8
6.967
−22.203
−27.066
1.00
20.05
D
C


ATOM
2522
CG2
ILE D
8
6.100
−20.128
−28.149
1.00
17.49
D
C


ATOM
2523
CD1
ILE D
8
7.431
−21.586
−25.758
1.00
19.55
D
C


ATOM
2524
N
THR D
9
2.746
−19.978
−26.190
1.00
29.37
D
N


ATOM
2525
CA
THR D
9
1.671
−19.059
−26.540
1.00
29.79
D
C


ATOM
2526
C
THR D
9
1.665
−17.890
−25.555
1.00
26.00
D
C


ATOM
2527
O
THR D
9
2.156
−18.019
−24.433
1.00
29.33
D
O


ATOM
2528
CB
THR D
9
0.297
−19.768
−26.584
1.00
36.05
D
C


ATOM
2529
OG1
THR D
9
−0.702
−18.862
−27.077
1.00
37.90
D
O


ATOM
2530
CG2
THR D
9
−0.098
−20.291
−25.203
1.00
27.70
D
C


ATOM
2531
N
ARG D
10
1.130
−16.751
−25.991
1.00
23.06
D
N


ATOM
2532
CA
ARG D
10
1.156
−15.516
−25.206
1.00
27.80
D
C


ATOM
2533
C
ARG D
10
0.578
−15.685
−23.805
1.00
27.06
D
C


ATOM
2534
O
ARG D
10
−0.579
−16.057
−23.644
1.00
29.74
D
O


ATOM
2535
CB
ARG D
10
0.411
−14.401
−25.943
1.00
26.90
D
C


ATOM
2536
CG
ARG D
10
0.455
−13.045
−25.259
1.00
27.50
D
C


ATOM
2537
CD
ARG D
10
−0.540
−12.091
−25.907
1.00
30.44
D
C


ATOM
2538
NE
ARG D
10
−0.591
−10.785
−25.255
1.00
44.07
D
N


ATOM
2539
CZ
ARG D
10
−1.163
−10.559
−24.076
1.00
41.22
D
C


ATOM
2540
NH1
ARG D
10
−1.722
−11.559
−23.409
1.00
42.54
D
N


ATOM
2541
NH2
ARG 0
10
−1.170
−9.337
−23.559
1.00
34.81
D
N


ATOM
2542
N
ILE D
11
1.400
−15.412
−22.799
1.00
19.71
D
N


ATOM
2543
CA
ILE D
11
0.982
−15.491
−21.405
1.00
20.19
D
C


ATOM
2544
C
ILE D
11
−0.007
−14.372
−21.096
1.00
26.44
D
C


ATOM
2545
O
ILE D
11
0.301
−13.192
−21.265
1.00
24.69
D
O


ATOM
2546
CB
ILE D
11
2.192
−15.388
−20.463
1.00
21.36
D
C


ATOM
2547
CG1
ILE D
11
3.143
−16.564
−20.704
1.00
16.61
D
C


ATOM
2548
CG2
ILE D
11
1.740
−15.337
−19.013
1.00
19.56
D
C


ATOM
2549
CD1
ILE D
11
4.479
−16.424
−20.027
1.00
18.65
D
C


ATOM
2550
N
MET D
12
−1.198
−14.753
−20.651
1.00
27.99
D
N


ATOM
2551
CA
MET D
12
−2.297
−13.806
−20.503
1.00
30.35
D
C


ATOM
2552
C
MET D
12
−2.204
−12.994
−19.216
1.00
36.56
D
C


ATOM
2553
O
MET D
12
−2.780
−−11.910
−19.122
1.00
31.16
D
O


ATOM
2554
CB
MET D
12
−3.644
−14.535
−20.576
1.00
30.86
D
C


ATOM
2555
CG
MET D
12
−3.858
−15.321
−21.870
1.00
35.87
D
C


ATOM
2556
SD
MET D
12
−3.790
−14.291
−23.356
1.00
41.14
D
S


ATOM
2557
CE
MET D
12
−5.282
−13.311
−23.140
1.00
28.21
D
C


ATOM
2558
N
ASP D
13
−1.483
−13.521
−18.231
1.00
43.22
D
N


ATOM
2559
CA
ASP D
13
−1.325
−12.844
−16.948
1.00
44.34
D
C


ATOM
2560
C
ASP D
13
−0.190
−11.830
−17.006
1.00
46.62
D
C


ATOM
2561
O
ASP D
13
0.960
−12.195
−17.240
1.00
41.87
D
O


ATOM
2562
CB
ASP D
13
−1.051
−13.860
−15.836
1.00
44.62
D
C


ATOM
2563
CG
ASP D
13
−0.742
−13.200
−14.501
1.00
64.34
D
C


ATOM
2564
OD1
ASP D
13
−1.403
−12.192
−14.165
1.00
63.68
D
O


ATOM
2565
OD2
ASP D
13
0.156
−13.692
−13.783
1.00
61.32
D
O


ATOM
2566
N
GLU D
14
−0.517
−10.560
−16.793
1.00
25.49
D
N


ATOM
2567
CA
GLU D
14
0.485
−9.499
−16.775
1.00
27.06
D
C


ATOM
2568
C
GLU D
14
1.566
−9.766
−15.735
1.00
32.28
D
C


ATOM
2569
O
GLU D
14
2.706
−9.342
−15.893
1.00
28.83
D
O


ATOM
2570
CB
GLU D
14
−0.163
−8.142
−16.485
1.00
25.86
D
C


ATOM
2571
CG
GLU D
14
0.825
−6.995
−16.330
1.00
32.28
D
C


ATOM
2572
CD
GLU D
14
0.144
−5.671
−16.005
1.00
57.66
D
C


ATOM
2573
OE1
GLU D
14
−0.716
−5.641
−15.094
1.00
62.11
D
O


ATOM
2574
OE2
GLU D
14
0.475
−4.657
−16.659
1.00
50.25
D
O


ATOM
2575
N
ARG D
15
1.208
−10.467
−14.667
1.00
43.07
D
N


ATOM
2576
CA
ARG D
15
2.156
−10.710
−13.590
1.00
36.63
D
C


ATOM
2577
C
ARG D
15
3.201
−11.745
−13.987
1.00
31.76
D
C


ATOM
2578
O
ARG D
15
4.397
−11.465
−13.948
1.00
27.80
D
O


ATOM
2579
CB
ARG D
15
1.435
−11.130
−12.309
1.00
44.69
D
C


ATOM
2580
CG
ARG D
15
2.312
−11.052
−11.080
1.00
50.57
D
C


ATOM
2581
CD
ARG D
15
1.567
−10.443
−9.904
1.00
58.18
D
C


ATOM
2582
NE
ARG D
15
2.426
−9.509
−9.180
1.00
64.06
D
N


ATOM
2583
CZ
ARG D
15
2.457
−8.198
−9.402
1.00
66.22
D
C


ATOM
2584
NH1
ARG D
15
1.665
−7.659
−10.322
1.00
71.07
D
N


ATOM
2585
NH2
ARG D
15
3.277
−7.422
−8.702
1.00
44.62
D
N


ATOM
2586
N
ASN D
16
2.748
−12.937
−14.372
1.00
36.62
D
N


ATOM
2587
CA
ASN D
16
3.664
−13.988
−14.798
1.00
31.52
D
C


ATOM
2588
C
ASN D
16
4.335
−13.633
−16.120
1.00
28.43
D
C


ATOM
2589
O
ASN D
16
5.345
−14.225
−16.487
1.00
29.39
D
O


ATOM
2590
CB
ASN D
16
2.957
−15.347
−14.911
1.00
36.44
D
C


ATOM
2591
CG
ASN D
16
3.906
−16.472
−15.369
1.00
46.78
D
C


ATOM
2592
OD1
ASN D
16
5.005
−16.634
−14.831
1.00
29.58
D
O


ATOM
2593
ND2
ASN D
16
3.474
−17.251
−16.364
1.00
33.15
D
N


ATOM
2594
N
ARG D
17
3.777
−12.666
−16.838
1.00
20.99
D
N


ATOM
2595
CA
ARG D
17
4.361
−12.290
−18.114
1.00
24.96
D
C


ATOM
2596
C
ARG D
17
5.567
−11.391
−17.900
1.00
26.75
D
C


ATOM
2597
O
ARG D
17
6.542
−11.461
−18.648
1.00
27.52
D
O


ATOM
2598
CB
ARG D
17
3.344
−11.615
−19.034
1.00
23.69
D
C


ATOM
2599
CG
ARG D
17
3.897
−11.348
−20.427
1.00
23.50
D
C


ATOM
2600
CD
ARG D
17
2.832
−10.841
−21.394
1.00
25.68
D
C


ATOM
2601
NE
ARG D
17
2.242
−9.593
−20.931
1.00
32.21
D
N


ATOM
2602
CZ
ARG D
17
0.991
−9.472
−20.502
1.00
33.52
D
C


ATOM
2603
NH1
ARG D
17
0.179
−10.526
−20.491
1.00
26.29
D
N


ATOM
2604
NH2
ARG D
17
0.552
−8.290
−20.091
1.00
33.61
D
N


ATOM
2605
N
GLN D
18
5.501
−10.545
−16.878
1.00
32.30
D
N


ATOM
2606
CA
GLN D
18
6.627
−9.685
−16.549
1.00
33.39
D
C


ATOM
2607
C
GLN D
18
7.768
−10.507
−15.957
1.00
28.83
D
C


ATOM
2608
O
GLN D
18
8.935
−10.301
−16.298
1.00
26.19
D
O


ATOM
2609
CB
GLN D
18
6.205
−8.574
−15.583
1.00
32.25
D
C


ATOM
2610
CG
GLN D
18
7.356
−7.676
−15.135
1.00
32.58
D
C


ATOM
2611
CD
GLN D
18
8.132
−7.084
−16.303
1.00
36.60
D
C


ATOM
2612
OE1
GLN D
18
7.694
−7.142
−17.453
1.00
41.80
D
O


ATOM
2613
NE2
GLN D
18
9.291
−6.504
−16.008
1.00
46.29
D
N


ATOM
2614
N
VAL D
19
7.415
−11.444
−15.078
1.00
21.98
D
N


ATOM
2615
CA
VAL D
19
8.385
−12.348
−14.470
1.00
25.53
D
C


ATOM
2616
C
VAL D
19
9.081
−13.228
−15.514
1.00
26.27
D
C


ATOM
2617
O
VAL D
19
10.310
−13.331
−15.540
1.00
27.24
D
O


ATOM
2618
CB
VAL D
19
7.719
−13.250
−13.421
1.00
24.87
D
C


ATOM
2619
CG1
VAL D
19
8.645
−14.396
−13.040
1.00
25.36
D
C


ATOM
2620
CG2
VAL D
19
7.335
−12.436
−12.203
1.00
28.33
D
C


ATOM
2621
N
THR D
20
8.293
−13.860
−16.376
1.00
28.30
D
N


ATOM
2622
CA
THR D
20
8.858
−14.702
−17.421
1.00
25.46
D
C


ATOM
2623
C
THR D
20
9.730
−13.875
−18.356
1.00
27.14
D
C


ATOM
2624
O
THR D
20
10.819
−14.298
−18.740
1.00
23.40
D
O


ATOM
2625
CB
THR D
20
7.770
−15.430
−18.210
1.00
27.19
D
C


ATOM
2626
OG1
THR D
20
7.211
−16.461
−17.388
1.00
29.35
D
O


ATOM
2627
CG2
THR D
20
8.353
−16.058
−19.471
1.00
24.16
D
C


ATOM
2628
N
PHE D
21
9.260
−12.684
−18.703
1.00
21.66
D
N


ATOM
2629
CA
PHE D
21
10.046
−11.782
−19.539
1.00
21.40
D
C


ATOM
2630
C
PHE D
21
11.423
−11.454
−18.939
1.00
18.44
D
C


ATOM
2631
O
PHE D
21
12.421
−11.444
−19.654
1.00
19.17
D
O


ATOM
2632
CB
PHE D
21
9.274
−10.492
−19.831
1.00
18.91
D
C


ATOM
2633
CG
PHE D
21
10.107
−9.427
−20.486
1.00
19.09
D
C


ATOM
2634
CD1
PHE D
21
10.249
−9.389
−21.862
1.00
16.77
D
C


ATOM
2635
CD2
PHE D
21
10.753
−8.466
−19.724
1.00
19.35
D
C


ATOM
2636
CE1
PHE D
21
11.016
−8.413
−22.474
1.00
19.96
D
C


ATOM
2637
CE2
PHE D
21
11.525
−7.482
−20.327
1.00
21.51
D
C


ATOM
2638
CZ
PHE D
21
11.657
−7.454
−21.703
1.00
27.86
D
C


ATOM
2639
N
THR D
22
11.474
−11.182
−17.638
1.00
21.93
D
N


ATOM
2640
CA
THR D
22
12.739
−10.847
−16.984
1.00
20.58
D
C


ATOM
2641
C
THR D
22
13.703
−12.041
−16.949
1.00
19.47
D
C


ATOM
2642
O
THR D
22
14.895
−11.893
−17.229
1.00
20.26
D
O


ATOM
2643
CB
THR D
22
12.537
−10.271
−15.544
1.00
24.22
D
C


ATOM
2644
O61
THR D
22
11.881
−8.995
−15.610
1.00
23.73
D
O


ATOM
2645
CG2
THR D
22
13.871
−10.089
−14.852
1.00
15.77
D
C


ATOM
2646
N
LYS D
23
13.194
−13.220
−16.607
1.00
17.92
D
N


ATOM
2647
CA
LYS D
23
14.027
−14.418
−16.621
1.00
19.68
D
C


ATOM
2648
C
LYS D
23
14.579
−14.696
−18.021
1.00
18.83
D
C


ATOM
2649
O
LYS D
23
15.793
−14.760
−18.214
1.00
18.51
D
O


ATOM
2650
CB
LYS D
23
13.256
−15.639
−16.108
1.00
21.03
D
C


ATOM
2651
CG
LYS D
23
12.993
−15.645
−14.606
1.00
27.11
D
C


ATOM
2652
CD
LYS D
23
12.078
−16.812
−14.227
1.00
29.06
D
C


ATOM
2653
CE
LYS D
23
11.843
−16.871
−12.728
1.00
28.46
D
C


ATOM
2654
NZ
LYS D
23
10.620
−17.648
−12.375
1.00
33.25
D
N


ATOM
2655
N
ARG D
24
13.685
−14.848
−18.994
1.00
17.07
D
N


ATOM
2656
CA
ARG D
24
14.081
−15.213
−20.359
1.00
17.05
D
C


ATOM
2657
C
ARG D
24
14.898
−14.148
−21.099
1.00
19.13
D
C


ATOM
2658
O
ARG D
24
15.738
−14.494
−21.936
1.00
16.57
D
O


ATOM
2659
CB
ARG D
24
12.868
−15.641
−21.190
1.00
14.08
D
C


ATOM
2660
CG
ARG D
24
12.442
−17.094
−20.962
1.00
15.74
D
C


ATOM
2661
CD
ARG D
24
11.183
−17.438
−21.750
1.00
15.25
D
C


ATOM
2662
NE
ARG D
24
10.793
−18.841
−21.593
1.00
16.71
D
N


ATOM
2663
CZ
ARG D
24
11.206
−19.831
−22.384
1.00
19.10
D
C


ATOM
2664
NH1
ARG D
24
12.030
−19.590
−23.399
1.00
16.99
D
N


ATOM
2665
NH2
ARG D
24
10.799
−21.069
−22.159
1.00
17.86
D
N


ATOM
2666
N
LYS D
25
14.673
−12.867
−20.794
1.00
22.27
D
N


ATOM
2667
CA
LYS D
25
15.468
−11.798
−21.413
1.00
2231
D
C


ATOM
2668
C
LYS D
25
16.932
−11.926
−21.021
1.00
21.68
D
C


ATOM
2669
O
LYS D
25
17.822
−11.822
−21.854
1.00
22.43
D
O


ATOM
2670
CB
LYS D
25
14.962
−10.409
−21.021
1.00
26.53
D
C


ATOM
2671
CG
LYS D
25
15.930
−9.285
−21.404
1.00
22.70
D
C


ATOM
2672
CD
LYS D
25
15.244
−7.918
−21.425
1.00
26.14
D
C


ATOM
2673
CE
LYS D
25
14.832
−7.453
−20.022
1.00
29.54
D
C


ATOM
2674
NZ
LYS D
25
15.996
−7.018
−19.195
1.00
23.97
D
N


ATOM
2675
N
PHE D
26
17.164
−12.143
−19.735
1.00
18.14
D
N


ATOM
2676
CA
PHE D
26
18.496
−12.396
−19.217
1.00
18.95
D
C


ATOM
2677
C
PHE D
26
19.113
−13.614
−19.920
1.00
20.89
D
C


ATOM
2678
O
PHE D
26
20.260
−13.576
−20.362
1.00
22.41
D
O


ATOM
2679
CB
PHE D
26
18.418
−12.620
−17.704
1.00
19.28
D
C


ATOM
2680
CG
PHE D
26
19.745
−12.842
−17.052
1.00
23.11
D
C


ATOM
2681
CD1
PHE D
26
20.424
−11.786
−16.458
1.00
27.39
D
C


ATOM
2682
CD2
PHE D
26
20.310
−14.106
−17.015
1.00
20.31
D
C


ATOM
2683
CE1
PHE D
26
21.653
−11.985
−15.845
1.00
27.22
D
C


ATOM
2684
CE2
PHE D
26
21.540
−14.313
−16.404
1.00
27.35
D
C


ATOM
2685
CZ
PHE D
26
22.211
−13.250
−15.818
1.00
25.37
D
C


ATOM
2686
N
GLY D
27
18.338
−14.688
−20.029
1.00
26.49
D
N


ATOM
2687
CA
GLY D
27
18.785
−15.895
−20.699
1.00
25.22
D
C


ATOM
2688
C
GLY D
27
19.100
−15.689
−22.168
1.00
24.07
D
C


ATOM
2689
O
GLY D
27
20.000
−16.328
−22.710
1.00
22.92
D
O


ATOM
2690
N
LEU D
28
18.358
−14.800
−22.820
1.00
19.89
D
N


ATOM
2891
CA
LEU D
28
18.568
−14.540
−24.243
1.00
20.40
D
C


ATOM
2692
C
LEU D
28
19.843
−13.731
−24.480
1.00
20.08
D
C


ATOM
2693
O
LEU D
28
20.624
−14.034
−25.380
1.00
17.81
D
O


ATOM
2694
CB
LEU D
28
17.362
−13.822
−24.851
1.00
19.92
D
C


ATOM
2695
CG
LEU D
28
17.417
−13.605
−26.370
1.00
19.33
D
C


ATOM
2696
CD1
LEU D
28
17.456
−14.923
−27.104
1.00
17.21
D
C


ATOM
2697
CD2
LEU D
28
16.237
−12.763
−26.841
1.00
18.71
D
C


ATOM
2698
N
MET D
29
20.054
−12.707
−23.659
1.00
23.68
D
N


ATOM
2699
CA
MET D
29
21.264
−11.897
−23.748
1.00
23.30
D
C


ATOM
2700
C
MET D
29
22.492
−12.725
−23.396
1.00
21.30
D
C


ATOM
2701
O
MET D
29
23.542
−12.574
−24.001
1.00
21.35
D
O


ATOM
2702
CB
MET D
29
21.173
−10.677
−22.828
1.00
24.49
D
C


ATOM
2703
CG
MET D
29
20.074
−9.685
−23.197
1.00
24.02
D
C


ATOM
2704
SD
MET D
29
20.345
−8.057
−22.447
1.00
28.67
D
S


ATOM
2705
CE
MET D
29
18.943
−7.151
−23.109
1.00
29.13
D
C


ATOM
2706
N
LYS D
30
22.358
−13.603
−22.411
1.00
20.43
D
N


ATOM
2707
CA
LYS D
30
23.473
−14.454
−22.016
1.00
22.74
D
C


ATOM
2708
C
LYS D
30
23.931
−15.339
−23.180
1.00
21.49
D
C


ATOM
2709
O
LYS D
30
25.126
−15.417
−23.474
1.00
22.26
D
O


ATOM
2710
CB
LYS D
30
23.117
−15.300
−20.791
1.00
22.13
D
C


ATOM
2711
CG
LYS D
30
24.277
−16.134
−20.270
1.00
30.47
D
C


ATOM
2712
CD
LYS D
30
23.915
−16.879
−18.989
1.00
29.56
D
C


ATOM
2713
CE
LYS D
30
25.042
−17.812
−18.567
1.00
31.49
D
C


ATOM
2714
NZ
LYS D
30
24.611
−18.830
−17568
1.00
32.20
D
N


ATOM
2715
N
LYS D
31
22.983
−15.992
−23.850
1.00
17.89
D
N


ATOM
2716
CA
LYS D
31
23.327
−16.821
−25.010
1.00
19.32
D
C


ATOM
2717
C
LYS D
31
23.835
−16.001
−26.200
1.00
16.48
D
C


ATOM
2718
O
LYS D
31
24.718
−16.442
−26.927
1.00
18.91
D
O


ATOM
2719
CB
LYS D
31
22.169
−17.749
−25.403
1.00
16.34
D
C


ATOM
2720
CG
LYS D
31
22.072
−18.956
−24.485
1.00
15.46
D
C


ATOM
2721
CD
LYS D
31
20.927
−19.876
−24.834
1.00
21.61
D
C


ATOM
2722
CE
LYS D
31
20.909
−21.083
−23.899
1.00
21.65
D
C


ATOM
2723
NZ
LYS D
31
22.219
−21.804
−23.873
1.00
22.50
D
N


ATOM
2724
N
ALA D
32
23.294
−14.801
−26.380
1.00
12.86
D
N


ATOM
2725
CA
ALA D
32
23.778
−13.905
−27.423
1.00
13.63
D
C


ATOM
2726
C
ALA D
32
25.246
−13.545
−27.177
1.00
17.24
D
C


ATOM
2727
O
ALA D
32
26.068
−13.598
−28.097
1.00
15.16
0
O


ATOM
2728
CB
ALA D
32
22.917
−12.649
−27.494
1.00
13.33
D
C


ATOM
2729
N
TYR D
33
25.567
−13.189
−25.931
1.00
20.78
D
N


ATOM
2730
CA
TYR D
33
26.941
−12.884
−25.524
1.00
19.80
D
C


ATOM
2731
C
TYR D
33
27.907
−14.059
−25.734
1.00
21.73
D
C


ATOM
2732
O
TYR D
33
29.020
−13.875
−26.231
1.00
23.12
D
O


ATOM
2733
CB
TYR D
33
26.982
−12.430
−24.053
1.00
25.20
D
C


ATOM
2734
CG
TYR D
33
28.347
−12.555
−23.402
1.00
23.34
D
C


ATOM
2735
CD1
TYR D
33
29.333
−11.604
−23.627
1.00
25.67
D
C


ATOM
2736
CD2
TYR D
33
28.649
−13.629
−22.571
1.00
23.73
D
C


ATOM
2737
CE1
TYR D
33
30.585
−11.713
−23.044
1.00
27.58
D
C


ATOM
2738
CE2
TYR D
33
29.900
−13.751
−21.983
1.00
23.48
D
C


ATOM
2739
CZ
TYR D
33
30.864
−12.788
−22.223
1.00
27.91
D
C


ATOM
2740
OH
TYR D
33
32.112
−12.893
−21.643
1.00
31.14
D
O


ATOM
2741
N
GLU D
34
27.485
−15.259
−25.344
1.00
16.30
D
N


ATOM
2742
CA
GLU D
34
28.327
−16.447
−25.480
1.00
18.09
D
C


ATOM
2743
C
GLU D
34
28.590
−16.796
−26.940
1.00
19.40
D
C


ATOM
2744
O
GLU D
34
29.687
−17.243
−27.289
1.00
16.16
D
O


ATOM
2745
CB
GLU D
34
27.713
−17.647
−24.749
1.00
16.91
D
C


ATOM
2746
CG
GLU D
34
27.580
−17.446
−23.240
1.00
18.31
D
C


ATOM
2747
CO
GLU D
34
27.022
−18.665
−22.526
1.00
24.07
D
C


ATOM
2748
OE1
GLU D
34
26.407
−19.524
−23.200
1.00
21.36
D
O


ATOM
2749
OE2
GLU D
34
27.194
−18.763
−21.291
1.00
19.79
D
O


ATOM
2750
N
LEU D
35
27.594
−16.583
−27.796
1.00
20.14
D
N


ATOM
2751
CA
LEU D
35
27.767
−16.883
−29.216
1.00
19.52
D
C


ATOM
2752
C
LEU D
35
28.752
−15.907
−29.858
1.00
19.84
D
C


ATOM
2753
O
LEU D
35
29.528
−16.279
−30.740
1.00
21.48
D
O


ATOM
2754
CB
LEU D
35
26.432
−16.881
−29.965
1.00
16.57
D
C


ATOM
2755
CG
LEU D
35
26.558
−17.224
−31.453
1.00
17.82
D
C


ATOM
2756
CD1
LEU D
35
26.909
−18.687
−31.634
1.00
18.16
D
C


ATOM
2757
CD2
LEU D
35
25.292
−16.887
−32.217
1.00
17.25
D
C


ATOM
2758
N
SER D
36
28.724
−14.660
−29.409
1.00
21.09
D
N


ATOM
2759
CA
SER D
36
29.663
−13.664
−29.913
1.00
30.15
D
C


ATOM
2760
C
SER D
36
31.111
−14.016
−29.541
1.00
25.03
D
C


ATOM
2761
O
SER D
36
32.021
−13.892
−30.356
1.00
27.24
D
O


ATOM
2762
CB
SER D
36
29.302
−12.273
−29.389
1.00
26.99
D
C


ATOM
2763
OG
SER D
36
30.134
−11.289
−29.975
1.00
30.97
D
O


ATOM
2764
N
VAL D
37
31.312
−14.466
−28.308
1.00
20.84
D
N


ATOM
2765
CA
VAL D
37
32.641
−14.814
−27.827
1.00
21.81
D
C


ATOM
2766
C
VAL D
37
33.133
−16.126
−28.435
1.00
22.28
D
C


ATOM
2767
O
VAL D
37
34.225
−16.187
−29.000
1.00
22.33
D
O


ATOM
2768
CB
VAL D
37
32.672
−14.916
−26.286
1.00
21.65
D
C


ATOM
2769
CG1
VAL D
37
33.953
−15.589
−25.815
1.00
17.21
D
C


ATOM
2770
CG2
VAL D
37
32.524
−13.535
−25.661
1.00
22.60
D
C


ATOM
2771
N
LEU D
38
32.324
−17.174
−28.313
1.00
26.55
D
N


ATOM
2772
CA
LEU D
38
32.696
−18.493
−28.808
1.00
26.12
D
C


ATOM
2773
C
LEU D
38
33.008
−18.494
−30.302
1.00
26.33
D
C


ATOM
2774
O
LEU D
38
33.987
−19.104
−30.733
1.00
26.16
D
O


ATOM
2775
CB
LEU D
38
31.584
−19.508
−28.529
1.00
24.58
D
C


ATOM
2776
CG
LEU D
38
31.256
−19.849
−27.078
1.00
23.98
D
C


ATOM
2777
CD1
LEU D
38
29.929
−20.597
−27.006
1.00
20.12
D
C


ATOM
2778
CD2
LEU D
38
32.379
−20.656
−26.435
1.00
21.85
D
C


ATOM
2779
N
CYS D
39
32.173
−17.822
−31.090
1.00
17.78
D
N


ATOM
2780
CA
CYS D
39
32.296
−17.907
−32.544
1.00
22.24
D
C


ATOM
2781
C
CYS D
39
32.771
−16.616
−33.215
1.00
21.51
D
C


ATOM
2782
O
CYS D
39
32.801
−16.523
−34.442
1.00
24.66
D
O


ATOM
2783
CB
CYS D
39
30.979
−18.382
−33.166
1.00
16.09
D
C


ATOM
2784
SG
CYS D
39
30.384
−19.924
−32.459
1.00
19.92
D
S


ATOM
2785
N
ASP D
40
33.142
−15.623
−32.418
1.00
28.98
D
N


ATOM
2786
CA
ASP D
40
33.704
−14.402
−32.978
1.00
34.97
D
C


ATOM
2787
C
ASP D
40
32.764
−13.804
−34.019
1.00
34.35
D
C


ATOM
2788
O
ASP D
40
33.042
−13.863
−35.217
1.00
31.75
D
O


ATOM
2789
CB
ASP D
40
35.063
−14.706
−33.620
1.00
30.63
D
C


ATOM
2790
CG
ASP D
40
35.796
−13.455
−34.078
1.00
38.54
D
C


ATOM
2791
OD1
ASP D
40
35.416
−12.338
−33.662
1.00
41.19
D
O


ATOM
2792
OD2
ASP D
40
36.764
−13.595
−34.859
1.00
49.72
D
O


ATOM
2793
N
CYS D
41
31.652
−13.233
−33.567
1.00
30.83
D
N


ATOM
2794
CA
CYS D
41
30.724
−12.582
−34.485
1.00
35.32
D
C


ATOM
2795
C
CYS D
41
30.102
−11.300
−33.926
1.00
33.52
D
C


ATOM
2796
O
CYS D
41
29.998
−11.126
−32.715
1.00
33.59
D
O


ATOM
2797
CB
CYS D
41
29.642
−13.562
−34.953
1.00
32.70
D
C


ATOM
2798
SG
CYS D
41
29.124
−14.785
−33.747
1.00
41.68
D
S


ATOM
2799
N
GLU D
42
29.723
−10.394
−34.824
1.00
38.03
D
N


ATOM
2800
CA
GLU D
42
29.026
−9.173
−34.443
1.00
39.78
D
C


ATOM
2801
C
GLU D
42
27.562
−9.498
−34.243
1.00
37.32
D
C


ATOM
2802
O
GLU D
42
26.922
−10.070
−35.125
1.00
38.07
D
O


ATOM
2803
CB
GLU D
42
29.129
−8.117
−35.540
1.00
41.70
D
C


ATOM
2804
CG
GLU D
42
30.421
−7.341
−35.586
1.00
51.65
D
C


ATOM
2805
CD
GLU D
42
30.296
−6.100
−36.446
1.00
52.72
D
C


ATOM
2806
OE1
GLU D
42
31.182
−5.870
−37.294
1.00
69.52
D
O


ATOM
2807
OE2
GLU D
42
29.301
−5.362
−36.279
1.00
42.59
D
O


ATOM
2808
N
ILE D
43
27.021
−9.121
−33.094
1.00
23.73
D
N


ATOM
2809
CA
ILE D
43
25.625
−9.403
−32.817
1.00
23.65
D
C


ATOM
2810
C
ILE D
43
24.911
−8.176
−32.283
1.00
22.94
D
C


ATOM
2811
O
ILE D
43
25.486
−7.383
−31.541
1.00
24.65
D
O


ATOM
2812
CB
ILE D
43
25.473
−10.568
−31.821
1.00
24.33
D
C


ATOM
2813
CG1
ILE D
43
26.097
−11.841
−32.402
1.00
21.59
D
C


ATOM
2814
CG2
ILE D
43
24.006
−10.775
−31.462
1.00
17.28
D
C


ATOM
2815
CD1
ILE D
43
25.800
−13.090
−31.606
1.00
15.31
D
C


ATOM
2816
N
ALA D
44
23.657
−8.015
−32.686
1.00
19.28
D
N


ATOM
2617
CA
ALA D
44
22.804
−6.973
−32.132
1.00
19.51
D
C


ATOM
2818
C
ALA D
44
21.447
−7.568
−31.789
1.00
17.23
D
C


ATOM
2819
O
ALA D
44
20.908
−8.386
−32.530
1.00
19.16
D
O


ATOM
2820
CB
ALA D
44
22.657
−5.807
−33.109
1.00
17.11
D
C


ATOM
2821
N
LEU D
45
20.906
−7.150
−30.654
1.00
21.67
D
N


ATOM
2822
CA
LEU D
45
19.642
−7.659
−30.167
1.00
18.49
D
C


ATOM
2823
C
LEU D
45
18.854
−6.492
−29.594
1.00
22.56
D
C


ATOM
2824
O
LEU D
45
19.270
−5.884
−28.614
1.00
25.66
D
O


ATOM
2825
CB
LEU D
45
19.902
−8.704
−29.080
1.00
20.89
D
C


ATOM
2626
CG
LEU D
45
18.716
−9.287
−28.309
1.00
21.08
D
C


ATOM
2827
CD1
LEU D
45
17.745
−9.969
−29.262
1.00
18.48
D
C


ATOM
2828
CD2
LEU D
45
13.201
−10.255
−27.229
1.00
15.51
D
C


ATOM
2629
N
ILE D
46
17.724
−6.174
−30.215
1.00
30.84
D
N


ATOM
2830
CA
ILE D
46
16.851
−5.107
−29.735
1.00
30.74
D
C


ATOM
2831
C
ILE D
46
15.512
−5.683
−29.296
1.00
30.19
D
C


ATOM
2832
O
ILE D
46
14.876
−6.425
−30.045
1.00
30.65
D
O


ATOM
2833
CB
ILE D
46
16.599
−4.058
−30.832
1.00
32.03
D
C


ATOM
2834
CG1
ILE D
46
17.889
−3.301
−31.152
1.00
30.14
D
C


ATOM
2835
CG2
ILE D
46
15.507
−3.098
−30.408
1.00
31.39
D
C


ATOM
2836
CD1
ILE D
46
17.883
−2.633
−32.510
1.00
33.03
D
C


ATOM
2837
N
ILE D
47
15.084
−5.340
−28.087
1.00
26.87
D
N


ATOM
2838
CA
ILE D
47
13.849
−5.882
−27.528
1.00
24.21
D
C


ATOM
2839
C
ILE D
47
12.550
−4.803
−26.930
1.00
27.15
D
C


ATOM
2840
O
ILE D
47
13.366
−4.063
−26.036
1.00
28.75
D
O


ATOM
2841
CB
ILE D
47
14.146
−6.894
−26.406
1.00
27.99
D
C


ATOM
2842
CG1
ILE D
47
15.148
−7.952
−26.873
1.00
27.63
D
C


ATOM
2843
CG2
ILE D
47
12.851
−7.531
−25.900
1.00
30.34
D
C


ATOM
2844
CD1
ILE D
47
15.679
−8.797
−25.742
1.00
24.42
D
C


ATOM
2845
N
PHE D
48
11.716
−4.726
−27.413
1.00
25.17
D
N


ATOM
2846
CA
PHE D
48
10.718
−3.837
−26.829
1.00
26.76
D
C


ATOM
2847
C
PHE D
48
9.667
−4.690
−26.139
1.00
31.80
D
C


ATOM
2848
O
PHE D
48
8.925
−5.404
−26.806
1.00
30.22
D
O


ATOM
2849
CB
PHE D
48
10.033
−2.993
−27.908
1.00
26.58
D
C


ATOM
2850
CG
PHE D
48
10.962
−2.079
−28.659
1.00
27.99
D
C


ATOM
2851
CD1
PHE D
48
11.469
−2.448
−29.895
1.00
25.86
D
C


ATOM
2852
CD2
PHE D
48
11.315
−0.845
−28.136
1.00
29.84
D
C


ATOM
2853
CE1
PHE D
48
12.320
−1.603
−30.591
1.00
25.17
D
C


ATOM
2854
CE2
PHE D
48
12.161
0.001
−28.828
1.00
29.95
D
C


ATOM
2855
CZ
PHE D
48
12.664
−0.380
−30.058
1.00
27.12
D
C


ATOM
2856
N
ASN D
49
9.595
−4.619
−24.814
1.00
25.16
D
N


ATOM
2857
CA
ASN D
49
8.601
−5.402
−24.084
1.00
29.35
D
C


ATOM
2858
C
ASN D
49
7.180
−4.950
−24.428
1.00
29.70
D
C


ATOM
2859
O
ASN D
49
6.995
−4.009
−25.201
1.00
30.49
D
O


ATOM
2860
CB
ASN D
49
8.855
−5.348
−22.574
1.00
24.72
D
C


ATOM
2861
CG
ASN D
49
8.473
−4.016
−21.961
1.00
34.53
D
C


ATOM
2862
OD1
ASN D
49
7.997
−3.108
−22.647
1.00
32.64
D
O


ATOM
2863
ND2
ASN D
49
8.680
−3.893
−20.654
1.00
26.98
D
N


ATOM
2864
N
SER D
50
6.180
−5.621
−23.866
1.00
32.64
D
N


ATOM
2865
CA
SER D
50
4.789
−5.308
−24.192
1.00
40.15
D
C


ATOM
2866
C
SER D
50
4.389
−3.893
−23.767
1.00
39.76
D
C


ATOM
2867
O
SER D
50
3.391
−3.361
−24.247
1.00
41.34
D
O


ATOM
2868
CB
SER D
50
3.834
−6.344
−23.589
1.00
38.04
D
C


ATOM
2869
OG
SER D
50
3.958
−6.401
−22.179
1.00
41.22
D
O


ATOM
2870
N
SER D
51
5.173
−3.288
−22.876
1.00
39.13
D
N


ATOM
2871
CA
SER D
51
4.925
−1.918
−22.422
1.00
37.74
D
C


ATOM
2872
C
SER D
51
5.769
−0.912
−23.198
1.00
37.71
D
C


ATOM
2873
O
SER D
51
5.913
0.236
−22.777
1.00
28.82
D
O


ATOM
2874
CB
SER D
51
5.226
−1.770
−20.925
1.00
33.74
D
C


ATOM
2875
OG
SER D
51
4.546
−2.747
−20.155
1.00
44.43
D
O


ATOM
2876
N
ASN D
52
6.339
−1.356
−24.316
1.00
43.05
D
N


ATOM
2877
CA
ASN D
52
7.168
−0.503
−25.176
1.00
38.17
D
C


ATOM
2878
C
ASN D
52
8.504
−0.025
−24.602
1.00
37.13
D
C


ATOM
2879
O
ASN D
52
9.169
0.821
−25.202
1.00
38.98
D
O


ATOM
2880
CB
ASN D
52
6.375
0.695
−25.699
1.00
45.39
D
C


ATOM
2881
CG
ASN D
52
5.833
0.463
−27.088
1.00
52.26
D
C


ATOM
2882
OD1
ASN D
52
5.356
−0.625
−27.404
1.00
42.19
D
O


ATOM
2883
ND2
ASN D
52
5.909
1.486
−27.933
1.00
50.55
D
N


ATOM
2884
N
LYS D
53
8.902
−0.554
−23.451
1.00
34.11
D
N


ATOM
2885
CA
LYS D
53
10.225
−0.239
−22.920
1.00
35.69
D
C


ATOM
2886
C
LYS D
53
11.318
−0.965
−23.713
1.00
35.71
D
C


ATOM
2887
O
LYS D
53
11.209
−2.158
−23.997
1.00
29.83
D
O


ATOM
2888
CB
LYS D
53
10.326
−0.582
−21.434
1.00
29.99
D
C


ATOM
2889
CG
LYS D
53
11.644
−0.149
−20.803
1.00
38.94
D
C


ATOM
2890
CD
LYS D
53
11.669
−0.437
−19.309
1.00
44.66
D
C


ATOM
2891
CE
LYS D
53
12.963
0.052
−18.674
1.00
37.57
D
C


ATOM
2892
NZ
LYS D
53
13.105
−0.439
−17.277
1.00
38.18
D
N


ATOM
2893
N
LEU D
54
12.368
−0.232
−24.065
1.00
35.22
D
N


ATOM
2894
CA
LEU D
54
13.446
−0.762
−24.889
1.00
29.03
D
C


ATOM
2895
C
LEU D
54
14.521
−1.472
−24.060
1.00
31.24
D
C


ATOM
2896
O
LEU D
54
14.893
−1.012
−22.982
1.00
37.90
D
O


ATOM
2897
CB
LEU D
54
14.073
0.372
−25.704
1.00
33.09
D
C


ATOM
2898
CG
LEU D
54
15.377
0.103
−26.459
1.00
35.38
D
C


ATOM
2899
CD1
LEU D
54
15.202
−1.013
−27.480
1.00
29.21
D
C


ATOM
2900
CD2
LEU D
54
15.871
1.375
−27.131
1.00
34.55
D
C


ATOM
2901
N
PHE D
55
15.002
−2.602
−24.568
1.00
25.28
D
N


ATOM
2902
CA
PHE D
55
16.134
−3.308
−23.978
1.00
24.03
D
C


ATOM
2903
C
PHE D
55
17.035
−3.742
−25.115
1.00
22.40
D
C


ATOM
2904
O
PHE D
55
16.551
−4.179
−26.151
1.00
28.76
D
O


ATOM
2905
CS
PHE D
55
15.671
−4.538
−23.196
1.00
24.17
D
C


ATOM
2906
CG
PHE D
55
14.784
−4.220
−22.030
1.00
19.47
D
C


ATOM
2907
CD1
PHE D
55
13411
−4.163
−22.185
1.00
18.73
D
C


ATOM
2908
CD2
PHE D
55
15.325
−3.986
−20.775
1.00
24.11
D
C


ATOM
2909
CE1
PHE D
55
12.590
−3.873
−21.114
1.00
26.91
D
C


ATOM
2910
CE2
PHE D
55
14.511
−3.693
−19.691
1.00
22.97
D
C


ATOM
2911
CZ
PHE D
55
13.139
−3.638
−19.861
1.00
29.43
D
C


ATOM
2912
N
GLN D
56
18.343
−3.631
−24.936
1.00
24.35
D
N


ATOM
2913
CA
GLN D
56
19.245
−3.946
−26.028
1.00
23.77
D
C


ATOM
2914
C
GLN D
56
20.546
−4.595
−25.591
1.00
27.79
D
C


ATOM
2915
O
GLN D
56
20.981
−4.452
−24.453
1.00
34.31
D
O


ATOM
2916
CB
GLN D
56
19.540
−2.686
−26.843
1.00
29.59
D
C


ATOM
2917
CG
GLN D
56
20.008
−1.501
−26.014
1.00
28.77
D
C


ATOM
2918
CD
GLN D
56
20.233
−0.254
−26.855
1.00
37.59
D
C


ATOM
2919
OE1
GLN D
56
20.772
−0.324
−27.961
1.00
36.74
D
O


ATOM
2920
NE2
GLN D
56
19.821
0.893
−26.332
1.00
35.89
D
N


ATOM
2921
N
TYR D
57
21.151
−5.325
−26.521
1.00
22.60
D
N


ATOM
2922
CA
TYR D
57
22.489
−5.859
−26.355
1.00
23.14
D
C


ATOM
2923
C
TYR D
57
23.214
−5.785
−27.693
1.00
22.80
D
C


ATOM
2924
O
TYR D
57
22.613
−6.004
−28.747
1.00
24.23
D
O


ATOM
2925
CB
TYR D
57
22.468
−7.320
−25.880
1.00
25.34
D
C


ATOM
2926
CG
TYR D
57
23.786
−8.010
−26.165
1.00
23.93
D
C


ATOM
2927
CD1
TYR D
57
24.880
−7.833
−25.325
1.00
24.98
D
C


ATOM
2928
CD2
TYR D
57
23.955
−8.790
−27.302
1.00
22.24
D
C


ATOM
2929
CE1
TYR D
57
26.099
−8.431
−25.594
1.00
23.10
D
C


ATOM
2930
CE2
TYR D
57
25.170
−9.399
−27.581
1.00
21.19
D
C


ATOM
2931
CZ
TYR D
57
26.240
−9.215
−26.726
1.00
25.96
D
C


ATOM
2932
OH
TYR D
57
27.456
−9.814
−26.997
1.00
20.95
D
O


ATOM
2933
N
ALA D
58
24.508
−5.500
−27.654
1.00
23.20
D
N


ATOM
2954
CA
ALA D
58
25.312
−5.524
−28.866
1.00
25.98
D
C


ATOM
2935
C
ALA D
58
26.761
−5.845
−28.536
1.00
21.59
D
C


ATOM
2936
O
ALA D
58
27.281
−5.390
−27.522
1.00
22.42
D
O


ATOM
2937
CB
ALA D
58
25.204
−4.198
−29.595
1.00
28.83
D
C


ATOM
2938
N
SER D
59
27.409
−6.633
−29.394
1.00
22.61
D
N


ATOM
2939
CA
SER D
59
28.807
−7.013
−29.182
1.00
24.17
D
C


ATOM
2940
C
SER D
59
29.756
−5.829
−29.371
1.00
27.66
D
C


ATOM
2941
O
SER D
59
30.931
−5.913
−29.031
1.00
18.97
D
O


ATOM
2942
CB
SER D
59
29.209
−8.182
−30.087
1.00
20.53
D
C


ATOM
2943
OG
SER D
59
28.979
−7.887
−31.454
1.00
23.14
D
O


ATOM
2944
N
THR D
60
29.237
−4.739
−29.932
1.00
37.48
D
N


ATOM
2945
CA
THR D
60
29.942
−3.461
−29.992
1.00
35.18
D
C


ATOM
2946
C
THR D
60
28.887
−2.370
−29.967
1.00
41.12
D
C


ATOM
2947
O
THR D
60
27.719
−2.643
−29.695
1.00
38.33
D
O


ATOM
2948
CB
THR D
60
30.758
−3.289
−31.282
1.00
43.32
D
C


ATOM
2949
OG1
THR D
60
29.872
−3.275
−32.409
1.00
45.89
D
O


ATOM
2950
CG2
THR D
60
31.776
−4.410
−31.444
1.00
53.89
D
C


ATOM
2951
N
ASP D
61
29.287
−1.139
−30.267
1.00
32.58
D
N


ATOM
2952
CA
ASP D
61
28.330
−0.043
−30.326
1.00
31.13
D
C


ATOM
2953
C
ASP D
61
27.159
−0.437
−31.216
1.00
35.70
D
C


ATOM
2954
O
ASP D
61
27.335
−0.752
−32.398
1.00
31.62
D
O


ATOM
2955
CB
ASP D
61
28.983
1.240
−30.845
1.00
36.78
D
C


ATOM
2956
CG
ASP D
61
30.123
1.712
−29.963
1.00
44.94
D
C


ATOM
2957
OD1
ASP D
61
31.217
1.107
−30.021
1.00
48.90
D
O


ATOM
2958
OD2
ASP D
61
29.928
2.695
−29.220
1.00
39.72
D
O


ATOM
2959
N
MET D
62
25.967
−0.432
−30.629
1.00
43.29
D
N


ATOM
2960
CA
MET D
62
24.751
−0.809
−31.333
1.00
38.50
D
C


ATOM
2961
T
MET D
62
24.690
−0.227
−32.739
1.00
42.94
D
C


ATOM
2962
O
MET D
62
24.307
−0.909
−33.692
1.00
41.35
D
O


ATOM
2963
CB
MET D
62
23.525
−0.356
−30.545
1.00
31.73
D
C


ATOM
2964
CG
MET D
62
22.224
−0.571
−31.291
1.00
37.28
D
C


ATOM
2965
SD
MET D
62
22.020
−2.280
−31.823
1.00
31.31
D
S


ATOM
2966
CE
MET D
62
21.853
−3.121
−30.255
1.00
24.52
D
C


ATOM
2967
N
ASP D
63
25.074
1.038
−32.861
1.00
46.37
D
N


ATOM
2968
CA
ASP D
63
24.940
1.758
−34.120
1.00
44.58
D
C


ATOM
2969
C
ASP D
63
25.941
1.303
−35.182
1.00
41.10
D
C


ATOM
2970
O
ASP D
63
25.705
1.471
−36.377
1.00
43.44
D
O


ATOM
2971
CB
ASP D
63
25.030
3.263
−33.877
1.00
56.07
D
C


ATOM
2972
CG
ASP D
63
23.875
3.781
−33.033
1.00
63.85
D
C


ATOM
2973
CD1
ASP D
63
22.752
3.914
−33.570
1.00
56.52
D
O


ATOM
2974
OD2
ASP D
63
24.089
4.051
−31.830
1.00
64.52
D
O


ATOM
2975
N
LYS D
64
27.051
0.718
−34.750
1.00
39.39
D
N


ATOM
2976
CA
LYS D
64
28.013
0.173
−35.701
1.00
38.16
D
C


ATOM
2977
C
LYS D
64
27.443
−1.065
−36.399
1.00
38.15
D
C


ATOM
2978
O
LYS D
64
27.552
−1.205
−37.618
1.00
31.22
D
O


ATOM
2979
CB
LYS D
64
29.341
−0.148
−35.013
1.00
42.22
D
C


ATOM
2980
CG
LYS D
64
30.070
1.082
−34.497
1.00
52.48
D
C


ATOM
2981
CD
LYS D
64
31.475
0.748
−34.033
1.00
56.05
D
C


ATOM
2982
CE
LYS D
64
32.217
1.996
−33.586
1.00
54.72
D
C


ATOM
2983
NZ
LYS D
64
33.614
1.680
−33.185
1.00
55.86
D
N


ATOM
2984
N
VAL D
65
26.526
−1.952
−35.621
1.00
35.03
D
N


ATOM
2985
CA
VAL D
65
26.206
−3.151
−36.173
1.00
31.99
D
C


ATOM
2986
C
VAL D
65
25.102
−2.778
−37.157
1.00
32.00
D
C


ATOM
2587
O
VAL D
65
24.979
−3.375
−38.230
1.00
28.64
D
O


ATOM
2988
CB
VAL D
65
25.595
−4.036
−35.067
1.00
29.41
D
C


ATOM
2989
CG1
VAL D
65
25.033
−5.312
−35.664
1.00
24.64
D
C


ATOM
2990
CG2
VAL D
65
26.630
−4.351
−34.000
1.00
33.52
D
C


ATOM
2991
N
LEU D
66
24.304
−1.782
−36.785
1.00
30.13
D
N


ATOM
2992
CA
LEU D
66
23.175
−1.357
−37.598
1.00
34.53
D
C


ATOM
2993
C
LEU D
66
23.600
−0.784
−38.952
1.00
41.59
D
C


ATOM
2994
O
LEU D
66
23.020
−1.125
−39.985
1.00
39.34
D
O


ATOM
2995
CB
LEU D
66
22.309
−0.363
−36.825
1.00
35.86
D
C


ATOM
2996
CG
LEU D
66
21.616
−0.997
−35.616
1.00
36.70
D
C


ATOM
2997
CD1
LEU D
66
20.698
−0.009
−34.920
1.00
32.04
D
C


ATOM
2998
CD2
LEU D
66
20.844
−2.239
−36.046
1.00
31.94
D
C


ATOM
2999
N
LEU D
67
24.615
0.076
−38.950
1.00
45.33
D
N


ATOM
3000
CA
LEU D
67
25.112
0.643
−40.198
1.00
45.57
D
C


ATOM
3001
C
LEU D
67
25.707
−0.442
−41.082
1.00
45.23
D
C


ATOM
3002
O
LEU D
67
25.634
−0.367
−42.306
1.00
48.91
D
O


ATOM
3003
CB
LEU D
67
26.142
1.747
−39.940
1.00
48.90
D
C


ATOM
3004
CG
LEU D
67
25.592
3.174
−39.830
1.00
50.39
D
C


ATOM
3005
CD1
LEU D
67
24.565
3.429
−40.929
1.00
55.28
D
C


ATOM
3006
CD2
LEU D
67
24.986
3.442
−38.456
1.00
51.05
D
C


ATOM
3007
N
LYS D
68
26.298
−1.452
−40.455
1.00
30.19
D
N


ATOM
3008
CA
LYS D
68
26.851
−2.574
−41.195
1.00
28.53
D
C


ATOM
3009
C
LYS D
68
25.714
−3.334
−41.864
1.00
36.93
D
C


ATOM
3010
O
LYS D
68
25.860
−3.848
−42.974
1.00
38.76
D
O


ATOM
3011
CB
LYS D
68
27.650
−3.494
−40.269
1.00
31.26
D
C


ATOM
3012
CG
LYS D
68
28.446
−4.569
−41.002
1.00
36.31
D
C


ATOM
3013
CD
LYS D
68
29.462
−5.248
−40.092
1.00
41.17
D
C


ATOM
3014
CE
LYS D
68
30.185
−6.366
−40.824
1.00
38.47
D
C


ATOM
3015
NZ
LYS D
68
31.084
−7.147
−39.930
1.00
37.84
D
N


ATOM
3016
N
TYR D
69
24.574
−3.384
−41.182
1.00
36.80
D
N


ATOM
3017
CA
TYR D
69
23.388
−4.048
−41.711
1.00
38.58
D
C


ATOM
3018
C
TYR D
69
22.826
−3.312
−42.924
1.00
37.48
D
C


ATOM
3019
O
TYR D
69
22.574
−3.916
−43.969
1.00
36.91
D
O


ATOM
3020
CB
TYR D
69
22.312
−4.154
−40.628
1.00
33.48
D
C


ATOM
3021
CG
TYR D
69
20.993
−4.704
−41.125
1.00
28.61
D
C


ATOM
3022
CD1
TYR D
69
20.791
−6.071
−41.248
1.00
25.44
D
C


ATOM
3023
CD2
TYR D
69
19.949
−3.856
−41.466
1.00
29.91
D
C


ATOM
3024
CE1
TYR D
69
19.594
−6.577
−41.694
1.00
23.48
D
C


ATOM
3025
CE2
TYR D
69
18.743
−4.356
−41.915
1.00
23.47
D
C


ATOM
3026
CZ
TYR D
69
18.573
−5.719
−42.028
1.00
24.70
D
C


ATOM
3027
OH
TYR D
69
17.374
−6.229
−42.478
1.00
27.28
D
O


ATOM
3028
N
THR D
70
22.625
−2.007
−42.779
1.00
35.91
D
N


ATOM
3029
CA
THR D
70
22.044
−1.209
−43.851
1.00
41.72
D
C


ATOM
3030
C
THR D
70
22.985
−1.143
−45.048
1.00
45.23
D
C


ATOM
3031
O
THR D
70
22.556
−1.280
−46.195
1.00
54.00
D
O


ATOM
3032
CB
THR D
70
21.669
0.208
−43.371
1.00
43.34
D
C


ATOM
3033
OG1
THR D
70
22.794
0.812
−42.723
1.00
52.52
D
O


ATOM
3034
CG2
THR D
70
20.510
0.140
−42.386
1.00
39.54
D
C


ATOM
3035
N
GLU D
71
24.270
−0.950
−44.775
1.00
37.17
D
N


ATOM
3036
CA
GLU D
71
25.285
−0.959
−45.822
1.00
45.08
D
C


ATOM
3037
C
GLU D
71
25.360
−2.327
−46.502
1.00
40.36
D
C


ATOM
3038
O
GLU D
71
25.728
−2.431
−47.671
1.00
44.26
D
O


ATOM
3039
CB
GLU D
71
26.656
−0.580
−45.247
1.00
34.24
D
C


ATOM
3040
N
TYR D
72
25.014
−3.372
−45.756
1.00
43.08
D
N


ATOM
3041
CA
TYR D
72
25.049
−4.736
−46.269
1.00
44.67
D
C


ATOM
3042
C
TYR D
72
24.000
−4.905
−47.359
1.00
53.17
D
C


ATOM
3043
O
TYR D
72
24.293
−5.401
−48.450
1.00
52.85
D
O


ATOM
3044
CB
TYR D
72
24.790
−5.729
−45.133
1.00
45.47
D
C


ATOM
3045
CG
TYR D
72
25.057
−7.181
−45.473
1.00
41.46
D
C


ATOM
3046
CD1
TYR D
72
26.211
−7.816
−45.029
1.00
36.92
D
C


ATOM
3047
CD2
TYR D
72
24.149
−7.922
−46.224
1.00
42.67
D
C


ATOM
3048
CE1
TYR D
72
26.461
−9.148
−45.328
1.00
34.28
D
C


ATOM
3049
CE2
TYR D
72
24.386
−9.255
−46.526
1.00
36.45
D
C


ATOM
3050
CZ
TYR D
72
25.542
−9.863
−46.075
1.00
41.64
D
C


ATOM
3051
OH
TYR D
72
25.786
−11.187
−46.372
1.00
43.36
D
O


ATOM
3052
N
ASN D
73
22.775
−4.487
−47.047
1.00
80.06
D
N


ATOM
3053
CA
ASN D
73
21.657
−4.569
−47.981
1.00
81.24
D
C


ATOM
3054
C
ASN D
73
21.840
−3.626
−49.166
1.00
89.74
D
C


ATOM
3055
O
ASN D
73
21.953
−2.411
−48.994
1.00
87.49
D
O


ATOM
3056
CB
ASN D
73
20.332
−4.264
−47.268
1.00
78.13
D
C


ATOM
3057
CG
ASN D
73
19.902
−5.374
−46.315
1.00
68.24
D
C


ATOM
3058
OD1
ASN D
73
18.773
−5.859
−46.380
1.00
71.72
D
O


ATOM
3059
ND2
ASN D
73
20.801
−5.778
−45.426
1.00
60.27
D
N


TER


ATOM
3060
O5′
ADE G
1
2.089
−11.162
−3.297
1.00
30.09
G
O


ATOM
3061
C5′
ADE G
1
1.758
−9.795
−3.078
1.00
31.54
G
C


ATOM
3062
C4′
ADE G
1
2.994
−8.975
−2.748
1.00
32.18
G
C


ATOM
3063
O4′
ADE G
1
3.673
−9.553
−1.599
1.00
29.23
G
O


ATOM
3064
C3′
ADE G
1
4.047
−8.913
−3.851
1.00
36.39
G
C


ATOM
3065
O3′
ADE G
1
4.751
−7.683
−3.778
1.00
32.25
G
O


ATOM
3066
C2′
ADE G
1
4.963
−10.064
−3.462
1.00
36.96
G
C


ATOM
3067
C1′
ADE G
1
5.015
−9.805
−1.964
1.00
31.04
G
C


ATOM
3068
N9
ADE G
1
5.528
−10.926
−1.189
1.00
30.97
G
N


ATOM
3069
C8
ADE G
1
6.758
−11.000
−0.601
1.00
31.87
G
C


ATOM
3070
N7
ADE G
1
6.970
−12.124
0.035
1.00
29.74
G
N


ATOM
3071
C5
ADE G
1
5.802
−12.836
−0.151
1.00
25.19
G
C


ATOM
3072
C6
ADE G
1
5.409
−14.110
0.280
1.00
27.04
G
C


ATOM
3073
N6
ADE G
1
6.195
−14.892
1.021
1.00
29.70
G
N


ATOM
3074
N1
ADE G
1
4.179
−14.536
−0.076
1.00
33.56
G
N


ATOM
3075
C2
ADE G
1
3.408
−13.727
−0.818
1.00
33.14
G
C


ATOM
3076
N3
ADE G
1
3.673
−12.505
−1.284
1.00
29.79
G
N


ATOM
3077
C4
ADE G
1
4.899
−12.115
−0.907
1.00
29.22
G
C


ATOM
3078
P
ADE G
2
5.814
−7.300
−4.906
1.00
38.84
G
P


ATOM
3079
OP1
ADE G
2
6.230
−5.901
−4.689
1.00
40.00
G
O


ATOM
3080
OP2
ADE G
2
5.266
−7.699
−6.218
1.00
34.10
G
O


ATOM
3081
O5
ADE G
2
7.049
−8.252
−4.565
1.00
46.24
G
O


ATOM
3082
C5′
ADE G
2
8.141
−7.809
−3.759
1.00
34.96
G
C


ATOM
3083
C4′
ADE G
2
9.293
−8.790
−3.905
1.00
37.08
G
C


ATOM
3084
O4′
ADE G
2
8.859
−10.100
−3.448
1.00
40.16
G
O


ATOM
3085
C3′
ADE G
2
9.760
−9.022
−5.341
1.00
35.45
G
C


ATOM
3086
O3′
ADE G
2
11.106
−9.463
−5.356
1.00
43.32
G
O


ATOM
3087
C2′
ADE G
2
8.863
−10.169
−5.773
1.00
36.55
G
C


ATOM
3088
C1′
ADE G
2
9.019
−11.013
−4.517
1.00
31.98
G
C


ATOM
3089
N9
ADE G
2
8.071
−12.116
−4.422
1.00
29.90
G
N


ATOM
3090
C8
ADE G
2
7.016
−12.377
−5.252
1.00
32.71
G
C


ATOM
3091
N7
ADE G
2
6.345
−13.460
−4.924
1.00
30.52
G
N


ATOM
3092
C5
ADE G
2
7.008
−13.937
−3.804
1.00
29.99
G
C


ATOM
3093
C6
ADE G
2
6.796
−15.056
−2.977
1.00
29.21
G
C


ATOM
3094
N6
ADE G
2
5.803
−15.932
−3.158
1.00
29.86
G
N


ATOM
3095
N1
ADE G
2
7.649
−15.243
−1.950
1.00
27.42
G
N


ATOM
3096
C2
ADE G
2
8.642
−14.369
−1.759
1.00
26.74
G
C


ATOM
3097
N3
ADE G
2
8.938
−13.282
−2.466
1.00
27.47
G
N


ATOM
3098
C4
ADE G
2
8.076
−13.122
−3.483
1.00
29.22
G
C


ATOM
3099
P
ADE G
3
12.320
−8.428
−5.459
1.00
41.20
G
P


ATOM
3100
OP1
ADE G
3
11.995
−7.245
−4.633
1.00
36.86
G
O


ATOM
3101
OP2
ADE G
3
12.648
−8.262
−6.893
1.00
38.02
G
O


ATOM
3102
O5′
ADE G
3
13.507
−9.254
−4.767
1.00
33.94
G
O


ATOM
3103
C5′
ADE G
3
13.430
−9.595
−3.390
1.00
28.55
G
C


ATOM
3104
C4′
ADE G
3
14.057
−10.954
−3.120
1.00
32.01
G
C


ATOM
3105
O4′
ADE G
3
13.052
−12.001
−3.180
1.00
29.13
G
O


ATOM
3106
C3′
ADE G
3
15.169
−11.380
−4.075
1.00
39.18
G
C


ATOM
3107
O3′
ADE G
3
16.238
−11.933
−3.311
1.00
36.03
G
O


ATOM
3108
C2′
ADE G
3
14.504
−12.438
−4.960
1.00
33.01
G
C


ATOM
3109
C1′
ADE G
3
13.501
−13.065
−4.000
1.00
35.72
G
C


ATOM
3110
N9
ADE G
3
12.333
−13.631
−4.667
1.00
30.02
G
N


ATOM
3111
C8
ADE G
3
11.696
−13.134
−5.771
1.00
29.04
G
C


ATOM
3112
N7
ADE G
3
10.663
−13.842
−6.159
1.00
29.82
G
N


ATOM
3113
C5
ADE G
3
10.618
−14.879
−5.241
1.00
28.28
G
C


ATOM
3114
C6
ADE G
3
9.747
−15.976
−5.095
1.00
26.79
G
C


ATOM
3115
N6
ADE G
3
8.719
−16.211
−5.916
1.00
30.72
G
N


ATOM
3116
N1
ADE G
3
9.980
−16.825
−4.071
1.00
30.91
G
N


ATOM
3117
C2
ADE G
3
11.013
−16.589
−3.248
1.00
28.20
G
C


ATOM
3118
N3
ADE G
3
11.893
−15.589
−3.285
1.00
28.13
G
N


ATOM
3119
C4
ADE G
3
11.639
−14.764
−4.314
1.00
26.77
G
C


ATOM
3120
P
GUA G
4
17.525
−12.572
−4.017
1.00
44.94
G
P


ATOM
3121
OP1
GUA G
4
18.657
−12.319
−3.104
1.00
26.60
G
O


ATOM
3122
OP2
GUA G
4
17.569
−12.119
−5.430
1.00
43.10
G
O


ATOM
3123
O5′
GUA G
4
17.206
−14.141
−4.011
1.00
41.67
G
O


ATOM
3124
C5′
GUA G
4
17.066
−14.783
−2.751
1.00
41.51
G
C


ATOM
3125
C4′
GUA G
4
16.533
−16.199
−2.887
1.00
40.62
G
C


ATOM
3126
O4′
GUA G
4
15.266
−16.214
−3.593
1.00
41.42
G
O


ATOM
3127
C3′
GUA G
4
17.429
−17.186
−3.627
1.00
49.83
G
C


ATOM
3128
O3′
GUA G
4
17.570
−18.307
−2.768
1.00
51.67
G
O


ATOM
3329
C2′
GUA G
4
16.656
−17.515
−4.908
1.00
40.85
G
C


ATOM
3130
C1′
GUA G
4
15.220
−17.355
−4.420
1.00
36.12
G
C


ATOM
3131
N9
GUA G
4
14.207
−17.099
−5.442
1.00
35.49
G
N


ATOM
3132
C8
GUA G
4
14.154
−16.049
−6.329
1.00
31.33
G
C


ATOM
3133
N7
GUA G
4
13.109
−16.088
−7.115
1.00
30.40
G
N


ATOM
3134
C5
GUA G
4
12.422
−17.235
−6.723
1.00
31.20
G
C


ATOM
3135
C6
GUA G
4
11.212
−17.799
−7.209
1.00
29.78
G
C


ATOM
3136
O6
GUA G
4
10.467
−17.389
−8.120
1.00
26.03
G
O


ATOM
3137
N1
GUA G
4
10.882
−18.965
−6.518
1.00
27.82
G
N


ATOM
3138
C2
GUA G
4
11.619
−39.516
−5.497
1.00
32.35
G
C


ATOM
3139
N2
GUA G
4
11.140
−20.647
−4.957
1.00
36.86
G
N


ATOM
3140
N3
GUA G
4
12.750
−18.998
−5.034
1.00
30.81
G
N


ATOM
3141
C4
GUA G
4
13.087
−17.863
−5.691
1.00
32.84
G
C


ATOM
3142
P
CYT G
5
18.538
−19.531
−3.110
1.00
55.72
G
P


ATOM
3143
OP1
CYT G
5
19.281
−19.838
−1.867
1.00
38.31
G
O


ATOM
3144
OP2
CYT G
5
19.231
−19.265
−4.393
1.00
40.25
G
O


ATOM
3145
O5′
CYT G
5
17.491
−20.711
−3.363
1.00
37.47
G
O


ATOM
3146
C5′
CYT G
5
16.519
−20.951
−2.356
1.00
33.10
G
C


ATOM
3147
C4′
CYT G
5
15.692
−22.166
−2.706
1.00
33.20
G
C


ATOM
3148
O4′
CYT G
5
14.748
−21.822
−3.746
1.00
30.86
G
O


ATOM
3149
C3′
CYT G
5
16.490
−23.358
−3.215
1.00
34.33
G
C


ATOM
3150
O3′
CYT G
5
15.942
−24.508
−2.587
1.00
39.29
G
O


ATOM
3151
C2′
CYT G
5
16.264
−23.310
−4.729
1.00
31.29
G
C


ATOM
3152
C1′
CYT G
5
14.868
−22.703
−4.835
1.00
28.72
G
C


ATOM
3153
N1
CYT G
5
14.580
−21.859
−6.034
1.00
29.55
G
N


ATOM
3154
C2
CYT G
5
13.502
−22.187
−6.861
1.00
26.17
G
C


ATOM
3155
O2
CYT G
5
12.818
−23.189
−6.597
1.00
28.47
G
O


ATOM
3156
N3
CYT G
5
13.239
−21.397
−7.932
1.00
26.81
G
N


ATOM
3157
C4
CYT G
5
13.999
−20.328
−8.189
1.00
25.37
G
C


ATOM
3158
N4
CYT G
5
13.695
−19.590
−9.264
1.00
22.67
G
N


ATOM
3159
C5
CYT G
5
15.098
−19.973
−7.353
1.00
25.47
G
C


ATOM
3160
C6
CYT G
5
15.344
−20.758
−6.297
1.00
30.74
G
C


ATOM
3161
P
THY G
6
16.549
−25.968
−2.798
1.00
62.65
G
P


ATOM
3162
OP1
THY G
6
16.186
−26.778
−1.614
1.00
56.50
G
O


ATOM
3163
OP2
THY G
6
17.966
−25.841
−3.210
1.00
52.21
G
O


ATOM
3164
O5′
THY G
6
15.727
−26.497
−4.064
1.00
49.96
G
O


ATOM
3165
C5′
THY G
6
14.396
−26.977
−3.929
1.00
48.74
G
C


ATOM
3166
C4′
THY G
6
14.019
−27.782
−5.157
1.00
40.65
G
C


ATOM
3167
O4′
THY G
6
13.704
−26.874
−6.246
1.00
41.97
G
O


ATOM
3168
C3′
THY G
6
15.131
−28.676
−5.695
1.00
45.61
G
C


ATOM
3169
O3′
THY G
6
14.577
−29.772
−6.399
1.00
51.56
G
O


ATOM
3170
C2′
THY G
6
15.817
−27.746
−6.684
1.00
42.12
G
C


ATOM
3171
C1′
THY G
6
14.568
−27.158
−7.330
1.00
46.59
G
C


ATOM
3172
N1
THY G
6
14.811
−25.913
−8.108
1.00
38.83
G
N


ATOM
3173
C2
THY G
6
13.846
−25.493
−8.994
1.00
36.66
G
C


ATOM
3174
O2
THY G
6
12.799
−26.093
−9.164
1.00
35.66
G
O


ATOM
3175
N3
THY G
6
14.152
−24.339
−9.668
1.00
31.51
G
N


ATOM
3176
C4
THY G
6
15.308
−23.590
−9.545
1.00
33.13
G
C


ATOM
3177
O4
THY G
6
15.497
−22.569
−10.194
1.00
36.34
G
O


ATOM
3178
C5
THY G
6
16.280
−24.092
−8.604
1.00
35.08
G
C


ATOM
3179
C7
THY G
6
17.572
−23.358
−8.395
1.00
29.54
G
C


ATOM
3180
C6
THY G
6
15.990
−25.217
−7.938
1.00
33.15
G
C


ATOM
3181
P
ADE G
7
14.158
−31.112
−5.635
1.00
45.98
G
P


ATOM
3182
OP1
ADE G
7
13.536
−30.737
−4.346
1.00
49.15
G
O


ATOM
3183
OP2
ADE G
7
15.320
−32.024
−5.661
1.00
50.69
G
O


ATOM
3184
O5′
ADE G
7
13.029
−31.710
−6.594
1.00
37.82
G
O


ATOM
3185
C5′
ADE G
7
11.731
−31.143
−6.586
1.00
40.93
G
C


ATOM
3186
C4′
ADE G
7
11.136
−31.093
−7.982
1.00
41.28
G
C


ATOM
3187
O4′
ADE G
7
11.745
−30.022
−8.750
1.00
42.69
G
O


ATOM
3188
C3′
ADE G
7
11.307
−32.355
−8.812
1.00
44.26
G
C


ATOM
3189
O3′
ADE G
7
10.102
−32.546
−9.548
1.00
46.58
G
O


ATOM
3190
C2′
ADE G
7
12.522
−32.032
−9.691
1.00
39.03
G
C


ATOM
3191
C1′
ADE G
7
12.369
−30.527
−9.915
1.00
40.77
G
C


ATOM
3192
N9
ADE G
7
13.605
−29.761
−10.075
1.00
35.79
G
N


ATOM
3193
C8
ADE G
7
14.800
−29.956
−9.437
1.00
38.83
G
C


ATOM
3194
N7
ADE G
7
15.733
−29.090
−9.772
1.00
39.23
G
N


ATOM
3195
C5
ADE G
7
15.106
−28.261
−10.690
1.00
32.85
G
C


ATOM
3196
C6
ADE G
7
15.548
−27.137
−11.423
1.00
28.85
G
C


ATOM
3197
N6
ADE G
7
16.783
−26.630
−11.346
1.00
24.36
G
N


ATOM
3198
N1
ADE G
7
14.662
−26.547
−12.252
1.00
28.50
G
N


ATOM
3199
C2
ADE G
7
13.422
−27.042
−12.340
1.00
28.65
G
C


ATOM
3200
N3
ADE G
7
12.893
−28.087
−11.701
1.00
35.16
G
N


ATOM
3201
C4
ADE G
7
13.794
−28.659
−10.883
1.00
35.41
G
C


ATOM
3202
P
THY G
8
9.904
−33.839
−10.469
1.00
58.11
G
P


ATOM
3203
OP1
THY G
8
8.471
−34.212
−10.428
1.00
52.37
G
O


ATOM
3204
OP2
THY G
8
10.968
−34.817
−10.125
1.00
42.98
G
O


ATOM
3205
O5′
THY G
8
10.202
−33.255
−11.925
1.00
39.07
G
O


ATOM
3206
C5′
THY G
8
9.502
−32.094
−12.335
1.00
39.40
G
C


ATOM
3207
C4′
THY G
8
10.160
−31.489
−13.559
1.00
40.04
G
C


ATOM
3208
O4′
THY G
8
11.414
−30.863
−13.208
1.00
41.59
G
O


ATOM
3209
C3′
THY G
8
10.517
−32.477
−14.664
1.00
32.24
G
C


ATOM
3210
O3′
THY G
8
9.467
−32.466
−15.624
1.00
32.65
G
O


ATOM
3211
C2′
THY G
8
11.839
−31.938
−15.220
1.00
30.22
G
C


ATOM
3212
C1′
THY G
8
12.062
−30.645
−14.439
1.00
33.04
G
C


ATOM
3213
N1
THY G
8
13.493
−30.260
−14.190
1.00
32.43
G
N


ATOM
3214
C2
THY G
8
14.016
−29.165
−14.847
1.00
30.93
G
C


ATOM
3215
O2
THY G
8
13.380
−28.485
−15.636
1.00
29.88
G
O


ATOM
3216
N3
THY G
8
15.327
−28.890
−14.551
1.00
26.98
G
N


ATOM
3217
C4
THY G
8
16.154
−29.577
−13.683
1.00
29.88
G
C


ATOM
3218
O4
THY G
8
17.326
−29.246
−13.490
1.00
25.74
G
O


ATOM
3219
C5
THY G
8
15.541
−30.708
−13.027
1.00
30.10
G
C


ATOM
3220
C7
THY G
8
16.337
−31.538
−12.060
1.00
38.26
G
C


ATOM
3221
C6
THY G
8
14.263
−30.992
−13.307
1.00
28.43
G
C


ATOM
3222
P
THY G
9
9.616
−33.145
−17.068
1.00
40.40
G
P


ATOM
3223
OP1
THY G
9
8.257
−33.380
−17.598
1.00
29.13
G
O


ATOM
3224
OP2
THY G
9
10.591
−34.251
−16.958
1.00
33.30
G
O


ATOM
3225
O5′
THY G
9
10.257
−31.979
−17.948
1.00
35.54
G
O


ATOM
3226
C5′
THY G
9
9.490
−30.803
−18.126
1.00
33.56
G
C


ATOM
3227
C4′
THY G
9
10.278
−29.781
−18.911
1.00
31.82
G
C


ATOM
3228
O4′
THY G
9
11.559
−29.580
−18.269
1.00
27.85
G
O


ATOM
3229
C3′
THY G
9
10.574
−30.170
−20.355
1.00
26.02
G
C


ATOM
3230
O3′
THY G
9
10.419
−28.984
−21.121
1.00
29.19
G
O


ATOM
3231
C2′
THY G
9
12.015
−30.683
−20.291
1.00
25.44
G
C


ATOM
3232
C1′
THY G
9
12.588
−29.753
−19.223
1.00
29.00
G
C


ATOM
3233
N1
THY G
9
13.781
−30.239
−18.474
1.00
26.11
G
N


ATOM
3234
C2
THY G
9
14.842
−29.387
−18.366
1.00
23.17
G
C


ATOM
3235
O2
THY G
9
14.839
−28.276
−18.867
1.00
24.88
G
O


ATOM
3236
N3
THY G
9
15.901
−29.890
−17.652
1.00
24.78
G
N


ATOM
3237
C4
THY G
9
16.000
−31.129
−17.047
1.00
22.42
G
C


ATOM
3238
O4
THY G
9
16.996
−31.492
−16.427
1.00
25.07
G
O


ATOM
3239
C5
THY G
9
14.851
−31.971
−17.199
1.00
24.19
G
C


ATOM
3240
C7
THY G
9
14.855
−33.340
−16.582
1.00
24.67
G
C


ATOM
3241
C6
THY G
9
13.807
−31.492
−17.895
1.00
28.98
G
C


ATOM
3242
P
ADE G
10
10.667
−28.948
−22.697
1.00
27.55
G
P


ATOM
3243
OP1
ADE G
10
9.807
−27.892
−23.275
1.00
25.17
G
O


ATOM
3244
OP2
ADE G
10
10.572
−30.334
−23.209
1.00
31.35
G
O


ATOM
3245
O5′
ADE G
10
12.182
−28.437
−22.773
1.00
37.21
G
O


ATOM
3246
C5′
ADE G
10
12.484
−27.120
−22.314
1.00
23.68
G
C


ATOM
3247
C4′
ADE G
10
13.858
−26.640
−22.756
1.00
22.58
G
C


ATOM
3248
O4′
ADE G
10
14.884
−27.249
−21.939
1.00
22.97
G
O


ATOM
3249
C3′
ADE G
10
14.259
−26.935
−24.196
1.00
25.44
G
C


ATOM
3250
O3′
ADE G
10
14.904
−25.776
−24.681
1.00
22.78
G
O


ATOM
3251
C2′
ADE G
10
15.215
−28.121
−24.073
1.00
18.98
G
C


ATOM
3252
C1′
ADE G
10
15.893
−27.822
−22.744
1.00
23.52
G
C


ATOM
3253
N9
ADE G
10
16.359
−28.998
−22.015
1.00
23.49
G
N


ATOM
3254
C8
ADE G
10
15.649
−30.147
−21.787
1.00
20.29
G
C


ATOM
3255
N7
ADE G
10
16.309
−31.040
−21.086
1.00
21.42
G
N


ATOM
3256
C5
ADE G
10
17.529
−30.433
−20.832
1.00
20.13
G
C


ATOM
3257
C6
ADE G
10
18.673
−30.865
−20.131
1.00
23.13
G
C


ATOM
3258
N6
ADE G
10
18.761
−32.062
−19.540
1.00
22.41
G
N


ATOM
3259
N1
ADE G
10
19.723
−30.018
−20.065
1.00
21.54
G
N


ATOM
3260
C2
ADE G
10
19.626
−28.826
−20.665
1.00
19.94
G
C


ATOM
3261
N3
ADE G
10
18.602
−28.309
−21.347
1.00
21.70
G
N


ATOM
3262
C4
ADE G
10
17.577
−29.173
−21.396
1.00
20.19
G
C


ATOM
3263
P
THY G
11
15.529
−25.684
−26.145
1.00
28.15
G
P


ATOM
3264
OP1
THY G
11
15.315
−24.302
−26.619
1.00
28.86
G
O


ATOM
3265
OP2
THY G
11
15.080
−26.832
−26.967
1.00
20.38
G
O


ATOM
3266
O5′
THY G
11
17.085
−25.861
−25.826
1.00
29.02
G
O


ATOM
3267
C5′
THY G
11
17.711
−24.929
−24.951
1.00
22.15
G
C


ATOM
3268
C4′
THY G
11
19.189
−25.234
−24.789
1.00
25.89
G
C


ATOM
3269
O4′
THY G
11
19.351
−26.501
−24.106
1.00
23.80
G
O


ATOM
3270
C3′
THY G
11
19.983
−25.330
−26.086
1.00
27.91
G
C


ATOM
3271
O3′
THY G
11
21.157
−24.518
−25.923
1.00
24.16
G
O


ATOM
3272
C2′
THY G
11
20.256
−26.836
−26.215
1.00
24.53
G
C


ATOM
3273
C1′
THY G
11
20.358
−27.248
−24.746
1.00
23.90
G
C


ATOM
3274
N1
THY G
11
20.093
−28.677
−24.366
1.00
21.31
G
N


ATOM
3275
C2
THY G
11
21.003
−29.314
−23.544
1.00
22.11
G
C


ATOM
3276
O2
THY G
11
22.023
−28.796
−23.131
1.00
27.11
G
O


ATOM
3277
N3
THY G
11
20.696
−30.601
−23.208
1.00
20.87
G
N


ATOM
3278
C4
THY G
11
19.583
−31.305
−23.599
1.00
26.65
G
C


ATOM
3279
O4
THY G
11
19.404
−32.466
−23.242
1.00
34.71
G
O


ATOM
3280
C5
THY G
11
18.659
−30.590
−24.453
1.00
22.77
G
C


ATOM
3281
C7
THY G
11
17.411
−31.282
−24.931
1.00
22.15
G
C


ATOM
3282
C6
THY G
11
16.948
−29.321
−24.791
1.00
20.01
G
C


ATOM
3283
P
THY G
12
22.165
−24.182
−27.131
1.00
26.73
G
P


ATOM
3284
OP1
THY G
12
22.786
−22.874
−26.830
1.00
25.84
G
O


ATOM
3285
OP2
THY G
12
21.475
−24.391
−28.426
1.00
33.91
G
O


ATOM
3286
O5′
THY G
12
23.291
−25.310
−26.972
1.00
28.10
G
O


ATOM
3287
C5′
THY G
12
24.116
−25.288
−25.804
1.00
22.77
G
C


ATOM
3288
C4′
THY G
12
24.934
−26.556
−25.716
1.00
25.11
G
C


ATOM
3289
O4′
THY G
12
24.081
−27.685
−25.387
1.00
24.96
G
O


ATOM
3290
C3′
THY G
12
25.642
−26.935
−27.019
1.00
26.10
G
C


ATOM
3291
O3′
THY G
12
26.982
−27.309
−26.745
1.00
26.65
G
O


ATOM
3292
C2′
THY G
12
24.836
−28.135
−27.515
1.00
19.97
G
C


ATOM
3293
C1′
THY G
12
24.544
−28.771
−26.163
1.00
21.80
G
C


ATOM
3294
N1
THY G
12
23.535
−29.859
−26.186
1.00
22.69
G
N


ATOM
3295
C2
THY G
12
23.743
−30.974
−25.393
1.00
23.34
G
C


ATOM
3296
O2
THY G
12
24.706
−31.116
−24.664
1.00
22.76
G
O


ATOM
3297
N3
THY G
12
22.767
−31.929
−25.484
1.00
20.07
G
N


ATOM
3298
C4
THY G
12
21.637
−31.872
−26.270
1.00
20.42
G
C


ATOM
3299
O4
THY G
12
20.824
−32.787
−26.267
1.00
28.04
G
O


ATOM
3300
C5
THY G
12
21.484
−30.682
−27.080
1.00
19.54
G
C


ATOM
3301
C7
THY G
12
20.292
−30.510
−27.982
1.00
20.80
G
C


ATOM
3302
C6
THY G
12
22.431
−29.745
−27.003
1.00
20.75
G
C


ATOM
3303
P
ADE G
13
28.151
−26.224
−26.639
1.00
29.02
G
P


ATOM
3304
OP1
ADE G
13
27.795
−25.263
−25.558
1.00
26.54
G
O


ATOM
3305
OP2
ADE G
13
28.443
−25.746
−28.011
1.00
21.47
G
O


ATOM
3306
O5′
ADE G
13
29.379
−27.113
−26.119
1.00
27.76
G
O


ATOM
3307
C5′
ADE G
13
29.266
−27.784
−24.858
1.00
24.82
G
C


ATOM
3308
O4′
ADE G
13
30.220
−28.968
−24.783
1.00
29.40
G
C


ATOM
3309
O4′
ADE G
13
29.546
−30.226
−25.060
1.00
24.95
G
O


ATOM
3310
C3′
ADE G
13
31.405
−28.915
−25.739
1.00
22.88
G
C


ATOM
3311
O3′
ADE G
13
32.510
−29.502
−25.053
1.00
23.06
G
O


ATOM
3312
C2′
ADE G
13
30.900
−29.716
−26.940
1.00
22.97
G
C


ATOM
3313
C1′
ADE G
13
29.905
−30.707
−26.338
1.00
26.35
G
C


ATOM
3314
N9
ADE G
13
28.659
−30.840
−27.083
1.00
21.00
G
N


ATOM
3315
C8
ADE G
13
28.200
−30.019
−28.074
1.00
18.52
G
C


ATOM
3316
N7
ADE G
13
27.040
−30.383
−28.562
1.00
19.84
G
N


ATOM
3317
C5
ADE G
13
26.706
−31.513
−27.834
1.00
17.67
G
C


ATOM
3318
C6
ADE G
13
25.584
−32.365
−27.868
r.oo
18.34
G
C


ATOM
3319
K6
ADE G
13
24.554
−32.194
−28.711
1.00
17.04
G
N


ATOM
3320
N1
ADE G
13
25.566
−33.405
−27.004
1.00
19.91
G
N


ATOM
3321
C2
ADE G
13
26.602
−33.570
−26.170
1.00
19.44
G
C


ATOM
3322
N3
ADE G
13
27.705
−32.832
−26.046
1.00
18.84
G
N


ATOM
3323
C4
ADE G
13
27.694
−31.809
−26.915
1.00
19.36
G
C


ATOM
3324
P
GUA G
14
33.898
−29.846
−25.771
1.00
32.65
G
P


ATOM
3325
OP1
GUA G
14
34.973
−29.788
−24.754
1.00
32.33
G
O


ATOM
3326
OP2
GUA G
14
33.998
−29.022
−26.998
1.00
23.93
G
O


ATOM
3327
O5′
GUA G
14
33.703
−31.383
−26.160
1.00
26.41
G
O


ATOM
3328
C5′
GUA G
14
33.518
−32.312
−25.103
1.00
26.98
G
C


ATOM
3329
C4′
GUA G
14
33.190
−33.695
−25.629
1.00
35.30
G
C


ATOM
3330
O4′
GUA G
14
31.894
−33.698
−26.284
1.00
35.26
G
O


ATOM
3331
C3′
GUA G
14
34.194
−34.247
−26.636
1.00
38.49
G
C


ATOM
3332
O3′
GUA G
14
34.556
−35.547
−26.198
1.00
42.75
G
O


ATOM
3333
C2′
GUA G
14
33.433
−34.245
−27.963
1.00
35.46
G
C


ATOM
3334
C1′
GUA G
14
31.989
−34.402
−27.503
1.00
32.29
G
C


ATOM
3335
N9
GUA G
14
31.010
−33.838
−28.426
1.00
30.90
G
N


ATOM
3336
C8
GUA G
14
31.116
−32.675
−29.160
1.00
31.45
G
C


ATOM
3337
N7
GUA G
14
30.067
−32.428
−29.899
1.00
29.52
G
N


ATOM
3338
C5
GUA G
14
29.212
−33.493
−29.634
1.00
25.41
G
C


ATOM
3339
C6
GUA G
14
27.926
−33.776
−30.139
1.00
25.42
G
C


ATOM
3340
O6
GUA G
14
27.266
−33.118
−30.948
1.00
29.11
G
O


ATOM
3341
N1
GUA G
14
27.403
−34.958
−29.623
1.00
25.64
G
N


ATOM
3342
C2
GUA G
14
28.047
−35.770
−28.719
1.00
29.50
G
C


ATOM
3343
N2
GUA G
14
27.381
−36.867
−28.331
1.00
29.82
G
N


ATOM
3344
N3
GUA G
14
29.254
−35.516
−28.228
1.00
31.77
G
N


ATOM
3345
C4
GUA G
14
29.774
−34.368
−28.731
1.00
30.52
G
C


ATOM
3346
P
CYT G
15
35.505
−36.506
−27.051
1.00
54.28
G
P


ATOM
3347
OP1
CYT G
15
36.447
−37.139
−26.101
1.00
62.73
G
O


ATOM
3348
OP2
CYT G
15
36.014
−35.772
−28.233
1.00
47.29
G
O


ATOM
3349
O5′
CYT G
15
34.460
−37.607
−27.548
1.00
52.63
G
O


ATOM
3350
C5′
CYT G
15
33.573
−38.181
−26.592
1.00
53.62
G
C


ATOM
3351
C4′
CYT G
15
32.470
−38.966
−27.277
1.00
58.86
G
C


ATOM
3352
O4′
CYT G
15
31.601
−38.072
−28.021
1.00
51.47
G
O


ATOM
3353
C3′
CYT G
15
32.956
−40.011
−28.277
1.00
61.10
G
C


ATOM
3354
O3′
CYT G
15
32.168
−41.184
−28.119
1.00
67.43
G
O


ATOM
3355
C2′
CYT G
15
32.728
−39.339
−29.630
1.00
50.29
G
C


ATOM
3356
C1′
CYT G
15
31.450
−38.562
−29.339
1.00
46.79
G
C


ATOM
3357
N1
CYT G
15
31.213
−37.403
−30.243
1.00
40.11
G
N


ATOM
3358
C2
CYT G
15
30.017
−37.344
−30.967
1.00
34.63
G
C


ATOM
3359
O2
CYT G
15
29.188
−38.259
−30.840
1.00
36.27
G
O


ATOM
3360
N3
CYT G
15
29.803
−36.280
−31.785
1.00
29.35
G
N


ATOM
3361
C4
CYT G
15
30.722
−35.316
−31.891
1.00
33.10
G
C


ATOM
3362
N4
CYT G
15
30.454
−34.295
−32.714
1.00
30.61
G
N


ATOM
3363
CS
CYT G
15
31.949
−35.363
−31.159
1.00
34.90
6
C


ATOM
3364
C6
CYT G
15
32.148
−36.413
−30.354
1.00
36.04
G
C


ATOM
3365
P
THY G
16
32.672
−42.606
−28.657
1.00
78.68
G
P


ATOM
3366
OP1
THY G
16
32.518
−43.562
−27.536
1.00
50.64
G
O


ATOM
3367
OP2
THY G
16
33.979
−42.435
−29.342
1.00
63.43
G
O


ATOM
3368
O5′
THY G
16
31.590
−42.950
−29.783
1.00
70.30
G
O


ATOM
3369
C5′
THY G
16
30.199
−42.830
−29.506
1.00
65.85
G
C


ATOM
3370
C4′
THY G
16
29.414
−43.044
−30.786
1.00
64.65
G
C


ATOM
3371
O4′
THY G
16
29.315
−41.810
−31.544
1.00
56.89
G
O


ATOM
3372
C3′
THY G
16
30.042
−44.052
−31.730
1.00
65.14
G
C


ATOM
3373
O3′
THY G
16
29.007
−44.854
−32.288
1.00
70.25
G
O


ATOM
3374
C2′
THY G
16
30.740
−43.188
−32.771
1.00
55.68
G
C


ATOM
3375
C1′
THY G
16
29.732
−42.051
−32.873
1.00
50.22
G
C


ATOM
3376
N1
THY G
16
30.256
−40.770
−33.414
1.00
47.13
G
N


ATOM
3377
C2
THY G
16
29.417
−40.015
−34.201
1.00
41.96
G
C


ATOM
3378
O2
THY G
16
28.279
−40.363
−34.473
1.00
36.49
G
O


ATOM
3379
N3
THY G
16
29.965
−38.839
−34.656
1.00
36.69
G
N


ATOM
3380
C4
THY G
16
31.240
−38.363
−34.403
1.00
38.39
G
C


ATOM
3381
O4
THY G
16
31.554
−37.296
−34.849
1.00
36.45
G
O


ATOM
3382
C5
THY G
16
32.051
−39.205
−33.574
1.00
39.77
G
C


ATOM
3383
C7
THY G
16
33.458
−38.768
−33.250
1.00
36.90
G
C


ATOM
3384
C6
THY G
16
31.541
−40.355
−33.119
1.00
43.68
G
C


ATOM
3385
P
THY G
17
29.304
−46.363
−32.712
1.00
77.32
G
P


ATOM
3386
OP1
THY G
17
28.327
−47.238
−32.024
1.00
59.40
G
O


ATOM
3387
OP2
THY G
17
30.758
−46.597
−32.559
1.00
72.89
G
O


ATOM
3388
O5′
THY G
17
28.986
−46.342
−34.277
1.00
72.58
G
O


ATOM
3389
C5′
THY G
17
27.648
−46.174
−34.735
1.00
67.07
G
C


ATOM
3390
C4′
THY G
17
27.670
−45.705
−36.178
1.00
67.99
G
C


ATOM
3391
O4′
THY G
17
28.227
−44.366
−36.227
1.00
63.26
G
O


ATOM
3392
C3′
THY G
17
28.524
−46.566
−37.110
1.00
64.72
G
C


ATOM
3393
O3′
THY G
17
27.805
−46.864
−38.302
1.00
70.10
G
O


ATOM
3394
C2′
THY G
17
29.749
−45.700
−37.392
1.00
64.86
G
C


ATOM
3395
C1′
THY G
17
29.155
−44.302
−37.283
1.00
70.81
G
C


ATOM
3396
N1
THY G
17
30.165
−43.280
−36.948
1.00
61.92
G
N


ATOM
3397
C2
THY G
17
29.971
−41.973
−37.348
1.00
54.43
G
C


ATOM
3398
O2
THY G
17
28.988
−41.597
−37.970
1.00
42.14
G
O


ATOM
3399
N3
THY G
17
30.982
−41.118
−36.981
1.00
43.42
G
N


ATOM
3400
C4
THY G
17
32.130
−41.437
−36.279
1.00
45.64
G
C


ATOM
3401
O4
THY G
17
32.978
−40.598
−36.002
1.00
48.61
G
O


ATOM
3402
C5
THY G
17
32.264
−42.821
−35.897
1.00
61.56
G
C


ATOM
3403
C7
THY G
17
33.471
−43.283
−35.133
1.00
68.79
G
C


ATOM
3404
C6
THY G
17
31.288
−43.667
−36.248
1.00
58.84
G
C


TER


ATOM
3405
O5′
THY H
1
35.925
−36.030
−41.955
1.00
32.94
H
O


ATOM
3406
C5′
THY H
1
36.090
−35.750
−43.338
1.00
26.10
H
C


ATOM
3407
C4′
THY H
1
34.748
−35.736
−44.051
1.00
24.93
H
C


ATOM
3408
O4′
THY H
1
34.124
−37.044
−43.969
1.00
26.72
H
O


ATOM
3409
C3′
THY H
1
33.737
−34.740
−43.496
1.00
26.47
H
C


ATOM
3410
O3′
THY H
1
33.035
−34.134
−44.575
1.00
27.28
H
O


ATOM
3411
C2′
THY H
1
32.837
−35.598
−42.606
1.00
30.24
H
C


ATOM
3412
C1′
THY H
1
32.898
−36.976
−43.266
1.00
26.52
H
C


ATOM
3413
N1
THY H
1
32.836
−38.138
−42.310
1.00
25.05
H
N


ATOM
3414
C2
THY H
1
31.673
−38.878
−42.229
1.00
24.12
H
C


ATOM
3415
O2
THY H
1
30.678
−38.651
−42.891
1.00
29.79
H
O


ATOM
3416
N3
THY H
1
31.702
−39.913
−41.338
1.00
21.97
H
N


ATOM
3417
C4
THY H
1
32.752
−40.277
−40.528
1.00
24.78
H
C


ATOM
3418
O4
THY H
1
32.673
−41.229
−39.761
1.00
30.41
H
O


ATOM
3419
C5
THY H
1
33.938
−39.466
−40.649
1.00
23.79
H
C


ATOM
3420
C7
THY H
1
35.133
−39.787
−39.804
1.00
30.54
H
C


ATOM
3421
C6
THY H
1
33.930
−38.445
−41.520
1.00
24.66
H
C


ATOM
3422
P
ADE H
2
32.281
−32.738
−44.373
1.00
39.81
H
P


ATOM
3423
OP1
ADE H
2
32.238
−32.023
−45.662
1.00
40.11
H
O


ATOM
3424
OP2
ADE H
2
32.845
−32.071
−43.182
1.00
31.36
H
O


ATOM
3425
O5′
ADE H
2
30.800
−33.199
−44.012
1.00
38.96
H
O


ATOM
3426
C5′
ADE H
2
30.137
−34.174
−44.793
1.00
26.70
H
C


ATOM
3427
C4′
ADE H
2
28.912
−34.646
−44.031
1.00
33.63
H
C


ATOM
3428
O4′
ADE H
2
29.305
−35.527
−42.943
1.00
38.83
H
O


ATOM
3429
C3′
ADE H
2
28.096
−33.540
−43.370
1.00
35.55
H
C


ATOM
3430
O3′
ADE H
2
26.752
−33.943
−43.445
1.00
42.10
H
O


ATOM
3431
C2′
ADE H
2
28.613
−33.534
−41.931
1.00
30.13
H
C


ATOM
3432
C1′
ADE H
2
28.809
−35.029
−41.713
1.00
30.36
H
C


ATOM
3433
N9
ADE H
2
29.756
−35.402
−40.663
1.00
26.40
H
N


ATOM
3434
C8
ADE H
2
30.726
−34.630
−40.086
1.00
28.73
H
C


ATOM
3435
N7
ADE H
2
31.427
−35.260
−39.165
1.00
28.81
H
N


ATOM
3436
C5
ADE H
2
30.880
−36.532
−39.142
1.00
26.92
H
C


ATOM
3437
C6
ADE H
2
31.167
−37.686
−38.387
1.00
25.71
H
C


ATOM
3438
N6
ADE H
2
32.131
−37.739
−37.469
1.00
28.67
H
N


ATOM
3439
N1
ADE H
2
30.426
−38.793
−38.610
1.00
25.67
H
N


ATOM
3440
C2
ADE H
2
29.461
−38.747
−39.531
1.00
24.75
H
C


ATOM
3441
N3
ADE H
2
29.102
−37.723
−40.302
1.00
26.66
H
N


ATOM
3442
C4
ADE H
2
29.853
−36.636
−40.060
1.00
27.31
H
C


ATOM
3443
P
ADE H
3
25.537
−32.924
−43.269
1.00
37.68
H
P


ATOM
3444
OP1
ADE H
3
25.052
−32.573
−44.625
1.00
39.11
H
O


ATOM
3445
OP2
ADE H
3
25.908
−31.868
−42.298
1.00
36.68
H
O


ATOM
3446
O5′
ADE H
3
24.475
−33.891
−42.568
1.00
30.66
H
O


ATOM
3447
C5′
ADE H
3
24.342
−35.214
−43.063
1.00
30.61
H
C


ATOM
3448
C4′
ADE H
3
23.861
−35.132
−41.960
1.00
27.07
H
C


ATOM
3449
O4′
ADE H
3
24.945
−36.425
−41.041
1.00
27.15
H
O


ATOM
3450
C3′
ADE H
3
22.734
−35.546
−41.114
1.00
38.17
H
C


ATOM
3451
O3′
ADE H
3
21.727
−36.533
−40.943
1.00
35.18
H
O


ATOM
3452
C2′
ADE H
3
23.406
−35.175
−39.787
1.00
31.35
H
C


ATOM
3453
C1′
ADE H
3
24.503
−36.233
−39.709
1.00
34.45
H
C


ATOM
3454
N9
ADE H
3
25.666
−35.869
−38.903
1.00
26.51
H
N


ATOM
3455
C8
ADE H
3
26.333
−34673
−38.872
1.00
28.15
H
C


ATOM
3456
N7
ADE H
3
27.358
−34.655
−38.047
1.00
28.07
H
N


ATOM
3457
C5
ADE H
3
27.364
−35.933
−37.502
1.00
27.87
H
C


ATOM
3458
C6
ADE H
3
28.197
−36.572
−36.559
1.00
24.49
H
C


ATOM
3459
N6
ADE H
3
29.238
−35.984
−35.964
1.00
28.81
H
N


ATOM
3460
M1
ADE H
3
27.912
−37.853
−36.241
1.00
27.07
H
N


ATOM
3461
C2
ADE H
3
26.869
−38.458
−36.826
1.00
26.59
H
C


ATOM
3462
N3
ADE H
3
26.022
−37.964
−37.727
1.00
28.66
H
N


ATOM
3463
C4
ADE H
3
26.325
−36.690
−38.022
1.00
28.33
H
C


ATOM
3464
P
GUA H
4
20.373
−36.128
−40.204
1.00
38.36
H
P


ATOM
3465
OP1
GUA H
4
19.287
−36.963
−40.758
1.00
32.04
H
O


ATOM
3466
OP2
GUA H
4
20.290
−34.647
−40.237
1.00
39.60
H
O


ATOM
3467
O5′
GUA H
4
20.659
−36.603
−38.696
1.00
40.06
H
O


ATOM
3468
C5′
GUA H
4
20.817
−38.005
−38.466
1.00
36.35
H
C


ATOM
3469
C4′
GUA H
4
21.469
−38.332
−37.131
1.00
39.32
H
C


ATOM
3470
O4′
GUA H
4
22.664
−37.542
−36.913
1.00
41.95
H
O


ATOM
3471
C3′
GUA H
4
20.607
−38.121
−35.888
1.00
50.29
H
C


ATOM
3472
O3′
GUA H
4
20.415
−39.409
−35.314
1.00
52.14
H
O


ATOM
3473
C2′
GUA H
4
21.433
−37.180
−35.000
1.00
39.71
H
C


ATOM
3474
C1′
GUA H
4
22.845
−37.449
−35.516
1.00
37.91
H
C


ATOM
3475
N9
GUA H
4
23.873
−36.430
−35.285
1.00
34.32
H
N


ATOM
3476
C8
GUA H
4
23.917
−35.163
−35.816
1.00
32.75
H
C


ATOM
3477
N7
GUA H
4
24.967
−34.480
−35.455
1.00
32.33
H
N


ATOM
3478
C5
GUA H
4
25.678
−35.349
−34.635
1.00
32.09
H
C


ATOM
3479
C6
GUA H
4
26.908
−35.161
−33.949
1.00
29.46
H
C


ATOM
3480
O6
GUA H
4
27.644
−34.161
−33.920
1.00
27.01
H
O


ATOM
3481
M1
GUA H
4
27.269
−36.298
−33.234
1.00
30.36
H
N


ATOM
3482
C2
GUA H
4
26.540
−37.459
−33.182
1.00
33.51
H
C


ATOM
3483
N2
GUA H
4
27.060
−38.439
−32.431
1.00
38.20
H
N


ATOM
3484
N3
GUA H
4
25.387
−37.649
−33.815
1.00
32.09
H
N


ATOM
3485
C4
GUA H
4
25.018
−36.555
−34.524
1.00
33.22
H
C


ATOM
3486
P
CYT H
5
19.453
−39.649
−34.057
1.00
55.11
H
P


ATOM
3487
OP1
CYT H
5
18.684
−40.887
−34.324
1.00
35.30
H
O


ATOM
3488
OP2
CYT H
5
18.767
−38.374
−33.738
1.00
41.73
H
O


ATOM
3489
O5′
CYT H
5
20.505
−39.951
−32.890
1.00
44.98
H
O


ATOM
3490
C5′
CYT H
5
21.501
−40.935
−33.116
1.00
36.84
H
C


ATOM
3491
C4′
CYT H
5
22.377
−41.096
−31.890
1.00
34.69
H
C


ATOM
3492
O4′
CYT H
5
23.328
−40.005
−31.777
1.00
30.60
H
O


ATOM
3493
C3′
CYT H
5
21.623
−41.133
−30.569
1.00
32.70
H
C


ATOM
3494
O3′
CYT H
5
22.280
−42.089
−29.765
1.00
38.87
H
O


ATOM
3495
C2′
CYT H
5
21.779
−39.706
−30.040
1.00
29.93
H
C


ATOM
3496
C1′
CYT H
5
23.178
−39.355
−30.530
1.00
30.85
H
C


ATOM
3497
N1
CYT H
5
23.446
−37.923
−30.818
1.00
32.57
H
N


ATOM
3498
C2
CYT H
5
24.513
−37.289
−30.181
1.00
28.31
H
C


ATOM
3499
O2
CYT H
5
25.194
−37.930
−29.371
1.00
30.53
H
O


ATOM
3500
N3
CYT H
5
24.771
−35.990
−30.466
1.00
29.17
H
N


ATOM
3501
C4
CYT H
5
24.015
−35.331
−31.345
1.00
28.71
H
C


ATOM
3502
N4
CYT H
5
24.319
−34.049
−31.580
1.00
26.57
H
N


ATOM
3503
CS
CYT H
5
22.920
−35.958
−32.012
1.00
26.39
H
C


ATOM
3504
C6
CYT H
5
22.679
−37.244
−31.724
1.00
34.07
H
C


ATOM
3505
P
THY H
6
21.626
−42.654
−28.425
1.00
47.41
H
P


ATOM
3506
QP1
THY H
6
22.056
−44.059
−28.267
1.00
51.76
H
O


ATOM
3507
OP2
THY H
6
20.184
−42.310
−28.415
1.00
50.29
H
O


ATOM
3508
O5′
THY H
6
22.348
−41.762
−27.313
1.00
46.65
H
O


ATOM
3509
C5′
THY H
6
23.725
−41.957
−27.019
1.00
43.24
H
C


ATOM
3510
C4′
THY H
6
24.116
−41.139
−25.804
1.00
39.41
H
C


ATOM
3511
O4′
THY H
6
24.396
−39.776
−26.215
1.00
42.16
H
O


ATOM
3512
C3′
THY H
6
23.026
−41.017
−24.750
1.00
40.48
H
C


ATOM
3513
O3′
THY H
6
23.617
−40.802
−23.485
1.00
46.66
H
O


ATOM
3514
C2′
THY H
6
22.315
−39.745
−25.192
1.00
41.24
H
C


ATOM
3515
C1′
THY H
6
23.550
−38.906
−25.486
1.00
42.05
H
C


ATOM
3516
N1
THY H
6
23.298
−37.688
−26.293
1.00
34.71
H
N


ATOM
3517
C2
THY H
6
24.259
−36.704
−26.309
1.00
34.93
H
C


ATOM
3518
O2
THY H
6
25.305
−36.793
−25.692
1.00
37.85
H
O


ATOM
3519
N3
THY H
6
23.951
−35612
−27.080
1.00
31.24
H
H


ATOM
3520
C4
THY H
6
22.797
−35.421
−27.816
1.00
31.75
H
C


ATOM
3521
O4
THY H
6
22.607
−34.408
−28.479
1.00
30.53
H
O


ATOM
3522
C5
THY H
6
21.830
−36.489
−27.749
1.00
32.63
H
C


ATOM
3523
C7
THY H
6
20.538
−36.385
−28.507
1.00
28.89
H
C


ATOM
3524
C6
THY H
6
22.122
−37.560
−27.000
1.00
31.00
H
C


ATOM
3525
P
ADE H
7
23.900
−42.022
−22.497
1.00
44.28
H
P


ATOM
3526
OP1
ADE H
7
24.428
−43.144
−23.303
1.00
40.56
H
O


ATOM
3527
OP2
ADE H
7
22.691
−42.211
−21.665
1.00
44.27
H
O


ATOM
3528
O5′
ADE H
7
25.065
−41.436
−21.569
1.00
32.81
H
O


ATOM
3529
C5′
ADE H
7
25.365
−41.293
−22.115
1.00
32.80
H
C


ATOM
3530
C4′
ADE H
7
27.031
−40.015
−21.640
1.00
35.14
H
C


ATOM
3531
O4′
ADE H
7
26.448
−38.855
−22.294
1.00
37.44
H
O


ATOM
3532
C3′
ADE H
7
26.918
−39.744
−20.149
1.00
38.41
H
C


ATOM
3533
O3′
ADE H
7
28.144
−39.153
−19.715
1.00
38.15
H
O


ATOM
3534
C2′
ADE H
7
25.717
−38.794
−20.060
1.00
35.26
H
C


ATOM
3535
C1′
ADE H
7
25.863
−37.980
−21.345
1.00
37.50
H
C


ATOM
3536
N9
ADE H
7
24.621
−37.499
−21.953
1.00
30.16
H
N


ATOM
3537
C8
ADE H
7
23.424
−38.156
−22.049
1.00
32.36
H
C


ATOM
3538
N7
ADE H
7
22.490
−37.470
−22.674
1.00
33.29
H
N


ATOM
3539
C5
ADE H
7
23.119
−36.283
−23.023
1.00
27.61
H
C


ATOM
3540
C6
ADE H
7
22.680
−35.129
−23.709
1.00
23.15
H
C


ATOM
3541
N6
ADE H
7
21.441
−34.976
−24.190
1.00
21.35
H
N


ATOM
3542
N1
ADE H
7
23.570
−34.127
−23.879
1.00
23.18
H
N


ATOM
3543
C2
ADE H
7
24.810
−34.274
−23.404
1.00
24.54
H
C


ATOM
3544
N3
ADE H
7
25.341
−35.308
−22.749
1.00
29.70
H
N


ATOM
3545
C4
ADE H
7
24.435
−36.289
−22.588
1.00
31.92
H
C


ATOM
3546
P
ADE H
8
28.347
−38.809
−18.169
1.00
58.35
H
P


ATOM
3547
OP1
ADE H
8
29.786
−38.970
−17.855
1.00
45.52
H
O


ATOM
3548
OP2
ADE H
8
27.304
−39.547
−17.411
1.00
40.27
H
O


ATOM
3549
O5′
ADE H
8
27.993
−37.253
−18.109
1.00
41.83
H
O


ATOM
3550
C5′
ADE H
8
28.734
−36.350
−18.906
1.00
41.53
H
C


ATOM
3551
C4′
ADE H
8
28.065
−34.991
−18.913
1.00
43.43
H
C


ATOM
3552
O4′
ADE H
8
26.830
−35.073
−19.655
1.00
44.70
H
O


ATOM
3553
C3′
ADE H
8
27.682
−34.434
−17.544
1.00
38.12
H
C


ATOM
3554
O3′
ADE H
8
28.599
−33.402
−17.223
1.00
36.90
H
O


ATOM
3555
C2′
ADE H
8
26.262
−33.896
−17.724
1.00
35.36
H
C


ATOM
3556
C1′
ADE H
8
26.032
−33.996
−19.228
1.00
37.49
H
C


ATOM
3557
N9
ADE H
8
24.652
−34.286
−19.603
1.00
36.04
H
N


ATOM
3558
C8
ADE H
8
23.938
−35.416
−19.312
1.00
35.51
H
C


ATOM
3559
N7
ADE H
8
22.715
−35.408
−19.784
1.00
34.40
H
N


ATOM
3560
C5
ADE H
8
22.625
−34.186
−20.427
1.00
31.66
H
C


ATOM
3561
C6
ADE H
8
21.576
−33.572
−21.130
1.00
36.96
H
C


ATOM
3562
N6
ADE H
8
20.385
−34.157
−21.290
1.00
32.17
H
N


ATOM
3563
N1
ADE H
8
21.802
−32.347
−21.657
1.00
34.88
H
N


ATOM
3564
C2
ADE H
8
23.006
−31.781
−21.483
1.00
38.52
H
C


ATOM
3565
N3
ADE H
8
24.074
−32.262
−20.837
1.00
32.76
H
N


ATOM
3566
C4
ADE H
8
23.809
−33.480
−20.330
1.00
33.22
H
C


ATOM
3567
P
THY H
9
28.397
−32.411
−15.982
1.00
36.15
H
P


ATOM
3568
OP1
THY H
9
29.753
−32.044
−15.512
1.00
28.93
H
O


ATOM
3563
OP2
THY H
9
27.402
−32.984
−15.044
1.00
34.70
H
O


ATOM
3570
O5′
THY H
9
27.768
−31.124
−16.688
1.00
32.97
H
O


ATOM
3571
C5′
THY H
9
28.548
−30.497
−17.690
1.00
33.48
H
C


ATOM
3572
C4′
THY H
9
27.801
−29.333
−18.307
1.00
31.92
H
C


ATOM
3573
O4′
THY H
9
26.530
−29.798
−18.818
1.00
25.84
H
O


ATOM
3574
C3′
THY H
9
27.493
−28.172
−17.365
1.00
26.38
H
C


ATOM
3575
O3′
THY H
9
27.716
−26.976
−18.100
1.00
25.95
H
O


ATOM
3576
C2′
THY H
9
26.025
−28.395
−16.999
1.00
24.26
H
C


ATOM
3577
C1′
THY H
9
25.491
−29.001
−18.293
1.00
25.25
H
C


ATOM
3578
N1
THY H
9
24.315
−29.902
−18.168
1.00
23.43
H
N


ATOM
3579
C2
THY H
9
23.279
−29.705
−19.043
1.00
25.36
H
C


ATOM
3580
O2
THY H
9
23.298
−28.825
−19.883
1.00
27.24
H
O


ATOM
3581
N3
THY H
9
22.230
−30.577
−18.888
1.00
26.75
H
N


ATOM
3582
C4
THY H
9
22.123
−31.604
−17.968
1.00
24.08
H
C


ATOM
3583
O4
THY H
9
21.143
−32.337
−17.900
1.00
25.41
H
O


ATOM
3584
C5
THY H
9
23.243
−31.757
−17.084
1.00
25.32
H
C


ATOM
3585
C7
THY H
9
23.213
−32.843
−16.047
1.00
24.63
H
C


ATOM
3586
C6
THY H
9
24.278
−30.911
−17.223
1.00
25.76
H
C


ATOM
3587
P
ADE H
10
27.345
−25.528
−17.528
1.00
25.05
H-
P


ATOM
3588
OP1
ADE H
10
28.142
−24.542
−18.294
1.00
24.87
H
O


ATOM
3589
OP2
ADE H
10
27.446
−25.572
−16.053
1.00
32.93
H
O


ATOM
3590
O5′
ADE H
10
25.801
−25.365
−17.942
1.00
36.94
H
O


ATOM
3591
C5′
ADE H
10
25.438
−25.334
−19.320
1.00
27.06
H
C


ATOM
3592
C4′
ADE H
10
24.104
−24.641
−19.578
1.00
21.71
H
C


ATOM
3593
O4′
ADE H
10
22.992
−25.552
−19.403
1.00
23.14
H
O


ATOM
3594
C3′
ADE H
10
23.766
−23.430
−18.718
1.00
26.15
H
C


ATOM
3525
O3′
ADE H
10
23.199
−22.479
−19.609
1.00
22.80
H
O


ATOM
3596
C2′
ADE H
10
22.770
−23.973
−17.689
1.00
21.76
H
C


ATOM
3597
C1′
ADE H
10
22.042
−25.053
−18.482
1.00
22.72
H
C


ATOM
3598
N9
ADE H
10
21.627
−26.239
−17.736
1.00
25.17
H
H


ATOM
3599
C8
ADE H
10
22.386
−26.936
−16.836
1.00
21.36
H
C


ATOM
3600
N7
ADE H
10
21.773
−27.981
−16.336
1.00
23.59
H
N


ATOM
3601
C5
ADE H
10
20.529
−27.975
−16.953
1.00
20.38
H
C


ATOM
3602
C6
ADE H
10
19.407
−28.827
−16.848
1.00
23.03
H
C


ATOM
3603
N6
ADE H
10
19.372
−29.896
−16.046
1.00
23.54
H
N


ATOM
3604
N1
ADE H
10
18.319
−28.541
−17.599
1.00
21.58
H
N


ATOM
3605
C2
ADE H
10
18.362
−27.467
−18.396
1.00
22.37
H
C


ATOM
3606
N3
ADE H
10
19.360
−26.599
−18.579
1.00
22.34
H
N


ATOM
3607
C4
ADE H
10
20.426
−26.909
−17.824
1.00
19.27
H
C


ATOM
3608
P
ADE H
11
22.583
−21.095
−19.118
1.00
26.29
H
P


ATOM
3609
OP1
ADE H
11
22.825
−20.107
−20.187
1.00
33.92
H
O


ATOM
3610
OP2
ADE H
11
23.049
−20.823
−17.739
1.00
23.74
H
O


ATOM
3611
O5′
ADE H
11
21.019
−21.433
−19.082
1.00
30.07
H
O


ATOM
3612
C5′
ADE H
11
20.386
−21.868
−20.271
1.00
23.89
H
C


ATOM
3613
C4′
ADE H
11
18.893
−22.085
−20.087
1.00
26.01
H
C


ATOM
3614
O4′
ADE H
11
18.646
−23.201
−19.196
1.00
21.90
H
O


ATOM
3615
C3′
ADE H
11
18.092
−20.920
−19.519
1.00
27.43
H
C


ATOM
3616
O3′
ADE H
11
16.835
−20.955
−20.172
1.00
27.25
H
O


ATOM
3617
C2′
ADE H
11
17.979
−21.286
−18.042
1.00
22.72
H
C


ATOM
3618
C1′
ADE H
11
17.810
−22.801
−18.134
1.00
25.26
H
C


ATOM
3619
H9
ADE H
11
18.307
−23.581
−17.012
1.00
25.82
H
N


ATOM
3620
C8
ADE H
11
19.473
−23.388
−16.320
1.00
25.44
H
C


ATOM
3621
N7
ADE H
11
19.678
−24.271
−15.368
1.00
26.30
H
N


ATOM
3622
C5
ADE H
11
18.573
−25.103
−15.458
1.00
24.43
H
C


ATOM
3623
C6
ADE H
11
18.193
−26.240
−14.727
1.00
27.00
H
C


ATOM
3624
N6
ADE H
11
18.934
−26.728
−13.724
1.00
30.82
H
N


ATOM
3625
N1
ADE H
11
17.027
−26.842
−15.058
1.00
26.79
H
N


ATOM
3626
C2
ADE H
11
16.298
−26.332
−16.063
1.00
27.42
H
C


ATOM
3627
N3
ADE H
11
16.557
−25.265
−16.826
1.00
24.29
H
N


ATOM
3628
C4
ADE H
11
17.720
−24.697
−16.468
1.00
22.11
H
C


ATOM
3629
P
THY H
12
15.843
−19.698
−20.193
1.00
25.52
H
P


ATOM
3630
OP1
THY H
12
15.307
−19.601
−21.571
1.00
25.80
H
O


ATOM
3631
OP2
THY H
12
16.525
−18.534
−19.586
1.00
21.54
H
O


ATOM.
3632
O5′
THY H
12
14.679
−20.166
−19.189
1.00
24.83
H
O


ATOM
3633
C5′
THY H
12
13.875
−21.310
−19.552
1.00
23.42
H
C


ATOM
3634
C4′
THY H
12
13.066
−21.839
−18.381
1.00
25.89
H
C


ATOM
3635
O4′
THY H
12
13.908
−22.629
−17.499
1.00
23.76
H
O


ATOM
3636
C3′
THY H
12
12.424
−20.761
−17.504
1.00
26.04
H
C


ATOM
3637
O3′
THY H
12
11.060
−21.064
−17.263
1.00
25.66
H
O


ATOM
3638
C2′
THY H
12
13.230
−20.844
−16.208
1.00
20.86
H
C


ATOM
3639
C1′
THY H
12
13.490
−22.343
−16.179
1.00
22.54
H
C


ATOM
3640
N1
THY H
12
14.533
−22.765
−15.212
1.00
22.51
H
N


ATOM
3641
C2
THY H
12
14.403
−23.972
−14.554
1.00
23.00
H
C


ATOM
3642
O2
THY H
12
13.472
−24.737
−14.721
1.00
21.72
H
O


ATOM
3643
N3
THY H
12
15.419
−24.266
−13.684
1.00
20.48
H
N


ATOM
3644
C4
THY H
12
16.523
−23.486
−13.419
1.00
20.15
H
C


ATOM
3645
O4
THY H
12
17.373
−23.849
−12.617
1.00
25.63
H
O


ATOM
3646
C5
THY H
12
16.597
−22.234
−14.136
1.00
18.49
H
C


ATOM
3647
C7
THY H
12
17.746
−21.289
−13.933
1.00
19.45
H
C


ATOM
3648
C6
THY H
12
15.613
−21.936
−14.987
1.00
18.74
H
C


ATOM
3649
P
ADE H
13
9.921
−20.818
−18.362
1.00
34.68
H
P


ATOM
3650
OP1
ADE H
13
10.331
−21.523
−19.601
1.00
29.00
H
O


ATOM
3651
OP2
ADE H
13
9.602
−19.371
−18.385
1.00
23.43
H
O


ATOM
3652
O5′
ADE H
13
8.680
−21.612
−17.735
1.00
31.48
H
O


ATOM
3653
C5′
ADE H
13
8.703
−23.042
−17.751
1.00
29.17
H
C


ATOM
3654
C4′
ADE H
13
7.813
−23.633
−16.668
1.00
34.37
H
C


ATOM
3655
O4′
ADE H
13
8.562
−23.903
−15.452
1.00
29.36
H
O


ATOM
3656
C3′
ADE H
13
6.624
−22.779
−16.250
1.00
24.78
H
C


ATOM
3657
O3′
ADE H
13
5.562
−23.684
−15.966
1.00
27.24
H
O


ATOM
3658
C2′
ADE H
13
7.157
−22.038
−15.022
1.00
23.76
H
C


ATOM
3659
C1′
ADE H
13
8.208
−22.983
−14.437
1.00
26.59
H
C


ATOM
3660
N9
ADE H
13
9.444
−22.331
−14.012
1.00
23.20
H
N


ATOM
3661
C8
ADE H
13
9.886
−21.086
−14.361
1.00
19.68
H
C


ATOM
3662
N7
ADE H
13
11.043
−20.769
−13.826
1.00
21.48
H
N


ATOM
3663
C5
ADE H
13
11.394
−21.887
−13.084
1.00
20.04
H
C


ATOM
3664
C6
ADE H
13
12.518
−22.191
−12.283
1.00
20.93
H
C


ATOM
3665
N6
ADE H
13
13.542
−21.349
−12.085
1.00
17.98
H
N


ATOM
3666
N1
ADE H
13
12.548
−23.401
−11.684
1.00
21.14
H
N


ATOM
3667
C2
ADE H
13
11.525
−24.241
−11.878
1.00
21.71
H
C


ATOM
3668
N3
ADE H
13
10.422
−24.069
−12.608
1.00
21.94
H
N


ATOM
3669
C4
ADE H
13
10.437
−22.860
−13.191
1.00
21.50
H
C


ATOM
3670
P
GUA H
14
4.132
−23.212
−15.419
1.00
31.73
H
P


ATOM
3671
OP1
GUA H
14
3.121
−24.184
−15.895
1.00
30.37
H
O


ATOM
3672
OP2
GUA H
14
3.978
−21.769
−15.712
1.00
29.29
H
O


ATOM
3673
O5′
GUA H
14
4.287
−23.434
−13.842
1.00
22.88
H
O


ATOM
3674
C5′
GUA H
14
4.449
−24.775
−13.402
1.00
30.01
H
C


ATOM
3675
C4′
GUA H
14
4.825
−24.840
−11.937
1.00
36.42
H
C


ATOM
3676
O4′
GUA H
14
6.132
−24.244
−11.745
1.00
33.71
H
O


ATOM
3677
C3′
GUA H
14
3.857
−24.124
−11.000
1.00
42.57
H
C


ATOM
3678
O3′
GUA H
14
3.409
−25.076
−10.033
1.00
51.87
H
O


ATOM
3679
C2′
GUA H
14
4.680
−22.978
−10.410
1.00
36.34
H
C


ATOM
3680
C1′
GUA H
14
6.119
−23.462
−10.575
1.00
30.10
H
C


ATOM
3681
N9
GUA H
14
7.096
−22.389
−10.734
1.00
29.80
H
N


ATOM
3682
C8
GUA H
14
6.985
−21.257
−11.508
1.00
28.65
H
C


ATOM
3683
N7
GUA H
14
8.033
−20.476
−11.442
1.00
26.36
H
N


ATOM
3684
C5
GUA H
14
8.890
−21.137
−10.574
1.00
23.38
H
C


ATOM
3685
C6
GUA H
14
10.174
−20.779
−10.118
1.00
25.14
H
C


ATOM
3686
O6
GUA H
14
10.832
−19.768
−10.404
1.00
27.81
H
O


ATOM
3687
N1
GUA H
14
10.694
−21.728
−9.239
1.00
24.30
H
N


ATOM
3688
C2
GUA H
14
10.052
−22.880
−8.854
1.00
28.25
H
C


ATOM
3689
N2
GUA H
14
10.706
−23.682
−8.003
1.00
28.77
H
N


ATOM
3690
N3
GUA H
14
8.849
−23.227
−9.279
1.00
31.04
H
N


ATOM
3691
C4
GUA H
14
8.330
−22.312
−10.131
1.00
29.88
H
C


ATOM
3692
P
CYT H
15
2.723
−24.657
−8.650
1.00
56.18
H
P


ATOM
3693
OP1
CYT H
15
1.801
−25.752
−8.276
1.00
65.42
H
O


ATOM
3694
OP2
CYT H
15
2.225
−23.265
−8.747
1.00
43.75
H
O


ATOM
3695
O5′
CYT H
15
3.957
−24.676
−7.638
1.00
59.78
H
O


ATOM
3696
C5′
CYT H
15
4.712
−25.868
−7.488
1.00
59.36
H
C


ATOM
3697
C4′
CYT H
15
5.779
−25.661
−6.431
1.00
62.35
H
C


ATOM
3698
O4′
CYT H
15
6.708
−24.634
−6.865
1.00
55.00
H
O


ATOM
3699
C3′
CYT H
15
5.233
−25.203
−5.085
1.00
62.43
H
C


ATOM
3700
O3′
CYT H
15
5.951
−25.845
−4.045
1.00
67.79
H
O


ATOM
3701
C2′
CYT H
15
5.457
−23.692
−5.113
1.00
53.40
H
C


ATOM
3702
C1′
CYT H
15
6.753
−23.591
−5.910
1.00
48.72
H
C


ATOM
3703
N1
CYT H
15
6.917
−22.294
−6.633
1.00
40.77
H
N


ATOM
3704
C2
CYT H
15
8.077
−21.547
−6.422
1.00
37.46
H
C


ATOM
3705
O2
CYT H
15
8.931
−21.987
−5.643
1.00
37.14
H
O


ATOM
3706
N3
CYT H
15
8.232
−20.370
−7.075
1.00
31.15
H
N


ATOM
3707
C4
CYT H
15
7.280
−19.941
−7.906
1.00
35.33
H
C


ATOM
3708
N4
CYT H
15
7.478
−18.772
−8.528
1.00
30.93
H
N


ATOM
3709
C5
CYT H
15
6.084
−20.690
−8.137
1.00
34.65
H
C


ATOM
3710
C6
CYT H
15
5.946
−21.850
−7.485
1.00
36.08
H
C


ATOM
3711
P
THY H
16
5.394
−25.882
−2.548
1.00
79.66
H
P


ATOM
3712
OP1
THY H
16
5.429
−27.295
−2.109
1.00
68.24
H
O


ATOM
3713
OP2
THY H
16
4.135
−25.097
−2.487
1.00
58.67
H
O


ATOM
3714
O5′
THY H
16
6.493
−25.054
−1.734
1.00
73.70
H
Q


ATOM
3715
C5′
THY H
16
7.875
−25.332
−1.897
1.00
64.00
H
C


ATOM
3716
C4′
THY H
16
8.688
−24.210
−1.280
1.00
60.98
H
C


ATOM
3717
O4′
THY H
16
8.737
−23.062
−2.166
1.00
55.58
H
O


ATOM
3718
C3′
THY H
16
8.136
−23.697
0.047
1.00
64.34
H
C


ATOM
3719
O3′
THY H
16
9.212
−23.604
0.971
1.00
64.61
H
O


ATOM
3720
C2′
THY H
16
7.538
−22.334
−0.308
1.00
58.02
H
C


ATOM
3721
C1′
THY H
16
8.491
−21.892
−1.412
1.00
48.05
H
C


ATOM
3722
N1
THY H
16
7.964
−20.856
−2.347
1.00
44.06
H
N


ATOM
3723
C2
THY H
16
8.769
−19.783
−2.664
1.00
41.43
H
C


ATOM
3724
O2
THY H
16
9.893
−19.629
−2.209
1.00
36.22
H
O


ATOM
3725
N3
THY H
16
8.205
−18.887
−3.539
1.00
36.83
H
N


ATOM
3726
C4
THY H
16
6.950
−18.959
−4.114
1.00
37.73
H
C


ATOM
3727
O4
THY H
16
6.531
−18.106
−4.890
1.00
38.17
H
O


ATOM
3728
C5
THY H
16
6.164
−20.105
−3.738
1.00
39.00
H
C


ATOM
3729
C7
THY H
16
4.787
−20.274
−4.306
1.00
36.71
H
C


ATOM
3730
C6
THY H
16
6.700
−20.990
−2.886
1.00
42.86
H
C


ATOM
3731
P
THY H
17
8.919
−23.580
2.540
1.00
80.14
H
P


ATOM
3732
OP1
THY H
17
9.864
−24.510
3.199
1.00
54.65
H
O


ATOM
3733
OP2
THY H
17
7.458
−23.738
2.723
1.00
73.46
H
O


ATOM
3734
O5′
THY H
17
9.297
−22.079
2.943
1.00
75.28
H
O


ATOM
3735
C5′
THY H
17
10.651
−21.640
2.934
1.00
69.65
H
C


ATOM
3736
C4′
THY H
17
10.703
−20.132
3.111
1.00
70.06
H
C


ATOM
3737
O4′
THY H
17
10.081
−19.502
1.961
1.00
61.48
H
O


ATOM
3738
C3′
THY H
17
9.974
−19.599
4.346
1.00
63.21
H
C


ATOM
3739
O3′
THY H
17
10.758
−18.600
4.997
1.00
62.30
H
O


ATOM
3740
C2′
THY H
17
8.674
−19.028
3.783
1.00
62.44
H
C


ATOM
3741
C1′
THY H
17
9.119
−18.566
2.400
1.00
65.67
H
C


ATOM
3742
N1
THY H
17
8.020
−18.547
1.409
1.00
62.67
H
N


ATOM
3743
C2
THY H
17
8.090
−17.678
0.342
1.00
57.28
H
C


ATOM
3744
O2
THY H
17
9.023
−16.913
0.165
1.00
46.63
H
O


ATOM
3745
N3
THY H
17
7.019
−17.741
−0.515
1.00
45.14
H
N


ATOM
3746
C4
THY H
17
5.915
−18.568
−0.407
1.00
46.53
H
C


ATOM
3747
O4
THY H
17
5.002
−18.549
−1.227
1.00
52.84
H
O


ATOM
3748
C5
THY H
17
5.910
−19.451
0.738
1.00
55.61
H
C


ATOM
3749
C7
THY H
17
4.766
−20.397
0.969
1.00
59.50
H
C


ATOM
3750
C6
THY H
17
6.950
−19.398
1.581
1.00
61.26
H
C


ATOM
1
C1
BML
100
1.351
−22.636
17.329
1.00
20.00

C


ATOM
2
N1
BML
100
−2.345
−22.477
17.385
1.00
20.00

N


ATOM
3
O1
BML
100
−2.760
−23.946
19.172
1.00
20.00

O


ATOM
4
C10
BML
100
−4.869
−20.497
19.319
1.00
20.00

C


ATOM
5
C11
BML
100
−5.507
−19.741
20.482
1.00
20.00

C


ATOM
6
C12
BML
100
−5.137
−18.259
20.457
1.00
20.00

C


ATOM
7
C13
BML
100
−5.895
−17.473
21.526
1.00
20.00

C


ATOM
8
C14
BML
100
−5.909
−15.978
21.264
1.00
20.00

C


ATOM
9
C15
BML
100
−7.826
−14.603
22.201
1.00
20.00

C


ATOM
10
C16
BML
100
−7.966
−13.378
21.524
1.00
20.00

C


ATOM
11
C17
BML
100
−9.198
−12.742
21.447
1.00
20.00

C


ATOM
12
C18
BML
100
−10.316
−13.314
22.038
1.00
20.00

C


ATOM
13
C19
BML
100
−10.196
−14.520
22.715
1.00
20.00

C


ATOM
14
C2
BML
100
1.603
−23.425
16.212
1.00
20.00

C


ATOM
15
O2
BML
100
−5.383
−15.494
20.271
1.00
20.00

O


ATOM
16
N2
BML
100
−6.582
−15.302
22.279
1.00
20.00

N


ATOM
17
C20
BML
100
−8.959
−15.167
22.831
1.00
20.00

C


ATOM
18
C3
BML
100
0.544
−23.917
15.459
1.00
20.00

C


ATOM
19
N3
BML
100
−8.917
−16.414
23.490
1.00
20.00

N


ATOM
20
C4
BML
100
−0.770
−23.623
15.816
1.00
20.00

C


ATOM
21
C5
BML
100
−1.039
−22.828
16.942
1.00
20.00

C


ATOM
22
C6
BML
100
0.039
−22.340
17.692
1.00
20.00

C


ATOM
23
C7
BML
100
−3.131
−23.145
18.322
1.00
20.00

C


ATOM
24
CB
BML
100
−4.596
−22.775
18.212
1.00
20.00

C


ATOM
25
C9
BML
100
−5.105
−22.006
19.432
1.00
20.00

C


ATOM
1
C1
BML
200
22.035
3.898
−37.176
1.00
20.00

C


ATOM
2
M1
BML
200
19.679
2.774
−39.797
1.00
20.00

N


ATOM
3
O1
BML
200
17.888
2.589
−38.298
1.00
20.00

O


ATOM
4
C10
BML
200
16.884
0.264
−42.287
1.00
20.00

C


ATOM
5
C11
BML
200
16.812
−1.252
−42.480
1.00
20.00

C


ATOM
6
C12
BML
200
15.887
−1.617
−43.642
1.00
20.00

C


ATOM
7
C13
BML
200
15.592
−3.118
−43.719
1.00
20.00

C


ATOM
8
C14
BML
200
14.527
−3.479
−44.739
1.00
20.00

C


ATOM
9
C15
BML
200
13.205
−5.621
−44.418
1.00
20.00

C


ATOM
10
C16
BML
200
12.291
−6.196
−45.320
1.00
20.00

C


ATOM
11
C17
BML
200
11.237
−6.979
−44.865
1.00
20.00

C


ATOM
12
C18
BML
200
11.075
−7.203
−43.507
1.00
20.00

C


ATOM
13
C19
BML
200
11.958
−6.631
−42.603
1.00
20.00

C


ATOM
14
C2
BML
200
23.026
2.924
−37.221
1.00
20.00

C


ATOM
15
O2
BML
200
13.953
−2.593
−45.361
1.00
20.00

O


ATOM
16
N2
BML
200
14.331
−4.854
−44.847
1.00
20.00

N


ATOM
17
C20
BML
200
13.008
−5.810
−43.032
1.00
20.00

C


ATOM
18
C3
BML
200
22.921
1.873
−38.124
1.00
20.00

C


ATOM
19
N3
BML
200
13.896
−5.297
−42.064
1.00
20.00

N


ATOM
20
C4
BML
200
21.833
1.792
−38.990
1.00
20.00

C


ATOM
21
C5
BML
200
20.828
2.772
−38.956
1.00
20.00

C


ATOM
22
C6
BML
200
20.940
3.819
−38.033
1.00
20.00

C


ATOM
23
C7
BML
200
18.359
2.534
−39.426
1.00
20.00

C


ATOM
24
C8
BML
200
17.500
2.146
−40.618
1.00
20.00

C


ATOM
25
C9
BML
200
17.731
0.706
−41.088
1.00
20.00

C


END









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## Claims

1. A compound having a formula: